data_9HEC
# 
_entry.id   9HEC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9HEC         pdb_00009hec 10.2210/pdb9hec/pdb 
WWPDB D_1292137836 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Source and taxonomy' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' entity_src_gen        
2 2 'Structure model' pdbx_database_related 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_entity_src_gen.gene_src_common_name' 
2 2 'Structure model' '_entity_src_gen.host_org_common_name' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HEC 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9HE6 unspecified 
PDB . 9HE7 unspecified 
PDB . 9HE9 unspecified 
PDB . 9HEA unspecified 
PDB . 9HEB unspecified 
PDB . 9HED unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xjulia@iqfr.csic.es 
_pdbx_contact_author.name_first         Julia 
_pdbx_contact_author.name_last          Sanz-Aparicio 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6849-8621 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fernandez-Garcia, A.' 1 0000-0003-2052-6483 
'Sanz-Aparicio, J.'    2 0000-0002-6849-8621 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Characterization of Recombinant Unspecific Peroxygenase from Candolleomyces aberdarensis through Crystallographic and Substrate Selectivity Studies
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202402015 
_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 'Menes-Rubio, A.'      1 ? 
primary 'Fernandez-Garcia, A.' 2 ? 
primary 'Monterrey, D.T.'      3 ? 
primary 'de Santos, P.G.'      4 ? 
primary 'Sanchez-Moreno, I.'   5 ? 
primary 'Sanz-Aparicio, J.'    6 ? 
primary 'Alcalde, M.'          7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Heme-thiolate peroxidase' 36630.445 3   1.11.2.1 ? ? ? 
2  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1   ?        ? ? ? 
3  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1235.105  1   ?        ? ? ? 
4  branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   2   
?        ? ? ? 
5  branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1   ?        ? ? ? 
6  branched    man 
;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1   ?        ? ? ? 
7  non-polymer syn alpha-ionone 192.297   5   ?        ? ? ? 
8  non-polymer syn GLYCEROL 92.094    3   ?        ? ? ? 
9  non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
10 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
11 non-polymer syn 'SULFATE ION' 96.063    3   ?        ? ? ? 
12 non-polymer syn 'ACETATE ION' 59.044    1   ?        ? ? ? 
13 water       nat water 18.015    562 ?        ? ? ? 
# 
_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       
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
7  alpha-ionone                      A1IUB 
8  GLYCEROL                          GOL   
9  'PROTOPORPHYRIN IX CONTAINING FE' HEM   
10 'MAGNESIUM ION'                   MG    
11 'SULFATE ION'                     SO4   
12 'ACETATE ION'                     ACT   
13 water                             HOH   
# 
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   GLY n 
1 3   VAL n 
1 4   ASP n 
1 5   PRO n 
1 6   PRO n 
1 7   PRO n 
1 8   PRO n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  PRO n 
1 13  SER n 
1 14  PHE n 
1 15  THR n 
1 16  GLY n 
1 17  THR n 
1 18  LYS n 
1 19  LEU n 
1 20  VAL n 
1 21  ASN n 
1 22  ASP n 
1 23  ALA n 
1 24  ASP n 
1 25  HIS n 
1 26  PRO n 
1 27  TRP n 
1 28  GLN n 
1 29  PRO n 
1 30  LEU n 
1 31  ARG n 
1 32  GLU n 
1 33  GLY n 
1 34  ASP n 
1 35  ILE n 
1 36  ARG n 
1 37  GLY n 
1 38  PRO n 
1 39  CYS n 
1 40  PRO n 
1 41  GLY n 
1 42  LEU n 
1 43  ASN n 
1 44  THR n 
1 45  LEU n 
1 46  ALA n 
1 47  SER n 
1 48  HIS n 
1 49  GLY n 
1 50  TYR n 
1 51  LEU n 
1 52  PRO n 
1 53  ARG n 
1 54  ASP n 
1 55  GLY n 
1 56  VAL n 
1 57  ALA n 
1 58  THR n 
1 59  PRO n 
1 60  ALA n 
1 61  GLN n 
1 62  ILE n 
1 63  ILE n 
1 64  THR n 
1 65  ALA n 
1 66  THR n 
1 67  GLN n 
1 68  GLU n 
1 69  GLY n 
1 70  PHE n 
1 71  ASN n 
1 72  PHE n 
1 73  GLU n 
1 74  ASN n 
1 75  ASN n 
1 76  ALA n 
1 77  ALA n 
1 78  ILE n 
1 79  VAL n 
1 80  ALA n 
1 81  THR n 
1 82  TYR n 
1 83  LEU n 
1 84  GLY n 
1 85  HIS n 
1 86  LEU n 
1 87  LEU n 
1 88  ASN n 
1 89  GLY n 
1 90  ASN n 
1 91  LEU n 
1 92  VAL n 
1 93  THR n 
1 94  ASP n 
1 95  LEU n 
1 96  LEU n 
1 97  SER n 
1 98  ILE n 
1 99  GLY n 
1 100 GLY n 
1 101 ALA n 
1 102 THR n 
1 103 PRO n 
1 104 LYS n 
1 105 THR n 
1 106 GLY n 
1 107 PRO n 
1 108 PRO n 
1 109 PRO n 
1 110 PRO n 
1 111 PRO n 
1 112 PRO n 
1 113 ALA n 
1 114 HIS n 
1 115 ALA n 
1 116 GLY n 
1 117 GLY n 
1 118 LEU n 
1 119 ASN n 
1 120 VAL n 
1 121 HIS n 
1 122 GLY n 
1 123 THR n 
1 124 PHE n 
1 125 GLU n 
1 126 GLY n 
1 127 ASP n 
1 128 ALA n 
1 129 GLY n 
1 130 MET n 
1 131 THR n 
1 132 ARG n 
1 133 ALA n 
1 134 ASP n 
1 135 GLU n 
1 136 PHE n 
1 137 PHE n 
1 138 GLY n 
1 139 ASP n 
1 140 ASN n 
1 141 HIS n 
1 142 SER n 
1 143 PHE n 
1 144 ASN n 
1 145 GLN n 
1 146 THR n 
1 147 LEU n 
1 148 PHE n 
1 149 ASP n 
1 150 LYS n 
1 151 PHE n 
1 152 VAL n 
1 153 ASP n 
1 154 PHE n 
1 155 SER n 
1 156 ASN n 
1 157 ARG n 
1 158 TYR n 
1 159 GLY n 
1 160 GLY n 
1 161 GLY n 
1 162 PHE n 
1 163 TYR n 
1 164 ASN n 
1 165 LEU n 
1 166 THR n 
1 167 VAL n 
1 168 ALA n 
1 169 GLY n 
1 170 GLU n 
1 171 LEU n 
1 172 ARG n 
1 173 TYR n 
1 174 SER n 
1 175 ARG n 
1 176 ILE n 
1 177 GLN n 
1 178 ASP n 
1 179 SER n 
1 180 ILE n 
1 181 ALA n 
1 182 THR n 
1 183 ASN n 
1 184 PRO n 
1 185 GLU n 
1 186 PHE n 
1 187 GLN n 
1 188 PHE n 
1 189 LYS n 
1 190 ASN n 
1 191 VAL n 
1 192 ARG n 
1 193 PHE n 
1 194 ILE n 
1 195 THR n 
1 196 ALA n 
1 197 TYR n 
1 198 GLY n 
1 199 GLU n 
1 200 THR n 
1 201 VAL n 
1 202 PHE n 
1 203 PRO n 
1 204 ILE n 
1 205 ASN n 
1 206 LEU n 
1 207 PHE n 
1 208 VAL n 
1 209 ASP n 
1 210 GLY n 
1 211 ARG n 
1 212 VAL n 
1 213 THR n 
1 214 THR n 
1 215 ASP n 
1 216 ARG n 
1 217 LYS n 
1 218 LEU n 
1 219 SER n 
1 220 MET n 
1 221 GLU n 
1 222 ASP n 
1 223 ALA n 
1 224 ALA n 
1 225 SER n 
1 226 ILE n 
1 227 PHE n 
1 228 ARG n 
1 229 ASP n 
1 230 MET n 
1 231 ARG n 
1 232 PHE n 
1 233 PRO n 
1 234 ASP n 
1 235 ASP n 
1 236 PHE n 
1 237 HIS n 
1 238 ARG n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 PRO n 
1 243 ALA n 
1 244 SER n 
1 245 ASN n 
1 246 GLU n 
1 247 GLY n 
1 248 ALA n 
1 249 ASP n 
1 250 GLN n 
1 251 VAL n 
1 252 LEU n 
1 253 ALA n 
1 254 ALA n 
1 255 HIS n 
1 256 PRO n 
1 257 TRP n 
1 258 VAL n 
1 259 PRO n 
1 260 GLY n 
1 261 GLY n 
1 262 ASN n 
1 263 ALA n 
1 264 ASP n 
1 265 ASN n 
1 266 GLN n 
1 267 VAL n 
1 268 ASN n 
1 269 ASN n 
1 270 TYR n 
1 271 VAL n 
1 272 GLU n 
1 273 ASP n 
1 274 PRO n 
1 275 ASP n 
1 276 SER n 
1 277 ALA n 
1 278 ASP n 
1 279 PHE n 
1 280 THR n 
1 281 HIS n 
1 282 LEU n 
1 283 CYS n 
1 284 ARG n 
1 285 LEU n 
1 286 TYR n 
1 287 GLU n 
1 288 PHE n 
1 289 VAL n 
1 290 VAL n 
1 291 GLY n 
1 292 SER n 
1 293 VAL n 
1 294 GLN n 
1 295 GLU n 
1 296 LEU n 
1 297 TYR n 
1 298 PRO n 
1 299 ASN n 
1 300 PRO n 
1 301 THR n 
1 302 GLY n 
1 303 ILE n 
1 304 LEU n 
1 305 ARG n 
1 306 ARG n 
1 307 ASN n 
1 308 LEU n 
1 309 ILE n 
1 310 LYS n 
1 311 ASN n 
1 312 LEU n 
1 313 HIS n 
1 314 TYR n 
1 315 TRP n 
1 316 TRP n 
1 317 THR n 
1 318 GLY n 
1 319 VAL n 
1 320 ASN n 
1 321 VAL n 
1 322 ALA n 
1 323 PHE n 
1 324 GLY n 
1 325 GLY n 
1 326 CYS n 
1 327 ASP n 
1 328 GLU n 
1 329 LEU n 
1 330 PHE n 
1 331 PRO n 
1 332 TYR n 
1 333 GLY n 
1 334 GLN n 
1 335 LEU 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                   335 
_entity_src_gen.gene_src_common_name               'basidiomycete fungi' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EST38_g8238 
_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      'Candolleomyces aberdarensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2316362 
_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               yeast 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella phaffii CBS 7435' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     981350 
_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_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
6 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1  2 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
2  2 'WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1' WURCS PDB2Glycan 
1.1.0 
3  2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}' LINUCS PDB-CARE   ? 
4  3 'DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
5  3 'WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1' 
WURCS                       PDB2Glycan 1.1.0 
6  3 
;[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}
;
LINUCS                      PDB-CARE   ?     
7  4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
8  4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
9  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}' LINUCS                      PDB-CARE   ?     
10 5 'DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1' WURCS 
PDB2Glycan 1.1.0 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
13 6 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1' WURCS PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   
?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3  2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4  2 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
5  3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
7  3 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
8  3 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
9  3 6 MAN C1 O1 4 MAN O6 HO6 sing ? 
10 3 7 MAN C1 O1 3 BMA O3 HO3 sing ? 
11 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
12 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
13 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
14 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
15 5 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
16 5 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
17 5 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
18 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
19 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
20 6 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
# 
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 
A1IUB non-polymer                   . alpha-ionone                             
'(~{E})-4-(2,6,6-trimethylcyclohex-2-en-1-yl)but-3-en-2-one' 'C13 H20 O'        192.297 
ACT   non-polymer                   . 'ACETATE ION'                            ? 'C2 H3 O2 -1'      59.044  
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 
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
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  
GOL   non-polymer                   . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         
92.094  
HEM   non-polymer                   . 'PROTOPORPHYRIN IX CONTAINING FE'        HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer                   . WATER                                    ? 'H2 O'             18.015  
ILE   'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1'   147.195 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose                    'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
MET   'L-peptide linking'           y METHIONINE                               ? 'C5 H11 N O2 S'    149.211 
MG    non-polymer                   . 'MAGNESIUM ION'                          ? 'Mg 2'             24.305  
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
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 
SO4   non-polymer                   . 'SULFATE ION'                            ? 'O4 S -2'          96.063  
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   14  14  GLN GLN A . n 
A 1 2   GLY 2   15  15  GLY GLY A . n 
A 1 3   VAL 3   16  16  VAL VAL A . n 
A 1 4   ASP 4   17  17  ASP ASP A . n 
A 1 5   PRO 5   18  18  PRO PRO A . n 
A 1 6   PRO 6   19  19  PRO PRO A . n 
A 1 7   PRO 7   20  20  PRO PRO A . n 
A 1 8   PRO 8   21  21  PRO PRO A . n 
A 1 9   PRO 9   22  22  PRO PRO A . n 
A 1 10  GLY 10  23  23  GLY GLY A . n 
A 1 11  PRO 11  24  24  PRO PRO A . n 
A 1 12  PRO 12  25  25  PRO PRO A . n 
A 1 13  SER 13  26  26  SER SER A . n 
A 1 14  PHE 14  27  27  PHE PHE A . n 
A 1 15  THR 15  28  28  THR THR A . n 
A 1 16  GLY 16  29  29  GLY GLY A . n 
A 1 17  THR 17  30  30  THR THR A . n 
A 1 18  LYS 18  31  31  LYS LYS A . n 
A 1 19  LEU 19  32  32  LEU LEU A . n 
A 1 20  VAL 20  33  33  VAL VAL A . n 
A 1 21  ASN 21  34  34  ASN ASN A . n 
A 1 22  ASP 22  35  35  ASP ASP A . n 
A 1 23  ALA 23  36  36  ALA ALA A . n 
A 1 24  ASP 24  37  37  ASP ASP A . n 
A 1 25  HIS 25  38  38  HIS HIS A . n 
A 1 26  PRO 26  39  39  PRO PRO A . n 
A 1 27  TRP 27  40  40  TRP TRP A . n 
A 1 28  GLN 28  41  41  GLN GLN A . n 
A 1 29  PRO 29  42  42  PRO PRO A . n 
A 1 30  LEU 30  43  43  LEU LEU A . n 
A 1 31  ARG 31  44  44  ARG ARG A . n 
A 1 32  GLU 32  45  45  GLU GLU A . n 
A 1 33  GLY 33  46  46  GLY GLY A . n 
A 1 34  ASP 34  47  47  ASP ASP A . n 
A 1 35  ILE 35  48  48  ILE ILE A . n 
A 1 36  ARG 36  49  49  ARG ARG A . n 
A 1 37  GLY 37  50  50  GLY GLY A . n 
A 1 38  PRO 38  51  51  PRO PRO A . n 
A 1 39  CYS 39  52  52  CYS CYS A . n 
A 1 40  PRO 40  53  53  PRO PRO A . n 
A 1 41  GLY 41  54  54  GLY GLY A . n 
A 1 42  LEU 42  55  55  LEU LEU A . n 
A 1 43  ASN 43  56  56  ASN ASN A . n 
A 1 44  THR 44  57  57  THR THR A . n 
A 1 45  LEU 45  58  58  LEU LEU A . n 
A 1 46  ALA 46  59  59  ALA ALA A . n 
A 1 47  SER 47  60  60  SER SER A . n 
A 1 48  HIS 48  61  61  HIS HIS A . n 
A 1 49  GLY 49  62  62  GLY GLY A . n 
A 1 50  TYR 50  63  63  TYR TYR A . n 
A 1 51  LEU 51  64  64  LEU LEU A . n 
A 1 52  PRO 52  65  65  PRO PRO A . n 
A 1 53  ARG 53  66  66  ARG ARG A . n 
A 1 54  ASP 54  67  67  ASP ASP A . n 
A 1 55  GLY 55  68  68  GLY GLY A . n 
A 1 56  VAL 56  69  69  VAL VAL A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  THR 58  71  71  THR THR A . n 
A 1 59  PRO 59  72  72  PRO PRO A . n 
A 1 60  ALA 60  73  73  ALA ALA A . n 
A 1 61  GLN 61  74  74  GLN GLN A . n 
A 1 62  ILE 62  75  75  ILE ILE A . n 
A 1 63  ILE 63  76  76  ILE ILE A . n 
A 1 64  THR 64  77  77  THR THR A . n 
A 1 65  ALA 65  78  78  ALA ALA A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  GLN 67  80  80  GLN GLN A . n 
A 1 68  GLU 68  81  81  GLU GLU A . n 
A 1 69  GLY 69  82  82  GLY GLY A . n 
A 1 70  PHE 70  83  83  PHE PHE A . n 
A 1 71  ASN 71  84  84  ASN ASN A . n 
A 1 72  PHE 72  85  85  PHE PHE A . n 
A 1 73  GLU 73  86  86  GLU GLU A . n 
A 1 74  ASN 74  87  87  ASN ASN A . n 
A 1 75  ASN 75  88  88  ASN ASN A . n 
A 1 76  ALA 76  89  89  ALA ALA A . n 
A 1 77  ALA 77  90  90  ALA ALA A . n 
A 1 78  ILE 78  91  91  ILE ILE A . n 
A 1 79  VAL 79  92  92  VAL VAL A . n 
A 1 80  ALA 80  93  93  ALA ALA A . n 
A 1 81  THR 81  94  94  THR THR A . n 
A 1 82  TYR 82  95  95  TYR TYR A . n 
A 1 83  LEU 83  96  96  LEU LEU A . n 
A 1 84  GLY 84  97  97  GLY GLY A . n 
A 1 85  HIS 85  98  98  HIS HIS A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  LEU 87  100 100 LEU LEU A . n 
A 1 88  ASN 88  101 101 ASN ASN A . n 
A 1 89  GLY 89  102 102 GLY GLY A . n 
A 1 90  ASN 90  103 103 ASN ASN A . n 
A 1 91  LEU 91  104 104 LEU LEU A . n 
A 1 92  VAL 92  105 105 VAL VAL A . n 
A 1 93  THR 93  106 106 THR THR A . n 
A 1 94  ASP 94  107 107 ASP ASP A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LEU 96  109 109 LEU LEU A . n 
A 1 97  SER 97  110 110 SER SER A . n 
A 1 98  ILE 98  111 111 ILE ILE A . n 
A 1 99  GLY 99  112 112 GLY GLY A . n 
A 1 100 GLY 100 113 113 GLY GLY A . n 
A 1 101 ALA 101 114 114 ALA ALA A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 PRO 103 116 116 PRO PRO A . n 
A 1 104 LYS 104 117 117 LYS LYS A . n 
A 1 105 THR 105 118 118 THR THR A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 PRO 107 120 120 PRO PRO A . n 
A 1 108 PRO 108 121 121 PRO PRO A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PRO 110 123 123 PRO PRO A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 PRO 112 125 125 PRO PRO A . n 
A 1 113 ALA 113 126 126 ALA ALA A . n 
A 1 114 HIS 114 127 127 HIS HIS A . n 
A 1 115 ALA 115 128 128 ALA ALA A . n 
A 1 116 GLY 116 129 129 GLY GLY A . n 
A 1 117 GLY 117 130 130 GLY GLY A . n 
A 1 118 LEU 118 131 131 LEU LEU A . n 
A 1 119 ASN 119 132 132 ASN ASN A . n 
A 1 120 VAL 120 133 133 VAL VAL A . n 
A 1 121 HIS 121 134 134 HIS HIS A . n 
A 1 122 GLY 122 135 135 GLY GLY A . n 
A 1 123 THR 123 136 136 THR THR A . n 
A 1 124 PHE 124 137 137 PHE PHE A . n 
A 1 125 GLU 125 138 138 GLU GLU A . n 
A 1 126 GLY 126 139 139 GLY GLY A . n 
A 1 127 ASP 127 140 140 ASP ASP A . n 
A 1 128 ALA 128 141 141 ALA ALA A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 MET 130 143 143 MET MET A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 ARG 132 145 145 ARG ARG A . n 
A 1 133 ALA 133 146 146 ALA ALA A . n 
A 1 134 ASP 134 147 147 ASP ASP A . n 
A 1 135 GLU 135 148 148 GLU GLU A . n 
A 1 136 PHE 136 149 149 PHE PHE A . n 
A 1 137 PHE 137 150 150 PHE PHE A . n 
A 1 138 GLY 138 151 151 GLY GLY A . n 
A 1 139 ASP 139 152 152 ASP ASP A . n 
A 1 140 ASN 140 153 153 ASN ASN A . n 
A 1 141 HIS 141 154 154 HIS HIS A . n 
A 1 142 SER 142 155 155 SER SER A . n 
A 1 143 PHE 143 156 156 PHE PHE A . n 
A 1 144 ASN 144 157 157 ASN ASN A . n 
A 1 145 GLN 145 158 158 GLN GLN A . n 
A 1 146 THR 146 159 159 THR THR A . n 
A 1 147 LEU 147 160 160 LEU LEU A . n 
A 1 148 PHE 148 161 161 PHE PHE A . n 
A 1 149 ASP 149 162 162 ASP ASP A . n 
A 1 150 LYS 150 163 163 LYS LYS A . n 
A 1 151 PHE 151 164 164 PHE PHE A . n 
A 1 152 VAL 152 165 165 VAL VAL A . n 
A 1 153 ASP 153 166 166 ASP ASP A . n 
A 1 154 PHE 154 167 167 PHE PHE A . n 
A 1 155 SER 155 168 168 SER SER A . n 
A 1 156 ASN 156 169 169 ASN ASN A . n 
A 1 157 ARG 157 170 170 ARG ARG A . n 
A 1 158 TYR 158 171 171 TYR TYR A . n 
A 1 159 GLY 159 172 172 GLY GLY A . n 
A 1 160 GLY 160 173 173 GLY GLY A . n 
A 1 161 GLY 161 174 174 GLY GLY A . n 
A 1 162 PHE 162 175 175 PHE PHE A . n 
A 1 163 TYR 163 176 176 TYR TYR A . n 
A 1 164 ASN 164 177 177 ASN ASN A . n 
A 1 165 LEU 165 178 178 LEU LEU A . n 
A 1 166 THR 166 179 179 THR THR A . n 
A 1 167 VAL 167 180 180 VAL VAL A . n 
A 1 168 ALA 168 181 181 ALA ALA A . n 
A 1 169 GLY 169 182 182 GLY GLY A . n 
A 1 170 GLU 170 183 183 GLU GLU A . n 
A 1 171 LEU 171 184 184 LEU LEU A . n 
A 1 172 ARG 172 185 185 ARG ARG A . n 
A 1 173 TYR 173 186 186 TYR TYR A . n 
A 1 174 SER 174 187 187 SER SER A . n 
A 1 175 ARG 175 188 188 ARG ARG A . n 
A 1 176 ILE 176 189 189 ILE ILE A . n 
A 1 177 GLN 177 190 190 GLN GLN A . n 
A 1 178 ASP 178 191 191 ASP ASP A . n 
A 1 179 SER 179 192 192 SER SER A . n 
A 1 180 ILE 180 193 193 ILE ILE A . n 
A 1 181 ALA 181 194 194 ALA ALA A . n 
A 1 182 THR 182 195 195 THR THR A . n 
A 1 183 ASN 183 196 196 ASN ASN A . n 
A 1 184 PRO 184 197 197 PRO PRO A . n 
A 1 185 GLU 185 198 198 GLU GLU A . n 
A 1 186 PHE 186 199 199 PHE PHE A . n 
A 1 187 GLN 187 200 200 GLN GLN A . n 
A 1 188 PHE 188 201 201 PHE PHE A . n 
A 1 189 LYS 189 202 202 LYS LYS A . n 
A 1 190 ASN 190 203 203 ASN ASN A . n 
A 1 191 VAL 191 204 204 VAL VAL A . n 
A 1 192 ARG 192 205 205 ARG ARG A . n 
A 1 193 PHE 193 206 206 PHE PHE A . n 
A 1 194 ILE 194 207 207 ILE ILE A . n 
A 1 195 THR 195 208 208 THR THR A . n 
A 1 196 ALA 196 209 209 ALA ALA A . n 
A 1 197 TYR 197 210 210 TYR TYR A . n 
A 1 198 GLY 198 211 211 GLY GLY A . n 
A 1 199 GLU 199 212 212 GLU GLU A . n 
A 1 200 THR 200 213 213 THR THR A . n 
A 1 201 VAL 201 214 214 VAL VAL A . n 
A 1 202 PHE 202 215 215 PHE PHE A . n 
A 1 203 PRO 203 216 216 PRO PRO A . n 
A 1 204 ILE 204 217 217 ILE ILE A . n 
A 1 205 ASN 205 218 218 ASN ASN A . n 
A 1 206 LEU 206 219 219 LEU LEU A . n 
A 1 207 PHE 207 220 220 PHE PHE A . n 
A 1 208 VAL 208 221 221 VAL VAL A . n 
A 1 209 ASP 209 222 222 ASP ASP A . n 
A 1 210 GLY 210 223 223 GLY GLY A . n 
A 1 211 ARG 211 224 224 ARG ARG A . n 
A 1 212 VAL 212 225 225 VAL VAL A . n 
A 1 213 THR 213 226 226 THR THR A . n 
A 1 214 THR 214 227 227 THR THR A . n 
A 1 215 ASP 215 228 228 ASP ASP A . n 
A 1 216 ARG 216 229 229 ARG ARG A . n 
A 1 217 LYS 217 230 230 LYS LYS A . n 
A 1 218 LEU 218 231 231 LEU LEU A . n 
A 1 219 SER 219 232 232 SER SER A . n 
A 1 220 MET 220 233 233 MET MET A . n 
A 1 221 GLU 221 234 234 GLU GLU A . n 
A 1 222 ASP 222 235 235 ASP ASP A . n 
A 1 223 ALA 223 236 236 ALA ALA A . n 
A 1 224 ALA 224 237 237 ALA ALA A . n 
A 1 225 SER 225 238 238 SER SER A . n 
A 1 226 ILE 226 239 239 ILE ILE A . n 
A 1 227 PHE 227 240 240 PHE PHE A . n 
A 1 228 ARG 228 241 241 ARG ARG A . n 
A 1 229 ASP 229 242 242 ASP ASP A . n 
A 1 230 MET 230 243 243 MET MET A . n 
A 1 231 ARG 231 244 244 ARG ARG A . n 
A 1 232 PHE 232 245 245 PHE PHE A . n 
A 1 233 PRO 233 246 246 PRO PRO A . n 
A 1 234 ASP 234 247 247 ASP ASP A . n 
A 1 235 ASP 235 248 248 ASP ASP A . n 
A 1 236 PHE 236 249 249 PHE PHE A . n 
A 1 237 HIS 237 250 250 HIS HIS A . n 
A 1 238 ARG 238 251 251 ARG ARG A . n 
A 1 239 SER 239 252 252 SER SER A . n 
A 1 240 ALA 240 253 253 ALA ALA A . n 
A 1 241 VAL 241 254 254 VAL VAL A . n 
A 1 242 PRO 242 255 255 PRO PRO A . n 
A 1 243 ALA 243 256 256 ALA ALA A . n 
A 1 244 SER 244 257 257 SER SER A . n 
A 1 245 ASN 245 258 258 ASN ASN A . n 
A 1 246 GLU 246 259 259 GLU GLU A . n 
A 1 247 GLY 247 260 260 GLY GLY A . n 
A 1 248 ALA 248 261 261 ALA ALA A . n 
A 1 249 ASP 249 262 262 ASP ASP A . n 
A 1 250 GLN 250 263 263 GLN GLN A . n 
A 1 251 VAL 251 264 264 VAL VAL A . n 
A 1 252 LEU 252 265 265 LEU LEU A . n 
A 1 253 ALA 253 266 266 ALA ALA A . n 
A 1 254 ALA 254 267 267 ALA ALA A . n 
A 1 255 HIS 255 268 268 HIS HIS A . n 
A 1 256 PRO 256 269 269 PRO PRO A . n 
A 1 257 TRP 257 270 270 TRP TRP A . n 
A 1 258 VAL 258 271 271 VAL VAL A . n 
A 1 259 PRO 259 272 272 PRO PRO A . n 
A 1 260 GLY 260 273 273 GLY GLY A . n 
A 1 261 GLY 261 274 274 GLY GLY A . n 
A 1 262 ASN 262 275 275 ASN ASN A . n 
A 1 263 ALA 263 276 276 ALA ALA A . n 
A 1 264 ASP 264 277 277 ASP ASP A . n 
A 1 265 ASN 265 278 278 ASN ASN A . n 
A 1 266 GLN 266 279 279 GLN GLN A . n 
A 1 267 VAL 267 280 280 VAL VAL A . n 
A 1 268 ASN 268 281 281 ASN ASN A . n 
A 1 269 ASN 269 282 282 ASN ASN A . n 
A 1 270 TYR 270 283 283 TYR TYR A . n 
A 1 271 VAL 271 284 284 VAL VAL A . n 
A 1 272 GLU 272 285 285 GLU GLU A . n 
A 1 273 ASP 273 286 286 ASP ASP A . n 
A 1 274 PRO 274 287 287 PRO PRO A . n 
A 1 275 ASP 275 288 288 ASP ASP A . n 
A 1 276 SER 276 289 289 SER SER A . n 
A 1 277 ALA 277 290 290 ALA ALA A . n 
A 1 278 ASP 278 291 291 ASP ASP A . n 
A 1 279 PHE 279 292 292 PHE PHE A . n 
A 1 280 THR 280 293 293 THR THR A . n 
A 1 281 HIS 281 294 294 HIS HIS A . n 
A 1 282 LEU 282 295 295 LEU LEU A . n 
A 1 283 CYS 283 296 296 CYS CYS A . n 
A 1 284 ARG 284 297 297 ARG ARG A . n 
A 1 285 LEU 285 298 298 LEU LEU A . n 
A 1 286 TYR 286 299 299 TYR TYR A . n 
A 1 287 GLU 287 300 300 GLU GLU A . n 
A 1 288 PHE 288 301 301 PHE PHE A . n 
A 1 289 VAL 289 302 302 VAL VAL A . n 
A 1 290 VAL 290 303 303 VAL VAL A . n 
A 1 291 GLY 291 304 304 GLY GLY A . n 
A 1 292 SER 292 305 305 SER SER A . n 
A 1 293 VAL 293 306 306 VAL VAL A . n 
A 1 294 GLN 294 307 307 GLN GLN A . n 
A 1 295 GLU 295 308 308 GLU GLU A . n 
A 1 296 LEU 296 309 309 LEU LEU A . n 
A 1 297 TYR 297 310 310 TYR TYR A . n 
A 1 298 PRO 298 311 311 PRO PRO A . n 
A 1 299 ASN 299 312 312 ASN ASN A . n 
A 1 300 PRO 300 313 313 PRO PRO A . n 
A 1 301 THR 301 314 314 THR THR A . n 
A 1 302 GLY 302 315 315 GLY GLY A . n 
A 1 303 ILE 303 316 316 ILE ILE A . n 
A 1 304 LEU 304 317 317 LEU LEU A . n 
A 1 305 ARG 305 318 318 ARG ARG A . n 
A 1 306 ARG 306 319 319 ARG ARG A . n 
A 1 307 ASN 307 320 320 ASN ASN A . n 
A 1 308 LEU 308 321 321 LEU LEU A . n 
A 1 309 ILE 309 322 322 ILE ILE A . n 
A 1 310 LYS 310 323 323 LYS LYS A . n 
A 1 311 ASN 311 324 324 ASN ASN A . n 
A 1 312 LEU 312 325 325 LEU LEU A . n 
A 1 313 HIS 313 326 326 HIS HIS A . n 
A 1 314 TYR 314 327 327 TYR TYR A . n 
A 1 315 TRP 315 328 328 TRP TRP A . n 
A 1 316 TRP 316 329 329 TRP TRP A . n 
A 1 317 THR 317 330 330 THR THR A . n 
A 1 318 GLY 318 331 331 GLY GLY A . n 
A 1 319 VAL 319 332 332 VAL VAL A . n 
A 1 320 ASN 320 333 333 ASN ASN A . n 
A 1 321 VAL 321 334 334 VAL VAL A . n 
A 1 322 ALA 322 335 335 ALA ALA A . n 
A 1 323 PHE 323 336 336 PHE PHE A . n 
A 1 324 GLY 324 337 337 GLY GLY A . n 
A 1 325 GLY 325 338 338 GLY GLY A . n 
A 1 326 CYS 326 339 339 CYS CYS A . n 
A 1 327 ASP 327 340 340 ASP ASP A . n 
A 1 328 GLU 328 341 341 GLU GLU A . n 
A 1 329 LEU 329 342 342 LEU LEU A . n 
A 1 330 PHE 330 343 343 PHE PHE A . n 
A 1 331 PRO 331 344 344 PRO PRO A . n 
A 1 332 TYR 332 345 345 TYR TYR A . n 
A 1 333 GLY 333 346 346 GLY GLY A . n 
A 1 334 GLN 334 347 347 GLN GLN A . n 
A 1 335 LEU 335 348 348 LEU LEU A . n 
B 1 1   GLN 1   14  14  GLN GLN B . n 
B 1 2   GLY 2   15  15  GLY GLY B . n 
B 1 3   VAL 3   16  16  VAL VAL B . n 
B 1 4   ASP 4   17  17  ASP ASP B . n 
B 1 5   PRO 5   18  18  PRO PRO B . n 
B 1 6   PRO 6   19  19  PRO PRO B . n 
B 1 7   PRO 7   20  20  PRO PRO B . n 
B 1 8   PRO 8   21  21  PRO PRO B . n 
B 1 9   PRO 9   22  22  PRO PRO B . n 
B 1 10  GLY 10  23  23  GLY GLY B . n 
B 1 11  PRO 11  24  24  PRO PRO B . n 
B 1 12  PRO 12  25  25  PRO PRO B . n 
B 1 13  SER 13  26  26  SER SER B . n 
B 1 14  PHE 14  27  27  PHE PHE B . n 
B 1 15  THR 15  28  28  THR THR B . n 
B 1 16  GLY 16  29  29  GLY GLY B . n 
B 1 17  THR 17  30  30  THR THR B . n 
B 1 18  LYS 18  31  31  LYS LYS B . n 
B 1 19  LEU 19  32  32  LEU LEU B . n 
B 1 20  VAL 20  33  33  VAL VAL B . n 
B 1 21  ASN 21  34  34  ASN ASN B . n 
B 1 22  ASP 22  35  35  ASP ASP B . n 
B 1 23  ALA 23  36  36  ALA ALA B . n 
B 1 24  ASP 24  37  37  ASP ASP B . n 
B 1 25  HIS 25  38  38  HIS HIS B . n 
B 1 26  PRO 26  39  39  PRO PRO B . n 
B 1 27  TRP 27  40  40  TRP TRP B . n 
B 1 28  GLN 28  41  41  GLN GLN B . n 
B 1 29  PRO 29  42  42  PRO PRO B . n 
B 1 30  LEU 30  43  43  LEU LEU B . n 
B 1 31  ARG 31  44  44  ARG ARG B . n 
B 1 32  GLU 32  45  45  GLU GLU B . n 
B 1 33  GLY 33  46  46  GLY GLY B . n 
B 1 34  ASP 34  47  47  ASP ASP B . n 
B 1 35  ILE 35  48  48  ILE ILE B . n 
B 1 36  ARG 36  49  49  ARG ARG B . n 
B 1 37  GLY 37  50  50  GLY GLY B . n 
B 1 38  PRO 38  51  51  PRO PRO B . n 
B 1 39  CYS 39  52  52  CYS CYS B . n 
B 1 40  PRO 40  53  53  PRO PRO B . n 
B 1 41  GLY 41  54  54  GLY GLY B . n 
B 1 42  LEU 42  55  55  LEU LEU B . n 
B 1 43  ASN 43  56  56  ASN ASN B . n 
B 1 44  THR 44  57  57  THR THR B . n 
B 1 45  LEU 45  58  58  LEU LEU B . n 
B 1 46  ALA 46  59  59  ALA ALA B . n 
B 1 47  SER 47  60  60  SER SER B . n 
B 1 48  HIS 48  61  61  HIS HIS B . n 
B 1 49  GLY 49  62  62  GLY GLY B . n 
B 1 50  TYR 50  63  63  TYR TYR B . n 
B 1 51  LEU 51  64  64  LEU LEU B . n 
B 1 52  PRO 52  65  65  PRO PRO B . n 
B 1 53  ARG 53  66  66  ARG ARG B . n 
B 1 54  ASP 54  67  67  ASP ASP B . n 
B 1 55  GLY 55  68  68  GLY GLY B . n 
B 1 56  VAL 56  69  69  VAL VAL B . n 
B 1 57  ALA 57  70  70  ALA ALA B . n 
B 1 58  THR 58  71  71  THR THR B . n 
B 1 59  PRO 59  72  72  PRO PRO B . n 
B 1 60  ALA 60  73  73  ALA ALA B . n 
B 1 61  GLN 61  74  74  GLN GLN B . n 
B 1 62  ILE 62  75  75  ILE ILE B . n 
B 1 63  ILE 63  76  76  ILE ILE B . n 
B 1 64  THR 64  77  77  THR THR B . n 
B 1 65  ALA 65  78  78  ALA ALA B . n 
B 1 66  THR 66  79  79  THR THR B . n 
B 1 67  GLN 67  80  80  GLN GLN B . n 
B 1 68  GLU 68  81  81  GLU GLU B . n 
B 1 69  GLY 69  82  82  GLY GLY B . n 
B 1 70  PHE 70  83  83  PHE PHE B . n 
B 1 71  ASN 71  84  84  ASN ASN B . n 
B 1 72  PHE 72  85  85  PHE PHE B . n 
B 1 73  GLU 73  86  86  GLU GLU B . n 
B 1 74  ASN 74  87  87  ASN ASN B . n 
B 1 75  ASN 75  88  88  ASN ASN B . n 
B 1 76  ALA 76  89  89  ALA ALA B . n 
B 1 77  ALA 77  90  90  ALA ALA B . n 
B 1 78  ILE 78  91  91  ILE ILE B . n 
B 1 79  VAL 79  92  92  VAL VAL B . n 
B 1 80  ALA 80  93  93  ALA ALA B . n 
B 1 81  THR 81  94  94  THR THR B . n 
B 1 82  TYR 82  95  95  TYR TYR B . n 
B 1 83  LEU 83  96  96  LEU LEU B . n 
B 1 84  GLY 84  97  97  GLY GLY B . n 
B 1 85  HIS 85  98  98  HIS HIS B . n 
B 1 86  LEU 86  99  99  LEU LEU B . n 
B 1 87  LEU 87  100 100 LEU LEU B . n 
B 1 88  ASN 88  101 101 ASN ASN B . n 
B 1 89  GLY 89  102 102 GLY GLY B . n 
B 1 90  ASN 90  103 103 ASN ASN B . n 
B 1 91  LEU 91  104 104 LEU LEU B . n 
B 1 92  VAL 92  105 105 VAL VAL B . n 
B 1 93  THR 93  106 106 THR THR B . n 
B 1 94  ASP 94  107 107 ASP ASP B . n 
B 1 95  LEU 95  108 108 LEU LEU B . n 
B 1 96  LEU 96  109 109 LEU LEU B . n 
B 1 97  SER 97  110 110 SER SER B . n 
B 1 98  ILE 98  111 111 ILE ILE B . n 
B 1 99  GLY 99  112 112 GLY GLY B . n 
B 1 100 GLY 100 113 113 GLY GLY B . n 
B 1 101 ALA 101 114 114 ALA ALA B . n 
B 1 102 THR 102 115 115 THR THR B . n 
B 1 103 PRO 103 116 116 PRO PRO B . n 
B 1 104 LYS 104 117 117 LYS LYS B . n 
B 1 105 THR 105 118 118 THR THR B . n 
B 1 106 GLY 106 119 119 GLY GLY B . n 
B 1 107 PRO 107 120 120 PRO PRO B . n 
B 1 108 PRO 108 121 121 PRO PRO B . n 
B 1 109 PRO 109 122 122 PRO PRO B . n 
B 1 110 PRO 110 123 123 PRO PRO B . n 
B 1 111 PRO 111 124 124 PRO PRO B . n 
B 1 112 PRO 112 125 125 PRO PRO B . n 
B 1 113 ALA 113 126 126 ALA ALA B . n 
B 1 114 HIS 114 127 127 HIS HIS B . n 
B 1 115 ALA 115 128 128 ALA ALA B . n 
B 1 116 GLY 116 129 129 GLY GLY B . n 
B 1 117 GLY 117 130 130 GLY GLY B . n 
B 1 118 LEU 118 131 131 LEU LEU B . n 
B 1 119 ASN 119 132 132 ASN ASN B . n 
B 1 120 VAL 120 133 133 VAL VAL B . n 
B 1 121 HIS 121 134 134 HIS HIS B . n 
B 1 122 GLY 122 135 135 GLY GLY B . n 
B 1 123 THR 123 136 136 THR THR B . n 
B 1 124 PHE 124 137 137 PHE PHE B . n 
B 1 125 GLU 125 138 138 GLU GLU B . n 
B 1 126 GLY 126 139 139 GLY GLY B . n 
B 1 127 ASP 127 140 140 ASP ASP B . n 
B 1 128 ALA 128 141 141 ALA ALA B . n 
B 1 129 GLY 129 142 142 GLY GLY B . n 
B 1 130 MET 130 143 143 MET MET B . n 
B 1 131 THR 131 144 144 THR THR B . n 
B 1 132 ARG 132 145 145 ARG ARG B . n 
B 1 133 ALA 133 146 146 ALA ALA B . n 
B 1 134 ASP 134 147 147 ASP ASP B . n 
B 1 135 GLU 135 148 148 GLU GLU B . n 
B 1 136 PHE 136 149 149 PHE PHE B . n 
B 1 137 PHE 137 150 150 PHE PHE B . n 
B 1 138 GLY 138 151 151 GLY GLY B . n 
B 1 139 ASP 139 152 152 ASP ASP B . n 
B 1 140 ASN 140 153 153 ASN ASN B . n 
B 1 141 HIS 141 154 154 HIS HIS B . n 
B 1 142 SER 142 155 155 SER SER B . n 
B 1 143 PHE 143 156 156 PHE PHE B . n 
B 1 144 ASN 144 157 157 ASN ASN B . n 
B 1 145 GLN 145 158 158 GLN GLN B . n 
B 1 146 THR 146 159 159 THR THR B . n 
B 1 147 LEU 147 160 160 LEU LEU B . n 
B 1 148 PHE 148 161 161 PHE PHE B . n 
B 1 149 ASP 149 162 162 ASP ASP B . n 
B 1 150 LYS 150 163 163 LYS LYS B . n 
B 1 151 PHE 151 164 164 PHE PHE B . n 
B 1 152 VAL 152 165 165 VAL VAL B . n 
B 1 153 ASP 153 166 166 ASP ASP B . n 
B 1 154 PHE 154 167 167 PHE PHE B . n 
B 1 155 SER 155 168 168 SER SER B . n 
B 1 156 ASN 156 169 169 ASN ASN B . n 
B 1 157 ARG 157 170 170 ARG ARG B . n 
B 1 158 TYR 158 171 171 TYR TYR B . n 
B 1 159 GLY 159 172 172 GLY GLY B . n 
B 1 160 GLY 160 173 173 GLY GLY B . n 
B 1 161 GLY 161 174 174 GLY GLY B . n 
B 1 162 PHE 162 175 175 PHE PHE B . n 
B 1 163 TYR 163 176 176 TYR TYR B . n 
B 1 164 ASN 164 177 177 ASN ASN B . n 
B 1 165 LEU 165 178 178 LEU LEU B . n 
B 1 166 THR 166 179 179 THR THR B . n 
B 1 167 VAL 167 180 180 VAL VAL B . n 
B 1 168 ALA 168 181 181 ALA ALA B . n 
B 1 169 GLY 169 182 182 GLY GLY B . n 
B 1 170 GLU 170 183 183 GLU GLU B . n 
B 1 171 LEU 171 184 184 LEU LEU B . n 
B 1 172 ARG 172 185 185 ARG ARG B . n 
B 1 173 TYR 173 186 186 TYR TYR B . n 
B 1 174 SER 174 187 187 SER SER B . n 
B 1 175 ARG 175 188 188 ARG ARG B . n 
B 1 176 ILE 176 189 189 ILE ILE B . n 
B 1 177 GLN 177 190 190 GLN GLN B . n 
B 1 178 ASP 178 191 191 ASP ASP B . n 
B 1 179 SER 179 192 192 SER SER B . n 
B 1 180 ILE 180 193 193 ILE ILE B . n 
B 1 181 ALA 181 194 194 ALA ALA B . n 
B 1 182 THR 182 195 195 THR THR B . n 
B 1 183 ASN 183 196 196 ASN ASN B . n 
B 1 184 PRO 184 197 197 PRO PRO B . n 
B 1 185 GLU 185 198 198 GLU GLU B . n 
B 1 186 PHE 186 199 199 PHE PHE B . n 
B 1 187 GLN 187 200 200 GLN GLN B . n 
B 1 188 PHE 188 201 201 PHE PHE B . n 
B 1 189 LYS 189 202 202 LYS LYS B . n 
B 1 190 ASN 190 203 203 ASN ASN B . n 
B 1 191 VAL 191 204 204 VAL VAL B . n 
B 1 192 ARG 192 205 205 ARG ARG B . n 
B 1 193 PHE 193 206 206 PHE PHE B . n 
B 1 194 ILE 194 207 207 ILE ILE B . n 
B 1 195 THR 195 208 208 THR THR B . n 
B 1 196 ALA 196 209 209 ALA ALA B . n 
B 1 197 TYR 197 210 210 TYR TYR B . n 
B 1 198 GLY 198 211 211 GLY GLY B . n 
B 1 199 GLU 199 212 212 GLU GLU B . n 
B 1 200 THR 200 213 213 THR THR B . n 
B 1 201 VAL 201 214 214 VAL VAL B . n 
B 1 202 PHE 202 215 215 PHE PHE B . n 
B 1 203 PRO 203 216 216 PRO PRO B . n 
B 1 204 ILE 204 217 217 ILE ILE B . n 
B 1 205 ASN 205 218 218 ASN ASN B . n 
B 1 206 LEU 206 219 219 LEU LEU B . n 
B 1 207 PHE 207 220 220 PHE PHE B . n 
B 1 208 VAL 208 221 221 VAL VAL B . n 
B 1 209 ASP 209 222 222 ASP ASP B . n 
B 1 210 GLY 210 223 223 GLY GLY B . n 
B 1 211 ARG 211 224 224 ARG ARG B . n 
B 1 212 VAL 212 225 225 VAL VAL B . n 
B 1 213 THR 213 226 226 THR THR B . n 
B 1 214 THR 214 227 227 THR THR B . n 
B 1 215 ASP 215 228 228 ASP ASP B . n 
B 1 216 ARG 216 229 229 ARG ARG B . n 
B 1 217 LYS 217 230 230 LYS LYS B . n 
B 1 218 LEU 218 231 231 LEU LEU B . n 
B 1 219 SER 219 232 232 SER SER B . n 
B 1 220 MET 220 233 233 MET MET B . n 
B 1 221 GLU 221 234 234 GLU GLU B . n 
B 1 222 ASP 222 235 235 ASP ASP B . n 
B 1 223 ALA 223 236 236 ALA ALA B . n 
B 1 224 ALA 224 237 237 ALA ALA B . n 
B 1 225 SER 225 238 238 SER SER B . n 
B 1 226 ILE 226 239 239 ILE ILE B . n 
B 1 227 PHE 227 240 240 PHE PHE B . n 
B 1 228 ARG 228 241 241 ARG ARG B . n 
B 1 229 ASP 229 242 242 ASP ASP B . n 
B 1 230 MET 230 243 243 MET MET B . n 
B 1 231 ARG 231 244 244 ARG ARG B . n 
B 1 232 PHE 232 245 245 PHE PHE B . n 
B 1 233 PRO 233 246 246 PRO PRO B . n 
B 1 234 ASP 234 247 247 ASP ASP B . n 
B 1 235 ASP 235 248 248 ASP ASP B . n 
B 1 236 PHE 236 249 249 PHE PHE B . n 
B 1 237 HIS 237 250 250 HIS HIS B . n 
B 1 238 ARG 238 251 251 ARG ARG B . n 
B 1 239 SER 239 252 252 SER SER B . n 
B 1 240 ALA 240 253 253 ALA ALA B . n 
B 1 241 VAL 241 254 254 VAL VAL B . n 
B 1 242 PRO 242 255 255 PRO PRO B . n 
B 1 243 ALA 243 256 256 ALA ALA B . n 
B 1 244 SER 244 257 257 SER SER B . n 
B 1 245 ASN 245 258 258 ASN ASN B . n 
B 1 246 GLU 246 259 259 GLU GLU B . n 
B 1 247 GLY 247 260 260 GLY GLY B . n 
B 1 248 ALA 248 261 261 ALA ALA B . n 
B 1 249 ASP 249 262 262 ASP ASP B . n 
B 1 250 GLN 250 263 263 GLN GLN B . n 
B 1 251 VAL 251 264 264 VAL VAL B . n 
B 1 252 LEU 252 265 265 LEU LEU B . n 
B 1 253 ALA 253 266 266 ALA ALA B . n 
B 1 254 ALA 254 267 267 ALA ALA B . n 
B 1 255 HIS 255 268 268 HIS HIS B . n 
B 1 256 PRO 256 269 269 PRO PRO B . n 
B 1 257 TRP 257 270 270 TRP TRP B . n 
B 1 258 VAL 258 271 271 VAL VAL B . n 
B 1 259 PRO 259 272 272 PRO PRO B . n 
B 1 260 GLY 260 273 273 GLY GLY B . n 
B 1 261 GLY 261 274 274 GLY GLY B . n 
B 1 262 ASN 262 275 275 ASN ASN B . n 
B 1 263 ALA 263 276 276 ALA ALA B . n 
B 1 264 ASP 264 277 277 ASP ASP B . n 
B 1 265 ASN 265 278 278 ASN ASN B . n 
B 1 266 GLN 266 279 279 GLN GLN B . n 
B 1 267 VAL 267 280 280 VAL VAL B . n 
B 1 268 ASN 268 281 281 ASN ASN B . n 
B 1 269 ASN 269 282 282 ASN ASN B . n 
B 1 270 TYR 270 283 283 TYR TYR B . n 
B 1 271 VAL 271 284 284 VAL VAL B . n 
B 1 272 GLU 272 285 285 GLU GLU B . n 
B 1 273 ASP 273 286 286 ASP ASP B . n 
B 1 274 PRO 274 287 287 PRO PRO B . n 
B 1 275 ASP 275 288 288 ASP ASP B . n 
B 1 276 SER 276 289 289 SER SER B . n 
B 1 277 ALA 277 290 290 ALA ALA B . n 
B 1 278 ASP 278 291 291 ASP ASP B . n 
B 1 279 PHE 279 292 292 PHE PHE B . n 
B 1 280 THR 280 293 293 THR THR B . n 
B 1 281 HIS 281 294 294 HIS HIS B . n 
B 1 282 LEU 282 295 295 LEU LEU B . n 
B 1 283 CYS 283 296 296 CYS CYS B . n 
B 1 284 ARG 284 297 297 ARG ARG B . n 
B 1 285 LEU 285 298 298 LEU LEU B . n 
B 1 286 TYR 286 299 299 TYR TYR B . n 
B 1 287 GLU 287 300 300 GLU GLU B . n 
B 1 288 PHE 288 301 301 PHE PHE B . n 
B 1 289 VAL 289 302 302 VAL VAL B . n 
B 1 290 VAL 290 303 303 VAL VAL B . n 
B 1 291 GLY 291 304 304 GLY GLY B . n 
B 1 292 SER 292 305 305 SER SER B . n 
B 1 293 VAL 293 306 306 VAL VAL B . n 
B 1 294 GLN 294 307 307 GLN GLN B . n 
B 1 295 GLU 295 308 308 GLU GLU B . n 
B 1 296 LEU 296 309 309 LEU LEU B . n 
B 1 297 TYR 297 310 310 TYR TYR B . n 
B 1 298 PRO 298 311 311 PRO PRO B . n 
B 1 299 ASN 299 312 312 ASN ASN B . n 
B 1 300 PRO 300 313 313 PRO PRO B . n 
B 1 301 THR 301 314 314 THR THR B . n 
B 1 302 GLY 302 315 315 GLY GLY B . n 
B 1 303 ILE 303 316 316 ILE ILE B . n 
B 1 304 LEU 304 317 317 LEU LEU B . n 
B 1 305 ARG 305 318 318 ARG ARG B . n 
B 1 306 ARG 306 319 319 ARG ARG B . n 
B 1 307 ASN 307 320 320 ASN ASN B . n 
B 1 308 LEU 308 321 321 LEU LEU B . n 
B 1 309 ILE 309 322 322 ILE ILE B . n 
B 1 310 LYS 310 323 323 LYS LYS B . n 
B 1 311 ASN 311 324 324 ASN ASN B . n 
B 1 312 LEU 312 325 325 LEU LEU B . n 
B 1 313 HIS 313 326 326 HIS HIS B . n 
B 1 314 TYR 314 327 327 TYR TYR B . n 
B 1 315 TRP 315 328 328 TRP TRP B . n 
B 1 316 TRP 316 329 329 TRP TRP B . n 
B 1 317 THR 317 330 330 THR THR B . n 
B 1 318 GLY 318 331 331 GLY GLY B . n 
B 1 319 VAL 319 332 332 VAL VAL B . n 
B 1 320 ASN 320 333 333 ASN ASN B . n 
B 1 321 VAL 321 334 334 VAL VAL B . n 
B 1 322 ALA 322 335 335 ALA ALA B . n 
B 1 323 PHE 323 336 336 PHE PHE B . n 
B 1 324 GLY 324 337 337 GLY GLY B . n 
B 1 325 GLY 325 338 338 GLY GLY B . n 
B 1 326 CYS 326 339 339 CYS CYS B . n 
B 1 327 ASP 327 340 340 ASP ASP B . n 
B 1 328 GLU 328 341 341 GLU GLU B . n 
B 1 329 LEU 329 342 342 LEU LEU B . n 
B 1 330 PHE 330 343 343 PHE PHE B . n 
B 1 331 PRO 331 344 344 PRO PRO B . n 
B 1 332 TYR 332 345 345 TYR TYR B . n 
B 1 333 GLY 333 346 346 GLY GLY B . n 
B 1 334 GLN 334 347 347 GLN GLN B . n 
B 1 335 LEU 335 348 348 LEU LEU B . n 
C 1 1   GLN 1   14  14  GLN GLN C . n 
C 1 2   GLY 2   15  15  GLY GLY C . n 
C 1 3   VAL 3   16  16  VAL VAL C . n 
C 1 4   ASP 4   17  17  ASP ASP C . n 
C 1 5   PRO 5   18  18  PRO PRO C . n 
C 1 6   PRO 6   19  19  PRO PRO C . n 
C 1 7   PRO 7   20  20  PRO PRO C . n 
C 1 8   PRO 8   21  21  PRO PRO C . n 
C 1 9   PRO 9   22  22  PRO PRO C . n 
C 1 10  GLY 10  23  23  GLY GLY C . n 
C 1 11  PRO 11  24  24  PRO PRO C . n 
C 1 12  PRO 12  25  25  PRO PRO C . n 
C 1 13  SER 13  26  26  SER SER C . n 
C 1 14  PHE 14  27  27  PHE PHE C . n 
C 1 15  THR 15  28  28  THR THR C . n 
C 1 16  GLY 16  29  29  GLY GLY C . n 
C 1 17  THR 17  30  30  THR THR C . n 
C 1 18  LYS 18  31  31  LYS LYS C . n 
C 1 19  LEU 19  32  32  LEU LEU C . n 
C 1 20  VAL 20  33  33  VAL VAL C . n 
C 1 21  ASN 21  34  34  ASN ASN C . n 
C 1 22  ASP 22  35  35  ASP ASP C . n 
C 1 23  ALA 23  36  36  ALA ALA C . n 
C 1 24  ASP 24  37  37  ASP ASP C . n 
C 1 25  HIS 25  38  38  HIS HIS C . n 
C 1 26  PRO 26  39  39  PRO PRO C . n 
C 1 27  TRP 27  40  40  TRP TRP C . n 
C 1 28  GLN 28  41  41  GLN GLN C . n 
C 1 29  PRO 29  42  42  PRO PRO C . n 
C 1 30  LEU 30  43  43  LEU LEU C . n 
C 1 31  ARG 31  44  44  ARG ARG C . n 
C 1 32  GLU 32  45  45  GLU GLU C . n 
C 1 33  GLY 33  46  46  GLY GLY C . n 
C 1 34  ASP 34  47  47  ASP ASP C . n 
C 1 35  ILE 35  48  48  ILE ILE C . n 
C 1 36  ARG 36  49  49  ARG ARG C . n 
C 1 37  GLY 37  50  50  GLY GLY C . n 
C 1 38  PRO 38  51  51  PRO PRO C . n 
C 1 39  CYS 39  52  52  CYS CYS C . n 
C 1 40  PRO 40  53  53  PRO PRO C . n 
C 1 41  GLY 41  54  54  GLY GLY C . n 
C 1 42  LEU 42  55  55  LEU LEU C . n 
C 1 43  ASN 43  56  56  ASN ASN C . n 
C 1 44  THR 44  57  57  THR THR C . n 
C 1 45  LEU 45  58  58  LEU LEU C . n 
C 1 46  ALA 46  59  59  ALA ALA C . n 
C 1 47  SER 47  60  60  SER SER C . n 
C 1 48  HIS 48  61  61  HIS HIS C . n 
C 1 49  GLY 49  62  62  GLY GLY C . n 
C 1 50  TYR 50  63  63  TYR TYR C . n 
C 1 51  LEU 51  64  64  LEU LEU C . n 
C 1 52  PRO 52  65  65  PRO PRO C . n 
C 1 53  ARG 53  66  66  ARG ARG C . n 
C 1 54  ASP 54  67  67  ASP ASP C . n 
C 1 55  GLY 55  68  68  GLY GLY C . n 
C 1 56  VAL 56  69  69  VAL VAL C . n 
C 1 57  ALA 57  70  70  ALA ALA C . n 
C 1 58  THR 58  71  71  THR THR C . n 
C 1 59  PRO 59  72  72  PRO PRO C . n 
C 1 60  ALA 60  73  73  ALA ALA C . n 
C 1 61  GLN 61  74  74  GLN GLN C . n 
C 1 62  ILE 62  75  75  ILE ILE C . n 
C 1 63  ILE 63  76  76  ILE ILE C . n 
C 1 64  THR 64  77  77  THR THR C . n 
C 1 65  ALA 65  78  78  ALA ALA C . n 
C 1 66  THR 66  79  79  THR THR C . n 
C 1 67  GLN 67  80  80  GLN GLN C . n 
C 1 68  GLU 68  81  81  GLU GLU C . n 
C 1 69  GLY 69  82  82  GLY GLY C . n 
C 1 70  PHE 70  83  83  PHE PHE C . n 
C 1 71  ASN 71  84  84  ASN ASN C . n 
C 1 72  PHE 72  85  85  PHE PHE C . n 
C 1 73  GLU 73  86  86  GLU GLU C . n 
C 1 74  ASN 74  87  87  ASN ASN C . n 
C 1 75  ASN 75  88  88  ASN ASN C . n 
C 1 76  ALA 76  89  89  ALA ALA C . n 
C 1 77  ALA 77  90  90  ALA ALA C . n 
C 1 78  ILE 78  91  91  ILE ILE C . n 
C 1 79  VAL 79  92  92  VAL VAL C . n 
C 1 80  ALA 80  93  93  ALA ALA C . n 
C 1 81  THR 81  94  94  THR THR C . n 
C 1 82  TYR 82  95  95  TYR TYR C . n 
C 1 83  LEU 83  96  96  LEU LEU C . n 
C 1 84  GLY 84  97  97  GLY GLY C . n 
C 1 85  HIS 85  98  98  HIS HIS C . n 
C 1 86  LEU 86  99  99  LEU LEU C . n 
C 1 87  LEU 87  100 100 LEU LEU C . n 
C 1 88  ASN 88  101 101 ASN ASN C . n 
C 1 89  GLY 89  102 102 GLY GLY C . n 
C 1 90  ASN 90  103 103 ASN ASN C . n 
C 1 91  LEU 91  104 104 LEU LEU C . n 
C 1 92  VAL 92  105 105 VAL VAL C . n 
C 1 93  THR 93  106 106 THR THR C . n 
C 1 94  ASP 94  107 107 ASP ASP C . n 
C 1 95  LEU 95  108 108 LEU LEU C . n 
C 1 96  LEU 96  109 109 LEU LEU C . n 
C 1 97  SER 97  110 110 SER SER C . n 
C 1 98  ILE 98  111 111 ILE ILE C . n 
C 1 99  GLY 99  112 112 GLY GLY C . n 
C 1 100 GLY 100 113 113 GLY GLY C . n 
C 1 101 ALA 101 114 114 ALA ALA C . n 
C 1 102 THR 102 115 115 THR THR C . n 
C 1 103 PRO 103 116 116 PRO PRO C . n 
C 1 104 LYS 104 117 117 LYS LYS C . n 
C 1 105 THR 105 118 118 THR THR C . n 
C 1 106 GLY 106 119 119 GLY GLY C . n 
C 1 107 PRO 107 120 120 PRO PRO C . n 
C 1 108 PRO 108 121 121 PRO PRO C . n 
C 1 109 PRO 109 122 122 PRO PRO C . n 
C 1 110 PRO 110 123 123 PRO PRO C . n 
C 1 111 PRO 111 124 124 PRO PRO C . n 
C 1 112 PRO 112 125 125 PRO PRO C . n 
C 1 113 ALA 113 126 126 ALA ALA C . n 
C 1 114 HIS 114 127 127 HIS HIS C . n 
C 1 115 ALA 115 128 128 ALA ALA C . n 
C 1 116 GLY 116 129 129 GLY GLY C . n 
C 1 117 GLY 117 130 130 GLY GLY C . n 
C 1 118 LEU 118 131 131 LEU LEU C . n 
C 1 119 ASN 119 132 132 ASN ASN C . n 
C 1 120 VAL 120 133 133 VAL VAL C . n 
C 1 121 HIS 121 134 134 HIS HIS C . n 
C 1 122 GLY 122 135 135 GLY GLY C . n 
C 1 123 THR 123 136 136 THR THR C . n 
C 1 124 PHE 124 137 137 PHE PHE C . n 
C 1 125 GLU 125 138 138 GLU GLU C . n 
C 1 126 GLY 126 139 139 GLY GLY C . n 
C 1 127 ASP 127 140 140 ASP ASP C . n 
C 1 128 ALA 128 141 141 ALA ALA C . n 
C 1 129 GLY 129 142 142 GLY GLY C . n 
C 1 130 MET 130 143 143 MET MET C . n 
C 1 131 THR 131 144 144 THR THR C . n 
C 1 132 ARG 132 145 145 ARG ARG C . n 
C 1 133 ALA 133 146 146 ALA ALA C . n 
C 1 134 ASP 134 147 147 ASP ASP C . n 
C 1 135 GLU 135 148 148 GLU GLU C . n 
C 1 136 PHE 136 149 149 PHE PHE C . n 
C 1 137 PHE 137 150 150 PHE PHE C . n 
C 1 138 GLY 138 151 151 GLY GLY C . n 
C 1 139 ASP 139 152 152 ASP ASP C . n 
C 1 140 ASN 140 153 153 ASN ASN C . n 
C 1 141 HIS 141 154 154 HIS HIS C . n 
C 1 142 SER 142 155 155 SER SER C . n 
C 1 143 PHE 143 156 156 PHE PHE C . n 
C 1 144 ASN 144 157 157 ASN ASN C . n 
C 1 145 GLN 145 158 158 GLN GLN C . n 
C 1 146 THR 146 159 159 THR THR C . n 
C 1 147 LEU 147 160 160 LEU LEU C . n 
C 1 148 PHE 148 161 161 PHE PHE C . n 
C 1 149 ASP 149 162 162 ASP ASP C . n 
C 1 150 LYS 150 163 163 LYS LYS C . n 
C 1 151 PHE 151 164 164 PHE PHE C . n 
C 1 152 VAL 152 165 165 VAL VAL C . n 
C 1 153 ASP 153 166 166 ASP ASP C . n 
C 1 154 PHE 154 167 167 PHE PHE C . n 
C 1 155 SER 155 168 168 SER SER C . n 
C 1 156 ASN 156 169 169 ASN ASN C . n 
C 1 157 ARG 157 170 170 ARG ARG C . n 
C 1 158 TYR 158 171 171 TYR TYR C . n 
C 1 159 GLY 159 172 172 GLY GLY C . n 
C 1 160 GLY 160 173 173 GLY GLY C . n 
C 1 161 GLY 161 174 174 GLY GLY C . n 
C 1 162 PHE 162 175 175 PHE PHE C . n 
C 1 163 TYR 163 176 176 TYR TYR C . n 
C 1 164 ASN 164 177 177 ASN ASN C . n 
C 1 165 LEU 165 178 178 LEU LEU C . n 
C 1 166 THR 166 179 179 THR THR C . n 
C 1 167 VAL 167 180 180 VAL VAL C . n 
C 1 168 ALA 168 181 181 ALA ALA C . n 
C 1 169 GLY 169 182 182 GLY GLY C . n 
C 1 170 GLU 170 183 183 GLU GLU C . n 
C 1 171 LEU 171 184 184 LEU LEU C . n 
C 1 172 ARG 172 185 185 ARG ARG C . n 
C 1 173 TYR 173 186 186 TYR TYR C . n 
C 1 174 SER 174 187 187 SER SER C . n 
C 1 175 ARG 175 188 188 ARG ARG C . n 
C 1 176 ILE 176 189 189 ILE ILE C . n 
C 1 177 GLN 177 190 190 GLN GLN C . n 
C 1 178 ASP 178 191 191 ASP ASP C . n 
C 1 179 SER 179 192 192 SER SER C . n 
C 1 180 ILE 180 193 193 ILE ILE C . n 
C 1 181 ALA 181 194 194 ALA ALA C . n 
C 1 182 THR 182 195 195 THR THR C . n 
C 1 183 ASN 183 196 196 ASN ASN C . n 
C 1 184 PRO 184 197 197 PRO PRO C . n 
C 1 185 GLU 185 198 198 GLU GLU C . n 
C 1 186 PHE 186 199 199 PHE PHE C . n 
C 1 187 GLN 187 200 200 GLN GLN C . n 
C 1 188 PHE 188 201 201 PHE PHE C . n 
C 1 189 LYS 189 202 202 LYS LYS C . n 
C 1 190 ASN 190 203 203 ASN ASN C . n 
C 1 191 VAL 191 204 204 VAL VAL C . n 
C 1 192 ARG 192 205 205 ARG ARG C . n 
C 1 193 PHE 193 206 206 PHE PHE C . n 
C 1 194 ILE 194 207 207 ILE ILE C . n 
C 1 195 THR 195 208 208 THR THR C . n 
C 1 196 ALA 196 209 209 ALA ALA C . n 
C 1 197 TYR 197 210 210 TYR TYR C . n 
C 1 198 GLY 198 211 211 GLY GLY C . n 
C 1 199 GLU 199 212 212 GLU GLU C . n 
C 1 200 THR 200 213 213 THR THR C . n 
C 1 201 VAL 201 214 214 VAL VAL C . n 
C 1 202 PHE 202 215 215 PHE PHE C . n 
C 1 203 PRO 203 216 216 PRO PRO C . n 
C 1 204 ILE 204 217 217 ILE ILE C . n 
C 1 205 ASN 205 218 218 ASN ASN C . n 
C 1 206 LEU 206 219 219 LEU LEU C . n 
C 1 207 PHE 207 220 220 PHE PHE C . n 
C 1 208 VAL 208 221 221 VAL VAL C . n 
C 1 209 ASP 209 222 222 ASP ASP C . n 
C 1 210 GLY 210 223 223 GLY GLY C . n 
C 1 211 ARG 211 224 224 ARG ARG C . n 
C 1 212 VAL 212 225 225 VAL VAL C . n 
C 1 213 THR 213 226 226 THR THR C . n 
C 1 214 THR 214 227 227 THR THR C . n 
C 1 215 ASP 215 228 228 ASP ASP C . n 
C 1 216 ARG 216 229 229 ARG ARG C . n 
C 1 217 LYS 217 230 230 LYS LYS C . n 
C 1 218 LEU 218 231 231 LEU LEU C . n 
C 1 219 SER 219 232 232 SER SER C . n 
C 1 220 MET 220 233 233 MET MET C . n 
C 1 221 GLU 221 234 234 GLU GLU C . n 
C 1 222 ASP 222 235 235 ASP ASP C . n 
C 1 223 ALA 223 236 236 ALA ALA C . n 
C 1 224 ALA 224 237 237 ALA ALA C . n 
C 1 225 SER 225 238 238 SER SER C . n 
C 1 226 ILE 226 239 239 ILE ILE C . n 
C 1 227 PHE 227 240 240 PHE PHE C . n 
C 1 228 ARG 228 241 241 ARG ARG C . n 
C 1 229 ASP 229 242 242 ASP ASP C . n 
C 1 230 MET 230 243 243 MET MET C . n 
C 1 231 ARG 231 244 244 ARG ARG C . n 
C 1 232 PHE 232 245 245 PHE PHE C . n 
C 1 233 PRO 233 246 246 PRO PRO C . n 
C 1 234 ASP 234 247 247 ASP ASP C . n 
C 1 235 ASP 235 248 248 ASP ASP C . n 
C 1 236 PHE 236 249 249 PHE PHE C . n 
C 1 237 HIS 237 250 250 HIS HIS C . n 
C 1 238 ARG 238 251 251 ARG ARG C . n 
C 1 239 SER 239 252 252 SER SER C . n 
C 1 240 ALA 240 253 253 ALA ALA C . n 
C 1 241 VAL 241 254 254 VAL VAL C . n 
C 1 242 PRO 242 255 255 PRO PRO C . n 
C 1 243 ALA 243 256 256 ALA ALA C . n 
C 1 244 SER 244 257 257 SER SER C . n 
C 1 245 ASN 245 258 258 ASN ASN C . n 
C 1 246 GLU 246 259 259 GLU GLU C . n 
C 1 247 GLY 247 260 260 GLY GLY C . n 
C 1 248 ALA 248 261 261 ALA ALA C . n 
C 1 249 ASP 249 262 262 ASP ASP C . n 
C 1 250 GLN 250 263 263 GLN GLN C . n 
C 1 251 VAL 251 264 264 VAL VAL C . n 
C 1 252 LEU 252 265 265 LEU LEU C . n 
C 1 253 ALA 253 266 266 ALA ALA C . n 
C 1 254 ALA 254 267 267 ALA ALA C . n 
C 1 255 HIS 255 268 268 HIS HIS C . n 
C 1 256 PRO 256 269 269 PRO PRO C . n 
C 1 257 TRP 257 270 270 TRP TRP C . n 
C 1 258 VAL 258 271 271 VAL VAL C . n 
C 1 259 PRO 259 272 272 PRO PRO C . n 
C 1 260 GLY 260 273 273 GLY GLY C . n 
C 1 261 GLY 261 274 274 GLY GLY C . n 
C 1 262 ASN 262 275 275 ASN ASN C . n 
C 1 263 ALA 263 276 276 ALA ALA C . n 
C 1 264 ASP 264 277 277 ASP ASP C . n 
C 1 265 ASN 265 278 278 ASN ASN C . n 
C 1 266 GLN 266 279 279 GLN GLN C . n 
C 1 267 VAL 267 280 280 VAL VAL C . n 
C 1 268 ASN 268 281 281 ASN ASN C . n 
C 1 269 ASN 269 282 282 ASN ASN C . n 
C 1 270 TYR 270 283 283 TYR TYR C . n 
C 1 271 VAL 271 284 284 VAL VAL C . n 
C 1 272 GLU 272 285 285 GLU GLU C . n 
C 1 273 ASP 273 286 286 ASP ASP C . n 
C 1 274 PRO 274 287 287 PRO PRO C . n 
C 1 275 ASP 275 288 288 ASP ASP C . n 
C 1 276 SER 276 289 289 SER SER C . n 
C 1 277 ALA 277 290 290 ALA ALA C . n 
C 1 278 ASP 278 291 291 ASP ASP C . n 
C 1 279 PHE 279 292 292 PHE PHE C . n 
C 1 280 THR 280 293 293 THR THR C . n 
C 1 281 HIS 281 294 294 HIS HIS C . n 
C 1 282 LEU 282 295 295 LEU LEU C . n 
C 1 283 CYS 283 296 296 CYS CYS C . n 
C 1 284 ARG 284 297 297 ARG ARG C . n 
C 1 285 LEU 285 298 298 LEU LEU C . n 
C 1 286 TYR 286 299 299 TYR TYR C . n 
C 1 287 GLU 287 300 300 GLU GLU C . n 
C 1 288 PHE 288 301 301 PHE PHE C . n 
C 1 289 VAL 289 302 302 VAL VAL C . n 
C 1 290 VAL 290 303 303 VAL VAL C . n 
C 1 291 GLY 291 304 304 GLY GLY C . n 
C 1 292 SER 292 305 305 SER SER C . n 
C 1 293 VAL 293 306 306 VAL VAL C . n 
C 1 294 GLN 294 307 307 GLN GLN C . n 
C 1 295 GLU 295 308 308 GLU GLU C . n 
C 1 296 LEU 296 309 309 LEU LEU C . n 
C 1 297 TYR 297 310 310 TYR TYR C . n 
C 1 298 PRO 298 311 311 PRO PRO C . n 
C 1 299 ASN 299 312 312 ASN ASN C . n 
C 1 300 PRO 300 313 313 PRO PRO C . n 
C 1 301 THR 301 314 314 THR THR C . n 
C 1 302 GLY 302 315 315 GLY GLY C . n 
C 1 303 ILE 303 316 316 ILE ILE C . n 
C 1 304 LEU 304 317 317 LEU LEU C . n 
C 1 305 ARG 305 318 318 ARG ARG C . n 
C 1 306 ARG 306 319 319 ARG ARG C . n 
C 1 307 ASN 307 320 320 ASN ASN C . n 
C 1 308 LEU 308 321 321 LEU LEU C . n 
C 1 309 ILE 309 322 322 ILE ILE C . n 
C 1 310 LYS 310 323 323 LYS LYS C . n 
C 1 311 ASN 311 324 324 ASN ASN C . n 
C 1 312 LEU 312 325 325 LEU LEU C . n 
C 1 313 HIS 313 326 326 HIS HIS C . n 
C 1 314 TYR 314 327 327 TYR TYR C . n 
C 1 315 TRP 315 328 328 TRP TRP C . n 
C 1 316 TRP 316 329 329 TRP TRP C . n 
C 1 317 THR 317 330 330 THR THR C . n 
C 1 318 GLY 318 331 331 GLY GLY C . n 
C 1 319 VAL 319 332 332 VAL VAL C . n 
C 1 320 ASN 320 333 333 ASN ASN C . n 
C 1 321 VAL 321 334 334 VAL VAL C . n 
C 1 322 ALA 322 335 335 ALA ALA C . n 
C 1 323 PHE 323 336 336 PHE PHE C . n 
C 1 324 GLY 324 337 337 GLY GLY C . n 
C 1 325 GLY 325 338 338 GLY GLY C . n 
C 1 326 CYS 326 339 339 CYS CYS C . n 
C 1 327 ASP 327 340 340 ASP ASP C . n 
C 1 328 GLU 328 341 341 GLU GLU C . n 
C 1 329 LEU 329 342 342 LEU LEU C . n 
C 1 330 PHE 330 343 343 PHE PHE C . n 
C 1 331 PRO 331 344 344 PRO PRO C . n 
C 1 332 TYR 332 345 345 TYR TYR C . n 
C 1 333 GLY 333 346 346 GLY GLY C . n 
C 1 334 GLN 334 347 347 GLN GLN C . n 
C 1 335 LEU 335 348 348 LEU LEU C . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
D 2 NAG 1 G NAG 1 A NAG 402 n 
D 2 NAG 2 G NAG 2 A NAG 403 n 
D 2 BMA 3 G BMA 3 A BMA 425 n 
D 2 MAN 4 G MAN 4 A MAN 427 n 
D 2 MAN 5 G MAN 5 A MAN 426 n 
E 3 NAG 1 I NAG 1 A NAG 404 n 
E 3 NAG 2 I NAG 2 A NAG 405 n 
E 3 BMA 3 I BMA 3 A BMA 406 n 
E 3 MAN 4 I MAN 4 A MAN 407 n 
E 3 MAN 5 I MAN 5 A MAN 408 n 
E 3 MAN 6 I MAN 6 A MAN 409 n 
E 3 MAN 7 I MAN 7 A MAN 414 n 
F 4 NAG 1 W NAG 1 B NAG 402 n 
F 4 NAG 2 W NAG 2 B NAG 413 n 
F 4 BMA 3 W BMA 3 B BMA 416 n 
G 5 NAG 1 X NAG 1 B NAG 404 n 
G 5 NAG 2 X NAG 2 B NAG 405 n 
G 5 BMA 3 X BMA 3 B BMA 406 n 
G 5 MAN 4 X MAN 4 B MAN 408 n 
G 5 MAN 5 X MAN 5 B MAN 409 n 
G 5 MAN 6 X MAN 6 B MAN 407 n 
H 6 NAG 1 j NAG 1 C NAG 402 n 
H 6 NAG 2 j NAG 2 C NAG 403 n 
H 6 BMA 3 j BMA 3 C BMA 407 n 
H 6 MAN 4 j MAN 4 C MAN 411 n 
I 4 NAG 1 l NAG 1 C NAG 404 n 
I 4 NAG 2 l NAG 2 C NAG 405 n 
I 4 BMA 3 l BMA 3 C BMA 406 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1IUB ? ? A1IUB ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HEM   ? ? HEM   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
J  7  A1IUB 1   401 428 A1IUB INI A . 
K  7  A1IUB 1   402 429 A1IUB INI A . 
L  8  GOL   1   403 430 GOL   GOL A . 
M  9  HEM   1   404 431 HEM   HEM A . 
N  10 MG    1   405 1   MG    MG  A . 
O  11 SO4   1   406 1   SO4   SO4 A . 
P  7  A1IUB 1   401 417 A1IUB INI B . 
Q  8  GOL   1   402 418 GOL   GOL B . 
R  12 ACT   1   403 419 ACT   ACT B . 
S  9  HEM   1   404 420 HEM   HEM B . 
T  10 MG    1   405 2   MG    MG  B . 
U  11 SO4   1   406 2   SO4   SO4 B . 
V  7  A1IUB 1   401 412 A1IUB INI C . 
W  8  GOL   1   402 413 GOL   GOL C . 
X  7  A1IUB 1   403 414 A1IUB INI C . 
Y  9  HEM   1   404 415 HEM   HEM C . 
Z  10 MG    1   405 3   MG    MG  C . 
AA 11 SO4   1   406 3   SO4   SO4 C . 
BA 13 HOH   1   501 436 HOH   HOH A . 
BA 13 HOH   2   502 470 HOH   HOH A . 
BA 13 HOH   3   503 329 HOH   HOH A . 
BA 13 HOH   4   504 306 HOH   HOH A . 
BA 13 HOH   5   505 248 HOH   HOH A . 
BA 13 HOH   6   506 289 HOH   HOH A . 
BA 13 HOH   7   507 549 HOH   HOH A . 
BA 13 HOH   8   508 435 HOH   HOH A . 
BA 13 HOH   9   509 345 HOH   HOH A . 
BA 13 HOH   10  510 62  HOH   HOH A . 
BA 13 HOH   11  511 466 HOH   HOH A . 
BA 13 HOH   12  512 426 HOH   HOH A . 
BA 13 HOH   13  513 32  HOH   HOH A . 
BA 13 HOH   14  514 250 HOH   HOH A . 
BA 13 HOH   15  515 454 HOH   HOH A . 
BA 13 HOH   16  516 170 HOH   HOH A . 
BA 13 HOH   17  517 87  HOH   HOH A . 
BA 13 HOH   18  518 471 HOH   HOH A . 
BA 13 HOH   19  519 552 HOH   HOH A . 
BA 13 HOH   20  520 24  HOH   HOH A . 
BA 13 HOH   21  521 6   HOH   HOH A . 
BA 13 HOH   22  522 80  HOH   HOH A . 
BA 13 HOH   23  523 152 HOH   HOH A . 
BA 13 HOH   24  524 179 HOH   HOH A . 
BA 13 HOH   25  525 309 HOH   HOH A . 
BA 13 HOH   26  526 467 HOH   HOH A . 
BA 13 HOH   27  527 366 HOH   HOH A . 
BA 13 HOH   28  528 172 HOH   HOH A . 
BA 13 HOH   29  529 211 HOH   HOH A . 
BA 13 HOH   30  530 15  HOH   HOH A . 
BA 13 HOH   31  531 4   HOH   HOH A . 
BA 13 HOH   32  532 272 HOH   HOH A . 
BA 13 HOH   33  533 127 HOH   HOH A . 
BA 13 HOH   34  534 194 HOH   HOH A . 
BA 13 HOH   35  535 427 HOH   HOH A . 
BA 13 HOH   36  536 166 HOH   HOH A . 
BA 13 HOH   37  537 42  HOH   HOH A . 
BA 13 HOH   38  538 153 HOH   HOH A . 
BA 13 HOH   39  539 148 HOH   HOH A . 
BA 13 HOH   40  540 3   HOH   HOH A . 
BA 13 HOH   41  541 176 HOH   HOH A . 
BA 13 HOH   42  542 108 HOH   HOH A . 
BA 13 HOH   43  543 175 HOH   HOH A . 
BA 13 HOH   44  544 96  HOH   HOH A . 
BA 13 HOH   45  545 201 HOH   HOH A . 
BA 13 HOH   46  546 22  HOH   HOH A . 
BA 13 HOH   47  547 137 HOH   HOH A . 
BA 13 HOH   48  548 188 HOH   HOH A . 
BA 13 HOH   49  549 300 HOH   HOH A . 
BA 13 HOH   50  550 29  HOH   HOH A . 
BA 13 HOH   51  551 9   HOH   HOH A . 
BA 13 HOH   52  552 273 HOH   HOH A . 
BA 13 HOH   53  553 122 HOH   HOH A . 
BA 13 HOH   54  554 90  HOH   HOH A . 
BA 13 HOH   55  555 534 HOH   HOH A . 
BA 13 HOH   56  556 50  HOH   HOH A . 
BA 13 HOH   57  557 126 HOH   HOH A . 
BA 13 HOH   58  558 310 HOH   HOH A . 
BA 13 HOH   59  559 419 HOH   HOH A . 
BA 13 HOH   60  560 540 HOH   HOH A . 
BA 13 HOH   61  561 219 HOH   HOH A . 
BA 13 HOH   62  562 344 HOH   HOH A . 
BA 13 HOH   63  563 5   HOH   HOH A . 
BA 13 HOH   64  564 452 HOH   HOH A . 
BA 13 HOH   65  565 75  HOH   HOH A . 
BA 13 HOH   66  566 316 HOH   HOH A . 
BA 13 HOH   67  567 16  HOH   HOH A . 
BA 13 HOH   68  568 88  HOH   HOH A . 
BA 13 HOH   69  569 330 HOH   HOH A . 
BA 13 HOH   70  570 18  HOH   HOH A . 
BA 13 HOH   71  571 113 HOH   HOH A . 
BA 13 HOH   72  572 52  HOH   HOH A . 
BA 13 HOH   73  573 328 HOH   HOH A . 
BA 13 HOH   74  574 537 HOH   HOH A . 
BA 13 HOH   75  575 225 HOH   HOH A . 
BA 13 HOH   76  576 65  HOH   HOH A . 
BA 13 HOH   77  577 379 HOH   HOH A . 
BA 13 HOH   78  578 324 HOH   HOH A . 
BA 13 HOH   79  579 44  HOH   HOH A . 
BA 13 HOH   80  580 222 HOH   HOH A . 
BA 13 HOH   81  581 440 HOH   HOH A . 
BA 13 HOH   82  582 71  HOH   HOH A . 
BA 13 HOH   83  583 548 HOH   HOH A . 
BA 13 HOH   84  584 157 HOH   HOH A . 
BA 13 HOH   85  585 339 HOH   HOH A . 
BA 13 HOH   86  586 247 HOH   HOH A . 
BA 13 HOH   87  587 132 HOH   HOH A . 
BA 13 HOH   88  588 541 HOH   HOH A . 
BA 13 HOH   89  589 25  HOH   HOH A . 
BA 13 HOH   90  590 27  HOH   HOH A . 
BA 13 HOH   91  591 523 HOH   HOH A . 
BA 13 HOH   92  592 313 HOH   HOH A . 
BA 13 HOH   93  593 294 HOH   HOH A . 
BA 13 HOH   94  594 295 HOH   HOH A . 
BA 13 HOH   95  595 516 HOH   HOH A . 
BA 13 HOH   96  596 296 HOH   HOH A . 
BA 13 HOH   97  597 543 HOH   HOH A . 
BA 13 HOH   98  598 317 HOH   HOH A . 
BA 13 HOH   99  599 279 HOH   HOH A . 
BA 13 HOH   100 600 237 HOH   HOH A . 
BA 13 HOH   101 601 84  HOH   HOH A . 
BA 13 HOH   102 602 214 HOH   HOH A . 
BA 13 HOH   103 603 193 HOH   HOH A . 
BA 13 HOH   104 604 535 HOH   HOH A . 
BA 13 HOH   105 605 319 HOH   HOH A . 
BA 13 HOH   106 606 86  HOH   HOH A . 
BA 13 HOH   107 607 367 HOH   HOH A . 
BA 13 HOH   108 608 142 HOH   HOH A . 
BA 13 HOH   109 609 162 HOH   HOH A . 
BA 13 HOH   110 610 260 HOH   HOH A . 
BA 13 HOH   111 611 217 HOH   HOH A . 
BA 13 HOH   112 612 51  HOH   HOH A . 
BA 13 HOH   113 613 101 HOH   HOH A . 
BA 13 HOH   114 614 311 HOH   HOH A . 
BA 13 HOH   115 615 423 HOH   HOH A . 
BA 13 HOH   116 616 228 HOH   HOH A . 
BA 13 HOH   117 617 437 HOH   HOH A . 
BA 13 HOH   118 618 439 HOH   HOH A . 
BA 13 HOH   119 619 232 HOH   HOH A . 
BA 13 HOH   120 620 386 HOH   HOH A . 
BA 13 HOH   121 621 533 HOH   HOH A . 
BA 13 HOH   122 622 252 HOH   HOH A . 
BA 13 HOH   123 623 283 HOH   HOH A . 
BA 13 HOH   124 624 61  HOH   HOH A . 
BA 13 HOH   125 625 107 HOH   HOH A . 
BA 13 HOH   126 626 418 HOH   HOH A . 
BA 13 HOH   127 627 428 HOH   HOH A . 
BA 13 HOH   128 628 53  HOH   HOH A . 
BA 13 HOH   129 629 131 HOH   HOH A . 
BA 13 HOH   130 630 93  HOH   HOH A . 
BA 13 HOH   131 631 215 HOH   HOH A . 
BA 13 HOH   132 632 517 HOH   HOH A . 
BA 13 HOH   133 633 463 HOH   HOH A . 
BA 13 HOH   134 634 218 HOH   HOH A . 
BA 13 HOH   135 635 151 HOH   HOH A . 
BA 13 HOH   136 636 229 HOH   HOH A . 
BA 13 HOH   137 637 338 HOH   HOH A . 
BA 13 HOH   138 638 59  HOH   HOH A . 
BA 13 HOH   139 639 461 HOH   HOH A . 
BA 13 HOH   140 640 160 HOH   HOH A . 
BA 13 HOH   141 641 251 HOH   HOH A . 
BA 13 HOH   142 642 253 HOH   HOH A . 
BA 13 HOH   143 643 110 HOH   HOH A . 
BA 13 HOH   144 644 78  HOH   HOH A . 
BA 13 HOH   145 645 171 HOH   HOH A . 
BA 13 HOH   146 646 13  HOH   HOH A . 
BA 13 HOH   147 647 464 HOH   HOH A . 
BA 13 HOH   148 648 318 HOH   HOH A . 
BA 13 HOH   149 649 206 HOH   HOH A . 
BA 13 HOH   150 650 207 HOH   HOH A . 
BA 13 HOH   151 651 278 HOH   HOH A . 
BA 13 HOH   152 652 185 HOH   HOH A . 
BA 13 HOH   153 653 116 HOH   HOH A . 
BA 13 HOH   154 654 12  HOH   HOH A . 
BA 13 HOH   155 655 37  HOH   HOH A . 
BA 13 HOH   156 656 243 HOH   HOH A . 
BA 13 HOH   157 657 82  HOH   HOH A . 
BA 13 HOH   158 658 7   HOH   HOH A . 
BA 13 HOH   159 659 79  HOH   HOH A . 
BA 13 HOH   160 660 460 HOH   HOH A . 
BA 13 HOH   161 661 518 HOH   HOH A . 
BA 13 HOH   162 662 364 HOH   HOH A . 
BA 13 HOH   163 663 532 HOH   HOH A . 
BA 13 HOH   164 664 312 HOH   HOH A . 
BA 13 HOH   165 665 187 HOH   HOH A . 
BA 13 HOH   166 666 528 HOH   HOH A . 
BA 13 HOH   167 667 544 HOH   HOH A . 
BA 13 HOH   168 668 240 HOH   HOH A . 
BA 13 HOH   169 669 550 HOH   HOH A . 
BA 13 HOH   170 670 342 HOH   HOH A . 
BA 13 HOH   171 671 195 HOH   HOH A . 
BA 13 HOH   172 672 41  HOH   HOH A . 
BA 13 HOH   173 673 337 HOH   HOH A . 
BA 13 HOH   174 674 336 HOH   HOH A . 
BA 13 HOH   175 675 231 HOH   HOH A . 
BA 13 HOH   176 676 315 HOH   HOH A . 
BA 13 HOH   177 677 274 HOH   HOH A . 
BA 13 HOH   178 678 261 HOH   HOH A . 
BA 13 HOH   179 679 21  HOH   HOH A . 
BA 13 HOH   180 680 8   HOH   HOH A . 
BA 13 HOH   181 681 472 HOH   HOH A . 
BA 13 HOH   182 682 462 HOH   HOH A . 
BA 13 HOH   183 683 465 HOH   HOH A . 
BA 13 HOH   184 684 422 HOH   HOH A . 
BA 13 HOH   185 685 270 HOH   HOH A . 
BA 13 HOH   186 686 269 HOH   HOH A . 
BA 13 HOH   187 687 469 HOH   HOH A . 
BA 13 HOH   188 688 438 HOH   HOH A . 
BA 13 HOH   189 689 291 HOH   HOH A . 
BA 13 HOH   190 690 275 HOH   HOH A . 
BA 13 HOH   191 691 276 HOH   HOH A . 
BA 13 HOH   192 692 267 HOH   HOH A . 
BA 13 HOH   193 693 365 HOH   HOH A . 
BA 13 HOH   194 694 325 HOH   HOH A . 
BA 13 HOH   195 695 298 HOH   HOH A . 
BA 13 HOH   196 696 299 HOH   HOH A . 
BA 13 HOH   197 697 321 HOH   HOH A . 
BA 13 HOH   198 698 36  HOH   HOH A . 
BA 13 HOH   199 699 530 HOH   HOH A . 
BA 13 HOH   200 700 522 HOH   HOH A . 
BA 13 HOH   201 701 553 HOH   HOH A . 
BA 13 HOH   202 702 281 HOH   HOH A . 
BA 13 HOH   203 703 529 HOH   HOH A . 
BA 13 HOH   204 704 340 HOH   HOH A . 
BA 13 HOH   205 705 314 HOH   HOH A . 
BA 13 HOH   206 706 322 HOH   HOH A . 
BA 13 HOH   207 707 468 HOH   HOH A . 
BA 13 HOH   208 708 286 HOH   HOH A . 
BA 13 HOH   209 709 199 HOH   HOH A . 
BA 13 HOH   210 710 301 HOH   HOH A . 
BA 13 HOH   211 711 459 HOH   HOH A . 
BA 13 HOH   212 712 326 HOH   HOH A . 
BA 13 HOH   213 713 455 HOH   HOH A . 
BA 13 HOH   214 714 287 HOH   HOH A . 
BA 13 HOH   215 715 512 HOH   HOH A . 
BA 13 HOH   216 716 385 HOH   HOH A . 
BA 13 HOH   217 717 431 HOH   HOH A . 
BA 13 HOH   218 718 327 HOH   HOH A . 
BA 13 HOH   219 719 473 HOH   HOH A . 
BA 13 HOH   220 720 542 HOH   HOH A . 
BA 13 HOH   221 721 288 HOH   HOH A . 
BA 13 HOH   222 722 277 HOH   HOH A . 
BA 13 HOH   223 723 416 HOH   HOH A . 
BA 13 HOH   224 724 308 HOH   HOH A . 
BA 13 HOH   225 725 531 HOH   HOH A . 
BA 13 HOH   226 726 536 HOH   HOH A . 
BA 13 HOH   227 727 129 HOH   HOH A . 
BA 13 HOH   228 728 335 HOH   HOH A . 
BA 13 HOH   229 729 545 HOH   HOH A . 
BA 13 HOH   230 730 302 HOH   HOH A . 
BA 13 HOH   231 731 213 HOH   HOH A . 
BA 13 HOH   232 732 280 HOH   HOH A . 
BA 13 HOH   233 733 341 HOH   HOH A . 
BA 13 HOH   234 734 547 HOH   HOH A . 
BA 13 HOH   235 735 451 HOH   HOH A . 
BA 13 HOH   236 736 263 HOH   HOH A . 
BA 13 HOH   237 737 453 HOH   HOH A . 
BA 13 HOH   238 738 333 HOH   HOH A . 
BA 13 HOH   239 739 271 HOH   HOH A . 
BA 13 HOH   240 740 268 HOH   HOH A . 
BA 13 HOH   241 741 265 HOH   HOH A . 
BA 13 HOH   242 742 457 HOH   HOH A . 
BA 13 HOH   243 743 307 HOH   HOH A . 
BA 13 HOH   244 744 514 HOH   HOH A . 
BA 13 HOH   245 745 290 HOH   HOH A . 
BA 13 HOH   246 746 515 HOH   HOH A . 
BA 13 HOH   247 747 456 HOH   HOH A . 
BA 13 HOH   248 748 334 HOH   HOH A . 
BA 13 HOH   249 749 546 HOH   HOH A . 
BA 13 HOH   250 750 282 HOH   HOH A . 
BA 13 HOH   251 751 521 HOH   HOH A . 
BA 13 HOH   252 752 415 HOH   HOH A . 
BA 13 HOH   253 753 47  HOH   HOH A . 
CA 13 HOH   1   501 370 HOH   HOH B . 
CA 13 HOH   2   502 479 HOH   HOH B . 
CA 13 HOH   3   503 49  HOH   HOH B . 
CA 13 HOH   4   504 203 HOH   HOH B . 
CA 13 HOH   5   505 425 HOH   HOH B . 
CA 13 HOH   6   506 347 HOH   HOH B . 
CA 13 HOH   7   507 102 HOH   HOH B . 
CA 13 HOH   8   508 362 HOH   HOH B . 
CA 13 HOH   9   509 89  HOH   HOH B . 
CA 13 HOH   10  510 85  HOH   HOH B . 
CA 13 HOH   11  511 351 HOH   HOH B . 
CA 13 HOH   12  512 241 HOH   HOH B . 
CA 13 HOH   13  513 64  HOH   HOH B . 
CA 13 HOH   14  514 433 HOH   HOH B . 
CA 13 HOH   15  515 212 HOH   HOH B . 
CA 13 HOH   16  516 475 HOH   HOH B . 
CA 13 HOH   17  517 35  HOH   HOH B . 
CA 13 HOH   18  518 103 HOH   HOH B . 
CA 13 HOH   19  519 140 HOH   HOH B . 
CA 13 HOH   20  520 56  HOH   HOH B . 
CA 13 HOH   21  521 139 HOH   HOH B . 
CA 13 HOH   22  522 104 HOH   HOH B . 
CA 13 HOH   23  523 354 HOH   HOH B . 
CA 13 HOH   24  524 230 HOH   HOH B . 
CA 13 HOH   25  525 204 HOH   HOH B . 
CA 13 HOH   26  526 198 HOH   HOH B . 
CA 13 HOH   27  527 10  HOH   HOH B . 
CA 13 HOH   28  528 447 HOH   HOH B . 
CA 13 HOH   29  529 434 HOH   HOH B . 
CA 13 HOH   30  530 81  HOH   HOH B . 
CA 13 HOH   31  531 360 HOH   HOH B . 
CA 13 HOH   32  532 346 HOH   HOH B . 
CA 13 HOH   33  533 74  HOH   HOH B . 
CA 13 HOH   34  534 178 HOH   HOH B . 
CA 13 HOH   35  535 117 HOH   HOH B . 
CA 13 HOH   36  536 39  HOH   HOH B . 
CA 13 HOH   37  537 429 HOH   HOH B . 
CA 13 HOH   38  538 496 HOH   HOH B . 
CA 13 HOH   39  539 525 HOH   HOH B . 
CA 13 HOH   40  540 476 HOH   HOH B . 
CA 13 HOH   41  541 177 HOH   HOH B . 
CA 13 HOH   42  542 554 HOH   HOH B . 
CA 13 HOH   43  543 332 HOH   HOH B . 
CA 13 HOH   44  544 76  HOH   HOH B . 
CA 13 HOH   45  545 432 HOH   HOH B . 
CA 13 HOH   46  546 120 HOH   HOH B . 
CA 13 HOH   47  547 164 HOH   HOH B . 
CA 13 HOH   48  548 111 HOH   HOH B . 
CA 13 HOH   49  549 180 HOH   HOH B . 
CA 13 HOH   50  550 359 HOH   HOH B . 
CA 13 HOH   51  551 169 HOH   HOH B . 
CA 13 HOH   52  552 34  HOH   HOH B . 
CA 13 HOH   53  553 363 HOH   HOH B . 
CA 13 HOH   54  554 11  HOH   HOH B . 
CA 13 HOH   55  555 376 HOH   HOH B . 
CA 13 HOH   56  556 106 HOH   HOH B . 
CA 13 HOH   57  557 200 HOH   HOH B . 
CA 13 HOH   58  558 105 HOH   HOH B . 
CA 13 HOH   59  559 68  HOH   HOH B . 
CA 13 HOH   60  560 94  HOH   HOH B . 
CA 13 HOH   61  561 145 HOH   HOH B . 
CA 13 HOH   62  562 189 HOH   HOH B . 
CA 13 HOH   63  563 478 HOH   HOH B . 
CA 13 HOH   64  564 163 HOH   HOH B . 
CA 13 HOH   65  565 477 HOH   HOH B . 
CA 13 HOH   66  566 449 HOH   HOH B . 
CA 13 HOH   67  567 352 HOH   HOH B . 
CA 13 HOH   68  568 92  HOH   HOH B . 
CA 13 HOH   69  569 353 HOH   HOH B . 
CA 13 HOH   70  570 494 HOH   HOH B . 
CA 13 HOH   71  571 146 HOH   HOH B . 
CA 13 HOH   72  572 382 HOH   HOH B . 
CA 13 HOH   73  573 197 HOH   HOH B . 
CA 13 HOH   74  574 257 HOH   HOH B . 
CA 13 HOH   75  575 72  HOH   HOH B . 
CA 13 HOH   76  576 119 HOH   HOH B . 
CA 13 HOH   77  577 520 HOH   HOH B . 
CA 13 HOH   78  578 99  HOH   HOH B . 
CA 13 HOH   79  579 355 HOH   HOH B . 
CA 13 HOH   80  580 242 HOH   HOH B . 
CA 13 HOH   81  581 256 HOH   HOH B . 
CA 13 HOH   82  582 220 HOH   HOH B . 
CA 13 HOH   83  583 208 HOH   HOH B . 
CA 13 HOH   84  584 77  HOH   HOH B . 
CA 13 HOH   85  585 57  HOH   HOH B . 
CA 13 HOH   86  586 109 HOH   HOH B . 
CA 13 HOH   87  587 143 HOH   HOH B . 
CA 13 HOH   88  588 216 HOH   HOH B . 
CA 13 HOH   89  589 371 HOH   HOH B . 
CA 13 HOH   90  590 30  HOH   HOH B . 
CA 13 HOH   91  591 155 HOH   HOH B . 
CA 13 HOH   92  592 555 HOH   HOH B . 
CA 13 HOH   93  593 98  HOH   HOH B . 
CA 13 HOH   94  594 444 HOH   HOH B . 
CA 13 HOH   95  595 128 HOH   HOH B . 
CA 13 HOH   96  596 246 HOH   HOH B . 
CA 13 HOH   97  597 174 HOH   HOH B . 
CA 13 HOH   98  598 375 HOH   HOH B . 
CA 13 HOH   99  599 235 HOH   HOH B . 
CA 13 HOH   100 600 480 HOH   HOH B . 
CA 13 HOH   101 601 14  HOH   HOH B . 
CA 13 HOH   102 602 70  HOH   HOH B . 
CA 13 HOH   103 603 69  HOH   HOH B . 
CA 13 HOH   104 604 258 HOH   HOH B . 
CA 13 HOH   105 605 125 HOH   HOH B . 
CA 13 HOH   106 606 481 HOH   HOH B . 
CA 13 HOH   107 607 249 HOH   HOH B . 
CA 13 HOH   108 608 538 HOH   HOH B . 
CA 13 HOH   109 609 293 HOH   HOH B . 
CA 13 HOH   110 610 133 HOH   HOH B . 
CA 13 HOH   111 611 369 HOH   HOH B . 
CA 13 HOH   112 612 556 HOH   HOH B . 
CA 13 HOH   113 613 20  HOH   HOH B . 
CA 13 HOH   114 614 383 HOH   HOH B . 
CA 13 HOH   115 615 527 HOH   HOH B . 
CA 13 HOH   116 616 356 HOH   HOH B . 
CA 13 HOH   117 617 524 HOH   HOH B . 
CA 13 HOH   118 618 513 HOH   HOH B . 
CA 13 HOH   119 619 358 HOH   HOH B . 
CA 13 HOH   120 620 357 HOH   HOH B . 
CA 13 HOH   121 621 377 HOH   HOH B . 
CA 13 HOH   122 622 560 HOH   HOH B . 
CA 13 HOH   123 623 121 HOH   HOH B . 
CA 13 HOH   124 624 343 HOH   HOH B . 
CA 13 HOH   125 625 181 HOH   HOH B . 
CA 13 HOH   126 626 446 HOH   HOH B . 
CA 13 HOH   127 627 38  HOH   HOH B . 
CA 13 HOH   128 628 368 HOH   HOH B . 
CA 13 HOH   129 629 348 HOH   HOH B . 
CA 13 HOH   130 630 266 HOH   HOH B . 
CA 13 HOH   131 631 445 HOH   HOH B . 
CA 13 HOH   132 632 557 HOH   HOH B . 
CA 13 HOH   133 633 526 HOH   HOH B . 
CA 13 HOH   134 634 558 HOH   HOH B . 
CA 13 HOH   135 635 448 HOH   HOH B . 
CA 13 HOH   136 636 165 HOH   HOH B . 
CA 13 HOH   137 637 559 HOH   HOH B . 
CA 13 HOH   138 638 115 HOH   HOH B . 
CA 13 HOH   139 639 373 HOH   HOH B . 
CA 13 HOH   140 640 482 HOH   HOH B . 
CA 13 HOH   141 641 55  HOH   HOH B . 
CA 13 HOH   142 642 372 HOH   HOH B . 
CA 13 HOH   143 643 297 HOH   HOH B . 
CA 13 HOH   144 644 443 HOH   HOH B . 
CA 13 HOH   145 645 450 HOH   HOH B . 
CA 13 HOH   146 646 350 HOH   HOH B . 
CA 13 HOH   147 647 374 HOH   HOH B . 
CA 13 HOH   148 648 492 HOH   HOH B . 
CA 13 HOH   149 649 495 HOH   HOH B . 
CA 13 HOH   150 650 493 HOH   HOH B . 
CA 13 HOH   151 651 519 HOH   HOH B . 
CA 13 HOH   152 652 378 HOH   HOH B . 
CA 13 HOH   153 653 292 HOH   HOH B . 
CA 13 HOH   154 654 349 HOH   HOH B . 
DA 13 HOH   1   501 551 HOH   HOH C . 
DA 13 HOH   2   502 182 HOH   HOH C . 
DA 13 HOH   3   503 40  HOH   HOH C . 
DA 13 HOH   4   504 134 HOH   HOH C . 
DA 13 HOH   5   505 417 HOH   HOH C . 
DA 13 HOH   6   506 234 HOH   HOH C . 
DA 13 HOH   7   507 210 HOH   HOH C . 
DA 13 HOH   8   508 130 HOH   HOH C . 
DA 13 HOH   9   509 202 HOH   HOH C . 
DA 13 HOH   10  510 399 HOH   HOH C . 
DA 13 HOH   11  511 487 HOH   HOH C . 
DA 13 HOH   12  512 395 HOH   HOH C . 
DA 13 HOH   13  513 124 HOH   HOH C . 
DA 13 HOH   14  514 561 HOH   HOH C . 
DA 13 HOH   15  515 488 HOH   HOH C . 
DA 13 HOH   16  516 97  HOH   HOH C . 
DA 13 HOH   17  517 392 HOH   HOH C . 
DA 13 HOH   18  518 490 HOH   HOH C . 
DA 13 HOH   19  519 405 HOH   HOH C . 
DA 13 HOH   20  520 238 HOH   HOH C . 
DA 13 HOH   21  521 73  HOH   HOH C . 
DA 13 HOH   22  522 58  HOH   HOH C . 
DA 13 HOH   23  523 150 HOH   HOH C . 
DA 13 HOH   24  524 239 HOH   HOH C . 
DA 13 HOH   25  525 409 HOH   HOH C . 
DA 13 HOH   26  526 66  HOH   HOH C . 
DA 13 HOH   27  527 562 HOH   HOH C . 
DA 13 HOH   28  528 67  HOH   HOH C . 
DA 13 HOH   29  529 114 HOH   HOH C . 
DA 13 HOH   30  530 485 HOH   HOH C . 
DA 13 HOH   31  531 497 HOH   HOH C . 
DA 13 HOH   32  532 411 HOH   HOH C . 
DA 13 HOH   33  533 394 HOH   HOH C . 
DA 13 HOH   34  534 387 HOH   HOH C . 
DA 13 HOH   35  535 186 HOH   HOH C . 
DA 13 HOH   36  536 60  HOH   HOH C . 
DA 13 HOH   37  537 361 HOH   HOH C . 
DA 13 HOH   38  538 33  HOH   HOH C . 
DA 13 HOH   39  539 192 HOH   HOH C . 
DA 13 HOH   40  540 190 HOH   HOH C . 
DA 13 HOH   41  541 406 HOH   HOH C . 
DA 13 HOH   42  542 474 HOH   HOH C . 
DA 13 HOH   43  543 499 HOH   HOH C . 
DA 13 HOH   44  544 63  HOH   HOH C . 
DA 13 HOH   45  545 458 HOH   HOH C . 
DA 13 HOH   46  546 154 HOH   HOH C . 
DA 13 HOH   47  547 303 HOH   HOH C . 
DA 13 HOH   48  548 123 HOH   HOH C . 
DA 13 HOH   49  549 19  HOH   HOH C . 
DA 13 HOH   50  550 226 HOH   HOH C . 
DA 13 HOH   51  551 138 HOH   HOH C . 
DA 13 HOH   52  552 389 HOH   HOH C . 
DA 13 HOH   53  553 191 HOH   HOH C . 
DA 13 HOH   54  554 489 HOH   HOH C . 
DA 13 HOH   55  555 414 HOH   HOH C . 
DA 13 HOH   56  556 400 HOH   HOH C . 
DA 13 HOH   57  557 31  HOH   HOH C . 
DA 13 HOH   58  558 2   HOH   HOH C . 
DA 13 HOH   59  559 17  HOH   HOH C . 
DA 13 HOH   60  560 380 HOH   HOH C . 
DA 13 HOH   61  561 500 HOH   HOH C . 
DA 13 HOH   62  562 1   HOH   HOH C . 
DA 13 HOH   63  563 209 HOH   HOH C . 
DA 13 HOH   64  564 23  HOH   HOH C . 
DA 13 HOH   65  565 158 HOH   HOH C . 
DA 13 HOH   66  566 227 HOH   HOH C . 
DA 13 HOH   67  567 408 HOH   HOH C . 
DA 13 HOH   68  568 254 HOH   HOH C . 
DA 13 HOH   69  569 401 HOH   HOH C . 
DA 13 HOH   70  570 149 HOH   HOH C . 
DA 13 HOH   71  571 100 HOH   HOH C . 
DA 13 HOH   72  572 509 HOH   HOH C . 
DA 13 HOH   73  573 45  HOH   HOH C . 
DA 13 HOH   74  574 184 HOH   HOH C . 
DA 13 HOH   75  575 396 HOH   HOH C . 
DA 13 HOH   76  576 508 HOH   HOH C . 
DA 13 HOH   77  577 91  HOH   HOH C . 
DA 13 HOH   78  578 135 HOH   HOH C . 
DA 13 HOH   79  579 83  HOH   HOH C . 
DA 13 HOH   80  580 491 HOH   HOH C . 
DA 13 HOH   81  581 398 HOH   HOH C . 
DA 13 HOH   82  582 255 HOH   HOH C . 
DA 13 HOH   83  583 483 HOH   HOH C . 
DA 13 HOH   84  584 141 HOH   HOH C . 
DA 13 HOH   85  585 28  HOH   HOH C . 
DA 13 HOH   86  586 236 HOH   HOH C . 
DA 13 HOH   87  587 112 HOH   HOH C . 
DA 13 HOH   88  588 259 HOH   HOH C . 
DA 13 HOH   89  589 54  HOH   HOH C . 
DA 13 HOH   90  590 486 HOH   HOH C . 
DA 13 HOH   91  591 503 HOH   HOH C . 
DA 13 HOH   92  592 404 HOH   HOH C . 
DA 13 HOH   93  593 505 HOH   HOH C . 
DA 13 HOH   94  594 173 HOH   HOH C . 
DA 13 HOH   95  595 245 HOH   HOH C . 
DA 13 HOH   96  596 118 HOH   HOH C . 
DA 13 HOH   97  597 159 HOH   HOH C . 
DA 13 HOH   98  598 223 HOH   HOH C . 
DA 13 HOH   99  599 161 HOH   HOH C . 
DA 13 HOH   100 600 168 HOH   HOH C . 
DA 13 HOH   101 601 539 HOH   HOH C . 
DA 13 HOH   102 602 95  HOH   HOH C . 
DA 13 HOH   103 603 26  HOH   HOH C . 
DA 13 HOH   104 604 147 HOH   HOH C . 
DA 13 HOH   105 605 48  HOH   HOH C . 
DA 13 HOH   106 606 244 HOH   HOH C . 
DA 13 HOH   107 607 233 HOH   HOH C . 
DA 13 HOH   108 608 43  HOH   HOH C . 
DA 13 HOH   109 609 410 HOH   HOH C . 
DA 13 HOH   110 610 421 HOH   HOH C . 
DA 13 HOH   111 611 284 HOH   HOH C . 
DA 13 HOH   112 612 507 HOH   HOH C . 
DA 13 HOH   113 613 196 HOH   HOH C . 
DA 13 HOH   114 614 403 HOH   HOH C . 
DA 13 HOH   115 615 183 HOH   HOH C . 
DA 13 HOH   116 616 46  HOH   HOH C . 
DA 13 HOH   117 617 390 HOH   HOH C . 
DA 13 HOH   118 618 502 HOH   HOH C . 
DA 13 HOH   119 619 136 HOH   HOH C . 
DA 13 HOH   120 620 264 HOH   HOH C . 
DA 13 HOH   121 621 205 HOH   HOH C . 
DA 13 HOH   122 622 221 HOH   HOH C . 
DA 13 HOH   123 623 224 HOH   HOH C . 
DA 13 HOH   124 624 262 HOH   HOH C . 
DA 13 HOH   125 625 156 HOH   HOH C . 
DA 13 HOH   126 626 304 HOH   HOH C . 
DA 13 HOH   127 627 420 HOH   HOH C . 
DA 13 HOH   128 628 384 HOH   HOH C . 
DA 13 HOH   129 629 511 HOH   HOH C . 
DA 13 HOH   130 630 506 HOH   HOH C . 
DA 13 HOH   131 631 285 HOH   HOH C . 
DA 13 HOH   132 632 388 HOH   HOH C . 
DA 13 HOH   133 633 391 HOH   HOH C . 
DA 13 HOH   134 634 144 HOH   HOH C . 
DA 13 HOH   135 635 402 HOH   HOH C . 
DA 13 HOH   136 636 484 HOH   HOH C . 
DA 13 HOH   137 637 442 HOH   HOH C . 
DA 13 HOH   138 638 397 HOH   HOH C . 
DA 13 HOH   139 639 412 HOH   HOH C . 
DA 13 HOH   140 640 510 HOH   HOH C . 
DA 13 HOH   141 641 393 HOH   HOH C . 
DA 13 HOH   142 642 413 HOH   HOH C . 
DA 13 HOH   143 643 498 HOH   HOH C . 
DA 13 HOH   144 644 501 HOH   HOH C . 
DA 13 HOH   145 645 504 HOH   HOH C . 
DA 13 HOH   146 646 424 HOH   HOH C . 
DA 13 HOH   147 647 381 HOH   HOH C . 
DA 13 HOH   148 648 331 HOH   HOH C . 
DA 13 HOH   149 649 407 HOH   HOH C . 
DA 13 HOH   150 650 441 HOH   HOH C . 
DA 13 HOH   151 651 305 HOH   HOH C . 
DA 13 HOH   152 652 167 HOH   HOH C . 
DA 13 HOH   153 653 320 HOH   HOH C . 
DA 13 HOH   154 654 430 HOH   HOH C . 
DA 13 HOH   155 655 323 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ALA 146 ? CB ? A ALA 133 CB 
2 1 Y 1 B ALA 146 ? CB ? B ALA 133 CB 
3 1 Y 1 C ALA 146 ? CB ? C ALA 133 CB 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.06 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HEC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     270.969 
_cell.length_a_esd                 ? 
_cell.length_b                     75.050 
_cell.length_b_esd                 ? 
_cell.length_c                     106.056 
_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                         9HEC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 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                   9HEC 
_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             4.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.36 
_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    
;1.85M ammonium sulphate, 100 mM BisTris pH 6.5

Soaking: 20 mM alpha-ionone 7 hours, cryoprotected with 20% glycerol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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                      'KB MIRRORS' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-19 
_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                    M 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HEC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               49.19 
_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                                     508304 
_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                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.81 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.130 
_reflns.pdbx_Rpim_I_all                                0.056 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.116 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.20 
_reflns_shell.d_res_low                                     2.24 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             25289 
_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                               5.3 
_reflns_shell.pdbx_chi_squared                              0.51 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.972 
_reflns_shell.pdbx_Rpim_I_all                               0.407 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.898 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.881 
_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]                            -2.71 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.14 
_refine.aniso_B[2][2]                            4.15 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.17 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               43.290 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HEC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             49.19 
_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                     93809 
_refine.ls_number_reflns_R_free                  4833 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.21 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18395 
_refine.ls_R_factor_R_free                       0.21267 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18246 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.162 
_refine.pdbx_overall_ESU_R_Free                  0.149 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.110 
_refine.overall_SU_ML                            0.121 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        49.19 
_refine_hist.number_atoms_solvent             562 
_refine_hist.number_atoms_total               8918 
_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        8338 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  8776  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7740  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.525  1.842  12116 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.565  1.763  17880 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.427  5.000  1042  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.474  5.000  52    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.908 10.000 1130  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  1320  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  10497 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2111  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.635  4.215  4060  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.635  4.215  4060  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.326  7.562  5079  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.327  7.562  5080  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.969  5.103  4716  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.938  5.092  4702  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.521  9.160  6998  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.948  41.98  9999  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.970  41.80  9893  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.200 
_refine_ls_shell.d_res_low                        2.257 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             331 
_refine_ls_shell.number_reflns_R_work             6875 
_refine_ls_shell.percent_reflns_obs               97.73 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.290 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.321 
# 
_struct.entry_id                     9HEC 
_struct.title                        
'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II) in complex with alpha-ionone' 
_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        9HEC 
_struct_keywords.text            'Peroxygenase, peroxidase, complex, alpha-ionone, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 1  ? 
D  N N 2  ? 
E  N N 3  ? 
F  N N 4  ? 
G  N N 5  ? 
H  N N 6  ? 
I  N N 4  ? 
J  N N 7  ? 
K  N N 7  ? 
L  N N 8  ? 
M  N N 9  ? 
N  N N 10 ? 
O  N N 11 ? 
P  N N 7  ? 
Q  N N 8  ? 
R  N N 12 ? 
S  N N 9  ? 
T  N N 10 ? 
U  N N 11 ? 
V  N N 7  ? 
W  N N 8  ? 
X  N N 7  ? 
Y  N N 9  ? 
Z  N N 10 ? 
AA N N 11 ? 
BA N N 13 ? 
CA N N 13 ? 
DA N N 13 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A4V1Q376_9AGAR 
_struct_ref.pdbx_db_accession          A0A4V1Q376 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_struct_ref.pdbx_align_begin           52 
# 
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 9HEC A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HEC B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HEC C 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,J,K,L,M,N,O,BA  
2 1 B,F,G,P,Q,R,S,T,U,CA  
3 1 C,H,I,V,W,X,Y,Z,AA,DA 
# 
_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                PISA-monomeric 
# 
_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 CYS A 39  ? HIS A 48  ? CYS A 52  HIS A 61  1 ? 10 
HELX_P HELX_P2  AA2 THR A 58  ? ASN A 71  ? THR A 71  ASN A 84  1 ? 14 
HELX_P HELX_P3  AA3 GLU A 73  ? GLY A 89  ? GLU A 86  GLY A 102 1 ? 17 
HELX_P HELX_P4  AA4 THR A 102 ? GLY A 106 ? THR A 115 GLY A 119 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 134 ? GLY A 138 ? ASP A 147 GLY A 151 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 144 ? GLY A 159 ? ASN A 157 GLY A 172 1 ? 16 
HELX_P HELX_P7  AA7 ASN A 164 ? ASN A 183 ? ASN A 177 ASN A 196 1 ? 20 
HELX_P HELX_P8  AA8 LYS A 189 ? PHE A 207 ? LYS A 202 PHE A 220 1 ? 19 
HELX_P HELX_P9  AA9 SER A 219 ? ARG A 228 ? SER A 232 ARG A 241 1 ? 10 
HELX_P HELX_P10 AB1 GLY A 247 ? HIS A 255 ? GLY A 260 HIS A 268 1 ? 9  
HELX_P HELX_P11 AB2 LEU A 282 ? TYR A 297 ? LEU A 295 TYR A 310 1 ? 16 
HELX_P HELX_P12 AB3 THR A 301 ? PHE A 323 ? THR A 314 PHE A 336 1 ? 23 
HELX_P HELX_P13 AB4 CYS B 39  ? HIS B 48  ? CYS B 52  HIS B 61  1 ? 10 
HELX_P HELX_P14 AB5 THR B 58  ? ASN B 71  ? THR B 71  ASN B 84  1 ? 14 
HELX_P HELX_P15 AB6 GLU B 73  ? GLY B 89  ? GLU B 86  GLY B 102 1 ? 17 
HELX_P HELX_P16 AB7 THR B 102 ? GLY B 106 ? THR B 115 GLY B 119 5 ? 5  
HELX_P HELX_P17 AB8 ASP B 134 ? GLY B 138 ? ASP B 147 GLY B 151 5 ? 5  
HELX_P HELX_P18 AB9 ASN B 144 ? GLY B 159 ? ASN B 157 GLY B 172 1 ? 16 
HELX_P HELX_P19 AC1 ASN B 164 ? ASN B 183 ? ASN B 177 ASN B 196 1 ? 20 
HELX_P HELX_P20 AC2 LYS B 189 ? LEU B 206 ? LYS B 202 LEU B 219 1 ? 18 
HELX_P HELX_P21 AC3 SER B 219 ? ARG B 228 ? SER B 232 ARG B 241 1 ? 10 
HELX_P HELX_P22 AC4 GLY B 247 ? HIS B 255 ? GLY B 260 HIS B 268 1 ? 9  
HELX_P HELX_P23 AC5 LEU B 282 ? TYR B 297 ? LEU B 295 TYR B 310 1 ? 16 
HELX_P HELX_P24 AC6 THR B 301 ? PHE B 323 ? THR B 314 PHE B 336 1 ? 23 
HELX_P HELX_P25 AC7 CYS C 39  ? HIS C 48  ? CYS C 52  HIS C 61  1 ? 10 
HELX_P HELX_P26 AC8 THR C 58  ? ASN C 71  ? THR C 71  ASN C 84  1 ? 14 
HELX_P HELX_P27 AC9 GLU C 73  ? GLY C 89  ? GLU C 86  GLY C 102 1 ? 17 
HELX_P HELX_P28 AD1 THR C 102 ? GLY C 106 ? THR C 115 GLY C 119 5 ? 5  
HELX_P HELX_P29 AD2 ASP C 134 ? GLY C 138 ? ASP C 147 GLY C 151 5 ? 5  
HELX_P HELX_P30 AD3 ASN C 144 ? GLY C 159 ? ASN C 157 GLY C 172 1 ? 16 
HELX_P HELX_P31 AD4 ASN C 164 ? ASN C 183 ? ASN C 177 ASN C 196 1 ? 20 
HELX_P HELX_P32 AD5 LYS C 189 ? PHE C 207 ? LYS C 202 PHE C 220 1 ? 19 
HELX_P HELX_P33 AD6 SER C 219 ? ARG C 228 ? SER C 232 ARG C 241 1 ? 10 
HELX_P HELX_P34 AD7 GLY C 247 ? HIS C 255 ? GLY C 260 HIS C 268 1 ? 9  
HELX_P HELX_P35 AD8 LEU C 282 ? TYR C 297 ? LEU C 295 TYR C 310 1 ? 16 
HELX_P HELX_P36 AD9 THR C 301 ? PHE C 323 ? THR C 314 PHE C 336 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 283 SG  ? ? ? 1_555 A  CYS 326 SG ? ? A CYS 296 A CYS 339 1_555 ? ? ? ? ? ? ? 2.162 ? ?               
disulf2  disulf ?    ? B CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.145 ? ?               
disulf3  disulf ?    ? C CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.146 ? ?               
covale1  covale one  ? A ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 G NAG 1   1_555 ? ? ? ? ? ? ? 1.447 ? N-Glycosylation 
covale2  covale one  ? A ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 I NAG 1   1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale3  covale one  ? B ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 W NAG 1   1_555 ? ? ? ? ? ? ? 1.485 ? N-Glycosylation 
covale4  covale one  ? B ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 X NAG 1   1_555 ? ? ? ? ? ? ? 1.452 ? N-Glycosylation 
covale5  covale one  ? C ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 j NAG 1   1_555 ? ? ? ? ? ? ? 1.452 ? N-Glycosylation 
covale6  covale one  ? C ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 l NAG 1   1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale7  covale both ? D NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.398 ? ?               
covale8  covale both ? D NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ?               
covale9  covale both ? D BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale10 covale both ? D BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 5   1_555 ? ? ? ? ? ? ? 1.407 ? ?               
covale11 covale both ? E NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.389 ? ?               
covale12 covale both ? E NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? I NAG 2   I BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ?               
covale13 covale both ? E BMA .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 4   1_555 ? ? ? ? ? ? ? 1.409 ? ?               
covale14 covale both ? E BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 7   1_555 ? ? ? ? ? ? ? 1.399 ? ?               
covale15 covale both ? E MAN .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 5   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale16 covale both ? E MAN .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 6   1_555 ? ? ? ? ? ? ? 1.409 ? ?               
covale17 covale both ? F NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? W NAG 1   W NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale18 covale both ? F NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? W NAG 2   W BMA 3   1_555 ? ? ? ? ? ? ? 1.401 ? ?               
covale19 covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? X NAG 1   X NAG 2   1_555 ? ? ? ? ? ? ? 1.383 ? ?               
covale20 covale both ? G NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? X NAG 2   X BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ?               
covale21 covale both ? G BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? X BMA 3   X MAN 4   1_555 ? ? ? ? ? ? ? 1.404 ? ?               
covale22 covale both ? G BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? X BMA 3   X MAN 6   1_555 ? ? ? ? ? ? ? 1.399 ? ?               
covale23 covale both ? G MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? X MAN 4   X MAN 5   1_555 ? ? ? ? ? ? ? 1.399 ? ?               
covale24 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? j NAG 1   j NAG 2   1_555 ? ? ? ? ? ? ? 1.377 ? ?               
covale25 covale both ? H NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? j NAG 2   j BMA 3   1_555 ? ? ? ? ? ? ? 1.391 ? ?               
covale26 covale both ? H BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? j BMA 3   j MAN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale27 covale both ? I NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? l NAG 1   l NAG 2   1_555 ? ? ? ? ? ? ? 1.391 ? ?               
covale28 covale both ? I NAG .   O4  ? ? ? 1_555 I  BMA .   C1 ? ? l NAG 2   l BMA 3   1_555 ? ? ? ? ? ? ? 1.395 ? ?               
metalc1  metalc ?    ? A CYS 39  SG  ? ? ? 1_555 M  HEM .   FE ? ? A CYS 52  A HEM 404 1_555 ? ? ? ? ? ? ? 2.233 ? ?               
metalc2  metalc ?    ? A GLU 125 OE2 ? ? ? 1_555 N  MG  .   MG ? ? A GLU 138 A MG  405 1_555 ? ? ? ? ? ? ? 2.571 ? ?               
metalc3  metalc ?    ? A GLY 126 O   ? ? ? 1_555 N  MG  .   MG ? ? A GLY 139 A MG  405 1_555 ? ? ? ? ? ? ? 2.335 ? ?               
metalc4  metalc ?    ? M HEM .   O2A ? ? ? 1_555 N  MG  .   MG ? ? A HEM 404 A MG  405 1_555 ? ? ? ? ? ? ? 1.948 ? ?               
metalc5  metalc ?    ? N MG  .   MG  ? ? ? 1_555 BA HOH .   O  ? ? A MG  405 A HOH 516 1_555 ? ? ? ? ? ? ? 2.076 ? ?               
metalc6  metalc ?    ? N MG  .   MG  ? ? ? 1_555 BA HOH .   O  ? ? A MG  405 A HOH 598 1_555 ? ? ? ? ? ? ? 2.379 ? ?               
metalc7  metalc ?    ? B CYS 39  SG  ? ? ? 1_555 S  HEM .   FE ? ? B CYS 52  B HEM 404 1_555 ? ? ? ? ? ? ? 2.342 ? ?               
metalc8  metalc ?    ? B GLU 125 OE2 ? ? ? 1_555 T  MG  .   MG ? ? B GLU 138 B MG  405 1_555 ? ? ? ? ? ? ? 2.312 ? ?               
metalc9  metalc ?    ? B GLY 126 O   ? ? ? 1_555 T  MG  .   MG ? ? B GLY 139 B MG  405 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
metalc10 metalc ?    ? S HEM .   O1A ? ? ? 1_555 T  MG  .   MG ? ? B HEM 404 B MG  405 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
metalc11 metalc ?    ? T MG  .   MG  ? ? ? 1_555 CA HOH .   O  ? ? B MG  405 B HOH 531 1_555 ? ? ? ? ? ? ? 2.257 ? ?               
metalc12 metalc ?    ? T MG  .   MG  ? ? ? 1_555 CA HOH .   O  ? ? B MG  405 B HOH 573 1_555 ? ? ? ? ? ? ? 2.164 ? ?               
metalc13 metalc ?    ? C CYS 39  SG  ? ? ? 1_555 Y  HEM .   FE ? ? C CYS 52  C HEM 404 1_555 ? ? ? ? ? ? ? 2.289 ? ?               
metalc14 metalc ?    ? C GLU 125 OE2 ? ? ? 1_555 Z  MG  .   MG ? ? C GLU 138 C MG  405 1_555 ? ? ? ? ? ? ? 2.302 ? ?               
metalc15 metalc ?    ? C GLY 126 O   ? ? ? 1_555 Z  MG  .   MG ? ? C GLY 139 C MG  405 1_555 ? ? ? ? ? ? ? 2.209 ? ?               
metalc16 metalc ?    ? Y HEM .   O2A ? ? ? 1_555 Z  MG  .   MG ? ? C HEM 404 C MG  405 1_555 ? ? ? ? ? ? ? 2.246 ? ?               
metalc17 metalc ?    ? Z MG  .   MG  ? ? ? 1_555 DA HOH .   O  ? ? C MG  405 C HOH 537 1_555 ? ? ? ? ? ? ? 2.265 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NA  ? M  HEM .   ? A HEM 404 ? 1_555 101.5 ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NB  ? M  HEM .   ? A HEM 404 ? 1_555 92.3  ? 
3  NA  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NB  ? M  HEM .   ? A HEM 404 ? 1_555 87.1  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NC  ? M  HEM .   ? A HEM 404 ? 1_555 89.3  ? 
5  NA  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NC  ? M  HEM .   ? A HEM 404 ? 1_555 168.0 ? 
6  NB  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 NC  ? M  HEM .   ? A HEM 404 ? 1_555 87.3  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 ND  ? M  HEM .   ? A HEM 404 ? 1_555 97.5  ? 
8  NA  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 ND  ? M  HEM .   ? A HEM 404 ? 1_555 93.3  ? 
9  NB  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 ND  ? M  HEM .   ? A HEM 404 ? 1_555 169.9 ? 
10 NC  ? M  HEM .   ? A HEM 404 ? 1_555 FE ? M HEM . ? A HEM 404 ? 1_555 ND  ? M  HEM .   ? A HEM 404 ? 1_555 90.5  ? 
11 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 67.9  ? 
12 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O2A ? M  HEM .   ? A HEM 404 ? 1_555 81.2  ? 
13 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O2A ? M  HEM .   ? A HEM 404 ? 1_555 93.4  ? 
14 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 516 ? 1_555 74.4  ? 
15 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 516 ? 1_555 142.1 ? 
16 O2A ? M  HEM .   ? A HEM 404 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 516 ? 1_555 77.6  ? 
17 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 598 ? 1_555 71.5  ? 
18 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 598 ? 1_555 82.9  ? 
19 O2A ? M  HEM .   ? A HEM 404 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 598 ? 1_555 151.8 ? 
20 O   ? BA HOH .   ? A HOH 516 ? 1_555 MG ? N MG  . ? A MG  405 ? 1_555 O   ? BA HOH .   ? A HOH 598 ? 1_555 88.2  ? 
21 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NA  ? S  HEM .   ? B HEM 404 ? 1_555 98.3  ? 
22 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NB  ? S  HEM .   ? B HEM 404 ? 1_555 89.7  ? 
23 NA  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NB  ? S  HEM .   ? B HEM 404 ? 1_555 87.4  ? 
24 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NC  ? S  HEM .   ? B HEM 404 ? 1_555 90.2  ? 
25 NA  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NC  ? S  HEM .   ? B HEM 404 ? 1_555 170.4 ? 
26 NB  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 NC  ? S  HEM .   ? B HEM 404 ? 1_555 88.0  ? 
27 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 ND  ? S  HEM .   ? B HEM 404 ? 1_555 97.0  ? 
28 NA  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 ND  ? S  HEM .   ? B HEM 404 ? 1_555 92.5  ? 
29 NB  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 ND  ? S  HEM .   ? B HEM 404 ? 1_555 173.2 ? 
30 NC  ? S  HEM .   ? B HEM 404 ? 1_555 FE ? S HEM . ? B HEM 404 ? 1_555 ND  ? S  HEM .   ? B HEM 404 ? 1_555 91.0  ? 
31 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 78.0  ? 
32 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O1A ? S  HEM .   ? B HEM 404 ? 1_555 89.9  ? 
33 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O1A ? S  HEM .   ? B HEM 404 ? 1_555 98.8  ? 
34 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 531 ? 1_555 82.0  ? 
35 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 531 ? 1_555 159.4 ? 
36 O1A ? S  HEM .   ? B HEM 404 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 531 ? 1_555 76.1  ? 
37 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 573 ? 1_555 80.0  ? 
38 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 573 ? 1_555 93.7  ? 
39 O1A ? S  HEM .   ? B HEM 404 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 573 ? 1_555 162.0 ? 
40 O   ? CA HOH .   ? B HOH 531 ? 1_555 MG ? T MG  . ? B MG  405 ? 1_555 O   ? CA HOH .   ? B HOH 573 ? 1_555 87.6  ? 
41 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NA  ? Y  HEM .   ? C HEM 404 ? 1_555 100.1 ? 
42 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NB  ? Y  HEM .   ? C HEM 404 ? 1_555 88.0  ? 
43 NA  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NB  ? Y  HEM .   ? C HEM 404 ? 1_555 86.6  ? 
44 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NC  ? Y  HEM .   ? C HEM 404 ? 1_555 88.4  ? 
45 NA  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NC  ? Y  HEM .   ? C HEM 404 ? 1_555 169.6 ? 
46 NB  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 NC  ? Y  HEM .   ? C HEM 404 ? 1_555 87.6  ? 
47 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 ND  ? Y  HEM .   ? C HEM 404 ? 1_555 99.2  ? 
48 NA  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 ND  ? Y  HEM .   ? C HEM 404 ? 1_555 93.6  ? 
49 NB  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 ND  ? Y  HEM .   ? C HEM 404 ? 1_555 172.6 ? 
50 NC  ? Y  HEM .   ? C HEM 404 ? 1_555 FE ? Y HEM . ? C HEM 404 ? 1_555 ND  ? Y  HEM .   ? C HEM 404 ? 1_555 91.0  ? 
51 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 74.8  ? 
52 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O2A ? Y  HEM .   ? C HEM 404 ? 1_555 85.6  ? 
53 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O2A ? Y  HEM .   ? C HEM 404 ? 1_555 92.1  ? 
54 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O   ? DA HOH .   ? C HOH 537 ? 1_555 82.1  ? 
55 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O   ? DA HOH .   ? C HOH 537 ? 1_555 153.3 ? 
56 O2A ? Y  HEM .   ? C HEM 404 ? 1_555 MG ? Z MG  . ? C MG  405 ? 1_555 O   ? DA HOH .   ? C HOH 537 ? 1_555 72.7  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG D .   ? ASN A 144 ? NAG G 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG I 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG W 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG X 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG j 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG l 1   ? 1_555 ASN C 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 283 ? CYS A 326 ? CYS A 296 ? 1_555 CYS A 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 283 ? CYS B 326 ? CYS B 296 ? 1_555 CYS B 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS C 283 ? CYS C 326 ? CYS C 296 ? 1_555 CYS C 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 111 A . ? PRO 124 A PRO 112 A ? PRO 125 A 1 7.50 
2 PRO 111 B . ? PRO 124 B PRO 112 B ? PRO 125 B 1 6.39 
3 PRO 111 C . ? PRO 124 C PRO 112 C ? PRO 125 C 1 6.45 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 56  ? ALA A 57  ? VAL A 69  ALA A 70  
AA1 2 LEU A 96  ? SER A 97  ? LEU A 109 SER A 110 
AA2 1 GLN A 187 ? PHE A 188 ? GLN A 200 PHE A 201 
AA2 2 GLY A 260 ? ASN A 262 ? GLY A 273 ASN A 275 
AA2 3 TYR A 270 ? GLU A 272 ? TYR A 283 GLU A 285 
AA3 1 VAL B 56  ? ALA B 57  ? VAL B 69  ALA B 70  
AA3 2 LEU B 96  ? SER B 97  ? LEU B 109 SER B 110 
AA4 1 GLN B 187 ? PHE B 188 ? GLN B 200 PHE B 201 
AA4 2 GLY B 260 ? ASN B 262 ? GLY B 273 ASN B 275 
AA4 3 TYR B 270 ? GLU B 272 ? TYR B 283 GLU B 285 
AA5 1 VAL C 56  ? ALA C 57  ? VAL C 69  ALA C 70  
AA5 2 LEU C 96  ? SER C 97  ? LEU C 109 SER C 110 
AA6 1 GLN C 187 ? PHE C 188 ? GLN C 200 PHE C 201 
AA6 2 GLY C 260 ? ASN C 262 ? GLY C 273 ASN C 275 
AA6 3 TYR C 270 ? GLU C 272 ? TYR C 283 GLU C 285 
# 
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 ALA A 57  ? N ALA A 70  O LEU A 96  ? O LEU A 109 
AA2 1 2 N PHE A 188 ? N PHE A 201 O GLY A 260 ? O GLY A 273 
AA2 2 3 N GLY A 261 ? N GLY A 274 O VAL A 271 ? O VAL A 284 
AA3 1 2 N ALA B 57  ? N ALA B 70  O LEU B 96  ? O LEU B 109 
AA4 1 2 N PHE B 188 ? N PHE B 201 O GLY B 260 ? O GLY B 273 
AA4 2 3 N GLY B 261 ? N GLY B 274 O VAL B 271 ? O VAL B 284 
AA5 1 2 N ALA C 57  ? N ALA C 70  O LEU C 96  ? O LEU C 109 
AA6 1 2 N PHE C 188 ? N PHE C 201 O GLY C 260 ? O GLY C 273 
AA6 2 3 N GLY C 261 ? N GLY C 274 O VAL C 271 ? O VAL C 284 
# 
_pdbx_entry_details.entry_id                   9HEC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O11 A A1IUB 401 ? ? O A HOH 501 ? ? 2.04 
2 1 NH1 C ARG   318 ? B O C HOH 501 ? ? 2.08 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                124.30 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            4.00 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                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 HIS A 127 ? ? -138.76 -33.29  
2  1 PHE A 137 ? ? -105.86 -85.43  
3  1 ASN A 203 ? ? 52.72   -126.31 
4  1 SER A 257 ? ? -156.64 -94.88  
5  1 ASN A 282 ? ? -142.35 52.58   
6  1 HIS A 294 ? ? -140.12 56.02   
7  1 ASN A 312 ? ? -150.85 63.92   
8  1 HIS B 127 ? ? -137.97 -34.25  
9  1 PHE B 137 ? ? -103.32 -82.74  
10 1 ASN B 203 ? ? 53.32   -126.54 
11 1 SER B 257 ? ? -157.83 -94.36  
12 1 ASN B 282 ? ? -141.09 54.20   
13 1 ASN B 312 ? ? -150.62 65.34   
14 1 HIS C 127 ? ? -139.31 -34.73  
15 1 PHE C 137 ? ? -106.02 -86.40  
16 1 ASN C 203 ? ? 52.66   -127.23 
17 1 PRO C 246 ? ? -48.86  153.45  
18 1 SER C 257 ? ? -156.29 -94.54  
19 1 ASN C 282 ? ? -140.60 54.15   
20 1 ASN C 312 ? ? -153.50 60.45   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 752 ? 6.02 . 
2 1 O ? B HOH 653 ? 5.86 . 
3 1 O ? B HOH 654 ? 6.08 . 
# 
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 
A1IUB C2   C  N N 1   
A1IUB C4   C  N N 2   
A1IUB C5   C  N N 3   
A1IUB C6   C  N N 4   
A1IUB C8   C  N N 5   
A1IUB C9   C  N N 6   
A1IUB C10  C  N N 7   
A1IUB O11  O  N N 8   
A1IUB C12  C  N N 9   
A1IUB C1   C  N N 10  
A1IUB C3   C  N N 11  
A1IUB C7   C  N N 12  
A1IUB C13  C  N N 13  
A1IUB C14  C  N N 14  
A1IUB H2   H  N N 15  
A1IUB H3   H  N N 16  
A1IUB H4   H  N N 17  
A1IUB H5   H  N N 18  
A1IUB H6   H  N N 19  
A1IUB H7   H  N N 20  
A1IUB H8   H  N N 21  
A1IUB H9   H  N N 22  
A1IUB H10  H  N N 23  
A1IUB H11  H  N N 24  
A1IUB H12  H  N N 25  
A1IUB H13  H  N N 26  
A1IUB H14  H  N N 27  
A1IUB H16  H  N N 28  
A1IUB H17  H  N N 29  
A1IUB H18  H  N N 30  
A1IUB H19  H  N N 31  
A1IUB H20  H  N N 32  
A1IUB H21  H  N N 33  
A1IUB H22  H  N N 34  
ACT   C    C  N N 35  
ACT   O    O  N N 36  
ACT   OXT  O  N N 37  
ACT   CH3  C  N N 38  
ACT   H1   H  N N 39  
ACT   H2   H  N N 40  
ACT   H3   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
BMA   C1   C  N R 115 
BMA   C2   C  N S 116 
BMA   C3   C  N S 117 
BMA   C4   C  N S 118 
BMA   C5   C  N R 119 
BMA   C6   C  N N 120 
BMA   O1   O  N N 121 
BMA   O2   O  N N 122 
BMA   O3   O  N N 123 
BMA   O4   O  N N 124 
BMA   O5   O  N N 125 
BMA   O6   O  N N 126 
BMA   H1   H  N N 127 
BMA   H2   H  N N 128 
BMA   H3   H  N N 129 
BMA   H4   H  N N 130 
BMA   H5   H  N N 131 
BMA   H61  H  N N 132 
BMA   H62  H  N N 133 
BMA   HO1  H  N N 134 
BMA   HO2  H  N N 135 
BMA   HO3  H  N N 136 
BMA   HO4  H  N N 137 
BMA   HO6  H  N N 138 
CYS   N    N  N N 139 
CYS   CA   C  N R 140 
CYS   C    C  N N 141 
CYS   O    O  N N 142 
CYS   CB   C  N N 143 
CYS   SG   S  N N 144 
CYS   OXT  O  N N 145 
CYS   H    H  N N 146 
CYS   H2   H  N N 147 
CYS   HA   H  N N 148 
CYS   HB2  H  N N 149 
CYS   HB3  H  N N 150 
CYS   HG   H  N N 151 
CYS   HXT  H  N N 152 
GLN   N    N  N N 153 
GLN   CA   C  N S 154 
GLN   C    C  N N 155 
GLN   O    O  N N 156 
GLN   CB   C  N N 157 
GLN   CG   C  N N 158 
GLN   CD   C  N N 159 
GLN   OE1  O  N N 160 
GLN   NE2  N  N N 161 
GLN   OXT  O  N N 162 
GLN   H    H  N N 163 
GLN   H2   H  N N 164 
GLN   HA   H  N N 165 
GLN   HB2  H  N N 166 
GLN   HB3  H  N N 167 
GLN   HG2  H  N N 168 
GLN   HG3  H  N N 169 
GLN   HE21 H  N N 170 
GLN   HE22 H  N N 171 
GLN   HXT  H  N N 172 
GLU   N    N  N N 173 
GLU   CA   C  N S 174 
GLU   C    C  N N 175 
GLU   O    O  N N 176 
GLU   CB   C  N N 177 
GLU   CG   C  N N 178 
GLU   CD   C  N N 179 
GLU   OE1  O  N N 180 
GLU   OE2  O  N N 181 
GLU   OXT  O  N N 182 
GLU   H    H  N N 183 
GLU   H2   H  N N 184 
GLU   HA   H  N N 185 
GLU   HB2  H  N N 186 
GLU   HB3  H  N N 187 
GLU   HG2  H  N N 188 
GLU   HG3  H  N N 189 
GLU   HE2  H  N N 190 
GLU   HXT  H  N N 191 
GLY   N    N  N N 192 
GLY   CA   C  N N 193 
GLY   C    C  N N 194 
GLY   O    O  N N 195 
GLY   OXT  O  N N 196 
GLY   H    H  N N 197 
GLY   H2   H  N N 198 
GLY   HA2  H  N N 199 
GLY   HA3  H  N N 200 
GLY   HXT  H  N N 201 
GOL   C1   C  N N 202 
GOL   O1   O  N N 203 
GOL   C2   C  N N 204 
GOL   O2   O  N N 205 
GOL   C3   C  N N 206 
GOL   O3   O  N N 207 
GOL   H11  H  N N 208 
GOL   H12  H  N N 209 
GOL   HO1  H  N N 210 
GOL   H2   H  N N 211 
GOL   HO2  H  N N 212 
GOL   H31  H  N N 213 
GOL   H32  H  N N 214 
GOL   HO3  H  N N 215 
HEM   CHA  C  N N 216 
HEM   CHB  C  N N 217 
HEM   CHC  C  N N 218 
HEM   CHD  C  N N 219 
HEM   C1A  C  Y N 220 
HEM   C2A  C  Y N 221 
HEM   C3A  C  Y N 222 
HEM   C4A  C  Y N 223 
HEM   CMA  C  N N 224 
HEM   CAA  C  N N 225 
HEM   CBA  C  N N 226 
HEM   CGA  C  N N 227 
HEM   O1A  O  N N 228 
HEM   O2A  O  N N 229 
HEM   C1B  C  N N 230 
HEM   C2B  C  N N 231 
HEM   C3B  C  N N 232 
HEM   C4B  C  N N 233 
HEM   CMB  C  N N 234 
HEM   CAB  C  N N 235 
HEM   CBB  C  N N 236 
HEM   C1C  C  Y N 237 
HEM   C2C  C  Y N 238 
HEM   C3C  C  Y N 239 
HEM   C4C  C  Y N 240 
HEM   CMC  C  N N 241 
HEM   CAC  C  N N 242 
HEM   CBC  C  N N 243 
HEM   C1D  C  N N 244 
HEM   C2D  C  N N 245 
HEM   C3D  C  N N 246 
HEM   C4D  C  N N 247 
HEM   CMD  C  N N 248 
HEM   CAD  C  N N 249 
HEM   CBD  C  N N 250 
HEM   CGD  C  N N 251 
HEM   O1D  O  N N 252 
HEM   O2D  O  N N 253 
HEM   NA   N  Y N 254 
HEM   NB   N  N N 255 
HEM   NC   N  Y N 256 
HEM   ND   N  N N 257 
HEM   FE   FE N N 258 
HEM   HHB  H  N N 259 
HEM   HHC  H  N N 260 
HEM   HHD  H  N N 261 
HEM   HMA  H  N N 262 
HEM   HMAA H  N N 263 
HEM   HMAB H  N N 264 
HEM   HAA  H  N N 265 
HEM   HAAA H  N N 266 
HEM   HBA  H  N N 267 
HEM   HBAA H  N N 268 
HEM   HMB  H  N N 269 
HEM   HMBA H  N N 270 
HEM   HMBB H  N N 271 
HEM   HAB  H  N N 272 
HEM   HBB  H  N N 273 
HEM   HBBA H  N N 274 
HEM   HMC  H  N N 275 
HEM   HMCA H  N N 276 
HEM   HMCB H  N N 277 
HEM   HAC  H  N N 278 
HEM   HBC  H  N N 279 
HEM   HBCA H  N N 280 
HEM   HMD  H  N N 281 
HEM   HMDA H  N N 282 
HEM   HMDB H  N N 283 
HEM   HAD  H  N N 284 
HEM   HADA H  N N 285 
HEM   HBD  H  N N 286 
HEM   HBDA H  N N 287 
HEM   H2A  H  N N 288 
HEM   H2D  H  N N 289 
HEM   HHA  H  N N 290 
HIS   N    N  N N 291 
HIS   CA   C  N S 292 
HIS   C    C  N N 293 
HIS   O    O  N N 294 
HIS   CB   C  N N 295 
HIS   CG   C  Y N 296 
HIS   ND1  N  Y N 297 
HIS   CD2  C  Y N 298 
HIS   CE1  C  Y N 299 
HIS   NE2  N  Y N 300 
HIS   OXT  O  N N 301 
HIS   H    H  N N 302 
HIS   H2   H  N N 303 
HIS   HA   H  N N 304 
HIS   HB2  H  N N 305 
HIS   HB3  H  N N 306 
HIS   HD1  H  N N 307 
HIS   HD2  H  N N 308 
HIS   HE1  H  N N 309 
HIS   HE2  H  N N 310 
HIS   HXT  H  N N 311 
HOH   O    O  N N 312 
HOH   H1   H  N N 313 
HOH   H2   H  N N 314 
ILE   N    N  N N 315 
ILE   CA   C  N S 316 
ILE   C    C  N N 317 
ILE   O    O  N N 318 
ILE   CB   C  N S 319 
ILE   CG1  C  N N 320 
ILE   CG2  C  N N 321 
ILE   CD1  C  N N 322 
ILE   OXT  O  N N 323 
ILE   H    H  N N 324 
ILE   H2   H  N N 325 
ILE   HA   H  N N 326 
ILE   HB   H  N N 327 
ILE   HG12 H  N N 328 
ILE   HG13 H  N N 329 
ILE   HG21 H  N N 330 
ILE   HG22 H  N N 331 
ILE   HG23 H  N N 332 
ILE   HD11 H  N N 333 
ILE   HD12 H  N N 334 
ILE   HD13 H  N N 335 
ILE   HXT  H  N N 336 
LEU   N    N  N N 337 
LEU   CA   C  N S 338 
LEU   C    C  N N 339 
LEU   O    O  N N 340 
LEU   CB   C  N N 341 
LEU   CG   C  N N 342 
LEU   CD1  C  N N 343 
LEU   CD2  C  N N 344 
LEU   OXT  O  N N 345 
LEU   H    H  N N 346 
LEU   H2   H  N N 347 
LEU   HA   H  N N 348 
LEU   HB2  H  N N 349 
LEU   HB3  H  N N 350 
LEU   HG   H  N N 351 
LEU   HD11 H  N N 352 
LEU   HD12 H  N N 353 
LEU   HD13 H  N N 354 
LEU   HD21 H  N N 355 
LEU   HD22 H  N N 356 
LEU   HD23 H  N N 357 
LEU   HXT  H  N N 358 
LYS   N    N  N N 359 
LYS   CA   C  N S 360 
LYS   C    C  N N 361 
LYS   O    O  N N 362 
LYS   CB   C  N N 363 
LYS   CG   C  N N 364 
LYS   CD   C  N N 365 
LYS   CE   C  N N 366 
LYS   NZ   N  N N 367 
LYS   OXT  O  N N 368 
LYS   H    H  N N 369 
LYS   H2   H  N N 370 
LYS   HA   H  N N 371 
LYS   HB2  H  N N 372 
LYS   HB3  H  N N 373 
LYS   HG2  H  N N 374 
LYS   HG3  H  N N 375 
LYS   HD2  H  N N 376 
LYS   HD3  H  N N 377 
LYS   HE2  H  N N 378 
LYS   HE3  H  N N 379 
LYS   HZ1  H  N N 380 
LYS   HZ2  H  N N 381 
LYS   HZ3  H  N N 382 
LYS   HXT  H  N N 383 
MAN   C1   C  N S 384 
MAN   C2   C  N S 385 
MAN   C3   C  N S 386 
MAN   C4   C  N S 387 
MAN   C5   C  N R 388 
MAN   C6   C  N N 389 
MAN   O1   O  N N 390 
MAN   O2   O  N N 391 
MAN   O3   O  N N 392 
MAN   O4   O  N N 393 
MAN   O5   O  N N 394 
MAN   O6   O  N N 395 
MAN   H1   H  N N 396 
MAN   H2   H  N N 397 
MAN   H3   H  N N 398 
MAN   H4   H  N N 399 
MAN   H5   H  N N 400 
MAN   H61  H  N N 401 
MAN   H62  H  N N 402 
MAN   HO1  H  N N 403 
MAN   HO2  H  N N 404 
MAN   HO3  H  N N 405 
MAN   HO4  H  N N 406 
MAN   HO6  H  N N 407 
MET   N    N  N N 408 
MET   CA   C  N S 409 
MET   C    C  N N 410 
MET   O    O  N N 411 
MET   CB   C  N N 412 
MET   CG   C  N N 413 
MET   SD   S  N N 414 
MET   CE   C  N N 415 
MET   OXT  O  N N 416 
MET   H    H  N N 417 
MET   H2   H  N N 418 
MET   HA   H  N N 419 
MET   HB2  H  N N 420 
MET   HB3  H  N N 421 
MET   HG2  H  N N 422 
MET   HG3  H  N N 423 
MET   HE1  H  N N 424 
MET   HE2  H  N N 425 
MET   HE3  H  N N 426 
MET   HXT  H  N N 427 
MG    MG   MG N N 428 
NAG   C1   C  N R 429 
NAG   C2   C  N R 430 
NAG   C3   C  N R 431 
NAG   C4   C  N S 432 
NAG   C5   C  N R 433 
NAG   C6   C  N N 434 
NAG   C7   C  N N 435 
NAG   C8   C  N N 436 
NAG   N2   N  N N 437 
NAG   O1   O  N N 438 
NAG   O3   O  N N 439 
NAG   O4   O  N N 440 
NAG   O5   O  N N 441 
NAG   O6   O  N N 442 
NAG   O7   O  N N 443 
NAG   H1   H  N N 444 
NAG   H2   H  N N 445 
NAG   H3   H  N N 446 
NAG   H4   H  N N 447 
NAG   H5   H  N N 448 
NAG   H61  H  N N 449 
NAG   H62  H  N N 450 
NAG   H81  H  N N 451 
NAG   H82  H  N N 452 
NAG   H83  H  N N 453 
NAG   HN2  H  N N 454 
NAG   HO1  H  N N 455 
NAG   HO3  H  N N 456 
NAG   HO4  H  N N 457 
NAG   HO6  H  N N 458 
PHE   N    N  N N 459 
PHE   CA   C  N S 460 
PHE   C    C  N N 461 
PHE   O    O  N N 462 
PHE   CB   C  N N 463 
PHE   CG   C  Y N 464 
PHE   CD1  C  Y N 465 
PHE   CD2  C  Y N 466 
PHE   CE1  C  Y N 467 
PHE   CE2  C  Y N 468 
PHE   CZ   C  Y N 469 
PHE   OXT  O  N N 470 
PHE   H    H  N N 471 
PHE   H2   H  N N 472 
PHE   HA   H  N N 473 
PHE   HB2  H  N N 474 
PHE   HB3  H  N N 475 
PHE   HD1  H  N N 476 
PHE   HD2  H  N N 477 
PHE   HE1  H  N N 478 
PHE   HE2  H  N N 479 
PHE   HZ   H  N N 480 
PHE   HXT  H  N N 481 
PRO   N    N  N N 482 
PRO   CA   C  N S 483 
PRO   C    C  N N 484 
PRO   O    O  N N 485 
PRO   CB   C  N N 486 
PRO   CG   C  N N 487 
PRO   CD   C  N N 488 
PRO   OXT  O  N N 489 
PRO   H    H  N N 490 
PRO   HA   H  N N 491 
PRO   HB2  H  N N 492 
PRO   HB3  H  N N 493 
PRO   HG2  H  N N 494 
PRO   HG3  H  N N 495 
PRO   HD2  H  N N 496 
PRO   HD3  H  N N 497 
PRO   HXT  H  N N 498 
SER   N    N  N N 499 
SER   CA   C  N S 500 
SER   C    C  N N 501 
SER   O    O  N N 502 
SER   CB   C  N N 503 
SER   OG   O  N N 504 
SER   OXT  O  N N 505 
SER   H    H  N N 506 
SER   H2   H  N N 507 
SER   HA   H  N N 508 
SER   HB2  H  N N 509 
SER   HB3  H  N N 510 
SER   HG   H  N N 511 
SER   HXT  H  N N 512 
SO4   S    S  N N 513 
SO4   O1   O  N N 514 
SO4   O2   O  N N 515 
SO4   O3   O  N N 516 
SO4   O4   O  N N 517 
THR   N    N  N N 518 
THR   CA   C  N S 519 
THR   C    C  N N 520 
THR   O    O  N N 521 
THR   CB   C  N R 522 
THR   OG1  O  N N 523 
THR   CG2  C  N N 524 
THR   OXT  O  N N 525 
THR   H    H  N N 526 
THR   H2   H  N N 527 
THR   HA   H  N N 528 
THR   HB   H  N N 529 
THR   HG1  H  N N 530 
THR   HG21 H  N N 531 
THR   HG22 H  N N 532 
THR   HG23 H  N N 533 
THR   HXT  H  N N 534 
TRP   N    N  N N 535 
TRP   CA   C  N S 536 
TRP   C    C  N N 537 
TRP   O    O  N N 538 
TRP   CB   C  N N 539 
TRP   CG   C  Y N 540 
TRP   CD1  C  Y N 541 
TRP   CD2  C  Y N 542 
TRP   NE1  N  Y N 543 
TRP   CE2  C  Y N 544 
TRP   CE3  C  Y N 545 
TRP   CZ2  C  Y N 546 
TRP   CZ3  C  Y N 547 
TRP   CH2  C  Y N 548 
TRP   OXT  O  N N 549 
TRP   H    H  N N 550 
TRP   H2   H  N N 551 
TRP   HA   H  N N 552 
TRP   HB2  H  N N 553 
TRP   HB3  H  N N 554 
TRP   HD1  H  N N 555 
TRP   HE1  H  N N 556 
TRP   HE3  H  N N 557 
TRP   HZ2  H  N N 558 
TRP   HZ3  H  N N 559 
TRP   HH2  H  N N 560 
TRP   HXT  H  N N 561 
TYR   N    N  N N 562 
TYR   CA   C  N S 563 
TYR   C    C  N N 564 
TYR   O    O  N N 565 
TYR   CB   C  N N 566 
TYR   CG   C  Y N 567 
TYR   CD1  C  Y N 568 
TYR   CD2  C  Y N 569 
TYR   CE1  C  Y N 570 
TYR   CE2  C  Y N 571 
TYR   CZ   C  Y N 572 
TYR   OH   O  N N 573 
TYR   OXT  O  N N 574 
TYR   H    H  N N 575 
TYR   H2   H  N N 576 
TYR   HA   H  N N 577 
TYR   HB2  H  N N 578 
TYR   HB3  H  N N 579 
TYR   HD1  H  N N 580 
TYR   HD2  H  N N 581 
TYR   HE1  H  N N 582 
TYR   HE2  H  N N 583 
TYR   HH   H  N N 584 
TYR   HXT  H  N N 585 
VAL   N    N  N N 586 
VAL   CA   C  N S 587 
VAL   C    C  N N 588 
VAL   O    O  N N 589 
VAL   CB   C  N N 590 
VAL   CG1  C  N N 591 
VAL   CG2  C  N N 592 
VAL   OXT  O  N N 593 
VAL   H    H  N N 594 
VAL   H2   H  N N 595 
VAL   HA   H  N N 596 
VAL   HB   H  N N 597 
VAL   HG11 H  N N 598 
VAL   HG12 H  N N 599 
VAL   HG13 H  N N 600 
VAL   HG21 H  N N 601 
VAL   HG22 H  N N 602 
VAL   HG23 H  N N 603 
VAL   HXT  H  N N 604 
# 
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 
A1IUB O11 C10  doub N N 1   
A1IUB C10 C12  sing N N 2   
A1IUB C10 C9   sing N N 3   
A1IUB C9  C8   doub N E 4   
A1IUB C1  C2   sing N N 5   
A1IUB C8  C7   sing N N 6   
A1IUB C7  C2   sing N N 7   
A1IUB C7  C6   sing N N 8   
A1IUB C2  C3   doub N N 9   
A1IUB C14 C6   sing N N 10  
A1IUB C6  C13  sing N N 11  
A1IUB C6  C5   sing N N 12  
A1IUB C3  C4   sing N N 13  
A1IUB C5  C4   sing N N 14  
A1IUB C4  H2   sing N N 15  
A1IUB C4  H3   sing N N 16  
A1IUB C5  H4   sing N N 17  
A1IUB C5  H5   sing N N 18  
A1IUB C8  H6   sing N N 19  
A1IUB C9  H7   sing N N 20  
A1IUB C12 H8   sing N N 21  
A1IUB C12 H9   sing N N 22  
A1IUB C12 H10  sing N N 23  
A1IUB C1  H11  sing N N 24  
A1IUB C1  H12  sing N N 25  
A1IUB C1  H13  sing N N 26  
A1IUB C3  H14  sing N N 27  
A1IUB C7  H16  sing N N 28  
A1IUB C13 H17  sing N N 29  
A1IUB C13 H18  sing N N 30  
A1IUB C13 H19  sing N N 31  
A1IUB C14 H20  sing N N 32  
A1IUB C14 H21  sing N N 33  
A1IUB C14 H22  sing N N 34  
ACT   C   O    doub N N 35  
ACT   C   OXT  sing N N 36  
ACT   C   CH3  sing N N 37  
ACT   CH3 H1   sing N N 38  
ACT   CH3 H2   sing N N 39  
ACT   CH3 H3   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
BMA   C1  C2   sing N N 110 
BMA   C1  O1   sing N N 111 
BMA   C1  O5   sing N N 112 
BMA   C1  H1   sing N N 113 
BMA   C2  C3   sing N N 114 
BMA   C2  O2   sing N N 115 
BMA   C2  H2   sing N N 116 
BMA   C3  C4   sing N N 117 
BMA   C3  O3   sing N N 118 
BMA   C3  H3   sing N N 119 
BMA   C4  C5   sing N N 120 
BMA   C4  O4   sing N N 121 
BMA   C4  H4   sing N N 122 
BMA   C5  C6   sing N N 123 
BMA   C5  O5   sing N N 124 
BMA   C5  H5   sing N N 125 
BMA   C6  O6   sing N N 126 
BMA   C6  H61  sing N N 127 
BMA   C6  H62  sing N N 128 
BMA   O1  HO1  sing N N 129 
BMA   O2  HO2  sing N N 130 
BMA   O3  HO3  sing N N 131 
BMA   O4  HO4  sing N N 132 
BMA   O6  HO6  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
GOL   C1  O1   sing N N 193 
GOL   C1  C2   sing N N 194 
GOL   C1  H11  sing N N 195 
GOL   C1  H12  sing N N 196 
GOL   O1  HO1  sing N N 197 
GOL   C2  O2   sing N N 198 
GOL   C2  C3   sing N N 199 
GOL   C2  H2   sing N N 200 
GOL   O2  HO2  sing N N 201 
GOL   C3  O3   sing N N 202 
GOL   C3  H31  sing N N 203 
GOL   C3  H32  sing N N 204 
GOL   O3  HO3  sing N N 205 
HEM   CHA C1A  sing N N 206 
HEM   CHA C4D  doub N N 207 
HEM   CHA HHA  sing N N 208 
HEM   CHB C4A  sing N N 209 
HEM   CHB C1B  doub N N 210 
HEM   CHB HHB  sing N N 211 
HEM   CHC C4B  sing N N 212 
HEM   CHC C1C  doub N N 213 
HEM   CHC HHC  sing N N 214 
HEM   CHD C4C  doub N N 215 
HEM   CHD C1D  sing N N 216 
HEM   CHD HHD  sing N N 217 
HEM   C1A C2A  doub Y N 218 
HEM   C1A NA   sing Y N 219 
HEM   C2A C3A  sing Y N 220 
HEM   C2A CAA  sing N N 221 
HEM   C3A C4A  doub Y N 222 
HEM   C3A CMA  sing N N 223 
HEM   C4A NA   sing Y N 224 
HEM   CMA HMA  sing N N 225 
HEM   CMA HMAA sing N N 226 
HEM   CMA HMAB sing N N 227 
HEM   CAA CBA  sing N N 228 
HEM   CAA HAA  sing N N 229 
HEM   CAA HAAA sing N N 230 
HEM   CBA CGA  sing N N 231 
HEM   CBA HBA  sing N N 232 
HEM   CBA HBAA sing N N 233 
HEM   CGA O1A  doub N N 234 
HEM   CGA O2A  sing N N 235 
HEM   C1B C2B  sing N N 236 
HEM   C1B NB   sing N N 237 
HEM   C2B C3B  doub N N 238 
HEM   C2B CMB  sing N N 239 
HEM   C3B C4B  sing N N 240 
HEM   C3B CAB  sing N N 241 
HEM   C4B NB   doub N N 242 
HEM   CMB HMB  sing N N 243 
HEM   CMB HMBA sing N N 244 
HEM   CMB HMBB sing N N 245 
HEM   CAB CBB  doub N N 246 
HEM   CAB HAB  sing N N 247 
HEM   CBB HBB  sing N N 248 
HEM   CBB HBBA sing N N 249 
HEM   C1C C2C  sing Y N 250 
HEM   C1C NC   sing Y N 251 
HEM   C2C C3C  doub Y N 252 
HEM   C2C CMC  sing N N 253 
HEM   C3C C4C  sing Y N 254 
HEM   C3C CAC  sing N N 255 
HEM   C4C NC   sing Y N 256 
HEM   CMC HMC  sing N N 257 
HEM   CMC HMCA sing N N 258 
HEM   CMC HMCB sing N N 259 
HEM   CAC CBC  doub N N 260 
HEM   CAC HAC  sing N N 261 
HEM   CBC HBC  sing N N 262 
HEM   CBC HBCA sing N N 263 
HEM   C1D C2D  sing N N 264 
HEM   C1D ND   doub N N 265 
HEM   C2D C3D  doub N N 266 
HEM   C2D CMD  sing N N 267 
HEM   C3D C4D  sing N N 268 
HEM   C3D CAD  sing N N 269 
HEM   C4D ND   sing N N 270 
HEM   CMD HMD  sing N N 271 
HEM   CMD HMDA sing N N 272 
HEM   CMD HMDB sing N N 273 
HEM   CAD CBD  sing N N 274 
HEM   CAD HAD  sing N N 275 
HEM   CAD HADA sing N N 276 
HEM   CBD CGD  sing N N 277 
HEM   CBD HBD  sing N N 278 
HEM   CBD HBDA sing N N 279 
HEM   CGD O1D  doub N N 280 
HEM   CGD O2D  sing N N 281 
HEM   O2A H2A  sing N N 282 
HEM   O2D H2D  sing N N 283 
HEM   FE  NA   sing N N 284 
HEM   FE  NB   sing N N 285 
HEM   FE  NC   sing N N 286 
HEM   FE  ND   sing N N 287 
HIS   N   CA   sing N N 288 
HIS   N   H    sing N N 289 
HIS   N   H2   sing N N 290 
HIS   CA  C    sing N N 291 
HIS   CA  CB   sing N N 292 
HIS   CA  HA   sing N N 293 
HIS   C   O    doub N N 294 
HIS   C   OXT  sing N N 295 
HIS   CB  CG   sing N N 296 
HIS   CB  HB2  sing N N 297 
HIS   CB  HB3  sing N N 298 
HIS   CG  ND1  sing Y N 299 
HIS   CG  CD2  doub Y N 300 
HIS   ND1 CE1  doub Y N 301 
HIS   ND1 HD1  sing N N 302 
HIS   CD2 NE2  sing Y N 303 
HIS   CD2 HD2  sing N N 304 
HIS   CE1 NE2  sing Y N 305 
HIS   CE1 HE1  sing N N 306 
HIS   NE2 HE2  sing N N 307 
HIS   OXT HXT  sing N N 308 
HOH   O   H1   sing N N 309 
HOH   O   H2   sing N N 310 
ILE   N   CA   sing N N 311 
ILE   N   H    sing N N 312 
ILE   N   H2   sing N N 313 
ILE   CA  C    sing N N 314 
ILE   CA  CB   sing N N 315 
ILE   CA  HA   sing N N 316 
ILE   C   O    doub N N 317 
ILE   C   OXT  sing N N 318 
ILE   CB  CG1  sing N N 319 
ILE   CB  CG2  sing N N 320 
ILE   CB  HB   sing N N 321 
ILE   CG1 CD1  sing N N 322 
ILE   CG1 HG12 sing N N 323 
ILE   CG1 HG13 sing N N 324 
ILE   CG2 HG21 sing N N 325 
ILE   CG2 HG22 sing N N 326 
ILE   CG2 HG23 sing N N 327 
ILE   CD1 HD11 sing N N 328 
ILE   CD1 HD12 sing N N 329 
ILE   CD1 HD13 sing N N 330 
ILE   OXT HXT  sing N N 331 
LEU   N   CA   sing N N 332 
LEU   N   H    sing N N 333 
LEU   N   H2   sing N N 334 
LEU   CA  C    sing N N 335 
LEU   CA  CB   sing N N 336 
LEU   CA  HA   sing N N 337 
LEU   C   O    doub N N 338 
LEU   C   OXT  sing N N 339 
LEU   CB  CG   sing N N 340 
LEU   CB  HB2  sing N N 341 
LEU   CB  HB3  sing N N 342 
LEU   CG  CD1  sing N N 343 
LEU   CG  CD2  sing N N 344 
LEU   CG  HG   sing N N 345 
LEU   CD1 HD11 sing N N 346 
LEU   CD1 HD12 sing N N 347 
LEU   CD1 HD13 sing N N 348 
LEU   CD2 HD21 sing N N 349 
LEU   CD2 HD22 sing N N 350 
LEU   CD2 HD23 sing N N 351 
LEU   OXT HXT  sing N N 352 
LYS   N   CA   sing N N 353 
LYS   N   H    sing N N 354 
LYS   N   H2   sing N N 355 
LYS   CA  C    sing N N 356 
LYS   CA  CB   sing N N 357 
LYS   CA  HA   sing N N 358 
LYS   C   O    doub N N 359 
LYS   C   OXT  sing N N 360 
LYS   CB  CG   sing N N 361 
LYS   CB  HB2  sing N N 362 
LYS   CB  HB3  sing N N 363 
LYS   CG  CD   sing N N 364 
LYS   CG  HG2  sing N N 365 
LYS   CG  HG3  sing N N 366 
LYS   CD  CE   sing N N 367 
LYS   CD  HD2  sing N N 368 
LYS   CD  HD3  sing N N 369 
LYS   CE  NZ   sing N N 370 
LYS   CE  HE2  sing N N 371 
LYS   CE  HE3  sing N N 372 
LYS   NZ  HZ1  sing N N 373 
LYS   NZ  HZ2  sing N N 374 
LYS   NZ  HZ3  sing N N 375 
LYS   OXT HXT  sing N N 376 
MAN   C1  C2   sing N N 377 
MAN   C1  O1   sing N N 378 
MAN   C1  O5   sing N N 379 
MAN   C1  H1   sing N N 380 
MAN   C2  C3   sing N N 381 
MAN   C2  O2   sing N N 382 
MAN   C2  H2   sing N N 383 
MAN   C3  C4   sing N N 384 
MAN   C3  O3   sing N N 385 
MAN   C3  H3   sing N N 386 
MAN   C4  C5   sing N N 387 
MAN   C4  O4   sing N N 388 
MAN   C4  H4   sing N N 389 
MAN   C5  C6   sing N N 390 
MAN   C5  O5   sing N N 391 
MAN   C5  H5   sing N N 392 
MAN   C6  O6   sing N N 393 
MAN   C6  H61  sing N N 394 
MAN   C6  H62  sing N N 395 
MAN   O1  HO1  sing N N 396 
MAN   O2  HO2  sing N N 397 
MAN   O3  HO3  sing N N 398 
MAN   O4  HO4  sing N N 399 
MAN   O6  HO6  sing N N 400 
MET   N   CA   sing N N 401 
MET   N   H    sing N N 402 
MET   N   H2   sing N N 403 
MET   CA  C    sing N N 404 
MET   CA  CB   sing N N 405 
MET   CA  HA   sing N N 406 
MET   C   O    doub N N 407 
MET   C   OXT  sing N N 408 
MET   CB  CG   sing N N 409 
MET   CB  HB2  sing N N 410 
MET   CB  HB3  sing N N 411 
MET   CG  SD   sing N N 412 
MET   CG  HG2  sing N N 413 
MET   CG  HG3  sing N N 414 
MET   SD  CE   sing N N 415 
MET   CE  HE1  sing N N 416 
MET   CE  HE2  sing N N 417 
MET   CE  HE3  sing N N 418 
MET   OXT HXT  sing N N 419 
NAG   C1  C2   sing N N 420 
NAG   C1  O1   sing N N 421 
NAG   C1  O5   sing N N 422 
NAG   C1  H1   sing N N 423 
NAG   C2  C3   sing N N 424 
NAG   C2  N2   sing N N 425 
NAG   C2  H2   sing N N 426 
NAG   C3  C4   sing N N 427 
NAG   C3  O3   sing N N 428 
NAG   C3  H3   sing N N 429 
NAG   C4  C5   sing N N 430 
NAG   C4  O4   sing N N 431 
NAG   C4  H4   sing N N 432 
NAG   C5  C6   sing N N 433 
NAG   C5  O5   sing N N 434 
NAG   C5  H5   sing N N 435 
NAG   C6  O6   sing N N 436 
NAG   C6  H61  sing N N 437 
NAG   C6  H62  sing N N 438 
NAG   C7  C8   sing N N 439 
NAG   C7  N2   sing N N 440 
NAG   C7  O7   doub N N 441 
NAG   C8  H81  sing N N 442 
NAG   C8  H82  sing N N 443 
NAG   C8  H83  sing N N 444 
NAG   N2  HN2  sing N N 445 
NAG   O1  HO1  sing N N 446 
NAG   O3  HO3  sing N N 447 
NAG   O4  HO4  sing N N 448 
NAG   O6  HO6  sing N N 449 
PHE   N   CA   sing N N 450 
PHE   N   H    sing N N 451 
PHE   N   H2   sing N N 452 
PHE   CA  C    sing N N 453 
PHE   CA  CB   sing N N 454 
PHE   CA  HA   sing N N 455 
PHE   C   O    doub N N 456 
PHE   C   OXT  sing N N 457 
PHE   CB  CG   sing N N 458 
PHE   CB  HB2  sing N N 459 
PHE   CB  HB3  sing N N 460 
PHE   CG  CD1  doub Y N 461 
PHE   CG  CD2  sing Y N 462 
PHE   CD1 CE1  sing Y N 463 
PHE   CD1 HD1  sing N N 464 
PHE   CD2 CE2  doub Y N 465 
PHE   CD2 HD2  sing N N 466 
PHE   CE1 CZ   doub Y N 467 
PHE   CE1 HE1  sing N N 468 
PHE   CE2 CZ   sing Y N 469 
PHE   CE2 HE2  sing N N 470 
PHE   CZ  HZ   sing N N 471 
PHE   OXT HXT  sing N N 472 
PRO   N   CA   sing N N 473 
PRO   N   CD   sing N N 474 
PRO   N   H    sing N N 475 
PRO   CA  C    sing N N 476 
PRO   CA  CB   sing N N 477 
PRO   CA  HA   sing N N 478 
PRO   C   O    doub N N 479 
PRO   C   OXT  sing N N 480 
PRO   CB  CG   sing N N 481 
PRO   CB  HB2  sing N N 482 
PRO   CB  HB3  sing N N 483 
PRO   CG  CD   sing N N 484 
PRO   CG  HG2  sing N N 485 
PRO   CG  HG3  sing N N 486 
PRO   CD  HD2  sing N N 487 
PRO   CD  HD3  sing N N 488 
PRO   OXT HXT  sing N N 489 
SER   N   CA   sing N N 490 
SER   N   H    sing N N 491 
SER   N   H2   sing N N 492 
SER   CA  C    sing N N 493 
SER   CA  CB   sing N N 494 
SER   CA  HA   sing N N 495 
SER   C   O    doub N N 496 
SER   C   OXT  sing N N 497 
SER   CB  OG   sing N N 498 
SER   CB  HB2  sing N N 499 
SER   CB  HB3  sing N N 500 
SER   OG  HG   sing N N 501 
SER   OXT HXT  sing N N 502 
SO4   S   O1   doub N N 503 
SO4   S   O2   doub N N 504 
SO4   S   O3   sing N N 505 
SO4   S   O4   sing N N 506 
THR   N   CA   sing N N 507 
THR   N   H    sing N N 508 
THR   N   H2   sing N N 509 
THR   CA  C    sing N N 510 
THR   CA  CB   sing N N 511 
THR   CA  HA   sing N N 512 
THR   C   O    doub N N 513 
THR   C   OXT  sing N N 514 
THR   CB  OG1  sing N N 515 
THR   CB  CG2  sing N N 516 
THR   CB  HB   sing N N 517 
THR   OG1 HG1  sing N N 518 
THR   CG2 HG21 sing N N 519 
THR   CG2 HG22 sing N N 520 
THR   CG2 HG23 sing N N 521 
THR   OXT HXT  sing N N 522 
TRP   N   CA   sing N N 523 
TRP   N   H    sing N N 524 
TRP   N   H2   sing N N 525 
TRP   CA  C    sing N N 526 
TRP   CA  CB   sing N N 527 
TRP   CA  HA   sing N N 528 
TRP   C   O    doub N N 529 
TRP   C   OXT  sing N N 530 
TRP   CB  CG   sing N N 531 
TRP   CB  HB2  sing N N 532 
TRP   CB  HB3  sing N N 533 
TRP   CG  CD1  doub Y N 534 
TRP   CG  CD2  sing Y N 535 
TRP   CD1 NE1  sing Y N 536 
TRP   CD1 HD1  sing N N 537 
TRP   CD2 CE2  doub Y N 538 
TRP   CD2 CE3  sing Y N 539 
TRP   NE1 CE2  sing Y N 540 
TRP   NE1 HE1  sing N N 541 
TRP   CE2 CZ2  sing Y N 542 
TRP   CE3 CZ3  doub Y N 543 
TRP   CE3 HE3  sing N N 544 
TRP   CZ2 CH2  doub Y N 545 
TRP   CZ2 HZ2  sing N N 546 
TRP   CZ3 CH2  sing Y N 547 
TRP   CZ3 HZ3  sing N N 548 
TRP   CH2 HH2  sing N N 549 
TRP   OXT HXT  sing N N 550 
TYR   N   CA   sing N N 551 
TYR   N   H    sing N N 552 
TYR   N   H2   sing N N 553 
TYR   CA  C    sing N N 554 
TYR   CA  CB   sing N N 555 
TYR   CA  HA   sing N N 556 
TYR   C   O    doub N N 557 
TYR   C   OXT  sing N N 558 
TYR   CB  CG   sing N N 559 
TYR   CB  HB2  sing N N 560 
TYR   CB  HB3  sing N N 561 
TYR   CG  CD1  doub Y N 562 
TYR   CG  CD2  sing Y N 563 
TYR   CD1 CE1  sing Y N 564 
TYR   CD1 HD1  sing N N 565 
TYR   CD2 CE2  doub Y N 566 
TYR   CD2 HD2  sing N N 567 
TYR   CE1 CZ   doub Y N 568 
TYR   CE1 HE1  sing N N 569 
TYR   CE2 CZ   sing Y N 570 
TYR   CE2 HE2  sing N N 571 
TYR   CZ  OH   sing N N 572 
TYR   OH  HH   sing N N 573 
TYR   OXT HXT  sing N N 574 
VAL   N   CA   sing N N 575 
VAL   N   H    sing N N 576 
VAL   N   H2   sing N N 577 
VAL   CA  C    sing N N 578 
VAL   CA  CB   sing N N 579 
VAL   CA  HA   sing N N 580 
VAL   C   O    doub N N 581 
VAL   C   OXT  sing N N 582 
VAL   CB  CG1  sing N N 583 
VAL   CB  CG2  sing N N 584 
VAL   CB  HB   sing N N 585 
VAL   CG1 HG11 sing N N 586 
VAL   CG1 HG12 sing N N 587 
VAL   CG1 HG13 sing N N 588 
VAL   CG2 HG21 sing N N 589 
VAL   CG2 HG22 sing N N 590 
VAL   CG2 HG23 sing N N 591 
VAL   OXT HXT  sing N N 592 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Spanish Ministry of Science, Innovation, and Universities' Spain 'Synergy CAM Project Y2018/BIO-4738-EVOQUIMERA-CM' 1 
'Spanish Ministry of Science, Innovation, and Universities' Spain PID2022-136367OB-C33                               2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 MAN 4 n 
2 MAN 5 n 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
3 MAN 4 n 
3 MAN 5 n 
3 MAN 6 n 
3 MAN 7 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
5 MAN 4 n 
5 MAN 5 n 
5 MAN 6 n 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
6 MAN 4 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5OXU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HEC 
_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]   0.003690 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001496 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013324 
_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]   0.010174 
_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  
FE 
MG 
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   . GLN   A  1  1   ? 60.581  3.921   59.377 1.00 121.64 ? 14  GLN   A N   1 
ATOM   2    C  CA  . GLN   A  1  1   ? 61.756  4.270   58.528 1.00 126.88 ? 14  GLN   A CA  1 
ATOM   3    C  C   . GLN   A  1  1   ? 61.638  3.674   57.120 1.00 115.83 ? 14  GLN   A C   1 
ATOM   4    O  O   . GLN   A  1  1   ? 62.081  4.328   56.178 1.00 99.80  ? 14  GLN   A O   1 
ATOM   5    C  CB  . GLN   A  1  1   ? 63.074  3.887   59.206 1.00 133.14 ? 14  GLN   A CB  1 
ATOM   6    C  CG  . GLN   A  1  1   ? 63.239  2.395   59.474 1.00 147.57 ? 14  GLN   A CG  1 
ATOM   7    C  CD  . GLN   A  1  1   ? 64.669  2.012   59.781 1.00 156.71 ? 14  GLN   A CD  1 
ATOM   8    O  OE1 . GLN   A  1  1   ? 65.577  2.850   59.747 1.00 166.30 ? 14  GLN   A OE1 1 
ATOM   9    N  NE2 . GLN   A  1  1   ? 64.881  0.737   60.071 1.00 152.32 ? 14  GLN   A NE2 1 
ATOM   10   N  N   . GLY   A  1  2   ? 61.097  2.442   56.990 1.00 103.32 ? 15  GLY   A N   1 
ATOM   11   C  CA  . GLY   A  1  2   ? 60.662  1.907   55.707 1.00 82.06  ? 15  GLY   A CA  1 
ATOM   12   C  C   . GLY   A  1  2   ? 60.696  0.380   55.603 1.00 67.07  ? 15  GLY   A C   1 
ATOM   13   O  O   . GLY   A  1  2   ? 61.218  -0.325  56.461 1.00 58.49  ? 15  GLY   A O   1 
ATOM   14   N  N   . VAL   A  1  3   ? 60.186  -0.104  54.471 1.00 56.05  ? 16  VAL   A N   1 
ATOM   15   C  CA  . VAL   A  1  3   ? 60.032  -1.519  54.178 1.00 53.22  ? 16  VAL   A CA  1 
ATOM   16   C  C   . VAL   A  1  3   ? 61.055  -1.925  53.119 1.00 50.79  ? 16  VAL   A C   1 
ATOM   17   O  O   . VAL   A  1  3   ? 61.489  -1.085  52.338 1.00 47.48  ? 16  VAL   A O   1 
ATOM   18   C  CB  . VAL   A  1  3   ? 58.573  -1.699  53.696 1.00 65.21  ? 16  VAL   A CB  1 
ATOM   19   C  CG1 . VAL   A  1  3   ? 58.309  -3.037  53.009 1.00 70.62  ? 16  VAL   A CG1 1 
ATOM   20   C  CG2 . VAL   A  1  3   ? 57.591  -1.487  54.843 1.00 66.00  ? 16  VAL   A CG2 1 
ATOM   21   N  N   . ASP   A  1  4   ? 61.415  -3.214  53.091 1.00 53.81  ? 17  ASP   A N   1 
ATOM   22   C  CA  . ASP   A  1  4   ? 62.178  -3.807  52.002 1.00 59.30  ? 17  ASP   A CA  1 
ATOM   23   C  C   . ASP   A  1  4   ? 61.205  -4.526  51.058 1.00 55.02  ? 17  ASP   A C   1 
ATOM   24   O  O   . ASP   A  1  4   ? 60.727  -5.612  51.382 1.00 53.00  ? 17  ASP   A O   1 
ATOM   25   C  CB  . ASP   A  1  4   ? 63.280  -4.699  52.556 1.00 69.69  ? 17  ASP   A CB  1 
ATOM   26   C  CG  . ASP   A  1  4   ? 64.485  -4.890  51.645 1.00 87.60  ? 17  ASP   A CG  1 
ATOM   27   O  OD1 . ASP   A  1  4   ? 64.498  -4.324  50.526 1.00 84.92  ? 17  ASP   A OD1 1 
ATOM   28   O  OD2 . ASP   A  1  4   ? 65.415  -5.601  52.070 1.00 104.17 ? 17  ASP   A OD2 1 
ATOM   29   N  N   . PRO   A  1  5   ? 60.867  -3.955  49.869 1.00 55.22  ? 18  PRO   A N   1 
ATOM   30   C  CA  . PRO   A  1  5   ? 59.784  -4.477  49.018 1.00 51.02  ? 18  PRO   A CA  1 
ATOM   31   C  C   . PRO   A  1  5   ? 60.139  -5.763  48.283 1.00 42.42  ? 18  PRO   A C   1 
ATOM   32   O  O   . PRO   A  1  5   ? 61.082  -5.768  47.501 1.00 41.50  ? 18  PRO   A O   1 
ATOM   33   C  CB  . PRO   A  1  5   ? 59.474  -3.365  47.995 1.00 46.12  ? 18  PRO   A CB  1 
ATOM   34   C  CG  . PRO   A  1  5   ? 60.646  -2.403  48.086 1.00 53.30  ? 18  PRO   A CG  1 
ATOM   35   C  CD  . PRO   A  1  5   ? 61.553  -2.811  49.246 1.00 49.36  ? 18  PRO   A CD  1 
ATOM   36   N  N   . PRO   A  1  6   ? 59.349  -6.848  48.427 1.00 42.40  ? 19  PRO   A N   1 
ATOM   37   C  CA  . PRO   A  1  6   ? 59.719  -8.145  47.861 1.00 48.08  ? 19  PRO   A CA  1 
ATOM   38   C  C   . PRO   A  1  6   ? 59.401  -8.149  46.372 1.00 46.29  ? 19  PRO   A C   1 
ATOM   39   O  O   . PRO   A  1  6   ? 58.629  -7.316  45.902 1.00 41.87  ? 19  PRO   A O   1 
ATOM   40   C  CB  . PRO   A  1  6   ? 58.838  -9.125  48.643 1.00 48.03  ? 19  PRO   A CB  1 
ATOM   41   C  CG  . PRO   A  1  6   ? 57.565  -8.331  48.872 1.00 50.96  ? 19  PRO   A CG  1 
ATOM   42   C  CD  . PRO   A  1  6   ? 58.022  -6.875  49.066 1.00 49.30  ? 19  PRO   A CD  1 
ATOM   43   N  N   . PRO   A  1  7   ? 59.994  -9.075  45.591 1.00 51.34  ? 20  PRO   A N   1 
ATOM   44   C  CA  . PRO   A  1  7   ? 59.667  -9.185  44.174 1.00 48.90  ? 20  PRO   A CA  1 
ATOM   45   C  C   . PRO   A  1  7   ? 58.206  -9.610  44.023 1.00 40.84  ? 20  PRO   A C   1 
ATOM   46   O  O   . PRO   A  1  7   ? 57.600  -10.127 44.949 1.00 34.29  ? 20  PRO   A O   1 
ATOM   47   C  CB  . PRO   A  1  7   ? 60.665  -10.212 43.622 1.00 55.91  ? 20  PRO   A CB  1 
ATOM   48   C  CG  . PRO   A  1  7   ? 61.155  -10.978 44.847 1.00 57.93  ? 20  PRO   A CG  1 
ATOM   49   C  CD  . PRO   A  1  7   ? 61.028  -10.031 46.029 1.00 57.08  ? 20  PRO   A CD  1 
ATOM   50   N  N   . PRO   A  1  8   ? 57.571  -9.318  42.875 1.00 35.34  ? 21  PRO   A N   1 
ATOM   51   C  CA  . PRO   A  1  8   ? 56.155  -9.619  42.717 1.00 38.12  ? 21  PRO   A CA  1 
ATOM   52   C  C   . PRO   A  1  8   ? 55.928  -11.122 42.730 1.00 34.35  ? 21  PRO   A C   1 
ATOM   53   O  O   . PRO   A  1  8   ? 56.780  -11.893 42.289 1.00 32.88  ? 21  PRO   A O   1 
ATOM   54   C  CB  . PRO   A  1  8   ? 55.794  -9.007  41.367 1.00 37.01  ? 21  PRO   A CB  1 
ATOM   55   C  CG  . PRO   A  1  8   ? 57.125  -8.988  40.632 1.00 37.27  ? 21  PRO   A CG  1 
ATOM   56   C  CD  . PRO   A  1  8   ? 58.182  -8.704  41.682 1.00 36.02  ? 21  PRO   A CD  1 
ATOM   57   N  N   . PRO   A  1  9   ? 54.738  -11.562 43.181 1.00 34.05  ? 22  PRO   A N   1 
ATOM   58   C  CA  . PRO   A  1  9   ? 54.300  -12.951 43.050 1.00 33.55  ? 22  PRO   A CA  1 
ATOM   59   C  C   . PRO   A  1  9   ? 54.322  -13.346 41.593 1.00 34.44  ? 22  PRO   A C   1 
ATOM   60   O  O   . PRO   A  1  9   ? 54.136  -12.490 40.731 1.00 34.03  ? 22  PRO   A O   1 
ATOM   61   C  CB  . PRO   A  1  9   ? 52.869  -12.956 43.542 1.00 34.87  ? 22  PRO   A CB  1 
ATOM   62   C  CG  . PRO   A  1  9   ? 52.783  -11.747 44.430 1.00 36.26  ? 22  PRO   A CG  1 
ATOM   63   C  CD  . PRO   A  1  9   ? 53.724  -10.727 43.826 1.00 35.81  ? 22  PRO   A CD  1 
ATOM   64   N  N   . GLY   A  1  10  ? 54.516  -14.646 41.363 1.00 35.24  ? 23  GLY   A N   1 
ATOM   65   C  CA  . GLY   A  1  10  ? 54.366  -15.237 40.048 1.00 35.05  ? 23  GLY   A CA  1 
ATOM   66   C  C   . GLY   A  1  10  ? 52.903  -15.609 39.830 1.00 35.97  ? 23  GLY   A C   1 
ATOM   67   O  O   . GLY   A  1  10  ? 52.049  -15.227 40.631 1.00 34.90  ? 23  GLY   A O   1 
ATOM   68   N  N   . PRO   A  1  11  ? 52.584  -16.358 38.752 1.00 43.06  ? 24  PRO   A N   1 
ATOM   69   C  CA  . PRO   A  1  11  ? 51.213  -16.816 38.512 1.00 40.03  ? 24  PRO   A CA  1 
ATOM   70   C  C   . PRO   A  1  11  ? 50.695  -17.687 39.645 1.00 37.05  ? 24  PRO   A C   1 
ATOM   71   O  O   . PRO   A  1  11  ? 51.477  -18.311 40.333 1.00 36.45  ? 24  PRO   A O   1 
ATOM   72   C  CB  . PRO   A  1  11  ? 51.303  -17.616 37.206 1.00 42.59  ? 24  PRO   A CB  1 
ATOM   73   C  CG  . PRO   A  1  11  ? 52.597  -17.133 36.558 1.00 43.39  ? 24  PRO   A CG  1 
ATOM   74   C  CD  . PRO   A  1  11  ? 53.534  -16.800 37.713 1.00 40.27  ? 24  PRO   A CD  1 
ATOM   75   N  N   . PRO   A  1  12  ? 49.366  -17.778 39.851 1.00 37.98  ? 25  PRO   A N   1 
ATOM   76   C  CA  . PRO   A  1  12  ? 48.815  -18.714 40.831 1.00 43.27  ? 25  PRO   A CA  1 
ATOM   77   C  C   . PRO   A  1  12  ? 49.038  -20.165 40.394 1.00 42.00  ? 25  PRO   A C   1 
ATOM   78   O  O   . PRO   A  1  12  ? 49.065  -20.454 39.210 1.00 40.84  ? 25  PRO   A O   1 
ATOM   79   C  CB  . PRO   A  1  12  ? 47.340  -18.319 40.886 1.00 44.04  ? 25  PRO   A CB  1 
ATOM   80   C  CG  . PRO   A  1  12  ? 47.052  -17.748 39.514 1.00 46.14  ? 25  PRO   A CG  1 
ATOM   81   C  CD  . PRO   A  1  12  ? 48.337  -17.046 39.114 1.00 38.54  ? 25  PRO   A CD  1 
ATOM   82   N  N   . SER   A  1  13  ? 49.284  -21.035 41.377 1.00 45.77  ? 26  SER   A N   1 
ATOM   83   C  CA  A SER   A  1  13  ? 49.415  -22.475 41.193 0.50 44.30  ? 26  SER   A CA  1 
ATOM   84   C  CA  B SER   A  1  13  ? 49.427  -22.472 41.175 0.50 44.75  ? 26  SER   A CA  1 
ATOM   85   C  C   . SER   A  1  13  ? 48.239  -23.016 40.387 1.00 39.79  ? 26  SER   A C   1 
ATOM   86   O  O   . SER   A  1  13  ? 48.425  -23.763 39.450 1.00 45.20  ? 26  SER   A O   1 
ATOM   87   C  CB  A SER   A  1  13  ? 49.482  -23.179 42.534 0.50 44.38  ? 26  SER   A CB  1 
ATOM   88   C  CB  B SER   A  1  13  ? 49.552  -23.204 42.495 0.50 45.78  ? 26  SER   A CB  1 
ATOM   89   O  OG  A SER   A  1  13  ? 50.531  -22.652 43.326 0.50 46.38  ? 26  SER   A OG  1 
ATOM   90   O  OG  B SER   A  1  13  ? 49.540  -24.610 42.280 0.50 49.01  ? 26  SER   A OG  1 
ATOM   91   N  N   . PHE   A  1  14  ? 47.027  -22.646 40.804 1.00 37.41  ? 27  PHE   A N   1 
ATOM   92   C  CA  . PHE   A  1  14  ? 45.788  -23.060 40.159 1.00 39.49  ? 27  PHE   A CA  1 
ATOM   93   C  C   . PHE   A  1  14  ? 45.267  -21.907 39.295 1.00 37.28  ? 27  PHE   A C   1 
ATOM   94   O  O   . PHE   A  1  14  ? 45.045  -20.810 39.809 1.00 37.28  ? 27  PHE   A O   1 
ATOM   95   C  CB  . PHE   A  1  14  ? 44.744  -23.462 41.207 1.00 35.34  ? 27  PHE   A CB  1 
ATOM   96   C  CG  . PHE   A  1  14  ? 43.428  -23.885 40.567 1.00 40.18  ? 27  PHE   A CG  1 
ATOM   97   C  CD1 . PHE   A  1  14  ? 43.359  -25.069 39.822 1.00 37.88  ? 27  PHE   A CD1 1 
ATOM   98   C  CD2 . PHE   A  1  14  ? 42.274  -23.097 40.677 1.00 37.29  ? 27  PHE   A CD2 1 
ATOM   99   C  CE1 . PHE   A  1  14  ? 42.183  -25.436 39.184 1.00 40.60  ? 27  PHE   A CE1 1 
ATOM   100  C  CE2 . PHE   A  1  14  ? 41.084  -23.482 40.049 1.00 38.89  ? 27  PHE   A CE2 1 
ATOM   101  C  CZ  . PHE   A  1  14  ? 41.040  -24.648 39.306 1.00 39.68  ? 27  PHE   A CZ  1 
ATOM   102  N  N   . THR   A  1  15  ? 45.058  -22.173 37.996 1.00 35.00  ? 28  THR   A N   1 
ATOM   103  C  CA  . THR   A  1  15  ? 44.736  -21.128 37.033 1.00 38.14  ? 28  THR   A CA  1 
ATOM   104  C  C   . THR   A  1  15  ? 43.359  -21.379 36.434 1.00 35.89  ? 28  THR   A C   1 
ATOM   105  O  O   . THR   A  1  15  ? 43.029  -20.720 35.450 1.00 33.72  ? 28  THR   A O   1 
ATOM   106  C  CB  . THR   A  1  15  ? 45.770  -21.050 35.903 1.00 40.86  ? 28  THR   A CB  1 
ATOM   107  O  OG1 . THR   A  1  15  ? 45.669  -22.237 35.113 1.00 38.37  ? 28  THR   A OG1 1 
ATOM   108  C  CG2 . THR   A  1  15  ? 47.184  -20.887 36.418 1.00 43.05  ? 28  THR   A CG2 1 
ATOM   109  N  N   . GLY   A  1  16  ? 42.593  -22.337 36.982 1.00 32.98  ? 29  GLY   A N   1 
ATOM   110  C  CA  . GLY   A  1  16  ? 41.275  -22.625 36.430 1.00 36.33  ? 29  GLY   A CA  1 
ATOM   111  C  C   . GLY   A  1  16  ? 40.199  -21.702 37.011 1.00 36.97  ? 29  GLY   A C   1 
ATOM   112  O  O   . GLY   A  1  16  ? 40.484  -20.837 37.853 1.00 34.79  ? 29  GLY   A O   1 
ATOM   113  N  N   . THR   A  1  17  ? 38.949  -21.932 36.572 1.00 35.62  ? 30  THR   A N   1 
ATOM   114  C  CA  . THR   A  1  17  ? 37.793  -21.236 37.118 1.00 34.51  ? 30  THR   A CA  1 
ATOM   115  C  C   . THR   A  1  17  ? 37.558  -21.716 38.548 1.00 35.41  ? 30  THR   A C   1 
ATOM   116  O  O   . THR   A  1  17  ? 37.937  -22.828 38.910 1.00 35.77  ? 30  THR   A O   1 
ATOM   117  C  CB  . THR   A  1  17  ? 36.536  -21.442 36.278 1.00 35.97  ? 30  THR   A CB  1 
ATOM   118  O  OG1 . THR   A  1  17  ? 35.654  -20.479 36.853 1.00 37.03  ? 30  THR   A OG1 1 
ATOM   119  C  CG2 . THR   A  1  17  ? 35.972  -22.851 36.376 1.00 33.97  ? 30  THR   A CG2 1 
ATOM   120  N  N   . LYS   A  1  18  ? 36.932  -20.852 39.347 1.00 33.29  ? 31  LYS   A N   1 
ATOM   121  C  CA  . LYS   A  1  18  ? 36.508  -21.205 40.693 1.00 34.86  ? 31  LYS   A CA  1 
ATOM   122  C  C   . LYS   A  1  18  ? 35.565  -20.125 41.201 1.00 35.52  ? 31  LYS   A C   1 
ATOM   123  O  O   . LYS   A  1  18  ? 35.522  -19.022 40.653 1.00 37.61  ? 31  LYS   A O   1 
ATOM   124  C  CB  . LYS   A  1  18  ? 37.664  -21.320 41.690 1.00 34.81  ? 31  LYS   A CB  1 
ATOM   125  C  CG  . LYS   A  1  18  ? 38.515  -20.065 41.863 1.00 41.66  ? 31  LYS   A CG  1 
ATOM   126  C  CD  . LYS   A  1  18  ? 39.604  -20.289 42.908 1.00 47.39  ? 31  LYS   A CD  1 
ATOM   127  C  CE  . LYS   A  1  18  ? 40.163  -19.036 43.465 1.00 62.33  ? 31  LYS   A CE  1 
ATOM   128  N  NZ  . LYS   A  1  18  ? 41.053  -19.331 44.592 1.00 70.23  ? 31  LYS   A NZ  1 
ATOM   129  N  N   . LEU   A  1  19  ? 34.835  -20.452 42.268 1.00 33.53  ? 32  LEU   A N   1 
ATOM   130  C  CA  . LEU   A  1  19  ? 33.951  -19.514 42.921 1.00 33.49  ? 32  LEU   A CA  1 
ATOM   131  C  C   . LEU   A  1  19  ? 34.818  -18.475 43.610 1.00 31.83  ? 32  LEU   A C   1 
ATOM   132  O  O   . LEU   A  1  19  ? 35.657  -18.832 44.418 1.00 32.02  ? 32  LEU   A O   1 
ATOM   133  C  CB  . LEU   A  1  19  ? 33.052  -20.242 43.928 1.00 35.70  ? 32  LEU   A CB  1 
ATOM   134  C  CG  . LEU   A  1  19  ? 32.148  -19.341 44.775 1.00 39.30  ? 32  LEU   A CG  1 
ATOM   135  C  CD1 . LEU   A  1  19  ? 31.135  -18.632 43.894 1.00 37.41  ? 32  LEU   A CD1 1 
ATOM   136  C  CD2 . LEU   A  1  19  ? 31.422  -20.095 45.898 1.00 39.78  ? 32  LEU   A CD2 1 
ATOM   137  N  N   . VAL   A  1  20  ? 34.597  -17.193 43.301 1.00 33.98  ? 33  VAL   A N   1 
ATOM   138  C  CA  . VAL   A  1  20  ? 35.372  -16.155 43.955 1.00 31.98  ? 33  VAL   A CA  1 
ATOM   139  C  C   . VAL   A  1  20  ? 34.490  -15.345 44.887 1.00 29.53  ? 33  VAL   A C   1 
ATOM   140  O  O   . VAL   A  1  20  ? 34.996  -14.793 45.861 1.00 31.25  ? 33  VAL   A O   1 
ATOM   141  C  CB  . VAL   A  1  20  ? 36.145  -15.271 42.967 1.00 32.22  ? 33  VAL   A CB  1 
ATOM   142  C  CG1 . VAL   A  1  20  ? 37.210  -16.080 42.243 1.00 31.68  ? 33  VAL   A CG1 1 
ATOM   143  C  CG2 . VAL   A  1  20  ? 35.253  -14.573 41.975 1.00 33.78  ? 33  VAL   A CG2 1 
ATOM   144  N  N   . ASN   A  1  21  ? 33.189  -15.286 44.608 1.00 30.66  ? 34  ASN   A N   1 
ATOM   145  C  CA  . ASN   A  1  21  ? 32.236  -14.683 45.533 1.00 32.51  ? 34  ASN   A CA  1 
ATOM   146  C  C   . ASN   A  1  21  ? 31.819  -15.715 46.580 1.00 33.19  ? 34  ASN   A C   1 
ATOM   147  O  O   . ASN   A  1  21  ? 30.748  -16.288 46.511 1.00 33.72  ? 34  ASN   A O   1 
ATOM   148  C  CB  . ASN   A  1  21  ? 31.040  -14.141 44.772 1.00 33.28  ? 34  ASN   A CB  1 
ATOM   149  C  CG  . ASN   A  1  21  ? 30.087  -13.345 45.632 1.00 33.42  ? 34  ASN   A CG  1 
ATOM   150  O  OD1 . ASN   A  1  21  ? 30.291  -13.168 46.840 1.00 32.31  ? 34  ASN   A OD1 1 
ATOM   151  N  ND2 . ASN   A  1  21  ? 29.038  -12.852 44.997 1.00 32.19  ? 34  ASN   A ND2 1 
ATOM   152  N  N   . ASP   A  1  22  ? 32.671  -15.943 47.575 1.00 37.16  ? 35  ASP   A N   1 
ATOM   153  C  CA  . ASP   A  1  22  ? 32.530  -17.088 48.466 1.00 39.12  ? 35  ASP   A CA  1 
ATOM   154  C  C   . ASP   A  1  22  ? 32.411  -16.590 49.902 1.00 39.11  ? 35  ASP   A C   1 
ATOM   155  O  O   . ASP   A  1  22  ? 32.443  -15.381 50.172 1.00 42.04  ? 35  ASP   A O   1 
ATOM   156  C  CB  . ASP   A  1  22  ? 33.680  -18.068 48.253 1.00 42.74  ? 35  ASP   A CB  1 
ATOM   157  C  CG  . ASP   A  1  22  ? 35.099  -17.571 48.539 1.00 42.43  ? 35  ASP   A CG  1 
ATOM   158  O  OD1 . ASP   A  1  22  ? 35.263  -16.469 49.112 1.00 52.40  ? 35  ASP   A OD1 1 
ATOM   159  O  OD2 . ASP   A  1  22  ? 36.052  -18.297 48.208 1.00 50.92  ? 35  ASP   A OD2 1 
ATOM   160  N  N   . ALA   A  1  23  ? 32.321  -17.537 50.826 1.00 41.01  ? 36  ALA   A N   1 
ATOM   161  C  CA  . ALA   A  1  23  ? 31.970  -17.223 52.203 1.00 48.70  ? 36  ALA   A CA  1 
ATOM   162  C  C   . ALA   A  1  23  ? 33.088  -16.425 52.881 1.00 42.74  ? 36  ALA   A C   1 
ATOM   163  O  O   . ALA   A  1  23  ? 32.818  -15.585 53.726 1.00 39.79  ? 36  ALA   A O   1 
ATOM   164  C  CB  . ALA   A  1  23  ? 31.659  -18.504 52.958 1.00 52.58  ? 36  ALA   A CB  1 
ATOM   165  N  N   . ASP   A  1  24  ? 34.336  -16.681 52.494 1.00 41.71  ? 37  ASP   A N   1 
ATOM   166  C  CA  . ASP   A  1  24  ? 35.468  -15.993 53.089 1.00 40.81  ? 37  ASP   A CA  1 
ATOM   167  C  C   . ASP   A  1  24  ? 35.648  -14.574 52.521 1.00 37.46  ? 37  ASP   A C   1 
ATOM   168  O  O   . ASP   A  1  24  ? 36.440  -13.803 53.059 1.00 35.70  ? 37  ASP   A O   1 
ATOM   169  C  CB  . ASP   A  1  24  ? 36.734  -16.816 52.911 1.00 44.04  ? 37  ASP   A CB  1 
ATOM   170  C  CG  . ASP   A  1  24  ? 37.792  -16.635 53.988 1.00 47.64  ? 37  ASP   A CG  1 
ATOM   171  O  OD1 . ASP   A  1  24  ? 37.415  -16.730 55.169 1.00 54.90  ? 37  ASP   A OD1 1 
ATOM   172  O  OD2 . ASP   A  1  24  ? 38.973  -16.449 53.626 1.00 61.01  ? 37  ASP   A OD2 1 
ATOM   173  N  N   . HIS   A  1  25  ? 34.924  -14.222 51.444 1.00 33.80  ? 38  HIS   A N   1 
ATOM   174  C  CA  . HIS   A  1  25  ? 35.134  -12.959 50.739 1.00 30.49  ? 38  HIS   A CA  1 
ATOM   175  C  C   . HIS   A  1  25  ? 33.782  -12.284 50.525 1.00 30.64  ? 38  HIS   A C   1 
ATOM   176  O  O   . HIS   A  1  25  ? 33.343  -12.048 49.402 1.00 28.49  ? 38  HIS   A O   1 
ATOM   177  C  CB  . HIS   A  1  25  ? 35.926  -13.193 49.435 1.00 32.15  ? 38  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A  1  25  ? 37.298  -13.746 49.650 1.00 32.59  ? 38  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A  1  25  ? 37.640  -15.066 49.428 1.00 34.99  ? 38  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A  1  25  ? 38.429  -13.139 50.029 1.00 34.80  ? 38  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A  1  25  ? 38.936  -15.236 49.689 1.00 37.09  ? 38  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A  1  25  ? 39.436  -14.073 50.049 1.00 36.57  ? 38  HIS   A NE2 1 
ATOM   183  N  N   . PRO   A  1  26  ? 33.032  -12.006 51.610 1.00 27.54  ? 39  PRO   A N   1 
ATOM   184  C  CA  . PRO   A  1  26  ? 31.724  -11.387 51.493 1.00 28.56  ? 39  PRO   A CA  1 
ATOM   185  C  C   . PRO   A  1  26  ? 31.795  -9.904  51.156 1.00 30.01  ? 39  PRO   A C   1 
ATOM   186  O  O   . PRO   A  1  26  ? 32.665  -9.195  51.644 1.00 26.93  ? 39  PRO   A O   1 
ATOM   187  C  CB  . PRO   A  1  26  ? 31.115  -11.582 52.889 1.00 27.41  ? 39  PRO   A CB  1 
ATOM   188  C  CG  . PRO   A  1  26  ? 32.316  -11.588 53.818 1.00 27.25  ? 39  PRO   A CG  1 
ATOM   189  C  CD  . PRO   A  1  26  ? 33.417  -12.249 53.010 1.00 29.17  ? 39  PRO   A CD  1 
ATOM   190  N  N   . TRP   A  1  27  ? 30.836  -9.440  50.364 1.00 28.48  ? 40  TRP   A N   1 
ATOM   191  C  CA  . TRP   A  1  27  ? 30.693  -8.011  50.161 1.00 29.27  ? 40  TRP   A CA  1 
ATOM   192  C  C   . TRP   A  1  27  ? 30.347  -7.377  51.500 1.00 28.81  ? 40  TRP   A C   1 
ATOM   193  O  O   . TRP   A  1  27  ? 29.565  -7.929  52.255 1.00 31.92  ? 40  TRP   A O   1 
ATOM   194  C  CB  . TRP   A  1  27  ? 29.621  -7.727  49.100 1.00 27.29  ? 40  TRP   A CB  1 
ATOM   195  C  CG  . TRP   A  1  27  ? 29.465  -6.263  48.813 1.00 30.15  ? 40  TRP   A CG  1 
ATOM   196  C  CD1 . TRP   A  1  27  ? 30.119  -5.554  47.859 1.00 32.31  ? 40  TRP   A CD1 1 
ATOM   197  C  CD2 . TRP   A  1  27  ? 28.654  -5.318  49.537 1.00 35.42  ? 40  TRP   A CD2 1 
ATOM   198  N  NE1 . TRP   A  1  27  ? 29.743  -4.244  47.905 1.00 34.77  ? 40  TRP   A NE1 1 
ATOM   199  C  CE2 . TRP   A  1  27  ? 28.860  -4.060  48.935 1.00 35.45  ? 40  TRP   A CE2 1 
ATOM   200  C  CE3 . TRP   A  1  27  ? 27.777  -5.412  50.629 1.00 36.86  ? 40  TRP   A CE3 1 
ATOM   201  C  CZ2 . TRP   A  1  27  ? 28.213  -2.904  49.386 1.00 35.41  ? 40  TRP   A CZ2 1 
ATOM   202  C  CZ3 . TRP   A  1  27  ? 27.147  -4.267  51.074 1.00 39.48  ? 40  TRP   A CZ3 1 
ATOM   203  C  CH2 . TRP   A  1  27  ? 27.378  -3.027  50.472 1.00 38.00  ? 40  TRP   A CH2 1 
ATOM   204  N  N   . GLN   A  1  28  ? 30.955  -6.237  51.798 1.00 29.19  ? 41  GLN   A N   1 
ATOM   205  C  CA  . GLN   A  1  28  ? 30.602  -5.471  52.974 1.00 28.56  ? 41  GLN   A CA  1 
ATOM   206  C  C   . GLN   A  1  28  ? 30.579  -3.995  52.604 1.00 30.22  ? 41  GLN   A C   1 
ATOM   207  O  O   . GLN   A  1  28  ? 31.296  -3.555  51.721 1.00 32.65  ? 41  GLN   A O   1 
ATOM   208  C  CB  . GLN   A  1  28  ? 31.598  -5.670  54.108 1.00 30.37  ? 41  GLN   A CB  1 
ATOM   209  C  CG  . GLN   A  1  28  ? 31.582  -7.085  54.653 1.00 36.14  ? 41  GLN   A CG  1 
ATOM   210  C  CD  . GLN   A  1  28  ? 32.629  -7.359  55.704 1.00 33.36  ? 41  GLN   A CD  1 
ATOM   211  O  OE1 . GLN   A  1  28  ? 33.426  -6.499  56.119 1.00 32.52  ? 41  GLN   A OE1 1 
ATOM   212  N  NE2 . GLN   A  1  28  ? 32.614  -8.613  56.121 1.00 34.58  ? 41  GLN   A NE2 1 
ATOM   213  N  N   . PRO   A  1  29  ? 29.731  -3.197  53.271 1.00 35.64  ? 42  PRO   A N   1 
ATOM   214  C  CA  . PRO   A  1  29  ? 29.665  -1.768  53.000 1.00 35.69  ? 42  PRO   A CA  1 
ATOM   215  C  C   . PRO   A  1  29  ? 30.913  -1.038  53.489 1.00 35.77  ? 42  PRO   A C   1 
ATOM   216  O  O   . PRO   A  1  29  ? 31.648  -1.543  54.330 1.00 33.80  ? 42  PRO   A O   1 
ATOM   217  C  CB  . PRO   A  1  29  ? 28.397  -1.325  53.736 1.00 37.61  ? 42  PRO   A CB  1 
ATOM   218  C  CG  . PRO   A  1  29  ? 28.193  -2.356  54.834 1.00 38.28  ? 42  PRO   A CG  1 
ATOM   219  C  CD  . PRO   A  1  29  ? 28.782  -3.651  54.307 1.00 35.97  ? 42  PRO   A CD  1 
ATOM   220  N  N   . LEU   A  1  30  ? 31.130  0.156   52.918 1.00 36.77  ? 43  LEU   A N   1 
ATOM   221  C  CA  . LEU   A  1  30  ? 32.230  1.038   53.277 1.00 35.33  ? 43  LEU   A CA  1 
ATOM   222  C  C   . LEU   A  1  30  ? 32.127  1.486   54.728 1.00 38.50  ? 43  LEU   A C   1 
ATOM   223  O  O   . LEU   A  1  30  ? 31.047  1.790   55.212 1.00 39.11  ? 43  LEU   A O   1 
ATOM   224  C  CB  . LEU   A  1  30  ? 32.184  2.265   52.369 1.00 37.66  ? 43  LEU   A CB  1 
ATOM   225  C  CG  . LEU   A  1  30  ? 32.444  2.032   50.877 1.00 42.18  ? 43  LEU   A CG  1 
ATOM   226  C  CD1 . LEU   A  1  30  ? 32.564  3.386   50.190 1.00 41.27  ? 43  LEU   A CD1 1 
ATOM   227  C  CD2 . LEU   A  1  30  ? 33.681  1.158   50.587 1.00 41.12  ? 43  LEU   A CD2 1 
ATOM   228  N  N   . ARG   A  1  31  ? 33.270  1.512   55.417 1.00 40.14  ? 44  ARG   A N   1 
ATOM   229  C  CA  . ARG   A  1  31  ? 33.416  2.195   56.695 1.00 41.64  ? 44  ARG   A CA  1 
ATOM   230  C  C   . ARG   A  1  31  ? 34.115  3.542   56.487 1.00 47.29  ? 44  ARG   A C   1 
ATOM   231  O  O   . ARG   A  1  31  ? 34.637  3.819   55.416 1.00 44.77  ? 44  ARG   A O   1 
ATOM   232  C  CB  . ARG   A  1  31  ? 34.270  1.376   57.662 1.00 39.07  ? 44  ARG   A CB  1 
ATOM   233  C  CG  . ARG   A  1  31  ? 33.780  -0.035  57.959 1.00 44.91  ? 44  ARG   A CG  1 
ATOM   234  C  CD  . ARG   A  1  31  ? 34.922  -0.884  58.509 1.00 55.36  ? 44  ARG   A CD  1 
ATOM   235  N  NE  . ARG   A  1  31  ? 36.040  -0.826  57.551 1.00 63.22  ? 44  ARG   A NE  1 
ATOM   236  C  CZ  . ARG   A  1  31  ? 37.175  -1.514  57.552 1.00 66.14  ? 44  ARG   A CZ  1 
ATOM   237  N  NH1 . ARG   A  1  31  ? 37.331  -2.546  58.371 1.00 76.44  ? 44  ARG   A NH1 1 
ATOM   238  N  NH2 . ARG   A  1  31  ? 38.130  -1.192  56.692 1.00 56.40  ? 44  ARG   A NH2 1 
ATOM   239  N  N   . GLU   A  1  32  ? 34.121  4.379   57.519 1.00 49.52  ? 45  GLU   A N   1 
ATOM   240  C  CA  . GLU   A  1  32  ? 34.776  5.676   57.464 1.00 58.81  ? 45  GLU   A CA  1 
ATOM   241  C  C   . GLU   A  1  32  ? 36.260  5.462   57.165 1.00 51.60  ? 45  GLU   A C   1 
ATOM   242  O  O   . GLU   A  1  32  ? 36.905  4.625   57.790 1.00 40.23  ? 45  GLU   A O   1 
ATOM   243  C  CB  . GLU   A  1  32  ? 34.567  6.388   58.805 1.00 74.52  ? 45  GLU   A CB  1 
ATOM   244  C  CG  . GLU   A  1  32  ? 35.100  7.818   58.845 1.00 87.57  ? 45  GLU   A CG  1 
ATOM   245  C  CD  . GLU   A  1  32  ? 34.836  8.588   60.134 1.00 109.56 ? 45  GLU   A CD  1 
ATOM   246  O  OE1 . GLU   A  1  32  ? 34.431  8.010   61.171 1.00 113.52 ? 45  GLU   A OE1 1 
ATOM   247  O  OE2 . GLU   A  1  32  ? 35.032  9.818   60.084 1.00 118.71 ? 45  GLU   A OE2 1 
ATOM   248  N  N   . GLY   A  1  33  ? 36.798  6.214   56.200 1.00 48.13  ? 46  GLY   A N   1 
ATOM   249  C  CA  . GLY   A  1  33  ? 38.216  6.144   55.880 1.00 47.10  ? 46  GLY   A CA  1 
ATOM   250  C  C   . GLY   A  1  33  ? 38.554  5.084   54.827 1.00 43.17  ? 46  GLY   A C   1 
ATOM   251  O  O   . GLY   A  1  33  ? 39.696  5.030   54.380 1.00 47.60  ? 46  GLY   A O   1 
ATOM   252  N  N   . ASP   A  1  34  ? 37.601  4.218   54.458 1.00 38.92  ? 47  ASP   A N   1 
ATOM   253  C  CA  . ASP   A  1  34  ? 37.802  3.247   53.387 1.00 37.79  ? 47  ASP   A CA  1 
ATOM   254  C  C   . ASP   A  1  34  ? 37.920  3.987   52.061 1.00 35.09  ? 47  ASP   A C   1 
ATOM   255  O  O   . ASP   A  1  34  ? 37.159  4.896   51.804 1.00 35.24  ? 47  ASP   A O   1 
ATOM   256  C  CB  . ASP   A  1  34  ? 36.692  2.210   53.289 1.00 38.89  ? 47  ASP   A CB  1 
ATOM   257  C  CG  . ASP   A  1  34  ? 36.678  1.136   54.378 1.00 41.50  ? 47  ASP   A CG  1 
ATOM   258  O  OD1 . ASP   A  1  34  ? 37.644  1.090   55.184 1.00 37.82  ? 47  ASP   A OD1 1 
ATOM   259  O  OD2 . ASP   A  1  34  ? 35.685  0.336   54.413 1.00 37.59  ? 47  ASP   A OD2 1 
ATOM   260  N  N   . ILE   A  1  35  ? 38.875  3.578   51.231 1.00 31.46  ? 48  ILE   A N   1 
ATOM   261  C  CA  . ILE   A  1  35  ? 39.179  4.272   49.999 1.00 30.82  ? 48  ILE   A CA  1 
ATOM   262  C  C   . ILE   A  1  35  ? 38.718  3.427   48.813 1.00 28.42  ? 48  ILE   A C   1 
ATOM   263  O  O   . ILE   A  1  35  ? 38.957  2.228   48.741 1.00 26.57  ? 48  ILE   A O   1 
ATOM   264  C  CB  . ILE   A  1  35  ? 40.689  4.556   49.938 1.00 32.09  ? 48  ILE   A CB  1 
ATOM   265  C  CG1 . ILE   A  1  35  ? 41.147  5.495   51.058 1.00 36.30  ? 48  ILE   A CG1 1 
ATOM   266  C  CG2 . ILE   A  1  35  ? 41.077  5.087   48.570 1.00 31.70  ? 48  ILE   A CG2 1 
ATOM   267  C  CD1 . ILE   A  1  35  ? 40.490  6.876   51.045 1.00 37.46  ? 48  ILE   A CD1 1 
ATOM   268  N  N   . ARG   A  1  36  ? 38.092  4.089   47.852 1.00 25.45  ? 49  ARG   A N   1 
ATOM   269  C  CA  . ARG   A  1  36  ? 37.761  3.480   46.587 1.00 26.76  ? 49  ARG   A CA  1 
ATOM   270  C  C   . ARG   A  1  36  ? 38.078  4.514   45.525 1.00 27.16  ? 49  ARG   A C   1 
ATOM   271  O  O   . ARG   A  1  36  ? 38.201  5.688   45.857 1.00 28.82  ? 49  ARG   A O   1 
ATOM   272  C  CB  . ARG   A  1  36  ? 36.280  3.087   46.555 1.00 26.97  ? 49  ARG   A CB  1 
ATOM   273  C  CG  . ARG   A  1  36  ? 35.903  2.051   47.607 1.00 26.61  ? 49  ARG   A CG  1 
ATOM   274  C  CD  . ARG   A  1  36  ? 36.525  0.695   47.277 1.00 27.71  ? 49  ARG   A CD  1 
ATOM   275  N  NE  . ARG   A  1  36  ? 36.071  -0.309  48.242 1.00 27.19  ? 49  ARG   A NE  1 
ATOM   276  C  CZ  . ARG   A  1  36  ? 36.597  -0.528  49.430 1.00 28.48  ? 49  ARG   A CZ  1 
ATOM   277  N  NH1 . ARG   A  1  36  ? 37.610  0.195   49.871 1.00 31.06  ? 49  ARG   A NH1 1 
ATOM   278  N  NH2 . ARG   A  1  36  ? 36.101  -1.483  50.192 1.00 28.80  ? 49  ARG   A NH2 1 
ATOM   279  N  N   . GLY   A  1  37  ? 38.184  4.068   44.265 1.00 28.44  ? 50  GLY   A N   1 
ATOM   280  C  CA  . GLY   A  1  37  ? 38.750  4.894   43.226 1.00 26.00  ? 50  GLY   A CA  1 
ATOM   281  C  C   . GLY   A  1  37  ? 38.180  4.578   41.855 1.00 26.09  ? 50  GLY   A C   1 
ATOM   282  O  O   . GLY   A  1  37  ? 37.078  4.052   41.724 1.00 26.12  ? 50  GLY   A O   1 
ATOM   283  N  N   . PRO   A  1  38  ? 38.953  4.855   40.792 1.00 26.25  ? 51  PRO   A N   1 
ATOM   284  C  CA  . PRO   A  1  38  ? 38.451  4.753   39.427 1.00 28.25  ? 51  PRO   A CA  1 
ATOM   285  C  C   . PRO   A  1  38  ? 38.432  3.347   38.840 1.00 27.65  ? 51  PRO   A C   1 
ATOM   286  O  O   . PRO   A  1  38  ? 37.909  3.186   37.736 1.00 28.54  ? 51  PRO   A O   1 
ATOM   287  C  CB  . PRO   A  1  38  ? 39.447  5.627   38.678 1.00 27.50  ? 51  PRO   A CB  1 
ATOM   288  C  CG  . PRO   A  1  38  ? 40.760  5.381   39.399 1.00 26.82  ? 51  PRO   A CG  1 
ATOM   289  C  CD  . PRO   A  1  38  ? 40.382  5.186   40.847 1.00 28.62  ? 51  PRO   A CD  1 
ATOM   290  N  N   . CYS   A  1  39  ? 39.016  2.365   39.544 1.00 26.12  ? 52  CYS   A N   1 
ATOM   291  C  CA  . CYS   A  1  39  ? 39.114  1.005   39.023 1.00 25.82  ? 52  CYS   A CA  1 
ATOM   292  C  C   . CYS   A  1  39  ? 38.042  0.092   39.618 1.00 25.75  ? 52  CYS   A C   1 
ATOM   293  O  O   . CYS   A  1  39  ? 38.061  -0.236  40.818 1.00 25.79  ? 52  CYS   A O   1 
ATOM   294  C  CB  . CYS   A  1  39  ? 40.460  0.350   39.319 1.00 27.61  ? 52  CYS   A CB  1 
ATOM   295  S  SG  . CYS   A  1  39  ? 40.635  -1.295  38.559 1.00 28.63  ? 52  CYS   A SG  1 
ATOM   296  N  N   . PRO   A  1  40  ? 37.080  -0.382  38.805 1.00 25.20  ? 53  PRO   A N   1 
ATOM   297  C  CA  . PRO   A  1  40  ? 36.032  -1.264  39.322 1.00 27.66  ? 53  PRO   A CA  1 
ATOM   298  C  C   . PRO   A  1  40  ? 36.589  -2.612  39.781 1.00 25.79  ? 53  PRO   A C   1 
ATOM   299  O  O   . PRO   A  1  40  ? 36.054  -3.213  40.694 1.00 29.60  ? 53  PRO   A O   1 
ATOM   300  C  CB  . PRO   A  1  40  ? 35.045  -1.377  38.146 1.00 28.79  ? 53  PRO   A CB  1 
ATOM   301  C  CG  . PRO   A  1  40  ? 35.906  -1.137  36.923 1.00 31.55  ? 53  PRO   A CG  1 
ATOM   302  C  CD  . PRO   A  1  40  ? 36.934  -0.108  37.374 1.00 29.03  ? 53  PRO   A CD  1 
ATOM   303  N  N   . GLY   A  1  41  ? 37.693  -3.062  39.182 1.00 25.62  ? 54  GLY   A N   1 
ATOM   304  C  CA  . GLY   A  1  41  ? 38.321  -4.322  39.567 1.00 24.53  ? 54  GLY   A CA  1 
ATOM   305  C  C   . GLY   A  1  41  ? 38.835  -4.288  41.008 1.00 25.26  ? 54  GLY   A C   1 
ATOM   306  O  O   . GLY   A  1  41  ? 38.388  -5.048  41.866 1.00 26.70  ? 54  GLY   A O   1 
ATOM   307  N  N   . LEU   A  1  42  ? 39.742  -3.345  41.278 1.00 24.52  ? 55  LEU   A N   1 
ATOM   308  C  CA  . LEU   A  1  42  ? 40.311  -3.164  42.597 1.00 24.76  ? 55  LEU   A CA  1 
ATOM   309  C  C   . LEU   A  1  42  ? 39.217  -2.831  43.607 1.00 26.26  ? 55  LEU   A C   1 
ATOM   310  O  O   . LEU   A  1  42  ? 39.263  -3.309  44.736 1.00 23.92  ? 55  LEU   A O   1 
ATOM   311  C  CB  . LEU   A  1  42  ? 41.373  -2.059  42.519 1.00 25.89  ? 55  LEU   A CB  1 
ATOM   312  C  CG  . LEU   A  1  42  ? 42.571  -2.364  41.617 1.00 26.32  ? 55  LEU   A CG  1 
ATOM   313  C  CD1 . LEU   A  1  42  ? 43.581  -1.226  41.616 1.00 27.51  ? 55  LEU   A CD1 1 
ATOM   314  C  CD2 . LEU   A  1  42  ? 43.288  -3.658  42.001 1.00 26.11  ? 55  LEU   A CD2 1 
ATOM   315  N  N   . ASN   A  1  43  ? 38.278  -1.960  43.221 1.00 25.50  ? 56  ASN   A N   1 
ATOM   316  C  CA  . ASN   A  1  43  ? 37.187  -1.592  44.095 1.00 25.09  ? 56  ASN   A CA  1 
ATOM   317  C  C   . ASN   A  1  43  ? 36.411  -2.835  44.541 1.00 26.06  ? 56  ASN   A C   1 
ATOM   318  O  O   . ASN   A  1  43  ? 36.111  -2.988  45.733 1.00 22.69  ? 56  ASN   A O   1 
ATOM   319  C  CB  . ASN   A  1  43  ? 36.226  -0.632  43.414 1.00 25.75  ? 56  ASN   A CB  1 
ATOM   320  C  CG  . ASN   A  1  43  ? 36.754  0.774   43.278 1.00 25.88  ? 56  ASN   A CG  1 
ATOM   321  O  OD1 . ASN   A  1  43  ? 37.757  1.154   43.895 1.00 25.84  ? 56  ASN   A OD1 1 
ATOM   322  N  ND2 . ASN   A  1  43  ? 36.049  1.562   42.479 1.00 25.81  ? 56  ASN   A ND2 1 
ATOM   323  N  N   . THR   A  1  44  ? 36.084  -3.716  43.588 1.00 23.61  ? 57  THR   A N   1 
ATOM   324  C  CA  . THR   A  1  44  ? 35.335  -4.915  43.930 1.00 25.65  ? 57  THR   A CA  1 
ATOM   325  C  C   . THR   A  1  44  ? 36.173  -5.826  44.825 1.00 23.14  ? 57  THR   A C   1 
ATOM   326  O  O   . THR   A  1  44  ? 35.671  -6.357  45.797 1.00 21.68  ? 57  THR   A O   1 
ATOM   327  C  CB  . THR   A  1  44  ? 34.889  -5.630  42.658 1.00 25.44  ? 57  THR   A CB  1 
ATOM   328  O  OG1 . THR   A  1  44  ? 34.044  -4.692  41.991 1.00 25.80  ? 57  THR   A OG1 1 
ATOM   329  C  CG2 . THR   A  1  44  ? 34.133  -6.906  42.965 1.00 24.76  ? 57  THR   A CG2 1 
ATOM   330  N  N   . LEU   A  1  45  ? 37.457  -5.987  44.517 1.00 26.42  ? 58  LEU   A N   1 
ATOM   331  C  CA  . LEU   A  1  45  ? 38.325  -6.815  45.344 1.00 25.20  ? 58  LEU   A CA  1 
ATOM   332  C  C   . LEU   A  1  45  ? 38.419  -6.256  46.768 1.00 27.59  ? 58  LEU   A C   1 
ATOM   333  O  O   . LEU   A  1  45  ? 38.433  -7.021  47.725 1.00 26.92  ? 58  LEU   A O   1 
ATOM   334  C  CB  . LEU   A  1  45  ? 39.698  -6.908  44.699 1.00 26.33  ? 58  LEU   A CB  1 
ATOM   335  C  CG  . LEU   A  1  45  ? 39.748  -7.620  43.356 1.00 26.21  ? 58  LEU   A CG  1 
ATOM   336  C  CD1 . LEU   A  1  45  ? 41.063  -7.339  42.647 1.00 27.24  ? 58  LEU   A CD1 1 
ATOM   337  C  CD2 . LEU   A  1  45  ? 39.582  -9.083  43.546 1.00 26.05  ? 58  LEU   A CD2 1 
ATOM   338  N  N   . ALA   A  1  46  ? 38.494  -4.931  46.928 1.00 26.41  ? 59  ALA   A N   1 
ATOM   339  C  CA  . ALA   A  1  46  ? 38.537  -4.352  48.257 1.00 27.05  ? 59  ALA   A CA  1 
ATOM   340  C  C   . ALA   A  1  46  ? 37.224  -4.593  48.994 1.00 25.37  ? 59  ALA   A C   1 
ATOM   341  O  O   . ALA   A  1  46  ? 37.222  -4.919  50.179 1.00 27.74  ? 59  ALA   A O   1 
ATOM   342  C  CB  . ALA   A  1  46  ? 38.853  -2.880  48.175 1.00 27.91  ? 59  ALA   A CB  1 
ATOM   343  N  N   . SER   A  1  47  ? 36.092  -4.431  48.310 1.00 24.03  ? 60  SER   A N   1 
ATOM   344  C  CA  . SER   A  1  47  ? 34.805  -4.553  48.977 1.00 25.61  ? 60  SER   A CA  1 
ATOM   345  C  C   . SER   A  1  47  ? 34.429  -6.007  49.277 1.00 25.75  ? 60  SER   A C   1 
ATOM   346  O  O   . SER   A  1  47  ? 33.495  -6.222  50.051 1.00 29.73  ? 60  SER   A O   1 
ATOM   347  C  CB  . SER   A  1  47  ? 33.719  -3.850  48.214 1.00 28.16  ? 60  SER   A CB  1 
ATOM   348  O  OG  . SER   A  1  47  ? 33.803  -2.450  48.412 1.00 26.75  ? 60  SER   A OG  1 
ATOM   349  N  N   . HIS   A  1  48  ? 35.138  -6.982  48.687 1.00 25.03  ? 61  HIS   A N   1 
ATOM   350  C  CA  . HIS   A  1  48  ? 34.991  -8.385  49.056 1.00 26.44  ? 61  HIS   A CA  1 
ATOM   351  C  C   . HIS   A  1  48  ? 36.152  -8.922  49.893 1.00 26.91  ? 61  HIS   A C   1 
ATOM   352  O  O   . HIS   A  1  48  ? 36.211  -10.114 50.151 1.00 26.79  ? 61  HIS   A O   1 
ATOM   353  C  CB  . HIS   A  1  48  ? 34.853  -9.260  47.809 1.00 25.13  ? 61  HIS   A CB  1 
ATOM   354  C  CG  . HIS   A  1  48  ? 33.483  -9.202  47.208 1.00 27.82  ? 61  HIS   A CG  1 
ATOM   355  N  ND1 . HIS   A  1  48  ? 32.500  -10.135 47.478 1.00 27.91  ? 61  HIS   A ND1 1 
ATOM   356  C  CD2 . HIS   A  1  48  ? 32.948  -8.335  46.336 1.00 28.81  ? 61  HIS   A CD2 1 
ATOM   357  C  CE1 . HIS   A  1  48  ? 31.427  -9.844  46.762 1.00 30.11  ? 61  HIS   A CE1 1 
ATOM   358  N  NE2 . HIS   A  1  48  ? 31.673  -8.745  46.065 1.00 30.80  ? 61  HIS   A NE2 1 
ATOM   359  N  N   . GLY   A  1  49  ? 37.093  -8.068  50.299 1.00 25.73  ? 62  GLY   A N   1 
ATOM   360  C  CA  . GLY   A  1  49  ? 38.163  -8.493  51.205 1.00 25.47  ? 62  GLY   A CA  1 
ATOM   361  C  C   . GLY   A  1  49  ? 39.284  -9.297  50.541 1.00 24.39  ? 62  GLY   A C   1 
ATOM   362  O  O   . GLY   A  1  49  ? 40.103  -9.850  51.233 1.00 29.34  ? 62  GLY   A O   1 
ATOM   363  N  N   . TYR   A  1  50  ? 39.362  -9.340  49.216 1.00 25.58  ? 63  TYR   A N   1 
ATOM   364  C  CA  . TYR   A  1  50  ? 40.536  -9.843  48.509 1.00 26.11  ? 63  TYR   A CA  1 
ATOM   365  C  C   . TYR   A  1  50  ? 41.735  -8.911  48.687 1.00 28.60  ? 63  TYR   A C   1 
ATOM   366  O  O   . TYR   A  1  50  ? 42.875  -9.354  48.668 1.00 30.35  ? 63  TYR   A O   1 
ATOM   367  C  CB  . TYR   A  1  50  ? 40.254  -10.025 47.009 1.00 26.97  ? 63  TYR   A CB  1 
ATOM   368  C  CG  . TYR   A  1  50  ? 39.533  -11.328 46.725 1.00 27.88  ? 63  TYR   A CG  1 
ATOM   369  C  CD1 . TYR   A  1  50  ? 40.239  -12.533 46.681 1.00 31.89  ? 63  TYR   A CD1 1 
ATOM   370  C  CD2 . TYR   A  1  50  ? 38.157  -11.366 46.560 1.00 26.89  ? 63  TYR   A CD2 1 
ATOM   371  C  CE1 . TYR   A  1  50  ? 39.586  -13.741 46.474 1.00 31.71  ? 63  TYR   A CE1 1 
ATOM   372  C  CE2 . TYR   A  1  50  ? 37.505  -12.561 46.329 1.00 28.22  ? 63  TYR   A CE2 1 
ATOM   373  C  CZ  . TYR   A  1  50  ? 38.215  -13.746 46.286 1.00 29.55  ? 63  TYR   A CZ  1 
ATOM   374  O  OH  . TYR   A  1  50  ? 37.557  -14.910 46.094 1.00 30.17  ? 63  TYR   A OH  1 
ATOM   375  N  N   . LEU   A  1  51  ? 41.450  -7.610  48.743 1.00 33.58  ? 64  LEU   A N   1 
ATOM   376  C  CA  . LEU   A  1  51  ? 42.370  -6.570  49.168 1.00 31.42  ? 64  LEU   A CA  1 
ATOM   377  C  C   . LEU   A  1  51  ? 41.927  -6.127  50.555 1.00 32.87  ? 64  LEU   A C   1 
ATOM   378  O  O   . LEU   A  1  51  ? 40.755  -6.277  50.893 1.00 31.66  ? 64  LEU   A O   1 
ATOM   379  C  CB  . LEU   A  1  51  ? 42.300  -5.369  48.229 1.00 30.47  ? 64  LEU   A CB  1 
ATOM   380  C  CG  . LEU   A  1  51  ? 42.885  -5.562  46.831 1.00 36.48  ? 64  LEU   A CG  1 
ATOM   381  C  CD1 . LEU   A  1  51  ? 42.607  -4.337  46.003 1.00 35.98  ? 64  LEU   A CD1 1 
ATOM   382  C  CD2 . LEU   A  1  51  ? 44.375  -5.838  46.901 1.00 39.40  ? 64  LEU   A CD2 1 
ATOM   383  N  N   . PRO   A  1  52  ? 42.806  -5.475  51.346 1.00 31.75  ? 65  PRO   A N   1 
ATOM   384  C  CA  . PRO   A  1  52  ? 42.357  -4.770  52.547 1.00 30.13  ? 65  PRO   A CA  1 
ATOM   385  C  C   . PRO   A  1  52  ? 41.152  -3.878  52.229 1.00 28.17  ? 65  PRO   A C   1 
ATOM   386  O  O   . PRO   A  1  52  ? 41.145  -3.156  51.233 1.00 29.11  ? 65  PRO   A O   1 
ATOM   387  C  CB  . PRO   A  1  52  ? 43.607  -3.986  52.964 1.00 31.58  ? 65  PRO   A CB  1 
ATOM   388  C  CG  . PRO   A  1  52  ? 44.766  -4.784  52.412 1.00 31.54  ? 65  PRO   A CG  1 
ATOM   389  C  CD  . PRO   A  1  52  ? 44.253  -5.354  51.104 1.00 33.08  ? 65  PRO   A CD  1 
ATOM   390  N  N   . ARG   A  1  53  ? 40.126  -3.946  53.086 1.00 27.71  ? 66  ARG   A N   1 
ATOM   391  C  CA  . ARG   A  1  53  ? 38.849  -3.309  52.827 1.00 28.84  ? 66  ARG   A CA  1 
ATOM   392  C  C   . ARG   A  1  53  ? 38.964  -1.788  52.850 1.00 29.43  ? 66  ARG   A C   1 
ATOM   393  O  O   . ARG   A  1  53  ? 38.065  -1.099  52.375 1.00 29.62  ? 66  ARG   A O   1 
ATOM   394  C  CB  . ARG   A  1  53  ? 37.815  -3.833  53.834 1.00 32.28  ? 66  ARG   A CB  1 
ATOM   395  C  CG  . ARG   A  1  53  ? 37.506  -5.307  53.597 1.00 32.40  ? 66  ARG   A CG  1 
ATOM   396  C  CD  . ARG   A  1  53  ? 36.426  -5.840  54.487 1.00 34.31  ? 66  ARG   A CD  1 
ATOM   397  N  NE  . ARG   A  1  53  ? 36.183  -7.261  54.232 1.00 32.94  ? 66  ARG   A NE  1 
ATOM   398  C  CZ  . ARG   A  1  53  ? 35.285  -7.712  53.359 1.00 33.39  ? 66  ARG   A CZ  1 
ATOM   399  N  NH1 . ARG   A  1  53  ? 34.593  -6.886  52.588 1.00 29.82  ? 66  ARG   A NH1 1 
ATOM   400  N  NH2 . ARG   A  1  53  ? 35.090  -9.010  53.232 1.00 35.22  ? 66  ARG   A NH2 1 
ATOM   401  N  N   . ASP   A  1  54  ? 40.070  -1.268  53.387 1.00 29.25  ? 67  ASP   A N   1 
ATOM   402  C  CA  . ASP   A  1  54  ? 40.283  0.170   53.441 1.00 32.26  ? 67  ASP   A CA  1 
ATOM   403  C  C   . ASP   A  1  54  ? 40.839  0.701   52.133 1.00 30.27  ? 67  ASP   A C   1 
ATOM   404  O  O   . ASP   A  1  54  ? 40.930  1.909   51.958 1.00 30.64  ? 67  ASP   A O   1 
ATOM   405  C  CB  . ASP   A  1  54  ? 41.140  0.617   54.615 1.00 36.98  ? 67  ASP   A CB  1 
ATOM   406  C  CG  . ASP   A  1  54  ? 42.561  0.087   54.658 1.00 43.20  ? 67  ASP   A CG  1 
ATOM   407  O  OD1 . ASP   A  1  54  ? 42.959  -0.593  53.687 1.00 44.01  ? 67  ASP   A OD1 1 
ATOM   408  O  OD2 . ASP   A  1  54  ? 43.245  0.345   55.679 1.00 50.08  ? 67  ASP   A OD2 1 
ATOM   409  N  N   . GLY   A  1  55  ? 41.188  -0.180  51.201 1.00 29.04  ? 68  GLY   A N   1 
ATOM   410  C  CA  . GLY   A  1  55  ? 41.539  0.268   49.861 1.00 29.42  ? 68  GLY   A CA  1 
ATOM   411  C  C   . GLY   A  1  55  ? 42.992  0.711   49.746 1.00 28.82  ? 68  GLY   A C   1 
ATOM   412  O  O   . GLY   A  1  55  ? 43.354  1.387   48.793 1.00 29.42  ? 68  GLY   A O   1 
ATOM   413  N  N   . VAL   A  1  56  ? 43.826  0.296   50.704 1.00 30.55  ? 69  VAL   A N   1 
ATOM   414  C  CA  . VAL   A  1  56  ? 45.245  0.601   50.686 1.00 34.24  ? 69  VAL   A CA  1 
ATOM   415  C  C   . VAL   A  1  56  ? 45.991  -0.718  50.813 1.00 30.41  ? 69  VAL   A C   1 
ATOM   416  O  O   . VAL   A  1  56  ? 45.771  -1.442  51.767 1.00 32.42  ? 69  VAL   A O   1 
ATOM   417  C  CB  . VAL   A  1  56  ? 45.599  1.575   51.835 1.00 34.98  ? 69  VAL   A CB  1 
ATOM   418  C  CG1 . VAL   A  1  56  ? 47.099  1.732   52.026 1.00 35.88  ? 69  VAL   A CG1 1 
ATOM   419  C  CG2 . VAL   A  1  56  ? 44.963  2.935   51.600 1.00 36.04  ? 69  VAL   A CG2 1 
ATOM   420  N  N   . ALA   A  1  57  ? 46.894  -0.986  49.885 1.00 28.18  ? 70  ALA   A N   1 
ATOM   421  C  CA  . ALA   A  1  57  ? 47.516  -2.289  49.784 1.00 32.23  ? 70  ALA   A CA  1 
ATOM   422  C  C   . ALA   A  1  57  ? 48.947  -2.173  49.262 1.00 31.86  ? 70  ALA   A C   1 
ATOM   423  O  O   . ALA   A  1  57  ? 49.312  -1.153  48.671 1.00 28.68  ? 70  ALA   A O   1 
ATOM   424  C  CB  . ALA   A  1  57  ? 46.673  -3.137  48.862 1.00 32.85  ? 70  ALA   A CB  1 
ATOM   425  N  N   . THR   A  1  58  ? 49.728  -3.250  49.462 1.00 28.97  ? 71  THR   A N   1 
ATOM   426  C  CA  . THR   A  1  58  ? 51.041  -3.365  48.857 1.00 28.08  ? 71  THR   A CA  1 
ATOM   427  C  C   . THR   A  1  58  ? 50.872  -3.788  47.414 1.00 28.17  ? 71  THR   A C   1 
ATOM   428  O  O   . THR   A  1  58  ? 49.853  -4.358  47.062 1.00 30.07  ? 71  THR   A O   1 
ATOM   429  C  CB  . THR   A  1  58  ? 51.948  -4.350  49.592 1.00 31.28  ? 71  THR   A CB  1 
ATOM   430  O  OG1 . THR   A  1  58  ? 51.431  -5.647  49.339 1.00 31.73  ? 71  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A  1  58  ? 52.058  -4.083  51.091 1.00 27.33  ? 71  THR   A CG2 1 
ATOM   432  N  N   . PRO   A  1  59  ? 51.870  -3.530  46.550 1.00 30.41  ? 72  PRO   A N   1 
ATOM   433  C  CA  . PRO   A  1  59  ? 51.881  -4.074  45.200 1.00 31.19  ? 72  PRO   A CA  1 
ATOM   434  C  C   . PRO   A  1  59  ? 51.661  -5.584  45.174 1.00 33.55  ? 72  PRO   A C   1 
ATOM   435  O  O   . PRO   A  1  59  ? 50.947  -6.093  44.321 1.00 32.77  ? 72  PRO   A O   1 
ATOM   436  C  CB  . PRO   A  1  59  ? 53.287  -3.698  44.710 1.00 30.51  ? 72  PRO   A CB  1 
ATOM   437  C  CG  . PRO   A  1  59  ? 53.592  -2.410  45.447 1.00 31.98  ? 72  PRO   A CG  1 
ATOM   438  C  CD  . PRO   A  1  59  ? 53.029  -2.656  46.816 1.00 30.93  ? 72  PRO   A CD  1 
ATOM   439  N  N   . ALA   A  1  60  ? 52.338  -6.291  46.070 1.00 30.48  ? 73  ALA   A N   1 
ATOM   440  C  CA  . ALA   A  1  60  ? 52.224  -7.734  46.131 1.00 31.15  ? 73  ALA   A CA  1 
ATOM   441  C  C   . ALA   A  1  60  ? 50.774  -8.141  46.408 1.00 32.02  ? 73  ALA   A C   1 
ATOM   442  O  O   . ALA   A  1  60  ? 50.278  -9.074  45.804 1.00 28.88  ? 73  ALA   A O   1 
ATOM   443  C  CB  . ALA   A  1  60  ? 53.145  -8.291  47.202 1.00 29.30  ? 73  ALA   A CB  1 
ATOM   444  N  N   . GLN   A  1  61  ? 50.103  -7.464  47.344 1.00 29.89  ? 74  GLN   A N   1 
ATOM   445  C  CA  . GLN   A  1  61  ? 48.719  -7.783  47.646 1.00 29.46  ? 74  GLN   A CA  1 
ATOM   446  C  C   . GLN   A  1  61  ? 47.811  -7.534  46.447 1.00 29.52  ? 74  GLN   A C   1 
ATOM   447  O  O   . GLN   A  1  61  ? 46.883  -8.291  46.226 1.00 28.58  ? 74  GLN   A O   1 
ATOM   448  C  CB  . GLN   A  1  61  ? 48.208  -6.994  48.843 1.00 30.45  ? 74  GLN   A CB  1 
ATOM   449  C  CG  . GLN   A  1  61  ? 48.820  -7.448  50.162 1.00 31.54  ? 74  GLN   A CG  1 
ATOM   450  C  CD  . GLN   A  1  61  ? 48.459  -6.513  51.298 1.00 36.74  ? 74  GLN   A CD  1 
ATOM   451  O  OE1 . GLN   A  1  61  ? 48.400  -5.288  51.137 1.00 36.90  ? 74  GLN   A OE1 1 
ATOM   452  N  NE2 . GLN   A  1  61  ? 48.152  -7.082  52.452 1.00 36.32  ? 74  GLN   A NE2 1 
ATOM   453  N  N   . ILE   A  1  62  ? 48.075  -6.469  45.690 1.00 28.28  ? 75  ILE   A N   1 
ATOM   454  C  CA  . ILE   A  1  62  ? 47.256  -6.112  44.548 1.00 29.47  ? 75  ILE   A CA  1 
ATOM   455  C  C   . ILE   A  1  62  ? 47.396  -7.201  43.492 1.00 28.01  ? 75  ILE   A C   1 
ATOM   456  O  O   . ILE   A  1  62  ? 46.417  -7.649  42.899 1.00 29.08  ? 75  ILE   A O   1 
ATOM   457  C  CB  . ILE   A  1  62  ? 47.625  -4.703  44.034 1.00 28.54  ? 75  ILE   A CB  1 
ATOM   458  C  CG1 . ILE   A  1  62  ? 47.187  -3.655  45.055 1.00 33.06  ? 75  ILE   A CG1 1 
ATOM   459  C  CG2 . ILE   A  1  62  ? 47.016  -4.413  42.664 1.00 29.26  ? 75  ILE   A CG2 1 
ATOM   460  C  CD1 . ILE   A  1  62  ? 47.682  -2.242  44.793 1.00 33.94  ? 75  ILE   A CD1 1 
ATOM   461  N  N   . ILE   A  1  63  ? 48.626  -7.646  43.274 1.00 28.44  ? 76  ILE   A N   1 
ATOM   462  C  CA  . ILE   A  1  63  ? 48.879  -8.656  42.263 1.00 27.91  ? 76  ILE   A CA  1 
ATOM   463  C  C   . ILE   A  1  63  ? 48.167  -9.951  42.632 1.00 26.55  ? 76  ILE   A C   1 
ATOM   464  O  O   . ILE   A  1  63  ? 47.440  -10.483 41.807 1.00 26.67  ? 76  ILE   A O   1 
ATOM   465  C  CB  . ILE   A  1  63  ? 50.375  -8.834  42.011 1.00 27.95  ? 76  ILE   A CB  1 
ATOM   466  C  CG1 . ILE   A  1  63  ? 50.910  -7.606  41.277 1.00 31.59  ? 76  ILE   A CG1 1 
ATOM   467  C  CG2 . ILE   A  1  63  ? 50.671  -10.113 41.237 1.00 26.96  ? 76  ILE   A CG2 1 
ATOM   468  C  CD1 . ILE   A  1  63  ? 52.391  -7.363  41.495 1.00 34.94  ? 76  ILE   A CD1 1 
ATOM   469  N  N   . THR   A  1  64  ? 48.322  -10.428 43.863 1.00 27.90  ? 77  THR   A N   1 
ATOM   470  C  CA  A THR   A  1  64  ? 47.722  -11.695 44.248 0.50 30.20  ? 77  THR   A CA  1 
ATOM   471  C  CA  B THR   A  1  64  ? 47.725  -11.705 44.229 0.50 30.26  ? 77  THR   A CA  1 
ATOM   472  C  C   . THR   A  1  64  ? 46.200  -11.569 44.203 1.00 29.95  ? 77  THR   A C   1 
ATOM   473  O  O   . THR   A  1  64  ? 45.519  -12.458 43.728 1.00 31.76  ? 77  THR   A O   1 
ATOM   474  C  CB  A THR   A  1  64  ? 48.223  -12.123 45.625 0.50 28.82  ? 77  THR   A CB  1 
ATOM   475  C  CB  B THR   A  1  64  ? 48.311  -12.337 45.506 0.50 29.79  ? 77  THR   A CB  1 
ATOM   476  O  OG1 A THR   A  1  64  ? 47.690  -11.088 46.445 0.50 36.31  ? 77  THR   A OG1 1 
ATOM   477  O  OG1 B THR   A  1  64  ? 47.304  -12.961 46.315 0.50 25.11  ? 77  THR   A OG1 1 
ATOM   478  C  CG2 A THR   A  1  64  ? 49.734  -12.255 45.689 0.50 23.57  ? 77  THR   A CG2 1 
ATOM   479  C  CG2 B THR   A  1  64  ? 49.092  -11.409 46.411 0.50 31.69  ? 77  THR   A CG2 1 
ATOM   480  N  N   . ALA   A  1  65  ? 45.664  -10.424 44.638 1.00 29.81  ? 78  ALA   A N   1 
ATOM   481  C  CA  . ALA   A  1  65  ? 44.222  -10.191 44.605 1.00 26.40  ? 78  ALA   A CA  1 
ATOM   482  C  C   . ALA   A  1  65  ? 43.659  -10.215 43.187 1.00 27.88  ? 78  ALA   A C   1 
ATOM   483  O  O   . ALA   A  1  65  ? 42.598  -10.799 42.974 1.00 30.07  ? 78  ALA   A O   1 
ATOM   484  C  CB  . ALA   A  1  65  ? 43.854  -8.898  45.264 1.00 27.95  ? 78  ALA   A CB  1 
ATOM   485  N  N   . THR   A  1  66  ? 44.318  -9.571  42.222 1.00 25.37  ? 79  THR   A N   1 
ATOM   486  C  CA  . THR   A  1  66  ? 43.785  -9.533  40.873 1.00 27.24  ? 79  THR   A CA  1 
ATOM   487  C  C   . THR   A  1  66  ? 43.841  -10.931 40.259 1.00 27.56  ? 79  THR   A C   1 
ATOM   488  O  O   . THR   A  1  66  ? 42.980  -11.285 39.455 1.00 26.10  ? 79  THR   A O   1 
ATOM   489  C  CB  . THR   A  1  66  ? 44.491  -8.499  39.992 1.00 29.05  ? 79  THR   A CB  1 
ATOM   490  O  OG1 . THR   A  1  66  ? 45.869  -8.843  39.949 1.00 31.14  ? 79  THR   A OG1 1 
ATOM   491  C  CG2 . THR   A  1  66  ? 44.305  -7.083  40.513 1.00 30.35  ? 79  THR   A CG2 1 
ATOM   492  N  N   . GLN   A  1  67  ? 44.852  -11.718 40.626 1.00 29.20  ? 80  GLN   A N   1 
ATOM   493  C  CA  . GLN   A  1  67  ? 44.950  -13.109 40.187 1.00 30.01  ? 80  GLN   A CA  1 
ATOM   494  C  C   . GLN   A  1  67  ? 43.890  -13.984 40.859 1.00 28.84  ? 80  GLN   A C   1 
ATOM   495  O  O   . GLN   A  1  67  ? 43.155  -14.675 40.199 1.00 30.49  ? 80  GLN   A O   1 
ATOM   496  C  CB  . GLN   A  1  67  ? 46.369  -13.627 40.429 1.00 32.69  ? 80  GLN   A CB  1 
ATOM   497  C  CG  . GLN   A  1  67  ? 47.396  -12.873 39.585 1.00 33.32  ? 80  GLN   A CG  1 
ATOM   498  C  CD  . GLN   A  1  67  ? 48.839  -13.303 39.737 1.00 30.62  ? 80  GLN   A CD  1 
ATOM   499  O  OE1 . GLN   A  1  67  ? 49.672  -12.950 38.906 1.00 36.34  ? 80  GLN   A OE1 1 
ATOM   500  N  NE2 . GLN   A  1  67  ? 49.167  -14.067 40.764 1.00 31.84  ? 80  GLN   A NE2 1 
ATOM   501  N  N   . GLU   A  1  68  ? 43.794  -13.947 42.173 1.00 31.74  ? 81  GLU   A N   1 
ATOM   502  C  CA  . GLU   A  1  68  ? 42.876  -14.799 42.905 1.00 35.44  ? 81  GLU   A CA  1 
ATOM   503  C  C   . GLU   A  1  68  ? 41.439  -14.478 42.537 1.00 31.78  ? 81  GLU   A C   1 
ATOM   504  O  O   . GLU   A  1  68  ? 40.645  -15.383 42.323 1.00 31.11  ? 81  GLU   A O   1 
ATOM   505  C  CB  . GLU   A  1  68  ? 43.040  -14.643 44.418 1.00 37.53  ? 81  GLU   A CB  1 
ATOM   506  C  CG  . GLU   A  1  68  ? 44.320  -15.278 44.955 1.00 49.20  ? 81  GLU   A CG  1 
ATOM   507  C  CD  . GLU   A  1  68  ? 44.569  -16.743 44.597 1.00 57.26  ? 81  GLU   A CD  1 
ATOM   508  O  OE1 . GLU   A  1  68  ? 45.716  -17.088 44.196 1.00 54.72  ? 81  GLU   A OE1 1 
ATOM   509  O  OE2 . GLU   A  1  68  ? 43.595  -17.524 44.698 1.00 63.10  ? 81  GLU   A OE2 1 
ATOM   510  N  N   . GLY   A  1  69  ? 41.119  -13.179 42.463 1.00 32.98  ? 82  GLY   A N   1 
ATOM   511  C  CA  . GLY   A  1  69  ? 39.745  -12.718 42.304 1.00 26.86  ? 82  GLY   A CA  1 
ATOM   512  C  C   . GLY   A  1  69  ? 39.250  -12.827 40.866 1.00 26.65  ? 82  GLY   A C   1 
ATOM   513  O  O   . GLY   A  1  69  ? 38.082  -13.115 40.646 1.00 26.45  ? 82  GLY   A O   1 
ATOM   514  N  N   . PHE   A  1  70  ? 40.112  -12.524 39.891 1.00 28.16  ? 83  PHE   A N   1 
ATOM   515  C  CA  . PHE   A  1  70  ? 39.665  -12.368 38.518 1.00 27.28  ? 83  PHE   A CA  1 
ATOM   516  C  C   . PHE   A  1  70  ? 40.476  -13.186 37.521 1.00 26.23  ? 83  PHE   A C   1 
ATOM   517  O  O   . PHE   A  1  70  ? 40.154  -13.149 36.348 1.00 29.38  ? 83  PHE   A O   1 
ATOM   518  C  CB  . PHE   A  1  70  ? 39.768  -10.906 38.070 1.00 26.99  ? 83  PHE   A CB  1 
ATOM   519  C  CG  . PHE   A  1  70  ? 38.682  -10.021 38.645 1.00 26.92  ? 83  PHE   A CG  1 
ATOM   520  C  CD1 . PHE   A  1  70  ? 37.379  -10.116 38.188 1.00 27.49  ? 83  PHE   A CD1 1 
ATOM   521  C  CD2 . PHE   A  1  70  ? 38.961  -9.098  39.636 1.00 29.14  ? 83  PHE   A CD2 1 
ATOM   522  C  CE1 . PHE   A  1  70  ? 36.378  -9.327  38.705 1.00 26.48  ? 83  PHE   A CE1 1 
ATOM   523  C  CE2 . PHE   A  1  70  ? 37.959  -8.292  40.136 1.00 27.63  ? 83  PHE   A CE2 1 
ATOM   524  C  CZ  . PHE   A  1  70  ? 36.675  -8.416  39.679 1.00 30.06  ? 83  PHE   A CZ  1 
ATOM   525  N  N   . ASN   A  1  71  ? 41.551  -13.842 37.960 1.00 30.91  ? 84  ASN   A N   1 
ATOM   526  C  CA  . ASN   A  1  71  ? 42.490  -14.531 37.083 1.00 27.48  ? 84  ASN   A CA  1 
ATOM   527  C  C   . ASN   A  1  71  ? 43.149  -13.544 36.128 1.00 25.42  ? 84  ASN   A C   1 
ATOM   528  O  O   . ASN   A  1  71  ? 43.418  -13.863 34.969 1.00 25.79  ? 84  ASN   A O   1 
ATOM   529  C  CB  . ASN   A  1  71  ? 41.825  -15.664 36.301 1.00 30.51  ? 84  ASN   A CB  1 
ATOM   530  C  CG  . ASN   A  1  71  ? 42.698  -16.905 36.218 1.00 33.17  ? 84  ASN   A CG  1 
ATOM   531  O  OD1 . ASN   A  1  71  ? 43.902  -16.873 36.520 1.00 32.16  ? 84  ASN   A OD1 1 
ATOM   532  N  ND2 . ASN   A  1  71  ? 42.095  -18.029 35.862 1.00 33.96  ? 84  ASN   A ND2 1 
ATOM   533  N  N   . PHE   A  1  72  ? 43.427  -12.335 36.605 1.00 26.34  ? 85  PHE   A N   1 
ATOM   534  C  CA  . PHE   A  1  72  ? 44.185  -11.398 35.797 1.00 27.76  ? 85  PHE   A CA  1 
ATOM   535  C  C   . PHE   A  1  72  ? 45.567  -12.011 35.548 1.00 28.05  ? 85  PHE   A C   1 
ATOM   536  O  O   . PHE   A  1  72  ? 46.165  -12.564 36.462 1.00 24.73  ? 85  PHE   A O   1 
ATOM   537  C  CB  . PHE   A  1  72  ? 44.249  -10.082 36.568 1.00 28.18  ? 85  PHE   A CB  1 
ATOM   538  C  CG  . PHE   A  1  72  ? 44.623  -8.872  35.739 1.00 28.55  ? 85  PHE   A CG  1 
ATOM   539  C  CD1 . PHE   A  1  72  ? 43.987  -8.625  34.541 1.00 33.71  ? 85  PHE   A CD1 1 
ATOM   540  C  CD2 . PHE   A  1  72  ? 45.573  -7.968  36.178 1.00 29.55  ? 85  PHE   A CD2 1 
ATOM   541  C  CE1 . PHE   A  1  72  ? 44.276  -7.484  33.817 1.00 35.25  ? 85  PHE   A CE1 1 
ATOM   542  C  CE2 . PHE   A  1  72  ? 45.860  -6.832  35.453 1.00 31.21  ? 85  PHE   A CE2 1 
ATOM   543  C  CZ  . PHE   A  1  72  ? 45.236  -6.608  34.254 1.00 32.09  ? 85  PHE   A CZ  1 
ATOM   544  N  N   . GLU   A  1  73  ? 46.044  -11.974 34.309 1.00 28.63  ? 86  GLU   A N   1 
ATOM   545  C  CA  . GLU   A  1  73  ? 47.304  -12.607 33.973 1.00 29.07  ? 86  GLU   A CA  1 
ATOM   546  C  C   . GLU   A  1  73  ? 48.476  -11.906 34.672 1.00 30.50  ? 86  GLU   A C   1 
ATOM   547  O  O   . GLU   A  1  73  ? 48.499  -10.688 34.797 1.00 28.82  ? 86  GLU   A O   1 
ATOM   548  C  CB  . GLU   A  1  73  ? 47.395  -12.644 32.450 1.00 34.39  ? 86  GLU   A CB  1 
ATOM   549  C  CG  . GLU   A  1  73  ? 48.595  -13.431 31.919 1.00 37.32  ? 86  GLU   A CG  1 
ATOM   550  C  CD  . GLU   A  1  73  ? 49.909  -12.652 31.836 1.00 47.54  ? 86  GLU   A CD  1 
ATOM   551  O  OE1 . GLU   A  1  73  ? 50.987  -13.261 32.172 1.00 48.26  ? 86  GLU   A OE1 1 
ATOM   552  O  OE2 . GLU   A  1  73  ? 49.855  -11.431 31.472 1.00 46.45  ? 86  GLU   A OE2 1 
ATOM   553  N  N   . ASN   A  1  74  ? 49.467  -12.699 35.100 1.00 30.88  ? 87  ASN   A N   1 
ATOM   554  C  CA  . ASN   A  1  74  ? 50.516  -12.269 36.009 1.00 33.77  ? 87  ASN   A CA  1 
ATOM   555  C  C   . ASN   A  1  74  ? 51.301  -11.067 35.468 1.00 35.79  ? 87  ASN   A C   1 
ATOM   556  O  O   . ASN   A  1  74  ? 51.540  -10.089 36.191 1.00 32.59  ? 87  ASN   A O   1 
ATOM   557  C  CB  . ASN   A  1  74  ? 51.444  -13.429 36.334 1.00 34.73  ? 87  ASN   A CB  1 
ATOM   558  C  CG  . ASN   A  1  74  ? 52.614  -13.056 37.219 1.00 31.79  ? 87  ASN   A CG  1 
ATOM   559  O  OD1 . ASN   A  1  74  ? 53.772  -13.105 36.781 1.00 37.00  ? 87  ASN   A OD1 1 
ATOM   560  N  ND2 . ASN   A  1  74  ? 52.352  -12.714 38.465 1.00 31.55  ? 87  ASN   A ND2 1 
ATOM   561  N  N   . ASN   A  1  75  ? 51.738  -11.141 34.212 1.00 35.13  ? 88  ASN   A N   1 
ATOM   562  C  CA  A ASN   A  1  75  ? 52.564  -10.081 33.658 0.50 35.18  ? 88  ASN   A CA  1 
ATOM   563  C  CA  B ASN   A  1  75  ? 52.556  -10.085 33.641 0.50 36.19  ? 88  ASN   A CA  1 
ATOM   564  C  C   . ASN   A  1  75  ? 51.742  -8.795  33.517 1.00 35.64  ? 88  ASN   A C   1 
ATOM   565  O  O   . ASN   A  1  75  ? 52.234  -7.699  33.821 1.00 33.62  ? 88  ASN   A O   1 
ATOM   566  C  CB  A ASN   A  1  75  ? 53.326  -10.560 32.426 0.50 35.63  ? 88  ASN   A CB  1 
ATOM   567  C  CB  B ASN   A  1  75  ? 53.154  -10.512 32.307 0.50 37.90  ? 88  ASN   A CB  1 
ATOM   568  C  CG  A ASN   A  1  75  ? 54.545  -11.386 32.827 0.50 36.35  ? 88  ASN   A CG  1 
ATOM   569  C  CG  B ASN   A  1  75  ? 54.493  -9.889  32.075 0.50 41.05  ? 88  ASN   A CG  1 
ATOM   570  O  OD1 A ASN   A  1  75  ? 54.681  -12.548 32.427 0.50 37.21  ? 88  ASN   A OD1 1 
ATOM   571  O  OD1 B ASN   A  1  75  ? 55.478  -10.270 32.721 0.50 44.42  ? 88  ASN   A OD1 1 
ATOM   572  N  ND2 A ASN   A  1  75  ? 55.444  -10.844 33.642 0.50 33.99  ? 88  ASN   A ND2 1 
ATOM   573  N  ND2 B ASN   A  1  75  ? 54.522  -8.942  31.157 0.50 46.84  ? 88  ASN   A ND2 1 
ATOM   574  N  N   . ALA   A  1  76  ? 50.485  -8.926  33.079 1.00 32.43  ? 89  ALA   A N   1 
ATOM   575  C  CA  . ALA   A  1  76  ? 49.606  -7.776  33.010 1.00 33.79  ? 89  ALA   A CA  1 
ATOM   576  C  C   . ALA   A  1  76  ? 49.419  -7.167  34.405 1.00 30.84  ? 89  ALA   A C   1 
ATOM   577  O  O   . ALA   A  1  76  ? 49.400  -5.942  34.563 1.00 30.66  ? 89  ALA   A O   1 
ATOM   578  C  CB  . ALA   A  1  76  ? 48.282  -8.156  32.386 1.00 32.91  ? 89  ALA   A CB  1 
ATOM   579  N  N   . ALA   A  1  77  ? 49.315  -8.015  35.428 1.00 27.05  ? 90  ALA   A N   1 
ATOM   580  C  CA  . ALA   A  1  77  ? 49.167  -7.532  36.790 1.00 25.97  ? 90  ALA   A CA  1 
ATOM   581  C  C   . ALA   A  1  77  ? 50.407  -6.744  37.226 1.00 26.85  ? 90  ALA   A C   1 
ATOM   582  O  O   . ALA   A  1  77  ? 50.288  -5.693  37.866 1.00 28.95  ? 90  ALA   A O   1 
ATOM   583  C  CB  . ALA   A  1  77  ? 48.882  -8.674  37.715 1.00 24.78  ? 90  ALA   A CB  1 
ATOM   584  N  N   . ILE   A  1  78  ? 51.582  -7.244  36.854 1.00 27.31  ? 91  ILE   A N   1 
ATOM   585  C  CA  . ILE   A  1  78  ? 52.838  -6.617  37.226 1.00 29.11  ? 91  ILE   A CA  1 
ATOM   586  C  C   . ILE   A  1  78  ? 52.961  -5.265  36.520 1.00 29.04  ? 91  ILE   A C   1 
ATOM   587  O  O   . ILE   A  1  78  ? 53.294  -4.271  37.142 1.00 27.12  ? 91  ILE   A O   1 
ATOM   588  C  CB  . ILE   A  1  78  ? 53.993  -7.585  36.925 1.00 28.02  ? 91  ILE   A CB  1 
ATOM   589  C  CG1 . ILE   A  1  78  ? 53.995  -8.713  37.936 1.00 29.61  ? 91  ILE   A CG1 1 
ATOM   590  C  CG2 . ILE   A  1  78  ? 55.337  -6.862  36.895 1.00 31.23  ? 91  ILE   A CG2 1 
ATOM   591  C  CD1 . ILE   A  1  78  ? 54.922  -9.861  37.576 1.00 27.91  ? 91  ILE   A CD1 1 
ATOM   592  N  N   . VAL   A  1  79  ? 52.602  -5.215  35.238 1.00 29.96  ? 92  VAL   A N   1 
ATOM   593  C  CA  . VAL   A  1  79  ? 52.702  -3.982  34.491 1.00 30.85  ? 92  VAL   A CA  1 
ATOM   594  C  C   . VAL   A  1  79  ? 51.793  -2.922  35.098 1.00 32.95  ? 92  VAL   A C   1 
ATOM   595  O  O   . VAL   A  1  79  ? 52.206  -1.783  35.292 1.00 34.82  ? 92  VAL   A O   1 
ATOM   596  C  CB  . VAL   A  1  79  ? 52.410  -4.194  33.002 1.00 31.79  ? 92  VAL   A CB  1 
ATOM   597  C  CG1 . VAL   A  1  79  ? 52.327  -2.861  32.274 1.00 31.75  ? 92  VAL   A CG1 1 
ATOM   598  C  CG2 . VAL   A  1  79  ? 53.486  -5.078  32.352 1.00 33.07  ? 92  VAL   A CG2 1 
ATOM   599  N  N   . ALA   A  1  80  ? 50.540  -3.268  35.373 1.00 31.78  ? 93  ALA   A N   1 
ATOM   600  C  CA  . ALA   A  1  80  ? 49.606  -2.274  35.869 1.00 28.82  ? 93  ALA   A CA  1 
ATOM   601  C  C   . ALA   A  1  80  ? 49.965  -1.865  37.299 1.00 30.71  ? 93  ALA   A C   1 
ATOM   602  O  O   . ALA   A  1  80  ? 49.877  -0.685  37.662 1.00 29.46  ? 93  ALA   A O   1 
ATOM   603  C  CB  . ALA   A  1  80  ? 48.200  -2.814  35.796 1.00 29.67  ? 93  ALA   A CB  1 
ATOM   604  N  N   . THR   A  1  81  ? 50.340  -2.839  38.132 1.00 28.20  ? 94  THR   A N   1 
ATOM   605  C  CA  . THR   A  1  81  ? 50.492  -2.561  39.547 1.00 28.64  ? 94  THR   A CA  1 
ATOM   606  C  C   . THR   A  1  81  ? 51.685  -1.633  39.801 1.00 28.84  ? 94  THR   A C   1 
ATOM   607  O  O   . THR   A  1  81  ? 51.553  -0.647  40.513 1.00 27.76  ? 94  THR   A O   1 
ATOM   608  C  CB  . THR   A  1  81  ? 50.638  -3.865  40.323 1.00 28.40  ? 94  THR   A CB  1 
ATOM   609  O  OG1 . THR   A  1  81  ? 49.410  -4.567  40.166 1.00 30.71  ? 94  THR   A OG1 1 
ATOM   610  C  CG2 . THR   A  1  81  ? 50.848  -3.598  41.795 1.00 28.56  ? 94  THR   A CG2 1 
ATOM   611  N  N   . TYR   A  1  82  ? 52.844  -1.936  39.214 1.00 29.33  ? 95  TYR   A N   1 
ATOM   612  C  CA  . TYR   A  1  82  ? 54.048  -1.173  39.509 1.00 30.85  ? 95  TYR   A CA  1 
ATOM   613  C  C   . TYR   A  1  82  ? 53.993  0.176   38.800 1.00 31.38  ? 95  TYR   A C   1 
ATOM   614  O  O   . TYR   A  1  82  ? 54.593  1.128   39.279 1.00 32.66  ? 95  TYR   A O   1 
ATOM   615  C  CB  . TYR   A  1  82  ? 55.317  -1.979  39.218 1.00 28.47  ? 95  TYR   A CB  1 
ATOM   616  C  CG  . TYR   A  1  82  ? 55.495  -3.105  40.229 1.00 33.06  ? 95  TYR   A CG  1 
ATOM   617  C  CD1 . TYR   A  1  82  ? 55.907  -2.840  41.526 1.00 29.07  ? 95  TYR   A CD1 1 
ATOM   618  C  CD2 . TYR   A  1  82  ? 55.209  -4.430  39.900 1.00 34.47  ? 95  TYR   A CD2 1 
ATOM   619  C  CE1 . TYR   A  1  82  ? 56.011  -3.842  42.472 1.00 27.76  ? 95  TYR   A CE1 1 
ATOM   620  C  CE2 . TYR   A  1  82  ? 55.336  -5.445  40.831 1.00 31.61  ? 95  TYR   A CE2 1 
ATOM   621  C  CZ  . TYR   A  1  82  ? 55.727  -5.148  42.117 1.00 29.28  ? 95  TYR   A CZ  1 
ATOM   622  O  OH  . TYR   A  1  82  ? 55.832  -6.137  43.032 1.00 32.03  ? 95  TYR   A OH  1 
ATOM   623  N  N   . LEU   A  1  83  ? 53.261  0.257   37.681 1.00 29.82  ? 96  LEU   A N   1 
ATOM   624  C  CA  . LEU   A  1  83  ? 52.994  1.528   37.038 1.00 30.53  ? 96  LEU   A CA  1 
ATOM   625  C  C   . LEU   A  1  83  ? 52.251  2.422   38.020 1.00 32.28  ? 96  LEU   A C   1 
ATOM   626  O  O   . LEU   A  1  83  ? 52.616  3.574   38.244 1.00 31.25  ? 96  LEU   A O   1 
ATOM   627  C  CB  . LEU   A  1  83  ? 52.191  1.313   35.762 1.00 32.16  ? 96  LEU   A CB  1 
ATOM   628  C  CG  . LEU   A  1  83  ? 51.676  2.586   35.084 1.00 39.29  ? 96  LEU   A CG  1 
ATOM   629  C  CD1 . LEU   A  1  83  ? 52.806  3.486   34.647 1.00 41.99  ? 96  LEU   A CD1 1 
ATOM   630  C  CD2 . LEU   A  1  83  ? 50.781  2.246   33.897 1.00 43.71  ? 96  LEU   A CD2 1 
ATOM   631  N  N   . GLY   A  1  84  ? 51.198  1.859   38.613 1.00 30.65  ? 97  GLY   A N   1 
ATOM   632  C  CA  . GLY   A  1  84  ? 50.379  2.600   39.545 1.00 31.73  ? 97  GLY   A CA  1 
ATOM   633  C  C   . GLY   A  1  84  ? 51.189  3.003   40.769 1.00 29.37  ? 97  GLY   A C   1 
ATOM   634  O  O   . GLY   A  1  84  ? 51.074  4.122   41.251 1.00 31.46  ? 97  GLY   A O   1 
ATOM   635  N  N   . HIS   A  1  85  ? 52.001  2.078   41.260 1.00 29.61  ? 98  HIS   A N   1 
ATOM   636  C  CA  . HIS   A  1  85  ? 52.773  2.289   42.469 1.00 30.87  ? 98  HIS   A CA  1 
ATOM   637  C  C   . HIS   A  1  85  ? 53.900  3.311   42.254 1.00 29.55  ? 98  HIS   A C   1 
ATOM   638  O  O   . HIS   A  1  85  ? 54.071  4.206   43.071 1.00 27.10  ? 98  HIS   A O   1 
ATOM   639  C  CB  . HIS   A  1  85  ? 53.338  0.949   42.926 1.00 30.18  ? 98  HIS   A CB  1 
ATOM   640  C  CG  . HIS   A  1  85  ? 54.004  1.006   44.238 1.00 29.73  ? 98  HIS   A CG  1 
ATOM   641  N  ND1 . HIS   A  1  85  ? 53.356  1.529   45.332 1.00 30.86  ? 98  HIS   A ND1 1 
ATOM   642  C  CD2 . HIS   A  1  85  ? 55.195  0.581   44.661 1.00 30.94  ? 98  HIS   A CD2 1 
ATOM   643  C  CE1 . HIS   A  1  85  ? 54.148  1.426   46.388 1.00 32.31  ? 98  HIS   A CE1 1 
ATOM   644  N  NE2 . HIS   A  1  85  ? 55.277  0.846   46.003 1.00 31.05  ? 98  HIS   A NE2 1 
ATOM   645  N  N   . LEU   A  1  86  ? 54.673  3.168   41.179 1.00 27.97  ? 99  LEU   A N   1 
ATOM   646  C  CA  . LEU   A  1  86  ? 55.767  4.091   40.902 1.00 33.64  ? 99  LEU   A CA  1 
ATOM   647  C  C   . LEU   A  1  86  ? 55.256  5.535   40.851 1.00 32.31  ? 99  LEU   A C   1 
ATOM   648  O  O   . LEU   A  1  86  ? 55.837  6.422   41.470 1.00 32.32  ? 99  LEU   A O   1 
ATOM   649  C  CB  . LEU   A  1  86  ? 56.466  3.711   39.598 1.00 33.51  ? 99  LEU   A CB  1 
ATOM   650  C  CG  . LEU   A  1  86  ? 57.445  2.537   39.682 1.00 35.82  ? 99  LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A  1  86  ? 57.819  2.061   38.295 1.00 35.21  ? 99  LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A  1  86  ? 58.686  2.935   40.470 1.00 37.79  ? 99  LEU   A CD2 1 
ATOM   653  N  N   . LEU   A  1  87  ? 54.133  5.742   40.160 1.00 29.92  ? 100 LEU   A N   1 
ATOM   654  C  CA  . LEU   A  1  87  ? 53.594  7.071   39.939 1.00 31.30  ? 100 LEU   A CA  1 
ATOM   655  C  C   . LEU   A  1  87  ? 52.812  7.567   41.147 1.00 31.09  ? 100 LEU   A C   1 
ATOM   656  O  O   . LEU   A  1  87  ? 52.808  8.765   41.408 1.00 31.54  ? 100 LEU   A O   1 
ATOM   657  C  CB  . LEU   A  1  87  ? 52.684  7.039   38.717 1.00 34.15  ? 100 LEU   A CB  1 
ATOM   658  C  CG  . LEU   A  1  87  ? 53.369  6.742   37.386 1.00 35.03  ? 100 LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A  1  87  ? 52.376  6.751   36.235 1.00 38.41  ? 100 LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A  1  87  ? 54.458  7.746   37.113 1.00 36.90  ? 100 LEU   A CD2 1 
ATOM   661  N  N   . ASN   A  1  88  ? 52.118  6.661   41.852 1.00 31.92  ? 101 ASN   A N   1 
ATOM   662  C  CA  . ASN   A  1  88  ? 51.032  7.079   42.726 1.00 30.29  ? 101 ASN   A CA  1 
ATOM   663  C  C   . ASN   A  1  88  ? 51.107  6.492   44.124 1.00 28.55  ? 101 ASN   A C   1 
ATOM   664  O  O   . ASN   A  1  88  ? 50.301  6.867   44.967 1.00 29.23  ? 101 ASN   A O   1 
ATOM   665  C  CB  . ASN   A  1  88  ? 49.657  6.724   42.186 1.00 30.22  ? 101 ASN   A CB  1 
ATOM   666  C  CG  . ASN   A  1  88  ? 49.355  7.411   40.885 1.00 33.23  ? 101 ASN   A CG  1 
ATOM   667  O  OD1 . ASN   A  1  88  ? 49.590  8.621   40.742 1.00 35.32  ? 101 ASN   A OD1 1 
ATOM   668  N  ND2 . ASN   A  1  88  ? 48.806  6.658   39.946 1.00 36.68  ? 101 ASN   A ND2 1 
ATOM   669  N  N   . GLY   A  1  89  ? 52.058  5.589   44.367 1.00 29.90  ? 102 GLY   A N   1 
ATOM   670  C  CA  . GLY   A  1  89  ? 52.169  4.977   45.681 1.00 31.37  ? 102 GLY   A CA  1 
ATOM   671  C  C   . GLY   A  1  89  ? 53.327  5.555   46.485 1.00 29.19  ? 102 GLY   A C   1 
ATOM   672  O  O   . GLY   A  1  89  ? 54.132  6.354   45.994 1.00 28.68  ? 102 GLY   A O   1 
ATOM   673  N  N   . ASN   A  1  90  ? 53.410  5.089   47.719 1.00 28.15  ? 103 ASN   A N   1 
ATOM   674  C  CA  . ASN   A  1  90  ? 54.485  5.461   48.603 1.00 29.10  ? 103 ASN   A CA  1 
ATOM   675  C  C   . ASN   A  1  90  ? 55.503  4.332   48.583 1.00 31.95  ? 103 ASN   A C   1 
ATOM   676  O  O   . ASN   A  1  90  ? 55.224  3.239   49.087 1.00 30.40  ? 103 ASN   A O   1 
ATOM   677  C  CB  . ASN   A  1  90  ? 53.936  5.668   50.002 1.00 31.17  ? 103 ASN   A CB  1 
ATOM   678  C  CG  . ASN   A  1  90  ? 54.977  6.214   50.950 1.00 31.60  ? 103 ASN   A CG  1 
ATOM   679  O  OD1 . ASN   A  1  90  ? 56.105  5.713   51.016 1.00 33.52  ? 103 ASN   A OD1 1 
ATOM   680  N  ND2 . ASN   A  1  90  ? 54.603  7.263   51.656 1.00 33.62  ? 103 ASN   A ND2 1 
ATOM   681  N  N   . LEU   A  1  91  ? 56.684  4.625   48.045 1.00 33.72  ? 104 LEU   A N   1 
ATOM   682  C  CA  . LEU   A  1  91  ? 57.702  3.621   47.788 1.00 36.93  ? 104 LEU   A CA  1 
ATOM   683  C  C   . LEU   A  1  91  ? 58.430  3.214   49.062 1.00 35.32  ? 104 LEU   A C   1 
ATOM   684  O  O   . LEU   A  1  91  ? 58.997  2.133   49.125 1.00 33.84  ? 104 LEU   A O   1 
ATOM   685  C  CB  . LEU   A  1  91  ? 58.651  4.183   46.733 1.00 39.31  ? 104 LEU   A CB  1 
ATOM   686  C  CG  . LEU   A  1  91  ? 57.961  4.479   45.405 1.00 42.82  ? 104 LEU   A CG  1 
ATOM   687  C  CD1 . LEU   A  1  91  ? 58.766  5.405   44.572 1.00 51.22  ? 104 LEU   A CD1 1 
ATOM   688  C  CD2 . LEU   A  1  91  ? 57.709  3.219   44.648 1.00 45.84  ? 104 LEU   A CD2 1 
ATOM   689  N  N   . VAL   A  1  92  ? 58.352  4.049   50.098 1.00 35.52  ? 105 VAL   A N   1 
ATOM   690  C  CA  . VAL   A  1  92  ? 59.055  3.766   51.334 1.00 33.73  ? 105 VAL   A CA  1 
ATOM   691  C  C   . VAL   A  1  92  ? 58.230  2.806   52.177 1.00 33.39  ? 105 VAL   A C   1 
ATOM   692  O  O   . VAL   A  1  92  ? 58.777  1.856   52.734 1.00 34.80  ? 105 VAL   A O   1 
ATOM   693  C  CB  . VAL   A  1  92  ? 59.383  5.064   52.086 1.00 35.07  ? 105 VAL   A CB  1 
ATOM   694  C  CG1 . VAL   A  1  92  ? 59.913  4.794   53.493 1.00 38.16  ? 105 VAL   A CG1 1 
ATOM   695  C  CG2 . VAL   A  1  92  ? 60.362  5.905   51.290 1.00 34.06  ? 105 VAL   A CG2 1 
ATOM   696  N  N   . THR   A  1  93  ? 56.921  3.077   52.294 1.00 36.39  ? 106 THR   A N   1 
ATOM   697  C  CA  . THR   A  1  93  ? 56.021  2.223   53.063 1.00 33.22  ? 106 THR   A CA  1 
ATOM   698  C  C   . THR   A  1  93  ? 55.518  1.039   52.231 1.00 30.44  ? 106 THR   A C   1 
ATOM   699  O  O   . THR   A  1  93  ? 54.973  0.103   52.787 1.00 35.63  ? 106 THR   A O   1 
ATOM   700  C  CB  . THR   A  1  93  ? 54.868  3.051   53.613 1.00 35.77  ? 106 THR   A CB  1 
ATOM   701  O  OG1 . THR   A  1  93  ? 54.169  3.589   52.488 1.00 32.01  ? 106 THR   A OG1 1 
ATOM   702  C  CG2 . THR   A  1  93  ? 55.373  4.109   54.581 1.00 34.74  ? 106 THR   A CG2 1 
ATOM   703  N  N   . ASP   A  1  94  ? 55.711  1.087   50.910 1.00 33.03  ? 107 ASP   A N   1 
ATOM   704  C  CA  . ASP   A  1  94  ? 55.282  0.053   49.982 1.00 32.75  ? 107 ASP   A CA  1 
ATOM   705  C  C   . ASP   A  1  94  ? 53.759  -0.055  49.964 1.00 31.79  ? 107 ASP   A C   1 
ATOM   706  O  O   . ASP   A  1  94  ? 53.235  -1.158  49.916 1.00 32.57  ? 107 ASP   A O   1 
ATOM   707  C  CB  . ASP   A  1  94  ? 55.913  -1.292  50.316 1.00 33.83  ? 107 ASP   A CB  1 
ATOM   708  C  CG  . ASP   A  1  94  ? 55.937  -2.301  49.171 1.00 33.35  ? 107 ASP   A CG  1 
ATOM   709  O  OD1 . ASP   A  1  94  ? 56.154  -1.844  48.030 1.00 36.05  ? 107 ASP   A OD1 1 
ATOM   710  O  OD2 . ASP   A  1  94  ? 55.768  -3.531  49.413 1.00 35.60  ? 107 ASP   A OD2 1 
ATOM   711  N  N   . LEU   A  1  95  ? 53.062  1.087   50.008 1.00 31.88  ? 108 LEU   A N   1 
ATOM   712  C  CA  . LEU   A  1  95  ? 51.613  1.125   50.081 1.00 33.30  ? 108 LEU   A CA  1 
ATOM   713  C  C   . LEU   A  1  95  ? 51.074  2.013   48.961 1.00 32.15  ? 108 LEU   A C   1 
ATOM   714  O  O   . LEU   A  1  95  ? 51.638  3.055   48.653 1.00 32.59  ? 108 LEU   A O   1 
ATOM   715  C  CB  . LEU   A  1  95  ? 51.160  1.618   51.447 1.00 31.10  ? 108 LEU   A CB  1 
ATOM   716  C  CG  . LEU   A  1  95  ? 51.429  0.685   52.630 1.00 33.58  ? 108 LEU   A CG  1 
ATOM   717  C  CD1 . LEU   A  1  95  ? 51.097  1.410   53.956 1.00 32.79  ? 108 LEU   A CD1 1 
ATOM   718  C  CD2 . LEU   A  1  95  ? 50.658  -0.642  52.556 1.00 34.25  ? 108 LEU   A CD2 1 
ATOM   719  N  N   . LEU   A  1  96  ? 49.977  1.559   48.352 1.00 33.29  ? 109 LEU   A N   1 
ATOM   720  C  CA  . LEU   A  1  96  ? 49.305  2.268   47.269 1.00 30.30  ? 109 LEU   A CA  1 
ATOM   721  C  C   . LEU   A  1  96  ? 47.820  2.382   47.609 1.00 33.00  ? 109 LEU   A C   1 
ATOM   722  O  O   . LEU   A  1  96  ? 47.187  1.380   47.926 1.00 30.65  ? 109 LEU   A O   1 
ATOM   723  C  CB  . LEU   A  1  96  ? 49.514  1.501   45.973 1.00 30.83  ? 109 LEU   A CB  1 
ATOM   724  C  CG  . LEU   A  1  96  ? 48.672  1.972   44.789 1.00 30.78  ? 109 LEU   A CG  1 
ATOM   725  C  CD1 . LEU   A  1  96  ? 48.985  3.423   44.428 1.00 30.87  ? 109 LEU   A CD1 1 
ATOM   726  C  CD2 . LEU   A  1  96  ? 48.879  1.081   43.588 1.00 30.35  ? 109 LEU   A CD2 1 
ATOM   727  N  N   . SER   A  1  97  ? 47.293  3.611   47.563 1.00 30.24  ? 110 SER   A N   1 
ATOM   728  C  CA  . SER   A  1  97  ? 45.863  3.865   47.643 1.00 28.84  ? 110 SER   A CA  1 
ATOM   729  C  C   . SER   A  1  97  ? 45.209  3.587   46.297 1.00 27.25  ? 110 SER   A C   1 
ATOM   730  O  O   . SER   A  1  97  ? 45.664  4.118   45.303 1.00 28.27  ? 110 SER   A O   1 
ATOM   731  C  CB  . SER   A  1  97  ? 45.604  5.293   48.040 1.00 30.14  ? 110 SER   A CB  1 
ATOM   732  O  OG  . SER   A  1  97  ? 44.260  5.675   47.804 1.00 28.78  ? 110 SER   A OG  1 
ATOM   733  N  N   . ILE   A  1  98  ? 44.097  2.845   46.282 1.00 26.21  ? 111 ILE   A N   1 
ATOM   734  C  CA  . ILE   A  1  98  ? 43.410  2.550   45.036 1.00 28.29  ? 111 ILE   A CA  1 
ATOM   735  C  C   . ILE   A  1  98  ? 42.505  3.725   44.664 1.00 29.22  ? 111 ILE   A C   1 
ATOM   736  O  O   . ILE   A  1  98  ? 41.812  3.694   43.647 1.00 28.90  ? 111 ILE   A O   1 
ATOM   737  C  CB  . ILE   A  1  98  ? 42.645  1.217   45.108 1.00 29.23  ? 111 ILE   A CB  1 
ATOM   738  C  CG1 . ILE   A  1  98  ? 41.455  1.267   46.067 1.00 27.93  ? 111 ILE   A CG1 1 
ATOM   739  C  CG2 . ILE   A  1  98  ? 43.590  0.082   45.479 1.00 31.15  ? 111 ILE   A CG2 1 
ATOM   740  C  CD1 . ILE   A  1  98  ? 40.563  0.036   46.024 1.00 29.84  ? 111 ILE   A CD1 1 
ATOM   741  N  N   . GLY   A  1  99  ? 42.509  4.761   45.494 1.00 27.58  ? 112 GLY   A N   1 
ATOM   742  C  CA  . GLY   A  1  99  ? 41.748  5.966   45.216 1.00 31.84  ? 112 GLY   A CA  1 
ATOM   743  C  C   . GLY   A  1  99  ? 42.572  7.226   45.437 1.00 30.02  ? 112 GLY   A C   1 
ATOM   744  O  O   . GLY   A  1  99  ? 43.497  7.477   44.694 1.00 32.99  ? 112 GLY   A O   1 
ATOM   745  N  N   . GLY   A  1  100 ? 42.172  8.021   46.417 1.00 35.37  ? 113 GLY   A N   1 
ATOM   746  C  CA  . GLY   A  1  100 ? 42.762  9.328   46.636 1.00 37.53  ? 113 GLY   A CA  1 
ATOM   747  C  C   . GLY   A  1  100 ? 43.693  9.303   47.833 1.00 36.70  ? 113 GLY   A C   1 
ATOM   748  O  O   . GLY   A  1  100 ? 44.066  8.241   48.329 1.00 34.00  ? 113 GLY   A O   1 
ATOM   749  N  N   . ALA   A  1  101 ? 44.029  10.511  48.280 1.00 42.24  ? 114 ALA   A N   1 
ATOM   750  C  CA  . ALA   A  1  101 ? 45.003  10.710  49.337 1.00 41.65  ? 114 ALA   A CA  1 
ATOM   751  C  C   . ALA   A  1  101 ? 44.455  10.184  50.657 1.00 34.26  ? 114 ALA   A C   1 
ATOM   752  O  O   . ALA   A  1  101 ? 43.276  10.293  50.926 1.00 34.22  ? 114 ALA   A O   1 
ATOM   753  C  CB  . ALA   A  1  101 ? 45.356  12.190  49.432 1.00 42.89  ? 114 ALA   A CB  1 
ATOM   754  N  N   . THR   A  1  102 ? 45.332  9.605   51.463 1.00 35.74  ? 115 THR   A N   1 
ATOM   755  C  CA  . THR   A  1  102 ? 44.935  9.050   52.737 1.00 37.32  ? 115 THR   A CA  1 
ATOM   756  C  C   . THR   A  1  102 ? 46.183  9.011   53.610 1.00 38.27  ? 115 THR   A C   1 
ATOM   757  O  O   . THR   A  1  102 ? 47.256  8.698   53.106 1.00 36.46  ? 115 THR   A O   1 
ATOM   758  C  CB  . THR   A  1  102 ? 44.335  7.653   52.540 1.00 35.80  ? 115 THR   A CB  1 
ATOM   759  O  OG1 . THR   A  1  102 ? 44.136  7.076   53.829 1.00 33.18  ? 115 THR   A OG1 1 
ATOM   760  C  CG2 . THR   A  1  102 ? 45.259  6.679   51.842 1.00 33.20  ? 115 THR   A CG2 1 
ATOM   761  N  N   . PRO   A  1  103 ? 46.083  9.329   54.918 1.00 44.02  ? 116 PRO   A N   1 
ATOM   762  C  CA  . PRO   A  1  103 ? 47.185  9.061   55.850 1.00 42.84  ? 116 PRO   A CA  1 
ATOM   763  C  C   . PRO   A  1  103 ? 47.602  7.589   55.949 1.00 39.84  ? 116 PRO   A C   1 
ATOM   764  O  O   . PRO   A  1  103 ? 48.690  7.297   56.452 1.00 36.13  ? 116 PRO   A O   1 
ATOM   765  C  CB  . PRO   A  1  103 ? 46.644  9.573   57.221 1.00 42.95  ? 116 PRO   A CB  1 
ATOM   766  C  CG  . PRO   A  1  103 ? 45.129  9.654   57.052 1.00 42.87  ? 116 PRO   A CG  1 
ATOM   767  C  CD  . PRO   A  1  103 ? 44.899  9.934   55.572 1.00 43.13  ? 116 PRO   A CD  1 
ATOM   768  N  N   . LYS   A  1  104 ? 46.746  6.662   55.480 1.00 36.87  ? 117 LYS   A N   1 
ATOM   769  C  CA  . LYS   A  1  104 ? 47.031  5.237   55.591 1.00 38.45  ? 117 LYS   A CA  1 
ATOM   770  C  C   . LYS   A  1  104 ? 48.232  4.799   54.744 1.00 37.92  ? 117 LYS   A C   1 
ATOM   771  O  O   . LYS   A  1  104 ? 48.753  3.722   54.989 1.00 40.14  ? 117 LYS   A O   1 
ATOM   772  C  CB  . LYS   A  1  104 ? 45.809  4.426   55.161 1.00 41.91  ? 117 LYS   A CB  1 
ATOM   773  C  CG  . LYS   A  1  104 ? 44.634  4.512   56.104 1.00 40.48  ? 117 LYS   A CG  1 
ATOM   774  C  CD  . LYS   A  1  104 ? 43.298  4.150   55.456 1.00 50.35  ? 117 LYS   A CD  1 
ATOM   775  C  CE  . LYS   A  1  104 ? 42.180  4.080   56.474 1.00 50.73  ? 117 LYS   A CE  1 
ATOM   776  N  NZ  . LYS   A  1  104 ? 42.371  2.915   57.341 1.00 49.98  ? 117 LYS   A NZ  1 
ATOM   777  N  N   . THR   A  1  105 ? 48.673  5.603   53.758 1.00 35.54  ? 118 THR   A N   1 
ATOM   778  C  CA  . THR   A  1  105 ? 49.859  5.248   52.973 1.00 37.39  ? 118 THR   A CA  1 
ATOM   779  C  C   . THR   A  1  105 ? 51.128  5.670   53.712 1.00 37.92  ? 118 THR   A C   1 
ATOM   780  O  O   . THR   A  1  105 ? 52.213  5.325   53.257 1.00 36.84  ? 118 THR   A O   1 
ATOM   781  C  CB  . THR   A  1  105 ? 49.848  5.830   51.554 1.00 35.41  ? 118 THR   A CB  1 
ATOM   782  O  OG1 . THR   A  1  105 ? 49.608  7.236   51.557 1.00 34.98  ? 118 THR   A OG1 1 
ATOM   783  C  CG2 . THR   A  1  105 ? 48.810  5.184   50.658 1.00 35.50  ? 118 THR   A CG2 1 
ATOM   784  N  N   . GLY   A  1  106 ? 50.984  6.367   54.856 1.00 38.48  ? 119 GLY   A N   1 
ATOM   785  C  CA  . GLY   A  1  106 ? 52.113  6.700   55.710 1.00 39.09  ? 119 GLY   A CA  1 
ATOM   786  C  C   . GLY   A  1  106 ? 52.671  8.105   55.436 1.00 42.10  ? 119 GLY   A C   1 
ATOM   787  O  O   . GLY   A  1  106 ? 52.059  8.899   54.728 1.00 35.85  ? 119 GLY   A O   1 
ATOM   788  N  N   . PRO   A  1  107 ? 53.861  8.441   55.988 1.00 46.39  ? 120 PRO   A N   1 
ATOM   789  C  CA  . PRO   A  1  107 ? 54.470  9.762   55.793 1.00 52.58  ? 120 PRO   A CA  1 
ATOM   790  C  C   . PRO   A  1  107 ? 54.675  10.099  54.315 1.00 46.73  ? 120 PRO   A C   1 
ATOM   791  O  O   . PRO   A  1  107 ? 55.217  9.300   53.568 1.00 39.60  ? 120 PRO   A O   1 
ATOM   792  C  CB  . PRO   A  1  107 ? 55.822  9.702   56.549 1.00 53.88  ? 120 PRO   A CB  1 
ATOM   793  C  CG  . PRO   A  1  107 ? 55.693  8.489   57.468 1.00 54.10  ? 120 PRO   A CG  1 
ATOM   794  C  CD  . PRO   A  1  107 ? 54.660  7.562   56.856 1.00 46.57  ? 120 PRO   A CD  1 
ATOM   795  N  N   . PRO   A  1  108 ? 54.277  11.295  53.838 1.00 48.78  ? 121 PRO   A N   1 
ATOM   796  C  CA  . PRO   A  1  108 ? 54.367  11.613  52.416 1.00 52.40  ? 121 PRO   A CA  1 
ATOM   797  C  C   . PRO   A  1  108 ? 55.801  11.609  51.872 1.00 49.71  ? 121 PRO   A C   1 
ATOM   798  O  O   . PRO   A  1  108 ? 56.760  11.866  52.594 1.00 45.80  ? 121 PRO   A O   1 
ATOM   799  C  CB  . PRO   A  1  108 ? 53.686  12.999  52.296 1.00 53.82  ? 121 PRO   A CB  1 
ATOM   800  C  CG  . PRO   A  1  108 ? 53.775  13.594  53.684 1.00 57.99  ? 121 PRO   A CG  1 
ATOM   801  C  CD  . PRO   A  1  108 ? 53.724  12.402  54.634 1.00 54.91  ? 121 PRO   A CD  1 
ATOM   802  N  N   . PRO   A  1  109 ? 55.994  11.298  50.568 1.00 45.32  ? 122 PRO   A N   1 
ATOM   803  C  CA  . PRO   A  1  109 ? 57.309  11.418  49.942 1.00 46.86  ? 122 PRO   A CA  1 
ATOM   804  C  C   . PRO   A  1  109 ? 57.678  12.886  49.734 1.00 46.78  ? 122 PRO   A C   1 
ATOM   805  O  O   . PRO   A  1  109 ? 56.811  13.741  49.790 1.00 41.77  ? 122 PRO   A O   1 
ATOM   806  C  CB  . PRO   A  1  109 ? 57.068  10.703  48.617 1.00 46.07  ? 122 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A  1  109 ? 55.633  11.023  48.297 1.00 46.18  ? 122 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A  1  109 ? 54.932  10.889  49.625 1.00 44.71  ? 122 PRO   A CD  1 
ATOM   809  N  N   . PRO   A  1  110 ? 58.953  13.219  49.429 1.00 53.55  ? 123 PRO   A N   1 
ATOM   810  C  CA  . PRO   A  1  110 ? 59.314  14.593  49.046 1.00 51.62  ? 123 PRO   A CA  1 
ATOM   811  C  C   . PRO   A  1  110 ? 58.637  15.053  47.747 1.00 47.20  ? 123 PRO   A C   1 
ATOM   812  O  O   . PRO   A  1  110 ? 58.655  14.358  46.734 1.00 42.69  ? 123 PRO   A O   1 
ATOM   813  C  CB  . PRO   A  1  110 ? 60.851  14.551  48.942 1.00 49.78  ? 123 PRO   A CB  1 
ATOM   814  C  CG  . PRO   A  1  110 ? 61.171  13.082  48.706 1.00 52.66  ? 123 PRO   A CG  1 
ATOM   815  C  CD  . PRO   A  1  110 ? 60.099  12.289  49.431 1.00 48.44  ? 123 PRO   A CD  1 
ATOM   816  N  N   . PRO   A  1  111 ? 57.980  16.232  47.741 1.00 45.89  ? 124 PRO   A N   1 
ATOM   817  C  CA  . PRO   A  1  111 ? 57.378  16.784  46.523 1.00 46.23  ? 124 PRO   A CA  1 
ATOM   818  C  C   . PRO   A  1  111 ? 58.459  16.961  45.471 1.00 43.07  ? 124 PRO   A C   1 
ATOM   819  O  O   . PRO   A  1  111 ? 59.605  17.192  45.829 1.00 51.43  ? 124 PRO   A O   1 
ATOM   820  C  CB  . PRO   A  1  111 ? 56.752  18.129  46.947 1.00 48.86  ? 124 PRO   A CB  1 
ATOM   821  C  CG  . PRO   A  1  111 ? 56.673  18.049  48.463 1.00 53.04  ? 124 PRO   A CG  1 
ATOM   822  C  CD  . PRO   A  1  111 ? 57.752  17.080  48.923 1.00 49.47  ? 124 PRO   A CD  1 
ATOM   823  N  N   . PRO   A  1  112 ? 58.165  16.872  44.156 1.00 46.68  ? 125 PRO   A N   1 
ATOM   824  C  CA  . PRO   A  1  112 ? 56.798  16.763  43.629 1.00 44.76  ? 125 PRO   A CA  1 
ATOM   825  C  C   . PRO   A  1  112 ? 56.120  15.391  43.619 1.00 44.03  ? 125 PRO   A C   1 
ATOM   826  O  O   . PRO   A  1  112 ? 54.984  15.296  43.149 1.00 41.51  ? 125 PRO   A O   1 
ATOM   827  C  CB  . PRO   A  1  112 ? 56.978  17.274  42.185 1.00 50.38  ? 125 PRO   A CB  1 
ATOM   828  C  CG  . PRO   A  1  112 ? 58.379  16.834  41.825 1.00 51.19  ? 125 PRO   A CG  1 
ATOM   829  C  CD  . PRO   A  1  112 ? 59.195  16.838  43.109 1.00 44.59  ? 125 PRO   A CD  1 
ATOM   830  N  N   . ALA   A  1  113 ? 56.765  14.358  44.193 1.00 38.72  ? 126 ALA   A N   1 
ATOM   831  C  CA  . ALA   A  1  113 ? 56.080  13.088  44.425 1.00 39.53  ? 126 ALA   A CA  1 
ATOM   832  C  C   . ALA   A  1  113 ? 54.976  13.303  45.453 1.00 41.32  ? 126 ALA   A C   1 
ATOM   833  O  O   . ALA   A  1  113 ? 55.046  14.250  46.248 1.00 41.94  ? 126 ALA   A O   1 
ATOM   834  C  CB  . ALA   A  1  113 ? 57.034  12.012  44.881 1.00 36.02  ? 126 ALA   A CB  1 
ATOM   835  N  N   . HIS   A  1  114 ? 53.950  12.441  45.420 1.00 39.43  ? 127 HIS   A N   1 
ATOM   836  C  CA  . HIS   A  1  114 ? 52.719  12.719  46.152 1.00 36.21  ? 127 HIS   A CA  1 
ATOM   837  C  C   . HIS   A  1  114 ? 52.152  11.478  46.847 1.00 34.53  ? 127 HIS   A C   1 
ATOM   838  O  O   . HIS   A  1  114 ? 51.528  11.627  47.892 1.00 34.54  ? 127 HIS   A O   1 
ATOM   839  C  CB  . HIS   A  1  114 ? 51.707  13.367  45.203 1.00 35.95  ? 127 HIS   A CB  1 
ATOM   840  C  CG  . HIS   A  1  114 ? 51.600  12.658  43.886 1.00 37.93  ? 127 HIS   A CG  1 
ATOM   841  N  ND1 . HIS   A  1  114 ? 50.858  11.512  43.726 1.00 36.21  ? 127 HIS   A ND1 1 
ATOM   842  C  CD2 . HIS   A  1  114 ? 52.124  12.914  42.677 1.00 37.19  ? 127 HIS   A CD2 1 
ATOM   843  C  CE1 . HIS   A  1  114 ? 50.940  11.105  42.476 1.00 38.33  ? 127 HIS   A CE1 1 
ATOM   844  N  NE2 . HIS   A  1  114 ? 51.727  11.922  41.818 1.00 37.43  ? 127 HIS   A NE2 1 
ATOM   845  N  N   . ALA   A  1  115 ? 52.313  10.271  46.265 1.00 35.34  ? 128 ALA   A N   1 
ATOM   846  C  CA  . ALA   A  1  115 ? 51.621  9.084   46.765 1.00 33.09  ? 128 ALA   A CA  1 
ATOM   847  C  C   . ALA   A  1  115 ? 50.115  9.340   46.913 1.00 29.85  ? 128 ALA   A C   1 
ATOM   848  O  O   . ALA   A  1  115 ? 49.482  8.946   47.884 1.00 30.87  ? 128 ALA   A O   1 
ATOM   849  C  CB  . ALA   A  1  115 ? 52.255  8.645   48.065 1.00 29.28  ? 128 ALA   A CB  1 
ATOM   850  N  N   . GLY   A  1  116 ? 49.527  9.971   45.896 1.00 31.82  ? 129 GLY   A N   1 
ATOM   851  C  CA  . GLY   A  1  116 ? 48.172  10.490  45.940 1.00 31.79  ? 129 GLY   A CA  1 
ATOM   852  C  C   . GLY   A  1  116 ? 47.137  9.468   45.475 1.00 34.09  ? 129 GLY   A C   1 
ATOM   853  O  O   . GLY   A  1  116 ? 45.953  9.779   45.495 1.00 32.64  ? 129 GLY   A O   1 
ATOM   854  N  N   . GLY   A  1  117 ? 47.589  8.268   45.080 1.00 32.01  ? 130 GLY   A N   1 
ATOM   855  C  CA  . GLY   A  1  117 ? 46.702  7.174   44.752 1.00 30.83  ? 130 GLY   A CA  1 
ATOM   856  C  C   . GLY   A  1  117 ? 46.275  7.210   43.292 1.00 29.47  ? 130 GLY   A C   1 
ATOM   857  O  O   . GLY   A  1  117 ? 46.602  8.145   42.563 1.00 29.73  ? 130 GLY   A O   1 
ATOM   858  N  N   . LEU   A  1  118 ? 45.520  6.179   42.876 1.00 30.58  ? 131 LEU   A N   1 
ATOM   859  C  CA  . LEU   A  1  118 ? 45.136  5.998   41.482 1.00 29.27  ? 131 LEU   A CA  1 
ATOM   860  C  C   . LEU   A  1  118 ? 44.227  7.116   40.972 1.00 27.61  ? 131 LEU   A C   1 
ATOM   861  O  O   . LEU   A  1  118 ? 44.105  7.264   39.769 1.00 28.34  ? 131 LEU   A O   1 
ATOM   862  C  CB  . LEU   A  1  118 ? 44.453  4.651   41.329 1.00 30.05  ? 131 LEU   A CB  1 
ATOM   863  C  CG  . LEU   A  1  118 ? 45.309  3.427   41.675 1.00 29.97  ? 131 LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A  1  118 ? 44.479  2.168   41.423 1.00 30.62  ? 131 LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A  1  118 ? 46.586  3.378   40.892 1.00 29.90  ? 131 LEU   A CD2 1 
ATOM   866  N  N   . ASN   A  1  119 ? 43.602  7.891   41.861 1.00 28.66  ? 132 ASN   A N   1 
ATOM   867  C  CA  . ASN   A  1  119 ? 42.813  9.044   41.447 1.00 32.88  ? 132 ASN   A CA  1 
ATOM   868  C  C   . ASN   A  1  119 ? 43.638  10.137  40.772 1.00 33.38  ? 132 ASN   A C   1 
ATOM   869  O  O   . ASN   A  1  119 ? 43.066  10.965  40.089 1.00 36.65  ? 132 ASN   A O   1 
ATOM   870  C  CB  . ASN   A  1  119 ? 42.126  9.734   42.617 1.00 35.10  ? 132 ASN   A CB  1 
ATOM   871  C  CG  . ASN   A  1  119 ? 40.957  8.953   43.163 1.00 35.41  ? 132 ASN   A CG  1 
ATOM   872  O  OD1 . ASN   A  1  119 ? 40.624  7.871   42.679 1.00 35.10  ? 132 ASN   A OD1 1 
ATOM   873  N  ND2 . ASN   A  1  119 ? 40.317  9.505   44.173 1.00 37.49  ? 132 ASN   A ND2 1 
ATOM   874  N  N   . VAL   A  1  120 ? 44.954  10.191  40.992 1.00 31.18  ? 133 VAL   A N   1 
ATOM   875  C  CA  . VAL   A  1  120 ? 45.747  11.279  40.436 1.00 33.78  ? 133 VAL   A CA  1 
ATOM   876  C  C   . VAL   A  1  120 ? 45.721  11.241  38.900 1.00 34.20  ? 133 VAL   A C   1 
ATOM   877  O  O   . VAL   A  1  120 ? 46.052  10.250  38.277 1.00 35.47  ? 133 VAL   A O   1 
ATOM   878  C  CB  . VAL   A  1  120 ? 47.187  11.274  40.986 1.00 33.99  ? 133 VAL   A CB  1 
ATOM   879  C  CG1 . VAL   A  1  120 ? 48.109  12.233  40.228 1.00 36.70  ? 133 VAL   A CG1 1 
ATOM   880  C  CG2 . VAL   A  1  120 ? 47.199  11.581  42.470 1.00 33.20  ? 133 VAL   A CG2 1 
ATOM   881  N  N   . HIS   A  1  121 ? 45.394  12.387  38.309 1.00 35.11  ? 134 HIS   A N   1 
ATOM   882  C  CA  . HIS   A  1  121 ? 45.144  12.549  36.893 1.00 39.47  ? 134 HIS   A CA  1 
ATOM   883  C  C   . HIS   A  1  121 ? 46.410  12.930  36.132 1.00 37.58  ? 134 HIS   A C   1 
ATOM   884  O  O   . HIS   A  1  121 ? 47.261  13.652  36.653 1.00 39.93  ? 134 HIS   A O   1 
ATOM   885  C  CB  . HIS   A  1  121 ? 44.143  13.691  36.688 1.00 43.18  ? 134 HIS   A CB  1 
ATOM   886  C  CG  . HIS   A  1  121 ? 43.867  14.015  35.265 1.00 44.59  ? 134 HIS   A CG  1 
ATOM   887  N  ND1 . HIS   A  1  121 ? 43.188  13.156  34.430 1.00 46.94  ? 134 HIS   A ND1 1 
ATOM   888  C  CD2 . HIS   A  1  121 ? 44.194  15.102  34.536 1.00 45.74  ? 134 HIS   A CD2 1 
ATOM   889  C  CE1 . HIS   A  1  121 ? 43.087  13.719  33.227 1.00 51.29  ? 134 HIS   A CE1 1 
ATOM   890  N  NE2 . HIS   A  1  121 ? 43.679  14.914  33.283 1.00 48.27  ? 134 HIS   A NE2 1 
ATOM   891  N  N   . GLY   A  1  122 ? 46.523  12.419  34.902 1.00 42.60  ? 135 GLY   A N   1 
ATOM   892  C  CA  . GLY   A  1  122 ? 47.335  13.064  33.882 1.00 46.72  ? 135 GLY   A CA  1 
ATOM   893  C  C   . GLY   A  1  122 ? 48.506  12.234  33.361 1.00 44.11  ? 135 GLY   A C   1 
ATOM   894  O  O   . GLY   A  1  122 ? 48.964  12.514  32.250 1.00 42.86  ? 135 GLY   A O   1 
ATOM   895  N  N   . THR   A  1  123 ? 49.022  11.274  34.151 1.00 45.31  ? 136 THR   A N   1 
ATOM   896  C  CA  A THR   A  1  123 ? 50.099  10.411  33.700 0.50 45.37  ? 136 THR   A CA  1 
ATOM   897  C  CA  B THR   A  1  123 ? 50.097  10.412  33.673 0.50 45.30  ? 136 THR   A CA  1 
ATOM   898  C  C   . THR   A  1  123 ? 49.614  8.961   33.614 1.00 42.79  ? 136 THR   A C   1 
ATOM   899  O  O   . THR   A  1  123 ? 49.964  8.263   32.669 1.00 44.10  ? 136 THR   A O   1 
ATOM   900  C  CB  A THR   A  1  123 ? 51.302  10.581  34.626 0.50 47.47  ? 136 THR   A CB  1 
ATOM   901  C  CB  B THR   A  1  123 ? 51.390  10.596  34.478 0.50 48.91  ? 136 THR   A CB  1 
ATOM   902  O  OG1 A THR   A  1  123 ? 50.817  10.127  35.884 0.50 64.86  ? 136 THR   A OG1 1 
ATOM   903  O  OG1 B THR   A  1  123 ? 52.381  9.690   33.989 0.50 43.19  ? 136 THR   A OG1 1 
ATOM   904  C  CG2 A THR   A  1  123 ? 51.775  12.021  34.713 0.50 40.69  ? 136 THR   A CG2 1 
ATOM   905  C  CG2 B THR   A  1  123 ? 51.194  10.358  35.959 0.50 56.50  ? 136 THR   A CG2 1 
ATOM   906  N  N   . PHE   A  1  124 ? 48.811  8.504   34.599 1.00 41.48  ? 137 PHE   A N   1 
ATOM   907  C  CA  . PHE   A  1  124 ? 48.147  7.191   34.544 1.00 38.60  ? 137 PHE   A CA  1 
ATOM   908  C  C   . PHE   A  1  124 ? 46.644  7.373   34.251 1.00 41.20  ? 137 PHE   A C   1 
ATOM   909  O  O   . PHE   A  1  124 ? 46.230  7.285   33.090 1.00 42.25  ? 137 PHE   A O   1 
ATOM   910  C  CB  . PHE   A  1  124 ? 48.406  6.348   35.802 1.00 39.48  ? 137 PHE   A CB  1 
ATOM   911  C  CG  . PHE   A  1  124 ? 48.014  4.873   35.756 1.00 38.25  ? 137 PHE   A CG  1 
ATOM   912  C  CD1 . PHE   A  1  124 ? 47.315  4.318   34.691 1.00 39.36  ? 137 PHE   A CD1 1 
ATOM   913  C  CD2 . PHE   A  1  124 ? 48.359  4.019   36.799 1.00 39.95  ? 137 PHE   A CD2 1 
ATOM   914  C  CE1 . PHE   A  1  124 ? 46.980  2.956   34.676 1.00 39.12  ? 137 PHE   A CE1 1 
ATOM   915  C  CE2 . PHE   A  1  124 ? 48.014  2.660   36.781 1.00 37.69  ? 137 PHE   A CE2 1 
ATOM   916  C  CZ  . PHE   A  1  124 ? 47.327  2.135   35.721 1.00 36.23  ? 137 PHE   A CZ  1 
ATOM   917  N  N   . GLU   A  1  125 ? 45.810  7.604   35.281 1.00 33.93  ? 138 GLU   A N   1 
ATOM   918  C  CA  . GLU   A  1  125 ? 44.389  7.898   35.081 1.00 37.73  ? 138 GLU   A CA  1 
ATOM   919  C  C   . GLU   A  1  125 ? 44.215  9.027   34.050 1.00 39.09  ? 138 GLU   A C   1 
ATOM   920  O  O   . GLU   A  1  125 ? 44.890  10.057  34.103 1.00 36.83  ? 138 GLU   A O   1 
ATOM   921  C  CB  . GLU   A  1  125 ? 43.747  8.284   36.415 1.00 34.76  ? 138 GLU   A CB  1 
ATOM   922  C  CG  . GLU   A  1  125 ? 42.248  8.556   36.398 1.00 37.93  ? 138 GLU   A CG  1 
ATOM   923  C  CD  . GLU   A  1  125 ? 41.717  9.766   35.608 1.00 42.07  ? 138 GLU   A CD  1 
ATOM   924  O  OE1 . GLU   A  1  125 ? 42.330  10.867  35.696 1.00 39.03  ? 138 GLU   A OE1 1 
ATOM   925  O  OE2 . GLU   A  1  125 ? 40.662  9.587   34.912 1.00 39.53  ? 138 GLU   A OE2 1 
ATOM   926  N  N   . GLY   A  1  126 ? 43.275  8.837   33.122 1.00 32.70  ? 139 GLY   A N   1 
ATOM   927  C  CA  . GLY   A  1  126 ? 42.986  9.812   32.087 1.00 34.80  ? 139 GLY   A CA  1 
ATOM   928  C  C   . GLY   A  1  126 ? 41.558  9.697   31.558 1.00 33.75  ? 139 GLY   A C   1 
ATOM   929  O  O   . GLY   A  1  126 ? 40.695  9.109   32.208 1.00 35.56  ? 139 GLY   A O   1 
ATOM   930  N  N   . ASP   A  1  127 ? 41.355  10.199  30.329 1.00 36.95  ? 140 ASP   A N   1 
ATOM   931  C  CA  . ASP   A  1  127 ? 40.043  10.634  29.875 1.00 33.76  ? 140 ASP   A CA  1 
ATOM   932  C  C   . ASP   A  1  127 ? 39.342  9.559   29.042 1.00 31.86  ? 140 ASP   A C   1 
ATOM   933  O  O   . ASP   A  1  127 ? 39.941  8.585   28.619 1.00 32.05  ? 140 ASP   A O   1 
ATOM   934  C  CB  . ASP   A  1  127 ? 40.171  11.931  29.101 1.00 36.41  ? 140 ASP   A CB  1 
ATOM   935  C  CG  . ASP   A  1  127 ? 40.780  13.118  29.842 1.00 40.82  ? 140 ASP   A CG  1 
ATOM   936  O  OD1 . ASP   A  1  127 ? 40.520  13.254  31.051 1.00 39.48  ? 140 ASP   A OD1 1 
ATOM   937  O  OD2 . ASP   A  1  127 ? 41.495  13.925  29.185 1.00 43.79  ? 140 ASP   A OD2 1 
ATOM   938  N  N   . ALA   A  1  128 ? 38.051  9.782   28.775 1.00 34.12  ? 141 ALA   A N   1 
ATOM   939  C  CA  . ALA   A  1  128 ? 37.250  8.927   27.909 1.00 35.72  ? 141 ALA   A CA  1 
ATOM   940  C  C   . ALA   A  1  128 ? 37.061  7.530   28.519 1.00 34.64  ? 141 ALA   A C   1 
ATOM   941  O  O   . ALA   A  1  128 ? 37.029  6.526   27.816 1.00 33.89  ? 141 ALA   A O   1 
ATOM   942  C  CB  . ALA   A  1  128 ? 37.817  8.872   26.499 1.00 35.64  ? 141 ALA   A CB  1 
ATOM   943  N  N   . GLY   A  1  129 ? 36.873  7.473   29.837 1.00 31.76  ? 142 GLY   A N   1 
ATOM   944  C  CA  . GLY   A  1  129 ? 36.465  6.246   30.498 1.00 33.86  ? 142 GLY   A CA  1 
ATOM   945  C  C   . GLY   A  1  129 ? 35.006  5.888   30.205 1.00 33.28  ? 142 GLY   A C   1 
ATOM   946  O  O   . GLY   A  1  129 ? 34.254  6.697   29.671 1.00 34.63  ? 142 GLY   A O   1 
ATOM   947  N  N   . MET   A  1  130 ? 34.638  4.655   30.566 1.00 31.91  ? 143 MET   A N   1 
ATOM   948  C  CA  . MET   A  1  130 ? 33.331  4.108   30.280 1.00 33.18  ? 143 MET   A CA  1 
ATOM   949  C  C   . MET   A  1  130 ? 32.305  4.541   31.325 1.00 33.51  ? 143 MET   A C   1 
ATOM   950  O  O   . MET   A  1  130 ? 31.186  4.875   30.952 1.00 34.44  ? 143 MET   A O   1 
ATOM   951  C  CB  . MET   A  1  130 ? 33.369  2.578   30.262 1.00 38.11  ? 143 MET   A CB  1 
ATOM   952  C  CG  . MET   A  1  130 ? 34.079  1.970   29.047 1.00 37.34  ? 143 MET   A CG  1 
ATOM   953  S  SD  . MET   A  1  130 ? 34.220  0.166   29.161 1.00 40.87  ? 143 MET   A SD  1 
ATOM   954  C  CE  . MET   A  1  130 ? 35.266  -0.098  30.590 1.00 36.23  ? 143 MET   A CE  1 
ATOM   955  N  N   . THR   A  1  131 ? 32.650  4.481   32.625 1.00 33.30  ? 144 THR   A N   1 
ATOM   956  C  CA  . THR   A  1  131 ? 31.700  4.813   33.673 1.00 31.00  ? 144 THR   A CA  1 
ATOM   957  C  C   . THR   A  1  131 ? 32.204  5.941   34.573 1.00 31.67  ? 144 THR   A C   1 
ATOM   958  O  O   . THR   A  1  131 ? 31.530  6.280   35.550 1.00 34.03  ? 144 THR   A O   1 
ATOM   959  C  CB  . THR   A  1  131 ? 31.369  3.567   34.500 1.00 33.78  ? 144 THR   A CB  1 
ATOM   960  O  OG1 . THR   A  1  131 ? 32.490  3.233   35.318 1.00 30.47  ? 144 THR   A OG1 1 
ATOM   961  C  CG2 . THR   A  1  131 ? 30.930  2.390   33.637 1.00 32.90  ? 144 THR   A CG2 1 
ATOM   962  N  N   . ARG   A  1  132 ? 33.369  6.516   34.266 1.00 29.46  ? 145 ARG   A N   1 
ATOM   963  C  CA  . ARG   A  1  132 ? 33.885  7.664   35.002 1.00 29.90  ? 145 ARG   A CA  1 
ATOM   964  C  C   . ARG   A  1  132 ? 34.046  8.843   34.045 1.00 28.33  ? 145 ARG   A C   1 
ATOM   965  O  O   . ARG   A  1  132 ? 34.456  8.643   32.921 1.00 29.57  ? 145 ARG   A O   1 
ATOM   966  C  CB  . ARG   A  1  132 ? 35.222  7.302   35.663 1.00 33.35  ? 145 ARG   A CB  1 
ATOM   967  C  CG  . ARG   A  1  132 ? 35.115  6.685   37.051 1.00 35.02  ? 145 ARG   A CG  1 
ATOM   968  C  CD  . ARG   A  1  132 ? 34.529  5.274   37.083 1.00 34.58  ? 145 ARG   A CD  1 
ATOM   969  N  NE  . ARG   A  1  132 ? 34.373  4.876   38.486 1.00 35.97  ? 145 ARG   A NE  1 
ATOM   970  C  CZ  . ARG   A  1  132 ? 33.689  3.848   38.985 1.00 38.30  ? 145 ARG   A CZ  1 
ATOM   971  N  NH1 . ARG   A  1  132 ? 33.615  3.746   40.309 1.00 40.60  ? 145 ARG   A NH1 1 
ATOM   972  N  NH2 . ARG   A  1  132 ? 33.038  2.977   38.218 1.00 35.90  ? 145 ARG   A NH2 1 
ATOM   973  N  N   . ALA   A  1  133 ? 33.754  10.063  34.509 1.00 33.10  ? 146 ALA   A N   1 
ATOM   974  C  CA  . ALA   A  1  133 ? 33.829  11.277  33.705 1.00 29.23  ? 146 ALA   A CA  1 
ATOM   975  C  C   . ALA   A  1  133 ? 35.264  11.808  33.750 1.00 30.06  ? 146 ALA   A C   1 
ATOM   976  O  O   . ALA   A  1  133 ? 36.001  11.555  34.697 1.00 28.55  ? 146 ALA   A O   1 
ATOM   977  N  N   . ASP   A  1  134 ? 35.642  12.580  32.727 1.00 33.36  ? 147 ASP   A N   1 
ATOM   978  C  CA  . ASP   A  1  134 ? 36.946  13.216  32.628 1.00 33.42  ? 147 ASP   A CA  1 
ATOM   979  C  C   . ASP   A  1  134 ? 37.155  14.131  33.823 1.00 30.48  ? 147 ASP   A C   1 
ATOM   980  O  O   . ASP   A  1  134 ? 36.200  14.703  34.347 1.00 32.20  ? 147 ASP   A O   1 
ATOM   981  C  CB  . ASP   A  1  134 ? 37.079  13.982  31.320 1.00 35.26  ? 147 ASP   A CB  1 
ATOM   982  C  CG  . ASP   A  1  134 ? 36.984  13.147  30.054 1.00 36.78  ? 147 ASP   A CG  1 
ATOM   983  O  OD1 . ASP   A  1  134 ? 36.731  11.934  30.188 1.00 38.03  ? 147 ASP   A OD1 1 
ATOM   984  O  OD2 . ASP   A  1  134 ? 37.197  13.707  28.942 1.00 35.14  ? 147 ASP   A OD2 1 
ATOM   985  N  N   . GLU   A  1  135 ? 38.415  14.229  34.260 1.00 33.16  ? 148 GLU   A N   1 
ATOM   986  C  CA  . GLU   A  1  135 ? 38.801  15.025  35.420 1.00 36.39  ? 148 GLU   A CA  1 
ATOM   987  C  C   . GLU   A  1  135 ? 38.424  16.499  35.230 1.00 36.42  ? 148 GLU   A C   1 
ATOM   988  O  O   . GLU   A  1  135 ? 38.156  17.182  36.206 1.00 34.84  ? 148 GLU   A O   1 
ATOM   989  C  CB  . GLU   A  1  135 ? 40.304  14.890  35.667 1.00 40.09  ? 148 GLU   A CB  1 
ATOM   990  C  CG  . GLU   A  1  135 ? 40.785  15.578  36.946 1.00 49.06  ? 148 GLU   A CG  1 
ATOM   991  C  CD  . GLU   A  1  135 ? 41.231  17.033  36.786 1.00 57.93  ? 148 GLU   A CD  1 
ATOM   992  O  OE1 . GLU   A  1  135 ? 41.160  17.615  35.674 1.00 59.92  ? 148 GLU   A OE1 1 
ATOM   993  O  OE2 . GLU   A  1  135 ? 41.703  17.590  37.795 1.00 72.52  ? 148 GLU   A OE2 1 
ATOM   994  N  N   . PHE   A  1  136 ? 38.405  16.981  33.981 1.00 36.09  ? 149 PHE   A N   1 
ATOM   995  C  CA  . PHE   A  1  136 ? 38.054  18.356  33.681 1.00 42.23  ? 149 PHE   A CA  1 
ATOM   996  C  C   . PHE   A  1  136 ? 36.698  18.711  34.274 1.00 40.39  ? 149 PHE   A C   1 
ATOM   997  O  O   . PHE   A  1  136 ? 36.524  19.842  34.722 1.00 46.66  ? 149 PHE   A O   1 
ATOM   998  C  CB  . PHE   A  1  136 ? 38.003  18.645  32.181 1.00 47.81  ? 149 PHE   A CB  1 
ATOM   999  C  CG  . PHE   A  1  136 ? 37.557  20.069  31.872 1.00 51.96  ? 149 PHE   A CG  1 
ATOM   1000 C  CD1 . PHE   A  1  136 ? 38.379  21.153  32.186 1.00 57.52  ? 149 PHE   A CD1 1 
ATOM   1001 C  CD2 . PHE   A  1  136 ? 36.315  20.317  31.283 1.00 54.40  ? 149 PHE   A CD2 1 
ATOM   1002 C  CE1 . PHE   A  1  136 ? 37.970  22.449  31.909 1.00 52.98  ? 149 PHE   A CE1 1 
ATOM   1003 C  CE2 . PHE   A  1  136 ? 35.910  21.614  31.014 1.00 51.61  ? 149 PHE   A CE2 1 
ATOM   1004 C  CZ  . PHE   A  1  136 ? 36.734  22.676  31.339 1.00 51.29  ? 149 PHE   A CZ  1 
ATOM   1005 N  N   . PHE   A  1  137 ? 35.758  17.755  34.293 1.00 38.83  ? 150 PHE   A N   1 
ATOM   1006 C  CA  . PHE   A  1  137 ? 34.411  18.025  34.773 1.00 38.51  ? 150 PHE   A CA  1 
ATOM   1007 C  C   . PHE   A  1  137 ? 34.280  17.892  36.291 1.00 42.77  ? 150 PHE   A C   1 
ATOM   1008 O  O   . PHE   A  1  137 ? 33.187  18.066  36.798 1.00 39.81  ? 150 PHE   A O   1 
ATOM   1009 C  CB  . PHE   A  1  137 ? 33.431  17.092  34.068 1.00 42.00  ? 150 PHE   A CB  1 
ATOM   1010 C  CG  . PHE   A  1  137 ? 33.488  17.156  32.545 1.00 45.60  ? 150 PHE   A CG  1 
ATOM   1011 C  CD1 . PHE   A  1  137 ? 33.343  18.367  31.873 1.00 49.14  ? 150 PHE   A CD1 1 
ATOM   1012 C  CD2 . PHE   A  1  137 ? 33.712  16.008  31.788 1.00 44.56  ? 150 PHE   A CD2 1 
ATOM   1013 C  CE1 . PHE   A  1  137 ? 33.401  18.421  30.487 1.00 47.42  ? 150 PHE   A CE1 1 
ATOM   1014 C  CE2 . PHE   A  1  137 ? 33.769  16.067  30.407 1.00 43.88  ? 150 PHE   A CE2 1 
ATOM   1015 C  CZ  . PHE   A  1  137 ? 33.589  17.268  29.758 1.00 44.96  ? 150 PHE   A CZ  1 
ATOM   1016 N  N   . GLY   A  1  138 ? 35.360  17.600  37.035 1.00 42.98  ? 151 GLY   A N   1 
ATOM   1017 C  CA  . GLY   A  1  138 ? 35.317  17.747  38.484 1.00 44.42  ? 151 GLY   A CA  1 
ATOM   1018 C  C   . GLY   A  1  138 ? 35.453  16.441  39.275 1.00 49.52  ? 151 GLY   A C   1 
ATOM   1019 O  O   . GLY   A  1  138 ? 35.758  16.515  40.467 1.00 47.53  ? 151 GLY   A O   1 
ATOM   1020 N  N   . ASP   A  1  139 ? 35.222  15.268  38.648 1.00 44.23  ? 152 ASP   A N   1 
ATOM   1021 C  CA  . ASP   A  1  139 ? 35.238  14.005  39.387 1.00 45.08  ? 152 ASP   A CA  1 
ATOM   1022 C  C   . ASP   A  1  139 ? 35.630  12.833  38.484 1.00 39.08  ? 152 ASP   A C   1 
ATOM   1023 O  O   . ASP   A  1  139 ? 34.823  12.363  37.674 1.00 34.97  ? 152 ASP   A O   1 
ATOM   1024 C  CB  . ASP   A  1  139 ? 33.904  13.732  40.074 1.00 48.89  ? 152 ASP   A CB  1 
ATOM   1025 C  CG  . ASP   A  1  139 ? 33.844  12.487  40.953 1.00 49.60  ? 152 ASP   A CG  1 
ATOM   1026 O  OD1 . ASP   A  1  139 ? 34.749  11.618  40.819 1.00 43.20  ? 152 ASP   A OD1 1 
ATOM   1027 O  OD2 . ASP   A  1  139 ? 32.907  12.403  41.787 1.00 46.69  ? 152 ASP   A OD2 1 
ATOM   1028 N  N   . ASN   A  1  140 ? 36.857  12.326  38.668 1.00 35.48  ? 153 ASN   A N   1 
ATOM   1029 C  CA  . ASN   A  1  140 ? 37.396  11.317  37.771 1.00 35.21  ? 153 ASN   A CA  1 
ATOM   1030 C  C   . ASN   A  1  140 ? 37.309  9.898   38.349 1.00 33.07  ? 153 ASN   A C   1 
ATOM   1031 O  O   . ASN   A  1  140 ? 37.812  8.967   37.726 1.00 32.97  ? 153 ASN   A O   1 
ATOM   1032 C  CB  . ASN   A  1  140 ? 38.844  11.619  37.399 1.00 36.02  ? 153 ASN   A CB  1 
ATOM   1033 C  CG  . ASN   A  1  140 ? 39.813  11.474  38.555 1.00 35.79  ? 153 ASN   A CG  1 
ATOM   1034 O  OD1 . ASN   A  1  140 ? 39.418  11.375  39.726 1.00 39.97  ? 153 ASN   A OD1 1 
ATOM   1035 N  ND2 . ASN   A  1  140 ? 41.099  11.490  38.238 1.00 36.58  ? 153 ASN   A ND2 1 
ATOM   1036 N  N   . HIS   A  1  141 ? 36.700  9.726   39.527 1.00 34.14  ? 154 HIS   A N   1 
ATOM   1037 C  CA  . HIS   A  1  141 ? 36.772  8.463   40.253 1.00 37.34  ? 154 HIS   A CA  1 
ATOM   1038 C  C   . HIS   A  1  141 ? 35.377  7.874   40.503 1.00 36.18  ? 154 HIS   A C   1 
ATOM   1039 O  O   . HIS   A  1  141 ? 35.246  6.656   40.559 1.00 33.91  ? 154 HIS   A O   1 
ATOM   1040 C  CB  . HIS   A  1  141 ? 37.592  8.607   41.546 1.00 35.20  ? 154 HIS   A CB  1 
ATOM   1041 C  CG  . HIS   A  1  141 ? 37.139  9.728   42.410 1.00 41.79  ? 154 HIS   A CG  1 
ATOM   1042 N  ND1 . HIS   A  1  141 ? 36.207  9.530   43.400 1.00 48.23  ? 154 HIS   A ND1 1 
ATOM   1043 C  CD2 . HIS   A  1  141 ? 37.427  11.062  42.417 1.00 45.90  ? 154 HIS   A CD2 1 
ATOM   1044 C  CE1 . HIS   A  1  141 ? 35.958  10.695  43.998 1.00 50.77  ? 154 HIS   A CE1 1 
ATOM   1045 N  NE2 . HIS   A  1  141 ? 36.680  11.636  43.408 1.00 49.19  ? 154 HIS   A NE2 1 
ATOM   1046 N  N   . SER   A  1  142 ? 34.351  8.719   40.693 1.00 35.57  ? 155 SER   A N   1 
ATOM   1047 C  CA  . SER   A  1  142 ? 33.015  8.259   41.024 1.00 34.05  ? 155 SER   A CA  1 
ATOM   1048 C  C   . SER   A  1  142 ? 32.353  7.606   39.814 1.00 32.96  ? 155 SER   A C   1 
ATOM   1049 O  O   . SER   A  1  142 ? 32.531  8.028   38.675 1.00 31.94  ? 155 SER   A O   1 
ATOM   1050 C  CB  . SER   A  1  142 ? 32.120  9.373   41.513 1.00 34.98  ? 155 SER   A CB  1 
ATOM   1051 O  OG  . SER   A  1  142 ? 32.525  9.811   42.786 1.00 40.82  ? 155 SER   A OG  1 
ATOM   1052 N  N   . PHE   A  1  143 ? 31.503  6.624   40.113 1.00 33.45  ? 156 PHE   A N   1 
ATOM   1053 C  CA  . PHE   A  1  143 ? 30.591  6.102   39.122 1.00 34.39  ? 156 PHE   A CA  1 
ATOM   1054 C  C   . PHE   A  1  143 ? 29.676  7.231   38.645 1.00 35.67  ? 156 PHE   A C   1 
ATOM   1055 O  O   . PHE   A  1  143 ? 29.186  8.011   39.445 1.00 33.24  ? 156 PHE   A O   1 
ATOM   1056 C  CB  . PHE   A  1  143 ? 29.817  4.931   39.729 1.00 31.64  ? 156 PHE   A CB  1 
ATOM   1057 C  CG  . PHE   A  1  143 ? 28.739  4.405   38.805 1.00 30.44  ? 156 PHE   A CG  1 
ATOM   1058 C  CD1 . PHE   A  1  143 ? 29.029  3.429   37.869 1.00 30.81  ? 156 PHE   A CD1 1 
ATOM   1059 C  CD2 . PHE   A  1  143 ? 27.446  4.894   38.880 1.00 31.24  ? 156 PHE   A CD2 1 
ATOM   1060 C  CE1 . PHE   A  1  143 ? 28.045  2.929   37.039 1.00 34.19  ? 156 PHE   A CE1 1 
ATOM   1061 C  CE2 . PHE   A  1  143 ? 26.464  4.400   38.036 1.00 33.10  ? 156 PHE   A CE2 1 
ATOM   1062 C  CZ  . PHE   A  1  143 ? 26.763  3.418   37.121 1.00 30.46  ? 156 PHE   A CZ  1 
ATOM   1063 N  N   . ASN   A  1  144 ? 29.443  7.272   37.332 1.00 32.65  ? 157 ASN   A N   1 
ATOM   1064 C  CA  . ASN   A  1  144 ? 28.605  8.280   36.722 1.00 32.44  ? 157 ASN   A CA  1 
ATOM   1065 C  C   . ASN   A  1  144 ? 27.474  7.597   35.944 1.00 28.90  ? 157 ASN   A C   1 
ATOM   1066 O  O   . ASN   A  1  144 ? 27.718  6.924   34.949 1.00 26.62  ? 157 ASN   A O   1 
ATOM   1067 C  CB  . ASN   A  1  144 ? 29.509  9.178   35.901 1.00 35.13  ? 157 ASN   A CB  1 
ATOM   1068 C  CG  . ASN   A  1  144 ? 28.750  10.186  35.074 1.00 37.49  ? 157 ASN   A CG  1 
ATOM   1069 O  OD1 . ASN   A  1  144 ? 27.822  9.820   34.347 1.00 35.13  ? 157 ASN   A OD1 1 
ATOM   1070 N  ND2 . ASN   A  1  144 ? 29.138  11.451  35.186 1.00 45.51  ? 157 ASN   A ND2 1 
ATOM   1071 N  N   . GLN   A  1  145 ? 26.246  7.788   36.416 1.00 29.88  ? 158 GLN   A N   1 
ATOM   1072 C  CA  . GLN   A  1  145 ? 25.063  7.087   35.943 1.00 34.53  ? 158 GLN   A CA  1 
ATOM   1073 C  C   . GLN   A  1  145 ? 24.774  7.454   34.484 1.00 34.39  ? 158 GLN   A C   1 
ATOM   1074 O  O   . GLN   A  1  145 ? 24.366  6.592   33.712 1.00 34.84  ? 158 GLN   A O   1 
ATOM   1075 C  CB  . GLN   A  1  145 ? 23.871  7.380   36.869 1.00 34.57  ? 158 GLN   A CB  1 
ATOM   1076 C  CG  . GLN   A  1  145 ? 22.594  6.607   36.540 1.00 35.52  ? 158 GLN   A CG  1 
ATOM   1077 C  CD  . GLN   A  1  145 ? 22.742  5.089   36.611 1.00 40.17  ? 158 GLN   A CD  1 
ATOM   1078 O  OE1 . GLN   A  1  145 ? 23.123  4.497   37.628 1.00 38.13  ? 158 GLN   A OE1 1 
ATOM   1079 N  NE2 . GLN   A  1  145 ? 22.416  4.415   35.522 1.00 39.37  ? 158 GLN   A NE2 1 
ATOM   1080 N  N   . THR   A  1  146 ? 24.996  8.714   34.097 1.00 32.32  ? 159 THR   A N   1 
ATOM   1081 C  CA  . THR   A  1  146 ? 24.783  9.134   32.718 1.00 34.92  ? 159 THR   A CA  1 
ATOM   1082 C  C   . THR   A  1  146 ? 25.669  8.316   31.781 1.00 33.51  ? 159 THR   A C   1 
ATOM   1083 O  O   . THR   A  1  146 ? 25.245  7.916   30.705 1.00 33.15  ? 159 THR   A O   1 
ATOM   1084 C  CB  . THR   A  1  146 ? 25.091  10.620  32.518 1.00 35.36  ? 159 THR   A CB  1 
ATOM   1085 O  OG1 . THR   A  1  146 ? 24.253  11.362  33.388 1.00 36.33  ? 159 THR   A OG1 1 
ATOM   1086 C  CG2 . THR   A  1  146 ? 24.792  11.090  31.105 1.00 36.49  ? 159 THR   A CG2 1 
ATOM   1087 N  N   . LEU   A  1  147 ? 26.930  8.131   32.171 1.00 32.86  ? 160 LEU   A N   1 
ATOM   1088 C  CA  . LEU   A  1  147 ? 27.849  7.365   31.343 1.00 30.15  ? 160 LEU   A CA  1 
ATOM   1089 C  C   . LEU   A  1  147 ? 27.466  5.889   31.311 1.00 29.21  ? 160 LEU   A C   1 
ATOM   1090 O  O   . LEU   A  1  147 ? 27.553  5.240   30.268 1.00 27.21  ? 160 LEU   A O   1 
ATOM   1091 C  CB  . LEU   A  1  147 ? 29.264  7.583   31.851 1.00 33.80  ? 160 LEU   A CB  1 
ATOM   1092 C  CG  . LEU   A  1  147 ? 29.854  8.965   31.545 1.00 34.84  ? 160 LEU   A CG  1 
ATOM   1093 C  CD1 . LEU   A  1  147 ? 31.272  9.044   32.065 1.00 35.77  ? 160 LEU   A CD1 1 
ATOM   1094 C  CD2 . LEU   A  1  147 ? 29.817  9.264   30.062 1.00 34.50  ? 160 LEU   A CD2 1 
ATOM   1095 N  N   . PHE   A  1  148 ? 27.001  5.373   32.452 1.00 29.70  ? 161 PHE   A N   1 
ATOM   1096 C  CA  . PHE   A  1  148 ? 26.524  4.008   32.493 1.00 30.26  ? 161 PHE   A CA  1 
ATOM   1097 C  C   . PHE   A  1  148 ? 25.284  3.848   31.610 1.00 31.41  ? 161 PHE   A C   1 
ATOM   1098 O  O   . PHE   A  1  148 ? 25.139  2.817   30.978 1.00 32.18  ? 161 PHE   A O   1 
ATOM   1099 C  CB  . PHE   A  1  148 ? 26.244  3.552   33.921 1.00 30.61  ? 161 PHE   A CB  1 
ATOM   1100 C  CG  . PHE   A  1  148 ? 25.921  2.068   33.960 1.00 30.11  ? 161 PHE   A CG  1 
ATOM   1101 C  CD1 . PHE   A  1  148 ? 26.926  1.119   33.826 1.00 32.37  ? 161 PHE   A CD1 1 
ATOM   1102 C  CD2 . PHE   A  1  148 ? 24.615  1.632   34.077 1.00 29.79  ? 161 PHE   A CD2 1 
ATOM   1103 C  CE1 . PHE   A  1  148 ? 26.629  -0.240  33.875 1.00 32.80  ? 161 PHE   A CE1 1 
ATOM   1104 C  CE2 . PHE   A  1  148 ? 24.316  0.274   34.085 1.00 30.10  ? 161 PHE   A CE2 1 
ATOM   1105 C  CZ  . PHE   A  1  148 ? 25.313  -0.654  33.998 1.00 30.37  ? 161 PHE   A CZ  1 
ATOM   1106 N  N   . ASP   A  1  149 ? 24.403  4.861   31.558 1.00 31.86  ? 162 ASP   A N   1 
ATOM   1107 C  CA  . ASP   A  1  149 ? 23.239  4.828   30.679 1.00 33.87  ? 162 ASP   A CA  1 
ATOM   1108 C  C   . ASP   A  1  149 ? 23.665  4.725   29.207 1.00 31.78  ? 162 ASP   A C   1 
ATOM   1109 O  O   . ASP   A  1  149 ? 23.032  4.015   28.429 1.00 31.42  ? 162 ASP   A O   1 
ATOM   1110 C  CB  . ASP   A  1  149 ? 22.313  6.018   30.914 1.00 35.51  ? 162 ASP   A CB  1 
ATOM   1111 C  CG  . ASP   A  1  149 ? 21.595  6.050   32.259 1.00 38.92  ? 162 ASP   A CG  1 
ATOM   1112 O  OD1 . ASP   A  1  149 ? 21.435  4.969   32.872 1.00 44.80  ? 162 ASP   A OD1 1 
ATOM   1113 O  OD2 . ASP   A  1  149 ? 21.258  7.163   32.708 1.00 41.54  ? 162 ASP   A OD2 1 
ATOM   1114 N  N   . LYS   A  1  150 ? 24.732  5.424   28.820 1.00 33.03  ? 163 LYS   A N   1 
ATOM   1115 C  CA  . LYS   A  1  150 ? 25.269  5.297   27.465 1.00 34.59  ? 163 LYS   A CA  1 
ATOM   1116 C  C   . LYS   A  1  150 ? 25.839  3.894   27.231 1.00 32.87  ? 163 LYS   A C   1 
ATOM   1117 O  O   . LYS   A  1  150 ? 25.707  3.349   26.151 1.00 32.88  ? 163 LYS   A O   1 
ATOM   1118 C  CB  . LYS   A  1  150 ? 26.323  6.384   27.251 1.00 34.60  ? 163 LYS   A CB  1 
ATOM   1119 C  CG  . LYS   A  1  150 ? 27.027  6.363   25.913 1.00 36.00  ? 163 LYS   A CG  1 
ATOM   1120 C  CD  . LYS   A  1  150 ? 28.080  7.454   25.806 1.00 41.42  ? 163 LYS   A CD  1 
ATOM   1121 C  CE  . LYS   A  1  150 ? 28.829  7.461   24.499 1.00 45.69  ? 163 LYS   A CE  1 
ATOM   1122 N  NZ  . LYS   A  1  150 ? 28.469  8.622   23.696 1.00 42.82  ? 163 LYS   A NZ  1 
ATOM   1123 N  N   . PHE   A  1  151 ? 26.476  3.306   28.249 1.00 30.68  ? 164 PHE   A N   1 
ATOM   1124 C  CA  . PHE   A  1  151 ? 27.008  1.953   28.167 1.00 29.48  ? 164 PHE   A CA  1 
ATOM   1125 C  C   . PHE   A  1  151 ? 25.863  0.989   27.883 1.00 29.20  ? 164 PHE   A C   1 
ATOM   1126 O  O   . PHE   A  1  151 ? 25.976  0.115   27.035 1.00 29.70  ? 164 PHE   A O   1 
ATOM   1127 C  CB  . PHE   A  1  151 ? 27.748  1.641   29.479 1.00 28.30  ? 164 PHE   A CB  1 
ATOM   1128 C  CG  . PHE   A  1  151 ? 28.285  0.231   29.653 1.00 29.11  ? 164 PHE   A CG  1 
ATOM   1129 C  CD1 . PHE   A  1  151 ? 27.480  -0.795  30.132 1.00 30.29  ? 164 PHE   A CD1 1 
ATOM   1130 C  CD2 . PHE   A  1  151 ? 29.627  -0.045  29.419 1.00 32.74  ? 164 PHE   A CD2 1 
ATOM   1131 C  CE1 . PHE   A  1  151 ? 27.987  -2.070  30.312 1.00 31.51  ? 164 PHE   A CE1 1 
ATOM   1132 C  CE2 . PHE   A  1  151 ? 30.140  -1.321  29.615 1.00 34.48  ? 164 PHE   A CE2 1 
ATOM   1133 C  CZ  . PHE   A  1  151 ? 29.311  -2.337  30.048 1.00 35.39  ? 164 PHE   A CZ  1 
ATOM   1134 N  N   . VAL   A  1  152 ? 24.752  1.162   28.598 1.00 29.92  ? 165 VAL   A N   1 
ATOM   1135 C  CA  . VAL   A  1  152 ? 23.559  0.360   28.368 1.00 33.42  ? 165 VAL   A CA  1 
ATOM   1136 C  C   . VAL   A  1  152 ? 23.019  0.617   26.953 1.00 32.03  ? 165 VAL   A C   1 
ATOM   1137 O  O   . VAL   A  1  152 ? 22.697  -0.312  26.204 1.00 30.98  ? 165 VAL   A O   1 
ATOM   1138 C  CB  . VAL   A  1  152 ? 22.501  0.645   29.449 1.00 31.10  ? 165 VAL   A CB  1 
ATOM   1139 C  CG1 . VAL   A  1  152 ? 21.207  -0.097  29.153 1.00 31.70  ? 165 VAL   A CG1 1 
ATOM   1140 C  CG2 . VAL   A  1  152 ? 22.992  0.277   30.843 1.00 29.82  ? 165 VAL   A CG2 1 
ATOM   1141 N  N   . ASP   A  1  153 ? 22.945  1.887   26.569 1.00 31.96  ? 166 ASP   A N   1 
ATOM   1142 C  CA  . ASP   A  1  153 ? 22.445  2.251   25.245 1.00 33.73  ? 166 ASP   A CA  1 
ATOM   1143 C  C   . ASP   A  1  153 ? 23.240  1.542   24.146 1.00 32.56  ? 166 ASP   A C   1 
ATOM   1144 O  O   . ASP   A  1  153 ? 22.669  0.931   23.249 1.00 31.95  ? 166 ASP   A O   1 
ATOM   1145 C  CB  . ASP   A  1  153 ? 22.402  3.761   25.075 1.00 38.12  ? 166 ASP   A CB  1 
ATOM   1146 C  CG  . ASP   A  1  153 ? 21.842  4.252   23.745 1.00 42.85  ? 166 ASP   A CG  1 
ATOM   1147 O  OD1 . ASP   A  1  153 ? 20.759  3.754   23.358 1.00 41.18  ? 166 ASP   A OD1 1 
ATOM   1148 O  OD2 . ASP   A  1  153 ? 22.499  5.115   23.110 1.00 42.35  ? 166 ASP   A OD2 1 
ATOM   1149 N  N   . PHE   A  1  154 ? 24.569  1.612   24.221 1.00 30.48  ? 167 PHE   A N   1 
ATOM   1150 C  CA  . PHE   A  1  154 ? 25.418  1.005   23.213 1.00 29.81  ? 167 PHE   A CA  1 
ATOM   1151 C  C   . PHE   A  1  154 ? 25.345  -0.515  23.283 1.00 28.51  ? 167 PHE   A C   1 
ATOM   1152 O  O   . PHE   A  1  154 ? 25.453  -1.175  22.265 1.00 27.57  ? 167 PHE   A O   1 
ATOM   1153 C  CB  . PHE   A  1  154 ? 26.868  1.473   23.339 1.00 31.47  ? 167 PHE   A CB  1 
ATOM   1154 C  CG  . PHE   A  1  154 ? 27.134  2.758   22.574 1.00 31.25  ? 167 PHE   A CG  1 
ATOM   1155 C  CD1 . PHE   A  1  154 ? 26.482  3.936   22.906 1.00 32.87  ? 167 PHE   A CD1 1 
ATOM   1156 C  CD2 . PHE   A  1  154 ? 28.008  2.766   21.511 1.00 33.74  ? 167 PHE   A CD2 1 
ATOM   1157 C  CE1 . PHE   A  1  154 ? 26.748  5.109   22.224 1.00 33.33  ? 167 PHE   A CE1 1 
ATOM   1158 C  CE2 . PHE   A  1  154 ? 28.240  3.935   20.803 1.00 37.28  ? 167 PHE   A CE2 1 
ATOM   1159 C  CZ  . PHE   A  1  154 ? 27.609  5.097   21.158 1.00 37.12  ? 167 PHE   A CZ  1 
ATOM   1160 N  N   . SER   A  1  155 ? 25.179  -1.088  24.467 1.00 25.56  ? 168 SER   A N   1 
ATOM   1161 C  CA  . SER   A  1  155 ? 24.982  -2.531  24.538 1.00 30.05  ? 168 SER   A CA  1 
ATOM   1162 C  C   . SER   A  1  155 ? 23.662  -2.911  23.852 1.00 32.81  ? 168 SER   A C   1 
ATOM   1163 O  O   . SER   A  1  155 ? 23.561  -3.967  23.236 1.00 31.41  ? 168 SER   A O   1 
ATOM   1164 C  CB  . SER   A  1  155 ? 25.005  -3.024  25.968 1.00 30.50  ? 168 SER   A CB  1 
ATOM   1165 O  OG  . SER   A  1  155 ? 26.221  -2.681  26.613 1.00 31.48  ? 168 SER   A OG  1 
ATOM   1166 N  N   . ASN   A  1  156 ? 22.624  -2.062  23.985 1.00 33.51  ? 169 ASN   A N   1 
ATOM   1167 C  CA  . ASN   A  1  156 ? 21.357  -2.316  23.312 1.00 31.53  ? 169 ASN   A CA  1 
ATOM   1168 C  C   . ASN   A  1  156 ? 21.523  -2.231  21.799 1.00 31.64  ? 169 ASN   A C   1 
ATOM   1169 O  O   . ASN   A  1  156 ? 20.998  -3.066  21.076 1.00 30.57  ? 169 ASN   A O   1 
ATOM   1170 C  CB  . ASN   A  1  156 ? 20.270  -1.313  23.687 1.00 32.55  ? 169 ASN   A CB  1 
ATOM   1171 C  CG  . ASN   A  1  156 ? 19.723  -1.506  25.077 1.00 31.56  ? 169 ASN   A CG  1 
ATOM   1172 O  OD1 . ASN   A  1  156 ? 19.810  -2.599  25.641 1.00 31.93  ? 169 ASN   A OD1 1 
ATOM   1173 N  ND2 . ASN   A  1  156 ? 19.181  -0.446  25.640 1.00 32.75  ? 169 ASN   A ND2 1 
ATOM   1174 N  N   . ARG   A  1  157 ? 22.265  -1.221  21.330 1.00 30.65  ? 170 ARG   A N   1 
ATOM   1175 C  CA  . ARG   A  1  157 ? 22.367  -0.935  19.909 1.00 31.86  ? 170 ARG   A CA  1 
ATOM   1176 C  C   . ARG   A  1  157 ? 23.219  -1.973  19.190 1.00 32.88  ? 170 ARG   A C   1 
ATOM   1177 O  O   . ARG   A  1  157 ? 22.921  -2.277  18.049 1.00 39.51  ? 170 ARG   A O   1 
ATOM   1178 C  CB  . ARG   A  1  157 ? 22.900  0.491   19.713 1.00 30.70  ? 170 ARG   A CB  1 
ATOM   1179 C  CG  . ARG   A  1  157 ? 21.787  1.487   20.003 1.00 33.14  ? 170 ARG   A CG  1 
ATOM   1180 C  CD  . ARG   A  1  157 ? 22.238  2.899   20.279 1.00 32.89  ? 170 ARG   A CD  1 
ATOM   1181 N  NE  . ARG   A  1  157 ? 23.163  3.404   19.271 1.00 37.06  ? 170 ARG   A NE  1 
ATOM   1182 C  CZ  . ARG   A  1  157 ? 23.797  4.566   19.358 1.00 40.40  ? 170 ARG   A CZ  1 
ATOM   1183 N  NH1 . ARG   A  1  157 ? 24.571  4.917   18.367 1.00 39.01  ? 170 ARG   A NH1 1 
ATOM   1184 N  NH2 . ARG   A  1  157 ? 23.662  5.366   20.414 1.00 42.49  ? 170 ARG   A NH2 1 
ATOM   1185 N  N   . TYR   A  1  158 ? 24.285  -2.487  19.833 1.00 36.07  ? 171 TYR   A N   1 
ATOM   1186 C  CA  . TYR   A  1  158 ? 25.303  -3.274  19.139 1.00 33.68  ? 171 TYR   A CA  1 
ATOM   1187 C  C   . TYR   A  1  158 ? 25.499  -4.674  19.713 1.00 32.61  ? 171 TYR   A C   1 
ATOM   1188 O  O   . TYR   A  1  158 ? 26.150  -5.497  19.076 1.00 36.57  ? 171 TYR   A O   1 
ATOM   1189 C  CB  . TYR   A  1  158 ? 26.641  -2.542  19.106 1.00 31.26  ? 171 TYR   A CB  1 
ATOM   1190 C  CG  . TYR   A  1  158 ? 26.537  -1.187  18.426 1.00 34.48  ? 171 TYR   A CG  1 
ATOM   1191 C  CD1 . TYR   A  1  158 ? 26.386  -1.079  17.038 1.00 38.02  ? 171 TYR   A CD1 1 
ATOM   1192 C  CD2 . TYR   A  1  158 ? 26.584  -0.018  19.162 1.00 33.71  ? 171 TYR   A CD2 1 
ATOM   1193 C  CE1 . TYR   A  1  158 ? 26.248  0.157   16.424 1.00 34.34  ? 171 TYR   A CE1 1 
ATOM   1194 C  CE2 . TYR   A  1  158 ? 26.476  1.225   18.557 1.00 34.65  ? 171 TYR   A CE2 1 
ATOM   1195 C  CZ  . TYR   A  1  158 ? 26.287  1.308   17.190 1.00 36.35  ? 171 TYR   A CZ  1 
ATOM   1196 O  OH  . TYR   A  1  158 ? 26.138  2.542   16.638 1.00 42.63  ? 171 TYR   A OH  1 
ATOM   1197 N  N   . GLY   A  1  159 ? 24.946  -4.967  20.893 1.00 33.50  ? 172 GLY   A N   1 
ATOM   1198 C  CA  . GLY   A  1  159 ? 25.240  -6.240  21.543 1.00 30.78  ? 172 GLY   A CA  1 
ATOM   1199 C  C   . GLY   A  1  159 ? 24.006  -7.021  21.995 1.00 30.33  ? 172 GLY   A C   1 
ATOM   1200 O  O   . GLY   A  1  159 ? 24.121  -7.888  22.836 1.00 33.29  ? 172 GLY   A O   1 
ATOM   1201 N  N   . GLY   A  1  160 ? 22.828  -6.733  21.439 1.00 33.84  ? 173 GLY   A N   1 
ATOM   1202 C  CA  . GLY   A  1  160 ? 21.626  -7.464  21.813 1.00 32.21  ? 173 GLY   A CA  1 
ATOM   1203 C  C   . GLY   A  1  160 ? 21.197  -7.183  23.253 1.00 34.13  ? 173 GLY   A C   1 
ATOM   1204 O  O   . GLY   A  1  160 ? 20.444  -7.955  23.824 1.00 30.37  ? 173 GLY   A O   1 
ATOM   1205 N  N   . GLY   A  1  161 ? 21.670  -6.078  23.845 1.00 33.03  ? 174 GLY   A N   1 
ATOM   1206 C  CA  . GLY   A  1  161 ? 21.374  -5.762  25.240 1.00 35.45  ? 174 GLY   A CA  1 
ATOM   1207 C  C   . GLY   A  1  161 ? 22.460  -6.229  26.212 1.00 34.38  ? 174 GLY   A C   1 
ATOM   1208 O  O   . GLY   A  1  161 ? 22.329  -6.036  27.425 1.00 38.38  ? 174 GLY   A O   1 
ATOM   1209 N  N   . PHE   A  1  162 ? 23.552  -6.766  25.652 1.00 32.79  ? 175 PHE   A N   1 
ATOM   1210 C  CA  . PHE   A  1  162 ? 24.716  -7.200  26.390 1.00 30.48  ? 175 PHE   A CA  1 
ATOM   1211 C  C   . PHE   A  1  162 ? 25.956  -6.470  25.900 1.00 32.51  ? 175 PHE   A C   1 
ATOM   1212 O  O   . PHE   A  1  162 ? 25.998  -5.998  24.774 1.00 31.60  ? 175 PHE   A O   1 
ATOM   1213 C  CB  . PHE   A  1  162 ? 24.899  -8.697  26.176 1.00 32.29  ? 175 PHE   A CB  1 
ATOM   1214 C  CG  . PHE   A  1  162 ? 23.744  -9.511  26.713 1.00 31.88  ? 175 PHE   A CG  1 
ATOM   1215 C  CD1 . PHE   A  1  162 ? 22.611  -9.737  25.926 1.00 36.00  ? 175 PHE   A CD1 1 
ATOM   1216 C  CD2 . PHE   A  1  162 ? 23.793  -10.047 27.988 1.00 34.08  ? 175 PHE   A CD2 1 
ATOM   1217 C  CE1 . PHE   A  1  162 ? 21.550  -10.484 26.420 1.00 36.91  ? 175 PHE   A CE1 1 
ATOM   1218 C  CE2 . PHE   A  1  162 ? 22.720  -10.798 28.483 1.00 36.91  ? 175 PHE   A CE2 1 
ATOM   1219 C  CZ  . PHE   A  1  162 ? 21.599  -11.003 27.698 1.00 35.06  ? 175 PHE   A CZ  1 
ATOM   1220 N  N   . TYR   A  1  163 ? 26.975  -6.399  26.758 1.00 33.88  ? 176 TYR   A N   1 
ATOM   1221 C  CA  . TYR   A  1  163 ? 28.249  -5.808  26.383 1.00 31.36  ? 176 TYR   A CA  1 
ATOM   1222 C  C   . TYR   A  1  163 ? 29.136  -6.911  25.827 1.00 30.19  ? 176 TYR   A C   1 
ATOM   1223 O  O   . TYR   A  1  163 ? 29.465  -7.865  26.535 1.00 29.97  ? 176 TYR   A O   1 
ATOM   1224 C  CB  . TYR   A  1  163 ? 28.930  -5.120  27.572 1.00 32.75  ? 176 TYR   A CB  1 
ATOM   1225 C  CG  . TYR   A  1  163 ? 30.198  -4.362  27.224 1.00 31.60  ? 176 TYR   A CG  1 
ATOM   1226 C  CD1 . TYR   A  1  163 ? 30.141  -3.082  26.707 1.00 31.73  ? 176 TYR   A CD1 1 
ATOM   1227 C  CD2 . TYR   A  1  163 ? 31.455  -4.908  27.434 1.00 32.56  ? 176 TYR   A CD2 1 
ATOM   1228 C  CE1 . TYR   A  1  163 ? 31.290  -2.366  26.409 1.00 34.06  ? 176 TYR   A CE1 1 
ATOM   1229 C  CE2 . TYR   A  1  163 ? 32.614  -4.198  27.144 1.00 31.49  ? 176 TYR   A CE2 1 
ATOM   1230 C  CZ  . TYR   A  1  163 ? 32.531  -2.919  26.636 1.00 31.21  ? 176 TYR   A CZ  1 
ATOM   1231 O  OH  . TYR   A  1  163 ? 33.646  -2.200  26.333 1.00 30.75  ? 176 TYR   A OH  1 
ATOM   1232 N  N   . ASN   A  1  164 ? 29.522  -6.759  24.561 1.00 30.80  ? 177 ASN   A N   1 
ATOM   1233 C  CA  . ASN   A  1  164 ? 30.440  -7.691  23.927 1.00 33.96  ? 177 ASN   A CA  1 
ATOM   1234 C  C   . ASN   A  1  164 ? 31.455  -6.896  23.113 1.00 30.52  ? 177 ASN   A C   1 
ATOM   1235 O  O   . ASN   A  1  164 ? 31.471  -5.662  23.140 1.00 29.67  ? 177 ASN   A O   1 
ATOM   1236 C  CB  . ASN   A  1  164 ? 29.663  -8.760  23.159 1.00 37.08  ? 177 ASN   A CB  1 
ATOM   1237 C  CG  . ASN   A  1  164 ? 29.082  -8.287  21.844 1.00 36.35  ? 177 ASN   A CG  1 
ATOM   1238 O  OD1 . ASN   A  1  164 ? 29.351  -7.172  21.365 1.00 34.12  ? 177 ASN   A OD1 1 
ATOM   1239 N  ND2 . ASN   A  1  164 ? 28.300  -9.164  21.238 1.00 41.72  ? 177 ASN   A ND2 1 
ATOM   1240 N  N   . LEU   A  1  165 ? 32.314  -7.603  22.377 1.00 31.43  ? 178 LEU   A N   1 
ATOM   1241 C  CA  . LEU   A  1  165 ? 33.444  -6.936  21.750 1.00 34.31  ? 178 LEU   A CA  1 
ATOM   1242 C  C   . LEU   A  1  165 ? 33.001  -5.908  20.705 1.00 33.33  ? 178 LEU   A C   1 
ATOM   1243 O  O   . LEU   A  1  165 ? 33.658  -4.878  20.550 1.00 32.50  ? 178 LEU   A O   1 
ATOM   1244 C  CB  . LEU   A  1  165 ? 34.355  -8.016  21.184 1.00 38.43  ? 178 LEU   A CB  1 
ATOM   1245 C  CG  . LEU   A  1  165 ? 35.793  -7.603  20.871 1.00 42.30  ? 178 LEU   A CG  1 
ATOM   1246 C  CD1 . LEU   A  1  165 ? 36.563  -7.182  22.096 1.00 42.69  ? 178 LEU   A CD1 1 
ATOM   1247 C  CD2 . LEU   A  1  165 ? 36.474  -8.822  20.254 1.00 45.33  ? 178 LEU   A CD2 1 
ATOM   1248 N  N   . THR   A  1  166 ? 31.884  -6.157  20.003 1.00 33.80  ? 179 THR   A N   1 
ATOM   1249 C  CA  . THR   A  1  166 ? 31.369  -5.199  19.021 1.00 32.89  ? 179 THR   A CA  1 
ATOM   1250 C  C   . THR   A  1  166 ? 30.973  -3.899  19.733 1.00 33.61  ? 179 THR   A C   1 
ATOM   1251 O  O   . THR   A  1  166 ? 31.268  -2.797  19.276 1.00 32.91  ? 179 THR   A O   1 
ATOM   1252 C  CB  . THR   A  1  166 ? 30.152  -5.795  18.299 1.00 34.84  ? 179 THR   A CB  1 
ATOM   1253 O  OG1 . THR   A  1  166 ? 30.377  -7.169  17.967 1.00 33.80  ? 179 THR   A OG1 1 
ATOM   1254 C  CG2 . THR   A  1  166 ? 29.706  -4.930  17.133 1.00 32.59  ? 179 THR   A CG2 1 
ATOM   1255 N  N   . VAL   A  1  167 ? 30.303  -4.030  20.884 1.00 33.16  ? 180 VAL   A N   1 
ATOM   1256 C  CA  . VAL   A  1  167 ? 29.902  -2.862  21.653 1.00 33.87  ? 180 VAL   A CA  1 
ATOM   1257 C  C   . VAL   A  1  167 ? 31.134  -2.074  22.083 1.00 31.33  ? 180 VAL   A C   1 
ATOM   1258 O  O   . VAL   A  1  167 ? 31.130  -0.848  22.033 1.00 34.33  ? 180 VAL   A O   1 
ATOM   1259 C  CB  . VAL   A  1  167 ? 29.064  -3.214  22.898 1.00 32.21  ? 180 VAL   A CB  1 
ATOM   1260 C  CG1 . VAL   A  1  167 ? 28.587  -1.954  23.598 1.00 28.94  ? 180 VAL   A CG1 1 
ATOM   1261 C  CG2 . VAL   A  1  167 ? 27.887  -4.129  22.572 1.00 33.01  ? 180 VAL   A CG2 1 
ATOM   1262 N  N   . ALA   A  1  168 ? 32.164  -2.782  22.554 1.00 35.18  ? 181 ALA   A N   1 
ATOM   1263 C  CA  . ALA   A  1  168 ? 33.391  -2.161  23.037 1.00 33.32  ? 181 ALA   A CA  1 
ATOM   1264 C  C   . ALA   A  1  168 ? 34.003  -1.258  21.969 1.00 32.42  ? 181 ALA   A C   1 
ATOM   1265 O  O   . ALA   A  1  168 ? 34.375  -0.118  22.241 1.00 32.62  ? 181 ALA   A O   1 
ATOM   1266 C  CB  . ALA   A  1  168 ? 34.358  -3.233  23.470 1.00 33.44  ? 181 ALA   A CB  1 
ATOM   1267 N  N   . GLY   A  1  169 ? 34.076  -1.758  20.736 1.00 35.42  ? 182 GLY   A N   1 
ATOM   1268 C  CA  . GLY   A  1  169 ? 34.612  -0.969  19.631 1.00 36.00  ? 182 GLY   A CA  1 
ATOM   1269 C  C   . GLY   A  1  169 ? 33.849  0.350   19.439 1.00 38.83  ? 182 GLY   A C   1 
ATOM   1270 O  O   . GLY   A  1  169 ? 34.443  1.429   19.295 1.00 38.18  ? 182 GLY   A O   1 
ATOM   1271 N  N   . GLU   A  1  170 ? 32.510  0.251   19.444 1.00 38.37  ? 183 GLU   A N   1 
ATOM   1272 C  CA  . GLU   A  1  170 ? 31.670  1.408   19.187 1.00 34.65  ? 183 GLU   A CA  1 
ATOM   1273 C  C   . GLU   A  1  170 ? 31.726  2.375   20.363 1.00 36.13  ? 183 GLU   A C   1 
ATOM   1274 O  O   . GLU   A  1  170 ? 31.837  3.583   20.173 1.00 37.05  ? 183 GLU   A O   1 
ATOM   1275 C  CB  . GLU   A  1  170 ? 30.234  0.971   18.929 1.00 33.04  ? 183 GLU   A CB  1 
ATOM   1276 C  CG  . GLU   A  1  170 ? 30.080  0.117   17.680 1.00 38.43  ? 183 GLU   A CG  1 
ATOM   1277 C  CD  . GLU   A  1  170 ? 30.417  0.845   16.389 1.00 45.93  ? 183 GLU   A CD  1 
ATOM   1278 O  OE1 . GLU   A  1  170 ? 30.500  2.096   16.394 1.00 46.92  ? 183 GLU   A OE1 1 
ATOM   1279 O  OE2 . GLU   A  1  170 ? 30.637  0.129   15.390 1.00 64.46  ? 183 GLU   A OE2 1 
ATOM   1280 N  N   . LEU   A  1  171 ? 31.651  1.842   21.587 1.00 33.49  ? 184 LEU   A N   1 
ATOM   1281 C  CA  . LEU   A  1  171 ? 31.588  2.705   22.748 1.00 33.81  ? 184 LEU   A CA  1 
ATOM   1282 C  C   . LEU   A  1  171 ? 32.893  3.482   22.901 1.00 31.97  ? 184 LEU   A C   1 
ATOM   1283 O  O   . LEU   A  1  171 ? 32.888  4.671   23.212 1.00 32.91  ? 184 LEU   A O   1 
ATOM   1284 C  CB  . LEU   A  1  171 ? 31.251  1.873   23.985 1.00 33.01  ? 184 LEU   A CB  1 
ATOM   1285 C  CG  . LEU   A  1  171 ? 31.148  2.653   25.297 1.00 33.84  ? 184 LEU   A CG  1 
ATOM   1286 C  CD1 . LEU   A  1  171 ? 30.062  3.714   25.262 1.00 33.58  ? 184 LEU   A CD1 1 
ATOM   1287 C  CD2 . LEU   A  1  171 ? 30.920  1.661   26.426 1.00 37.23  ? 184 LEU   A CD2 1 
ATOM   1288 N  N   . ARG   A  1  172 ? 34.020  2.809   22.695 1.00 33.29  ? 185 ARG   A N   1 
ATOM   1289 C  CA  . ARG   A  1  172 ? 35.317  3.438   22.898 1.00 35.60  ? 185 ARG   A CA  1 
ATOM   1290 C  C   . ARG   A  1  172 ? 35.450  4.670   22.001 1.00 34.07  ? 185 ARG   A C   1 
ATOM   1291 O  O   . ARG   A  1  172 ? 35.870  5.736   22.445 1.00 33.53  ? 185 ARG   A O   1 
ATOM   1292 C  CB  . ARG   A  1  172 ? 36.397  2.369   22.671 1.00 34.21  ? 185 ARG   A CB  1 
ATOM   1293 C  CG  . ARG   A  1  172 ? 37.796  2.844   22.324 1.00 34.21  ? 185 ARG   A CG  1 
ATOM   1294 C  CD  . ARG   A  1  172 ? 38.385  3.823   23.306 1.00 38.72  ? 185 ARG   A CD  1 
ATOM   1295 N  NE  . ARG   A  1  172 ? 38.286  3.420   24.715 1.00 35.49  ? 185 ARG   A NE  1 
ATOM   1296 C  CZ  . ARG   A  1  172 ? 37.892  4.198   25.694 1.00 36.96  ? 185 ARG   A CZ  1 
ATOM   1297 N  NH1 . ARG   A  1  172 ? 37.396  5.396   25.422 1.00 40.70  ? 185 ARG   A NH1 1 
ATOM   1298 N  NH2 . ARG   A  1  172 ? 37.993  3.773   26.942 1.00 38.28  ? 185 ARG   A NH2 1 
ATOM   1299 N  N   . TYR   A  1  173 ? 35.107  4.502   20.723 1.00 35.31  ? 186 TYR   A N   1 
ATOM   1300 C  CA  . TYR   A  1  173 ? 35.230  5.585   19.764 1.00 40.02  ? 186 TYR   A CA  1 
ATOM   1301 C  C   . TYR   A  1  173 ? 34.295  6.726   20.162 1.00 37.17  ? 186 TYR   A C   1 
ATOM   1302 O  O   . TYR   A  1  173 ? 34.672  7.893   20.130 1.00 35.49  ? 186 TYR   A O   1 
ATOM   1303 C  CB  . TYR   A  1  173 ? 34.920  5.048   18.358 1.00 42.53  ? 186 TYR   A CB  1 
ATOM   1304 C  CG  . TYR   A  1  173 ? 34.948  6.117   17.272 1.00 45.56  ? 186 TYR   A CG  1 
ATOM   1305 C  CD1 . TYR   A  1  173 ? 36.143  6.725   16.905 1.00 49.32  ? 186 TYR   A CD1 1 
ATOM   1306 C  CD2 . TYR   A  1  173 ? 33.792  6.504   16.601 1.00 50.75  ? 186 TYR   A CD2 1 
ATOM   1307 C  CE1 . TYR   A  1  173 ? 36.183  7.697   15.921 1.00 50.78  ? 186 TYR   A CE1 1 
ATOM   1308 C  CE2 . TYR   A  1  173 ? 33.819  7.465   15.600 1.00 54.78  ? 186 TYR   A CE2 1 
ATOM   1309 C  CZ  . TYR   A  1  173 ? 35.024  8.056   15.257 1.00 55.23  ? 186 TYR   A CZ  1 
ATOM   1310 O  OH  . TYR   A  1  173 ? 35.093  9.006   14.284 1.00 59.58  ? 186 TYR   A OH  1 
ATOM   1311 N  N   . SER   A  1  174 ? 33.056  6.371   20.531 1.00 34.78  ? 187 SER   A N   1 
ATOM   1312 C  CA  . SER   A  1  174 ? 32.057  7.371   20.846 1.00 32.36  ? 187 SER   A CA  1 
ATOM   1313 C  C   . SER   A  1  174 ? 32.470  8.175   22.079 1.00 35.55  ? 187 SER   A C   1 
ATOM   1314 O  O   . SER   A  1  174 ? 32.234  9.376   22.139 1.00 38.24  ? 187 SER   A O   1 
ATOM   1315 C  CB  . SER   A  1  174 ? 30.728  6.744   21.019 1.00 33.00  ? 187 SER   A CB  1 
ATOM   1316 O  OG  . SER   A  1  174 ? 29.788  7.735   21.404 1.00 37.55  ? 187 SER   A OG  1 
ATOM   1317 N  N   . ARG   A  1  175 ? 33.103  7.521   23.055 1.00 33.56  ? 188 ARG   A N   1 
ATOM   1318 C  CA  . ARG   A  1  175 ? 33.547  8.215   24.258 1.00 32.81  ? 188 ARG   A CA  1 
ATOM   1319 C  C   . ARG   A  1  175 ? 34.694  9.173   23.923 1.00 30.37  ? 188 ARG   A C   1 
ATOM   1320 O  O   . ARG   A  1  175 ? 34.772  10.249  24.491 1.00 30.21  ? 188 ARG   A O   1 
ATOM   1321 C  CB  . ARG   A  1  175 ? 33.921  7.223   25.380 1.00 32.61  ? 188 ARG   A CB  1 
ATOM   1322 C  CG  . ARG   A  1  175 ? 32.722  6.511   25.992 1.00 30.48  ? 188 ARG   A CG  1 
ATOM   1323 C  CD  . ARG   A  1  175 ? 31.814  7.451   26.760 1.00 31.68  ? 188 ARG   A CD  1 
ATOM   1324 N  NE  . ARG   A  1  175 ? 32.564  7.953   27.913 1.00 32.61  ? 188 ARG   A NE  1 
ATOM   1325 C  CZ  . ARG   A  1  175 ? 32.892  9.205   28.199 1.00 34.16  ? 188 ARG   A CZ  1 
ATOM   1326 N  NH1 . ARG   A  1  175 ? 32.379  10.196  27.505 1.00 34.53  ? 188 ARG   A NH1 1 
ATOM   1327 N  NH2 . ARG   A  1  175 ? 33.672  9.474   29.238 1.00 31.86  ? 188 ARG   A NH2 1 
ATOM   1328 N  N   . ILE   A  1  176 ? 35.567  8.796   22.986 1.00 29.45  ? 189 ILE   A N   1 
ATOM   1329 C  CA  . ILE   A  1  176 ? 36.590  9.713   22.509 1.00 33.17  ? 189 ILE   A CA  1 
ATOM   1330 C  C   . ILE   A  1  176 ? 35.946  10.960  21.899 1.00 36.16  ? 189 ILE   A C   1 
ATOM   1331 O  O   . ILE   A  1  176 ? 36.307  12.084  22.253 1.00 35.23  ? 189 ILE   A O   1 
ATOM   1332 C  CB  . ILE   A  1  176 ? 37.509  8.998   21.515 1.00 35.63  ? 189 ILE   A CB  1 
ATOM   1333 C  CG1 . ILE   A  1  176 ? 38.366  7.947   22.234 1.00 36.48  ? 189 ILE   A CG1 1 
ATOM   1334 C  CG2 . ILE   A  1  176 ? 38.370  9.996   20.748 1.00 37.59  ? 189 ILE   A CG2 1 
ATOM   1335 C  CD1 . ILE   A  1  176 ? 39.024  6.938   21.317 1.00 37.52  ? 189 ILE   A CD1 1 
ATOM   1336 N  N   . GLN   A  1  177 ? 34.964  10.766  21.013 1.00 36.54  ? 190 GLN   A N   1 
ATOM   1337 C  CA  . GLN   A  1  177 ? 34.239  11.884  20.419 1.00 37.85  ? 190 GLN   A CA  1 
ATOM   1338 C  C   . GLN   A  1  177 ? 33.579  12.767  21.476 1.00 37.01  ? 190 GLN   A C   1 
ATOM   1339 O  O   . GLN   A  1  177 ? 33.651  13.982  21.365 1.00 38.59  ? 190 GLN   A O   1 
ATOM   1340 C  CB  . GLN   A  1  177 ? 33.218  11.401  19.385 1.00 42.42  ? 190 GLN   A CB  1 
ATOM   1341 C  CG  . GLN   A  1  177 ? 33.840  10.682  18.193 1.00 44.58  ? 190 GLN   A CG  1 
ATOM   1342 C  CD  . GLN   A  1  177 ? 34.836  11.531  17.428 1.00 55.89  ? 190 GLN   A CD  1 
ATOM   1343 O  OE1 . GLN   A  1  177 ? 34.746  12.766  17.364 1.00 60.58  ? 190 GLN   A OE1 1 
ATOM   1344 N  NE2 . GLN   A  1  177 ? 35.795  10.861  16.807 1.00 58.05  ? 190 GLN   A NE2 1 
ATOM   1345 N  N   . ASP   A  1  178 ? 32.944  12.181  22.507 1.00 38.02  ? 191 ASP   A N   1 
ATOM   1346 C  CA  . ASP   A  1  178 ? 32.340  12.980  23.561 1.00 37.93  ? 191 ASP   A CA  1 
ATOM   1347 C  C   . ASP   A  1  178 ? 33.380  13.914  24.151 1.00 38.32  ? 191 ASP   A C   1 
ATOM   1348 O  O   . ASP   A  1  178 ? 33.100  15.089  24.367 1.00 40.40  ? 191 ASP   A O   1 
ATOM   1349 C  CB  . ASP   A  1  178 ? 31.790  12.162  24.725 1.00 41.25  ? 191 ASP   A CB  1 
ATOM   1350 C  CG  . ASP   A  1  178 ? 30.587  11.277  24.432 1.00 49.21  ? 191 ASP   A CG  1 
ATOM   1351 O  OD1 . ASP   A  1  178 ? 29.961  11.489  23.375 1.00 49.14  ? 191 ASP   A OD1 1 
ATOM   1352 O  OD2 . ASP   A  1  178 ? 30.284  10.377  25.269 1.00 51.13  ? 191 ASP   A OD2 1 
ATOM   1353 N  N   . SER   A  1  179 ? 34.556  13.358  24.468 1.00 40.31  ? 192 SER   A N   1 
ATOM   1354 C  CA  . SER   A  1  179 ? 35.591  14.119  25.150 1.00 40.48  ? 192 SER   A CA  1 
ATOM   1355 C  C   . SER   A  1  179 ? 36.155  15.204  24.226 1.00 36.73  ? 192 SER   A C   1 
ATOM   1356 O  O   . SER   A  1  179 ? 36.435  16.305  24.676 1.00 36.47  ? 192 SER   A O   1 
ATOM   1357 C  CB  . SER   A  1  179 ? 36.679  13.199  25.728 1.00 38.93  ? 192 SER   A CB  1 
ATOM   1358 O  OG  . SER   A  1  179 ? 36.293  12.628  26.981 1.00 37.11  ? 192 SER   A OG  1 
ATOM   1359 N  N   . ILE   A  1  180 ? 36.344  14.894  22.939 1.00 36.92  ? 193 ILE   A N   1 
ATOM   1360 C  CA  . ILE   A  1  180 ? 36.807  15.895  21.983 1.00 40.98  ? 193 ILE   A CA  1 
ATOM   1361 C  C   . ILE   A  1  180 ? 35.849  17.091  21.964 1.00 43.67  ? 193 ILE   A C   1 
ATOM   1362 O  O   . ILE   A  1  180 ? 36.294  18.242  22.027 1.00 35.95  ? 193 ILE   A O   1 
ATOM   1363 C  CB  . ILE   A  1  180 ? 36.956  15.307  20.576 1.00 41.35  ? 193 ILE   A CB  1 
ATOM   1364 C  CG1 . ILE   A  1  180 ? 38.147  14.362  20.493 1.00 41.07  ? 193 ILE   A CG1 1 
ATOM   1365 C  CG2 . ILE   A  1  180 ? 37.050  16.433  19.540 1.00 44.74  ? 193 ILE   A CG2 1 
ATOM   1366 C  CD1 . ILE   A  1  180 ? 38.193  13.550  19.214 1.00 43.01  ? 193 ILE   A CD1 1 
ATOM   1367 N  N   . ALA   A  1  181 ? 34.541  16.797  21.915 1.00 41.03  ? 194 ALA   A N   1 
ATOM   1368 C  CA  . ALA   A  1  181 ? 33.513  17.818  21.762 1.00 44.41  ? 194 ALA   A CA  1 
ATOM   1369 C  C   . ALA   A  1  181 ? 33.313  18.646  23.026 1.00 41.10  ? 194 ALA   A C   1 
ATOM   1370 O  O   . ALA   A  1  181 ? 32.837  19.768  22.926 1.00 47.96  ? 194 ALA   A O   1 
ATOM   1371 C  CB  . ALA   A  1  181 ? 32.198  17.186  21.327 1.00 45.27  ? 194 ALA   A CB  1 
ATOM   1372 N  N   . THR   A  1  182 ? 33.632  18.116  24.209 1.00 37.73  ? 195 THR   A N   1 
ATOM   1373 C  CA  . THR   A  1  182 ? 33.168  18.773  25.425 1.00 43.20  ? 195 THR   A CA  1 
ATOM   1374 C  C   . THR   A  1  182 ? 34.300  19.097  26.393 1.00 41.25  ? 195 THR   A C   1 
ATOM   1375 O  O   . THR   A  1  182 ? 34.052  19.796  27.367 1.00 42.54  ? 195 THR   A O   1 
ATOM   1376 C  CB  . THR   A  1  182 ? 32.112  17.918  26.137 1.00 50.96  ? 195 THR   A CB  1 
ATOM   1377 O  OG1 . THR   A  1  182 ? 32.726  16.698  26.556 1.00 50.42  ? 195 THR   A OG1 1 
ATOM   1378 C  CG2 . THR   A  1  182 ? 30.895  17.623  25.272 1.00 48.60  ? 195 THR   A CG2 1 
ATOM   1379 N  N   . ASN   A  1  183 ? 35.498  18.552  26.176 1.00 41.08  ? 196 ASN   A N   1 
ATOM   1380 C  CA  . ASN   A  1  183 ? 36.573  18.654  27.153 1.00 41.33  ? 196 ASN   A CA  1 
ATOM   1381 C  C   . ASN   A  1  183 ? 37.771  19.332  26.500 1.00 39.33  ? 196 ASN   A C   1 
ATOM   1382 O  O   . ASN   A  1  183 ? 38.497  18.720  25.722 1.00 37.18  ? 196 ASN   A O   1 
ATOM   1383 C  CB  . ASN   A  1  183 ? 36.981  17.289  27.703 1.00 41.56  ? 196 ASN   A CB  1 
ATOM   1384 C  CG  . ASN   A  1  183 ? 38.070  17.386  28.747 1.00 43.41  ? 196 ASN   A CG  1 
ATOM   1385 O  OD1 . ASN   A  1  183 ? 38.570  18.487  29.022 1.00 40.71  ? 196 ASN   A OD1 1 
ATOM   1386 N  ND2 . ASN   A  1  183 ? 38.475  16.250  29.310 1.00 40.85  ? 196 ASN   A ND2 1 
ATOM   1387 N  N   . PRO   A  1  184 ? 38.018  20.621  26.781 1.00 40.55  ? 197 PRO   A N   1 
ATOM   1388 C  CA  . PRO   A  1  184 ? 39.119  21.336  26.138 1.00 45.57  ? 197 PRO   A CA  1 
ATOM   1389 C  C   . PRO   A  1  184 ? 40.517  20.946  26.621 1.00 46.25  ? 197 PRO   A C   1 
ATOM   1390 O  O   . PRO   A  1  184 ? 41.493  21.299  25.965 1.00 52.89  ? 197 PRO   A O   1 
ATOM   1391 C  CB  . PRO   A  1  184 ? 38.765  22.796  26.456 1.00 42.99  ? 197 PRO   A CB  1 
ATOM   1392 C  CG  . PRO   A  1  184 ? 38.135  22.710  27.824 1.00 43.39  ? 197 PRO   A CG  1 
ATOM   1393 C  CD  . PRO   A  1  184 ? 37.260  21.450  27.726 1.00 45.21  ? 197 PRO   A CD  1 
ATOM   1394 N  N   . GLU   A  1  185 ? 40.609  20.230  27.753 1.00 49.48  ? 198 GLU   A N   1 
ATOM   1395 C  CA  . GLU   A  1  185 ? 41.876  19.693  28.246 1.00 47.69  ? 198 GLU   A CA  1 
ATOM   1396 C  C   . GLU   A  1  185 ? 42.039  18.214  27.869 1.00 43.90  ? 198 GLU   A C   1 
ATOM   1397 O  O   . GLU   A  1  185 ? 42.938  17.541  28.362 1.00 41.70  ? 198 GLU   A O   1 
ATOM   1398 C  CB  . GLU   A  1  185 ? 41.983  19.866  29.762 1.00 53.54  ? 198 GLU   A CB  1 
ATOM   1399 C  CG  . GLU   A  1  185 ? 41.983  21.324  30.217 1.00 60.52  ? 198 GLU   A CG  1 
ATOM   1400 C  CD  . GLU   A  1  185 ? 41.993  21.558  31.722 1.00 63.34  ? 198 GLU   A CD  1 
ATOM   1401 O  OE1 . GLU   A  1  185 ? 42.159  20.568  32.462 1.00 58.16  ? 198 GLU   A OE1 1 
ATOM   1402 O  OE2 . GLU   A  1  185 ? 41.841  22.724  32.162 1.00 66.44  ? 198 GLU   A OE2 1 
ATOM   1403 N  N   . PHE   A  1  186 ? 41.193  17.706  26.969 1.00 39.32  ? 199 PHE   A N   1 
ATOM   1404 C  CA  . PHE   A  1  186 ? 41.219  16.303  26.586 1.00 38.87  ? 199 PHE   A CA  1 
ATOM   1405 C  C   . PHE   A  1  186 ? 42.596  15.892  26.071 1.00 41.47  ? 199 PHE   A C   1 
ATOM   1406 O  O   . PHE   A  1  186 ? 43.116  16.497  25.139 1.00 39.96  ? 199 PHE   A O   1 
ATOM   1407 C  CB  . PHE   A  1  186 ? 40.201  16.000  25.486 1.00 37.54  ? 199 PHE   A CB  1 
ATOM   1408 C  CG  . PHE   A  1  186 ? 40.153  14.553  25.017 1.00 38.54  ? 199 PHE   A CG  1 
ATOM   1409 C  CD1 . PHE   A  1  186 ? 40.156  13.495  25.924 1.00 37.84  ? 199 PHE   A CD1 1 
ATOM   1410 C  CD2 . PHE   A  1  186 ? 40.139  14.248  23.664 1.00 37.16  ? 199 PHE   A CD2 1 
ATOM   1411 C  CE1 . PHE   A  1  186 ? 40.088  12.179  25.490 1.00 36.70  ? 199 PHE   A CE1 1 
ATOM   1412 C  CE2 . PHE   A  1  186 ? 40.097  12.929  23.233 1.00 40.85  ? 199 PHE   A CE2 1 
ATOM   1413 C  CZ  . PHE   A  1  186 ? 40.072  11.896  24.149 1.00 41.24  ? 199 PHE   A CZ  1 
ATOM   1414 N  N   . GLN   A  1  187 ? 43.142  14.836  26.684 1.00 42.88  ? 200 GLN   A N   1 
ATOM   1415 C  CA  . GLN   A  1  187 ? 44.404  14.223  26.308 1.00 42.25  ? 200 GLN   A CA  1 
ATOM   1416 C  C   . GLN   A  1  187 ? 44.157  12.733  26.106 1.00 40.69  ? 200 GLN   A C   1 
ATOM   1417 O  O   . GLN   A  1  187 ? 43.451  12.106  26.896 1.00 41.89  ? 200 GLN   A O   1 
ATOM   1418 C  CB  . GLN   A  1  187 ? 45.434  14.423  27.424 1.00 44.76  ? 200 GLN   A CB  1 
ATOM   1419 C  CG  . GLN   A  1  187 ? 45.932  15.858  27.569 1.00 51.76  ? 200 GLN   A CG  1 
ATOM   1420 C  CD  . GLN   A  1  187 ? 46.816  16.290  26.408 1.00 56.56  ? 200 GLN   A CD  1 
ATOM   1421 O  OE1 . GLN   A  1  187 ? 47.961  15.837  26.259 1.00 60.63  ? 200 GLN   A OE1 1 
ATOM   1422 N  NE2 . GLN   A  1  187 ? 46.279  17.157  25.560 1.00 50.72  ? 200 GLN   A NE2 1 
ATOM   1423 N  N   . PHE   A  1  188 ? 44.738  12.163  25.050 1.00 37.07  ? 201 PHE   A N   1 
ATOM   1424 C  CA  . PHE   A  1  188 ? 44.578  10.748  24.771 1.00 36.22  ? 201 PHE   A CA  1 
ATOM   1425 C  C   . PHE   A  1  188 ? 45.864  10.212  24.162 1.00 36.02  ? 201 PHE   A C   1 
ATOM   1426 O  O   . PHE   A  1  188 ? 45.891  9.786   23.010 1.00 39.92  ? 201 PHE   A O   1 
ATOM   1427 C  CB  . PHE   A  1  188 ? 43.377  10.571  23.847 1.00 36.50  ? 201 PHE   A CB  1 
ATOM   1428 C  CG  . PHE   A  1  188 ? 42.764  9.183   23.868 1.00 33.93  ? 201 PHE   A CG  1 
ATOM   1429 C  CD1 . PHE   A  1  188 ? 42.097  8.744   24.998 1.00 36.96  ? 201 PHE   A CD1 1 
ATOM   1430 C  CD2 . PHE   A  1  188 ? 42.787  8.368   22.746 1.00 33.93  ? 201 PHE   A CD2 1 
ATOM   1431 C  CE1 . PHE   A  1  188 ? 41.533  7.481   25.033 1.00 33.82  ? 201 PHE   A CE1 1 
ATOM   1432 C  CE2 . PHE   A  1  188 ? 42.202  7.117   22.776 1.00 33.07  ? 201 PHE   A CE2 1 
ATOM   1433 C  CZ  . PHE   A  1  188 ? 41.566  6.684   23.915 1.00 34.17  ? 201 PHE   A CZ  1 
ATOM   1434 N  N   . LYS   A  1  189 ? 46.923  10.210  24.965 1.00 38.10  ? 202 LYS   A N   1 
ATOM   1435 C  CA  . LYS   A  1  189 ? 48.235  9.826   24.478 1.00 40.41  ? 202 LYS   A CA  1 
ATOM   1436 C  C   . LYS   A  1  189 ? 49.000  9.091   25.574 1.00 39.09  ? 202 LYS   A C   1 
ATOM   1437 O  O   . LYS   A  1  189 ? 48.531  8.967   26.701 1.00 38.80  ? 202 LYS   A O   1 
ATOM   1438 C  CB  . LYS   A  1  189 ? 48.940  11.115  24.046 1.00 42.30  ? 202 LYS   A CB  1 
ATOM   1439 C  CG  . LYS   A  1  189 ? 49.098  12.140  25.155 1.00 47.78  ? 202 LYS   A CG  1 
ATOM   1440 C  CD  . LYS   A  1  189 ? 50.058  13.286  24.856 1.00 52.78  ? 202 LYS   A CD  1 
ATOM   1441 C  CE  . LYS   A  1  189 ? 49.509  14.205  23.811 1.00 57.82  ? 202 LYS   A CE  1 
ATOM   1442 N  NZ  . LYS   A  1  189 ? 50.295  15.428  23.689 1.00 63.14  ? 202 LYS   A NZ  1 
ATOM   1443 N  N   . ASN   A  1  190 ? 50.186  8.589   25.221 1.00 39.73  ? 203 ASN   A N   1 
ATOM   1444 C  CA  . ASN   A  1  190 ? 51.069  7.924   26.172 1.00 39.72  ? 203 ASN   A CA  1 
ATOM   1445 C  C   . ASN   A  1  190 ? 50.319  6.815   26.914 1.00 37.64  ? 203 ASN   A C   1 
ATOM   1446 O  O   . ASN   A  1  190 ? 49.724  5.954   26.280 1.00 43.12  ? 203 ASN   A O   1 
ATOM   1447 C  CB  . ASN   A  1  190 ? 51.782  8.977   27.018 1.00 40.84  ? 203 ASN   A CB  1 
ATOM   1448 C  CG  . ASN   A  1  190 ? 52.715  9.807   26.155 1.00 46.88  ? 203 ASN   A CG  1 
ATOM   1449 O  OD1 . ASN   A  1  190 ? 53.446  9.258   25.312 1.00 44.89  ? 203 ASN   A OD1 1 
ATOM   1450 N  ND2 . ASN   A  1  190 ? 52.685  11.115  26.335 1.00 46.29  ? 203 ASN   A ND2 1 
ATOM   1451 N  N   . VAL   A  1  191 ? 50.334  6.829   28.251 1.00 38.31  ? 204 VAL   A N   1 
ATOM   1452 C  CA  . VAL   A  1  191 ? 49.809  5.701   28.999 1.00 38.26  ? 204 VAL   A CA  1 
ATOM   1453 C  C   . VAL   A  1  191 ? 48.324  5.535   28.672 1.00 35.63  ? 204 VAL   A C   1 
ATOM   1454 O  O   . VAL   A  1  191 ? 47.850  4.439   28.411 1.00 31.65  ? 204 VAL   A O   1 
ATOM   1455 C  CB  . VAL   A  1  191 ? 50.024  5.861   30.511 1.00 38.59  ? 204 VAL   A CB  1 
ATOM   1456 C  CG1 . VAL   A  1  191 ? 49.330  4.743   31.297 1.00 38.09  ? 204 VAL   A CG1 1 
ATOM   1457 C  CG2 . VAL   A  1  191 ? 51.504  5.926   30.857 1.00 39.83  ? 204 VAL   A CG2 1 
ATOM   1458 N  N   . ARG   A  1  192 ? 47.596  6.648   28.665 1.00 34.23  ? 205 ARG   A N   1 
ATOM   1459 C  CA  . ARG   A  1  192 ? 46.159  6.610   28.534 1.00 32.31  ? 205 ARG   A CA  1 
ATOM   1460 C  C   . ARG   A  1  192 ? 45.757  6.007   27.197 1.00 33.13  ? 205 ARG   A C   1 
ATOM   1461 O  O   . ARG   A  1  192 ? 44.764  5.287   27.120 1.00 35.29  ? 205 ARG   A O   1 
ATOM   1462 C  CB  . ARG   A  1  192 ? 45.553  8.004   28.654 1.00 35.50  ? 205 ARG   A CB  1 
ATOM   1463 C  CG  . ARG   A  1  192 ? 44.033  7.973   28.560 1.00 36.35  ? 205 ARG   A CG  1 
ATOM   1464 C  CD  . ARG   A  1  192 ? 43.443  6.986   29.538 1.00 34.84  ? 205 ARG   A CD  1 
ATOM   1465 N  NE  . ARG   A  1  192 ? 41.980  6.906   29.516 1.00 34.06  ? 205 ARG   A NE  1 
ATOM   1466 C  CZ  . ARG   A  1  192 ? 41.275  5.849   29.866 1.00 33.10  ? 205 ARG   A CZ  1 
ATOM   1467 N  NH1 . ARG   A  1  192 ? 41.867  4.772   30.351 1.00 34.25  ? 205 ARG   A NH1 1 
ATOM   1468 N  NH2 . ARG   A  1  192 ? 39.965  5.874   29.734 1.00 34.49  ? 205 ARG   A NH2 1 
ATOM   1469 N  N   . PHE   A  1  193 ? 46.502  6.301   26.132 1.00 33.92  ? 206 PHE   A N   1 
ATOM   1470 C  CA  . PHE   A  1  193 ? 46.140  5.779   24.835 1.00 34.56  ? 206 PHE   A CA  1 
ATOM   1471 C  C   . PHE   A  1  193 ? 46.180  4.252   24.894 1.00 37.35  ? 206 PHE   A C   1 
ATOM   1472 O  O   . PHE   A  1  193 ? 45.328  3.587   24.318 1.00 40.75  ? 206 PHE   A O   1 
ATOM   1473 C  CB  . PHE   A  1  193 ? 47.026  6.317   23.714 1.00 37.99  ? 206 PHE   A CB  1 
ATOM   1474 C  CG  . PHE   A  1  193 ? 46.686  5.727   22.358 1.00 36.97  ? 206 PHE   A CG  1 
ATOM   1475 C  CD1 . PHE   A  1  193 ? 45.645  6.244   21.605 1.00 37.82  ? 206 PHE   A CD1 1 
ATOM   1476 C  CD2 . PHE   A  1  193 ? 47.400  4.656   21.844 1.00 38.95  ? 206 PHE   A CD2 1 
ATOM   1477 C  CE1 . PHE   A  1  193 ? 45.319  5.695   20.377 1.00 38.49  ? 206 PHE   A CE1 1 
ATOM   1478 C  CE2 . PHE   A  1  193 ? 47.076  4.119   20.611 1.00 40.00  ? 206 PHE   A CE2 1 
ATOM   1479 C  CZ  . PHE   A  1  193 ? 46.031  4.628   19.885 1.00 41.14  ? 206 PHE   A CZ  1 
ATOM   1480 N  N   . ILE   A  1  194 ? 47.161  3.686   25.598 1.00 34.75  ? 207 ILE   A N   1 
ATOM   1481 C  CA  . ILE   A  1  194 ? 47.280  2.238   25.649 1.00 37.36  ? 207 ILE   A CA  1 
ATOM   1482 C  C   . ILE   A  1  194 ? 46.204  1.643   26.570 1.00 35.74  ? 207 ILE   A C   1 
ATOM   1483 O  O   . ILE   A  1  194 ? 45.523  0.684   26.206 1.00 38.32  ? 207 ILE   A O   1 
ATOM   1484 C  CB  . ILE   A  1  194 ? 48.717  1.878   26.069 1.00 41.15  ? 207 ILE   A CB  1 
ATOM   1485 C  CG1 . ILE   A  1  194 ? 49.750  2.440   25.097 1.00 41.69  ? 207 ILE   A CG1 1 
ATOM   1486 C  CG2 . ILE   A  1  194 ? 48.873  0.382   26.219 1.00 40.36  ? 207 ILE   A CG2 1 
ATOM   1487 C  CD1 . ILE   A  1  194 ? 49.551  1.984   23.659 1.00 43.37  ? 207 ILE   A CD1 1 
ATOM   1488 N  N   . THR   A  1  195 ? 46.042  2.213   27.772 1.00 36.65  ? 208 THR   A N   1 
ATOM   1489 C  CA  . THR   A  1  195 ? 45.164  1.634   28.777 1.00 36.17  ? 208 THR   A CA  1 
ATOM   1490 C  C   . THR   A  1  195 ? 43.701  1.749   28.344 1.00 33.85  ? 208 THR   A C   1 
ATOM   1491 O  O   . THR   A  1  195 ? 42.895  0.897   28.678 1.00 37.25  ? 208 THR   A O   1 
ATOM   1492 C  CB  . THR   A  1  195 ? 45.402  2.257   30.156 1.00 35.87  ? 208 THR   A CB  1 
ATOM   1493 O  OG1 . THR   A  1  195 ? 45.109  3.644   30.071 1.00 37.35  ? 208 THR   A OG1 1 
ATOM   1494 C  CG2 . THR   A  1  195 ? 46.808  2.021   30.668 1.00 35.87  ? 208 THR   A CG2 1 
ATOM   1495 N  N   . ALA   A  1  196 ? 43.345  2.784   27.578 1.00 33.10  ? 209 ALA   A N   1 
ATOM   1496 C  CA  . ALA   A  1  196 ? 41.962  3.007   27.200 1.00 30.64  ? 209 ALA   A CA  1 
ATOM   1497 C  C   . ALA   A  1  196 ? 41.399  1.863   26.364 1.00 32.56  ? 209 ALA   A C   1 
ATOM   1498 O  O   . ALA   A  1  196 ? 40.192  1.678   26.352 1.00 35.82  ? 209 ALA   A O   1 
ATOM   1499 C  CB  . ALA   A  1  196 ? 41.814  4.312   26.467 1.00 30.68  ? 209 ALA   A CB  1 
ATOM   1500 N  N   . TYR   A  1  197 ? 42.238  1.128   25.626 1.00 31.12  ? 210 TYR   A N   1 
ATOM   1501 C  CA  . TYR   A  1  197 ? 41.753  0.039   24.798 1.00 30.38  ? 210 TYR   A CA  1 
ATOM   1502 C  C   . TYR   A  1  197 ? 41.630  -1.221  25.649 1.00 32.69  ? 210 TYR   A C   1 
ATOM   1503 O  O   . TYR   A  1  197 ? 40.622  -1.928  25.583 1.00 37.46  ? 210 TYR   A O   1 
ATOM   1504 C  CB  . TYR   A  1  197 ? 42.615  -0.051  23.531 1.00 32.78  ? 210 TYR   A CB  1 
ATOM   1505 C  CG  . TYR   A  1  197 ? 42.263  1.090   22.589 1.00 30.88  ? 210 TYR   A CG  1 
ATOM   1506 C  CD1 . TYR   A  1  197 ? 41.221  0.963   21.672 1.00 30.47  ? 210 TYR   A CD1 1 
ATOM   1507 C  CD2 . TYR   A  1  197 ? 42.891  2.321   22.684 1.00 31.36  ? 210 TYR   A CD2 1 
ATOM   1508 C  CE1 . TYR   A  1  197 ? 40.841  2.014   20.853 1.00 30.29  ? 210 TYR   A CE1 1 
ATOM   1509 C  CE2 . TYR   A  1  197 ? 42.537  3.379   21.861 1.00 32.86  ? 210 TYR   A CE2 1 
ATOM   1510 C  CZ  . TYR   A  1  197 ? 41.501  3.226   20.950 1.00 34.20  ? 210 TYR   A CZ  1 
ATOM   1511 O  OH  . TYR   A  1  197 ? 41.097  4.263   20.164 1.00 32.27  ? 210 TYR   A OH  1 
ATOM   1512 N  N   . GLY   A  1  198 ? 42.630  -1.495  26.479 1.00 33.31  ? 211 GLY   A N   1 
ATOM   1513 C  CA  . GLY   A  1  198 ? 42.570  -2.651  27.370 1.00 34.46  ? 211 GLY   A CA  1 
ATOM   1514 C  C   . GLY   A  1  198 ? 41.357  -2.614  28.309 1.00 31.38  ? 211 GLY   A C   1 
ATOM   1515 O  O   . GLY   A  1  198 ? 40.679  -3.624  28.503 1.00 28.56  ? 211 GLY   A O   1 
ATOM   1516 N  N   . GLU   A  1  199 ? 41.042  -1.433  28.850 1.00 29.23  ? 212 GLU   A N   1 
ATOM   1517 C  CA  A GLU   A  1  199 ? 39.968  -1.328  29.822 0.50 32.21  ? 212 GLU   A CA  1 
ATOM   1518 C  CA  B GLU   A  1  199 ? 39.966  -1.308  29.820 0.50 28.93  ? 212 GLU   A CA  1 
ATOM   1519 C  C   . GLU   A  1  199 ? 38.632  -1.725  29.196 1.00 30.25  ? 212 GLU   A C   1 
ATOM   1520 O  O   . GLU   A  1  199 ? 37.734  -2.171  29.899 1.00 30.59  ? 212 GLU   A O   1 
ATOM   1521 C  CB  A GLU   A  1  199 ? 39.920  0.066   30.453 0.50 33.91  ? 212 GLU   A CB  1 
ATOM   1522 C  CB  B GLU   A  1  199 ? 39.886  0.110   30.409 0.50 26.09  ? 212 GLU   A CB  1 
ATOM   1523 C  CG  A GLU   A  1  199 ? 40.902  0.181   31.610 0.50 36.93  ? 212 GLU   A CG  1 
ATOM   1524 C  CG  B GLU   A  1  199 ? 39.092  1.119   29.577 0.50 23.61  ? 212 GLU   A CG  1 
ATOM   1525 C  CD  A GLU   A  1  199 ? 41.473  1.550   31.882 0.50 35.94  ? 212 GLU   A CD  1 
ATOM   1526 C  CD  B GLU   A  1  199 ? 39.148  2.540   30.130 0.50 22.17  ? 212 GLU   A CD  1 
ATOM   1527 O  OE1 A GLU   A  1  199 ? 40.780  2.513   31.509 0.50 35.88  ? 212 GLU   A OE1 1 
ATOM   1528 O  OE1 B GLU   A  1  199 ? 39.818  2.806   31.144 0.50 22.11  ? 212 GLU   A OE1 1 
ATOM   1529 O  OE2 A GLU   A  1  199 ? 42.582  1.641   32.448 0.50 35.35  ? 212 GLU   A OE2 1 
ATOM   1530 O  OE2 B GLU   A  1  199 ? 38.547  3.427   29.536 0.50 19.72  ? 212 GLU   A OE2 1 
ATOM   1531 N  N   . THR   A  1  200 ? 38.499  -1.561  27.870 1.00 32.97  ? 213 THR   A N   1 
ATOM   1532 C  CA  . THR   A  1  200 ? 37.211  -1.790  27.242 1.00 32.58  ? 213 THR   A CA  1 
ATOM   1533 C  C   . THR   A  1  200 ? 36.973  -3.280  27.055 1.00 30.34  ? 213 THR   A C   1 
ATOM   1534 O  O   . THR   A  1  200 ? 35.829  -3.666  26.846 1.00 32.32  ? 213 THR   A O   1 
ATOM   1535 C  CB  . THR   A  1  200 ? 37.067  -1.059  25.908 1.00 36.06  ? 213 THR   A CB  1 
ATOM   1536 O  OG1 . THR   A  1  200 ? 37.950  -1.660  24.976 1.00 40.65  ? 213 THR   A OG1 1 
ATOM   1537 C  CG2 . THR   A  1  200 ? 37.340  0.425   26.015 1.00 37.39  ? 213 THR   A CG2 1 
ATOM   1538 N  N   . VAL   A  1  201 ? 38.024  -4.110  27.115 1.00 29.78  ? 214 VAL   A N   1 
ATOM   1539 C  CA  . VAL   A  1  201 ? 37.828  -5.552  26.987 1.00 29.32  ? 214 VAL   A CA  1 
ATOM   1540 C  C   . VAL   A  1  201 ? 37.900  -6.266  28.330 1.00 28.66  ? 214 VAL   A C   1 
ATOM   1541 O  O   . VAL   A  1  201 ? 37.474  -7.413  28.427 1.00 29.64  ? 214 VAL   A O   1 
ATOM   1542 C  CB  . VAL   A  1  201 ? 38.795  -6.176  25.969 1.00 31.16  ? 214 VAL   A CB  1 
ATOM   1543 C  CG1 . VAL   A  1  201 ? 38.557  -5.601  24.577 1.00 31.00  ? 214 VAL   A CG1 1 
ATOM   1544 C  CG2 . VAL   A  1  201 ? 40.255  -6.021  26.369 1.00 32.76  ? 214 VAL   A CG2 1 
ATOM   1545 N  N   . PHE   A  1  202 ? 38.396  -5.612  29.383 1.00 28.71  ? 215 PHE   A N   1 
ATOM   1546 C  CA  . PHE   A  1  202 ? 38.413  -6.255  30.691 1.00 30.39  ? 215 PHE   A CA  1 
ATOM   1547 C  C   . PHE   A  1  202 ? 37.016  -6.713  31.111 1.00 29.54  ? 215 PHE   A C   1 
ATOM   1548 O  O   . PHE   A  1  202 ? 36.890  -7.785  31.679 1.00 31.52  ? 215 PHE   A O   1 
ATOM   1549 C  CB  . PHE   A  1  202 ? 38.990  -5.370  31.792 1.00 29.83  ? 215 PHE   A CB  1 
ATOM   1550 C  CG  . PHE   A  1  202 ? 40.482  -5.113  31.652 1.00 31.62  ? 215 PHE   A CG  1 
ATOM   1551 C  CD1 . PHE   A  1  202 ? 41.271  -5.854  30.782 1.00 33.26  ? 215 PHE   A CD1 1 
ATOM   1552 C  CD2 . PHE   A  1  202 ? 41.096  -4.127  32.412 1.00 34.88  ? 215 PHE   A CD2 1 
ATOM   1553 C  CE1 . PHE   A  1  202 ? 42.629  -5.600  30.669 1.00 35.44  ? 215 PHE   A CE1 1 
ATOM   1554 C  CE2 . PHE   A  1  202 ? 42.456  -3.904  32.319 1.00 37.82  ? 215 PHE   A CE2 1 
ATOM   1555 C  CZ  . PHE   A  1  202 ? 43.222  -4.651  31.460 1.00 36.06  ? 215 PHE   A CZ  1 
ATOM   1556 N  N   . PRO   A  1  203 ? 35.920  -5.948  30.886 1.00 33.56  ? 216 PRO   A N   1 
ATOM   1557 C  CA  . PRO   A  1  203 ? 34.581  -6.419  31.249 1.00 34.07  ? 216 PRO   A CA  1 
ATOM   1558 C  C   . PRO   A  1  203 ? 34.204  -7.745  30.585 1.00 34.66  ? 216 PRO   A C   1 
ATOM   1559 O  O   . PRO   A  1  203 ? 33.491  -8.539  31.181 1.00 34.04  ? 216 PRO   A O   1 
ATOM   1560 C  CB  . PRO   A  1  203 ? 33.672  -5.281  30.795 1.00 34.05  ? 216 PRO   A CB  1 
ATOM   1561 C  CG  . PRO   A  1  203 ? 34.559  -4.076  30.832 1.00 33.30  ? 216 PRO   A CG  1 
ATOM   1562 C  CD  . PRO   A  1  203 ? 35.892  -4.582  30.330 1.00 33.30  ? 216 PRO   A CD  1 
ATOM   1563 N  N   . ILE   A  1  204 ? 34.666  -7.962  29.353 1.00 33.67  ? 217 ILE   A N   1 
ATOM   1564 C  CA  . ILE   A  1  204 ? 34.368  -9.169  28.604 1.00 32.73  ? 217 ILE   A CA  1 
ATOM   1565 C  C   . ILE   A  1  204 ? 35.230  -10.318 29.115 1.00 31.56  ? 217 ILE   A C   1 
ATOM   1566 O  O   . ILE   A  1  204 ? 34.736  -11.412 29.366 1.00 34.53  ? 217 ILE   A O   1 
ATOM   1567 C  CB  . ILE   A  1  204 ? 34.579  -8.938  27.094 1.00 37.02  ? 217 ILE   A CB  1 
ATOM   1568 C  CG1 . ILE   A  1  204 ? 33.712  -7.810  26.579 1.00 38.62  ? 217 ILE   A CG1 1 
ATOM   1569 C  CG2 . ILE   A  1  204 ? 34.357  -10.231 26.303 1.00 40.57  ? 217 ILE   A CG2 1 
ATOM   1570 C  CD1 . ILE   A  1  204 ? 34.126  -7.254  25.228 1.00 41.56  ? 217 ILE   A CD1 1 
ATOM   1571 N  N   . ASN   A  1  205 ? 36.533  -10.076 29.285 1.00 30.65  ? 218 ASN   A N   1 
ATOM   1572 C  CA  . ASN   A  1  205 ? 37.444  -11.155 29.597 1.00 29.46  ? 218 ASN   A CA  1 
ATOM   1573 C  C   . ASN   A  1  205 ? 37.436  -11.502 31.072 1.00 31.04  ? 218 ASN   A C   1 
ATOM   1574 O  O   . ASN   A  1  205 ? 37.729  -12.652 31.403 1.00 31.62  ? 218 ASN   A O   1 
ATOM   1575 C  CB  . ASN   A  1  205 ? 38.873  -10.849 29.181 1.00 34.68  ? 218 ASN   A CB  1 
ATOM   1576 C  CG  . ASN   A  1  205 ? 38.970  -10.568 27.702 1.00 31.55  ? 218 ASN   A CG  1 
ATOM   1577 O  OD1 . ASN   A  1  205 ? 38.191  -11.107 26.923 1.00 37.48  ? 218 ASN   A OD1 1 
ATOM   1578 N  ND2 . ASN   A  1  205 ? 39.844  -9.660  27.308 1.00 35.79  ? 218 ASN   A ND2 1 
ATOM   1579 N  N   . LEU   A  1  206 ? 37.101  -10.540 31.949 1.00 28.54  ? 219 LEU   A N   1 
ATOM   1580 C  CA  . LEU   A  1  206 ? 37.238  -10.770 33.380 1.00 28.39  ? 219 LEU   A CA  1 
ATOM   1581 C  C   . LEU   A  1  206 ? 35.930  -10.673 34.165 1.00 29.30  ? 219 LEU   A C   1 
ATOM   1582 O  O   . LEU   A  1  206 ? 35.830  -11.237 35.256 1.00 27.11  ? 219 LEU   A O   1 
ATOM   1583 C  CB  . LEU   A  1  206 ? 38.271  -9.770  33.885 1.00 29.48  ? 219 LEU   A CB  1 
ATOM   1584 C  CG  . LEU   A  1  206 ? 39.651  -9.895  33.237 1.00 30.13  ? 219 LEU   A CG  1 
ATOM   1585 C  CD1 . LEU   A  1  206 ? 40.516  -8.703  33.598 1.00 30.55  ? 219 LEU   A CD1 1 
ATOM   1586 C  CD2 . LEU   A  1  206 ? 40.320  -11.191 33.643 1.00 30.28  ? 219 LEU   A CD2 1 
ATOM   1587 N  N   . PHE   A  1  207 ? 34.945  -9.914  33.671 1.00 29.22  ? 220 PHE   A N   1 
ATOM   1588 C  CA  . PHE   A  1  207 ? 33.719  -9.724  34.434 1.00 30.81  ? 220 PHE   A CA  1 
ATOM   1589 C  C   . PHE   A  1  207 ? 32.644  -10.713 33.980 1.00 30.20  ? 220 PHE   A C   1 
ATOM   1590 O  O   . PHE   A  1  207 ? 31.635  -10.859 34.643 1.00 31.70  ? 220 PHE   A O   1 
ATOM   1591 C  CB  . PHE   A  1  207 ? 33.150  -8.312  34.309 1.00 28.42  ? 220 PHE   A CB  1 
ATOM   1592 C  CG  . PHE   A  1  207 ? 33.976  -7.182  34.890 1.00 27.40  ? 220 PHE   A CG  1 
ATOM   1593 C  CD1 . PHE   A  1  207 ? 35.022  -7.418  35.758 1.00 28.85  ? 220 PHE   A CD1 1 
ATOM   1594 C  CD2 . PHE   A  1  207 ? 33.650  -5.865  34.588 1.00 28.92  ? 220 PHE   A CD2 1 
ATOM   1595 C  CE1 . PHE   A  1  207 ? 35.735  -6.367  36.301 1.00 31.03  ? 220 PHE   A CE1 1 
ATOM   1596 C  CE2 . PHE   A  1  207 ? 34.373  -4.821  35.120 1.00 27.86  ? 220 PHE   A CE2 1 
ATOM   1597 C  CZ  . PHE   A  1  207 ? 35.423  -5.078  35.966 1.00 30.94  ? 220 PHE   A CZ  1 
ATOM   1598 N  N   . VAL   A  1  208 ? 32.837  -11.367 32.835 1.00 32.29  ? 221 VAL   A N   1 
ATOM   1599 C  CA  . VAL   A  1  208 ? 31.946  -12.436 32.416 1.00 34.01  ? 221 VAL   A CA  1 
ATOM   1600 C  C   . VAL   A  1  208 ? 32.356  -13.709 33.135 1.00 32.33  ? 221 VAL   A C   1 
ATOM   1601 O  O   . VAL   A  1  208 ? 33.537  -14.030 33.196 1.00 37.41  ? 221 VAL   A O   1 
ATOM   1602 C  CB  . VAL   A  1  208 ? 31.945  -12.649 30.896 1.00 33.10  ? 221 VAL   A CB  1 
ATOM   1603 C  CG1 . VAL   A  1  208 ? 31.146  -13.885 30.501 1.00 31.26  ? 221 VAL   A CG1 1 
ATOM   1604 C  CG2 . VAL   A  1  208 ? 31.435  -11.407 30.192 1.00 33.01  ? 221 VAL   A CG2 1 
ATOM   1605 N  N   . ASP   A  1  209 ? 31.354  -14.402 33.692 1.00 34.01  ? 222 ASP   A N   1 
ATOM   1606 C  CA  . ASP   A  1  209 ? 31.560  -15.620 34.453 1.00 32.49  ? 222 ASP   A CA  1 
ATOM   1607 C  C   . ASP   A  1  209 ? 32.402  -16.607 33.651 1.00 30.77  ? 222 ASP   A C   1 
ATOM   1608 O  O   . ASP   A  1  209 ? 32.197  -16.800 32.456 1.00 32.49  ? 222 ASP   A O   1 
ATOM   1609 C  CB  . ASP   A  1  209 ? 30.237  -16.243 34.856 1.00 34.00  ? 222 ASP   A CB  1 
ATOM   1610 C  CG  . ASP   A  1  209 ? 30.350  -17.346 35.897 1.00 36.22  ? 222 ASP   A CG  1 
ATOM   1611 O  OD1 . ASP   A  1  209 ? 30.741  -18.466 35.496 1.00 38.27  ? 222 ASP   A OD1 1 
ATOM   1612 O  OD2 . ASP   A  1  209 ? 30.106  -17.057 37.107 1.00 36.27  ? 222 ASP   A OD2 1 
ATOM   1613 N  N   . GLY   A  1  210 ? 33.345  -17.248 34.329 1.00 32.55  ? 223 GLY   A N   1 
ATOM   1614 C  CA  . GLY   A  1  210 ? 34.306  -18.123 33.675 1.00 34.76  ? 223 GLY   A CA  1 
ATOM   1615 C  C   . GLY   A  1  210 ? 33.682  -19.428 33.179 1.00 35.42  ? 223 GLY   A C   1 
ATOM   1616 O  O   . GLY   A  1  210 ? 34.302  -20.129 32.399 1.00 38.69  ? 223 GLY   A O   1 
ATOM   1617 N  N   . ARG   A  1  211 ? 32.477  -19.771 33.653 1.00 39.69  ? 224 ARG   A N   1 
ATOM   1618 C  CA  . ARG   A  1  211 ? 31.771  -20.950 33.168 1.00 39.31  ? 224 ARG   A CA  1 
ATOM   1619 C  C   . ARG   A  1  211 ? 31.133  -20.680 31.804 1.00 42.18  ? 224 ARG   A C   1 
ATOM   1620 O  O   . ARG   A  1  211 ? 30.705  -21.618 31.149 1.00 43.30  ? 224 ARG   A O   1 
ATOM   1621 C  CB  . ARG   A  1  211 ? 30.722  -21.410 34.180 1.00 39.06  ? 224 ARG   A CB  1 
ATOM   1622 C  CG  . ARG   A  1  211 ? 31.330  -21.966 35.461 1.00 39.11  ? 224 ARG   A CG  1 
ATOM   1623 C  CD  . ARG   A  1  211 ? 30.323  -22.061 36.592 1.00 39.99  ? 224 ARG   A CD  1 
ATOM   1624 N  NE  . ARG   A  1  211 ? 29.798  -20.738 36.977 1.00 44.86  ? 224 ARG   A NE  1 
ATOM   1625 C  CZ  . ARG   A  1  211 ? 28.916  -20.494 37.948 1.00 46.29  ? 224 ARG   A CZ  1 
ATOM   1626 N  NH1 . ARG   A  1  211 ? 28.394  -21.510 38.627 1.00 46.91  ? 224 ARG   A NH1 1 
ATOM   1627 N  NH2 . ARG   A  1  211 ? 28.561  -19.248 38.239 1.00 41.24  ? 224 ARG   A NH2 1 
ATOM   1628 N  N   . VAL   A  1  212 ? 31.092  -19.416 31.351 1.00 40.97  ? 225 VAL   A N   1 
ATOM   1629 C  CA  . VAL   A  1  212 ? 30.646  -19.116 30.001 1.00 40.56  ? 225 VAL   A CA  1 
ATOM   1630 C  C   . VAL   A  1  212 ? 31.825  -19.287 29.039 1.00 46.85  ? 225 VAL   A C   1 
ATOM   1631 O  O   . VAL   A  1  212 ? 32.751  -18.476 29.032 1.00 44.71  ? 225 VAL   A O   1 
ATOM   1632 C  CB  . VAL   A  1  212 ? 30.077  -17.688 29.913 1.00 43.60  ? 225 VAL   A CB  1 
ATOM   1633 C  CG1 . VAL   A  1  212 ? 29.631  -17.324 28.496 1.00 40.24  ? 225 VAL   A CG1 1 
ATOM   1634 C  CG2 . VAL   A  1  212 ? 28.933  -17.470 30.903 1.00 44.47  ? 225 VAL   A CG2 1 
ATOM   1635 N  N   . THR   A  1  213 ? 31.759  -20.309 28.179 1.00 54.68  ? 226 THR   A N   1 
ATOM   1636 C  CA  . THR   A  1  213 ? 32.860  -20.658 27.281 1.00 68.34  ? 226 THR   A CA  1 
ATOM   1637 C  C   . THR   A  1  213 ? 32.667  -20.001 25.912 1.00 72.95  ? 226 THR   A C   1 
ATOM   1638 O  O   . THR   A  1  213 ? 33.641  -19.708 25.228 1.00 72.00  ? 226 THR   A O   1 
ATOM   1639 C  CB  . THR   A  1  213 ? 32.974  -22.180 27.136 1.00 68.48  ? 226 THR   A CB  1 
ATOM   1640 O  OG1 . THR   A  1  213 ? 31.740  -22.685 26.623 1.00 63.84  ? 226 THR   A OG1 1 
ATOM   1641 C  CG2 . THR   A  1  213 ? 33.259  -22.883 28.451 1.00 66.70  ? 226 THR   A CG2 1 
ATOM   1642 N  N   . THR   A  1  214 ? 31.410  -19.766 25.523 1.00 76.50  ? 227 THR   A N   1 
ATOM   1643 C  CA  . THR   A  1  214 ? 31.094  -19.355 24.167 1.00 76.84  ? 227 THR   A CA  1 
ATOM   1644 C  C   . THR   A  1  214 ? 30.243  -18.078 24.196 1.00 64.73  ? 227 THR   A C   1 
ATOM   1645 O  O   . THR   A  1  214 ? 29.405  -17.910 25.070 1.00 65.76  ? 227 THR   A O   1 
ATOM   1646 C  CB  . THR   A  1  214 ? 30.408  -20.556 23.498 1.00 77.62  ? 227 THR   A CB  1 
ATOM   1647 O  OG1 . THR   A  1  214 ? 30.263  -20.198 22.129 1.00 79.81  ? 227 THR   A OG1 1 
ATOM   1648 C  CG2 . THR   A  1  214 ? 29.078  -20.942 24.133 1.00 76.25  ? 227 THR   A CG2 1 
ATOM   1649 N  N   . ASP   A  1  215 ? 30.459  -17.175 23.234 1.00 63.89  ? 228 ASP   A N   1 
ATOM   1650 C  CA  . ASP   A  1  215 ? 29.627  -15.987 23.073 1.00 70.83  ? 228 ASP   A CA  1 
ATOM   1651 C  C   . ASP   A  1  215 ? 29.673  -15.190 24.379 1.00 56.71  ? 228 ASP   A C   1 
ATOM   1652 O  O   . ASP   A  1  215 ? 28.666  -14.973 25.045 1.00 48.32  ? 228 ASP   A O   1 
ATOM   1653 C  CB  . ASP   A  1  215 ? 28.228  -16.352 22.579 1.00 84.95  ? 228 ASP   A CB  1 
ATOM   1654 C  CG  . ASP   A  1  215 ? 27.283  -15.191 22.266 1.00 110.06 ? 228 ASP   A CG  1 
ATOM   1655 O  OD1 . ASP   A  1  215 ? 27.735  -14.202 21.632 1.00 116.96 ? 228 ASP   A OD1 1 
ATOM   1656 O  OD2 . ASP   A  1  215 ? 26.077  -15.290 22.630 1.00 108.89 ? 228 ASP   A OD2 1 
ATOM   1657 N  N   . ARG   A  1  216 ? 30.876  -14.763 24.751 1.00 45.56  ? 229 ARG   A N   1 
ATOM   1658 C  CA  . ARG   A  1  216 ? 31.087  -14.145 26.041 1.00 44.55  ? 229 ARG   A CA  1 
ATOM   1659 C  C   . ARG   A  1  216 ? 30.558  -12.719 25.978 1.00 36.70  ? 229 ARG   A C   1 
ATOM   1660 O  O   . ARG   A  1  216 ? 30.955  -11.957 25.119 1.00 39.43  ? 229 ARG   A O   1 
ATOM   1661 C  CB  . ARG   A  1  216 ? 32.557  -14.282 26.451 1.00 47.50  ? 229 ARG   A CB  1 
ATOM   1662 C  CG  . ARG   A  1  216 ? 32.894  -15.673 26.995 1.00 50.44  ? 229 ARG   A CG  1 
ATOM   1663 C  CD  . ARG   A  1  216 ? 34.400  -15.801 27.276 1.00 49.39  ? 229 ARG   A CD  1 
ATOM   1664 N  NE  . ARG   A  1  216 ? 34.861  -14.905 28.345 1.00 51.20  ? 229 ARG   A NE  1 
ATOM   1665 C  CZ  . ARG   A  1  216 ? 34.607  -15.061 29.642 1.00 49.17  ? 229 ARG   A CZ  1 
ATOM   1666 N  NH1 . ARG   A  1  216 ? 33.917  -16.107 30.068 1.00 48.57  ? 229 ARG   A NH1 1 
ATOM   1667 N  NH2 . ARG   A  1  216 ? 35.074  -14.182 30.523 1.00 53.27  ? 229 ARG   A NH2 1 
ATOM   1668 N  N   . LYS   A  1  217 ? 29.673  -12.377 26.912 1.00 33.28  ? 230 LYS   A N   1 
ATOM   1669 C  CA  . LYS   A  1  217 ? 28.976  -11.104 26.897 1.00 33.63  ? 230 LYS   A CA  1 
ATOM   1670 C  C   . LYS   A  1  217 ? 28.516  -10.796 28.324 1.00 31.50  ? 230 LYS   A C   1 
ATOM   1671 O  O   . LYS   A  1  217 ? 28.185  -11.701 29.070 1.00 29.94  ? 230 LYS   A O   1 
ATOM   1672 C  CB  . LYS   A  1  217 ? 27.822  -11.193 25.893 1.00 35.85  ? 230 LYS   A CB  1 
ATOM   1673 C  CG  . LYS   A  1  217 ? 26.717  -12.144 26.343 1.00 39.70  ? 230 LYS   A CG  1 
ATOM   1674 C  CD  . LYS   A  1  217 ? 25.602  -12.404 25.339 1.00 43.01  ? 230 LYS   A CD  1 
ATOM   1675 C  CE  . LYS   A  1  217 ? 24.506  -13.220 25.970 1.00 47.75  ? 230 LYS   A CE  1 
ATOM   1676 N  NZ  . LYS   A  1  217 ? 23.460  -13.561 25.003 1.00 50.09  ? 230 LYS   A NZ  1 
ATOM   1677 N  N   . LEU   A  1  218 ? 28.496  -9.511  28.695 1.00 33.97  ? 231 LEU   A N   1 
ATOM   1678 C  CA  . LEU   A  1  218 ? 28.193  -9.117  30.060 1.00 32.00  ? 231 LEU   A CA  1 
ATOM   1679 C  C   . LEU   A  1  218 ? 26.783  -8.528  30.143 1.00 29.68  ? 231 LEU   A C   1 
ATOM   1680 O  O   . LEU   A  1  218 ? 26.453  -7.621  29.395 1.00 35.85  ? 231 LEU   A O   1 
ATOM   1681 C  CB  . LEU   A  1  218 ? 29.260  -8.106  30.459 1.00 29.51  ? 231 LEU   A CB  1 
ATOM   1682 C  CG  . LEU   A  1  218 ? 29.190  -7.595  31.891 1.00 31.60  ? 231 LEU   A CG  1 
ATOM   1683 C  CD1 . LEU   A  1  218 ? 29.477  -8.703  32.876 1.00 34.32  ? 231 LEU   A CD1 1 
ATOM   1684 C  CD2 . LEU   A  1  218 ? 30.156  -6.463  32.106 1.00 34.50  ? 231 LEU   A CD2 1 
ATOM   1685 N  N   . SER   A  1  219 ? 25.971  -9.013  31.080 1.00 28.73  ? 232 SER   A N   1 
ATOM   1686 C  CA  . SER   A  1  219 ? 24.649  -8.452  31.330 1.00 31.26  ? 232 SER   A CA  1 
ATOM   1687 C  C   . SER   A  1  219 ? 24.781  -7.083  31.978 1.00 30.99  ? 232 SER   A C   1 
ATOM   1688 O  O   . SER   A  1  219 ? 25.789  -6.777  32.611 1.00 35.12  ? 232 SER   A O   1 
ATOM   1689 C  CB  . SER   A  1  219 ? 23.828  -9.350  32.193 1.00 30.53  ? 232 SER   A CB  1 
ATOM   1690 O  OG  . SER   A  1  219 ? 24.300  -9.284  33.537 1.00 33.97  ? 232 SER   A OG  1 
ATOM   1691 N  N   . MET   A  1  220 ? 23.744  -6.264  31.846 1.00 30.43  ? 233 MET   A N   1 
ATOM   1692 C  CA  . MET   A  1  220 ? 23.783  -4.927  32.420 1.00 31.61  ? 233 MET   A CA  1 
ATOM   1693 C  C   . MET   A  1  220 ? 23.663  -4.993  33.947 1.00 33.12  ? 233 MET   A C   1 
ATOM   1694 O  O   . MET   A  1  220 ? 24.138  -4.102  34.659 1.00 29.61  ? 233 MET   A O   1 
ATOM   1695 C  CB  . MET   A  1  220 ? 22.673  -4.081  31.810 1.00 30.74  ? 233 MET   A CB  1 
ATOM   1696 C  CG  . MET   A  1  220 ? 22.875  -3.795  30.327 1.00 30.26  ? 233 MET   A CG  1 
ATOM   1697 S  SD  . MET   A  1  220 ? 24.436  -2.981  29.924 1.00 33.19  ? 233 MET   A SD  1 
ATOM   1698 C  CE  . MET   A  1  220 ? 25.350  -4.400  29.322 1.00 36.46  ? 233 MET   A CE  1 
ATOM   1699 N  N   . GLU   A  1  221 ? 23.021  -6.055  34.453 1.00 34.10  ? 234 GLU   A N   1 
ATOM   1700 C  CA  . GLU   A  1  221 ? 22.879  -6.275  35.884 1.00 34.73  ? 234 GLU   A CA  1 
ATOM   1701 C  C   . GLU   A  1  221 ? 24.263  -6.531  36.488 1.00 30.87  ? 234 GLU   A C   1 
ATOM   1702 O  O   . GLU   A  1  221 ? 24.606  -5.956  37.506 1.00 29.95  ? 234 GLU   A O   1 
ATOM   1703 C  CB  . GLU   A  1  221 ? 21.937  -7.435  36.223 1.00 40.14  ? 234 GLU   A CB  1 
ATOM   1704 C  CG  . GLU   A  1  221 ? 20.504  -7.253  35.708 1.00 51.63  ? 234 GLU   A CG  1 
ATOM   1705 C  CD  . GLU   A  1  221 ? 20.186  -7.367  34.197 1.00 58.13  ? 234 GLU   A CD  1 
ATOM   1706 O  OE1 . GLU   A  1  221 ? 21.014  -7.817  33.342 1.00 41.80  ? 234 GLU   A OE1 1 
ATOM   1707 O  OE2 . GLU   A  1  221 ? 19.053  -6.926  33.860 1.00 67.20  ? 234 GLU   A OE2 1 
ATOM   1708 N  N   . ASP   A  1  222 ? 25.041  -7.414  35.861 1.00 28.86  ? 235 ASP   A N   1 
ATOM   1709 C  CA  . ASP   A  1  222 ? 26.372  -7.742  36.335 1.00 29.97  ? 235 ASP   A CA  1 
ATOM   1710 C  C   . ASP   A  1  222 ? 27.284  -6.521  36.197 1.00 31.52  ? 235 ASP   A C   1 
ATOM   1711 O  O   . ASP   A  1  222 ? 28.067  -6.213  37.100 1.00 30.17  ? 235 ASP   A O   1 
ATOM   1712 C  CB  . ASP   A  1  222 ? 26.932  -8.961  35.637 1.00 29.68  ? 235 ASP   A CB  1 
ATOM   1713 C  CG  . ASP   A  1  222 ? 26.256  -10.286 35.970 1.00 35.07  ? 235 ASP   A CG  1 
ATOM   1714 O  OD1 . ASP   A  1  222 ? 25.409  -10.304 36.891 1.00 39.81  ? 235 ASP   A OD1 1 
ATOM   1715 O  OD2 . ASP   A  1  222 ? 26.582  -11.302 35.294 1.00 37.81  ? 235 ASP   A OD2 1 
ATOM   1716 N  N   . ALA   A  1  223 ? 27.149  -5.805  35.085 1.00 26.74  ? 236 ALA   A N   1 
ATOM   1717 C  CA  . ALA   A  1  223 ? 27.928  -4.600  34.895 1.00 28.68  ? 236 ALA   A CA  1 
ATOM   1718 C  C   . ALA   A  1  223 ? 27.628  -3.616  36.011 1.00 28.65  ? 236 ALA   A C   1 
ATOM   1719 O  O   . ALA   A  1  223 ? 28.552  -3.074  36.589 1.00 30.76  ? 236 ALA   A O   1 
ATOM   1720 C  CB  . ALA   A  1  223 ? 27.678  -4.005  33.551 1.00 29.86  ? 236 ALA   A CB  1 
ATOM   1721 N  N   . ALA   A  1  224 ? 26.354  -3.410  36.358 1.00 29.70  ? 237 ALA   A N   1 
ATOM   1722 C  CA  . ALA   A  1  224 ? 26.033  -2.415  37.369 1.00 30.62  ? 237 ALA   A CA  1 
ATOM   1723 C  C   . ALA   A  1  224 ? 26.586  -2.874  38.714 1.00 27.86  ? 237 ALA   A C   1 
ATOM   1724 O  O   . ALA   A  1  224 ? 27.115  -2.090  39.504 1.00 27.69  ? 237 ALA   A O   1 
ATOM   1725 C  CB  . ALA   A  1  224 ? 24.547  -2.163  37.436 1.00 31.60  ? 237 ALA   A CB  1 
ATOM   1726 N  N   . SER   A  1  225 ? 26.492  -4.169  38.958 1.00 27.34  ? 238 SER   A N   1 
ATOM   1727 C  CA  . SER   A  1  225 ? 26.903  -4.716  40.239 1.00 30.37  ? 238 SER   A CA  1 
ATOM   1728 C  C   . SER   A  1  225 ? 28.370  -4.375  40.492 1.00 27.52  ? 238 SER   A C   1 
ATOM   1729 O  O   . SER   A  1  225 ? 28.723  -3.931  41.585 1.00 27.51  ? 238 SER   A O   1 
ATOM   1730 C  CB  . SER   A  1  225 ? 26.608  -6.208  40.273 1.00 33.97  ? 238 SER   A CB  1 
ATOM   1731 O  OG  . SER   A  1  225 ? 27.086  -6.798  41.466 1.00 41.28  ? 238 SER   A OG  1 
ATOM   1732 N  N   . ILE   A  1  226 ? 29.213  -4.542  39.459 1.00 27.50  ? 239 ILE   A N   1 
ATOM   1733 C  CA  . ILE   A  1  226 ? 30.643  -4.321  39.592 1.00 29.19  ? 239 ILE   A CA  1 
ATOM   1734 C  C   . ILE   A  1  226 ? 31.001  -2.828  39.475 1.00 27.75  ? 239 ILE   A C   1 
ATOM   1735 O  O   . ILE   A  1  226 ? 31.681  -2.285  40.330 1.00 26.75  ? 239 ILE   A O   1 
ATOM   1736 C  CB  . ILE   A  1  226 ? 31.374  -5.167  38.546 1.00 29.65  ? 239 ILE   A CB  1 
ATOM   1737 C  CG1 . ILE   A  1  226 ? 31.199  -6.643  38.851 1.00 33.81  ? 239 ILE   A CG1 1 
ATOM   1738 C  CG2 . ILE   A  1  226 ? 32.850  -4.799  38.494 1.00 32.07  ? 239 ILE   A CG2 1 
ATOM   1739 C  CD1 . ILE   A  1  226 ? 31.558  -7.566  37.704 1.00 35.46  ? 239 ILE   A CD1 1 
ATOM   1740 N  N   . PHE   A  1  227 ? 30.552  -2.176  38.408 1.00 26.86  ? 240 PHE   A N   1 
ATOM   1741 C  CA  . PHE   A  1  227 ? 30.952  -0.812  38.099 1.00 28.70  ? 240 PHE   A CA  1 
ATOM   1742 C  C   . PHE   A  1  227 ? 30.407  0.174   39.124 1.00 26.43  ? 240 PHE   A C   1 
ATOM   1743 O  O   . PHE   A  1  227 ? 31.111  1.110   39.492 1.00 27.32  ? 240 PHE   A O   1 
ATOM   1744 C  CB  . PHE   A  1  227 ? 30.497  -0.338  36.722 1.00 28.44  ? 240 PHE   A CB  1 
ATOM   1745 C  CG  . PHE   A  1  227 ? 31.298  -0.854  35.541 1.00 31.85  ? 240 PHE   A CG  1 
ATOM   1746 C  CD1 . PHE   A  1  227 ? 32.533  -0.297  35.230 1.00 34.22  ? 240 PHE   A CD1 1 
ATOM   1747 C  CD2 . PHE   A  1  227 ? 30.802  -1.847  34.703 1.00 35.94  ? 240 PHE   A CD2 1 
ATOM   1748 C  CE1 . PHE   A  1  227 ? 33.237  -0.717  34.120 1.00 32.61  ? 240 PHE   A CE1 1 
ATOM   1749 C  CE2 . PHE   A  1  227 ? 31.521  -2.265  33.593 1.00 35.39  ? 240 PHE   A CE2 1 
ATOM   1750 C  CZ  . PHE   A  1  227 ? 32.738  -1.716  33.317 1.00 31.55  ? 240 PHE   A CZ  1 
ATOM   1751 N  N   . ARG   A  1  228 ? 29.184  -0.054  39.585 1.00 27.05  ? 241 ARG   A N   1 
ATOM   1752 C  CA  . ARG   A  1  228 ? 28.525  0.832   40.527 1.00 27.90  ? 241 ARG   A CA  1 
ATOM   1753 C  C   . ARG   A  1  228 ? 28.688  0.323   41.958 1.00 27.77  ? 241 ARG   A C   1 
ATOM   1754 O  O   . ARG   A  1  228 ? 29.088  1.096   42.818 1.00 27.58  ? 241 ARG   A O   1 
ATOM   1755 C  CB  . ARG   A  1  228 ? 27.046  1.043   40.190 1.00 28.58  ? 241 ARG   A CB  1 
ATOM   1756 C  CG  . ARG   A  1  228 ? 26.388  2.050   41.129 1.00 33.27  ? 241 ARG   A CG  1 
ATOM   1757 C  CD  . ARG   A  1  228 ? 24.952  2.494   40.768 1.00 31.43  ? 241 ARG   A CD  1 
ATOM   1758 N  NE  . ARG   A  1  228 ? 24.028  1.362   40.762 1.00 35.41  ? 241 ARG   A NE  1 
ATOM   1759 C  CZ  . ARG   A  1  228 ? 23.279  0.947   39.752 1.00 37.93  ? 241 ARG   A CZ  1 
ATOM   1760 N  NH1 . ARG   A  1  228 ? 23.229  1.618   38.610 1.00 43.54  ? 241 ARG   A NH1 1 
ATOM   1761 N  NH2 . ARG   A  1  228 ? 22.550  -0.148  39.909 1.00 35.96  ? 241 ARG   A NH2 1 
ATOM   1762 N  N   . ASP   A  1  229 ? 28.357  -0.949  42.231 1.00 26.57  ? 242 ASP   A N   1 
ATOM   1763 C  CA  . ASP   A  1  229 ? 28.233  -1.379  43.618 1.00 27.71  ? 242 ASP   A CA  1 
ATOM   1764 C  C   . ASP   A  1  229 ? 29.513  -2.024  44.165 1.00 27.31  ? 242 ASP   A C   1 
ATOM   1765 O  O   . ASP   A  1  229 ? 29.588  -2.290  45.366 1.00 27.55  ? 242 ASP   A O   1 
ATOM   1766 C  CB  . ASP   A  1  229 ? 27.022  -2.275  43.823 1.00 29.54  ? 242 ASP   A CB  1 
ATOM   1767 C  CG  . ASP   A  1  229 ? 25.651  -1.639  43.617 1.00 31.81  ? 242 ASP   A CG  1 
ATOM   1768 O  OD1 . ASP   A  1  229 ? 25.522  -0.406  43.731 1.00 37.00  ? 242 ASP   A OD1 1 
ATOM   1769 O  OD2 . ASP   A  1  229 ? 24.709  -2.389  43.359 1.00 32.29  ? 242 ASP   A OD2 1 
ATOM   1770 N  N   . MET   A  1  230 ? 30.499  -2.294  43.308 1.00 25.26  ? 243 MET   A N   1 
ATOM   1771 C  CA  A MET   A  1  230 ? 31.748  -2.909  43.735 0.50 26.47  ? 243 MET   A CA  1 
ATOM   1772 C  CA  B MET   A  1  230 ? 31.749  -2.907  43.737 0.50 27.27  ? 243 MET   A CA  1 
ATOM   1773 C  C   . MET   A  1  230 ? 31.465  -4.291  44.316 1.00 27.68  ? 243 MET   A C   1 
ATOM   1774 O  O   . MET   A  1  230 ? 32.057  -4.673  45.332 1.00 29.76  ? 243 MET   A O   1 
ATOM   1775 C  CB  A MET   A  1  230 ? 32.449  -2.056  44.802 0.50 26.23  ? 243 MET   A CB  1 
ATOM   1776 C  CB  B MET   A  1  230 ? 32.452  -2.054  44.804 0.50 28.23  ? 243 MET   A CB  1 
ATOM   1777 C  CG  A MET   A  1  230 ? 32.606  -0.610  44.398 0.50 26.94  ? 243 MET   A CG  1 
ATOM   1778 C  CG  B MET   A  1  230 ? 32.602  -0.596  44.416 0.50 30.24  ? 243 MET   A CG  1 
ATOM   1779 S  SD  A MET   A  1  230 ? 33.328  0.352   45.732 0.50 27.98  ? 243 MET   A SD  1 
ATOM   1780 S  SD  B MET   A  1  230 ? 33.271  0.412   45.751 0.50 33.97  ? 243 MET   A SD  1 
ATOM   1781 C  CE  A MET   A  1  230 ? 31.995  0.473   46.927 0.50 26.59  ? 243 MET   A CE  1 
ATOM   1782 C  CE  B MET   A  1  230 ? 32.980  2.079   45.108 0.50 33.56  ? 243 MET   A CE  1 
ATOM   1783 N  N   . ARG   A  1  231 ? 30.537  -5.015  43.671 1.00 27.06  ? 244 ARG   A N   1 
ATOM   1784 C  CA  A ARG   A  1  231 ? 30.019  -6.276  44.171 0.50 27.18  ? 244 ARG   A CA  1 
ATOM   1785 C  CA  B ARG   A  1  231 ? 30.025  -6.277  44.170 0.50 26.00  ? 244 ARG   A CA  1 
ATOM   1786 C  C   . ARG   A  1  231 ? 30.084  -7.301  43.049 1.00 26.88  ? 244 ARG   A C   1 
ATOM   1787 O  O   . ARG   A  1  231 ? 29.637  -7.035  41.942 1.00 23.16  ? 244 ARG   A O   1 
ATOM   1788 C  CB  A ARG   A  1  231 ? 28.573  -6.127  44.653 0.50 30.23  ? 244 ARG   A CB  1 
ATOM   1789 C  CB  B ARG   A  1  231 ? 28.581  -6.109  44.643 0.50 27.02  ? 244 ARG   A CB  1 
ATOM   1790 C  CG  A ARG   A  1  231 ? 28.022  -7.366  45.357 0.50 32.71  ? 244 ARG   A CG  1 
ATOM   1791 C  CG  B ARG   A  1  231 ? 27.971  -7.317  45.344 0.50 27.28  ? 244 ARG   A CG  1 
ATOM   1792 C  CD  A ARG   A  1  231 ? 26.552  -7.304  45.759 0.50 34.99  ? 244 ARG   A CD  1 
ATOM   1793 C  CD  B ARG   A  1  231 ? 26.510  -6.983  45.707 0.50 27.37  ? 244 ARG   A CD  1 
ATOM   1794 N  NE  A ARG   A  1  231 ? 25.666  -7.427  44.593 0.50 44.77  ? 244 ARG   A NE  1 
ATOM   1795 N  NE  B ARG   A  1  231 ? 25.659  -6.642  44.551 0.50 32.41  ? 244 ARG   A NE  1 
ATOM   1796 C  CZ  A ARG   A  1  231 ? 25.372  -8.552  43.941 0.50 43.71  ? 244 ARG   A CZ  1 
ATOM   1797 C  CZ  B ARG   A  1  231 ? 24.953  -5.528  44.336 0.50 28.62  ? 244 ARG   A CZ  1 
ATOM   1798 N  NH1 A ARG   A  1  231 ? 25.629  -9.735  44.487 0.50 45.01  ? 244 ARG   A NH1 1 
ATOM   1799 N  NH1 B ARG   A  1  231 ? 24.898  -4.578  45.251 0.50 29.22  ? 244 ARG   A NH1 1 
ATOM   1800 N  NH2 A ARG   A  1  231 ? 24.795  -8.465  42.757 0.50 38.76  ? 244 ARG   A NH2 1 
ATOM   1801 N  NH2 B ARG   A  1  231 ? 24.297  -5.385  43.210 0.50 26.95  ? 244 ARG   A NH2 1 
ATOM   1802 N  N   . PHE   A  1  232 ? 30.674  -8.464  43.339 1.00 26.42  ? 245 PHE   A N   1 
ATOM   1803 C  CA  . PHE   A  1  232 ? 30.660  -9.569  42.387 1.00 27.20  ? 245 PHE   A CA  1 
ATOM   1804 C  C   . PHE   A  1  232 ? 29.229  -10.024 42.162 1.00 27.38  ? 245 PHE   A C   1 
ATOM   1805 O  O   . PHE   A  1  232 ? 28.460  -10.084 43.105 1.00 30.01  ? 245 PHE   A O   1 
ATOM   1806 C  CB  . PHE   A  1  232 ? 31.357  -10.809 42.926 1.00 24.90  ? 245 PHE   A CB  1 
ATOM   1807 C  CG  . PHE   A  1  232 ? 32.861  -10.730 42.906 1.00 28.85  ? 245 PHE   A CG  1 
ATOM   1808 C  CD1 . PHE   A  1  232 ? 33.534  -10.707 41.697 1.00 26.84  ? 245 PHE   A CD1 1 
ATOM   1809 C  CD2 . PHE   A  1  232 ? 33.593  -10.775 44.084 1.00 34.53  ? 245 PHE   A CD2 1 
ATOM   1810 C  CE1 . PHE   A  1  232 ? 34.917  -10.683 41.675 1.00 31.64  ? 245 PHE   A CE1 1 
ATOM   1811 C  CE2 . PHE   A  1  232 ? 34.982  -10.762 44.044 1.00 31.39  ? 245 PHE   A CE2 1 
ATOM   1812 C  CZ  . PHE   A  1  232 ? 35.628  -10.688 42.851 1.00 31.66  ? 245 PHE   A CZ  1 
ATOM   1813 N  N   . PRO   A  1  233 ? 28.844  -10.423 40.943 1.00 29.79  ? 246 PRO   A N   1 
ATOM   1814 C  CA  . PRO   A  1  233 ? 27.578  -11.138 40.762 1.00 33.11  ? 246 PRO   A CA  1 
ATOM   1815 C  C   . PRO   A  1  233 ? 27.483  -12.301 41.748 1.00 31.69  ? 246 PRO   A C   1 
ATOM   1816 O  O   . PRO   A  1  233 ? 28.488  -12.831 42.223 1.00 26.06  ? 246 PRO   A O   1 
ATOM   1817 C  CB  . PRO   A  1  233 ? 27.628  -11.599 39.294 1.00 32.09  ? 246 PRO   A CB  1 
ATOM   1818 C  CG  . PRO   A  1  233 ? 28.542  -10.572 38.626 1.00 32.29  ? 246 PRO   A CG  1 
ATOM   1819 C  CD  . PRO   A  1  233 ? 29.594  -10.247 39.692 1.00 33.16  ? 246 PRO   A CD  1 
ATOM   1820 N  N   . ASP   A  1  234 ? 26.251  -12.674 42.090 1.00 32.24  ? 247 ASP   A N   1 
ATOM   1821 C  CA  . ASP   A  1  234 ? 26.012  -13.865 42.895 1.00 35.18  ? 247 ASP   A CA  1 
ATOM   1822 C  C   . ASP   A  1  234 ? 26.666  -15.071 42.223 1.00 31.16  ? 247 ASP   A C   1 
ATOM   1823 O  O   . ASP   A  1  234 ? 26.544  -15.249 41.027 1.00 28.62  ? 247 ASP   A O   1 
ATOM   1824 C  CB  . ASP   A  1  234 ? 24.528  -14.105 43.126 1.00 36.76  ? 247 ASP   A CB  1 
ATOM   1825 C  CG  . ASP   A  1  234 ? 23.781  -13.091 43.994 1.00 40.53  ? 247 ASP   A CG  1 
ATOM   1826 O  OD1 . ASP   A  1  234 ? 24.372  -12.076 44.453 1.00 37.29  ? 247 ASP   A OD1 1 
ATOM   1827 O  OD2 . ASP   A  1  234 ? 22.568  -13.313 44.189 1.00 41.03  ? 247 ASP   A OD2 1 
ATOM   1828 N  N   . ASP   A  1  235 ? 27.367  -15.876 43.015 1.00 30.03  ? 248 ASP   A N   1 
ATOM   1829 C  CA  . ASP   A  1  235 ? 27.930  -17.131 42.556 1.00 34.86  ? 248 ASP   A CA  1 
ATOM   1830 C  C   . ASP   A  1  235 ? 28.995  -16.913 41.476 1.00 32.33  ? 248 ASP   A C   1 
ATOM   1831 O  O   . ASP   A  1  235 ? 29.252  -17.811 40.678 1.00 30.04  ? 248 ASP   A O   1 
ATOM   1832 C  CB  . ASP   A  1  235 ? 26.849  -18.099 42.087 1.00 38.44  ? 248 ASP   A CB  1 
ATOM   1833 C  CG  . ASP   A  1  235 ? 27.341  -19.538 41.929 1.00 41.61  ? 248 ASP   A CG  1 
ATOM   1834 O  OD1 . ASP   A  1  235 ? 27.996  -20.046 42.867 1.00 42.10  ? 248 ASP   A OD1 1 
ATOM   1835 O  OD2 . ASP   A  1  235 ? 27.091  -20.138 40.863 1.00 45.30  ? 248 ASP   A OD2 1 
ATOM   1836 N  N   . PHE   A  1  236 ? 29.645  -15.741 41.461 1.00 30.42  ? 249 PHE   A N   1 
ATOM   1837 C  CA  . PHE   A  1  236 ? 30.563  -15.402 40.386 1.00 26.48  ? 249 PHE   A CA  1 
ATOM   1838 C  C   . PHE   A  1  236 ? 31.766  -16.338 40.396 1.00 25.60  ? 249 PHE   A C   1 
ATOM   1839 O  O   . PHE   A  1  236 ? 32.445  -16.509 41.411 1.00 27.50  ? 249 PHE   A O   1 
ATOM   1840 C  CB  . PHE   A  1  236 ? 31.070  -13.961 40.531 1.00 28.65  ? 249 PHE   A CB  1 
ATOM   1841 C  CG  . PHE   A  1  236 ? 31.975  -13.545 39.390 1.00 26.42  ? 249 PHE   A CG  1 
ATOM   1842 C  CD1 . PHE   A  1  236 ? 31.460  -13.329 38.124 1.00 26.53  ? 249 PHE   A CD1 1 
ATOM   1843 C  CD2 . PHE   A  1  236 ? 33.336  -13.397 39.592 1.00 27.30  ? 249 PHE   A CD2 1 
ATOM   1844 C  CE1 . PHE   A  1  236 ? 32.292  -12.952 37.088 1.00 27.17  ? 249 PHE   A CE1 1 
ATOM   1845 C  CE2 . PHE   A  1  236 ? 34.153  -13.015 38.554 1.00 27.66  ? 249 PHE   A CE2 1 
ATOM   1846 C  CZ  . PHE   A  1  236 ? 33.626  -12.790 37.309 1.00 27.98  ? 249 PHE   A CZ  1 
ATOM   1847 N  N   . HIS   A  1  237 ? 32.038  -16.892 39.225 1.00 28.39  ? 250 HIS   A N   1 
ATOM   1848 C  CA  . HIS   A  1  237 ? 33.216  -17.700 38.981 1.00 30.03  ? 250 HIS   A CA  1 
ATOM   1849 C  C   . HIS   A  1  237 ? 34.132  -16.919 38.049 1.00 29.11  ? 250 HIS   A C   1 
ATOM   1850 O  O   . HIS   A  1  237 ? 33.704  -16.497 36.989 1.00 29.21  ? 250 HIS   A O   1 
ATOM   1851 C  CB  . HIS   A  1  237 ? 32.853  -19.051 38.342 1.00 30.31  ? 250 HIS   A CB  1 
ATOM   1852 C  CG  . HIS   A  1  237 ? 32.242  -20.009 39.282 1.00 34.06  ? 250 HIS   A CG  1 
ATOM   1853 N  ND1 . HIS   A  1  237 ? 31.215  -19.640 40.130 1.00 34.96  ? 250 HIS   A ND1 1 
ATOM   1854 C  CD2 . HIS   A  1  237 ? 32.493  -21.319 39.514 1.00 35.56  ? 250 HIS   A CD2 1 
ATOM   1855 C  CE1 . HIS   A  1  237 ? 30.870  -20.703 40.864 1.00 37.53  ? 250 HIS   A CE1 1 
ATOM   1856 N  NE2 . HIS   A  1  237 ? 31.643  -21.728 40.525 1.00 38.23  ? 250 HIS   A NE2 1 
ATOM   1857 N  N   . ARG   A  1  238 ? 35.406  -16.791 38.436 1.00 31.57  ? 251 ARG   A N   1 
ATOM   1858 C  CA  . ARG   A  1  238 ? 36.393  -16.067 37.646 1.00 31.60  ? 251 ARG   A CA  1 
ATOM   1859 C  C   . ARG   A  1  238 ? 36.667  -16.760 36.320 1.00 27.05  ? 251 ARG   A C   1 
ATOM   1860 O  O   . ARG   A  1  238 ? 36.360  -17.930 36.166 1.00 29.63  ? 251 ARG   A O   1 
ATOM   1861 C  CB  . ARG   A  1  238 ? 37.727  -15.940 38.393 1.00 33.08  ? 251 ARG   A CB  1 
ATOM   1862 C  CG  . ARG   A  1  238 ? 38.434  -17.269 38.611 1.00 32.72  ? 251 ARG   A CG  1 
ATOM   1863 C  CD  . ARG   A  1  238 ? 39.697  -17.067 39.426 1.00 31.75  ? 251 ARG   A CD  1 
ATOM   1864 N  NE  . ARG   A  1  238 ? 40.598  -18.181 39.159 1.00 30.96  ? 251 ARG   A NE  1 
ATOM   1865 C  CZ  . ARG   A  1  238 ? 41.717  -18.479 39.817 1.00 34.63  ? 251 ARG   A CZ  1 
ATOM   1866 N  NH1 . ARG   A  1  238 ? 42.244  -17.647 40.703 1.00 33.90  ? 251 ARG   A NH1 1 
ATOM   1867 N  NH2 . ARG   A  1  238 ? 42.340  -19.611 39.532 1.00 36.01  ? 251 ARG   A NH2 1 
ATOM   1868 N  N   . SER   A  1  239 ? 37.273  -16.008 35.393 1.00 28.88  ? 252 SER   A N   1 
ATOM   1869 C  CA  . SER   A  1  239 ? 37.772  -16.522 34.123 1.00 31.33  ? 252 SER   A CA  1 
ATOM   1870 C  C   . SER   A  1  239 ? 38.453  -17.883 34.307 1.00 34.42  ? 252 SER   A C   1 
ATOM   1871 O  O   . SER   A  1  239 ? 39.153  -18.097 35.300 1.00 33.62  ? 252 SER   A O   1 
ATOM   1872 C  CB  . SER   A  1  239 ? 38.769  -15.543 33.526 1.00 29.34  ? 252 SER   A CB  1 
ATOM   1873 O  OG  . SER   A  1  239 ? 39.285  -16.026 32.291 1.00 32.49  ? 252 SER   A OG  1 
ATOM   1874 N  N   . ALA   A  1  240 ? 38.309  -18.755 33.310 1.00 37.12  ? 253 ALA   A N   1 
ATOM   1875 C  CA  . ALA   A  1  240 ? 38.818  -20.124 33.388 1.00 39.56  ? 253 ALA   A CA  1 
ATOM   1876 C  C   . ALA   A  1  240 ? 40.303  -20.182 33.020 1.00 35.85  ? 253 ALA   A C   1 
ATOM   1877 O  O   . ALA   A  1  240 ? 40.935  -21.204 33.243 1.00 35.66  ? 253 ALA   A O   1 
ATOM   1878 C  CB  . ALA   A  1  240 ? 38.000  -21.041 32.484 1.00 37.10  ? 253 ALA   A CB  1 
ATOM   1879 N  N   . VAL   A  1  241 ? 40.839  -19.088 32.455 1.00 36.91  ? 254 VAL   A N   1 
ATOM   1880 C  CA  . VAL   A  1  241 ? 42.242  -18.961 32.072 1.00 38.43  ? 254 VAL   A CA  1 
ATOM   1881 C  C   . VAL   A  1  241 ? 42.731  -17.578 32.479 1.00 37.18  ? 254 VAL   A C   1 
ATOM   1882 O  O   . VAL   A  1  241 ? 41.954  -16.625 32.532 1.00 37.50  ? 254 VAL   A O   1 
ATOM   1883 C  CB  . VAL   A  1  241 ? 42.476  -19.148 30.560 1.00 45.27  ? 254 VAL   A CB  1 
ATOM   1884 C  CG1 . VAL   A  1  241 ? 42.192  -20.578 30.109 1.00 49.89  ? 254 VAL   A CG1 1 
ATOM   1885 C  CG2 . VAL   A  1  241 ? 41.660  -18.159 29.734 1.00 44.27  ? 254 VAL   A CG2 1 
ATOM   1886 N  N   . PRO   A  1  242 ? 44.031  -17.400 32.777 1.00 34.81  ? 255 PRO   A N   1 
ATOM   1887 C  CA  . PRO   A  1  242 ? 44.553  -16.065 33.024 1.00 33.13  ? 255 PRO   A CA  1 
ATOM   1888 C  C   . PRO   A  1  242 ? 44.224  -15.212 31.816 1.00 31.83  ? 255 PRO   A C   1 
ATOM   1889 O  O   . PRO   A  1  242 ? 44.308  -15.688 30.684 1.00 32.01  ? 255 PRO   A O   1 
ATOM   1890 C  CB  . PRO   A  1  242 ? 46.051  -16.316 33.239 1.00 33.47  ? 255 PRO   A CB  1 
ATOM   1891 C  CG  . PRO   A  1  242 ? 46.072  -17.710 33.824 1.00 35.51  ? 255 PRO   A CG  1 
ATOM   1892 C  CD  . PRO   A  1  242 ? 45.038  -18.446 32.976 1.00 35.60  ? 255 PRO   A CD  1 
ATOM   1893 N  N   . ALA   A  1  243 ? 43.805  -13.968 32.061 1.00 29.69  ? 256 ALA   A N   1 
ATOM   1894 C  CA  . ALA   A  1  243 ? 43.439  -13.123 30.946 1.00 26.98  ? 256 ALA   A CA  1 
ATOM   1895 C  C   . ALA   A  1  243 ? 43.683  -11.665 31.277 1.00 27.72  ? 256 ALA   A C   1 
ATOM   1896 O  O   . ALA   A  1  243 ? 43.899  -11.300 32.425 1.00 31.80  ? 256 ALA   A O   1 
ATOM   1897 C  CB  . ALA   A  1  243 ? 41.999  -13.358 30.582 1.00 27.90  ? 256 ALA   A CB  1 
ATOM   1898 N  N   . SER   A  1  244 ? 43.631  -10.840 30.230 1.00 27.96  ? 257 SER   A N   1 
ATOM   1899 C  CA  . SER   A  1  244 ? 43.775  -9.408  30.388 1.00 29.95  ? 257 SER   A CA  1 
ATOM   1900 C  C   . SER   A  1  244 ? 43.117  -8.720  29.202 1.00 30.26  ? 257 SER   A C   1 
ATOM   1901 O  O   . SER   A  1  244 ? 41.895  -8.579  29.192 1.00 28.83  ? 257 SER   A O   1 
ATOM   1902 C  CB  . SER   A  1  244 ? 45.227  -9.023  30.581 1.00 30.19  ? 257 SER   A CB  1 
ATOM   1903 O  OG  . SER   A  1  244 ? 46.030  -9.573  29.539 1.00 30.80  ? 257 SER   A OG  1 
ATOM   1904 N  N   . ASN   A  1  245 ? 43.906  -8.391  28.171 1.00 31.95  ? 258 ASN   A N   1 
ATOM   1905 C  CA  . ASN   A  1  245 ? 43.489  -7.439  27.158 1.00 33.66  ? 258 ASN   A CA  1 
ATOM   1906 C  C   . ASN   A  1  245 ? 43.217  -8.106  25.813 1.00 33.59  ? 258 ASN   A C   1 
ATOM   1907 O  O   . ASN   A  1  245 ? 43.272  -7.425  24.795 1.00 34.97  ? 258 ASN   A O   1 
ATOM   1908 C  CB  . ASN   A  1  245 ? 44.515  -6.318  27.028 1.00 36.10  ? 258 ASN   A CB  1 
ATOM   1909 C  CG  . ASN   A  1  245 ? 45.807  -6.777  26.395 1.00 40.48  ? 258 ASN   A CG  1 
ATOM   1910 O  OD1 . ASN   A  1  245 ? 46.125  -7.971  26.357 1.00 38.27  ? 258 ASN   A OD1 1 
ATOM   1911 N  ND2 . ASN   A  1  245 ? 46.565  -5.833  25.866 1.00 54.37  ? 258 ASN   A ND2 1 
ATOM   1912 N  N   . GLU   A  1  246 ? 42.890  -9.408  25.813 1.00 35.08  ? 259 GLU   A N   1 
ATOM   1913 C  CA  . GLU   A  1  246 ? 42.583  -10.114 24.575 1.00 35.41  ? 259 GLU   A CA  1 
ATOM   1914 C  C   . GLU   A  1  246 ? 41.446  -9.379  23.874 1.00 33.31  ? 259 GLU   A C   1 
ATOM   1915 O  O   . GLU   A  1  246 ? 40.410  -9.132  24.487 1.00 31.35  ? 259 GLU   A O   1 
ATOM   1916 C  CB  . GLU   A  1  246 ? 42.198  -11.584 24.799 1.00 35.61  ? 259 GLU   A CB  1 
ATOM   1917 C  CG  . GLU   A  1  246 ? 43.348  -12.427 25.353 1.00 40.22  ? 259 GLU   A CG  1 
ATOM   1918 C  CD  . GLU   A  1  246 ? 43.691  -12.261 26.840 1.00 44.11  ? 259 GLU   A CD  1 
ATOM   1919 O  OE1 . GLU   A  1  246 ? 43.065  -11.417 27.535 1.00 37.72  ? 259 GLU   A OE1 1 
ATOM   1920 O  OE2 . GLU   A  1  246 ? 44.587  -13.008 27.320 1.00 41.84  ? 259 GLU   A OE2 1 
ATOM   1921 N  N   . GLY   A  1  247 ? 41.676  -9.012  22.603 1.00 31.70  ? 260 GLY   A N   1 
ATOM   1922 C  CA  . GLY   A  1  247 ? 40.655  -8.404  21.771 1.00 31.89  ? 260 GLY   A CA  1 
ATOM   1923 C  C   . GLY   A  1  247 ? 40.809  -6.891  21.671 1.00 34.27  ? 260 GLY   A C   1 
ATOM   1924 O  O   . GLY   A  1  247 ? 40.106  -6.264  20.886 1.00 36.37  ? 260 GLY   A O   1 
ATOM   1925 N  N   . ALA   A  1  248 ? 41.725  -6.297  22.444 1.00 32.57  ? 261 ALA   A N   1 
ATOM   1926 C  CA  . ALA   A  1  248 ? 41.882  -4.843  22.441 1.00 37.11  ? 261 ALA   A CA  1 
ATOM   1927 C  C   . ALA   A  1  248 ? 42.267  -4.319  21.051 1.00 37.89  ? 261 ALA   A C   1 
ATOM   1928 O  O   . ALA   A  1  248 ? 41.880  -3.215  20.662 1.00 37.08  ? 261 ALA   A O   1 
ATOM   1929 C  CB  . ALA   A  1  248 ? 42.909  -4.432  23.476 1.00 35.26  ? 261 ALA   A CB  1 
ATOM   1930 N  N   . ASP   A  1  249 ? 43.060  -5.113  20.330 1.00 39.51  ? 262 ASP   A N   1 
ATOM   1931 C  CA  . ASP   A  1  249 ? 43.433  -4.856  18.941 1.00 46.08  ? 262 ASP   A CA  1 
ATOM   1932 C  C   . ASP   A  1  249 ? 42.190  -4.698  18.050 1.00 44.00  ? 262 ASP   A C   1 
ATOM   1933 O  O   . ASP   A  1  249 ? 42.132  -3.795  17.222 1.00 41.99  ? 262 ASP   A O   1 
ATOM   1934 C  CB  . ASP   A  1  249 ? 44.387  -5.932  18.423 1.00 49.80  ? 262 ASP   A CB  1 
ATOM   1935 C  CG  . ASP   A  1  249 ? 43.963  -7.395  18.604 1.00 67.75  ? 262 ASP   A CG  1 
ATOM   1936 O  OD1 . ASP   A  1  249 ? 42.936  -7.681  19.291 1.00 57.61  ? 262 ASP   A OD1 1 
ATOM   1937 O  OD2 . ASP   A  1  249 ? 44.683  -8.274  18.072 1.00 77.60  ? 262 ASP   A OD2 1 
ATOM   1938 N  N   . GLN   A  1  250 ? 41.192  -5.580  18.203 1.00 37.99  ? 263 GLN   A N   1 
ATOM   1939 C  CA  . GLN   A  1  250 ? 39.987  -5.514  17.395 1.00 40.15  ? 263 GLN   A CA  1 
ATOM   1940 C  C   . GLN   A  1  250 ? 39.180  -4.261  17.735 1.00 39.49  ? 263 GLN   A C   1 
ATOM   1941 O  O   . GLN   A  1  250 ? 38.470  -3.730  16.883 1.00 44.45  ? 263 GLN   A O   1 
ATOM   1942 C  CB  . GLN   A  1  250 ? 39.118  -6.749  17.597 1.00 39.95  ? 263 GLN   A CB  1 
ATOM   1943 C  CG  . GLN   A  1  250 ? 39.755  -8.040  17.106 1.00 43.39  ? 263 GLN   A CG  1 
ATOM   1944 C  CD  . GLN   A  1  250 ? 38.853  -9.227  17.372 1.00 50.99  ? 263 GLN   A CD  1 
ATOM   1945 O  OE1 . GLN   A  1  250 ? 37.694  -9.263  16.942 1.00 50.36  ? 263 GLN   A OE1 1 
ATOM   1946 N  NE2 . GLN   A  1  250 ? 39.358  -10.193 18.127 1.00 50.92  ? 263 GLN   A NE2 1 
ATOM   1947 N  N   . VAL   A  1  251 ? 39.287  -3.795  18.986 1.00 35.14  ? 264 VAL   A N   1 
ATOM   1948 C  CA  . VAL   A  1  251 ? 38.557  -2.613  19.398 1.00 35.36  ? 264 VAL   A CA  1 
ATOM   1949 C  C   . VAL   A  1  251 ? 39.126  -1.404  18.662 1.00 35.25  ? 264 VAL   A C   1 
ATOM   1950 O  O   . VAL   A  1  251 ? 38.368  -0.588  18.141 1.00 37.51  ? 264 VAL   A O   1 
ATOM   1951 C  CB  . VAL   A  1  251 ? 38.558  -2.432  20.924 1.00 34.60  ? 264 VAL   A CB  1 
ATOM   1952 C  CG1 . VAL   A  1  251 ? 38.107  -1.045  21.353 1.00 37.59  ? 264 VAL   A CG1 1 
ATOM   1953 C  CG2 . VAL   A  1  251 ? 37.704  -3.483  21.594 1.00 34.57  ? 264 VAL   A CG2 1 
ATOM   1954 N  N   . LEU   A  1  252 ? 40.454  -1.313  18.608 1.00 36.12  ? 265 LEU   A N   1 
ATOM   1955 C  CA  . LEU   A  1  252 ? 41.127  -0.257  17.864 1.00 40.82  ? 265 LEU   A CA  1 
ATOM   1956 C  C   . LEU   A  1  252 ? 40.811  -0.348  16.370 1.00 40.06  ? 265 LEU   A C   1 
ATOM   1957 O  O   . LEU   A  1  252 ? 40.523  0.667   15.748 1.00 43.13  ? 265 LEU   A O   1 
ATOM   1958 C  CB  . LEU   A  1  252 ? 42.634  -0.299  18.088 1.00 43.74  ? 265 LEU   A CB  1 
ATOM   1959 C  CG  . LEU   A  1  252 ? 43.436  0.776   17.344 1.00 47.56  ? 265 LEU   A CG  1 
ATOM   1960 C  CD1 . LEU   A  1  252 ? 43.048  2.190   17.831 1.00 46.42  ? 265 LEU   A CD1 1 
ATOM   1961 C  CD2 . LEU   A  1  252 ? 44.943  0.491   17.483 1.00 44.75  ? 265 LEU   A CD2 1 
ATOM   1962 N  N   . ALA   A  1  253 ? 40.840  -1.553  15.805 1.00 35.13  ? 266 ALA   A N   1 
ATOM   1963 C  CA  . ALA   A  1  253 ? 40.665  -1.718  14.368 1.00 39.64  ? 266 ALA   A CA  1 
ATOM   1964 C  C   . ALA   A  1  253 ? 39.248  -1.342  13.929 1.00 46.89  ? 266 ALA   A C   1 
ATOM   1965 O  O   . ALA   A  1  253 ? 39.066  -0.875  12.812 1.00 47.73  ? 266 ALA   A O   1 
ATOM   1966 C  CB  . ALA   A  1  253 ? 41.019  -3.136  13.949 1.00 37.90  ? 266 ALA   A CB  1 
ATOM   1967 N  N   . ALA   A  1  254 ? 38.248  -1.504  14.804 1.00 45.20  ? 267 ALA   A N   1 
ATOM   1968 C  CA  . ALA   A  1  254 ? 36.888  -1.107  14.484 1.00 45.67  ? 267 ALA   A CA  1 
ATOM   1969 C  C   . ALA   A  1  254 ? 36.787  0.391   14.185 1.00 47.81  ? 267 ALA   A C   1 
ATOM   1970 O  O   . ALA   A  1  254 ? 35.940  0.795   13.383 1.00 47.36  ? 267 ALA   A O   1 
ATOM   1971 C  CB  . ALA   A  1  254 ? 35.956  -1.483  15.615 1.00 46.18  ? 267 ALA   A CB  1 
ATOM   1972 N  N   . HIS   A  1  255 ? 37.589  1.212   14.880 1.00 44.05  ? 268 HIS   A N   1 
ATOM   1973 C  CA  . HIS   A  1  255 ? 37.642  2.650   14.639 1.00 45.36  ? 268 HIS   A CA  1 
ATOM   1974 C  C   . HIS   A  1  255 ? 39.074  3.156   14.828 1.00 45.47  ? 268 HIS   A C   1 
ATOM   1975 O  O   . HIS   A  1  255 ? 39.433  3.666   15.884 1.00 45.94  ? 268 HIS   A O   1 
ATOM   1976 C  CB  . HIS   A  1  255 ? 36.646  3.421   15.517 1.00 47.79  ? 268 HIS   A CB  1 
ATOM   1977 C  CG  . HIS   A  1  255 ? 35.225  3.306   15.083 1.00 56.11  ? 268 HIS   A CG  1 
ATOM   1978 N  ND1 . HIS   A  1  255 ? 34.719  4.013   14.014 1.00 56.69  ? 268 HIS   A ND1 1 
ATOM   1979 C  CD2 . HIS   A  1  255 ? 34.209  2.560   15.562 1.00 62.87  ? 268 HIS   A CD2 1 
ATOM   1980 C  CE1 . HIS   A  1  255 ? 33.441  3.702   13.867 1.00 64.90  ? 268 HIS   A CE1 1 
ATOM   1981 N  NE2 . HIS   A  1  255 ? 33.112  2.828   14.803 1.00 61.00  ? 268 HIS   A NE2 1 
ATOM   1982 N  N   . PRO   A  1  256 ? 39.948  3.020   13.805 1.00 44.94  ? 269 PRO   A N   1 
ATOM   1983 C  CA  . PRO   A  1  256 ? 41.341  3.433   13.940 1.00 42.79  ? 269 PRO   A CA  1 
ATOM   1984 C  C   . PRO   A  1  256 ? 41.455  4.855   14.472 1.00 42.30  ? 269 PRO   A C   1 
ATOM   1985 O  O   . PRO   A  1  256 ? 40.700  5.760   14.083 1.00 39.89  ? 269 PRO   A O   1 
ATOM   1986 C  CB  . PRO   A  1  256 ? 41.894  3.285   12.519 1.00 51.88  ? 269 PRO   A CB  1 
ATOM   1987 C  CG  . PRO   A  1  256 ? 41.045  2.176   11.924 1.00 53.69  ? 269 PRO   A CG  1 
ATOM   1988 C  CD  . PRO   A  1  256 ? 39.646  2.416   12.494 1.00 48.72  ? 269 PRO   A CD  1 
ATOM   1989 N  N   . TRP   A  1  257 ? 42.396  5.011   15.404 1.00 37.04  ? 270 TRP   A N   1 
ATOM   1990 C  CA  . TRP   A  1  257 ? 42.579  6.261   16.107 1.00 37.20  ? 270 TRP   A CA  1 
ATOM   1991 C  C   . TRP   A  1  257 ? 44.053  6.448   16.466 1.00 38.89  ? 270 TRP   A C   1 
ATOM   1992 O  O   . TRP   A  1  257 ? 44.795  5.484   16.658 1.00 40.79  ? 270 TRP   A O   1 
ATOM   1993 C  CB  . TRP   A  1  257 ? 41.685  6.292   17.353 1.00 37.95  ? 270 TRP   A CB  1 
ATOM   1994 C  CG  . TRP   A  1  257 ? 41.559  7.684   17.903 1.00 36.89  ? 270 TRP   A CG  1 
ATOM   1995 C  CD1 . TRP   A  1  257 ? 42.190  8.196   18.989 1.00 38.01  ? 270 TRP   A CD1 1 
ATOM   1996 C  CD2 . TRP   A  1  257 ? 40.823  8.772   17.309 1.00 36.78  ? 270 TRP   A CD2 1 
ATOM   1997 N  NE1 . TRP   A  1  257 ? 41.871  9.520   19.136 1.00 40.57  ? 270 TRP   A NE1 1 
ATOM   1998 C  CE2 . TRP   A  1  257 ? 41.050  9.905   18.114 1.00 38.20  ? 270 TRP   A CE2 1 
ATOM   1999 C  CE3 . TRP   A  1  257 ? 39.997  8.893   16.187 1.00 39.44  ? 270 TRP   A CE3 1 
ATOM   2000 C  CZ2 . TRP   A  1  257 ? 40.486  11.147  17.839 1.00 40.25  ? 270 TRP   A CZ2 1 
ATOM   2001 C  CZ3 . TRP   A  1  257 ? 39.438  10.125  15.914 1.00 42.79  ? 270 TRP   A CZ3 1 
ATOM   2002 C  CH2 . TRP   A  1  257 ? 39.687  11.234  16.722 1.00 43.64  ? 270 TRP   A CH2 1 
ATOM   2003 N  N   . VAL   A  1  258 ? 44.444  7.708   16.601 1.00 41.47  ? 271 VAL   A N   1 
ATOM   2004 C  CA  . VAL   A  1  258 ? 45.833  8.080   16.779 1.00 45.92  ? 271 VAL   A CA  1 
ATOM   2005 C  C   . VAL   A  1  258 ? 45.973  8.887   18.068 1.00 40.84  ? 271 VAL   A C   1 
ATOM   2006 O  O   . VAL   A  1  258 ? 45.136  9.728   18.378 1.00 40.31  ? 271 VAL   A O   1 
ATOM   2007 C  CB  . VAL   A  1  258 ? 46.260  8.853   15.512 1.00 54.16  ? 271 VAL   A CB  1 
ATOM   2008 C  CG1 . VAL   A  1  258 ? 47.537  9.650   15.699 1.00 65.98  ? 271 VAL   A CG1 1 
ATOM   2009 C  CG2 . VAL   A  1  258 ? 46.444  7.898   14.337 1.00 55.23  ? 271 VAL   A CG2 1 
ATOM   2010 N  N   . PRO   A  1  259 ? 47.028  8.642   18.869 1.00 38.24  ? 272 PRO   A N   1 
ATOM   2011 C  CA  . PRO   A  1  259 ? 47.216  9.376   20.110 1.00 40.60  ? 272 PRO   A CA  1 
ATOM   2012 C  C   . PRO   A  1  259 ? 47.266  10.867  19.817 1.00 39.35  ? 272 PRO   A C   1 
ATOM   2013 O  O   . PRO   A  1  259 ? 47.676  11.267  18.741 1.00 45.85  ? 272 PRO   A O   1 
ATOM   2014 C  CB  . PRO   A  1  259 ? 48.529  8.838   20.691 1.00 40.87  ? 272 PRO   A CB  1 
ATOM   2015 C  CG  . PRO   A  1  259 ? 49.204  8.148   19.534 1.00 40.10  ? 272 PRO   A CG  1 
ATOM   2016 C  CD  . PRO   A  1  259 ? 48.078  7.636   18.648 1.00 40.67  ? 272 PRO   A CD  1 
ATOM   2017 N  N   . GLY   A  1  260 ? 46.852  11.672  20.791 1.00 38.45  ? 273 GLY   A N   1 
ATOM   2018 C  CA  . GLY   A  1  260 ? 46.804  13.109  20.629 1.00 38.43  ? 273 GLY   A CA  1 
ATOM   2019 C  C   . GLY   A  1  260 ? 45.963  13.748  21.726 1.00 40.88  ? 273 GLY   A C   1 
ATOM   2020 O  O   . GLY   A  1  260 ? 45.835  13.182  22.809 1.00 43.17  ? 273 GLY   A O   1 
ATOM   2021 N  N   . GLY   A  1  261 ? 45.396  14.918  21.410 1.00 42.14  ? 274 GLY   A N   1 
ATOM   2022 C  CA  . GLY   A  1  261 ? 44.636  15.710  22.355 1.00 44.03  ? 274 GLY   A CA  1 
ATOM   2023 C  C   . GLY   A  1  261 ? 44.079  16.988  21.731 1.00 45.18  ? 274 GLY   A C   1 
ATOM   2024 O  O   . GLY   A  1  261 ? 44.480  17.393  20.649 1.00 52.67  ? 274 GLY   A O   1 
ATOM   2025 N  N   . ASN   A  1  262 ? 43.125  17.608  22.427 1.00 43.34  ? 275 ASN   A N   1 
ATOM   2026 C  CA  . ASN   A  1  262 ? 42.647  18.936  22.087 1.00 46.03  ? 275 ASN   A CA  1 
ATOM   2027 C  C   . ASN   A  1  262 ? 43.761  19.939  22.376 1.00 49.78  ? 275 ASN   A C   1 
ATOM   2028 O  O   . ASN   A  1  262 ? 44.232  20.006  23.510 1.00 53.38  ? 275 ASN   A O   1 
ATOM   2029 C  CB  . ASN   A  1  262 ? 41.396  19.303  22.882 1.00 45.51  ? 275 ASN   A CB  1 
ATOM   2030 C  CG  . ASN   A  1  262 ? 40.117  18.844  22.223 1.00 45.22  ? 275 ASN   A CG  1 
ATOM   2031 O  OD1 . ASN   A  1  262 ? 40.093  18.624  21.007 1.00 44.04  ? 275 ASN   A OD1 1 
ATOM   2032 N  ND2 . ASN   A  1  262 ? 39.047  18.701  22.999 1.00 41.29  ? 275 ASN   A ND2 1 
ATOM   2033 N  N   . ALA   A  1  263 ? 44.144  20.728  21.359 1.00 53.39  ? 276 ALA   A N   1 
ATOM   2034 C  CA  . ALA   A  1  263 ? 45.178  21.742  21.530 1.00 56.89  ? 276 ALA   A CA  1 
ATOM   2035 C  C   . ALA   A  1  263 ? 44.570  23.094  21.895 1.00 54.89  ? 276 ALA   A C   1 
ATOM   2036 O  O   . ALA   A  1  263 ? 43.436  23.392  21.516 1.00 51.32  ? 276 ALA   A O   1 
ATOM   2037 C  CB  . ALA   A  1  263 ? 46.014  21.844  20.276 1.00 60.10  ? 276 ALA   A CB  1 
ATOM   2038 N  N   . ASP   A  1  264 ? 45.347  23.878  22.662 1.00 63.61  ? 277 ASP   A N   1 
ATOM   2039 C  CA  . ASP   A  1  264 ? 45.121  25.302  22.905 1.00 73.00  ? 277 ASP   A CA  1 
ATOM   2040 C  C   . ASP   A  1  264 ? 43.813  25.541  23.651 1.00 69.12  ? 277 ASP   A C   1 
ATOM   2041 O  O   . ASP   A  1  264 ? 43.130  26.533  23.392 1.00 59.74  ? 277 ASP   A O   1 
ATOM   2042 C  CB  . ASP   A  1  264 ? 45.159  26.131  21.626 1.00 83.59  ? 277 ASP   A CB  1 
ATOM   2043 C  CG  . ASP   A  1  264 ? 46.475  26.087  20.859 1.00 101.29 ? 277 ASP   A CG  1 
ATOM   2044 O  OD1 . ASP   A  1  264 ? 47.533  26.337  21.490 1.00 99.04  ? 277 ASP   A OD1 1 
ATOM   2045 O  OD2 . ASP   A  1  264 ? 46.435  25.819  19.634 1.00 108.43 ? 277 ASP   A OD2 1 
ATOM   2046 N  N   . ASN   A  1  265 ? 43.477  24.614  24.560 1.00 68.70  ? 278 ASN   A N   1 
ATOM   2047 C  CA  . ASN   A  1  265 ? 42.370  24.782  25.480 1.00 63.37  ? 278 ASN   A CA  1 
ATOM   2048 C  C   . ASN   A  1  265 ? 41.078  25.057  24.709 1.00 55.70  ? 278 ASN   A C   1 
ATOM   2049 O  O   . ASN   A  1  265 ? 40.286  25.914  25.108 1.00 53.47  ? 278 ASN   A O   1 
ATOM   2050 C  CB  . ASN   A  1  265 ? 42.700  25.852  26.520 1.00 69.17  ? 278 ASN   A CB  1 
ATOM   2051 C  CG  . ASN   A  1  265 ? 41.766  25.779  27.705 1.00 80.38  ? 278 ASN   A CG  1 
ATOM   2052 O  OD1 . ASN   A  1  265 ? 41.652  24.719  28.333 1.00 93.91  ? 278 ASN   A OD1 1 
ATOM   2053 N  ND2 . ASN   A  1  265 ? 41.077  26.868  28.017 1.00 84.67  ? 278 ASN   A ND2 1 
ATOM   2054 N  N   . GLN   A  1  266 ? 40.855  24.314  23.615 1.00 49.89  ? 279 GLN   A N   1 
ATOM   2055 C  CA  . GLN   A  1  266 ? 39.633  24.435  22.830 1.00 56.82  ? 279 GLN   A CA  1 
ATOM   2056 C  C   . GLN   A  1  266 ? 39.059  23.055  22.517 1.00 51.87  ? 279 GLN   A C   1 
ATOM   2057 O  O   . GLN   A  1  266 ? 39.793  22.109  22.258 1.00 46.16  ? 279 GLN   A O   1 
ATOM   2058 C  CB  . GLN   A  1  266 ? 39.859  25.179  21.510 1.00 66.46  ? 279 GLN   A CB  1 
ATOM   2059 C  CG  . GLN   A  1  266 ? 40.007  26.688  21.709 1.00 76.45  ? 279 GLN   A CG  1 
ATOM   2060 C  CD  . GLN   A  1  266 ? 40.385  27.447  20.459 1.00 84.83  ? 279 GLN   A CD  1 
ATOM   2061 O  OE1 . GLN   A  1  266 ? 40.898  26.889  19.483 1.00 73.70  ? 279 GLN   A OE1 1 
ATOM   2062 N  NE2 . GLN   A  1  266 ? 40.127  28.746  20.486 1.00 89.89  ? 279 GLN   A NE2 1 
ATOM   2063 N  N   . VAL   A  1  267 ? 37.731  22.963  22.473 1.00 44.68  ? 280 VAL   A N   1 
ATOM   2064 C  CA  . VAL   A  1  267 ? 37.081  21.733  22.057 1.00 49.03  ? 280 VAL   A CA  1 
ATOM   2065 C  C   . VAL   A  1  267 ? 37.134  21.622  20.534 1.00 52.64  ? 280 VAL   A C   1 
ATOM   2066 O  O   . VAL   A  1  267 ? 37.506  22.561  19.851 1.00 59.77  ? 280 VAL   A O   1 
ATOM   2067 C  CB  . VAL   A  1  267 ? 35.645  21.634  22.607 1.00 53.76  ? 280 VAL   A CB  1 
ATOM   2068 C  CG1 . VAL   A  1  267 ? 35.645  21.697  24.130 1.00 50.98  ? 280 VAL   A CG1 1 
ATOM   2069 C  CG2 . VAL   A  1  267 ? 34.711  22.696  22.038 1.00 53.10  ? 280 VAL   A CG2 1 
ATOM   2070 N  N   . ASN   A  1  268 ? 36.821  20.427  20.030 1.00 55.85  ? 281 ASN   A N   1 
ATOM   2071 C  CA  . ASN   A  1  268 ? 36.782  20.116  18.609 1.00 57.96  ? 281 ASN   A CA  1 
ATOM   2072 C  C   . ASN   A  1  268 ? 38.076  20.523  17.911 1.00 56.20  ? 281 ASN   A C   1 
ATOM   2073 O  O   . ASN   A  1  268 ? 38.042  20.976  16.772 1.00 57.74  ? 281 ASN   A O   1 
ATOM   2074 C  CB  . ASN   A  1  268 ? 35.536  20.697  17.950 1.00 58.87  ? 281 ASN   A CB  1 
ATOM   2075 C  CG  . ASN   A  1  268 ? 34.288  19.989  18.421 1.00 61.17  ? 281 ASN   A CG  1 
ATOM   2076 O  OD1 . ASN   A  1  268 ? 34.116  18.777  18.203 1.00 62.04  ? 281 ASN   A OD1 1 
ATOM   2077 N  ND2 . ASN   A  1  268 ? 33.416  20.730  19.078 1.00 59.95  ? 281 ASN   A ND2 1 
ATOM   2078 N  N   . ASN   A  1  269 ? 39.212  20.259  18.564 1.00 54.61  ? 282 ASN   A N   1 
ATOM   2079 C  CA  . ASN   A  1  269 ? 40.508  20.723  18.096 1.00 50.87  ? 282 ASN   A CA  1 
ATOM   2080 C  C   . ASN   A  1  269 ? 41.573  19.652  18.355 1.00 48.52  ? 282 ASN   A C   1 
ATOM   2081 O  O   . ASN   A  1  269 ? 42.623  19.931  18.942 1.00 44.83  ? 282 ASN   A O   1 
ATOM   2082 C  CB  . ASN   A  1  269 ? 40.815  22.085  18.719 1.00 52.02  ? 282 ASN   A CB  1 
ATOM   2083 C  CG  . ASN   A  1  269 ? 41.994  22.764  18.067 1.00 50.53  ? 282 ASN   A CG  1 
ATOM   2084 O  OD1 . ASN   A  1  269 ? 42.165  22.650  16.851 1.00 49.54  ? 282 ASN   A OD1 1 
ATOM   2085 N  ND2 . ASN   A  1  269 ? 42.841  23.409  18.857 1.00 52.66  ? 282 ASN   A ND2 1 
ATOM   2086 N  N   . TYR   A  1  270 ? 41.306  18.421  17.893 1.00 45.53  ? 283 TYR   A N   1 
ATOM   2087 C  CA  . TYR   A  1  270 ? 42.160  17.292  18.227 1.00 47.86  ? 283 TYR   A CA  1 
ATOM   2088 C  C   . TYR   A  1  270 ? 43.363  17.239  17.284 1.00 46.93  ? 283 TYR   A C   1 
ATOM   2089 O  O   . TYR   A  1  270 ? 43.196  17.059  16.083 1.00 49.94  ? 283 TYR   A O   1 
ATOM   2090 C  CB  . TYR   A  1  270 ? 41.376  15.977  18.138 1.00 46.71  ? 283 TYR   A CB  1 
ATOM   2091 C  CG  . TYR   A  1  270 ? 42.099  14.741  18.662 1.00 42.62  ? 283 TYR   A CG  1 
ATOM   2092 C  CD1 . TYR   A  1  270 ? 42.063  14.412  20.012 1.00 42.74  ? 283 TYR   A CD1 1 
ATOM   2093 C  CD2 . TYR   A  1  270 ? 42.809  13.902  17.825 1.00 42.52  ? 283 TYR   A CD2 1 
ATOM   2094 C  CE1 . TYR   A  1  270 ? 42.700  13.286  20.506 1.00 38.96  ? 283 TYR   A CE1 1 
ATOM   2095 C  CE2 . TYR   A  1  270 ? 43.466  12.774  18.309 1.00 43.68  ? 283 TYR   A CE2 1 
ATOM   2096 C  CZ  . TYR   A  1  270 ? 43.408  12.463  19.653 1.00 41.78  ? 283 TYR   A CZ  1 
ATOM   2097 O  OH  . TYR   A  1  270 ? 44.041  11.349  20.120 1.00 38.50  ? 283 TYR   A OH  1 
ATOM   2098 N  N   . VAL   A  1  271 ? 44.568  17.299  17.866 1.00 47.75  ? 284 VAL   A N   1 
ATOM   2099 C  CA  . VAL   A  1  271 ? 45.834  17.272  17.141 1.00 49.93  ? 284 VAL   A CA  1 
ATOM   2100 C  C   . VAL   A  1  271 ? 46.614  16.015  17.521 1.00 48.11  ? 284 VAL   A C   1 
ATOM   2101 O  O   . VAL   A  1  271 ? 46.817  15.744  18.703 1.00 54.84  ? 284 VAL   A O   1 
ATOM   2102 C  CB  . VAL   A  1  271 ? 46.650  18.543  17.468 1.00 50.99  ? 284 VAL   A CB  1 
ATOM   2103 C  CG1 . VAL   A  1  271 ? 48.062  18.498  16.894 1.00 50.98  ? 284 VAL   A CG1 1 
ATOM   2104 C  CG2 . VAL   A  1  271 ? 45.929  19.812  17.023 1.00 50.67  ? 284 VAL   A CG2 1 
ATOM   2105 N  N   . GLU   A  1  272 ? 47.124  15.316  16.508 1.00 47.82  ? 285 GLU   A N   1 
ATOM   2106 C  CA  A GLU   A  1  272 ? 47.881  14.088  16.696 0.50 50.37  ? 285 GLU   A CA  1 
ATOM   2107 C  CA  B GLU   A  1  272 ? 47.892  14.088  16.682 0.50 53.76  ? 285 GLU   A CA  1 
ATOM   2108 C  C   . GLU   A  1  272 ? 49.229  14.395  17.356 1.00 51.36  ? 285 GLU   A C   1 
ATOM   2109 O  O   . GLU   A  1  272 ? 49.795  15.470  17.164 1.00 56.10  ? 285 GLU   A O   1 
ATOM   2110 C  CB  A GLU   A  1  272 ? 47.999  13.396  15.334 0.50 52.14  ? 285 GLU   A CB  1 
ATOM   2111 C  CB  B GLU   A  1  272 ? 48.102  13.383  15.333 0.50 61.43  ? 285 GLU   A CB  1 
ATOM   2112 C  CG  A GLU   A  1  272 ? 46.646  13.125  14.668 0.50 51.28  ? 285 GLU   A CG  1 
ATOM   2113 C  CG  B GLU   A  1  272 ? 49.281  12.403  15.303 0.50 66.01  ? 285 GLU   A CG  1 
ATOM   2114 C  CD  A GLU   A  1  272 ? 46.633  12.513  13.269 0.50 47.41  ? 285 GLU   A CD  1 
ATOM   2115 C  CD  B GLU   A  1  272 ? 49.522  11.579  14.039 0.50 66.36  ? 285 GLU   A CD  1 
ATOM   2116 O  OE1 A GLU   A  1  272 ? 47.690  12.174  12.714 0.50 49.88  ? 285 GLU   A OE1 1 
ATOM   2117 O  OE1 B GLU   A  1  272 ? 48.792  11.728  13.031 0.50 68.81  ? 285 GLU   A OE1 1 
ATOM   2118 O  OE2 A GLU   A  1  272 ? 45.530  12.356  12.726 0.50 42.89  ? 285 GLU   A OE2 1 
ATOM   2119 O  OE2 B GLU   A  1  272 ? 50.462  10.753  14.078 0.50 61.25  ? 285 GLU   A OE2 1 
ATOM   2120 N  N   . ASP   A  1  273 ? 49.716  13.446  18.179 1.00 52.78  ? 286 ASP   A N   1 
ATOM   2121 C  CA  . ASP   A  1  273 ? 51.053  13.485  18.762 1.00 55.65  ? 286 ASP   A CA  1 
ATOM   2122 C  C   . ASP   A  1  273 ? 51.863  12.324  18.189 1.00 57.91  ? 286 ASP   A C   1 
ATOM   2123 O  O   . ASP   A  1  273 ? 51.658  11.173  18.571 1.00 44.63  ? 286 ASP   A O   1 
ATOM   2124 C  CB  . ASP   A  1  273 ? 51.050  13.433  20.285 1.00 61.72  ? 286 ASP   A CB  1 
ATOM   2125 C  CG  . ASP   A  1  273 ? 52.421  13.494  20.949 1.00 66.07  ? 286 ASP   A CG  1 
ATOM   2126 O  OD1 . ASP   A  1  273 ? 53.428  13.604  20.221 1.00 68.00  ? 286 ASP   A OD1 1 
ATOM   2127 O  OD2 . ASP   A  1  273 ? 52.482  13.429  22.197 1.00 64.83  ? 286 ASP   A OD2 1 
ATOM   2128 N  N   . PRO   A  1  274 ? 52.811  12.581  17.255 1.00 65.53  ? 287 PRO   A N   1 
ATOM   2129 C  CA  . PRO   A  1  274 ? 53.585  11.496  16.646 1.00 63.85  ? 287 PRO   A CA  1 
ATOM   2130 C  C   . PRO   A  1  274 ? 54.661  10.882  17.548 1.00 57.11  ? 287 PRO   A C   1 
ATOM   2131 O  O   . PRO   A  1  274 ? 55.159  9.807   17.236 1.00 43.86  ? 287 PRO   A O   1 
ATOM   2132 C  CB  . PRO   A  1  274 ? 54.177  12.200  15.404 1.00 64.49  ? 287 PRO   A CB  1 
ATOM   2133 C  CG  . PRO   A  1  274 ? 54.391  13.633  15.862 1.00 67.64  ? 287 PRO   A CG  1 
ATOM   2134 C  CD  . PRO   A  1  274 ? 53.199  13.915  16.763 1.00 63.46  ? 287 PRO   A CD  1 
ATOM   2135 N  N   . ASP   A  1  275 ? 54.989  11.548  18.670 1.00 58.91  ? 288 ASP   A N   1 
ATOM   2136 C  CA  . ASP   A  1  275 ? 55.956  11.055  19.650 1.00 61.33  ? 288 ASP   A CA  1 
ATOM   2137 C  C   . ASP   A  1  275 ? 55.351  10.109  20.692 1.00 57.13  ? 288 ASP   A C   1 
ATOM   2138 O  O   . ASP   A  1  275 ? 56.111  9.457   21.408 1.00 51.53  ? 288 ASP   A O   1 
ATOM   2139 C  CB  . ASP   A  1  275 ? 56.629  12.204  20.390 1.00 63.86  ? 288 ASP   A CB  1 
ATOM   2140 C  CG  . ASP   A  1  275 ? 57.523  13.079  19.522 1.00 73.20  ? 288 ASP   A CG  1 
ATOM   2141 O  OD1 . ASP   A  1  275 ? 57.828  12.633  18.383 1.00 64.97  ? 288 ASP   A OD1 1 
ATOM   2142 O  OD2 . ASP   A  1  275 ? 57.882  14.193  19.986 1.00 73.88  ? 288 ASP   A OD2 1 
ATOM   2143 N  N   . SER   A  1  276 ? 54.012  10.030  20.772 1.00 46.69  ? 289 SER   A N   1 
ATOM   2144 C  CA  . SER   A  1  276 ? 53.357  9.206   21.772 1.00 47.04  ? 289 SER   A CA  1 
ATOM   2145 C  C   . SER   A  1  276 ? 53.605  7.721   21.511 1.00 41.57  ? 289 SER   A C   1 
ATOM   2146 O  O   . SER   A  1  276 ? 53.759  7.293   20.378 1.00 38.70  ? 289 SER   A O   1 
ATOM   2147 C  CB  . SER   A  1  276 ? 51.876  9.501   21.819 1.00 45.30  ? 289 SER   A CB  1 
ATOM   2148 O  OG  . SER   A  1  276 ? 51.180  8.463   22.489 1.00 45.49  ? 289 SER   A OG  1 
ATOM   2149 N  N   . ALA   A  1  277 ? 53.627  6.931   22.585 1.00 41.52  ? 290 ALA   A N   1 
ATOM   2150 C  CA  . ALA   A  1  277 ? 53.487  5.486   22.456 1.00 38.54  ? 290 ALA   A CA  1 
ATOM   2151 C  C   . ALA   A  1  277 ? 52.219  5.175   21.674 1.00 37.50  ? 290 ALA   A C   1 
ATOM   2152 O  O   . ALA   A  1  277 ? 51.277  5.956   21.660 1.00 38.91  ? 290 ALA   A O   1 
ATOM   2153 C  CB  . ALA   A  1  277 ? 53.452  4.836   23.816 1.00 40.53  ? 290 ALA   A CB  1 
ATOM   2154 N  N   . ASP   A  1  278 ? 52.219  4.026   21.016 1.00 35.76  ? 291 ASP   A N   1 
ATOM   2155 C  CA  . ASP   A  1  278 ? 51.023  3.472   20.406 1.00 36.00  ? 291 ASP   A CA  1 
ATOM   2156 C  C   . ASP   A  1  278 ? 51.252  1.965   20.387 1.00 37.53  ? 291 ASP   A C   1 
ATOM   2157 O  O   . ASP   A  1  278 ? 52.233  1.504   20.982 1.00 37.03  ? 291 ASP   A O   1 
ATOM   2158 C  CB  . ASP   A  1  278 ? 50.710  4.127   19.068 1.00 39.97  ? 291 ASP   A CB  1 
ATOM   2159 C  CG  . ASP   A  1  278 ? 51.698  3.857   17.933 1.00 46.72  ? 291 ASP   A CG  1 
ATOM   2160 O  OD1 . ASP   A  1  278 ? 52.412  2.823   17.988 1.00 45.58  ? 291 ASP   A OD1 1 
ATOM   2161 O  OD2 . ASP   A  1  278 ? 51.782  4.711   17.020 1.00 47.23  ? 291 ASP   A OD2 1 
ATOM   2162 N  N   . PHE   A  1  279 ? 50.389  1.215   19.698 1.00 35.18  ? 292 PHE   A N   1 
ATOM   2163 C  CA  . PHE   A  1  279 ? 50.399  -0.236  19.820 1.00 42.44  ? 292 PHE   A CA  1 
ATOM   2164 C  C   . PHE   A  1  279 ? 51.541  -0.889  19.030 1.00 46.23  ? 292 PHE   A C   1 
ATOM   2165 O  O   . PHE   A  1  279 ? 51.868  -2.046  19.304 1.00 46.06  ? 292 PHE   A O   1 
ATOM   2166 C  CB  . PHE   A  1  279 ? 49.029  -0.823  19.463 1.00 43.68  ? 292 PHE   A CB  1 
ATOM   2167 C  CG  . PHE   A  1  279 ? 48.063  -0.636  20.617 1.00 41.00  ? 292 PHE   A CG  1 
ATOM   2168 C  CD1 . PHE   A  1  279 ? 48.138  -1.464  21.734 1.00 43.77  ? 292 PHE   A CD1 1 
ATOM   2169 C  CD2 . PHE   A  1  279 ? 47.156  0.412   20.628 1.00 41.52  ? 292 PHE   A CD2 1 
ATOM   2170 C  CE1 . PHE   A  1  279 ? 47.291  -1.275  22.817 1.00 45.14  ? 292 PHE   A CE1 1 
ATOM   2171 C  CE2 . PHE   A  1  279 ? 46.313  0.607   21.722 1.00 44.92  ? 292 PHE   A CE2 1 
ATOM   2172 C  CZ  . PHE   A  1  279 ? 46.390  -0.233  22.816 1.00 47.48  ? 292 PHE   A CZ  1 
ATOM   2173 N  N   . THR   A  1  280 ? 52.185  -0.169  18.102 1.00 43.82  ? 293 THR   A N   1 
ATOM   2174 C  CA  . THR   A  1  280 ? 53.382  -0.708  17.455 1.00 56.01  ? 293 THR   A CA  1 
ATOM   2175 C  C   . THR   A  1  280 ? 54.667  -0.069  18.004 1.00 53.81  ? 293 THR   A C   1 
ATOM   2176 O  O   . THR   A  1  280 ? 55.744  -0.344  17.483 1.00 50.34  ? 293 THR   A O   1 
ATOM   2177 C  CB  . THR   A  1  280 ? 53.260  -0.551  15.933 1.00 57.69  ? 293 THR   A CB  1 
ATOM   2178 O  OG1 . THR   A  1  280 ? 53.115  0.839   15.645 1.00 53.61  ? 293 THR   A OG1 1 
ATOM   2179 C  CG2 . THR   A  1  280 ? 52.080  -1.325  15.366 1.00 55.72  ? 293 THR   A CG2 1 
ATOM   2180 N  N   . HIS   A  1  281 ? 54.557  0.765   19.052 1.00 53.35  ? 294 HIS   A N   1 
ATOM   2181 C  CA  . HIS   A  1  281 ? 55.699  1.446   19.654 1.00 51.38  ? 294 HIS   A CA  1 
ATOM   2182 C  C   . HIS   A  1  281 ? 55.554  1.462   21.179 1.00 51.43  ? 294 HIS   A C   1 
ATOM   2183 O  O   . HIS   A  1  281 ? 55.571  2.526   21.816 1.00 47.10  ? 294 HIS   A O   1 
ATOM   2184 C  CB  . HIS   A  1  281 ? 55.833  2.887   19.134 1.00 56.33  ? 294 HIS   A CB  1 
ATOM   2185 C  CG  . HIS   A  1  281 ? 56.023  3.036   17.657 1.00 70.66  ? 294 HIS   A CG  1 
ATOM   2186 N  ND1 . HIS   A  1  281 ? 54.964  3.063   16.773 1.00 76.94  ? 294 HIS   A ND1 1 
ATOM   2187 C  CD2 . HIS   A  1  281 ? 57.132  3.170   16.914 1.00 71.14  ? 294 HIS   A CD2 1 
ATOM   2188 C  CE1 . HIS   A  1  281 ? 55.426  3.216   15.544 1.00 77.71  ? 294 HIS   A CE1 1 
ATOM   2189 N  NE2 . HIS   A  1  281 ? 56.741  3.285   15.606 1.00 76.20  ? 294 HIS   A NE2 1 
ATOM   2190 N  N   . LEU   A  1  282 ? 55.404  0.272   21.770 1.00 48.64  ? 295 LEU   A N   1 
ATOM   2191 C  CA  . LEU   A  1  282 ? 55.041  0.162   23.174 1.00 46.84  ? 295 LEU   A CA  1 
ATOM   2192 C  C   . LEU   A  1  282 ? 56.174  0.635   24.081 1.00 47.60  ? 295 LEU   A C   1 
ATOM   2193 O  O   . LEU   A  1  282 ? 55.912  1.147   25.163 1.00 48.59  ? 295 LEU   A O   1 
ATOM   2194 C  CB  . LEU   A  1  282 ? 54.628  -1.264  23.511 1.00 45.92  ? 295 LEU   A CB  1 
ATOM   2195 C  CG  . LEU   A  1  282 ? 53.240  -1.676  23.025 1.00 48.00  ? 295 LEU   A CG  1 
ATOM   2196 C  CD1 . LEU   A  1  282 ? 53.005  -3.184  23.181 1.00 46.63  ? 295 LEU   A CD1 1 
ATOM   2197 C  CD2 . LEU   A  1  282 ? 52.198  -0.833  23.755 1.00 45.55  ? 295 LEU   A CD2 1 
ATOM   2198 N  N   . CYS   A  1  283 ? 57.424  0.475   23.650 1.00 43.57  ? 296 CYS   A N   1 
ATOM   2199 C  CA  . CYS   A  1  283 ? 58.561  0.782   24.504 1.00 46.12  ? 296 CYS   A CA  1 
ATOM   2200 C  C   . CYS   A  1  283 ? 58.610  2.268   24.846 1.00 43.00  ? 296 CYS   A C   1 
ATOM   2201 O  O   . CYS   A  1  283 ? 59.158  2.640   25.879 1.00 44.40  ? 296 CYS   A O   1 
ATOM   2202 C  CB  . CYS   A  1  283 ? 59.882  0.285   23.910 1.00 52.42  ? 296 CYS   A CB  1 
ATOM   2203 S  SG  . CYS   A  1  283 ? 60.096  -1.518  24.012 1.00 69.99  ? 296 CYS   A SG  1 
ATOM   2204 N  N   . ARG   A  1  284 ? 57.999  3.111   24.013 1.00 41.52  ? 297 ARG   A N   1 
ATOM   2205 C  CA  . ARG   A  1  284 ? 57.939  4.532   24.312 1.00 45.32  ? 297 ARG   A CA  1 
ATOM   2206 C  C   . ARG   A  1  284 ? 57.187  4.770   25.620 1.00 44.29  ? 297 ARG   A C   1 
ATOM   2207 O  O   . ARG   A  1  284 ? 57.489  5.713   26.343 1.00 44.70  ? 297 ARG   A O   1 
ATOM   2208 C  CB  . ARG   A  1  284 ? 57.210  5.316   23.222 1.00 48.01  ? 297 ARG   A CB  1 
ATOM   2209 C  CG  . ARG   A  1  284 ? 57.940  5.302   21.887 1.00 52.64  ? 297 ARG   A CG  1 
ATOM   2210 C  CD  . ARG   A  1  284 ? 57.211  6.194   20.900 1.00 53.30  ? 297 ARG   A CD  1 
ATOM   2211 N  NE  . ARG   A  1  284 ? 57.796  6.135   19.563 1.00 55.58  ? 297 ARG   A NE  1 
ATOM   2212 C  CZ  . ARG   A  1  284 ? 57.318  6.713   18.474 1.00 58.12  ? 297 ARG   A CZ  1 
ATOM   2213 N  NH1 . ARG   A  1  284 ? 56.209  7.425   18.521 1.00 53.30  ? 297 ARG   A NH1 1 
ATOM   2214 N  NH2 . ARG   A  1  284 ? 57.961  6.573   17.326 1.00 62.31  ? 297 ARG   A NH2 1 
ATOM   2215 N  N   . LEU   A  1  285 ? 56.193  3.925   25.902 1.00 40.11  ? 298 LEU   A N   1 
ATOM   2216 C  CA  . LEU   A  1  285 ? 55.431  4.042   27.129 1.00 41.75  ? 298 LEU   A CA  1 
ATOM   2217 C  C   . LEU   A  1  285 ? 56.374  3.805   28.310 1.00 39.59  ? 298 LEU   A C   1 
ATOM   2218 O  O   . LEU   A  1  285 ? 56.354  4.583   29.262 1.00 36.07  ? 298 LEU   A O   1 
ATOM   2219 C  CB  . LEU   A  1  285 ? 54.231  3.093   27.109 1.00 43.47  ? 298 LEU   A CB  1 
ATOM   2220 C  CG  . LEU   A  1  285 ? 53.267  3.207   28.292 1.00 45.96  ? 298 LEU   A CG  1 
ATOM   2221 C  CD1 . LEU   A  1  285 ? 51.923  2.624   27.918 1.00 49.14  ? 298 LEU   A CD1 1 
ATOM   2222 C  CD2 . LEU   A  1  285 ? 53.778  2.519   29.549 1.00 47.89  ? 298 LEU   A CD2 1 
ATOM   2223 N  N   . TYR   A  1  286 ? 57.229  2.777   28.220 1.00 37.73  ? 299 TYR   A N   1 
ATOM   2224 C  CA  . TYR   A  1  286 ? 58.212  2.490   29.259 1.00 36.99  ? 299 TYR   A CA  1 
ATOM   2225 C  C   . TYR   A  1  286 ? 59.134  3.694   29.477 1.00 37.31  ? 299 TYR   A C   1 
ATOM   2226 O  O   . TYR   A  1  286 ? 59.323  4.145   30.603 1.00 38.70  ? 299 TYR   A O   1 
ATOM   2227 C  CB  . TYR   A  1  286 ? 59.006  1.224   28.923 1.00 36.99  ? 299 TYR   A CB  1 
ATOM   2228 C  CG  . TYR   A  1  286 ? 60.175  0.964   29.861 1.00 37.28  ? 299 TYR   A CG  1 
ATOM   2229 C  CD1 . TYR   A  1  286 ? 59.961  0.643   31.188 1.00 38.80  ? 299 TYR   A CD1 1 
ATOM   2230 C  CD2 . TYR   A  1  286 ? 61.487  1.013   29.411 1.00 41.20  ? 299 TYR   A CD2 1 
ATOM   2231 C  CE1 . TYR   A  1  286 ? 61.012  0.399   32.060 1.00 40.23  ? 299 TYR   A CE1 1 
ATOM   2232 C  CE2 . TYR   A  1  286 ? 62.555  0.798   30.273 1.00 39.20  ? 299 TYR   A CE2 1 
ATOM   2233 C  CZ  . TYR   A  1  286 ? 62.318  0.495   31.597 1.00 36.98  ? 299 TYR   A CZ  1 
ATOM   2234 O  OH  . TYR   A  1  286 ? 63.366  0.281   32.423 1.00 34.23  ? 299 TYR   A OH  1 
ATOM   2235 N  N   . GLU   A  1  287 ? 59.673  4.243   28.395 1.00 40.24  ? 300 GLU   A N   1 
ATOM   2236 C  CA  . GLU   A  1  287 ? 60.599  5.370   28.472 1.00 48.03  ? 300 GLU   A CA  1 
ATOM   2237 C  C   . GLU   A  1  287 ? 59.878  6.596   29.041 1.00 43.98  ? 300 GLU   A C   1 
ATOM   2238 O  O   . GLU   A  1  287 ? 60.417  7.277   29.905 1.00 39.77  ? 300 GLU   A O   1 
ATOM   2239 C  CB  . GLU   A  1  287 ? 61.241  5.665   27.115 1.00 51.69  ? 300 GLU   A CB  1 
ATOM   2240 C  CG  . GLU   A  1  287 ? 62.021  4.466   26.562 1.00 63.91  ? 300 GLU   A CG  1 
ATOM   2241 C  CD  . GLU   A  1  287 ? 62.460  4.463   25.095 1.00 78.68  ? 300 GLU   A CD  1 
ATOM   2242 O  OE1 . GLU   A  1  287 ? 61.692  4.881   24.186 1.00 69.93  ? 300 GLU   A OE1 1 
ATOM   2243 O  OE2 . GLU   A  1  287 ? 63.602  3.986   24.843 1.00 90.31  ? 300 GLU   A OE2 1 
ATOM   2244 N  N   . PHE   A  1  288 ? 58.646  6.845   28.581 1.00 36.94  ? 301 PHE   A N   1 
ATOM   2245 C  CA  . PHE   A  1  288 ? 57.864  7.978   29.035 1.00 36.42  ? 301 PHE   A CA  1 
ATOM   2246 C  C   . PHE   A  1  288 ? 57.696  7.919   30.550 1.00 37.78  ? 301 PHE   A C   1 
ATOM   2247 O  O   . PHE   A  1  288 ? 57.872  8.909   31.252 1.00 38.27  ? 301 PHE   A O   1 
ATOM   2248 C  CB  . PHE   A  1  288 ? 56.511  7.992   28.310 1.00 39.38  ? 301 PHE   A CB  1 
ATOM   2249 C  CG  . PHE   A  1  288 ? 55.696  9.217   28.685 1.00 42.53  ? 301 PHE   A CG  1 
ATOM   2250 C  CD1 . PHE   A  1  288 ? 55.905  10.443  28.044 1.00 42.95  ? 301 PHE   A CD1 1 
ATOM   2251 C  CD2 . PHE   A  1  288 ? 54.791  9.161   29.730 1.00 42.83  ? 301 PHE   A CD2 1 
ATOM   2252 C  CE1 . PHE   A  1  288 ? 55.189  11.569  28.422 1.00 46.74  ? 301 PHE   A CE1 1 
ATOM   2253 C  CE2 . PHE   A  1  288 ? 54.081  10.295  30.111 1.00 44.06  ? 301 PHE   A CE2 1 
ATOM   2254 C  CZ  . PHE   A  1  288 ? 54.278  11.495  29.458 1.00 44.19  ? 301 PHE   A CZ  1 
ATOM   2255 N  N   . VAL   A  1  289 ? 57.374  6.733   31.059 1.00 36.27  ? 302 VAL   A N   1 
ATOM   2256 C  CA  . VAL   A  1  289 ? 57.051  6.565   32.467 1.00 33.88  ? 302 VAL   A CA  1 
ATOM   2257 C  C   . VAL   A  1  289 ? 58.306  6.711   33.304 1.00 30.46  ? 302 VAL   A C   1 
ATOM   2258 O  O   . VAL   A  1  289 ? 58.228  7.260   34.386 1.00 33.53  ? 302 VAL   A O   1 
ATOM   2259 C  CB  . VAL   A  1  289 ? 56.352  5.215   32.748 1.00 31.58  ? 302 VAL   A CB  1 
ATOM   2260 C  CG1 . VAL   A  1  289 ? 56.278  4.901   34.229 1.00 31.11  ? 302 VAL   A CG1 1 
ATOM   2261 C  CG2 . VAL   A  1  289 ? 54.950  5.215   32.168 1.00 33.40  ? 302 VAL   A CG2 1 
ATOM   2262 N  N   . VAL   A  1  290 ? 59.441  6.181   32.828 1.00 35.14  ? 303 VAL   A N   1 
ATOM   2263 C  CA  . VAL   A  1  290 ? 60.672  6.316   33.585 1.00 32.42  ? 303 VAL   A CA  1 
ATOM   2264 C  C   . VAL   A  1  290 ? 61.001  7.803   33.697 1.00 30.12  ? 303 VAL   A C   1 
ATOM   2265 O  O   . VAL   A  1  290 ? 61.359  8.279   34.759 1.00 29.76  ? 303 VAL   A O   1 
ATOM   2266 C  CB  . VAL   A  1  290 ? 61.815  5.507   32.976 1.00 34.68  ? 303 VAL   A CB  1 
ATOM   2267 C  CG1 . VAL   A  1  290 ? 63.139  5.858   33.631 1.00 37.36  ? 303 VAL   A CG1 1 
ATOM   2268 C  CG2 . VAL   A  1  290 ? 61.554  4.010   33.065 1.00 34.15  ? 303 VAL   A CG2 1 
ATOM   2269 N  N   . GLY   A  1  291 ? 60.786  8.538   32.614 1.00 30.76  ? 304 GLY   A N   1 
ATOM   2270 C  CA  . GLY   A  1  291 ? 60.896  9.991   32.594 1.00 33.20  ? 304 GLY   A CA  1 
ATOM   2271 C  C   . GLY   A  1  291 ? 59.993  10.634  33.639 1.00 36.49  ? 304 GLY   A C   1 
ATOM   2272 O  O   . GLY   A  1  291 ? 60.419  11.505  34.395 1.00 37.66  ? 304 GLY   A O   1 
ATOM   2273 N  N   . SER   A  1  292 ? 58.740  10.172  33.706 1.00 35.18  ? 305 SER   A N   1 
ATOM   2274 C  CA  . SER   A  1  292 ? 57.795  10.737  34.644 1.00 32.76  ? 305 SER   A CA  1 
ATOM   2275 C  C   . SER   A  1  292 ? 58.261  10.480  36.064 1.00 32.46  ? 305 SER   A C   1 
ATOM   2276 O  O   . SER   A  1  292 ? 58.119  11.339  36.920 1.00 38.21  ? 305 SER   A O   1 
ATOM   2277 C  CB  . SER   A  1  292 ? 56.397  10.234  34.401 1.00 33.63  ? 305 SER   A CB  1 
ATOM   2278 O  OG  . SER   A  1  292 ? 56.044  10.443  33.042 1.00 37.63  ? 305 SER   A OG  1 
ATOM   2279 N  N   . VAL   A  1  293 ? 58.817  9.301   36.312 1.00 32.95  ? 306 VAL   A N   1 
ATOM   2280 C  CA  . VAL   A  1  293 ? 59.298  8.956   37.641 1.00 33.78  ? 306 VAL   A CA  1 
ATOM   2281 C  C   . VAL   A  1  293 ? 60.451  9.883   38.020 1.00 31.56  ? 306 VAL   A C   1 
ATOM   2282 O  O   . VAL   A  1  293 ? 60.542  10.273  39.167 1.00 31.01  ? 306 VAL   A O   1 
ATOM   2283 C  CB  . VAL   A  1  293 ? 59.735  7.478   37.714 1.00 34.26  ? 306 VAL   A CB  1 
ATOM   2284 C  CG1 . VAL   A  1  293 ? 60.503  7.157   38.994 1.00 30.34  ? 306 VAL   A CG1 1 
ATOM   2285 C  CG2 . VAL   A  1  293 ? 58.539  6.551   37.550 1.00 37.92  ? 306 VAL   A CG2 1 
ATOM   2286 N  N   . GLN   A  1  294 ? 61.327  10.217  37.071 1.00 32.24  ? 307 GLN   A N   1 
ATOM   2287 C  CA  . GLN   A  1  294 ? 62.451  11.101  37.342 1.00 37.52  ? 307 GLN   A CA  1 
ATOM   2288 C  C   . GLN   A  1  294 ? 61.955  12.494  37.717 1.00 37.23  ? 307 GLN   A C   1 
ATOM   2289 O  O   . GLN   A  1  294 ? 62.527  13.115  38.607 1.00 41.75  ? 307 GLN   A O   1 
ATOM   2290 C  CB  . GLN   A  1  294 ? 63.425  11.191  36.171 1.00 37.17  ? 307 GLN   A CB  1 
ATOM   2291 C  CG  . GLN   A  1  294 ? 64.135  9.868   35.892 1.00 42.85  ? 307 GLN   A CG  1 
ATOM   2292 C  CD  . GLN   A  1  294 ? 64.992  9.906   34.649 1.00 41.05  ? 307 GLN   A CD  1 
ATOM   2293 O  OE1 . GLN   A  1  294 ? 64.540  9.672   33.526 1.00 48.99  ? 307 GLN   A OE1 1 
ATOM   2294 N  NE2 . GLN   A  1  294 ? 66.264  10.193  34.845 1.00 41.94  ? 307 GLN   A NE2 1 
ATOM   2295 N  N   . GLU   A  1  295 ? 60.886  12.964  37.057 1.00 38.68  ? 308 GLU   A N   1 
ATOM   2296 C  CA  . GLU   A  1  295 ? 60.293  14.248  37.408 1.00 42.47  ? 308 GLU   A CA  1 
ATOM   2297 C  C   . GLU   A  1  295 ? 59.735  14.186  38.826 1.00 40.60  ? 308 GLU   A C   1 
ATOM   2298 O  O   . GLU   A  1  295 ? 59.831  15.172  39.541 1.00 42.16  ? 308 GLU   A O   1 
ATOM   2299 C  CB  . GLU   A  1  295 ? 59.170  14.709  36.475 1.00 48.52  ? 308 GLU   A CB  1 
ATOM   2300 C  CG  . GLU   A  1  295 ? 59.607  14.976  35.038 1.00 61.68  ? 308 GLU   A CG  1 
ATOM   2301 C  CD  . GLU   A  1  295 ? 58.445  15.212  34.075 1.00 76.05  ? 308 GLU   A CD  1 
ATOM   2302 O  OE1 . GLU   A  1  295 ? 57.361  14.570  34.227 1.00 72.94  ? 308 GLU   A OE1 1 
ATOM   2303 O  OE2 . GLU   A  1  295 ? 58.635  16.043  33.148 1.00 77.33  ? 308 GLU   A OE2 1 
ATOM   2304 N  N   . LEU   A  1  296 ? 59.170  13.037  39.237 1.00 37.33  ? 309 LEU   A N   1 
ATOM   2305 C  CA  . LEU   A  1  296 ? 58.609  12.889  40.574 1.00 36.49  ? 309 LEU   A CA  1 
ATOM   2306 C  C   . LEU   A  1  296 ? 59.723  12.769  41.607 1.00 35.07  ? 309 LEU   A C   1 
ATOM   2307 O  O   . LEU   A  1  296 ? 59.563  13.220  42.738 1.00 34.74  ? 309 LEU   A O   1 
ATOM   2308 C  CB  . LEU   A  1  296 ? 57.677  11.680  40.685 1.00 35.60  ? 309 LEU   A CB  1 
ATOM   2309 C  CG  . LEU   A  1  296 ? 56.352  11.769  39.920 1.00 39.14  ? 309 LEU   A CG  1 
ATOM   2310 C  CD1 . LEU   A  1  296 ? 55.661  10.420  40.095 1.00 42.63  ? 309 LEU   A CD1 1 
ATOM   2311 C  CD2 . LEU   A  1  296 ? 55.411  12.906  40.316 1.00 35.68  ? 309 LEU   A CD2 1 
ATOM   2312 N  N   . TYR   A  1  297 ? 60.819  12.102  41.229 1.00 32.29  ? 310 TYR   A N   1 
ATOM   2313 C  CA  . TYR   A  1  297 ? 61.899  11.775  42.154 1.00 36.89  ? 310 TYR   A CA  1 
ATOM   2314 C  C   . TYR   A  1  297 ? 63.233  12.260  41.575 1.00 38.15  ? 310 TYR   A C   1 
ATOM   2315 O  O   . TYR   A  1  297 ? 64.020  11.474  41.070 1.00 34.09  ? 310 TYR   A O   1 
ATOM   2316 C  CB  . TYR   A  1  297 ? 61.904  10.269  42.436 1.00 34.68  ? 310 TYR   A CB  1 
ATOM   2317 C  CG  . TYR   A  1  297 ? 60.676  9.784   43.185 1.00 34.69  ? 310 TYR   A CG  1 
ATOM   2318 C  CD1 . TYR   A  1  297 ? 60.546  9.966   44.558 1.00 32.87  ? 310 TYR   A CD1 1 
ATOM   2319 C  CD2 . TYR   A  1  297 ? 59.637  9.146   42.509 1.00 35.14  ? 310 TYR   A CD2 1 
ATOM   2320 C  CE1 . TYR   A  1  297 ? 59.415  9.536   45.240 1.00 35.46  ? 310 TYR   A CE1 1 
ATOM   2321 C  CE2 . TYR   A  1  297 ? 58.516  8.684   43.192 1.00 33.00  ? 310 TYR   A CE2 1 
ATOM   2322 C  CZ  . TYR   A  1  297 ? 58.402  8.879   44.554 1.00 32.48  ? 310 TYR   A CZ  1 
ATOM   2323 O  OH  . TYR   A  1  297 ? 57.289  8.474   45.220 1.00 34.37  ? 310 TYR   A OH  1 
ATOM   2324 N  N   . PRO   A  1  298 ? 63.490  13.587  41.559 1.00 40.34  ? 311 PRO   A N   1 
ATOM   2325 C  CA  . PRO   A  1  298 ? 64.663  14.136  40.884 1.00 42.43  ? 311 PRO   A CA  1 
ATOM   2326 C  C   . PRO   A  1  298 ? 65.998  13.783  41.537 1.00 38.50  ? 311 PRO   A C   1 
ATOM   2327 O  O   . PRO   A  1  298 ? 66.979  13.682  40.811 1.00 37.82  ? 311 PRO   A O   1 
ATOM   2328 C  CB  . PRO   A  1  298 ? 64.404  15.660  40.854 1.00 44.86  ? 311 PRO   A CB  1 
ATOM   2329 C  CG  . PRO   A  1  298 ? 63.468  15.908  42.018 1.00 52.28  ? 311 PRO   A CG  1 
ATOM   2330 C  CD  . PRO   A  1  298 ? 62.644  14.633  42.144 1.00 43.03  ? 311 PRO   A CD  1 
ATOM   2331 N  N   . ASN   A  1  299 ? 66.042  13.595  42.871 1.00 39.21  ? 312 ASN   A N   1 
ATOM   2332 C  CA  . ASN   A  1  299 ? 67.307  13.290  43.533 1.00 36.40  ? 312 ASN   A CA  1 
ATOM   2333 C  C   . ASN   A  1  299 ? 67.119  12.451  44.789 1.00 32.24  ? 312 ASN   A C   1 
ATOM   2334 O  O   . ASN   A  1  299 ? 67.514  12.852  45.867 1.00 31.06  ? 312 ASN   A O   1 
ATOM   2335 C  CB  . ASN   A  1  299 ? 68.116  14.544  43.851 1.00 38.47  ? 312 ASN   A CB  1 
ATOM   2336 C  CG  . ASN   A  1  299 ? 69.524  14.223  44.305 1.00 37.51  ? 312 ASN   A CG  1 
ATOM   2337 O  OD1 . ASN   A  1  299 ? 70.254  13.424  43.694 1.00 37.84  ? 312 ASN   A OD1 1 
ATOM   2338 N  ND2 . ASN   A  1  299 ? 69.904  14.835  45.406 1.00 36.56  ? 312 ASN   A ND2 1 
ATOM   2339 N  N   . PRO   A  1  300 ? 66.617  11.210  44.681 1.00 34.17  ? 313 PRO   A N   1 
ATOM   2340 C  CA  . PRO   A  1  300 ? 66.407  10.378  45.865 1.00 36.11  ? 313 PRO   A CA  1 
ATOM   2341 C  C   . PRO   A  1  300 ? 67.698  9.802   46.433 1.00 31.38  ? 313 PRO   A C   1 
ATOM   2342 O  O   . PRO   A  1  300 ? 68.605  9.516   45.677 1.00 33.22  ? 313 PRO   A O   1 
ATOM   2343 C  CB  . PRO   A  1  300 ? 65.497  9.280   45.324 1.00 32.75  ? 313 PRO   A CB  1 
ATOM   2344 C  CG  . PRO   A  1  300 ? 65.972  9.114   43.917 1.00 34.79  ? 313 PRO   A CG  1 
ATOM   2345 C  CD  . PRO   A  1  300 ? 66.232  10.543  43.428 1.00 36.54  ? 313 PRO   A CD  1 
ATOM   2346 N  N   . THR   A  1  301 ? 67.711  9.559   47.748 1.00 33.47  ? 314 THR   A N   1 
ATOM   2347 C  CA  . THR   A  1  301 ? 68.806  8.884   48.436 1.00 42.31  ? 314 THR   A CA  1 
ATOM   2348 C  C   . THR   A  1  301 ? 68.219  7.904   49.446 1.00 39.27  ? 314 THR   A C   1 
ATOM   2349 O  O   . THR   A  1  301 ? 67.010  7.915   49.685 1.00 43.31  ? 314 THR   A O   1 
ATOM   2350 C  CB  . THR   A  1  301 ? 69.718  9.902   49.140 1.00 49.30  ? 314 THR   A CB  1 
ATOM   2351 O  OG1 . THR   A  1  301 ? 68.971  10.711  50.038 1.00 46.56  ? 314 THR   A OG1 1 
ATOM   2352 C  CG2 . THR   A  1  301 ? 70.356  10.898  48.187 1.00 53.13  ? 314 THR   A CG2 1 
ATOM   2353 N  N   . GLY   A  1  302 ? 69.082  7.099   50.076 1.00 37.95  ? 315 GLY   A N   1 
ATOM   2354 C  CA  . GLY   A  1  302 ? 68.672  6.205   51.156 1.00 38.88  ? 315 GLY   A CA  1 
ATOM   2355 C  C   . GLY   A  1  302 ? 67.640  5.153   50.714 1.00 39.45  ? 315 GLY   A C   1 
ATOM   2356 O  O   . GLY   A  1  302 ? 67.719  4.640   49.600 1.00 39.53  ? 315 GLY   A O   1 
ATOM   2357 N  N   . ILE   A  1  303 ? 66.685  4.840   51.599 1.00 39.09  ? 316 ILE   A N   1 
ATOM   2358 C  CA  . ILE   A  1  303 ? 65.710  3.781   51.374 1.00 45.65  ? 316 ILE   A CA  1 
ATOM   2359 C  C   . ILE   A  1  303 ? 64.830  4.130   50.173 1.00 40.29  ? 316 ILE   A C   1 
ATOM   2360 O  O   . ILE   A  1  303 ? 64.478  3.250   49.392 1.00 36.96  ? 316 ILE   A O   1 
ATOM   2361 C  CB  . ILE   A  1  303 ? 64.890  3.495   52.653 1.00 56.45  ? 316 ILE   A CB  1 
ATOM   2362 C  CG1 . ILE   A  1  303 ? 65.796  2.954   53.773 1.00 79.33  ? 316 ILE   A CG1 1 
ATOM   2363 C  CG2 . ILE   A  1  303 ? 63.758  2.498   52.394 1.00 61.46  ? 316 ILE   A CG2 1 
ATOM   2364 C  CD1 . ILE   A  1  303 ? 65.126  2.831   55.140 1.00 91.01  ? 316 ILE   A CD1 1 
ATOM   2365 N  N   . LEU   A  1  304 ? 64.485  5.415   50.010 1.00 35.20  ? 317 LEU   A N   1 
ATOM   2366 C  CA  . LEU   A  1  304 ? 63.664  5.817   48.881 1.00 37.36  ? 317 LEU   A CA  1 
ATOM   2367 C  C   . LEU   A  1  304 ? 64.375  5.455   47.576 1.00 35.58  ? 317 LEU   A C   1 
ATOM   2368 O  O   . LEU   A  1  304 ? 63.772  4.893   46.678 1.00 33.42  ? 317 LEU   A O   1 
ATOM   2369 C  CB  . LEU   A  1  304 ? 63.350  7.309   48.972 1.00 35.43  ? 317 LEU   A CB  1 
ATOM   2370 C  CG  . LEU   A  1  304 ? 62.625  7.916   47.773 1.00 35.32  ? 317 LEU   A CG  1 
ATOM   2371 C  CD1 . LEU   A  1  304 ? 61.305  7.202   47.493 1.00 37.21  ? 317 LEU   A CD1 1 
ATOM   2372 C  CD2 . LEU   A  1  304 ? 62.401  9.406   48.021 1.00 33.84  ? 317 LEU   A CD2 1 
ATOM   2373 N  N   . ARG   A  1  305 ? 65.671  5.765   47.464 1.00 36.89  ? 318 ARG   A N   1 
ATOM   2374 C  CA  A ARG   A  1  305 ? 66.411  5.452   46.253 0.50 32.89  ? 318 ARG   A CA  1 
ATOM   2375 C  CA  B ARG   A  1  305 ? 66.416  5.453   46.255 0.50 36.97  ? 318 ARG   A CA  1 
ATOM   2376 C  C   . ARG   A  1  305 ? 66.429  3.941   46.046 1.00 32.88  ? 318 ARG   A C   1 
ATOM   2377 O  O   . ARG   A  1  305 ? 66.223  3.478   44.944 1.00 36.09  ? 318 ARG   A O   1 
ATOM   2378 C  CB  A ARG   A  1  305 ? 67.840  5.994   46.315 0.50 28.75  ? 318 ARG   A CB  1 
ATOM   2379 C  CB  B ARG   A  1  305 ? 67.851  5.989   46.308 0.50 38.41  ? 318 ARG   A CB  1 
ATOM   2380 C  CG  A ARG   A  1  305 ? 68.741  5.612   45.152 0.50 26.26  ? 318 ARG   A CG  1 
ATOM   2381 C  CG  B ARG   A  1  305 ? 68.738  5.602   45.130 0.50 41.63  ? 318 ARG   A CG  1 
ATOM   2382 C  CD  A ARG   A  1  305 ? 70.207  5.919   45.464 0.50 24.25  ? 318 ARG   A CD  1 
ATOM   2383 C  CD  B ARG   A  1  305 ? 70.210  5.985   45.333 0.50 45.18  ? 318 ARG   A CD  1 
ATOM   2384 N  NE  A ARG   A  1  305 ? 71.037  5.353   44.398 0.50 20.29  ? 318 ARG   A NE  1 
ATOM   2385 N  NE  B ARG   A  1  305 ? 71.089  5.761   44.176 0.50 46.43  ? 318 ARG   A NE  1 
ATOM   2386 C  CZ  A ARG   A  1  305 ? 71.602  4.172   44.461 0.50 16.79  ? 318 ARG   A CZ  1 
ATOM   2387 C  CZ  B ARG   A  1  305 ? 71.254  6.525   43.071 0.50 46.35  ? 318 ARG   A CZ  1 
ATOM   2388 N  NH1 A ARG   A  1  305 ? 71.596  3.555   45.613 0.50 15.08  ? 318 ARG   A NH1 1 
ATOM   2389 N  NH1 B ARG   A  1  305 ? 70.536  7.584   42.792 0.50 40.75  ? 318 ARG   A NH1 1 
ATOM   2390 N  NH2 A ARG   A  1  305 ? 72.176  3.675   43.385 0.50 15.77  ? 318 ARG   A NH2 1 
ATOM   2391 N  NH2 B ARG   A  1  305 ? 72.177  6.208   42.191 0.50 56.96  ? 318 ARG   A NH2 1 
ATOM   2392 N  N   . ARG   A  1  306 ? 66.700  3.194   47.109 1.00 32.40  ? 319 ARG   A N   1 
ATOM   2393 C  CA  . ARG   A  1  306 ? 66.807  1.745   47.025 1.00 37.11  ? 319 ARG   A CA  1 
ATOM   2394 C  C   . ARG   A  1  306 ? 65.479  1.157   46.549 1.00 34.84  ? 319 ARG   A C   1 
ATOM   2395 O  O   . ARG   A  1  306 ? 65.463  0.307   45.674 1.00 34.04  ? 319 ARG   A O   1 
ATOM   2396 C  CB  . ARG   A  1  306 ? 67.267  1.189   48.380 1.00 40.61  ? 319 ARG   A CB  1 
ATOM   2397 C  CG  . ARG   A  1  306 ? 67.382  -0.332  48.454 1.00 57.15  ? 319 ARG   A CG  1 
ATOM   2398 C  CD  . ARG   A  1  306 ? 67.326  -0.918  49.878 1.00 65.75  ? 319 ARG   A CD  1 
ATOM   2399 N  NE  . ARG   A  1  306 ? 65.944  -1.006  50.377 1.00 76.22  ? 319 ARG   A NE  1 
ATOM   2400 C  CZ  . ARG   A  1  306 ? 65.570  -1.160  51.653 1.00 82.06  ? 319 ARG   A CZ  1 
ATOM   2401 N  NH1 . ARG   A  1  306 ? 66.473  -1.343  52.606 1.00 75.98  ? 319 ARG   A NH1 1 
ATOM   2402 N  NH2 . ARG   A  1  306 ? 64.289  -1.112  51.970 1.00 84.16  ? 319 ARG   A NH2 1 
ATOM   2403 N  N   . ASN   A  1  307 ? 64.368  1.650   47.104 1.00 33.01  ? 320 ASN   A N   1 
ATOM   2404 C  CA  . ASN   A  1  307 ? 63.062  1.105   46.791 1.00 34.67  ? 320 ASN   A CA  1 
ATOM   2405 C  C   . ASN   A  1  307 ? 62.623  1.522   45.390 1.00 35.40  ? 320 ASN   A C   1 
ATOM   2406 O  O   . ASN   A  1  307 ? 61.977  0.737   44.704 1.00 34.72  ? 320 ASN   A O   1 
ATOM   2407 C  CB  . ASN   A  1  307 ? 62.048  1.476   47.859 1.00 34.63  ? 320 ASN   A CB  1 
ATOM   2408 C  CG  . ASN   A  1  307 ? 62.289  0.699   49.123 1.00 33.95  ? 320 ASN   A CG  1 
ATOM   2409 O  OD1 . ASN   A  1  307 ? 63.292  -0.016  49.226 1.00 35.41  ? 320 ASN   A OD1 1 
ATOM   2410 N  ND2 . ASN   A  1  307 ? 61.387  0.820   50.082 1.00 36.61  ? 320 ASN   A ND2 1 
ATOM   2411 N  N   . LEU   A  1  308 ? 63.040  2.717   44.949 1.00 33.26  ? 321 LEU   A N   1 
ATOM   2412 C  CA  . LEU   A  1  308 ? 62.807  3.146   43.583 1.00 34.23  ? 321 LEU   A CA  1 
ATOM   2413 C  C   . LEU   A  1  308 ? 63.484  2.208   42.600 1.00 33.07  ? 321 LEU   A C   1 
ATOM   2414 O  O   . LEU   A  1  308 ? 62.897  1.839   41.583 1.00 31.93  ? 321 LEU   A O   1 
ATOM   2415 C  CB  . LEU   A  1  308 ? 63.311  4.563   43.345 1.00 37.11  ? 321 LEU   A CB  1 
ATOM   2416 C  CG  . LEU   A  1  308 ? 62.248  5.648   43.409 1.00 47.30  ? 321 LEU   A CG  1 
ATOM   2417 C  CD1 . LEU   A  1  308 ? 62.951  6.969   43.480 1.00 52.92  ? 321 LEU   A CD1 1 
ATOM   2418 C  CD2 . LEU   A  1  308 ? 61.332  5.575   42.192 1.00 51.08  ? 321 LEU   A CD2 1 
ATOM   2419 N  N   . ILE   A  1  309 ? 64.740  1.881   42.883 1.00 30.03  ? 322 ILE   A N   1 
ATOM   2420 C  CA  . ILE   A  1  309 ? 65.496  1.021   41.990 1.00 33.08  ? 322 ILE   A CA  1 
ATOM   2421 C  C   . ILE   A  1  309 ? 64.820  -0.350  41.892 1.00 30.34  ? 322 ILE   A C   1 
ATOM   2422 O  O   . ILE   A  1  309 ? 64.693  -0.886  40.807 1.00 34.71  ? 322 ILE   A O   1 
ATOM   2423 C  CB  . ILE   A  1  309 ? 66.960  0.923   42.452 1.00 32.96  ? 322 ILE   A CB  1 
ATOM   2424 C  CG1 . ILE   A  1  309 ? 67.701  2.263   42.225 1.00 39.49  ? 322 ILE   A CG1 1 
ATOM   2425 C  CG2 . ILE   A  1  309 ? 67.680  -0.237  41.762 1.00 32.06  ? 322 ILE   A CG2 1 
ATOM   2426 C  CD1 . ILE   A  1  309 ? 69.034  2.345   42.956 1.00 39.67  ? 322 ILE   A CD1 1 
ATOM   2427 N  N   . LYS   A  1  310 ? 64.396  -0.907  43.021 1.00 31.01  ? 323 LYS   A N   1 
ATOM   2428 C  CA  . LYS   A  1  310 ? 63.782  -2.231  43.036 1.00 37.04  ? 323 LYS   A CA  1 
ATOM   2429 C  C   . LYS   A  1  310 ? 62.443  -2.228  42.298 1.00 34.08  ? 323 LYS   A C   1 
ATOM   2430 O  O   . LYS   A  1  310 ? 62.221  -3.068  41.445 1.00 33.03  ? 323 LYS   A O   1 
ATOM   2431 C  CB  . LYS   A  1  310 ? 63.614  -2.710  44.476 1.00 37.42  ? 323 LYS   A CB  1 
ATOM   2432 C  CG  . LYS   A  1  310 ? 64.923  -3.111  45.102 1.00 38.87  ? 323 LYS   A CG  1 
ATOM   2433 C  CD  . LYS   A  1  310 ? 64.774  -3.542  46.549 1.00 46.90  ? 323 LYS   A CD  1 
ATOM   2434 C  CE  . LYS   A  1  310 ? 65.892  -4.469  46.990 1.00 49.09  ? 323 LYS   A CE  1 
ATOM   2435 N  NZ  . LYS   A  1  310 ? 65.932  -4.442  48.453 1.00 58.21  ? 323 LYS   A NZ  1 
ATOM   2436 N  N   . ASN   A  1  311 ? 61.609  -1.217  42.556 1.00 33.28  ? 324 ASN   A N   1 
ATOM   2437 C  CA  . ASN   A  1  311 ? 60.299  -1.148  41.940 1.00 32.22  ? 324 ASN   A CA  1 
ATOM   2438 C  C   . ASN   A  1  311 ? 60.440  -0.957  40.432 1.00 31.96  ? 324 ASN   A C   1 
ATOM   2439 O  O   . ASN   A  1  311 ? 59.696  -1.542  39.665 1.00 33.20  ? 324 ASN   A O   1 
ATOM   2440 C  CB  . ASN   A  1  311 ? 59.443  -0.088  42.614 1.00 32.18  ? 324 ASN   A CB  1 
ATOM   2441 C  CG  . ASN   A  1  311 ? 58.753  -0.624  43.846 1.00 33.56  ? 324 ASN   A CG  1 
ATOM   2442 O  OD1 . ASN   A  1  311 ? 57.729  -1.313  43.745 1.00 34.45  ? 324 ASN   A OD1 1 
ATOM   2443 N  ND2 . ASN   A  1  311 ? 59.261  -0.287  45.022 1.00 36.63  ? 324 ASN   A ND2 1 
ATOM   2444 N  N   . LEU   A  1  312 ? 61.425  -0.163  40.013 1.00 32.23  ? 325 LEU   A N   1 
ATOM   2445 C  CA  . LEU   A  1  312 ? 61.638  0.083   38.604 1.00 31.66  ? 325 LEU   A CA  1 
ATOM   2446 C  C   . LEU   A  1  312 ? 62.028  -1.231  37.940 1.00 30.24  ? 325 LEU   A C   1 
ATOM   2447 O  O   . LEU   A  1  312 ? 61.546  -1.514  36.860 1.00 31.64  ? 325 LEU   A O   1 
ATOM   2448 C  CB  . LEU   A  1  312 ? 62.687  1.169   38.382 1.00 32.82  ? 325 LEU   A CB  1 
ATOM   2449 C  CG  . LEU   A  1  312 ? 62.189  2.613   38.441 1.00 37.50  ? 325 LEU   A CG  1 
ATOM   2450 C  CD1 . LEU   A  1  312 ? 63.367  3.562   38.675 1.00 41.37  ? 325 LEU   A CD1 1 
ATOM   2451 C  CD2 . LEU   A  1  312 ? 61.457  3.010   37.188 1.00 36.19  ? 325 LEU   A CD2 1 
ATOM   2452 N  N   . HIS   A  1  313 ? 62.905  -2.010  38.583 1.00 31.42  ? 326 HIS   A N   1 
ATOM   2453 C  CA  . HIS   A  1  313 ? 63.312  -3.306  38.056 1.00 33.62  ? 326 HIS   A CA  1 
ATOM   2454 C  C   . HIS   A  1  313 ? 62.116  -4.254  37.994 1.00 31.02  ? 326 HIS   A C   1 
ATOM   2455 O  O   . HIS   A  1  313 ? 61.871  -4.854  36.961 1.00 31.67  ? 326 HIS   A O   1 
ATOM   2456 C  CB  . HIS   A  1  313 ? 64.476  -3.907  38.850 1.00 35.87  ? 326 HIS   A CB  1 
ATOM   2457 C  CG  . HIS   A  1  313 ? 64.947  -5.200  38.272 1.00 40.11  ? 326 HIS   A CG  1 
ATOM   2458 N  ND1 . HIS   A  1  313 ? 65.484  -5.238  37.002 1.00 39.76  ? 326 HIS   A ND1 1 
ATOM   2459 C  CD2 . HIS   A  1  313 ? 64.879  -6.484  38.706 1.00 38.38  ? 326 HIS   A CD2 1 
ATOM   2460 C  CE1 . HIS   A  1  313 ? 65.786  -6.502  36.704 1.00 41.83  ? 326 HIS   A CE1 1 
ATOM   2461 N  NE2 . HIS   A  1  313 ? 65.423  -7.278  37.720 1.00 41.38  ? 326 HIS   A NE2 1 
ATOM   2462 N  N   . TYR   A  1  314 ? 61.325  -4.322  39.064 1.00 34.74  ? 327 TYR   A N   1 
ATOM   2463 C  CA  . TYR   A  1  314 ? 60.138  -5.176  39.058 1.00 34.16  ? 327 TYR   A CA  1 
ATOM   2464 C  C   . TYR   A  1  314 ? 59.249  -4.810  37.878 1.00 34.41  ? 327 TYR   A C   1 
ATOM   2465 O  O   . TYR   A  1  314 ? 58.790  -5.681  37.149 1.00 41.73  ? 327 TYR   A O   1 
ATOM   2466 C  CB  . TYR   A  1  314 ? 59.321  -5.064  40.341 1.00 31.58  ? 327 TYR   A CB  1 
ATOM   2467 C  CG  . TYR   A  1  314 ? 60.081  -5.430  41.608 1.00 35.19  ? 327 TYR   A CG  1 
ATOM   2468 C  CD1 . TYR   A  1  314 ? 61.166  -6.302  41.596 1.00 35.59  ? 327 TYR   A CD1 1 
ATOM   2469 C  CD2 . TYR   A  1  314 ? 59.707  -4.877  42.820 1.00 36.36  ? 327 TYR   A CD2 1 
ATOM   2470 C  CE1 . TYR   A  1  314 ? 61.849  -6.621  42.762 1.00 35.16  ? 327 TYR   A CE1 1 
ATOM   2471 C  CE2 . TYR   A  1  314 ? 60.363  -5.199  43.993 1.00 42.82  ? 327 TYR   A CE2 1 
ATOM   2472 C  CZ  . TYR   A  1  314 ? 61.442  -6.067  43.963 1.00 40.40  ? 327 TYR   A CZ  1 
ATOM   2473 O  OH  . TYR   A  1  314 ? 62.052  -6.333  45.151 1.00 37.11  ? 327 TYR   A OH  1 
ATOM   2474 N  N   . TRP   A  1  315 ? 59.041  -3.507  37.661 1.00 34.71  ? 328 TRP   A N   1 
ATOM   2475 C  CA  . TRP   A  1  315 ? 58.151  -3.093  36.598 1.00 33.47  ? 328 TRP   A CA  1 
ATOM   2476 C  C   . TRP   A  1  315 ? 58.706  -3.557  35.251 1.00 35.30  ? 328 TRP   A C   1 
ATOM   2477 O  O   . TRP   A  1  315 ? 57.984  -4.113  34.432 1.00 34.61  ? 328 TRP   A O   1 
ATOM   2478 C  CB  . TRP   A  1  315 ? 57.923  -1.581  36.630 1.00 33.11  ? 328 TRP   A CB  1 
ATOM   2479 C  CG  . TRP   A  1  315 ? 56.835  -1.143  35.692 1.00 30.12  ? 328 TRP   A CG  1 
ATOM   2480 C  CD1 . TRP   A  1  315 ? 55.590  -1.694  35.564 1.00 28.62  ? 328 TRP   A CD1 1 
ATOM   2481 C  CD2 . TRP   A  1  315 ? 56.923  -0.092  34.714 1.00 32.93  ? 328 TRP   A CD2 1 
ATOM   2482 N  NE1 . TRP   A  1  315 ? 54.891  -1.042  34.587 1.00 32.78  ? 328 TRP   A NE1 1 
ATOM   2483 C  CE2 . TRP   A  1  315 ? 55.680  -0.058  34.045 1.00 33.41  ? 328 TRP   A CE2 1 
ATOM   2484 C  CE3 . TRP   A  1  315 ? 57.915  0.824   34.367 1.00 33.89  ? 328 TRP   A CE3 1 
ATOM   2485 C  CZ2 . TRP   A  1  315 ? 55.406  0.864   33.044 1.00 33.07  ? 328 TRP   A CZ2 1 
ATOM   2486 C  CZ3 . TRP   A  1  315 ? 57.638  1.733   33.374 1.00 36.17  ? 328 TRP   A CZ3 1 
ATOM   2487 C  CH2 . TRP   A  1  315 ? 56.406  1.748   32.722 1.00 35.62  ? 328 TRP   A CH2 1 
ATOM   2488 N  N   . TRP   A  1  316 ? 60.018  -3.373  35.064 1.00 38.26  ? 329 TRP   A N   1 
ATOM   2489 C  CA  . TRP   A  1  316 ? 60.681  -3.748  33.831 1.00 37.35  ? 329 TRP   A CA  1 
ATOM   2490 C  C   . TRP   A  1  316 ? 60.485  -5.246  33.569 1.00 36.73  ? 329 TRP   A C   1 
ATOM   2491 O  O   . TRP   A  1  316 ? 60.287  -5.625  32.428 1.00 38.44  ? 329 TRP   A O   1 
ATOM   2492 C  CB  . TRP   A  1  316 ? 62.174  -3.338  33.833 1.00 38.99  ? 329 TRP   A CB  1 
ATOM   2493 C  CG  . TRP   A  1  316 ? 62.913  -3.892  32.645 1.00 36.77  ? 329 TRP   A CG  1 
ATOM   2494 C  CD1 . TRP   A  1  316 ? 62.930  -3.396  31.371 1.00 41.68  ? 329 TRP   A CD1 1 
ATOM   2495 C  CD2 . TRP   A  1  316 ? 63.594  -5.154  32.585 1.00 37.20  ? 329 TRP   A CD2 1 
ATOM   2496 N  NE1 . TRP   A  1  316 ? 63.628  -4.237  30.537 1.00 39.67  ? 329 TRP   A NE1 1 
ATOM   2497 C  CE2 . TRP   A  1  316 ? 64.035  -5.326  31.252 1.00 41.62  ? 329 TRP   A CE2 1 
ATOM   2498 C  CE3 . TRP   A  1  316 ? 63.881  -6.143  33.522 1.00 38.23  ? 329 TRP   A CE3 1 
ATOM   2499 C  CZ2 . TRP   A  1  316 ? 64.737  -6.455  30.840 1.00 40.12  ? 329 TRP   A CZ2 1 
ATOM   2500 C  CZ3 . TRP   A  1  316 ? 64.586  -7.257  33.113 1.00 38.93  ? 329 TRP   A CZ3 1 
ATOM   2501 C  CH2 . TRP   A  1  316 ? 64.980  -7.421  31.789 1.00 38.81  ? 329 TRP   A CH2 1 
ATOM   2502 N  N   . THR   A  1  317 ? 60.501  -6.097  34.601 1.00 39.99  ? 330 THR   A N   1 
ATOM   2503 C  CA  . THR   A  1  317 ? 60.387  -7.534  34.364 1.00 45.09  ? 330 THR   A CA  1 
ATOM   2504 C  C   . THR   A  1  317 ? 59.053  -7.832  33.683 1.00 39.51  ? 330 THR   A C   1 
ATOM   2505 O  O   . THR   A  1  317 ? 58.973  -8.700  32.843 1.00 46.93  ? 330 THR   A O   1 
ATOM   2506 C  CB  . THR   A  1  317 ? 60.520  -8.381  35.632 1.00 44.79  ? 330 THR   A CB  1 
ATOM   2507 O  OG1 . THR   A  1  317 ? 59.416  -8.108  36.487 1.00 47.88  ? 330 THR   A OG1 1 
ATOM   2508 C  CG2 . THR   A  1  317 ? 61.825  -8.165  36.375 1.00 45.72  ? 330 THR   A CG2 1 
ATOM   2509 N  N   . GLY   A  1  318 ? 58.000  -7.114  34.056 1.00 39.63  ? 331 GLY   A N   1 
ATOM   2510 C  CA  . GLY   A  1  318 ? 56.718  -7.272  33.400 1.00 36.51  ? 331 GLY   A CA  1 
ATOM   2511 C  C   . GLY   A  1  318 ? 56.707  -6.639  32.009 1.00 35.13  ? 331 GLY   A C   1 
ATOM   2512 O  O   . GLY   A  1  318 ? 56.242  -7.233  31.044 1.00 35.28  ? 331 GLY   A O   1 
ATOM   2513 N  N   . VAL   A  1  319 ? 57.203  -5.408  31.928 1.00 35.00  ? 332 VAL   A N   1 
ATOM   2514 C  CA  . VAL   A  1  319 ? 57.187  -4.656  30.689 1.00 35.15  ? 332 VAL   A CA  1 
ATOM   2515 C  C   . VAL   A  1  319 ? 57.946  -5.425  29.623 1.00 37.47  ? 332 VAL   A C   1 
ATOM   2516 O  O   . VAL   A  1  319 ? 57.548  -5.434  28.468 1.00 41.72  ? 332 VAL   A O   1 
ATOM   2517 C  CB  . VAL   A  1  319 ? 57.783  -3.255  30.913 1.00 38.67  ? 332 VAL   A CB  1 
ATOM   2518 C  CG1 . VAL   A  1  319 ? 58.267  -2.608  29.625 1.00 39.94  ? 332 VAL   A CG1 1 
ATOM   2519 C  CG2 . VAL   A  1  319 ? 56.781  -2.361  31.622 1.00 42.11  ? 332 VAL   A CG2 1 
ATOM   2520 N  N   . ASN   A  1  320 ? 59.065  -6.034  30.009 1.00 45.94  ? 333 ASN   A N   1 
ATOM   2521 C  CA  . ASN   A  1  320 ? 59.959  -6.660  29.044 1.00 44.99  ? 333 ASN   A CA  1 
ATOM   2522 C  C   . ASN   A  1  320 ? 59.199  -7.740  28.296 1.00 46.59  ? 333 ASN   A C   1 
ATOM   2523 O  O   . ASN   A  1  320 ? 59.348  -7.840  27.087 1.00 51.19  ? 333 ASN   A O   1 
ATOM   2524 C  CB  . ASN   A  1  320 ? 61.227  -7.219  29.683 1.00 44.45  ? 333 ASN   A CB  1 
ATOM   2525 C  CG  . ASN   A  1  320 ? 62.254  -7.642  28.663 1.00 42.40  ? 333 ASN   A CG  1 
ATOM   2526 O  OD1 . ASN   A  1  320 ? 62.583  -6.887  27.747 1.00 44.68  ? 333 ASN   A OD1 1 
ATOM   2527 N  ND2 . ASN   A  1  320 ? 62.759  -8.851  28.787 1.00 42.46  ? 333 ASN   A ND2 1 
ATOM   2528 N  N   . VAL   A  1  321 ? 58.364  -8.503  29.006 1.00 46.89  ? 334 VAL   A N   1 
ATOM   2529 C  CA  . VAL   A  1  321 ? 57.555  -9.533  28.374 1.00 46.14  ? 334 VAL   A CA  1 
ATOM   2530 C  C   . VAL   A  1  321 ? 56.385  -8.878  27.640 1.00 45.73  ? 334 VAL   A C   1 
ATOM   2531 O  O   . VAL   A  1  321 ? 56.148  -9.170  26.484 1.00 49.97  ? 334 VAL   A O   1 
ATOM   2532 C  CB  . VAL   A  1  321 ? 57.066  -10.568 29.406 1.00 49.17  ? 334 VAL   A CB  1 
ATOM   2533 C  CG1 . VAL   A  1  321 ? 56.119  -11.607 28.801 1.00 46.80  ? 334 VAL   A CG1 1 
ATOM   2534 C  CG2 . VAL   A  1  321 ? 58.223  -11.230 30.152 1.00 50.50  ? 334 VAL   A CG2 1 
ATOM   2535 N  N   . ALA   A  1  322 ? 55.652  -7.983  28.299 1.00 46.40  ? 335 ALA   A N   1 
ATOM   2536 C  CA  . ALA   A  1  322 ? 54.384  -7.531  27.748 1.00 46.67  ? 335 ALA   A CA  1 
ATOM   2537 C  C   . ALA   A  1  322 ? 54.602  -6.711  26.484 1.00 47.63  ? 335 ALA   A C   1 
ATOM   2538 O  O   . ALA   A  1  322 ? 53.769  -6.730  25.589 1.00 46.74  ? 335 ALA   A O   1 
ATOM   2539 C  CB  . ALA   A  1  322 ? 53.616  -6.719  28.769 1.00 50.19  ? 335 ALA   A CB  1 
ATOM   2540 N  N   . PHE   A  1  323 ? 55.690  -5.939  26.446 1.00 49.02  ? 336 PHE   A N   1 
ATOM   2541 C  CA  . PHE   A  1  323 ? 55.920  -5.021  25.344 1.00 48.85  ? 336 PHE   A CA  1 
ATOM   2542 C  C   . PHE   A  1  323 ? 56.814  -5.677  24.290 1.00 49.39  ? 336 PHE   A C   1 
ATOM   2543 O  O   . PHE   A  1  323 ? 57.094  -5.054  23.285 1.00 49.54  ? 336 PHE   A O   1 
ATOM   2544 C  CB  . PHE   A  1  323 ? 56.544  -3.733  25.877 1.00 45.31  ? 336 PHE   A CB  1 
ATOM   2545 C  CG  . PHE   A  1  323 ? 55.635  -2.851  26.718 1.00 45.11  ? 336 PHE   A CG  1 
ATOM   2546 C  CD1 . PHE   A  1  323 ? 54.345  -3.243  27.045 1.00 49.81  ? 336 PHE   A CD1 1 
ATOM   2547 C  CD2 . PHE   A  1  323 ? 56.092  -1.636  27.205 1.00 43.65  ? 336 PHE   A CD2 1 
ATOM   2548 C  CE1 . PHE   A  1  323 ? 53.526  -2.429  27.811 1.00 53.14  ? 336 PHE   A CE1 1 
ATOM   2549 C  CE2 . PHE   A  1  323 ? 55.279  -0.840  27.991 1.00 52.14  ? 336 PHE   A CE2 1 
ATOM   2550 C  CZ  . PHE   A  1  323 ? 53.986  -1.225  28.272 1.00 55.07  ? 336 PHE   A CZ  1 
ATOM   2551 N  N   . GLY   A  1  324 ? 57.266  -6.918  24.520 1.00 50.37  ? 337 GLY   A N   1 
ATOM   2552 C  CA  . GLY   A  1  324 ? 58.031  -7.673  23.537 1.00 54.64  ? 337 GLY   A CA  1 
ATOM   2553 C  C   . GLY   A  1  324 ? 59.501  -7.256  23.464 1.00 54.60  ? 337 GLY   A C   1 
ATOM   2554 O  O   . GLY   A  1  324 ? 60.063  -7.252  22.384 1.00 53.98  ? 337 GLY   A O   1 
ATOM   2555 N  N   . GLY   A  1  325 ? 60.114  -6.916  24.608 1.00 58.52  ? 338 GLY   A N   1 
ATOM   2556 C  CA  . GLY   A  1  325 ? 61.531  -6.578  24.713 1.00 51.67  ? 338 GLY   A CA  1 
ATOM   2557 C  C   . GLY   A  1  325 ? 61.734  -5.067  24.780 1.00 55.29  ? 338 GLY   A C   1 
ATOM   2558 O  O   . GLY   A  1  325 ? 61.440  -4.384  23.798 1.00 57.91  ? 338 GLY   A O   1 
ATOM   2559 N  N   . CYS   A  1  326 ? 62.182  -4.544  25.941 1.00 46.51  ? 339 CYS   A N   1 
ATOM   2560 C  CA  . CYS   A  1  326 ? 62.582  -3.146  26.065 1.00 49.65  ? 339 CYS   A CA  1 
ATOM   2561 C  C   . CYS   A  1  326 ? 63.918  -3.100  26.790 1.00 46.09  ? 339 CYS   A C   1 
ATOM   2562 O  O   . CYS   A  1  326 ? 64.132  -3.867  27.726 1.00 45.32  ? 339 CYS   A O   1 
ATOM   2563 C  CB  . CYS   A  1  326 ? 61.608  -2.271  26.863 1.00 56.53  ? 339 CYS   A CB  1 
ATOM   2564 S  SG  . CYS   A  1  326 ? 59.970  -2.044  26.105 1.00 78.33  ? 339 CYS   A SG  1 
ATOM   2565 N  N   . ASP   A  1  327 ? 64.790  -2.178  26.380 1.00 46.38  ? 340 ASP   A N   1 
ATOM   2566 C  CA  . ASP   A  1  327 ? 66.059  -1.991  27.073 1.00 52.08  ? 340 ASP   A CA  1 
ATOM   2567 C  C   . ASP   A  1  327 ? 65.789  -1.379  28.443 1.00 47.19  ? 340 ASP   A C   1 
ATOM   2568 O  O   . ASP   A  1  327 ? 65.176  -0.308  28.534 1.00 49.87  ? 340 ASP   A O   1 
ATOM   2569 C  CB  . ASP   A  1  327 ? 67.016  -1.117  26.266 1.00 58.12  ? 340 ASP   A CB  1 
ATOM   2570 C  CG  . ASP   A  1  327 ? 67.521  -1.698  24.946 1.00 58.35  ? 340 ASP   A CG  1 
ATOM   2571 O  OD1 . ASP   A  1  327 ? 67.485  -2.939  24.790 1.00 55.17  ? 340 ASP   A OD1 1 
ATOM   2572 O  OD2 . ASP   A  1  327 ? 67.909  -0.901  24.072 1.00 56.56  ? 340 ASP   A OD2 1 
ATOM   2573 N  N   . GLU   A  1  328 ? 66.255  -2.059  29.493 1.00 40.75  ? 341 GLU   A N   1 
ATOM   2574 C  CA  . GLU   A  1  328 ? 66.089  -1.554  30.847 1.00 44.01  ? 341 GLU   A CA  1 
ATOM   2575 C  C   . GLU   A  1  328 ? 66.840  -0.233  31.023 1.00 41.59  ? 341 GLU   A C   1 
ATOM   2576 O  O   . GLU   A  1  328 ? 67.966  -0.112  30.582 1.00 43.56  ? 341 GLU   A O   1 
ATOM   2577 C  CB  . GLU   A  1  328 ? 66.553  -2.581  31.878 1.00 40.01  ? 341 GLU   A CB  1 
ATOM   2578 C  CG  . GLU   A  1  328 ? 66.134  -2.185  33.293 1.00 43.64  ? 341 GLU   A CG  1 
ATOM   2579 C  CD  . GLU   A  1  328 ? 66.300  -3.249  34.368 1.00 43.13  ? 341 GLU   A CD  1 
ATOM   2580 O  OE1 . GLU   A  1  328 ? 66.828  -4.342  34.041 1.00 47.45  ? 341 GLU   A OE1 1 
ATOM   2581 O  OE2 . GLU   A  1  328 ? 65.909  -2.989  35.528 1.00 39.92  ? 341 GLU   A OE2 1 
ATOM   2582 N  N   . LEU   A  1  329 ? 66.190  0.753   31.647 1.00 41.74  ? 342 LEU   A N   1 
ATOM   2583 C  CA  . LEU   A  1  329 ? 66.826  1.999   32.043 1.00 39.01  ? 342 LEU   A CA  1 
ATOM   2584 C  C   . LEU   A  1  329 ? 67.171  1.956   33.528 1.00 41.28  ? 342 LEU   A C   1 
ATOM   2585 O  O   . LEU   A  1  329 ? 66.473  1.311   34.325 1.00 39.44  ? 342 LEU   A O   1 
ATOM   2586 C  CB  . LEU   A  1  329 ? 65.887  3.159   31.713 1.00 40.21  ? 342 LEU   A CB  1 
ATOM   2587 C  CG  . LEU   A  1  329 ? 65.575  3.340   30.225 1.00 44.71  ? 342 LEU   A CG  1 
ATOM   2588 C  CD1 . LEU   A  1  329 ? 64.487  4.370   30.001 1.00 43.69  ? 342 LEU   A CD1 1 
ATOM   2589 C  CD2 . LEU   A  1  329 ? 66.838  3.741   29.454 1.00 43.33  ? 342 LEU   A CD2 1 
ATOM   2590 N  N   . PHE   A  1  330 ? 68.248  2.676   33.890 1.00 42.00  ? 343 PHE   A N   1 
ATOM   2591 C  CA  . PHE   A  1  330 ? 68.755  2.713   35.252 1.00 43.23  ? 343 PHE   A CA  1 
ATOM   2592 C  C   . PHE   A  1  330 ? 68.951  4.161   35.692 1.00 44.92  ? 343 PHE   A C   1 
ATOM   2593 O  O   . PHE   A  1  330 ? 70.061  4.602   35.955 1.00 43.89  ? 343 PHE   A O   1 
ATOM   2594 C  CB  . PHE   A  1  330 ? 70.070  1.942   35.309 1.00 40.44  ? 343 PHE   A CB  1 
ATOM   2595 C  CG  . PHE   A  1  330 ? 69.913  0.473   34.951 1.00 44.39  ? 343 PHE   A CG  1 
ATOM   2596 C  CD1 . PHE   A  1  330 ? 69.390  -0.446  35.865 1.00 45.99  ? 343 PHE   A CD1 1 
ATOM   2597 C  CD2 . PHE   A  1  330 ? 70.284  0.022   33.690 1.00 44.63  ? 343 PHE   A CD2 1 
ATOM   2598 C  CE1 . PHE   A  1  330 ? 69.220  -1.781  35.514 1.00 48.19  ? 343 PHE   A CE1 1 
ATOM   2599 C  CE2 . PHE   A  1  330 ? 70.136  -1.321  33.357 1.00 51.60  ? 343 PHE   A CE2 1 
ATOM   2600 C  CZ  . PHE   A  1  330 ? 69.617  -2.221  34.277 1.00 45.99  ? 343 PHE   A CZ  1 
ATOM   2601 N  N   . PRO   A  1  331 ? 67.876  4.960   35.820 1.00 41.44  ? 344 PRO   A N   1 
ATOM   2602 C  CA  . PRO   A  1  331 ? 68.035  6.382   36.121 1.00 38.73  ? 344 PRO   A CA  1 
ATOM   2603 C  C   . PRO   A  1  331 ? 68.704  6.681   37.458 1.00 36.56  ? 344 PRO   A C   1 
ATOM   2604 O  O   . PRO   A  1  331 ? 69.187  7.787   37.639 1.00 37.22  ? 344 PRO   A O   1 
ATOM   2605 C  CB  . PRO   A  1  331 ? 66.599  6.907   36.053 1.00 39.82  ? 344 PRO   A CB  1 
ATOM   2606 C  CG  . PRO   A  1  331 ? 65.777  5.689   36.393 1.00 42.88  ? 344 PRO   A CG  1 
ATOM   2607 C  CD  . PRO   A  1  331 ? 66.473  4.559   35.668 1.00 41.48  ? 344 PRO   A CD  1 
ATOM   2608 N  N   . TYR   A  1  332 ? 68.724  5.715   38.380 1.00 32.44  ? 345 TYR   A N   1 
ATOM   2609 C  CA  . TYR   A  1  332 ? 69.355  5.881   39.680 1.00 33.66  ? 345 TYR   A CA  1 
ATOM   2610 C  C   . TYR   A  1  332 ? 70.497  4.875   39.874 1.00 32.45  ? 345 TYR   A C   1 
ATOM   2611 O  O   . TYR   A  1  332 ? 70.903  4.589   41.001 1.00 33.50  ? 345 TYR   A O   1 
ATOM   2612 C  CB  . TYR   A  1  332 ? 68.319  5.726   40.794 1.00 32.56  ? 345 TYR   A CB  1 
ATOM   2613 C  CG  . TYR   A  1  332 ? 67.140  6.657   40.592 1.00 38.55  ? 345 TYR   A CG  1 
ATOM   2614 C  CD1 . TYR   A  1  332 ? 67.267  8.042   40.707 1.00 38.71  ? 345 TYR   A CD1 1 
ATOM   2615 C  CD2 . TYR   A  1  332 ? 65.898  6.143   40.238 1.00 42.15  ? 345 TYR   A CD2 1 
ATOM   2616 C  CE1 . TYR   A  1  332 ? 66.200  8.880   40.421 1.00 40.46  ? 345 TYR   A CE1 1 
ATOM   2617 C  CE2 . TYR   A  1  332 ? 64.819  6.971   39.975 1.00 43.00  ? 345 TYR   A CE2 1 
ATOM   2618 C  CZ  . TYR   A  1  332 ? 64.966  8.340   40.083 1.00 42.72  ? 345 TYR   A CZ  1 
ATOM   2619 O  OH  . TYR   A  1  332 ? 63.897  9.134   39.819 1.00 41.58  ? 345 TYR   A OH  1 
ATOM   2620 N  N   . GLY   A  1  333 ? 71.041  4.373   38.772 1.00 34.87  ? 346 GLY   A N   1 
ATOM   2621 C  CA  . GLY   A  1  333 ? 72.083  3.361   38.832 1.00 40.98  ? 346 GLY   A CA  1 
ATOM   2622 C  C   . GLY   A  1  333 ? 71.568  2.038   39.399 1.00 45.52  ? 346 GLY   A C   1 
ATOM   2623 O  O   . GLY   A  1  333 ? 70.395  1.703   39.217 1.00 48.65  ? 346 GLY   A O   1 
ATOM   2624 N  N   . GLN   A  1  334 ? 72.460  1.343   40.125 1.00 51.59  ? 347 GLN   A N   1 
ATOM   2625 C  CA  A GLN   A  1  334 ? 72.225  0.012   40.657 0.50 52.90  ? 347 GLN   A CA  1 
ATOM   2626 C  CA  B GLN   A  1  334 ? 72.202  0.011   40.657 0.50 52.63  ? 347 GLN   A CA  1 
ATOM   2627 C  C   . GLN   A  1  334 ? 72.341  0.042   42.175 1.00 53.49  ? 347 GLN   A C   1 
ATOM   2628 O  O   . GLN   A  1  334 ? 72.803  1.035   42.742 1.00 48.08  ? 347 GLN   A O   1 
ATOM   2629 C  CB  A GLN   A  1  334 ? 73.218  -0.946  40.001 0.50 59.30  ? 347 GLN   A CB  1 
ATOM   2630 C  CB  B GLN   A  1  334 ? 73.085  -1.047  39.987 0.50 58.95  ? 347 GLN   A CB  1 
ATOM   2631 C  CG  A GLN   A  1  334 ? 72.778  -1.352  38.597 0.50 67.08  ? 347 GLN   A CG  1 
ATOM   2632 C  CG  B GLN   A  1  334 ? 72.693  -1.302  38.533 0.50 64.81  ? 347 GLN   A CG  1 
ATOM   2633 C  CD  A GLN   A  1  334 ? 73.303  -0.493  37.469 0.50 66.88  ? 347 GLN   A CD  1 
ATOM   2634 C  CD  B GLN   A  1  334 ? 72.429  -2.763  38.218 0.50 62.95  ? 347 GLN   A CD  1 
ATOM   2635 O  OE1 A GLN   A  1  334 ? 74.052  0.471   37.659 0.50 66.53  ? 347 GLN   A OE1 1 
ATOM   2636 O  OE1 B GLN   A  1  334 ? 72.314  -3.617  39.107 0.50 65.31  ? 347 GLN   A OE1 1 
ATOM   2637 N  NE2 A GLN   A  1  334 ? 72.907  -0.869  36.262 0.50 64.43  ? 347 GLN   A NE2 1 
ATOM   2638 N  NE2 B GLN   A  1  334 ? 72.310  -3.062  36.936 0.50 58.31  ? 347 GLN   A NE2 1 
ATOM   2639 N  N   . LEU   A  1  335 ? 71.937  -1.066  42.818 1.00 54.06  ? 348 LEU   A N   1 
ATOM   2640 C  CA  . LEU   A  1  335 ? 71.904  -1.145  44.274 1.00 66.26  ? 348 LEU   A CA  1 
ATOM   2641 C  C   . LEU   A  1  335 ? 73.315  -1.032  44.893 1.00 64.49  ? 348 LEU   A C   1 
ATOM   2642 O  O   . LEU   A  1  335 ? 74.218  -1.669  44.340 1.00 61.96  ? 348 LEU   A O   1 
ATOM   2643 C  CB  . LEU   A  1  335 ? 71.191  -2.423  44.715 1.00 60.78  ? 348 LEU   A CB  1 
ATOM   2644 C  CG  . LEU   A  1  335 ? 69.667  -2.414  44.555 1.00 64.98  ? 348 LEU   A CG  1 
ATOM   2645 C  CD1 . LEU   A  1  335 ? 69.042  -3.750  44.931 1.00 60.40  ? 348 LEU   A CD1 1 
ATOM   2646 C  CD2 . LEU   A  1  335 ? 69.039  -1.279  45.370 1.00 66.17  ? 348 LEU   A CD2 1 
ATOM   2647 N  N   . GLN   B  1  1   ? 0.027   19.021  57.645 1.00 155.23 ? 14  GLN   B N   1 
ATOM   2648 C  CA  . GLN   B  1  1   ? 0.198   18.625  59.072 1.00 156.71 ? 14  GLN   B CA  1 
ATOM   2649 C  C   . GLN   B  1  1   ? -0.525  17.300  59.325 1.00 147.30 ? 14  GLN   B C   1 
ATOM   2650 O  O   . GLN   B  1  1   ? 0.113   16.270  59.556 1.00 125.60 ? 14  GLN   B O   1 
ATOM   2651 C  CB  . GLN   B  1  1   ? -0.376  19.661  60.044 1.00 159.99 ? 14  GLN   B CB  1 
ATOM   2652 C  CG  . GLN   B  1  1   ? 0.150   21.084  59.885 1.00 150.24 ? 14  GLN   B CG  1 
ATOM   2653 C  CD  . GLN   B  1  1   ? -0.748  22.096  60.564 1.00 143.05 ? 14  GLN   B CD  1 
ATOM   2654 O  OE1 . GLN   B  1  1   ? -1.652  21.742  61.330 1.00 128.86 ? 14  GLN   B OE1 1 
ATOM   2655 N  NE2 . GLN   B  1  1   ? -0.512  23.369  60.284 1.00 140.01 ? 14  GLN   B NE2 1 
ATOM   2656 N  N   . GLY   B  1  2   ? -1.869  17.349  59.248 1.00 130.30 ? 15  GLY   B N   1 
ATOM   2657 C  CA  . GLY   B  1  2   ? -2.729  16.209  59.512 1.00 97.07  ? 15  GLY   B CA  1 
ATOM   2658 C  C   . GLY   B  1  2   ? -3.326  15.670  58.216 1.00 79.38  ? 15  GLY   B C   1 
ATOM   2659 O  O   . GLY   B  1  2   ? -3.824  16.427  57.388 1.00 78.52  ? 15  GLY   B O   1 
ATOM   2660 N  N   . VAL   B  1  3   ? -3.307  14.343  58.093 1.00 70.75  ? 16  VAL   B N   1 
ATOM   2661 C  CA  . VAL   B  1  3   ? -3.706  13.646  56.888 1.00 76.22  ? 16  VAL   B CA  1 
ATOM   2662 C  C   . VAL   B  1  3   ? -5.041  12.954  57.147 1.00 57.93  ? 16  VAL   B C   1 
ATOM   2663 O  O   . VAL   B  1  3   ? -5.340  12.596  58.278 1.00 61.01  ? 16  VAL   B O   1 
ATOM   2664 C  CB  . VAL   B  1  3   ? -2.563  12.659  56.552 1.00 84.18  ? 16  VAL   B CB  1 
ATOM   2665 C  CG1 . VAL   B  1  3   ? -2.946  11.626  55.498 1.00 84.78  ? 16  VAL   B CG1 1 
ATOM   2666 C  CG2 . VAL   B  1  3   ? -1.305  13.405  56.120 1.00 83.53  ? 16  VAL   B CG2 1 
ATOM   2667 N  N   . ASP   B  1  4   ? -5.815  12.756  56.078 1.00 58.19  ? 17  ASP   B N   1 
ATOM   2668 C  CA  . ASP   B  1  4   ? -6.985  11.898  56.075 1.00 73.00  ? 17  ASP   B CA  1 
ATOM   2669 C  C   . ASP   B  1  4   ? -6.572  10.545  55.477 1.00 76.36  ? 17  ASP   B C   1 
ATOM   2670 O  O   . ASP   B  1  4   ? -6.421  10.426  54.257 1.00 74.15  ? 17  ASP   B O   1 
ATOM   2671 C  CB  . ASP   B  1  4   ? -8.113  12.619  55.343 1.00 82.49  ? 17  ASP   B CB  1 
ATOM   2672 C  CG  . ASP   B  1  4   ? -9.517  12.079  55.567 1.00 93.68  ? 17  ASP   B CG  1 
ATOM   2673 O  OD1 . ASP   B  1  4   ? -9.780  11.659  56.720 1.00 113.82 ? 17  ASP   B OD1 1 
ATOM   2674 O  OD2 . ASP   B  1  4   ? -10.309 12.042  54.587 1.00 83.58  ? 17  ASP   B OD2 1 
ATOM   2675 N  N   . PRO   B  1  5   ? -6.361  9.480   56.302 1.00 80.17  ? 18  PRO   B N   1 
ATOM   2676 C  CA  . PRO   B  1  5   ? -5.711  8.246   55.834 1.00 71.93  ? 18  PRO   B CA  1 
ATOM   2677 C  C   . PRO   B  1  5   ? -6.633  7.360   55.013 1.00 58.81  ? 18  PRO   B C   1 
ATOM   2678 O  O   . PRO   B  1  5   ? -7.673  6.959   55.515 1.00 59.70  ? 18  PRO   B O   1 
ATOM   2679 C  CB  . PRO   B  1  5   ? -5.253  7.494   57.093 1.00 71.60  ? 18  PRO   B CB  1 
ATOM   2680 C  CG  . PRO   B  1  5   ? -5.909  8.196   58.236 1.00 77.94  ? 18  PRO   B CG  1 
ATOM   2681 C  CD  . PRO   B  1  5   ? -6.709  9.396   57.729 1.00 79.24  ? 18  PRO   B CD  1 
ATOM   2682 N  N   . PRO   B  1  6   ? -6.246  6.956   53.780 1.00 57.07  ? 19  PRO   B N   1 
ATOM   2683 C  CA  . PRO   B  1  6   ? -7.137  6.208   52.893 1.00 55.51  ? 19  PRO   B CA  1 
ATOM   2684 C  C   . PRO   B  1  6   ? -7.178  4.757   53.340 1.00 51.06  ? 19  PRO   B C   1 
ATOM   2685 O  O   . PRO   B  1  6   ? -6.317  4.324   54.099 1.00 46.44  ? 19  PRO   B O   1 
ATOM   2686 C  CB  . PRO   B  1  6   ? -6.486  6.356   51.522 1.00 57.87  ? 19  PRO   B CB  1 
ATOM   2687 C  CG  . PRO   B  1  6   ? -5.005  6.404   51.848 1.00 60.76  ? 19  PRO   B CG  1 
ATOM   2688 C  CD  . PRO   B  1  6   ? -4.907  7.128   53.194 1.00 59.47  ? 19  PRO   B CD  1 
ATOM   2689 N  N   . PRO   B  1  7   ? -8.181  3.979   52.899 1.00 58.94  ? 20  PRO   B N   1 
ATOM   2690 C  CA  . PRO   B  1  7   ? -8.239  2.565   53.241 1.00 64.32  ? 20  PRO   B CA  1 
ATOM   2691 C  C   . PRO   B  1  7   ? -7.042  1.846   52.634 1.00 58.69  ? 20  PRO   B C   1 
ATOM   2692 O  O   . PRO   B  1  7   ? -6.417  2.341   51.712 1.00 52.54  ? 20  PRO   B O   1 
ATOM   2693 C  CB  . PRO   B  1  7   ? -9.605  2.073   52.699 1.00 65.92  ? 20  PRO   B CB  1 
ATOM   2694 C  CG  . PRO   B  1  7   ? -10.008 3.116   51.691 1.00 70.61  ? 20  PRO   B CG  1 
ATOM   2695 C  CD  . PRO   B  1  7   ? -9.342  4.424   52.117 1.00 67.49  ? 20  PRO   B CD  1 
ATOM   2696 N  N   . PRO   B  1  8   ? -6.669  0.665   53.151 1.00 59.88  ? 21  PRO   B N   1 
ATOM   2697 C  CA  . PRO   B  1  8   ? -5.533  -0.060  52.605 1.00 57.55  ? 21  PRO   B CA  1 
ATOM   2698 C  C   . PRO   B  1  8   ? -5.832  -0.520  51.186 1.00 48.11  ? 21  PRO   B C   1 
ATOM   2699 O  O   . PRO   B  1  8   ? -6.972  -0.803  50.846 1.00 47.91  ? 21  PRO   B O   1 
ATOM   2700 C  CB  . PRO   B  1  8   ? -5.350  -1.234  53.560 1.00 58.66  ? 21  PRO   B CB  1 
ATOM   2701 C  CG  . PRO   B  1  8   ? -6.725  -1.450  54.124 1.00 60.47  ? 21  PRO   B CG  1 
ATOM   2702 C  CD  . PRO   B  1  8   ? -7.334  -0.060  54.241 1.00 58.65  ? 21  PRO   B CD  1 
ATOM   2703 N  N   . PRO   B  1  9   ? -4.787  -0.652  50.348 1.00 45.54  ? 22  PRO   B N   1 
ATOM   2704 C  CA  . PRO   B  1  9   ? -4.909  -1.268  49.034 1.00 41.64  ? 22  PRO   B CA  1 
ATOM   2705 C  C   . PRO   B  1  9   ? -5.434  -2.678  49.199 1.00 39.60  ? 22  PRO   B C   1 
ATOM   2706 O  O   . PRO   B  1  9   ? -5.180  -3.296  50.232 1.00 39.04  ? 22  PRO   B O   1 
ATOM   2707 C  CB  . PRO   B  1  9   ? -3.475  -1.316  48.495 1.00 44.57  ? 22  PRO   B CB  1 
ATOM   2708 C  CG  . PRO   B  1  9   ? -2.716  -0.311  49.300 1.00 46.03  ? 22  PRO   B CG  1 
ATOM   2709 C  CD  . PRO   B  1  9   ? -3.421  -0.194  50.639 1.00 49.06  ? 22  PRO   B CD  1 
ATOM   2710 N  N   . GLY   B  1  10  ? -6.096  -3.172  48.149 1.00 35.89  ? 23  GLY   B N   1 
ATOM   2711 C  CA  . GLY   B  1  10  ? -6.448  -4.577  48.031 1.00 39.27  ? 23  GLY   B CA  1 
ATOM   2712 C  C   . GLY   B  1  10  ? -5.264  -5.350  47.448 1.00 46.29  ? 23  GLY   B C   1 
ATOM   2713 O  O   . GLY   B  1  10  ? -4.162  -4.796  47.327 1.00 39.34  ? 23  GLY   B O   1 
ATOM   2714 N  N   . PRO   B  1  11  ? -5.453  -6.628  47.048 1.00 44.20  ? 24  PRO   B N   1 
ATOM   2715 C  CA  . PRO   B  1  11  ? -4.385  -7.397  46.415 1.00 51.16  ? 24  PRO   B CA  1 
ATOM   2716 C  C   . PRO   B  1  11  ? -3.885  -6.717  45.137 1.00 53.75  ? 24  PRO   B C   1 
ATOM   2717 O  O   . PRO   B  1  11  ? -4.566  -5.881  44.556 1.00 46.97  ? 24  PRO   B O   1 
ATOM   2718 C  CB  . PRO   B  1  11  ? -5.026  -8.762  46.128 1.00 49.93  ? 24  PRO   B CB  1 
ATOM   2719 C  CG  . PRO   B  1  11  ? -6.217  -8.817  47.061 1.00 52.74  ? 24  PRO   B CG  1 
ATOM   2720 C  CD  . PRO   B  1  11  ? -6.706  -7.381  47.154 1.00 48.35  ? 24  PRO   B CD  1 
ATOM   2721 N  N   . PRO   B  1  12  ? -2.656  -7.026  44.674 1.00 61.16  ? 25  PRO   B N   1 
ATOM   2722 C  CA  . PRO   B  1  12  ? -2.194  -6.510  43.382 1.00 58.81  ? 25  PRO   B CA  1 
ATOM   2723 C  C   . PRO   B  1  12  ? -3.008  -7.142  42.247 1.00 54.74  ? 25  PRO   B C   1 
ATOM   2724 O  O   . PRO   B  1  12  ? -3.449  -8.295  42.365 1.00 45.04  ? 25  PRO   B O   1 
ATOM   2725 C  CB  . PRO   B  1  12  ? -0.713  -6.896  43.379 1.00 56.59  ? 25  PRO   B CB  1 
ATOM   2726 C  CG  . PRO   B  1  12  ? -0.663  -8.150  44.246 1.00 60.30  ? 25  PRO   B CG  1 
ATOM   2727 C  CD  . PRO   B  1  12  ? -1.681  -7.905  45.342 1.00 56.53  ? 25  PRO   B CD  1 
ATOM   2728 N  N   . SER   B  1  13  ? -3.253  -6.342  41.193 1.00 51.90  ? 26  SER   B N   1 
ATOM   2729 C  CA  . SER   B  1  13  ? -3.901  -6.796  39.965 1.00 56.79  ? 26  SER   B CA  1 
ATOM   2730 C  C   . SER   B  1  13  ? -3.281  -8.104  39.467 1.00 56.33  ? 26  SER   B C   1 
ATOM   2731 O  O   . SER   B  1  13  ? -3.997  -9.062  39.184 1.00 50.09  ? 26  SER   B O   1 
ATOM   2732 C  CB  . SER   B  1  13  ? -3.777  -5.747  38.873 1.00 65.68  ? 26  SER   B CB  1 
ATOM   2733 O  OG  . SER   B  1  13  ? -4.090  -4.431  39.326 1.00 71.03  ? 26  SER   B OG  1 
ATOM   2734 N  N   . PHE   B  1  14  ? -1.939  -8.119  39.351 1.00 45.42  ? 27  PHE   B N   1 
ATOM   2735 C  CA  . PHE   B  1  14  ? -1.194  -9.287  38.906 1.00 47.63  ? 27  PHE   B CA  1 
ATOM   2736 C  C   . PHE   B  1  14  ? -0.551  -9.954  40.124 1.00 40.26  ? 27  PHE   B C   1 
ATOM   2737 O  O   . PHE   B  1  14  ? 0.183   -9.285  40.851 1.00 35.94  ? 27  PHE   B O   1 
ATOM   2738 C  CB  . PHE   B  1  14  ? -0.132  -8.870  37.873 1.00 49.54  ? 27  PHE   B CB  1 
ATOM   2739 C  CG  . PHE   B  1  14  ? 0.756   -10.031 37.432 1.00 49.12  ? 27  PHE   B CG  1 
ATOM   2740 C  CD1 . PHE   B  1  14  ? 0.227   -11.063 36.655 1.00 48.26  ? 27  PHE   B CD1 1 
ATOM   2741 C  CD2 . PHE   B  1  14  ? 2.096   -10.111 37.813 1.00 46.40  ? 27  PHE   B CD2 1 
ATOM   2742 C  CE1 . PHE   B  1  14  ? 1.012   -12.141 36.267 1.00 49.57  ? 27  PHE   B CE1 1 
ATOM   2743 C  CE2 . PHE   B  1  14  ? 2.884   -11.197 37.427 1.00 47.08  ? 27  PHE   B CE2 1 
ATOM   2744 C  CZ  . PHE   B  1  14  ? 2.343   -12.206 36.648 1.00 45.80  ? 27  PHE   B CZ  1 
ATOM   2745 N  N   . THR   B  1  15  ? -0.807  -11.259 40.313 1.00 40.40  ? 28  THR   B N   1 
ATOM   2746 C  CA  . THR   B  1  15  ? -0.386  -11.962 41.518 1.00 45.32  ? 28  THR   B CA  1 
ATOM   2747 C  C   . THR   B  1  15  ? 0.606   -13.074 41.188 1.00 46.16  ? 28  THR   B C   1 
ATOM   2748 O  O   . THR   B  1  15  ? 0.865   -13.926 42.045 1.00 48.85  ? 28  THR   B O   1 
ATOM   2749 C  CB  . THR   B  1  15  ? -1.585  -12.560 42.270 1.00 48.30  ? 28  THR   B CB  1 
ATOM   2750 O  OG1 . THR   B  1  15  ? -2.129  -13.649 41.526 1.00 41.07  ? 28  THR   B OG1 1 
ATOM   2751 C  CG2 . THR   B  1  15  ? -2.679  -11.548 42.546 1.00 52.02  ? 28  THR   B CG2 1 
ATOM   2752 N  N   . GLY   B  1  16  ? 1.113   -13.114 39.944 1.00 43.01  ? 29  GLY   B N   1 
ATOM   2753 C  CA  . GLY   B  1  16  ? 2.075   -14.142 39.568 1.00 40.95  ? 29  GLY   B CA  1 
ATOM   2754 C  C   . GLY   B  1  16  ? 3.512   -13.747 39.940 1.00 42.68  ? 29  GLY   B C   1 
ATOM   2755 O  O   . GLY   B  1  16  ? 3.742   -12.665 40.495 1.00 38.22  ? 29  GLY   B O   1 
ATOM   2756 N  N   . THR   B  1  17  ? 4.470   -14.634 39.615 1.00 42.32  ? 30  THR   B N   1 
ATOM   2757 C  CA  . THR   B  1  17  ? 5.887   -14.358 39.781 1.00 43.96  ? 30  THR   B CA  1 
ATOM   2758 C  C   . THR   B  1  17  ? 6.313   -13.284 38.787 1.00 40.75  ? 30  THR   B C   1 
ATOM   2759 O  O   . THR   B  1  17  ? 5.699   -13.115 37.753 1.00 42.11  ? 30  THR   B O   1 
ATOM   2760 C  CB  . THR   B  1  17  ? 6.756   -15.606 39.598 1.00 47.72  ? 30  THR   B CB  1 
ATOM   2761 O  OG1 . THR   B  1  17  ? 8.035   -15.143 40.052 1.00 42.76  ? 30  THR   B OG1 1 
ATOM   2762 C  CG2 . THR   B  1  17  ? 6.790   -16.093 38.160 1.00 40.99  ? 30  THR   B CG2 1 
ATOM   2763 N  N   . LYS   B  1  18  ? 7.375   -12.562 39.134 1.00 42.73  ? 31  LYS   B N   1 
ATOM   2764 C  CA  . LYS   B  1  18  ? 7.970   -11.572 38.251 1.00 42.54  ? 31  LYS   B CA  1 
ATOM   2765 C  C   . LYS   B  1  18  ? 9.299   -11.128 38.848 1.00 39.12  ? 31  LYS   B C   1 
ATOM   2766 O  O   . LYS   B  1  18  ? 9.560   -11.351 40.029 1.00 41.66  ? 31  LYS   B O   1 
ATOM   2767 C  CB  . LYS   B  1  18  ? 7.105   -10.323 38.043 1.00 43.38  ? 31  LYS   B CB  1 
ATOM   2768 C  CG  . LYS   B  1  18  ? 6.784   -9.519  39.305 1.00 51.25  ? 31  LYS   B CG  1 
ATOM   2769 C  CD  . LYS   B  1  18  ? 6.003   -8.244  39.006 1.00 54.18  ? 31  LYS   B CD  1 
ATOM   2770 C  CE  . LYS   B  1  18  ? 6.303   -7.114  39.932 1.00 65.67  ? 31  LYS   B CE  1 
ATOM   2771 N  NZ  . LYS   B  1  18  ? 5.630   -5.894  39.475 1.00 71.34  ? 31  LYS   B NZ  1 
ATOM   2772 N  N   . LEU   B  1  19  ? 10.119  -10.501 38.007 1.00 39.19  ? 32  LEU   B N   1 
ATOM   2773 C  CA  . LEU   B  1  19  ? 11.402  -9.981  38.420 1.00 41.74  ? 32  LEU   B CA  1 
ATOM   2774 C  C   . LEU   B  1  19  ? 11.139  -8.778  39.316 1.00 40.61  ? 32  LEU   B C   1 
ATOM   2775 O  O   . LEU   B  1  19  ? 10.468  -7.836  38.893 1.00 39.30  ? 32  LEU   B O   1 
ATOM   2776 C  CB  . LEU   B  1  19  ? 12.249  -9.601  37.202 1.00 41.63  ? 32  LEU   B CB  1 
ATOM   2777 C  CG  . LEU   B  1  19  ? 13.568  -8.879  37.522 1.00 41.21  ? 32  LEU   B CG  1 
ATOM   2778 C  CD1 . LEU   B  1  19  ? 14.495  -9.862  38.246 1.00 39.34  ? 32  LEU   B CD1 1 
ATOM   2779 C  CD2 . LEU   B  1  19  ? 14.216  -8.261  36.273 1.00 43.61  ? 32  LEU   B CD2 1 
ATOM   2780 N  N   . VAL   B  1  20  ? 11.681  -8.804  40.542 1.00 37.14  ? 33  VAL   B N   1 
ATOM   2781 C  CA  . VAL   B  1  20  ? 11.467  -7.694  41.442 1.00 38.71  ? 33  VAL   B CA  1 
ATOM   2782 C  C   . VAL   B  1  20  ? 12.768  -6.940  41.654 1.00 39.08  ? 33  VAL   B C   1 
ATOM   2783 O  O   . VAL   B  1  20  ? 12.735  -5.739  41.957 1.00 37.37  ? 33  VAL   B O   1 
ATOM   2784 C  CB  . VAL   B  1  20  ? 10.829  -8.111  42.778 1.00 40.42  ? 33  VAL   B CB  1 
ATOM   2785 C  CG1 . VAL   B  1  20  ? 9.432   -8.641  42.545 1.00 44.25  ? 33  VAL   B CG1 1 
ATOM   2786 C  CG2 . VAL   B  1  20  ? 11.642  -9.121  43.561 1.00 42.05  ? 33  VAL   B CG2 1 
ATOM   2787 N  N   . ASN   B  1  21  ? 13.902  -7.641  41.501 1.00 40.30  ? 34  ASN   B N   1 
ATOM   2788 C  CA  . ASN   B  1  21  ? 15.202  -6.987  41.536 1.00 42.02  ? 34  ASN   B CA  1 
ATOM   2789 C  C   . ASN   B  1  21  ? 15.514  -6.420  40.148 1.00 44.08  ? 34  ASN   B C   1 
ATOM   2790 O  O   . ASN   B  1  21  ? 16.271  -7.011  39.393 1.00 44.07  ? 34  ASN   B O   1 
ATOM   2791 C  CB  . ASN   B  1  21  ? 16.259  -7.967  42.014 1.00 39.63  ? 34  ASN   B CB  1 
ATOM   2792 C  CG  . ASN   B  1  21  ? 17.610  -7.329  42.236 1.00 41.14  ? 34  ASN   B CG  1 
ATOM   2793 O  OD1 . ASN   B  1  21  ? 17.794  -6.113  42.065 1.00 39.71  ? 34  ASN   B OD1 1 
ATOM   2794 N  ND2 . ASN   B  1  21  ? 18.559  -8.153  42.658 1.00 41.83  ? 34  ASN   B ND2 1 
ATOM   2795 N  N   . ASP   B  1  22  ? 14.939  -5.259  39.827 1.00 44.80  ? 35  ASP   B N   1 
ATOM   2796 C  CA  . ASP   B  1  22  ? 14.961  -4.737  38.468 1.00 47.01  ? 35  ASP   B CA  1 
ATOM   2797 C  C   . ASP   B  1  22  ? 15.588  -3.347  38.448 1.00 43.54  ? 35  ASP   B C   1 
ATOM   2798 O  O   . ASP   B  1  22  ? 16.010  -2.839  39.471 1.00 46.41  ? 35  ASP   B O   1 
ATOM   2799 C  CB  . ASP   B  1  22  ? 13.562  -4.777  37.870 1.00 53.24  ? 35  ASP   B CB  1 
ATOM   2800 C  CG  . ASP   B  1  22  ? 12.477  -3.935  38.547 1.00 48.26  ? 35  ASP   B CG  1 
ATOM   2801 O  OD1 . ASP   B  1  22  ? 12.799  -3.095  39.411 1.00 51.11  ? 35  ASP   B OD1 1 
ATOM   2802 O  OD2 . ASP   B  1  22  ? 11.307  -4.103  38.153 1.00 57.89  ? 35  ASP   B OD2 1 
ATOM   2803 N  N   . ALA   B  1  23  ? 15.621  -2.724  37.270 1.00 51.09  ? 36  ALA   B N   1 
ATOM   2804 C  CA  . ALA   B  1  23  ? 16.372  -1.491  37.086 1.00 55.50  ? 36  ALA   B CA  1 
ATOM   2805 C  C   . ALA   B  1  23  ? 15.655  -0.314  37.724 1.00 47.34  ? 36  ALA   B C   1 
ATOM   2806 O  O   . ALA   B  1  23  ? 16.331  0.606   38.172 1.00 49.98  ? 36  ALA   B O   1 
ATOM   2807 C  CB  . ALA   B  1  23  ? 16.632  -1.228  35.619 1.00 65.80  ? 36  ALA   B CB  1 
ATOM   2808 N  N   . ASP   B  1  24  ? 14.317  -0.357  37.815 1.00 50.53  ? 37  ASP   B N   1 
ATOM   2809 C  CA  . ASP   B  1  24  ? 13.602  0.693   38.540 1.00 56.22  ? 37  ASP   B CA  1 
ATOM   2810 C  C   . ASP   B  1  24  ? 13.800  0.586   40.054 1.00 54.16  ? 37  ASP   B C   1 
ATOM   2811 O  O   . ASP   B  1  24  ? 13.570  1.574   40.761 1.00 46.97  ? 37  ASP   B O   1 
ATOM   2812 C  CB  . ASP   B  1  24  ? 12.120  0.735   38.213 1.00 63.17  ? 37  ASP   B CB  1 
ATOM   2813 C  CG  . ASP   B  1  24  ? 11.724  1.564   37.005 1.00 70.63  ? 37  ASP   B CG  1 
ATOM   2814 O  OD1 . ASP   B  1  24  ? 12.514  2.444   36.588 1.00 75.95  ? 37  ASP   B OD1 1 
ATOM   2815 O  OD2 . ASP   B  1  24  ? 10.608  1.324   36.535 1.00 103.24 ? 37  ASP   B OD2 1 
ATOM   2816 N  N   . HIS   B  1  25  ? 14.252  -0.585  40.552 1.00 49.78  ? 38  HIS   B N   1 
ATOM   2817 C  CA  . HIS   B  1  25  ? 14.301  -0.840  41.986 1.00 49.34  ? 38  HIS   B CA  1 
ATOM   2818 C  C   . HIS   B  1  25  ? 15.685  -1.363  42.377 1.00 52.48  ? 38  HIS   B C   1 
ATOM   2819 O  O   . HIS   B  1  25  ? 15.868  -2.491  42.850 1.00 54.04  ? 38  HIS   B O   1 
ATOM   2820 C  CB  . HIS   B  1  25  ? 13.162  -1.781  42.362 1.00 46.82  ? 38  HIS   B CB  1 
ATOM   2821 C  CG  . HIS   B  1  25  ? 11.800  -1.222  42.128 1.00 48.62  ? 38  HIS   B CG  1 
ATOM   2822 N  ND1 . HIS   B  1  25  ? 10.990  -1.680  41.112 1.00 48.51  ? 38  HIS   B ND1 1 
ATOM   2823 C  CD2 . HIS   B  1  25  ? 11.084  -0.308  42.827 1.00 46.13  ? 38  HIS   B CD2 1 
ATOM   2824 C  CE1 . HIS   B  1  25  ? 9.820   -1.047  41.178 1.00 55.13  ? 38  HIS   B CE1 1 
ATOM   2825 N  NE2 . HIS   B  1  25  ? 9.859   -0.209  42.204 1.00 51.93  ? 38  HIS   B NE2 1 
ATOM   2826 N  N   . PRO   B  1  26  ? 16.728  -0.537  42.167 1.00 52.21  ? 39  PRO   B N   1 
ATOM   2827 C  CA  . PRO   B  1  26  ? 18.092  -0.959  42.438 1.00 44.52  ? 39  PRO   B CA  1 
ATOM   2828 C  C   . PRO   B  1  26  ? 18.481  -0.824  43.889 1.00 42.10  ? 39  PRO   B C   1 
ATOM   2829 O  O   . PRO   B  1  26  ? 18.106  0.130   44.559 1.00 44.53  ? 39  PRO   B O   1 
ATOM   2830 C  CB  . PRO   B  1  26  ? 18.918  -0.000  41.579 1.00 50.13  ? 39  PRO   B CB  1 
ATOM   2831 C  CG  . PRO   B  1  26  ? 18.100  1.283   41.577 1.00 49.93  ? 39  PRO   B CG  1 
ATOM   2832 C  CD  . PRO   B  1  26  ? 16.653  0.828   41.613 1.00 48.92  ? 39  PRO   B CD  1 
ATOM   2833 N  N   . TRP   B  1  27  ? 19.327  -1.743  44.338 1.00 38.12  ? 40  TRP   B N   1 
ATOM   2834 C  CA  . TRP   B  1  27  ? 19.895  -1.604  45.657 1.00 34.55  ? 40  TRP   B CA  1 
ATOM   2835 C  C   . TRP   B  1  27  ? 20.762  -0.351  45.671 1.00 33.14  ? 40  TRP   B C   1 
ATOM   2836 O  O   . TRP   B  1  27  ? 21.456  -0.079  44.709 1.00 38.04  ? 40  TRP   B O   1 
ATOM   2837 C  CB  . TRP   B  1  27  ? 20.701  -2.858  46.007 1.00 31.26  ? 40  TRP   B CB  1 
ATOM   2838 C  CG  . TRP   B  1  27  ? 21.279  -2.802  47.379 1.00 30.16  ? 40  TRP   B CG  1 
ATOM   2839 C  CD1 . TRP   B  1  27  ? 20.677  -3.253  48.516 1.00 33.73  ? 40  TRP   B CD1 1 
ATOM   2840 C  CD2 . TRP   B  1  27  ? 22.521  -2.191  47.779 1.00 35.05  ? 40  TRP   B CD2 1 
ATOM   2841 N  NE1 . TRP   B  1  27  ? 21.485  -3.006  49.587 1.00 37.43  ? 40  TRP   B NE1 1 
ATOM   2842 C  CE2 . TRP   B  1  27  ? 22.618  -2.349  49.169 1.00 31.37  ? 40  TRP   B CE2 1 
ATOM   2843 C  CE3 . TRP   B  1  27  ? 23.557  -1.533  47.100 1.00 38.32  ? 40  TRP   B CE3 1 
ATOM   2844 C  CZ2 . TRP   B  1  27  ? 23.699  -1.864  49.895 1.00 36.64  ? 40  TRP   B CZ2 1 
ATOM   2845 C  CZ3 . TRP   B  1  27  ? 24.625  -1.047  47.819 1.00 34.43  ? 40  TRP   B CZ3 1 
ATOM   2846 C  CH2 . TRP   B  1  27  ? 24.686  -1.201  49.203 1.00 38.87  ? 40  TRP   B CH2 1 
ATOM   2847 N  N   . GLN   B  1  28  ? 20.700  0.412   46.756 1.00 36.48  ? 41  GLN   B N   1 
ATOM   2848 C  CA  . GLN   B  1  28  ? 21.574  1.550   46.950 1.00 35.74  ? 41  GLN   B CA  1 
ATOM   2849 C  C   . GLN   B  1  28  ? 21.993  1.584   48.401 1.00 36.59  ? 41  GLN   B C   1 
ATOM   2850 O  O   . GLN   B  1  28  ? 21.274  1.138   49.275 1.00 41.91  ? 41  GLN   B O   1 
ATOM   2851 C  CB  . GLN   B  1  28  ? 20.924  2.880   46.590 1.00 36.07  ? 41  GLN   B CB  1 
ATOM   2852 C  CG  . GLN   B  1  28  ? 20.588  3.009   45.112 1.00 36.51  ? 41  GLN   B CG  1 
ATOM   2853 C  CD  . GLN   B  1  28  ? 19.812  4.280   44.793 1.00 40.82  ? 41  GLN   B CD  1 
ATOM   2854 O  OE1 . GLN   B  1  28  ? 19.535  5.127   45.662 1.00 41.99  ? 41  GLN   B OE1 1 
ATOM   2855 N  NE2 . GLN   B  1  28  ? 19.384  4.371   43.543 1.00 38.93  ? 41  GLN   B NE2 1 
ATOM   2856 N  N   . PRO   B  1  29  ? 23.201  2.091   48.700 1.00 41.03  ? 42  PRO   B N   1 
ATOM   2857 C  CA  . PRO   B  1  29  ? 23.664  2.170   50.077 1.00 41.86  ? 42  PRO   B CA  1 
ATOM   2858 C  C   . PRO   B  1  29  ? 22.890  3.215   50.884 1.00 43.37  ? 42  PRO   B C   1 
ATOM   2859 O  O   . PRO   B  1  29  ? 22.259  4.097   50.324 1.00 42.49  ? 42  PRO   B O   1 
ATOM   2860 C  CB  . PRO   B  1  29  ? 25.156  2.527   49.919 1.00 43.52  ? 42  PRO   B CB  1 
ATOM   2861 C  CG  . PRO   B  1  29  ? 25.257  3.196   48.576 1.00 45.08  ? 42  PRO   B CG  1 
ATOM   2862 C  CD  . PRO   B  1  29  ? 24.176  2.592   47.723 1.00 42.25  ? 42  PRO   B CD  1 
ATOM   2863 N  N   . LEU   B  1  30  ? 22.984  3.106   52.207 1.00 46.07  ? 43  LEU   B N   1 
ATOM   2864 C  CA  . LEU   B  1  30  ? 22.362  4.045   53.129 1.00 52.82  ? 43  LEU   B CA  1 
ATOM   2865 C  C   . LEU   B  1  30  ? 22.985  5.433   53.000 1.00 56.72  ? 43  LEU   B C   1 
ATOM   2866 O  O   . LEU   B  1  30  ? 24.196  5.566   52.865 1.00 50.31  ? 43  LEU   B O   1 
ATOM   2867 C  CB  . LEU   B  1  30  ? 22.547  3.508   54.543 1.00 51.42  ? 43  LEU   B CB  1 
ATOM   2868 C  CG  . LEU   B  1  30  ? 21.917  2.136   54.805 1.00 55.99  ? 43  LEU   B CG  1 
ATOM   2869 C  CD1 . LEU   B  1  30  ? 22.257  1.657   56.201 1.00 57.80  ? 43  LEU   B CD1 1 
ATOM   2870 C  CD2 . LEU   B  1  30  ? 20.410  2.164   54.554 1.00 53.43  ? 43  LEU   B CD2 1 
ATOM   2871 N  N   . ARG   B  1  31  ? 22.125  6.455   53.036 1.00 62.03  ? 44  ARG   B N   1 
ATOM   2872 C  CA  . ARG   B  1  31  ? 22.529  7.844   53.168 1.00 59.01  ? 44  ARG   B CA  1 
ATOM   2873 C  C   . ARG   B  1  31  ? 22.281  8.308   54.603 1.00 68.28  ? 44  ARG   B C   1 
ATOM   2874 O  O   . ARG   B  1  31  ? 21.673  7.597   55.403 1.00 60.42  ? 44  ARG   B O   1 
ATOM   2875 C  CB  . ARG   B  1  31  ? 21.708  8.757   52.254 1.00 58.36  ? 44  ARG   B CB  1 
ATOM   2876 C  CG  . ARG   B  1  31  ? 21.726  8.447   50.761 1.00 63.14  ? 44  ARG   B CG  1 
ATOM   2877 C  CD  . ARG   B  1  31  ? 20.524  9.027   50.031 1.00 68.72  ? 44  ARG   B CD  1 
ATOM   2878 N  NE  . ARG   B  1  31  ? 19.304  8.708   50.794 1.00 82.70  ? 44  ARG   B NE  1 
ATOM   2879 C  CZ  . ARG   B  1  31  ? 18.031  8.824   50.426 1.00 81.73  ? 44  ARG   B CZ  1 
ATOM   2880 N  NH1 . ARG   B  1  31  ? 17.699  9.052   49.168 1.00 81.62  ? 44  ARG   B NH1 1 
ATOM   2881 N  NH2 . ARG   B  1  31  ? 17.093  8.634   51.332 1.00 75.90  ? 44  ARG   B NH2 1 
ATOM   2882 N  N   . GLU   B  1  32  ? 22.726  9.537   54.885 1.00 85.43  ? 45  GLU   B N   1 
ATOM   2883 C  CA  . GLU   B  1  32  ? 22.491  10.235  56.138 1.00 90.18  ? 45  GLU   B CA  1 
ATOM   2884 C  C   . GLU   B  1  32  ? 21.008  10.185  56.506 1.00 79.07  ? 45  GLU   B C   1 
ATOM   2885 O  O   . GLU   B  1  32  ? 20.142  10.533  55.685 1.00 57.72  ? 45  GLU   B O   1 
ATOM   2886 C  CB  . GLU   B  1  32  ? 22.945  11.689  55.933 1.00 106.53 ? 45  GLU   B CB  1 
ATOM   2887 C  CG  . GLU   B  1  32  ? 22.855  12.584  57.167 1.00 116.30 ? 45  GLU   B CG  1 
ATOM   2888 C  CD  . GLU   B  1  32  ? 23.760  12.187  58.321 1.00 123.09 ? 45  GLU   B CD  1 
ATOM   2889 O  OE1 . GLU   B  1  32  ? 24.436  11.123  58.312 1.00 122.59 ? 45  GLU   B OE1 1 
ATOM   2890 O  OE2 . GLU   B  1  32  ? 23.812  13.019  59.255 1.00 117.18 ? 45  GLU   B OE2 1 
ATOM   2891 N  N   . GLY   B  1  33  ? 20.731  9.716   57.741 1.00 64.97  ? 46  GLY   B N   1 
ATOM   2892 C  CA  . GLY   B  1  33  ? 19.389  9.733   58.316 1.00 68.75  ? 46  GLY   B CA  1 
ATOM   2893 C  C   . GLY   B  1  33  ? 18.408  8.693   57.750 1.00 70.53  ? 46  GLY   B C   1 
ATOM   2894 O  O   . GLY   B  1  33  ? 17.227  8.728   58.091 1.00 74.21  ? 46  GLY   B O   1 
ATOM   2895 N  N   . ASP   B  1  34  ? 18.882  7.775   56.884 1.00 61.17  ? 47  ASP   B N   1 
ATOM   2896 C  CA  . ASP   B  1  34  ? 18.072  6.658   56.421 1.00 56.19  ? 47  ASP   B CA  1 
ATOM   2897 C  C   . ASP   B  1  34  ? 17.837  5.714   57.601 1.00 48.38  ? 47  ASP   B C   1 
ATOM   2898 O  O   . ASP   B  1  34  ? 18.727  5.489   58.408 1.00 46.37  ? 47  ASP   B O   1 
ATOM   2899 C  CB  . ASP   B  1  34  ? 18.708  5.920   55.251 1.00 62.79  ? 47  ASP   B CB  1 
ATOM   2900 C  CG  . ASP   B  1  34  ? 18.636  6.600   53.885 1.00 66.05  ? 47  ASP   B CG  1 
ATOM   2901 O  OD1 . ASP   B  1  34  ? 17.962  7.657   53.770 1.00 68.13  ? 47  ASP   B OD1 1 
ATOM   2902 O  OD2 . ASP   B  1  34  ? 19.266  6.060   52.935 1.00 72.49  ? 47  ASP   B OD2 1 
ATOM   2903 N  N   . ILE   B  1  35  ? 16.614  5.193   57.712 1.00 43.32  ? 48  ILE   B N   1 
ATOM   2904 C  CA  . ILE   B  1  35  ? 16.229  4.374   58.847 1.00 40.23  ? 48  ILE   B CA  1 
ATOM   2905 C  C   . ILE   B  1  35  ? 16.088  2.919   58.401 1.00 32.18  ? 48  ILE   B C   1 
ATOM   2906 O  O   . ILE   B  1  35  ? 15.456  2.611   57.388 1.00 28.51  ? 48  ILE   B O   1 
ATOM   2907 C  CB  . ILE   B  1  35  ? 14.923  4.897   59.463 1.00 43.35  ? 48  ILE   B CB  1 
ATOM   2908 C  CG1 . ILE   B  1  35  ? 15.038  6.367   59.921 1.00 48.39  ? 48  ILE   B CG1 1 
ATOM   2909 C  CG2 . ILE   B  1  35  ? 14.492  3.971   60.595 1.00 42.44  ? 48  ILE   B CG2 1 
ATOM   2910 C  CD1 . ILE   B  1  35  ? 16.016  6.595   61.068 1.00 48.03  ? 48  ILE   B CD1 1 
ATOM   2911 N  N   . ARG   B  1  36  ? 16.663  2.026   59.197 1.00 32.96  ? 49  ARG   B N   1 
ATOM   2912 C  CA  . ARG   B  1  36  ? 16.460  0.603   59.008 1.00 39.44  ? 49  ARG   B CA  1 
ATOM   2913 C  C   . ARG   B  1  36  ? 16.218  0.013   60.387 1.00 38.53  ? 49  ARG   B C   1 
ATOM   2914 O  O   . ARG   B  1  36  ? 16.576  0.636   61.384 1.00 40.91  ? 49  ARG   B O   1 
ATOM   2915 C  CB  . ARG   B  1  36  ? 17.658  -0.048  58.308 1.00 35.53  ? 49  ARG   B CB  1 
ATOM   2916 C  CG  . ARG   B  1  36  ? 17.916  0.494   56.908 1.00 34.87  ? 49  ARG   B CG  1 
ATOM   2917 C  CD  . ARG   B  1  36  ? 16.864  0.076   55.945 1.00 35.62  ? 49  ARG   B CD  1 
ATOM   2918 N  NE  . ARG   B  1  36  ? 17.155  0.527   54.582 1.00 37.38  ? 49  ARG   B NE  1 
ATOM   2919 C  CZ  . ARG   B  1  36  ? 16.918  1.733   54.087 1.00 44.32  ? 49  ARG   B CZ  1 
ATOM   2920 N  NH1 . ARG   B  1  36  ? 16.337  2.666   54.834 1.00 45.49  ? 49  ARG   B NH1 1 
ATOM   2921 N  NH2 . ARG   B  1  36  ? 17.241  1.990   52.829 1.00 40.75  ? 49  ARG   B NH2 1 
ATOM   2922 N  N   . GLY   B  1  37  ? 15.611  -1.179  60.427 1.00 40.13  ? 50  GLY   B N   1 
ATOM   2923 C  CA  . GLY   B  1  37  ? 15.134  -1.714  61.689 1.00 40.19  ? 50  GLY   B CA  1 
ATOM   2924 C  C   . GLY   B  1  37  ? 15.151  -3.234  61.711 1.00 40.34  ? 50  GLY   B C   1 
ATOM   2925 O  O   . GLY   B  1  37  ? 15.945  -3.873  61.020 1.00 36.08  ? 50  GLY   B O   1 
ATOM   2926 N  N   . PRO   B  1  38  ? 14.265  -3.853  62.514 1.00 37.14  ? 51  PRO   B N   1 
ATOM   2927 C  CA  . PRO   B  1  38  ? 14.354  -5.282  62.797 1.00 33.08  ? 51  PRO   B CA  1 
ATOM   2928 C  C   . PRO   B  1  38  ? 13.790  -6.192  61.722 1.00 30.39  ? 51  PRO   B C   1 
ATOM   2929 O  O   . PRO   B  1  38  ? 13.940  -7.398  61.827 1.00 33.79  ? 51  PRO   B O   1 
ATOM   2930 C  CB  . PRO   B  1  38  ? 13.539  -5.384  64.075 1.00 35.90  ? 51  PRO   B CB  1 
ATOM   2931 C  CG  . PRO   B  1  38  ? 12.458  -4.351  63.908 1.00 40.43  ? 51  PRO   B CG  1 
ATOM   2932 C  CD  . PRO   B  1  38  ? 13.099  -3.220  63.141 1.00 41.24  ? 51  PRO   B CD  1 
ATOM   2933 N  N   . CYS   B  1  39  ? 13.129  -5.612  60.707 1.00 33.41  ? 52  CYS   B N   1 
ATOM   2934 C  CA  . CYS   B  1  39  ? 12.478  -6.386  59.664 1.00 31.56  ? 52  CYS   B CA  1 
ATOM   2935 C  C   . CYS   B  1  39  ? 13.323  -6.471  58.399 1.00 34.57  ? 52  CYS   B C   1 
ATOM   2936 O  O   . CYS   B  1  39  ? 13.507  -5.472  57.696 1.00 35.47  ? 52  CYS   B O   1 
ATOM   2937 C  CB  . CYS   B  1  39  ? 11.125  -5.819  59.277 1.00 32.29  ? 52  CYS   B CB  1 
ATOM   2938 S  SG  . CYS   B  1  39  ? 10.243  -6.881  58.113 1.00 33.08  ? 52  CYS   B SG  1 
ATOM   2939 N  N   . PRO   B  1  40  ? 13.817  -7.671  58.030 1.00 31.59  ? 53  PRO   B N   1 
ATOM   2940 C  CA  . PRO   B  1  40  ? 14.610  -7.793  56.811 1.00 33.14  ? 53  PRO   B CA  1 
ATOM   2941 C  C   . PRO   B  1  40  ? 13.777  -7.533  55.565 1.00 32.30  ? 53  PRO   B C   1 
ATOM   2942 O  O   . PRO   B  1  40  ? 14.304  -7.057  54.569 1.00 36.53  ? 53  PRO   B O   1 
ATOM   2943 C  CB  . PRO   B  1  40  ? 15.162  -9.238  56.875 1.00 33.24  ? 53  PRO   B CB  1 
ATOM   2944 C  CG  . PRO   B  1  40  ? 14.176  -9.972  57.741 1.00 33.30  ? 53  PRO   B CG  1 
ATOM   2945 C  CD  . PRO   B  1  40  ? 13.670  -8.938  58.758 1.00 31.75  ? 53  PRO   B CD  1 
ATOM   2946 N  N   . GLY   B  1  41  ? 12.465  -7.830  55.625 1.00 32.79  ? 54  GLY   B N   1 
ATOM   2947 C  CA  . GLY   B  1  41  ? 11.579  -7.584  54.493 1.00 29.65  ? 54  GLY   B CA  1 
ATOM   2948 C  C   . GLY   B  1  41  ? 11.479  -6.093  54.162 1.00 30.41  ? 54  GLY   B C   1 
ATOM   2949 O  O   . GLY   B  1  41  ? 11.846  -5.660  53.078 1.00 32.29  ? 54  GLY   B O   1 
ATOM   2950 N  N   . LEU   B  1  42  ? 11.032  -5.306  55.139 1.00 31.90  ? 55  LEU   B N   1 
ATOM   2951 C  CA  . LEU   B  1  42  ? 10.908  -3.869  54.977 1.00 33.39  ? 55  LEU   B CA  1 
ATOM   2952 C  C   . LEU   B  1  42  ? 12.267  -3.237  54.681 1.00 34.92  ? 55  LEU   B C   1 
ATOM   2953 O  O   . LEU   B  1  42  ? 12.348  -2.323  53.873 1.00 32.60  ? 55  LEU   B O   1 
ATOM   2954 C  CB  . LEU   B  1  42  ? 10.276  -3.277  56.236 1.00 33.76  ? 55  LEU   B CB  1 
ATOM   2955 C  CG  . LEU   B  1  42  ? 8.846   -3.749  56.542 1.00 34.26  ? 55  LEU   B CG  1 
ATOM   2956 C  CD1 . LEU   B  1  42  ? 8.313   -3.012  57.753 1.00 39.21  ? 55  LEU   B CD1 1 
ATOM   2957 C  CD2 . LEU   B  1  42  ? 7.891   -3.569  55.403 1.00 34.70  ? 55  LEU   B CD2 1 
ATOM   2958 N  N   . ASN   B  1  43  ? 13.319  -3.686  55.375 1.00 32.21  ? 56  ASN   B N   1 
ATOM   2959 C  CA  . ASN   B  1  43  ? 14.659  -3.170  55.133 1.00 31.92  ? 56  ASN   B CA  1 
ATOM   2960 C  C   . ASN   B  1  43  ? 15.066  -3.357  53.671 1.00 32.37  ? 56  ASN   B C   1 
ATOM   2961 O  O   . ASN   B  1  43  ? 15.564  -2.418  53.053 1.00 31.18  ? 56  ASN   B O   1 
ATOM   2962 C  CB  . ASN   B  1  43  ? 15.684  -3.860  56.010 1.00 32.84  ? 56  ASN   B CB  1 
ATOM   2963 C  CG  . ASN   B  1  43  ? 15.627  -3.405  57.440 1.00 33.27  ? 56  ASN   B CG  1 
ATOM   2964 O  OD1 . ASN   B  1  43  ? 14.993  -2.399  57.788 1.00 33.52  ? 56  ASN   B OD1 1 
ATOM   2965 N  ND2 . ASN   B  1  43  ? 16.313  -4.148  58.284 1.00 33.06  ? 56  ASN   B ND2 1 
ATOM   2966 N  N   . THR   B  1  44  ? 14.819  -4.547  53.116 1.00 31.05  ? 57  THR   B N   1 
ATOM   2967 C  CA  . THR   B  1  44  ? 15.191  -4.807  51.736 1.00 32.24  ? 57  THR   B CA  1 
ATOM   2968 C  C   . THR   B  1  44  ? 14.350  -3.935  50.814 1.00 33.40  ? 57  THR   B C   1 
ATOM   2969 O  O   . THR   B  1  44  ? 14.869  -3.390  49.855 1.00 34.81  ? 57  THR   B O   1 
ATOM   2970 C  CB  . THR   B  1  44  ? 15.027  -6.292  51.414 1.00 28.88  ? 57  THR   B CB  1 
ATOM   2971 O  OG1 . THR   B  1  44  ? 15.941  -6.962  52.268 1.00 29.02  ? 57  THR   B OG1 1 
ATOM   2972 C  CG2 . THR   B  1  44  ? 15.365  -6.614  49.978 1.00 28.64  ? 57  THR   B CG2 1 
ATOM   2973 N  N   . LEU   B  1  45  ? 13.055  -3.805  51.091 1.00 32.80  ? 58  LEU   B N   1 
ATOM   2974 C  CA  . LEU   B  1  45  ? 12.196  -2.982  50.260 1.00 31.83  ? 58  LEU   B CA  1 
ATOM   2975 C  C   . LEU   B  1  45  ? 12.636  -1.515  50.294 1.00 29.92  ? 58  LEU   B C   1 
ATOM   2976 O  O   . LEU   B  1  45  ? 12.639  -0.843  49.269 1.00 30.03  ? 58  LEU   B O   1 
ATOM   2977 C  CB  . LEU   B  1  45  ? 10.755  -3.173  50.692 1.00 32.65  ? 58  LEU   B CB  1 
ATOM   2978 C  CG  . LEU   B  1  45  ? 10.203  -4.584  50.464 1.00 30.84  ? 58  LEU   B CG  1 
ATOM   2979 C  CD1 . LEU   B  1  45  ? 8.914   -4.738  51.236 1.00 32.47  ? 58  LEU   B CD1 1 
ATOM   2980 C  CD2 . LEU   B  1  45  ? 9.942   -4.863  49.006 1.00 29.45  ? 58  LEU   B CD2 1 
ATOM   2981 N  N   . ALA   B  1  46  ? 13.050  -1.016  51.450 1.00 34.14  ? 59  ALA   B N   1 
ATOM   2982 C  CA  . ALA   B  1  46  ? 13.546  0.352   51.525 1.00 39.15  ? 59  ALA   B CA  1 
ATOM   2983 C  C   . ALA   B  1  46  ? 14.846  0.507   50.720 1.00 42.72  ? 59  ALA   B C   1 
ATOM   2984 O  O   . ALA   B  1  46  ? 15.035  1.489   50.008 1.00 46.25  ? 59  ALA   B O   1 
ATOM   2985 C  CB  . ALA   B  1  46  ? 13.733  0.760   52.969 1.00 35.89  ? 59  ALA   B CB  1 
ATOM   2986 N  N   . SER   B  1  47  ? 15.746  -0.471  50.828 1.00 39.34  ? 60  SER   B N   1 
ATOM   2987 C  CA  . SER   B  1  47  ? 17.048  -0.374  50.187 1.00 36.36  ? 60  SER   B CA  1 
ATOM   2988 C  C   . SER   B  1  47  ? 16.985  -0.589  48.677 1.00 35.53  ? 60  SER   B C   1 
ATOM   2989 O  O   . SER   B  1  47  ? 17.958  -0.256  48.010 1.00 36.63  ? 60  SER   B O   1 
ATOM   2990 C  CB  . SER   B  1  47  ? 18.044  -1.273  50.830 1.00 33.41  ? 60  SER   B CB  1 
ATOM   2991 O  OG  . SER   B  1  47  ? 18.490  -0.700  52.050 1.00 32.31  ? 60  SER   B OG  1 
ATOM   2992 N  N   . HIS   B  1  48  ? 15.871  -1.118  48.154 1.00 35.49  ? 61  HIS   B N   1 
ATOM   2993 C  CA  . HIS   B  1  48  ? 15.650  -1.202  46.717 1.00 34.58  ? 61  HIS   B CA  1 
ATOM   2994 C  C   . HIS   B  1  48  ? 14.625  -0.174  46.210 1.00 36.61  ? 61  HIS   B C   1 
ATOM   2995 O  O   . HIS   B  1  48  ? 14.236  -0.219  45.044 1.00 34.85  ? 61  HIS   B O   1 
ATOM   2996 C  CB  . HIS   B  1  48  ? 15.159  -2.597  46.320 1.00 34.28  ? 61  HIS   B CB  1 
ATOM   2997 C  CG  . HIS   B  1  48  ? 16.244  -3.615  46.258 1.00 38.00  ? 61  HIS   B CG  1 
ATOM   2998 N  ND1 . HIS   B  1  48  ? 16.862  -3.976  45.080 1.00 34.52  ? 61  HIS   B ND1 1 
ATOM   2999 C  CD2 . HIS   B  1  48  ? 16.811  -4.365  47.217 1.00 34.50  ? 61  HIS   B CD2 1 
ATOM   3000 C  CE1 . HIS   B  1  48  ? 17.765  -4.903  45.342 1.00 35.57  ? 61  HIS   B CE1 1 
ATOM   3001 N  NE2 . HIS   B  1  48  ? 17.738  -5.163  46.630 1.00 35.04  ? 61  HIS   B NE2 1 
ATOM   3002 N  N   . GLY   B  1  49  ? 14.166  0.745   47.066 1.00 44.87  ? 62  GLY   B N   1 
ATOM   3003 C  CA  . GLY   B  1  49  ? 13.281  1.819   46.632 1.00 48.57  ? 62  GLY   B CA  1 
ATOM   3004 C  C   . GLY   B  1  49  ? 11.830  1.387   46.382 1.00 46.70  ? 62  GLY   B C   1 
ATOM   3005 O  O   . GLY   B  1  49  ? 11.073  2.156   45.807 1.00 54.32  ? 62  GLY   B O   1 
ATOM   3006 N  N   . TYR   B  1  50  ? 11.427  0.183   46.822 1.00 43.78  ? 63  TYR   B N   1 
ATOM   3007 C  CA  . TYR   B  1  50  ? 10.025  -0.192  46.863 1.00 40.85  ? 63  TYR   B CA  1 
ATOM   3008 C  C   . TYR   B  1  50  ? 9.266   0.643   47.903 1.00 40.05  ? 63  TYR   B C   1 
ATOM   3009 O  O   . TYR   B  1  50  ? 8.082   0.891   47.735 1.00 34.51  ? 63  TYR   B O   1 
ATOM   3010 C  CB  . TYR   B  1  50  ? 9.890   -1.688  47.156 1.00 40.76  ? 63  TYR   B CB  1 
ATOM   3011 C  CG  . TYR   B  1  50  ? 10.002  -2.513  45.884 1.00 40.73  ? 63  TYR   B CG  1 
ATOM   3012 C  CD1 . TYR   B  1  50  ? 8.942   -2.624  44.995 1.00 36.48  ? 63  TYR   B CD1 1 
ATOM   3013 C  CD2 . TYR   B  1  50  ? 11.192  -3.153  45.562 1.00 40.50  ? 63  TYR   B CD2 1 
ATOM   3014 C  CE1 . TYR   B  1  50  ? 9.058   -3.353  43.824 1.00 43.67  ? 63  TYR   B CE1 1 
ATOM   3015 C  CE2 . TYR   B  1  50  ? 11.310  -3.898  44.402 1.00 37.73  ? 63  TYR   B CE2 1 
ATOM   3016 C  CZ  . TYR   B  1  50  ? 10.250  -3.993  43.524 1.00 38.72  ? 63  TYR   B CZ  1 
ATOM   3017 O  OH  . TYR   B  1  50  ? 10.393  -4.708  42.369 1.00 36.57  ? 63  TYR   B OH  1 
ATOM   3018 N  N   . LEU   B  1  51  ? 9.951   0.955   49.002 1.00 39.79  ? 64  LEU   B N   1 
ATOM   3019 C  CA  . LEU   B  1  51  ? 9.557   1.920   50.005 1.00 43.35  ? 64  LEU   B CA  1 
ATOM   3020 C  C   . LEU   B  1  51  ? 10.475  3.123   49.859 1.00 50.28  ? 64  LEU   B C   1 
ATOM   3021 O  O   . LEU   B  1  51  ? 11.576  2.995   49.342 1.00 52.59  ? 64  LEU   B O   1 
ATOM   3022 C  CB  . LEU   B  1  51  ? 9.775   1.352   51.410 1.00 43.30  ? 64  LEU   B CB  1 
ATOM   3023 C  CG  . LEU   B  1  51  ? 8.847   0.218   51.846 1.00 45.45  ? 64  LEU   B CG  1 
ATOM   3024 C  CD1 . LEU   B  1  51  ? 9.257   -0.364  53.168 1.00 45.29  ? 64  LEU   B CD1 1 
ATOM   3025 C  CD2 . LEU   B  1  51  ? 7.441   0.742   51.927 1.00 46.73  ? 64  LEU   B CD2 1 
ATOM   3026 N  N   . PRO   B  1  52  ? 10.094  4.306   50.382 1.00 53.19  ? 65  PRO   B N   1 
ATOM   3027 C  CA  . PRO   B  1  52  ? 11.028  5.417   50.515 1.00 49.78  ? 65  PRO   B CA  1 
ATOM   3028 C  C   . PRO   B  1  52  ? 12.337  4.949   51.144 1.00 51.74  ? 65  PRO   B C   1 
ATOM   3029 O  O   . PRO   B  1  52  ? 12.341  4.240   52.145 1.00 45.89  ? 65  PRO   B O   1 
ATOM   3030 C  CB  . PRO   B  1  52  ? 10.250  6.405   51.404 1.00 50.40  ? 65  PRO   B CB  1 
ATOM   3031 C  CG  . PRO   B  1  52  ? 8.800   6.130   51.088 1.00 50.09  ? 65  PRO   B CG  1 
ATOM   3032 C  CD  . PRO   B  1  52  ? 8.734   4.641   50.840 1.00 53.09  ? 65  PRO   B CD  1 
ATOM   3033 N  N   . ARG   B  1  53  ? 13.459  5.383   50.562 1.00 48.32  ? 66  ARG   B N   1 
ATOM   3034 C  CA  . ARG   B  1  53  ? 14.766  4.859   50.926 1.00 39.63  ? 66  ARG   B CA  1 
ATOM   3035 C  C   . ARG   B  1  53  ? 15.172  5.312   52.311 1.00 40.44  ? 66  ARG   B C   1 
ATOM   3036 O  O   . ARG   B  1  53  ? 16.087  4.730   52.902 1.00 42.01  ? 66  ARG   B O   1 
ATOM   3037 C  CB  . ARG   B  1  53  ? 15.805  5.244   49.867 1.00 44.21  ? 66  ARG   B CB  1 
ATOM   3038 C  CG  . ARG   B  1  53  ? 15.510  4.601   48.519 1.00 39.59  ? 66  ARG   B CG  1 
ATOM   3039 C  CD  . ARG   B  1  53  ? 16.613  4.868   47.507 1.00 42.00  ? 66  ARG   B CD  1 
ATOM   3040 N  NE  . ARG   B  1  53  ? 16.290  4.200   46.242 1.00 39.48  ? 66  ARG   B NE  1 
ATOM   3041 C  CZ  . ARG   B  1  53  ? 16.688  2.978   45.927 1.00 39.79  ? 66  ARG   B CZ  1 
ATOM   3042 N  NH1 . ARG   B  1  53  ? 17.402  2.255   46.778 1.00 43.53  ? 66  ARG   B NH1 1 
ATOM   3043 N  NH2 . ARG   B  1  53  ? 16.352  2.481   44.758 1.00 38.74  ? 66  ARG   B NH2 1 
ATOM   3044 N  N   . ASP   B  1  54  ? 14.482  6.332   52.845 1.00 42.30  ? 67  ASP   B N   1 
ATOM   3045 C  CA  . ASP   B  1  54  ? 14.775  6.815   54.189 1.00 43.99  ? 67  ASP   B CA  1 
ATOM   3046 C  C   . ASP   B  1  54  ? 14.106  5.947   55.253 1.00 38.00  ? 67  ASP   B C   1 
ATOM   3047 O  O   . ASP   B  1  54  ? 14.398  6.107   56.418 1.00 40.99  ? 67  ASP   B O   1 
ATOM   3048 C  CB  . ASP   B  1  54  ? 14.432  8.283   54.391 1.00 53.90  ? 67  ASP   B CB  1 
ATOM   3049 C  CG  . ASP   B  1  54  ? 12.970  8.671   54.233 1.00 61.62  ? 67  ASP   B CG  1 
ATOM   3050 O  OD1 . ASP   B  1  54  ? 12.136  7.757   54.026 1.00 60.68  ? 67  ASP   B OD1 1 
ATOM   3051 O  OD2 . ASP   B  1  54  ? 12.683  9.892   54.307 1.00 61.57  ? 67  ASP   B OD2 1 
ATOM   3052 N  N   . GLY   B  1  55  ? 13.259  5.004   54.866 1.00 37.79  ? 68  GLY   B N   1 
ATOM   3053 C  CA  . GLY   B  1  55  ? 12.750  4.025   55.814 1.00 42.29  ? 68  GLY   B CA  1 
ATOM   3054 C  C   . GLY   B  1  55  ? 11.546  4.551   56.604 1.00 44.57  ? 68  GLY   B C   1 
ATOM   3055 O  O   . GLY   B  1  55  ? 11.229  4.018   57.654 1.00 40.95  ? 68  GLY   B O   1 
ATOM   3056 N  N   . VAL   B  1  56  ? 10.888  5.599   56.096 1.00 47.08  ? 69  VAL   B N   1 
ATOM   3057 C  CA  . VAL   B  1  56  ? 9.704   6.164   56.715 1.00 44.79  ? 69  VAL   B CA  1 
ATOM   3058 C  C   . VAL   B  1  56  ? 8.611   6.199   55.661 1.00 38.95  ? 69  VAL   B C   1 
ATOM   3059 O  O   . VAL   B  1  56  ? 8.803   6.804   54.626 1.00 40.19  ? 69  VAL   B O   1 
ATOM   3060 C  CB  . VAL   B  1  56  ? 9.997   7.567   57.271 1.00 50.66  ? 69  VAL   B CB  1 
ATOM   3061 C  CG1 . VAL   B  1  56  ? 8.728   8.293   57.702 1.00 56.10  ? 69  VAL   B CG1 1 
ATOM   3062 C  CG2 . VAL   B  1  56  ? 10.987  7.510   58.417 1.00 49.97  ? 69  VAL   B CG2 1 
ATOM   3063 N  N   . ALA   B  1  57  ? 7.477   5.546   55.933 1.00 40.33  ? 70  ALA   B N   1 
ATOM   3064 C  CA  . ALA   B  1  57  ? 6.462   5.333   54.919 1.00 41.26  ? 70  ALA   B CA  1 
ATOM   3065 C  C   . ALA   B  1  57  ? 5.054   5.376   55.521 1.00 42.67  ? 70  ALA   B C   1 
ATOM   3066 O  O   . ALA   B  1  57  ? 4.890   5.234   56.731 1.00 42.90  ? 70  ALA   B O   1 
ATOM   3067 C  CB  . ALA   B  1  57  ? 6.726   4.005   54.252 1.00 45.06  ? 70  ALA   B CB  1 
ATOM   3068 N  N   . THR   B  1  58  ? 4.049   5.540   54.649 1.00 42.60  ? 71  THR   B N   1 
ATOM   3069 C  CA  . THR   B  1  58  ? 2.661   5.418   55.037 1.00 42.79  ? 71  THR   B CA  1 
ATOM   3070 C  C   . THR   B  1  58  ? 2.324   3.938   55.093 1.00 48.37  ? 71  THR   B C   1 
ATOM   3071 O  O   . THR   B  1  58  ? 2.983   3.123   54.460 1.00 48.66  ? 71  THR   B O   1 
ATOM   3072 C  CB  . THR   B  1  58  ? 1.694   6.141   54.092 1.00 40.89  ? 71  THR   B CB  1 
ATOM   3073 O  OG1 . THR   B  1  58  ? 1.676   5.401   52.879 1.00 38.14  ? 71  THR   B OG1 1 
ATOM   3074 C  CG2 . THR   B  1  58  ? 2.041   7.599   53.880 1.00 42.64  ? 71  THR   B CG2 1 
ATOM   3075 N  N   . PRO   B  1  59  ? 1.268   3.566   55.838 1.00 43.76  ? 72  PRO   B N   1 
ATOM   3076 C  CA  . PRO   B  1  59  ? 0.759   2.204   55.815 1.00 42.51  ? 72  PRO   B CA  1 
ATOM   3077 C  C   . PRO   B  1  59  ? 0.467   1.724   54.410 1.00 41.62  ? 72  PRO   B C   1 
ATOM   3078 O  O   . PRO   B  1  59  ? 0.735   0.575   54.082 1.00 41.69  ? 72  PRO   B O   1 
ATOM   3079 C  CB  . PRO   B  1  59  ? -0.509  2.325   56.656 1.00 43.88  ? 72  PRO   B CB  1 
ATOM   3080 C  CG  . PRO   B  1  59  ? -0.169  3.413   57.658 1.00 44.35  ? 72  PRO   B CG  1 
ATOM   3081 C  CD  . PRO   B  1  59  ? 0.562   4.427   56.800 1.00 46.10  ? 72  PRO   B CD  1 
ATOM   3082 N  N   . ALA   B  1  60  ? -0.144  2.592   53.606 1.00 44.68  ? 73  ALA   B N   1 
ATOM   3083 C  CA  . ALA   B  1  60  ? -0.499  2.224   52.240 1.00 48.67  ? 73  ALA   B CA  1 
ATOM   3084 C  C   . ALA   B  1  60  ? 0.759   1.875   51.446 1.00 41.98  ? 73  ALA   B C   1 
ATOM   3085 O  O   . ALA   B  1  60  ? 0.748   0.915   50.713 1.00 36.56  ? 73  ALA   B O   1 
ATOM   3086 C  CB  . ALA   B  1  60  ? -1.269  3.337   51.564 1.00 49.14  ? 73  ALA   B CB  1 
ATOM   3087 N  N   . GLN   B  1  61  ? 1.826   2.661   51.593 1.00 43.71  ? 74  GLN   B N   1 
ATOM   3088 C  CA  . GLN   B  1  61  ? 3.071   2.393   50.885 1.00 46.17  ? 74  GLN   B CA  1 
ATOM   3089 C  C   . GLN   B  1  61  ? 3.661   1.047   51.314 1.00 44.69  ? 74  GLN   B C   1 
ATOM   3090 O  O   . GLN   B  1  61  ? 4.184   0.321   50.479 1.00 43.08  ? 74  GLN   B O   1 
ATOM   3091 C  CB  . GLN   B  1  61  ? 4.098   3.503   51.108 1.00 38.51  ? 74  GLN   B CB  1 
ATOM   3092 C  CG  . GLN   B  1  61  ? 3.723   4.807   50.419 1.00 37.63  ? 74  GLN   B CG  1 
ATOM   3093 C  CD  . GLN   B  1  61  ? 4.628   5.961   50.778 1.00 43.36  ? 74  GLN   B CD  1 
ATOM   3094 O  OE1 . GLN   B  1  61  ? 5.033   6.166   51.932 1.00 42.35  ? 74  GLN   B OE1 1 
ATOM   3095 N  NE2 . GLN   B  1  61  ? 4.987   6.717   49.758 1.00 49.29  ? 74  GLN   B NE2 1 
ATOM   3096 N  N   . ILE   B  1  62  ? 3.579   0.732   52.613 1.00 41.42  ? 75  ILE   B N   1 
ATOM   3097 C  CA  . ILE   B  1  62  ? 4.149   -0.490  53.142 1.00 38.08  ? 75  ILE   B CA  1 
ATOM   3098 C  C   . ILE   B  1  62  ? 3.411   -1.685  52.553 1.00 38.82  ? 75  ILE   B C   1 
ATOM   3099 O  O   . ILE   B  1  62  ? 4.022   -2.673  52.115 1.00 37.40  ? 75  ILE   B O   1 
ATOM   3100 C  CB  . ILE   B  1  62  ? 4.151   -0.467  54.685 1.00 36.30  ? 75  ILE   B CB  1 
ATOM   3101 C  CG1 . ILE   B  1  62  ? 5.131   0.578   55.193 1.00 34.91  ? 75  ILE   B CG1 1 
ATOM   3102 C  CG2 . ILE   B  1  62  ? 4.466   -1.851  55.281 1.00 38.25  ? 75  ILE   B CG2 1 
ATOM   3103 C  CD1 . ILE   B  1  62  ? 5.055   0.815   56.690 1.00 37.43  ? 75  ILE   B CD1 1 
ATOM   3104 N  N   . ILE   B  1  63  ? 2.087   -1.570  52.515 1.00 36.63  ? 76  ILE   B N   1 
ATOM   3105 C  CA  . ILE   B  1  63  ? 1.279   -2.660  52.016 1.00 38.19  ? 76  ILE   B CA  1 
ATOM   3106 C  C   . ILE   B  1  63  ? 1.585   -2.903  50.544 1.00 38.87  ? 76  ILE   B C   1 
ATOM   3107 O  O   . ILE   B  1  63  ? 1.868   -4.042  50.178 1.00 42.31  ? 76  ILE   B O   1 
ATOM   3108 C  CB  . ILE   B  1  63  ? -0.210  -2.426  52.296 1.00 37.55  ? 76  ILE   B CB  1 
ATOM   3109 C  CG1 . ILE   B  1  63  ? -0.474  -2.576  53.781 1.00 39.00  ? 76  ILE   B CG1 1 
ATOM   3110 C  CG2 . ILE   B  1  63  ? -1.080  -3.371  51.476 1.00 33.49  ? 76  ILE   B CG2 1 
ATOM   3111 C  CD1 . ILE   B  1  63  ? -1.690  -1.818  54.255 1.00 46.27  ? 76  ILE   B CD1 1 
ATOM   3112 N  N   . THR   B  1  64  ? 1.582   -1.862  49.709 1.00 40.09  ? 77  THR   B N   1 
ATOM   3113 C  CA  A THR   B  1  64  ? 1.801   -2.060  48.284 0.50 38.03  ? 77  THR   B CA  1 
ATOM   3114 C  CA  B THR   B  1  64  ? 1.788   -2.084  48.285 0.50 38.98  ? 77  THR   B CA  1 
ATOM   3115 C  C   . THR   B  1  64  ? 3.216   -2.596  48.060 1.00 34.71  ? 77  THR   B C   1 
ATOM   3116 O  O   . THR   B  1  64  ? 3.416   -3.500  47.263 1.00 32.46  ? 77  THR   B O   1 
ATOM   3117 C  CB  A THR   B  1  64  ? 1.565   -0.761  47.518 0.50 40.87  ? 77  THR   B CB  1 
ATOM   3118 C  CB  B THR   B  1  64  ? 1.386   -0.880  47.422 0.50 44.39  ? 77  THR   B CB  1 
ATOM   3119 O  OG1 A THR   B  1  64  ? 2.585   0.076   48.056 0.50 51.22  ? 77  THR   B OG1 1 
ATOM   3120 O  OG1 B THR   B  1  64  ? 2.061   -0.957  46.165 0.50 42.38  ? 77  THR   B OG1 1 
ATOM   3121 C  CG2 A THR   B  1  64  ? 0.167   -0.206  47.708 0.50 36.61  ? 77  THR   B CG2 1 
ATOM   3122 C  CG2 B THR   B  1  64  ? 1.742   0.477   47.993 0.50 49.07  ? 77  THR   B CG2 1 
ATOM   3123 N  N   . ALA   B  1  65  ? 4.196   -2.078  48.814 1.00 35.47  ? 78  ALA   B N   1 
ATOM   3124 C  CA  . ALA   B  1  65  ? 5.577   -2.538  48.687 1.00 35.88  ? 78  ALA   B CA  1 
ATOM   3125 C  C   . ALA   B  1  65  ? 5.733   -4.025  49.027 1.00 35.66  ? 78  ALA   B C   1 
ATOM   3126 O  O   . ALA   B  1  65  ? 6.441   -4.727  48.318 1.00 34.75  ? 78  ALA   B O   1 
ATOM   3127 C  CB  . ALA   B  1  65  ? 6.497   -1.725  49.550 1.00 34.65  ? 78  ALA   B CB  1 
ATOM   3128 N  N   . THR   B  1  66  ? 5.121   -4.507  50.111 1.00 33.85  ? 79  THR   B N   1 
ATOM   3129 C  CA  . THR   B  1  66  ? 5.277   -5.904  50.487 1.00 33.67  ? 79  THR   B CA  1 
ATOM   3130 C  C   . THR   B  1  66  ? 4.612   -6.802  49.449 1.00 33.30  ? 79  THR   B C   1 
ATOM   3131 O  O   . THR   B  1  66  ? 5.050   -7.921  49.203 1.00 36.74  ? 79  THR   B O   1 
ATOM   3132 C  CB  . THR   B  1  66  ? 4.749   -6.192  51.892 1.00 32.71  ? 79  THR   B CB  1 
ATOM   3133 O  OG1 . THR   B  1  66  ? 3.368   -5.861  51.918 1.00 32.12  ? 79  THR   B OG1 1 
ATOM   3134 C  CG2 . THR   B  1  66  ? 5.527   -5.447  52.955 1.00 32.24  ? 79  THR   B CG2 1 
ATOM   3135 N  N   . GLN   B  1  67  ? 3.541   -6.318  48.831 1.00 36.87  ? 80  GLN   B N   1 
ATOM   3136 C  CA  . GLN   B  1  67  ? 2.873   -7.057  47.772 1.00 36.76  ? 80  GLN   B CA  1 
ATOM   3137 C  C   . GLN   B  1  67  ? 3.703   -7.046  46.490 1.00 36.08  ? 80  GLN   B C   1 
ATOM   3138 O  O   . GLN   B  1  67  ? 3.939   -8.090  45.903 1.00 40.39  ? 80  GLN   B O   1 
ATOM   3139 C  CB  . GLN   B  1  67  ? 1.474   -6.476  47.582 1.00 40.91  ? 80  GLN   B CB  1 
ATOM   3140 C  CG  . GLN   B  1  67  ? 0.591   -6.685  48.805 1.00 40.82  ? 80  GLN   B CG  1 
ATOM   3141 C  CD  . GLN   B  1  67  ? -0.832  -6.176  48.681 1.00 44.98  ? 80  GLN   B CD  1 
ATOM   3142 O  OE1 . GLN   B  1  67  ? -1.698  -6.574  49.468 1.00 45.92  ? 80  GLN   B OE1 1 
ATOM   3143 N  NE2 . GLN   B  1  67  ? -1.105  -5.307  47.716 1.00 39.72  ? 80  GLN   B NE2 1 
ATOM   3144 N  N   . GLU   B  1  68  ? 4.127   -5.873  46.032 1.00 37.58  ? 81  GLU   B N   1 
ATOM   3145 C  CA  . GLU   B  1  68  ? 4.872   -5.763  44.791 1.00 41.90  ? 81  GLU   B CA  1 
ATOM   3146 C  C   . GLU   B  1  68  ? 6.187   -6.532  44.893 1.00 41.38  ? 81  GLU   B C   1 
ATOM   3147 O  O   . GLU   B  1  68  ? 6.548   -7.250  43.976 1.00 40.83  ? 81  GLU   B O   1 
ATOM   3148 C  CB  . GLU   B  1  68  ? 5.180   -4.302  44.453 1.00 48.49  ? 81  GLU   B CB  1 
ATOM   3149 C  CG  . GLU   B  1  68  ? 3.979   -3.495  43.971 1.00 59.81  ? 81  GLU   B CG  1 
ATOM   3150 C  CD  . GLU   B  1  68  ? 3.252   -4.081  42.759 1.00 74.58  ? 81  GLU   B CD  1 
ATOM   3151 O  OE1 . GLU   B  1  68  ? 1.989   -4.149  42.768 1.00 69.62  ? 81  GLU   B OE1 1 
ATOM   3152 O  OE2 . GLU   B  1  68  ? 3.956   -4.500  41.801 1.00 86.66  ? 81  GLU   B OE2 1 
ATOM   3153 N  N   . GLY   B  1  69  ? 6.893   -6.367  46.012 1.00 40.18  ? 82  GLY   B N   1 
ATOM   3154 C  CA  . GLY   B  1  69  ? 8.254   -6.861  46.170 1.00 38.67  ? 82  GLY   B CA  1 
ATOM   3155 C  C   . GLY   B  1  69  ? 8.307   -8.363  46.478 1.00 37.28  ? 82  GLY   B C   1 
ATOM   3156 O  O   . GLY   B  1  69  ? 9.185   -9.068  45.989 1.00 35.99  ? 82  GLY   B O   1 
ATOM   3157 N  N   . PHE   B  1  70  ? 7.371   -8.863  47.293 1.00 32.66  ? 83  PHE   B N   1 
ATOM   3158 C  CA  . PHE   B  1  70  ? 7.478   -10.212 47.805 1.00 30.55  ? 83  PHE   B CA  1 
ATOM   3159 C  C   . PHE   B  1  70  ? 6.223   -11.038 47.591 1.00 31.38  ? 83  PHE   B C   1 
ATOM   3160 O  O   . PHE   B  1  70  ? 6.238   -12.218 47.934 1.00 31.89  ? 83  PHE   B O   1 
ATOM   3161 C  CB  . PHE   B  1  70  ? 7.750   -10.190 49.305 1.00 31.40  ? 83  PHE   B CB  1 
ATOM   3162 C  CG  . PHE   B  1  70  ? 9.179   -9.842  49.667 1.00 34.07  ? 83  PHE   B CG  1 
ATOM   3163 C  CD1 . PHE   B  1  70  ? 10.210  -10.747 49.431 1.00 37.66  ? 83  PHE   B CD1 1 
ATOM   3164 C  CD2 . PHE   B  1  70  ? 9.485   -8.623  50.248 1.00 34.84  ? 83  PHE   B CD2 1 
ATOM   3165 C  CE1 . PHE   B  1  70  ? 11.517  -10.430 49.776 1.00 37.08  ? 83  PHE   B CE1 1 
ATOM   3166 C  CE2 . PHE   B  1  70  ? 10.784  -8.310  50.596 1.00 36.80  ? 83  PHE   B CE2 1 
ATOM   3167 C  CZ  . PHE   B  1  70  ? 11.801  -9.209  50.348 1.00 37.62  ? 83  PHE   B CZ  1 
ATOM   3168 N  N   . ASN   B  1  71  ? 5.141   -10.424 47.092 1.00 34.09  ? 84  ASN   B N   1 
ATOM   3169 C  CA  . ASN   B  1  71  ? 3.833   -11.066 46.997 1.00 33.53  ? 84  ASN   B CA  1 
ATOM   3170 C  C   . ASN   B  1  71  ? 3.337   -11.469 48.382 1.00 31.83  ? 84  ASN   B C   1 
ATOM   3171 O  O   . ASN   B  1  71  ? 2.733   -12.520 48.558 1.00 30.52  ? 84  ASN   B O   1 
ATOM   3172 C  CB  . ASN   B  1  71  ? 3.854   -12.270 46.067 1.00 34.98  ? 84  ASN   B CB  1 
ATOM   3173 C  CG  . ASN   B  1  71  ? 2.636   -12.350 45.167 1.00 35.10  ? 84  ASN   B CG  1 
ATOM   3174 O  OD1 . ASN   B  1  71  ? 1.635   -11.658 45.373 1.00 41.23  ? 84  ASN   B OD1 1 
ATOM   3175 N  ND2 . ASN   B  1  71  ? 2.716   -13.172 44.137 1.00 35.14  ? 84  ASN   B ND2 1 
ATOM   3176 N  N   . PHE   B  1  72  ? 3.608   -10.630 49.379 1.00 31.03  ? 85  PHE   B N   1 
ATOM   3177 C  CA  . PHE   B  1  72  ? 3.025   -10.848 50.691 1.00 32.86  ? 85  PHE   B CA  1 
ATOM   3178 C  C   . PHE   B  1  72  ? 1.509   -10.753 50.545 1.00 34.48  ? 85  PHE   B C   1 
ATOM   3179 O  O   . PHE   B  1  72  ? 1.009   -9.844  49.881 1.00 34.79  ? 85  PHE   B O   1 
ATOM   3180 C  CB  . PHE   B  1  72  ? 3.596   -9.785  51.630 1.00 34.65  ? 85  PHE   B CB  1 
ATOM   3181 C  CG  . PHE   B  1  72  ? 3.456   -10.105 53.108 1.00 34.43  ? 85  PHE   B CG  1 
ATOM   3182 C  CD1 . PHE   B  1  72  ? 3.732   -11.374 53.604 1.00 37.01  ? 85  PHE   B CD1 1 
ATOM   3183 C  CD2 . PHE   B  1  72  ? 3.054   -9.123  53.995 1.00 34.25  ? 85  PHE   B CD2 1 
ATOM   3184 C  CE1 . PHE   B  1  72  ? 3.607   -11.644 54.952 1.00 39.29  ? 85  PHE   B CE1 1 
ATOM   3185 C  CE2 . PHE   B  1  72  ? 2.964   -9.389  55.356 1.00 35.33  ? 85  PHE   B CE2 1 
ATOM   3186 C  CZ  . PHE   B  1  72  ? 3.236   -10.650 55.827 1.00 36.95  ? 85  PHE   B CZ  1 
ATOM   3187 N  N   . GLU   B  1  73  ? 0.780   -11.714 51.107 1.00 37.26  ? 86  GLU   B N   1 
ATOM   3188 C  CA  . GLU   B  1  73  ? -0.668  -11.756 50.947 1.00 39.51  ? 86  GLU   B CA  1 
ATOM   3189 C  C   . GLU   B  1  73  ? -1.320  -10.536 51.606 1.00 35.55  ? 86  GLU   B C   1 
ATOM   3190 O  O   . GLU   B  1  73  ? -0.898  -10.078 52.659 1.00 36.37  ? 86  GLU   B O   1 
ATOM   3191 C  CB  . GLU   B  1  73  ? -1.144  -13.106 51.472 1.00 40.61  ? 86  GLU   B CB  1 
ATOM   3192 C  CG  . GLU   B  1  73  ? -2.626  -13.383 51.247 1.00 47.71  ? 86  GLU   B CG  1 
ATOM   3193 C  CD  . GLU   B  1  73  ? -3.573  -12.788 52.285 1.00 55.02  ? 86  GLU   B CD  1 
ATOM   3194 O  OE1 . GLU   B  1  73  ? -4.657  -12.266 51.881 1.00 54.07  ? 86  GLU   B OE1 1 
ATOM   3195 O  OE2 . GLU   B  1  73  ? -3.219  -12.818 53.500 1.00 53.47  ? 86  GLU   B OE2 1 
ATOM   3196 N  N   . ASN   B  1  74  ? -2.369  -10.019 50.975 1.00 37.89  ? 87  ASN   B N   1 
ATOM   3197 C  CA  . ASN   B  1  74  ? -2.959  -8.713  51.282 1.00 36.08  ? 87  ASN   B CA  1 
ATOM   3198 C  C   . ASN   B  1  74  ? -3.402  -8.611  52.743 1.00 32.55  ? 87  ASN   B C   1 
ATOM   3199 O  O   . ASN   B  1  74  ? -3.099  -7.634  53.421 1.00 32.86  ? 87  ASN   B O   1 
ATOM   3200 C  CB  . ASN   B  1  74  ? -4.117  -8.445  50.315 1.00 35.68  ? 87  ASN   B CB  1 
ATOM   3201 C  CG  . ASN   B  1  74  ? -4.862  -7.160  50.591 1.00 40.74  ? 87  ASN   B CG  1 
ATOM   3202 O  OD1 . ASN   B  1  74  ? -6.052  -7.215  50.949 1.00 44.79  ? 87  ASN   B OD1 1 
ATOM   3203 N  ND2 . ASN   B  1  74  ? -4.206  -6.015  50.412 1.00 36.87  ? 87  ASN   B ND2 1 
ATOM   3204 N  N   . ASN   B  1  75  ? -4.136  -9.608  53.229 1.00 31.68  ? 88  ASN   B N   1 
ATOM   3205 C  CA  . ASN   B  1  75  ? -4.668  -9.554  54.585 1.00 35.52  ? 88  ASN   B CA  1 
ATOM   3206 C  C   . ASN   B  1  75  ? -3.529  -9.641  55.597 1.00 38.90  ? 88  ASN   B C   1 
ATOM   3207 O  O   . ASN   B  1  75  ? -3.532  -8.902  56.581 1.00 36.25  ? 88  ASN   B O   1 
ATOM   3208 C  CB  . ASN   B  1  75  ? -5.748  -10.608 54.830 1.00 38.38  ? 88  ASN   B CB  1 
ATOM   3209 C  CG  . ASN   B  1  75  ? -7.051  -10.290 54.118 1.00 43.80  ? 88  ASN   B CG  1 
ATOM   3210 O  OD1 . ASN   B  1  75  ? -7.599  -9.177  54.220 1.00 37.03  ? 88  ASN   B OD1 1 
ATOM   3211 N  ND2 . ASN   B  1  75  ? -7.556  -11.270 53.385 1.00 45.74  ? 88  ASN   B ND2 1 
ATOM   3212 N  N   . ALA   B  1  76  ? -2.541  -10.514 55.332 1.00 38.09  ? 89  ALA   B N   1 
ATOM   3213 C  CA  . ALA   B  1  76  ? -1.362  -10.587 56.179 1.00 34.94  ? 89  ALA   B CA  1 
ATOM   3214 C  C   . ALA   B  1  76  ? -0.650  -9.236  56.202 1.00 31.36  ? 89  ALA   B C   1 
ATOM   3215 O  O   . ALA   B  1  76  ? -0.222  -8.795  57.263 1.00 31.98  ? 89  ALA   B O   1 
ATOM   3216 C  CB  . ALA   B  1  76  ? -0.446  -11.699 55.721 1.00 32.49  ? 89  ALA   B CB  1 
ATOM   3217 N  N   . ALA   B  1  77  ? -0.570  -8.562  55.051 1.00 29.52  ? 90  ALA   B N   1 
ATOM   3218 C  CA  . ALA   B  1  77  ? 0.059   -7.247  54.990 1.00 29.56  ? 90  ALA   B CA  1 
ATOM   3219 C  C   . ALA   B  1  77  ? -0.697  -6.222  55.835 1.00 33.29  ? 90  ALA   B C   1 
ATOM   3220 O  O   . ALA   B  1  77  ? -0.089  -5.408  56.541 1.00 34.66  ? 90  ALA   B O   1 
ATOM   3221 C  CB  . ALA   B  1  77  ? 0.170   -6.789  53.553 1.00 32.62  ? 90  ALA   B CB  1 
ATOM   3222 N  N   . ILE   B  1  78  ? -2.030  -6.289  55.783 1.00 37.90  ? 91  ILE   B N   1 
ATOM   3223 C  CA  . ILE   B  1  78  ? -2.865  -5.352  56.509 1.00 34.66  ? 91  ILE   B CA  1 
ATOM   3224 C  C   . ILE   B  1  78  ? -2.717  -5.592  58.011 1.00 33.26  ? 91  ILE   B C   1 
ATOM   3225 O  O   . ILE   B  1  78  ? -2.536  -4.655  58.783 1.00 34.56  ? 91  ILE   B O   1 
ATOM   3226 C  CB  . ILE   B  1  78  ? -4.310  -5.475  55.999 1.00 38.14  ? 91  ILE   B CB  1 
ATOM   3227 C  CG1 . ILE   B  1  78  ? -4.438  -4.850  54.621 1.00 37.62  ? 91  ILE   B CG1 1 
ATOM   3228 C  CG2 . ILE   B  1  78  ? -5.294  -4.837  56.969 1.00 37.85  ? 91  ILE   B CG2 1 
ATOM   3229 C  CD1 . ILE   B  1  78  ? -5.738  -5.192  53.917 1.00 39.00  ? 91  ILE   B CD1 1 
ATOM   3230 N  N   . VAL   B  1  79  ? -2.708  -6.858  58.420 1.00 29.32  ? 92  VAL   B N   1 
ATOM   3231 C  CA  . VAL   B  1  79  ? -2.576  -7.195  59.818 1.00 30.70  ? 92  VAL   B CA  1 
ATOM   3232 C  C   . VAL   B  1  79  ? -1.247  -6.688  60.359 1.00 30.38  ? 92  VAL   B C   1 
ATOM   3233 O  O   . VAL   B  1  79  ? -1.203  -6.089  61.432 1.00 34.20  ? 92  VAL   B O   1 
ATOM   3234 C  CB  . VAL   B  1  79  ? -2.729  -8.705  60.069 1.00 33.11  ? 92  VAL   B CB  1 
ATOM   3235 C  CG1 . VAL   B  1  79  ? -2.382  -9.075  61.505 1.00 32.85  ? 92  VAL   B CG1 1 
ATOM   3236 C  CG2 . VAL   B  1  79  ? -4.127  -9.170  59.723 1.00 33.52  ? 92  VAL   B CG2 1 
ATOM   3237 N  N   . ALA   B  1  80  ? -0.151  -6.940  59.648 1.00 31.17  ? 93  ALA   B N   1 
ATOM   3238 C  CA  . ALA   B  1  80  ? 1.145   -6.551  60.163 1.00 31.91  ? 93  ALA   B CA  1 
ATOM   3239 C  C   . ALA   B  1  80  ? 1.301   -5.028  60.139 1.00 31.61  ? 93  ALA   B C   1 
ATOM   3240 O  O   . ALA   B  1  80  ? 1.820   -4.424  61.090 1.00 35.11  ? 93  ALA   B O   1 
ATOM   3241 C  CB  . ALA   B  1  80  ? 2.223   -7.265  59.396 1.00 33.29  ? 93  ALA   B CB  1 
ATOM   3242 N  N   . THR   B  1  81  ? 0.847   -4.396  59.057 1.00 32.72  ? 94  THR   B N   1 
ATOM   3243 C  CA  . THR   B  1  81  ? 1.156   -2.984  58.858 1.00 33.62  ? 94  THR   B CA  1 
ATOM   3244 C  C   . THR   B  1  81  ? 0.416   -2.114  59.877 1.00 36.94  ? 94  THR   B C   1 
ATOM   3245 O  O   . THR   B  1  81  ? 1.030   -1.261  60.523 1.00 37.50  ? 94  THR   B O   1 
ATOM   3246 C  CB  . THR   B  1  81  ? 0.833   -2.573  57.431 1.00 37.57  ? 94  THR   B CB  1 
ATOM   3247 O  OG1 . THR   B  1  81  ? 1.669   -3.344  56.571 1.00 34.99  ? 94  THR   B OG1 1 
ATOM   3248 C  CG2 . THR   B  1  81  ? 1.053   -1.090  57.222 1.00 41.17  ? 94  THR   B CG2 1 
ATOM   3249 N  N   . TYR   B  1  82  ? -0.894  -2.341  60.055 1.00 34.64  ? 95  TYR   B N   1 
ATOM   3250 C  CA  . TYR   B  1  82  ? -1.669  -1.460  60.924 1.00 36.46  ? 95  TYR   B CA  1 
ATOM   3251 C  C   . TYR   B  1  82  ? -1.381  -1.775  62.393 1.00 37.93  ? 95  TYR   B C   1 
ATOM   3252 O  O   . TYR   B  1  82  ? -1.488  -0.890  63.242 1.00 36.56  ? 95  TYR   B O   1 
ATOM   3253 C  CB  . TYR   B  1  82  ? -3.150  -1.468  60.553 1.00 38.60  ? 95  TYR   B CB  1 
ATOM   3254 C  CG  . TYR   B  1  82  ? -3.406  -0.793  59.220 1.00 35.23  ? 95  TYR   B CG  1 
ATOM   3255 C  CD1 . TYR   B  1  82  ? -3.353  0.595   59.105 1.00 36.61  ? 95  TYR   B CD1 1 
ATOM   3256 C  CD2 . TYR   B  1  82  ? -3.690  -1.534  58.082 1.00 38.55  ? 95  TYR   B CD2 1 
ATOM   3257 C  CE1 . TYR   B  1  82  ? -3.588  1.233   57.898 1.00 30.39  ? 95  TYR   B CE1 1 
ATOM   3258 C  CE2 . TYR   B  1  82  ? -3.916  -0.907  56.866 1.00 39.85  ? 95  TYR   B CE2 1 
ATOM   3259 C  CZ  . TYR   B  1  82  ? -3.858  0.479   56.775 1.00 36.05  ? 95  TYR   B CZ  1 
ATOM   3260 O  OH  . TYR   B  1  82  ? -4.051  1.108   55.576 1.00 44.59  ? 95  TYR   B OH  1 
ATOM   3261 N  N   . LEU   B  1  83  ? -0.972  -3.017  62.689 1.00 33.92  ? 96  LEU   B N   1 
ATOM   3262 C  CA  . LEU   B  1  83  ? -0.491  -3.344  64.020 1.00 32.55  ? 96  LEU   B CA  1 
ATOM   3263 C  C   . LEU   B  1  83  ? 0.722   -2.476  64.326 1.00 35.51  ? 96  LEU   B C   1 
ATOM   3264 O  O   . LEU   B  1  83  ? 0.804   -1.836  65.380 1.00 33.43  ? 96  LEU   B O   1 
ATOM   3265 C  CB  . LEU   B  1  83  ? -0.146  -4.823  64.092 1.00 33.75  ? 96  LEU   B CB  1 
ATOM   3266 C  CG  . LEU   B  1  83  ? 0.598   -5.282  65.344 1.00 37.98  ? 96  LEU   B CG  1 
ATOM   3267 C  CD1 . LEU   B  1  83  ? -0.226  -5.078  66.597 1.00 38.55  ? 96  LEU   B CD1 1 
ATOM   3268 C  CD2 . LEU   B  1  83  ? 0.982   -6.744  65.209 1.00 41.08  ? 96  LEU   B CD2 1 
ATOM   3269 N  N   . GLY   B  1  84  ? 1.660   -2.456  63.377 1.00 34.23  ? 97  GLY   B N   1 
ATOM   3270 C  CA  . GLY   B  1  84  ? 2.874   -1.684  63.549 1.00 33.77  ? 97  GLY   B CA  1 
ATOM   3271 C  C   . GLY   B  1  84  ? 2.574   -0.193  63.670 1.00 33.82  ? 97  GLY   B C   1 
ATOM   3272 O  O   . GLY   B  1  84  ? 3.137   0.500   64.519 1.00 35.40  ? 97  GLY   B O   1 
ATOM   3273 N  N   . HIS   B  1  85  ? 1.666   0.280   62.821 1.00 33.80  ? 98  HIS   B N   1 
ATOM   3274 C  CA  . HIS   B  1  85  ? 1.317   1.692   62.779 1.00 38.98  ? 98  HIS   B CA  1 
ATOM   3275 C  C   . HIS   B  1  85  ? 0.558   2.149   64.036 1.00 39.88  ? 98  HIS   B C   1 
ATOM   3276 O  O   . HIS   B  1  85  ? 0.872   3.181   64.617 1.00 39.75  ? 98  HIS   B O   1 
ATOM   3277 C  CB  . HIS   B  1  85  ? 0.478   1.946   61.536 1.00 37.88  ? 98  HIS   B CB  1 
ATOM   3278 C  CG  . HIS   B  1  85  ? 0.242   3.379   61.283 1.00 44.59  ? 98  HIS   B CG  1 
ATOM   3279 N  ND1 . HIS   B  1  85  ? 1.268   4.296   61.243 1.00 47.55  ? 98  HIS   B ND1 1 
ATOM   3280 C  CD2 . HIS   B  1  85  ? -0.891  4.043   60.987 1.00 45.77  ? 98  HIS   B CD2 1 
ATOM   3281 C  CE1 . HIS   B  1  85  ? 0.763   5.481   60.958 1.00 47.25  ? 98  HIS   B CE1 1 
ATOM   3282 N  NE2 . HIS   B  1  85  ? -0.547  5.352   60.801 1.00 49.68  ? 98  HIS   B NE2 1 
ATOM   3283 N  N   . LEU   B  1  86  ? -0.445  1.385   64.472 1.00 39.97  ? 99  LEU   B N   1 
ATOM   3284 C  CA  . LEU   B  1  86  ? -1.248  1.779   65.627 1.00 36.28  ? 99  LEU   B CA  1 
ATOM   3285 C  C   . LEU   B  1  86  ? -0.352  1.932   66.842 1.00 37.44  ? 99  LEU   B C   1 
ATOM   3286 O  O   . LEU   B  1  86  ? -0.466  2.903   67.582 1.00 43.32  ? 99  LEU   B O   1 
ATOM   3287 C  CB  . LEU   B  1  86  ? -2.362  0.762   65.871 1.00 36.44  ? 99  LEU   B CB  1 
ATOM   3288 C  CG  . LEU   B  1  86  ? -3.571  0.887   64.933 1.00 35.93  ? 99  LEU   B CG  1 
ATOM   3289 C  CD1 . LEU   B  1  86  ? -4.433  -0.345  64.947 1.00 35.58  ? 99  LEU   B CD1 1 
ATOM   3290 C  CD2 . LEU   B  1  86  ? -4.377  2.104   65.340 1.00 40.22  ? 99  LEU   B CD2 1 
ATOM   3291 N  N   . LEU   B  1  87  ? 0.556   0.971   67.027 1.00 38.92  ? 100 LEU   B N   1 
ATOM   3292 C  CA  . LEU   B  1  87  ? 1.414   0.938   68.195 1.00 37.24  ? 100 LEU   B CA  1 
ATOM   3293 C  C   . LEU   B  1  87  ? 2.579   1.915   68.067 1.00 40.26  ? 100 LEU   B C   1 
ATOM   3294 O  O   . LEU   B  1  87  ? 3.028   2.449   69.085 1.00 41.69  ? 100 LEU   B O   1 
ATOM   3295 C  CB  . LEU   B  1  87  ? 1.936   -0.477  68.401 1.00 37.89  ? 100 LEU   B CB  1 
ATOM   3296 C  CG  . LEU   B  1  87  ? 0.880   -1.539  68.715 1.00 41.98  ? 100 LEU   B CG  1 
ATOM   3297 C  CD1 . LEU   B  1  87  ? 1.552   -2.893  68.943 1.00 43.30  ? 100 LEU   B CD1 1 
ATOM   3298 C  CD2 . LEU   B  1  87  ? 0.017   -1.187  69.913 1.00 41.62  ? 100 LEU   B CD2 1 
ATOM   3299 N  N   . ASN   B  1  88  ? 3.111   2.091   66.844 1.00 41.50  ? 101 ASN   B N   1 
ATOM   3300 C  CA  . ASN   B  1  88  ? 4.460   2.621   66.694 1.00 42.58  ? 101 ASN   B CA  1 
ATOM   3301 C  C   . ASN   B  1  88  ? 4.559   3.756   65.688 1.00 42.05  ? 101 ASN   B C   1 
ATOM   3302 O  O   . ASN   B  1  88  ? 5.625   4.348   65.561 1.00 44.46  ? 101 ASN   B O   1 
ATOM   3303 C  CB  . ASN   B  1  88  ? 5.454   1.559   66.241 1.00 41.20  ? 101 ASN   B CB  1 
ATOM   3304 C  CG  . ASN   B  1  88  ? 5.625   0.455   67.253 1.00 39.69  ? 101 ASN   B CG  1 
ATOM   3305 O  OD1 . ASN   B  1  88  ? 5.738   0.718   68.454 1.00 41.79  ? 101 ASN   B OD1 1 
ATOM   3306 N  ND2 . ASN   B  1  88  ? 5.673   -0.781  66.784 1.00 45.07  ? 101 ASN   B ND2 1 
ATOM   3307 N  N   . GLY   B  1  89  ? 3.480   4.043   64.960 1.00 43.12  ? 102 GLY   B N   1 
ATOM   3308 C  CA  . GLY   B  1  89  ? 3.498   5.119   63.989 1.00 42.07  ? 102 GLY   B CA  1 
ATOM   3309 C  C   . GLY   B  1  89  ? 2.825   6.387   64.506 1.00 45.46  ? 102 GLY   B C   1 
ATOM   3310 O  O   . GLY   B  1  89  ? 2.210   6.425   65.575 1.00 42.00  ? 102 GLY   B O   1 
ATOM   3311 N  N   . ASN   B  1  90  ? 2.906   7.412   63.672 1.00 52.35  ? 103 ASN   B N   1 
ATOM   3312 C  CA  . ASN   B  1  90  ? 2.264   8.677   63.947 1.00 51.14  ? 103 ASN   B CA  1 
ATOM   3313 C  C   . ASN   B  1  90  ? 0.959   8.703   63.172 1.00 46.49  ? 103 ASN   B C   1 
ATOM   3314 O  O   . ASN   B  1  90  ? 0.986   8.757   61.942 1.00 46.18  ? 103 ASN   B O   1 
ATOM   3315 C  CB  . ASN   B  1  90  ? 3.171   9.826   63.543 1.00 55.97  ? 103 ASN   B CB  1 
ATOM   3316 C  CG  . ASN   B  1  90  ? 2.602   11.167  63.936 1.00 53.47  ? 103 ASN   B CG  1 
ATOM   3317 O  OD1 . ASN   B  1  90  ? 1.429   11.450  63.682 1.00 53.01  ? 103 ASN   B OD1 1 
ATOM   3318 N  ND2 . ASN   B  1  90  ? 3.405   11.997  64.569 1.00 51.73  ? 103 ASN   B ND2 1 
ATOM   3319 N  N   . LEU   B  1  91  ? -0.164  8.702   63.901 1.00 45.94  ? 104 LEU   B N   1 
ATOM   3320 C  CA  . LEU   B  1  91  ? -1.472  8.517   63.289 1.00 50.42  ? 104 LEU   B CA  1 
ATOM   3321 C  C   . LEU   B  1  91  ? -1.969  9.809   62.654 1.00 43.92  ? 104 LEU   B C   1 
ATOM   3322 O  O   . LEU   B  1  91  ? -2.804  9.757   61.754 1.00 45.41  ? 104 LEU   B O   1 
ATOM   3323 C  CB  . LEU   B  1  91  ? -2.421  7.981   64.354 1.00 52.13  ? 104 LEU   B CB  1 
ATOM   3324 C  CG  . LEU   B  1  91  ? -1.980  6.638   64.941 1.00 55.45  ? 104 LEU   B CG  1 
ATOM   3325 C  CD1 . LEU   B  1  91  ? -2.579  6.373   66.289 1.00 59.85  ? 104 LEU   B CD1 1 
ATOM   3326 C  CD2 . LEU   B  1  91  ? -2.359  5.552   63.972 1.00 56.34  ? 104 LEU   B CD2 1 
ATOM   3327 N  N   . VAL   B  1  92  ? -1.392  10.948  63.043 1.00 47.45  ? 105 VAL   B N   1 
ATOM   3328 C  CA  . VAL   B  1  92  ? -1.812  12.228  62.490 1.00 55.57  ? 105 VAL   B CA  1 
ATOM   3329 C  C   . VAL   B  1  92  ? -1.166  12.437  61.125 1.00 51.77  ? 105 VAL   B C   1 
ATOM   3330 O  O   . VAL   B  1  92  ? -1.848  12.851  60.191 1.00 53.97  ? 105 VAL   B O   1 
ATOM   3331 C  CB  . VAL   B  1  92  ? -1.456  13.397  63.430 1.00 60.50  ? 105 VAL   B CB  1 
ATOM   3332 C  CG1 . VAL   B  1  92  ? -1.758  14.750  62.794 1.00 56.22  ? 105 VAL   B CG1 1 
ATOM   3333 C  CG2 . VAL   B  1  92  ? -2.106  13.248  64.797 1.00 65.13  ? 105 VAL   B CG2 1 
ATOM   3334 N  N   . THR   B  1  93  ? 0.151   12.175  61.035 1.00 57.07  ? 106 THR   B N   1 
ATOM   3335 C  CA  . THR   B  1  93  ? 0.895   12.347  59.789 1.00 56.06  ? 106 THR   B CA  1 
ATOM   3336 C  C   . THR   B  1  93  ? 0.785   11.108  58.906 1.00 48.43  ? 106 THR   B C   1 
ATOM   3337 O  O   . THR   B  1  93  ? 1.095   11.183  57.728 1.00 53.00  ? 106 THR   B O   1 
ATOM   3338 C  CB  . THR   B  1  93  ? 2.353   12.678  60.088 1.00 60.69  ? 106 THR   B CB  1 
ATOM   3339 O  OG1 . THR   B  1  93  ? 2.884   11.578  60.830 1.00 58.35  ? 106 THR   B OG1 1 
ATOM   3340 C  CG2 . THR   B  1  93  ? 2.478   13.989  60.850 1.00 59.00  ? 106 THR   B CG2 1 
ATOM   3341 N  N   . ASP   B  1  94  ? 0.312   9.987   59.466 1.00 42.39  ? 107 ASP   B N   1 
ATOM   3342 C  CA  . ASP   B  1  94  ? 0.139   8.745   58.728 1.00 42.63  ? 107 ASP   B CA  1 
ATOM   3343 C  C   . ASP   B  1  94  ? 1.498   8.186   58.298 1.00 41.80  ? 107 ASP   B C   1 
ATOM   3344 O  O   . ASP   B  1  94  ? 1.609   7.670   57.202 1.00 40.17  ? 107 ASP   B O   1 
ATOM   3345 C  CB  . ASP   B  1  94  ? -0.782  8.917   57.530 1.00 37.83  ? 107 ASP   B CB  1 
ATOM   3346 C  CG  . ASP   B  1  94  ? -1.402  7.623   57.013 1.00 48.17  ? 107 ASP   B CG  1 
ATOM   3347 O  OD1 . ASP   B  1  94  ? -1.737  6.761   57.865 1.00 54.43  ? 107 ASP   B OD1 1 
ATOM   3348 O  OD2 . ASP   B  1  94  ? -1.597  7.491   55.773 1.00 51.04  ? 107 ASP   B OD2 1 
ATOM   3349 N  N   . LEU   B  1  95  ? 2.510   8.282   59.167 1.00 42.83  ? 108 LEU   B N   1 
ATOM   3350 C  CA  . LEU   B  1  95  ? 3.862   7.864   58.844 1.00 50.45  ? 108 LEU   B CA  1 
ATOM   3351 C  C   . LEU   B  1  95  ? 4.368   6.918   59.923 1.00 45.14  ? 108 LEU   B C   1 
ATOM   3352 O  O   . LEU   B  1  95  ? 4.122   7.137   61.107 1.00 49.01  ? 108 LEU   B O   1 
ATOM   3353 C  CB  . LEU   B  1  95  ? 4.806   9.061   58.696 1.00 53.46  ? 108 LEU   B CB  1 
ATOM   3354 C  CG  . LEU   B  1  95  ? 4.520   10.003  57.522 1.00 51.99  ? 108 LEU   B CG  1 
ATOM   3355 C  CD1 . LEU   B  1  95  ? 5.391   11.242  57.676 1.00 52.64  ? 108 LEU   B CD1 1 
ATOM   3356 C  CD2 . LEU   B  1  95  ? 4.756   9.356   56.165 1.00 51.15  ? 108 LEU   B CD2 1 
ATOM   3357 N  N   . LEU   B  1  96  ? 5.089   5.874   59.477 1.00 42.65  ? 109 LEU   B N   1 
ATOM   3358 C  CA  . LEU   B  1  96  ? 5.699   4.889   60.352 1.00 36.48  ? 109 LEU   B CA  1 
ATOM   3359 C  C   . LEU   B  1  96  ? 7.168   4.733   59.995 1.00 35.16  ? 109 LEU   B C   1 
ATOM   3360 O  O   . LEU   B  1  96  ? 7.496   4.549   58.843 1.00 41.82  ? 109 LEU   B O   1 
ATOM   3361 C  CB  . LEU   B  1  96  ? 4.941   3.579   60.179 1.00 35.83  ? 109 LEU   B CB  1 
ATOM   3362 C  CG  . LEU   B  1  96  ? 5.577   2.346   60.823 1.00 34.60  ? 109 LEU   B CG  1 
ATOM   3363 C  CD1 . LEU   B  1  96  ? 5.655   2.479   62.301 1.00 36.15  ? 109 LEU   B CD1 1 
ATOM   3364 C  CD2 . LEU   B  1  96  ? 4.772   1.113   60.430 1.00 40.24  ? 109 LEU   B CD2 1 
ATOM   3365 N  N   . SER   B  1  97  ? 8.038   4.815   60.993 1.00 38.01  ? 110 SER   B N   1 
ATOM   3366 C  CA  . SER   B  1  97  ? 9.448   4.496   60.858 1.00 41.46  ? 110 SER   B CA  1 
ATOM   3367 C  C   . SER   B  1  97  ? 9.626   2.984   60.938 1.00 43.99  ? 110 SER   B C   1 
ATOM   3368 O  O   . SER   B  1  97  ? 9.142   2.364   61.884 1.00 39.91  ? 110 SER   B O   1 
ATOM   3369 C  CB  . SER   B  1  97  ? 10.252  5.140   61.945 1.00 38.98  ? 110 SER   B CB  1 
ATOM   3370 O  OG  . SER   B  1  97  ? 11.547  4.554   62.056 1.00 42.15  ? 110 SER   B OG  1 
ATOM   3371 N  N   . ILE   B  1  98  ? 10.392  2.400   59.999 1.00 41.38  ? 111 ILE   B N   1 
ATOM   3372 C  CA  . ILE   B  1  98  ? 10.598  0.962   60.008 1.00 36.57  ? 111 ILE   B CA  1 
ATOM   3373 C  C   . ILE   B  1  98  ? 11.706  0.610   60.987 1.00 37.98  ? 111 ILE   B C   1 
ATOM   3374 O  O   . ILE   B  1  98  ? 12.045  -0.563  61.140 1.00 42.08  ? 111 ILE   B O   1 
ATOM   3375 C  CB  . ILE   B  1  98  ? 10.846  0.417   58.599 1.00 38.53  ? 111 ILE   B CB  1 
ATOM   3376 C  CG1 . ILE   B  1  98  ? 12.205  0.840   58.037 1.00 37.96  ? 111 ILE   B CG1 1 
ATOM   3377 C  CG2 . ILE   B  1  98  ? 9.692   0.795   57.678 1.00 35.58  ? 111 ILE   B CG2 1 
ATOM   3378 C  CD1 . ILE   B  1  98  ? 12.553  0.165   56.731 1.00 38.46  ? 111 ILE   B CD1 1 
ATOM   3379 N  N   . GLY   B  1  99  ? 12.254  1.629   61.659 1.00 36.24  ? 112 GLY   B N   1 
ATOM   3380 C  CA  . GLY   B  1  99  ? 13.250  1.405   62.689 1.00 40.21  ? 112 GLY   B CA  1 
ATOM   3381 C  C   . GLY   B  1  99  ? 12.929  2.210   63.954 1.00 48.85  ? 112 GLY   B C   1 
ATOM   3382 O  O   . GLY   B  1  99  ? 11.959  1.924   64.658 1.00 51.62  ? 112 GLY   B O   1 
ATOM   3383 N  N   . GLY   B  1  100 ? 13.791  3.182   64.265 1.00 45.47  ? 113 GLY   B N   1 
ATOM   3384 C  CA  . GLY   B  1  100 ? 13.710  3.920   65.508 1.00 47.45  ? 113 GLY   B CA  1 
ATOM   3385 C  C   . GLY   B  1  100 ? 13.128  5.308   65.280 1.00 45.45  ? 113 GLY   B C   1 
ATOM   3386 O  O   . GLY   B  1  100 ? 12.588  5.604   64.222 1.00 41.07  ? 113 GLY   B O   1 
ATOM   3387 N  N   . ALA   B  1  101 ? 13.261  6.141   66.312 1.00 52.61  ? 114 ALA   B N   1 
ATOM   3388 C  CA  . ALA   B  1  101 ? 12.646  7.455   66.339 1.00 57.38  ? 114 ALA   B CA  1 
ATOM   3389 C  C   . ALA   B  1  101 ? 13.329  8.367   65.331 1.00 57.48  ? 114 ALA   B C   1 
ATOM   3390 O  O   . ALA   B  1  101 ? 14.533  8.273   65.125 1.00 54.71  ? 114 ALA   B O   1 
ATOM   3391 C  CB  . ALA   B  1  101 ? 12.744  8.022   67.744 1.00 62.46  ? 114 ALA   B CB  1 
ATOM   3392 N  N   . THR   B  1  102 ? 12.549  9.260   64.727 1.00 58.95  ? 115 THR   B N   1 
ATOM   3393 C  CA  . THR   B  1  102 ? 13.074  10.145  63.712 1.00 65.34  ? 115 THR   B CA  1 
ATOM   3394 C  C   . THR   B  1  102 ? 12.153  11.351  63.642 1.00 68.01  ? 115 THR   B C   1 
ATOM   3395 O  O   . THR   B  1  102 ? 10.948  11.184  63.758 1.00 70.52  ? 115 THR   B O   1 
ATOM   3396 C  CB  . THR   B  1  102 ? 13.151  9.399   62.377 1.00 64.54  ? 115 THR   B CB  1 
ATOM   3397 O  OG1 . THR   B  1  102 ? 13.478  10.336  61.358 1.00 64.49  ? 115 THR   B OG1 1 
ATOM   3398 C  CG2 . THR   B  1  102 ? 11.826  8.826   61.908 1.00 65.92  ? 115 THR   B CG2 1 
ATOM   3399 N  N   . PRO   B  1  103 ? 12.675  12.582  63.441 1.00 74.18  ? 116 PRO   B N   1 
ATOM   3400 C  CA  . PRO   B  1  103 ? 11.818  13.724  63.104 1.00 72.76  ? 116 PRO   B CA  1 
ATOM   3401 C  C   . PRO   B  1  103 ? 11.022  13.570  61.807 1.00 61.22  ? 116 PRO   B C   1 
ATOM   3402 O  O   . PRO   B  1  103 ? 10.074  14.311  61.580 1.00 62.63  ? 116 PRO   B O   1 
ATOM   3403 C  CB  . PRO   B  1  103 ? 12.787  14.930  63.045 1.00 77.26  ? 116 PRO   B CB  1 
ATOM   3404 C  CG  . PRO   B  1  103 ? 14.158  14.312  62.890 1.00 75.64  ? 116 PRO   B CG  1 
ATOM   3405 C  CD  . PRO   B  1  103 ? 14.095  12.945  63.565 1.00 71.98  ? 116 PRO   B CD  1 
ATOM   3406 N  N   . LYS   B  1  104 ? 11.396  12.610  60.955 1.00 62.53  ? 117 LYS   B N   1 
ATOM   3407 C  CA  . LYS   B  1  104 ? 10.730  12.422  59.673 1.00 62.35  ? 117 LYS   B CA  1 
ATOM   3408 C  C   . LYS   B  1  104 ? 9.281   11.945  59.828 1.00 58.77  ? 117 LYS   B C   1 
ATOM   3409 O  O   . LYS   B  1  104 ? 8.528   12.029  58.860 1.00 53.37  ? 117 LYS   B O   1 
ATOM   3410 C  CB  . LYS   B  1  104 ? 11.500  11.409  58.818 1.00 76.40  ? 117 LYS   B CB  1 
ATOM   3411 C  CG  . LYS   B  1  104 ? 12.874  11.859  58.322 1.00 89.96  ? 117 LYS   B CG  1 
ATOM   3412 C  CD  . LYS   B  1  104 ? 13.815  10.715  57.940 1.00 89.19  ? 117 LYS   B CD  1 
ATOM   3413 C  CE  . LYS   B  1  104 ? 15.059  11.157  57.216 1.00 85.70  ? 117 LYS   B CE  1 
ATOM   3414 N  NZ  . LYS   B  1  104 ? 14.769  11.712  55.885 1.00 79.84  ? 117 LYS   B NZ  1 
ATOM   3415 N  N   . THR   B  1  105 ? 8.880   11.412  61.000 1.00 53.81  ? 118 THR   B N   1 
ATOM   3416 C  CA  . THR   B  1  105 ? 7.490   11.006  61.207 1.00 58.54  ? 118 THR   B CA  1 
ATOM   3417 C  C   . THR   B  1  105 ? 6.640   12.212  61.610 1.00 65.54  ? 118 THR   B C   1 
ATOM   3418 O  O   . THR   B  1  105 ? 5.420   12.086  61.711 1.00 71.62  ? 118 THR   B O   1 
ATOM   3419 C  CB  . THR   B  1  105 ? 7.314   9.856   62.206 1.00 52.00  ? 118 THR   B CB  1 
ATOM   3420 O  OG1 . THR   B  1  105 ? 8.012   10.136  63.409 1.00 48.74  ? 118 THR   B OG1 1 
ATOM   3421 C  CG2 . THR   B  1  105 ? 7.819   8.524   61.684 1.00 54.09  ? 118 THR   B CG2 1 
ATOM   3422 N  N   . GLY   B  1  106 ? 7.278   13.369  61.828 1.00 74.60  ? 119 GLY   B N   1 
ATOM   3423 C  CA  . GLY   B  1  106 ? 6.571   14.623  62.049 1.00 75.81  ? 119 GLY   B CA  1 
ATOM   3424 C  C   . GLY   B  1  106 ? 6.463   14.958  63.536 1.00 81.57  ? 119 GLY   B C   1 
ATOM   3425 O  O   . GLY   B  1  106 ? 7.114   14.330  64.369 1.00 71.44  ? 119 GLY   B O   1 
ATOM   3426 N  N   . PRO   B  1  107 ? 5.624   15.955  63.910 1.00 98.08  ? 120 PRO   B N   1 
ATOM   3427 C  CA  . PRO   B  1  107 ? 5.459   16.340  65.318 1.00 91.95  ? 120 PRO   B CA  1 
ATOM   3428 C  C   . PRO   B  1  107 ? 5.008   15.167  66.193 1.00 80.77  ? 120 PRO   B C   1 
ATOM   3429 O  O   . PRO   B  1  107 ? 4.055   14.472  65.863 1.00 72.86  ? 120 PRO   B O   1 
ATOM   3430 C  CB  . PRO   B  1  107 ? 4.403   17.467  65.285 1.00 96.67  ? 120 PRO   B CB  1 
ATOM   3431 C  CG  . PRO   B  1  107 ? 4.336   17.922  63.835 1.00 99.34  ? 120 PRO   B CG  1 
ATOM   3432 C  CD  . PRO   B  1  107 ? 4.798   16.751  62.985 1.00 97.85  ? 120 PRO   B CD  1 
ATOM   3433 N  N   . PRO   B  1  108 ? 5.653   14.909  67.350 1.00 78.95  ? 121 PRO   B N   1 
ATOM   3434 C  CA  . PRO   B  1  108 ? 5.331   13.721  68.149 1.00 81.12  ? 121 PRO   B CA  1 
ATOM   3435 C  C   . PRO   B  1  108 ? 3.904   13.714  68.703 1.00 82.71  ? 121 PRO   B C   1 
ATOM   3436 O  O   . PRO   B  1  108 ? 3.305   14.764  68.917 1.00 73.73  ? 121 PRO   B O   1 
ATOM   3437 C  CB  . PRO   B  1  108 ? 6.392   13.722  69.277 1.00 83.51  ? 121 PRO   B CB  1 
ATOM   3438 C  CG  . PRO   B  1  108 ? 6.882   15.156  69.337 1.00 84.50  ? 121 PRO   B CG  1 
ATOM   3439 C  CD  . PRO   B  1  108 ? 6.709   15.745  67.943 1.00 83.32  ? 121 PRO   B CD  1 
ATOM   3440 N  N   . PRO   B  1  109 ? 3.304   12.528  68.949 1.00 82.24  ? 122 PRO   B N   1 
ATOM   3441 C  CA  . PRO   B  1  109 ? 1.973   12.453  69.550 1.00 81.85  ? 122 PRO   B CA  1 
ATOM   3442 C  C   . PRO   B  1  109 ? 2.034   12.786  71.039 1.00 83.28  ? 122 PRO   B C   1 
ATOM   3443 O  O   . PRO   B  1  109 ? 3.115   12.765  71.624 1.00 83.69  ? 122 PRO   B O   1 
ATOM   3444 C  CB  . PRO   B  1  109 ? 1.597   10.988  69.304 1.00 80.53  ? 122 PRO   B CB  1 
ATOM   3445 C  CG  . PRO   B  1  109 ? 2.926   10.272  69.447 1.00 78.06  ? 122 PRO   B CG  1 
ATOM   3446 C  CD  . PRO   B  1  109 ? 3.888   11.195  68.709 1.00 79.88  ? 122 PRO   B CD  1 
ATOM   3447 N  N   . PRO   B  1  110 ? 0.883   13.070  71.700 1.00 84.42  ? 123 PRO   B N   1 
ATOM   3448 C  CA  . PRO   B  1  110 ? 0.846   13.198  73.159 1.00 81.47  ? 123 PRO   B CA  1 
ATOM   3449 C  C   . PRO   B  1  110 ? 1.258   11.918  73.895 1.00 78.25  ? 123 PRO   B C   1 
ATOM   3450 O  O   . PRO   B  1  110 ? 0.766   10.829  73.601 1.00 75.96  ? 123 PRO   B O   1 
ATOM   3451 C  CB  . PRO   B  1  110 ? -0.610  13.617  73.463 1.00 85.25  ? 123 PRO   B CB  1 
ATOM   3452 C  CG  . PRO   B  1  110 ? -1.388  13.197  72.246 1.00 84.60  ? 123 PRO   B CG  1 
ATOM   3453 C  CD  . PRO   B  1  110 ? -0.429  13.298  71.073 1.00 84.38  ? 123 PRO   B CD  1 
ATOM   3454 N  N   . PRO   B  1  111 ? 2.202   12.003  74.862 1.00 74.73  ? 124 PRO   B N   1 
ATOM   3455 C  CA  . PRO   B  1  111 ? 2.588   10.846  75.674 1.00 73.34  ? 124 PRO   B CA  1 
ATOM   3456 C  C   . PRO   B  1  111 ? 1.358   10.305  76.395 1.00 75.00  ? 124 PRO   B C   1 
ATOM   3457 O  O   . PRO   B  1  111 ? 0.440   11.066  76.679 1.00 70.41  ? 124 PRO   B O   1 
ATOM   3458 C  CB  . PRO   B  1  111 ? 3.647   11.385  76.661 1.00 74.49  ? 124 PRO   B CB  1 
ATOM   3459 C  CG  . PRO   B  1  111 ? 4.054   12.748  76.122 1.00 73.14  ? 124 PRO   B CG  1 
ATOM   3460 C  CD  . PRO   B  1  111 ? 2.950   13.224  75.204 1.00 69.65  ? 124 PRO   B CD  1 
ATOM   3461 N  N   . PRO   B  1  112 ? 1.280   8.995   76.730 1.00 74.07  ? 125 PRO   B N   1 
ATOM   3462 C  CA  . PRO   B  1  112 ? 2.391   8.041   76.561 1.00 65.17  ? 125 PRO   B CA  1 
ATOM   3463 C  C   . PRO   B  1  112 ? 2.574   7.392   75.183 1.00 61.63  ? 125 PRO   B C   1 
ATOM   3464 O  O   . PRO   B  1  112 ? 3.356   6.443   75.035 1.00 59.03  ? 125 PRO   B O   1 
ATOM   3465 C  CB  . PRO   B  1  112 ? 2.063   6.986   77.629 1.00 66.23  ? 125 PRO   B CB  1 
ATOM   3466 C  CG  . PRO   B  1  112 ? 0.546   6.980   77.686 1.00 68.83  ? 125 PRO   B CG  1 
ATOM   3467 C  CD  . PRO   B  1  112 ? 0.074   8.373   77.297 1.00 70.41  ? 125 PRO   B CD  1 
ATOM   3468 N  N   . ALA   B  1  113 ? 1.850   7.886   74.166 1.00 55.39  ? 126 ALA   B N   1 
ATOM   3469 C  CA  . ALA   B  1  113 ? 2.152   7.506   72.793 1.00 59.82  ? 126 ALA   B CA  1 
ATOM   3470 C  C   . ALA   B  1  113 ? 3.517   8.083   72.409 1.00 67.52  ? 126 ALA   B C   1 
ATOM   3471 O  O   . ALA   B  1  113 ? 3.948   9.087   72.992 1.00 61.60  ? 126 ALA   B O   1 
ATOM   3472 C  CB  . ALA   B  1  113 ? 1.074   7.971   71.844 1.00 57.54  ? 126 ALA   B CB  1 
ATOM   3473 N  N   . HIS   B  1  114 ? 4.163   7.467   71.405 1.00 63.06  ? 127 HIS   B N   1 
ATOM   3474 C  CA  . HIS   B  1  114 ? 5.560   7.749   71.113 1.00 53.92  ? 127 HIS   B CA  1 
ATOM   3475 C  C   . HIS   B  1  114 ? 5.862   7.868   69.616 1.00 51.78  ? 127 HIS   B C   1 
ATOM   3476 O  O   . HIS   B  1  114 ? 6.739   8.640   69.249 1.00 53.44  ? 127 HIS   B O   1 
ATOM   3477 C  CB  . HIS   B  1  114 ? 6.417   6.687   71.800 1.00 55.57  ? 127 HIS   B CB  1 
ATOM   3478 C  CG  . HIS   B  1  114 ? 5.948   5.286   71.562 1.00 56.81  ? 127 HIS   B CG  1 
ATOM   3479 N  ND1 . HIS   B  1  114 ? 6.227   4.603   70.402 1.00 53.13  ? 127 HIS   B ND1 1 
ATOM   3480 C  CD2 . HIS   B  1  114 ? 5.233   4.435   72.308 1.00 57.12  ? 127 HIS   B CD2 1 
ATOM   3481 C  CE1 . HIS   B  1  114 ? 5.712   3.385   70.460 1.00 50.21  ? 127 HIS   B CE1 1 
ATOM   3482 N  NE2 . HIS   B  1  114 ? 5.100   3.254   71.604 1.00 48.69  ? 127 HIS   B NE2 1 
ATOM   3483 N  N   . ALA   B  1  115 ? 5.181   7.097   68.753 1.00 49.68  ? 128 ALA   B N   1 
ATOM   3484 C  CA  . ALA   B  1  115 ? 5.534   6.988   67.336 1.00 52.83  ? 128 ALA   B CA  1 
ATOM   3485 C  C   . ALA   B  1  115 ? 7.035   6.687   67.163 1.00 48.79  ? 128 ALA   B C   1 
ATOM   3486 O  O   . ALA   B  1  115 ? 7.713   7.269   66.322 1.00 49.14  ? 128 ALA   B O   1 
ATOM   3487 C  CB  . ALA   B  1  115 ? 5.121   8.243   66.607 1.00 55.09  ? 128 ALA   B CB  1 
ATOM   3488 N  N   . GLY   B  1  116 ? 7.531   5.724   67.943 1.00 44.20  ? 129 GLY   B N   1 
ATOM   3489 C  CA  . GLY   B  1  116 ? 8.951   5.445   68.056 1.00 47.54  ? 129 GLY   B CA  1 
ATOM   3490 C  C   . GLY   B  1  116 ? 9.457   4.412   67.042 1.00 45.29  ? 129 GLY   B C   1 
ATOM   3491 O  O   . GLY   B  1  116 ? 10.631  4.065   67.082 1.00 49.01  ? 129 GLY   B O   1 
ATOM   3492 N  N   . GLY   B  1  117 ? 8.567   3.914   66.169 1.00 42.50  ? 130 GLY   B N   1 
ATOM   3493 C  CA  . GLY   B  1  117 ? 8.929   3.017   65.088 1.00 40.77  ? 130 GLY   B CA  1 
ATOM   3494 C  C   . GLY   B  1  117 ? 8.959   1.552   65.530 1.00 40.21  ? 130 GLY   B C   1 
ATOM   3495 O  O   . GLY   B  1  117 ? 8.789   1.252   66.703 1.00 37.76  ? 130 GLY   B O   1 
ATOM   3496 N  N   . LEU   B  1  118 ? 9.226   0.651   64.573 1.00 39.59  ? 131 LEU   B N   1 
ATOM   3497 C  CA  . LEU   B  1  118 ? 9.184   -0.788  64.781 1.00 38.83  ? 131 LEU   B CA  1 
ATOM   3498 C  C   . LEU   B  1  118 ? 10.238  -1.263  65.779 1.00 42.35  ? 131 LEU   B C   1 
ATOM   3499 O  O   . LEU   B  1  118 ? 10.127  -2.376  66.276 1.00 47.11  ? 131 LEU   B O   1 
ATOM   3500 C  CB  . LEU   B  1  118 ? 9.366   -1.524  63.456 1.00 38.83  ? 131 LEU   B CB  1 
ATOM   3501 C  CG  . LEU   B  1  118 ? 8.312   -1.231  62.388 1.00 41.48  ? 131 LEU   B CG  1 
ATOM   3502 C  CD1 . LEU   B  1  118 ? 8.597   -2.075  61.151 1.00 39.24  ? 131 LEU   B CD1 1 
ATOM   3503 C  CD2 . LEU   B  1  118 ? 6.886   -1.449  62.908 1.00 42.85  ? 131 LEU   B CD2 1 
ATOM   3504 N  N   . ASN   B  1  119 ? 11.266  -0.454  66.060 1.00 40.42  ? 132 ASN   B N   1 
ATOM   3505 C  CA  . ASN   B  1  119 ? 12.259  -0.823  67.054 1.00 44.12  ? 132 ASN   B CA  1 
ATOM   3506 C  C   . ASN   B  1  119 ? 11.680  -0.879  68.469 1.00 46.39  ? 132 ASN   B C   1 
ATOM   3507 O  O   . ASN   B  1  119 ? 12.292  -1.500  69.339 1.00 42.94  ? 132 ASN   B O   1 
ATOM   3508 C  CB  . ASN   B  1  119 ? 13.423  0.157   67.125 1.00 44.61  ? 132 ASN   B CB  1 
ATOM   3509 C  CG  . ASN   B  1  119 ? 14.367  0.047   65.954 1.00 47.70  ? 132 ASN   B CG  1 
ATOM   3510 O  OD1 . ASN   B  1  119 ? 14.182  -0.790  65.057 1.00 47.32  ? 132 ASN   B OD1 1 
ATOM   3511 N  ND2 . ASN   B  1  119 ? 15.391  0.893   65.962 1.00 45.20  ? 132 ASN   B ND2 1 
ATOM   3512 N  N   . VAL   B  1  120 ? 10.549  -0.211  68.730 1.00 44.70  ? 133 VAL   B N   1 
ATOM   3513 C  CA  . VAL   B  1  120 ? 10.016  -0.170  70.085 1.00 49.41  ? 133 VAL   B CA  1 
ATOM   3514 C  C   . VAL   B  1  120 ? 9.635   -1.579  70.551 1.00 44.42  ? 133 VAL   B C   1 
ATOM   3515 O  O   . VAL   B  1  120 ? 8.857   -2.285  69.911 1.00 40.02  ? 133 VAL   B O   1 
ATOM   3516 C  CB  . VAL   B  1  120 ? 8.837   0.817   70.221 1.00 52.53  ? 133 VAL   B CB  1 
ATOM   3517 C  CG1 . VAL   B  1  120 ? 8.111   0.676   71.559 1.00 51.02  ? 133 VAL   B CG1 1 
ATOM   3518 C  CG2 . VAL   B  1  120 ? 9.289   2.257   70.017 1.00 48.71  ? 133 VAL   B CG2 1 
ATOM   3519 N  N   . HIS   B  1  121 ? 10.160  -1.930  71.730 1.00 41.57  ? 134 HIS   B N   1 
ATOM   3520 C  CA  . HIS   B  1  121 ? 10.092  -3.271  72.281 1.00 47.06  ? 134 HIS   B CA  1 
ATOM   3521 C  C   . HIS   B  1  121 ? 8.863   -3.442  73.170 1.00 48.29  ? 134 HIS   B C   1 
ATOM   3522 O  O   . HIS   B  1  121 ? 8.443   -2.497  73.836 1.00 44.82  ? 134 HIS   B O   1 
ATOM   3523 C  CB  . HIS   B  1  121 ? 11.330  -3.508  73.144 1.00 43.45  ? 134 HIS   B CB  1 
ATOM   3524 C  CG  . HIS   B  1  121 ? 11.325  -4.810  73.870 1.00 48.55  ? 134 HIS   B CG  1 
ATOM   3525 N  ND1 . HIS   B  1  121 ? 11.461  -6.018  73.215 1.00 44.88  ? 134 HIS   B ND1 1 
ATOM   3526 C  CD2 . HIS   B  1  121 ? 11.175  -5.102  75.184 1.00 45.40  ? 134 HIS   B CD2 1 
ATOM   3527 C  CE1 . HIS   B  1  121 ? 11.438  -6.999  74.110 1.00 49.48  ? 134 HIS   B CE1 1 
ATOM   3528 N  NE2 . HIS   B  1  121 ? 11.256  -6.465  75.307 1.00 49.20  ? 134 HIS   B NE2 1 
ATOM   3529 N  N   . GLY   B  1  122 ? 8.291   -4.654  73.159 1.00 48.49  ? 135 GLY   B N   1 
ATOM   3530 C  CA  . GLY   B  1  122 ? 7.489   -5.123  74.278 1.00 53.25  ? 135 GLY   B CA  1 
ATOM   3531 C  C   . GLY   B  1  122 ? 6.025   -5.426  73.945 1.00 56.68  ? 135 GLY   B C   1 
ATOM   3532 O  O   . GLY   B  1  122 ? 5.408   -6.211  74.668 1.00 51.62  ? 135 GLY   B O   1 
ATOM   3533 N  N   . THR   B  1  123 ? 5.464   -4.792  72.904 1.00 56.22  ? 136 THR   B N   1 
ATOM   3534 C  CA  . THR   B  1  123 ? 4.084   -5.074  72.523 1.00 58.61  ? 136 THR   B CA  1 
ATOM   3535 C  C   . THR   B  1  123 ? 4.044   -5.742  71.148 1.00 57.71  ? 136 THR   B C   1 
ATOM   3536 O  O   . THR   B  1  123 ? 3.318   -6.719  70.998 1.00 49.53  ? 136 THR   B O   1 
ATOM   3537 C  CB  . THR   B  1  123 ? 3.220   -3.817  72.554 1.00 55.62  ? 136 THR   B CB  1 
ATOM   3538 O  OG1 . THR   B  1  123 ? 3.650   -3.097  73.700 1.00 57.04  ? 136 THR   B OG1 1 
ATOM   3539 C  CG2 . THR   B  1  123 ? 1.734   -4.151  72.544 1.00 51.24  ? 136 THR   B CG2 1 
ATOM   3540 N  N   . PHE   B  1  124 ? 4.837   -5.227  70.184 1.00 52.60  ? 137 PHE   B N   1 
ATOM   3541 C  CA  . PHE   B  1  124 ? 5.037   -5.868  68.884 1.00 49.71  ? 137 PHE   B CA  1 
ATOM   3542 C  C   . PHE   B  1  124 ? 6.408   -6.565  68.844 1.00 46.14  ? 137 PHE   B C   1 
ATOM   3543 O  O   . PHE   B  1  124 ? 6.479   -7.781  69.063 1.00 43.27  ? 137 PHE   B O   1 
ATOM   3544 C  CB  . PHE   B  1  124 ? 4.871   -4.845  67.755 1.00 43.39  ? 137 PHE   B CB  1 
ATOM   3545 C  CG  . PHE   B  1  124 ? 4.778   -5.385  66.329 1.00 41.25  ? 137 PHE   B CG  1 
ATOM   3546 C  CD1 . PHE   B  1  124 ? 4.980   -6.732  66.037 1.00 45.33  ? 137 PHE   B CD1 1 
ATOM   3547 C  CD2 . PHE   B  1  124 ? 4.513   -4.523  65.267 1.00 40.86  ? 137 PHE   B CD2 1 
ATOM   3548 C  CE1 . PHE   B  1  124 ? 4.867   -7.210  64.731 1.00 47.55  ? 137 PHE   B CE1 1 
ATOM   3549 C  CE2 . PHE   B  1  124 ? 4.397   -5.001  63.967 1.00 42.72  ? 137 PHE   B CE2 1 
ATOM   3550 C  CZ  . PHE   B  1  124 ? 4.579   -6.345  63.697 1.00 42.21  ? 137 PHE   B CZ  1 
ATOM   3551 N  N   . GLU   B  1  125 ? 7.489   -5.812  68.555 1.00 42.76  ? 138 GLU   B N   1 
ATOM   3552 C  CA  . GLU   B  1  125 ? 8.836   -6.369  68.532 1.00 44.97  ? 138 GLU   B CA  1 
ATOM   3553 C  C   . GLU   B  1  125 ? 9.109   -7.101  69.849 1.00 44.97  ? 138 GLU   B C   1 
ATOM   3554 O  O   . GLU   B  1  125 ? 8.842   -6.570  70.925 1.00 48.24  ? 138 GLU   B O   1 
ATOM   3555 C  CB  . GLU   B  1  125 ? 9.869   -5.262  68.291 1.00 45.67  ? 138 GLU   B CB  1 
ATOM   3556 C  CG  . GLU   B  1  125 ? 11.316  -5.742  68.166 1.00 48.29  ? 138 GLU   B CG  1 
ATOM   3557 C  CD  . GLU   B  1  125 ? 12.009  -6.324  69.401 1.00 50.79  ? 138 GLU   B CD  1 
ATOM   3558 O  OE1 . GLU   B  1  125 ? 11.841  -5.744  70.501 1.00 49.01  ? 138 GLU   B OE1 1 
ATOM   3559 O  OE2 . GLU   B  1  125 ? 12.741  -7.350  69.262 1.00 48.18  ? 138 GLU   B OE2 1 
ATOM   3560 N  N   . GLY   B  1  126 ? 9.670   -8.307  69.758 1.00 39.06  ? 139 GLY   B N   1 
ATOM   3561 C  CA  . GLY   B  1  126 ? 10.000  -9.095  70.926 1.00 41.22  ? 139 GLY   B CA  1 
ATOM   3562 C  C   . GLY   B  1  126 ? 11.141  -10.080 70.660 1.00 39.94  ? 139 GLY   B C   1 
ATOM   3563 O  O   . GLY   B  1  126 ? 11.905  -9.924  69.725 1.00 41.12  ? 139 GLY   B O   1 
ATOM   3564 N  N   . ASP   B  1  127 ? 11.202  -11.121 71.490 1.00 40.75  ? 140 ASP   B N   1 
ATOM   3565 C  CA  . ASP   B  1  127 ? 12.418  -11.859 71.757 1.00 39.35  ? 140 ASP   B CA  1 
ATOM   3566 C  C   . ASP   B  1  127 ? 12.511  -13.141 70.919 1.00 37.50  ? 140 ASP   B C   1 
ATOM   3567 O  O   . ASP   B  1  127 ? 11.550  -13.578 70.306 1.00 37.28  ? 140 ASP   B O   1 
ATOM   3568 C  CB  . ASP   B  1  127 ? 12.517  -12.168 73.247 1.00 38.49  ? 140 ASP   B CB  1 
ATOM   3569 C  CG  . ASP   B  1  127 ? 12.524  -10.979 74.198 1.00 44.29  ? 140 ASP   B CG  1 
ATOM   3570 O  OD1 . ASP   B  1  127 ? 13.096  -9.926  73.831 1.00 49.66  ? 140 ASP   B OD1 1 
ATOM   3571 O  OD2 . ASP   B  1  127 ? 11.959  -11.119 75.319 1.00 51.46  ? 140 ASP   B OD2 1 
ATOM   3572 N  N   . ALA   B  1  128 ? 13.689  -13.775 70.959 1.00 35.73  ? 141 ALA   B N   1 
ATOM   3573 C  CA  . ALA   B  1  128 ? 13.955  -15.059 70.323 1.00 38.29  ? 141 ALA   B CA  1 
ATOM   3574 C  C   . ALA   B  1  128 ? 13.848  -14.947 68.795 1.00 37.19  ? 141 ALA   B C   1 
ATOM   3575 O  O   . ALA   B  1  128 ? 13.382  -15.854 68.109 1.00 35.79  ? 141 ALA   B O   1 
ATOM   3576 C  CB  . ALA   B  1  128 ? 13.066  -16.150 70.885 1.00 37.47  ? 141 ALA   B CB  1 
ATOM   3577 N  N   . GLY   B  1  129 ? 14.360  -13.844 68.256 1.00 31.38  ? 142 GLY   B N   1 
ATOM   3578 C  CA  . GLY   B  1  129 ? 14.484  -13.691 66.818 1.00 32.93  ? 142 GLY   B CA  1 
ATOM   3579 C  C   . GLY   B  1  129 ? 15.610  -14.542 66.256 1.00 36.68  ? 142 GLY   B C   1 
ATOM   3580 O  O   . GLY   B  1  129 ? 16.422  -15.083 67.007 1.00 36.56  ? 142 GLY   B O   1 
ATOM   3581 N  N   . MET   B  1  130 ? 15.637  -14.638 64.920 1.00 36.17  ? 143 MET   B N   1 
ATOM   3582 C  CA  . MET   B  1  130 ? 16.574  -15.472 64.195 1.00 38.41  ? 143 MET   B CA  1 
ATOM   3583 C  C   . MET   B  1  130 ? 17.919  -14.769 64.022 1.00 38.60  ? 143 MET   B C   1 
ATOM   3584 O  O   . MET   B  1  130 ? 18.945  -15.414 64.189 1.00 34.76  ? 143 MET   B O   1 
ATOM   3585 C  CB  . MET   B  1  130 ? 16.015  -15.834 62.817 1.00 39.67  ? 143 MET   B CB  1 
ATOM   3586 C  CG  . MET   B  1  130 ? 14.927  -16.900 62.838 1.00 42.42  ? 143 MET   B CG  1 
ATOM   3587 S  SD  . MET   B  1  130 ? 14.096  -17.138 61.245 1.00 43.27  ? 143 MET   B SD  1 
ATOM   3588 C  CE  . MET   B  1  130 ? 13.463  -15.518 60.788 1.00 39.22  ? 143 MET   B CE  1 
ATOM   3589 N  N   . THR   B  1  131 ? 17.906  -13.491 63.615 1.00 33.20  ? 144 THR   B N   1 
ATOM   3590 C  CA  . THR   B  1  131 ? 19.130  -12.784 63.283 1.00 35.44  ? 144 THR   B CA  1 
ATOM   3591 C  C   . THR   B  1  131 ? 19.258  -11.500 64.099 1.00 38.32  ? 144 THR   B C   1 
ATOM   3592 O  O   . THR   B  1  131 ? 20.194  -10.735 63.879 1.00 33.46  ? 144 THR   B O   1 
ATOM   3593 C  CB  . THR   B  1  131 ? 19.198  -12.484 61.779 1.00 35.42  ? 144 THR   B CB  1 
ATOM   3594 O  OG1 . THR   B  1  131 ? 18.248  -11.480 61.440 1.00 30.67  ? 144 THR   B OG1 1 
ATOM   3595 C  CG2 . THR   B  1  131 ? 18.962  -13.709 60.912 1.00 36.00  ? 144 THR   B CG2 1 
ATOM   3596 N  N   . ARG   B  1  132 ? 18.298  -11.220 64.990 1.00 37.77  ? 145 ARG   B N   1 
ATOM   3597 C  CA  . ARG   B  1  132 ? 18.370  -10.068 65.882 1.00 35.51  ? 145 ARG   B CA  1 
ATOM   3598 C  C   . ARG   B  1  132 ? 18.357  -10.558 67.330 1.00 34.36  ? 145 ARG   B C   1 
ATOM   3599 O  O   . ARG   B  1  132 ? 17.659  -11.515 67.631 1.00 36.03  ? 145 ARG   B O   1 
ATOM   3600 C  CB  . ARG   B  1  132 ? 17.212  -9.111  65.617 1.00 35.21  ? 145 ARG   B CB  1 
ATOM   3601 C  CG  . ARG   B  1  132 ? 17.451  -8.069  64.543 1.00 37.94  ? 145 ARG   B CG  1 
ATOM   3602 C  CD  . ARG   B  1  132 ? 17.534  -8.627  63.125 1.00 41.47  ? 145 ARG   B CD  1 
ATOM   3603 N  NE  . ARG   B  1  132 ? 17.853  -7.525  62.216 1.00 46.69  ? 145 ARG   B NE  1 
ATOM   3604 C  CZ  . ARG   B  1  132 ? 18.265  -7.651  60.953 1.00 50.94  ? 145 ARG   B CZ  1 
ATOM   3605 N  NH1 . ARG   B  1  132 ? 18.449  -8.840  60.387 1.00 42.68  ? 145 ARG   B NH1 1 
ATOM   3606 N  NH2 . ARG   B  1  132 ? 18.525  -6.567  60.252 1.00 51.51  ? 145 ARG   B NH2 1 
ATOM   3607 N  N   . ALA   B  1  133 ? 19.128  -9.900  68.209 1.00 38.79  ? 146 ALA   B N   1 
ATOM   3608 C  CA  . ALA   B  1  133 ? 19.251  -10.271 69.615 1.00 37.66  ? 146 ALA   B CA  1 
ATOM   3609 C  C   . ALA   B  1  133 ? 18.105  -9.621  70.406 1.00 38.56  ? 146 ALA   B C   1 
ATOM   3610 O  O   . ALA   B  1  133 ? 17.555  -8.593  70.007 1.00 33.67  ? 146 ALA   B O   1 
ATOM   3611 N  N   . ASP   B  1  134 ? 17.771  -10.218 71.557 1.00 40.36  ? 147 ASP   B N   1 
ATOM   3612 C  CA  . ASP   B  1  134 ? 16.757  -9.697  72.468 1.00 39.61  ? 147 ASP   B CA  1 
ATOM   3613 C  C   . ASP   B  1  134 ? 17.139  -8.286  72.905 1.00 42.46  ? 147 ASP   B C   1 
ATOM   3614 O  O   . ASP   B  1  134 ? 18.321  -7.972  73.008 1.00 44.93  ? 147 ASP   B O   1 
ATOM   3615 C  CB  . ASP   B  1  134 ? 16.555  -10.622 73.656 1.00 35.66  ? 147 ASP   B CB  1 
ATOM   3616 C  CG  . ASP   B  1  134 ? 16.065  -12.024 73.309 1.00 40.35  ? 147 ASP   B CG  1 
ATOM   3617 O  OD1 . ASP   B  1  134 ? 15.928  -12.324 72.096 1.00 37.98  ? 147 ASP   B OD1 1 
ATOM   3618 O  OD2 . ASP   B  1  134 ? 15.806  -12.814 74.244 1.00 40.21  ? 147 ASP   B OD2 1 
ATOM   3619 N  N   . GLU   B  1  135 ? 16.121  -7.446  73.136 1.00 47.33  ? 148 GLU   B N   1 
ATOM   3620 C  CA  . GLU   B  1  135 ? 16.301  -6.058  73.542 1.00 48.72  ? 148 GLU   B CA  1 
ATOM   3621 C  C   . GLU   B  1  135 ? 17.084  -5.952  74.855 1.00 49.28  ? 148 GLU   B C   1 
ATOM   3622 O  O   . GLU   B  1  135 ? 17.811  -4.982  75.060 1.00 46.02  ? 148 GLU   B O   1 
ATOM   3623 C  CB  . GLU   B  1  135 ? 14.955  -5.357  73.701 1.00 51.84  ? 148 GLU   B CB  1 
ATOM   3624 C  CG  . GLU   B  1  135 ? 15.071  -3.847  73.924 1.00 60.53  ? 148 GLU   B CG  1 
ATOM   3625 C  CD  . GLU   B  1  135 ? 15.155  -3.381  75.376 1.00 65.32  ? 148 GLU   B CD  1 
ATOM   3626 O  OE1 . GLU   B  1  135 ? 15.159  -4.213  76.324 1.00 62.41  ? 148 GLU   B OE1 1 
ATOM   3627 O  OE2 . GLU   B  1  135 ? 15.192  -2.144  75.547 1.00 73.00  ? 148 GLU   B OE2 1 
ATOM   3628 N  N   . PHE   B  1  136 ? 16.930  -6.945  75.735 1.00 49.92  ? 149 PHE   B N   1 
ATOM   3629 C  CA  . PHE   B  1  136 ? 17.644  -6.989  76.999 1.00 57.43  ? 149 PHE   B CA  1 
ATOM   3630 C  C   . PHE   B  1  136 ? 19.151  -6.807  76.799 1.00 58.26  ? 149 PHE   B C   1 
ATOM   3631 O  O   . PHE   B  1  136 ? 19.790  -6.183  77.635 1.00 57.99  ? 149 PHE   B O   1 
ATOM   3632 C  CB  . PHE   B  1  136 ? 17.419  -8.309  77.741 1.00 63.47  ? 149 PHE   B CB  1 
ATOM   3633 C  CG  . PHE   B  1  136 ? 18.202  -8.376  79.045 1.00 70.22  ? 149 PHE   B CG  1 
ATOM   3634 C  CD1 . PHE   B  1  136 ? 17.876  -7.533  80.110 1.00 73.71  ? 149 PHE   B CD1 1 
ATOM   3635 C  CD2 . PHE   B  1  136 ? 19.262  -9.265  79.198 1.00 65.47  ? 149 PHE   B CD2 1 
ATOM   3636 C  CE1 . PHE   B  1  136 ? 18.582  -7.593  81.298 1.00 73.56  ? 149 PHE   B CE1 1 
ATOM   3637 C  CE2 . PHE   B  1  136 ? 19.962  -9.323  80.394 1.00 69.94  ? 149 PHE   B CE2 1 
ATOM   3638 C  CZ  . PHE   B  1  136 ? 19.632  -8.478  81.433 1.00 72.31  ? 149 PHE   B CZ  1 
ATOM   3639 N  N   . PHE   B  1  137 ? 19.708  -7.345  75.703 1.00 50.89  ? 150 PHE   B N   1 
ATOM   3640 C  CA  . PHE   B  1  137 ? 21.142  -7.296  75.471 1.00 48.37  ? 150 PHE   B CA  1 
ATOM   3641 C  C   . PHE   B  1  137 ? 21.585  -6.002  74.782 1.00 47.61  ? 150 PHE   B C   1 
ATOM   3642 O  O   . PHE   B  1  137 ? 22.768  -5.855  74.500 1.00 52.39  ? 150 PHE   B O   1 
ATOM   3643 C  CB  . PHE   B  1  137 ? 21.560  -8.523  74.663 1.00 45.19  ? 150 PHE   B CB  1 
ATOM   3644 C  CG  . PHE   B  1  137 ? 21.164  -9.851  75.293 1.00 47.57  ? 150 PHE   B CG  1 
ATOM   3645 C  CD1 . PHE   B  1  137 ? 21.567  -10.180 76.582 1.00 49.18  ? 150 PHE   B CD1 1 
ATOM   3646 C  CD2 . PHE   B  1  137 ? 20.378  -10.770 74.598 1.00 46.94  ? 150 PHE   B CD2 1 
ATOM   3647 C  CE1 . PHE   B  1  137 ? 21.226  -11.418 77.142 1.00 53.23  ? 150 PHE   B CE1 1 
ATOM   3648 C  CE2 . PHE   B  1  137 ? 20.019  -11.992 75.162 1.00 51.26  ? 150 PHE   B CE2 1 
ATOM   3649 C  CZ  . PHE   B  1  137 ? 20.442  -12.319 76.433 1.00 54.98  ? 150 PHE   B CZ  1 
ATOM   3650 N  N   . GLY   B  1  138 ? 20.678  -5.062  74.488 1.00 45.07  ? 151 GLY   B N   1 
ATOM   3651 C  CA  . GLY   B  1  138 ? 21.100  -3.707  74.128 1.00 49.38  ? 151 GLY   B CA  1 
ATOM   3652 C  C   . GLY   B  1  138 ? 20.775  -3.283  72.688 1.00 54.71  ? 151 GLY   B C   1 
ATOM   3653 O  O   . GLY   B  1  138 ? 20.809  -2.088  72.380 1.00 51.85  ? 151 GLY   B O   1 
ATOM   3654 N  N   . ASP   B  1  139 ? 20.486  -4.245  71.793 1.00 54.50  ? 152 ASP   B N   1 
ATOM   3655 C  CA  . ASP   B  1  139 ? 20.235  -3.934  70.390 1.00 55.68  ? 152 ASP   B CA  1 
ATOM   3656 C  C   . ASP   B  1  139 ? 19.282  -4.955  69.761 1.00 47.59  ? 152 ASP   B C   1 
ATOM   3657 O  O   . ASP   B  1  139 ? 19.664  -6.088  69.471 1.00 42.20  ? 152 ASP   B O   1 
ATOM   3658 C  CB  . ASP   B  1  139 ? 21.542  -3.848  69.607 1.00 59.44  ? 152 ASP   B CB  1 
ATOM   3659 C  CG  . ASP   B  1  139 ? 21.411  -3.391  68.160 1.00 60.33  ? 152 ASP   B CG  1 
ATOM   3660 O  OD1 . ASP   B  1  139 ? 20.293  -3.485  67.621 1.00 60.29  ? 152 ASP   B OD1 1 
ATOM   3661 O  OD2 . ASP   B  1  139 ? 22.425  -2.915  67.590 1.00 63.92  ? 152 ASP   B OD2 1 
ATOM   3662 N  N   . ASN   B  1  140 ? 18.053  -4.517  69.490 1.00 42.17  ? 153 ASN   B N   1 
ATOM   3663 C  CA  . ASN   B  1  140 ? 17.008  -5.413  69.027 1.00 44.77  ? 153 ASN   B CA  1 
ATOM   3664 C  C   . ASN   B  1  140 ? 16.786  -5.294  67.522 1.00 40.60  ? 153 ASN   B C   1 
ATOM   3665 O  O   . ASN   B  1  140 ? 15.879  -5.950  67.021 1.00 43.87  ? 153 ASN   B O   1 
ATOM   3666 C  CB  . ASN   B  1  140 ? 15.684  -5.187  69.760 1.00 42.22  ? 153 ASN   B CB  1 
ATOM   3667 C  CG  . ASN   B  1  140 ? 15.038  -3.854  69.451 1.00 47.85  ? 153 ASN   B CG  1 
ATOM   3668 O  OD1 . ASN   B  1  140 ? 15.655  -2.947  68.866 1.00 45.28  ? 153 ASN   B OD1 1 
ATOM   3669 N  ND2 . ASN   B  1  140 ? 13.792  -3.709  69.881 1.00 49.73  ? 153 ASN   B ND2 1 
ATOM   3670 N  N   . HIS   B  1  141 ? 17.575  -4.466  66.825 1.00 40.24  ? 154 HIS   B N   1 
ATOM   3671 C  CA  . HIS   B  1  141 ? 17.303  -4.126  65.434 1.00 45.23  ? 154 HIS   B CA  1 
ATOM   3672 C  C   . HIS   B  1  141 ? 18.437  -4.545  64.485 1.00 38.71  ? 154 HIS   B C   1 
ATOM   3673 O  O   . HIS   B  1  141 ? 18.176  -4.871  63.334 1.00 43.63  ? 154 HIS   B O   1 
ATOM   3674 C  CB  . HIS   B  1  141 ? 16.923  -2.644  65.318 1.00 47.00  ? 154 HIS   B CB  1 
ATOM   3675 C  CG  . HIS   B  1  141 ? 17.920  -1.708  65.894 1.00 56.86  ? 154 HIS   B CG  1 
ATOM   3676 N  ND1 . HIS   B  1  141 ? 17.998  -1.396  67.236 1.00 60.62  ? 154 HIS   B ND1 1 
ATOM   3677 C  CD2 . HIS   B  1  141 ? 18.885  -1.004  65.296 1.00 64.17  ? 154 HIS   B CD2 1 
ATOM   3678 C  CE1 . HIS   B  1  141 ? 18.995  -0.547  67.434 1.00 62.51  ? 154 HIS   B CE1 1 
ATOM   3679 N  NE2 . HIS   B  1  141 ? 19.547  -0.298  66.269 1.00 65.44  ? 154 HIS   B NE2 1 
ATOM   3680 N  N   . SER   B  1  142 ? 19.691  -4.506  64.946 1.00 43.53  ? 155 SER   B N   1 
ATOM   3681 C  CA  . SER   B  1  142 ? 20.845  -4.785  64.102 1.00 44.04  ? 155 SER   B CA  1 
ATOM   3682 C  C   . SER   B  1  142 ? 20.934  -6.268  63.768 1.00 43.34  ? 155 SER   B C   1 
ATOM   3683 O  O   . SER   B  1  142 ? 20.643  -7.124  64.595 1.00 40.59  ? 155 SER   B O   1 
ATOM   3684 C  CB  . SER   B  1  142 ? 22.144  -4.356  64.762 1.00 45.45  ? 155 SER   B CB  1 
ATOM   3685 O  OG  . SER   B  1  142 ? 22.252  -2.941  64.784 1.00 53.19  ? 155 SER   B OG  1 
ATOM   3686 N  N   . PHE   B  1  143 ? 21.442  -6.549  62.572 1.00 44.19  ? 156 PHE   B N   1 
ATOM   3687 C  CA  . PHE   B  1  143 ? 21.871  -7.883  62.223 1.00 35.62  ? 156 PHE   B CA  1 
ATOM   3688 C  C   . PHE   B  1  143 ? 22.959  -8.312  63.199 1.00 37.69  ? 156 PHE   B C   1 
ATOM   3689 O  O   . PHE   B  1  143 ? 23.868  -7.549  63.502 1.00 36.33  ? 156 PHE   B O   1 
ATOM   3690 C  CB  . PHE   B  1  143 ? 22.361  -7.894  60.774 1.00 34.85  ? 156 PHE   B CB  1 
ATOM   3691 C  CG  . PHE   B  1  143 ? 22.946  -9.227  60.344 1.00 34.64  ? 156 PHE   B CG  1 
ATOM   3692 C  CD1 . PHE   B  1  143 ? 22.126  -10.246 59.859 1.00 32.54  ? 156 PHE   B CD1 1 
ATOM   3693 C  CD2 . PHE   B  1  143 ? 24.299  -9.476  60.464 1.00 34.22  ? 156 PHE   B CD2 1 
ATOM   3694 C  CE1 . PHE   B  1  143 ? 22.650  -11.472 59.472 1.00 33.84  ? 156 PHE   B CE1 1 
ATOM   3695 C  CE2 . PHE   B  1  143 ? 24.817  -10.711 60.085 1.00 37.13  ? 156 PHE   B CE2 1 
ATOM   3696 C  CZ  . PHE   B  1  143 ? 23.988  -11.699 59.570 1.00 36.84  ? 156 PHE   B CZ  1 
ATOM   3697 N  N   . ASN   B  1  144 ? 22.867  -9.567  63.636 1.00 37.88  ? 157 ASN   B N   1 
ATOM   3698 C  CA  . ASN   B  1  144 ? 23.797  -10.141 64.578 1.00 36.25  ? 157 ASN   B CA  1 
ATOM   3699 C  C   . ASN   B  1  144 ? 24.390  -11.415 63.975 1.00 38.95  ? 157 ASN   B C   1 
ATOM   3700 O  O   . ASN   B  1  144 ? 23.701  -12.424 63.814 1.00 32.61  ? 157 ASN   B O   1 
ATOM   3701 C  CB  . ASN   B  1  144 ? 23.068  -10.322 65.890 1.00 38.13  ? 157 ASN   B CB  1 
ATOM   3702 C  CG  . ASN   B  1  144 ? 23.859  -11.069 66.931 1.00 41.90  ? 157 ASN   B CG  1 
ATOM   3703 O  OD1 . ASN   B  1  144 ? 24.410  -12.131 66.629 1.00 38.74  ? 157 ASN   B OD1 1 
ATOM   3704 N  ND2 . ASN   B  1  144 ? 23.904  -10.524 68.146 1.00 52.40  ? 157 ASN   B ND2 1 
ATOM   3705 N  N   . GLN   B  1  145 ? 25.697  -11.350 63.692 1.00 38.47  ? 158 GLN   B N   1 
ATOM   3706 C  CA  . GLN   B  1  145 ? 26.431  -12.368 62.965 1.00 39.83  ? 158 GLN   B CA  1 
ATOM   3707 C  C   . GLN   B  1  145 ? 26.458  -13.688 63.742 1.00 38.70  ? 158 GLN   B C   1 
ATOM   3708 O  O   . GLN   B  1  145 ? 26.380  -14.753 63.133 1.00 33.39  ? 158 GLN   B O   1 
ATOM   3709 C  CB  . GLN   B  1  145 ? 27.843  -11.847 62.638 1.00 40.77  ? 158 GLN   B CB  1 
ATOM   3710 C  CG  . GLN   B  1  145 ? 28.691  -12.779 61.769 1.00 36.97  ? 158 GLN   B CG  1 
ATOM   3711 C  CD  . GLN   B  1  145 ? 28.084  -13.082 60.407 1.00 43.47  ? 158 GLN   B CD  1 
ATOM   3712 O  OE1 . GLN   B  1  145 ? 27.785  -12.191 59.601 1.00 36.27  ? 158 GLN   B OE1 1 
ATOM   3713 N  NE2 . GLN   B  1  145 ? 27.924  -14.362 60.112 1.00 46.38  ? 158 GLN   B NE2 1 
ATOM   3714 N  N   . THR   B  1  146 ? 26.575  -13.618 65.074 1.00 33.58  ? 159 THR   B N   1 
ATOM   3715 C  CA  . THR   B  1  146 ? 26.601  -14.812 65.908 1.00 35.85  ? 159 THR   B CA  1 
ATOM   3716 C  C   . THR   B  1  146 ? 25.297  -15.579 65.729 1.00 36.06  ? 159 THR   B C   1 
ATOM   3717 O  O   . THR   B  1  146 ? 25.289  -16.810 65.674 1.00 36.57  ? 159 THR   B O   1 
ATOM   3718 C  CB  . THR   B  1  146 ? 26.757  -14.443 67.389 1.00 42.04  ? 159 THR   B CB  1 
ATOM   3719 O  OG1 . THR   B  1  146 ? 27.916  -13.634 67.541 1.00 45.70  ? 159 THR   B OG1 1 
ATOM   3720 C  CG2 . THR   B  1  146 ? 26.852  -15.663 68.287 1.00 39.87  ? 159 THR   B CG2 1 
ATOM   3721 N  N   . LEU   B  1  147 ? 24.179  -14.850 65.713 1.00 32.71  ? 160 LEU   B N   1 
ATOM   3722 C  CA  . LEU   B  1  147 ? 22.889  -15.501 65.533 1.00 35.96  ? 160 LEU   B CA  1 
ATOM   3723 C  C   . LEU   B  1  147 ? 22.745  -16.064 64.123 1.00 31.28  ? 160 LEU   B C   1 
ATOM   3724 O  O   . LEU   B  1  147 ? 22.193  -17.146 63.922 1.00 31.38  ? 160 LEU   B O   1 
ATOM   3725 C  CB  . LEU   B  1  147 ? 21.792  -14.509 65.890 1.00 37.04  ? 160 LEU   B CB  1 
ATOM   3726 C  CG  . LEU   B  1  147 ? 21.636  -14.221 67.387 1.00 39.17  ? 160 LEU   B CG  1 
ATOM   3727 C  CD1 . LEU   B  1  147 ? 20.468  -13.246 67.588 1.00 42.16  ? 160 LEU   B CD1 1 
ATOM   3728 C  CD2 . LEU   B  1  147 ? 21.405  -15.524 68.162 1.00 38.96  ? 160 LEU   B CD2 1 
ATOM   3729 N  N   . PHE   B  1  148 ? 23.271  -15.343 63.143 1.00 31.01  ? 161 PHE   B N   1 
ATOM   3730 C  CA  . PHE   B  1  148 ? 23.257  -15.829 61.779 1.00 32.14  ? 161 PHE   B CA  1 
ATOM   3731 C  C   . PHE   B  1  148 ? 24.125  -17.084 61.664 1.00 38.15  ? 161 PHE   B C   1 
ATOM   3732 O  O   . PHE   B  1  148 ? 23.766  -17.983 60.908 1.00 35.23  ? 161 PHE   B O   1 
ATOM   3733 C  CB  . PHE   B  1  148 ? 23.683  -14.748 60.793 1.00 32.81  ? 161 PHE   B CB  1 
ATOM   3734 C  CG  . PHE   B  1  148 ? 23.541  -15.227 59.360 1.00 33.34  ? 161 PHE   B CG  1 
ATOM   3735 C  CD1 . PHE   B  1  148 ? 22.290  -15.287 58.754 1.00 34.42  ? 161 PHE   B CD1 1 
ATOM   3736 C  CD2 . PHE   B  1  148 ? 24.643  -15.659 58.639 1.00 33.52  ? 161 PHE   B CD2 1 
ATOM   3737 C  CE1 . PHE   B  1  148 ? 22.160  -15.739 57.451 1.00 33.74  ? 161 PHE   B CE1 1 
ATOM   3738 C  CE2 . PHE   B  1  148 ? 24.504  -16.102 57.331 1.00 34.65  ? 161 PHE   B CE2 1 
ATOM   3739 C  CZ  . PHE   B  1  148 ? 23.270  -16.130 56.733 1.00 32.16  ? 161 PHE   B CZ  1 
ATOM   3740 N  N   . ASP   B  1  149 ? 25.242  -17.160 62.417 1.00 35.69  ? 162 ASP   B N   1 
ATOM   3741 C  CA  . ASP   B  1  149 ? 26.078  -18.356 62.427 1.00 37.04  ? 162 ASP   B CA  1 
ATOM   3742 C  C   . ASP   B  1  149 ? 25.288  -19.562 62.955 1.00 35.89  ? 162 ASP   B C   1 
ATOM   3743 O  O   . ASP   B  1  149 ? 25.431  -20.667 62.457 1.00 33.85  ? 162 ASP   B O   1 
ATOM   3744 C  CB  . ASP   B  1  149 ? 27.377  -18.132 63.195 1.00 40.17  ? 162 ASP   B CB  1 
ATOM   3745 C  CG  . ASP   B  1  149 ? 28.369  -17.159 62.558 1.00 48.63  ? 162 ASP   B CG  1 
ATOM   3746 O  OD1 . ASP   B  1  149 ? 28.305  -16.967 61.310 1.00 48.13  ? 162 ASP   B OD1 1 
ATOM   3747 O  OD2 . ASP   B  1  149 ? 29.166  -16.546 63.321 1.00 53.67  ? 162 ASP   B OD2 1 
ATOM   3748 N  N   . LYS   B  1  150 ? 24.450  -19.360 63.972 1.00 35.10  ? 163 LYS   B N   1 
ATOM   3749 C  CA  . LYS   B  1  150 ? 23.585  -20.426 64.459 1.00 36.17  ? 163 LYS   B CA  1 
ATOM   3750 C  C   . LYS   B  1  150 ? 22.545  -20.828 63.400 1.00 37.01  ? 163 LYS   B C   1 
ATOM   3751 O  O   . LYS   B  1  150 ? 22.237  -22.006 63.240 1.00 38.49  ? 163 LYS   B O   1 
ATOM   3752 C  CB  . LYS   B  1  150 ? 22.924  -19.959 65.755 1.00 37.83  ? 163 LYS   B CB  1 
ATOM   3753 C  CG  . LYS   B  1  150 ? 22.004  -20.982 66.390 1.00 42.66  ? 163 LYS   B CG  1 
ATOM   3754 C  CD  . LYS   B  1  150 ? 21.352  -20.442 67.658 1.00 48.90  ? 163 LYS   B CD  1 
ATOM   3755 C  CE  . LYS   B  1  150 ? 20.340  -21.377 68.278 1.00 53.91  ? 163 LYS   B CE  1 
ATOM   3756 N  NZ  . LYS   B  1  150 ? 20.841  -21.912 69.539 1.00 57.54  ? 163 LYS   B NZ  1 
ATOM   3757 N  N   . PHE   B  1  151 ? 22.015  -19.851 62.656 1.00 35.64  ? 164 PHE   B N   1 
ATOM   3758 C  CA  . PHE   B  1  151 ? 21.092  -20.125 61.559 1.00 34.83  ? 164 PHE   B CA  1 
ATOM   3759 C  C   . PHE   B  1  151 ? 21.757  -21.045 60.534 1.00 31.50  ? 164 PHE   B C   1 
ATOM   3760 O  O   . PHE   B  1  151 ? 21.178  -22.029 60.072 1.00 30.56  ? 164 PHE   B O   1 
ATOM   3761 C  CB  . PHE   B  1  151 ? 20.642  -18.780 60.975 1.00 34.06  ? 164 PHE   B CB  1 
ATOM   3762 C  CG  . PHE   B  1  151 ? 19.742  -18.822 59.753 1.00 34.25  ? 164 PHE   B CG  1 
ATOM   3763 C  CD1 . PHE   B  1  151 ? 20.264  -18.932 58.474 1.00 32.80  ? 164 PHE   B CD1 1 
ATOM   3764 C  CD2 . PHE   B  1  151 ? 18.363  -18.673 59.878 1.00 37.87  ? 164 PHE   B CD2 1 
ATOM   3765 C  CE1 . PHE   B  1  151 ? 19.419  -18.950 57.361 1.00 33.75  ? 164 PHE   B CE1 1 
ATOM   3766 C  CE2 . PHE   B  1  151 ? 17.530  -18.681 58.760 1.00 32.44  ? 164 PHE   B CE2 1 
ATOM   3767 C  CZ  . PHE   B  1  151 ? 18.063  -18.836 57.515 1.00 32.21  ? 164 PHE   B CZ  1 
ATOM   3768 N  N   . VAL   B  1  152 ? 22.994  -20.723 60.183 1.00 31.98  ? 165 VAL   B N   1 
ATOM   3769 C  CA  . VAL   B  1  152 ? 23.775  -21.543 59.267 1.00 33.80  ? 165 VAL   B CA  1 
ATOM   3770 C  C   . VAL   B  1  152 ? 24.009  -22.925 59.885 1.00 35.02  ? 165 VAL   B C   1 
ATOM   3771 O  O   . VAL   B  1  152 ? 23.827  -23.952 59.242 1.00 30.79  ? 165 VAL   B O   1 
ATOM   3772 C  CB  . VAL   B  1  152 ? 25.101  -20.826 58.931 1.00 34.43  ? 165 VAL   B CB  1 
ATOM   3773 C  CG1 . VAL   B  1  152 ? 26.060  -21.733 58.161 1.00 32.40  ? 165 VAL   B CG1 1 
ATOM   3774 C  CG2 . VAL   B  1  152 ? 24.872  -19.507 58.174 1.00 34.02  ? 165 VAL   B CG2 1 
ATOM   3775 N  N   . ASP   B  1  153 ? 24.394  -22.950 61.160 1.00 35.71  ? 166 ASP   B N   1 
ATOM   3776 C  CA  . ASP   B  1  153 ? 24.672  -24.205 61.839 1.00 38.67  ? 166 ASP   B CA  1 
ATOM   3777 C  C   . ASP   B  1  153 ? 23.462  -25.142 61.760 1.00 36.81  ? 166 ASP   B C   1 
ATOM   3778 O  O   . ASP   B  1  153 ? 23.582  -26.316 61.407 1.00 32.27  ? 166 ASP   B O   1 
ATOM   3779 C  CB  . ASP   B  1  153 ? 25.141  -23.951 63.266 1.00 39.88  ? 166 ASP   B CB  1 
ATOM   3780 C  CG  . ASP   B  1  153 ? 25.517  -25.205 64.044 1.00 47.47  ? 166 ASP   B CG  1 
ATOM   3781 O  OD1 . ASP   B  1  153 ? 26.252  -26.059 63.461 1.00 45.72  ? 166 ASP   B OD1 1 
ATOM   3782 O  OD2 . ASP   B  1  153 ? 25.035  -25.330 65.203 1.00 45.19  ? 166 ASP   B OD2 1 
ATOM   3783 N  N   . PHE   B  1  154 ? 22.287  -24.622 62.112 1.00 35.02  ? 167 PHE   B N   1 
ATOM   3784 C  CA  . PHE   B  1  154 ? 21.083  -25.431 62.111 1.00 33.25  ? 167 PHE   B CA  1 
ATOM   3785 C  C   . PHE   B  1  154 ? 20.682  -25.816 60.700 1.00 31.47  ? 167 PHE   B C   1 
ATOM   3786 O  O   . PHE   B  1  154 ? 20.129  -26.896 60.505 1.00 31.96  ? 167 PHE   B O   1 
ATOM   3787 C  CB  . PHE   B  1  154 ? 19.943  -24.700 62.814 1.00 34.57  ? 167 PHE   B CB  1 
ATOM   3788 C  CG  . PHE   B  1  154 ? 19.930  -24.953 64.307 1.00 37.20  ? 167 PHE   B CG  1 
ATOM   3789 C  CD1 . PHE   B  1  154 ? 20.973  -24.524 65.116 1.00 44.89  ? 167 PHE   B CD1 1 
ATOM   3790 C  CD2 . PHE   B  1  154 ? 18.863  -25.605 64.896 1.00 44.02  ? 167 PHE   B CD2 1 
ATOM   3791 C  CE1 . PHE   B  1  154 ? 20.950  -24.743 66.482 1.00 43.52  ? 167 PHE   B CE1 1 
ATOM   3792 C  CE2 . PHE   B  1  154 ? 18.849  -25.831 66.255 1.00 45.24  ? 167 PHE   B CE2 1 
ATOM   3793 C  CZ  . PHE   B  1  154 ? 19.893  -25.396 67.043 1.00 46.58  ? 167 PHE   B CZ  1 
ATOM   3794 N  N   . SER   B  1  155 ? 20.923  -24.941 59.718 1.00 30.55  ? 168 SER   B N   1 
ATOM   3795 C  CA  . SER   B  1  155 ? 20.648  -25.338 58.343 1.00 33.05  ? 168 SER   B CA  1 
ATOM   3796 C  C   . SER   B  1  155 ? 21.561  -26.505 57.950 1.00 35.67  ? 168 SER   B C   1 
ATOM   3797 O  O   . SER   B  1  155 ? 21.168  -27.390 57.185 1.00 37.04  ? 168 SER   B O   1 
ATOM   3798 C  CB  . SER   B  1  155 ? 20.785  -24.171 57.385 1.00 31.24  ? 168 SER   B CB  1 
ATOM   3799 O  OG  . SER   B  1  155 ? 19.951  -23.081 57.747 1.00 29.82  ? 168 SER   B OG  1 
ATOM   3800 N  N   . ASN   B  1  156 ? 22.819  -26.479 58.422 1.00 33.46  ? 169 ASN   B N   1 
ATOM   3801 C  CA  . ASN   B  1  156 ? 23.749  -27.565 58.135 1.00 32.26  ? 169 ASN   B CA  1 
ATOM   3802 C  C   . ASN   B  1  156 ? 23.275  -28.865 58.791 1.00 30.83  ? 169 ASN   B C   1 
ATOM   3803 O  O   . ASN   B  1  156 ? 23.334  -29.914 58.181 1.00 32.33  ? 169 ASN   B O   1 
ATOM   3804 C  CB  . ASN   B  1  156 ? 25.154  -27.288 58.657 1.00 31.09  ? 169 ASN   B CB  1 
ATOM   3805 C  CG  . ASN   B  1  156 ? 25.900  -26.239 57.881 1.00 32.52  ? 169 ASN   B CG  1 
ATOM   3806 O  OD1 . ASN   B  1  156 ? 25.620  -25.985 56.701 1.00 35.19  ? 169 ASN   B OD1 1 
ATOM   3807 N  ND2 . ASN   B  1  156 ? 26.891  -25.662 58.533 1.00 32.31  ? 169 ASN   B ND2 1 
ATOM   3808 N  N   . ARG   B  1  157 ? 22.838  -28.787 60.050 1.00 32.65  ? 170 ARG   B N   1 
ATOM   3809 C  CA  . ARG   B  1  157 ? 22.502  -29.963 60.826 1.00 35.01  ? 170 ARG   B CA  1 
ATOM   3810 C  C   . ARG   B  1  157 ? 21.206  -30.621 60.350 1.00 41.82  ? 170 ARG   B C   1 
ATOM   3811 O  O   . ARG   B  1  157 ? 21.119  -31.843 60.381 1.00 39.75  ? 170 ARG   B O   1 
ATOM   3812 C  CB  . ARG   B  1  157 ? 22.425  -29.574 62.301 1.00 37.16  ? 170 ARG   B CB  1 
ATOM   3813 C  CG  . ARG   B  1  157 ? 23.815  -29.402 62.879 1.00 41.44  ? 170 ARG   B CG  1 
ATOM   3814 C  CD  . ARG   B  1  157 ? 23.827  -28.532 64.135 1.00 44.55  ? 170 ARG   B CD  1 
ATOM   3815 N  NE  . ARG   B  1  157 ? 22.982  -29.067 65.201 1.00 47.92  ? 170 ARG   B NE  1 
ATOM   3816 C  CZ  . ARG   B  1  157 ? 22.802  -28.453 66.362 1.00 49.27  ? 170 ARG   B CZ  1 
ATOM   3817 N  NH1 . ARG   B  1  157 ? 21.952  -28.957 67.241 1.00 54.38  ? 170 ARG   B NH1 1 
ATOM   3818 N  NH2 . ARG   B  1  157 ? 23.429  -27.320 66.634 1.00 45.66  ? 170 ARG   B NH2 1 
ATOM   3819 N  N   . TYR   B  1  158 ? 20.209  -29.830 59.908 1.00 45.21  ? 171 TYR   B N   1 
ATOM   3820 C  CA  . TYR   B  1  158 ? 18.867  -30.353 59.683 1.00 38.36  ? 171 TYR   B CA  1 
ATOM   3821 C  C   . TYR   B  1  158 ? 18.335  -30.121 58.274 1.00 38.59  ? 171 TYR   B C   1 
ATOM   3822 O  O   . TYR   B  1  158 ? 17.305  -30.698 57.923 1.00 42.41  ? 171 TYR   B O   1 
ATOM   3823 C  CB  . TYR   B  1  158 ? 17.878  -29.731 60.663 1.00 39.89  ? 171 TYR   B CB  1 
ATOM   3824 C  CG  . TYR   B  1  158 ? 18.245  -30.000 62.114 1.00 39.82  ? 171 TYR   B CG  1 
ATOM   3825 C  CD1 . TYR   B  1  158 ? 18.073  -31.259 62.693 1.00 43.59  ? 171 TYR   B CD1 1 
ATOM   3826 C  CD2 . TYR   B  1  158 ? 18.746  -28.980 62.908 1.00 36.49  ? 171 TYR   B CD2 1 
ATOM   3827 C  CE1 . TYR   B  1  158 ? 18.396  -31.490 64.024 1.00 43.26  ? 171 TYR   B CE1 1 
ATOM   3828 C  CE2 . TYR   B  1  158 ? 19.073  -29.198 64.236 1.00 42.92  ? 171 TYR   B CE2 1 
ATOM   3829 C  CZ  . TYR   B  1  158 ? 18.906  -30.454 64.793 1.00 45.58  ? 171 TYR   B CZ  1 
ATOM   3830 O  OH  . TYR   B  1  158 ? 19.265  -30.579 66.098 1.00 45.24  ? 171 TYR   B OH  1 
ATOM   3831 N  N   . GLY   B  1  159 ? 19.015  -29.315 57.455 1.00 33.21  ? 172 GLY   B N   1 
ATOM   3832 C  CA  . GLY   B  1  159 ? 18.489  -28.991 56.140 1.00 32.70  ? 172 GLY   B CA  1 
ATOM   3833 C  C   . GLY   B  1  159 ? 19.471  -29.192 54.993 1.00 33.17  ? 172 GLY   B C   1 
ATOM   3834 O  O   . GLY   B  1  159 ? 19.264  -28.620 53.919 1.00 34.35  ? 172 GLY   B O   1 
ATOM   3835 N  N   . GLY   B  1  160 ? 20.522  -30.009 55.189 1.00 34.56  ? 173 GLY   B N   1 
ATOM   3836 C  CA  . GLY   B  1  160 ? 21.445  -30.274 54.095 1.00 34.04  ? 173 GLY   B CA  1 
ATOM   3837 C  C   . GLY   B  1  160 ? 22.257  -29.036 53.700 1.00 32.64  ? 173 GLY   B C   1 
ATOM   3838 O  O   . GLY   B  1  160 ? 22.733  -28.976 52.571 1.00 36.62  ? 173 GLY   B O   1 
ATOM   3839 N  N   . GLY   B  1  161 ? 22.367  -28.041 54.602 1.00 33.70  ? 174 GLY   B N   1 
ATOM   3840 C  CA  . GLY   B  1  161 ? 23.058  -26.790 54.313 1.00 33.90  ? 174 GLY   B CA  1 
ATOM   3841 C  C   . GLY   B  1  161 ? 22.123  -25.676 53.808 1.00 31.83  ? 174 GLY   B C   1 
ATOM   3842 O  O   . GLY   B  1  161 ? 22.576  -24.563 53.503 1.00 31.84  ? 174 GLY   B O   1 
ATOM   3843 N  N   . PHE   B  1  162 ? 20.819  -25.970 53.797 1.00 34.26  ? 175 PHE   B N   1 
ATOM   3844 C  CA  . PHE   B  1  162 ? 19.779  -25.044 53.377 1.00 33.61  ? 175 PHE   B CA  1 
ATOM   3845 C  C   . PHE   B  1  162 ? 18.770  -24.856 54.500 1.00 34.73  ? 175 PHE   B C   1 
ATOM   3846 O  O   . PHE   B  1  162 ? 18.613  -25.739 55.346 1.00 36.29  ? 175 PHE   B O   1 
ATOM   3847 C  CB  . PHE   B  1  162 ? 19.057  -25.569 52.139 1.00 34.79  ? 175 PHE   B CB  1 
ATOM   3848 C  CG  . PHE   B  1  162 ? 19.971  -25.717 50.939 1.00 34.56  ? 175 PHE   B CG  1 
ATOM   3849 C  CD1 . PHE   B  1  162 ? 20.230  -24.626 50.114 1.00 35.22  ? 175 PHE   B CD1 1 
ATOM   3850 C  CD2 . PHE   B  1  162 ? 20.586  -26.935 50.655 1.00 35.80  ? 175 PHE   B CD2 1 
ATOM   3851 C  CE1 . PHE   B  1  162 ? 21.074  -24.748 49.017 1.00 37.91  ? 175 PHE   B CE1 1 
ATOM   3852 C  CE2 . PHE   B  1  162 ? 21.453  -27.049 49.568 1.00 37.24  ? 175 PHE   B CE2 1 
ATOM   3853 C  CZ  . PHE   B  1  162 ? 21.698  -25.952 48.750 1.00 37.02  ? 175 PHE   B CZ  1 
ATOM   3854 N  N   . TYR   B  1  163 ? 18.094  -23.696 54.497 1.00 32.37  ? 176 TYR   B N   1 
ATOM   3855 C  CA  . TYR   B  1  163 ? 17.033  -23.454 55.452 1.00 33.61  ? 176 TYR   B CA  1 
ATOM   3856 C  C   . TYR   B  1  163 ? 15.721  -23.944 54.843 1.00 33.25  ? 176 TYR   B C   1 
ATOM   3857 O  O   . TYR   B  1  163 ? 15.299  -23.464 53.799 1.00 34.23  ? 176 TYR   B O   1 
ATOM   3858 C  CB  . TYR   B  1  163 ? 16.920  -21.970 55.793 1.00 34.49  ? 176 TYR   B CB  1 
ATOM   3859 C  CG  . TYR   B  1  163 ? 15.916  -21.646 56.886 1.00 35.02  ? 176 TYR   B CG  1 
ATOM   3860 C  CD1 . TYR   B  1  163 ? 16.258  -21.790 58.228 1.00 34.43  ? 176 TYR   B CD1 1 
ATOM   3861 C  CD2 . TYR   B  1  163 ? 14.649  -21.159 56.582 1.00 33.82  ? 176 TYR   B CD2 1 
ATOM   3862 C  CE1 . TYR   B  1  163 ? 15.369  -21.462 59.239 1.00 35.00  ? 176 TYR   B CE1 1 
ATOM   3863 C  CE2 . TYR   B  1  163 ? 13.753  -20.823 57.592 1.00 32.63  ? 176 TYR   B CE2 1 
ATOM   3864 C  CZ  . TYR   B  1  163 ? 14.114  -20.969 58.918 1.00 32.03  ? 176 TYR   B CZ  1 
ATOM   3865 O  OH  . TYR   B  1  163 ? 13.243  -20.644 59.912 1.00 29.13  ? 176 TYR   B OH  1 
ATOM   3866 N  N   . ASN   B  1  164 ? 15.107  -24.920 55.508 1.00 34.44  ? 177 ASN   B N   1 
ATOM   3867 C  CA  . ASN   B  1  164 ? 13.814  -25.436 55.092 1.00 34.51  ? 177 ASN   B CA  1 
ATOM   3868 C  C   . ASN   B  1  164 ? 12.944  -25.595 56.338 1.00 33.72  ? 177 ASN   B C   1 
ATOM   3869 O  O   . ASN   B  1  164 ? 13.345  -25.240 57.444 1.00 30.28  ? 177 ASN   B O   1 
ATOM   3870 C  CB  . ASN   B  1  164 ? 13.998  -26.678 54.223 1.00 36.28  ? 177 ASN   B CB  1 
ATOM   3871 C  CG  . ASN   B  1  164 ? 14.353  -27.929 54.997 1.00 36.90  ? 177 ASN   B CG  1 
ATOM   3872 O  OD1 . ASN   B  1  164 ? 14.353  -27.959 56.234 1.00 34.17  ? 177 ASN   B OD1 1 
ATOM   3873 N  ND2 . ASN   B  1  164 ? 14.638  -28.995 54.271 1.00 42.97  ? 177 ASN   B ND2 1 
ATOM   3874 N  N   . LEU   B  1  165 ? 11.755  -26.162 56.164 1.00 36.69  ? 178 LEU   B N   1 
ATOM   3875 C  CA  . LEU   B  1  165 ? 10.797  -26.176 57.253 1.00 37.56  ? 178 LEU   B CA  1 
ATOM   3876 C  C   . LEU   B  1  165 ? 11.278  -27.016 58.443 1.00 38.56  ? 178 LEU   B C   1 
ATOM   3877 O  O   . LEU   B  1  165 ? 10.979  -26.674 59.585 1.00 38.12  ? 178 LEU   B O   1 
ATOM   3878 C  CB  . LEU   B  1  165 ? 9.462   -26.657 56.696 1.00 45.14  ? 178 LEU   B CB  1 
ATOM   3879 C  CG  . LEU   B  1  165 ? 8.222   -26.326 57.525 1.00 47.32  ? 178 LEU   B CG  1 
ATOM   3880 C  CD1 . LEU   B  1  165 ? 7.975   -24.843 57.568 1.00 47.01  ? 178 LEU   B CD1 1 
ATOM   3881 C  CD2 . LEU   B  1  165 ? 7.034   -27.019 56.897 1.00 51.79  ? 178 LEU   B CD2 1 
ATOM   3882 N  N   . THR   B  1  166 ? 12.043  -28.097 58.204 1.00 38.73  ? 179 THR   B N   1 
ATOM   3883 C  CA  . THR   B  1  166 ? 12.610  -28.891 59.296 1.00 35.94  ? 179 THR   B CA  1 
ATOM   3884 C  C   . THR   B  1  166 ? 13.567  -28.033 60.135 1.00 35.68  ? 179 THR   B C   1 
ATOM   3885 O  O   . THR   B  1  166 ? 13.547  -28.035 61.365 1.00 35.87  ? 179 THR   B O   1 
ATOM   3886 C  CB  . THR   B  1  166 ? 13.349  -30.111 58.738 1.00 39.27  ? 179 THR   B CB  1 
ATOM   3887 O  OG1 . THR   B  1  166 ? 12.541  -30.746 57.750 1.00 39.13  ? 179 THR   B OG1 1 
ATOM   3888 C  CG2 . THR   B  1  166 ? 13.749  -31.092 59.826 1.00 42.00  ? 179 THR   B CG2 1 
ATOM   3889 N  N   . VAL   B  1  167 ? 14.405  -27.254 59.454 1.00 34.66  ? 180 VAL   B N   1 
ATOM   3890 C  CA  . VAL   B  1  167 ? 15.337  -26.379 60.147 1.00 36.57  ? 180 VAL   B CA  1 
ATOM   3891 C  C   . VAL   B  1  167 ? 14.564  -25.357 60.977 1.00 33.45  ? 180 VAL   B C   1 
ATOM   3892 O  O   . VAL   B  1  167 ? 14.970  -25.057 62.094 1.00 35.84  ? 180 VAL   B O   1 
ATOM   3893 C  CB  . VAL   B  1  167 ? 16.306  -25.648 59.197 1.00 32.16  ? 180 VAL   B CB  1 
ATOM   3894 C  CG1 . VAL   B  1  167 ? 17.321  -24.835 59.977 1.00 29.79  ? 180 VAL   B CG1 1 
ATOM   3895 C  CG2 . VAL   B  1  167 ? 17.005  -26.596 58.257 1.00 38.71  ? 180 VAL   B CG2 1 
ATOM   3896 N  N   . ALA   B  1  168 ? 13.507  -24.770 60.387 1.00 35.63  ? 181 ALA   B N   1 
ATOM   3897 C  CA  . ALA   B  1  168 ? 12.708  -23.741 61.044 1.00 35.45  ? 181 ALA   B CA  1 
ATOM   3898 C  C   . ALA   B  1  168 ? 12.184  -24.246 62.385 1.00 35.55  ? 181 ALA   B C   1 
ATOM   3899 O  O   . ALA   B  1  168 ? 12.296  -23.549 63.399 1.00 36.47  ? 181 ALA   B O   1 
ATOM   3900 C  CB  . ALA   B  1  168 ? 11.584  -23.294 60.132 1.00 34.03  ? 181 ALA   B CB  1 
ATOM   3901 N  N   . GLY   B  1  169 ? 11.654  -25.478 62.395 1.00 38.42  ? 182 GLY   B N   1 
ATOM   3902 C  CA  . GLY   B  1  169 ? 11.161  -26.061 63.641 1.00 36.94  ? 182 GLY   B CA  1 
ATOM   3903 C  C   . GLY   B  1  169 ? 12.249  -26.154 64.717 1.00 39.35  ? 182 GLY   B C   1 
ATOM   3904 O  O   . GLY   B  1  169 ? 12.033  -25.819 65.882 1.00 38.78  ? 182 GLY   B O   1 
ATOM   3905 N  N   . GLU   B  1  170 ? 13.440  -26.620 64.324 1.00 39.51  ? 183 GLU   B N   1 
ATOM   3906 C  CA  . GLU   B  1  170 ? 14.519  -26.816 65.277 1.00 37.25  ? 183 GLU   B CA  1 
ATOM   3907 C  C   . GLU   B  1  170 ? 15.051  -25.472 65.749 1.00 33.87  ? 183 GLU   B C   1 
ATOM   3908 O  O   . GLU   B  1  170 ? 15.281  -25.279 66.941 1.00 37.01  ? 183 GLU   B O   1 
ATOM   3909 C  CB  . GLU   B  1  170 ? 15.634  -27.658 64.661 1.00 41.54  ? 183 GLU   B CB  1 
ATOM   3910 C  CG  . GLU   B  1  170 ? 15.189  -29.073 64.310 1.00 43.69  ? 183 GLU   B CG  1 
ATOM   3911 C  CD  . GLU   B  1  170 ? 14.820  -29.919 65.514 1.00 53.94  ? 183 GLU   B CD  1 
ATOM   3912 O  OE1 . GLU   B  1  170 ? 15.092  -29.512 66.667 1.00 55.56  ? 183 GLU   B OE1 1 
ATOM   3913 O  OE2 . GLU   B  1  170 ? 14.268  -31.015 65.294 1.00 62.66  ? 183 GLU   B OE2 1 
ATOM   3914 N  N   . LEU   B  1  171 ? 15.253  -24.540 64.813 1.00 34.78  ? 184 LEU   B N   1 
ATOM   3915 C  CA  . LEU   B  1  171 ? 15.871  -23.277 65.172 1.00 34.76  ? 184 LEU   B CA  1 
ATOM   3916 C  C   . LEU   B  1  171 ? 14.959  -22.491 66.106 1.00 33.91  ? 184 LEU   B C   1 
ATOM   3917 O  O   . LEU   B  1  171 ? 15.418  -21.904 67.077 1.00 34.96  ? 184 LEU   B O   1 
ATOM   3918 C  CB  . LEU   B  1  171 ? 16.220  -22.494 63.909 1.00 38.53  ? 184 LEU   B CB  1 
ATOM   3919 C  CG  . LEU   B  1  171 ? 16.887  -21.133 64.141 1.00 37.78  ? 184 LEU   B CG  1 
ATOM   3920 C  CD1 . LEU   B  1  171 ? 18.224  -21.272 64.851 1.00 39.17  ? 184 LEU   B CD1 1 
ATOM   3921 C  CD2 . LEU   B  1  171 ? 17.065  -20.429 62.816 1.00 36.90  ? 184 LEU   B CD2 1 
ATOM   3922 N  N   . ARG   B  1  172 ? 13.653  -22.487 65.823 1.00 36.56  ? 185 ARG   B N   1 
ATOM   3923 C  CA  . ARG   B  1  172 ? 12.715  -21.700 66.610 1.00 37.41  ? 185 ARG   B CA  1 
ATOM   3924 C  C   . ARG   B  1  172 ? 12.756  -22.130 68.078 1.00 36.48  ? 185 ARG   B C   1 
ATOM   3925 O  O   . ARG   B  1  172 ? 12.842  -21.293 68.975 1.00 33.59  ? 185 ARG   B O   1 
ATOM   3926 C  CB  . ARG   B  1  172 ? 11.331  -21.829 65.972 1.00 35.57  ? 185 ARG   B CB  1 
ATOM   3927 C  CG  . ARG   B  1  172 ? 10.126  -21.486 66.832 1.00 37.99  ? 185 ARG   B CG  1 
ATOM   3928 C  CD  . ARG   B  1  172 ? 10.157  -20.151 67.535 1.00 39.24  ? 185 ARG   B CD  1 
ATOM   3929 N  NE  . ARG   B  1  172 ? 10.459  -19.032 66.637 1.00 40.08  ? 185 ARG   B NE  1 
ATOM   3930 C  CZ  . ARG   B  1  172 ? 11.334  -18.075 66.893 1.00 39.44  ? 185 ARG   B CZ  1 
ATOM   3931 N  NH1 . ARG   B  1  172 ? 12.154  -18.182 67.929 1.00 40.23  ? 185 ARG   B NH1 1 
ATOM   3932 N  NH2 . ARG   B  1  172 ? 11.389  -17.015 66.109 1.00 40.54  ? 185 ARG   B NH2 1 
ATOM   3933 N  N   . TYR   B  1  173 ? 12.677  -23.441 68.308 1.00 37.33  ? 186 TYR   B N   1 
ATOM   3934 C  CA  . TYR   B  1  173 ? 12.684  -23.973 69.661 1.00 41.35  ? 186 TYR   B CA  1 
ATOM   3935 C  C   . TYR   B  1  173 ? 14.001  -23.629 70.355 1.00 39.29  ? 186 TYR   B C   1 
ATOM   3936 O  O   . TYR   B  1  173 ? 14.013  -23.221 71.509 1.00 41.00  ? 186 TYR   B O   1 
ATOM   3937 C  CB  . TYR   B  1  173 ? 12.432  -25.485 69.584 1.00 45.97  ? 186 TYR   B CB  1 
ATOM   3938 C  CG  . TYR   B  1  173 ? 12.476  -26.180 70.939 1.00 50.30  ? 186 TYR   B CG  1 
ATOM   3939 C  CD1 . TYR   B  1  173 ? 11.487  -25.944 71.880 1.00 53.41  ? 186 TYR   B CD1 1 
ATOM   3940 C  CD2 . TYR   B  1  173 ? 13.484  -27.079 71.269 1.00 56.93  ? 186 TYR   B CD2 1 
ATOM   3941 C  CE1 . TYR   B  1  173 ? 11.502  -26.565 73.116 1.00 55.65  ? 186 TYR   B CE1 1 
ATOM   3942 C  CE2 . TYR   B  1  173 ? 13.514  -27.706 72.504 1.00 59.44  ? 186 TYR   B CE2 1 
ATOM   3943 C  CZ  . TYR   B  1  173 ? 12.515  -27.448 73.428 1.00 60.75  ? 186 TYR   B CZ  1 
ATOM   3944 O  OH  . TYR   B  1  173 ? 12.480  -28.026 74.659 1.00 61.47  ? 186 TYR   B OH  1 
ATOM   3945 N  N   . SER   B  1  174 ? 15.113  -23.798 69.632 1.00 40.66  ? 187 SER   B N   1 
ATOM   3946 C  CA  . SER   B  1  174 ? 16.430  -23.595 70.206 1.00 40.77  ? 187 SER   B CA  1 
ATOM   3947 C  C   . SER   B  1  174 ? 16.630  -22.135 70.584 1.00 43.77  ? 187 SER   B C   1 
ATOM   3948 O  O   . SER   B  1  174 ? 17.249  -21.844 71.612 1.00 43.72  ? 187 SER   B O   1 
ATOM   3949 C  CB  . SER   B  1  174 ? 17.510  -24.053 69.280 1.00 43.17  ? 187 SER   B CB  1 
ATOM   3950 O  OG  . SER   B  1  174 ? 18.781  -23.762 69.843 1.00 43.27  ? 187 SER   B OG  1 
ATOM   3951 N  N   . ARG   B  1  175 ? 16.084  -21.218 69.776 1.00 40.54  ? 188 ARG   B N   1 
ATOM   3952 C  CA  . ARG   B  1  175 ? 16.203  -19.799 70.080 1.00 43.32  ? 188 ARG   B CA  1 
ATOM   3953 C  C   . ARG   B  1  175 ? 15.390  -19.451 71.327 1.00 39.61  ? 188 ARG   B C   1 
ATOM   3954 O  O   . ARG   B  1  175 ? 15.808  -18.612 72.129 1.00 38.01  ? 188 ARG   B O   1 
ATOM   3955 C  CB  . ARG   B  1  175 ? 15.844  -18.934 68.866 1.00 42.81  ? 188 ARG   B CB  1 
ATOM   3956 C  CG  . ARG   B  1  175 ? 16.876  -18.985 67.745 1.00 40.53  ? 188 ARG   B CG  1 
ATOM   3957 C  CD  . ARG   B  1  175 ? 18.187  -18.323 68.130 1.00 38.20  ? 188 ARG   B CD  1 
ATOM   3958 N  NE  . ARG   B  1  175 ? 17.936  -16.900 68.354 1.00 35.01  ? 188 ARG   B NE  1 
ATOM   3959 C  CZ  . ARG   B  1  175 ? 18.115  -16.212 69.459 1.00 36.76  ? 188 ARG   B CZ  1 
ATOM   3960 N  NH1 . ARG   B  1  175 ? 18.730  -16.771 70.483 1.00 39.24  ? 188 ARG   B NH1 1 
ATOM   3961 N  NH2 . ARG   B  1  175 ? 17.730  -14.931 69.517 1.00 35.30  ? 188 ARG   B NH2 1 
ATOM   3962 N  N   . ILE   B  1  176 ? 14.244  -20.111 71.509 1.00 39.94  ? 189 ILE   B N   1 
ATOM   3963 C  CA  . ILE   B  1  176 ? 13.481  -19.925 72.731 1.00 38.97  ? 189 ILE   B CA  1 
ATOM   3964 C  C   . ILE   B  1  176 ? 14.309  -20.365 73.944 1.00 43.28  ? 189 ILE   B C   1 
ATOM   3965 O  O   . ILE   B  1  176 ? 14.425  -19.621 74.920 1.00 39.62  ? 189 ILE   B O   1 
ATOM   3966 C  CB  . ILE   B  1  176 ? 12.145  -20.667 72.647 1.00 38.64  ? 189 ILE   B CB  1 
ATOM   3967 C  CG1 . ILE   B  1  176 ? 11.226  -20.039 71.601 1.00 40.63  ? 189 ILE   B CG1 1 
ATOM   3968 C  CG2 . ILE   B  1  176 ? 11.469  -20.706 74.024 1.00 39.26  ? 189 ILE   B CG2 1 
ATOM   3969 C  CD1 . ILE   B  1  176 ? 10.059  -20.923 71.198 1.00 39.67  ? 189 ILE   B CD1 1 
ATOM   3970 N  N   . GLN   B  1  177 ? 14.904  -21.564 73.873 1.00 42.77  ? 190 GLN   B N   1 
ATOM   3971 C  CA  . GLN   B  1  177 ? 15.785  -22.045 74.936 1.00 44.37  ? 190 GLN   B CA  1 
ATOM   3972 C  C   . GLN   B  1  177 ? 16.936  -21.065 75.225 1.00 44.71  ? 190 GLN   B C   1 
ATOM   3973 O  O   . GLN   B  1  177 ? 17.233  -20.810 76.388 1.00 46.64  ? 190 GLN   B O   1 
ATOM   3974 C  CB  . GLN   B  1  177 ? 16.306  -23.452 74.635 1.00 45.06  ? 190 GLN   B CB  1 
ATOM   3975 C  CG  . GLN   B  1  177 ? 15.205  -24.502 74.521 1.00 49.86  ? 190 GLN   B CG  1 
ATOM   3976 C  CD  . GLN   B  1  177 ? 14.355  -24.625 75.777 1.00 68.24  ? 190 GLN   B CD  1 
ATOM   3977 O  OE1 . GLN   B  1  177 ? 14.787  -24.376 76.913 1.00 64.56  ? 190 GLN   B OE1 1 
ATOM   3978 N  NE2 . GLN   B  1  177 ? 13.114  -25.041 75.589 1.00 73.51  ? 190 GLN   B NE2 1 
ATOM   3979 N  N   . ASP   B  1  178 ? 17.589  -20.511 74.192 1.00 43.43  ? 191 ASP   B N   1 
ATOM   3980 C  CA  . ASP   B  1  178 ? 18.654  -19.544 74.415 1.00 44.83  ? 191 ASP   B CA  1 
ATOM   3981 C  C   . ASP   B  1  178 ? 18.145  -18.392 75.271 1.00 48.61  ? 191 ASP   B C   1 
ATOM   3982 O  O   . ASP   B  1  178 ? 18.832  -17.963 76.205 1.00 46.71  ? 191 ASP   B O   1 
ATOM   3983 C  CB  . ASP   B  1  178 ? 19.212  -18.913 73.142 1.00 47.38  ? 191 ASP   B CB  1 
ATOM   3984 C  CG  . ASP   B  1  178 ? 19.962  -19.836 72.193 1.00 52.71  ? 191 ASP   B CG  1 
ATOM   3985 O  OD1 . ASP   B  1  178 ? 20.306  -20.969 72.626 1.00 53.80  ? 191 ASP   B OD1 1 
ATOM   3986 O  OD2 . ASP   B  1  178 ? 20.156  -19.427 71.010 1.00 53.86  ? 191 ASP   B OD2 1 
ATOM   3987 N  N   . SER   B  1  179 ? 16.963  -17.864 74.911 1.00 46.02  ? 192 SER   B N   1 
ATOM   3988 C  CA  . SER   B  1  179 ? 16.429  -16.688 75.585 1.00 44.41  ? 192 SER   B CA  1 
ATOM   3989 C  C   . SER   B  1  179 ? 16.019  -17.036 77.020 1.00 43.99  ? 192 SER   B C   1 
ATOM   3990 O  O   . SER   B  1  179 ? 16.220  -16.231 77.918 1.00 42.29  ? 192 SER   B O   1 
ATOM   3991 C  CB  . SER   B  1  179 ? 15.298  -16.041 74.805 1.00 44.81  ? 192 SER   B CB  1 
ATOM   3992 O  OG  . SER   B  1  179 ? 15.790  -15.179 73.787 1.00 41.00  ? 192 SER   B OG  1 
ATOM   3993 N  N   . ILE   B  1  180 ? 15.447  -18.226 77.239 1.00 45.41  ? 193 ILE   B N   1 
ATOM   3994 C  CA  . ILE   B  1  180 ? 15.102  -18.666 78.580 1.00 49.93  ? 193 ILE   B CA  1 
ATOM   3995 C  C   . ILE   B  1  180 ? 16.350  -18.669 79.462 1.00 51.17  ? 193 ILE   B C   1 
ATOM   3996 O  O   . ILE   B  1  180 ? 16.305  -18.171 80.583 1.00 48.33  ? 193 ILE   B O   1 
ATOM   3997 C  CB  . ILE   B  1  180 ? 14.441  -20.054 78.566 1.00 52.44  ? 193 ILE   B CB  1 
ATOM   3998 C  CG1 . ILE   B  1  180 ? 13.021  -19.980 78.019 1.00 50.30  ? 193 ILE   B CG1 1 
ATOM   3999 C  CG2 . ILE   B  1  180 ? 14.467  -20.672 79.967 1.00 56.73  ? 193 ILE   B CG2 1 
ATOM   4000 C  CD1 . ILE   B  1  180 ? 12.391  -21.338 77.756 1.00 50.96  ? 193 ILE   B CD1 1 
ATOM   4001 N  N   . ALA   B  1  181 ? 17.449  -19.229 78.935 1.00 50.69  ? 194 ALA   B N   1 
ATOM   4002 C  CA  . ALA   B  1  181 ? 18.667  -19.456 79.700 1.00 51.21  ? 194 ALA   B CA  1 
ATOM   4003 C  C   . ALA   B  1  181 ? 19.427  -18.160 79.965 1.00 50.82  ? 194 ALA   B C   1 
ATOM   4004 O  O   . ALA   B  1  181 ? 20.183  -18.104 80.930 1.00 54.37  ? 194 ALA   B O   1 
ATOM   4005 C  CB  . ALA   B  1  181 ? 19.556  -20.462 79.002 1.00 46.25  ? 194 ALA   B CB  1 
ATOM   4006 N  N   . THR   B  1  182 ? 19.251  -17.119 79.141 1.00 45.72  ? 195 THR   B N   1 
ATOM   4007 C  CA  . THR   B  1  182 ? 20.179  -15.995 79.215 1.00 46.15  ? 195 THR   B CA  1 
ATOM   4008 C  C   . THR   B  1  182 ? 19.472  -14.664 79.407 1.00 44.12  ? 195 THR   B C   1 
ATOM   4009 O  O   . THR   B  1  182 ? 20.148  -13.658 79.620 1.00 50.77  ? 195 THR   B O   1 
ATOM   4010 C  CB  . THR   B  1  182 ? 21.056  -15.923 77.957 1.00 54.63  ? 195 THR   B CB  1 
ATOM   4011 O  OG1 . THR   B  1  182 ? 20.210  -15.674 76.829 1.00 63.33  ? 195 THR   B OG1 1 
ATOM   4012 C  CG2 . THR   B  1  182 ? 21.873  -17.183 77.729 1.00 50.55  ? 195 THR   B CG2 1 
ATOM   4013 N  N   . ASN   B  1  183 ? 18.144  -14.625 79.251 1.00 45.87  ? 196 ASN   B N   1 
ATOM   4014 C  CA  . ASN   B  1  183 ? 17.433  -13.354 79.229 1.00 46.82  ? 196 ASN   B CA  1 
ATOM   4015 C  C   . ASN   B  1  183 ? 16.395  -13.370 80.342 1.00 53.44  ? 196 ASN   B C   1 
ATOM   4016 O  O   . ASN   B  1  183 ? 15.350  -13.998 80.220 1.00 46.84  ? 196 ASN   B O   1 
ATOM   4017 C  CB  . ASN   B  1  183 ? 16.775  -13.075 77.883 1.00 46.49  ? 196 ASN   B CB  1 
ATOM   4018 C  CG  . ASN   B  1  183 ? 16.074  -11.738 77.860 1.00 45.79  ? 196 ASN   B CG  1 
ATOM   4019 O  OD1 . ASN   B  1  183 ? 16.052  -11.028 78.870 1.00 47.65  ? 196 ASN   B OD1 1 
ATOM   4020 N  ND2 . ASN   B  1  183 ? 15.488  -11.371 76.728 1.00 48.43  ? 196 ASN   B ND2 1 
ATOM   4021 N  N   . PRO   B  1  184 ? 16.652  -12.682 81.469 1.00 56.53  ? 197 PRO   B N   1 
ATOM   4022 C  CA  . PRO   B  1  184 ? 15.717  -12.711 82.588 1.00 61.56  ? 197 PRO   B CA  1 
ATOM   4023 C  C   . PRO   B  1  184 ? 14.440  -11.897 82.374 1.00 58.92  ? 197 PRO   B C   1 
ATOM   4024 O  O   . PRO   B  1  184 ? 13.494  -12.080 83.129 1.00 59.38  ? 197 PRO   B O   1 
ATOM   4025 C  CB  . PRO   B  1  184 ? 16.603  -12.157 83.722 1.00 59.02  ? 197 PRO   B CB  1 
ATOM   4026 C  CG  . PRO   B  1  184 ? 17.497  -11.164 83.025 1.00 59.24  ? 197 PRO   B CG  1 
ATOM   4027 C  CD  . PRO   B  1  184 ? 17.836  -11.847 81.715 1.00 58.04  ? 197 PRO   B CD  1 
ATOM   4028 N  N   . GLU   B  1  185 ? 14.412  -11.029 81.347 1.00 56.53  ? 198 GLU   B N   1 
ATOM   4029 C  CA  . GLU   B  1  185 ? 13.207  -10.299 80.969 1.00 54.79  ? 198 GLU   B CA  1 
ATOM   4030 C  C   . GLU   B  1  185 ? 12.481  -10.979 79.801 1.00 51.02  ? 198 GLU   B C   1 
ATOM   4031 O  O   . GLU   B  1  185 ? 11.570  -10.407 79.214 1.00 45.00  ? 198 GLU   B O   1 
ATOM   4032 C  CB  . GLU   B  1  185 ? 13.557  -8.859  80.596 1.00 55.49  ? 198 GLU   B CB  1 
ATOM   4033 C  CG  . GLU   B  1  185 ? 14.152  -8.052  81.748 1.00 59.40  ? 198 GLU   B CG  1 
ATOM   4034 C  CD  . GLU   B  1  185 ? 14.565  -6.631  81.392 1.00 66.73  ? 198 GLU   B CD  1 
ATOM   4035 O  OE1 . GLU   B  1  185 ? 14.297  -6.196  80.251 1.00 59.39  ? 198 GLU   B OE1 1 
ATOM   4036 O  OE2 . GLU   B  1  185 ? 15.171  -5.955  82.256 1.00 77.44  ? 198 GLU   B OE2 1 
ATOM   4037 N  N   . PHE   B  1  186 ? 12.859  -12.217 79.477 1.00 44.49  ? 199 PHE   B N   1 
ATOM   4038 C  CA  . PHE   B  1  186 ? 12.300  -12.918 78.334 1.00 41.94  ? 199 PHE   B CA  1 
ATOM   4039 C  C   . PHE   B  1  186 ? 10.782  -13.029 78.445 1.00 46.56  ? 199 PHE   B C   1 
ATOM   4040 O  O   . PHE   B  1  186 ? 10.258  -13.543 79.427 1.00 47.88  ? 199 PHE   B O   1 
ATOM   4041 C  CB  . PHE   B  1  186 ? 12.854  -14.338 78.229 1.00 38.65  ? 199 PHE   B CB  1 
ATOM   4042 C  CG  . PHE   B  1  186 ? 12.332  -15.158 77.060 1.00 39.69  ? 199 PHE   B CG  1 
ATOM   4043 C  CD1 . PHE   B  1  186 ? 12.237  -14.616 75.781 1.00 40.95  ? 199 PHE   B CD1 1 
ATOM   4044 C  CD2 . PHE   B  1  186 ? 11.939  -16.473 77.244 1.00 38.68  ? 199 PHE   B CD2 1 
ATOM   4045 C  CE1 . PHE   B  1  186 ? 11.787  -15.386 74.718 1.00 39.51  ? 199 PHE   B CE1 1 
ATOM   4046 C  CE2 . PHE   B  1  186 ? 11.475  -17.233 76.187 1.00 39.22  ? 199 PHE   B CE2 1 
ATOM   4047 C  CZ  . PHE   B  1  186 ? 11.413  -16.697 74.919 1.00 39.27  ? 199 PHE   B CZ  1 
ATOM   4048 N  N   . GLN   B  1  187 ? 10.102  -12.562 77.394 1.00 48.38  ? 200 GLN   B N   1 
ATOM   4049 C  CA  . GLN   B  1  187 ? 8.655   -12.645 77.246 1.00 50.75  ? 200 GLN   B CA  1 
ATOM   4050 C  C   . GLN   B  1  187 ? 8.362   -13.309 75.905 1.00 44.18  ? 200 GLN   B C   1 
ATOM   4051 O  O   . GLN   B  1  187 ? 9.008   -12.999 74.907 1.00 41.79  ? 200 GLN   B O   1 
ATOM   4052 C  CB  . GLN   B  1  187 ? 8.041   -11.243 77.275 1.00 54.20  ? 200 GLN   B CB  1 
ATOM   4053 C  CG  . GLN   B  1  187 ? 8.081   -10.573 78.650 1.00 61.47  ? 200 GLN   B CG  1 
ATOM   4054 C  CD  . GLN   B  1  187 ? 7.121   -11.213 79.633 1.00 63.81  ? 200 GLN   B CD  1 
ATOM   4055 O  OE1 . GLN   B  1  187 ? 5.898   -11.067 79.518 1.00 67.85  ? 200 GLN   B OE1 1 
ATOM   4056 N  NE2 . GLN   B  1  187 ? 7.654   -11.960 80.587 1.00 59.32  ? 200 GLN   B NE2 1 
ATOM   4057 N  N   . PHE   B  1  188 ? 7.403   -14.228 75.896 1.00 40.99  ? 201 PHE   B N   1 
ATOM   4058 C  CA  . PHE   B  1  188 ? 7.026   -14.918 74.675 1.00 40.68  ? 201 PHE   B CA  1 
ATOM   4059 C  C   . PHE   B  1  188 ? 5.522   -15.167 74.671 1.00 37.79  ? 201 PHE   B C   1 
ATOM   4060 O  O   . PHE   B  1  188 ? 5.068   -16.302 74.684 1.00 36.41  ? 201 PHE   B O   1 
ATOM   4061 C  CB  . PHE   B  1  188 ? 7.852   -16.201 74.598 1.00 38.82  ? 201 PHE   B CB  1 
ATOM   4062 C  CG  . PHE   B  1  188 ? 7.982   -16.768 73.202 1.00 35.98  ? 201 PHE   B CG  1 
ATOM   4063 C  CD1 . PHE   B  1  188 ? 8.730   -16.082 72.253 1.00 37.34  ? 201 PHE   B CD1 1 
ATOM   4064 C  CD2 . PHE   B  1  188 ? 7.410   -17.988 72.855 1.00 34.83  ? 201 PHE   B CD2 1 
ATOM   4065 C  CE1 . PHE   B  1  188 ? 8.855   -16.569 70.975 1.00 38.43  ? 201 PHE   B CE1 1 
ATOM   4066 C  CE2 . PHE   B  1  188 ? 7.563   -18.490 71.578 1.00 37.58  ? 201 PHE   B CE2 1 
ATOM   4067 C  CZ  . PHE   B  1  188 ? 8.283   -17.779 70.643 1.00 38.29  ? 201 PHE   B CZ  1 
ATOM   4068 N  N   . LYS   B  1  189 ? 4.758   -14.085 74.641 1.00 37.67  ? 202 LYS   B N   1 
ATOM   4069 C  CA  . LYS   B  1  189 ? 3.314   -14.180 74.755 1.00 44.49  ? 202 LYS   B CA  1 
ATOM   4070 C  C   . LYS   B  1  189 ? 2.658   -13.121 73.871 1.00 40.66  ? 202 LYS   B C   1 
ATOM   4071 O  O   . LYS   B  1  189 ? 3.329   -12.291 73.266 1.00 37.88  ? 202 LYS   B O   1 
ATOM   4072 C  CB  . LYS   B  1  189 ? 2.958   -13.998 76.232 1.00 42.61  ? 202 LYS   B CB  1 
ATOM   4073 C  CG  . LYS   B  1  189 ? 3.426   -12.675 76.811 1.00 51.26  ? 202 LYS   B CG  1 
ATOM   4074 C  CD  . LYS   B  1  189 ? 2.833   -12.328 78.178 1.00 58.01  ? 202 LYS   B CD  1 
ATOM   4075 C  CE  . LYS   B  1  189 ? 3.331   -13.203 79.278 1.00 63.79  ? 202 LYS   B CE  1 
ATOM   4076 N  NZ  . LYS   B  1  189 ? 2.902   -12.652 80.565 1.00 66.73  ? 202 LYS   B NZ  1 
ATOM   4077 N  N   . ASN   B  1  190 ? 1.332   -13.180 73.787 1.00 42.19  ? 203 ASN   B N   1 
ATOM   4078 C  CA  . ASN   B  1  190 ? 0.552   -12.199 73.050 1.00 42.86  ? 203 ASN   B CA  1 
ATOM   4079 C  C   . ASN   B  1  190 ? 1.077   -12.072 71.620 1.00 40.67  ? 203 ASN   B C   1 
ATOM   4080 O  O   . ASN   B  1  190 ? 1.178   -13.075 70.923 1.00 40.22  ? 203 ASN   B O   1 
ATOM   4081 C  CB  . ASN   B  1  190 ? 0.423   -10.927 73.878 1.00 44.94  ? 203 ASN   B CB  1 
ATOM   4082 C  CG  . ASN   B  1  190 ? -0.384  -11.202 75.136 1.00 50.33  ? 203 ASN   B CG  1 
ATOM   4083 O  OD1 . ASN   B  1  190 ? -1.437  -11.858 75.073 1.00 46.77  ? 203 ASN   B OD1 1 
ATOM   4084 N  ND2 . ASN   B  1  190 ? 0.098   -10.716 76.273 1.00 46.48  ? 203 ASN   B ND2 1 
ATOM   4085 N  N   . VAL   B  1  191 ? 1.398   -10.854 71.172 1.00 39.20  ? 204 VAL   B N   1 
ATOM   4086 C  CA  . VAL   B  1  191 ? 1.712   -10.657 69.766 1.00 40.14  ? 204 VAL   B CA  1 
ATOM   4087 C  C   . VAL   B  1  191 ? 2.932   -11.502 69.413 1.00 39.03  ? 204 VAL   B C   1 
ATOM   4088 O  O   . VAL   B  1  191 ? 2.936   -12.199 68.400 1.00 37.62  ? 204 VAL   B O   1 
ATOM   4089 C  CB  . VAL   B  1  191 ? 1.972   -9.175  69.446 1.00 40.24  ? 204 VAL   B CB  1 
ATOM   4090 C  CG1 . VAL   B  1  191 ? 2.479   -8.983  68.020 1.00 39.10  ? 204 VAL   B CG1 1 
ATOM   4091 C  CG2 . VAL   B  1  191 ? 0.737   -8.319  69.708 1.00 35.34  ? 204 VAL   B CG2 1 
ATOM   4092 N  N   . ARG   B  1  192 ? 3.957   -11.446 70.274 1.00 33.53  ? 205 ARG   B N   1 
ATOM   4093 C  CA  . ARG   B  1  192 ? 5.218   -12.081 69.969 1.00 33.14  ? 205 ARG   B CA  1 
ATOM   4094 C  C   . ARG   B  1  192 ? 5.062   -13.589 69.799 1.00 32.40  ? 205 ARG   B C   1 
ATOM   4095 O  O   . ARG   B  1  192 ? 5.720   -14.188 68.957 1.00 33.94  ? 205 ARG   B O   1 
ATOM   4096 C  CB  . ARG   B  1  192 ? 6.255   -11.806 71.052 1.00 38.11  ? 205 ARG   B CB  1 
ATOM   4097 C  CG  . ARG   B  1  192 ? 7.604   -12.421 70.695 1.00 42.04  ? 205 ARG   B CG  1 
ATOM   4098 C  CD  . ARG   B  1  192 ? 8.069   -11.984 69.319 1.00 38.38  ? 205 ARG   B CD  1 
ATOM   4099 N  NE  . ARG   B  1  192 ? 9.375   -12.512 68.932 1.00 39.92  ? 205 ARG   B NE  1 
ATOM   4100 C  CZ  . ARG   B  1  192 ? 9.789   -12.690 67.670 1.00 46.04  ? 205 ARG   B CZ  1 
ATOM   4101 N  NH1 . ARG   B  1  192 ? 9.020   -12.326 66.647 1.00 44.13  ? 205 ARG   B NH1 1 
ATOM   4102 N  NH2 . ARG   B  1  192 ? 10.969  -13.261 67.446 1.00 45.57  ? 205 ARG   B NH2 1 
ATOM   4103 N  N   . PHE   B  1  193 ? 4.193   -14.218 70.581 1.00 33.22  ? 206 PHE   B N   1 
ATOM   4104 C  CA  . PHE   B  1  193 ? 4.030   -15.657 70.476 1.00 31.45  ? 206 PHE   B CA  1 
ATOM   4105 C  C   . PHE   B  1  193 ? 3.515   -15.987 69.084 1.00 33.37  ? 206 PHE   B C   1 
ATOM   4106 O  O   . PHE   B  1  193 ? 3.944   -16.971 68.499 1.00 36.46  ? 206 PHE   B O   1 
ATOM   4107 C  CB  . PHE   B  1  193 ? 3.106   -16.225 71.553 1.00 33.63  ? 206 PHE   B CB  1 
ATOM   4108 C  CG  . PHE   B  1  193 ? 2.905   -17.722 71.412 1.00 34.80  ? 206 PHE   B CG  1 
ATOM   4109 C  CD1 . PHE   B  1  193 ? 3.845   -18.612 71.915 1.00 34.41  ? 206 PHE   B CD1 1 
ATOM   4110 C  CD2 . PHE   B  1  193 ? 1.789   -18.236 70.767 1.00 38.61  ? 206 PHE   B CD2 1 
ATOM   4111 C  CE1 . PHE   B  1  193 ? 3.674   -19.977 71.761 1.00 36.42  ? 206 PHE   B CE1 1 
ATOM   4112 C  CE2 . PHE   B  1  193 ? 1.613   -19.602 70.637 1.00 38.11  ? 206 PHE   B CE2 1 
ATOM   4113 C  CZ  . PHE   B  1  193 ? 2.565   -20.470 71.121 1.00 37.20  ? 206 PHE   B CZ  1 
ATOM   4114 N  N   . ILE   B  1  194 ? 2.619   -15.161 68.535 1.00 33.62  ? 207 ILE   B N   1 
ATOM   4115 C  CA  . ILE   B  1  194 ? 2.074   -15.461 67.218 1.00 35.08  ? 207 ILE   B CA  1 
ATOM   4116 C  C   . ILE   B  1  194 ? 3.112   -15.158 66.132 1.00 35.98  ? 207 ILE   B C   1 
ATOM   4117 O  O   . ILE   B  1  194 ? 3.350   -15.989 65.245 1.00 36.08  ? 207 ILE   B O   1 
ATOM   4118 C  CB  . ILE   B  1  194 ? 0.749   -14.701 67.017 1.00 41.01  ? 207 ILE   B CB  1 
ATOM   4119 C  CG1 . ILE   B  1  194 ? -0.270  -15.059 68.081 1.00 40.91  ? 207 ILE   B CG1 1 
ATOM   4120 C  CG2 . ILE   B  1  194 ? 0.187   -14.939 65.620 1.00 43.99  ? 207 ILE   B CG2 1 
ATOM   4121 C  CD1 . ILE   B  1  194 ? -0.572  -16.556 68.155 1.00 42.97  ? 207 ILE   B CD1 1 
ATOM   4122 N  N   . THR   B  1  195 ? 3.733   -13.969 66.200 1.00 34.58  ? 208 THR   B N   1 
ATOM   4123 C  CA  . THR   B  1  195 ? 4.613   -13.513 65.136 1.00 34.54  ? 208 THR   B CA  1 
ATOM   4124 C  C   . THR   B  1  195 ? 5.884   -14.361 65.085 1.00 31.23  ? 208 THR   B C   1 
ATOM   4125 O  O   . THR   B  1  195 ? 6.427   -14.581 64.018 1.00 36.92  ? 208 THR   B O   1 
ATOM   4126 C  CB  . THR   B  1  195 ? 4.923   -12.023 65.272 1.00 37.22  ? 208 THR   B CB  1 
ATOM   4127 O  OG1 . THR   B  1  195 ? 5.608   -11.813 66.499 1.00 39.40  ? 208 THR   B OG1 1 
ATOM   4128 C  CG2 . THR   B  1  195 ? 3.679   -11.155 65.193 1.00 38.19  ? 208 THR   B CG2 1 
ATOM   4129 N  N   . ALA   B  1  196 ? 6.338   -14.896 66.214 1.00 33.30  ? 209 ALA   B N   1 
ATOM   4130 C  CA  . ALA   B  1  196 ? 7.582   -15.652 66.235 1.00 35.49  ? 209 ALA   B CA  1 
ATOM   4131 C  C   . ALA   B  1  196 ? 7.509   -16.917 65.386 1.00 35.32  ? 209 ALA   B C   1 
ATOM   4132 O  O   . ALA   B  1  196 ? 8.549   -17.361 64.929 1.00 45.09  ? 209 ALA   B O   1 
ATOM   4133 C  CB  . ALA   B  1  196 ? 7.980   -16.000 67.644 1.00 38.43  ? 209 ALA   B CB  1 
ATOM   4134 N  N   . TYR   B  1  197 ? 6.328   -17.503 65.178 1.00 32.63  ? 210 TYR   B N   1 
ATOM   4135 C  CA  . TYR   B  1  197 ? 6.230   -18.701 64.363 1.00 33.14  ? 210 TYR   B CA  1 
ATOM   4136 C  C   . TYR   B  1  197 ? 6.140   -18.312 62.885 1.00 39.17  ? 210 TYR   B C   1 
ATOM   4137 O  O   . TYR   B  1  197 ? 6.799   -18.916 62.034 1.00 41.33  ? 210 TYR   B O   1 
ATOM   4138 C  CB  . TYR   B  1  197 ? 5.094   -19.593 64.871 1.00 35.39  ? 210 TYR   B CB  1 
ATOM   4139 C  CG  . TYR   B  1  197 ? 5.528   -20.271 66.155 1.00 33.25  ? 210 TYR   B CG  1 
ATOM   4140 C  CD1 . TYR   B  1  197 ? 6.250   -21.458 66.125 1.00 34.69  ? 210 TYR   B CD1 1 
ATOM   4141 C  CD2 . TYR   B  1  197 ? 5.346   -19.649 67.384 1.00 33.66  ? 210 TYR   B CD2 1 
ATOM   4142 C  CE1 . TYR   B  1  197 ? 6.732   -22.035 67.291 1.00 33.13  ? 210 TYR   B CE1 1 
ATOM   4143 C  CE2 . TYR   B  1  197 ? 5.859   -20.188 68.548 1.00 32.28  ? 210 TYR   B CE2 1 
ATOM   4144 C  CZ  . TYR   B  1  197 ? 6.533   -21.398 68.501 1.00 35.00  ? 210 TYR   B CZ  1 
ATOM   4145 O  OH  . TYR   B  1  197 ? 7.008   -21.972 69.644 1.00 39.29  ? 210 TYR   B OH  1 
ATOM   4146 N  N   . GLY   B  1  198 ? 5.354   -17.285 62.571 1.00 35.55  ? 211 GLY   B N   1 
ATOM   4147 C  CA  . GLY   B  1  198 ? 5.234   -16.842 61.190 1.00 34.37  ? 211 GLY   B CA  1 
ATOM   4148 C  C   . GLY   B  1  198 ? 6.572   -16.398 60.610 1.00 30.33  ? 211 GLY   B C   1 
ATOM   4149 O  O   . GLY   B  1  198 ? 6.901   -16.710 59.468 1.00 30.79  ? 211 GLY   B O   1 
ATOM   4150 N  N   . GLU   B  1  199 ? 7.370   -15.678 61.401 1.00 32.03  ? 212 GLU   B N   1 
ATOM   4151 C  CA  A GLU   B  1  199 ? 8.613   -15.126 60.891 0.50 33.16  ? 212 GLU   B CA  1 
ATOM   4152 C  CA  B GLU   B  1  199 ? 8.628   -15.123 60.926 0.50 30.42  ? 212 GLU   B CA  1 
ATOM   4153 C  C   . GLU   B  1  199 ? 9.568   -16.252 60.494 1.00 32.39  ? 212 GLU   B C   1 
ATOM   4154 O  O   . GLU   B  1  199 ? 10.420  -16.054 59.642 1.00 33.38  ? 212 GLU   B O   1 
ATOM   4155 C  CB  A GLU   B  1  199 ? 9.229   -14.127 61.865 0.50 36.82  ? 212 GLU   B CB  1 
ATOM   4156 C  CB  B GLU   B  1  199 ? 9.284   -14.210 61.971 0.50 30.10  ? 212 GLU   B CB  1 
ATOM   4157 C  CG  A GLU   B  1  199 ? 8.539   -12.766 61.803 0.50 40.08  ? 212 GLU   B CG  1 
ATOM   4158 C  CG  B GLU   B  1  199 ? 9.987   -14.922 63.133 0.50 28.54  ? 212 GLU   B CG  1 
ATOM   4159 C  CD  A GLU   B  1  199 ? 8.618   -11.949 63.079 0.50 39.13  ? 212 GLU   B CD  1 
ATOM   4160 C  CD  B GLU   B  1  199 ? 10.626  -14.009 64.177 0.50 26.02  ? 212 GLU   B CD  1 
ATOM   4161 O  OE1 A GLU   B  1  199 ? 9.493   -12.223 63.935 0.50 39.49  ? 212 GLU   B OE1 1 
ATOM   4162 O  OE1 B GLU   B  1  199 ? 10.286  -12.821 64.226 0.50 26.60  ? 212 GLU   B OE1 1 
ATOM   4163 O  OE2 A GLU   B  1  199 ? 7.750   -11.059 63.200 0.50 38.40  ? 212 GLU   B OE2 1 
ATOM   4164 O  OE2 B GLU   B  1  199 ? 11.491  -14.449 64.936 0.50 23.35  ? 212 GLU   B OE2 1 
ATOM   4165 N  N   . THR   B  1  200 ? 9.429   -17.438 61.093 1.00 31.83  ? 213 THR   B N   1 
ATOM   4166 C  CA  . THR   B  1  200 ? 10.356  -18.517 60.802 1.00 34.25  ? 213 THR   B CA  1 
ATOM   4167 C  C   . THR   B  1  200 ? 10.040  -19.167 59.463 1.00 34.70  ? 213 THR   B C   1 
ATOM   4168 O  O   . THR   B  1  200 ? 10.916  -19.849 58.923 1.00 36.61  ? 213 THR   B O   1 
ATOM   4169 C  CB  . THR   B  1  200 ? 10.401  -19.584 61.894 1.00 39.32  ? 213 THR   B CB  1 
ATOM   4170 O  OG1 . THR   B  1  200 ? 9.183   -20.312 61.873 1.00 41.81  ? 213 THR   B OG1 1 
ATOM   4171 C  CG2 . THR   B  1  200 ? 10.661  -18.999 63.264 1.00 40.67  ? 213 THR   B CG2 1 
ATOM   4172 N  N   . VAL   B  1  201 ? 8.825   -18.975 58.930 1.00 33.29  ? 214 VAL   B N   1 
ATOM   4173 C  CA  . VAL   B  1  201 ? 8.500   -19.544 57.628 1.00 32.27  ? 214 VAL   B CA  1 
ATOM   4174 C  C   . VAL   B  1  201 ? 8.539   -18.498 56.516 1.00 29.32  ? 214 VAL   B C   1 
ATOM   4175 O  O   . VAL   B  1  201 ? 8.589   -18.871 55.354 1.00 31.31  ? 214 VAL   B O   1 
ATOM   4176 C  CB  . VAL   B  1  201 ? 7.166   -20.302 57.615 1.00 31.60  ? 214 VAL   B CB  1 
ATOM   4177 C  CG1 . VAL   B  1  201 ? 7.263   -21.501 58.540 1.00 34.33  ? 214 VAL   B CG1 1 
ATOM   4178 C  CG2 . VAL   B  1  201 ? 5.974   -19.408 57.960 1.00 34.20  ? 214 VAL   B CG2 1 
ATOM   4179 N  N   . PHE   B  1  202 ? 8.536   -17.207 56.841 1.00 30.48  ? 215 PHE   B N   1 
ATOM   4180 C  CA  . PHE   B  1  202 ? 8.652   -16.188 55.811 1.00 30.59  ? 215 PHE   B CA  1 
ATOM   4181 C  C   . PHE   B  1  202 ? 9.887   -16.409 54.936 1.00 33.60  ? 215 PHE   B C   1 
ATOM   4182 O  O   . PHE   B  1  202 ? 9.796   -16.219 53.723 1.00 35.61  ? 215 PHE   B O   1 
ATOM   4183 C  CB  . PHE   B  1  202 ? 8.681   -14.769 56.367 1.00 30.88  ? 215 PHE   B CB  1 
ATOM   4184 C  CG  . PHE   B  1  202 ? 7.375   -14.303 56.976 1.00 32.71  ? 215 PHE   B CG  1 
ATOM   4185 C  CD1 . PHE   B  1  202 ? 6.189   -15.010 56.794 1.00 38.35  ? 215 PHE   B CD1 1 
ATOM   4186 C  CD2 . PHE   B  1  202 ? 7.327   -13.127 57.702 1.00 39.14  ? 215 PHE   B CD2 1 
ATOM   4187 C  CE1 . PHE   B  1  202 ? 5.003   -14.574 57.368 1.00 38.23  ? 215 PHE   B CE1 1 
ATOM   4188 C  CE2 . PHE   B  1  202 ? 6.134   -12.680 58.244 1.00 42.56  ? 215 PHE   B CE2 1 
ATOM   4189 C  CZ  . PHE   B  1  202 ? 4.974   -13.407 58.074 1.00 40.51  ? 215 PHE   B CZ  1 
ATOM   4190 N  N   . PRO   B  1  203 ? 11.071  -16.793 55.464 1.00 33.80  ? 216 PRO   B N   1 
ATOM   4191 C  CA  . PRO   B  1  203 ? 12.230  -17.050 54.616 1.00 33.55  ? 216 PRO   B CA  1 
ATOM   4192 C  C   . PRO   B  1  203 ? 11.992  -18.127 53.568 1.00 32.38  ? 216 PRO   B C   1 
ATOM   4193 O  O   . PRO   B  1  203 ? 12.536  -18.035 52.468 1.00 41.54  ? 216 PRO   B O   1 
ATOM   4194 C  CB  . PRO   B  1  203 ? 13.330  -17.454 55.605 1.00 34.86  ? 216 PRO   B CB  1 
ATOM   4195 C  CG  . PRO   B  1  203 ? 12.930  -16.802 56.893 1.00 33.64  ? 216 PRO   B CG  1 
ATOM   4196 C  CD  . PRO   B  1  203 ? 11.407  -16.915 56.890 1.00 35.89  ? 216 PRO   B CD  1 
ATOM   4197 N  N   . ILE   B  1  204 ? 11.212  -19.149 53.920 1.00 30.02  ? 217 ILE   B N   1 
ATOM   4198 C  CA  . ILE   B  1  204 ? 10.895  -20.232 52.991 1.00 33.07  ? 217 ILE   B CA  1 
ATOM   4199 C  C   . ILE   B  1  204 ? 9.859   -19.765 51.959 1.00 33.69  ? 217 ILE   B C   1 
ATOM   4200 O  O   . ILE   B  1  204 ? 10.007  -19.996 50.766 1.00 34.43  ? 217 ILE   B O   1 
ATOM   4201 C  CB  . ILE   B  1  204 ? 10.402  -21.466 53.767 1.00 36.24  ? 217 ILE   B CB  1 
ATOM   4202 C  CG1 . ILE   B  1  204 ? 11.443  -21.927 54.774 1.00 35.73  ? 217 ILE   B CG1 1 
ATOM   4203 C  CG2 . ILE   B  1  204 ? 9.964   -22.585 52.824 1.00 35.14  ? 217 ILE   B CG2 1 
ATOM   4204 C  CD1 . ILE   B  1  204 ? 10.923  -22.893 55.813 1.00 39.11  ? 217 ILE   B CD1 1 
ATOM   4205 N  N   . ASN   B  1  205 ? 8.801   -19.096 52.412 1.00 34.28  ? 218 ASN   B N   1 
ATOM   4206 C  CA  . ASN   B  1  205 ? 7.685   -18.780 51.533 1.00 33.12  ? 218 ASN   B CA  1 
ATOM   4207 C  C   . ASN   B  1  205 ? 7.931   -17.539 50.695 1.00 31.88  ? 218 ASN   B C   1 
ATOM   4208 O  O   . ASN   B  1  205 ? 7.354   -17.440 49.613 1.00 36.87  ? 218 ASN   B O   1 
ATOM   4209 C  CB  . ASN   B  1  205 ? 6.394   -18.571 52.309 1.00 31.68  ? 218 ASN   B CB  1 
ATOM   4210 C  CG  . ASN   B  1  205 ? 6.031   -19.808 53.089 1.00 28.87  ? 218 ASN   B CG  1 
ATOM   4211 O  OD1 . ASN   B  1  205 ? 6.359   -20.921 52.675 1.00 33.53  ? 218 ASN   B OD1 1 
ATOM   4212 N  ND2 . ASN   B  1  205 ? 5.397   -19.628 54.233 1.00 32.79  ? 218 ASN   B ND2 1 
ATOM   4213 N  N   . LEU   B  1  206 ? 8.763   -16.611 51.176 1.00 33.46  ? 219 LEU   B N   1 
ATOM   4214 C  CA  . LEU   B  1  206 ? 8.911   -15.320 50.507 1.00 34.19  ? 219 LEU   B CA  1 
ATOM   4215 C  C   . LEU   B  1  206 ? 10.340  -15.029 50.048 1.00 34.11  ? 219 LEU   B C   1 
ATOM   4216 O  O   . LEU   B  1  206 ? 10.517  -14.236 49.137 1.00 31.34  ? 219 LEU   B O   1 
ATOM   4217 C  CB  . LEU   B  1  206 ? 8.411   -14.242 51.456 1.00 33.91  ? 219 LEU   B CB  1 
ATOM   4218 C  CG  . LEU   B  1  206 ? 6.955   -14.397 51.898 1.00 36.48  ? 219 LEU   B CG  1 
ATOM   4219 C  CD1 . LEU   B  1  206 ? 6.647   -13.438 53.049 1.00 40.24  ? 219 LEU   B CD1 1 
ATOM   4220 C  CD2 . LEU   B  1  206 ? 6.026   -14.148 50.718 1.00 37.33  ? 219 LEU   B CD2 1 
ATOM   4221 N  N   . PHE   B  1  207 ? 11.361  -15.623 50.690 1.00 32.22  ? 220 PHE   B N   1 
ATOM   4222 C  CA  . PHE   B  1  207 ? 12.725  -15.305 50.328 1.00 34.55  ? 220 PHE   B CA  1 
ATOM   4223 C  C   . PHE   B  1  207 ? 13.260  -16.305 49.305 1.00 34.22  ? 220 PHE   B C   1 
ATOM   4224 O  O   . PHE   B  1  207 ? 14.281  -16.037 48.686 1.00 33.97  ? 220 PHE   B O   1 
ATOM   4225 C  CB  . PHE   B  1  207 ? 13.679  -15.261 51.517 1.00 33.95  ? 220 PHE   B CB  1 
ATOM   4226 C  CG  . PHE   B  1  207 ? 13.443  -14.158 52.528 1.00 37.34  ? 220 PHE   B CG  1 
ATOM   4227 C  CD1 . PHE   B  1  207 ? 12.653  -13.054 52.226 1.00 39.52  ? 220 PHE   B CD1 1 
ATOM   4228 C  CD2 . PHE   B  1  207 ? 14.088  -14.188 53.758 1.00 36.79  ? 220 PHE   B CD2 1 
ATOM   4229 C  CE1 . PHE   B  1  207 ? 12.457  -12.053 53.162 1.00 36.28  ? 220 PHE   B CE1 1 
ATOM   4230 C  CE2 . PHE   B  1  207 ? 13.887  -13.186 54.674 1.00 33.81  ? 220 PHE   B CE2 1 
ATOM   4231 C  CZ  . PHE   B  1  207 ? 13.078  -12.123 54.376 1.00 37.97  ? 220 PHE   B CZ  1 
ATOM   4232 N  N   . VAL   B  1  208 ? 12.614  -17.464 49.167 1.00 31.52  ? 221 VAL   B N   1 
ATOM   4233 C  CA  . VAL   B  1  208 ? 12.968  -18.397 48.113 1.00 32.74  ? 221 VAL   B CA  1 
ATOM   4234 C  C   . VAL   B  1  208 ? 12.333  -17.923 46.808 1.00 33.66  ? 221 VAL   B C   1 
ATOM   4235 O  O   . VAL   B  1  208 ? 11.164  -17.570 46.773 1.00 35.83  ? 221 VAL   B O   1 
ATOM   4236 C  CB  . VAL   B  1  208 ? 12.523  -19.827 48.469 1.00 34.03  ? 221 VAL   B CB  1 
ATOM   4237 C  CG1 . VAL   B  1  208 ? 12.746  -20.778 47.313 1.00 35.34  ? 221 VAL   B CG1 1 
ATOM   4238 C  CG2 . VAL   B  1  208 ? 13.236  -20.340 49.710 1.00 35.08  ? 221 VAL   B CG2 1 
ATOM   4239 N  N   . ASP   B  1  209 ? 13.136  -17.922 45.745 1.00 33.86  ? 222 ASP   B N   1 
ATOM   4240 C  CA  . ASP   B  1  209 ? 12.736  -17.470 44.430 1.00 37.34  ? 222 ASP   B CA  1 
ATOM   4241 C  C   . ASP   B  1  209 ? 11.451  -18.172 43.999 1.00 36.61  ? 222 ASP   B C   1 
ATOM   4242 O  O   . ASP   B  1  209 ? 11.295  -19.377 44.194 1.00 34.34  ? 222 ASP   B O   1 
ATOM   4243 C  CB  . ASP   B  1  209 ? 13.854  -17.687 43.415 1.00 38.46  ? 222 ASP   B CB  1 
ATOM   4244 C  CG  . ASP   B  1  209 ? 13.624  -17.016 42.071 1.00 39.08  ? 222 ASP   B CG  1 
ATOM   4245 O  OD1 . ASP   B  1  209 ? 12.810  -17.558 41.281 1.00 42.36  ? 222 ASP   B OD1 1 
ATOM   4246 O  OD2 . ASP   B  1  209 ? 14.215  -15.929 41.850 1.00 39.07  ? 222 ASP   B OD2 1 
ATOM   4247 N  N   . GLY   B  1  210 ? 10.546  -17.383 43.399 1.00 40.74  ? 223 GLY   B N   1 
ATOM   4248 C  CA  . GLY   B  1  210 ? 9.226   -17.855 43.008 1.00 42.83  ? 223 GLY   B CA  1 
ATOM   4249 C  C   . GLY   B  1  210 ? 9.252   -18.903 41.893 1.00 43.90  ? 223 GLY   B C   1 
ATOM   4250 O  O   . GLY   B  1  210 ? 8.269   -19.619 41.711 1.00 45.24  ? 223 GLY   B O   1 
ATOM   4251 N  N   . ARG   B  1  211 ? 10.361  -18.984 41.144 1.00 41.64  ? 224 ARG   B N   1 
ATOM   4252 C  CA  . ARG   B  1  211 ? 10.510  -19.988 40.096 1.00 43.05  ? 224 ARG   B CA  1 
ATOM   4253 C  C   . ARG   B  1  211 ? 10.829  -21.365 40.681 1.00 41.07  ? 224 ARG   B C   1 
ATOM   4254 O  O   . ARG   B  1  211 ? 10.794  -22.356 39.968 1.00 42.10  ? 224 ARG   B O   1 
ATOM   4255 C  CB  . ARG   B  1  211 ? 11.569  -19.568 39.065 1.00 40.71  ? 224 ARG   B CB  1 
ATOM   4256 C  CG  . ARG   B  1  211 ? 11.127  -18.365 38.240 1.00 40.39  ? 224 ARG   B CG  1 
ATOM   4257 C  CD  . ARG   B  1  211 ? 12.266  -17.643 37.544 1.00 44.76  ? 224 ARG   B CD  1 
ATOM   4258 N  NE  . ARG   B  1  211 ? 13.256  -17.112 38.489 1.00 46.61  ? 224 ARG   B NE  1 
ATOM   4259 C  CZ  . ARG   B  1  211 ? 14.391  -16.502 38.171 1.00 46.47  ? 224 ARG   B CZ  1 
ATOM   4260 N  NH1 . ARG   B  1  211 ? 14.764  -16.382 36.909 1.00 44.31  ? 224 ARG   B NH1 1 
ATOM   4261 N  NH2 . ARG   B  1  211 ? 15.190  -16.029 39.119 1.00 43.97  ? 224 ARG   B NH2 1 
ATOM   4262 N  N   . VAL   B  1  212 ? 11.160  -21.444 41.972 1.00 45.90  ? 225 VAL   B N   1 
ATOM   4263 C  CA  . VAL   B  1  212 ? 11.356  -22.737 42.617 1.00 50.59  ? 225 VAL   B CA  1 
ATOM   4264 C  C   . VAL   B  1  212 ? 9.996   -23.276 43.074 1.00 56.15  ? 225 VAL   B C   1 
ATOM   4265 O  O   . VAL   B  1  212 ? 9.410   -22.750 44.014 1.00 54.58  ? 225 VAL   B O   1 
ATOM   4266 C  CB  . VAL   B  1  212 ? 12.333  -22.638 43.805 1.00 48.22  ? 225 VAL   B CB  1 
ATOM   4267 C  CG1 . VAL   B  1  212 ? 12.535  -23.990 44.475 1.00 48.57  ? 225 VAL   B CG1 1 
ATOM   4268 C  CG2 . VAL   B  1  212 ? 13.671  -22.036 43.390 1.00 49.52  ? 225 VAL   B CG2 1 
ATOM   4269 N  N   . THR   B  1  213 ? 9.513   -24.351 42.441 1.00 61.31  ? 226 THR   B N   1 
ATOM   4270 C  CA  . THR   B  1  213 ? 8.171   -24.871 42.706 1.00 70.96  ? 226 THR   B CA  1 
ATOM   4271 C  C   . THR   B  1  213 ? 8.234   -26.016 43.717 1.00 70.95  ? 226 THR   B C   1 
ATOM   4272 O  O   . THR   B  1  213 ? 7.284   -26.255 44.454 1.00 71.41  ? 226 THR   B O   1 
ATOM   4273 C  CB  . THR   B  1  213 ? 7.498   -25.329 41.405 1.00 71.18  ? 226 THR   B CB  1 
ATOM   4274 O  OG1 . THR   B  1  213 ? 8.307   -26.342 40.810 1.00 70.27  ? 226 THR   B OG1 1 
ATOM   4275 C  CG2 . THR   B  1  213 ? 7.338   -24.207 40.393 1.00 67.33  ? 226 THR   B CG2 1 
ATOM   4276 N  N   . THR   B  1  214 ? 9.360   -26.725 43.747 1.00 74.25  ? 227 THR   B N   1 
ATOM   4277 C  CA  . THR   B  1  214 ? 9.469   -27.975 44.480 1.00 85.86  ? 227 THR   B CA  1 
ATOM   4278 C  C   . THR   B  1  214 ? 10.668  -27.904 45.434 1.00 78.00  ? 227 THR   B C   1 
ATOM   4279 O  O   . THR   B  1  214 ? 11.694  -27.313 45.099 1.00 71.29  ? 227 THR   B O   1 
ATOM   4280 C  CB  . THR   B  1  214 ? 9.564   -29.096 43.438 1.00 90.53  ? 227 THR   B CB  1 
ATOM   4281 O  OG1 . THR   B  1  214 ? 9.560   -30.327 44.154 1.00 85.06  ? 227 THR   B OG1 1 
ATOM   4282 C  CG2 . THR   B  1  214 ? 10.799  -29.012 42.549 1.00 91.18  ? 227 THR   B CG2 1 
ATOM   4283 N  N   . ASP   B  1  215 ? 10.527  -28.492 46.634 1.00 73.35  ? 228 ASP   B N   1 
ATOM   4284 C  CA  . ASP   B  1  215 ? 11.635  -28.622 47.574 1.00 73.08  ? 228 ASP   B CA  1 
ATOM   4285 C  C   . ASP   B  1  215 ? 12.177  -27.223 47.877 1.00 58.59  ? 228 ASP   B C   1 
ATOM   4286 O  O   . ASP   B  1  215 ? 13.328  -26.906 47.610 1.00 59.47  ? 228 ASP   B O   1 
ATOM   4287 C  CB  . ASP   B  1  215 ? 12.655  -29.628 47.046 1.00 88.17  ? 228 ASP   B CB  1 
ATOM   4288 C  CG  . ASP   B  1  215 ? 13.865  -29.938 47.925 1.00 113.62 ? 228 ASP   B CG  1 
ATOM   4289 O  OD1 . ASP   B  1  215 ? 13.671  -30.140 49.148 1.00 121.30 ? 228 ASP   B OD1 1 
ATOM   4290 O  OD2 . ASP   B  1  215 ? 14.999  -30.007 47.374 1.00 108.64 ? 228 ASP   B OD2 1 
ATOM   4291 N  N   . ARG   B  1  216 ? 11.316  -26.350 48.395 1.00 47.66  ? 229 ARG   B N   1 
ATOM   4292 C  CA  . ARG   B  1  216 ? 11.675  -24.954 48.542 1.00 42.15  ? 229 ARG   B CA  1 
ATOM   4293 C  C   . ARG   B  1  216 ? 12.569  -24.825 49.769 1.00 38.14  ? 229 ARG   B C   1 
ATOM   4294 O  O   . ARG   B  1  216 ? 12.244  -25.306 50.854 1.00 40.89  ? 229 ARG   B O   1 
ATOM   4295 C  CB  . ARG   B  1  216 ? 10.450  -24.042 48.627 1.00 42.72  ? 229 ARG   B CB  1 
ATOM   4296 C  CG  . ARG   B  1  216 ? 9.779   -23.798 47.288 1.00 46.45  ? 229 ARG   B CG  1 
ATOM   4297 C  CD  . ARG   B  1  216 ? 8.416   -23.126 47.466 1.00 47.25  ? 229 ARG   B CD  1 
ATOM   4298 N  NE  . ARG   B  1  216 ? 8.504   -21.760 47.992 1.00 49.02  ? 229 ARG   B NE  1 
ATOM   4299 C  CZ  . ARG   B  1  216 ? 8.997   -20.708 47.333 1.00 53.26  ? 229 ARG   B CZ  1 
ATOM   4300 N  NH1 . ARG   B  1  216 ? 9.380   -20.814 46.065 1.00 54.42  ? 229 ARG   B NH1 1 
ATOM   4301 N  NH2 . ARG   B  1  216 ? 9.085   -19.533 47.935 1.00 56.87  ? 229 ARG   B NH2 1 
ATOM   4302 N  N   . LYS   B  1  217 ? 13.711  -24.170 49.564 1.00 35.25  ? 230 LYS   B N   1 
ATOM   4303 C  CA  . LYS   B  1  217 ? 14.742  -24.094 50.590 1.00 38.68  ? 230 LYS   B CA  1 
ATOM   4304 C  C   . LYS   B  1  217 ? 15.612  -22.880 50.289 1.00 34.59  ? 230 LYS   B C   1 
ATOM   4305 O  O   . LYS   B  1  217 ? 15.821  -22.544 49.129 1.00 32.62  ? 230 LYS   B O   1 
ATOM   4306 C  CB  . LYS   B  1  217 ? 15.519  -25.423 50.599 1.00 38.40  ? 230 LYS   B CB  1 
ATOM   4307 C  CG  . LYS   B  1  217 ? 16.327  -25.660 49.343 1.00 44.48  ? 230 LYS   B CG  1 
ATOM   4308 C  CD  . LYS   B  1  217 ? 16.975  -27.029 49.205 1.00 50.25  ? 230 LYS   B CD  1 
ATOM   4309 C  CE  . LYS   B  1  217 ? 17.877  -27.039 47.982 1.00 59.98  ? 230 LYS   B CE  1 
ATOM   4310 N  NZ  . LYS   B  1  217 ? 18.514  -28.339 47.740 1.00 63.14  ? 230 LYS   B NZ  1 
ATOM   4311 N  N   . LEU   B  1  218 ? 16.137  -22.230 51.331 1.00 35.13  ? 231 LEU   B N   1 
ATOM   4312 C  CA  . LEU   B  1  218 ? 16.885  -20.998 51.134 1.00 31.21  ? 231 LEU   B CA  1 
ATOM   4313 C  C   . LEU   B  1  218 ? 18.383  -21.252 51.301 1.00 32.75  ? 231 LEU   B C   1 
ATOM   4314 O  O   . LEU   B  1  218 ? 18.802  -21.812 52.311 1.00 33.79  ? 231 LEU   B O   1 
ATOM   4315 C  CB  . LEU   B  1  218 ? 16.361  -20.004 52.154 1.00 29.01  ? 231 LEU   B CB  1 
ATOM   4316 C  CG  . LEU   B  1  218 ? 16.924  -18.590 52.039 1.00 31.56  ? 231 LEU   B CG  1 
ATOM   4317 C  CD1 . LEU   B  1  218 ? 16.496  -17.926 50.754 1.00 31.74  ? 231 LEU   B CD1 1 
ATOM   4318 C  CD2 . LEU   B  1  218 ? 16.480  -17.782 53.245 1.00 35.06  ? 231 LEU   B CD2 1 
ATOM   4319 N  N   . SER   B  1  219 ? 19.189  -20.810 50.317 1.00 30.56  ? 232 SER   B N   1 
ATOM   4320 C  CA  . SER   B  1  219 ? 20.641  -20.851 50.448 1.00 31.17  ? 232 SER   B CA  1 
ATOM   4321 C  C   . SER   B  1  219 ? 21.107  -19.843 51.494 1.00 29.94  ? 232 SER   B C   1 
ATOM   4322 O  O   . SER   B  1  219 ? 20.424  -18.855 51.779 1.00 30.77  ? 232 SER   B O   1 
ATOM   4323 C  CB  . SER   B  1  219 ? 21.291  -20.575 49.149 1.00 29.53  ? 232 SER   B CB  1 
ATOM   4324 O  OG  . SER   B  1  219 ? 21.197  -19.184 48.861 1.00 31.16  ? 232 SER   B OG  1 
ATOM   4325 N  N   . MET   B  1  220 ? 22.286  -20.084 52.056 1.00 28.73  ? 233 MET   B N   1 
ATOM   4326 C  CA  . MET   B  1  220 ? 22.819  -19.199 53.070 1.00 30.50  ? 233 MET   B CA  1 
ATOM   4327 C  C   . MET   B  1  220 ? 23.291  -17.891 52.430 1.00 30.29  ? 233 MET   B C   1 
ATOM   4328 O  O   . MET   B  1  220 ? 23.305  -16.858 53.090 1.00 31.63  ? 233 MET   B O   1 
ATOM   4329 C  CB  . MET   B  1  220 ? 23.967  -19.873 53.822 1.00 32.02  ? 233 MET   B CB  1 
ATOM   4330 C  CG  . MET   B  1  220 ? 23.540  -21.090 54.633 1.00 33.26  ? 233 MET   B CG  1 
ATOM   4331 S  SD  . MET   B  1  220 ? 22.258  -20.754 55.866 1.00 36.56  ? 233 MET   B SD  1 
ATOM   4332 C  CE  . MET   B  1  220 ? 20.823  -21.389 54.990 1.00 30.64  ? 233 MET   B CE  1 
ATOM   4333 N  N   . GLU   B  1  221 ? 23.664  -17.937 51.149 1.00 30.85  ? 234 GLU   B N   1 
ATOM   4334 C  CA  . GLU   B  1  221 ? 24.060  -16.754 50.399 1.00 35.16  ? 234 GLU   B CA  1 
ATOM   4335 C  C   . GLU   B  1  221 ? 22.865  -15.803 50.263 1.00 34.70  ? 234 GLU   B C   1 
ATOM   4336 O  O   . GLU   B  1  221 ? 22.993  -14.606 50.504 1.00 32.17  ? 234 GLU   B O   1 
ATOM   4337 C  CB  . GLU   B  1  221 ? 24.601  -17.101 49.006 1.00 37.59  ? 234 GLU   B CB  1 
ATOM   4338 C  CG  . GLU   B  1  221 ? 25.848  -17.993 49.011 1.00 46.83  ? 234 GLU   B CG  1 
ATOM   4339 C  CD  . GLU   B  1  221 ? 25.734  -19.489 49.369 1.00 53.26  ? 234 GLU   B CD  1 
ATOM   4340 O  OE1 . GLU   B  1  221 ? 24.635  -20.106 49.496 1.00 43.70  ? 234 GLU   B OE1 1 
ATOM   4341 O  OE2 . GLU   B  1  221 ? 26.833  -20.061 49.534 1.00 55.87  ? 234 GLU   B OE2 1 
ATOM   4342 N  N   . ASP   B  1  222 ? 21.706  -16.344 49.867 1.00 34.85  ? 235 ASP   B N   1 
ATOM   4343 C  CA  . ASP   B  1  222 ? 20.489  -15.550 49.726 1.00 34.28  ? 235 ASP   B CA  1 
ATOM   4344 C  C   . ASP   B  1  222 ? 20.058  -15.030 51.087 1.00 31.44  ? 235 ASP   B C   1 
ATOM   4345 O  O   . ASP   B  1  222 ? 19.688  -13.862 51.214 1.00 31.04  ? 235 ASP   B O   1 
ATOM   4346 C  CB  . ASP   B  1  222 ? 19.392  -16.326 49.013 1.00 36.03  ? 235 ASP   B CB  1 
ATOM   4347 C  CG  . ASP   B  1  222 ? 19.658  -16.594 47.530 1.00 41.53  ? 235 ASP   B CG  1 
ATOM   4348 O  OD1 . ASP   B  1  222 ? 20.658  -16.022 46.986 1.00 38.98  ? 235 ASP   B OD1 1 
ATOM   4349 O  OD2 . ASP   B  1  222 ? 18.888  -17.398 46.925 1.00 39.57  ? 235 ASP   B OD2 1 
ATOM   4350 N  N   . ALA   B  1  223 ? 20.133  -15.895 52.101 1.00 28.15  ? 236 ALA   B N   1 
ATOM   4351 C  CA  . ALA   B  1  223 ? 19.777  -15.471 53.440 1.00 29.28  ? 236 ALA   B CA  1 
ATOM   4352 C  C   . ALA   B  1  223 ? 20.660  -14.296 53.856 1.00 31.38  ? 236 ALA   B C   1 
ATOM   4353 O  O   . ALA   B  1  223 ? 20.147  -13.307 54.342 1.00 33.52  ? 236 ALA   B O   1 
ATOM   4354 C  CB  . ALA   B  1  223 ? 19.877  -16.619 54.403 1.00 31.69  ? 236 ALA   B CB  1 
ATOM   4355 N  N   . ALA   B  1  224 ? 21.978  -14.369 53.632 1.00 31.60  ? 237 ALA   B N   1 
ATOM   4356 C  CA  . ALA   B  1  224 ? 22.845  -13.301 54.097 1.00 31.52  ? 237 ALA   B CA  1 
ATOM   4357 C  C   . ALA   B  1  224 ? 22.533  -12.018 53.315 1.00 34.24  ? 237 ALA   B C   1 
ATOM   4358 O  O   . ALA   B  1  224 ? 22.520  -10.911 53.856 1.00 34.17  ? 237 ALA   B O   1 
ATOM   4359 C  CB  . ALA   B  1  224 ? 24.291  -13.692 53.963 1.00 30.43  ? 237 ALA   B CB  1 
ATOM   4360 N  N   . SER   B  1  225 ? 22.247  -12.179 52.025 1.00 31.57  ? 238 SER   B N   1 
ATOM   4361 C  CA  . SER   B  1  225 ? 21.992  -11.035 51.176 1.00 34.29  ? 238 SER   B CA  1 
ATOM   4362 C  C   . SER   B  1  225 ? 20.838  -10.204 51.746 1.00 34.11  ? 238 SER   B C   1 
ATOM   4363 O  O   . SER   B  1  225 ? 20.936  -8.976  51.845 1.00 30.36  ? 238 SER   B O   1 
ATOM   4364 C  CB  . SER   B  1  225 ? 21.753  -11.486 49.748 1.00 36.11  ? 238 SER   B CB  1 
ATOM   4365 O  OG  . SER   B  1  225 ? 21.468  -10.382 48.899 1.00 41.72  ? 238 SER   B OG  1 
ATOM   4366 N  N   . ILE   B  1  226 ? 19.771  -10.893 52.168 1.00 33.39  ? 239 ILE   B N   1 
ATOM   4367 C  CA  . ILE   B  1  226 ? 18.561  -10.232 52.629 1.00 31.52  ? 239 ILE   B CA  1 
ATOM   4368 C  C   . ILE   B  1  226 ? 18.693  -9.820  54.096 1.00 32.14  ? 239 ILE   B C   1 
ATOM   4369 O  O   . ILE   B  1  226 ? 18.453  -8.661  54.437 1.00 33.49  ? 239 ILE   B O   1 
ATOM   4370 C  CB  . ILE   B  1  226 ? 17.355  -11.148 52.410 1.00 32.54  ? 239 ILE   B CB  1 
ATOM   4371 C  CG1 . ILE   B  1  226 ? 17.114  -11.361 50.929 1.00 33.48  ? 239 ILE   B CG1 1 
ATOM   4372 C  CG2 . ILE   B  1  226 ? 16.106  -10.594 53.100 1.00 34.79  ? 239 ILE   B CG2 1 
ATOM   4373 C  CD1 . ILE   B  1  226 ? 16.224  -12.546 50.622 1.00 33.65  ? 239 ILE   B CD1 1 
ATOM   4374 N  N   . PHE   B  1  227 ? 19.052  -10.772 54.969 1.00 29.37  ? 240 PHE   B N   1 
ATOM   4375 C  CA  . PHE   B  1  227 ? 19.048  -10.527 56.397 1.00 28.84  ? 240 PHE   B CA  1 
ATOM   4376 C  C   . PHE   B  1  227 ? 20.130  -9.518  56.776 1.00 31.31  ? 240 PHE   B C   1 
ATOM   4377 O  O   . PHE   B  1  227 ? 19.900  -8.704  57.663 1.00 34.83  ? 240 PHE   B O   1 
ATOM   4378 C  CB  . PHE   B  1  227 ? 19.262  -11.787 57.227 1.00 31.12  ? 240 PHE   B CB  1 
ATOM   4379 C  CG  . PHE   B  1  227 ? 18.078  -12.726 57.343 1.00 32.40  ? 240 PHE   B CG  1 
ATOM   4380 C  CD1 . PHE   B  1  227 ? 17.059  -12.456 58.234 1.00 34.92  ? 240 PHE   B CD1 1 
ATOM   4381 C  CD2 . PHE   B  1  227 ? 18.050  -13.935 56.674 1.00 38.71  ? 240 PHE   B CD2 1 
ATOM   4382 C  CE1 . PHE   B  1  227 ? 15.999  -13.336 58.393 1.00 35.74  ? 240 PHE   B CE1 1 
ATOM   4383 C  CE2 . PHE   B  1  227 ? 16.991  -14.815 56.834 1.00 42.34  ? 240 PHE   B CE2 1 
ATOM   4384 C  CZ  . PHE   B  1  227 ? 15.960  -14.503 57.687 1.00 40.34  ? 240 PHE   B CZ  1 
ATOM   4385 N  N   . ARG   B  1  228 ? 21.299  -9.581  56.124 1.00 32.66  ? 241 ARG   B N   1 
ATOM   4386 C  CA  . ARG   B  1  228 ? 22.424  -8.721  56.462 1.00 30.25  ? 241 ARG   B CA  1 
ATOM   4387 C  C   . ARG   B  1  228 ? 22.491  -7.512  55.541 1.00 28.74  ? 241 ARG   B C   1 
ATOM   4388 O  O   . ARG   B  1  228 ? 22.598  -6.397  56.013 1.00 32.33  ? 241 ARG   B O   1 
ATOM   4389 C  CB  . ARG   B  1  228 ? 23.774  -9.447  56.429 1.00 33.75  ? 241 ARG   B CB  1 
ATOM   4390 C  CG  . ARG   B  1  228 ? 24.946  -8.563  56.858 1.00 34.70  ? 241 ARG   B CG  1 
ATOM   4391 C  CD  . ARG   B  1  228 ? 26.293  -9.283  57.056 1.00 35.94  ? 241 ARG   B CD  1 
ATOM   4392 N  NE  . ARG   B  1  228 ? 26.807  -9.925  55.842 1.00 35.10  ? 241 ARG   B NE  1 
ATOM   4393 C  CZ  . ARG   B  1  228 ? 27.066  -11.219 55.676 1.00 37.44  ? 241 ARG   B CZ  1 
ATOM   4394 N  NH1 . ARG   B  1  228 ? 26.971  -12.085 56.683 1.00 39.88  ? 241 ARG   B NH1 1 
ATOM   4395 N  NH2 . ARG   B  1  228 ? 27.429  -11.667 54.482 1.00 35.84  ? 241 ARG   B NH2 1 
ATOM   4396 N  N   . ASP   B  1  229 ? 22.429  -7.720  54.228 1.00 31.40  ? 242 ASP   B N   1 
ATOM   4397 C  CA  . ASP   B  1  229 ? 22.752  -6.645  53.307 1.00 32.49  ? 242 ASP   B CA  1 
ATOM   4398 C  C   . ASP   B  1  229 ? 21.510  -5.872  52.857 1.00 33.28  ? 242 ASP   B C   1 
ATOM   4399 O  O   . ASP   B  1  229 ? 21.658  -4.844  52.205 1.00 32.64  ? 242 ASP   B O   1 
ATOM   4400 C  CB  . ASP   B  1  229 ? 23.584  -7.160  52.144 1.00 32.63  ? 242 ASP   B CB  1 
ATOM   4401 C  CG  . ASP   B  1  229 ? 24.986  -7.670  52.470 1.00 36.36  ? 242 ASP   B CG  1 
ATOM   4402 O  OD1 . ASP   B  1  229 ? 25.573  -7.234  53.478 1.00 39.18  ? 242 ASP   B OD1 1 
ATOM   4403 O  OD2 . ASP   B  1  229 ? 25.486  -8.543  51.725 1.00 39.10  ? 242 ASP   B OD2 1 
ATOM   4404 N  N   . MET   B  1  230 ? 20.300  -6.379  53.157 1.00 34.51  ? 243 MET   B N   1 
ATOM   4405 C  CA  A MET   B  1  230 ? 19.068  -5.726  52.744 0.50 34.19  ? 243 MET   B CA  1 
ATOM   4406 C  CA  B MET   B  1  230 ? 19.066  -5.729  52.743 0.50 34.12  ? 243 MET   B CA  1 
ATOM   4407 C  C   . MET   B  1  230 ? 19.013  -5.655  51.221 1.00 32.90  ? 243 MET   B C   1 
ATOM   4408 O  O   . MET   B  1  230 ? 18.621  -4.625  50.667 1.00 31.74  ? 243 MET   B O   1 
ATOM   4409 C  CB  A MET   B  1  230 ? 18.980  -4.308  53.323 0.50 34.77  ? 243 MET   B CB  1 
ATOM   4410 C  CB  B MET   B  1  230 ? 18.972  -4.306  53.309 0.50 34.59  ? 243 MET   B CB  1 
ATOM   4411 C  CG  A MET   B  1  230 ? 19.235  -4.227  54.810 0.50 35.49  ? 243 MET   B CG  1 
ATOM   4412 C  CG  B MET   B  1  230 ? 19.186  -4.221  54.792 0.50 35.06  ? 243 MET   B CG  1 
ATOM   4413 S  SD  A MET   B  1  230 ? 19.260  -2.534  55.439 0.50 35.64  ? 243 MET   B SD  1 
ATOM   4414 S  SD  B MET   B  1  230 ? 19.247  -2.506  55.345 0.50 35.38  ? 243 MET   B SD  1 
ATOM   4415 C  CE  A MET   B  1  230 ? 19.875  -2.808  57.113 0.50 35.63  ? 243 MET   B CE  1 
ATOM   4416 C  CE  B MET   B  1  230 ? 20.954  -2.065  54.986 0.50 33.17  ? 243 MET   B CE  1 
ATOM   4417 N  N   . ARG   B  1  231 ? 19.423  -6.762  50.573 1.00 33.63  ? 244 ARG   B N   1 
ATOM   4418 C  CA  A ARG   B  1  231 ? 19.596  -6.817  49.130 0.50 30.19  ? 244 ARG   B CA  1 
ATOM   4419 C  CA  B ARG   B  1  231 ? 19.584  -6.816  49.131 0.50 30.59  ? 244 ARG   B CA  1 
ATOM   4420 C  C   . ARG   B  1  231 ? 18.921  -8.085  48.611 1.00 30.40  ? 244 ARG   B C   1 
ATOM   4421 O  O   . ARG   B  1  231 ? 19.162  -9.170  49.121 1.00 32.12  ? 244 ARG   B O   1 
ATOM   4422 C  CB  A ARG   B  1  231 ? 21.080  -6.826  48.745 0.50 30.41  ? 244 ARG   B CB  1 
ATOM   4423 C  CB  B ARG   B  1  231 ? 21.068  -6.812  48.762 0.50 31.35  ? 244 ARG   B CB  1 
ATOM   4424 C  CG  A ARG   B  1  231 ? 21.345  -6.703  47.242 0.50 31.58  ? 244 ARG   B CG  1 
ATOM   4425 C  CG  B ARG   B  1  231 ? 21.369  -6.682  47.271 0.50 33.29  ? 244 ARG   B CG  1 
ATOM   4426 C  CD  A ARG   B  1  231 ? 22.794  -6.851  46.754 0.50 31.97  ? 244 ARG   B CD  1 
ATOM   4427 C  CD  B ARG   B  1  231 ? 22.880  -6.571  47.042 0.50 34.05  ? 244 ARG   B CD  1 
ATOM   4428 N  NE  A ARG   B  1  231 ? 23.301  -8.227  46.865 0.50 34.81  ? 244 ARG   B NE  1 
ATOM   4429 N  NE  B ARG   B  1  231 ? 23.506  -7.844  47.422 0.50 38.58  ? 244 ARG   B NE  1 
ATOM   4430 C  CZ  A ARG   B  1  231 ? 23.078  -9.234  46.028 0.50 34.08  ? 244 ARG   B CZ  1 
ATOM   4431 C  CZ  B ARG   B  1  231 ? 24.445  -8.042  48.351 0.50 36.26  ? 244 ARG   B CZ  1 
ATOM   4432 N  NH1 A ARG   B  1  231 ? 22.593  -8.989  44.822 0.50 36.52  ? 244 ARG   B NH1 1 
ATOM   4433 N  NH1 B ARG   B  1  231 ? 25.139  -7.033  48.842 0.50 36.20  ? 244 ARG   B NH1 1 
ATOM   4434 N  NH2 A ARG   B  1  231 ? 23.356  -10.474 46.409 0.50 30.72  ? 244 ARG   B NH2 1 
ATOM   4435 N  NH2 B ARG   B  1  231 ? 24.722  -9.268  48.750 0.50 35.17  ? 244 ARG   B NH2 1 
ATOM   4436 N  N   . PHE   B  1  232 ? 18.071  -7.942  47.597 1.00 28.63  ? 245 PHE   B N   1 
ATOM   4437 C  CA  . PHE   B  1  232 ? 17.497  -9.085  46.922 1.00 30.14  ? 245 PHE   B CA  1 
ATOM   4438 C  C   . PHE   B  1  232 ? 18.596  -9.903  46.255 1.00 33.38  ? 245 PHE   B C   1 
ATOM   4439 O  O   . PHE   B  1  232 ? 19.521  -9.329  45.689 1.00 33.48  ? 245 PHE   B O   1 
ATOM   4440 C  CB  . PHE   B  1  232 ? 16.591  -8.647  45.775 1.00 30.84  ? 245 PHE   B CB  1 
ATOM   4441 C  CG  . PHE   B  1  232 ? 15.235  -8.131  46.204 1.00 32.28  ? 245 PHE   B CG  1 
ATOM   4442 C  CD1 . PHE   B  1  232 ? 14.325  -9.000  46.786 1.00 33.36  ? 245 PHE   B CD1 1 
ATOM   4443 C  CD2 . PHE   B  1  232 ? 14.851  -6.812  45.974 1.00 34.40  ? 245 PHE   B CD2 1 
ATOM   4444 C  CE1 . PHE   B  1  232 ? 13.076  -8.542  47.174 1.00 35.79  ? 245 PHE   B CE1 1 
ATOM   4445 C  CE2 . PHE   B  1  232 ? 13.587  -6.362  46.341 1.00 35.12  ? 245 PHE   B CE2 1 
ATOM   4446 C  CZ  . PHE   B  1  232 ? 12.711  -7.228  46.950 1.00 37.35  ? 245 PHE   B CZ  1 
ATOM   4447 N  N   . PRO   B  1  233 ? 18.514  -11.248 46.231 1.00 30.26  ? 246 PRO   B N   1 
ATOM   4448 C  CA  . PRO   B  1  233 ? 19.382  -12.026 45.362 1.00 31.52  ? 246 PRO   B CA  1 
ATOM   4449 C  C   . PRO   B  1  233 ? 19.337  -11.480 43.936 1.00 33.90  ? 246 PRO   B C   1 
ATOM   4450 O  O   . PRO   B  1  233 ? 18.367  -10.836 43.527 1.00 34.60  ? 246 PRO   B O   1 
ATOM   4451 C  CB  . PRO   B  1  233 ? 18.818  -13.455 45.470 1.00 34.04  ? 246 PRO   B CB  1 
ATOM   4452 C  CG  . PRO   B  1  233 ? 18.144  -13.499 46.824 1.00 31.60  ? 246 PRO   B CG  1 
ATOM   4453 C  CD  . PRO   B  1  233 ? 17.584  -12.081 46.992 1.00 31.38  ? 246 PRO   B CD  1 
ATOM   4454 N  N   . ASP   B  1  234 ? 20.427  -11.693 43.190 1.00 34.51  ? 247 ASP   B N   1 
ATOM   4455 C  CA  . ASP   B  1  234 ? 20.450  -11.350 41.777 1.00 35.54  ? 247 ASP   B CA  1 
ATOM   4456 C  C   . ASP   B  1  234 ? 19.282  -12.047 41.079 1.00 34.84  ? 247 ASP   B C   1 
ATOM   4457 O  O   . ASP   B  1  234 ? 19.008  -13.234 41.314 1.00 35.77  ? 247 ASP   B O   1 
ATOM   4458 C  CB  . ASP   B  1  234 ? 21.762  -11.741 41.112 1.00 37.20  ? 247 ASP   B CB  1 
ATOM   4459 C  CG  . ASP   B  1  234 ? 23.014  -10.980 41.547 1.00 39.57  ? 247 ASP   B CG  1 
ATOM   4460 O  OD1 . ASP   B  1  234 ? 22.943  -10.074 42.426 1.00 42.65  ? 247 ASP   B OD1 1 
ATOM   4461 O  OD2 . ASP   B  1  234 ? 24.076  -11.309 41.003 1.00 38.73  ? 247 ASP   B OD2 1 
ATOM   4462 N  N   . ASP   B  1  235 ? 18.598  -11.279 40.222 1.00 34.95  ? 248 ASP   B N   1 
ATOM   4463 C  CA  . ASP   B  1  235 ? 17.551  -11.805 39.362 1.00 40.14  ? 248 ASP   B CA  1 
ATOM   4464 C  C   . ASP   B  1  235 ? 16.373  -12.358 40.183 1.00 35.94  ? 248 ASP   B C   1 
ATOM   4465 O  O   . ASP   B  1  235 ? 15.675  -13.265 39.740 1.00 35.94  ? 248 ASP   B O   1 
ATOM   4466 C  CB  . ASP   B  1  235 ? 18.115  -12.854 38.407 1.00 42.67  ? 248 ASP   B CB  1 
ATOM   4467 C  CG  . ASP   B  1  235 ? 17.159  -13.228 37.277 1.00 45.89  ? 248 ASP   B CG  1 
ATOM   4468 O  OD1 . ASP   B  1  235 ? 16.626  -12.271 36.647 1.00 38.90  ? 248 ASP   B OD1 1 
ATOM   4469 O  OD2 . ASP   B  1  235 ? 16.932  -14.457 37.069 1.00 39.49  ? 248 ASP   B OD2 1 
ATOM   4470 N  N   . PHE   B  1  236 ? 16.151  -11.817 41.384 1.00 37.33  ? 249 PHE   B N   1 
ATOM   4471 C  CA  . PHE   B  1  236 ? 15.168  -12.381 42.294 1.00 37.58  ? 249 PHE   B CA  1 
ATOM   4472 C  C   . PHE   B  1  236 ? 13.769  -12.206 41.715 1.00 34.20  ? 249 PHE   B C   1 
ATOM   4473 O  O   . PHE   B  1  236 ? 13.357  -11.094 41.361 1.00 28.19  ? 249 PHE   B O   1 
ATOM   4474 C  CB  . PHE   B  1  236 ? 15.227  -11.724 43.675 1.00 35.44  ? 249 PHE   B CB  1 
ATOM   4475 C  CG  . PHE   B  1  236 ? 14.247  -12.343 44.659 1.00 37.03  ? 249 PHE   B CG  1 
ATOM   4476 C  CD1 . PHE   B  1  236 ? 14.470  -13.612 45.185 1.00 33.30  ? 249 PHE   B CD1 1 
ATOM   4477 C  CD2 . PHE   B  1  236 ? 13.106  -11.654 45.051 1.00 38.68  ? 249 PHE   B CD2 1 
ATOM   4478 C  CE1 . PHE   B  1  236 ? 13.597  -14.158 46.107 1.00 33.68  ? 249 PHE   B CE1 1 
ATOM   4479 C  CE2 . PHE   B  1  236 ? 12.221  -12.220 45.958 1.00 37.10  ? 249 PHE   B CE2 1 
ATOM   4480 C  CZ  . PHE   B  1  236 ? 12.478  -13.468 46.491 1.00 34.31  ? 249 PHE   B CZ  1 
ATOM   4481 N  N   . HIS   B  1  237 ? 13.055  -13.329 41.672 1.00 32.42  ? 250 HIS   B N   1 
ATOM   4482 C  CA  . HIS   B  1  237 ? 11.656  -13.338 41.301 1.00 35.38  ? 250 HIS   B CA  1 
ATOM   4483 C  C   . HIS   B  1  237 ? 10.849  -13.670 42.549 1.00 33.17  ? 250 HIS   B C   1 
ATOM   4484 O  O   . HIS   B  1  237 ? 11.111  -14.687 43.207 1.00 31.13  ? 250 HIS   B O   1 
ATOM   4485 C  CB  . HIS   B  1  237 ? 11.385  -14.386 40.217 1.00 39.16  ? 250 HIS   B CB  1 
ATOM   4486 C  CG  . HIS   B  1  237 ? 11.866  -13.992 38.869 1.00 44.47  ? 250 HIS   B CG  1 
ATOM   4487 N  ND1 . HIS   B  1  237 ? 13.137  -13.499 38.677 1.00 49.50  ? 250 HIS   B ND1 1 
ATOM   4488 C  CD2 . HIS   B  1  237 ? 11.287  -14.036 37.661 1.00 47.30  ? 250 HIS   B CD2 1 
ATOM   4489 C  CE1 . HIS   B  1  237 ? 13.301  -13.236 37.387 1.00 50.40  ? 250 HIS   B CE1 1 
ATOM   4490 N  NE2 . HIS   B  1  237 ? 12.190  -13.545 36.757 1.00 47.95  ? 250 HIS   B NE2 1 
ATOM   4491 N  N   . ARG   B  1  238 ? 9.839   -12.836 42.825 1.00 31.38  ? 251 ARG   B N   1 
ATOM   4492 C  CA  . ARG   B  1  238 ? 8.978   -13.030 43.985 1.00 33.46  ? 251 ARG   B CA  1 
ATOM   4493 C  C   . ARG   B  1  238 ? 8.153   -14.303 43.870 1.00 34.12  ? 251 ARG   B C   1 
ATOM   4494 O  O   . ARG   B  1  238 ? 8.029   -14.875 42.793 1.00 35.38  ? 251 ARG   B O   1 
ATOM   4495 C  CB  . ARG   B  1  238 ? 7.997   -11.875 44.128 1.00 36.70  ? 251 ARG   B CB  1 
ATOM   4496 C  CG  . ARG   B  1  238 ? 6.976   -11.783 43.003 1.00 38.49  ? 251 ARG   B CG  1 
ATOM   4497 C  CD  . ARG   B  1  238 ? 6.110   -10.555 43.180 1.00 36.97  ? 251 ARG   B CD  1 
ATOM   4498 N  NE  . ARG   B  1  238 ? 4.851   -10.777 42.468 1.00 42.92  ? 251 ARG   B NE  1 
ATOM   4499 C  CZ  . ARG   B  1  238 ? 3.922   -9.868  42.218 1.00 41.21  ? 251 ARG   B CZ  1 
ATOM   4500 N  NH1 . ARG   B  1  238 ? 3.968   -8.668  42.783 1.00 41.93  ? 251 ARG   B NH1 1 
ATOM   4501 N  NH2 . ARG   B  1  238 ? 2.935   -10.185 41.411 1.00 44.53  ? 251 ARG   B NH2 1 
ATOM   4502 N  N   . SER   B  1  239 ? 7.612   -14.737 45.015 1.00 36.37  ? 252 SER   B N   1 
ATOM   4503 C  CA  . SER   B  1  239 ? 6.695   -15.863 45.102 1.00 36.75  ? 252 SER   B CA  1 
ATOM   4504 C  C   . SER   B  1  239 ? 5.668   -15.814 43.972 1.00 38.34  ? 252 SER   B C   1 
ATOM   4505 O  O   . SER   B  1  239 ? 5.211   -14.733 43.592 1.00 36.99  ? 252 SER   B O   1 
ATOM   4506 C  CB  . SER   B  1  239 ? 5.991   -15.858 46.433 1.00 35.89  ? 252 SER   B CB  1 
ATOM   4507 O  OG  . SER   B  1  239 ? 5.070   -16.934 46.528 1.00 35.49  ? 252 SER   B OG  1 
ATOM   4508 N  N   . ALA   B  1  240 ? 5.287   -16.999 43.479 1.00 38.68  ? 253 ALA   B N   1 
ATOM   4509 C  CA  . ALA   B  1  240 ? 4.399   -17.118 42.330 1.00 47.72  ? 253 ALA   B CA  1 
ATOM   4510 C  C   . ALA   B  1  240 ? 2.932   -16.935 42.747 1.00 48.18  ? 253 ALA   B C   1 
ATOM   4511 O  O   . ALA   B  1  240 ? 2.073   -16.765 41.886 1.00 47.79  ? 253 ALA   B O   1 
ATOM   4512 C  CB  . ALA   B  1  240 ? 4.627   -18.461 41.657 1.00 42.81  ? 253 ALA   B CB  1 
ATOM   4513 N  N   . VAL   B  1  241 ? 2.664   -16.991 44.064 1.00 47.32  ? 254 VAL   B N   1 
ATOM   4514 C  CA  . VAL   B  1  241 ? 1.342   -16.802 44.643 1.00 44.88  ? 254 VAL   B CA  1 
ATOM   4515 C  C   . VAL   B  1  241 ? 1.466   -15.887 45.861 1.00 47.55  ? 254 VAL   B C   1 
ATOM   4516 O  O   . VAL   B  1  241 ? 2.498   -15.860 46.536 1.00 41.48  ? 254 VAL   B O   1 
ATOM   4517 C  CB  . VAL   B  1  241 ? 0.722   -18.146 45.072 1.00 48.80  ? 254 VAL   B CB  1 
ATOM   4518 C  CG1 . VAL   B  1  241 ? 0.408   -19.054 43.884 1.00 48.75  ? 254 VAL   B CG1 1 
ATOM   4519 C  CG2 . VAL   B  1  241 ? 1.591   -18.891 46.078 1.00 46.52  ? 254 VAL   B CG2 1 
ATOM   4520 N  N   . PRO   B  1  242 ? 0.416   -15.118 46.219 1.00 43.97  ? 255 PRO   B N   1 
ATOM   4521 C  CA  . PRO   B  1  242 ? 0.440   -14.381 47.475 1.00 40.31  ? 255 PRO   B CA  1 
ATOM   4522 C  C   . PRO   B  1  242 ? 0.700   -15.388 48.590 1.00 39.40  ? 255 PRO   B C   1 
ATOM   4523 O  O   . PRO   B  1  242 ? 0.180   -16.507 48.552 1.00 38.76  ? 255 PRO   B O   1 
ATOM   4524 C  CB  . PRO   B  1  242 ? -0.951  -13.753 47.521 1.00 42.67  ? 255 PRO   B CB  1 
ATOM   4525 C  CG  . PRO   B  1  242 ? -1.305  -13.602 46.069 1.00 42.59  ? 255 PRO   B CG  1 
ATOM   4526 C  CD  . PRO   B  1  242 ? -0.819  -14.899 45.451 1.00 40.67  ? 255 PRO   B CD  1 
ATOM   4527 N  N   . ALA   B  1  243 ? 1.563   -15.021 49.546 1.00 36.65  ? 256 ALA   B N   1 
ATOM   4528 C  CA  . ALA   B  1  243 ? 1.875   -15.961 50.612 1.00 35.38  ? 256 ALA   B CA  1 
ATOM   4529 C  C   . ALA   B  1  243 ? 2.217   -15.220 51.890 1.00 32.64  ? 256 ALA   B C   1 
ATOM   4530 O  O   . ALA   B  1  243 ? 2.439   -14.006 51.873 1.00 35.14  ? 256 ALA   B O   1 
ATOM   4531 C  CB  . ALA   B  1  243 ? 3.001   -16.856 50.171 1.00 37.92  ? 256 ALA   B CB  1 
ATOM   4532 N  N   . SER   B  1  244 ? 2.287   -15.982 52.983 1.00 33.88  ? 257 SER   B N   1 
ATOM   4533 C  CA  . SER   B  1  244 ? 2.678   -15.436 54.268 1.00 36.47  ? 257 SER   B CA  1 
ATOM   4534 C  C   . SER   B  1  244 ? 3.194   -16.558 55.159 1.00 34.89  ? 257 SER   B C   1 
ATOM   4535 O  O   . SER   B  1  244 ? 4.348   -16.940 55.019 1.00 35.29  ? 257 SER   B O   1 
ATOM   4536 C  CB  . SER   B  1  244 ? 1.540   -14.669 54.900 1.00 40.13  ? 257 SER   B CB  1 
ATOM   4537 O  OG  . SER   B  1  244 ? 0.364   -15.453 54.942 1.00 38.20  ? 257 SER   B OG  1 
ATOM   4538 N  N   . ASN   B  1  245 ? 2.326   -17.138 56.000 1.00 34.93  ? 258 ASN   B N   1 
ATOM   4539 C  CA  . ASN   B  1  245 ? 2.768   -17.961 57.118 1.00 37.01  ? 258 ASN   B CA  1 
ATOM   4540 C  C   . ASN   B  1  245 ? 2.443   -19.447 56.923 1.00 34.51  ? 258 ASN   B C   1 
ATOM   4541 O  O   . ASN   B  1  245 ? 2.338   -20.185 57.898 1.00 35.72  ? 258 ASN   B O   1 
ATOM   4542 C  CB  . ASN   B  1  245 ? 2.177   -17.442 58.423 1.00 42.81  ? 258 ASN   B CB  1 
ATOM   4543 C  CG  . ASN   B  1  245 ? 0.681   -17.667 58.522 1.00 48.18  ? 258 ASN   B CG  1 
ATOM   4544 O  OD1 . ASN   B  1  245 ? -0.008  -17.906 57.519 1.00 47.93  ? 258 ASN   B OD1 1 
ATOM   4545 N  ND2 . ASN   B  1  245 ? 0.165   -17.621 59.737 1.00 55.66  ? 258 ASN   B ND2 1 
ATOM   4546 N  N   . GLU   B  1  246 ? 2.313   -19.894 55.675 1.00 34.90  ? 259 GLU   B N   1 
ATOM   4547 C  CA  . GLU   B  1  246 ? 2.057   -21.295 55.389 1.00 39.11  ? 259 GLU   B CA  1 
ATOM   4548 C  C   . GLU   B  1  246 ? 3.177   -22.122 56.024 1.00 42.43  ? 259 GLU   B C   1 
ATOM   4549 O  O   . GLU   B  1  246 ? 4.356   -21.832 55.811 1.00 38.74  ? 259 GLU   B O   1 
ATOM   4550 C  CB  . GLU   B  1  246 ? 2.006   -21.581 53.883 1.00 41.74  ? 259 GLU   B CB  1 
ATOM   4551 C  CG  . GLU   B  1  246 ? 0.848   -20.898 53.158 1.00 45.17  ? 259 GLU   B CG  1 
ATOM   4552 C  CD  . GLU   B  1  246 ? 0.958   -19.398 52.882 1.00 50.55  ? 259 GLU   B CD  1 
ATOM   4553 O  OE1 . GLU   B  1  246 ? 1.976   -18.765 53.252 1.00 44.77  ? 259 GLU   B OE1 1 
ATOM   4554 O  OE2 . GLU   B  1  246 ? -0.011  -18.841 52.302 1.00 51.08  ? 259 GLU   B OE2 1 
ATOM   4555 N  N   . GLY   B  1  247 ? 2.798   -23.121 56.834 1.00 38.45  ? 260 GLY   B N   1 
ATOM   4556 C  CA  . GLY   B  1  247 ? 3.729   -24.050 57.450 1.00 35.16  ? 260 GLY   B CA  1 
ATOM   4557 C  C   . GLY   B  1  247 ? 4.053   -23.682 58.894 1.00 33.64  ? 260 GLY   B C   1 
ATOM   4558 O  O   . GLY   B  1  247 ? 4.712   -24.458 59.585 1.00 39.80  ? 260 GLY   B O   1 
ATOM   4559 N  N   . ALA   B  1  248 ? 3.580   -22.524 59.376 1.00 34.91  ? 261 ALA   B N   1 
ATOM   4560 C  CA  . ALA   B  1  248 ? 3.918   -22.088 60.733 1.00 38.56  ? 261 ALA   B CA  1 
ATOM   4561 C  C   . ALA   B  1  248 ? 3.401   -23.074 61.782 1.00 39.99  ? 261 ALA   B C   1 
ATOM   4562 O  O   . ALA   B  1  248 ? 4.030   -23.269 62.827 1.00 37.31  ? 261 ALA   B O   1 
ATOM   4563 C  CB  . ALA   B  1  248 ? 3.373   -20.702 60.998 1.00 38.07  ? 261 ALA   B CB  1 
ATOM   4564 N  N   . ASP   B  1  249 ? 2.238   -23.671 61.490 1.00 43.94  ? 262 ASP   B N   1 
ATOM   4565 C  CA  . ASP   B  1  249 ? 1.644   -24.734 62.293 1.00 53.43  ? 262 ASP   B CA  1 
ATOM   4566 C  C   . ASP   B  1  249 ? 2.621   -25.903 62.476 1.00 47.26  ? 262 ASP   B C   1 
ATOM   4567 O  O   . ASP   B  1  249 ? 2.755   -26.421 63.582 1.00 43.72  ? 262 ASP   B O   1 
ATOM   4568 C  CB  . ASP   B  1  249 ? 0.302   -25.195 61.725 1.00 55.26  ? 262 ASP   B CB  1 
ATOM   4569 C  CG  . ASP   B  1  249 ? 0.264   -25.594 60.248 1.00 74.24  ? 262 ASP   B CG  1 
ATOM   4570 O  OD1 . ASP   B  1  249 ? 1.258   -25.322 59.501 1.00 67.72  ? 262 ASP   B OD1 1 
ATOM   4571 O  OD2 . ASP   B  1  249 ? -0.765  -26.192 59.841 1.00 74.84  ? 262 ASP   B OD2 1 
ATOM   4572 N  N   . GLN   B  1  250 ? 3.288   -26.334 61.401 1.00 40.37  ? 263 GLN   B N   1 
ATOM   4573 C  CA  . GLN   B  1  250 ? 4.198   -27.465 61.487 1.00 44.28  ? 263 GLN   B CA  1 
ATOM   4574 C  C   . GLN   B  1  250 ? 5.439   -27.106 62.308 1.00 44.38  ? 263 GLN   B C   1 
ATOM   4575 O  O   . GLN   B  1  250 ? 6.039   -27.972 62.934 1.00 43.08  ? 263 GLN   B O   1 
ATOM   4576 C  CB  . GLN   B  1  250 ? 4.615   -27.933 60.100 1.00 49.55  ? 263 GLN   B CB  1 
ATOM   4577 C  CG  . GLN   B  1  250 ? 3.469   -28.508 59.276 1.00 50.42  ? 263 GLN   B CG  1 
ATOM   4578 C  CD  . GLN   B  1  250 ? 3.924   -28.866 57.880 1.00 55.19  ? 263 GLN   B CD  1 
ATOM   4579 O  OE1 . GLN   B  1  250 ? 4.820   -29.701 57.702 1.00 55.25  ? 263 GLN   B OE1 1 
ATOM   4580 N  NE2 . GLN   B  1  250 ? 3.369   -28.187 56.882 1.00 55.91  ? 263 GLN   B NE2 1 
ATOM   4581 N  N   . VAL   B  1  251 ? 5.807   -25.823 62.318 1.00 40.51  ? 264 VAL   B N   1 
ATOM   4582 C  CA  . VAL   B  1  251 ? 6.953   -25.385 63.089 1.00 38.58  ? 264 VAL   B CA  1 
ATOM   4583 C  C   . VAL   B  1  251 ? 6.636   -25.546 64.571 1.00 38.70  ? 264 VAL   B C   1 
ATOM   4584 O  O   . VAL   B  1  251 ? 7.452   -26.053 65.329 1.00 37.80  ? 264 VAL   B O   1 
ATOM   4585 C  CB  . VAL   B  1  251 ? 7.363   -23.942 62.741 1.00 36.57  ? 264 VAL   B CB  1 
ATOM   4586 C  CG1 . VAL   B  1  251 ? 8.348   -23.357 63.742 1.00 38.07  ? 264 VAL   B CG1 1 
ATOM   4587 C  CG2 . VAL   B  1  251 ? 7.941   -23.852 61.338 1.00 38.75  ? 264 VAL   B CG2 1 
ATOM   4588 N  N   . LEU   B  1  252 ? 5.442   -25.111 64.969 1.00 44.13  ? 265 LEU   B N   1 
ATOM   4589 C  CA  . LEU   B  1  252 ? 4.982   -25.249 66.343 1.00 44.61  ? 265 LEU   B CA  1 
ATOM   4590 C  C   . LEU   B  1  252 ? 4.856   -26.725 66.721 1.00 44.16  ? 265 LEU   B C   1 
ATOM   4591 O  O   . LEU   B  1  252 ? 5.298   -27.111 67.803 1.00 44.32  ? 265 LEU   B O   1 
ATOM   4592 C  CB  . LEU   B  1  252 ? 3.661   -24.516 66.549 1.00 41.45  ? 265 LEU   B CB  1 
ATOM   4593 C  CG  . LEU   B  1  252 ? 3.094   -24.600 67.968 1.00 48.50  ? 265 LEU   B CG  1 
ATOM   4594 C  CD1 . LEU   B  1  252 ? 4.023   -23.963 69.000 1.00 42.62  ? 265 LEU   B CD1 1 
ATOM   4595 C  CD2 . LEU   B  1  252 ? 1.695   -23.994 68.028 1.00 47.93  ? 265 LEU   B CD2 1 
ATOM   4596 N  N   . ALA   B  1  253 ? 4.284   -27.545 65.829 1.00 41.71  ? 266 ALA   B N   1 
ATOM   4597 C  CA  . ALA   B  1  253 ? 4.031   -28.946 66.142 1.00 43.97  ? 266 ALA   B CA  1 
ATOM   4598 C  C   . ALA   B  1  253 ? 5.334   -29.729 66.334 1.00 50.07  ? 266 ALA   B C   1 
ATOM   4599 O  O   . ALA   B  1  253 ? 5.375   -30.671 67.108 1.00 55.29  ? 266 ALA   B O   1 
ATOM   4600 C  CB  . ALA   B  1  253 ? 3.169   -29.580 65.074 1.00 42.12  ? 266 ALA   B CB  1 
ATOM   4601 N  N   . ALA   B  1  254 ? 6.412   -29.349 65.645 1.00 53.39  ? 267 ALA   B N   1 
ATOM   4602 C  CA  . ALA   B  1  254 ? 7.692   -30.023 65.812 1.00 54.20  ? 267 ALA   B CA  1 
ATOM   4603 C  C   . ALA   B  1  254 ? 8.209   -29.916 67.253 1.00 55.03  ? 267 ALA   B C   1 
ATOM   4604 O  O   . ALA   B  1  254 ? 8.906   -30.815 67.720 1.00 53.33  ? 267 ALA   B O   1 
ATOM   4605 C  CB  . ALA   B  1  254 ? 8.696   -29.432 64.850 1.00 58.79  ? 267 ALA   B CB  1 
ATOM   4606 N  N   . HIS   B  1  255 ? 7.927   -28.788 67.932 1.00 52.99  ? 268 HIS   B N   1 
ATOM   4607 C  CA  . HIS   B  1  255 ? 8.282   -28.599 69.334 1.00 53.27  ? 268 HIS   B CA  1 
ATOM   4608 C  C   . HIS   B  1  255 ? 7.185   -27.808 70.050 1.00 53.10  ? 268 HIS   B C   1 
ATOM   4609 O  O   . HIS   B  1  255 ? 7.288   -26.592 70.216 1.00 51.91  ? 268 HIS   B O   1 
ATOM   4610 C  CB  . HIS   B  1  255 ? 9.656   -27.940 69.496 1.00 56.86  ? 268 HIS   B CB  1 
ATOM   4611 C  CG  . HIS   B  1  255 ? 10.808  -28.846 69.225 1.00 63.31  ? 268 HIS   B CG  1 
ATOM   4612 N  ND1 . HIS   B  1  255 ? 11.225  -29.798 70.130 1.00 70.13  ? 268 HIS   B ND1 1 
ATOM   4613 C  CD2 . HIS   B  1  255 ? 11.609  -28.957 68.160 1.00 62.15  ? 268 HIS   B CD2 1 
ATOM   4614 C  CE1 . HIS   B  1  255 ? 12.245  -30.464 69.609 1.00 76.92  ? 268 HIS   B CE1 1 
ATOM   4615 N  NE2 . HIS   B  1  255 ? 12.497  -29.971 68.411 1.00 68.12  ? 268 HIS   B NE2 1 
ATOM   4616 N  N   . PRO   B  1  256 ? 6.098   -28.480 70.498 1.00 48.94  ? 269 PRO   B N   1 
ATOM   4617 C  CA  . PRO   B  1  256 ? 4.992   -27.788 71.157 1.00 48.03  ? 269 PRO   B CA  1 
ATOM   4618 C  C   . PRO   B  1  256 ? 5.488   -26.874 72.265 1.00 45.15  ? 269 PRO   B C   1 
ATOM   4619 O  O   . PRO   B  1  256 ? 6.382   -27.224 73.034 1.00 48.84  ? 269 PRO   B O   1 
ATOM   4620 C  CB  . PRO   B  1  256 ? 4.108   -28.923 71.684 1.00 52.46  ? 269 PRO   B CB  1 
ATOM   4621 C  CG  . PRO   B  1  256 ? 4.366   -30.044 70.677 1.00 58.23  ? 269 PRO   B CG  1 
ATOM   4622 C  CD  . PRO   B  1  256 ? 5.856   -29.923 70.341 1.00 48.49  ? 269 PRO   B CD  1 
ATOM   4623 N  N   . TRP   B  1  257 ? 4.894   -25.684 72.301 1.00 42.98  ? 270 TRP   B N   1 
ATOM   4624 C  CA  . TRP   B  1  257 ? 5.315   -24.633 73.201 1.00 44.06  ? 270 TRP   B CA  1 
ATOM   4625 C  C   . TRP   B  1  257 ? 4.123   -23.744 73.545 1.00 44.89  ? 270 TRP   B C   1 
ATOM   4626 O  O   . TRP   B  1  257 ? 3.201   -23.576 72.752 1.00 44.09  ? 270 TRP   B O   1 
ATOM   4627 C  CB  . TRP   B  1  257 ? 6.464   -23.818 72.589 1.00 42.33  ? 270 TRP   B CB  1 
ATOM   4628 C  CG  . TRP   B  1  257 ? 7.152   -22.976 73.620 1.00 40.97  ? 270 TRP   B CG  1 
ATOM   4629 C  CD1 . TRP   B  1  257 ? 7.000   -21.642 73.833 1.00 44.38  ? 270 TRP   B CD1 1 
ATOM   4630 C  CD2 . TRP   B  1  257 ? 8.018   -23.457 74.665 1.00 38.93  ? 270 TRP   B CD2 1 
ATOM   4631 N  NE1 . TRP   B  1  257 ? 7.754   -21.249 74.901 1.00 43.20  ? 270 TRP   B NE1 1 
ATOM   4632 C  CE2 . TRP   B  1  257 ? 8.381   -22.341 75.435 1.00 39.31  ? 270 TRP   B CE2 1 
ATOM   4633 C  CE3 . TRP   B  1  257 ? 8.512   -24.717 75.014 1.00 43.98  ? 270 TRP   B CE3 1 
ATOM   4634 C  CZ2 . TRP   B  1  257 ? 9.219   -22.440 76.536 1.00 45.01  ? 270 TRP   B CZ2 1 
ATOM   4635 C  CZ3 . TRP   B  1  257 ? 9.338   -24.822 76.107 1.00 43.13  ? 270 TRP   B CZ3 1 
ATOM   4636 C  CH2 . TRP   B  1  257 ? 9.680   -23.697 76.859 1.00 48.80  ? 270 TRP   B CH2 1 
ATOM   4637 N  N   . VAL   B  1  258 ? 4.186   -23.152 74.737 1.00 42.84  ? 271 VAL   B N   1 
ATOM   4638 C  CA  . VAL   B  1  258 ? 3.064   -22.433 75.299 1.00 46.42  ? 271 VAL   B CA  1 
ATOM   4639 C  C   . VAL   B  1  258 ? 3.510   -21.008 75.612 1.00 43.95  ? 271 VAL   B C   1 
ATOM   4640 O  O   . VAL   B  1  258 ? 4.621   -20.790 76.088 1.00 46.05  ? 271 VAL   B O   1 
ATOM   4641 C  CB  . VAL   B  1  258 ? 2.589   -23.218 76.542 1.00 56.74  ? 271 VAL   B CB  1 
ATOM   4642 C  CG1 . VAL   B  1  258 ? 1.685   -22.407 77.458 1.00 62.08  ? 271 VAL   B CG1 1 
ATOM   4643 C  CG2 . VAL   B  1  258 ? 1.889   -24.514 76.145 1.00 58.28  ? 271 VAL   B CG2 1 
ATOM   4644 N  N   . PRO   B  1  259 ? 2.670   -19.987 75.341 1.00 41.24  ? 272 PRO   B N   1 
ATOM   4645 C  CA  . PRO   B  1  259 ? 3.038   -18.608 75.619 1.00 42.18  ? 272 PRO   B CA  1 
ATOM   4646 C  C   . PRO   B  1  259 ? 3.401   -18.474 77.087 1.00 46.36  ? 272 PRO   B C   1 
ATOM   4647 O  O   . PRO   B  1  259 ? 2.894   -19.209 77.923 1.00 46.65  ? 272 PRO   B O   1 
ATOM   4648 C  CB  . PRO   B  1  259 ? 1.810   -17.769 75.252 1.00 40.01  ? 272 PRO   B CB  1 
ATOM   4649 C  CG  . PRO   B  1  259 ? 0.684   -18.783 75.140 1.00 45.08  ? 272 PRO   B CG  1 
ATOM   4650 C  CD  . PRO   B  1  259 ? 1.331   -20.098 74.736 1.00 44.34  ? 272 PRO   B CD  1 
ATOM   4651 N  N   . GLY   B  1  260 ? 4.275   -17.515 77.385 1.00 46.45  ? 273 GLY   B N   1 
ATOM   4652 C  CA  . GLY   B  1  260 ? 4.713   -17.295 78.742 1.00 46.84  ? 273 GLY   B CA  1 
ATOM   4653 C  C   . GLY   B  1  260 ? 5.948   -16.414 78.762 1.00 51.29  ? 273 GLY   B C   1 
ATOM   4654 O  O   . GLY   B  1  260 ? 6.142   -15.617 77.849 1.00 51.45  ? 273 GLY   B O   1 
ATOM   4655 N  N   . GLY   B  1  261 ? 6.755   -16.587 79.815 1.00 48.49  ? 274 GLY   B N   1 
ATOM   4656 C  CA  . GLY   B  1  261 ? 7.930   -15.767 80.036 1.00 49.40  ? 274 GLY   B CA  1 
ATOM   4657 C  C   . GLY   B  1  261 ? 8.691   -16.182 81.295 1.00 53.02  ? 274 GLY   B C   1 
ATOM   4658 O  O   . GLY   B  1  261 ? 8.189   -16.925 82.137 1.00 48.02  ? 274 GLY   B O   1 
ATOM   4659 N  N   . ASN   B  1  262 ? 9.929   -15.696 81.389 1.00 53.28  ? 275 ASN   B N   1 
ATOM   4660 C  CA  . ASN   B  1  262 ? 10.716  -15.801 82.603 1.00 53.40  ? 275 ASN   B CA  1 
ATOM   4661 C  C   . ASN   B  1  262 ? 10.097  -14.884 83.651 1.00 55.54  ? 275 ASN   B C   1 
ATOM   4662 O  O   . ASN   B  1  262 ? 9.982   -13.689 83.413 1.00 53.02  ? 275 ASN   B O   1 
ATOM   4663 C  CB  . ASN   B  1  262 ? 12.175  -15.417 82.362 1.00 49.19  ? 275 ASN   B CB  1 
ATOM   4664 C  CG  . ASN   B  1  262 ? 13.021  -16.575 81.890 1.00 45.52  ? 275 ASN   B CG  1 
ATOM   4665 O  OD1 . ASN   B  1  262 ? 12.658  -17.742 82.090 1.00 44.87  ? 275 ASN   B OD1 1 
ATOM   4666 N  ND2 . ASN   B  1  262 ? 14.149  -16.275 81.263 1.00 47.84  ? 275 ASN   B ND2 1 
ATOM   4667 N  N   . ALA   B  1  263 ? 9.734   -15.448 84.809 1.00 64.24  ? 276 ALA   B N   1 
ATOM   4668 C  CA  . ALA   B  1  263 ? 9.144   -14.671 85.890 1.00 76.72  ? 276 ALA   B CA  1 
ATOM   4669 C  C   . ALA   B  1  263 ? 10.224  -14.176 86.855 1.00 78.08  ? 276 ALA   B C   1 
ATOM   4670 O  O   . ALA   B  1  263 ? 11.256  -14.829 87.035 1.00 65.21  ? 276 ALA   B O   1 
ATOM   4671 C  CB  . ALA   B  1  263 ? 8.098   -15.504 86.609 1.00 80.43  ? 276 ALA   B CB  1 
ATOM   4672 N  N   . ASP   B  1  264 ? 9.953   -13.005 87.455 1.00 83.69  ? 277 ASP   B N   1 
ATOM   4673 C  CA  . ASP   B  1  264 ? 10.669  -12.473 88.611 1.00 96.60  ? 277 ASP   B CA  1 
ATOM   4674 C  C   . ASP   B  1  264 ? 12.132  -12.184 88.275 1.00 95.60  ? 277 ASP   B C   1 
ATOM   4675 O  O   . ASP   B  1  264 ? 13.002  -12.374 89.124 1.00 92.79  ? 277 ASP   B O   1 
ATOM   4676 C  CB  . ASP   B  1  264 ? 10.574  -13.373 89.840 1.00 97.53  ? 277 ASP   B CB  1 
ATOM   4677 C  CG  . ASP   B  1  264 ? 9.168   -13.687 90.342 1.00 100.53 ? 277 ASP   B CG  1 
ATOM   4678 O  OD1 . ASP   B  1  264 ? 8.373   -12.728 90.529 1.00 90.38  ? 277 ASP   B OD1 1 
ATOM   4679 O  OD2 . ASP   B  1  264 ? 8.878   -14.895 90.527 1.00 85.32  ? 277 ASP   B OD2 1 
ATOM   4680 N  N   . ASN   B  1  265 ? 12.389  -11.726 87.041 1.00 83.83  ? 278 ASN   B N   1 
ATOM   4681 C  CA  . ASN   B  1  265 ? 13.700  -11.246 86.634 1.00 72.40  ? 278 ASN   B CA  1 
ATOM   4682 C  C   . ASN   B  1  265 ? 14.761  -12.322 86.892 1.00 63.72  ? 278 ASN   B C   1 
ATOM   4683 O  O   . ASN   B  1  265 ? 15.858  -12.017 87.358 1.00 57.90  ? 278 ASN   B O   1 
ATOM   4684 C  CB  . ASN   B  1  265 ? 13.969  -9.897  87.291 1.00 75.57  ? 278 ASN   B CB  1 
ATOM   4685 C  CG  . ASN   B  1  265 ? 15.221  -9.212  86.805 1.00 82.60  ? 278 ASN   B CG  1 
ATOM   4686 O  OD1 . ASN   B  1  265 ? 16.192  -9.870  86.418 1.00 93.17  ? 278 ASN   B OD1 1 
ATOM   4687 N  ND2 . ASN   B  1  265 ? 15.258  -7.893  86.904 1.00 86.85  ? 278 ASN   B ND2 1 
ATOM   4688 N  N   . GLN   B  1  266 ? 14.441  -13.582 86.564 1.00 60.64  ? 279 GLN   B N   1 
ATOM   4689 C  CA  . GLN   B  1  266 ? 15.389  -14.680 86.682 1.00 66.04  ? 279 GLN   B CA  1 
ATOM   4690 C  C   . GLN   B  1  266 ? 15.390  -15.528 85.407 1.00 64.34  ? 279 GLN   B C   1 
ATOM   4691 O  O   . GLN   B  1  266 ? 14.353  -15.768 84.795 1.00 58.80  ? 279 GLN   B O   1 
ATOM   4692 C  CB  . GLN   B  1  266 ? 15.041  -15.610 87.844 1.00 75.33  ? 279 GLN   B CB  1 
ATOM   4693 C  CG  . GLN   B  1  266 ? 15.311  -15.019 89.222 1.00 89.04  ? 279 GLN   B CG  1 
ATOM   4694 C  CD  . GLN   B  1  266 ? 14.741  -15.847 90.356 1.00 91.18  ? 279 GLN   B CD  1 
ATOM   4695 O  OE1 . GLN   B  1  266 ? 14.411  -17.033 90.221 1.00 82.97  ? 279 GLN   B OE1 1 
ATOM   4696 N  NE2 . GLN   B  1  266 ? 14.621  -15.203 91.505 1.00 97.10  ? 279 GLN   B NE2 1 
ATOM   4697 N  N   . VAL   B  1  267 ? 16.566  -16.044 85.044 1.00 55.83  ? 280 VAL   B N   1 
ATOM   4698 C  CA  . VAL   B  1  267 ? 16.670  -16.964 83.927 1.00 54.99  ? 280 VAL   B CA  1 
ATOM   4699 C  C   . VAL   B  1  267 ? 16.197  -18.346 84.365 1.00 53.56  ? 280 VAL   B C   1 
ATOM   4700 O  O   . VAL   B  1  267 ? 15.977  -18.591 85.539 1.00 60.73  ? 280 VAL   B O   1 
ATOM   4701 C  CB  . VAL   B  1  267 ? 18.097  -16.975 83.349 1.00 57.48  ? 280 VAL   B CB  1 
ATOM   4702 C  CG1 . VAL   B  1  267 ? 18.504  -15.581 82.874 1.00 57.35  ? 280 VAL   B CG1 1 
ATOM   4703 C  CG2 . VAL   B  1  267 ? 19.129  -17.533 84.329 1.00 60.55  ? 280 VAL   B CG2 1 
ATOM   4704 N  N   . ASN   B  1  268 ? 15.991  -19.225 83.389 1.00 57.96  ? 281 ASN   B N   1 
ATOM   4705 C  CA  . ASN   B  1  268 ? 15.570  -20.607 83.593 1.00 63.63  ? 281 ASN   B CA  1 
ATOM   4706 C  C   . ASN   B  1  268 ? 14.336  -20.694 84.487 1.00 61.47  ? 281 ASN   B C   1 
ATOM   4707 O  O   . ASN   B  1  268 ? 14.219  -21.626 85.269 1.00 56.88  ? 281 ASN   B O   1 
ATOM   4708 C  CB  . ASN   B  1  268 ? 16.723  -21.475 84.083 1.00 66.07  ? 281 ASN   B CB  1 
ATOM   4709 C  CG  . ASN   B  1  268 ? 17.773  -21.647 83.009 1.00 69.82  ? 281 ASN   B CG  1 
ATOM   4710 O  OD1 . ASN   B  1  268 ? 17.504  -22.230 81.948 1.00 71.35  ? 281 ASN   B OD1 1 
ATOM   4711 N  ND2 . ASN   B  1  268 ? 18.970  -21.137 83.253 1.00 67.21  ? 281 ASN   B ND2 1 
ATOM   4712 N  N   . ASN   B  1  269 ? 13.382  -19.777 84.283 1.00 65.92  ? 282 ASN   B N   1 
ATOM   4713 C  CA  . ASN   B  1  269 ? 12.223  -19.639 85.153 1.00 66.51  ? 282 ASN   B CA  1 
ATOM   4714 C  C   . ASN   B  1  269 ? 10.972  -19.333 84.317 1.00 57.03  ? 282 ASN   B C   1 
ATOM   4715 O  O   . ASN   B  1  269 ? 10.242  -18.374 84.573 1.00 47.85  ? 282 ASN   B O   1 
ATOM   4716 C  CB  . ASN   B  1  269 ? 12.527  -18.608 86.239 1.00 66.73  ? 282 ASN   B CB  1 
ATOM   4717 C  CG  . ASN   B  1  269 ? 11.489  -18.590 87.342 1.00 61.34  ? 282 ASN   B CG  1 
ATOM   4718 O  OD1 . ASN   B  1  269 ? 10.945  -19.639 87.715 1.00 50.08  ? 282 ASN   B OD1 1 
ATOM   4719 N  ND2 . ASN   B  1  269 ? 11.170  -17.404 87.834 1.00 53.87  ? 282 ASN   B ND2 1 
ATOM   4720 N  N   . TYR   B  1  270 ? 10.707  -20.190 83.330 1.00 60.40  ? 283 TYR   B N   1 
ATOM   4721 C  CA  . TYR   B  1  270 ? 9.659   -19.927 82.357 1.00 61.83  ? 283 TYR   B CA  1 
ATOM   4722 C  C   . TYR   B  1  270 ? 8.310   -20.392 82.904 1.00 61.68  ? 283 TYR   B C   1 
ATOM   4723 O  O   . TYR   B  1  270 ? 8.120   -21.588 83.131 1.00 52.00  ? 283 TYR   B O   1 
ATOM   4724 C  CB  . TYR   B  1  270 ? 9.939   -20.640 81.030 1.00 54.20  ? 283 TYR   B CB  1 
ATOM   4725 C  CG  . TYR   B  1  270 ? 9.034   -20.214 79.879 1.00 50.07  ? 283 TYR   B CG  1 
ATOM   4726 C  CD1 . TYR   B  1  270 ? 9.318   -19.093 79.103 1.00 54.60  ? 283 TYR   B CD1 1 
ATOM   4727 C  CD2 . TYR   B  1  270 ? 7.901   -20.945 79.557 1.00 48.92  ? 283 TYR   B CD2 1 
ATOM   4728 C  CE1 . TYR   B  1  270 ? 8.506   -18.722 78.042 1.00 53.91  ? 283 TYR   B CE1 1 
ATOM   4729 C  CE2 . TYR   B  1  270 ? 7.083   -20.586 78.499 1.00 54.04  ? 283 TYR   B CE2 1 
ATOM   4730 C  CZ  . TYR   B  1  270 ? 7.389   -19.474 77.737 1.00 53.17  ? 283 TYR   B CZ  1 
ATOM   4731 O  OH  . TYR   B  1  270 ? 6.567   -19.142 76.701 1.00 47.17  ? 283 TYR   B OH  1 
ATOM   4732 N  N   . VAL   B  1  271 ? 7.370   -19.439 83.017 1.00 61.25  ? 284 VAL   B N   1 
ATOM   4733 C  CA  . VAL   B  1  271 ? 6.027   -19.683 83.517 1.00 62.28  ? 284 VAL   B CA  1 
ATOM   4734 C  C   . VAL   B  1  271 ? 5.019   -19.398 82.407 1.00 54.20  ? 284 VAL   B C   1 
ATOM   4735 O  O   . VAL   B  1  271 ? 5.029   -18.323 81.818 1.00 51.63  ? 284 VAL   B O   1 
ATOM   4736 C  CB  . VAL   B  1  271 ? 5.742   -18.788 84.741 1.00 69.92  ? 284 VAL   B CB  1 
ATOM   4737 C  CG1 . VAL   B  1  271 ? 4.297   -18.915 85.218 1.00 71.41  ? 284 VAL   B CG1 1 
ATOM   4738 C  CG2 . VAL   B  1  271 ? 6.718   -19.052 85.889 1.00 74.12  ? 284 VAL   B CG2 1 
ATOM   4739 N  N   . GLU   B  1  272 ? 4.090   -20.336 82.216 1.00 53.66  ? 285 GLU   B N   1 
ATOM   4740 C  CA  . GLU   B  1  272 ? 3.024   -20.228 81.233 1.00 53.51  ? 285 GLU   B CA  1 
ATOM   4741 C  C   . GLU   B  1  272 ? 2.065   -19.081 81.578 1.00 56.29  ? 285 GLU   B C   1 
ATOM   4742 O  O   . GLU   B  1  272 ? 1.837   -18.792 82.746 1.00 55.01  ? 285 GLU   B O   1 
ATOM   4743 C  CB  . GLU   B  1  272 ? 2.334   -21.587 81.124 1.00 55.26  ? 285 GLU   B CB  1 
ATOM   4744 C  CG  . GLU   B  1  272 ? 3.320   -22.712 80.802 1.00 62.69  ? 285 GLU   B CG  1 
ATOM   4745 C  CD  . GLU   B  1  272 ? 2.776   -24.131 80.751 1.00 77.35  ? 285 GLU   B CD  1 
ATOM   4746 O  OE1 . GLU   B  1  272 ? 1.575   -24.332 81.039 1.00 89.33  ? 285 GLU   B OE1 1 
ATOM   4747 O  OE2 . GLU   B  1  272 ? 3.561   -25.044 80.402 1.00 71.28  ? 285 GLU   B OE2 1 
ATOM   4748 N  N   . ASP   B  1  273 ? 1.547   -18.399 80.540 1.00 54.99  ? 286 ASP   B N   1 
ATOM   4749 C  CA  . ASP   B  1  273 ? 0.462   -17.433 80.666 1.00 58.13  ? 286 ASP   B CA  1 
ATOM   4750 C  C   . ASP   B  1  273 ? -0.763  -17.991 79.944 1.00 62.54  ? 286 ASP   B C   1 
ATOM   4751 O  O   . ASP   B  1  273 ? -0.822  -17.996 78.719 1.00 62.68  ? 286 ASP   B O   1 
ATOM   4752 C  CB  . ASP   B  1  273 ? 0.822   -16.047 80.147 1.00 57.52  ? 286 ASP   B CB  1 
ATOM   4753 C  CG  . ASP   B  1  273 ? -0.290  -15.001 80.193 1.00 61.21  ? 286 ASP   B CG  1 
ATOM   4754 O  OD1 . ASP   B  1  273 ? -1.369  -15.321 80.730 1.00 64.10  ? 286 ASP   B OD1 1 
ATOM   4755 O  OD2 . ASP   B  1  273 ? -0.071  -13.871 79.694 1.00 60.68  ? 286 ASP   B OD2 1 
ATOM   4756 N  N   . PRO   B  1  274 ? -1.787  -18.493 80.668 1.00 65.56  ? 287 PRO   B N   1 
ATOM   4757 C  CA  . PRO   B  1  274 ? -2.938  -19.114 80.006 1.00 62.22  ? 287 PRO   B CA  1 
ATOM   4758 C  C   . PRO   B  1  274 ? -3.922  -18.120 79.381 1.00 56.71  ? 287 PRO   B C   1 
ATOM   4759 O  O   . PRO   B  1  274 ? -4.785  -18.538 78.614 1.00 55.93  ? 287 PRO   B O   1 
ATOM   4760 C  CB  . PRO   B  1  274 ? -3.556  -19.930 81.169 1.00 73.01  ? 287 PRO   B CB  1 
ATOM   4761 C  CG  . PRO   B  1  274 ? -3.257  -19.092 82.402 1.00 70.57  ? 287 PRO   B CG  1 
ATOM   4762 C  CD  . PRO   B  1  274 ? -1.888  -18.478 82.139 1.00 70.86  ? 287 PRO   B CD  1 
ATOM   4763 N  N   . ASP   B  1  275 ? -3.785  -16.818 79.708 1.00 52.09  ? 288 ASP   B N   1 
ATOM   4764 C  CA  . ASP   B  1  275 ? -4.613  -15.754 79.143 1.00 56.98  ? 288 ASP   B CA  1 
ATOM   4765 C  C   . ASP   B  1  275 ? -4.081  -15.208 77.807 1.00 56.45  ? 288 ASP   B C   1 
ATOM   4766 O  O   . ASP   B  1  275 ? -4.767  -14.432 77.143 1.00 52.62  ? 288 ASP   B O   1 
ATOM   4767 C  CB  . ASP   B  1  275 ? -4.737  -14.581 80.101 1.00 61.33  ? 288 ASP   B CB  1 
ATOM   4768 C  CG  . ASP   B  1  275 ? -5.516  -14.867 81.380 1.00 74.14  ? 288 ASP   B CG  1 
ATOM   4769 O  OD1 . ASP   B  1  275 ? -5.936  -16.030 81.594 1.00 63.11  ? 288 ASP   B OD1 1 
ATOM   4770 O  OD2 . ASP   B  1  275 ? -5.723  -13.906 82.150 1.00 89.66  ? 288 ASP   B OD2 1 
ATOM   4771 N  N   . SER   B  1  276 ? -2.857  -15.585 77.412 1.00 53.41  ? 289 SER   B N   1 
ATOM   4772 C  CA  . SER   B  1  276 ? -2.257  -15.093 76.180 1.00 51.14  ? 289 SER   B CA  1 
ATOM   4773 C  C   . SER   B  1  276 ? -3.005  -15.642 74.967 1.00 45.11  ? 289 SER   B C   1 
ATOM   4774 O  O   . SER   B  1  276 ? -3.550  -16.745 75.006 1.00 45.09  ? 289 SER   B O   1 
ATOM   4775 C  CB  . SER   B  1  276 ? -0.792  -15.452 76.110 1.00 49.56  ? 289 SER   B CB  1 
ATOM   4776 O  OG  . SER   B  1  276 ? -0.306  -15.366 74.778 1.00 46.41  ? 289 SER   B OG  1 
ATOM   4777 N  N   . ALA   B  1  277 ? -3.011  -14.868 73.882 1.00 43.45  ? 290 ALA   B N   1 
ATOM   4778 C  CA  . ALA   B  1  277 ? -3.353  -15.429 72.577 1.00 39.85  ? 290 ALA   B CA  1 
ATOM   4779 C  C   . ALA   B  1  277 ? -2.487  -16.653 72.304 1.00 38.26  ? 290 ALA   B C   1 
ATOM   4780 O  O   . ALA   B  1  277 ? -1.370  -16.768 72.817 1.00 39.22  ? 290 ALA   B O   1 
ATOM   4781 C  CB  . ALA   B  1  277 ? -3.144  -14.409 71.487 1.00 36.18  ? 290 ALA   B CB  1 
ATOM   4782 N  N   . ASP   B  1  278 ? -3.028  -17.560 71.499 1.00 40.11  ? 291 ASP   B N   1 
ATOM   4783 C  CA  . ASP   B  1  278 ? -2.262  -18.653 70.941 1.00 44.01  ? 291 ASP   B CA  1 
ATOM   4784 C  C   . ASP   B  1  278 ? -2.934  -18.990 69.611 1.00 42.52  ? 291 ASP   B C   1 
ATOM   4785 O  O   . ASP   B  1  278 ? -3.792  -18.237 69.175 1.00 40.20  ? 291 ASP   B O   1 
ATOM   4786 C  CB  . ASP   B  1  278 ? -2.105  -19.778 71.954 1.00 46.57  ? 291 ASP   B CB  1 
ATOM   4787 C  CG  . ASP   B  1  278 ? -3.372  -20.557 72.279 1.00 51.65  ? 291 ASP   B CG  1 
ATOM   4788 O  OD1 . ASP   B  1  278 ? -4.339  -20.507 71.474 1.00 46.29  ? 291 ASP   B OD1 1 
ATOM   4789 O  OD2 . ASP   B  1  278 ? -3.392  -21.198 73.341 1.00 53.45  ? 291 ASP   B OD2 1 
ATOM   4790 N  N   . PHE   B  1  279 ? -2.565  -20.115 68.984 1.00 40.92  ? 292 PHE   B N   1 
ATOM   4791 C  CA  . PHE   B  1  279 ? -2.989  -20.376 67.617 1.00 46.23  ? 292 PHE   B CA  1 
ATOM   4792 C  C   . PHE   B  1  279 ? -4.436  -20.864 67.542 1.00 48.85  ? 292 PHE   B C   1 
ATOM   4793 O  O   . PHE   B  1  279 ? -5.019  -20.819 66.462 1.00 50.53  ? 292 PHE   B O   1 
ATOM   4794 C  CB  . PHE   B  1  279 ? -2.008  -21.307 66.895 1.00 46.33  ? 292 PHE   B CB  1 
ATOM   4795 C  CG  . PHE   B  1  279 ? -0.786  -20.515 66.462 1.00 50.13  ? 292 PHE   B CG  1 
ATOM   4796 C  CD1 . PHE   B  1  279 ? -0.842  -19.718 65.324 1.00 54.71  ? 292 PHE   B CD1 1 
ATOM   4797 C  CD2 . PHE   B  1  279 ? 0.373   -20.495 67.234 1.00 50.77  ? 292 PHE   B CD2 1 
ATOM   4798 C  CE1 . PHE   B  1  279 ? 0.248   -18.949 64.942 1.00 55.47  ? 292 PHE   B CE1 1 
ATOM   4799 C  CE2 . PHE   B  1  279 ? 1.457   -19.727 66.848 1.00 54.02  ? 292 PHE   B CE2 1 
ATOM   4800 C  CZ  . PHE   B  1  279 ? 1.392   -18.953 65.707 1.00 52.87  ? 292 PHE   B CZ  1 
ATOM   4801 N  N   . THR   B  1  280 ? -5.037  -21.290 68.662 1.00 50.59  ? 293 THR   B N   1 
ATOM   4802 C  CA  . THR   B  1  280 ? -6.460  -21.620 68.651 1.00 53.97  ? 293 THR   B CA  1 
ATOM   4803 C  C   . THR   B  1  280 ? -7.292  -20.511 69.312 1.00 54.11  ? 293 THR   B C   1 
ATOM   4804 O  O   . THR   B  1  280 ? -8.500  -20.675 69.461 1.00 53.49  ? 293 THR   B O   1 
ATOM   4805 C  CB  . THR   B  1  280 ? -6.682  -22.987 69.304 1.00 54.77  ? 293 THR   B CB  1 
ATOM   4806 O  OG1 . THR   B  1  280 ? -6.189  -22.916 70.642 1.00 51.48  ? 293 THR   B OG1 1 
ATOM   4807 C  CG2 . THR   B  1  280 ? -5.977  -24.101 68.547 1.00 55.72  ? 293 THR   B CG2 1 
ATOM   4808 N  N   . HIS   B  1  281 ? -6.656  -19.384 69.680 1.00 47.15  ? 294 HIS   B N   1 
ATOM   4809 C  CA  . HIS   B  1  281 ? -7.328  -18.262 70.322 1.00 52.10  ? 294 HIS   B CA  1 
ATOM   4810 C  C   . HIS   B  1  281 ? -6.775  -16.957 69.749 1.00 47.36  ? 294 HIS   B C   1 
ATOM   4811 O  O   . HIS   B  1  281 ? -6.324  -16.095 70.496 1.00 48.25  ? 294 HIS   B O   1 
ATOM   4812 C  CB  . HIS   B  1  281 ? -7.152  -18.292 71.854 1.00 54.47  ? 294 HIS   B CB  1 
ATOM   4813 C  CG  . HIS   B  1  281 ? -7.657  -19.521 72.548 1.00 61.38  ? 294 HIS   B CG  1 
ATOM   4814 N  ND1 . HIS   B  1  281 ? -6.905  -20.674 72.658 1.00 65.67  ? 294 HIS   B ND1 1 
ATOM   4815 C  CD2 . HIS   B  1  281 ? -8.826  -19.777 73.164 1.00 59.17  ? 294 HIS   B CD2 1 
ATOM   4816 C  CE1 . HIS   B  1  281 ? -7.601  -21.589 73.320 1.00 71.33  ? 294 HIS   B CE1 1 
ATOM   4817 N  NE2 . HIS   B  1  281 ? -8.766  -21.058 73.646 1.00 69.27  ? 294 HIS   B NE2 1 
ATOM   4818 N  N   . LEU   B  1  282 ? -6.855  -16.803 68.423 1.00 42.43  ? 295 LEU   B N   1 
ATOM   4819 C  CA  . LEU   B  1  282 ? -6.216  -15.691 67.739 1.00 42.67  ? 295 LEU   B CA  1 
ATOM   4820 C  C   . LEU   B  1  282 ? -6.864  -14.362 68.099 1.00 42.91  ? 295 LEU   B C   1 
ATOM   4821 O  O   . LEU   B  1  282 ? -6.182  -13.326 68.133 1.00 40.84  ? 295 LEU   B O   1 
ATOM   4822 C  CB  . LEU   B  1  282 ? -6.224  -15.902 66.225 1.00 44.12  ? 295 LEU   B CB  1 
ATOM   4823 C  CG  . LEU   B  1  282 ? -5.201  -16.920 65.714 1.00 49.13  ? 295 LEU   B CG  1 
ATOM   4824 C  CD1 . LEU   B  1  282 ? -5.389  -17.137 64.212 1.00 48.61  ? 295 LEU   B CD1 1 
ATOM   4825 C  CD2 . LEU   B  1  282 ? -3.786  -16.429 66.023 1.00 48.43  ? 295 LEU   B CD2 1 
ATOM   4826 N  N   . CYS   B  1  283 ? -8.172  -14.388 68.386 1.00 43.21  ? 296 CYS   B N   1 
ATOM   4827 C  CA  . CYS   B  1  283 ? -8.894  -13.148 68.619 1.00 48.72  ? 296 CYS   B CA  1 
ATOM   4828 C  C   . CYS   B  1  283 ? -8.391  -12.459 69.884 1.00 42.52  ? 296 CYS   B C   1 
ATOM   4829 O  O   . CYS   B  1  283 ? -8.537  -11.258 70.027 1.00 43.56  ? 296 CYS   B O   1 
ATOM   4830 C  CB  . CYS   B  1  283 ? -10.408 -13.362 68.604 1.00 58.66  ? 296 CYS   B CB  1 
ATOM   4831 S  SG  . CYS   B  1  283 ? -11.080 -13.660 66.938 1.00 70.27  ? 296 CYS   B SG  1 
ATOM   4832 N  N   . ARG   B  1  284 ? -7.769  -13.196 70.798 1.00 44.20  ? 297 ARG   B N   1 
ATOM   4833 C  CA  . ARG   B  1  284 ? -7.226  -12.568 71.992 1.00 46.37  ? 297 ARG   B CA  1 
ATOM   4834 C  C   . ARG   B  1  284 ? -6.129  -11.581 71.624 1.00 45.59  ? 297 ARG   B C   1 
ATOM   4835 O  O   . ARG   B  1  284 ? -5.954  -10.573 72.311 1.00 42.35  ? 297 ARG   B O   1 
ATOM   4836 C  CB  . ARG   B  1  284 ? -6.618  -13.587 72.946 1.00 48.90  ? 297 ARG   B CB  1 
ATOM   4837 C  CG  . ARG   B  1  284 ? -7.638  -14.532 73.557 1.00 51.51  ? 297 ARG   B CG  1 
ATOM   4838 C  CD  . ARG   B  1  284 ? -6.953  -15.395 74.592 1.00 58.73  ? 297 ARG   B CD  1 
ATOM   4839 N  NE  . ARG   B  1  284 ? -7.863  -16.406 75.143 1.00 64.69  ? 297 ARG   B NE  1 
ATOM   4840 C  CZ  . ARG   B  1  284 ? -7.489  -17.422 75.913 1.00 67.96  ? 297 ARG   B CZ  1 
ATOM   4841 N  NH1 . ARG   B  1  284 ? -6.213  -17.597 76.230 1.00 61.36  ? 297 ARG   B NH1 1 
ATOM   4842 N  NH2 . ARG   B  1  284 ? -8.404  -18.275 76.341 1.00 68.50  ? 297 ARG   B NH2 1 
ATOM   4843 N  N   . LEU   B  1  285 ? -5.400  -11.881 70.540 1.00 43.34  ? 298 LEU   B N   1 
ATOM   4844 C  CA  . LEU   B  1  285 ? -4.368  -10.971 70.077 1.00 40.99  ? 298 LEU   B CA  1 
ATOM   4845 C  C   . LEU   B  1  285 ? -5.029  -9.655  69.673 1.00 35.51  ? 298 LEU   B C   1 
ATOM   4846 O  O   . LEU   B  1  285 ? -4.555  -8.585  70.067 1.00 36.11  ? 298 LEU   B O   1 
ATOM   4847 C  CB  . LEU   B  1  285 ? -3.541  -11.605 68.960 1.00 42.47  ? 298 LEU   B CB  1 
ATOM   4848 C  CG  . LEU   B  1  285 ? -2.357  -10.780 68.440 1.00 44.99  ? 298 LEU   B CG  1 
ATOM   4849 C  CD1 . LEU   B  1  285 ? -1.405  -11.689 67.712 1.00 53.09  ? 298 LEU   B CD1 1 
ATOM   4850 C  CD2 . LEU   B  1  285 ? -2.777  -9.665  67.487 1.00 48.52  ? 298 LEU   B CD2 1 
ATOM   4851 N  N   . TYR   B  1  286 ? -6.151  -9.741  68.945 1.00 37.74  ? 299 TYR   B N   1 
ATOM   4852 C  CA  . TYR   B  1  286 ? -6.888  -8.556  68.519 1.00 37.77  ? 299 TYR   B CA  1 
ATOM   4853 C  C   . TYR   B  1  286 ? -7.331  -7.733  69.734 1.00 37.70  ? 299 TYR   B C   1 
ATOM   4854 O  O   . TYR   B  1  286 ? -7.084  -6.527  69.799 1.00 37.47  ? 299 TYR   B O   1 
ATOM   4855 C  CB  . TYR   B  1  286 ? -8.056  -8.964  67.616 1.00 37.61  ? 299 TYR   B CB  1 
ATOM   4856 C  CG  . TYR   B  1  286 ? -8.984  -7.811  67.282 1.00 38.30  ? 299 TYR   B CG  1 
ATOM   4857 C  CD1 . TYR   B  1  286 ? -8.545  -6.729  66.531 1.00 37.77  ? 299 TYR   B CD1 1 
ATOM   4858 C  CD2 . TYR   B  1  286 ? -10.296 -7.800  67.733 1.00 40.83  ? 299 TYR   B CD2 1 
ATOM   4859 C  CE1 . TYR   B  1  286 ? -9.375  -5.659  66.243 1.00 40.24  ? 299 TYR   B CE1 1 
ATOM   4860 C  CE2 . TYR   B  1  286 ? -11.152 -6.755  67.415 1.00 40.38  ? 299 TYR   B CE2 1 
ATOM   4861 C  CZ  . TYR   B  1  286 ? -10.684 -5.675  66.698 1.00 40.55  ? 299 TYR   B CZ  1 
ATOM   4862 O  OH  . TYR   B  1  286 ? -11.520 -4.654  66.424 1.00 37.38  ? 299 TYR   B OH  1 
ATOM   4863 N  N   . GLU   B  1  287 ? -7.937  -8.394  70.715 1.00 39.54  ? 300 GLU   B N   1 
ATOM   4864 C  CA  . GLU   B  1  287 ? -8.438  -7.717  71.908 1.00 44.03  ? 300 GLU   B CA  1 
ATOM   4865 C  C   . GLU   B  1  287 ? -7.269  -7.123  72.691 1.00 42.98  ? 300 GLU   B C   1 
ATOM   4866 O  O   . GLU   B  1  287 ? -7.344  -5.980  73.142 1.00 41.88  ? 300 GLU   B O   1 
ATOM   4867 C  CB  . GLU   B  1  287 ? -9.250  -8.651  72.810 1.00 46.13  ? 300 GLU   B CB  1 
ATOM   4868 C  CG  . GLU   B  1  287 ? -10.551 -9.159  72.194 1.00 62.14  ? 300 GLU   B CG  1 
ATOM   4869 C  CD  . GLU   B  1  287 ? -11.103 -10.488 72.730 1.00 82.52  ? 300 GLU   B CD  1 
ATOM   4870 O  OE1 . GLU   B  1  287 ? -10.418 -11.276 73.445 1.00 77.42  ? 300 GLU   B OE1 1 
ATOM   4871 O  OE2 . GLU   B  1  287 ? -12.275 -10.751 72.379 1.00 91.48  ? 300 GLU   B OE2 1 
ATOM   4872 N  N   . PHE   B  1  288 ? -6.181  -7.891  72.845 1.00 40.10  ? 301 PHE   B N   1 
ATOM   4873 C  CA  . PHE   B  1  288 ? -5.020  -7.422  73.590 1.00 41.57  ? 301 PHE   B CA  1 
ATOM   4874 C  C   . PHE   B  1  288 ? -4.510  -6.107  72.995 1.00 38.20  ? 301 PHE   B C   1 
ATOM   4875 O  O   . PHE   B  1  288 ? -4.222  -5.151  73.714 1.00 37.70  ? 301 PHE   B O   1 
ATOM   4876 C  CB  . PHE   B  1  288 ? -3.941  -8.511  73.580 1.00 45.87  ? 301 PHE   B CB  1 
ATOM   4877 C  CG  . PHE   B  1  288 ? -2.730  -8.107  74.397 1.00 46.55  ? 301 PHE   B CG  1 
ATOM   4878 C  CD1 . PHE   B  1  288 ? -2.705  -8.334  75.764 1.00 49.89  ? 301 PHE   B CD1 1 
ATOM   4879 C  CD2 . PHE   B  1  288 ? -1.661  -7.444  73.808 1.00 46.07  ? 301 PHE   B CD2 1 
ATOM   4880 C  CE1 . PHE   B  1  288 ? -1.616  -7.928  76.525 1.00 58.28  ? 301 PHE   B CE1 1 
ATOM   4881 C  CE2 . PHE   B  1  288 ? -0.579  -7.031  74.572 1.00 50.79  ? 301 PHE   B CE2 1 
ATOM   4882 C  CZ  . PHE   B  1  288 ? -0.552  -7.274  75.927 1.00 51.94  ? 301 PHE   B CZ  1 
ATOM   4883 N  N   . VAL   B  1  289 ? -4.431  -6.062  71.661 1.00 36.62  ? 302 VAL   B N   1 
ATOM   4884 C  CA  . VAL   B  1  289 ? -3.838  -4.930  70.981 1.00 38.83  ? 302 VAL   B CA  1 
ATOM   4885 C  C   . VAL   B  1  289 ? -4.749  -3.720  71.093 1.00 36.40  ? 302 VAL   B C   1 
ATOM   4886 O  O   . VAL   B  1  289 ? -4.254  -2.613  71.241 1.00 37.65  ? 302 VAL   B O   1 
ATOM   4887 C  CB  . VAL   B  1  289 ? -3.501  -5.242  69.510 1.00 38.78  ? 302 VAL   B CB  1 
ATOM   4888 C  CG1 . VAL   B  1  289 ? -3.137  -3.984  68.732 1.00 37.28  ? 302 VAL   B CG1 1 
ATOM   4889 C  CG2 . VAL   B  1  289 ? -2.377  -6.261  69.412 1.00 41.95  ? 302 VAL   B CG2 1 
ATOM   4890 N  N   . VAL   B  1  290 ? -6.061  -3.919  70.981 1.00 37.90  ? 303 VAL   B N   1 
ATOM   4891 C  CA  . VAL   B  1  290 ? -6.993  -2.804  71.111 1.00 40.35  ? 303 VAL   B CA  1 
ATOM   4892 C  C   . VAL   B  1  290 ? -6.825  -2.193  72.500 1.00 36.65  ? 303 VAL   B C   1 
ATOM   4893 O  O   . VAL   B  1  290 ? -6.739  -0.971  72.647 1.00 36.39  ? 303 VAL   B O   1 
ATOM   4894 C  CB  . VAL   B  1  290 ? -8.445  -3.241  70.841 1.00 43.72  ? 303 VAL   B CB  1 
ATOM   4895 C  CG1 . VAL   B  1  290 ? -9.446  -2.183  71.273 1.00 43.29  ? 303 VAL   B CG1 1 
ATOM   4896 C  CG2 . VAL   B  1  290 ? -8.654  -3.645  69.378 1.00 42.62  ? 303 VAL   B CG2 1 
ATOM   4897 N  N   . GLY   B  1  291 ? -6.674  -3.065  73.500 1.00 36.42  ? 304 GLY   B N   1 
ATOM   4898 C  CA  . GLY   B  1  291 ? -6.362  -2.634  74.855 1.00 44.78  ? 304 GLY   B CA  1 
ATOM   4899 C  C   . GLY   B  1  291 ? -5.071  -1.810  74.907 1.00 46.26  ? 304 GLY   B C   1 
ATOM   4900 O  O   . GLY   B  1  291 ? -5.050  -0.730  75.494 1.00 45.22  ? 304 GLY   B O   1 
ATOM   4901 N  N   . SER   B  1  292 ? -4.019  -2.305  74.241 1.00 40.91  ? 305 SER   B N   1 
ATOM   4902 C  CA  . SER   B  1  292 ? -2.745  -1.616  74.264 1.00 37.79  ? 305 SER   B CA  1 
ATOM   4903 C  C   . SER   B  1  292 ? -2.879  -0.240  73.623 1.00 35.63  ? 305 SER   B C   1 
ATOM   4904 O  O   . SER   B  1  292 ? -2.253  0.714   74.082 1.00 39.25  ? 305 SER   B O   1 
ATOM   4905 C  CB  . SER   B  1  292 ? -1.664  -2.416  73.581 1.00 38.18  ? 305 SER   B CB  1 
ATOM   4906 O  OG  . SER   B  1  292 ? -1.602  -3.722  74.116 1.00 44.52  ? 305 SER   B OG  1 
ATOM   4907 N  N   . VAL   B  1  293 ? -3.681  -0.141  72.561 1.00 33.85  ? 306 VAL   B N   1 
ATOM   4908 C  CA  . VAL   B  1  293 ? -3.861  1.131   71.880 1.00 38.32  ? 306 VAL   B CA  1 
ATOM   4909 C  C   . VAL   B  1  293 ? -4.511  2.146   72.823 1.00 43.28  ? 306 VAL   B C   1 
ATOM   4910 O  O   . VAL   B  1  293 ? -4.159  3.330   72.827 1.00 39.73  ? 306 VAL   B O   1 
ATOM   4911 C  CB  . VAL   B  1  293 ? -4.706  0.971   70.604 1.00 34.85  ? 306 VAL   B CB  1 
ATOM   4912 C  CG1 . VAL   B  1  293 ? -5.100  2.316   70.019 1.00 34.84  ? 306 VAL   B CG1 1 
ATOM   4913 C  CG2 . VAL   B  1  293 ? -4.010  0.123   69.557 1.00 38.95  ? 306 VAL   B CG2 1 
ATOM   4914 N  N   . GLN   B  1  294 ? -5.486  1.674   73.610 1.00 45.67  ? 307 GLN   B N   1 
ATOM   4915 C  CA  . GLN   B  1  294 ? -6.185  2.554   74.531 1.00 47.89  ? 307 GLN   B CA  1 
ATOM   4916 C  C   . GLN   B  1  294 ? -5.233  3.042   75.616 1.00 44.34  ? 307 GLN   B C   1 
ATOM   4917 O  O   . GLN   B  1  294 ? -5.338  4.188   76.023 1.00 52.28  ? 307 GLN   B O   1 
ATOM   4918 C  CB  . GLN   B  1  294 ? -7.396  1.898   75.176 1.00 44.49  ? 307 GLN   B CB  1 
ATOM   4919 C  CG  . GLN   B  1  294 ? -8.444  1.470   74.168 1.00 45.53  ? 307 GLN   B CG  1 
ATOM   4920 C  CD  . GLN   B  1  294 ? -9.558  0.721   74.845 1.00 53.35  ? 307 GLN   B CD  1 
ATOM   4921 O  OE1 . GLN   B  1  294 ? -9.553  -0.511  74.950 1.00 57.19  ? 307 GLN   B OE1 1 
ATOM   4922 N  NE2 . GLN   B  1  294 ? -10.493 1.508   75.336 1.00 56.29  ? 307 GLN   B NE2 1 
ATOM   4923 N  N   . GLU   B  1  295 ? -4.301  2.194   76.063 1.00 44.10  ? 308 GLU   B N   1 
ATOM   4924 C  CA  . GLU   B  1  295 ? -3.283  2.621   77.021 1.00 48.83  ? 308 GLU   B CA  1 
ATOM   4925 C  C   . GLU   B  1  295 ? -2.394  3.698   76.404 1.00 48.98  ? 308 GLU   B C   1 
ATOM   4926 O  O   . GLU   B  1  295 ? -2.010  4.610   77.114 1.00 51.96  ? 308 GLU   B O   1 
ATOM   4927 C  CB  . GLU   B  1  295 ? -2.441  1.474   77.572 1.00 56.17  ? 308 GLU   B CB  1 
ATOM   4928 C  CG  . GLU   B  1  295 ? -3.259  0.518   78.443 1.00 68.24  ? 308 GLU   B CG  1 
ATOM   4929 C  CD  . GLU   B  1  295 ? -2.610  -0.804  78.844 1.00 77.78  ? 308 GLU   B CD  1 
ATOM   4930 O  OE1 . GLU   B  1  295 ? -1.388  -0.974  78.675 1.00 92.89  ? 308 GLU   B OE1 1 
ATOM   4931 O  OE2 . GLU   B  1  295 ? -3.358  -1.696  79.286 1.00 81.48  ? 308 GLU   B OE2 1 
ATOM   4932 N  N   . LEU   B  1  296 ? -2.100  3.624   75.093 1.00 48.63  ? 309 LEU   B N   1 
ATOM   4933 C  CA  . LEU   B  1  296 ? -1.270  4.633   74.437 1.00 48.06  ? 309 LEU   B CA  1 
ATOM   4934 C  C   . LEU   B  1  296 ? -2.057  5.923   74.243 1.00 44.10  ? 309 LEU   B C   1 
ATOM   4935 O  O   . LEU   B  1  296 ? -1.471  7.007   74.279 1.00 41.95  ? 309 LEU   B O   1 
ATOM   4936 C  CB  . LEU   B  1  296 ? -0.715  4.185   73.081 1.00 49.84  ? 309 LEU   B CB  1 
ATOM   4937 C  CG  . LEU   B  1  296 ? 0.283   3.028   73.086 1.00 54.85  ? 309 LEU   B CG  1 
ATOM   4938 C  CD1 . LEU   B  1  296 ? 0.508   2.593   71.646 1.00 54.61  ? 309 LEU   B CD1 1 
ATOM   4939 C  CD2 . LEU   B  1  296 ? 1.601   3.387   73.750 1.00 52.19  ? 309 LEU   B CD2 1 
ATOM   4940 N  N   . TYR   B  1  297 ? -3.357  5.781   73.947 1.00 39.98  ? 310 TYR   B N   1 
ATOM   4941 C  CA  . TYR   B  1  297 ? -4.199  6.908   73.582 1.00 50.62  ? 310 TYR   B CA  1 
ATOM   4942 C  C   . TYR   B  1  297 ? -5.466  6.915   74.453 1.00 55.91  ? 310 TYR   B C   1 
ATOM   4943 O  O   . TYR   B  1  297 ? -6.546  6.532   73.997 1.00 48.26  ? 310 TYR   B O   1 
ATOM   4944 C  CB  . TYR   B  1  297 ? -4.554  6.814   72.101 1.00 52.74  ? 310 TYR   B CB  1 
ATOM   4945 C  CG  . TYR   B  1  297 ? -3.371  6.960   71.165 1.00 56.64  ? 310 TYR   B CG  1 
ATOM   4946 C  CD1 . TYR   B  1  297 ? -2.858  8.211   70.856 1.00 49.89  ? 310 TYR   B CD1 1 
ATOM   4947 C  CD2 . TYR   B  1  297 ? -2.789  5.842   70.574 1.00 56.03  ? 310 TYR   B CD2 1 
ATOM   4948 C  CE1 . TYR   B  1  297 ? -1.785  8.345   69.990 1.00 52.80  ? 310 TYR   B CE1 1 
ATOM   4949 C  CE2 . TYR   B  1  297 ? -1.721  5.969   69.696 1.00 57.40  ? 310 TYR   B CE2 1 
ATOM   4950 C  CZ  . TYR   B  1  297 ? -1.217  7.224   69.406 1.00 56.52  ? 310 TYR   B CZ  1 
ATOM   4951 O  OH  . TYR   B  1  297 ? -0.162  7.362   68.555 1.00 55.07  ? 310 TYR   B OH  1 
ATOM   4952 N  N   . PRO   B  1  298 ? -5.364  7.295   75.747 1.00 52.00  ? 311 PRO   B N   1 
ATOM   4953 C  CA  . PRO   B  1  298 ? -6.501  7.182   76.666 1.00 58.49  ? 311 PRO   B CA  1 
ATOM   4954 C  C   . PRO   B  1  298 ? -7.656  8.138   76.385 1.00 59.42  ? 311 PRO   B C   1 
ATOM   4955 O  O   . PRO   B  1  298 ? -8.805  7.759   76.594 1.00 65.66  ? 311 PRO   B O   1 
ATOM   4956 C  CB  . PRO   B  1  298 ? -5.926  7.395   78.076 1.00 59.00  ? 311 PRO   B CB  1 
ATOM   4957 C  CG  . PRO   B  1  298 ? -4.537  7.981   77.856 1.00 60.24  ? 311 PRO   B CG  1 
ATOM   4958 C  CD  . PRO   B  1  298 ? -4.144  7.799   76.393 1.00 59.88  ? 311 PRO   B CD  1 
ATOM   4959 N  N   . ASN   B  1  299 ? -7.363  9.340   75.858 1.00 63.91  ? 312 ASN   B N   1 
ATOM   4960 C  CA  . ASN   B  1  299 ? -8.394  10.346  75.627 1.00 67.33  ? 312 ASN   B CA  1 
ATOM   4961 C  C   . ASN   B  1  299 ? -8.023  11.239  74.449 1.00 63.96  ? 312 ASN   B C   1 
ATOM   4962 O  O   . ASN   B  1  299 ? -7.859  12.454  74.594 1.00 66.46  ? 312 ASN   B O   1 
ATOM   4963 C  CB  . ASN   B  1  299 ? -8.627  11.259  76.830 1.00 73.96  ? 312 ASN   B CB  1 
ATOM   4964 C  CG  . ASN   B  1  299 ? -9.428  10.622  77.934 1.00 80.57  ? 312 ASN   B CG  1 
ATOM   4965 O  OD1 . ASN   B  1  299 ? -8.985  10.625  79.090 1.00 86.36  ? 312 ASN   B OD1 1 
ATOM   4966 N  ND2 . ASN   B  1  299 ? -10.600 10.090  77.606 1.00 76.66  ? 312 ASN   B ND2 1 
ATOM   4967 N  N   . PRO   B  1  300 ? -7.954  10.686  73.218 1.00 57.56  ? 313 PRO   B N   1 
ATOM   4968 C  CA  . PRO   B  1  300 ? -7.641  11.510  72.057 1.00 51.78  ? 313 PRO   B CA  1 
ATOM   4969 C  C   . PRO   B  1  300 ? -8.805  12.391  71.625 1.00 55.03  ? 313 PRO   B C   1 
ATOM   4970 O  O   . PRO   B  1  300 ? -9.961  12.017  71.835 1.00 56.01  ? 313 PRO   B O   1 
ATOM   4971 C  CB  . PRO   B  1  300 ? -7.347  10.395  71.048 1.00 55.58  ? 313 PRO   B CB  1 
ATOM   4972 C  CG  . PRO   B  1  300 ? -8.337  9.288   71.395 1.00 50.21  ? 313 PRO   B CG  1 
ATOM   4973 C  CD  . PRO   B  1  300 ? -8.206  9.268   72.890 1.00 52.95  ? 313 PRO   B CD  1 
ATOM   4974 N  N   . THR   B  1  301 ? -8.482  13.498  70.945 1.00 58.80  ? 314 THR   B N   1 
ATOM   4975 C  CA  . THR   B  1  301 ? -9.483  14.356  70.323 1.00 67.91  ? 314 THR   B CA  1 
ATOM   4976 C  C   . THR   B  1  301 ? -9.034  14.726  68.912 1.00 66.06  ? 314 THR   B C   1 
ATOM   4977 O  O   . THR   B  1  301 ? -7.902  14.466  68.541 1.00 64.52  ? 314 THR   B O   1 
ATOM   4978 C  CB  . THR   B  1  301 ? -9.710  15.619  71.168 1.00 73.49  ? 314 THR   B CB  1 
ATOM   4979 O  OG1 . THR   B  1  301 ? -8.485  16.343  71.315 1.00 65.57  ? 314 THR   B OG1 1 
ATOM   4980 C  CG2 . THR   B  1  301 ? -10.275 15.306  72.542 1.00 72.17  ? 314 THR   B CG2 1 
ATOM   4981 N  N   . GLY   B  1  302 ? -9.925  15.372  68.157 1.00 68.20  ? 315 GLY   B N   1 
ATOM   4982 C  CA  . GLY   B  1  302 ? -9.580  15.953  66.871 1.00 72.03  ? 315 GLY   B CA  1 
ATOM   4983 C  C   . GLY   B  1  302 ? -9.172  14.895  65.846 1.00 70.70  ? 315 GLY   B C   1 
ATOM   4984 O  O   . GLY   B  1  302 ? -9.730  13.792  65.816 1.00 61.96  ? 315 GLY   B O   1 
ATOM   4985 N  N   . ILE   B  1  303 ? -8.180  15.254  65.016 1.00 72.15  ? 316 ILE   B N   1 
ATOM   4986 C  CA  . ILE   B  1  303 ? -7.766  14.417  63.898 1.00 70.53  ? 316 ILE   B CA  1 
ATOM   4987 C  C   . ILE   B  1  303 ? -7.164  13.112  64.432 1.00 51.68  ? 316 ILE   B C   1 
ATOM   4988 O  O   . ILE   B  1  303 ? -7.385  12.052  63.874 1.00 52.87  ? 316 ILE   B O   1 
ATOM   4989 C  CB  . ILE   B  1  303 ? -6.819  15.163  62.940 1.00 79.03  ? 316 ILE   B CB  1 
ATOM   4990 C  CG1 . ILE   B  1  303 ? -7.382  16.545  62.527 1.00 105.29 ? 316 ILE   B CG1 1 
ATOM   4991 C  CG2 . ILE   B  1  303 ? -6.564  14.294  61.717 1.00 74.14  ? 316 ILE   B CG2 1 
ATOM   4992 C  CD1 . ILE   B  1  303 ? -6.483  17.381  61.623 1.00 108.67 ? 316 ILE   B CD1 1 
ATOM   4993 N  N   . LEU   B  1  304 ? -6.435  13.171  65.540 1.00 43.49  ? 317 LEU   B N   1 
ATOM   4994 C  CA  . LEU   B  1  304 ? -5.876  11.976  66.151 1.00 46.51  ? 317 LEU   B CA  1 
ATOM   4995 C  C   . LEU   B  1  304 ? -6.980  10.971  66.502 1.00 54.18  ? 317 LEU   B C   1 
ATOM   4996 O  O   . LEU   B  1  304 ? -6.853  9.791   66.205 1.00 52.95  ? 317 LEU   B O   1 
ATOM   4997 C  CB  . LEU   B  1  304 ? -5.049  12.382  67.369 1.00 48.57  ? 317 LEU   B CB  1 
ATOM   4998 C  CG  . LEU   B  1  304 ? -4.542  11.242  68.259 1.00 53.18  ? 317 LEU   B CG  1 
ATOM   4999 C  CD1 . LEU   B  1  304 ? -3.666  10.298  67.452 1.00 56.64  ? 317 LEU   B CD1 1 
ATOM   5000 C  CD2 . LEU   B  1  304 ? -3.799  11.815  69.438 1.00 55.10  ? 317 LEU   B CD2 1 
ATOM   5001 N  N   . ARG   B  1  305 ? -8.074  11.431  67.115 1.00 57.17  ? 318 ARG   B N   1 
ATOM   5002 C  CA  . ARG   B  1  305 ? -9.173  10.549  67.467 1.00 59.52  ? 318 ARG   B CA  1 
ATOM   5003 C  C   . ARG   B  1  305 ? -9.743  9.935   66.192 1.00 48.15  ? 318 ARG   B C   1 
ATOM   5004 O  O   . ARG   B  1  305 ? -10.016 8.725   66.126 1.00 53.92  ? 318 ARG   B O   1 
ATOM   5005 C  CB  . ARG   B  1  305 ? -10.267 11.276  68.275 1.00 67.36  ? 318 ARG   B CB  1 
ATOM   5006 C  CG  . ARG   B  1  305 ? -11.506 10.411  68.537 1.00 64.13  ? 318 ARG   B CG  1 
ATOM   5007 C  CD  . ARG   B  1  305 ? -12.710 10.982  69.289 1.00 63.49  ? 318 ARG   B CD  1 
ATOM   5008 N  NE  . ARG   B  1  305 ? -12.451 10.783  70.718 1.00 58.91  ? 318 ARG   B NE  1 
ATOM   5009 C  CZ  . ARG   B  1  305 ? -12.963 9.849   71.520 1.00 52.74  ? 318 ARG   B CZ  1 
ATOM   5010 N  NH1 . ARG   B  1  305 ? -12.379 9.599   72.682 1.00 52.13  ? 318 ARG   B NH1 1 
ATOM   5011 N  NH2 . ARG   B  1  305 ? -13.988 9.106   71.153 1.00 53.42  ? 318 ARG   B NH2 1 
ATOM   5012 N  N   . ARG   B  1  306 ? -9.966  10.795  65.199 1.00 44.87  ? 319 ARG   B N   1 
ATOM   5013 C  CA  . ARG   B  1  306 ? -10.592 10.355  63.963 1.00 51.79  ? 319 ARG   B CA  1 
ATOM   5014 C  C   . ARG   B  1  306 ? -9.705  9.311   63.278 1.00 47.43  ? 319 ARG   B C   1 
ATOM   5015 O  O   . ARG   B  1  306 ? -10.198 8.303   62.783 1.00 47.18  ? 319 ARG   B O   1 
ATOM   5016 C  CB  . ARG   B  1  306 ? -10.854 11.593  63.101 1.00 62.29  ? 319 ARG   B CB  1 
ATOM   5017 C  CG  . ARG   B  1  306 ? -11.684 11.358  61.847 1.00 83.26  ? 319 ARG   B CG  1 
ATOM   5018 C  CD  . ARG   B  1  306 ? -11.695 12.611  60.946 1.00 99.91  ? 319 ARG   B CD  1 
ATOM   5019 N  NE  . ARG   B  1  306 ? -10.441 12.749  60.188 1.00 120.88 ? 319 ARG   B NE  1 
ATOM   5020 C  CZ  . ARG   B  1  306 ? -10.047 13.800  59.469 1.00 129.18 ? 319 ARG   B CZ  1 
ATOM   5021 N  NH1 . ARG   B  1  306 ? -10.866 14.814  59.262 1.00 126.79 ? 319 ARG   B NH1 1 
ATOM   5022 N  NH2 . ARG   B  1  306 ? -8.855  13.797  58.889 1.00 130.25 ? 319 ARG   B NH2 1 
ATOM   5023 N  N   . ASN   B  1  307 ? -8.390  9.548   63.273 1.00 45.60  ? 320 ASN   B N   1 
ATOM   5024 C  CA  . ASN   B  1  307 ? -7.458  8.667   62.585 1.00 52.08  ? 320 ASN   B CA  1 
ATOM   5025 C  C   . ASN   B  1  307 ? -7.309  7.359   63.342 1.00 48.62  ? 320 ASN   B C   1 
ATOM   5026 O  O   . ASN   B  1  307 ? -7.149  6.324   62.702 1.00 45.48  ? 320 ASN   B O   1 
ATOM   5027 C  CB  . ASN   B  1  307 ? -6.123  9.346   62.303 1.00 48.24  ? 320 ASN   B CB  1 
ATOM   5028 C  CG  . ASN   B  1  307 ? -6.278  10.350  61.187 1.00 53.91  ? 320 ASN   B CG  1 
ATOM   5029 O  OD1 . ASN   B  1  307 ? -7.393  10.540  60.686 1.00 60.34  ? 320 ASN   B OD1 1 
ATOM   5030 N  ND2 . ASN   B  1  307 ? -5.188  10.999  60.790 1.00 57.97  ? 320 ASN   B ND2 1 
ATOM   5031 N  N   . LEU   B  1  308 ? -7.409  7.403   64.675 1.00 45.32  ? 321 LEU   B N   1 
ATOM   5032 C  CA  . LEU   B  1  308 ? -7.411  6.184   65.470 1.00 44.32  ? 321 LEU   B CA  1 
ATOM   5033 C  C   . LEU   B  1  308 ? -8.573  5.279   65.078 1.00 43.89  ? 321 LEU   B C   1 
ATOM   5034 O  O   . LEU   B  1  308 ? -8.417  4.064   64.913 1.00 46.67  ? 321 LEU   B O   1 
ATOM   5035 C  CB  . LEU   B  1  308 ? -7.470  6.495   66.954 1.00 45.67  ? 321 LEU   B CB  1 
ATOM   5036 C  CG  . LEU   B  1  308 ? -6.112  6.597   67.639 1.00 53.33  ? 321 LEU   B CG  1 
ATOM   5037 C  CD1 . LEU   B  1  308 ? -6.276  7.275   68.976 1.00 56.58  ? 321 LEU   B CD1 1 
ATOM   5038 C  CD2 . LEU   B  1  308 ? -5.499  5.217   67.796 1.00 57.00  ? 321 LEU   B CD2 1 
ATOM   5039 N  N   . ILE   B  1  309 ? -9.748  5.882   64.944 1.00 42.32  ? 322 ILE   B N   1 
ATOM   5040 C  CA  . ILE   B  1  309 ? -10.939 5.127   64.610 1.00 44.33  ? 322 ILE   B CA  1 
ATOM   5041 C  C   . ILE   B  1  309 ? -10.760 4.453   63.251 1.00 43.78  ? 322 ILE   B C   1 
ATOM   5042 O  O   . ILE   B  1  309 ? -11.086 3.271   63.086 1.00 48.39  ? 322 ILE   B O   1 
ATOM   5043 C  CB  . ILE   B  1  309 ? -12.185 6.034   64.657 1.00 43.75  ? 322 ILE   B CB  1 
ATOM   5044 C  CG1 . ILE   B  1  309 ? -12.491 6.486   66.094 1.00 46.18  ? 322 ILE   B CG1 1 
ATOM   5045 C  CG2 . ILE   B  1  309 ? -13.378 5.333   64.006 1.00 40.38  ? 322 ILE   B CG2 1 
ATOM   5046 C  CD1 . ILE   B  1  309 ? -13.527 7.597   66.205 1.00 48.11  ? 322 ILE   B CD1 1 
ATOM   5047 N  N   . LYS   B  1  310 ? -10.274 5.218   62.266 1.00 45.93  ? 323 LYS   B N   1 
ATOM   5048 C  CA  . LYS   B  1  310 ? -10.127 4.713   60.905 1.00 46.51  ? 323 LYS   B CA  1 
ATOM   5049 C  C   . LYS   B  1  310 ? -9.090  3.587   60.848 1.00 39.71  ? 323 LYS   B C   1 
ATOM   5050 O  O   . LYS   B  1  310 ? -9.364  2.525   60.298 1.00 35.30  ? 323 LYS   B O   1 
ATOM   5051 C  CB  . LYS   B  1  310 ? -9.753  5.849   59.956 1.00 50.75  ? 323 LYS   B CB  1 
ATOM   5052 C  CG  . LYS   B  1  310 ? -10.902 6.789   59.680 1.00 60.12  ? 323 LYS   B CG  1 
ATOM   5053 C  CD  . LYS   B  1  310 ? -10.517 7.995   58.834 1.00 65.55  ? 323 LYS   B CD  1 
ATOM   5054 C  CE  . LYS   B  1  310 ? -11.671 8.578   58.095 1.00 71.85  ? 323 LYS   B CE  1 
ATOM   5055 N  NZ  . LYS   B  1  310 ? -11.318 9.916   57.637 1.00 72.49  ? 323 LYS   B NZ  1 
ATOM   5056 N  N   . ASN   B  1  311 ? -7.937  3.799   61.493 1.00 37.13  ? 324 ASN   B N   1 
ATOM   5057 C  CA  . ASN   B  1  311 ? -6.859  2.827   61.455 1.00 38.14  ? 324 ASN   B CA  1 
ATOM   5058 C  C   . ASN   B  1  311 ? -7.290  1.543   62.152 1.00 39.35  ? 324 ASN   B C   1 
ATOM   5059 O  O   . ASN   B  1  311 ? -6.965  0.461   61.702 1.00 39.96  ? 324 ASN   B O   1 
ATOM   5060 C  CB  . ASN   B  1  311 ? -5.578  3.414   62.030 1.00 39.66  ? 324 ASN   B CB  1 
ATOM   5061 C  CG  . ASN   B  1  311 ? -4.798  4.198   61.000 1.00 44.89  ? 324 ASN   B CG  1 
ATOM   5062 O  OD1 . ASN   B  1  311 ? -4.107  3.619   60.153 1.00 52.31  ? 324 ASN   B OD1 1 
ATOM   5063 N  ND2 . ASN   B  1  311 ? -4.899  5.517   61.047 1.00 45.62  ? 324 ASN   B ND2 1 
ATOM   5064 N  N   . LEU   B  1  312 ? -8.047  1.666   63.241 1.00 41.48  ? 325 LEU   B N   1 
ATOM   5065 C  CA  . LEU   B  1  312 ? -8.506  0.497   63.958 1.00 40.73  ? 325 LEU   B CA  1 
ATOM   5066 C  C   . LEU   B  1  312 ? -9.427  -0.318  63.060 1.00 38.07  ? 325 LEU   B C   1 
ATOM   5067 O  O   . LEU   B  1  312 ? -9.344  -1.543  63.045 1.00 36.10  ? 325 LEU   B O   1 
ATOM   5068 C  CB  . LEU   B  1  312 ? -9.165  0.892   65.278 1.00 42.05  ? 325 LEU   B CB  1 
ATOM   5069 C  CG  . LEU   B  1  312 ? -8.190  1.113   66.439 1.00 40.98  ? 325 LEU   B CG  1 
ATOM   5070 C  CD1 . LEU   B  1  312 ? -8.777  1.968   67.531 1.00 41.78  ? 325 LEU   B CD1 1 
ATOM   5071 C  CD2 . LEU   B  1  312 ? -7.753  -0.222  67.012 1.00 40.33  ? 325 LEU   B CD2 1 
ATOM   5072 N  N   . HIS   B  1  313 ? -10.300 0.369   62.322 1.00 38.71  ? 326 HIS   B N   1 
ATOM   5073 C  CA  . HIS   B  1  313 ? -11.203 -0.303  61.401 1.00 38.50  ? 326 HIS   B CA  1 
ATOM   5074 C  C   . HIS   B  1  313 ? -10.395 -0.988  60.296 1.00 39.77  ? 326 HIS   B C   1 
ATOM   5075 O  O   . HIS   B  1  313 ? -10.618 -2.163  59.983 1.00 39.61  ? 326 HIS   B O   1 
ATOM   5076 C  CB  . HIS   B  1  313 ? -12.283 0.651   60.859 1.00 36.56  ? 326 HIS   B CB  1 
ATOM   5077 C  CG  . HIS   B  1  313 ? -13.212 -0.035  59.925 1.00 38.99  ? 326 HIS   B CG  1 
ATOM   5078 N  ND1 . HIS   B  1  313 ? -14.000 -1.084  60.357 1.00 42.88  ? 326 HIS   B ND1 1 
ATOM   5079 C  CD2 . HIS   B  1  313 ? -13.409 0.070   58.595 1.00 41.55  ? 326 HIS   B CD2 1 
ATOM   5080 C  CE1 . HIS   B  1  313 ? -14.669 -1.577  59.317 1.00 45.29  ? 326 HIS   B CE1 1 
ATOM   5081 N  NE2 . HIS   B  1  313 ? -14.325 -0.894  58.241 1.00 44.21  ? 326 HIS   B NE2 1 
ATOM   5082 N  N   . TYR   B  1  314 ? -9.429  -0.263  59.721 1.00 37.32  ? 327 TYR   B N   1 
ATOM   5083 C  CA  . TYR   B  1  314 ? -8.610  -0.848  58.668 1.00 40.80  ? 327 TYR   B CA  1 
ATOM   5084 C  C   . TYR   B  1  314 ? -7.944  -2.119  59.183 1.00 37.14  ? 327 TYR   B C   1 
ATOM   5085 O  O   . TYR   B  1  314 ? -7.952  -3.145  58.519 1.00 36.52  ? 327 TYR   B O   1 
ATOM   5086 C  CB  . TYR   B  1  314 ? -7.536  0.117   58.195 1.00 39.90  ? 327 TYR   B CB  1 
ATOM   5087 C  CG  . TYR   B  1  314 ? -8.053  1.416   57.605 1.00 39.88  ? 327 TYR   B CG  1 
ATOM   5088 C  CD1 . TYR   B  1  314 ? -9.325  1.516   57.047 1.00 46.25  ? 327 TYR   B CD1 1 
ATOM   5089 C  CD2 . TYR   B  1  314 ? -7.255  2.545   57.625 1.00 41.61  ? 327 TYR   B CD2 1 
ATOM   5090 C  CE1 . TYR   B  1  314 ? -9.784  2.706   56.509 1.00 45.60  ? 327 TYR   B CE1 1 
ATOM   5091 C  CE2 . TYR   B  1  314 ? -7.692  3.740   57.088 1.00 44.60  ? 327 TYR   B CE2 1 
ATOM   5092 C  CZ  . TYR   B  1  314 ? -8.962  3.822   56.538 1.00 50.84  ? 327 TYR   B CZ  1 
ATOM   5093 O  OH  . TYR   B  1  314 ? -9.337  5.021   56.016 1.00 49.73  ? 327 TYR   B OH  1 
ATOM   5094 N  N   . TRP   B  1  315 ? -7.423  -2.069  60.402 1.00 34.89  ? 328 TRP   B N   1 
ATOM   5095 C  CA  . TRP   B  1  315 ? -6.729  -3.217  60.938 1.00 33.62  ? 328 TRP   B CA  1 
ATOM   5096 C  C   . TRP   B  1  315 ? -7.698  -4.393  61.028 1.00 36.91  ? 328 TRP   B C   1 
ATOM   5097 O  O   . TRP   B  1  315 ? -7.385  -5.508  60.604 1.00 34.49  ? 328 TRP   B O   1 
ATOM   5098 C  CB  . TRP   B  1  315 ? -6.078  -2.882  62.282 1.00 32.76  ? 328 TRP   B CB  1 
ATOM   5099 C  CG  . TRP   B  1  315 ? -5.191  -3.984  62.785 1.00 34.08  ? 328 TRP   B CG  1 
ATOM   5100 C  CD1 . TRP   B  1  315 ? -4.238  -4.644  62.073 1.00 34.23  ? 328 TRP   B CD1 1 
ATOM   5101 C  CD2 . TRP   B  1  315 ? -5.174  -4.557  64.100 1.00 33.73  ? 328 TRP   B CD2 1 
ATOM   5102 N  NE1 . TRP   B  1  315 ? -3.647  -5.604  62.842 1.00 34.30  ? 328 TRP   B NE1 1 
ATOM   5103 C  CE2 . TRP   B  1  315 ? -4.188  -5.568  64.090 1.00 33.89  ? 328 TRP   B CE2 1 
ATOM   5104 C  CE3 . TRP   B  1  315 ? -5.882  -4.315  65.281 1.00 36.04  ? 328 TRP   B CE3 1 
ATOM   5105 C  CZ2 . TRP   B  1  315 ? -3.883  -6.334  65.206 1.00 35.14  ? 328 TRP   B CZ2 1 
ATOM   5106 C  CZ3 . TRP   B  1  315 ? -5.586  -5.075  66.389 1.00 35.95  ? 328 TRP   B CZ3 1 
ATOM   5107 C  CH2 . TRP   B  1  315 ? -4.607  -6.078  66.351 1.00 36.10  ? 328 TRP   B CH2 1 
ATOM   5108 N  N   . TRP   B  1  316 ? -8.902  -4.114  61.531 1.00 36.95  ? 329 TRP   B N   1 
ATOM   5109 C  CA  . TRP   B  1  316 ? -9.905  -5.146  61.699 1.00 36.94  ? 329 TRP   B CA  1 
ATOM   5110 C  C   . TRP   B  1  316 ? -10.235 -5.800  60.360 1.00 32.16  ? 329 TRP   B C   1 
ATOM   5111 O  O   . TRP   B  1  316 ? -10.446 -7.002  60.326 1.00 32.45  ? 329 TRP   B O   1 
ATOM   5112 C  CB  . TRP   B  1  316 ? -11.159 -4.594  62.396 1.00 39.90  ? 329 TRP   B CB  1 
ATOM   5113 C  CG  . TRP   B  1  316 ? -12.279 -5.599  62.415 1.00 36.69  ? 329 TRP   B CG  1 
ATOM   5114 C  CD1 . TRP   B  1  316 ? -12.452 -6.618  63.296 1.00 38.25  ? 329 TRP   B CD1 1 
ATOM   5115 C  CD2 . TRP   B  1  316 ? -13.302 -5.748  61.414 1.00 36.33  ? 329 TRP   B CD2 1 
ATOM   5116 N  NE1 . TRP   B  1  316 ? -13.547 -7.358  62.952 1.00 39.86  ? 329 TRP   B NE1 1 
ATOM   5117 C  CE2 . TRP   B  1  316 ? -14.080 -6.855  61.798 1.00 38.45  ? 329 TRP   B CE2 1 
ATOM   5118 C  CE3 . TRP   B  1  316 ? -13.648 -5.033  60.264 1.00 37.87  ? 329 TRP   B CE3 1 
ATOM   5119 C  CZ2 . TRP   B  1  316 ? -15.176 -7.280  61.060 1.00 42.14  ? 329 TRP   B CZ2 1 
ATOM   5120 C  CZ3 . TRP   B  1  316 ? -14.753 -5.443  59.550 1.00 41.65  ? 329 TRP   B CZ3 1 
ATOM   5121 C  CH2 . TRP   B  1  316 ? -15.482 -6.572  59.922 1.00 38.34  ? 329 TRP   B CH2 1 
ATOM   5122 N  N   . THR   B  1  317 ? -10.257 -5.047  59.254 1.00 34.37  ? 330 THR   B N   1 
ATOM   5123 C  CA  . THR   B  1  317 ? -10.621 -5.653  57.974 1.00 40.74  ? 330 THR   B CA  1 
ATOM   5124 C  C   . THR   B  1  317 ? -9.652  -6.791  57.646 1.00 41.09  ? 330 THR   B C   1 
ATOM   5125 O  O   . THR   B  1  317 ? -10.042 -7.814  57.101 1.00 39.00  ? 330 THR   B O   1 
ATOM   5126 C  CB  . THR   B  1  317 ? -10.656 -4.657  56.811 1.00 45.30  ? 330 THR   B CB  1 
ATOM   5127 O  OG1 . THR   B  1  317 ? -9.337  -4.160  56.621 1.00 39.99  ? 330 THR   B OG1 1 
ATOM   5128 C  CG2 . THR   B  1  317 ? -11.616 -3.497  57.023 1.00 47.23  ? 330 THR   B CG2 1 
ATOM   5129 N  N   . GLY   B  1  318 ? -8.378  -6.618  57.988 1.00 40.70  ? 331 GLY   B N   1 
ATOM   5130 C  CA  . GLY   B  1  318 ? -7.416  -7.686  57.784 1.00 39.74  ? 331 GLY   B CA  1 
ATOM   5131 C  C   . GLY   B  1  318 ? -7.565  -8.782  58.825 1.00 35.45  ? 331 GLY   B C   1 
ATOM   5132 O  O   . GLY   B  1  318 ? -7.563  -9.967  58.482 1.00 33.85  ? 331 GLY   B O   1 
ATOM   5133 N  N   . VAL   B  1  319 ? -7.674  -8.370  60.093 1.00 31.99  ? 332 VAL   B N   1 
ATOM   5134 C  CA  . VAL   B  1  319 ? -7.736  -9.317  61.185 1.00 34.19  ? 332 VAL   B CA  1 
ATOM   5135 C  C   . VAL   B  1  319 ? -8.910  -10.257 60.972 1.00 33.50  ? 332 VAL   B C   1 
ATOM   5136 O  O   . VAL   B  1  319 ? -8.812  -11.450 61.245 1.00 36.09  ? 332 VAL   B O   1 
ATOM   5137 C  CB  . VAL   B  1  319 ? -7.850  -8.583  62.534 1.00 36.59  ? 332 VAL   B CB  1 
ATOM   5138 C  CG1 . VAL   B  1  319 ? -8.344  -9.496  63.647 1.00 36.74  ? 332 VAL   B CG1 1 
ATOM   5139 C  CG2 . VAL   B  1  319 ? -6.530  -7.958  62.952 1.00 37.16  ? 332 VAL   B CG2 1 
ATOM   5140 N  N   . ASN   B  1  320 ? -10.044 -9.699  60.537 1.00 35.59  ? 333 ASN   B N   1 
ATOM   5141 C  CA  . ASN   B  1  320 ? -11.275 -10.465 60.480 1.00 36.78  ? 333 ASN   B CA  1 
ATOM   5142 C  C   . ASN   B  1  320 ? -11.069 -11.680 59.588 1.00 39.55  ? 333 ASN   B C   1 
ATOM   5143 O  O   . ASN   B  1  320 ? -11.532 -12.766 59.917 1.00 39.64  ? 333 ASN   B O   1 
ATOM   5144 C  CB  . ASN   B  1  320 ? -12.463 -9.641  59.991 1.00 41.65  ? 333 ASN   B CB  1 
ATOM   5145 C  CG  . ASN   B  1  320 ? -13.782 -10.363 60.186 1.00 41.07  ? 333 ASN   B CG  1 
ATOM   5146 O  OD1 . ASN   B  1  320 ? -14.071 -10.905 61.256 1.00 44.97  ? 333 ASN   B OD1 1 
ATOM   5147 N  ND2 . ASN   B  1  320 ? -14.594 -10.404 59.157 1.00 43.33  ? 333 ASN   B ND2 1 
ATOM   5148 N  N   . VAL   B  1  321 ? -10.368 -11.482 58.463 1.00 45.04  ? 334 VAL   B N   1 
ATOM   5149 C  CA  . VAL   B  1  321 ? -10.121 -12.568 57.531 1.00 45.77  ? 334 VAL   B CA  1 
ATOM   5150 C  C   . VAL   B  1  321 ? -9.002  -13.446 58.084 1.00 42.19  ? 334 VAL   B C   1 
ATOM   5151 O  O   . VAL   B  1  321 ? -9.140  -14.667 58.139 1.00 41.90  ? 334 VAL   B O   1 
ATOM   5152 C  CB  . VAL   B  1  321 ? -9.809  -12.075 56.104 1.00 50.51  ? 334 VAL   B CB  1 
ATOM   5153 C  CG1 . VAL   B  1  321 ? -9.518  -13.245 55.159 1.00 46.80  ? 334 VAL   B CG1 1 
ATOM   5154 C  CG2 . VAL   B  1  321 ? -10.935 -11.182 55.558 1.00 44.53  ? 334 VAL   B CG2 1 
ATOM   5155 N  N   . ALA   B  1  322 ? -7.898  -12.836 58.513 1.00 40.80  ? 335 ALA   B N   1 
ATOM   5156 C  CA  . ALA   B  1  322 ? -6.725  -13.629 58.849 1.00 44.60  ? 335 ALA   B CA  1 
ATOM   5157 C  C   . ALA   B  1  322 ? -6.973  -14.513 60.065 1.00 42.86  ? 335 ALA   B C   1 
ATOM   5158 O  O   . ALA   B  1  322 ? -6.434  -15.613 60.151 1.00 43.08  ? 335 ALA   B O   1 
ATOM   5159 C  CB  . ALA   B  1  322 ? -5.541  -12.733 59.072 1.00 47.69  ? 335 ALA   B CB  1 
ATOM   5160 N  N   . PHE   B  1  323 ? -7.768  -14.013 61.020 1.00 41.57  ? 336 PHE   B N   1 
ATOM   5161 C  CA  . PHE   B  1  323 ? -7.956  -14.725 62.267 1.00 42.93  ? 336 PHE   B CA  1 
ATOM   5162 C  C   . PHE   B  1  323 ? -9.220  -15.579 62.222 1.00 48.13  ? 336 PHE   B C   1 
ATOM   5163 O  O   . PHE   B  1  323 ? -9.531  -16.224 63.209 1.00 49.16  ? 336 PHE   B O   1 
ATOM   5164 C  CB  . PHE   B  1  323 ? -7.999  -13.747 63.438 1.00 39.18  ? 336 PHE   B CB  1 
ATOM   5165 C  CG  . PHE   B  1  323 ? -6.694  -13.055 63.783 1.00 42.04  ? 336 PHE   B CG  1 
ATOM   5166 C  CD1 . PHE   B  1  323 ? -5.553  -13.205 63.000 1.00 48.60  ? 336 PHE   B CD1 1 
ATOM   5167 C  CD2 . PHE   B  1  323 ? -6.629  -12.197 64.866 1.00 43.50  ? 336 PHE   B CD2 1 
ATOM   5168 C  CE1 . PHE   B  1  323 ? -4.383  -12.522 63.310 1.00 47.55  ? 336 PHE   B CE1 1 
ATOM   5169 C  CE2 . PHE   B  1  323 ? -5.465  -11.506 65.161 1.00 48.16  ? 336 PHE   B CE2 1 
ATOM   5170 C  CZ  . PHE   B  1  323 ? -4.342  -11.674 64.386 1.00 51.14  ? 336 PHE   B CZ  1 
ATOM   5171 N  N   . GLY   B  1  324 ? -9.954  -15.564 61.101 1.00 54.08  ? 337 GLY   B N   1 
ATOM   5172 C  CA  . GLY   B  1  324 ? -11.131 -16.405 60.922 1.00 54.32  ? 337 GLY   B CA  1 
ATOM   5173 C  C   . GLY   B  1  324 ? -12.373 -15.896 61.664 1.00 51.26  ? 337 GLY   B C   1 
ATOM   5174 O  O   . GLY   B  1  324 ? -13.145 -16.701 62.162 1.00 52.69  ? 337 GLY   B O   1 
ATOM   5175 N  N   . GLY   B  1  325 ? -12.573 -14.569 61.716 1.00 51.91  ? 338 GLY   B N   1 
ATOM   5176 C  CA  . GLY   B  1  325 ? -13.749 -13.940 62.313 1.00 47.24  ? 338 GLY   B CA  1 
ATOM   5177 C  C   . GLY   B  1  325 ? -13.450 -13.434 63.731 1.00 47.31  ? 338 GLY   B C   1 
ATOM   5178 O  O   . GLY   B  1  325 ? -13.175 -14.244 64.611 1.00 44.52  ? 338 GLY   B O   1 
ATOM   5179 N  N   . CYS   B  1  326 ? -13.413 -12.103 63.916 1.00 43.92  ? 339 CYS   B N   1 
ATOM   5180 C  CA  . CYS   B  1  326 ? -13.319 -11.489 65.233 1.00 50.13  ? 339 CYS   B CA  1 
ATOM   5181 C  C   . CYS   B  1  326 ? -14.360 -10.382 65.322 1.00 50.70  ? 339 CYS   B C   1 
ATOM   5182 O  O   . CYS   B  1  326 ? -14.547 -9.638  64.361 1.00 46.15  ? 339 CYS   B O   1 
ATOM   5183 C  CB  . CYS   B  1  326 ? -11.967 -10.828 65.519 1.00 52.62  ? 339 CYS   B CB  1 
ATOM   5184 S  SG  . CYS   B  1  326 ? -10.580 -11.980 65.702 1.00 73.07  ? 339 CYS   B SG  1 
ATOM   5185 N  N   . ASP   B  1  327 ? -14.992 -10.259 66.491 1.00 48.98  ? 340 ASP   B N   1 
ATOM   5186 C  CA  . ASP   B  1  327 ? -15.967 -9.205  66.708 1.00 52.06  ? 340 ASP   B CA  1 
ATOM   5187 C  C   . ASP   B  1  327 ? -15.224 -7.868  66.757 1.00 46.87  ? 340 ASP   B C   1 
ATOM   5188 O  O   . ASP   B  1  327 ? -14.317 -7.684  67.576 1.00 43.15  ? 340 ASP   B O   1 
ATOM   5189 C  CB  . ASP   B  1  327 ? -16.765 -9.409  67.989 1.00 61.10  ? 340 ASP   B CB  1 
ATOM   5190 C  CG  . ASP   B  1  327 ? -17.543 -10.711 68.163 1.00 65.43  ? 340 ASP   B CG  1 
ATOM   5191 O  OD1 . ASP   B  1  327 ? -17.858 -11.372 67.147 1.00 64.11  ? 340 ASP   B OD1 1 
ATOM   5192 O  OD2 . ASP   B  1  327 ? -17.801 -11.065 69.332 1.00 68.08  ? 340 ASP   B OD2 1 
ATOM   5193 N  N   . GLU   B  1  328 ? -15.608 -6.942  65.874 1.00 42.42  ? 341 GLU   B N   1 
ATOM   5194 C  CA  . GLU   B  1  328 ? -14.970 -5.642  65.832 1.00 38.65  ? 341 GLU   B CA  1 
ATOM   5195 C  C   . GLU   B  1  328 ? -15.221 -4.883  67.135 1.00 40.88  ? 341 GLU   B C   1 
ATOM   5196 O  O   . GLU   B  1  328 ? -16.339 -4.871  67.628 1.00 37.36  ? 341 GLU   B O   1 
ATOM   5197 C  CB  . GLU   B  1  328 ? -15.452 -4.830  64.635 1.00 37.96  ? 341 GLU   B CB  1 
ATOM   5198 C  CG  . GLU   B  1  328 ? -14.603 -3.571  64.440 1.00 38.88  ? 341 GLU   B CG  1 
ATOM   5199 C  CD  . GLU   B  1  328 ? -14.820 -2.834  63.140 1.00 39.10  ? 341 GLU   B CD  1 
ATOM   5200 O  OE1 . GLU   B  1  328 ? -15.713 -3.223  62.348 1.00 45.06  ? 341 GLU   B OE1 1 
ATOM   5201 O  OE2 . GLU   B  1  328 ? -14.075 -1.863  62.925 1.00 38.78  ? 341 GLU   B OE2 1 
ATOM   5202 N  N   . LEU   B  1  329 ? -14.161 -4.264  67.674 1.00 36.97  ? 342 LEU   B N   1 
ATOM   5203 C  CA  . LEU   B  1  329 ? -14.259 -3.386  68.825 1.00 36.69  ? 342 LEU   B CA  1 
ATOM   5204 C  C   . LEU   B  1  329 ? -14.182 -1.940  68.356 1.00 35.85  ? 342 LEU   B C   1 
ATOM   5205 O  O   . LEU   B  1  329 ? -13.527 -1.639  67.372 1.00 45.67  ? 342 LEU   B O   1 
ATOM   5206 C  CB  . LEU   B  1  329 ? -13.158 -3.720  69.833 1.00 37.47  ? 342 LEU   B CB  1 
ATOM   5207 C  CG  . LEU   B  1  329 ? -13.172 -5.161  70.361 1.00 42.19  ? 342 LEU   B CG  1 
ATOM   5208 C  CD1 . LEU   B  1  329 ? -11.941 -5.492  71.180 1.00 45.75  ? 342 LEU   B CD1 1 
ATOM   5209 C  CD2 . LEU   B  1  329 ? -14.429 -5.461  71.172 1.00 45.38  ? 342 LEU   B CD2 1 
ATOM   5210 N  N   . PHE   B  1  330 ? -14.859 -1.042  69.072 1.00 36.96  ? 343 PHE   B N   1 
ATOM   5211 C  CA  . PHE   B  1  330 ? -14.925 0.373   68.739 1.00 38.05  ? 343 PHE   B CA  1 
ATOM   5212 C  C   . PHE   B  1  330 ? -14.598 1.182   69.993 1.00 44.36  ? 343 PHE   B C   1 
ATOM   5213 O  O   . PHE   B  1  330 ? -15.450 1.856   70.567 1.00 49.27  ? 343 PHE   B O   1 
ATOM   5214 C  CB  . PHE   B  1  330 ? -16.315 0.741   68.230 1.00 38.55  ? 343 PHE   B CB  1 
ATOM   5215 C  CG  . PHE   B  1  330 ? -16.748 -0.057  67.021 1.00 38.60  ? 343 PHE   B CG  1 
ATOM   5216 C  CD1 . PHE   B  1  330 ? -16.336 0.321   65.756 1.00 40.77  ? 343 PHE   B CD1 1 
ATOM   5217 C  CD2 . PHE   B  1  330 ? -17.571 -1.170  67.154 1.00 44.54  ? 343 PHE   B CD2 1 
ATOM   5218 C  CE1 . PHE   B  1  330 ? -16.739 -0.407  64.643 1.00 39.93  ? 343 PHE   B CE1 1 
ATOM   5219 C  CE2 . PHE   B  1  330 ? -17.965 -1.895  66.045 1.00 45.87  ? 343 PHE   B CE2 1 
ATOM   5220 C  CZ  . PHE   B  1  330 ? -17.542 -1.524  64.797 1.00 42.44  ? 343 PHE   B CZ  1 
ATOM   5221 N  N   . PRO   B  1  331 ? -13.343 1.153   70.473 1.00 45.55  ? 344 PRO   B N   1 
ATOM   5222 C  CA  . PRO   B  1  331 ? -13.005 1.821   71.725 1.00 48.68  ? 344 PRO   B CA  1 
ATOM   5223 C  C   . PRO   B  1  331 ? -13.220 3.330   71.720 1.00 45.51  ? 344 PRO   B C   1 
ATOM   5224 O  O   . PRO   B  1  331 ? -13.299 3.902   72.796 1.00 47.47  ? 344 PRO   B O   1 
ATOM   5225 C  CB  . PRO   B  1  331 ? -11.529 1.450   71.923 1.00 47.10  ? 344 PRO   B CB  1 
ATOM   5226 C  CG  . PRO   B  1  331 ? -11.045 1.211   70.530 1.00 48.80  ? 344 PRO   B CG  1 
ATOM   5227 C  CD  . PRO   B  1  331 ? -12.196 0.477   69.858 1.00 45.86  ? 344 PRO   B CD  1 
ATOM   5228 N  N   . TYR   B  1  332 ? -13.317 3.957   70.540 1.00 40.09  ? 345 TYR   B N   1 
ATOM   5229 C  CA  . TYR   B  1  332 ? -13.570 5.392   70.473 1.00 42.54  ? 345 TYR   B CA  1 
ATOM   5230 C  C   . TYR   B  1  332 ? -14.887 5.682   69.748 1.00 42.75  ? 345 TYR   B C   1 
ATOM   5231 O  O   . TYR   B  1  332 ? -15.120 6.794   69.288 1.00 45.39  ? 345 TYR   B O   1 
ATOM   5232 C  CB  . TYR   B  1  332 ? -12.397 6.104   69.802 1.00 47.13  ? 345 TYR   B CB  1 
ATOM   5233 C  CG  . TYR   B  1  332 ? -11.055 5.752   70.423 1.00 47.29  ? 345 TYR   B CG  1 
ATOM   5234 C  CD1 . TYR   B  1  332 ? -10.713 6.268   71.660 1.00 50.53  ? 345 TYR   B CD1 1 
ATOM   5235 C  CD2 . TYR   B  1  332 ? -10.147 4.900   69.795 1.00 43.36  ? 345 TYR   B CD2 1 
ATOM   5236 C  CE1 . TYR   B  1  332 ? -9.489  5.987   72.251 1.00 52.20  ? 345 TYR   B CE1 1 
ATOM   5237 C  CE2 . TYR   B  1  332 ? -8.935  4.580   70.390 1.00 43.18  ? 345 TYR   B CE2 1 
ATOM   5238 C  CZ  . TYR   B  1  332 ? -8.603  5.120   71.621 1.00 49.38  ? 345 TYR   B CZ  1 
ATOM   5239 O  OH  . TYR   B  1  332 ? -7.401  4.789   72.184 1.00 46.63  ? 345 TYR   B OH  1 
ATOM   5240 N  N   . GLY   B  1  333 ? -15.765 4.680   69.669 1.00 45.80  ? 346 GLY   B N   1 
ATOM   5241 C  CA  . GLY   B  1  333 ? -16.989 4.796   68.898 1.00 49.09  ? 346 GLY   B CA  1 
ATOM   5242 C  C   . GLY   B  1  333 ? -16.709 4.756   67.397 1.00 58.71  ? 346 GLY   B C   1 
ATOM   5243 O  O   . GLY   B  1  333 ? -15.671 4.242   66.967 1.00 54.24  ? 346 GLY   B O   1 
ATOM   5244 N  N   . GLN   B  1  334 ? -17.699 5.261   66.636 1.00 65.67  ? 347 GLN   B N   1 
ATOM   5245 C  CA  A GLN   B  1  334 ? -17.645 5.338   65.180 0.50 67.66  ? 347 GLN   B CA  1 
ATOM   5246 C  CA  B GLN   B  1  334 ? -17.703 5.342   65.183 0.50 72.89  ? 347 GLN   B CA  1 
ATOM   5247 C  C   . GLN   B  1  334 ? -17.568 6.805   64.763 1.00 74.33  ? 347 GLN   B C   1 
ATOM   5248 O  O   . GLN   B  1  334 ? -17.602 7.689   65.614 1.00 69.88  ? 347 GLN   B O   1 
ATOM   5249 C  CB  A GLN   B  1  334 ? -18.770 4.507   64.559 0.50 65.49  ? 347 GLN   B CB  1 
ATOM   5250 C  CB  B GLN   B  1  334 ? -19.004 4.754   64.638 0.50 78.54  ? 347 GLN   B CB  1 
ATOM   5251 C  CG  A GLN   B  1  334 ? -18.496 3.010   64.729 0.50 62.42  ? 347 GLN   B CG  1 
ATOM   5252 C  CG  B GLN   B  1  334 ? -18.946 3.259   64.332 0.50 86.68  ? 347 GLN   B CG  1 
ATOM   5253 C  CD  A GLN   B  1  334 ? -19.418 2.021   64.039 0.50 58.27  ? 347 GLN   B CD  1 
ATOM   5254 C  CD  B GLN   B  1  334 ? -19.633 2.389   65.362 0.50 97.00  ? 347 GLN   B CD  1 
ATOM   5255 O  OE1 A GLN   B  1  334 ? -19.338 1.782   62.831 0.50 52.89  ? 347 GLN   B OE1 1 
ATOM   5256 O  OE1 B GLN   B  1  334 ? -20.590 1.670   65.050 0.50 95.45  ? 347 GLN   B OE1 1 
ATOM   5257 N  NE2 A GLN   B  1  334 ? -20.203 1.307   64.833 0.50 56.15  ? 347 GLN   B NE2 1 
ATOM   5258 N  NE2 B GLN   B  1  334 ? -19.145 2.416   66.594 0.50 106.07 ? 347 GLN   B NE2 1 
ATOM   5259 N  N   . LEU   B  1  335 ? -17.371 7.051   63.459 1.00 81.28  ? 348 LEU   B N   1 
ATOM   5260 C  CA  . LEU   B  1  335 ? -17.038 8.391   62.980 1.00 92.07  ? 348 LEU   B CA  1 
ATOM   5261 C  C   . LEU   B  1  335 ? -18.217 9.363   63.175 1.00 91.50  ? 348 LEU   B C   1 
ATOM   5262 O  O   . LEU   B  1  335 ? -19.356 8.938   62.896 1.00 90.51  ? 348 LEU   B O   1 
ATOM   5263 C  CB  . LEU   B  1  335 ? -16.588 8.336   61.521 1.00 92.62  ? 348 LEU   B CB  1 
ATOM   5264 C  CG  . LEU   B  1  335 ? -15.192 7.751   61.288 1.00 93.18  ? 348 LEU   B CG  1 
ATOM   5265 C  CD1 . LEU   B  1  335 ? -14.942 7.535   59.790 1.00 96.52  ? 348 LEU   B CD1 1 
ATOM   5266 C  CD2 . LEU   B  1  335 ? -14.122 8.643   61.928 1.00 81.86  ? 348 LEU   B CD2 1 
ATOM   5267 N  N   . GLN   C  1  1   ? 5.258   -16.992 27.128 1.00 152.05 ? 14  GLN   C N   1 
ATOM   5268 C  CA  . GLN   C  1  1   ? 5.496   -16.888 25.662 1.00 152.78 ? 14  GLN   C CA  1 
ATOM   5269 C  C   . GLN   C  1  1   ? 4.742   -15.671 25.125 1.00 146.38 ? 14  GLN   C C   1 
ATOM   5270 O  O   . GLN   C  1  1   ? 4.178   -14.911 25.913 1.00 152.15 ? 14  GLN   C O   1 
ATOM   5271 C  CB  . GLN   C  1  1   ? 5.021   -18.174 24.987 1.00 151.87 ? 14  GLN   C CB  1 
ATOM   5272 C  CG  . GLN   C  1  1   ? 5.838   -18.586 23.769 1.00 146.73 ? 14  GLN   C CG  1 
ATOM   5273 C  CD  . GLN   C  1  1   ? 5.305   -19.845 23.123 1.00 133.54 ? 14  GLN   C CD  1 
ATOM   5274 O  OE1 . GLN   C  1  1   ? 4.322   -20.437 23.585 1.00 115.88 ? 14  GLN   C OE1 1 
ATOM   5275 N  NE2 . GLN   C  1  1   ? 5.952   -20.268 22.047 1.00 132.03 ? 14  GLN   C NE2 1 
ATOM   5276 N  N   . GLY   C  1  2   ? 4.751   -15.486 23.796 1.00 120.63 ? 15  GLY   C N   1 
ATOM   5277 C  CA  . GLY   C  1  2   ? 3.945   -14.457 23.156 1.00 94.28  ? 15  GLY   C CA  1 
ATOM   5278 C  C   . GLY   C  1  2   ? 3.772   -14.682 21.652 1.00 82.08  ? 15  GLY   C C   1 
ATOM   5279 O  O   . GLY   C  1  2   ? 3.831   -15.799 21.151 1.00 73.77  ? 15  GLY   C O   1 
ATOM   5280 N  N   . VAL   C  1  3   ? 3.549   -13.573 20.945 1.00 71.19  ? 16  VAL   C N   1 
ATOM   5281 C  CA  . VAL   C  1  3   ? 3.123   -13.563 19.557 1.00 67.66  ? 16  VAL   C CA  1 
ATOM   5282 C  C   . VAL   C  1  3   ? 4.284   -13.083 18.688 1.00 59.68  ? 16  VAL   C C   1 
ATOM   5283 O  O   . VAL   C  1  3   ? 5.144   -12.352 19.173 1.00 45.13  ? 16  VAL   C O   1 
ATOM   5284 C  CB  . VAL   C  1  3   ? 1.890   -12.635 19.481 1.00 67.89  ? 16  VAL   C CB  1 
ATOM   5285 C  CG1 . VAL   C  1  3   ? 1.519   -12.230 18.057 1.00 72.32  ? 16  VAL   C CG1 1 
ATOM   5286 C  CG2 . VAL   C  1  3   ? 0.694   -13.262 20.187 1.00 69.56  ? 16  VAL   C CG2 1 
ATOM   5287 N  N   . ASP   C  1  4   ? 4.289   -13.506 17.415 1.00 60.47  ? 17  ASP   C N   1 
ATOM   5288 C  CA  . ASP   C  1  4   ? 5.168   -12.953 16.393 1.00 62.13  ? 17  ASP   C CA  1 
ATOM   5289 C  C   . ASP   C  1  4   ? 4.393   -11.902 15.584 1.00 59.41  ? 17  ASP   C C   1 
ATOM   5290 O  O   . ASP   C  1  4   ? 3.571   -12.264 14.746 1.00 57.93  ? 17  ASP   C O   1 
ATOM   5291 C  CB  . ASP   C  1  4   ? 5.751   -14.074 15.547 1.00 69.99  ? 17  ASP   C CB  1 
ATOM   5292 C  CG  . ASP   C  1  4   ? 7.100   -13.771 14.909 1.00 82.31  ? 17  ASP   C CG  1 
ATOM   5293 O  OD1 . ASP   C  1  4   ? 7.599   -12.638 15.074 1.00 86.10  ? 17  ASP   C OD1 1 
ATOM   5294 O  OD2 . ASP   C  1  4   ? 7.685   -14.691 14.303 1.00 85.20  ? 17  ASP   C OD2 1 
ATOM   5295 N  N   . PRO   C  1  5   ? 4.593   -10.578 15.821 1.00 51.12  ? 18  PRO   C N   1 
ATOM   5296 C  CA  . PRO   C  1  5   ? 3.692   -9.544  15.291 1.00 52.50  ? 18  PRO   C CA  1 
ATOM   5297 C  C   . PRO   C  1  5   ? 3.867   -9.250  13.800 1.00 46.96  ? 18  PRO   C C   1 
ATOM   5298 O  O   . PRO   C  1  5   ? 4.945   -8.859  13.385 1.00 44.65  ? 18  PRO   C O   1 
ATOM   5299 C  CB  . PRO   C  1  5   ? 3.989   -8.279  16.112 1.00 48.00  ? 18  PRO   C CB  1 
ATOM   5300 C  CG  . PRO   C  1  5   ? 5.362   -8.532  16.745 1.00 49.24  ? 18  PRO   C CG  1 
ATOM   5301 C  CD  . PRO   C  1  5   ? 5.722   -10.009 16.570 1.00 47.52  ? 18  PRO   C CD  1 
ATOM   5302 N  N   . PRO   C  1  6   ? 2.802   -9.349  12.974 1.00 50.67  ? 19  PRO   C N   1 
ATOM   5303 C  CA  . PRO   C  1  6   ? 2.944   -9.265  11.519 1.00 49.94  ? 19  PRO   C CA  1 
ATOM   5304 C  C   . PRO   C  1  6   ? 3.058   -7.803  11.111 1.00 43.08  ? 19  PRO   C C   1 
ATOM   5305 O  O   . PRO   C  1  6   ? 2.724   -6.909  11.886 1.00 35.99  ? 19  PRO   C O   1 
ATOM   5306 C  CB  . PRO   C  1  6   ? 1.643   -9.903  11.009 1.00 50.24  ? 19  PRO   C CB  1 
ATOM   5307 C  CG  . PRO   C  1  6   ? 0.627   -9.494  12.050 1.00 51.10  ? 19  PRO   C CG  1 
ATOM   5308 C  CD  . PRO   C  1  6   ? 1.393   -9.465  13.390 1.00 51.70  ? 19  PRO   C CD  1 
ATOM   5309 N  N   . PRO   C  1  7   ? 3.547   -7.516  9.893  1.00 44.25  ? 20  PRO   C N   1 
ATOM   5310 C  CA  . PRO   C  1  7   ? 3.630   -6.142  9.420  1.00 40.38  ? 20  PRO   C CA  1 
ATOM   5311 C  C   . PRO   C  1  7   ? 2.231   -5.571  9.274  1.00 36.40  ? 20  PRO   C C   1 
ATOM   5312 O  O   . PRO   C  1  7   ? 1.253   -6.307  9.179  1.00 35.06  ? 20  PRO   C O   1 
ATOM   5313 C  CB  . PRO   C  1  7   ? 4.409   -6.205  8.099  1.00 47.56  ? 20  PRO   C CB  1 
ATOM   5314 C  CG  . PRO   C  1  7   ? 4.353   -7.661  7.698  1.00 53.85  ? 20  PRO   C CG  1 
ATOM   5315 C  CD  . PRO   C  1  7   ? 4.115   -8.489  8.947  1.00 52.21  ? 20  PRO   C CD  1 
ATOM   5316 N  N   . PRO   C  1  8   ? 2.082   -4.230  9.329  1.00 31.76  ? 21  PRO   C N   1 
ATOM   5317 C  CA  . PRO   C  1  8   ? 0.771   -3.616  9.238  1.00 28.73  ? 21  PRO   C CA  1 
ATOM   5318 C  C   . PRO   C  1  8   ? 0.200   -3.868  7.849  1.00 31.47  ? 21  PRO   C C   1 
ATOM   5319 O  O   . PRO   C  1  8   ? 0.932   -3.999  6.868  1.00 30.42  ? 21  PRO   C O   1 
ATOM   5320 C  CB  . PRO   C  1  8   ? 1.030   -2.147  9.480  1.00 29.07  ? 21  PRO   C CB  1 
ATOM   5321 C  CG  . PRO   C  1  8   ? 2.462   -1.965  9.087  1.00 33.04  ? 21  PRO   C CG  1 
ATOM   5322 C  CD  . PRO   C  1  8   ? 3.158   -3.249  9.458  1.00 31.35  ? 21  PRO   C CD  1 
ATOM   5323 N  N   . PRO   C  1  9   ? -1.136  -3.894  7.731  1.00 32.22  ? 22  PRO   C N   1 
ATOM   5324 C  CA  . PRO   C  1  9   ? -1.800  -3.912  6.435  1.00 34.62  ? 22  PRO   C CA  1 
ATOM   5325 C  C   . PRO   C  1  9   ? -1.387  -2.691  5.644  1.00 30.02  ? 22  PRO   C C   1 
ATOM   5326 O  O   . PRO   C  1  9   ? -1.093  -1.668  6.249  1.00 27.83  ? 22  PRO   C O   1 
ATOM   5327 C  CB  . PRO   C  1  9   ? -3.304  -3.838  6.753  1.00 34.76  ? 22  PRO   C CB  1 
ATOM   5328 C  CG  . PRO   C  1  9   ? -3.398  -4.218  8.195  1.00 38.56  ? 22  PRO   C CG  1 
ATOM   5329 C  CD  . PRO   C  1  9   ? -2.076  -3.910  8.848  1.00 34.16  ? 22  PRO   C CD  1 
ATOM   5330 N  N   . GLY   C  1  10  ? -1.458  -2.822  4.311  1.00 33.62  ? 23  GLY   C N   1 
ATOM   5331 C  CA  . GLY   C  1  10  ? -1.385  -1.699  3.392  1.00 31.54  ? 23  GLY   C CA  1 
ATOM   5332 C  C   . GLY   C  1  10  ? -2.758  -1.049  3.260  1.00 30.57  ? 23  GLY   C C   1 
ATOM   5333 O  O   . GLY   C  1  10  ? -3.669  -1.376  4.012  1.00 28.63  ? 23  GLY   C O   1 
ATOM   5334 N  N   . PRO   C  1  11  ? -2.944  -0.110  2.308  1.00 32.75  ? 24  PRO   C N   1 
ATOM   5335 C  CA  . PRO   C  1  11  ? -4.241  0.524   2.073  1.00 35.33  ? 24  PRO   C CA  1 
ATOM   5336 C  C   . PRO   C  1  11  ? -5.316  -0.507  1.765  1.00 31.35  ? 24  PRO   C C   1 
ATOM   5337 O  O   . PRO   C  1  11  ? -5.022  -1.641  1.382  1.00 30.00  ? 24  PRO   C O   1 
ATOM   5338 C  CB  . PRO   C  1  11  ? -3.981  1.448   0.864  1.00 33.96  ? 24  PRO   C CB  1 
ATOM   5339 C  CG  . PRO   C  1  11  ? -2.508  1.753   0.964  1.00 31.44  ? 24  PRO   C CG  1 
ATOM   5340 C  CD  . PRO   C  1  11  ? -1.911  0.407   1.396  1.00 32.26  ? 24  PRO   C CD  1 
ATOM   5341 N  N   . PRO   C  1  12  ? -6.601  -0.163  1.952  1.00 33.71  ? 25  PRO   C N   1 
ATOM   5342 C  CA  . PRO   C  1  12  ? -7.676  -1.092  1.586  1.00 36.51  ? 25  PRO   C CA  1 
ATOM   5343 C  C   . PRO   C  1  12  ? -7.726  -1.232  0.058  1.00 37.61  ? 25  PRO   C C   1 
ATOM   5344 O  O   . PRO   C  1  12  ? -7.389  -0.276  -0.654 1.00 33.73  ? 25  PRO   C O   1 
ATOM   5345 C  CB  . PRO   C  1  12  ? -8.917  -0.431  2.188  1.00 37.66  ? 25  PRO   C CB  1 
ATOM   5346 C  CG  . PRO   C  1  12  ? -8.570  1.063   2.200  1.00 39.35  ? 25  PRO   C CG  1 
ATOM   5347 C  CD  . PRO   C  1  12  ? -7.079  1.124   2.488  1.00 34.98  ? 25  PRO   C CD  1 
ATOM   5348 N  N   . SER   C  1  13  ? -8.068  -2.445  -0.412 1.00 39.51  ? 26  SER   C N   1 
ATOM   5349 C  CA  A SER   C  1  13  ? -8.262  -2.736  -1.827 0.50 41.77  ? 26  SER   C CA  1 
ATOM   5350 C  CA  B SER   C  1  13  ? -8.278  -2.750  -1.824 0.50 45.00  ? 26  SER   C CA  1 
ATOM   5351 C  C   . SER   C  1  13  ? -9.123  -1.668  -2.498 1.00 38.06  ? 26  SER   C C   1 
ATOM   5352 O  O   . SER   C  1  13  ? -8.761  -1.145  -3.540 1.00 32.60  ? 26  SER   C O   1 
ATOM   5353 C  CB  A SER   C  1  13  ? -8.890  -4.100  -2.008 0.50 42.75  ? 26  SER   C CB  1 
ATOM   5354 C  CB  B SER   C  1  13  ? -8.935  -4.119  -1.965 0.50 50.21  ? 26  SER   C CB  1 
ATOM   5355 O  OG  A SER   C  1  13  ? -7.976  -5.115  -1.618 0.50 39.87  ? 26  SER   C OG  1 
ATOM   5356 O  OG  B SER   C  1  13  ? -9.046  -4.513  -3.326 0.50 58.90  ? 26  SER   C OG  1 
ATOM   5357 N  N   . PHE   C  1  14  ? -10.269 -1.364  -1.885 1.00 35.96  ? 27  PHE   C N   1 
ATOM   5358 C  CA  . PHE   C  1  14  ? -11.201 -0.364  -2.375 1.00 34.72  ? 27  PHE   C CA  1 
ATOM   5359 C  C   . PHE   C  1  14  ? -11.105 0.867   -1.484 1.00 33.52  ? 27  PHE   C C   1 
ATOM   5360 O  O   . PHE   C  1  14  ? -11.297 0.741   -0.279 1.00 33.42  ? 27  PHE   C O   1 
ATOM   5361 C  CB  . PHE   C  1  14  ? -12.617 -0.963  -2.379 1.00 34.77  ? 27  PHE   C CB  1 
ATOM   5362 C  CG  . PHE   C  1  14  ? -13.665 0.047   -2.810 1.00 36.13  ? 27  PHE   C CG  1 
ATOM   5363 C  CD1 . PHE   C  1  14  ? -13.724 0.495   -4.123 1.00 39.94  ? 27  PHE   C CD1 1 
ATOM   5364 C  CD2 . PHE   C  1  14  ? -14.590 0.550   -1.899 1.00 40.83  ? 27  PHE   C CD2 1 
ATOM   5365 C  CE1 . PHE   C  1  14  ? -14.691 1.423   -4.513 1.00 39.04  ? 27  PHE   C CE1 1 
ATOM   5366 C  CE2 . PHE   C  1  14  ? -15.549 1.483   -2.289 1.00 42.95  ? 27  PHE   C CE2 1 
ATOM   5367 C  CZ  . PHE   C  1  14  ? -15.601 1.921   -3.594 1.00 37.04  ? 27  PHE   C CZ  1 
ATOM   5368 N  N   . THR   C  1  15  ? -10.883 2.046   -2.075 1.00 31.14  ? 28  THR   C N   1 
ATOM   5369 C  CA  . THR   C  1  15  ? -10.688 3.271   -1.313 1.00 32.96  ? 28  THR   C CA  1 
ATOM   5370 C  C   . THR   C  1  15  ? -11.780 4.291   -1.593 1.00 32.41  ? 28  THR   C C   1 
ATOM   5371 O  O   . THR   C  1  15  ? -11.607 5.461   -1.267 1.00 31.99  ? 28  THR   C O   1 
ATOM   5372 C  CB  . THR   C  1  15  ? -9.328  3.911   -1.625 1.00 38.02  ? 28  THR   C CB  1 
ATOM   5373 O  OG1 . THR   C  1  15  ? -9.328  4.461   -2.946 1.00 36.96  ? 28  THR   C OG1 1 
ATOM   5374 C  CG2 . THR   C  1  15  ? -8.165  2.957   -1.403 1.00 39.90  ? 28  THR   C CG2 1 
ATOM   5375 N  N   . GLY   C  1  16  ? -12.883 3.888   -2.223 1.00 32.85  ? 29  GLY   C N   1 
ATOM   5376 C  CA  . GLY   C  1  16  ? -13.985 4.810   -2.461 1.00 32.18  ? 29  GLY   C CA  1 
ATOM   5377 C  C   . GLY   C  1  16  ? -14.950 4.879   -1.274 1.00 39.25  ? 29  GLY   C C   1 
ATOM   5378 O  O   . GLY   C  1  16  ? -14.739 4.204   -0.267 1.00 39.64  ? 29  GLY   C O   1 
ATOM   5379 N  N   . THR   C  1  17  ? -16.022 5.681   -1.416 1.00 41.58  ? 30  THR   C N   1 
ATOM   5380 C  CA  . THR   C  1  17  ? -17.090 5.754   -0.428 1.00 40.60  ? 30  THR   C CA  1 
ATOM   5381 C  C   . THR   C  1  17  ? -17.872 4.448   -0.414 1.00 41.63  ? 30  THR   C C   1 
ATOM   5382 O  O   . THR   C  1  17  ? -17.907 3.728   -1.403 1.00 41.79  ? 30  THR   C O   1 
ATOM   5383 C  CB  . THR   C  1  17  ? -18.037 6.929   -0.666 1.00 45.63  ? 30  THR   C CB  1 
ATOM   5384 O  OG1 . THR   C  1  17  ? -18.772 6.959   0.554  1.00 42.02  ? 30  THR   C OG1 1 
ATOM   5385 C  CG2 . THR   C  1  17  ? -18.953 6.733   -1.864 1.00 46.19  ? 30  THR   C CG2 1 
ATOM   5386 N  N   . LYS   C  1  18  ? -18.472 4.148   0.739  1.00 42.30  ? 31  LYS   C N   1 
ATOM   5387 C  CA  . LYS   C  1  18  ? -19.382 3.022   0.876  1.00 44.42  ? 31  LYS   C CA  1 
ATOM   5388 C  C   . LYS   C  1  18  ? -20.142 3.161   2.190  1.00 45.10  ? 31  LYS   C C   1 
ATOM   5389 O  O   . LYS   C  1  18  ? -19.733 3.918   3.074  1.00 44.33  ? 31  LYS   C O   1 
ATOM   5390 C  CB  . LYS   C  1  18  ? -18.681 1.664   0.848  1.00 43.23  ? 31  LYS   C CB  1 
ATOM   5391 C  CG  . LYS   C  1  18  ? -17.665 1.451   1.965  1.00 47.41  ? 31  LYS   C CG  1 
ATOM   5392 C  CD  . LYS   C  1  18  ? -17.020 0.069   1.984  1.00 50.38  ? 31  LYS   C CD  1 
ATOM   5393 C  CE  . LYS   C  1  18  ? -17.903 -0.974  2.568  1.00 54.57  ? 31  LYS   C CE  1 
ATOM   5394 N  NZ  . LYS   C  1  18  ? -17.264 -2.293  2.527  1.00 57.03  ? 31  LYS   C NZ  1 
ATOM   5395 N  N   . LEU   C  1  19  ? -21.230 2.394   2.305  1.00 44.01  ? 32  LEU   C N   1 
ATOM   5396 C  CA  . LEU   C  1  19  ? -22.013 2.342   3.524  1.00 43.03  ? 32  LEU   C CA  1 
ATOM   5397 C  C   . LEU   C  1  19  ? -21.176 1.618   4.573  1.00 38.24  ? 32  LEU   C C   1 
ATOM   5398 O  O   . LEU   C  1  19  ? -20.763 0.483   4.350  1.00 38.89  ? 32  LEU   C O   1 
ATOM   5399 C  CB  . LEU   C  1  19  ? -23.338 1.614   3.282  1.00 42.12  ? 32  LEU   C CB  1 
ATOM   5400 C  CG  . LEU   C  1  19  ? -24.206 1.384   4.524  1.00 46.14  ? 32  LEU   C CG  1 
ATOM   5401 C  CD1 . LEU   C  1  19  ? -24.675 2.708   5.092  1.00 42.86  ? 32  LEU   C CD1 1 
ATOM   5402 C  CD2 . LEU   C  1  19  ? -25.404 0.461   4.239  1.00 48.32  ? 32  LEU   C CD2 1 
ATOM   5403 N  N   . VAL   C  1  20  ? -20.952 2.264   5.719  1.00 38.29  ? 33  VAL   C N   1 
ATOM   5404 C  CA  . VAL   C  1  20  ? -20.181 1.605   6.765  1.00 40.76  ? 33  VAL   C CA  1 
ATOM   5405 C  C   . VAL   C  1  20  ? -21.073 1.246   7.941  1.00 40.18  ? 33  VAL   C C   1 
ATOM   5406 O  O   . VAL   C  1  20  ? -20.782 0.294   8.650  1.00 41.45  ? 33  VAL   C O   1 
ATOM   5407 C  CB  . VAL   C  1  20  ? -18.953 2.423   7.197  1.00 39.02  ? 33  VAL   C CB  1 
ATOM   5408 C  CG1 . VAL   C  1  20  ? -17.956 2.512   6.052  1.00 38.72  ? 33  VAL   C CG1 1 
ATOM   5409 C  CG2 . VAL   C  1  20  ? -19.306 3.805   7.712  1.00 39.62  ? 33  VAL   C CG2 1 
ATOM   5410 N  N   . ASN   C  1  21  ? -22.155 2.002   8.128  1.00 43.40  ? 34  ASN   C N   1 
ATOM   5411 C  CA  . ASN   C  1  21  ? -23.164 1.654   9.121  1.00 46.74  ? 34  ASN   C CA  1 
ATOM   5412 C  C   . ASN   C  1  21  ? -24.136 0.632   8.533  1.00 45.05  ? 34  ASN   C C   1 
ATOM   5413 O  O   . ASN   C  1  21  ? -25.239 0.983   8.142  1.00 49.19  ? 34  ASN   C O   1 
ATOM   5414 C  CB  . ASN   C  1  21  ? -23.870 2.918   9.590  1.00 43.69  ? 34  ASN   C CB  1 
ATOM   5415 C  CG  . ASN   C  1  21  ? -24.783 2.682   10.765 1.00 43.73  ? 34  ASN   C CG  1 
ATOM   5416 O  OD1 . ASN   C  1  21  ? -24.952 1.557   11.259 1.00 41.63  ? 34  ASN   C OD1 1 
ATOM   5417 N  ND2 . ASN   C  1  21  ? -25.388 3.769   11.210 1.00 41.97  ? 34  ASN   C ND2 1 
ATOM   5418 N  N   . ASP   C  1  22  ? -23.723 -0.634  8.472  1.00 45.31  ? 35  ASP   C N   1 
ATOM   5419 C  CA  . ASP   C  1  22  ? -24.394 -1.631  7.648  1.00 46.52  ? 35  ASP   C CA  1 
ATOM   5420 C  C   . ASP   C  1  22  ? -24.818 -2.803  8.526  1.00 49.67  ? 35  ASP   C C   1 
ATOM   5421 O  O   . ASP   C  1  22  ? -24.564 -2.813  9.732  1.00 49.26  ? 35  ASP   C O   1 
ATOM   5422 C  CB  . ASP   C  1  22  ? -23.500 -2.034  6.480  1.00 52.25  ? 35  ASP   C CB  1 
ATOM   5423 C  CG  . ASP   C  1  22  ? -22.181 -2.753  6.788  1.00 62.62  ? 35  ASP   C CG  1 
ATOM   5424 O  OD1 . ASP   C  1  22  ? -21.926 -3.083  7.974  1.00 54.90  ? 35  ASP   C OD1 1 
ATOM   5425 O  OD2 . ASP   C  1  22  ? -21.403 -3.015  5.836  1.00 64.62  ? 35  ASP   C OD2 1 
ATOM   5426 N  N   . ALA   C  1  23  ? -25.410 -3.822  7.904  1.00 55.53  ? 36  ALA   C N   1 
ATOM   5427 C  CA  . ALA   C  1  23  ? -26.042 -4.910  8.639  1.00 62.06  ? 36  ALA   C CA  1 
ATOM   5428 C  C   . ALA   C  1  23  ? -25.010 -5.738  9.405  1.00 55.30  ? 36  ALA   C C   1 
ATOM   5429 O  O   . ALA   C  1  23  ? -25.295 -6.240  10.490 1.00 53.61  ? 36  ALA   C O   1 
ATOM   5430 C  CB  . ALA   C  1  23  ? -26.845 -5.793  7.701  1.00 61.10  ? 36  ALA   C CB  1 
ATOM   5431 N  N   . ASP   C  1  24  ? -23.814 -5.877  8.841  1.00 53.42  ? 37  ASP   C N   1 
ATOM   5432 C  CA  . ASP   C  1  24  ? -22.768 -6.674  9.464  1.00 57.75  ? 37  ASP   C CA  1 
ATOM   5433 C  C   . ASP   C  1  24  ? -22.092 -5.929  10.626 1.00 46.85  ? 37  ASP   C C   1 
ATOM   5434 O  O   . ASP   C  1  24  ? -21.359 -6.549  11.380 1.00 43.30  ? 37  ASP   C O   1 
ATOM   5435 C  CB  . ASP   C  1  24  ? -21.737 -7.140  8.445  1.00 69.67  ? 37  ASP   C CB  1 
ATOM   5436 C  CG  . ASP   C  1  24  ? -22.135 -8.352  7.611  1.00 79.57  ? 37  ASP   C CG  1 
ATOM   5437 O  OD1 . ASP   C  1  24  ? -22.811 -9.250  8.150  1.00 87.14  ? 37  ASP   C OD1 1 
ATOM   5438 O  OD2 . ASP   C  1  24  ? -21.734 -8.405  6.439  1.00 87.45  ? 37  ASP   C OD2 1 
ATOM   5439 N  N   . HIS   C  1  25  ? -22.334 -4.614  10.770 1.00 37.42  ? 38  HIS   C N   1 
ATOM   5440 C  CA  . HIS   C  1  25  ? -21.621 -3.770  11.719 1.00 37.00  ? 38  HIS   C CA  1 
ATOM   5441 C  C   . HIS   C  1  25  ? -22.633 -2.923  12.485 1.00 36.53  ? 38  HIS   C C   1 
ATOM   5442 O  O   . HIS   C  1  25  ? -22.611 -1.679  12.463 1.00 34.08  ? 38  HIS   C O   1 
ATOM   5443 C  CB  . HIS   C  1  25  ? -20.547 -2.931  11.006 1.00 41.19  ? 38  HIS   C CB  1 
ATOM   5444 C  CG  . HIS   C  1  25  ? -19.484 -3.744  10.343 1.00 41.80  ? 38  HIS   C CG  1 
ATOM   5445 N  ND1 . HIS   C  1  25  ? -19.419 -3.946  8.979  1.00 46.81  ? 38  HIS   C ND1 1 
ATOM   5446 C  CD2 . HIS   C  1  25  ? -18.415 -4.372  10.862 1.00 45.03  ? 38  HIS   C CD2 1 
ATOM   5447 C  CE1 . HIS   C  1  25  ? -18.361 -4.701  8.708  1.00 48.67  ? 38  HIS   C CE1 1 
ATOM   5448 N  NE2 . HIS   C  1  25  ? -17.727 -4.959  9.838  1.00 48.82  ? 38  HIS   C NE2 1 
ATOM   5449 N  N   . PRO   C  1  26  ? -23.574 -3.582  13.194 1.00 36.27  ? 39  PRO   C N   1 
ATOM   5450 C  CA  . PRO   C  1  26  ? -24.579 -2.858  13.967 1.00 38.31  ? 39  PRO   C CA  1 
ATOM   5451 C  C   . PRO   C  1  26  ? -23.993 -2.253  15.242 1.00 41.23  ? 39  PRO   C C   1 
ATOM   5452 O  O   . PRO   C  1  26  ? -23.174 -2.865  15.917 1.00 37.82  ? 39  PRO   C O   1 
ATOM   5453 C  CB  . PRO   C  1  26  ? -25.601 -3.947  14.320 1.00 35.04  ? 39  PRO   C CB  1 
ATOM   5454 C  CG  . PRO   C  1  26  ? -24.776 -5.225  14.390 1.00 36.76  ? 39  PRO   C CG  1 
ATOM   5455 C  CD  . PRO   C  1  26  ? -23.680 -5.052  13.339 1.00 36.19  ? 39  PRO   C CD  1 
ATOM   5456 N  N   . TRP   C  1  27  ? -24.463 -1.060  15.589 1.00 39.02  ? 40  TRP   C N   1 
ATOM   5457 C  CA  . TRP   C  1  27  ? -24.162 -0.521  16.891 1.00 40.06  ? 40  TRP   C CA  1 
ATOM   5458 C  C   . TRP   C  1  27  ? -24.780 -1.432  17.943 1.00 43.98  ? 40  TRP   C C   1 
ATOM   5459 O  O   . TRP   C  1  27  ? -25.897 -1.917  17.776 1.00 47.30  ? 40  TRP   C O   1 
ATOM   5460 C  CB  . TRP   C  1  27  ? -24.708 0.897   17.012 1.00 38.30  ? 40  TRP   C CB  1 
ATOM   5461 C  CG  . TRP   C  1  27  ? -24.349 1.525   18.329 1.00 47.03  ? 40  TRP   C CG  1 
ATOM   5462 C  CD1 . TRP   C  1  27  ? -23.277 2.303   18.616 1.00 42.14  ? 40  TRP   C CD1 1 
ATOM   5463 C  CD2 . TRP   C  1  27  ? -25.119 1.443   19.542 1.00 51.06  ? 40  TRP   C CD2 1 
ATOM   5464 N  NE1 . TRP   C  1  27  ? -23.323 2.718   19.916 1.00 49.41  ? 40  TRP   C NE1 1 
ATOM   5465 C  CE2 . TRP   C  1  27  ? -24.433 2.201   20.515 1.00 54.90  ? 40  TRP   C CE2 1 
ATOM   5466 C  CE3 . TRP   C  1  27  ? -26.309 0.807   19.898 1.00 53.24  ? 40  TRP   C CE3 1 
ATOM   5467 C  CZ2 . TRP   C  1  27  ? -24.894 2.348   21.820 1.00 51.15  ? 40  TRP   C CZ2 1 
ATOM   5468 C  CZ3 . TRP   C  1  27  ? -26.757 0.929   21.191 1.00 55.86  ? 40  TRP   C CZ3 1 
ATOM   5469 C  CH2 . TRP   C  1  27  ? -26.056 1.684   22.141 1.00 52.48  ? 40  TRP   C CH2 1 
ATOM   5470 N  N   . GLN   C  1  28  ? -24.037 -1.676  19.016 1.00 41.19  ? 41  GLN   C N   1 
ATOM   5471 C  CA  . GLN   C  1  28  ? -24.547 -2.413  20.154 1.00 42.31  ? 41  GLN   C CA  1 
ATOM   5472 C  C   . GLN   C  1  28  ? -24.066 -1.723  21.422 1.00 44.80  ? 41  GLN   C C   1 
ATOM   5473 O  O   . GLN   C  1  28  ? -22.994 -1.125  21.445 1.00 45.99  ? 41  GLN   C O   1 
ATOM   5474 C  CB  . GLN   C  1  28  ? -24.078 -3.860  20.143 1.00 37.90  ? 41  GLN   C CB  1 
ATOM   5475 C  CG  . GLN   C  1  28  ? -24.607 -4.656  18.964 1.00 39.25  ? 41  GLN   C CG  1 
ATOM   5476 C  CD  . GLN   C  1  28  ? -24.069 -6.072  18.903 1.00 42.58  ? 41  GLN   C CD  1 
ATOM   5477 O  OE1 . GLN   C  1  28  ? -23.276 -6.520  19.734 1.00 44.06  ? 41  GLN   C OE1 1 
ATOM   5478 N  NE2 . GLN   C  1  28  ? -24.470 -6.801  17.879 1.00 46.75  ? 41  GLN   C NE2 1 
ATOM   5479 N  N   . PRO   C  1  29  ? -24.863 -1.764  22.505 1.00 51.82  ? 42  PRO   C N   1 
ATOM   5480 C  CA  . PRO   C  1  29  ? -24.481 -1.102  23.753 1.00 47.57  ? 42  PRO   C CA  1 
ATOM   5481 C  C   . PRO   C  1  29  ? -23.305 -1.797  24.419 1.00 38.12  ? 42  PRO   C C   1 
ATOM   5482 O  O   . PRO   C  1  29  ? -23.060 -2.989  24.169 1.00 37.42  ? 42  PRO   C O   1 
ATOM   5483 C  CB  . PRO   C  1  29  ? -25.750 -1.160  24.608 1.00 55.53  ? 42  PRO   C CB  1 
ATOM   5484 C  CG  . PRO   C  1  29  ? -26.554 -2.323  24.027 1.00 59.97  ? 42  PRO   C CG  1 
ATOM   5485 C  CD  . PRO   C  1  29  ? -26.169 -2.434  22.563 1.00 56.12  ? 42  PRO   C CD  1 
ATOM   5486 N  N   . LEU   C  1  30  ? -22.591 -1.028  25.249 1.00 32.49  ? 43  LEU   C N   1 
ATOM   5487 C  CA  . LEU   C  1  30  ? -21.508 -1.544  26.068 1.00 37.16  ? 43  LEU   C CA  1 
ATOM   5488 C  C   . LEU   C  1  30  ? -21.985 -2.638  27.017 1.00 38.14  ? 43  LEU   C C   1 
ATOM   5489 O  O   . LEU   C  1  30  ? -23.047 -2.516  27.622 1.00 42.53  ? 43  LEU   C O   1 
ATOM   5490 C  CB  . LEU   C  1  30  ? -20.931 -0.379  26.862 1.00 41.58  ? 43  LEU   C CB  1 
ATOM   5491 C  CG  . LEU   C  1  30  ? -20.350 0.772   26.044 1.00 47.73  ? 43  LEU   C CG  1 
ATOM   5492 C  CD1 . LEU   C  1  30  ? -19.876 1.899   26.937 1.00 47.64  ? 43  LEU   C CD1 1 
ATOM   5493 C  CD2 . LEU   C  1  30  ? -19.222 0.223   25.175 1.00 48.86  ? 43  LEU   C CD2 1 
ATOM   5494 N  N   . ARG   C  1  31  ? -21.194 -3.701  27.108 1.00 39.50  ? 44  ARG   C N   1 
ATOM   5495 C  CA  . ARG   C  1  31  ? -21.344 -4.729  28.118 1.00 43.49  ? 44  ARG   C CA  1 
ATOM   5496 C  C   . ARG   C  1  31  ? -20.318 -4.465  29.225 1.00 45.74  ? 44  ARG   C C   1 
ATOM   5497 O  O   . ARG   C  1  31  ? -19.364 -3.723  29.034 1.00 48.35  ? 44  ARG   C O   1 
ATOM   5498 C  CB  . ARG   C  1  31  ? -21.115 -6.138  27.567 1.00 44.50  ? 44  ARG   C CB  1 
ATOM   5499 C  CG  . ARG   C  1  31  ? -21.995 -6.581  26.411 1.00 59.60  ? 44  ARG   C CG  1 
ATOM   5500 C  CD  . ARG   C  1  31  ? -21.353 -7.787  25.709 1.00 69.20  ? 44  ARG   C CD  1 
ATOM   5501 N  NE  . ARG   C  1  31  ? -20.045 -7.348  25.192 1.00 90.27  ? 44  ARG   C NE  1 
ATOM   5502 C  CZ  . ARG   C  1  31  ? -19.101 -8.070  24.562 1.00 85.50  ? 44  ARG   C CZ  1 
ATOM   5503 N  NH1 . ARG   C  1  31  ? -19.319 -9.339  24.259 1.00 95.51  ? 44  ARG   C NH1 1 
ATOM   5504 N  NH2 . ARG   C  1  31  ? -17.932 -7.523  24.234 1.00 69.84  ? 44  ARG   C NH2 1 
ATOM   5505 N  N   . GLU   C  1  32  ? -20.534 -5.054  30.406 1.00 45.68  ? 45  GLU   C N   1 
ATOM   5506 C  CA  . GLU   C  1  32  ? -19.557 -5.024  31.485 1.00 47.62  ? 45  GLU   C CA  1 
ATOM   5507 C  C   . GLU   C  1  32  ? -18.223 -5.544  30.942 1.00 45.70  ? 45  GLU   C C   1 
ATOM   5508 O  O   . GLU   C  1  32  ? -18.195 -6.598  30.314 1.00 44.55  ? 45  GLU   C O   1 
ATOM   5509 C  CB  . GLU   C  1  32  ? -20.091 -5.898  32.628 1.00 47.46  ? 45  GLU   C CB  1 
ATOM   5510 C  CG  . GLU   C  1  32  ? -19.206 -5.951  33.875 1.00 51.73  ? 45  GLU   C CG  1 
ATOM   5511 C  CD  . GLU   C  1  32  ? -18.971 -4.609  34.570 1.00 57.03  ? 45  GLU   C CD  1 
ATOM   5512 O  OE1 . GLU   C  1  32  ? -19.925 -3.790  34.642 1.00 57.37  ? 45  GLU   C OE1 1 
ATOM   5513 O  OE2 . GLU   C  1  32  ? -17.823 -4.377  35.027 1.00 60.19  ? 45  GLU   C OE2 1 
ATOM   5514 N  N   . GLY   C  1  33  ? -17.131 -4.817  31.201 1.00 47.37  ? 46  GLY   C N   1 
ATOM   5515 C  CA  . GLY   C  1  33  ? -15.805 -5.271  30.809 1.00 50.15  ? 46  GLY   C CA  1 
ATOM   5516 C  C   . GLY   C  1  33  ? -15.344 -4.699  29.466 1.00 49.13  ? 46  GLY   C C   1 
ATOM   5517 O  O   . GLY   C  1  33  ? -14.149 -4.752  29.159 1.00 52.75  ? 46  GLY   C O   1 
ATOM   5518 N  N   . ASP   C  1  34  ? -16.282 -4.167  28.670 1.00 47.03  ? 47  ASP   C N   1 
ATOM   5519 C  CA  . ASP   C  1  34  ? -15.949 -3.494  27.416 1.00 49.05  ? 47  ASP   C CA  1 
ATOM   5520 C  C   . ASP   C  1  34  ? -15.193 -2.206  27.722 1.00 45.79  ? 47  ASP   C C   1 
ATOM   5521 O  O   . ASP   C  1  34  ? -15.558 -1.475  28.626 1.00 40.74  ? 47  ASP   C O   1 
ATOM   5522 C  CB  . ASP   C  1  34  ? -17.169 -3.162  26.561 1.00 43.86  ? 47  ASP   C CB  1 
ATOM   5523 C  CG  . ASP   C  1  34  ? -17.860 -4.338  25.878 1.00 47.69  ? 47  ASP   C CG  1 
ATOM   5524 O  OD1 . ASP   C  1  34  ? -17.290 -5.456  25.917 1.00 43.99  ? 47  ASP   C OD1 1 
ATOM   5525 O  OD2 . ASP   C  1  34  ? -18.971 -4.139  25.312 1.00 46.65  ? 47  ASP   C OD2 1 
ATOM   5526 N  N   . ILE   C  1  35  ? -14.141 -1.941  26.937 1.00 44.38  ? 48  ILE   C N   1 
ATOM   5527 C  CA  . ILE   C  1  35  ? -13.289 -0.793  27.162 1.00 38.59  ? 48  ILE   C CA  1 
ATOM   5528 C  C   . ILE   C  1  35  ? -13.520 0.249   26.078 1.00 36.17  ? 48  ILE   C C   1 
ATOM   5529 O  O   . ILE   C  1  35  ? -13.602 -0.060  24.902 1.00 33.16  ? 48  ILE   C O   1 
ATOM   5530 C  CB  . ILE   C  1  35  ? -11.827 -1.249  27.242 1.00 43.78  ? 48  ILE   C CB  1 
ATOM   5531 C  CG1 . ILE   C  1  35  ? -11.643 -2.152  28.472 1.00 50.91  ? 48  ILE   C CG1 1 
ATOM   5532 C  CG2 . ILE   C  1  35  ? -10.889 -0.045  27.275 1.00 41.17  ? 48  ILE   C CG2 1 
ATOM   5533 C  CD1 . ILE   C  1  35  ? -10.348 -2.910  28.503 1.00 68.17  ? 48  ILE   C CD1 1 
ATOM   5534 N  N   . ARG   C  1  36  ? -13.614 1.498   26.505 1.00 33.58  ? 49  ARG   C N   1 
ATOM   5535 C  CA  . ARG   C  1  36  ? -13.666 2.625   25.603 1.00 35.50  ? 49  ARG   C CA  1 
ATOM   5536 C  C   . ARG   C  1  36  ? -12.766 3.702   26.191 1.00 34.03  ? 49  ARG   C C   1 
ATOM   5537 O  O   . ARG   C  1  36  ? -12.442 3.642   27.356 1.00 34.45  ? 49  ARG   C O   1 
ATOM   5538 C  CB  . ARG   C  1  36  ? -15.105 3.135   25.459 1.00 36.62  ? 49  ARG   C CB  1 
ATOM   5539 C  CG  . ARG   C  1  36  ? -16.045 2.109   24.854 1.00 34.34  ? 49  ARG   C CG  1 
ATOM   5540 C  CD  . ARG   C  1  36  ? -15.740 1.873   23.402 1.00 36.73  ? 49  ARG   C CD  1 
ATOM   5541 N  NE  . ARG   C  1  36  ? -16.670 0.954   22.750 1.00 32.56  ? 49  ARG   C NE  1 
ATOM   5542 C  CZ  . ARG   C  1  36  ? -16.629 -0.362  22.831 1.00 32.34  ? 49  ARG   C CZ  1 
ATOM   5543 N  NH1 . ARG   C  1  36  ? -15.680 -0.982  23.501 1.00 33.19  ? 49  ARG   C NH1 1 
ATOM   5544 N  NH2 . ARG   C  1  36  ? -17.554 -1.076  22.228 1.00 34.46  ? 49  ARG   C NH2 1 
ATOM   5545 N  N   . GLY   C  1  37  ? -12.365 4.678   25.375 1.00 36.34  ? 50  GLY   C N   1 
ATOM   5546 C  CA  . GLY   C  1  37  ? -11.312 5.590   25.760 1.00 33.74  ? 50  GLY   C CA  1 
ATOM   5547 C  C   . GLY   C  1  37  ? -11.480 6.974   25.162 1.00 33.00  ? 50  GLY   C C   1 
ATOM   5548 O  O   . GLY   C  1  37  ? -12.577 7.386   24.816 1.00 35.71  ? 50  GLY   C O   1 
ATOM   5549 N  N   . PRO   C  1  38  ? -10.369 7.712   24.997 1.00 30.54  ? 51  PRO   C N   1 
ATOM   5550 C  CA  . PRO   C  1  38  ? -10.420 9.115   24.598 1.00 32.03  ? 51  PRO   C CA  1 
ATOM   5551 C  C   . PRO   C  1  38  ? -10.626 9.368   23.105 1.00 31.11  ? 51  PRO   C C   1 
ATOM   5552 O  O   . PRO   C  1  38  ? -10.781 10.524  22.709 1.00 31.78  ? 51  PRO   C O   1 
ATOM   5553 C  CB  . PRO   C  1  38  ? -9.059  9.616   25.044 1.00 32.05  ? 51  PRO   C CB  1 
ATOM   5554 C  CG  . PRO   C  1  38  ? -8.154  8.432   24.802 1.00 33.62  ? 51  PRO   C CG  1 
ATOM   5555 C  CD  . PRO   C  1  38  ? -9.001  7.189   25.081 1.00 33.32  ? 51  PRO   C CD  1 
ATOM   5556 N  N   . CYS   C  1  39  ? -10.619 8.303   22.297 1.00 31.98  ? 52  CYS   C N   1 
ATOM   5557 C  CA  . CYS   C  1  39  ? -10.743 8.441   20.846 1.00 34.16  ? 52  CYS   C CA  1 
ATOM   5558 C  C   . CYS   C  1  39  ? -12.154 8.110   20.355 1.00 30.94  ? 52  CYS   C C   1 
ATOM   5559 O  O   . CYS   C  1  39  ? -12.605 6.955   20.402 1.00 29.27  ? 52  CYS   C O   1 
ATOM   5560 C  CB  . CYS   C  1  39  ? -9.806  7.504   20.099 1.00 34.63  ? 52  CYS   C CB  1 
ATOM   5561 S  SG  . CYS   C  1  39  ? -9.804  7.794   18.312 1.00 36.18  ? 52  CYS   C SG  1 
ATOM   5562 N  N   . PRO   C  1  40  ? -12.906 9.100   19.845 1.00 31.00  ? 53  PRO   C N   1 
ATOM   5563 C  CA  . PRO   C  1  40  ? -14.244 8.838   19.323 1.00 35.19  ? 53  PRO   C CA  1 
ATOM   5564 C  C   . PRO   C  1  40  ? -14.217 7.918   18.103 1.00 36.96  ? 53  PRO   C C   1 
ATOM   5565 O  O   . PRO   C  1  40  ? -15.149 7.142   17.898 1.00 32.18  ? 53  PRO   C O   1 
ATOM   5566 C  CB  . PRO   C  1  40  ? -14.795 10.226  19.016 1.00 36.99  ? 53  PRO   C CB  1 
ATOM   5567 C  CG  . PRO   C  1  40  ? -13.590 11.076  18.801 1.00 35.41  ? 53  PRO   C CG  1 
ATOM   5568 C  CD  . PRO   C  1  40  ? -12.526 10.510  19.724 1.00 34.86  ? 53  PRO   C CD  1 
ATOM   5569 N  N   . GLY   C  1  41  ? -13.122 7.964   17.324 1.00 34.75  ? 54  GLY   C N   1 
ATOM   5570 C  CA  . GLY   C  1  41  ? -13.007 7.102   16.157 1.00 32.06  ? 54  GLY   C CA  1 
ATOM   5571 C  C   . GLY   C  1  41  ? -12.953 5.621   16.536 1.00 34.55  ? 54  GLY   C C   1 
ATOM   5572 O  O   . GLY   C  1  41  ? -13.811 4.835   16.123 1.00 35.54  ? 54  GLY   C O   1 
ATOM   5573 N  N   . LEU   C  1  42  ? -11.966 5.255   17.360 1.00 33.81  ? 55  LEU   C N   1 
ATOM   5574 C  CA  . LEU   C  1  42  ? -11.802 3.882   17.807 1.00 34.40  ? 55  LEU   C CA  1 
ATOM   5575 C  C   . LEU   C  1  42  ? -13.024 3.427   18.603 1.00 35.53  ? 55  LEU   C C   1 
ATOM   5576 O  O   . LEU   C  1  42  ? -13.462 2.281   18.482 1.00 35.13  ? 55  LEU   C O   1 
ATOM   5577 C  CB  . LEU   C  1  42  ? -10.517 3.742   18.619 1.00 33.69  ? 55  LEU   C CB  1 
ATOM   5578 C  CG  . LEU   C  1  42  ? -9.224  4.125   17.890 1.00 36.96  ? 55  LEU   C CG  1 
ATOM   5579 C  CD1 . LEU   C  1  42  ? -8.043  3.957   18.820 1.00 41.17  ? 55  LEU   C CD1 1 
ATOM   5580 C  CD2 . LEU   C  1  42  ? -9.021  3.281   16.650 1.00 35.59  ? 55  LEU   C CD2 1 
ATOM   5581 N  N   . ASN   C  1  43  ? -13.557 4.324   19.433 1.00 33.90  ? 56  ASN   C N   1 
ATOM   5582 C  CA  . ASN   C  1  43  ? -14.747 4.006   20.206 1.00 38.16  ? 56  ASN   C CA  1 
ATOM   5583 C  C   . ASN   C  1  43  ? -15.899 3.594   19.284 1.00 38.82  ? 56  ASN   C C   1 
ATOM   5584 O  O   . ASN   C  1  43  ? -16.556 2.568   19.513 1.00 33.25  ? 56  ASN   C O   1 
ATOM   5585 C  CB  . ASN   C  1  43  ? -15.172 5.183   21.069 1.00 36.90  ? 56  ASN   C CB  1 
ATOM   5586 C  CG  . ASN   C  1  43  ? -14.274 5.389   22.271 1.00 38.93  ? 56  ASN   C CG  1 
ATOM   5587 O  OD1 . ASN   C  1  43  ? -13.450 4.523   22.621 1.00 36.01  ? 56  ASN   C OD1 1 
ATOM   5588 N  ND2 . ASN   C  1  43  ? -14.437 6.536   22.917 1.00 34.87  ? 56  ASN   C ND2 1 
ATOM   5589 N  N   . THR   C  1  44  ? -16.125 4.386   18.228 1.00 33.23  ? 57  THR   C N   1 
ATOM   5590 C  CA  . THR   C  1  44  ? -17.217 4.094   17.311 1.00 33.39  ? 57  THR   C CA  1 
ATOM   5591 C  C   . THR   C  1  44  ? -16.960 2.778   16.588 1.00 35.34  ? 57  THR   C C   1 
ATOM   5592 O  O   . THR   C  1  44  ? -17.867 1.962   16.451 1.00 34.61  ? 57  THR   C O   1 
ATOM   5593 C  CB  . THR   C  1  44  ? -17.409 5.249   16.344 1.00 36.94  ? 57  THR   C CB  1 
ATOM   5594 O  OG1 . THR   C  1  44  ? -17.724 6.378   17.155 1.00 32.03  ? 57  THR   C OG1 1 
ATOM   5595 C  CG2 . THR   C  1  44  ? -18.511 4.966   15.343 1.00 38.16  ? 57  THR   C CG2 1 
ATOM   5596 N  N   . LEU   C  1  45  ? -15.713 2.547   16.175 1.00 33.13  ? 58  LEU   C N   1 
ATOM   5597 C  CA  . LEU   C  1  45  ? -15.389 1.312   15.497 1.00 32.38  ? 58  LEU   C CA  1 
ATOM   5598 C  C   . LEU   C  1  45  ? -15.630 0.108   16.397 1.00 32.08  ? 58  LEU   C C   1 
ATOM   5599 O  O   . LEU   C  1  45  ? -16.137 -0.927  15.951 1.00 37.57  ? 58  LEU   C O   1 
ATOM   5600 C  CB  . LEU   C  1  45  ? -13.945 1.380   14.999 1.00 32.61  ? 58  LEU   C CB  1 
ATOM   5601 C  CG  . LEU   C  1  45  ? -13.710 2.444   13.931 1.00 36.06  ? 58  LEU   C CG  1 
ATOM   5602 C  CD1 . LEU   C  1  45  ? -12.233 2.681   13.767 1.00 35.32  ? 58  LEU   C CD1 1 
ATOM   5603 C  CD2 . LEU   C  1  45  ? -14.349 2.020   12.605 1.00 37.93  ? 58  LEU   C CD2 1 
ATOM   5604 N  N   . ALA   C  1  46  ? -15.247 0.206   17.671 1.00 33.12  ? 59  ALA   C N   1 
ATOM   5605 C  CA  . ALA   C  1  46  ? -15.478 -0.912  18.574 1.00 35.67  ? 59  ALA   C CA  1 
ATOM   5606 C  C   . ALA   C  1  46  ? -16.982 -1.153  18.772 1.00 34.11  ? 59  ALA   C C   1 
ATOM   5607 O  O   . ALA   C  1  46  ? -17.437 -2.291  18.806 1.00 33.98  ? 59  ALA   C O   1 
ATOM   5608 C  CB  . ALA   C  1  46  ? -14.773 -0.642  19.884 1.00 37.29  ? 59  ALA   C CB  1 
ATOM   5609 N  N   . SER   C  1  47  ? -17.758 -0.074  18.903 1.00 32.17  ? 60  SER   C N   1 
ATOM   5610 C  CA  . SER   C  1  47  ? -19.176 -0.207  19.192 1.00 39.85  ? 60  SER   C CA  1 
ATOM   5611 C  C   . SER   C  1  47  ? -19.987 -0.656  17.971 1.00 42.48  ? 60  SER   C C   1 
ATOM   5612 O  O   . SER   C  1  47  ? -21.127 -1.076  18.151 1.00 35.67  ? 60  SER   C O   1 
ATOM   5613 C  CB  . SER   C  1  47  ? -19.719 1.069   19.781 1.00 35.91  ? 60  SER   C CB  1 
ATOM   5614 O  OG  . SER   C  1  47  ? -19.325 1.176   21.147 1.00 38.63  ? 60  SER   C OG  1 
ATOM   5615 N  N   . HIS   C  1  48  ? -19.401 -0.600  16.756 1.00 36.55  ? 61  HIS   C N   1 
ATOM   5616 C  CA  . HIS   C  1  48  ? -20.029 -1.178  15.574 1.00 37.87  ? 61  HIS   C CA  1 
ATOM   5617 C  C   . HIS   C  1  48  ? -19.388 -2.494  15.132 1.00 37.38  ? 61  HIS   C C   1 
ATOM   5618 O  O   . HIS   C  1  48  ? -19.746 -3.023  14.079 1.00 37.55  ? 61  HIS   C O   1 
ATOM   5619 C  CB  . HIS   C  1  48  ? -20.014 -0.205  14.406 1.00 35.90  ? 61  HIS   C CB  1 
ATOM   5620 C  CG  . HIS   C  1  48  ? -21.027 0.871   14.503 1.00 36.53  ? 61  HIS   C CG  1 
ATOM   5621 N  ND1 . HIS   C  1  48  ? -22.235 0.786   13.831 1.00 36.39  ? 61  HIS   C ND1 1 
ATOM   5622 C  CD2 . HIS   C  1  48  ? -21.001 2.061   15.131 1.00 34.43  ? 61  HIS   C CD2 1 
ATOM   5623 C  CE1 . HIS   C  1  48  ? -22.911 1.917   14.074 1.00 35.92  ? 61  HIS   C CE1 1 
ATOM   5624 N  NE2 . HIS   C  1  48  ? -22.179 2.712   14.845 1.00 31.66  ? 61  HIS   C NE2 1 
ATOM   5625 N  N   . GLY   C  1  49  ? -18.456 -3.037  15.919 1.00 34.92  ? 62  GLY   C N   1 
ATOM   5626 C  CA  . GLY   C  1  49  ? -17.866 -4.335  15.617 1.00 35.63  ? 62  GLY   C CA  1 
ATOM   5627 C  C   . GLY   C  1  49  ? -16.814 -4.298  14.501 1.00 34.57  ? 62  GLY   C C   1 
ATOM   5628 O  O   . GLY   C  1  49  ? -16.414 -5.350  14.023 1.00 34.22  ? 62  GLY   C O   1 
ATOM   5629 N  N   . TYR   C  1  50  ? -16.344 -3.113  14.090 1.00 37.21  ? 63  TYR   C N   1 
ATOM   5630 C  CA  . TYR   C  1  50  ? -15.179 -2.996  13.212 1.00 35.15  ? 63  TYR   C CA  1 
ATOM   5631 C  C   . TYR   C  1  50  ? -13.912 -3.415  13.959 1.00 35.38  ? 63  TYR   C C   1 
ATOM   5632 O  O   . TYR   C  1  50  ? -12.986 -3.931  13.347 1.00 39.87  ? 63  TYR   C O   1 
ATOM   5633 C  CB  . TYR   C  1  50  ? -15.057 -1.580  12.646 1.00 36.60  ? 63  TYR   C CB  1 
ATOM   5634 C  CG  . TYR   C  1  50  ? -15.974 -1.350  11.452 1.00 41.27  ? 63  TYR   C CG  1 
ATOM   5635 C  CD1 . TYR   C  1  50  ? -15.633 -1.825  10.195 1.00 43.00  ? 63  TYR   C CD1 1 
ATOM   5636 C  CD2 . TYR   C  1  50  ? -17.195 -0.702  11.578 1.00 39.19  ? 63  TYR   C CD2 1 
ATOM   5637 C  CE1 . TYR   C  1  50  ? -16.469 -1.657  9.100  1.00 45.49  ? 63  TYR   C CE1 1 
ATOM   5638 C  CE2 . TYR   C  1  50  ? -18.038 -0.515  10.494 1.00 40.14  ? 63  TYR   C CE2 1 
ATOM   5639 C  CZ  . TYR   C  1  50  ? -17.679 -0.998  9.250  1.00 43.89  ? 63  TYR   C CZ  1 
ATOM   5640 O  OH  . TYR   C  1  50  ? -18.504 -0.859  8.174  1.00 44.09  ? 63  TYR   C OH  1 
ATOM   5641 N  N   . LEU   C  1  51  ? -13.866 -3.115  15.260 1.00 38.89  ? 64  LEU   C N   1 
ATOM   5642 C  CA  . LEU   C  1  51  ? -12.892 -3.637  16.213 1.00 41.42  ? 64  LEU   C CA  1 
ATOM   5643 C  C   . LEU   C  1  51  ? -13.602 -4.643  17.102 1.00 40.34  ? 64  LEU   C C   1 
ATOM   5644 O  O   . LEU   C  1  51  ? -14.820 -4.565  17.224 1.00 46.39  ? 64  LEU   C O   1 
ATOM   5645 C  CB  . LEU   C  1  51  ? -12.327 -2.520  17.104 1.00 37.89  ? 64  LEU   C CB  1 
ATOM   5646 C  CG  . LEU   C  1  51  ? -11.430 -1.489  16.428 1.00 37.52  ? 64  LEU   C CG  1 
ATOM   5647 C  CD1 . LEU   C  1  51  ? -11.094 -0.305  17.284 1.00 38.35  ? 64  LEU   C CD1 1 
ATOM   5648 C  CD2 . LEU   C  1  51  ? -10.177 -2.199  15.983 1.00 39.03  ? 64  LEU   C CD2 1 
ATOM   5649 N  N   . PRO   C  1  52  ? -12.879 -5.532  17.820 1.00 40.91  ? 65  PRO   C N   1 
ATOM   5650 C  CA  . PRO   C  1  52  ? -13.490 -6.301  18.911 1.00 42.00  ? 65  PRO   C CA  1 
ATOM   5651 C  C   . PRO   C  1  52  ? -14.269 -5.373  19.849 1.00 42.00  ? 65  PRO   C C   1 
ATOM   5652 O  O   . PRO   C  1  52  ? -13.775 -4.310  20.236 1.00 41.50  ? 65  PRO   C O   1 
ATOM   5653 C  CB  . PRO   C  1  52  ? -12.278 -6.972  19.603 1.00 41.62  ? 65  PRO   C CB  1 
ATOM   5654 C  CG  . PRO   C  1  52  ? -11.244 -7.100  18.493 1.00 39.93  ? 65  PRO   C CG  1 
ATOM   5655 C  CD  . PRO   C  1  52  ? -11.453 -5.840  17.639 1.00 38.68  ? 65  PRO   C CD  1 
ATOM   5656 N  N   . ARG   C  1  53  ? -15.497 -5.774  20.203 1.00 41.99  ? 66  ARG   C N   1 
ATOM   5657 C  CA  . ARG   C  1  53  ? -16.417 -4.898  20.915 1.00 46.19  ? 66  ARG   C CA  1 
ATOM   5658 C  C   . ARG   C  1  53  ? -15.933 -4.627  22.347 1.00 41.49  ? 66  ARG   C C   1 
ATOM   5659 O  O   . ARG   C  1  53  ? -16.370 -3.647  22.968 1.00 37.70  ? 66  ARG   C O   1 
ATOM   5660 C  CB  . ARG   C  1  53  ? -17.828 -5.497  20.875 1.00 47.95  ? 66  ARG   C CB  1 
ATOM   5661 C  CG  . ARG   C  1  53  ? -18.398 -5.507  19.463 1.00 49.96  ? 66  ARG   C CG  1 
ATOM   5662 C  CD  . ARG   C  1  53  ? -19.818 -6.057  19.385 1.00 45.80  ? 66  ARG   C CD  1 
ATOM   5663 N  NE  . ARG   C  1  53  ? -20.359 -6.063  18.020 1.00 39.69  ? 66  ARG   C NE  1 
ATOM   5664 C  CZ  . ARG   C  1  53  ? -20.965 -5.043  17.451 1.00 37.31  ? 66  ARG   C CZ  1 
ATOM   5665 N  NH1 . ARG   C  1  53  ? -21.148 -3.895  18.100 1.00 34.53  ? 66  ARG   C NH1 1 
ATOM   5666 N  NH2 . ARG   C  1  53  ? -21.407 -5.162  16.211 1.00 43.32  ? 66  ARG   C NH2 1 
ATOM   5667 N  N   . ASP   C  1  54  ? -15.004 -5.457  22.847 1.00 34.38  ? 67  ASP   C N   1 
ATOM   5668 C  CA  . ASP   C  1  54  ? -14.451 -5.250  24.181 1.00 40.02  ? 67  ASP   C CA  1 
ATOM   5669 C  C   . ASP   C  1  54  ? -13.356 -4.178  24.205 1.00 39.14  ? 67  ASP   C C   1 
ATOM   5670 O  O   . ASP   C  1  54  ? -12.915 -3.787  25.283 1.00 35.72  ? 67  ASP   C O   1 
ATOM   5671 C  CB  . ASP   C  1  54  ? -13.958 -6.543  24.815 1.00 42.89  ? 67  ASP   C CB  1 
ATOM   5672 C  CG  . ASP   C  1  54  ? -12.770 -7.218  24.129 1.00 49.49  ? 67  ASP   C CG  1 
ATOM   5673 O  OD1 . ASP   C  1  54  ? -12.223 -6.645  23.144 1.00 53.00  ? 67  ASP   C OD1 1 
ATOM   5674 O  OD2 . ASP   C  1  54  ? -12.398 -8.318  24.590 1.00 50.02  ? 67  ASP   C OD2 1 
ATOM   5675 N  N   . GLY   C  1  55  ? -12.943 -3.669  23.037 1.00 37.40  ? 68  GLY   C N   1 
ATOM   5676 C  CA  . GLY   C  1  55  ? -12.091 -2.490  23.003 1.00 37.52  ? 68  GLY   C CA  1 
ATOM   5677 C  C   . GLY   C  1  55  ? -10.606 -2.814  23.204 1.00 32.93  ? 68  GLY   C C   1 
ATOM   5678 O  O   . GLY   C  1  55  ? -9.805  -1.930  23.478 1.00 36.56  ? 68  GLY   C O   1 
ATOM   5679 N  N   . VAL   C  1  56  ? -10.239 -4.075  22.998 1.00 32.53  ? 69  VAL   C N   1 
ATOM   5680 C  CA  . VAL   C  1  56  ? -8.859  -4.516  23.034 1.00 35.03  ? 69  VAL   C CA  1 
ATOM   5681 C  C   . VAL   C  1  56  ? -8.570  -5.201  21.704 1.00 36.06  ? 69  VAL   C C   1 
ATOM   5682 O  O   . VAL   C  1  56  ? -9.269  -6.138  21.331 1.00 36.62  ? 69  VAL   C O   1 
ATOM   5683 C  CB  . VAL   C  1  56  ? -8.640  -5.471  24.220 1.00 40.79  ? 69  VAL   C CB  1 
ATOM   5684 C  CG1 . VAL   C  1  56  ? -7.309  -6.211  24.159 1.00 42.20  ? 69  VAL   C CG1 1 
ATOM   5685 C  CG2 . VAL   C  1  56  ? -8.764  -4.713  25.532 1.00 43.52  ? 69  VAL   C CG2 1 
ATOM   5686 N  N   . ALA   C  1  57  ? -7.528  -4.728  21.010 1.00 34.01  ? 70  ALA   C N   1 
ATOM   5687 C  CA  . ALA   C  1  57  ? -7.269  -5.146  19.646 1.00 35.66  ? 70  ALA   C CA  1 
ATOM   5688 C  C   . ALA   C  1  57  ? -5.768  -5.199  19.366 1.00 32.97  ? 70  ALA   C C   1 
ATOM   5689 O  O   . ALA   C  1  57  ? -4.982  -4.602  20.092 1.00 31.54  ? 70  ALA   C O   1 
ATOM   5690 C  CB  . ALA   C  1  57  ? -7.972  -4.174  18.739 1.00 35.04  ? 70  ALA   C CB  1 
ATOM   5691 N  N   . THR   C  1  58  ? -5.393  -5.910  18.294 1.00 31.83  ? 71  THR   C N   1 
ATOM   5692 C  CA  . THR   C  1  58  ? -4.036  -5.879  17.771 1.00 29.58  ? 71  THR   C CA  1 
ATOM   5693 C  C   . THR   C  1  58  ? -3.869  -4.602  16.966 1.00 29.62  ? 71  THR   C C   1 
ATOM   5694 O  O   . THR   C  1  58  ? -4.842  -4.005  16.509 1.00 32.86  ? 71  THR   C O   1 
ATOM   5695 C  CB  . THR   C  1  58  ? -3.695  -7.085  16.905 1.00 31.31  ? 71  THR   C CB  1 
ATOM   5696 O  OG1 . THR   C  1  58  ? -4.445  -6.911  15.697 1.00 32.38  ? 71  THR   C OG1 1 
ATOM   5697 C  CG2 . THR   C  1  58  ? -3.979  -8.408  17.604 1.00 30.47  ? 71  THR   C CG2 1 
ATOM   5698 N  N   . PRO   C  1  59  ? -2.622  -4.133  16.787 1.00 31.67  ? 72  PRO   C N   1 
ATOM   5699 C  CA  . PRO   C  1  59  ? -2.370  -2.989  15.913 1.00 31.49  ? 72  PRO   C CA  1 
ATOM   5700 C  C   . PRO   C  1  59  ? -2.936  -3.206  14.514 1.00 28.38  ? 72  PRO   C C   1 
ATOM   5701 O  O   . PRO   C  1  59  ? -3.470  -2.294  13.908 1.00 26.83  ? 72  PRO   C O   1 
ATOM   5702 C  CB  . PRO   C  1  59  ? -0.847  -2.935  15.911 1.00 31.56  ? 72  PRO   C CB  1 
ATOM   5703 C  CG  . PRO   C  1  59  ? -0.453  -3.498  17.250 1.00 35.42  ? 72  PRO   C CG  1 
ATOM   5704 C  CD  . PRO   C  1  59  ? -1.411  -4.648  17.447 1.00 34.12  ? 72  PRO   C CD  1 
ATOM   5705 N  N   . ALA   C  1  60  ? -2.765  -4.415  13.991 1.00 29.66  ? 73  ALA   C N   1 
ATOM   5706 C  CA  . ALA   C  1  60  ? -3.253  -4.740  12.667 1.00 34.52  ? 73  ALA   C CA  1 
ATOM   5707 C  C   . ALA   C  1  60  ? -4.762  -4.548  12.601 1.00 33.28  ? 73  ALA   C C   1 
ATOM   5708 O  O   . ALA   C  1  60  ? -5.254  -4.020  11.619 1.00 29.17  ? 73  ALA   C O   1 
ATOM   5709 C  CB  . ALA   C  1  60  ? -2.877  -6.165  12.282 1.00 37.35  ? 73  ALA   C CB  1 
ATOM   5710 N  N   . GLN   C  1  61  ? -5.496  -5.002  13.620 1.00 30.90  ? 74  GLN   C N   1 
ATOM   5711 C  CA  . GLN   C  1  61  ? -6.940  -4.858  13.626 1.00 32.70  ? 74  GLN   C CA  1 
ATOM   5712 C  C   . GLN   C  1  61  ? -7.339  -3.389  13.652 1.00 32.71  ? 74  GLN   C C   1 
ATOM   5713 O  O   . GLN   C  1  61  ? -8.317  -3.021  13.017 1.00 34.43  ? 74  GLN   C O   1 
ATOM   5714 C  CB  . GLN   C  1  61  ? -7.587  -5.590  14.796 1.00 33.11  ? 74  GLN   C CB  1 
ATOM   5715 C  CG  . GLN   C  1  61  ? -7.561  -7.103  14.650 1.00 34.02  ? 74  GLN   C CG  1 
ATOM   5716 C  CD  . GLN   C  1  61  ? -7.957  -7.802  15.939 1.00 42.10  ? 74  GLN   C CD  1 
ATOM   5717 O  OE1 . GLN   C  1  61  ? -7.668  -7.364  17.063 1.00 37.44  ? 74  GLN   C OE1 1 
ATOM   5718 N  NE2 . GLN   C  1  61  ? -8.689  -8.888  15.785 1.00 48.27  ? 74  GLN   C NE2 1 
ATOM   5719 N  N   . ILE   C  1  62  ? -6.599  -2.568  14.395 1.00 30.51  ? 75  ILE   C N   1 
ATOM   5720 C  CA  . ILE   C  1  62  ? -6.922  -1.153  14.522 1.00 31.22  ? 75  ILE   C CA  1 
ATOM   5721 C  C   . ILE   C  1  62  ? -6.748  -0.486  13.158 1.00 34.17  ? 75  ILE   C C   1 
ATOM   5722 O  O   . ILE   C  1  62  ? -7.570  0.324   12.723 1.00 31.16  ? 75  ILE   C O   1 
ATOM   5723 C  CB  . ILE   C  1  62  ? -6.073  -0.501  15.630 1.00 28.46  ? 75  ILE   C CB  1 
ATOM   5724 C  CG1 . ILE   C  1  62  ? -6.485  -1.042  16.988 1.00 31.16  ? 75  ILE   C CG1 1 
ATOM   5725 C  CG2 . ILE   C  1  62  ? -6.153  1.025   15.584 1.00 27.15  ? 75  ILE   C CG2 1 
ATOM   5726 C  CD1 . ILE   C  1  62  ? -5.627  -0.575  18.149 1.00 33.51  ? 75  ILE   C CD1 1 
ATOM   5727 N  N   . ILE   C  1  63  ? -5.656  -0.838  12.476 1.00 33.02  ? 76  ILE   C N   1 
ATOM   5728 C  CA  . ILE   C  1  63  ? -5.365  -0.220  11.202 1.00 34.91  ? 76  ILE   C CA  1 
ATOM   5729 C  C   . ILE   C  1  63  ? -6.446  -0.590  10.193 1.00 31.44  ? 76  ILE   C C   1 
ATOM   5730 O  O   . ILE   C  1  63  ? -6.997  0.316   9.577  1.00 28.76  ? 76  ILE   C O   1 
ATOM   5731 C  CB  . ILE   C  1  63  ? -3.952  -0.570  10.724 1.00 38.16  ? 76  ILE   C CB  1 
ATOM   5732 C  CG1 . ILE   C  1  63  ? -2.933  0.164   11.575 1.00 37.12  ? 76  ILE   C CG1 1 
ATOM   5733 C  CG2 . ILE   C  1  63  ? -3.766  -0.269  9.230  1.00 37.02  ? 76  ILE   C CG2 1 
ATOM   5734 C  CD1 . ILE   C  1  63  ? -1.616  -0.560  11.633 1.00 39.68  ? 76  ILE   C CD1 1 
ATOM   5735 N  N   . THR   C  1  64  ? -6.796  -1.885  10.065 1.00 29.25  ? 77  THR   C N   1 
ATOM   5736 C  CA  A THR   C  1  64  ? -7.792  -2.281  9.094  0.50 28.74  ? 77  THR   C CA  1 
ATOM   5737 C  CA  B THR   C  1  64  ? -7.789  -2.252  9.062  0.50 28.42  ? 77  THR   C CA  1 
ATOM   5738 C  C   . THR   C  1  64  ? -9.131  -1.636  9.445  1.00 28.90  ? 77  THR   C C   1 
ATOM   5739 O  O   . THR   C  1  64  ? -9.827  -1.156  8.559  1.00 28.97  ? 77  THR   C O   1 
ATOM   5740 C  CB  A THR   C  1  64  ? -7.897  -3.802  9.028  0.50 29.58  ? 77  THR   C CB  1 
ATOM   5741 C  CB  B THR   C  1  64  ? -7.885  -3.732  8.649  0.50 29.88  ? 77  THR   C CB  1 
ATOM   5742 O  OG1 A THR   C  1  64  ? -8.354  -4.112  10.332 0.50 35.86  ? 77  THR   C OG1 1 
ATOM   5743 O  OG1 B THR   C  1  64  ? -9.231  -4.238  8.576  0.50 26.72  ? 77  THR   C OG1 1 
ATOM   5744 C  CG2 A THR   C  1  64  ? -6.588  -4.490  8.722  0.50 26.20  ? 77  THR   C CG2 1 
ATOM   5745 C  CG2 B THR   C  1  64  ? -7.026  -4.669  9.465  0.50 26.99  ? 77  THR   C CG2 1 
ATOM   5746 N  N   . ALA   C  1  65  ? -9.460  -1.572  10.747 1.00 30.87  ? 78  ALA   C N   1 
ATOM   5747 C  CA  . ALA   C  1  65  ? -10.712 -0.969  11.193 1.00 30.40  ? 78  ALA   C CA  1 
ATOM   5748 C  C   . ALA   C  1  65  ? -10.810 0.501   10.821 1.00 28.68  ? 78  ALA   C C   1 
ATOM   5749 O  O   . ALA   C  1  65  ? -11.872 0.939   10.374 1.00 32.94  ? 78  ALA   C O   1 
ATOM   5750 C  CB  . ALA   C  1  65  ? -10.926 -1.131  12.680 1.00 34.50  ? 78  ALA   C CB  1 
ATOM   5751 N  N   . THR   C  1  66  ? -9.756  1.285   11.052 1.00 30.51  ? 79  THR   C N   1 
ATOM   5752 C  CA  . THR   C  1  66  ? -9.827  2.718   10.768 1.00 29.40  ? 79  THR   C CA  1 
ATOM   5753 C  C   . THR   C  1  66  ? -9.947  2.930   9.254  1.00 32.35  ? 79  THR   C C   1 
ATOM   5754 O  O   . THR   C  1  66  ? -10.566 3.888   8.799  1.00 29.06  ? 79  THR   C O   1 
ATOM   5755 C  CB  . THR   C  1  66  ? -8.633  3.485   11.334 1.00 28.89  ? 79  THR   C CB  1 
ATOM   5756 O  OG1 . THR   C  1  66  ? -7.445  2.945   10.774 1.00 28.05  ? 79  THR   C OG1 1 
ATOM   5757 C  CG2 . THR   C  1  66  ? -8.560  3.391   12.843 1.00 29.74  ? 79  THR   C CG2 1 
ATOM   5758 N  N   . GLN   C  1  67  ? -9.354  2.033   8.465  1.00 32.70  ? 80  GLN   C N   1 
ATOM   5759 C  CA  . GLN   C  1  67  ? -9.466  2.109   7.014  1.00 36.21  ? 80  GLN   C CA  1 
ATOM   5760 C  C   . GLN   C  1  67  ? -10.870 1.702   6.548  1.00 35.26  ? 80  GLN   C C   1 
ATOM   5761 O  O   . GLN   C  1  67  ? -11.503 2.437   5.805  1.00 35.98  ? 80  GLN   C O   1 
ATOM   5762 C  CB  . GLN   C  1  67  ? -8.363  1.256   6.397  1.00 32.06  ? 80  GLN   C CB  1 
ATOM   5763 C  CG  . GLN   C  1  67  ? -6.979  1.837   6.663  1.00 32.79  ? 80  GLN   C CG  1 
ATOM   5764 C  CD  . GLN   C  1  67  ? -5.823  1.058   6.083  1.00 33.48  ? 80  GLN   C CD  1 
ATOM   5765 O  OE1 . GLN   C  1  67  ? -4.712  1.578   6.021  1.00 36.28  ? 80  GLN   C OE1 1 
ATOM   5766 N  NE2 . GLN   C  1  67  ? -6.029  -0.191  5.688  1.00 34.46  ? 80  GLN   C NE2 1 
ATOM   5767 N  N   . GLU   C  1  68  ? -11.342 0.530   6.976  1.00 32.59  ? 81  GLU   C N   1 
ATOM   5768 C  CA  . GLU   C  1  68  ? -12.619 0.019   6.521  1.00 37.56  ? 81  GLU   C CA  1 
ATOM   5769 C  C   . GLU   C  1  68  ? -13.736 0.972   6.960  1.00 37.73  ? 81  GLU   C C   1 
ATOM   5770 O  O   . GLU   C  1  68  ? -14.631 1.280   6.181  1.00 38.03  ? 81  GLU   C O   1 
ATOM   5771 C  CB  . GLU   C  1  68  ? -12.911 -1.357  7.113  1.00 42.54  ? 81  GLU   C CB  1 
ATOM   5772 C  CG  . GLU   C  1  68  ? -12.051 -2.493  6.570  1.00 56.21  ? 81  GLU   C CG  1 
ATOM   5773 C  CD  . GLU   C  1  68  ? -12.069 -2.688  5.064  1.00 70.92  ? 81  GLU   C CD  1 
ATOM   5774 O  OE1 . GLU   C  1  68  ? -10.969 -2.886  4.479  1.00 60.31  ? 81  GLU   C OE1 1 
ATOM   5775 O  OE2 . GLU   C  1  68  ? -13.186 -2.628  4.489  1.00 79.83  ? 81  GLU   C OE2 1 
ATOM   5776 N  N   . GLY   C  1  69  ? -13.684 1.442   8.209  1.00 33.21  ? 82  GLY   C N   1 
ATOM   5777 C  CA  . GLY   C  1  69  ? -14.773 2.203   8.790  1.00 30.98  ? 82  GLY   C CA  1 
ATOM   5778 C  C   . GLY   C  1  69  ? -14.786 3.671   8.391  1.00 29.72  ? 82  GLY   C C   1 
ATOM   5779 O  O   . GLY   C  1  69  ? -15.858 4.242   8.209  1.00 34.50  ? 82  GLY   C O   1 
ATOM   5780 N  N   . PHE   C  1  70  ? -13.624 4.296   8.259  1.00 26.89  ? 83  PHE   C N   1 
ATOM   5781 C  CA  . PHE   C  1  70  ? -13.582 5.740   8.045  1.00 31.06  ? 83  PHE   C CA  1 
ATOM   5782 C  C   . PHE   C  1  70  ? -12.733 6.163   6.855  1.00 29.39  ? 83  PHE   C C   1 
ATOM   5783 O  O   . PHE   C  1  70  ? -12.660 7.356   6.577  1.00 33.62  ? 83  PHE   C O   1 
ATOM   5784 C  CB  . PHE   C  1  70  ? -12.957 6.453   9.246  1.00 30.16  ? 83  PHE   C CB  1 
ATOM   5785 C  CG  . PHE   C  1  70  ? -13.883 6.551   10.437 1.00 35.14  ? 83  PHE   C CG  1 
ATOM   5786 C  CD1 . PHE   C  1  70  ? -14.965 7.427   10.412 1.00 39.62  ? 83  PHE   C CD1 1 
ATOM   5787 C  CD2 . PHE   C  1  70  ? -13.669 5.779   11.562 1.00 36.94  ? 83  PHE   C CD2 1 
ATOM   5788 C  CE1 . PHE   C  1  70  ? -15.795 7.548   11.506 1.00 39.58  ? 83  PHE   C CE1 1 
ATOM   5789 C  CE2 . PHE   C  1  70  ? -14.525 5.883   12.640 1.00 40.85  ? 83  PHE   C CE2 1 
ATOM   5790 C  CZ  . PHE   C  1  70  ? -15.580 6.764   12.608 1.00 41.26  ? 83  PHE   C CZ  1 
ATOM   5791 N  N   . ASN   C  1  71  ? -12.047 5.211   6.212  1.00 32.65  ? 84  ASN   C N   1 
ATOM   5792 C  CA  . ASN   C  1  71  ? -11.092 5.508   5.149  1.00 36.09  ? 84  ASN   C CA  1 
ATOM   5793 C  C   . ASN   C  1  71  ? -9.961  6.375   5.686  1.00 30.65  ? 84  ASN   C C   1 
ATOM   5794 O  O   . ASN   C  1  71  ? -9.488  7.296   5.023  1.00 27.54  ? 84  ASN   C O   1 
ATOM   5795 C  CB  . ASN   C  1  71  ? -11.764 6.166   3.946  1.00 37.20  ? 84  ASN   C CB  1 
ATOM   5796 C  CG  . ASN   C  1  71  ? -11.252 5.657   2.621  1.00 38.06  ? 84  ASN   C CG  1 
ATOM   5797 O  OD1 . ASN   C  1  71  ? -10.222 4.971   2.549  1.00 41.24  ? 84  ASN   C OD1 1 
ATOM   5798 N  ND2 . ASN   C  1  71  ? -11.977 5.974   1.559  1.00 39.16  ? 84  ASN   C ND2 1 
ATOM   5799 N  N   . PHE   C  1  72  ? -9.527  6.070   6.908  1.00 32.91  ? 85  PHE   C N   1 
ATOM   5800 C  CA  . PHE   C  1  72  ? -8.363  6.747   7.454  1.00 31.11  ? 85  PHE   C CA  1 
ATOM   5801 C  C   . PHE   C  1  72  ? -7.177  6.344   6.596  1.00 25.96  ? 85  PHE   C C   1 
ATOM   5802 O  O   . PHE   C  1  72  ? -7.058  5.168   6.254  1.00 28.83  ? 85  PHE   C O   1 
ATOM   5803 C  CB  . PHE   C  1  72  ? -8.222  6.328   8.922  1.00 31.23  ? 85  PHE   C CB  1 
ATOM   5804 C  CG  . PHE   C  1  72  ? -7.333  7.237   9.757  1.00 32.79  ? 85  PHE   C CG  1 
ATOM   5805 C  CD1 . PHE   C  1  72  ? -7.465  8.617   9.705  1.00 34.12  ? 85  PHE   C CD1 1 
ATOM   5806 C  CD2 . PHE   C  1  72  ? -6.371  6.700   10.608 1.00 36.69  ? 85  PHE   C CD2 1 
ATOM   5807 C  CE1 . PHE   C  1  72  ? -6.658  9.436   10.494 1.00 39.36  ? 85  PHE   C CE1 1 
ATOM   5808 C  CE2 . PHE   C  1  72  ? -5.584  7.526   11.400 1.00 35.24  ? 85  PHE   C CE2 1 
ATOM   5809 C  CZ  . PHE   C  1  72  ? -5.723  8.885   11.340 1.00 33.37  ? 85  PHE   C CZ  1 
ATOM   5810 N  N   . GLU   C  1  73  ? -6.343  7.299   6.204  1.00 27.31  ? 86  GLU   C N   1 
ATOM   5811 C  CA  . GLU   C  1  73  ? -5.226  7.004   5.308  1.00 32.24  ? 86  GLU   C CA  1 
ATOM   5812 C  C   . GLU   C  1  73  ? -4.210  6.065   5.973  1.00 29.03  ? 86  GLU   C C   1 
ATOM   5813 O  O   . GLU   C  1  73  ? -3.927  6.195   7.150  1.00 31.11  ? 86  GLU   C O   1 
ATOM   5814 C  CB  . GLU   C  1  73  ? -4.646  8.327   4.810  1.00 34.90  ? 86  GLU   C CB  1 
ATOM   5815 C  CG  . GLU   C  1  73  ? -3.578  8.157   3.722  1.00 40.30  ? 86  GLU   C CG  1 
ATOM   5816 C  CD  . GLU   C  1  73  ? -2.151  7.854   4.200  1.00 46.60  ? 86  GLU   C CD  1 
ATOM   5817 O  OE1 . GLU   C  1  73  ? -1.442  7.005   3.584  1.00 43.46  ? 86  GLU   C OE1 1 
ATOM   5818 O  OE2 . GLU   C  1  73  ? -1.749  8.465   5.221  1.00 46.49  ? 86  GLU   C OE2 1 
ATOM   5819 N  N   . ASN   C  1  74  ? -3.655  5.125   5.202  1.00 26.55  ? 87  ASN   C N   1 
ATOM   5820 C  CA  . ASN   C  1  74  ? -2.872  4.000   5.709  1.00 29.04  ? 87  ASN   C CA  1 
ATOM   5821 C  C   . ASN   C  1  74  ? -1.691  4.453   6.574  1.00 30.98  ? 87  ASN   C C   1 
ATOM   5822 O  O   . ASN   C  1  74  ? -1.484  3.936   7.664  1.00 30.13  ? 87  ASN   C O   1 
ATOM   5823 C  CB  . ASN   C  1  74  ? -2.407  3.123   4.554  1.00 28.51  ? 87  ASN   C CB  1 
ATOM   5824 C  CG  . ASN   C  1  74  ? -1.524  1.967   4.940  1.00 28.32  ? 87  ASN   C CG  1 
ATOM   5825 O  OD1 . ASN   C  1  74  ? -0.354  1.933   4.547  1.00 30.11  ? 87  ASN   C OD1 1 
ATOM   5826 N  ND2 . ASN   C  1  74  ? -2.060  1.000   5.653  1.00 27.17  ? 87  ASN   C ND2 1 
ATOM   5827 N  N   . ASN   C  1  75  ? -0.884  5.388   6.073  1.00 32.09  ? 88  ASN   C N   1 
ATOM   5828 C  CA  . ASN   C  1  75  ? 0.304   5.817   6.787  1.00 33.14  ? 88  ASN   C CA  1 
ATOM   5829 C  C   . ASN   C  1  75  ? -0.080  6.578   8.056  1.00 33.91  ? 88  ASN   C C   1 
ATOM   5830 O  O   . ASN   C  1  75  ? 0.538   6.377   9.091  1.00 33.97  ? 88  ASN   C O   1 
ATOM   5831 C  CB  . ASN   C  1  75  ? 1.284   6.533   5.862  1.00 33.20  ? 88  ASN   C CB  1 
ATOM   5832 C  CG  . ASN   C  1  75  ? 2.117   5.535   5.063  1.00 39.99  ? 88  ASN   C CG  1 
ATOM   5833 O  OD1 . ASN   C  1  75  ? 2.664   4.544   5.588  1.00 38.66  ? 88  ASN   C OD1 1 
ATOM   5834 N  ND2 . ASN   C  1  75  ? 2.215   5.747   3.766  1.00 40.44  ? 88  ASN   C ND2 1 
ATOM   5835 N  N   . ALA   C  1  76  ? -1.113  7.417   7.984  1.00 31.47  ? 89  ALA   C N   1 
ATOM   5836 C  CA  . ALA   C  1  76  ? -1.644  8.071   9.164  1.00 31.26  ? 89  ALA   C CA  1 
ATOM   5837 C  C   . ALA   C  1  76  ? -2.104  7.032   10.193 1.00 31.98  ? 89  ALA   C C   1 
ATOM   5838 O  O   . ALA   C  1  76  ? -1.851  7.177   11.391 1.00 33.51  ? 89  ALA   C O   1 
ATOM   5839 C  CB  . ALA   C  1  76  ? -2.747  9.024   8.779  1.00 31.93  ? 89  ALA   C CB  1 
ATOM   5840 N  N   . ALA   C  1  77  ? -2.733  5.956   9.730  1.00 29.88  ? 90  ALA   C N   1 
ATOM   5841 C  CA  . ALA   C  1  77  ? -3.168  4.890   10.622 1.00 30.01  ? 90  ALA   C CA  1 
ATOM   5842 C  C   . ALA   C  1  77  ? -1.972  4.205   11.283 1.00 28.56  ? 90  ALA   C C   1 
ATOM   5843 O  O   . ALA   C  1  77  ? -2.005  3.903   12.480 1.00 27.91  ? 90  ALA   C O   1 
ATOM   5844 C  CB  . ALA   C  1  77  ? -4.015  3.875   9.895  1.00 28.20  ? 90  ALA   C CB  1 
ATOM   5845 N  N   . ILE   C  1  78  ? -0.910  3.988   10.506 1.00 26.78  ? 91  ILE   C N   1 
ATOM   5846 C  CA  . ILE   C  1  78  ? 0.266   3.317   11.016 1.00 28.36  ? 91  ILE   C CA  1 
ATOM   5847 C  C   . ILE   C  1  78  ? 0.965   4.218   12.036 1.00 29.05  ? 91  ILE   C C   1 
ATOM   5848 O  O   . ILE   C  1  78  ? 1.324   3.769   13.117 1.00 27.72  ? 91  ILE   C O   1 
ATOM   5849 C  CB  . ILE   C  1  78  ? 1.151   2.898   9.840  1.00 32.16  ? 91  ILE   C CB  1 
ATOM   5850 C  CG1 . ILE   C  1  78  ? 0.554   1.710   9.109  1.00 31.07  ? 91  ILE   C CG1 1 
ATOM   5851 C  CG2 . ILE   C  1  78  ? 2.567   2.573   10.294 1.00 31.23  ? 91  ILE   C CG2 1 
ATOM   5852 C  CD1 . ILE   C  1  78  ? 1.201   1.446   7.761  1.00 30.51  ? 91  ILE   C CD1 1 
ATOM   5853 N  N   . VAL   C  1  79  ? 1.057   5.515   11.747 1.00 27.70  ? 92  VAL   C N   1 
ATOM   5854 C  CA  . VAL   C  1  79  ? 1.689   6.440   12.664 1.00 28.29  ? 92  VAL   C CA  1 
ATOM   5855 C  C   . VAL   C  1  79  ? 0.943   6.472   13.991 1.00 32.05  ? 92  VAL   C C   1 
ATOM   5856 O  O   . VAL   C  1  79  ? 1.578   6.409   15.037 1.00 31.63  ? 92  VAL   C O   1 
ATOM   5857 C  CB  . VAL   C  1  79  ? 1.828   7.841   12.065 1.00 30.72  ? 92  VAL   C CB  1 
ATOM   5858 C  CG1 . VAL   C  1  79  ? 2.290   8.850   13.100 1.00 30.93  ? 92  VAL   C CG1 1 
ATOM   5859 C  CG2 . VAL   C  1  79  ? 2.791   7.840   10.897 1.00 31.53  ? 92  VAL   C CG2 1 
ATOM   5860 N  N   . ALA   C  1  80  ? -0.386  6.593   13.961 1.00 28.38  ? 93  ALA   C N   1 
ATOM   5861 C  CA  . ALA   C  1  80  ? -1.124  6.699   15.200 1.00 29.82  ? 93  ALA   C CA  1 
ATOM   5862 C  C   . ALA   C  1  80  ? -1.125  5.368   15.950 1.00 29.04  ? 93  ALA   C C   1 
ATOM   5863 O  O   . ALA   C  1  80  ? -0.969  5.321   17.165 1.00 32.87  ? 93  ALA   C O   1 
ATOM   5864 C  CB  . ALA   C  1  80  ? -2.527  7.166   14.920 1.00 29.82  ? 93  ALA   C CB  1 
ATOM   5865 N  N   . THR   C  1  81  ? -1.325  4.266   15.231 1.00 30.74  ? 94  THR   C N   1 
ATOM   5866 C  CA  . THR   C  1  81  ? -1.548  2.989   15.889 1.00 27.16  ? 94  THR   C CA  1 
ATOM   5867 C  C   . THR   C  1  81  ? -0.276  2.522   16.603 1.00 30.38  ? 94  THR   C C   1 
ATOM   5868 O  O   . THR   C  1  81  ? -0.338  2.133   17.771 1.00 30.44  ? 94  THR   C O   1 
ATOM   5869 C  CB  . THR   C  1  81  ? -2.026  1.957   14.884 1.00 29.36  ? 94  THR   C CB  1 
ATOM   5870 O  OG1 . THR   C  1  81  ? -3.286  2.404   14.390 1.00 27.71  ? 94  THR   C OG1 1 
ATOM   5871 C  CG2 . THR   C  1  81  ? -2.153  0.583   15.504 1.00 31.82  ? 94  THR   C CG2 1 
ATOM   5872 N  N   . TYR   C  1  82  ? 0.878   2.557   15.925 1.00 27.56  ? 95  TYR   C N   1 
ATOM   5873 C  CA  . TYR   C  1  82  ? 2.090   2.003   16.510 1.00 29.98  ? 95  TYR   C CA  1 
ATOM   5874 C  C   . TYR   C  1  82  ? 2.639   2.960   17.566 1.00 28.45  ? 95  TYR   C C   1 
ATOM   5875 O  O   . TYR   C  1  82  ? 3.288   2.513   18.497 1.00 31.97  ? 95  TYR   C O   1 
ATOM   5876 C  CB  . TYR   C  1  82  ? 3.101   1.603   15.427 1.00 28.22  ? 95  TYR   C CB  1 
ATOM   5877 C  CG  . TYR   C  1  82  ? 2.633   0.363   14.682 1.00 28.36  ? 95  TYR   C CG  1 
ATOM   5878 C  CD1 . TYR   C  1  82  ? 2.711   -0.893  15.265 1.00 29.71  ? 95  TYR   C CD1 1 
ATOM   5879 C  CD2 . TYR   C  1  82  ? 2.076   0.450   13.415 1.00 32.57  ? 95  TYR   C CD2 1 
ATOM   5880 C  CE1 . TYR   C  1  82  ? 2.289   -2.033  14.607 1.00 26.64  ? 95  TYR   C CE1 1 
ATOM   5881 C  CE2 . TYR   C  1  82  ? 1.662   -0.682  12.736 1.00 31.74  ? 95  TYR   C CE2 1 
ATOM   5882 C  CZ  . TYR   C  1  82  ? 1.754   -1.923  13.337 1.00 31.26  ? 95  TYR   C CZ  1 
ATOM   5883 O  OH  . TYR   C  1  82  ? 1.285   -3.033  12.691 1.00 34.81  ? 95  TYR   C OH  1 
ATOM   5884 N  N   . LEU   C  1  83  ? 2.365   4.260   17.438 1.00 28.12  ? 96  LEU   C N   1 
ATOM   5885 C  CA  . LEU   C  1  83  ? 2.684   5.201   18.496 1.00 27.89  ? 96  LEU   C CA  1 
ATOM   5886 C  C   . LEU   C  1  83  ? 1.922   4.789   19.749 1.00 31.42  ? 96  LEU   C C   1 
ATOM   5887 O  O   . LEU   C  1  83  ? 2.488   4.692   20.826 1.00 33.65  ? 96  LEU   C O   1 
ATOM   5888 C  CB  . LEU   C  1  83  ? 2.302   6.608   18.053 1.00 27.85  ? 96  LEU   C CB  1 
ATOM   5889 C  CG  . LEU   C  1  83  ? 2.306   7.695   19.127 1.00 31.63  ? 96  LEU   C CG  1 
ATOM   5890 C  CD1 . LEU   C  1  83  ? 3.697   7.904   19.680 1.00 33.88  ? 96  LEU   C CD1 1 
ATOM   5891 C  CD2 . LEU   C  1  83  ? 1.777   8.983   18.539 1.00 33.94  ? 96  LEU   C CD2 1 
ATOM   5892 N  N   . GLY   C  1  84  ? 0.619   4.547   19.594 1.00 30.08  ? 97  GLY   C N   1 
ATOM   5893 C  CA  . GLY   C  1  84  ? -0.211  4.153   20.715 1.00 30.17  ? 97  GLY   C CA  1 
ATOM   5894 C  C   . GLY   C  1  84  ? 0.252   2.824   21.305 1.00 29.33  ? 97  GLY   C C   1 
ATOM   5895 O  O   . GLY   C  1  84  ? 0.314   2.678   22.514 1.00 27.14  ? 97  GLY   C O   1 
ATOM   5896 N  N   . HIS   C  1  85  ? 0.587   1.869   20.442 1.00 27.88  ? 98  HIS   C N   1 
ATOM   5897 C  CA  . HIS   C  1  85  ? 0.974   0.536   20.875 1.00 28.68  ? 98  HIS   C CA  1 
ATOM   5898 C  C   . HIS   C  1  85  ? 2.351   0.539   21.555 1.00 31.19  ? 98  HIS   C C   1 
ATOM   5899 O  O   . HIS   C  1  85  ? 2.529   -0.076  22.602 1.00 30.63  ? 98  HIS   C O   1 
ATOM   5900 C  CB  . HIS   C  1  85  ? 1.014   -0.386  19.664 1.00 27.42  ? 98  HIS   C CB  1 
ATOM   5901 C  CG  . HIS   C  1  85  ? 1.222   -1.802  20.007 1.00 26.10  ? 98  HIS   C CG  1 
ATOM   5902 N  ND1 . HIS   C  1  85  ? 0.422   -2.444  20.917 1.00 29.40  ? 98  HIS   C ND1 1 
ATOM   5903 C  CD2 . HIS   C  1  85  ? 2.060   -2.730  19.517 1.00 29.20  ? 98  HIS   C CD2 1 
ATOM   5904 C  CE1 . HIS   C  1  85  ? 0.813   -3.728  20.994 1.00 32.62  ? 98  HIS   C CE1 1 
ATOM   5905 N  NE2 . HIS   C  1  85  ? 1.812   -3.931  20.156 1.00 30.96  ? 98  HIS   C NE2 1 
ATOM   5906 N  N   . LEU   C  1  86  ? 3.346   1.206   20.955 1.00 29.97  ? 99  LEU   C N   1 
ATOM   5907 C  CA  . LEU   C  1  86  ? 4.688   1.239   21.529 1.00 32.98  ? 99  LEU   C CA  1 
ATOM   5908 C  C   . LEU   C  1  86  ? 4.645   1.784   22.958 1.00 31.03  ? 99  LEU   C C   1 
ATOM   5909 O  O   . LEU   C  1  86  ? 5.237   1.209   23.858 1.00 34.04  ? 99  LEU   C O   1 
ATOM   5910 C  CB  . LEU   C  1  86  ? 5.609   2.077   20.643 1.00 31.49  ? 99  LEU   C CB  1 
ATOM   5911 C  CG  . LEU   C  1  86  ? 6.149   1.388   19.392 1.00 31.54  ? 99  LEU   C CG  1 
ATOM   5912 C  CD1 . LEU   C  1  86  ? 6.766   2.424   18.468 1.00 33.57  ? 99  LEU   C CD1 1 
ATOM   5913 C  CD2 . LEU   C  1  86  ? 7.154   0.314   19.763 1.00 34.65  ? 99  LEU   C CD2 1 
ATOM   5914 N  N   . LEU   C  1  87  ? 3.896   2.873   23.149 1.00 32.64  ? 100 LEU   C N   1 
ATOM   5915 C  CA  . LEU   C  1  87  ? 3.826   3.570   24.413 1.00 31.45  ? 100 LEU   C CA  1 
ATOM   5916 C  C   . LEU   C  1  87  ? 2.884   2.877   25.384 1.00 33.40  ? 100 LEU   C C   1 
ATOM   5917 O  O   . LEU   C  1  87  ? 3.137   2.919   26.587 1.00 32.42  ? 100 LEU   C O   1 
ATOM   5918 C  CB  . LEU   C  1  87  ? 3.353   4.999   24.182 1.00 31.13  ? 100 LEU   C CB  1 
ATOM   5919 C  CG  . LEU   C  1  87  ? 4.299   5.887   23.382 1.00 31.16  ? 100 LEU   C CG  1 
ATOM   5920 C  CD1 . LEU   C  1  87  ? 3.733   7.286   23.262 1.00 33.58  ? 100 LEU   C CD1 1 
ATOM   5921 C  CD2 . LEU   C  1  87  ? 5.661   5.938   24.006 1.00 32.66  ? 100 LEU   C CD2 1 
ATOM   5922 N  N   . ASN   C  1  88  ? 1.787   2.289   24.877 1.00 31.08  ? 101 ASN   C N   1 
ATOM   5923 C  CA  . ASN   C  1  88  ? 0.649   1.992   25.727 1.00 29.44  ? 101 ASN   C CA  1 
ATOM   5924 C  C   . ASN   C  1  88  ? 0.133   0.565   25.575 1.00 29.65  ? 101 ASN   C C   1 
ATOM   5925 O  O   . ASN   C  1  88  ? -0.788  0.174   26.292 1.00 28.93  ? 101 ASN   C O   1 
ATOM   5926 C  CB  . ASN   C  1  88  ? -0.533  2.909   25.480 1.00 29.00  ? 101 ASN   C CB  1 
ATOM   5927 C  CG  . ASN   C  1  88  ? -0.234  4.357   25.758 1.00 32.49  ? 101 ASN   C CG  1 
ATOM   5928 O  OD1 . ASN   C  1  88  ? 0.377   4.693   26.764 1.00 35.92  ? 101 ASN   C OD1 1 
ATOM   5929 N  ND2 . ASN   C  1  88  ? -0.664  5.253   24.890 1.00 38.01  ? 101 ASN   C ND2 1 
ATOM   5930 N  N   . GLY   C  1  89  ? 0.701   -0.221  24.672 1.00 29.43  ? 102 GLY   C N   1 
ATOM   5931 C  CA  . GLY   C  1  89  ? 0.217   -1.582  24.465 1.00 27.99  ? 102 GLY   C CA  1 
ATOM   5932 C  C   . GLY   C  1  89  ? 1.191   -2.620  25.016 1.00 29.57  ? 102 GLY   C C   1 
ATOM   5933 O  O   . GLY   C  1  89  ? 2.307   -2.305  25.449 1.00 29.62  ? 102 GLY   C O   1 
ATOM   5934 N  N   . ASN   C  1  90  ? 0.783   -3.875  24.903 1.00 25.03  ? 103 ASN   C N   1 
ATOM   5935 C  CA  . ASN   C  1  90  ? 1.595   -4.979  25.341 1.00 28.57  ? 103 ASN   C CA  1 
ATOM   5936 C  C   . ASN   C  1  90  ? 2.256   -5.580  24.123 1.00 32.04  ? 103 ASN   C C   1 
ATOM   5937 O  O   . ASN   C  1  90  ? 1.572   -6.173  23.297 1.00 32.46  ? 103 ASN   C O   1 
ATOM   5938 C  CB  . ASN   C  1  90  ? 0.737   -6.007  26.068 1.00 31.10  ? 103 ASN   C CB  1 
ATOM   5939 C  CG  . ASN   C  1  90  ? 1.561   -7.108  26.701 1.00 34.87  ? 103 ASN   C CG  1 
ATOM   5940 O  OD1 . ASN   C  1  90  ? 2.442   -7.686  26.047 1.00 37.13  ? 103 ASN   C OD1 1 
ATOM   5941 N  ND2 . ASN   C  1  90  ? 1.279   -7.402  27.969 1.00 38.68  ? 103 ASN   C ND2 1 
ATOM   5942 N  N   . LEU   C  1  91  ? 3.588   -5.473  24.049 1.00 33.02  ? 104 LEU   C N   1 
ATOM   5943 C  CA  . LEU   C  1  91  ? 4.316   -5.819  22.836 1.00 34.38  ? 104 LEU   C CA  1 
ATOM   5944 C  C   . LEU   C  1  91  ? 4.499   -7.327  22.716 1.00 34.15  ? 104 LEU   C C   1 
ATOM   5945 O  O   . LEU   C  1  91  ? 4.684   -7.842  21.617 1.00 35.84  ? 104 LEU   C O   1 
ATOM   5946 C  CB  . LEU   C  1  91  ? 5.632   -5.061  22.842 1.00 39.08  ? 104 LEU   C CB  1 
ATOM   5947 C  CG  . LEU   C  1  91  ? 5.450   -3.541  22.868 1.00 45.32  ? 104 LEU   C CG  1 
ATOM   5948 C  CD1 . LEU   C  1  91  ? 6.674   -2.848  23.339 1.00 53.55  ? 104 LEU   C CD1 1 
ATOM   5949 C  CD2 . LEU   C  1  91  ? 5.094   -3.044  21.499 1.00 54.59  ? 104 LEU   C CD2 1 
ATOM   5950 N  N   . VAL   C  1  92  ? 4.346   -8.048  23.831 1.00 35.18  ? 105 VAL   C N   1 
ATOM   5951 C  CA  . VAL   C  1  92  ? 4.531   -9.484  23.819 1.00 36.32  ? 105 VAL   C CA  1 
ATOM   5952 C  C   . VAL   C  1  92  ? 3.258   -10.160 23.330 1.00 36.67  ? 105 VAL   C C   1 
ATOM   5953 O  O   . VAL   C  1  92  ? 3.339   -11.079 22.524 1.00 39.07  ? 105 VAL   C O   1 
ATOM   5954 C  CB  . VAL   C  1  92  ? 5.007   -10.001 25.183 1.00 40.03  ? 105 VAL   C CB  1 
ATOM   5955 C  CG1 . VAL   C  1  92  ? 4.917   -11.526 25.287 1.00 37.32  ? 105 VAL   C CG1 1 
ATOM   5956 C  CG2 . VAL   C  1  92  ? 6.441   -9.511  25.430 1.00 40.28  ? 105 VAL   C CG2 1 
ATOM   5957 N  N   . THR   C  1  93  ? 2.101   -9.717  23.825 1.00 37.83  ? 106 THR   C N   1 
ATOM   5958 C  CA  . THR   C  1  93  ? 0.822   -10.281 23.414 1.00 42.31  ? 106 THR   C CA  1 
ATOM   5959 C  C   . THR   C  1  93  ? 0.289   -9.608  22.143 1.00 40.42  ? 106 THR   C C   1 
ATOM   5960 O  O   . THR   C  1  93  ? -0.641  -10.124 21.537 1.00 39.93  ? 106 THR   C O   1 
ATOM   5961 C  CB  . THR   C  1  93  ? -0.188  -10.171 24.557 1.00 41.73  ? 106 THR   C CB  1 
ATOM   5962 O  OG1 . THR   C  1  93  ? -0.329  -8.774  24.825 1.00 36.01  ? 106 THR   C OG1 1 
ATOM   5963 C  CG2 . THR   C  1  93  ? 0.245   -10.969 25.775 1.00 46.27  ? 106 THR   C CG2 1 
ATOM   5964 N  N   . ASP   C  1  94  ? 0.867   -8.464  21.763 1.00 36.89  ? 107 ASP   C N   1 
ATOM   5965 C  CA  . ASP   C  1  94  ? 0.454   -7.711  20.591 1.00 34.76  ? 107 ASP   C CA  1 
ATOM   5966 C  C   . ASP   C  1  94  ? -0.956  -7.155  20.760 1.00 36.26  ? 107 ASP   C C   1 
ATOM   5967 O  O   . ASP   C  1  94  ? -1.724  -7.147  19.798 1.00 37.53  ? 107 ASP   C O   1 
ATOM   5968 C  CB  . ASP   C  1  94  ? 0.586   -8.543  19.324 1.00 38.18  ? 107 ASP   C CB  1 
ATOM   5969 C  CG  . ASP   C  1  94  ? 0.651   -7.744  18.021 1.00 42.61  ? 107 ASP   C CG  1 
ATOM   5970 O  OD1 . ASP   C  1  94  ? 1.300   -6.662  18.055 1.00 40.83  ? 107 ASP   C OD1 1 
ATOM   5971 O  OD2 . ASP   C  1  94  ? 0.054   -8.210  16.987 1.00 40.42  ? 107 ASP   C OD2 1 
ATOM   5972 N  N   . LEU   C  1  95  ? -1.296  -6.677  21.970 1.00 33.27  ? 108 LEU   C N   1 
ATOM   5973 C  CA  . LEU   C  1  95  ? -2.639  -6.182  22.246 1.00 31.38  ? 108 LEU   C CA  1 
ATOM   5974 C  C   . LEU   C  1  95  ? -2.561  -4.784  22.841 1.00 31.96  ? 108 LEU   C C   1 
ATOM   5975 O  O   . LEU   C  1  95  ? -1.684  -4.505  23.658 1.00 31.35  ? 108 LEU   C O   1 
ATOM   5976 C  CB  . LEU   C  1  95  ? -3.396  -7.131  23.176 1.00 34.16  ? 108 LEU   C CB  1 
ATOM   5977 C  CG  . LEU   C  1  95  ? -3.687  -8.537  22.639 1.00 38.24  ? 108 LEU   C CG  1 
ATOM   5978 C  CD1 . LEU   C  1  95  ? -4.174  -9.437  23.746 1.00 39.71  ? 108 LEU   C CD1 1 
ATOM   5979 C  CD2 . LEU   C  1  95  ? -4.730  -8.499  21.512 1.00 38.20  ? 108 LEU   C CD2 1 
ATOM   5980 N  N   . LEU   C  1  96  ? -3.494  -3.923  22.425 1.00 29.95  ? 109 LEU   C N   1 
ATOM   5981 C  CA  . LEU   C  1  96  ? -3.601  -2.561  22.900 1.00 29.01  ? 109 LEU   C CA  1 
ATOM   5982 C  C   . LEU   C  1  96  ? -5.046  -2.310  23.350 1.00 40.17  ? 109 LEU   C C   1 
ATOM   5983 O  O   . LEU   C  1  96  ? -5.990  -2.607  22.616 1.00 35.91  ? 109 LEU   C O   1 
ATOM   5984 C  CB  . LEU   C  1  96  ? -3.252  -1.636  21.752 1.00 29.90  ? 109 LEU   C CB  1 
ATOM   5985 C  CG  . LEU   C  1  96  ? -3.523  -0.143  21.968 1.00 31.95  ? 109 LEU   C CG  1 
ATOM   5986 C  CD1 . LEU   C  1  96  ? -2.742  0.416   23.141 1.00 35.02  ? 109 LEU   C CD1 1 
ATOM   5987 C  CD2 . LEU   C  1  96  ? -3.201  0.657   20.751 1.00 30.45  ? 109 LEU   C CD2 1 
ATOM   5988 N  N   . SER   C  1  97  ? -5.208  -1.767  24.563 1.00 32.91  ? 110 SER   C N   1 
ATOM   5989 C  CA  . SER   C  1  97  ? -6.483  -1.267  25.030 1.00 32.66  ? 110 SER   C CA  1 
ATOM   5990 C  C   . SER   C  1  97  ? -6.736  0.122   24.469 1.00 33.47  ? 110 SER   C C   1 
ATOM   5991 O  O   . SER   C  1  97  ? -5.877  0.992   24.599 1.00 31.46  ? 110 SER   C O   1 
ATOM   5992 C  CB  . SER   C  1  97  ? -6.508  -1.223  26.537 1.00 35.71  ? 110 SER   C CB  1 
ATOM   5993 O  OG  . SER   C  1  97  ? -7.589  -0.423  26.997 1.00 33.33  ? 110 SER   C OG  1 
ATOM   5994 N  N   . ILE   C  1  98  ? -7.949  0.364   23.944 1.00 32.02  ? 111 ILE   C N   1 
ATOM   5995 C  CA  . ILE   C  1  98  ? -8.257  1.684   23.406 1.00 31.23  ? 111 ILE   C CA  1 
ATOM   5996 C  C   . ILE   C  1  98  ? -8.650  2.627   24.538 1.00 32.87  ? 111 ILE   C C   1 
ATOM   5997 O  O   . ILE   C  1  98  ? -8.967  3.792   24.305 1.00 36.11  ? 111 ILE   C O   1 
ATOM   5998 C  CB  . ILE   C  1  98  ? -9.324  1.611   22.302 1.00 31.40  ? 111 ILE   C CB  1 
ATOM   5999 C  CG1 . ILE   C  1  98  ? -10.700 1.188   22.821 1.00 33.68  ? 111 ILE   C CG1 1 
ATOM   6000 C  CG2 . ILE   C  1  98  ? -8.854  0.691   21.192 1.00 31.30  ? 111 ILE   C CG2 1 
ATOM   6001 C  CD1 . ILE   C  1  98  ? -11.808 1.273   21.777 1.00 36.42  ? 111 ILE   C CD1 1 
ATOM   6002 N  N   . GLY   C  1  99  ? -8.631  2.112   25.768 1.00 36.21  ? 112 GLY   C N   1 
ATOM   6003 C  CA  . GLY   C  1  99  ? -8.933  2.913   26.939 1.00 38.79  ? 112 GLY   C CA  1 
ATOM   6004 C  C   . GLY   C  1  99  ? -7.917  2.684   28.056 1.00 41.58  ? 112 GLY   C C   1 
ATOM   6005 O  O   . GLY   C  1  99  ? -6.755  3.070   27.922 1.00 36.52  ? 112 GLY   C O   1 
ATOM   6006 N  N   . GLY   C  1  100 ? -8.390  2.109   29.171 1.00 39.48  ? 113 GLY   C N   1 
ATOM   6007 C  CA  . GLY   C  1  100 ? -7.584  1.955   30.368 1.00 41.80  ? 113 GLY   C CA  1 
ATOM   6008 C  C   . GLY   C  1  100 ? -7.082  0.518   30.510 1.00 41.98  ? 113 GLY   C C   1 
ATOM   6009 O  O   . GLY   C  1  100 ? -7.265  -0.314  29.623 1.00 37.95  ? 113 GLY   C O   1 
ATOM   6010 N  N   . ALA   C  1  101 ? -6.489  0.233   31.666 1.00 37.88  ? 114 ALA   C N   1 
ATOM   6011 C  CA  . ALA   C  1  101 ? -5.800  -1.029  31.874 1.00 39.23  ? 114 ALA   C CA  1 
ATOM   6012 C  C   . ALA   C  1  101 ? -6.813  -2.146  32.048 1.00 36.61  ? 114 ALA   C C   1 
ATOM   6013 O  O   . ALA   C  1  101 ? -7.927  -1.934  32.510 1.00 40.69  ? 114 ALA   C O   1 
ATOM   6014 C  CB  . ALA   C  1  101 ? -4.893  -0.921  33.097 1.00 49.33  ? 114 ALA   C CB  1 
ATOM   6015 N  N   . THR   C  1  102 ? -6.403  -3.349  31.688 1.00 35.27  ? 115 THR   C N   1 
ATOM   6016 C  CA  . THR   C  1  102 ? -7.296  -4.480  31.657 1.00 45.67  ? 115 THR   C CA  1 
ATOM   6017 C  C   . THR   C  1  102 ? -6.447  -5.737  31.659 1.00 46.05  ? 115 THR   C C   1 
ATOM   6018 O  O   . THR   C  1  102 ? -5.404  -5.756  31.029 1.00 43.84  ? 115 THR   C O   1 
ATOM   6019 C  CB  . THR   C  1  102 ? -8.186  -4.392  30.410 1.00 55.86  ? 115 THR   C CB  1 
ATOM   6020 O  OG1 . THR   C  1  102 ? -8.938  -5.599  30.324 1.00 49.89  ? 115 THR   C OG1 1 
ATOM   6021 C  CG2 . THR   C  1  102 ? -7.414  -4.295  29.104 1.00 56.30  ? 115 THR   C CG2 1 
ATOM   6022 N  N   . PRO   C  1  103 ? -6.858  -6.826  32.344 1.00 54.28  ? 116 PRO   C N   1 
ATOM   6023 C  CA  . PRO   C  1  103 ? -6.203  -8.127  32.151 1.00 57.36  ? 116 PRO   C CA  1 
ATOM   6024 C  C   . PRO   C  1  103 ? -6.306  -8.686  30.727 1.00 47.94  ? 116 PRO   C C   1 
ATOM   6025 O  O   . PRO   C  1  103 ? -5.577  -9.612  30.390 1.00 47.35  ? 116 PRO   C O   1 
ATOM   6026 C  CB  . PRO   C  1  103 ? -6.891  -9.059  33.185 1.00 56.88  ? 116 PRO   C CB  1 
ATOM   6027 C  CG  . PRO   C  1  103 ? -8.218  -8.358  33.490 1.00 61.16  ? 116 PRO   C CG  1 
ATOM   6028 C  CD  . PRO   C  1  103 ? -7.936  -6.860  33.350 1.00 55.93  ? 116 PRO   C CD  1 
ATOM   6029 N  N   . LYS   C  1  104 ? -7.206  -8.142  29.896 1.00 48.84  ? 117 LYS   C N   1 
ATOM   6030 C  CA  . LYS   C  1  104 ? -7.396  -8.628  28.533 1.00 52.91  ? 117 LYS   C CA  1 
ATOM   6031 C  C   . LYS   C  1  104 ? -6.155  -8.413  27.651 1.00 48.79  ? 117 LYS   C C   1 
ATOM   6032 O  O   . LYS   C  1  104 ? -6.043  -9.067  26.619 1.00 50.54  ? 117 LYS   C O   1 
ATOM   6033 C  CB  . LYS   C  1  104 ? -8.595  -7.931  27.877 1.00 57.25  ? 117 LYS   C CB  1 
ATOM   6034 C  CG  . LYS   C  1  104 ? -9.970  -8.259  28.442 1.00 64.29  ? 117 LYS   C CG  1 
ATOM   6035 C  CD  . LYS   C  1  104 ? -11.029 -7.201  28.117 1.00 71.36  ? 117 LYS   C CD  1 
ATOM   6036 C  CE  . LYS   C  1  104 ? -12.440 -7.576  28.486 1.00 78.61  ? 117 LYS   C CE  1 
ATOM   6037 N  NZ  . LYS   C  1  104 ? -12.913 -8.743  27.726 1.00 75.66  ? 117 LYS   C NZ  1 
ATOM   6038 N  N   . THR   C  1  105 ? -5.238  -7.495  28.029 1.00 44.53  ? 118 THR   C N   1 
ATOM   6039 C  CA  . THR   C  1  105 ? -4.014  -7.282  27.266 1.00 45.21  ? 118 THR   C CA  1 
ATOM   6040 C  C   . THR   C  1  105 ? -2.961  -8.316  27.645 1.00 48.70  ? 118 THR   C C   1 
ATOM   6041 O  O   . THR   C  1  105 ? -1.914  -8.368  27.015 1.00 48.07  ? 118 THR   C O   1 
ATOM   6042 C  CB  . THR   C  1  105 ? -3.454  -5.862  27.367 1.00 41.26  ? 118 THR   C CB  1 
ATOM   6043 O  OG1 . THR   C  1  105 ? -3.270  -5.491  28.724 1.00 40.79  ? 118 THR   C OG1 1 
ATOM   6044 C  CG2 . THR   C  1  105 ? -4.329  -4.834  26.658 1.00 41.42  ? 118 THR   C CG2 1 
ATOM   6045 N  N   . GLY   C  1  106 ? -3.247  -9.146  28.656 1.00 51.74  ? 119 GLY   C N   1 
ATOM   6046 C  CA  . GLY   C  1  106 ? -2.356  -10.222 29.063 1.00 51.08  ? 119 GLY   C CA  1 
ATOM   6047 C  C   . GLY   C  1  106 ? -1.483  -9.829  30.254 1.00 46.15  ? 119 GLY   C C   1 
ATOM   6048 O  O   . GLY   C  1  106 ? -1.636  -8.752  30.835 1.00 46.06  ? 119 GLY   C O   1 
ATOM   6049 N  N   . PRO   C  1  107 ? -0.529  -10.700 30.648 1.00 51.10  ? 120 PRO   C N   1 
ATOM   6050 C  CA  . PRO   C  1  107 ? 0.403   -10.401 31.743 1.00 53.51  ? 120 PRO   C CA  1 
ATOM   6051 C  C   . PRO   C  1  107 ? 1.158   -9.093  31.516 1.00 49.42  ? 120 PRO   C C   1 
ATOM   6052 O  O   . PRO   C  1  107 ? 1.719   -8.873  30.445 1.00 51.46  ? 120 PRO   C O   1 
ATOM   6053 C  CB  . PRO   C  1  107 ? 1.365   -11.613 31.791 1.00 56.10  ? 120 PRO   C CB  1 
ATOM   6054 C  CG  . PRO   C  1  107 ? 0.642   -12.709 31.032 1.00 60.83  ? 120 PRO   C CG  1 
ATOM   6055 C  CD  . PRO   C  1  107 ? -0.307  -12.027 30.050 1.00 59.78  ? 120 PRO   C CD  1 
ATOM   6056 N  N   . PRO   C  1  108 ? 1.234   -8.197  32.521 1.00 56.30  ? 121 PRO   C N   1 
ATOM   6057 C  CA  . PRO   C  1  108 ? 1.834   -6.878  32.314 1.00 59.03  ? 121 PRO   C CA  1 
ATOM   6058 C  C   . PRO   C  1  108 ? 3.321   -6.939  31.958 1.00 53.82  ? 121 PRO   C C   1 
ATOM   6059 O  O   . PRO   C  1  108 ? 4.023   -7.874  32.345 1.00 45.99  ? 121 PRO   C O   1 
ATOM   6060 C  CB  . PRO   C  1  108 ? 1.569   -6.116  33.644 1.00 59.64  ? 121 PRO   C CB  1 
ATOM   6061 C  CG  . PRO   C  1  108 ? 1.327   -7.214  34.656 1.00 66.67  ? 121 PRO   C CG  1 
ATOM   6062 C  CD  . PRO   C  1  108 ? 0.743   -8.401  33.895 1.00 62.85  ? 121 PRO   C CD  1 
ATOM   6063 N  N   . PRO   C  1  109 ? 3.840   -5.932  31.212 1.00 48.42  ? 122 PRO   C N   1 
ATOM   6064 C  CA  . PRO   C  1  109 ? 5.267   -5.837  30.922 1.00 50.33  ? 122 PRO   C CA  1 
ATOM   6065 C  C   . PRO   C  1  109 ? 6.057   -5.465  32.172 1.00 50.05  ? 122 PRO   C C   1 
ATOM   6066 O  O   . PRO   C  1  109 ? 5.470   -4.967  33.125 1.00 52.55  ? 122 PRO   C O   1 
ATOM   6067 C  CB  . PRO   C  1  109 ? 5.305   -4.710  29.887 1.00 43.93  ? 122 PRO   C CB  1 
ATOM   6068 C  CG  . PRO   C  1  109 ? 4.195   -3.821  30.310 1.00 42.68  ? 122 PRO   C CG  1 
ATOM   6069 C  CD  . PRO   C  1  109 ? 3.097   -4.790  30.665 1.00 42.71  ? 122 PRO   C CD  1 
ATOM   6070 N  N   . PRO   C  1  110 ? 7.398   -5.640  32.174 1.00 52.15  ? 123 PRO   C N   1 
ATOM   6071 C  CA  . PRO   C  1  110 ? 8.247   -5.106  33.239 1.00 52.63  ? 123 PRO   C CA  1 
ATOM   6072 C  C   . PRO   C  1  110 ? 8.172   -3.584  33.352 1.00 49.80  ? 123 PRO   C C   1 
ATOM   6073 O  O   . PRO   C  1  110 ? 8.321   -2.862  32.370 1.00 45.83  ? 123 PRO   C O   1 
ATOM   6074 C  CB  . PRO   C  1  110 ? 9.671   -5.599  32.879 1.00 55.39  ? 123 PRO   C CB  1 
ATOM   6075 C  CG  . PRO   C  1  110 ? 9.596   -5.922  31.388 1.00 60.74  ? 123 PRO   C CG  1 
ATOM   6076 C  CD  . PRO   C  1  110 ? 8.164   -6.375  31.152 1.00 60.20  ? 123 PRO   C CD  1 
ATOM   6077 N  N   . PRO   C  1  111 ? 7.928   -3.036  34.565 1.00 53.43  ? 124 PRO   C N   1 
ATOM   6078 C  CA  . PRO   C  1  111 ? 7.957   -1.585  34.785 1.00 47.53  ? 124 PRO   C CA  1 
ATOM   6079 C  C   . PRO   C  1  111 ? 9.326   -1.056  34.401 1.00 42.92  ? 124 PRO   C C   1 
ATOM   6080 O  O   . PRO   C  1  111 ? 10.296  -1.791  34.530 1.00 36.79  ? 124 PRO   C O   1 
ATOM   6081 C  CB  . PRO   C  1  111 ? 7.673   -1.407  36.292 1.00 55.45  ? 124 PRO   C CB  1 
ATOM   6082 C  CG  . PRO   C  1  111 ? 6.982   -2.703  36.683 1.00 58.31  ? 124 PRO   C CG  1 
ATOM   6083 C  CD  . PRO   C  1  111 ? 7.586   -3.786  35.786 1.00 58.33  ? 124 PRO   C CD  1 
ATOM   6084 N  N   . PRO   C  1  112 ? 9.474   0.213   33.956 1.00 38.23  ? 125 PRO   C N   1 
ATOM   6085 C  CA  . PRO   C  1  112 ? 8.390   1.206   33.936 1.00 41.79  ? 125 PRO   C CA  1 
ATOM   6086 C  C   . PRO   C  1  112 ? 7.376   1.166   32.780 1.00 46.06  ? 125 PRO   C C   1 
ATOM   6087 O  O   . PRO   C  1  112 ? 6.509   2.044   32.682 1.00 39.10  ? 125 PRO   C O   1 
ATOM   6088 C  CB  . PRO   C  1  112 ? 9.174   2.533   33.910 1.00 39.41  ? 125 PRO   C CB  1 
ATOM   6089 C  CG  . PRO   C  1  112 ? 10.421  2.195   33.131 1.00 43.96  ? 125 PRO   C CG  1 
ATOM   6090 C  CD  . PRO   C  1  112 ? 10.737  0.739   33.442 1.00 40.12  ? 125 PRO   C CD  1 
ATOM   6091 N  N   . ALA   C  1  113 ? 7.452   0.143   31.922 1.00 40.52  ? 126 ALA   C N   1 
ATOM   6092 C  CA  . ALA   C  1  113 ? 6.401   -0.078  30.935 1.00 43.80  ? 126 ALA   C CA  1 
ATOM   6093 C  C   . ALA   C  1  113 ? 5.125   -0.506  31.665 1.00 46.81  ? 126 ALA   C C   1 
ATOM   6094 O  O   . ALA   C  1  113 ? 5.203   -1.010  32.786 1.00 39.71  ? 126 ALA   C O   1 
ATOM   6095 C  CB  . ALA   C  1  113 ? 6.824   -1.111  29.925 1.00 38.10  ? 126 ALA   C CB  1 
ATOM   6096 N  N   . HIS   C  1  114 ? 3.967   -0.299  31.026 1.00 40.47  ? 127 HIS   C N   1 
ATOM   6097 C  CA  . HIS   C  1  114 ? 2.690   -0.426  31.711 1.00 40.14  ? 127 HIS   C CA  1 
ATOM   6098 C  C   . HIS   C  1  114 ? 1.617   -1.115  30.869 1.00 41.11  ? 127 HIS   C C   1 
ATOM   6099 O  O   . HIS   C  1  114 ? 0.778   -1.809  31.436 1.00 42.56  ? 127 HIS   C O   1 
ATOM   6100 C  CB  . HIS   C  1  114 ? 2.225   0.947   32.192 1.00 37.84  ? 127 HIS   C CB  1 
ATOM   6101 C  CG  . HIS   C  1  114 ? 2.357   2.008   31.152 1.00 42.58  ? 127 HIS   C CG  1 
ATOM   6102 N  ND1 . HIS   C  1  114 ? 1.381   2.181   30.197 1.00 41.58  ? 127 HIS   C ND1 1 
ATOM   6103 C  CD2 . HIS   C  1  114 ? 3.293   2.965   30.923 1.00 41.12  ? 127 HIS   C CD2 1 
ATOM   6104 C  CE1 . HIS   C  1  114 ? 1.715   3.217   29.431 1.00 41.26  ? 127 HIS   C CE1 1 
ATOM   6105 N  NE2 . HIS   C  1  114 ? 2.867   3.715   29.855 1.00 36.94  ? 127 HIS   C NE2 1 
ATOM   6106 N  N   . ALA   C  1  115 ? 1.604   -0.908  29.539 1.00 41.07  ? 128 ALA   C N   1 
ATOM   6107 C  CA  . ALA   C  1  115 ? 0.516   -1.394  28.697 1.00 35.28  ? 128 ALA   C CA  1 
ATOM   6108 C  C   . ALA   C  1  115 ? -0.841  -0.944  29.255 1.00 33.52  ? 128 ALA   C C   1 
ATOM   6109 O  O   . ALA   C  1  115 ? -1.800  -1.705  29.295 1.00 29.55  ? 128 ALA   C O   1 
ATOM   6110 C  CB  . ALA   C  1  115 ? 0.592   -2.901  28.537 1.00 36.85  ? 128 ALA   C CB  1 
ATOM   6111 N  N   . GLY   C  1  116 ? -0.918  0.342   29.616 1.00 34.34  ? 129 GLY   C N   1 
ATOM   6112 C  CA  . GLY   C  1  116 ? -2.055  0.885   30.329 1.00 37.02  ? 129 GLY   C CA  1 
ATOM   6113 C  C   . GLY   C  1  116 ? -3.139  1.447   29.419 1.00 37.95  ? 129 GLY   C C   1 
ATOM   6114 O  O   . GLY   C  1  116 ? -4.134  1.981   29.924 1.00 41.02  ? 129 GLY   C O   1 
ATOM   6115 N  N   . GLY   C  1  117 ? -2.914  1.382   28.095 1.00 36.68  ? 130 GLY   C N   1 
ATOM   6116 C  CA  . GLY   C  1  117 ? -3.914  1.774   27.120 1.00 30.13  ? 130 GLY   C CA  1 
ATOM   6117 C  C   . GLY   C  1  117 ? -3.854  3.270   26.814 1.00 29.24  ? 130 GLY   C C   1 
ATOM   6118 O  O   . GLY   C  1  117 ? -3.088  4.007   27.424 1.00 29.25  ? 130 GLY   C O   1 
ATOM   6119 N  N   . LEU   C  1  118 ? -4.682  3.699   25.845 1.00 28.75  ? 131 LEU   C N   1 
ATOM   6120 C  CA  . LEU   C  1  118 ? -4.665  5.059   25.333 1.00 29.42  ? 131 LEU   C CA  1 
ATOM   6121 C  C   . LEU   C  1  118 ? -5.031  6.104   26.372 1.00 30.10  ? 131 LEU   C C   1 
ATOM   6122 O  O   . LEU   C  1  118 ? -4.775  7.280   26.147 1.00 34.71  ? 131 LEU   C O   1 
ATOM   6123 C  CB  . LEU   C  1  118 ? -5.600  5.152   24.129 1.00 31.55  ? 131 LEU   C CB  1 
ATOM   6124 C  CG  . LEU   C  1  118 ? -5.246  4.281   22.926 1.00 31.86  ? 131 LEU   C CG  1 
ATOM   6125 C  CD1 . LEU   C  1  118 ? -6.233  4.514   21.802 1.00 35.56  ? 131 LEU   C CD1 1 
ATOM   6126 C  CD2 . LEU   C  1  118 ? -3.855  4.614   22.469 1.00 31.46  ? 131 LEU   C CD2 1 
ATOM   6127 N  N   . ASN   C  1  119 ? -5.658  5.693   27.483 1.00 37.54  ? 132 ASN   C N   1 
ATOM   6128 C  CA  . ASN   C  1  119 ? -5.983  6.613   28.563 1.00 46.09  ? 132 ASN   C CA  1 
ATOM   6129 C  C   . ASN   C  1  119 ? -4.740  7.200   29.230 1.00 45.63  ? 132 ASN   C C   1 
ATOM   6130 O  O   . ASN   C  1  119 ? -4.839  8.252   29.851 1.00 43.03  ? 132 ASN   C O   1 
ATOM   6131 C  CB  . ASN   C  1  119 ? -6.808  5.945   29.660 1.00 49.40  ? 132 ASN   C CB  1 
ATOM   6132 C  CG  . ASN   C  1  119 ? -8.251  5.712   29.252 1.00 47.56  ? 132 ASN   C CG  1 
ATOM   6133 O  OD1 . ASN   C  1  119 ? -8.666  6.045   28.135 1.00 45.42  ? 132 ASN   C OD1 1 
ATOM   6134 N  ND2 . ASN   C  1  119 ? -9.043  5.144   30.143 1.00 44.82  ? 132 ASN   C ND2 1 
ATOM   6135 N  N   . VAL   C  1  120 ? -3.586  6.528   29.130 1.00 41.56  ? 133 VAL   C N   1 
ATOM   6136 C  CA  . VAL   C  1  120 ? -2.390  6.982   29.831 1.00 39.30  ? 133 VAL   C CA  1 
ATOM   6137 C  C   . VAL   C  1  120 ? -1.964  8.362   29.320 1.00 38.60  ? 133 VAL   C C   1 
ATOM   6138 O  O   . VAL   C  1  120 ? -1.757  8.577   28.128 1.00 42.20  ? 133 VAL   C O   1 
ATOM   6139 C  CB  . VAL   C  1  120 ? -1.247  5.958   29.717 1.00 38.25  ? 133 VAL   C CB  1 
ATOM   6140 C  CG1 . VAL   C  1  120 ? 0.083   6.526   30.222 1.00 41.87  ? 133 VAL   C CG1 1 
ATOM   6141 C  CG2 . VAL   C  1  120 ? -1.605  4.645   30.410 1.00 39.64  ? 133 VAL   C CG2 1 
ATOM   6142 N  N   . HIS   C  1  121 ? -1.766  9.284   30.263 1.00 38.60  ? 134 HIS   C N   1 
ATOM   6143 C  CA  . HIS   C  1  121 ? -1.532  10.691  29.988 1.00 43.13  ? 134 HIS   C CA  1 
ATOM   6144 C  C   . HIS   C  1  121 ? -0.048  11.013  29.870 1.00 42.51  ? 134 HIS   C C   1 
ATOM   6145 O  O   . HIS   C  1  121 ? 0.770   10.398  30.550 1.00 44.20  ? 134 HIS   C O   1 
ATOM   6146 C  CB  . HIS   C  1  121 ? -2.097  11.514  31.148 1.00 45.00  ? 134 HIS   C CB  1 
ATOM   6147 C  CG  . HIS   C  1  121 ? -1.822  12.976  31.066 1.00 46.35  ? 134 HIS   C CG  1 
ATOM   6148 N  ND1 . HIS   C  1  121 ? -2.421  13.781  30.117 1.00 54.81  ? 134 HIS   C ND1 1 
ATOM   6149 C  CD2 . HIS   C  1  121 ? -1.016  13.769  31.780 1.00 44.33  ? 134 HIS   C CD2 1 
ATOM   6150 C  CE1 . HIS   C  1  121 ? -2.007  15.034  30.291 1.00 56.54  ? 134 HIS   C CE1 1 
ATOM   6151 N  NE2 . HIS   C  1  121 ? -1.158  15.051  31.297 1.00 47.96  ? 134 HIS   C NE2 1 
ATOM   6152 N  N   . GLY   C  1  122 ? 0.288   11.977  28.997 1.00 48.06  ? 135 GLY   C N   1 
ATOM   6153 C  CA  . GLY   C  1  122 ? 1.509   12.756  29.147 1.00 53.47  ? 135 GLY   C CA  1 
ATOM   6154 C  C   . GLY   C  1  122 ? 2.515   12.624  28.000 1.00 56.22  ? 135 GLY   C C   1 
ATOM   6155 O  O   . GLY   C  1  122 ? 3.336   13.522  27.817 1.00 46.83  ? 135 GLY   C O   1 
ATOM   6156 N  N   . THR   C  1  123 ? 2.493   11.508  27.258 1.00 53.39  ? 136 THR   C N   1 
ATOM   6157 C  CA  A THR   C  1  123 ? 3.402   11.306  26.139 0.50 56.03  ? 136 THR   C CA  1 
ATOM   6158 C  CA  B THR   C  1  123 ? 3.406   11.350  26.134 0.50 53.88  ? 136 THR   C CA  1 
ATOM   6159 C  C   . THR   C  1  123 ? 2.607   11.217  24.834 1.00 52.66  ? 136 THR   C C   1 
ATOM   6160 O  O   . THR   C  1  123 ? 3.040   11.748  23.823 1.00 54.08  ? 136 THR   C O   1 
ATOM   6161 C  CB  A THR   C  1  123 ? 4.246   10.058  26.395 0.50 63.17  ? 136 THR   C CB  1 
ATOM   6162 C  CB  B THR   C  1  123 ? 4.407   10.216  26.402 0.50 59.05  ? 136 THR   C CB  1 
ATOM   6163 O  OG1 A THR   C  1  123 ? 3.279   9.017   26.507 0.50 75.67  ? 136 THR   C OG1 1 
ATOM   6164 O  OG1 B THR   C  1  123 ? 5.278   10.029  25.287 0.50 50.97  ? 136 THR   C OG1 1 
ATOM   6165 C  CG2 A THR   C  1  123 ? 5.085   10.167  27.658 0.50 59.73  ? 136 THR   C CG2 1 
ATOM   6166 C  CG2 B THR   C  1  123 ? 3.741   8.889   26.708 0.50 66.07  ? 136 THR   C CG2 1 
ATOM   6167 N  N   . PHE   C  1  124 ? 1.444   10.530  24.855 1.00 48.15  ? 137 PHE   C N   1 
ATOM   6168 C  CA  . PHE   C  1  124 ? 0.498   10.520  23.741 1.00 42.72  ? 137 PHE   C CA  1 
ATOM   6169 C  C   . PHE   C  1  124 ? -0.728  11.387  24.093 1.00 44.53  ? 137 PHE   C C   1 
ATOM   6170 O  O   . PHE   C  1  124 ? -0.772  12.568  23.729 1.00 45.63  ? 137 PHE   C O   1 
ATOM   6171 C  CB  . PHE   C  1  124 ? 0.119   9.095   23.314 1.00 39.36  ? 137 PHE   C CB  1 
ATOM   6172 C  CG  . PHE   C  1  124 ? -0.619  8.965   21.977 1.00 43.01  ? 137 PHE   C CG  1 
ATOM   6173 C  CD1 . PHE   C  1  124 ? -1.041  10.079  21.242 1.00 41.59  ? 137 PHE   C CD1 1 
ATOM   6174 C  CD2 . PHE   C  1  124 ? -0.927  7.708   21.465 1.00 38.89  ? 137 PHE   C CD2 1 
ATOM   6175 C  CE1 . PHE   C  1  124 ? -1.729  9.933   20.046 1.00 40.33  ? 137 PHE   C CE1 1 
ATOM   6176 C  CE2 . PHE   C  1  124 ? -1.574  7.568   20.251 1.00 37.93  ? 137 PHE   C CE2 1 
ATOM   6177 C  CZ  . PHE   C  1  124 ? -1.982  8.676   19.545 1.00 39.51  ? 137 PHE   C CZ  1 
ATOM   6178 N  N   . GLU   C  1  125 ? -1.741  10.810  24.770 1.00 41.84  ? 138 GLU   C N   1 
ATOM   6179 C  CA  . GLU   C  1  125 ? -2.914  11.563  25.215 1.00 43.12  ? 138 GLU   C CA  1 
ATOM   6180 C  C   . GLU   C  1  125 ? -2.480  12.829  25.964 1.00 44.28  ? 138 GLU   C C   1 
ATOM   6181 O  O   . GLU   C  1  125 ? -1.595  12.788  26.827 1.00 44.46  ? 138 GLU   C O   1 
ATOM   6182 C  CB  . GLU   C  1  125 ? -3.799  10.676  26.092 1.00 43.64  ? 138 GLU   C CB  1 
ATOM   6183 C  CG  . GLU   C  1  125 ? -5.101  11.318  26.571 1.00 49.40  ? 138 GLU   C CG  1 
ATOM   6184 C  CD  . GLU   C  1  125 ? -5.029  12.490  27.557 1.00 49.72  ? 138 GLU   C CD  1 
ATOM   6185 O  OE1 . GLU   C  1  125 ? -4.208  12.419  28.514 1.00 48.64  ? 138 GLU   C OE1 1 
ATOM   6186 O  OE2 . GLU   C  1  125 ? -5.809  13.470  27.377 1.00 48.13  ? 138 GLU   C OE2 1 
ATOM   6187 N  N   . GLY   C  1  126 ? -3.117  13.959  25.647 1.00 40.06  ? 139 GLY   C N   1 
ATOM   6188 C  CA  . GLY   C  1  126 ? -2.791  15.218  26.300 1.00 43.97  ? 139 GLY   C CA  1 
ATOM   6189 C  C   . GLY   C  1  126 ? -3.961  16.199  26.300 1.00 45.02  ? 139 GLY   C C   1 
ATOM   6190 O  O   . GLY   C  1  126 ? -5.106  15.802  26.119 1.00 42.30  ? 139 GLY   C O   1 
ATOM   6191 N  N   . ASP   C  1  127 ? -3.634  17.492  26.444 1.00 49.14  ? 140 ASP   C N   1 
ATOM   6192 C  CA  . ASP   C  1  127 ? -4.567  18.486  26.950 1.00 49.21  ? 140 ASP   C CA  1 
ATOM   6193 C  C   . ASP   C  1  127 ? -5.225  19.280  25.822 1.00 48.68  ? 140 ASP   C C   1 
ATOM   6194 O  O   . ASP   C  1  127 ? -4.797  19.237  24.681 1.00 43.35  ? 140 ASP   C O   1 
ATOM   6195 C  CB  . ASP   C  1  127 ? -3.856  19.426  27.916 1.00 51.07  ? 140 ASP   C CB  1 
ATOM   6196 C  CG  . ASP   C  1  127 ? -3.220  18.790  29.142 1.00 49.31  ? 140 ASP   C CG  1 
ATOM   6197 O  OD1 . ASP   C  1  127 ? -3.816  17.809  29.661 1.00 44.90  ? 140 ASP   C OD1 1 
ATOM   6198 O  OD2 . ASP   C  1  127 ? -2.131  19.288  29.572 1.00 50.76  ? 140 ASP   C OD2 1 
ATOM   6199 N  N   . ALA   C  1  128 ? -6.257  20.055  26.179 1.00 50.48  ? 141 ALA   C N   1 
ATOM   6200 C  CA  . ALA   C  1  128 ? -6.971  20.950  25.271 1.00 46.15  ? 141 ALA   C CA  1 
ATOM   6201 C  C   . ALA   C  1  128 ? -7.704  20.158  24.185 1.00 45.96  ? 141 ALA   C C   1 
ATOM   6202 O  O   . ALA   C  1  128 ? -7.772  20.582  23.040 1.00 49.32  ? 141 ALA   C O   1 
ATOM   6203 C  CB  . ALA   C  1  128 ? -6.035  21.999  24.687 1.00 41.49  ? 141 ALA   C CB  1 
ATOM   6204 N  N   . GLY   C  1  129 ? -8.310  19.036  24.568 1.00 44.63  ? 142 GLY   C N   1 
ATOM   6205 C  CA  . GLY   C  1  129 ? -9.213  18.314  23.687 1.00 50.17  ? 142 GLY   C CA  1 
ATOM   6206 C  C   . GLY   C  1  129 ? -10.534 19.055  23.470 1.00 55.78  ? 142 GLY   C C   1 
ATOM   6207 O  O   . GLY   C  1  129 ? -10.846 20.003  24.180 1.00 58.05  ? 142 GLY   C O   1 
ATOM   6208 N  N   . MET   C  1  130 ? -11.310 18.578  22.493 1.00 56.44  ? 143 MET   C N   1 
ATOM   6209 C  CA  . MET   C  1  130 ? -12.568 19.191  22.104 1.00 54.87  ? 143 MET   C CA  1 
ATOM   6210 C  C   . MET   C  1  130 ? -13.718 18.728  23.001 1.00 52.28  ? 143 MET   C C   1 
ATOM   6211 O  O   . MET   C  1  130 ? -14.551 19.544  23.396 1.00 51.31  ? 143 MET   C O   1 
ATOM   6212 C  CB  . MET   C  1  130 ? -12.913 18.820  20.658 1.00 59.27  ? 143 MET   C CB  1 
ATOM   6213 C  CG  . MET   C  1  130 ? -12.057 19.505  19.585 1.00 66.91  ? 143 MET   C CG  1 
ATOM   6214 S  SD  . MET   C  1  130 ? -12.426 18.943  17.899 1.00 62.22  ? 143 MET   C SD  1 
ATOM   6215 C  CE  . MET   C  1  130 ? -11.973 17.205  17.961 1.00 53.63  ? 143 MET   C CE  1 
ATOM   6216 N  N   . THR   C  1  131 ? -13.804 17.414  23.270 1.00 45.94  ? 144 THR   C N   1 
ATOM   6217 C  CA  . THR   C  1  131 ? -14.916 16.868  24.029 1.00 46.80  ? 144 THR   C CA  1 
ATOM   6218 C  C   . THR   C  1  131 ? -14.447 16.114  25.276 1.00 45.26  ? 144 THR   C C   1 
ATOM   6219 O  O   . THR   C  1  131 ? -15.276 15.542  25.985 1.00 47.89  ? 144 THR   C O   1 
ATOM   6220 C  CB  . THR   C  1  131 ? -15.792 15.972  23.148 1.00 45.85  ? 144 THR   C CB  1 
ATOM   6221 O  OG1 . THR   C  1  131 ? -15.115 14.750  22.886 1.00 41.87  ? 144 THR   C OG1 1 
ATOM   6222 C  CG2 . THR   C  1  131 ? -16.205 16.655  21.856 1.00 48.09  ? 144 THR   C CG2 1 
ATOM   6223 N  N   . ARG   C  1  132 ? -13.139 16.098  25.541 1.00 43.84  ? 145 ARG   C N   1 
ATOM   6224 C  CA  . ARG   C  1  132 ? -12.609 15.480  26.750 1.00 45.79  ? 145 ARG   C CA  1 
ATOM   6225 C  C   . ARG   C  1  132 ? -11.850 16.533  27.560 1.00 46.73  ? 145 ARG   C C   1 
ATOM   6226 O  O   . ARG   C  1  132 ? -11.197 17.382  26.959 1.00 46.75  ? 145 ARG   C O   1 
ATOM   6227 C  CB  . ARG   C  1  132 ? -11.671 14.320  26.401 1.00 43.78  ? 145 ARG   C CB  1 
ATOM   6228 C  CG  . ARG   C  1  132 ? -12.358 12.973  26.224 1.00 48.96  ? 145 ARG   C CG  1 
ATOM   6229 C  CD  . ARG   C  1  132 ? -13.220 12.864  24.968 1.00 44.68  ? 145 ARG   C CD  1 
ATOM   6230 N  NE  . ARG   C  1  132 ? -13.891 11.564  25.025 1.00 49.49  ? 145 ARG   C NE  1 
ATOM   6231 C  CZ  . ARG   C  1  132 ? -14.943 11.185  24.321 1.00 53.07  ? 145 ARG   C CZ  1 
ATOM   6232 N  NH1 . ARG   C  1  132 ? -15.528 12.040  23.490 1.00 47.12  ? 145 ARG   C NH1 1 
ATOM   6233 N  NH2 . ARG   C  1  132 ? -15.402 9.954   24.492 1.00 54.93  ? 145 ARG   C NH2 1 
ATOM   6234 N  N   . ALA   C  1  133 ? -11.940 16.458  28.904 1.00 47.86  ? 146 ALA   C N   1 
ATOM   6235 C  CA  . ALA   C  1  133 ? -11.283 17.413  29.778 1.00 50.99  ? 146 ALA   C CA  1 
ATOM   6236 C  C   . ALA   C  1  133 ? -9.838  16.970  30.029 1.00 48.66  ? 146 ALA   C C   1 
ATOM   6237 O  O   . ALA   C  1  133 ? -9.532  15.775  29.979 1.00 38.33  ? 146 ALA   C O   1 
ATOM   6238 N  N   . ASP   C  1  134 ? -8.968  17.943  30.351 1.00 48.56  ? 147 ASP   C N   1 
ATOM   6239 C  CA  . ASP   C  1  134 ? -7.581  17.692  30.714 1.00 46.57  ? 147 ASP   C CA  1 
ATOM   6240 C  C   . ASP   C  1  134 ? -7.527  16.715  31.882 1.00 50.96  ? 147 ASP   C C   1 
ATOM   6241 O  O   . ASP   C  1  134 ? -8.420  16.712  32.731 1.00 51.73  ? 147 ASP   C O   1 
ATOM   6242 C  CB  . ASP   C  1  134 ? -6.838  18.974  31.041 1.00 43.50  ? 147 ASP   C CB  1 
ATOM   6243 C  CG  . ASP   C  1  134 ? -6.753  19.978  29.900 1.00 50.33  ? 147 ASP   C CG  1 
ATOM   6244 O  OD1 . ASP   C  1  134 ? -7.365  19.696  28.845 1.00 55.34  ? 147 ASP   C OD1 1 
ATOM   6245 O  OD2 . ASP   C  1  134 ? -6.059  21.025  30.051 1.00 44.78  ? 147 ASP   C OD2 1 
ATOM   6246 N  N   . GLU   C  1  135 ? -6.477  15.883  31.890 1.00 47.74  ? 148 GLU   C N   1 
ATOM   6247 C  CA  . GLU   C  1  135 ? -6.281  14.848  32.891 1.00 47.74  ? 148 GLU   C CA  1 
ATOM   6248 C  C   . GLU   C  1  135 ? -6.198  15.451  34.297 1.00 52.64  ? 148 GLU   C C   1 
ATOM   6249 O  O   . GLU   C  1  135 ? -6.604  14.797  35.265 1.00 42.16  ? 148 GLU   C O   1 
ATOM   6250 C  CB  . GLU   C  1  135 ? -5.003  14.060  32.599 1.00 47.80  ? 148 GLU   C CB  1 
ATOM   6251 C  CG  . GLU   C  1  135 ? -4.843  12.830  33.489 1.00 53.85  ? 148 GLU   C CG  1 
ATOM   6252 C  CD  . GLU   C  1  135 ? -4.044  13.054  34.769 1.00 61.86  ? 148 GLU   C CD  1 
ATOM   6253 O  OE1 . GLU   C  1  135 ? -3.614  14.199  35.092 1.00 55.20  ? 148 GLU   C OE1 1 
ATOM   6254 O  OE2 . GLU   C  1  135 ? -3.835  12.022  35.439 1.00 70.13  ? 148 GLU   C OE2 1 
ATOM   6255 N  N   . PHE   C  1  136 ? -5.671  16.683  34.394 1.00 54.17  ? 149 PHE   C N   1 
ATOM   6256 C  CA  . PHE   C  1  136 ? -5.542  17.383  35.659 1.00 60.56  ? 149 PHE   C CA  1 
ATOM   6257 C  C   . PHE   C  1  136 ? -6.880  17.425  36.396 1.00 57.25  ? 149 PHE   C C   1 
ATOM   6258 O  O   . PHE   C  1  136 ? -6.888  17.325  37.609 1.00 55.15  ? 149 PHE   C O   1 
ATOM   6259 C  CB  . PHE   C  1  136 ? -5.022  18.811  35.477 1.00 65.58  ? 149 PHE   C CB  1 
ATOM   6260 C  CG  . PHE   C  1  136 ? -4.955  19.562  36.799 1.00 76.08  ? 149 PHE   C CG  1 
ATOM   6261 C  CD1 . PHE   C  1  136 ? -4.045  19.193  37.786 1.00 79.75  ? 149 PHE   C CD1 1 
ATOM   6262 C  CD2 . PHE   C  1  136 ? -5.814  20.621  37.066 1.00 79.81  ? 149 PHE   C CD2 1 
ATOM   6263 C  CE1 . PHE   C  1  136 ? -3.985  19.871  38.996 1.00 81.76  ? 149 PHE   C CE1 1 
ATOM   6264 C  CE2 . PHE   C  1  136 ? -5.745  21.310  38.271 1.00 79.35  ? 149 PHE   C CE2 1 
ATOM   6265 C  CZ  . PHE   C  1  136 ? -4.823  20.941  39.228 1.00 81.41  ? 149 PHE   C CZ  1 
ATOM   6266 N  N   . PHE   C  1  137 ? -7.992  17.569  35.668 1.00 53.71  ? 150 PHE   C N   1 
ATOM   6267 C  CA  . PHE   C  1  137 ? -9.302  17.709  36.283 1.00 52.23  ? 150 PHE   C CA  1 
ATOM   6268 C  C   . PHE   C  1  137 ? -9.968  16.361  36.580 1.00 53.44  ? 150 PHE   C C   1 
ATOM   6269 O  O   . PHE   C  1  137 ? -11.118 16.353  37.027 1.00 57.52  ? 150 PHE   C O   1 
ATOM   6270 C  CB  . PHE   C  1  137 ? -10.214 18.540  35.379 1.00 52.99  ? 150 PHE   C CB  1 
ATOM   6271 C  CG  . PHE   C  1  137 ? -9.646  19.893  34.981 1.00 55.61  ? 150 PHE   C CG  1 
ATOM   6272 C  CD1 . PHE   C  1  137 ? -9.204  20.802  35.933 1.00 56.79  ? 150 PHE   C CD1 1 
ATOM   6273 C  CD2 . PHE   C  1  137 ? -9.557  20.245  33.637 1.00 56.38  ? 150 PHE   C CD2 1 
ATOM   6274 C  CE1 . PHE   C  1  137 ? -8.687  22.029  35.545 1.00 58.63  ? 150 PHE   C CE1 1 
ATOM   6275 C  CE2 . PHE   C  1  137 ? -9.048  21.478  33.254 1.00 55.58  ? 150 PHE   C CE2 1 
ATOM   6276 C  CZ  . PHE   C  1  137 ? -8.614  22.366  34.209 1.00 59.87  ? 150 PHE   C CZ  1 
ATOM   6277 N  N   . GLY   C  1  138 ? -9.305  15.222  36.336 1.00 50.68  ? 151 GLY   C N   1 
ATOM   6278 C  CA  . GLY   C  1  138 ? -9.740  13.978  36.959 1.00 49.76  ? 151 GLY   C CA  1 
ATOM   6279 C  C   . GLY   C  1  138 ? -10.215 12.897  35.991 1.00 56.44  ? 151 GLY   C C   1 
ATOM   6280 O  O   . GLY   C  1  138 ? -10.273 11.735  36.390 1.00 61.27  ? 151 GLY   C O   1 
ATOM   6281 N  N   . ASP   C  1  139 ? -10.563 13.262  34.744 1.00 63.39  ? 152 ASP   C N   1 
ATOM   6282 C  CA  . ASP   C  1  139 ? -11.066 12.295  33.768 1.00 64.70  ? 152 ASP   C CA  1 
ATOM   6283 C  C   . ASP   C  1  139 ? -10.724 12.740  32.343 1.00 62.43  ? 152 ASP   C C   1 
ATOM   6284 O  O   . ASP   C  1  139 ? -11.332 13.687  31.823 1.00 52.46  ? 152 ASP   C O   1 
ATOM   6285 C  CB  . ASP   C  1  139 ? -12.561 12.067  33.929 1.00 65.58  ? 152 ASP   C CB  1 
ATOM   6286 C  CG  . ASP   C  1  139 ? -13.184 11.018  33.015 1.00 72.52  ? 152 ASP   C CG  1 
ATOM   6287 O  OD1 . ASP   C  1  139 ? -12.560 10.678  31.998 1.00 72.17  ? 152 ASP   C OD1 1 
ATOM   6288 O  OD2 . ASP   C  1  139 ? -14.284 10.530  33.340 1.00 73.36  ? 152 ASP   C OD2 1 
ATOM   6289 N  N   . ASN   C  1  140 ? -9.783  12.020  31.701 1.00 54.37  ? 153 ASN   C N   1 
ATOM   6290 C  CA  . ASN   C  1  140 ? -9.279  12.439  30.398 1.00 51.30  ? 153 ASN   C CA  1 
ATOM   6291 C  C   . ASN   C  1  140 ? -9.919  11.665  29.245 1.00 46.55  ? 153 ASN   C C   1 
ATOM   6292 O  O   . ASN   C  1  140 ? -9.536  11.898  28.106 1.00 55.83  ? 153 ASN   C O   1 
ATOM   6293 C  CB  . ASN   C  1  140 ? -7.762  12.315  30.291 1.00 46.47  ? 153 ASN   C CB  1 
ATOM   6294 C  CG  . ASN   C  1  140 ? -7.267  10.887  30.304 1.00 45.40  ? 153 ASN   C CG  1 
ATOM   6295 O  OD1 . ASN   C  1  140 ? -8.015  9.940   30.580 1.00 41.80  ? 153 ASN   C OD1 1 
ATOM   6296 N  ND2 . ASN   C  1  140 ? -5.980  10.715  30.046 1.00 50.64  ? 153 ASN   C ND2 1 
ATOM   6297 N  N   . HIS   C  1  141 ? -10.876 10.769  29.527 1.00 48.70  ? 154 HIS   C N   1 
ATOM   6298 C  CA  . HIS   C  1  141 ? -11.362 9.817   28.540 1.00 56.47  ? 154 HIS   C CA  1 
ATOM   6299 C  C   . HIS   C  1  141 ? -12.859 9.971   28.271 1.00 58.17  ? 154 HIS   C C   1 
ATOM   6300 O  O   . HIS   C  1  141 ? -13.301 9.713   27.156 1.00 57.75  ? 154 HIS   C O   1 
ATOM   6301 C  CB  . HIS   C  1  141 ? -10.939 8.388   28.920 1.00 59.80  ? 154 HIS   C CB  1 
ATOM   6302 C  CG  . HIS   C  1  141 ? -11.371 7.961   30.269 1.00 64.41  ? 154 HIS   C CG  1 
ATOM   6303 N  ND1 . HIS   C  1  141 ? -10.659 8.265   31.410 1.00 75.13  ? 154 HIS   C ND1 1 
ATOM   6304 C  CD2 . HIS   C  1  141 ? -12.430 7.241   30.656 1.00 69.15  ? 154 HIS   C CD2 1 
ATOM   6305 C  CE1 . HIS   C  1  141 ? -11.290 7.755   32.461 1.00 81.19  ? 154 HIS   C CE1 1 
ATOM   6306 N  NE2 . HIS   C  1  141 ? -12.365 7.128   32.025 1.00 76.14  ? 154 HIS   C NE2 1 
ATOM   6307 N  N   . SER   C  1  142 ? -13.637 10.360  29.288 1.00 59.56  ? 155 SER   C N   1 
ATOM   6308 C  CA  . SER   C  1  142 ? -15.084 10.436  29.171 1.00 55.38  ? 155 SER   C CA  1 
ATOM   6309 C  C   . SER   C  1  142 ? -15.492 11.634  28.330 1.00 51.19  ? 155 SER   C C   1 
ATOM   6310 O  O   . SER   C  1  142 ? -14.878 12.703  28.370 1.00 45.63  ? 155 SER   C O   1 
ATOM   6311 C  CB  . SER   C  1  142 ? -15.755 10.537  30.526 1.00 60.27  ? 155 SER   C CB  1 
ATOM   6312 O  OG  . SER   C  1  142 ? -15.679 9.299   31.214 1.00 57.93  ? 155 SER   C OG  1 
ATOM   6313 N  N   . PHE   C  1  143 ? -16.609 11.458  27.630 1.00 50.46  ? 156 PHE   C N   1 
ATOM   6314 C  CA  . PHE   C  1  143 ? -17.278 12.589  27.019 1.00 51.42  ? 156 PHE   C CA  1 
ATOM   6315 C  C   . PHE   C  1  143 ? -17.679 13.587  28.103 1.00 50.58  ? 156 PHE   C C   1 
ATOM   6316 O  O   . PHE   C  1  143 ? -18.179 13.203  29.153 1.00 50.17  ? 156 PHE   C O   1 
ATOM   6317 C  CB  . PHE   C  1  143 ? -18.484 12.070  26.246 1.00 51.52  ? 156 PHE   C CB  1 
ATOM   6318 C  CG  . PHE   C  1  143 ? -19.334 13.189  25.668 1.00 54.01  ? 156 PHE   C CG  1 
ATOM   6319 C  CD1 . PHE   C  1  143 ? -19.069 13.714  24.413 1.00 48.38  ? 156 PHE   C CD1 1 
ATOM   6320 C  CD2 . PHE   C  1  143 ? -20.425 13.684  26.386 1.00 58.52  ? 156 PHE   C CD2 1 
ATOM   6321 C  CE1 . PHE   C  1  143 ? -19.897 14.688  23.881 1.00 52.61  ? 156 PHE   C CE1 1 
ATOM   6322 C  CE2 . PHE   C  1  143 ? -21.238 14.671  25.853 1.00 57.94  ? 156 PHE   C CE2 1 
ATOM   6323 C  CZ  . PHE   C  1  143 ? -20.975 15.165  24.599 1.00 53.69  ? 156 PHE   C CZ  1 
ATOM   6324 N  N   . ASN   C  1  144 ? -17.481 14.869  27.807 1.00 51.03  ? 157 ASN   C N   1 
ATOM   6325 C  CA  . ASN   C  1  144 ? -17.776 15.935  28.734 1.00 51.09  ? 157 ASN   C CA  1 
ATOM   6326 C  C   . ASN   C  1  144 ? -18.746 16.915  28.071 1.00 53.05  ? 157 ASN   C C   1 
ATOM   6327 O  O   . ASN   C  1  144 ? -18.390 17.616  27.125 1.00 47.82  ? 157 ASN   C O   1 
ATOM   6328 C  CB  . ASN   C  1  144 ? -16.460 16.534  29.183 1.00 56.97  ? 157 ASN   C CB  1 
ATOM   6329 C  CG  . ASN   C  1  144 ? -16.623 17.784  30.012 1.00 68.07  ? 157 ASN   C CG  1 
ATOM   6330 O  OD1 . ASN   C  1  144 ? -17.347 18.704  29.604 1.00 58.52  ? 157 ASN   C OD1 1 
ATOM   6331 N  ND2 . ASN   C  1  144 ? -15.975 17.810  31.172 1.00 75.89  ? 157 ASN   C ND2 1 
ATOM   6332 N  N   . GLN   C  1  145 ? -19.965 16.966  28.620 1.00 59.46  ? 158 GLN   C N   1 
ATOM   6333 C  CA  . GLN   C  1  145 ? -21.092 17.680  28.037 1.00 58.98  ? 158 GLN   C CA  1 
ATOM   6334 C  C   . GLN   C  1  145 ? -20.826 19.186  28.007 1.00 54.59  ? 158 GLN   C C   1 
ATOM   6335 O  O   . GLN   C  1  145 ? -21.211 19.849  27.047 1.00 53.90  ? 158 GLN   C O   1 
ATOM   6336 C  CB  . GLN   C  1  145 ? -22.357 17.309  28.819 1.00 61.72  ? 158 GLN   C CB  1 
ATOM   6337 C  CG  . GLN   C  1  145 ? -23.650 17.927  28.286 1.00 61.42  ? 158 GLN   C CG  1 
ATOM   6338 C  CD  . GLN   C  1  145 ? -23.998 17.489  26.883 1.00 58.31  ? 158 GLN   C CD  1 
ATOM   6339 O  OE1 . GLN   C  1  145 ? -24.132 16.293  26.585 1.00 57.86  ? 158 GLN   C OE1 1 
ATOM   6340 N  NE2 . GLN   C  1  145 ? -24.166 18.469  26.006 1.00 59.92  ? 158 GLN   C NE2 1 
ATOM   6341 N  N   . THR   C  1  146 ? -20.160 19.725  29.038 1.00 51.81  ? 159 THR   C N   1 
ATOM   6342 C  CA  . THR   C  1  146 ? -19.835 21.148  29.082 1.00 59.06  ? 159 THR   C CA  1 
ATOM   6343 C  C   . THR   C  1  146 ? -18.975 21.515  27.880 1.00 57.99  ? 159 THR   C C   1 
ATOM   6344 O  O   . THR   C  1  146 ? -19.159 22.571  27.277 1.00 57.71  ? 159 THR   C O   1 
ATOM   6345 C  CB  . THR   C  1  146 ? -19.097 21.530  30.369 1.00 61.51  ? 159 THR   C CB  1 
ATOM   6346 O  OG1 . THR   C  1  146 ? -19.906 21.127  31.468 1.00 59.41  ? 159 THR   C OG1 1 
ATOM   6347 C  CG2 . THR   C  1  146 ? -18.809 23.019  30.464 1.00 58.67  ? 159 THR   C CG2 1 
ATOM   6348 N  N   . LEU   C  1  147 ? -17.985 20.663  27.589 1.00 63.38  ? 160 LEU   C N   1 
ATOM   6349 C  CA  . LEU   C  1  147 ? -17.094 20.919  26.469 1.00 60.44  ? 160 LEU   C CA  1 
ATOM   6350 C  C   . LEU   C  1  147 ? -17.837 20.777  25.144 1.00 49.34  ? 160 LEU   C C   1 
ATOM   6351 O  O   . LEU   C  1  147 ? -17.616 21.551  24.223 1.00 47.54  ? 160 LEU   C O   1 
ATOM   6352 C  CB  . LEU   C  1  147 ? -15.885 19.991  26.565 1.00 61.17  ? 160 LEU   C CB  1 
ATOM   6353 C  CG  . LEU   C  1  147 ? -14.883 20.369  27.660 1.00 58.76  ? 160 LEU   C CG  1 
ATOM   6354 C  CD1 . LEU   C  1  147 ? -13.721 19.389  27.637 1.00 57.78  ? 160 LEU   C CD1 1 
ATOM   6355 C  CD2 . LEU   C  1  147 ? -14.397 21.813  27.501 1.00 51.26  ? 160 LEU   C CD2 1 
ATOM   6356 N  N   . PHE   C  1  148 ? -18.734 19.802  25.066 1.00 45.41  ? 161 PHE   C N   1 
ATOM   6357 C  CA  . PHE   C  1  148 ? -19.554 19.638  23.883 1.00 49.55  ? 161 PHE   C CA  1 
ATOM   6358 C  C   . PHE   C  1  148 ? -20.462 20.855  23.697 1.00 54.38  ? 161 PHE   C C   1 
ATOM   6359 O  O   . PHE   C  1  148 ? -20.677 21.251  22.558 1.00 53.54  ? 161 PHE   C O   1 
ATOM   6360 C  CB  . PHE   C  1  148 ? -20.356 18.335  23.933 1.00 50.61  ? 161 PHE   C CB  1 
ATOM   6361 C  CG  . PHE   C  1  148 ? -21.096 18.104  22.629 1.00 57.49  ? 161 PHE   C CG  1 
ATOM   6362 C  CD1 . PHE   C  1  148 ? -20.409 17.666  21.502 1.00 63.81  ? 161 PHE   C CD1 1 
ATOM   6363 C  CD2 . PHE   C  1  148 ? -22.452 18.377  22.514 1.00 63.37  ? 161 PHE   C CD2 1 
ATOM   6364 C  CE1 . PHE   C  1  148 ? -21.065 17.464  20.301 1.00 71.44  ? 161 PHE   C CE1 1 
ATOM   6365 C  CE2 . PHE   C  1  148 ? -23.105 18.170  21.303 1.00 67.04  ? 161 PHE   C CE2 1 
ATOM   6366 C  CZ  . PHE   C  1  148 ? -22.410 17.705  20.202 1.00 68.50  ? 161 PHE   C CZ  1 
ATOM   6367 N  N   . ASP   C  1  149 ? -20.972 21.450  24.795 1.00 58.03  ? 162 ASP   C N   1 
ATOM   6368 C  CA  . ASP   C  1  149 ? -21.785 22.665  24.717 1.00 54.73  ? 162 ASP   C CA  1 
ATOM   6369 C  C   . ASP   C  1  149 ? -20.981 23.819  24.110 1.00 47.31  ? 162 ASP   C C   1 
ATOM   6370 O  O   . ASP   C  1  149 ? -21.506 24.595  23.313 1.00 55.14  ? 162 ASP   C O   1 
ATOM   6371 C  CB  . ASP   C  1  149 ? -22.386 23.045  26.068 1.00 57.10  ? 162 ASP   C CB  1 
ATOM   6372 C  CG  . ASP   C  1  149 ? -23.424 22.077  26.633 1.00 66.59  ? 162 ASP   C CG  1 
ATOM   6373 O  OD1 . ASP   C  1  149 ? -24.054 21.332  25.833 1.00 64.67  ? 162 ASP   C OD1 1 
ATOM   6374 O  OD2 . ASP   C  1  149 ? -23.569 22.031  27.878 1.00 76.46  ? 162 ASP   C OD2 1 
ATOM   6375 N  N   . LYS   C  1  150 ? -19.696 23.926  24.458 1.00 49.03  ? 163 LYS   C N   1 
ATOM   6376 C  CA  . LYS   C  1  150 ? -18.828 24.933  23.861 1.00 54.13  ? 163 LYS   C CA  1 
ATOM   6377 C  C   . LYS   C  1  150 ? -18.613 24.643  22.370 1.00 63.00  ? 163 LYS   C C   1 
ATOM   6378 O  O   . LYS   C  1  150 ? -18.565 25.563  21.555 1.00 58.03  ? 163 LYS   C O   1 
ATOM   6379 C  CB  . LYS   C  1  150 ? -17.510 24.976  24.636 1.00 53.85  ? 163 LYS   C CB  1 
ATOM   6380 C  CG  . LYS   C  1  150 ? -16.467 25.947  24.088 1.00 57.62  ? 163 LYS   C CG  1 
ATOM   6381 C  CD  . LYS   C  1  150 ? -15.151 25.870  24.852 1.00 59.15  ? 163 LYS   C CD  1 
ATOM   6382 C  CE  . LYS   C  1  150 ? -14.092 26.794  24.354 1.00 62.09  ? 163 LYS   C CE  1 
ATOM   6383 N  NZ  . LYS   C  1  150 ? -13.857 27.912  25.268 1.00 64.49  ? 163 LYS   C NZ  1 
ATOM   6384 N  N   . PHE   C  1  151 ? -18.485 23.359  22.009 1.00 65.25  ? 164 PHE   C N   1 
ATOM   6385 C  CA  . PHE   C  1  151 ? -18.326 22.959  20.617 1.00 69.59  ? 164 PHE   C CA  1 
ATOM   6386 C  C   . PHE   C  1  151 ? -19.544 23.417  19.815 1.00 63.73  ? 164 PHE   C C   1 
ATOM   6387 O  O   . PHE   C  1  151 ? -19.407 23.964  18.726 1.00 54.53  ? 164 PHE   C O   1 
ATOM   6388 C  CB  . PHE   C  1  151 ? -18.119 21.439  20.592 1.00 68.17  ? 164 PHE   C CB  1 
ATOM   6389 C  CG  . PHE   C  1  151 ? -18.068 20.771  19.226 1.00 68.30  ? 164 PHE   C CG  1 
ATOM   6390 C  CD1 . PHE   C  1  151 ? -16.864 20.655  18.547 1.00 66.63  ? 164 PHE   C CD1 1 
ATOM   6391 C  CD2 . PHE   C  1  151 ? -19.217 20.235  18.640 1.00 65.50  ? 164 PHE   C CD2 1 
ATOM   6392 C  CE1 . PHE   C  1  151 ? -16.812 20.031  17.311 1.00 66.36  ? 164 PHE   C CE1 1 
ATOM   6393 C  CE2 . PHE   C  1  151 ? -19.155 19.624  17.396 1.00 62.98  ? 164 PHE   C CE2 1 
ATOM   6394 C  CZ  . PHE   C  1  151 ? -17.952 19.524  16.737 1.00 58.97  ? 164 PHE   C CZ  1 
ATOM   6395 N  N   . VAL   C  1  152 ? -20.737 23.197  20.377 1.00 64.94  ? 165 VAL   C N   1 
ATOM   6396 C  CA  . VAL   C  1  152 ? -21.975 23.643  19.753 1.00 65.24  ? 165 VAL   C CA  1 
ATOM   6397 C  C   . VAL   C  1  152 ? -21.989 25.170  19.674 1.00 61.10  ? 165 VAL   C C   1 
ATOM   6398 O  O   . VAL   C  1  152 ? -22.320 25.744  18.635 1.00 59.64  ? 165 VAL   C O   1 
ATOM   6399 C  CB  . VAL   C  1  152 ? -23.178 23.091  20.543 1.00 68.85  ? 165 VAL   C CB  1 
ATOM   6400 C  CG1 . VAL   C  1  152 ? -24.507 23.715  20.132 1.00 68.92  ? 165 VAL   C CG1 1 
ATOM   6401 C  CG2 . VAL   C  1  152 ? -23.257 21.571  20.445 1.00 69.43  ? 165 VAL   C CG2 1 
ATOM   6402 N  N   . ASP   C  1  153 ? -21.601 25.826  20.771 1.00 67.09  ? 166 ASP   C N   1 
ATOM   6403 C  CA  . ASP   C  1  153 ? -21.587 27.277  20.807 1.00 76.17  ? 166 ASP   C CA  1 
ATOM   6404 C  C   . ASP   C  1  153 ? -20.736 27.831  19.664 1.00 64.81  ? 166 ASP   C C   1 
ATOM   6405 O  O   . ASP   C  1  153 ? -21.180 28.703  18.917 1.00 67.30  ? 166 ASP   C O   1 
ATOM   6406 C  CB  . ASP   C  1  153 ? -21.168 27.807  22.174 1.00 80.21  ? 166 ASP   C CB  1 
ATOM   6407 C  CG  . ASP   C  1  153 ? -21.265 29.328  22.298 1.00 85.68  ? 166 ASP   C CG  1 
ATOM   6408 O  OD1 . ASP   C  1  153 ? -22.318 29.878  21.906 1.00 84.15  ? 166 ASP   C OD1 1 
ATOM   6409 O  OD2 . ASP   C  1  153 ? -20.290 29.967  22.764 1.00 83.03  ? 166 ASP   C OD2 1 
ATOM   6410 N  N   . PHE   C  1  154 ? -19.502 27.331  19.537 1.00 69.66  ? 167 PHE   C N   1 
ATOM   6411 C  CA  . PHE   C  1  154 ? -18.579 27.818  18.523 1.00 62.87  ? 167 PHE   C CA  1 
ATOM   6412 C  C   . PHE   C  1  154 ? -19.074 27.452  17.123 1.00 59.02  ? 167 PHE   C C   1 
ATOM   6413 O  O   . PHE   C  1  154 ? -18.840 28.202  16.185 1.00 49.92  ? 167 PHE   C O   1 
ATOM   6414 C  CB  . PHE   C  1  154 ? -17.169 27.270  18.757 1.00 58.54  ? 167 PHE   C CB  1 
ATOM   6415 C  CG  . PHE   C  1  154 ? -16.335 28.138  19.679 1.00 60.12  ? 167 PHE   C CG  1 
ATOM   6416 C  CD1 . PHE   C  1  154 ? -16.697 28.298  21.006 1.00 59.39  ? 167 PHE   C CD1 1 
ATOM   6417 C  CD2 . PHE   C  1  154 ? -15.199 28.803  19.216 1.00 57.62  ? 167 PHE   C CD2 1 
ATOM   6418 C  CE1 . PHE   C  1  154 ? -15.942 29.104  21.852 1.00 61.75  ? 167 PHE   C CE1 1 
ATOM   6419 C  CE2 . PHE   C  1  154 ? -14.451 29.603  20.065 1.00 53.25  ? 167 PHE   C CE2 1 
ATOM   6420 C  CZ  . PHE   C  1  154 ? -14.829 29.766  21.375 1.00 55.62  ? 167 PHE   C CZ  1 
ATOM   6421 N  N   . SER   C  1  155 ? -19.729 26.299  16.960 1.00 59.55  ? 168 SER   C N   1 
ATOM   6422 C  CA  . SER   C  1  155 ? -20.301 25.976  15.664 1.00 67.19  ? 168 SER   C CA  1 
ATOM   6423 C  C   . SER   C  1  155 ? -21.413 26.975  15.324 1.00 73.20  ? 168 SER   C C   1 
ATOM   6424 O  O   . SER   C  1  155 ? -21.594 27.345  14.163 1.00 62.17  ? 168 SER   C O   1 
ATOM   6425 C  CB  . SER   C  1  155 ? -20.819 24.556  15.610 1.00 69.83  ? 168 SER   C CB  1 
ATOM   6426 O  OG  . SER   C  1  155 ? -19.802 23.611  15.911 1.00 64.01  ? 168 SER   C OG  1 
ATOM   6427 N  N   . ASN   C  1  156 ? -22.185 27.399  16.336 1.00 74.95  ? 169 ASN   C N   1 
ATOM   6428 C  CA  . ASN   C  1  156 ? -23.236 28.389  16.110 1.00 74.12  ? 169 ASN   C CA  1 
ATOM   6429 C  C   . ASN   C  1  156 ? -22.629 29.734  15.738 1.00 69.75  ? 169 ASN   C C   1 
ATOM   6430 O  O   . ASN   C  1  156 ? -23.127 30.392  14.840 1.00 66.86  ? 169 ASN   C O   1 
ATOM   6431 C  CB  . ASN   C  1  156 ? -24.154 28.577  17.311 1.00 71.56  ? 169 ASN   C CB  1 
ATOM   6432 C  CG  . ASN   C  1  156 ? -25.096 27.406  17.504 1.00 74.67  ? 169 ASN   C CG  1 
ATOM   6433 O  OD1 . ASN   C  1  156 ? -25.361 26.616  16.586 1.00 76.61  ? 169 ASN   C OD1 1 
ATOM   6434 N  ND2 . ASN   C  1  156 ? -25.630 27.270  18.702 1.00 66.71  ? 169 ASN   C ND2 1 
ATOM   6435 N  N   . ARG   C  1  157 ? -21.555 30.127  16.426 1.00 73.00  ? 170 ARG   C N   1 
ATOM   6436 C  CA  . ARG   C  1  157 ? -20.984 31.455  16.270 1.00 76.10  ? 170 ARG   C CA  1 
ATOM   6437 C  C   . ARG   C  1  157 ? -20.249 31.601  14.938 1.00 72.09  ? 170 ARG   C C   1 
ATOM   6438 O  O   . ARG   C  1  157 ? -20.298 32.675  14.348 1.00 68.91  ? 170 ARG   C O   1 
ATOM   6439 C  CB  . ARG   C  1  157 ? -20.052 31.774  17.441 1.00 82.44  ? 170 ARG   C CB  1 
ATOM   6440 C  CG  . ARG   C  1  157 ? -19.935 33.276  17.690 1.00 96.41  ? 170 ARG   C CG  1 
ATOM   6441 C  CD  . ARG   C  1  157 ? -18.897 33.685  18.730 1.00 93.69  ? 170 ARG   C CD  1 
ATOM   6442 N  NE  . ARG   C  1  157 ? -18.966 32.847  19.935 1.00 93.82  ? 170 ARG   C NE  1 
ATOM   6443 C  CZ  . ARG   C  1  157 ? -18.051 32.726  20.892 1.00 91.73  ? 170 ARG   C CZ  1 
ATOM   6444 N  NH1 . ARG   C  1  157 ? -16.945 33.453  20.879 1.00 93.09  ? 170 ARG   C NH1 1 
ATOM   6445 N  NH2 . ARG   C  1  157 ? -18.265 31.865  21.872 1.00 85.64  ? 170 ARG   C NH2 1 
ATOM   6446 N  N   . TYR   C  1  158 ? -19.577 30.538  14.459 1.00 71.79  ? 171 TYR   C N   1 
ATOM   6447 C  CA  . TYR   C  1  158 ? -18.657 30.675  13.335 1.00 64.96  ? 171 TYR   C CA  1 
ATOM   6448 C  C   . TYR   C  1  158 ? -18.994 29.765  12.154 1.00 62.39  ? 171 TYR   C C   1 
ATOM   6449 O  O   . TYR   C  1  158 ? -18.412 29.938  11.087 1.00 67.46  ? 171 TYR   C O   1 
ATOM   6450 C  CB  . TYR   C  1  158 ? -17.226 30.386  13.780 1.00 71.10  ? 171 TYR   C CB  1 
ATOM   6451 C  CG  . TYR   C  1  158 ? -16.745 31.313  14.882 1.00 75.63  ? 171 TYR   C CG  1 
ATOM   6452 C  CD1 . TYR   C  1  158 ? -16.426 32.638  14.612 1.00 78.44  ? 171 TYR   C CD1 1 
ATOM   6453 C  CD2 . TYR   C  1  158 ? -16.600 30.858  16.185 1.00 74.11  ? 171 TYR   C CD2 1 
ATOM   6454 C  CE1 . TYR   C  1  158 ? -15.971 33.490  15.609 1.00 77.79  ? 171 TYR   C CE1 1 
ATOM   6455 C  CE2 . TYR   C  1  158 ? -16.162 31.700  17.195 1.00 79.12  ? 171 TYR   C CE2 1 
ATOM   6456 C  CZ  . TYR   C  1  158 ? -15.846 33.018  16.905 1.00 77.73  ? 171 TYR   C CZ  1 
ATOM   6457 O  OH  . TYR   C  1  158 ? -15.405 33.822  17.911 1.00 73.08  ? 171 TYR   C OH  1 
ATOM   6458 N  N   . GLY   C  1  159 ? -19.924 28.814  12.318 1.00 63.37  ? 172 GLY   C N   1 
ATOM   6459 C  CA  . GLY   C  1  159 ? -20.172 27.847  11.263 1.00 58.49  ? 172 GLY   C CA  1 
ATOM   6460 C  C   . GLY   C  1  159 ? -21.642 27.684  10.884 1.00 56.19  ? 172 GLY   C C   1 
ATOM   6461 O  O   . GLY   C  1  159 ? -21.994 26.674  10.281 1.00 52.07  ? 172 GLY   C O   1 
ATOM   6462 N  N   . GLY   C  1  160 ? -22.498 28.666  11.206 1.00 61.09  ? 173 GLY   C N   1 
ATOM   6463 C  CA  . GLY   C  1  160 ? -23.915 28.601  10.867 1.00 52.37  ? 173 GLY   C CA  1 
ATOM   6464 C  C   . GLY   C  1  160 ? -24.635 27.436  11.550 1.00 57.49  ? 173 GLY   C C   1 
ATOM   6465 O  O   . GLY   C  1  160 ? -25.655 26.961  11.048 1.00 61.34  ? 173 GLY   C O   1 
ATOM   6466 N  N   . GLY   C  1  161 ? -24.094 26.967  12.687 1.00 58.80  ? 174 GLY   C N   1 
ATOM   6467 C  CA  . GLY   C  1  161 ? -24.670 25.845  13.423 1.00 57.14  ? 174 GLY   C CA  1 
ATOM   6468 C  C   . GLY   C  1  161 ? -24.053 24.492  13.059 1.00 54.76  ? 174 GLY   C C   1 
ATOM   6469 O  O   . GLY   C  1  161 ? -24.524 23.445  13.519 1.00 50.70  ? 174 GLY   C O   1 
ATOM   6470 N  N   . PHE   C  1  162 ? -23.005 24.540  12.225 1.00 56.51  ? 175 PHE   C N   1 
ATOM   6471 C  CA  . PHE   C  1  162 ? -22.267 23.367  11.792 1.00 60.55  ? 175 PHE   C CA  1 
ATOM   6472 C  C   . PHE   C  1  162 ? -20.797 23.543  12.157 1.00 58.93  ? 175 PHE   C C   1 
ATOM   6473 O  O   . PHE   C  1  162 ? -20.305 24.667  12.261 1.00 58.99  ? 175 PHE   C O   1 
ATOM   6474 C  CB  . PHE   C  1  162 ? -22.392 23.188  10.279 1.00 63.11  ? 175 PHE   C CB  1 
ATOM   6475 C  CG  . PHE   C  1  162 ? -23.815 22.952  9.811  1.00 68.26  ? 175 PHE   C CG  1 
ATOM   6476 C  CD1 . PHE   C  1  162 ? -24.335 21.662  9.788  1.00 68.41  ? 175 PHE   C CD1 1 
ATOM   6477 C  CD2 . PHE   C  1  162 ? -24.628 24.007  9.400  1.00 70.01  ? 175 PHE   C CD2 1 
ATOM   6478 C  CE1 . PHE   C  1  162 ? -25.632 21.418  9.344  1.00 71.22  ? 175 PHE   C CE1 1 
ATOM   6479 C  CE2 . PHE   C  1  162 ? -25.931 23.768  8.971  1.00 71.18  ? 175 PHE   C CE2 1 
ATOM   6480 C  CZ  . PHE   C  1  162 ? -26.435 22.473  8.948  1.00 73.08  ? 175 PHE   C CZ  1 
ATOM   6481 N  N   . TYR   C  1  163 ? -20.096 22.416  12.329 1.00 55.55  ? 176 TYR   C N   1 
ATOM   6482 C  CA  . TYR   C  1  163 ? -18.662 22.444  12.560 1.00 54.24  ? 176 TYR   C CA  1 
ATOM   6483 C  C   . TYR   C  1  163 ? -17.961 22.392  11.208 1.00 52.03  ? 176 TYR   C C   1 
ATOM   6484 O  O   . TYR   C  1  163 ? -18.122 21.429  10.454 1.00 54.54  ? 176 TYR   C O   1 
ATOM   6485 C  CB  . TYR   C  1  163 ? -18.224 21.265  13.431 1.00 58.88  ? 176 TYR   C CB  1 
ATOM   6486 C  CG  . TYR   C  1  163 ? -16.750 21.270  13.823 1.00 55.45  ? 176 TYR   C CG  1 
ATOM   6487 C  CD1 . TYR   C  1  163 ? -16.304 22.030  14.897 1.00 51.36  ? 176 TYR   C CD1 1 
ATOM   6488 C  CD2 . TYR   C  1  163 ? -15.810 20.505  13.135 1.00 51.02  ? 176 TYR   C CD2 1 
ATOM   6489 C  CE1 . TYR   C  1  163 ? -14.972 22.027  15.276 1.00 54.81  ? 176 TYR   C CE1 1 
ATOM   6490 C  CE2 . TYR   C  1  163 ? -14.471 20.503  13.499 1.00 55.46  ? 176 TYR   C CE2 1 
ATOM   6491 C  CZ  . TYR   C  1  163 ? -14.052 21.258  14.581 1.00 52.80  ? 176 TYR   C CZ  1 
ATOM   6492 O  OH  . TYR   C  1  163 ? -12.746 21.270  14.957 1.00 51.30  ? 176 TYR   C OH  1 
ATOM   6493 N  N   . ASN   C  1  164 ? -17.193 23.439  10.912 1.00 49.51  ? 177 ASN   C N   1 
ATOM   6494 C  CA  . ASN   C  1  164 ? -16.416 23.490  9.691  1.00 50.74  ? 177 ASN   C CA  1 
ATOM   6495 C  C   . ASN   C  1  164 ? -15.030 24.031  10.023 1.00 48.93  ? 177 ASN   C C   1 
ATOM   6496 O  O   . ASN   C  1  164 ? -14.714 24.254  11.181 1.00 51.34  ? 177 ASN   C O   1 
ATOM   6497 C  CB  . ASN   C  1  164 ? -17.182 24.235  8.604  1.00 58.33  ? 177 ASN   C CB  1 
ATOM   6498 C  CG  . ASN   C  1  164 ? -17.174 25.740  8.737  1.00 61.26  ? 177 ASN   C CG  1 
ATOM   6499 O  OD1 . ASN   C  1  164 ? -16.494 26.321  9.604  1.00 53.77  ? 177 ASN   C OD1 1 
ATOM   6500 N  ND2 . ASN   C  1  164 ? -17.893 26.369  7.813  1.00 69.30  ? 177 ASN   C ND2 1 
ATOM   6501 N  N   . LEU   C  1  165 ? -14.204 24.248  9.002  1.00 49.22  ? 178 LEU   C N   1 
ATOM   6502 C  CA  . LEU   C  1  165 ? -12.803 24.536  9.236  1.00 54.96  ? 178 LEU   C CA  1 
ATOM   6503 C  C   . LEU   C  1  165 ? -12.624 25.865  9.976  1.00 56.63  ? 178 LEU   C C   1 
ATOM   6504 O  O   . LEU   C  1  165 ? -11.693 26.000  10.770 1.00 61.52  ? 178 LEU   C O   1 
ATOM   6505 C  CB  . LEU   C  1  165 ? -12.072 24.500  7.896  1.00 58.58  ? 178 LEU   C CB  1 
ATOM   6506 C  CG  . LEU   C  1  165 ? -10.546 24.378  7.972  1.00 66.60  ? 178 LEU   C CG  1 
ATOM   6507 C  CD1 . LEU   C  1  165 ? -10.123 23.015  8.531  1.00 65.12  ? 178 LEU   C CD1 1 
ATOM   6508 C  CD2 . LEU   C  1  165 ? -9.913  24.648  6.614  1.00 70.12  ? 178 LEU   C CD2 1 
ATOM   6509 N  N   . THR   C  1  166 ? -13.510 26.848  9.744  1.00 58.18  ? 179 THR   C N   1 
ATOM   6510 C  CA  . THR   C  1  166 ? -13.427 28.126  10.451 1.00 60.44  ? 179 THR   C CA  1 
ATOM   6511 C  C   . THR   C  1  166 ? -13.679 27.909  11.945 1.00 50.55  ? 179 THR   C C   1 
ATOM   6512 O  O   . THR   C  1  166 ? -12.980 28.442  12.796 1.00 48.87  ? 179 THR   C O   1 
ATOM   6513 C  CB  . THR   C  1  166 ? -14.419 29.133  9.866  1.00 67.35  ? 179 THR   C CB  1 
ATOM   6514 O  OG1 . THR   C  1  166 ? -14.217 29.160  8.452  1.00 63.00  ? 179 THR   C OG1 1 
ATOM   6515 C  CG2 . THR   C  1  166 ? -14.195 30.531  10.420 1.00 65.25  ? 179 THR   C CG2 1 
ATOM   6516 N  N   . VAL   C  1  167 ? -14.671 27.085  12.264 1.00 48.09  ? 180 VAL   C N   1 
ATOM   6517 C  CA  . VAL   C  1  167 ? -14.974 26.773  13.652 1.00 53.98  ? 180 VAL   C CA  1 
ATOM   6518 C  C   . VAL   C  1  167 ? -13.770 26.088  14.296 1.00 59.98  ? 180 VAL   C C   1 
ATOM   6519 O  O   . VAL   C  1  167 ? -13.453 26.388  15.447 1.00 53.97  ? 180 VAL   C O   1 
ATOM   6520 C  CB  . VAL   C  1  167 ? -16.223 25.889  13.818 1.00 54.07  ? 180 VAL   C CB  1 
ATOM   6521 C  CG1 . VAL   C  1  167 ? -16.553 25.657  15.291 1.00 56.06  ? 180 VAL   C CG1 1 
ATOM   6522 C  CG2 . VAL   C  1  167 ? -17.442 26.444  13.072 1.00 55.36  ? 180 VAL   C CG2 1 
ATOM   6523 N  N   . ALA   C  1  168 ? -13.150 25.138  13.573 1.00 60.04  ? 181 ALA   C N   1 
ATOM   6524 C  CA  . ALA   C  1  168 ? -12.014 24.373  14.078 1.00 58.04  ? 181 ALA   C CA  1 
ATOM   6525 C  C   . ALA   C  1  168 ? -10.900 25.308  14.530 1.00 52.70  ? 181 ALA   C C   1 
ATOM   6526 O  O   . ALA   C  1  168 ? -10.358 25.149  15.622 1.00 53.90  ? 181 ALA   C O   1 
ATOM   6527 C  CB  . ALA   C  1  168 ? -11.508 23.394  13.035 1.00 59.06  ? 181 ALA   C CB  1 
ATOM   6528 N  N   . GLY   C  1  169 ? -10.580 26.301  13.700 1.00 54.19  ? 182 GLY   C N   1 
ATOM   6529 C  CA  . GLY   C  1  169 ? -9.541  27.263  14.038 1.00 59.29  ? 182 GLY   C CA  1 
ATOM   6530 C  C   . GLY   C  1  169 ? -9.858  28.008  15.339 1.00 63.11  ? 182 GLY   C C   1 
ATOM   6531 O  O   . GLY   C  1  169 ? -8.990  28.174  16.189 1.00 65.36  ? 182 GLY   C O   1 
ATOM   6532 N  N   . GLU   C  1  170 ? -11.109 28.454  15.490 1.00 61.99  ? 183 GLU   C N   1 
ATOM   6533 C  CA  . GLU   C  1  170 ? -11.498 29.249  16.642 1.00 59.62  ? 183 GLU   C CA  1 
ATOM   6534 C  C   . GLU   C  1  170 ? -11.542 28.363  17.879 1.00 52.61  ? 183 GLU   C C   1 
ATOM   6535 O  O   . GLU   C  1  170 ? -11.041 28.742  18.922 1.00 53.73  ? 183 GLU   C O   1 
ATOM   6536 C  CB  . GLU   C  1  170 ? -12.853 29.931  16.418 1.00 63.60  ? 183 GLU   C CB  1 
ATOM   6537 C  CG  . GLU   C  1  170 ? -12.856 30.962  15.293 1.00 64.63  ? 183 GLU   C CG  1 
ATOM   6538 C  CD  . GLU   C  1  170 ? -11.885 32.119  15.493 1.00 67.61  ? 183 GLU   C CD  1 
ATOM   6539 O  OE1 . GLU   C  1  170 ? -11.421 32.337  16.627 1.00 73.99  ? 183 GLU   C OE1 1 
ATOM   6540 O  OE2 . GLU   C  1  170 ? -11.569 32.786  14.494 1.00 82.61  ? 183 GLU   C OE2 1 
ATOM   6541 N  N   . LEU   C  1  171 ? -12.136 27.178  17.761 1.00 52.66  ? 184 LEU   C N   1 
ATOM   6542 C  CA  . LEU   C  1  171 ? -12.314 26.317  18.921 1.00 52.76  ? 184 LEU   C CA  1 
ATOM   6543 C  C   . LEU   C  1  171 ? -10.953 25.850  19.447 1.00 57.37  ? 184 LEU   C C   1 
ATOM   6544 O  O   . LEU   C  1  171 ? -10.735 25.838  20.650 1.00 50.76  ? 184 LEU   C O   1 
ATOM   6545 C  CB  . LEU   C  1  171 ? -13.214 25.140  18.560 1.00 55.46  ? 184 LEU   C CB  1 
ATOM   6546 C  CG  . LEU   C  1  171 ? -13.498 24.145  19.687 1.00 60.57  ? 184 LEU   C CG  1 
ATOM   6547 C  CD1 . LEU   C  1  171 ? -14.229 24.807  20.849 1.00 65.16  ? 184 LEU   C CD1 1 
ATOM   6548 C  CD2 . LEU   C  1  171 ? -14.279 22.952  19.167 1.00 61.36  ? 184 LEU   C CD2 1 
ATOM   6549 N  N   . ARG   C  1  172 ? -10.027 25.492  18.550 1.00 55.28  ? 185 ARG   C N   1 
ATOM   6550 C  CA  . ARG   C  1  172 ? -8.728  24.967  18.956 1.00 55.91  ? 185 ARG   C CA  1 
ATOM   6551 C  C   . ARG   C  1  172 ? -7.999  26.001  19.813 1.00 57.87  ? 185 ARG   C C   1 
ATOM   6552 O  O   . ARG   C  1  172 ? -7.468  25.671  20.878 1.00 51.87  ? 185 ARG   C O   1 
ATOM   6553 C  CB  . ARG   C  1  172 ? -7.933  24.556  17.708 1.00 51.56  ? 185 ARG   C CB  1 
ATOM   6554 C  CG  . ARG   C  1  172 ? -6.417  24.460  17.807 1.00 48.88  ? 185 ARG   C CG  1 
ATOM   6555 C  CD  . ARG   C  1  172 ? -5.904  23.579  18.917 1.00 47.81  ? 185 ARG   C CD  1 
ATOM   6556 N  NE  . ARG   C  1  172 ? -6.513  22.252  18.976 1.00 44.78  ? 185 ARG   C NE  1 
ATOM   6557 C  CZ  . ARG   C  1  172 ? -6.980  21.676  20.070 1.00 51.68  ? 185 ARG   C CZ  1 
ATOM   6558 N  NH1 . ARG   C  1  172 ? -7.065  22.366  21.194 1.00 52.39  ? 185 ARG   C NH1 1 
ATOM   6559 N  NH2 . ARG   C  1  172 ? -7.381  20.407  20.031 1.00 51.26  ? 185 ARG   C NH2 1 
ATOM   6560 N  N   . TYR   C  1  173 ? -7.956  27.248  19.331 1.00 57.51  ? 186 TYR   C N   1 
ATOM   6561 C  CA  . TYR   C  1  173 ? -7.260  28.308  20.044 1.00 61.22  ? 186 TYR   C CA  1 
ATOM   6562 C  C   . TYR   C  1  173 ? -7.927  28.548  21.401 1.00 60.98  ? 186 TYR   C C   1 
ATOM   6563 O  O   . TYR   C  1  173 ? -7.255  28.680  22.422 1.00 60.01  ? 186 TYR   C O   1 
ATOM   6564 C  CB  . TYR   C  1  173 ? -7.245  29.567  19.179 1.00 64.91  ? 186 TYR   C CB  1 
ATOM   6565 C  CG  . TYR   C  1  173 ? -6.575  30.759  19.841 1.00 71.28  ? 186 TYR   C CG  1 
ATOM   6566 C  CD1 . TYR   C  1  173 ? -5.206  30.759  20.083 1.00 70.23  ? 186 TYR   C CD1 1 
ATOM   6567 C  CD2 . TYR   C  1  173 ? -7.304  31.887  20.204 1.00 80.08  ? 186 TYR   C CD2 1 
ATOM   6568 C  CE1 . TYR   C  1  173 ? -4.576  31.839  20.678 1.00 78.19  ? 186 TYR   C CE1 1 
ATOM   6569 C  CE2 . TYR   C  1  173 ? -6.685  32.978  20.797 1.00 83.68  ? 186 TYR   C CE2 1 
ATOM   6570 C  CZ  . TYR   C  1  173 ? -5.321  32.950  21.033 1.00 82.22  ? 186 TYR   C CZ  1 
ATOM   6571 O  OH  . TYR   C  1  173 ? -4.704  34.014  21.615 1.00 83.38  ? 186 TYR   C OH  1 
ATOM   6572 N  N   . SER   C  1  174 ? -9.259  28.579  21.407 1.00 57.48  ? 187 SER   C N   1 
ATOM   6573 C  CA  . SER   C  1  174 ? -10.004 28.882  22.614 1.00 63.30  ? 187 SER   C CA  1 
ATOM   6574 C  C   . SER   C  1  174 ? -9.788  27.792  23.661 1.00 61.71  ? 187 SER   C C   1 
ATOM   6575 O  O   . SER   C  1  174 ? -9.701  28.094  24.847 1.00 55.05  ? 187 SER   C O   1 
ATOM   6576 C  CB  . SER   C  1  174 ? -11.466 29.075  22.321 1.00 63.59  ? 187 SER   C CB  1 
ATOM   6577 O  OG  . SER   C  1  174 ? -12.178 29.286  23.530 1.00 61.80  ? 187 SER   C OG  1 
ATOM   6578 N  N   . ARG   C  1  175 ? -9.690  26.531  23.222 1.00 57.47  ? 188 ARG   C N   1 
ATOM   6579 C  CA  . ARG   C  1  175 ? -9.470  25.425  24.143 1.00 54.17  ? 188 ARG   C CA  1 
ATOM   6580 C  C   . ARG   C  1  175 ? -8.066  25.502  24.742 1.00 54.67  ? 188 ARG   C C   1 
ATOM   6581 O  O   . ARG   C  1  175 ? -7.882  25.177  25.912 1.00 52.38  ? 188 ARG   C O   1 
ATOM   6582 C  CB  . ARG   C  1  175 ? -9.756  24.071  23.486 1.00 57.16  ? 188 ARG   C CB  1 
ATOM   6583 C  CG  . ARG   C  1  175 ? -11.246 23.846  23.229 1.00 57.58  ? 188 ARG   C CG  1 
ATOM   6584 C  CD  . ARG   C  1  175 ? -12.048 23.662  24.490 1.00 52.84  ? 188 ARG   C CD  1 
ATOM   6585 N  NE  . ARG   C  1  175 ? -11.587 22.445  25.156 1.00 58.31  ? 188 ARG   C NE  1 
ATOM   6586 C  CZ  . ARG   C  1  175 ? -11.040 22.343  26.360 1.00 62.21  ? 188 ARG   C CZ  1 
ATOM   6587 N  NH1 . ARG   C  1  175 ? -11.010 23.382  27.170 1.00 62.51  ? 188 ARG   C NH1 1 
ATOM   6588 N  NH2 . ARG   C  1  175 ? -10.554 21.175  26.764 1.00 64.15  ? 188 ARG   C NH2 1 
ATOM   6589 N  N   . ILE   C  1  176 ? -7.086  25.964  23.960 1.00 53.43  ? 189 ILE   C N   1 
ATOM   6590 C  CA  . ILE   C  1  176 ? -5.754  26.215  24.492 1.00 56.52  ? 189 ILE   C CA  1 
ATOM   6591 C  C   . ILE   C  1  176 ? -5.822  27.264  25.606 1.00 58.75  ? 189 ILE   C C   1 
ATOM   6592 O  O   . ILE   C  1  176 ? -5.286  27.054  26.689 1.00 53.33  ? 189 ILE   C O   1 
ATOM   6593 C  CB  . ILE   C  1  176 ? -4.796  26.630  23.360 1.00 51.68  ? 189 ILE   C CB  1 
ATOM   6594 C  CG1 . ILE   C  1  176 ? -4.520  25.445  22.431 1.00 53.69  ? 189 ILE   C CG1 1 
ATOM   6595 C  CG2 . ILE   C  1  176 ? -3.504  27.239  23.901 1.00 50.16  ? 189 ILE   C CG2 1 
ATOM   6596 C  CD1 . ILE   C  1  176 ? -3.874  25.818  21.108 1.00 53.77  ? 189 ILE   C CD1 1 
ATOM   6597 N  N   . GLN   C  1  177 ? -6.494  28.390  25.345 1.00 66.27  ? 190 GLN   C N   1 
ATOM   6598 C  CA  . GLN   C  1  177 ? -6.659  29.441  26.344 1.00 67.31  ? 190 GLN   C CA  1 
ATOM   6599 C  C   . GLN   C  1  177 ? -7.352  28.910  27.602 1.00 57.02  ? 190 GLN   C C   1 
ATOM   6600 O  O   . GLN   C  1  177 ? -6.919  29.228  28.700 1.00 60.83  ? 190 GLN   C O   1 
ATOM   6601 C  CB  . GLN   C  1  177 ? -7.394  30.655  25.766 1.00 71.31  ? 190 GLN   C CB  1 
ATOM   6602 C  CG  . GLN   C  1  177 ? -6.653  31.330  24.613 1.00 71.18  ? 190 GLN   C CG  1 
ATOM   6603 C  CD  . GLN   C  1  177 ? -5.265  31.815  24.980 1.00 80.30  ? 190 GLN   C CD  1 
ATOM   6604 O  OE1 . GLN   C  1  177 ? -4.986  32.174  26.131 1.00 87.59  ? 190 GLN   C OE1 1 
ATOM   6605 N  NE2 . GLN   C  1  177 ? -4.376  31.856  23.997 1.00 83.73  ? 190 GLN   C NE2 1 
ATOM   6606 N  N   . ASP   C  1  178 ? -8.412  28.100  27.467 1.00 55.72  ? 191 ASP   C N   1 
ATOM   6607 C  CA  . ASP   C  1  178 ? -9.064  27.518  28.632 1.00 58.65  ? 191 ASP   C CA  1 
ATOM   6608 C  C   . ASP   C  1  178 ? -8.039  26.781  29.493 1.00 69.28  ? 191 ASP   C C   1 
ATOM   6609 O  O   . ASP   C  1  178 ? -8.028  26.942  30.717 1.00 68.43  ? 191 ASP   C O   1 
ATOM   6610 C  CB  . ASP   C  1  178 ? -10.155 26.514  28.296 1.00 62.98  ? 191 ASP   C CB  1 
ATOM   6611 C  CG  . ASP   C  1  178 ? -11.402 27.048  27.598 1.00 71.08  ? 191 ASP   C CG  1 
ATOM   6612 O  OD1 . ASP   C  1  178 ? -11.561 28.288  27.561 1.00 83.04  ? 191 ASP   C OD1 1 
ATOM   6613 O  OD2 . ASP   C  1  178 ? -12.216 26.216  27.089 1.00 60.69  ? 191 ASP   C OD2 1 
ATOM   6614 N  N   . SER   C  1  179 ? -7.206  25.951  28.850 1.00 61.39  ? 192 SER   C N   1 
ATOM   6615 C  CA  . SER   C  1  179 ? -6.256  25.119  29.572 1.00 62.35  ? 192 SER   C CA  1 
ATOM   6616 C  C   . SER   C  1  179 ? -5.155  25.970  30.213 1.00 55.88  ? 192 SER   C C   1 
ATOM   6617 O  O   . SER   C  1  179 ? -4.733  25.681  31.330 1.00 53.17  ? 192 SER   C O   1 
ATOM   6618 C  CB  . SER   C  1  179 ? -5.690  24.006  28.699 1.00 60.63  ? 192 SER   C CB  1 
ATOM   6619 O  OG  . SER   C  1  179 ? -6.588  22.903  28.642 1.00 55.06  ? 192 SER   C OG  1 
ATOM   6620 N  N   . ILE   C  1  180 ? -4.685  27.011  29.517 1.00 53.54  ? 193 ILE   C N   1 
ATOM   6621 C  CA  . ILE   C  1  180 ? -3.699  27.913  30.091 1.00 57.22  ? 193 ILE   C CA  1 
ATOM   6622 C  C   . ILE   C  1  180 ? -4.238  28.527  31.385 1.00 64.51  ? 193 ILE   C C   1 
ATOM   6623 O  O   . ILE   C  1  180 ? -3.535  28.566  32.389 1.00 61.93  ? 193 ILE   C O   1 
ATOM   6624 C  CB  . ILE   C  1  180 ? -3.302  29.010  29.095 1.00 61.45  ? 193 ILE   C CB  1 
ATOM   6625 C  CG1 . ILE   C  1  180 ? -2.432  28.448  27.969 1.00 62.17  ? 193 ILE   C CG1 1 
ATOM   6626 C  CG2 . ILE   C  1  180 ? -2.602  30.161  29.823 1.00 61.14  ? 193 ILE   C CG2 1 
ATOM   6627 C  CD1 . ILE   C  1  180 ? -2.189  29.426  26.834 1.00 62.11  ? 193 ILE   C CD1 1 
ATOM   6628 N  N   . ALA   C  1  181 ? -5.496  28.985  31.343 1.00 69.22  ? 194 ALA   C N   1 
ATOM   6629 C  CA  . ALA   C  1  181 ? -6.099  29.740  32.431 1.00 69.50  ? 194 ALA   C CA  1 
ATOM   6630 C  C   . ALA   C  1  181 ? -6.443  28.854  33.623 1.00 68.93  ? 194 ALA   C C   1 
ATOM   6631 O  O   . ALA   C  1  181 ? -6.528  29.358  34.738 1.00 74.01  ? 194 ALA   C O   1 
ATOM   6632 C  CB  . ALA   C  1  181 ? -7.337  30.480  31.943 1.00 70.49  ? 194 ALA   C CB  1 
ATOM   6633 N  N   . THR   C  1  182 ? -6.666  27.551  33.413 1.00 64.96  ? 195 THR   C N   1 
ATOM   6634 C  CA  . THR   C  1  182 ? -7.279  26.756  34.468 1.00 64.09  ? 195 THR   C CA  1 
ATOM   6635 C  C   . THR   C  1  182 ? -6.451  25.530  34.838 1.00 63.66  ? 195 THR   C C   1 
ATOM   6636 O  O   . THR   C  1  182 ? -6.780  24.868  35.817 1.00 63.00  ? 195 THR   C O   1 
ATOM   6637 C  CB  . THR   C  1  182 ? -8.691  26.322  34.073 1.00 72.99  ? 195 THR   C CB  1 
ATOM   6638 O  OG1 . THR   C  1  182 ? -8.590  25.462  32.938 1.00 72.25  ? 195 THR   C OG1 1 
ATOM   6639 C  CG2 . THR   C  1  182 ? -9.610  27.495  33.772 1.00 77.29  ? 195 THR   C CG2 1 
ATOM   6640 N  N   . ASN   C  1  183 ? -5.431  25.189  34.046 1.00 61.69  ? 196 ASN   C N   1 
ATOM   6641 C  CA  . ASN   C  1  183 ? -4.720  23.935  34.236 1.00 63.99  ? 196 ASN   C CA  1 
ATOM   6642 C  C   . ASN   C  1  183 ? -3.249  24.240  34.474 1.00 59.34  ? 196 ASN   C C   1 
ATOM   6643 O  O   . ASN   C  1  183 ? -2.521  24.561  33.545 1.00 59.11  ? 196 ASN   C O   1 
ATOM   6644 C  CB  . ASN   C  1  183 ? -4.879  22.985  33.051 1.00 66.67  ? 196 ASN   C CB  1 
ATOM   6645 C  CG  . ASN   C  1  183 ? -4.190  21.662  33.285 1.00 62.62  ? 196 ASN   C CG  1 
ATOM   6646 O  OD1 . ASN   C  1  183 ? -3.537  21.466  34.317 1.00 65.66  ? 196 ASN   C OD1 1 
ATOM   6647 N  ND2 . ASN   C  1  183 ? -4.312  20.750  32.334 1.00 61.80  ? 196 ASN   C ND2 1 
ATOM   6648 N  N   . PRO   C  1  184 ? -2.770  24.170  35.729 1.00 58.86  ? 197 PRO   C N   1 
ATOM   6649 C  CA  . PRO   C  1  184 ? -1.376  24.506  36.013 1.00 60.97  ? 197 PRO   C CA  1 
ATOM   6650 C  C   . PRO   C  1  184 ? -0.354  23.469  35.548 1.00 59.11  ? 197 PRO   C C   1 
ATOM   6651 O  O   . PRO   C  1  184 ? 0.825   23.782  35.490 1.00 61.87  ? 197 PRO   C O   1 
ATOM   6652 C  CB  . PRO   C  1  184 ? -1.420  24.658  37.539 1.00 63.24  ? 197 PRO   C CB  1 
ATOM   6653 C  CG  . PRO   C  1  184 ? -2.455  23.644  37.977 1.00 65.06  ? 197 PRO   C CG  1 
ATOM   6654 C  CD  . PRO   C  1  184 ? -3.534  23.746  36.914 1.00 62.12  ? 197 PRO   C CD  1 
ATOM   6655 N  N   . GLU   C  1  185 ? -0.808  22.250  35.207 1.00 65.50  ? 198 GLU   C N   1 
ATOM   6656 C  CA  . GLU   C  1  185 ? 0.053   21.213  34.641 1.00 61.65  ? 198 GLU   C CA  1 
ATOM   6657 C  C   . GLU   C  1  185 ? -0.068  21.167  33.110 1.00 59.54  ? 198 GLU   C C   1 
ATOM   6658 O  O   . GLU   C  1  185 ? 0.436   20.246  32.472 1.00 60.38  ? 198 GLU   C O   1 
ATOM   6659 C  CB  . GLU   C  1  185 ? -0.300  19.844  35.229 1.00 65.99  ? 198 GLU   C CB  1 
ATOM   6660 C  CG  . GLU   C  1  185 ? -0.125  19.747  36.744 1.00 70.03  ? 198 GLU   C CG  1 
ATOM   6661 C  CD  . GLU   C  1  185 ? -0.513  18.408  37.364 1.00 79.20  ? 198 GLU   C CD  1 
ATOM   6662 O  OE1 . GLU   C  1  185 ? -0.899  17.466  36.639 1.00 76.25  ? 198 GLU   C OE1 1 
ATOM   6663 O  OE2 . GLU   C  1  185 ? -0.447  18.305  38.608 1.00 87.88  ? 198 GLU   C OE2 1 
ATOM   6664 N  N   . PHE   C  1  186 ? -0.700  22.184  32.511 1.00 55.44  ? 199 PHE   C N   1 
ATOM   6665 C  CA  . PHE   C  1  186 ? -0.930  22.232  31.079 1.00 55.16  ? 199 PHE   C CA  1 
ATOM   6666 C  C   . PHE   C  1  186 ? 0.375   22.100  30.302 1.00 56.31  ? 199 PHE   C C   1 
ATOM   6667 O  O   . PHE   C  1  186 ? 1.301   22.881  30.493 1.00 56.45  ? 199 PHE   C O   1 
ATOM   6668 C  CB  . PHE   C  1  186 ? -1.579  23.545  30.644 1.00 49.44  ? 199 PHE   C CB  1 
ATOM   6669 C  CG  . PHE   C  1  186 ? -1.892  23.665  29.158 1.00 49.20  ? 199 PHE   C CG  1 
ATOM   6670 C  CD1 . PHE   C  1  186 ? -2.491  22.624  28.456 1.00 48.92  ? 199 PHE   C CD1 1 
ATOM   6671 C  CD2 . PHE   C  1  186 ? -1.575  24.825  28.465 1.00 48.20  ? 199 PHE   C CD2 1 
ATOM   6672 C  CE1 . PHE   C  1  186 ? -2.778  22.756  27.103 1.00 48.00  ? 199 PHE   C CE1 1 
ATOM   6673 C  CE2 . PHE   C  1  186 ? -1.857  24.949  27.117 1.00 50.61  ? 199 PHE   C CE2 1 
ATOM   6674 C  CZ  . PHE   C  1  186 ? -2.463  23.916  26.439 1.00 50.74  ? 199 PHE   C CZ  1 
ATOM   6675 N  N   . GLN   C  1  187 ? 0.397   21.115  29.393 1.00 60.98  ? 200 GLN   C N   1 
ATOM   6676 C  CA  . GLN   C  1  187 ? 1.497   20.877  28.469 1.00 57.25  ? 200 GLN   C CA  1 
ATOM   6677 C  C   . GLN   C  1  187 ? 0.927   20.845  27.053 1.00 48.89  ? 200 GLN   C C   1 
ATOM   6678 O  O   . GLN   C  1  187 ? -0.130  20.250  26.824 1.00 50.79  ? 200 GLN   C O   1 
ATOM   6679 C  CB  . GLN   C  1  187 ? 2.158   19.536  28.802 1.00 61.34  ? 200 GLN   C CB  1 
ATOM   6680 C  CG  . GLN   C  1  187 ? 2.973   19.540  30.094 1.00 67.91  ? 200 GLN   C CG  1 
ATOM   6681 C  CD  . GLN   C  1  187 ? 4.243   20.360  29.977 1.00 67.80  ? 200 GLN   C CD  1 
ATOM   6682 O  OE1 . GLN   C  1  187 ? 5.206   19.969  29.309 1.00 74.47  ? 200 GLN   C OE1 1 
ATOM   6683 N  NE2 . GLN   C  1  187 ? 4.249   21.523  30.607 1.00 63.52  ? 200 GLN   C NE2 1 
ATOM   6684 N  N   . PHE   C  1  188 ? 1.639   21.462  26.110 1.00 43.90  ? 201 PHE   C N   1 
ATOM   6685 C  CA  . PHE   C  1  188 ? 1.197   21.476  24.725 1.00 44.66  ? 201 PHE   C CA  1 
ATOM   6686 C  C   . PHE   C  1  188 ? 2.406   21.422  23.803 1.00 43.30  ? 201 PHE   C C   1 
ATOM   6687 O  O   . PHE   C  1  188 ? 2.673   22.351  23.062 1.00 47.98  ? 201 PHE   C O   1 
ATOM   6688 C  CB  . PHE   C  1  188 ? 0.335   22.718  24.507 1.00 45.67  ? 201 PHE   C CB  1 
ATOM   6689 C  CG  . PHE   C  1  188 ? -0.614  22.626  23.328 1.00 45.79  ? 201 PHE   C CG  1 
ATOM   6690 C  CD1 . PHE   C  1  188 ? -1.692  21.757  23.373 1.00 45.61  ? 201 PHE   C CD1 1 
ATOM   6691 C  CD2 . PHE   C  1  188 ? -0.459  23.439  22.209 1.00 48.41  ? 201 PHE   C CD2 1 
ATOM   6692 C  CE1 . PHE   C  1  188 ? -2.581  21.681  22.312 1.00 46.70  ? 201 PHE   C CE1 1 
ATOM   6693 C  CE2 . PHE   C  1  188 ? -1.363  23.368  21.160 1.00 48.41  ? 201 PHE   C CE2 1 
ATOM   6694 C  CZ  . PHE   C  1  188 ? -2.417  22.489  21.214 1.00 47.03  ? 201 PHE   C CZ  1 
ATOM   6695 N  N   . LYS   C  1  189 ? 3.135   20.313  23.859 1.00 44.89  ? 202 LYS   C N   1 
ATOM   6696 C  CA  . LYS   C  1  189 ? 4.375   20.179  23.122 1.00 46.37  ? 202 LYS   C CA  1 
ATOM   6697 C  C   . LYS   C  1  189 ? 4.527   18.734  22.632 1.00 44.30  ? 202 LYS   C C   1 
ATOM   6698 O  O   . LYS   C  1  189 ? 3.729   17.861  22.947 1.00 44.53  ? 202 LYS   C O   1 
ATOM   6699 C  CB  . LYS   C  1  189 ? 5.510   20.608  24.055 1.00 48.27  ? 202 LYS   C CB  1 
ATOM   6700 C  CG  . LYS   C  1  189 ? 5.592   19.782  25.328 1.00 60.28  ? 202 LYS   C CG  1 
ATOM   6701 C  CD  . LYS   C  1  189 ? 6.871   19.945  26.147 1.00 60.90  ? 202 LYS   C CD  1 
ATOM   6702 C  CE  . LYS   C  1  189 ? 6.970   21.284  26.798 1.00 67.95  ? 202 LYS   C CE  1 
ATOM   6703 N  NZ  . LYS   C  1  189 ? 7.713   21.216  28.061 1.00 72.81  ? 202 LYS   C NZ  1 
ATOM   6704 N  N   . ASN   C  1  190 ? 5.571   18.500  21.843 1.00 46.70  ? 203 ASN   C N   1 
ATOM   6705 C  CA  . ASN   C  1  190 ? 5.907   17.174  21.355 1.00 47.83  ? 203 ASN   C CA  1 
ATOM   6706 C  C   . ASN   C  1  190 ? 4.684   16.537  20.685 1.00 44.55  ? 203 ASN   C C   1 
ATOM   6707 O  O   . ASN   C  1  190 ? 4.096   17.138  19.786 1.00 43.99  ? 203 ASN   C O   1 
ATOM   6708 C  CB  . ASN   C  1  190 ? 6.601   16.386  22.457 1.00 53.66  ? 203 ASN   C CB  1 
ATOM   6709 C  CG  . ASN   C  1  190 ? 7.935   17.012  22.809 1.00 53.31  ? 203 ASN   C CG  1 
ATOM   6710 O  OD1 . ASN   C  1  190 ? 8.706   17.391  21.916 1.00 56.18  ? 203 ASN   C OD1 1 
ATOM   6711 N  ND2 . ASN   C  1  190 ? 8.210   17.141  24.095 1.00 50.79  ? 203 ASN   C ND2 1 
ATOM   6712 N  N   . VAL   C  1  191 ? 4.304   15.321  21.091 1.00 37.00  ? 204 VAL   C N   1 
ATOM   6713 C  CA  . VAL   C  1  191 ? 3.287   14.598  20.348 1.00 40.11  ? 204 VAL   C CA  1 
ATOM   6714 C  C   . VAL   C  1  191 ? 1.985   15.403  20.380 1.00 40.26  ? 204 VAL   C C   1 
ATOM   6715 O  O   . VAL   C  1  191 ? 1.332   15.582  19.362 1.00 38.43  ? 204 VAL   C O   1 
ATOM   6716 C  CB  . VAL   C  1  191 ? 3.074   13.182  20.903 1.00 41.43  ? 204 VAL   C CB  1 
ATOM   6717 C  CG1 . VAL   C  1  191 ? 1.898   12.486  20.228 1.00 42.83  ? 204 VAL   C CG1 1 
ATOM   6718 C  CG2 . VAL   C  1  191 ? 4.336   12.344  20.788 1.00 39.66  ? 204 VAL   C CG2 1 
ATOM   6719 N  N   . ARG   C  1  192 ? 1.626   15.908  21.556 1.00 37.57  ? 205 ARG   C N   1 
ATOM   6720 C  CA  . ARG   C  1  192 ? 0.361   16.579  21.735 1.00 39.89  ? 205 ARG   C CA  1 
ATOM   6721 C  C   . ARG   C  1  192 ? 0.236   17.800  20.824 1.00 39.88  ? 205 ARG   C C   1 
ATOM   6722 O  O   . ARG   C  1  192 ? -0.840  18.075  20.312 1.00 40.29  ? 205 ARG   C O   1 
ATOM   6723 C  CB  . ARG   C  1  192 ? 0.155   17.038  23.186 1.00 45.18  ? 205 ARG   C CB  1 
ATOM   6724 C  CG  . ARG   C  1  192 ? -1.217  17.668  23.385 1.00 45.45  ? 205 ARG   C CG  1 
ATOM   6725 C  CD  . ARG   C  1  192 ? -2.330  16.765  22.848 1.00 47.39  ? 205 ARG   C CD  1 
ATOM   6726 N  NE  . ARG   C  1  192 ? -3.678  17.305  23.012 1.00 48.77  ? 205 ARG   C NE  1 
ATOM   6727 C  CZ  . ARG   C  1  192 ? -4.731  16.999  22.264 1.00 48.13  ? 205 ARG   C CZ  1 
ATOM   6728 N  NH1 . ARG   C  1  192 ? -4.641  16.096  21.310 1.00 50.10  ? 205 ARG   C NH1 1 
ATOM   6729 N  NH2 . ARG   C  1  192 ? -5.888  17.600  22.476 1.00 49.34  ? 205 ARG   C NH2 1 
ATOM   6730 N  N   . PHE   C  1  193 ? 1.321   18.547  20.627 1.00 40.19  ? 206 PHE   C N   1 
ATOM   6731 C  CA  . PHE   C  1  193 ? 1.240   19.742  19.811 1.00 40.34  ? 206 PHE   C CA  1 
ATOM   6732 C  C   . PHE   C  1  193 ? 0.843   19.342  18.395 1.00 44.35  ? 206 PHE   C C   1 
ATOM   6733 O  O   . PHE   C  1  193 ? 0.066   20.039  17.765 1.00 43.59  ? 206 PHE   C O   1 
ATOM   6734 C  CB  . PHE   C  1  193 ? 2.545   20.538  19.815 1.00 41.05  ? 206 PHE   C CB  1 
ATOM   6735 C  CG  . PHE   C  1  193 ? 2.479   21.766  18.927 1.00 45.87  ? 206 PHE   C CG  1 
ATOM   6736 C  CD1 . PHE   C  1  193 ? 1.898   22.945  19.374 1.00 51.07  ? 206 PHE   C CD1 1 
ATOM   6737 C  CD2 . PHE   C  1  193 ? 3.010   21.736  17.649 1.00 51.48  ? 206 PHE   C CD2 1 
ATOM   6738 C  CE1 . PHE   C  1  193 ? 1.828   24.061  18.552 1.00 52.87  ? 206 PHE   C CE1 1 
ATOM   6739 C  CE2 . PHE   C  1  193 ? 2.945   22.857  16.830 1.00 57.46  ? 206 PHE   C CE2 1 
ATOM   6740 C  CZ  . PHE   C  1  193 ? 2.352   24.016  17.285 1.00 52.68  ? 206 PHE   C CZ  1 
ATOM   6741 N  N   . ILE   C  1  194 ? 1.356   18.211  17.905 1.00 42.60  ? 207 ILE   C N   1 
ATOM   6742 C  CA  . ILE   C  1  194 ? 1.055   17.784  16.550 1.00 44.57  ? 207 ILE   C CA  1 
ATOM   6743 C  C   . ILE   C  1  194 ? -0.368  17.225  16.472 1.00 44.37  ? 207 ILE   C C   1 
ATOM   6744 O  O   . ILE   C  1  194 ? -1.144  17.611  15.591 1.00 43.33  ? 207 ILE   C O   1 
ATOM   6745 C  CB  . ILE   C  1  194 ? 2.124   16.790  16.063 1.00 47.98  ? 207 ILE   C CB  1 
ATOM   6746 C  CG1 . ILE   C  1  194 ? 3.529   17.406  16.118 1.00 51.58  ? 207 ILE   C CG1 1 
ATOM   6747 C  CG2 . ILE   C  1  194 ? 1.793   16.280  14.666 1.00 49.67  ? 207 ILE   C CG2 1 
ATOM   6748 C  CD1 . ILE   C  1  194 ? 3.677   18.677  15.307 1.00 53.42  ? 207 ILE   C CD1 1 
ATOM   6749 N  N   . THR   C  1  195 ? -0.723  16.330  17.403 1.00 40.15  ? 208 THR   C N   1 
ATOM   6750 C  CA  . THR   C  1  195 ? -1.992  15.625  17.336 1.00 41.49  ? 208 THR   C CA  1 
ATOM   6751 C  C   . THR   C  1  195 ? -3.156  16.583  17.591 1.00 43.43  ? 208 THR   C C   1 
ATOM   6752 O  O   . THR   C  1  195 ? -4.234  16.401  17.046 1.00 40.63  ? 208 THR   C O   1 
ATOM   6753 C  CB  . THR   C  1  195 ? -2.015  14.429  18.292 1.00 42.84  ? 208 THR   C CB  1 
ATOM   6754 O  OG1 . THR   C  1  195 ? -1.871  14.901  19.626 1.00 44.98  ? 208 THR   C OG1 1 
ATOM   6755 C  CG2 . THR   C  1  195 ? -0.957  13.399  17.951 1.00 43.59  ? 208 THR   C CG2 1 
ATOM   6756 N  N   . ALA   C  1  196 ? -2.944  17.638  18.375 1.00 47.74  ? 209 ALA   C N   1 
ATOM   6757 C  CA  . ALA   C  1  196 ? -4.030  18.549  18.718 1.00 53.59  ? 209 ALA   C CA  1 
ATOM   6758 C  C   . ALA   C  1  196 ? -4.588  19.272  17.499 1.00 51.92  ? 209 ALA   C C   1 
ATOM   6759 O  O   . ALA   C  1  196 ? -5.748  19.659  17.533 1.00 59.33  ? 209 ALA   C O   1 
ATOM   6760 C  CB  . ALA   C  1  196 ? -3.590  19.557  19.752 1.00 56.14  ? 209 ALA   C CB  1 
ATOM   6761 N  N   . TYR   C  1  197 ? -3.784  19.487  16.455 1.00 43.38  ? 210 TYR   C N   1 
ATOM   6762 C  CA  . TYR   C  1  197 ? -4.280  20.180  15.278 1.00 43.89  ? 210 TYR   C CA  1 
ATOM   6763 C  C   . TYR   C  1  197 ? -4.991  19.189  14.365 1.00 47.55  ? 210 TYR   C C   1 
ATOM   6764 O  O   . TYR   C  1  197 ? -6.062  19.483  13.845 1.00 49.29  ? 210 TYR   C O   1 
ATOM   6765 C  CB  . TYR   C  1  197 ? -3.148  20.973  14.621 1.00 48.22  ? 210 TYR   C CB  1 
ATOM   6766 C  CG  . TYR   C  1  197 ? -2.869  22.211  15.454 1.00 52.07  ? 210 TYR   C CG  1 
ATOM   6767 C  CD1 . TYR   C  1  197 ? -3.588  23.387  15.250 1.00 55.16  ? 210 TYR   C CD1 1 
ATOM   6768 C  CD2 . TYR   C  1  197 ? -1.975  22.166  16.512 1.00 47.75  ? 210 TYR   C CD2 1 
ATOM   6769 C  CE1 . TYR   C  1  197 ? -3.395  24.494  16.058 1.00 56.17  ? 210 TYR   C CE1 1 
ATOM   6770 C  CE2 . TYR   C  1  197 ? -1.768  23.270  17.316 1.00 54.45  ? 210 TYR   C CE2 1 
ATOM   6771 C  CZ  . TYR   C  1  197 ? -2.482  24.434  17.094 1.00 54.82  ? 210 TYR   C CZ  1 
ATOM   6772 O  OH  . TYR   C  1  197 ? -2.270  25.515  17.898 1.00 57.58  ? 210 TYR   C OH  1 
ATOM   6773 N  N   . GLY   C  1  198 ? -4.408  18.007  14.182 1.00 45.08  ? 211 GLY   C N   1 
ATOM   6774 C  CA  . GLY   C  1  198 ? -5.021  16.991  13.355 1.00 40.45  ? 211 GLY   C CA  1 
ATOM   6775 C  C   . GLY   C  1  198 ? -6.403  16.598  13.863 1.00 38.85  ? 211 GLY   C C   1 
ATOM   6776 O  O   . GLY   C  1  198 ? -7.331  16.435  13.081 1.00 38.78  ? 211 GLY   C O   1 
ATOM   6777 N  N   . GLU   C  1  199 ? -6.553  16.454  15.176 1.00 36.48  ? 212 GLU   C N   1 
ATOM   6778 C  CA  A GLU   C  1  199 ? -7.812  15.990  15.737 0.50 38.58  ? 212 GLU   C CA  1 
ATOM   6779 C  CA  B GLU   C  1  199 ? -7.805  16.002  15.751 0.50 37.61  ? 212 GLU   C CA  1 
ATOM   6780 C  C   . GLU   C  1  199 ? -8.929  16.976  15.413 1.00 37.35  ? 212 GLU   C C   1 
ATOM   6781 O  O   . GLU   C  1  199 ? -10.083 16.567  15.337 1.00 40.33  ? 212 GLU   C O   1 
ATOM   6782 C  CB  A GLU   C  1  199 ? -7.704  15.692  17.235 0.50 41.23  ? 212 GLU   C CB  1 
ATOM   6783 C  CB  B GLU   C  1  199 ? -7.701  15.823  17.268 0.50 38.69  ? 212 GLU   C CB  1 
ATOM   6784 C  CG  A GLU   C  1  199 ? -7.119  14.309  17.514 0.50 41.82  ? 212 GLU   C CG  1 
ATOM   6785 C  CG  B GLU   C  1  199 ? -7.709  17.125  18.065 0.50 37.91  ? 212 GLU   C CG  1 
ATOM   6786 C  CD  A GLU   C  1  199 ? -6.343  14.153  18.825 0.50 42.59  ? 212 GLU   C CD  1 
ATOM   6787 C  CD  B GLU   C  1  199 ? -7.620  16.889  19.559 0.50 36.09  ? 212 GLU   C CD  1 
ATOM   6788 O  OE1 A GLU   C  1  199 ? -6.619  14.958  19.729 0.50 37.38  ? 212 GLU   C OE1 1 
ATOM   6789 O  OE1 B GLU   C  1  199 ? -7.229  15.758  19.900 0.50 34.68  ? 212 GLU   C OE1 1 
ATOM   6790 O  OE2 A GLU   C  1  199 ? -5.465  13.257  18.960 0.50 41.11  ? 212 GLU   C OE2 1 
ATOM   6791 O  OE2 B GLU   C  1  199 ? -7.973  17.779  20.360 0.50 33.42  ? 212 GLU   C OE2 1 
ATOM   6792 N  N   . THR   C  1  200 ? -8.596  18.255  15.217 1.00 35.26  ? 213 THR   C N   1 
ATOM   6793 C  CA  . THR   C  1  200 ? -9.638  19.253  15.016 1.00 44.79  ? 213 THR   C CA  1 
ATOM   6794 C  C   . THR   C  1  200 ? -10.182 19.194  13.594 1.00 45.84  ? 213 THR   C C   1 
ATOM   6795 O  O   . THR   C  1  200 ? -11.274 19.707  13.364 1.00 45.74  ? 213 THR   C O   1 
ATOM   6796 C  CB  . THR   C  1  200 ? -9.185  20.681  15.337 1.00 50.56  ? 213 THR   C CB  1 
ATOM   6797 O  OG1 . THR   C  1  200 ? -8.253  21.098  14.352 1.00 49.39  ? 213 THR   C OG1 1 
ATOM   6798 C  CG2 . THR   C  1  200 ? -8.567  20.789  16.718 1.00 54.41  ? 213 THR   C CG2 1 
ATOM   6799 N  N   . VAL   C  1  201 ? -9.439  18.582  12.656 1.00 45.03  ? 214 VAL   C N   1 
ATOM   6800 C  CA  . VAL   C  1  201 ? -9.941  18.459  11.296 1.00 39.32  ? 214 VAL   C CA  1 
ATOM   6801 C  C   . VAL   C  1  201 ? -10.476 17.061  11.004 1.00 38.60  ? 214 VAL   C C   1 
ATOM   6802 O  O   . VAL   C  1  201 ? -11.209 16.901  10.033 1.00 40.47  ? 214 VAL   C O   1 
ATOM   6803 C  CB  . VAL   C  1  201 ? -8.908  18.887  10.252 1.00 44.24  ? 214 VAL   C CB  1 
ATOM   6804 C  CG1 . VAL   C  1  201 ? -8.584  20.364  10.418 1.00 43.05  ? 214 VAL   C CG1 1 
ATOM   6805 C  CG2 . VAL   C  1  201 ? -7.649  18.027  10.272 1.00 49.37  ? 214 VAL   C CG2 1 
ATOM   6806 N  N   . PHE   C  1  202 ? -10.163 16.057  11.831 1.00 36.87  ? 215 PHE   C N   1 
ATOM   6807 C  CA  . PHE   C  1  202 ? -10.718 14.734  11.605 1.00 40.34  ? 215 PHE   C CA  1 
ATOM   6808 C  C   . PHE   C  1  202 ? -12.248 14.771  11.538 1.00 42.68  ? 215 PHE   C C   1 
ATOM   6809 O  O   . PHE   C  1  202 ? -12.819 14.040  10.740 1.00 42.32  ? 215 PHE   C O   1 
ATOM   6810 C  CB  . PHE   C  1  202 ? -10.312 13.713  12.664 1.00 44.03  ? 215 PHE   C CB  1 
ATOM   6811 C  CG  . PHE   C  1  202 ? -8.844  13.334  12.649 1.00 42.95  ? 215 PHE   C CG  1 
ATOM   6812 C  CD1 . PHE   C  1  202 ? -8.020  13.661  11.586 1.00 41.42  ? 215 PHE   C CD1 1 
ATOM   6813 C  CD2 . PHE   C  1  202 ? -8.307  12.610  13.698 1.00 46.26  ? 215 PHE   C CD2 1 
ATOM   6814 C  CE1 . PHE   C  1  202 ? -6.680  13.314  11.589 1.00 39.89  ? 215 PHE   C CE1 1 
ATOM   6815 C  CE2 . PHE   C  1  202 ? -6.975  12.248  13.693 1.00 46.11  ? 215 PHE   C CE2 1 
ATOM   6816 C  CZ  . PHE   C  1  202 ? -6.164  12.590  12.630 1.00 43.44  ? 215 PHE   C CZ  1 
ATOM   6817 N  N   . PRO   C  1  203 ? -12.982 15.548  12.373 1.00 46.16  ? 216 PRO   C N   1 
ATOM   6818 C  CA  . PRO   C  1  203 ? -14.441 15.598  12.270 1.00 45.84  ? 216 PRO   C CA  1 
ATOM   6819 C  C   . PRO   C  1  203 ? -14.936 16.045  10.898 1.00 43.95  ? 216 PRO   C C   1 
ATOM   6820 O  O   . PRO   C  1  203 ? -15.966 15.576  10.447 1.00 46.06  ? 216 PRO   C O   1 
ATOM   6821 C  CB  . PRO   C  1  203 ? -14.849 16.583  13.362 1.00 46.12  ? 216 PRO   C CB  1 
ATOM   6822 C  CG  . PRO   C  1  203 ? -13.745 16.479  14.367 1.00 46.92  ? 216 PRO   C CG  1 
ATOM   6823 C  CD  . PRO   C  1  203 ? -12.492 16.348  13.501 1.00 46.65  ? 216 PRO   C CD  1 
ATOM   6824 N  N   . ILE   C  1  204 ? -14.205 16.959  10.259 1.00 41.91  ? 217 ILE   C N   1 
ATOM   6825 C  CA  . ILE   C  1  204 ? -14.559 17.452  8.938  1.00 41.32  ? 217 ILE   C CA  1 
ATOM   6826 C  C   . ILE   C  1  204 ? -14.203 16.415  7.876  1.00 40.83  ? 217 ILE   C C   1 
ATOM   6827 O  O   . ILE   C  1  204 ? -15.020 16.114  7.014  1.00 40.54  ? 217 ILE   C O   1 
ATOM   6828 C  CB  . ILE   C  1  204 ? -13.877 18.802  8.675  1.00 43.44  ? 217 ILE   C CB  1 
ATOM   6829 C  CG1 . ILE   C  1  204 ? -14.285 19.847  9.718  1.00 44.84  ? 217 ILE   C CG1 1 
ATOM   6830 C  CG2 . ILE   C  1  204 ? -14.166 19.287  7.258  1.00 45.35  ? 217 ILE   C CG2 1 
ATOM   6831 C  CD1 . ILE   C  1  204 ? -13.363 21.051  9.758  1.00 48.31  ? 217 ILE   C CD1 1 
ATOM   6832 N  N   . ASN   C  1  205 ? -12.996 15.846  7.944  1.00 37.92  ? 218 ASN   C N   1 
ATOM   6833 C  CA  . ASN   C  1  205 ? -12.517 14.983  6.876  1.00 36.21  ? 218 ASN   C CA  1 
ATOM   6834 C  C   . ASN   C  1  205 ? -13.075 13.574  6.978  1.00 35.18  ? 218 ASN   C C   1 
ATOM   6835 O  O   . ASN   C  1  205 ? -13.200 12.928  5.941  1.00 36.94  ? 218 ASN   C O   1 
ATOM   6836 C  CB  . ASN   C  1  205 ? -10.998 14.897  6.807  1.00 37.75  ? 218 ASN   C CB  1 
ATOM   6837 C  CG  . ASN   C  1  205 ? -10.386 16.261  6.618  1.00 39.97  ? 218 ASN   C CG  1 
ATOM   6838 O  OD1 . ASN   C  1  205 ? -11.006 17.147  6.016  1.00 42.21  ? 218 ASN   C OD1 1 
ATOM   6839 N  ND2 . ASN   C  1  205 ? -9.221  16.477  7.209  1.00 41.04  ? 218 ASN   C ND2 1 
ATOM   6840 N  N   . LEU   C  1  206 ? -13.420 13.109  8.185  1.00 35.11  ? 219 LEU   C N   1 
ATOM   6841 C  CA  . LEU   C  1  206 ? -13.791 11.713  8.373  1.00 32.78  ? 219 LEU   C CA  1 
ATOM   6842 C  C   . LEU   C  1  206 ? -15.196 11.510  8.943  1.00 37.94  ? 219 LEU   C C   1 
ATOM   6843 O  O   . LEU   C  1  206 ? -15.770 10.427  8.780  1.00 36.48  ? 219 LEU   C O   1 
ATOM   6844 C  CB  . LEU   C  1  206 ? -12.739 11.083  9.273  1.00 33.86  ? 219 LEU   C CB  1 
ATOM   6845 C  CG  . LEU   C  1  206 ? -11.309 11.138  8.736  1.00 37.08  ? 219 LEU   C CG  1 
ATOM   6846 C  CD1 . LEU   C  1  206 ? -10.314 10.780  9.798  1.00 38.41  ? 219 LEU   C CD1 1 
ATOM   6847 C  CD2 . LEU   C  1  206 ? -11.184 10.215  7.536  1.00 38.13  ? 219 LEU   C CD2 1 
ATOM   6848 N  N   . PHE   C  1  207 ? -15.743 12.489  9.671  1.00 42.64  ? 220 PHE   C N   1 
ATOM   6849 C  CA  . PHE   C  1  207 ? -17.052 12.292  10.291 1.00 43.26  ? 220 PHE   C CA  1 
ATOM   6850 C  C   . PHE   C  1  207 ? -18.159 12.857  9.398  1.00 42.99  ? 220 PHE   C C   1 
ATOM   6851 O  O   . PHE   C  1  207 ? -19.320 12.539  9.609  1.00 44.12  ? 220 PHE   C O   1 
ATOM   6852 C  CB  . PHE   C  1  207 ? -17.176 12.947  11.669 1.00 43.79  ? 220 PHE   C CB  1 
ATOM   6853 C  CG  . PHE   C  1  207 ? -16.303 12.380  12.775 1.00 46.05  ? 220 PHE   C CG  1 
ATOM   6854 C  CD1 . PHE   C  1  207 ? -15.681 11.142  12.650 1.00 44.75  ? 220 PHE   C CD1 1 
ATOM   6855 C  CD2 . PHE   C  1  207 ? -16.164 13.076  13.971 1.00 47.75  ? 220 PHE   C CD2 1 
ATOM   6856 C  CE1 . PHE   C  1  207 ? -14.903 10.638  13.682 1.00 44.58  ? 220 PHE   C CE1 1 
ATOM   6857 C  CE2 . PHE   C  1  207 ? -15.364 12.584  14.990 1.00 44.20  ? 220 PHE   C CE2 1 
ATOM   6858 C  CZ  . PHE   C  1  207 ? -14.738 11.365  14.842 1.00 42.90  ? 220 PHE   C CZ  1 
ATOM   6859 N  N   . VAL   C  1  208 ? -17.812 13.716  8.434  1.00 37.83  ? 221 VAL   C N   1 
ATOM   6860 C  CA  . VAL   C  1  208 ? -18.776 14.165  7.442  1.00 41.83  ? 221 VAL   C CA  1 
ATOM   6861 C  C   . VAL   C  1  208 ? -18.937 13.074  6.383  1.00 45.28  ? 221 VAL   C C   1 
ATOM   6862 O  O   . VAL   C  1  208 ? -17.952 12.506  5.896  1.00 42.97  ? 221 VAL   C O   1 
ATOM   6863 C  CB  . VAL   C  1  208 ? -18.342 15.489  6.802  1.00 40.70  ? 221 VAL   C CB  1 
ATOM   6864 C  CG1 . VAL   C  1  208 ? -19.240 15.883  5.644  1.00 45.44  ? 221 VAL   C CG1 1 
ATOM   6865 C  CG2 . VAL   C  1  208 ? -18.310 16.591  7.836  1.00 38.09  ? 221 VAL   C CG2 1 
ATOM   6866 N  N   . ASP   C  1  209 ? -20.193 12.807  6.029  1.00 45.88  ? 222 ASP   C N   1 
ATOM   6867 C  CA  . ASP   C  1  209 ? -20.544 11.753  5.090  1.00 45.73  ? 222 ASP   C CA  1 
ATOM   6868 C  C   . ASP   C  1  209 ? -19.771 11.938  3.785  1.00 40.65  ? 222 ASP   C C   1 
ATOM   6869 O  O   . ASP   C  1  209 ? -19.624 13.050  3.292  1.00 40.72  ? 222 ASP   C O   1 
ATOM   6870 C  CB  . ASP   C  1  209 ? -22.046 11.709  4.862  1.00 42.70  ? 222 ASP   C CB  1 
ATOM   6871 C  CG  . ASP   C  1  209 ? -22.524 10.493  4.085  1.00 46.96  ? 222 ASP   C CG  1 
ATOM   6872 O  OD1 . ASP   C  1  209 ? -22.326 10.462  2.833  1.00 48.07  ? 222 ASP   C OD1 1 
ATOM   6873 O  OD2 . ASP   C  1  209 ? -23.037 9.555   4.735  1.00 42.73  ? 222 ASP   C OD2 1 
ATOM   6874 N  N   . GLY   C  1  210 ? -19.278 10.821  3.241  1.00 40.19  ? 223 GLY   C N   1 
ATOM   6875 C  CA  . GLY   C  1  210 ? -18.434 10.834  2.050  1.00 49.33  ? 223 GLY   C CA  1 
ATOM   6876 C  C   . GLY   C  1  210 ? -19.173 11.265  0.774  1.00 49.44  ? 223 GLY   C C   1 
ATOM   6877 O  O   . GLY   C  1  210 ? -18.523 11.644  -0.197 1.00 46.90  ? 223 GLY   C O   1 
ATOM   6878 N  N   . ARG   C  1  211 ? -20.516 11.225  0.788  1.00 49.03  ? 224 ARG   C N   1 
ATOM   6879 C  CA  . ARG   C  1  211 ? -21.314 11.687  -0.339 1.00 49.34  ? 224 ARG   C CA  1 
ATOM   6880 C  C   . ARG   C  1  211 ? -21.387 13.217  -0.365 1.00 48.87  ? 224 ARG   C C   1 
ATOM   6881 O  O   . ARG   C  1  211 ? -21.819 13.778  -1.362 1.00 46.22  ? 224 ARG   C O   1 
ATOM   6882 C  CB  . ARG   C  1  211 ? -22.711 11.060  -0.325 1.00 46.23  ? 224 ARG   C CB  1 
ATOM   6883 C  CG  . ARG   C  1  211 ? -22.695 9.557   -0.571 1.00 47.33  ? 224 ARG   C CG  1 
ATOM   6884 C  CD  . ARG   C  1  211 ? -23.995 8.869   -0.156 1.00 48.84  ? 224 ARG   C CD  1 
ATOM   6885 N  NE  . ARG   C  1  211 ? -24.241 9.000   1.289  1.00 59.78  ? 224 ARG   C NE  1 
ATOM   6886 C  CZ  . ARG   C  1  211 ? -25.294 8.520   1.956  1.00 59.34  ? 224 ARG   C CZ  1 
ATOM   6887 N  NH1 . ARG   C  1  211 ? -26.260 7.895   1.313  1.00 55.11  ? 224 ARG   C NH1 1 
ATOM   6888 N  NH2 . ARG   C  1  211 ? -25.386 8.665   3.270  1.00 57.50  ? 224 ARG   C NH2 1 
ATOM   6889 N  N   . VAL   C  1  212 ? -20.952 13.901  0.699  1.00 46.12  ? 225 VAL   C N   1 
ATOM   6890 C  CA  . VAL   C  1  212 ? -20.889 15.359  0.684  1.00 53.95  ? 225 VAL   C CA  1 
ATOM   6891 C  C   . VAL   C  1  212 ? -19.581 15.812  0.036  1.00 61.01  ? 225 VAL   C C   1 
ATOM   6892 O  O   . VAL   C  1  212 ? -18.518 15.661  0.621  1.00 62.85  ? 225 VAL   C O   1 
ATOM   6893 C  CB  . VAL   C  1  212 ? -21.030 15.957  2.098  1.00 50.19  ? 225 VAL   C CB  1 
ATOM   6894 C  CG1 . VAL   C  1  212 ? -20.930 17.482  2.113  1.00 46.96  ? 225 VAL   C CG1 1 
ATOM   6895 C  CG2 . VAL   C  1  212 ? -22.319 15.505  2.768  1.00 50.19  ? 225 VAL   C CG2 1 
ATOM   6896 N  N   . THR   C  1  213 ? -19.675 16.409  -1.158 1.00 71.26  ? 226 THR   C N   1 
ATOM   6897 C  CA  . THR   C  1  213 ? -18.513 16.755  -1.967 1.00 74.99  ? 226 THR   C CA  1 
ATOM   6898 C  C   . THR   C  1  213 ? -18.106 18.209  -1.739 1.00 72.54  ? 226 THR   C C   1 
ATOM   6899 O  O   . THR   C  1  213 ? -16.941 18.558  -1.884 1.00 67.36  ? 226 THR   C O   1 
ATOM   6900 C  CB  . THR   C  1  213 ? -18.820 16.510  -3.449 1.00 85.15  ? 226 THR   C CB  1 
ATOM   6901 O  OG1 . THR   C  1  213 ? -19.954 17.299  -3.820 1.00 76.64  ? 226 THR   C OG1 1 
ATOM   6902 C  CG2 . THR   C  1  213 ? -19.059 15.041  -3.762 1.00 84.08  ? 226 THR   C CG2 1 
ATOM   6903 N  N   . THR   C  1  214 ? -19.072 19.056  -1.391 1.00 78.51  ? 227 THR   C N   1 
ATOM   6904 C  CA  . THR   C  1  214 ? -18.858 20.492  -1.360 1.00 88.49  ? 227 THR   C CA  1 
ATOM   6905 C  C   . THR   C  1  214 ? -19.259 21.034  0.018  1.00 83.37  ? 227 THR   C C   1 
ATOM   6906 O  O   . THR   C  1  214 ? -20.227 20.558  0.618  1.00 78.95  ? 227 THR   C O   1 
ATOM   6907 C  CB  . THR   C  1  214 ? -19.659 21.092  -2.523 1.00 94.52  ? 227 THR   C CB  1 
ATOM   6908 O  OG1 . THR   C  1  214 ? -19.333 22.479  -2.553 1.00 101.20 ? 227 THR   C OG1 1 
ATOM   6909 C  CG2 . THR   C  1  214 ? -21.165 20.892  -2.411 1.00 89.15  ? 227 THR   C CG2 1 
ATOM   6910 N  N   . ASP   C  1  215 ? -18.499 22.018  0.526  1.00 80.44  ? 228 ASP   C N   1 
ATOM   6911 C  CA  . ASP   C  1  215 ? -18.871 22.738  1.737  1.00 87.12  ? 228 ASP   C CA  1 
ATOM   6912 C  C   . ASP   C  1  215 ? -19.046 21.728  2.876  1.00 75.47  ? 228 ASP   C C   1 
ATOM   6913 O  O   . ASP   C  1  215 ? -20.128 21.573  3.434  1.00 70.83  ? 228 ASP   C O   1 
ATOM   6914 C  CB  . ASP   C  1  215 ? -20.079 23.632  1.468  1.00 99.45  ? 228 ASP   C CB  1 
ATOM   6915 C  CG  . ASP   C  1  215 ? -20.529 24.544  2.607  1.00 109.04 ? 228 ASP   C CG  1 
ATOM   6916 O  OD1 . ASP   C  1  215 ? -19.649 25.162  3.242  1.00 115.87 ? 228 ASP   C OD1 1 
ATOM   6917 O  OD2 . ASP   C  1  215 ? -21.761 24.650  2.840  1.00 102.77 ? 228 ASP   C OD2 1 
ATOM   6918 N  N   . ARG   C  1  216 ? -17.969 21.006  3.190  1.00 67.02  ? 229 ARG   C N   1 
ATOM   6919 C  CA  . ARG   C  1  216 ? -18.055 19.897  4.123  1.00 62.19  ? 229 ARG   C CA  1 
ATOM   6920 C  C   . ARG   C  1  216 ? -18.146 20.458  5.541  1.00 53.92  ? 229 ARG   C C   1 
ATOM   6921 O  O   . ARG   C  1  216 ? -17.343 21.298  5.933  1.00 52.04  ? 229 ARG   C O   1 
ATOM   6922 C  CB  . ARG   C  1  216 ? -16.894 18.912  3.936  1.00 61.70  ? 229 ARG   C CB  1 
ATOM   6923 C  CG  . ARG   C  1  216 ? -17.064 18.012  2.717  1.00 62.88  ? 229 ARG   C CG  1 
ATOM   6924 C  CD  . ARG   C  1  216 ? -15.806 17.222  2.417  1.00 58.61  ? 229 ARG   C CD  1 
ATOM   6925 N  NE  . ARG   C  1  216 ? -15.475 16.242  3.458  1.00 55.85  ? 229 ARG   C NE  1 
ATOM   6926 C  CZ  . ARG   C  1  216 ? -16.131 15.108  3.696  1.00 57.41  ? 229 ARG   C CZ  1 
ATOM   6927 N  NH1 . ARG   C  1  216 ? -17.163 14.752  2.949  1.00 56.44  ? 229 ARG   C NH1 1 
ATOM   6928 N  NH2 . ARG   C  1  216 ? -15.765 14.319  4.693  1.00 59.07  ? 229 ARG   C NH2 1 
ATOM   6929 N  N   . LYS   C  1  217 ? -19.161 20.003  6.278  1.00 50.36  ? 230 LYS   C N   1 
ATOM   6930 C  CA  . LYS   C  1  217 ? -19.474 20.539  7.590  1.00 56.85  ? 230 LYS   C CA  1 
ATOM   6931 C  C   . LYS   C  1  217 ? -20.259 19.487  8.373  1.00 53.52  ? 230 LYS   C C   1 
ATOM   6932 O  O   . LYS   C  1  217 ? -21.015 18.709  7.791  1.00 51.68  ? 230 LYS   C O   1 
ATOM   6933 C  CB  . LYS   C  1  217 ? -20.257 21.840  7.391  1.00 63.11  ? 230 LYS   C CB  1 
ATOM   6934 C  CG  . LYS   C  1  217 ? -21.630 21.644  6.774  1.00 67.55  ? 230 LYS   C CG  1 
ATOM   6935 C  CD  . LYS   C  1  217 ? -22.360 22.939  6.414  1.00 74.99  ? 230 LYS   C CD  1 
ATOM   6936 C  CE  . LYS   C  1  217 ? -23.759 22.642  5.943  1.00 75.97  ? 230 LYS   C CE  1 
ATOM   6937 N  NZ  . LYS   C  1  217 ? -24.477 23.858  5.566  1.00 71.42  ? 230 LYS   C NZ  1 
ATOM   6938 N  N   . LEU   C  1  218 ? -20.064 19.449  9.695  1.00 51.06  ? 231 LEU   C N   1 
ATOM   6939 C  CA  . LEU   C  1  218 ? -20.654 18.396  10.509 1.00 51.78  ? 231 LEU   C CA  1 
ATOM   6940 C  C   . LEU   C  1  218 ? -21.827 18.940  11.330 1.00 49.47  ? 231 LEU   C C   1 
ATOM   6941 O  O   . LEU   C  1  218 ? -21.670 19.934  12.024 1.00 48.92  ? 231 LEU   C O   1 
ATOM   6942 C  CB  . LEU   C  1  218 ? -19.537 17.864  11.403 1.00 46.86  ? 231 LEU   C CB  1 
ATOM   6943 C  CG  . LEU   C  1  218 ? -19.914 16.675  12.283 1.00 49.56  ? 231 LEU   C CG  1 
ATOM   6944 C  CD1 . LEU   C  1  218 ? -20.251 15.437  11.448 1.00 53.85  ? 231 LEU   C CD1 1 
ATOM   6945 C  CD2 . LEU   C  1  218 ? -18.802 16.399  13.272 1.00 54.03  ? 231 LEU   C CD2 1 
ATOM   6946 N  N   . SER   C  1  219 ? -22.988 18.270  11.275 1.00 50.41  ? 232 SER   C N   1 
ATOM   6947 C  CA  . SER   C  1  219 ? -24.128 18.638  12.105 1.00 50.30  ? 232 SER   C CA  1 
ATOM   6948 C  C   . SER   C  1  219 ? -23.848 18.289  13.567 1.00 61.17  ? 232 SER   C C   1 
ATOM   6949 O  O   . SER   C  1  219 ? -23.024 17.426  13.868 1.00 58.70  ? 232 SER   C O   1 
ATOM   6950 C  CB  . SER   C  1  219 ? -25.376 17.957  11.658 1.00 47.03  ? 232 SER   C CB  1 
ATOM   6951 O  OG  . SER   C  1  219 ? -25.371 16.593  12.053 1.00 50.66  ? 232 SER   C OG  1 
ATOM   6952 N  N   . MET   C  1  220 ? -24.559 18.951  14.479 1.00 54.69  ? 233 MET   C N   1 
ATOM   6953 C  CA  . MET   C  1  220 ? -24.360 18.727  15.898 1.00 51.10  ? 233 MET   C CA  1 
ATOM   6954 C  C   . MET   C  1  220 ? -24.931 17.375  16.310 1.00 51.11  ? 233 MET   C C   1 
ATOM   6955 O  O   . MET   C  1  220 ? -24.469 16.763  17.272 1.00 50.04  ? 233 MET   C O   1 
ATOM   6956 C  CB  . MET   C  1  220 ? -25.015 19.856  16.698 1.00 52.71  ? 233 MET   C CB  1 
ATOM   6957 C  CG  . MET   C  1  220 ? -24.362 21.206  16.488 1.00 57.10  ? 233 MET   C CG  1 
ATOM   6958 S  SD  . MET   C  1  220 ? -22.594 21.212  16.854 1.00 63.01  ? 233 MET   C SD  1 
ATOM   6959 C  CE  . MET   C  1  220 ? -21.872 21.106  15.212 1.00 69.59  ? 233 MET   C CE  1 
ATOM   6960 N  N   . GLU   C  1  221 ? -25.939 16.909  15.571 1.00 51.13  ? 234 GLU   C N   1 
ATOM   6961 C  CA  . GLU   C  1  221 ? -26.556 15.612  15.818 1.00 58.63  ? 234 GLU   C CA  1 
ATOM   6962 C  C   . GLU   C  1  221 ? -25.531 14.515  15.517 1.00 51.82  ? 234 GLU   C C   1 
ATOM   6963 O  O   . GLU   C  1  221 ? -25.374 13.587  16.297 1.00 55.69  ? 234 GLU   C O   1 
ATOM   6964 C  CB  . GLU   C  1  221 ? -27.829 15.404  14.984 1.00 67.40  ? 234 GLU   C CB  1 
ATOM   6965 C  CG  . GLU   C  1  221 ? -28.941 16.430  15.236 1.00 82.72  ? 234 GLU   C CG  1 
ATOM   6966 C  CD  . GLU   C  1  221 ? -28.796 17.887  14.756 1.00 90.22  ? 234 GLU   C CD  1 
ATOM   6967 O  OE1 . GLU   C  1  221 ? -27.915 18.267  13.933 1.00 76.38  ? 234 GLU   C OE1 1 
ATOM   6968 O  OE2 . GLU   C  1  221 ? -29.611 18.697  15.262 1.00 97.70  ? 234 GLU   C OE2 1 
ATOM   6969 N  N   . ASP   C  1  222 ? -24.854 14.617  14.369 1.00 51.17  ? 235 ASP   C N   1 
ATOM   6970 C  CA  . ASP   C  1  222 ? -23.847 13.646  13.968 1.00 53.05  ? 235 ASP   C CA  1 
ATOM   6971 C  C   . ASP   C  1  222 ? -22.665 13.711  14.935 1.00 47.42  ? 235 ASP   C C   1 
ATOM   6972 O  O   . ASP   C  1  222 ? -22.158 12.685  15.356 1.00 49.49  ? 235 ASP   C O   1 
ATOM   6973 C  CB  . ASP   C  1  222 ? -23.442 13.836  12.514 1.00 55.37  ? 235 ASP   C CB  1 
ATOM   6974 C  CG  . ASP   C  1  222 ? -24.510 13.488  11.484 1.00 59.71  ? 235 ASP   C CG  1 
ATOM   6975 O  OD1 . ASP   C  1  222 ? -25.553 12.922  11.881 1.00 64.12  ? 235 ASP   C OD1 1 
ATOM   6976 O  OD2 . ASP   C  1  222 ? -24.298 13.791  10.291 1.00 60.45  ? 235 ASP   C OD2 1 
ATOM   6977 N  N   . ALA   C  1  223 ? -22.256 14.924  15.303 1.00 44.41  ? 236 ALA   C N   1 
ATOM   6978 C  CA  . ALA   C  1  223 ? -21.185 15.091  16.260 1.00 47.87  ? 236 ALA   C CA  1 
ATOM   6979 C  C   . ALA   C  1  223 ? -21.544 14.375  17.558 1.00 53.78  ? 236 ALA   C C   1 
ATOM   6980 O  O   . ALA   C  1  223 ? -20.732 13.614  18.065 1.00 50.10  ? 236 ALA   C O   1 
ATOM   6981 C  CB  . ALA   C  1  223 ? -20.877 16.552  16.489 1.00 49.84  ? 236 ALA   C CB  1 
ATOM   6982 N  N   . ALA   C  1  224 ? -22.762 14.569  18.075 1.00 48.45  ? 237 ALA   C N   1 
ATOM   6983 C  CA  . ALA   C  1  224 ? -23.096 13.971  19.354 1.00 51.35  ? 237 ALA   C CA  1 
ATOM   6984 C  C   . ALA   C  1  224 ? -23.122 12.450  19.216 1.00 46.57  ? 237 ALA   C C   1 
ATOM   6985 O  O   . ALA   C  1  224 ? -22.689 11.706  20.095 1.00 43.10  ? 237 ALA   C O   1 
ATOM   6986 C  CB  . ALA   C  1  224 ? -24.421 14.509  19.844 1.00 58.12  ? 237 ALA   C CB  1 
ATOM   6987 N  N   . SER   C  1  225 ? -23.634 11.989  18.080 1.00 44.78  ? 238 SER   C N   1 
ATOM   6988 C  CA  . SER   C  1  225 ? -23.773 10.561  17.855 1.00 45.62  ? 238 SER   C CA  1 
ATOM   6989 C  C   . SER   C  1  225 ? -22.406 9.880   17.989 1.00 42.43  ? 238 SER   C C   1 
ATOM   6990 O  O   . SER   C  1  225 ? -22.286 8.846   18.638 1.00 41.27  ? 238 SER   C O   1 
ATOM   6991 C  CB  . SER   C  1  225 ? -24.433 10.307  16.512 1.00 41.22  ? 238 SER   C CB  1 
ATOM   6992 O  OG  . SER   C  1  225 ? -24.550 8.919   16.247 1.00 42.77  ? 238 SER   C OG  1 
ATOM   6993 N  N   . ILE   C  1  226 ? -21.372 10.488  17.410 1.00 40.51  ? 239 ILE   C N   1 
ATOM   6994 C  CA  . ILE   C  1  226 ? -20.043 9.892   17.379 1.00 44.68  ? 239 ILE   C CA  1 
ATOM   6995 C  C   . ILE   C  1  226 ? -19.282 10.179  18.673 1.00 40.95  ? 239 ILE   C C   1 
ATOM   6996 O  O   . ILE   C  1  226 ? -18.773 9.255   19.305 1.00 46.68  ? 239 ILE   C O   1 
ATOM   6997 C  CB  . ILE   C  1  226 ? -19.273 10.397  16.147 1.00 48.91  ? 239 ILE   C CB  1 
ATOM   6998 C  CG1 . ILE   C  1  226 ? -19.932 9.896   14.861 1.00 46.65  ? 239 ILE   C CG1 1 
ATOM   6999 C  CG2 . ILE   C  1  226 ? -17.796 9.999   16.216 1.00 49.83  ? 239 ILE   C CG2 1 
ATOM   7000 C  CD1 . ILE   C  1  226 ? -19.503 10.656  13.628 1.00 44.96  ? 239 ILE   C CD1 1 
ATOM   7001 N  N   . PHE   C  1  227 ? -19.194 11.462  19.052 1.00 37.59  ? 240 PHE   C N   1 
ATOM   7002 C  CA  . PHE   C  1  227 ? -18.376 11.873  20.178 1.00 43.44  ? 240 PHE   C CA  1 
ATOM   7003 C  C   . PHE   C  1  227 ? -18.932 11.327  21.490 1.00 45.85  ? 240 PHE   C C   1 
ATOM   7004 O  O   . PHE   C  1  227 ? -18.146 10.962  22.360 1.00 41.98  ? 240 PHE   C O   1 
ATOM   7005 C  CB  . PHE   C  1  227 ? -18.264 13.389  20.319 1.00 44.64  ? 240 PHE   C CB  1 
ATOM   7006 C  CG  . PHE   C  1  227 ? -17.318 14.074  19.350 1.00 46.95  ? 240 PHE   C CG  1 
ATOM   7007 C  CD1 . PHE   C  1  227 ? -15.942 14.015  19.539 1.00 50.50  ? 240 PHE   C CD1 1 
ATOM   7008 C  CD2 . PHE   C  1  227 ? -17.800 14.854  18.315 1.00 52.80  ? 240 PHE   C CD2 1 
ATOM   7009 C  CE1 . PHE   C  1  227 ? -15.082 14.684  18.692 1.00 48.24  ? 240 PHE   C CE1 1 
ATOM   7010 C  CE2 . PHE   C  1  227 ? -16.931 15.537  17.476 1.00 53.04  ? 240 PHE   C CE2 1 
ATOM   7011 C  CZ  . PHE   C  1  227 ? -15.578 15.461  17.673 1.00 50.84  ? 240 PHE   C CZ  1 
ATOM   7012 N  N   . ARG   C  1  228 ? -20.265 11.287  21.630 1.00 49.64  ? 241 ARG   C N   1 
ATOM   7013 C  CA  . ARG   C  1  228 ? -20.884 10.833  22.866 1.00 46.71  ? 241 ARG   C CA  1 
ATOM   7014 C  C   . ARG   C  1  228 ? -21.297 9.370   22.747 1.00 47.29  ? 241 ARG   C C   1 
ATOM   7015 O  O   . ARG   C  1  228 ? -20.969 8.563   23.613 1.00 49.73  ? 241 ARG   C O   1 
ATOM   7016 C  CB  . ARG   C  1  228 ? -22.107 11.659  23.278 1.00 53.71  ? 241 ARG   C CB  1 
ATOM   7017 C  CG  . ARG   C  1  228 ? -22.675 11.238  24.633 1.00 57.32  ? 241 ARG   C CG  1 
ATOM   7018 C  CD  . ARG   C  1  228 ? -23.843 12.119  25.098 1.00 64.28  ? 241 ARG   C CD  1 
ATOM   7019 N  NE  . ARG   C  1  228 ? -25.033 11.838  24.279 1.00 62.97  ? 241 ARG   C NE  1 
ATOM   7020 C  CZ  . ARG   C  1  228 ? -25.737 12.718  23.572 1.00 66.25  ? 241 ARG   C CZ  1 
ATOM   7021 N  NH1 . ARG   C  1  228 ? -25.528 14.021  23.704 1.00 63.82  ? 241 ARG   C NH1 1 
ATOM   7022 N  NH2 . ARG   C  1  228 ? -26.650 12.272  22.733 1.00 65.60  ? 241 ARG   C NH2 1 
ATOM   7023 N  N   . ASP   C  1  229 ? -22.043 9.011   21.699 1.00 40.56  ? 242 ASP   C N   1 
ATOM   7024 C  CA  . ASP   C  1  229 ? -22.704 7.714   21.699 1.00 43.53  ? 242 ASP   C CA  1 
ATOM   7025 C  C   . ASP   C  1  229 ? -21.886 6.626   21.017 1.00 40.51  ? 242 ASP   C C   1 
ATOM   7026 O  O   . ASP   C  1  229 ? -22.260 5.463   21.100 1.00 39.26  ? 242 ASP   C O   1 
ATOM   7027 C  CB  . ASP   C  1  229 ? -24.129 7.829   21.169 1.00 57.51  ? 242 ASP   C CB  1 
ATOM   7028 C  CG  . ASP   C  1  229 ? -25.102 8.516   22.136 1.00 65.78  ? 242 ASP   C CG  1 
ATOM   7029 O  OD1 . ASP   C  1  229 ? -24.993 8.216   23.360 1.00 67.65  ? 242 ASP   C OD1 1 
ATOM   7030 O  OD2 . ASP   C  1  229 ? -25.956 9.333   21.669 1.00 73.81  ? 242 ASP   C OD2 1 
ATOM   7031 N  N   . MET   C  1  230 ? -20.774 6.993   20.361 1.00 41.57  ? 243 MET   C N   1 
ATOM   7032 C  CA  A MET   C  1  230 ? -19.911 6.024   19.708 0.50 38.91  ? 243 MET   C CA  1 
ATOM   7033 C  CA  B MET   C  1  230 ? -19.914 6.012   19.719 0.50 40.87  ? 243 MET   C CA  1 
ATOM   7034 C  C   . MET   C  1  230 ? -20.701 5.318   18.611 1.00 39.11  ? 243 MET   C C   1 
ATOM   7035 O  O   . MET   C  1  230 ? -20.579 4.095   18.442 1.00 37.69  ? 243 MET   C O   1 
ATOM   7036 C  CB  A MET   C  1  230 ? -19.390 4.994   20.715 0.50 39.12  ? 243 MET   C CB  1 
ATOM   7037 C  CB  B MET   C  1  230 ? -19.465 4.900   20.682 0.50 43.95  ? 243 MET   C CB  1 
ATOM   7038 C  CG  A MET   C  1  230 ? -18.770 5.619   21.964 0.50 39.47  ? 243 MET   C CG  1 
ATOM   7039 C  CG  B MET   C  1  230 ? -18.890 5.350   22.021 0.50 48.11  ? 243 MET   C CG  1 
ATOM   7040 S  SD  A MET   C  1  230 ? -18.308 4.374   23.184 0.50 35.99  ? 243 MET   C SD  1 
ATOM   7041 S  SD  B MET   C  1  230 ? -18.656 3.898   23.070 0.50 48.04  ? 243 MET   C SD  1 
ATOM   7042 C  CE  A MET   C  1  230 ? -17.961 5.441   24.595 0.50 33.54  ? 243 MET   C CE  1 
ATOM   7043 C  CE  B MET   C  1  230 ? -20.373 3.390   23.279 0.50 56.44  ? 243 MET   C CE  1 
ATOM   7044 N  N   . ARG   C  1  231 ? -21.523 6.092   17.885 1.00 40.57  ? 244 ARG   C N   1 
ATOM   7045 C  CA  . ARG   C  1  231 ? -22.465 5.551   16.914 1.00 42.07  ? 244 ARG   C CA  1 
ATOM   7046 C  C   . ARG   C  1  231 ? -22.347 6.344   15.620 1.00 38.21  ? 244 ARG   C C   1 
ATOM   7047 O  O   . ARG   C  1  231 ? -22.372 7.573   15.631 1.00 33.94  ? 244 ARG   C O   1 
ATOM   7048 C  CB  . ARG   C  1  231 ? -23.904 5.643   17.441 1.00 46.01  ? 244 ARG   C CB  1 
ATOM   7049 C  CG  . ARG   C  1  231 ? -24.949 4.937   16.584 1.00 46.74  ? 244 ARG   C CG  1 
ATOM   7050 C  CD  . ARG   C  1  231 ? -26.221 4.477   17.303 1.00 47.89  ? 244 ARG   C CD  1 
ATOM   7051 N  NE  . ARG   C  1  231 ? -26.868 5.635   17.941 1.00 56.30  ? 244 ARG   C NE  1 
ATOM   7052 C  CZ  . ARG   C  1  231 ? -27.191 5.774   19.243 1.00 58.21  ? 244 ARG   C CZ  1 
ATOM   7053 N  NH1 . ARG   C  1  231 ? -27.080 4.759   20.110 1.00 53.56  ? 244 ARG   C NH1 1 
ATOM   7054 N  NH2 . ARG   C  1  231 ? -27.662 6.946   19.653 1.00 59.48  ? 244 ARG   C NH2 1 
ATOM   7055 N  N   . PHE   C  1  232 ? -22.183 5.622   14.510 1.00 38.66  ? 245 PHE   C N   1 
ATOM   7056 C  CA  . PHE   C  1  232 ? -22.234 6.248   13.197 1.00 41.51  ? 245 PHE   C CA  1 
ATOM   7057 C  C   . PHE   C  1  232 ? -23.603 6.867   12.960 1.00 40.17  ? 245 PHE   C C   1 
ATOM   7058 O  O   . PHE   C  1  232 ? -24.613 6.269   13.312 1.00 35.14  ? 245 PHE   C O   1 
ATOM   7059 C  CB  . PHE   C  1  232 ? -22.073 5.212   12.085 1.00 39.28  ? 245 PHE   C CB  1 
ATOM   7060 C  CG  . PHE   C  1  232 ? -20.653 4.705   11.905 1.00 36.53  ? 245 PHE   C CG  1 
ATOM   7061 C  CD1 . PHE   C  1  232 ? -19.643 5.570   11.501 1.00 35.00  ? 245 PHE   C CD1 1 
ATOM   7062 C  CD2 . PHE   C  1  232 ? -20.356 3.360   12.082 1.00 37.05  ? 245 PHE   C CD2 1 
ATOM   7063 C  CE1 . PHE   C  1  232 ? -18.362 5.100   11.311 1.00 33.36  ? 245 PHE   C CE1 1 
ATOM   7064 C  CE2 . PHE   C  1  232 ? -19.072 2.894   11.861 1.00 34.82  ? 245 PHE   C CE2 1 
ATOM   7065 C  CZ  . PHE   C  1  232 ? -18.079 3.766   11.504 1.00 31.90  ? 245 PHE   C CZ  1 
ATOM   7066 N  N   . PRO   C  1  233 ? -23.698 8.031   12.298 1.00 41.41  ? 246 PRO   C N   1 
ATOM   7067 C  CA  . PRO   C  1  233 ? -24.986 8.499   11.781 1.00 43.73  ? 246 PRO   C CA  1 
ATOM   7068 C  C   . PRO   C  1  233 ? -25.690 7.391   11.006 1.00 46.97  ? 246 PRO   C C   1 
ATOM   7069 O  O   . PRO   C  1  233 ? -25.058 6.454   10.504 1.00 41.25  ? 246 PRO   C O   1 
ATOM   7070 C  CB  . PRO   C  1  233 ? -24.607 9.697   10.913 1.00 43.79  ? 246 PRO   C CB  1 
ATOM   7071 C  CG  . PRO   C  1  233 ? -23.306 10.204  11.562 1.00 46.41  ? 246 PRO   C CG  1 
ATOM   7072 C  CD  . PRO   C  1  233 ? -22.587 8.939   11.988 1.00 45.00  ? 246 PRO   C CD  1 
ATOM   7073 N  N   . ASP   C  1  234 ? -27.021 7.460   10.958 1.00 50.22  ? 247 ASP   C N   1 
ATOM   7074 C  CA  . ASP   C  1  234 ? -27.806 6.540   10.136 1.00 58.22  ? 247 ASP   C CA  1 
ATOM   7075 C  C   . ASP   C  1  234 ? -27.320 6.637   8.687  1.00 48.37  ? 247 ASP   C C   1 
ATOM   7076 O  O   . ASP   C  1  234 ? -27.098 7.742   8.171  1.00 43.53  ? 247 ASP   C O   1 
ATOM   7077 C  CB  . ASP   C  1  234 ? -29.306 6.845   10.166 1.00 66.86  ? 247 ASP   C CB  1 
ATOM   7078 C  CG  . ASP   C  1  234 ? -30.009 6.747   11.517 1.00 76.97  ? 247 ASP   C CG  1 
ATOM   7079 O  OD1 . ASP   C  1  234 ? -29.727 5.763   12.233 1.00 76.03  ? 247 ASP   C OD1 1 
ATOM   7080 O  OD2 . ASP   C  1  234 ? -30.843 7.638   11.830 1.00 78.03  ? 247 ASP   C OD2 1 
ATOM   7081 N  N   . ASP   C  1  235 ? -27.129 5.471   8.054  1.00 47.46  ? 248 ASP   C N   1 
ATOM   7082 C  CA  . ASP   C  1  235 ? -26.782 5.402   6.637  1.00 56.36  ? 248 ASP   C CA  1 
ATOM   7083 C  C   . ASP   C  1  235 ? -25.421 6.064   6.349  1.00 49.99  ? 248 ASP   C C   1 
ATOM   7084 O  O   . ASP   C  1  235 ? -25.180 6.542   5.244  1.00 42.75  ? 248 ASP   C O   1 
ATOM   7085 C  CB  . ASP   C  1  235 ? -27.889 6.010   5.781  1.00 54.97  ? 248 ASP   C CB  1 
ATOM   7086 C  CG  . ASP   C  1  235 ? -27.758 5.738   4.287  1.00 57.62  ? 248 ASP   C CG  1 
ATOM   7087 O  OD1 . ASP   C  1  235 ? -27.602 4.533   3.932  1.00 46.73  ? 248 ASP   C OD1 1 
ATOM   7088 O  OD2 . ASP   C  1  235 ? -27.788 6.736   3.500  1.00 48.70  ? 248 ASP   C OD2 1 
ATOM   7089 N  N   . PHE   C  1  236 ? -24.519 6.087   7.340  1.00 43.25  ? 249 PHE   C N   1 
ATOM   7090 C  CA  . PHE   C  1  236 ? -23.255 6.792   7.195  1.00 39.94  ? 249 PHE   C CA  1 
ATOM   7091 C  C   . PHE   C  1  236 ? -22.395 6.138   6.117  1.00 34.31  ? 249 PHE   C C   1 
ATOM   7092 O  O   . PHE   C  1  236 ? -22.155 4.916   6.128  1.00 32.50  ? 249 PHE   C O   1 
ATOM   7093 C  CB  . PHE   C  1  236 ? -22.461 6.791   8.499  1.00 38.56  ? 249 PHE   C CB  1 
ATOM   7094 C  CG  . PHE   C  1  236 ? -21.175 7.589   8.408  1.00 37.29  ? 249 PHE   C CG  1 
ATOM   7095 C  CD1 . PHE   C  1  236 ? -21.200 8.978   8.339  1.00 35.69  ? 249 PHE   C CD1 1 
ATOM   7096 C  CD2 . PHE   C  1  236 ? -19.949 6.943   8.389  1.00 34.35  ? 249 PHE   C CD2 1 
ATOM   7097 C  CE1 . PHE   C  1  236 ? -20.015 9.693   8.256  1.00 34.71  ? 249 PHE   C CE1 1 
ATOM   7098 C  CE2 . PHE   C  1  236 ? -18.778 7.673   8.325  1.00 34.22  ? 249 PHE   C CE2 1 
ATOM   7099 C  CZ  . PHE   C  1  236 ? -18.815 9.040   8.268  1.00 32.90  ? 249 PHE   C CZ  1 
ATOM   7100 N  N   . HIS   C  1  237 ? -21.934 6.986   5.200  1.00 34.56  ? 250 HIS   C N   1 
ATOM   7101 C  CA  . HIS   C  1  237 ? -20.979 6.582   4.180  1.00 39.10  ? 250 HIS   C CA  1 
ATOM   7102 C  C   . HIS   C  1  237 ? -19.650 7.252   4.489  1.00 33.28  ? 250 HIS   C C   1 
ATOM   7103 O  O   . HIS   C  1  237 ? -19.595 8.476   4.637  1.00 32.69  ? 250 HIS   C O   1 
ATOM   7104 C  CB  . HIS   C  1  237 ? -21.449 6.988   2.773  1.00 42.39  ? 250 HIS   C CB  1 
ATOM   7105 C  CG  . HIS   C  1  237 ? -22.566 6.159   2.260  1.00 50.61  ? 250 HIS   C CG  1 
ATOM   7106 N  ND1 . HIS   C  1  237 ? -23.672 5.867   3.023  1.00 54.09  ? 250 HIS   C ND1 1 
ATOM   7107 C  CD2 . HIS   C  1  237 ? -22.759 5.563   1.074  1.00 53.06  ? 250 HIS   C CD2 1 
ATOM   7108 C  CE1 . HIS   C  1  237 ? -24.493 5.103   2.314  1.00 59.18  ? 250 HIS   C CE1 1 
ATOM   7109 N  NE2 . HIS   C  1  237 ? -23.953 4.895   1.134  1.00 51.30  ? 250 HIS   C NE2 1 
ATOM   7110 N  N   . ARG   C  1  238 ? -18.584 6.453   4.531  1.00 35.76  ? 251 ARG   C N   1 
ATOM   7111 C  CA  . ARG   C  1  238 ? -17.252 6.958   4.838  1.00 34.93  ? 251 ARG   C CA  1 
ATOM   7112 C  C   . ARG   C  1  238 ? -16.745 7.884   3.742  1.00 34.29  ? 251 ARG   C C   1 
ATOM   7113 O  O   . ARG   C  1  238 ? -17.272 7.889   2.631  1.00 34.00  ? 251 ARG   C O   1 
ATOM   7114 C  CB  . ARG   C  1  238 ? -16.240 5.817   4.975  1.00 35.46  ? 251 ARG   C CB  1 
ATOM   7115 C  CG  . ARG   C  1  238 ? -15.993 5.062   3.683  1.00 34.49  ? 251 ARG   C CG  1 
ATOM   7116 C  CD  . ARG   C  1  238 ? -15.075 3.888   3.898  1.00 34.01  ? 251 ARG   C CD  1 
ATOM   7117 N  NE  . ARG   C  1  238 ? -14.471 3.547   2.614  1.00 35.33  ? 251 ARG   C NE  1 
ATOM   7118 C  CZ  . ARG   C  1  238 ? -13.767 2.465   2.359  1.00 37.19  ? 251 ARG   C CZ  1 
ATOM   7119 N  NH1 . ARG   C  1  238 ? -13.490 1.595   3.308  1.00 42.14  ? 251 ARG   C NH1 1 
ATOM   7120 N  NH2 . ARG   C  1  238 ? -13.401 2.223   1.113  1.00 38.62  ? 251 ARG   C NH2 1 
ATOM   7121 N  N   . SER   C  1  239 ? -15.698 8.648   4.076  1.00 34.31  ? 252 SER   C N   1 
ATOM   7122 C  CA  . SER   C  1  239 ? -14.989 9.506   3.143  1.00 36.60  ? 252 SER   C CA  1 
ATOM   7123 C  C   . SER   C  1  239 ? -14.757 8.784   1.817  1.00 38.92  ? 252 SER   C C   1 
ATOM   7124 O  O   . SER   C  1  239 ? -14.483 7.580   1.804  1.00 36.95  ? 252 SER   C O   1 
ATOM   7125 C  CB  . SER   C  1  239 ? -13.680 9.943   3.725  1.00 40.62  ? 252 SER   C CB  1 
ATOM   7126 O  OG  . SER   C  1  239 ? -12.950 10.755  2.819  1.00 41.01  ? 252 SER   C OG  1 
ATOM   7127 N  N   . ALA   C  1  240 ? -14.828 9.549   0.715  1.00 39.57  ? 253 ALA   C N   1 
ATOM   7128 C  CA  . ALA   C  1  240 ? -14.714 8.994   -0.626 1.00 43.26  ? 253 ALA   C CA  1 
ATOM   7129 C  C   . ALA   C  1  240 ? -13.251 8.769   -1.011 1.00 37.92  ? 253 ALA   C C   1 
ATOM   7130 O  O   . ALA   C  1  240 ? -13.000 8.122   -2.017 1.00 38.66  ? 253 ALA   C O   1 
ATOM   7131 C  CB  . ALA   C  1  240 ? -15.419 9.904   -1.625 1.00 42.90  ? 253 ALA   C CB  1 
ATOM   7132 N  N   . VAL   C  1  241 ? -12.311 9.321   -0.227 1.00 38.58  ? 254 VAL   C N   1 
ATOM   7133 C  CA  . VAL   C  1  241 ? -10.874 9.159   -0.423 1.00 38.56  ? 254 VAL   C CA  1 
ATOM   7134 C  C   . VAL   C  1  241 ? -10.219 8.887   0.925  1.00 40.75  ? 254 VAL   C C   1 
ATOM   7135 O  O   . VAL   C  1  241 ? -10.707 9.337   1.966  1.00 37.20  ? 254 VAL   C O   1 
ATOM   7136 C  CB  . VAL   C  1  241 ? -10.223 10.407  -1.049 1.00 46.52  ? 254 VAL   C CB  1 
ATOM   7137 C  CG1 . VAL   C  1  241 ? -10.685 10.635  -2.471 1.00 55.32  ? 254 VAL   C CG1 1 
ATOM   7138 C  CG2 . VAL   C  1  241 ? -10.481 11.664  -0.231 1.00 44.29  ? 254 VAL   C CG2 1 
ATOM   7139 N  N   . PRO   C  1  242 ? -9.076  8.174   0.969  1.00 37.70  ? 255 PRO   C N   1 
ATOM   7140 C  CA  . PRO   C  1  242 ? -8.321  8.062   2.208  1.00 35.40  ? 255 PRO   C CA  1 
ATOM   7141 C  C   . PRO   C  1  242 ? -8.029  9.473   2.689  1.00 35.25  ? 255 PRO   C C   1 
ATOM   7142 O  O   . PRO   C  1  242 ? -7.736  10.353  1.892  1.00 33.85  ? 255 PRO   C O   1 
ATOM   7143 C  CB  . PRO   C  1  242 ? -7.071  7.291   1.798  1.00 35.05  ? 255 PRO   C CB  1 
ATOM   7144 C  CG  . PRO   C  1  242 ? -7.553  6.456   0.639  1.00 35.72  ? 255 PRO   C CG  1 
ATOM   7145 C  CD  . PRO   C  1  242 ? -8.455  7.418   -0.119 1.00 36.06  ? 255 PRO   C CD  1 
ATOM   7146 N  N   . ALA   C  1  243 ? -8.163  9.703   3.998  1.00 38.45  ? 256 ALA   C N   1 
ATOM   7147 C  CA  . ALA   C  1  243 ? -7.930  11.043  4.500  1.00 36.45  ? 256 ALA   C CA  1 
ATOM   7148 C  C   . ALA   C  1  243 ? -7.425  10.987  5.930  1.00 35.49  ? 256 ALA   C C   1 
ATOM   7149 O  O   . ALA   C  1  243 ? -7.510  9.947   6.584  1.00 32.53  ? 256 ALA   C O   1 
ATOM   7150 C  CB  . ALA   C  1  243 ? -9.209  11.854  4.381  1.00 38.66  ? 256 ALA   C CB  1 
ATOM   7151 N  N   . SER   C  1  244 ? -6.935  12.144  6.382  1.00 33.82  ? 257 SER   C N   1 
ATOM   7152 C  CA  . SER   C  1  244 ? -6.499  12.296  7.751  1.00 34.80  ? 257 SER   C CA  1 
ATOM   7153 C  C   . SER   C  1  244 ? -6.558  13.769  8.133  1.00 32.77  ? 257 SER   C C   1 
ATOM   7154 O  O   . SER   C  1  244 ? -7.632  14.246  8.449  1.00 34.46  ? 257 SER   C O   1 
ATOM   7155 C  CB  . SER   C  1  244 ? -5.150  11.673  7.944  1.00 34.62  ? 257 SER   C CB  1 
ATOM   7156 O  OG  . SER   C  1  244 ? -4.206  12.215  7.035  1.00 35.58  ? 257 SER   C OG  1 
ATOM   7157 N  N   . ASN   C  1  245 ? -5.442  14.498  8.008  1.00 37.69  ? 258 ASN   C N   1 
ATOM   7158 C  CA  . ASN   C  1  245 ? -5.306  15.792  8.660  1.00 39.26  ? 258 ASN   C CA  1 
ATOM   7159 C  C   . ASN   C  1  245 ? -5.268  16.950  7.664  1.00 38.77  ? 258 ASN   C C   1 
ATOM   7160 O  O   . ASN   C  1  245 ? -4.708  18.007  7.955  1.00 36.76  ? 258 ASN   C O   1 
ATOM   7161 C  CB  . ASN   C  1  245 ? -4.075  15.832  9.557  1.00 42.18  ? 258 ASN   C CB  1 
ATOM   7162 C  CG  . ASN   C  1  245 ? -2.776  15.768  8.795  1.00 44.52  ? 258 ASN   C CG  1 
ATOM   7163 O  OD1 . ASN   C  1  245 ? -2.731  15.393  7.625  1.00 44.26  ? 258 ASN   C OD1 1 
ATOM   7164 N  ND2 . ASN   C  1  245 ? -1.702  16.168  9.443  1.00 51.32  ? 258 ASN   C ND2 1 
ATOM   7165 N  N   . GLU   C  1  246 ? -5.892  16.770  6.499  1.00 42.65  ? 259 GLU   C N   1 
ATOM   7166 C  CA  . GLU   C  1  246 ? -5.993  17.839  5.517  1.00 45.56  ? 259 GLU   C CA  1 
ATOM   7167 C  C   . GLU   C  1  246 ? -6.647  19.053  6.180  1.00 43.52  ? 259 GLU   C C   1 
ATOM   7168 O  O   . GLU   C  1  246 ? -7.717  18.941  6.771  1.00 42.70  ? 259 GLU   C O   1 
ATOM   7169 C  CB  . GLU   C  1  246 ? -6.787  17.428  4.269  1.00 49.87  ? 259 GLU   C CB  1 
ATOM   7170 C  CG  . GLU   C  1  246 ? -6.135  16.308  3.456  1.00 53.80  ? 259 GLU   C CG  1 
ATOM   7171 C  CD  . GLU   C  1  246 ? -6.262  14.881  4.004  1.00 57.18  ? 259 GLU   C CD  1 
ATOM   7172 O  OE1 . GLU   C  1  246 ? -6.830  14.662  5.110  1.00 52.27  ? 259 GLU   C OE1 1 
ATOM   7173 O  OE2 . GLU   C  1  246 ? -5.776  13.965  3.302  1.00 48.90  ? 259 GLU   C OE2 1 
ATOM   7174 N  N   . GLY   C  1  247 ? -5.982  20.208  6.092  1.00 45.99  ? 260 GLY   C N   1 
ATOM   7175 C  CA  . GLY   C  1  247 ? -6.520  21.465  6.588  1.00 49.41  ? 260 GLY   C CA  1 
ATOM   7176 C  C   . GLY   C  1  247 ? -5.955  21.848  7.956  1.00 48.19  ? 260 GLY   C C   1 
ATOM   7177 O  O   . GLY   C  1  247 ? -6.199  22.960  8.416  1.00 50.25  ? 260 GLY   C O   1 
ATOM   7178 N  N   . ALA   C  1  248 ? -5.190  20.951  8.594  1.00 44.46  ? 261 ALA   C N   1 
ATOM   7179 C  CA  . ALA   C  1  248 ? -4.668  21.214  9.929  1.00 48.33  ? 261 ALA   C CA  1 
ATOM   7180 C  C   . ALA   C  1  248 ? -3.743  22.432  9.925  1.00 48.63  ? 261 ALA   C C   1 
ATOM   7181 O  O   . ALA   C  1  248 ? -3.694  23.182  10.901 1.00 46.11  ? 261 ALA   C O   1 
ATOM   7182 C  CB  . ALA   C  1  248 ? -3.953  19.996  10.473 1.00 47.46  ? 261 ALA   C CB  1 
ATOM   7183 N  N   . ASP   C  1  249 ? -3.010  22.609  8.823  1.00 50.00  ? 262 ASP   C N   1 
ATOM   7184 C  CA  . ASP   C  1  249 ? -2.176  23.784  8.577  1.00 59.44  ? 262 ASP   C CA  1 
ATOM   7185 C  C   . ASP   C  1  249 ? -2.983  25.086  8.698  1.00 59.33  ? 262 ASP   C C   1 
ATOM   7186 O  O   . ASP   C  1  249 ? -2.532  26.043  9.322  1.00 56.82  ? 262 ASP   C O   1 
ATOM   7187 C  CB  . ASP   C  1  249 ? -1.460  23.676  7.231  1.00 69.96  ? 262 ASP   C CB  1 
ATOM   7188 C  CG  . ASP   C  1  249 ? -2.309  23.394  5.987  1.00 80.71  ? 262 ASP   C CG  1 
ATOM   7189 O  OD1 . ASP   C  1  249 ? -3.505  23.045  6.120  1.00 84.66  ? 262 ASP   C OD1 1 
ATOM   7190 O  OD2 . ASP   C  1  249 ? -1.773  23.537  4.869  1.00 86.14  ? 262 ASP   C OD2 1 
ATOM   7191 N  N   . GLN   C  1  250 ? -4.177  25.133  8.098  1.00 61.61  ? 263 GLN   C N   1 
ATOM   7192 C  CA  . GLN   C  1  250 ? -4.981  26.341  8.120  1.00 61.87  ? 263 GLN   C CA  1 
ATOM   7193 C  C   . GLN   C  1  250 ? -5.529  26.593  9.518  1.00 61.33  ? 263 GLN   C C   1 
ATOM   7194 O  O   . GLN   C  1  250 ? -5.776  27.739  9.882  1.00 58.32  ? 263 GLN   C O   1 
ATOM   7195 C  CB  . GLN   C  1  250 ? -6.144  26.245  7.140  1.00 64.28  ? 263 GLN   C CB  1 
ATOM   7196 C  CG  . GLN   C  1  250 ? -5.723  26.193  5.678  1.00 65.47  ? 263 GLN   C CG  1 
ATOM   7197 C  CD  . GLN   C  1  250 ? -6.929  26.003  4.785  1.00 71.27  ? 263 GLN   C CD  1 
ATOM   7198 O  OE1 . GLN   C  1  250 ? -7.826  26.856  4.753  1.00 71.47  ? 263 GLN   C OE1 1 
ATOM   7199 N  NE2 . GLN   C  1  250 ? -6.999  24.856  4.116  1.00 66.34  ? 263 GLN   C NE2 1 
ATOM   7200 N  N   . VAL   C  1  251 ? -5.718  25.524  10.300 1.00 58.56  ? 264 VAL   C N   1 
ATOM   7201 C  CA  . VAL   C  1  251 ? -6.210  25.677  11.656 1.00 58.62  ? 264 VAL   C CA  1 
ATOM   7202 C  C   . VAL   C  1  251 ? -5.153  26.405  12.478 1.00 56.10  ? 264 VAL   C C   1 
ATOM   7203 O  O   . VAL   C  1  251 ? -5.478  27.330  13.219 1.00 59.86  ? 264 VAL   C O   1 
ATOM   7204 C  CB  . VAL   C  1  251 ? -6.625  24.332  12.288 1.00 60.98  ? 264 VAL   C CB  1 
ATOM   7205 C  CG1 . VAL   C  1  251 ? -6.852  24.432  13.793 1.00 60.09  ? 264 VAL   C CG1 1 
ATOM   7206 C  CG2 . VAL   C  1  251 ? -7.889  23.784  11.637 1.00 59.05  ? 264 VAL   C CG2 1 
ATOM   7207 N  N   . LEU   C  1  252 ? -3.896  25.986  12.329 1.00 59.64  ? 265 LEU   C N   1 
ATOM   7208 C  CA  . LEU   C  1  252 ? -2.781  26.626  13.007 1.00 62.10  ? 265 LEU   C CA  1 
ATOM   7209 C  C   . LEU   C  1  252 ? -2.622  28.068  12.526 1.00 64.96  ? 265 LEU   C C   1 
ATOM   7210 O  O   . LEU   C  1  252 ? -2.417  28.959  13.339 1.00 67.95  ? 265 LEU   C O   1 
ATOM   7211 C  CB  . LEU   C  1  252 ? -1.491  25.837  12.794 1.00 56.27  ? 265 LEU   C CB  1 
ATOM   7212 C  CG  . LEU   C  1  252 ? -0.234  26.415  13.441 1.00 56.98  ? 265 LEU   C CG  1 
ATOM   7213 C  CD1 . LEU   C  1  252 ? -0.380  26.456  14.943 1.00 56.94  ? 265 LEU   C CD1 1 
ATOM   7214 C  CD2 . LEU   C  1  252 ? 0.986   25.596  13.064 1.00 57.73  ? 265 LEU   C CD2 1 
ATOM   7215 N  N   . ALA   C  1  253 ? -2.710  28.303  11.213 1.00 70.24  ? 266 ALA   C N   1 
ATOM   7216 C  CA  . ALA   C  1  253 ? -2.466  29.631  10.659 1.00 71.06  ? 266 ALA   C CA  1 
ATOM   7217 C  C   . ALA   C  1  253 ? -3.526  30.644  11.122 1.00 68.02  ? 266 ALA   C C   1 
ATOM   7218 O  O   . ALA   C  1  253 ? -3.228  31.821  11.267 1.00 64.74  ? 266 ALA   C O   1 
ATOM   7219 C  CB  . ALA   C  1  253 ? -2.382  29.558  9.153  1.00 67.52  ? 266 ALA   C CB  1 
ATOM   7220 N  N   . ALA   C  1  254 ? -4.756  30.195  11.382 1.00 72.33  ? 267 ALA   C N   1 
ATOM   7221 C  CA  . ALA   C  1  254 ? -5.804  31.079  11.875 1.00 76.69  ? 267 ALA   C CA  1 
ATOM   7222 C  C   . ALA   C  1  254 ? -5.436  31.698  13.227 1.00 80.45  ? 267 ALA   C C   1 
ATOM   7223 O  O   . ALA   C  1  254 ? -5.861  32.811  13.519 1.00 82.12  ? 267 ALA   C O   1 
ATOM   7224 C  CB  . ALA   C  1  254 ? -7.111  30.321  11.975 1.00 74.65  ? 267 ALA   C CB  1 
ATOM   7225 N  N   . HIS   C  1  255 ? -4.707  30.952  14.074 1.00 78.85  ? 268 HIS   C N   1 
ATOM   7226 C  CA  . HIS   C  1  255 ? -4.211  31.452  15.352 1.00 74.90  ? 268 HIS   C CA  1 
ATOM   7227 C  C   . HIS   C  1  255 ? -2.824  30.870  15.636 1.00 71.28  ? 268 HIS   C C   1 
ATOM   7228 O  O   . HIS   C  1  255 ? -2.685  29.879  16.353 1.00 70.28  ? 268 HIS   C O   1 
ATOM   7229 C  CB  . HIS   C  1  255 ? -5.201  31.169  16.491 1.00 81.05  ? 268 HIS   C CB  1 
ATOM   7230 C  CG  . HIS   C  1  255 ? -6.389  32.074  16.508 1.00 89.00  ? 268 HIS   C CG  1 
ATOM   7231 N  ND1 . HIS   C  1  255 ? -6.331  33.386  16.934 1.00 89.54  ? 268 HIS   C ND1 1 
ATOM   7232 C  CD2 . HIS   C  1  255 ? -7.658  31.856  16.127 1.00 91.30  ? 268 HIS   C CD2 1 
ATOM   7233 C  CE1 . HIS   C  1  255 ? -7.532  33.931  16.820 1.00 94.75  ? 268 HIS   C CE1 1 
ATOM   7234 N  NE2 . HIS   C  1  255 ? -8.358  33.018  16.336 1.00 93.60  ? 268 HIS   C NE2 1 
ATOM   7235 N  N   . PRO   C  1  256 ? -1.746  31.457  15.067 1.00 65.10  ? 269 PRO   C N   1 
ATOM   7236 C  CA  . PRO   C  1  256 ? -0.397  30.932  15.252 1.00 60.82  ? 269 PRO   C CA  1 
ATOM   7237 C  C   . PRO   C  1  256 ? -0.097  30.673  16.720 1.00 58.69  ? 269 PRO   C C   1 
ATOM   7238 O  O   . PRO   C  1  256 ? -0.433  31.476  17.587 1.00 59.47  ? 269 PRO   C O   1 
ATOM   7239 C  CB  . PRO   C  1  256 ? 0.510   32.003  14.643 1.00 61.87  ? 269 PRO   C CB  1 
ATOM   7240 C  CG  . PRO   C  1  256 ? -0.373  32.623  13.574 1.00 66.56  ? 269 PRO   C CG  1 
ATOM   7241 C  CD  . PRO   C  1  256 ? -1.777  32.626  14.177 1.00 64.56  ? 269 PRO   C CD  1 
ATOM   7242 N  N   . TRP   C  1  257 ? 0.523   29.520  16.966 1.00 59.33  ? 270 TRP   C N   1 
ATOM   7243 C  CA  . TRP   C  1  257 ? 0.799   29.066  18.312 1.00 61.09  ? 270 TRP   C CA  1 
ATOM   7244 C  C   . TRP   C  1  257 ? 2.066   28.218  18.324 1.00 59.44  ? 270 TRP   C C   1 
ATOM   7245 O  O   . TRP   C  1  257 ? 2.422   27.582  17.341 1.00 57.88  ? 270 TRP   C O   1 
ATOM   7246 C  CB  . TRP   C  1  257 ? -0.401  28.299  18.878 1.00 65.70  ? 270 TRP   C CB  1 
ATOM   7247 C  CG  . TRP   C  1  257 ? -0.299  28.142  20.368 1.00 68.90  ? 270 TRP   C CG  1 
ATOM   7248 C  CD1 . TRP   C  1  257 ? 0.066   27.026  21.059 1.00 68.22  ? 270 TRP   C CD1 1 
ATOM   7249 C  CD2 . TRP   C  1  257 ? -0.475  29.188  21.345 1.00 69.86  ? 270 TRP   C CD2 1 
ATOM   7250 N  NE1 . TRP   C  1  257 ? 0.083   27.289  22.399 1.00 66.19  ? 270 TRP   C NE1 1 
ATOM   7251 C  CE2 . TRP   C  1  257 ? -0.231  28.605  22.603 1.00 69.75  ? 270 TRP   C CE2 1 
ATOM   7252 C  CE3 . TRP   C  1  257 ? -0.820  30.543  21.273 1.00 69.53  ? 270 TRP   C CE3 1 
ATOM   7253 C  CZ2 . TRP   C  1  257 ? -0.327  29.335  23.781 1.00 79.57  ? 270 TRP   C CZ2 1 
ATOM   7254 C  CZ3 . TRP   C  1  257 ? -0.917  31.264  22.439 1.00 74.17  ? 270 TRP   C CZ3 1 
ATOM   7255 C  CH2 . TRP   C  1  257 ? -0.665  30.667  23.675 1.00 79.21  ? 270 TRP   C CH2 1 
ATOM   7256 N  N   . VAL   C  1  258 ? 2.733   28.218  19.472 1.00 57.74  ? 271 VAL   C N   1 
ATOM   7257 C  CA  . VAL   C  1  258 ? 4.058   27.649  19.604 1.00 61.14  ? 271 VAL   C CA  1 
ATOM   7258 C  C   . VAL   C  1  258 ? 4.014   26.602  20.713 1.00 61.16  ? 271 VAL   C C   1 
ATOM   7259 O  O   . VAL   C  1  258 ? 3.383   26.813  21.747 1.00 59.54  ? 271 VAL   C O   1 
ATOM   7260 C  CB  . VAL   C  1  258 ? 5.036   28.802  19.899 1.00 65.83  ? 271 VAL   C CB  1 
ATOM   7261 C  CG1 . VAL   C  1  258 ? 6.392   28.311  20.398 1.00 71.61  ? 271 VAL   C CG1 1 
ATOM   7262 C  CG2 . VAL   C  1  258 ? 5.198   29.723  18.694 1.00 63.74  ? 271 VAL   C CG2 1 
ATOM   7263 N  N   . PRO   C  1  259 ? 4.657   25.429  20.526 1.00 59.03  ? 272 PRO   C N   1 
ATOM   7264 C  CA  . PRO   C  1  259 ? 4.646   24.396  21.556 1.00 58.27  ? 272 PRO   C CA  1 
ATOM   7265 C  C   . PRO   C  1  259 ? 5.192   24.967  22.859 1.00 57.89  ? 272 PRO   C C   1 
ATOM   7266 O  O   . PRO   C  1  259 ? 6.010   25.875  22.839 1.00 57.76  ? 272 PRO   C O   1 
ATOM   7267 C  CB  . PRO   C  1  259 ? 5.524   23.267  20.990 1.00 58.31  ? 272 PRO   C CB  1 
ATOM   7268 C  CG  . PRO   C  1  259 ? 6.305   23.910  19.868 1.00 59.09  ? 272 PRO   C CG  1 
ATOM   7269 C  CD  . PRO   C  1  259 ? 5.417   25.031  19.335 1.00 57.95  ? 272 PRO   C CD  1 
ATOM   7270 N  N   . GLY   C  1  260 ? 4.724   24.420  23.980 1.00 57.17  ? 273 GLY   C N   1 
ATOM   7271 C  CA  . GLY   C  1  260 ? 5.140   24.885  25.288 1.00 57.33  ? 273 GLY   C CA  1 
ATOM   7272 C  C   . GLY   C  1  260 ? 4.215   24.352  26.368 1.00 60.17  ? 273 GLY   C C   1 
ATOM   7273 O  O   . GLY   C  1  260 ? 3.602   23.302  26.191 1.00 61.78  ? 273 GLY   C O   1 
ATOM   7274 N  N   . GLY   C  1  261 ? 4.119   25.103  27.470 1.00 61.50  ? 274 GLY   C N   1 
ATOM   7275 C  CA  . GLY   C  1  261 ? 3.330   24.692  28.620 1.00 65.79  ? 274 GLY   C CA  1 
ATOM   7276 C  C   . GLY   C  1  261 ? 3.353   25.746  29.726 1.00 65.56  ? 274 GLY   C C   1 
ATOM   7277 O  O   . GLY   C  1  261 ? 4.170   26.673  29.712 1.00 58.11  ? 274 GLY   C O   1 
ATOM   7278 N  N   . ASN   C  1  262 ? 2.425   25.589  30.675 1.00 61.73  ? 275 ASN   C N   1 
ATOM   7279 C  CA  . ASN   C  1  262 ? 2.449   26.340  31.916 1.00 61.87  ? 275 ASN   C CA  1 
ATOM   7280 C  C   . ASN   C  1  262 ? 3.642   25.870  32.744 1.00 65.35  ? 275 ASN   C C   1 
ATOM   7281 O  O   . ASN   C  1  262 ? 3.734   24.687  33.055 1.00 62.16  ? 275 ASN   C O   1 
ATOM   7282 C  CB  . ASN   C  1  262 ? 1.153   26.152  32.701 1.00 62.21  ? 275 ASN   C CB  1 
ATOM   7283 C  CG  . ASN   C  1  262 ? 0.066   27.119  32.290 1.00 60.19  ? 275 ASN   C CG  1 
ATOM   7284 O  OD1 . ASN   C  1  262 ? 0.360   28.175  31.712 1.00 52.56  ? 275 ASN   C OD1 1 
ATOM   7285 N  ND2 . ASN   C  1  262 ? -1.182  26.788  32.601 1.00 57.79  ? 275 ASN   C ND2 1 
ATOM   7286 N  N   . ALA   C  1  263 ? 4.530   26.802  33.115 1.00 67.87  ? 276 ALA   C N   1 
ATOM   7287 C  CA  . ALA   C  1  263 ? 5.699   26.478  33.924 1.00 75.99  ? 276 ALA   C CA  1 
ATOM   7288 C  C   . ALA   C  1  263 ? 5.397   26.642  35.416 1.00 78.67  ? 276 ALA   C C   1 
ATOM   7289 O  O   . ALA   C  1  263 ? 4.575   27.477  35.801 1.00 75.10  ? 276 ALA   C O   1 
ATOM   7290 C  CB  . ALA   C  1  263 ? 6.879   27.336  33.506 1.00 72.62  ? 276 ALA   C CB  1 
ATOM   7291 N  N   . ASP   C  1  264 ? 6.071   25.806  36.226 1.00 81.74  ? 277 ASP   C N   1 
ATOM   7292 C  CA  . ASP   C  1  264 ? 6.172   25.940  37.675 1.00 85.64  ? 277 ASP   C CA  1 
ATOM   7293 C  C   . ASP   C  1  264 ? 4.808   25.806  38.348 1.00 80.25  ? 277 ASP   C C   1 
ATOM   7294 O  O   . ASP   C  1  264 ? 4.545   26.485  39.331 1.00 78.84  ? 277 ASP   C O   1 
ATOM   7295 C  CB  . ASP   C  1  264 ? 6.851   27.240  38.089 1.00 95.78  ? 277 ASP   C CB  1 
ATOM   7296 C  CG  . ASP   C  1  264 ? 8.272   27.447  37.580 1.00 98.84  ? 277 ASP   C CG  1 
ATOM   7297 O  OD1 . ASP   C  1  264 ? 9.109   26.535  37.788 1.00 96.15  ? 277 ASP   C OD1 1 
ATOM   7298 O  OD2 . ASP   C  1  264 ? 8.536   28.524  36.992 1.00 91.43  ? 277 ASP   C OD2 1 
ATOM   7299 N  N   . ASN   C  1  265 ? 3.953   24.931  37.812 1.00 78.50  ? 278 ASN   C N   1 
ATOM   7300 C  CA  . ASN   C  1  265 ? 2.691   24.574  38.442 1.00 73.48  ? 278 ASN   C CA  1 
ATOM   7301 C  C   . ASN   C  1  265 ? 1.853   25.832  38.710 1.00 65.76  ? 278 ASN   C C   1 
ATOM   7302 O  O   . ASN   C  1  265 ? 1.230   25.953  39.757 1.00 59.78  ? 278 ASN   C O   1 
ATOM   7303 C  CB  . ASN   C  1  265 ? 2.947   23.711  39.677 1.00 78.87  ? 278 ASN   C CB  1 
ATOM   7304 C  CG  . ASN   C  1  265 ? 1.692   23.036  40.179 1.00 86.82  ? 278 ASN   C CG  1 
ATOM   7305 O  OD1 . ASN   C  1  265 ? 1.057   22.286  39.431 1.00 95.02  ? 278 ASN   C OD1 1 
ATOM   7306 N  ND2 . ASN   C  1  265 ? 1.316   23.266  41.429 1.00 87.14  ? 278 ASN   C ND2 1 
ATOM   7307 N  N   . GLN   C  1  266 ? 1.804   26.749  37.739 1.00 69.28  ? 279 GLN   C N   1 
ATOM   7308 C  CA  . GLN   C  1  266 ? 0.974   27.940  37.836 1.00 76.02  ? 279 GLN   C CA  1 
ATOM   7309 C  C   . GLN   C  1  266 ? 0.172   28.146  36.547 1.00 77.04  ? 279 GLN   C C   1 
ATOM   7310 O  O   . GLN   C  1  266 ? 0.660   27.902  35.444 1.00 78.76  ? 279 GLN   C O   1 
ATOM   7311 C  CB  . GLN   C  1  266 ? 1.815   29.203  38.016 1.00 83.69  ? 279 GLN   C CB  1 
ATOM   7312 C  CG  . GLN   C  1  266 ? 2.594   29.345  39.318 1.00 92.29  ? 279 GLN   C CG  1 
ATOM   7313 C  CD  . GLN   C  1  266 ? 3.647   30.440  39.209 1.00 99.53  ? 279 GLN   C CD  1 
ATOM   7314 O  OE1 . GLN   C  1  266 ? 3.397   31.516  38.650 1.00 89.17  ? 279 GLN   C OE1 1 
ATOM   7315 N  NE2 . GLN   C  1  266 ? 4.863   30.168  39.670 1.00 100.80 ? 279 GLN   C NE2 1 
ATOM   7316 N  N   . VAL   C  1  267 ? -1.054  28.653  36.682 1.00 69.88  ? 280 VAL   C N   1 
ATOM   7317 C  CA  . VAL   C  1  267 ? -1.855  29.006  35.524 1.00 65.67  ? 280 VAL   C CA  1 
ATOM   7318 C  C   . VAL   C  1  267 ? -1.367  30.336  34.954 1.00 60.97  ? 280 VAL   C C   1 
ATOM   7319 O  O   . VAL   C  1  267 ? -0.560  31.024  35.561 1.00 65.85  ? 280 VAL   C O   1 
ATOM   7320 C  CB  . VAL   C  1  267 ? -3.356  29.027  35.870 1.00 74.39  ? 280 VAL   C CB  1 
ATOM   7321 C  CG1 . VAL   C  1  267 ? -3.821  27.665  36.379 1.00 74.51  ? 280 VAL   C CG1 1 
ATOM   7322 C  CG2 . VAL   C  1  267 ? -3.725  30.124  36.869 1.00 77.18  ? 280 VAL   C CG2 1 
ATOM   7323 N  N   . ASN   C  1  268 ? -1.826  30.647  33.744 1.00 64.00  ? 281 ASN   C N   1 
ATOM   7324 C  CA  . ASN   C  1  268 ? -1.505  31.875  33.027 1.00 72.75  ? 281 ASN   C CA  1 
ATOM   7325 C  C   . ASN   C  1  268 ? 0.001   32.118  32.970 1.00 69.49  ? 281 ASN   C C   1 
ATOM   7326 O  O   . ASN   C  1  268 ? 0.437   33.261  33.029 1.00 71.52  ? 281 ASN   C O   1 
ATOM   7327 C  CB  . ASN   C  1  268 ? -2.280  33.063  33.582 1.00 70.87  ? 281 ASN   C CB  1 
ATOM   7328 C  CG  . ASN   C  1  268 ? -3.760  32.937  33.301 1.00 71.92  ? 281 ASN   C CG  1 
ATOM   7329 O  OD1 . ASN   C  1  268 ? -4.184  32.931  32.141 1.00 74.22  ? 281 ASN   C OD1 1 
ATOM   7330 N  ND2 . ASN   C  1  268 ? -4.566  32.821  34.343 1.00 74.34  ? 281 ASN   C ND2 1 
ATOM   7331 N  N   . ASN   C  1  269 ? 0.773   31.049  32.744 1.00 73.36  ? 282 ASN   C N   1 
ATOM   7332 C  CA  . ASN   C  1  269 ? 2.227   31.100  32.797 1.00 72.72  ? 282 ASN   C CA  1 
ATOM   7333 C  C   . ASN   C  1  269 ? 2.824   30.239  31.673 1.00 73.82  ? 282 ASN   C C   1 
ATOM   7334 O  O   . ASN   C  1  269 ? 3.674   29.374  31.905 1.00 67.08  ? 282 ASN   C O   1 
ATOM   7335 C  CB  . ASN   C  1  269 ? 2.690   30.733  34.206 1.00 70.34  ? 282 ASN   C CB  1 
ATOM   7336 C  CG  . ASN   C  1  269 ? 4.165   30.988  34.422 1.00 65.93  ? 282 ASN   C CG  1 
ATOM   7337 O  OD1 . ASN   C  1  269 ? 4.715   31.973  33.917 1.00 61.68  ? 282 ASN   C OD1 1 
ATOM   7338 N  ND2 . ASN   C  1  269 ? 4.834   30.093  35.131 1.00 66.98  ? 282 ASN   C ND2 1 
ATOM   7339 N  N   . TYR   C  1  270 ? 2.402   30.508  30.435 1.00 67.95  ? 283 TYR   C N   1 
ATOM   7340 C  CA  . TYR   C  1  270 ? 2.770   29.678  29.302 1.00 70.01  ? 283 TYR   C CA  1 
ATOM   7341 C  C   . TYR   C  1  270 ? 4.140   30.088  28.763 1.00 71.66  ? 283 TYR   C C   1 
ATOM   7342 O  O   . TYR   C  1  270 ? 4.301   31.210  28.294 1.00 71.60  ? 283 TYR   C O   1 
ATOM   7343 C  CB  . TYR   C  1  270 ? 1.720   29.777  28.189 1.00 71.33  ? 283 TYR   C CB  1 
ATOM   7344 C  CG  . TYR   C  1  270 ? 1.881   28.755  27.067 1.00 68.69  ? 283 TYR   C CG  1 
ATOM   7345 C  CD1 . TYR   C  1  270 ? 1.332   27.480  27.171 1.00 65.12  ? 283 TYR   C CD1 1 
ATOM   7346 C  CD2 . TYR   C  1  270 ? 2.575   29.062  25.901 1.00 65.97  ? 283 TYR   C CD2 1 
ATOM   7347 C  CE1 . TYR   C  1  270 ? 1.467   26.546  26.158 1.00 62.32  ? 283 TYR   C CE1 1 
ATOM   7348 C  CE2 . TYR   C  1  270 ? 2.719   28.137  24.881 1.00 66.40  ? 283 TYR   C CE2 1 
ATOM   7349 C  CZ  . TYR   C  1  270 ? 2.159   26.877  25.008 1.00 63.89  ? 283 TYR   C CZ  1 
ATOM   7350 O  OH  . TYR   C  1  270 ? 2.284   25.977  23.990 1.00 65.04  ? 283 TYR   C OH  1 
ATOM   7351 N  N   . VAL   C  1  271 ? 5.084   29.133  28.765 1.00 77.56  ? 284 VAL   C N   1 
ATOM   7352 C  CA  . VAL   C  1  271 ? 6.448   29.333  28.289 1.00 78.13  ? 284 VAL   C CA  1 
ATOM   7353 C  C   . VAL   C  1  271 ? 6.709   28.430  27.080 1.00 75.84  ? 284 VAL   C C   1 
ATOM   7354 O  O   . VAL   C  1  271 ? 6.449   27.230  27.150 1.00 68.42  ? 284 VAL   C O   1 
ATOM   7355 C  CB  . VAL   C  1  271 ? 7.461   29.021  29.411 1.00 78.17  ? 284 VAL   C CB  1 
ATOM   7356 C  CG1 . VAL   C  1  271 ? 8.900   29.125  28.922 1.00 78.18  ? 284 VAL   C CG1 1 
ATOM   7357 C  CG2 . VAL   C  1  271 ? 7.255   29.899  30.641 1.00 85.10  ? 284 VAL   C CG2 1 
ATOM   7358 N  N   . GLU   C  1  272 ? 7.325   28.989  26.028 1.00 70.26  ? 285 GLU   C N   1 
ATOM   7359 C  CA  . GLU   C  1  272 ? 7.647   28.254  24.813 1.00 74.84  ? 285 GLU   C CA  1 
ATOM   7360 C  C   . GLU   C  1  272 ? 8.726   27.202  25.086 1.00 76.41  ? 285 GLU   C C   1 
ATOM   7361 O  O   . GLU   C  1  272 ? 9.591   27.409  25.932 1.00 68.37  ? 285 GLU   C O   1 
ATOM   7362 C  CB  . GLU   C  1  272 ? 8.073   29.216  23.701 1.00 77.43  ? 285 GLU   C CB  1 
ATOM   7363 C  CG  . GLU   C  1  272 ? 7.065   30.344  23.472 1.00 89.17  ? 285 GLU   C CG  1 
ATOM   7364 C  CD  . GLU   C  1  272 ? 7.361   31.309  22.328 1.00 91.77  ? 285 GLU   C CD  1 
ATOM   7365 O  OE1 . GLU   C  1  272 ? 8.396   31.161  21.631 1.00 87.80  ? 285 GLU   C OE1 1 
ATOM   7366 O  OE2 . GLU   C  1  272 ? 6.510   32.206  22.123 1.00 81.64  ? 285 GLU   C OE2 1 
ATOM   7367 N  N   . ASP   C  1  273 ? 8.635   26.059  24.377 1.00 80.23  ? 286 ASP   C N   1 
ATOM   7368 C  CA  . ASP   C  1  273 ? 9.702   25.070  24.310 1.00 76.69  ? 286 ASP   C CA  1 
ATOM   7369 C  C   . ASP   C  1  273 ? 10.257  25.054  22.887 1.00 81.88  ? 286 ASP   C C   1 
ATOM   7370 O  O   . ASP   C  1  273 ? 9.625   24.525  21.977 1.00 79.54  ? 286 ASP   C O   1 
ATOM   7371 C  CB  . ASP   C  1  273 ? 9.237   23.682  24.726 1.00 71.63  ? 286 ASP   C CB  1 
ATOM   7372 C  CG  . ASP   C  1  273 ? 10.303  22.592  24.690 1.00 76.91  ? 286 ASP   C CG  1 
ATOM   7373 O  OD1 . ASP   C  1  273 ? 11.469  22.917  24.361 1.00 76.81  ? 286 ASP   C OD1 1 
ATOM   7374 O  OD2 . ASP   C  1  273 ? 9.962   21.421  24.988 1.00 80.69  ? 286 ASP   C OD2 1 
ATOM   7375 N  N   . PRO   C  1  274 ? 11.458  25.625  22.642 1.00 86.87  ? 287 PRO   C N   1 
ATOM   7376 C  CA  . PRO   C  1  274 ? 12.007  25.674  21.286 1.00 84.20  ? 287 PRO   C CA  1 
ATOM   7377 C  C   . PRO   C  1  274 ? 12.555  24.340  20.767 1.00 72.67  ? 287 PRO   C C   1 
ATOM   7378 O  O   . PRO   C  1  274 ? 12.801  24.211  19.572 1.00 63.76  ? 287 PRO   C O   1 
ATOM   7379 C  CB  . PRO   C  1  274 ? 13.093  26.760  21.427 1.00 86.20  ? 287 PRO   C CB  1 
ATOM   7380 C  CG  . PRO   C  1  274 ? 13.593  26.595  22.848 1.00 88.83  ? 287 PRO   C CG  1 
ATOM   7381 C  CD  . PRO   C  1  274 ? 12.353  26.226  23.647 1.00 90.21  ? 287 PRO   C CD  1 
ATOM   7382 N  N   . ASP   C  1  275 ? 12.741  23.353  21.666 1.00 68.51  ? 288 ASP   C N   1 
ATOM   7383 C  CA  . ASP   C  1  275 ? 13.229  22.022  21.310 1.00 69.98  ? 288 ASP   C CA  1 
ATOM   7384 C  C   . ASP   C  1  275 ? 12.105  21.059  20.891 1.00 62.90  ? 288 ASP   C C   1 
ATOM   7385 O  O   . ASP   C  1  275 ? 12.389  19.966  20.407 1.00 51.95  ? 288 ASP   C O   1 
ATOM   7386 C  CB  . ASP   C  1  275 ? 13.999  21.392  22.461 1.00 75.47  ? 288 ASP   C CB  1 
ATOM   7387 C  CG  . ASP   C  1  275 ? 15.282  22.107  22.871 1.00 81.08  ? 288 ASP   C CG  1 
ATOM   7388 O  OD1 . ASP   C  1  275 ? 15.684  23.070  22.180 1.00 74.63  ? 288 ASP   C OD1 1 
ATOM   7389 O  OD2 . ASP   C  1  275 ? 15.857  21.714  23.900 1.00 84.12  ? 288 ASP   C OD2 1 
ATOM   7390 N  N   . SER   C  1  276 ? 10.834  21.444  21.088 1.00 55.44  ? 289 SER   C N   1 
ATOM   7391 C  CA  . SER   C  1  276 ? 9.704   20.588  20.767 1.00 51.01  ? 289 SER   C CA  1 
ATOM   7392 C  C   . SER   C  1  276 ? 9.590   20.417  19.258 1.00 54.03  ? 289 SER   C C   1 
ATOM   7393 O  O   . SER   C  1  276 ? 9.936   21.310  18.485 1.00 55.23  ? 289 SER   C O   1 
ATOM   7394 C  CB  . SER   C  1  276 ? 8.414   21.141  21.326 1.00 56.37  ? 289 SER   C CB  1 
ATOM   7395 O  OG  . SER   C  1  276 ? 7.275   20.566  20.695 1.00 52.25  ? 289 SER   C OG  1 
ATOM   7396 N  N   . ALA   C  1  277 ? 9.079   19.256  18.843 1.00 54.58  ? 290 ALA   C N   1 
ATOM   7397 C  CA  . ALA   C  1  277 ? 8.586   19.103  17.486 1.00 49.64  ? 290 ALA   C CA  1 
ATOM   7398 C  C   . ALA   C  1  277 ? 7.576   20.201  17.183 1.00 45.26  ? 290 ALA   C C   1 
ATOM   7399 O  O   . ALA   C  1  277 ? 6.928   20.723  18.082 1.00 45.77  ? 290 ALA   C O   1 
ATOM   7400 C  CB  . ALA   C  1  277 ? 7.967   17.744  17.329 1.00 47.44  ? 290 ALA   C CB  1 
ATOM   7401 N  N   . ASP   C  1  278 ? 7.467   20.543  15.905 1.00 42.19  ? 291 ASP   C N   1 
ATOM   7402 C  CA  . ASP   C  1  278 ? 6.420   21.416  15.413 1.00 45.20  ? 291 ASP   C CA  1 
ATOM   7403 C  C   . ASP   C  1  278 ? 6.193   21.008  13.959 1.00 49.95  ? 291 ASP   C C   1 
ATOM   7404 O  O   . ASP   C  1  278 ? 6.751   19.993  13.536 1.00 54.61  ? 291 ASP   C O   1 
ATOM   7405 C  CB  . ASP   C  1  278 ? 6.754   22.877  15.675 1.00 47.55  ? 291 ASP   C CB  1 
ATOM   7406 C  CG  . ASP   C  1  278 ? 7.916   23.455  14.876 1.00 53.55  ? 291 ASP   C CG  1 
ATOM   7407 O  OD1 . ASP   C  1  278 ? 8.240   22.902  13.805 1.00 55.00  ? 291 ASP   C OD1 1 
ATOM   7408 O  OD2 . ASP   C  1  278 ? 8.503   24.462  15.335 1.00 63.98  ? 291 ASP   C OD2 1 
ATOM   7409 N  N   . PHE   C  1  279 ? 5.419   21.796  13.197 1.00 50.65  ? 292 PHE   C N   1 
ATOM   7410 C  CA  . PHE   C  1  279 ? 4.972   21.363  11.882 1.00 52.29  ? 292 PHE   C CA  1 
ATOM   7411 C  C   . PHE   C  1  279 ? 6.069   21.469  10.825 1.00 55.34  ? 292 PHE   C C   1 
ATOM   7412 O  O   . PHE   C  1  279 ? 5.945   20.824  9.785  1.00 60.16  ? 292 PHE   C O   1 
ATOM   7413 C  CB  . PHE   C  1  279 ? 3.675   22.063  11.462 1.00 49.89  ? 292 PHE   C CB  1 
ATOM   7414 C  CG  . PHE   C  1  279 ? 2.502   21.387  12.153 1.00 54.11  ? 292 PHE   C CG  1 
ATOM   7415 C  CD1 . PHE   C  1  279 ? 2.018   20.169  11.672 1.00 51.13  ? 292 PHE   C CD1 1 
ATOM   7416 C  CD2 . PHE   C  1  279 ? 1.968   21.908  13.334 1.00 52.19  ? 292 PHE   C CD2 1 
ATOM   7417 C  CE1 . PHE   C  1  279 ? 0.990   19.516  12.329 1.00 56.73  ? 292 PHE   C CE1 1 
ATOM   7418 C  CE2 . PHE   C  1  279 ? 0.937   21.259  13.988 1.00 52.53  ? 292 PHE   C CE2 1 
ATOM   7419 C  CZ  . PHE   C  1  279 ? 0.448   20.062  13.488 1.00 60.42  ? 292 PHE   C CZ  1 
ATOM   7420 N  N   . THR   C  1  280 ? 7.151   22.216  11.087 1.00 60.56  ? 293 THR   C N   1 
ATOM   7421 C  CA  . THR   C  1  280 ? 8.279   22.225  10.160 1.00 62.90  ? 293 THR   C CA  1 
ATOM   7422 C  C   . THR   C  1  280 ? 9.449   21.387  10.696 1.00 57.50  ? 293 THR   C C   1 
ATOM   7423 O  O   . THR   C  1  280 ? 10.508  21.358  10.074 1.00 55.26  ? 293 THR   C O   1 
ATOM   7424 C  CB  . THR   C  1  280 ? 8.679   23.672  9.853  1.00 67.25  ? 293 THR   C CB  1 
ATOM   7425 O  OG1 . THR   C  1  280 ? 9.026   24.304  11.083 1.00 68.16  ? 293 THR   C OG1 1 
ATOM   7426 C  CG2 . THR   C  1  280 ? 7.562   24.444  9.165  1.00 66.15  ? 293 THR   C CG2 1 
ATOM   7427 N  N   . HIS   C  1  281 ? 9.261   20.693  11.832 1.00 52.60  ? 294 HIS   C N   1 
ATOM   7428 C  CA  . HIS   C  1  281 ? 10.297  19.870  12.447 1.00 53.65  ? 294 HIS   C CA  1 
ATOM   7429 C  C   . HIS   C  1  281 ? 9.677   18.567  12.960 1.00 49.70  ? 294 HIS   C C   1 
ATOM   7430 O  O   . HIS   C  1  281 ? 9.826   18.219  14.124 1.00 53.16  ? 294 HIS   C O   1 
ATOM   7431 C  CB  . HIS   C  1  281 ? 10.995  20.619  13.592 1.00 56.26  ? 294 HIS   C CB  1 
ATOM   7432 C  CG  . HIS   C  1  281 ? 11.681  21.891  13.207 1.00 63.01  ? 294 HIS   C CG  1 
ATOM   7433 N  ND1 . HIS   C  1  281 ? 11.010  23.095  13.146 1.00 72.69  ? 294 HIS   C ND1 1 
ATOM   7434 C  CD2 . HIS   C  1  281 ? 12.962  22.155  12.885 1.00 64.26  ? 294 HIS   C CD2 1 
ATOM   7435 C  CE1 . HIS   C  1  281 ? 11.858  24.049  12.784 1.00 76.46  ? 294 HIS   C CE1 1 
ATOM   7436 N  NE2 . HIS   C  1  281 ? 13.050  23.495  12.618 1.00 70.19  ? 294 HIS   C NE2 1 
ATOM   7437 N  N   . LEU   C  1  282 ? 9.017   17.828  12.071 1.00 46.81  ? 295 LEU   C N   1 
ATOM   7438 C  CA  . LEU   C  1  282 ? 8.259   16.648  12.448 1.00 43.92  ? 295 LEU   C CA  1 
ATOM   7439 C  C   . LEU   C  1  282 ? 9.187   15.528  12.903 1.00 43.25  ? 295 LEU   C C   1 
ATOM   7440 O  O   . LEU   C  1  282 ? 8.787   14.727  13.735 1.00 44.80  ? 295 LEU   C O   1 
ATOM   7441 C  CB  . LEU   C  1  282 ? 7.367   16.169  11.305 1.00 42.65  ? 295 LEU   C CB  1 
ATOM   7442 C  CG  . LEU   C  1  282 ? 6.148   17.043  11.020 1.00 48.31  ? 295 LEU   C CG  1 
ATOM   7443 C  CD1 . LEU   C  1  282 ? 5.441   16.624  9.746  1.00 50.36  ? 295 LEU   C CD1 1 
ATOM   7444 C  CD2 . LEU   C  1  282 ? 5.216   16.977  12.201 1.00 49.33  ? 295 LEU   C CD2 1 
ATOM   7445 N  N   . CYS   C  1  283 ? 10.418  15.467  12.393 1.00 41.59  ? 296 CYS   C N   1 
ATOM   7446 C  CA  . CYS   C  1  283 ? 11.298  14.353  12.733 1.00 45.62  ? 296 CYS   C CA  1 
ATOM   7447 C  C   . CYS   C  1  283 ? 11.685  14.393  14.214 1.00 45.24  ? 296 CYS   C C   1 
ATOM   7448 O  O   . CYS   C  1  283 ? 12.018  13.352  14.791 1.00 42.53  ? 296 CYS   C O   1 
ATOM   7449 C  CB  . CYS   C  1  283 ? 12.511  14.251  11.806 1.00 51.65  ? 296 CYS   C CB  1 
ATOM   7450 S  SG  . CYS   C  1  283 ? 12.078  13.690  10.125 1.00 63.08  ? 296 CYS   C SG  1 
ATOM   7451 N  N   . ARG   C  1  284 ? 11.594  15.562  14.855 1.00 41.30  ? 297 ARG   C N   1 
ATOM   7452 C  CA  . ARG   C  1  284 ? 11.863  15.627  16.283 1.00 44.27  ? 297 ARG   C CA  1 
ATOM   7453 C  C   . ARG   C  1  284 ? 10.858  14.775  17.056 1.00 43.69  ? 297 ARG   C C   1 
ATOM   7454 O  O   . ARG   C  1  284 ? 11.190  14.217  18.102 1.00 37.88  ? 297 ARG   C O   1 
ATOM   7455 C  CB  . ARG   C  1  284 ? 11.721  17.044  16.843 1.00 51.84  ? 297 ARG   C CB  1 
ATOM   7456 C  CG  . ARG   C  1  284 ? 12.799  17.975  16.323 1.00 56.66  ? 297 ARG   C CG  1 
ATOM   7457 C  CD  . ARG   C  1  284 ? 12.642  19.333  16.974 1.00 58.67  ? 297 ARG   C CD  1 
ATOM   7458 N  NE  . ARG   C  1  284 ? 13.586  20.311  16.426 1.00 63.82  ? 297 ARG   C NE  1 
ATOM   7459 C  CZ  . ARG   C  1  284 ? 13.600  21.609  16.683 1.00 64.90  ? 297 ARG   C CZ  1 
ATOM   7460 N  NH1 . ARG   C  1  284 ? 12.733  22.128  17.538 1.00 62.19  ? 297 ARG   C NH1 1 
ATOM   7461 N  NH2 . ARG   C  1  284 ? 14.489  22.381  16.075 1.00 65.65  ? 297 ARG   C NH2 1 
ATOM   7462 N  N   . LEU   C  1  285 ? 9.621   14.706  16.540 1.00 40.18  ? 298 LEU   C N   1 
ATOM   7463 C  CA  . LEU   C  1  285 ? 8.598   13.900  17.168 1.00 37.28  ? 298 LEU   C CA  1 
ATOM   7464 C  C   . LEU   C  1  285 ? 9.047   12.439  17.129 1.00 35.42  ? 298 LEU   C C   1 
ATOM   7465 O  O   . LEU   C  1  285 ? 8.952   11.748  18.140 1.00 36.25  ? 298 LEU   C O   1 
ATOM   7466 C  CB  . LEU   C  1  285 ? 7.246   14.150  16.513 1.00 38.82  ? 298 LEU   C CB  1 
ATOM   7467 C  CG  . LEU   C  1  285 ? 6.044   13.436  17.137 1.00 43.28  ? 298 LEU   C CG  1 
ATOM   7468 C  CD1 . LEU   C  1  285 ? 4.765   14.119  16.702 1.00 46.04  ? 298 LEU   C CD1 1 
ATOM   7469 C  CD2 . LEU   C  1  285 ? 5.952   11.957  16.781 1.00 46.48  ? 298 LEU   C CD2 1 
ATOM   7470 N  N   . TYR   C  1  286 ? 9.576   11.990  15.989 1.00 34.23  ? 299 TYR   C N   1 
ATOM   7471 C  CA  . TYR   C  1  286 ? 10.058  10.627  15.836 1.00 34.17  ? 299 TYR   C CA  1 
ATOM   7472 C  C   . TYR   C  1  286 ? 11.155  10.344  16.864 1.00 36.93  ? 299 TYR   C C   1 
ATOM   7473 O  O   . TYR   C  1  286 ? 11.074  9.349   17.604 1.00 35.15  ? 299 TYR   C O   1 
ATOM   7474 C  CB  . TYR   C  1  286 ? 10.512  10.357  14.393 1.00 30.98  ? 299 TYR   C CB  1 
ATOM   7475 C  CG  . TYR   C  1  286 ? 11.186  9.002   14.218 1.00 28.03  ? 299 TYR   C CG  1 
ATOM   7476 C  CD1 . TYR   C  1  286 ? 10.482  7.823   14.383 1.00 27.65  ? 299 TYR   C CD1 1 
ATOM   7477 C  CD2 . TYR   C  1  286 ? 12.531  8.906   13.909 1.00 27.75  ? 299 TYR   C CD2 1 
ATOM   7478 C  CE1 . TYR   C  1  286 ? 11.084  6.586   14.233 1.00 28.21  ? 299 TYR   C CE1 1 
ATOM   7479 C  CE2 . TYR   C  1  286 ? 13.148  7.683   13.756 1.00 27.68  ? 299 TYR   C CE2 1 
ATOM   7480 C  CZ  . TYR   C  1  286 ? 12.430  6.517   13.949 1.00 30.26  ? 299 TYR   C CZ  1 
ATOM   7481 O  OH  . TYR   C  1  286 ? 13.044  5.301   13.812 1.00 29.66  ? 299 TYR   C OH  1 
ATOM   7482 N  N   . GLU   C  1  287 ? 12.150  11.234  16.934 1.00 39.00  ? 300 GLU   C N   1 
ATOM   7483 C  CA  . GLU   C  1  287 ? 13.254  11.078  17.880 1.00 45.58  ? 300 GLU   C CA  1 
ATOM   7484 C  C   . GLU   C  1  287 ? 12.748  11.091  19.326 1.00 38.41  ? 300 GLU   C C   1 
ATOM   7485 O  O   . GLU   C  1  287 ? 13.132  10.243  20.117 1.00 37.47  ? 300 GLU   C O   1 
ATOM   7486 C  CB  . GLU   C  1  287 ? 14.338  12.138  17.674 1.00 53.63  ? 300 GLU   C CB  1 
ATOM   7487 C  CG  . GLU   C  1  287 ? 15.084  12.018  16.345 1.00 70.85  ? 300 GLU   C CG  1 
ATOM   7488 C  CD  . GLU   C  1  287 ? 15.714  13.296  15.774 1.00 83.94  ? 300 GLU   C CD  1 
ATOM   7489 O  OE1 . GLU   C  1  287 ? 15.434  14.438  16.210 1.00 85.84  ? 300 GLU   C OE1 1 
ATOM   7490 O  OE2 . GLU   C  1  287 ? 16.517  13.132  14.841 1.00 90.66  ? 300 GLU   C OE2 1 
ATOM   7491 N  N   . PHE   C  1  288 ? 11.853  12.025  19.648 1.00 34.83  ? 301 PHE   C N   1 
ATOM   7492 C  CA  . PHE   C  1  288 ? 11.312  12.142  20.994 1.00 38.38  ? 301 PHE   C CA  1 
ATOM   7493 C  C   . PHE   C  1  288 ? 10.676  10.816  21.433 1.00 36.46  ? 301 PHE   C C   1 
ATOM   7494 O  O   . PHE   C  1  288 ? 10.904  10.319  22.531 1.00 35.03  ? 301 PHE   C O   1 
ATOM   7495 C  CB  . PHE   C  1  288 ? 10.307  13.300  21.047 1.00 42.60  ? 301 PHE   C CB  1 
ATOM   7496 C  CG  . PHE   C  1  288 ? 9.778   13.512  22.456 1.00 44.50  ? 301 PHE   C CG  1 
ATOM   7497 C  CD1 . PHE   C  1  288 ? 10.479  14.299  23.365 1.00 50.11  ? 301 PHE   C CD1 1 
ATOM   7498 C  CD2 . PHE   C  1  288 ? 8.623   12.879  22.884 1.00 44.55  ? 301 PHE   C CD2 1 
ATOM   7499 C  CE1 . PHE   C  1  288 ? 10.020  14.462  24.664 1.00 50.61  ? 301 PHE   C CE1 1 
ATOM   7500 C  CE2 . PHE   C  1  288 ? 8.173   13.033  24.191 1.00 48.29  ? 301 PHE   C CE2 1 
ATOM   7501 C  CZ  . PHE   C  1  288 ? 8.870   13.822  25.077 1.00 46.63  ? 301 PHE   C CZ  1 
ATOM   7502 N  N   . VAL   C  1  289 ? 9.885   10.226  20.544 1.00 32.38  ? 302 VAL   C N   1 
ATOM   7503 C  CA  . VAL   C  1  289 ? 9.115   9.049   20.881 1.00 30.21  ? 302 VAL   C CA  1 
ATOM   7504 C  C   . VAL   C  1  289 ? 10.039  7.845   21.020 1.00 29.37  ? 302 VAL   C C   1 
ATOM   7505 O  O   . VAL   C  1  289 ? 9.796   6.998   21.879 1.00 31.44  ? 302 VAL   C O   1 
ATOM   7506 C  CB  . VAL   C  1  289 ? 8.009   8.770   19.855 1.00 31.58  ? 302 VAL   C CB  1 
ATOM   7507 C  CG1 . VAL   C  1  289 ? 7.393   7.394   20.046 1.00 33.75  ? 302 VAL   C CG1 1 
ATOM   7508 C  CG2 . VAL   C  1  289 ? 6.925   9.822   19.919 1.00 34.15  ? 302 VAL   C CG2 1 
ATOM   7509 N  N   . VAL   C  1  290 ? 11.058  7.739   20.165 1.00 28.18  ? 303 VAL   C N   1 
ATOM   7510 C  CA  . VAL   C  1  290 ? 11.977  6.619   20.280 1.00 33.26  ? 303 VAL   C CA  1 
ATOM   7511 C  C   . VAL   C  1  290 ? 12.668  6.705   21.641 1.00 34.82  ? 303 VAL   C C   1 
ATOM   7512 O  O   . VAL   C  1  290 ? 12.816  5.685   22.323 1.00 31.22  ? 303 VAL   C O   1 
ATOM   7513 C  CB  . VAL   C  1  290 ? 12.985  6.575   19.117 1.00 36.14  ? 303 VAL   C CB  1 
ATOM   7514 C  CG1 . VAL   C  1  290 ? 14.132  5.614   19.389 1.00 34.43  ? 303 VAL   C CG1 1 
ATOM   7515 C  CG2 . VAL   C  1  290 ? 12.270  6.205   17.816 1.00 39.35  ? 303 VAL   C CG2 1 
ATOM   7516 N  N   . GLY   C  1  291 ? 13.024  7.942   22.040 1.00 33.56  ? 304 GLY   C N   1 
ATOM   7517 C  CA  . GLY   C  1  291 ? 13.549  8.210   23.373 1.00 36.35  ? 304 GLY   C CA  1 
ATOM   7518 C  C   . GLY   C  1  291 ? 12.589  7.724   24.457 1.00 37.40  ? 304 GLY   C C   1 
ATOM   7519 O  O   . GLY   C  1  291 ? 12.989  7.047   25.404 1.00 36.48  ? 304 GLY   C O   1 
ATOM   7520 N  N   . SER   C  1  292 ? 11.298  8.052   24.293 1.00 35.43  ? 305 SER   C N   1 
ATOM   7521 C  CA  . SER   C  1  292 ? 10.308  7.661   25.280 1.00 34.50  ? 305 SER   C CA  1 
ATOM   7522 C  C   . SER   C  1  292 ? 10.230  6.140   25.385 1.00 33.03  ? 305 SER   C C   1 
ATOM   7523 O  O   . SER   C  1  292 ? 10.074  5.594   26.481 1.00 36.84  ? 305 SER   C O   1 
ATOM   7524 C  CB  . SER   C  1  292 ? 8.972   8.281   24.992 1.00 31.97  ? 305 SER   C CB  1 
ATOM   7525 O  OG  . SER   C  1  292 ? 9.117   9.694   24.840 1.00 38.61  ? 305 SER   C OG  1 
ATOM   7526 N  N   . VAL   C  1  293 ? 10.353  5.459   24.250 1.00 30.86  ? 306 VAL   C N   1 
ATOM   7527 C  CA  . VAL   C  1  293 ? 10.263  4.013   24.249 1.00 31.26  ? 306 VAL   C CA  1 
ATOM   7528 C  C   . VAL   C  1  293 ? 11.434  3.411   25.026 1.00 31.89  ? 306 VAL   C C   1 
ATOM   7529 O  O   . VAL   C  1  293 ? 11.254  2.422   25.764 1.00 28.90  ? 306 VAL   C O   1 
ATOM   7530 C  CB  . VAL   C  1  293 ? 10.175  3.454   22.823 1.00 30.60  ? 306 VAL   C CB  1 
ATOM   7531 C  CG1 . VAL   C  1  293 ? 10.335  1.931   22.805 1.00 29.62  ? 306 VAL   C CG1 1 
ATOM   7532 C  CG2 . VAL   C  1  293 ? 8.865   3.891   22.178 1.00 31.05  ? 306 VAL   C CG2 1 
ATOM   7533 N  N   . GLN   C  1  294 ? 12.619  4.011   24.851 1.00 33.74  ? 307 GLN   C N   1 
ATOM   7534 C  CA  . GLN   C  1  294 ? 13.812  3.553   25.549 1.00 40.38  ? 307 GLN   C CA  1 
ATOM   7535 C  C   . GLN   C  1  294 ? 13.645  3.715   27.064 1.00 38.92  ? 307 GLN   C C   1 
ATOM   7536 O  O   . GLN   C  1  294 ? 14.086  2.848   27.818 1.00 39.69  ? 307 GLN   C O   1 
ATOM   7537 C  CB  . GLN   C  1  294 ? 15.075  4.273   25.093 1.00 43.46  ? 307 GLN   C CB  1 
ATOM   7538 C  CG  . GLN   C  1  294 ? 15.455  3.978   23.649 1.00 51.27  ? 307 GLN   C CG  1 
ATOM   7539 C  CD  . GLN   C  1  294 ? 16.623  4.818   23.156 1.00 48.86  ? 307 GLN   C CD  1 
ATOM   7540 O  OE1 . GLN   C  1  294 ? 16.477  5.968   22.721 1.00 48.99  ? 307 GLN   C OE1 1 
ATOM   7541 N  NE2 . GLN   C  1  294 ? 17.809  4.242   23.201 1.00 45.22  ? 307 GLN   C NE2 1 
ATOM   7542 N  N   . GLU   C  1  295 ? 12.994  4.797   27.506 1.00 38.30  ? 308 GLU   C N   1 
ATOM   7543 C  CA  . GLU   C  1  295 ? 12.730  4.995   28.926 1.00 40.59  ? 308 GLU   C CA  1 
ATOM   7544 C  C   . GLU   C  1  295 ? 11.785  3.916   29.440 1.00 37.16  ? 308 GLU   C C   1 
ATOM   7545 O  O   . GLU   C  1  295 ? 11.983  3.437   30.557 1.00 39.79  ? 308 GLU   C O   1 
ATOM   7546 C  CB  . GLU   C  1  295 ? 12.149  6.362   29.282 1.00 46.40  ? 308 GLU   C CB  1 
ATOM   7547 C  CG  . GLU   C  1  295 ? 13.105  7.530   29.038 1.00 56.77  ? 308 GLU   C CG  1 
ATOM   7548 C  CD  . GLU   C  1  295 ? 12.452  8.921   29.104 1.00 74.46  ? 308 GLU   C CD  1 
ATOM   7549 O  OE1 . GLU   C  1  295 ? 11.209  9.055   29.295 1.00 79.10  ? 308 GLU   C OE1 1 
ATOM   7550 O  OE2 . GLU   C  1  295 ? 13.199  9.913   28.939 1.00 73.14  ? 308 GLU   C OE2 1 
ATOM   7551 N  N   . LEU   C  1  296 ? 10.812  3.483   28.614 1.00 31.78  ? 309 LEU   C N   1 
ATOM   7552 C  CA  . LEU   C  1  296 ? 9.884   2.440   29.022 1.00 27.88  ? 309 LEU   C CA  1 
ATOM   7553 C  C   . LEU   C  1  296 ? 10.577  1.078   29.047 1.00 27.27  ? 309 LEU   C C   1 
ATOM   7554 O  O   . LEU   C  1  296 ? 10.220  0.217   29.860 1.00 32.52  ? 309 LEU   C O   1 
ATOM   7555 C  CB  . LEU   C  1  296 ? 8.629   2.371   28.160 1.00 30.73  ? 309 LEU   C CB  1 
ATOM   7556 C  CG  . LEU   C  1  296 ? 7.708   3.603   28.183 1.00 36.41  ? 309 LEU   C CG  1 
ATOM   7557 C  CD1 . LEU   C  1  296 ? 6.627   3.411   27.162 1.00 37.50  ? 309 LEU   C CD1 1 
ATOM   7558 C  CD2 . LEU   C  1  296 ? 7.035   3.940   29.514 1.00 37.89  ? 309 LEU   C CD2 1 
ATOM   7559 N  N   . TYR   C  1  297 ? 11.492  0.857   28.102 1.00 29.04  ? 310 TYR   C N   1 
ATOM   7560 C  CA  . TYR   C  1  297 ? 12.112  -0.448  27.879 1.00 32.09  ? 310 TYR   C CA  1 
ATOM   7561 C  C   . TYR   C  1  297 ? 13.637  -0.275  27.832 1.00 33.37  ? 310 TYR   C C   1 
ATOM   7562 O  O   . TYR   C  1  297 ? 14.252  -0.250  26.766 1.00 29.65  ? 310 TYR   C O   1 
ATOM   7563 C  CB  . TYR   C  1  297 ? 11.583  -1.094  26.598 1.00 31.20  ? 310 TYR   C CB  1 
ATOM   7564 C  CG  . TYR   C  1  297 ? 10.096  -1.398  26.626 1.00 32.66  ? 310 TYR   C CG  1 
ATOM   7565 C  CD1 . TYR   C  1  297 ? 9.614   -2.540  27.264 1.00 33.39  ? 310 TYR   C CD1 1 
ATOM   7566 C  CD2 . TYR   C  1  297 ? 9.179   -0.558  26.014 1.00 30.47  ? 310 TYR   C CD2 1 
ATOM   7567 C  CE1 . TYR   C  1  297 ? 8.267   -2.846  27.290 1.00 32.95  ? 310 TYR   C CE1 1 
ATOM   7568 C  CE2 . TYR   C  1  297 ? 7.821   -0.855  26.022 1.00 33.05  ? 310 TYR   C CE2 1 
ATOM   7569 C  CZ  . TYR   C  1  297 ? 7.360   -1.992  26.672 1.00 33.91  ? 310 TYR   C CZ  1 
ATOM   7570 O  OH  . TYR   C  1  297 ? 6.013   -2.262  26.700 1.00 28.39  ? 310 TYR   C OH  1 
ATOM   7571 N  N   . PRO   C  1  298 ? 14.292  -0.051  28.995 1.00 36.39  ? 311 PRO   C N   1 
ATOM   7572 C  CA  . PRO   C  1  298 ? 15.699  0.347   29.029 1.00 31.91  ? 311 PRO   C CA  1 
ATOM   7573 C  C   . PRO   C  1  298 ? 16.680  -0.709  28.564 1.00 29.41  ? 311 PRO   C C   1 
ATOM   7574 O  O   . PRO   C  1  298 ? 17.719  -0.328  28.036 1.00 28.06  ? 311 PRO   C O   1 
ATOM   7575 C  CB  . PRO   C  1  298 ? 15.983  0.763   30.480 1.00 37.57  ? 311 PRO   C CB  1 
ATOM   7576 C  CG  . PRO   C  1  298 ? 14.644  0.764   31.160 1.00 39.00  ? 311 PRO   C CG  1 
ATOM   7577 C  CD  . PRO   C  1  298 ? 13.689  -0.072  30.329 1.00 37.33  ? 311 PRO   C CD  1 
ATOM   7578 N  N   . ASN   C  1  299 ? 16.388  -2.001  28.777 1.00 30.62  ? 312 ASN   C N   1 
ATOM   7579 C  CA  . ASN   C  1  299 ? 17.338  -3.052  28.437 1.00 30.46  ? 312 ASN   C CA  1 
ATOM   7580 C  C   . ASN   C  1  299 ? 16.641  -4.376  28.138 1.00 32.54  ? 312 ASN   C C   1 
ATOM   7581 O  O   . ASN   C  1  299 ? 16.897  -5.380  28.791 1.00 32.49  ? 312 ASN   C O   1 
ATOM   7582 C  CB  . ASN   C  1  299 ? 18.333  -3.264  29.574 1.00 35.26  ? 312 ASN   C CB  1 
ATOM   7583 C  CG  . ASN   C  1  299 ? 19.479  -4.178  29.202 1.00 36.42  ? 312 ASN   C CG  1 
ATOM   7584 O  OD1 . ASN   C  1  299 ? 19.775  -5.109  29.949 1.00 34.31  ? 312 ASN   C OD1 1 
ATOM   7585 N  ND2 . ASN   C  1  299 ? 20.142  -3.935  28.079 1.00 37.17  ? 312 ASN   C ND2 1 
ATOM   7586 N  N   . PRO   C  1  300 ? 15.758  -4.458  27.128 1.00 33.41  ? 313 PRO   C N   1 
ATOM   7587 C  CA  . PRO   C  1  300 ? 15.015  -5.693  26.868 1.00 33.07  ? 313 PRO   C CA  1 
ATOM   7588 C  C   . PRO   C  1  300 ? 15.852  -6.772  26.198 1.00 32.43  ? 313 PRO   C C   1 
ATOM   7589 O  O   . PRO   C  1  300 ? 16.776  -6.447  25.466 1.00 34.50  ? 313 PRO   C O   1 
ATOM   7590 C  CB  . PRO   C  1  300 ? 13.914  -5.195  25.916 1.00 34.92  ? 313 PRO   C CB  1 
ATOM   7591 C  CG  . PRO   C  1  300 ? 14.617  -4.104  25.136 1.00 32.83  ? 313 PRO   C CG  1 
ATOM   7592 C  CD  . PRO   C  1  300 ? 15.410  -3.369  26.208 1.00 33.50  ? 313 PRO   C CD  1 
ATOM   7593 N  N   . THR   C  1  301 ? 15.449  -8.029  26.390 1.00 33.23  ? 314 THR   C N   1 
ATOM   7594 C  CA  . THR   C  1  301 ? 15.987  -9.165  25.660 1.00 37.42  ? 314 THR   C CA  1 
ATOM   7595 C  C   . THR   C  1  301 ? 14.830  -10.080 25.249 1.00 34.78  ? 314 THR   C C   1 
ATOM   7596 O  O   . THR   C  1  301 ? 13.676  -9.848  25.614 1.00 34.50  ? 314 THR   C O   1 
ATOM   7597 C  CB  . THR   C  1  301 ? 17.024  -9.919  26.510 1.00 45.44  ? 314 THR   C CB  1 
ATOM   7598 O  OG1 . THR   C  1  301 ? 16.395  -10.438 27.676 1.00 43.98  ? 314 THR   C OG1 1 
ATOM   7599 C  CG2 . THR   C  1  301 ? 18.197  -9.056  26.947 1.00 48.38  ? 314 THR   C CG2 1 
ATOM   7600 N  N   . GLY   C  1  302 ? 15.154  -11.156 24.515 1.00 37.86  ? 315 GLY   C N   1 
ATOM   7601 C  CA  . GLY   C  1  302 ? 14.189  -12.195 24.198 1.00 37.80  ? 315 GLY   C CA  1 
ATOM   7602 C  C   . GLY   C  1  302 ? 13.089  -11.675 23.261 1.00 39.84  ? 315 GLY   C C   1 
ATOM   7603 O  O   . GLY   C  1  302 ? 13.323  -10.815 22.413 1.00 39.34  ? 315 GLY   C O   1 
ATOM   7604 N  N   . ILE   C  1  303 ? 11.882  -12.202 23.456 1.00 39.84  ? 316 ILE   C N   1 
ATOM   7605 C  CA  . ILE   C  1  303 ? 10.736  -11.907 22.612 1.00 44.56  ? 316 ILE   C CA  1 
ATOM   7606 C  C   . ILE   C  1  303 ? 10.379  -10.424 22.723 1.00 37.54  ? 316 ILE   C C   1 
ATOM   7607 O  O   . ILE   C  1  303 ? 10.006  -9.791  21.735 1.00 34.00  ? 316 ILE   C O   1 
ATOM   7608 C  CB  . ILE   C  1  303 ? 9.556   -12.841 22.951 1.00 51.59  ? 316 ILE   C CB  1 
ATOM   7609 C  CG1 . ILE   C  1  303 ? 9.987   -14.318 22.729 1.00 72.55  ? 316 ILE   C CG1 1 
ATOM   7610 C  CG2 . ILE   C  1  303 ? 8.312   -12.484 22.132 1.00 51.91  ? 316 ILE   C CG2 1 
ATOM   7611 C  CD1 . ILE   C  1  303 ? 8.966   -15.377 23.113 1.00 85.07  ? 316 ILE   C CD1 1 
ATOM   7612 N  N   . LEU   C  1  304 ? 10.510  -9.857  23.923 1.00 33.96  ? 317 LEU   C N   1 
ATOM   7613 C  CA  . LEU   C  1  304 ? 10.180  -8.459  24.122 1.00 32.60  ? 317 LEU   C CA  1 
ATOM   7614 C  C   . LEU   C  1  304 ? 11.083  -7.594  23.239 1.00 32.73  ? 317 LEU   C C   1 
ATOM   7615 O  O   . LEU   C  1  304 ? 10.605  -6.686  22.561 1.00 32.87  ? 317 LEU   C O   1 
ATOM   7616 C  CB  . LEU   C  1  304 ? 10.274  -8.108  25.604 1.00 34.33  ? 317 LEU   C CB  1 
ATOM   7617 C  CG  . LEU   C  1  304 ? 10.115  -6.624  25.950 1.00 37.19  ? 317 LEU   C CG  1 
ATOM   7618 C  CD1 . LEU   C  1  304 ? 8.785   -6.079  25.471 1.00 38.58  ? 317 LEU   C CD1 1 
ATOM   7619 C  CD2 . LEU   C  1  304 ? 10.262  -6.438  27.467 1.00 38.74  ? 317 LEU   C CD2 1 
ATOM   7620 N  N   . ARG   C  1  305 ? 12.390  -7.887  23.221 1.00 31.49  ? 318 ARG   C N   1 
ATOM   7621 C  CA  A ARG   C  1  305 ? 13.307  -7.123  22.386 0.50 31.15  ? 318 ARG   C CA  1 
ATOM   7622 C  CA  B ARG   C  1  305 ? 13.318  -7.137  22.383 0.50 35.37  ? 318 ARG   C CA  1 
ATOM   7623 C  C   . ARG   C  1  305 ? 12.936  -7.292  20.913 1.00 30.36  ? 318 ARG   C C   1 
ATOM   7624 O  O   . ARG   C  1  305 ? 12.942  -6.337  20.165 1.00 29.42  ? 318 ARG   C O   1 
ATOM   7625 C  CB  A ARG   C  1  305 ? 14.763  -7.549  22.597 0.50 25.74  ? 318 ARG   C CB  1 
ATOM   7626 C  CB  B ARG   C  1  305 ? 14.772  -7.601  22.526 0.50 35.38  ? 318 ARG   C CB  1 
ATOM   7627 C  CG  A ARG   C  1  305 ? 15.796  -6.896  21.695 0.50 24.20  ? 318 ARG   C CG  1 
ATOM   7628 C  CG  B ARG   C  1  305 ? 15.739  -6.942  21.548 0.50 40.23  ? 318 ARG   C CG  1 
ATOM   7629 C  CD  A ARG   C  1  305 ? 17.160  -7.605  21.766 0.50 21.60  ? 318 ARG   C CD  1 
ATOM   7630 C  CD  B ARG   C  1  305 ? 17.109  -7.625  21.426 0.50 44.28  ? 318 ARG   C CD  1 
ATOM   7631 N  NE  A ARG   C  1  305 ? 18.078  -7.149  20.713 0.50 19.46  ? 318 ARG   C NE  1 
ATOM   7632 N  NE  B ARG   C  1  305 ? 18.170  -6.644  21.141 0.50 48.03  ? 318 ARG   C NE  1 
ATOM   7633 C  CZ  A ARG   C  1  305 ? 18.213  -7.708  19.541 0.50 15.23  ? 318 ARG   C CZ  1 
ATOM   7634 C  CZ  B ARG   C  1  305 ? 18.621  -5.761  22.052 0.50 42.71  ? 318 ARG   C CZ  1 
ATOM   7635 N  NH1 A ARG   C  1  305 ? 17.703  -8.886  19.356 0.50 13.87  ? 318 ARG   C NH1 1 
ATOM   7636 N  NH1 B ARG   C  1  305 ? 18.311  -5.912  23.331 0.50 55.50  ? 318 ARG   C NH1 1 
ATOM   7637 N  NH2 A ARG   C  1  305 ? 18.867  -7.086  18.598 0.50 14.69  ? 318 ARG   C NH2 1 
ATOM   7638 N  NH2 B ARG   C  1  305 ? 19.388  -4.750  21.729 0.50 28.21  ? 318 ARG   C NH2 1 
ATOM   7639 N  N   . ARG   C  1  306 ? 12.656  -8.525  20.507 1.00 31.78  ? 319 ARG   C N   1 
ATOM   7640 C  CA  . ARG   C  1  306 ? 12.351  -8.823  19.111 1.00 37.15  ? 319 ARG   C CA  1 
ATOM   7641 C  C   . ARG   C  1  306 ? 11.095  -8.058  18.692 1.00 34.25  ? 319 ARG   C C   1 
ATOM   7642 O  O   . ARG   C  1  306 ? 11.080  -7.450  17.629 1.00 29.87  ? 319 ARG   C O   1 
ATOM   7643 C  CB  . ARG   C  1  306 ? 12.198  -10.340 18.942 1.00 44.14  ? 319 ARG   C CB  1 
ATOM   7644 C  CG  . ARG   C  1  306 ? 11.918  -10.865 17.542 1.00 51.52  ? 319 ARG   C CG  1 
ATOM   7645 C  CD  . ARG   C  1  306 ? 11.276  -12.264 17.545 1.00 58.70  ? 319 ARG   C CD  1 
ATOM   7646 N  NE  . ARG   C  1  306 ? 9.846   -12.204 17.895 1.00 68.49  ? 319 ARG   C NE  1 
ATOM   7647 C  CZ  . ARG   C  1  306 ? 9.067   -13.237 18.217 1.00 73.80  ? 319 ARG   C CZ  1 
ATOM   7648 N  NH1 . ARG   C  1  306 ? 9.545   -14.467 18.274 1.00 78.83  ? 319 ARG   C NH1 1 
ATOM   7649 N  NH2 . ARG   C  1  306 ? 7.808   -13.036 18.551 1.00 71.66  ? 319 ARG   C NH2 1 
ATOM   7650 N  N   . ASN   C  1  307 ? 10.072  -8.040  19.560 1.00 29.77  ? 320 ASN   C N   1 
ATOM   7651 C  CA  . ASN   C  1  307 ? 8.819   -7.403  19.216 1.00 29.67  ? 320 ASN   C CA  1 
ATOM   7652 C  C   . ASN   C  1  307 ? 8.961   -5.880  19.229 1.00 32.01  ? 320 ASN   C C   1 
ATOM   7653 O  O   . ASN   C  1  307 ? 8.341   -5.189  18.413 1.00 32.39  ? 320 ASN   C O   1 
ATOM   7654 C  CB  . ASN   C  1  307 ? 7.695   -7.914  20.087 1.00 30.19  ? 320 ASN   C CB  1 
ATOM   7655 C  CG  . ASN   C  1  307 ? 7.335   -9.333  19.729 1.00 30.65  ? 320 ASN   C CG  1 
ATOM   7656 O  OD1 . ASN   C  1  307 ? 8.006   -9.959  18.914 1.00 34.23  ? 320 ASN   C OD1 1 
ATOM   7657 N  ND2 . ASN   C  1  307 ? 6.267   -9.847  20.299 1.00 37.55  ? 320 ASN   C ND2 1 
ATOM   7658 N  N   . LEU   C  1  308 ? 9.827   -5.365  20.105 1.00 30.41  ? 321 LEU   C N   1 
ATOM   7659 C  CA  . LEU   C  1  308 ? 10.142  -3.940  20.111 1.00 32.70  ? 321 LEU   C CA  1 
ATOM   7660 C  C   . LEU   C  1  308 ? 10.773  -3.521  18.789 1.00 29.27  ? 321 LEU   C C   1 
ATOM   7661 O  O   . LEU   C  1  308 ? 10.439  -2.489  18.222 1.00 30.34  ? 321 LEU   C O   1 
ATOM   7662 C  CB  . LEU   C  1  308 ? 11.075  -3.556  21.251 1.00 33.85  ? 321 LEU   C CB  1 
ATOM   7663 C  CG  . LEU   C  1  308 ? 10.367  -3.113  22.529 1.00 37.36  ? 321 LEU   C CG  1 
ATOM   7664 C  CD1 . LEU   C  1  308 ? 11.331  -3.201  23.704 1.00 37.06  ? 321 LEU   C CD1 1 
ATOM   7665 C  CD2 . LEU   C  1  308 ? 9.813   -1.686  22.325 1.00 37.54  ? 321 LEU   C CD2 1 
ATOM   7666 N  N   . ILE   C  1  309 ? 11.723  -4.317  18.315 1.00 28.08  ? 322 ILE   C N   1 
ATOM   7667 C  CA  . ILE   C  1  309 ? 12.432  -3.982  17.093 1.00 29.94  ? 322 ILE   C CA  1 
ATOM   7668 C  C   . ILE   C  1  309 ? 11.443  -3.951  15.926 1.00 29.83  ? 322 ILE   C C   1 
ATOM   7669 O  O   . ILE   C  1  309 ? 11.497  -3.044  15.107 1.00 30.77  ? 322 ILE   C O   1 
ATOM   7670 C  CB  . ILE   C  1  309 ? 13.586  -4.971  16.854 1.00 29.53  ? 322 ILE   C CB  1 
ATOM   7671 C  CG1 . ILE   C  1  309 ? 14.705  -4.763  17.837 1.00 31.88  ? 322 ILE   C CG1 1 
ATOM   7672 C  CG2 . ILE   C  1  309 ? 14.103  -4.879  15.414 1.00 31.47  ? 322 ILE   C CG2 1 
ATOM   7673 C  CD1 . ILE   C  1  309 ? 15.705  -5.909  17.890 1.00 32.27  ? 322 ILE   C CD1 1 
ATOM   7674 N  N   . LYS   C  1  310 ? 10.557  -4.952  15.859 1.00 28.85  ? 323 LYS   C N   1 
ATOM   7675 C  CA  . LYS   C  1  310 ? 9.604   -5.044  14.767 1.00 31.94  ? 323 LYS   C CA  1 
ATOM   7676 C  C   . LYS   C  1  310 ? 8.638   -3.869  14.784 1.00 27.28  ? 323 LYS   C C   1 
ATOM   7677 O  O   . LYS   C  1  310 ? 8.465   -3.212  13.772 1.00 27.63  ? 323 LYS   C O   1 
ATOM   7678 C  CB  . LYS   C  1  310 ? 8.899   -6.389  14.842 1.00 32.04  ? 323 LYS   C CB  1 
ATOM   7679 C  CG  . LYS   C  1  310 ? 9.767   -7.518  14.343 1.00 34.11  ? 323 LYS   C CG  1 
ATOM   7680 C  CD  . LYS   C  1  310 ? 9.086   -8.873  14.493 1.00 41.31  ? 323 LYS   C CD  1 
ATOM   7681 C  CE  . LYS   C  1  310 ? 9.835   -9.903  13.730 1.00 52.03  ? 323 LYS   C CE  1 
ATOM   7682 N  NZ  . LYS   C  1  310 ? 9.446   -11.245 14.157 1.00 60.48  ? 323 LYS   C NZ  1 
ATOM   7683 N  N   . ASN   C  1  311 ? 8.087   -3.563  15.954 1.00 28.97  ? 324 ASN   C N   1 
ATOM   7684 C  CA  . ASN   C  1  311 ? 7.086   -2.522  16.072 1.00 27.53  ? 324 ASN   C CA  1 
ATOM   7685 C  C   . ASN   C  1  311 ? 7.709   -1.169  15.766 1.00 28.51  ? 324 ASN   C C   1 
ATOM   7686 O  O   . ASN   C  1  311 ? 7.081   -0.327  15.130 1.00 30.67  ? 324 ASN   C O   1 
ATOM   7687 C  CB  . ASN   C  1  311 ? 6.408   -2.580  17.429 1.00 30.95  ? 324 ASN   C CB  1 
ATOM   7688 C  CG  . ASN   C  1  311 ? 5.270   -3.564  17.462 1.00 30.70  ? 324 ASN   C CG  1 
ATOM   7689 O  OD1 . ASN   C  1  311 ? 4.159   -3.224  17.051 1.00 33.26  ? 324 ASN   C OD1 1 
ATOM   7690 N  ND2 . ASN   C  1  311 ? 5.507   -4.740  18.005 1.00 32.11  ? 324 ASN   C ND2 1 
ATOM   7691 N  N   . LEU   C  1  312 ? 8.954   -0.966  16.194 1.00 30.75  ? 325 LEU   C N   1 
ATOM   7692 C  CA  . LEU   C  1  312 ? 9.630   0.294   15.948 1.00 31.24  ? 325 LEU   C CA  1 
ATOM   7693 C  C   . LEU   C  1  312 ? 9.821   0.473   14.445 1.00 27.31  ? 325 LEU   C C   1 
ATOM   7694 O  O   . LEU   C  1  312 ? 9.626   1.565   13.931 1.00 26.45  ? 325 LEU   C O   1 
ATOM   7695 C  CB  . LEU   C  1  312 ? 10.958  0.347   16.701 1.00 30.60  ? 325 LEU   C CB  1 
ATOM   7696 C  CG  . LEU   C  1  312 ? 10.883  0.782   18.168 1.00 27.22  ? 325 LEU   C CG  1 
ATOM   7697 C  CD1 . LEU   C  1  312 ? 12.143  0.375   18.832 1.00 29.51  ? 325 LEU   C CD1 1 
ATOM   7698 C  CD2 . LEU   C  1  312 ? 10.675  2.274   18.341 1.00 26.18  ? 325 LEU   C CD2 1 
ATOM   7699 N  N   . HIS   C  1  313 ? 10.188  -0.603  13.751 1.00 28.70  ? 326 HIS   C N   1 
ATOM   7700 C  CA  . HIS   C  1  313 ? 10.349  -0.549  12.299 1.00 30.72  ? 326 HIS   C CA  1 
ATOM   7701 C  C   . HIS   C  1  313 ? 9.003   -0.287  11.635 1.00 28.68  ? 326 HIS   C C   1 
ATOM   7702 O  O   . HIS   C  1  313 ? 8.901   0.569   10.782 1.00 29.46  ? 326 HIS   C O   1 
ATOM   7703 C  CB  . HIS   C  1  313 ? 11.014  -1.813  11.756 1.00 32.64  ? 326 HIS   C CB  1 
ATOM   7704 C  CG  . HIS   C  1  313 ? 11.244  -1.747  10.292 1.00 38.07  ? 326 HIS   C CG  1 
ATOM   7705 N  ND1 . HIS   C  1  313 ? 12.027  -0.760  9.734  1.00 39.18  ? 326 HIS   C ND1 1 
ATOM   7706 C  CD2 . HIS   C  1  313 ? 10.722  -2.455  9.275  1.00 36.80  ? 326 HIS   C CD2 1 
ATOM   7707 C  CE1 . HIS   C  1  313 ? 11.992  -0.890  8.420  1.00 42.44  ? 326 HIS   C CE1 1 
ATOM   7708 N  NE2 . HIS   C  1  313 ? 11.215  -1.923  8.122  1.00 38.49  ? 326 HIS   C NE2 1 
ATOM   7709 N  N   . TYR   C  1  314 ? 7.949   -0.982  12.063 1.00 30.55  ? 327 TYR   C N   1 
ATOM   7710 C  CA  . TYR   C  1  314 ? 6.634   -0.763  11.484 1.00 28.49  ? 327 TYR   C CA  1 
ATOM   7711 C  C   . TYR   C  1  314 ? 6.258   0.703   11.634 1.00 29.53  ? 327 TYR   C C   1 
ATOM   7712 O  O   . TYR   C  1  314 ? 5.786   1.317   10.684 1.00 27.76  ? 327 TYR   C O   1 
ATOM   7713 C  CB  . TYR   C  1  314 ? 5.565   -1.621  12.145 1.00 28.18  ? 327 TYR   C CB  1 
ATOM   7714 C  CG  . TYR   C  1  314 ? 5.802   -3.114  12.039 1.00 27.20  ? 327 TYR   C CG  1 
ATOM   7715 C  CD1 . TYR   C  1  314 ? 6.553   -3.677  11.021 1.00 28.10  ? 327 TYR   C CD1 1 
ATOM   7716 C  CD2 . TYR   C  1  314 ? 5.258   -3.955  12.984 1.00 30.32  ? 327 TYR   C CD2 1 
ATOM   7717 C  CE1 . TYR   C  1  314 ? 6.747   -5.049  10.943 1.00 30.02  ? 327 TYR   C CE1 1 
ATOM   7718 C  CE2 . TYR   C  1  314 ? 5.447   -5.324  12.922 1.00 32.01  ? 327 TYR   C CE2 1 
ATOM   7719 C  CZ  . TYR   C  1  314 ? 6.201   -5.871  11.908 1.00 31.24  ? 327 TYR   C CZ  1 
ATOM   7720 O  OH  . TYR   C  1  314 ? 6.360   -7.221  11.896 1.00 35.84  ? 327 TYR   C OH  1 
ATOM   7721 N  N   . TRP   C  1  315 ? 6.518   1.275   12.808 1.00 26.70  ? 328 TRP   C N   1 
ATOM   7722 C  CA  . TRP   C  1  315 ? 6.152   2.658   13.042 1.00 28.91  ? 328 TRP   C CA  1 
ATOM   7723 C  C   . TRP   C  1  315 ? 6.909   3.548   12.059 1.00 28.39  ? 328 TRP   C C   1 
ATOM   7724 O  O   . TRP   C  1  315 ? 6.327   4.420   11.419 1.00 32.18  ? 328 TRP   C O   1 
ATOM   7725 C  CB  . TRP   C  1  315 ? 6.389   3.067   14.505 1.00 27.28  ? 328 TRP   C CB  1 
ATOM   7726 C  CG  . TRP   C  1  315 ? 5.832   4.424   14.823 1.00 27.44  ? 328 TRP   C CG  1 
ATOM   7727 C  CD1 . TRP   C  1  315 ? 4.583   4.867   14.536 1.00 30.74  ? 328 TRP   C CD1 1 
ATOM   7728 C  CD2 . TRP   C  1  315 ? 6.501   5.525   15.476 1.00 31.80  ? 328 TRP   C CD2 1 
ATOM   7729 N  NE1 . TRP   C  1  315 ? 4.423   6.163   14.947 1.00 33.81  ? 328 TRP   C NE1 1 
ATOM   7730 C  CE2 . TRP   C  1  315 ? 5.582   6.593   15.530 1.00 32.88  ? 328 TRP   C CE2 1 
ATOM   7731 C  CE3 . TRP   C  1  315 ? 7.776   5.710   16.007 1.00 33.27  ? 328 TRP   C CE3 1 
ATOM   7732 C  CZ2 . TRP   C  1  315 ? 5.892   7.824   16.089 1.00 35.56  ? 328 TRP   C CZ2 1 
ATOM   7733 C  CZ3 . TRP   C  1  315 ? 8.077   6.930   16.571 1.00 36.96  ? 328 TRP   C CZ3 1 
ATOM   7734 C  CH2 . TRP   C  1  315 ? 7.157   7.974   16.595 1.00 36.88  ? 328 TRP   C CH2 1 
ATOM   7735 N  N   . TRP   C  1  316 ? 8.201   3.287   11.904 1.00 30.22  ? 329 TRP   C N   1 
ATOM   7736 C  CA  . TRP   C  1  316 ? 9.047   4.078   11.029 1.00 27.88  ? 329 TRP   C CA  1 
ATOM   7737 C  C   . TRP   C  1  316 ? 8.509   4.036   9.591  1.00 27.56  ? 329 TRP   C C   1 
ATOM   7738 O  O   . TRP   C  1  316 ? 8.546   5.050   8.895  1.00 27.61  ? 329 TRP   C O   1 
ATOM   7739 C  CB  . TRP   C  1  316 ? 10.524  3.624   11.101 1.00 31.23  ? 329 TRP   C CB  1 
ATOM   7740 C  CG  . TRP   C  1  316 ? 11.373  4.354   10.087 1.00 29.47  ? 329 TRP   C CG  1 
ATOM   7741 C  CD1 . TRP   C  1  316 ? 11.888  5.614   10.161 1.00 28.79  ? 329 TRP   C CD1 1 
ATOM   7742 C  CD2 . TRP   C  1  316 ? 11.647  3.901   8.751  1.00 28.96  ? 329 TRP   C CD2 1 
ATOM   7743 N  NE1 . TRP   C  1  316 ? 12.502  5.954   8.985  1.00 30.61  ? 329 TRP   C NE1 1 
ATOM   7744 C  CE2 . TRP   C  1  316 ? 12.341  4.934   8.091  1.00 30.50  ? 329 TRP   C CE2 1 
ATOM   7745 C  CE3 . TRP   C  1  316 ? 11.357  2.729   8.056  1.00 33.43  ? 329 TRP   C CE3 1 
ATOM   7746 C  CZ2 . TRP   C  1  316 ? 12.756  4.821   6.771  1.00 30.53  ? 329 TRP   C CZ2 1 
ATOM   7747 C  CZ3 . TRP   C  1  316 ? 11.768  2.622   6.751  1.00 34.59  ? 329 TRP   C CZ3 1 
ATOM   7748 C  CH2 . TRP   C  1  316 ? 12.425  3.668   6.111  1.00 31.70  ? 329 TRP   C CH2 1 
ATOM   7749 N  N   . THR   C  1  317 ? 7.978   2.888   9.130  1.00 29.18  ? 330 THR   C N   1 
ATOM   7750 C  CA  . THR   C  1  317 ? 7.500   2.807   7.753  1.00 28.96  ? 330 THR   C CA  1 
ATOM   7751 C  C   . THR   C  1  317 ? 6.415   3.856   7.527  1.00 29.21  ? 330 THR   C C   1 
ATOM   7752 O  O   . THR   C  1  317 ? 6.341   4.462   6.466  1.00 30.22  ? 330 THR   C O   1 
ATOM   7753 C  CB  . THR   C  1  317 ? 6.978   1.430   7.358  1.00 29.37  ? 330 THR   C CB  1 
ATOM   7754 O  OG1 . THR   C  1  317 ? 5.797   1.152   8.090  1.00 29.91  ? 330 THR   C OG1 1 
ATOM   7755 C  CG2 . THR   C  1  317 ? 8.006   0.321   7.528  1.00 33.84  ? 330 THR   C CG2 1 
ATOM   7756 N  N   . GLY   C  1  318 ? 5.566   4.073   8.532  1.00 28.36  ? 331 GLY   C N   1 
ATOM   7757 C  CA  . GLY   C  1  318 ? 4.545   5.102   8.446  1.00 30.08  ? 331 GLY   C CA  1 
ATOM   7758 C  C   . GLY   C  1  318 ? 5.142   6.498   8.566  1.00 29.21  ? 331 GLY   C C   1 
ATOM   7759 O  O   . GLY   C  1  318 ? 4.822   7.380   7.775  1.00 30.05  ? 331 GLY   C O   1 
ATOM   7760 N  N   . VAL   C  1  319 ? 6.007   6.672   9.568  1.00 31.16  ? 332 VAL   C N   1 
ATOM   7761 C  CA  . VAL   C  1  319 ? 6.580   7.973   9.860  1.00 32.49  ? 332 VAL   C CA  1 
ATOM   7762 C  C   . VAL   C  1  319 ? 7.313   8.489   8.624  1.00 30.63  ? 332 VAL   C C   1 
ATOM   7763 O  O   . VAL   C  1  319 ? 7.261   9.668   8.311  1.00 34.56  ? 332 VAL   C O   1 
ATOM   7764 C  CB  . VAL   C  1  319 ? 7.518   7.884   11.079 1.00 32.57  ? 332 VAL   C CB  1 
ATOM   7765 C  CG1 . VAL   C  1  319 ? 8.496   9.063   11.153 1.00 32.65  ? 332 VAL   C CG1 1 
ATOM   7766 C  CG2 . VAL   C  1  319 ? 6.722   7.768   12.371 1.00 36.30  ? 332 VAL   C CG2 1 
ATOM   7767 N  N   . ASN   C  1  320 ? 8.042   7.600   7.956  1.00 31.84  ? 333 ASN   C N   1 
ATOM   7768 C  CA  . ASN   C  1  320 ? 8.929   8.029   6.887  1.00 36.97  ? 333 ASN   C CA  1 
ATOM   7769 C  C   . ASN   C  1  320 ? 8.121   8.748   5.812  1.00 33.91  ? 333 ASN   C C   1 
ATOM   7770 O  O   . ASN   C  1  320 ? 8.548   9.772   5.300  1.00 32.22  ? 333 ASN   C O   1 
ATOM   7771 C  CB  . ASN   C  1  320 ? 9.739   6.882   6.291  1.00 36.05  ? 333 ASN   C CB  1 
ATOM   7772 C  CG  . ASN   C  1  320 ? 10.820  7.380   5.356  1.00 37.14  ? 333 ASN   C CG  1 
ATOM   7773 O  OD1 . ASN   C  1  320 ? 11.602  8.269   5.728  1.00 34.98  ? 333 ASN   C OD1 1 
ATOM   7774 N  ND2 . ASN   C  1  320 ? 10.873  6.825   4.146  1.00 33.59  ? 333 ASN   C ND2 1 
ATOM   7775 N  N   . VAL   C  1  321 ? 6.944   8.200   5.498  1.00 32.68  ? 334 VAL   C N   1 
ATOM   7776 C  CA  . VAL   C  1  321 ? 6.106   8.797   4.484  1.00 33.35  ? 334 VAL   C CA  1 
ATOM   7777 C  C   . VAL   C  1  321 ? 5.404   10.008  5.087  1.00 35.15  ? 334 VAL   C C   1 
ATOM   7778 O  O   . VAL   C  1  321 ? 5.412   11.090  4.500  1.00 40.20  ? 334 VAL   C O   1 
ATOM   7779 C  CB  . VAL   C  1  321 ? 5.105   7.805   3.865  1.00 36.40  ? 334 VAL   C CB  1 
ATOM   7780 C  CG1 . VAL   C  1  321 ? 4.293   8.489   2.766  1.00 37.11  ? 334 VAL   C CG1 1 
ATOM   7781 C  CG2 . VAL   C  1  321 ? 5.797   6.551   3.331  1.00 34.98  ? 334 VAL   C CG2 1 
ATOM   7782 N  N   . ALA   C  1  322 ? 4.789   9.840   6.262  1.00 37.92  ? 335 ALA   C N   1 
ATOM   7783 C  CA  . ALA   C  1  322 ? 3.920   10.888  6.770  1.00 39.90  ? 335 ALA   C CA  1 
ATOM   7784 C  C   . ALA   C  1  322 ? 4.699   12.154  7.111  1.00 36.63  ? 335 ALA   C C   1 
ATOM   7785 O  O   . ALA   C  1  322 ? 4.168   13.255  6.986  1.00 38.97  ? 335 ALA   C O   1 
ATOM   7786 C  CB  . ALA   C  1  322 ? 3.148   10.398  7.960  1.00 42.24  ? 335 ALA   C CB  1 
ATOM   7787 N  N   . PHE   C  1  323 ? 5.938   12.005  7.568  1.00 35.08  ? 336 PHE   C N   1 
ATOM   7788 C  CA  . PHE   C  1  323 ? 6.704   13.157  8.025  1.00 41.96  ? 336 PHE   C CA  1 
ATOM   7789 C  C   . PHE   C  1  323 ? 7.605   13.686  6.915  1.00 40.95  ? 336 PHE   C C   1 
ATOM   7790 O  O   . PHE   C  1  323 ? 8.319   14.650  7.142  1.00 43.43  ? 336 PHE   C O   1 
ATOM   7791 C  CB  . PHE   C  1  323 ? 7.542   12.802  9.261  1.00 47.04  ? 336 PHE   C CB  1 
ATOM   7792 C  CG  . PHE   C  1  323 ? 6.746   12.552  10.535 1.00 46.90  ? 336 PHE   C CG  1 
ATOM   7793 C  CD1 . PHE   C  1  323 ? 5.354   12.583  10.542 1.00 46.57  ? 336 PHE   C CD1 1 
ATOM   7794 C  CD2 . PHE   C  1  323 ? 7.409   12.266  11.721 1.00 43.48  ? 336 PHE   C CD2 1 
ATOM   7795 C  CE1 . PHE   C  1  323 ? 4.650   12.319  11.705 1.00 49.53  ? 336 PHE   C CE1 1 
ATOM   7796 C  CE2 . PHE   C  1  323 ? 6.693   11.980  12.872 1.00 47.16  ? 336 PHE   C CE2 1 
ATOM   7797 C  CZ  . PHE   C  1  323 ? 5.311   11.996  12.860 1.00 47.77  ? 336 PHE   C CZ  1 
ATOM   7798 N  N   . GLY   C  1  324 ? 7.612   13.030  5.746  1.00 44.28  ? 337 GLY   C N   1 
ATOM   7799 C  CA  . GLY   C  1  324 ? 8.394   13.490  4.604  1.00 41.58  ? 337 GLY   C CA  1 
ATOM   7800 C  C   . GLY   C  1  324 ? 9.885   13.149  4.720  1.00 44.80  ? 337 GLY   C C   1 
ATOM   7801 O  O   . GLY   C  1  324 ? 10.706  13.939  4.274  1.00 42.57  ? 337 GLY   C O   1 
ATOM   7802 N  N   . GLY   C  1  325 ? 10.220  11.970  5.289  1.00 41.21  ? 338 GLY   C N   1 
ATOM   7803 C  CA  . GLY   C  1  325 ? 11.579  11.448  5.326  1.00 39.67  ? 338 GLY   C CA  1 
ATOM   7804 C  C   . GLY   C  1  325 ? 12.226  11.662  6.697  1.00 44.19  ? 338 GLY   C C   1 
ATOM   7805 O  O   . GLY   C  1  325 ? 12.429  12.808  7.082  1.00 40.74  ? 338 GLY   C O   1 
ATOM   7806 N  N   . CYS   C  1  326 ? 12.474  10.568  7.444  1.00 39.78  ? 339 CYS   C N   1 
ATOM   7807 C  CA  . CYS   C  1  326 ? 13.216  10.616  8.700  1.00 42.94  ? 339 CYS   C CA  1 
ATOM   7808 C  C   . CYS   C  1  326 ? 14.205  9.461   8.697  1.00 39.22  ? 339 CYS   C C   1 
ATOM   7809 O  O   . CYS   C  1  326 ? 13.860  8.368   8.257  1.00 34.80  ? 339 CYS   C O   1 
ATOM   7810 C  CB  . CYS   C  1  326 ? 12.360  10.439  9.972  1.00 43.05  ? 339 CYS   C CB  1 
ATOM   7811 S  SG  . CYS   C  1  326 ? 11.156  11.758  10.271 1.00 60.61  ? 339 CYS   C SG  1 
ATOM   7812 N  N   . ASP   C  1  327 ? 15.407  9.695   9.226  1.00 36.90  ? 340 ASP   C N   1 
ATOM   7813 C  CA  . ASP   C  1  327 ? 16.382  8.626   9.367  1.00 44.19  ? 340 ASP   C CA  1 
ATOM   7814 C  C   . ASP   C  1  327 ? 15.932  7.685   10.479 1.00 38.75  ? 340 ASP   C C   1 
ATOM   7815 O  O   . ASP   C  1  327 ? 15.686  8.101   11.605 1.00 40.42  ? 340 ASP   C O   1 
ATOM   7816 C  CB  . ASP   C  1  327 ? 17.792  9.162   9.590  1.00 51.14  ? 340 ASP   C CB  1 
ATOM   7817 C  CG  . ASP   C  1  327 ? 18.455  9.822   8.376  1.00 60.17  ? 340 ASP   C CG  1 
ATOM   7818 O  OD1 . ASP   C  1  327 ? 17.909  9.751   7.241  1.00 50.41  ? 340 ASP   C OD1 1 
ATOM   7819 O  OD2 . ASP   C  1  327 ? 19.542  10.412  8.558  1.00 65.53  ? 340 ASP   C OD2 1 
ATOM   7820 N  N   . GLU   C  1  328 ? 15.843  6.402   10.142 1.00 32.50  ? 341 GLU   C N   1 
ATOM   7821 C  CA  . GLU   C  1  328 ? 15.441  5.390   11.092 1.00 33.09  ? 341 GLU   C CA  1 
ATOM   7822 C  C   . GLU   C  1  328 ? 16.482  5.275   12.204 1.00 38.02  ? 341 GLU   C C   1 
ATOM   7823 O  O   . GLU   C  1  328 ? 17.682  5.266   11.934 1.00 34.88  ? 341 GLU   C O   1 
ATOM   7824 C  CB  . GLU   C  1  328 ? 15.263  4.054   10.384 1.00 33.77  ? 341 GLU   C CB  1 
ATOM   7825 C  CG  . GLU   C  1  328 ? 14.626  2.996   11.275 1.00 36.33  ? 341 GLU   C CG  1 
ATOM   7826 C  CD  . GLU   C  1  328 ? 14.164  1.737   10.567 1.00 38.20  ? 341 GLU   C CD  1 
ATOM   7827 O  OE1 . GLU   C  1  328 ? 14.403  1.625   9.350  1.00 37.79  ? 341 GLU   C OE1 1 
ATOM   7828 O  OE2 . GLU   C  1  328 ? 13.557  0.875   11.254 1.00 39.21  ? 341 GLU   C OE2 1 
ATOM   7829 N  N   . LEU   C  1  329 ? 16.008  5.166   13.451 1.00 34.92  ? 342 LEU   C N   1 
ATOM   7830 C  CA  . LEU   C  1  329 ? 16.843  4.847   14.599 1.00 32.64  ? 342 LEU   C CA  1 
ATOM   7831 C  C   . LEU   C  1  329 ? 16.725  3.367   14.951 1.00 33.25  ? 342 LEU   C C   1 
ATOM   7832 O  O   . LEU   C  1  329 ? 15.664  2.765   14.747 1.00 34.69  ? 342 LEU   C O   1 
ATOM   7833 C  CB  . LEU   C  1  329 ? 16.394  5.745   15.751 1.00 37.09  ? 342 LEU   C CB  1 
ATOM   7834 C  CG  . LEU   C  1  329 ? 16.625  7.244   15.537 1.00 41.32  ? 342 LEU   C CG  1 
ATOM   7835 C  CD1 . LEU   C  1  329 ? 15.968  8.062   16.618 1.00 42.75  ? 342 LEU   C CD1 1 
ATOM   7836 C  CD2 . LEU   C  1  329 ? 18.113  7.533   15.516 1.00 42.09  ? 342 LEU   C CD2 1 
ATOM   7837 N  N   . PHE   C  1  330 ? 17.800  2.800   15.514 1.00 31.46  ? 343 PHE   C N   1 
ATOM   7838 C  CA  . PHE   C  1  330 ? 17.835  1.389   15.856 1.00 34.62  ? 343 PHE   C CA  1 
ATOM   7839 C  C   . PHE   C  1  330 ? 18.264  1.215   17.309 1.00 36.72  ? 343 PHE   C C   1 
ATOM   7840 O  O   . PHE   C  1  330 ? 19.306  0.635   17.587 1.00 39.59  ? 343 PHE   C O   1 
ATOM   7841 C  CB  . PHE   C  1  330 ? 18.761  0.621   14.906 1.00 36.69  ? 343 PHE   C CB  1 
ATOM   7842 C  CG  . PHE   C  1  330 ? 18.335  0.716   13.447 1.00 38.91  ? 343 PHE   C CG  1 
ATOM   7843 C  CD1 . PHE   C  1  330 ? 17.319  -0.101  12.958 1.00 37.35  ? 343 PHE   C CD1 1 
ATOM   7844 C  CD2 . PHE   C  1  330 ? 18.945  1.613   12.577 1.00 36.45  ? 343 PHE   C CD2 1 
ATOM   7845 C  CE1 . PHE   C  1  330 ? 16.921  -0.033  11.626 1.00 38.97  ? 343 PHE   C CE1 1 
ATOM   7846 C  CE2 . PHE   C  1  330 ? 18.534  1.697   11.243 1.00 42.07  ? 343 PHE   C CE2 1 
ATOM   7847 C  CZ  . PHE   C  1  330 ? 17.522  0.871   10.768 1.00 40.26  ? 343 PHE   C CZ  1 
ATOM   7848 N  N   . PRO   C  1  331 ? 17.453  1.651   18.294 1.00 37.33  ? 344 PRO   C N   1 
ATOM   7849 C  CA  . PRO   C  1  331 ? 17.897  1.626   19.686 1.00 32.17  ? 344 PRO   C CA  1 
ATOM   7850 C  C   . PRO   C  1  331 ? 18.167  0.227   20.221 1.00 30.76  ? 344 PRO   C C   1 
ATOM   7851 O  O   . PRO   C  1  331 ? 18.873  0.118   21.213 1.00 33.72  ? 344 PRO   C O   1 
ATOM   7852 C  CB  . PRO   C  1  331 ? 16.748  2.320   20.423 1.00 35.56  ? 344 PRO   C CB  1 
ATOM   7853 C  CG  . PRO   C  1  331 ? 15.535  2.046   19.543 1.00 36.13  ? 344 PRO   C CG  1 
ATOM   7854 C  CD  . PRO   C  1  331 ? 16.086  2.186   18.130 1.00 34.25  ? 344 PRO   C CD  1 
ATOM   7855 N  N   . TYR   C  1  332 ? 17.620  -0.821  19.580 1.00 30.44  ? 345 TYR   C N   1 
ATOM   7856 C  CA  . TYR   C  1  332 ? 17.848  -2.193  20.003 1.00 28.91  ? 345 TYR   C CA  1 
ATOM   7857 C  C   . TYR   C  1  332 ? 18.545  -3.011  18.918 1.00 30.04  ? 345 TYR   C C   1 
ATOM   7858 O  O   . TYR   C  1  332 ? 18.616  -4.244  19.002 1.00 27.98  ? 345 TYR   C O   1 
ATOM   7859 C  CB  . TYR   C  1  332 ? 16.545  -2.851  20.428 1.00 31.45  ? 345 TYR   C CB  1 
ATOM   7860 C  CG  . TYR   C  1  332 ? 15.802  -2.025  21.460 1.00 33.13  ? 345 TYR   C CG  1 
ATOM   7861 C  CD1 . TYR   C  1  332 ? 16.281  -1.890  22.766 1.00 33.03  ? 345 TYR   C CD1 1 
ATOM   7862 C  CD2 . TYR   C  1  332 ? 14.631  -1.366  21.130 1.00 32.38  ? 345 TYR   C CD2 1 
ATOM   7863 C  CE1 . TYR   C  1  332 ? 15.623  -1.083  23.683 1.00 37.25  ? 345 TYR   C CE1 1 
ATOM   7864 C  CE2 . TYR   C  1  332 ? 13.945  -0.597  22.054 1.00 33.43  ? 345 TYR   C CE2 1 
ATOM   7865 C  CZ  . TYR   C  1  332 ? 14.438  -0.456  23.340 1.00 35.02  ? 345 TYR   C CZ  1 
ATOM   7866 O  OH  . TYR   C  1  332 ? 13.770  0.324   24.236 1.00 36.58  ? 345 TYR   C OH  1 
ATOM   7867 N  N   . GLY   C  1  333 ? 19.187  -2.315  17.979 1.00 31.28  ? 346 GLY   C N   1 
ATOM   7868 C  CA  . GLY   C  1  333 ? 19.828  -2.982  16.851 1.00 38.09  ? 346 GLY   C CA  1 
ATOM   7869 C  C   . GLY   C  1  333 ? 18.810  -3.635  15.908 1.00 38.59  ? 346 GLY   C C   1 
ATOM   7870 O  O   . GLY   C  1  333 ? 17.716  -3.115  15.753 1.00 37.89  ? 346 GLY   C O   1 
ATOM   7871 N  N   . GLN   C  1  334 ? 19.184  -4.801  15.376 1.00 40.22  ? 347 GLN   C N   1 
ATOM   7872 C  CA  . GLN   C  1  334 ? 18.509  -5.500  14.299 1.00 42.17  ? 347 GLN   C CA  1 
ATOM   7873 C  C   . GLN   C  1  334 ? 18.170  -6.905  14.799 1.00 41.52  ? 347 GLN   C C   1 
ATOM   7874 O  O   . GLN   C  1  334 ? 18.745  -7.380  15.792 1.00 37.91  ? 347 GLN   C O   1 
ATOM   7875 C  CB  . GLN   C  1  334 ? 19.455  -5.666  13.098 1.00 48.76  ? 347 GLN   C CB  1 
ATOM   7876 C  CG  . GLN   C  1  334 ? 20.170  -4.410  12.602 1.00 56.42  ? 347 GLN   C CG  1 
ATOM   7877 C  CD  . GLN   C  1  334 ? 19.219  -3.385  12.024 1.00 63.88  ? 347 GLN   C CD  1 
ATOM   7878 O  OE1 . GLN   C  1  334 ? 18.078  -3.701  11.660 1.00 70.72  ? 347 GLN   C OE1 1 
ATOM   7879 N  NE2 . GLN   C  1  334 ? 19.685  -2.145  11.945 1.00 59.36  ? 347 GLN   C NE2 1 
ATOM   7880 N  N   . LEU   C  1  335 ? 17.278  -7.599  14.080 1.00 37.67  ? 348 LEU   C N   1 
ATOM   7881 C  CA  . LEU   C  1  335 ? 16.800  -8.913  14.502 1.00 49.06  ? 348 LEU   C CA  1 
ATOM   7882 C  C   . LEU   C  1  335 ? 17.929  -9.973  14.506 1.00 54.59  ? 348 LEU   C C   1 
ATOM   7883 O  O   . LEU   C  1  335 ? 18.747  -9.946  13.559 1.00 56.32  ? 348 LEU   C O   1 
ATOM   7884 C  CB  . LEU   C  1  335 ? 15.658  -9.372  13.599 1.00 49.69  ? 348 LEU   C CB  1 
ATOM   7885 C  CG  . LEU   C  1  335 ? 14.331  -8.626  13.738 1.00 57.18  ? 348 LEU   C CG  1 
ATOM   7886 C  CD1 . LEU   C  1  335 ? 13.366  -9.085  12.647 1.00 58.94  ? 348 LEU   C CD1 1 
ATOM   7887 C  CD2 . LEU   C  1  335 ? 13.757  -8.856  15.124 1.00 58.26  ? 348 LEU   C CD2 1 
HETATM 7888 C  C1  . NAG   D  2  .   ? 28.598  12.535  34.394 1.00 53.62  ? 1   NAG   G C1  1 
HETATM 7889 C  C2  . NAG   D  2  .   ? 28.544  13.898  35.068 1.00 58.86  ? 1   NAG   G C2  1 
HETATM 7890 C  C3  . NAG   D  2  .   ? 28.178  15.010  34.083 1.00 60.70  ? 1   NAG   G C3  1 
HETATM 7891 C  C4  . NAG   D  2  .   ? 28.794  14.870  32.693 1.00 63.04  ? 1   NAG   G C4  1 
HETATM 7892 C  C5  . NAG   D  2  .   ? 28.753  13.428  32.180 1.00 60.54  ? 1   NAG   G C5  1 
HETATM 7893 C  C6  . NAG   D  2  .   ? 29.522  13.185  30.878 1.00 55.25  ? 1   NAG   G C6  1 
HETATM 7894 C  C7  . NAG   D  2  .   ? 27.619  14.102  37.365 1.00 88.54  ? 1   NAG   G C7  1 
HETATM 7895 C  C8  . NAG   D  2  .   ? 26.332  14.226  38.128 1.00 94.48  ? 1   NAG   G C8  1 
HETATM 7896 N  N2  . NAG   D  2  .   ? 27.506  13.763  36.073 1.00 72.21  ? 1   NAG   G N2  1 
HETATM 7897 O  O3  . NAG   D  2  .   ? 28.578  16.244  34.654 1.00 70.53  ? 1   NAG   G O3  1 
HETATM 7898 O  O4  . NAG   D  2  .   ? 28.027  15.678  31.804 1.00 69.61  ? 1   NAG   G O4  1 
HETATM 7899 O  O5  . NAG   D  2  .   ? 29.352  12.595  33.188 1.00 53.51  ? 1   NAG   G O5  1 
HETATM 7900 O  O6  . NAG   D  2  .   ? 30.948  13.508  30.977 1.00 48.63  ? 1   NAG   G O6  1 
HETATM 7901 O  O7  . NAG   D  2  .   ? 28.706  14.326  37.895 1.00 73.68  ? 1   NAG   G O7  1 
HETATM 7902 C  C1  . NAG   D  2  .   ? 28.633  16.444  30.804 1.00 70.74  ? 2   NAG   G C1  1 
HETATM 7903 C  C2  . NAG   D  2  .   ? 27.787  16.586  29.538 1.00 69.76  ? 2   NAG   G C2  1 
HETATM 7904 C  C3  . NAG   D  2  .   ? 28.481  17.535  28.565 1.00 80.73  ? 2   NAG   G C3  1 
HETATM 7905 C  C4  . NAG   D  2  .   ? 28.811  18.866  29.238 1.00 86.44  ? 2   NAG   G C4  1 
HETATM 7906 C  C5  . NAG   D  2  .   ? 29.600  18.621  30.523 1.00 73.74  ? 2   NAG   G C5  1 
HETATM 7907 C  C6  . NAG   D  2  .   ? 29.821  19.873  31.343 1.00 71.76  ? 2   NAG   G C6  1 
HETATM 7908 C  C7  . NAG   D  2  .   ? 26.422  14.620  28.904 1.00 73.68  ? 2   NAG   G C7  1 
HETATM 7909 C  C8  . NAG   D  2  .   ? 26.380  13.374  28.064 1.00 75.01  ? 2   NAG   G C8  1 
HETATM 7910 N  N2  . NAG   D  2  .   ? 27.534  15.359  28.808 1.00 72.30  ? 2   NAG   G N2  1 
HETATM 7911 O  O3  . NAG   D  2  .   ? 27.655  17.704  27.416 1.00 75.32  ? 2   NAG   G O3  1 
HETATM 7912 O  O4  . NAG   D  2  .   ? 29.597  19.681  28.352 1.00 96.00  ? 2   NAG   G O4  1 
HETATM 7913 O  O5  . NAG   D  2  .   ? 28.858  17.727  31.372 1.00 69.24  ? 2   NAG   G O5  1 
HETATM 7914 O  O6  . NAG   D  2  .   ? 28.659  20.181  32.121 1.00 70.42  ? 2   NAG   G O6  1 
HETATM 7915 O  O7  . NAG   D  2  .   ? 25.501  14.941  29.648 1.00 61.75  ? 2   NAG   G O7  1 
HETATM 7916 C  C1  . BMA   D  2  .   ? 29.085  20.881  27.861 1.00 110.48 ? 3   BMA   G C1  1 
HETATM 7917 C  C2  . BMA   D  2  .   ? 30.242  21.866  27.720 1.00 117.72 ? 3   BMA   G C2  1 
HETATM 7918 C  C3  . BMA   D  2  .   ? 29.782  23.186  27.056 1.00 132.93 ? 3   BMA   G C3  1 
HETATM 7919 C  C4  . BMA   D  2  .   ? 28.759  22.998  25.920 1.00 136.75 ? 3   BMA   G C4  1 
HETATM 7920 C  C5  . BMA   D  2  .   ? 27.751  21.862  26.152 1.00 132.52 ? 3   BMA   G C5  1 
HETATM 7921 C  C6  . BMA   D  2  .   ? 26.996  21.488  24.889 1.00 139.35 ? 3   BMA   G C6  1 
HETATM 7922 O  O2  . BMA   D  2  .   ? 31.357  21.245  27.071 1.00 84.39  ? 3   BMA   G O2  1 
HETATM 7923 O  O3  . BMA   D  2  .   ? 30.935  23.873  26.551 1.00 131.00 ? 3   BMA   G O3  1 
HETATM 7924 O  O4  . BMA   D  2  .   ? 27.997  24.202  25.769 1.00 132.33 ? 3   BMA   G O4  1 
HETATM 7925 O  O5  . BMA   D  2  .   ? 28.440  20.688  26.604 1.00 118.38 ? 3   BMA   G O5  1 
HETATM 7926 O  O6  . BMA   D  2  .   ? 27.075  20.083  24.572 1.00 143.43 ? 3   BMA   G O6  1 
HETATM 7927 C  C1  . MAN   D  2  .   ? 31.198  25.151  27.047 1.00 121.56 ? 4   MAN   G C1  1 
HETATM 7928 C  C2  . MAN   D  2  .   ? 31.824  25.928  25.899 1.00 120.96 ? 4   MAN   G C2  1 
HETATM 7929 C  C3  . MAN   D  2  .   ? 33.229  25.375  25.597 1.00 118.05 ? 4   MAN   G C3  1 
HETATM 7930 C  C4  . MAN   D  2  .   ? 34.104  25.369  26.851 1.00 117.72 ? 4   MAN   G C4  1 
HETATM 7931 C  C5  . MAN   D  2  .   ? 33.409  24.618  28.008 1.00 109.06 ? 4   MAN   G C5  1 
HETATM 7932 C  C6  . MAN   D  2  .   ? 34.135  24.724  29.348 1.00 96.70  ? 4   MAN   G C6  1 
HETATM 7933 O  O2  . MAN   D  2  .   ? 31.777  27.330  26.181 1.00 102.16 ? 4   MAN   G O2  1 
HETATM 7934 O  O3  . MAN   D  2  .   ? 33.853  26.136  24.553 1.00 109.99 ? 4   MAN   G O3  1 
HETATM 7935 O  O4  . MAN   D  2  .   ? 35.352  24.737  26.560 1.00 98.05  ? 4   MAN   G O4  1 
HETATM 7936 O  O5  . MAN   D  2  .   ? 32.058  25.143  28.210 1.00 116.28 ? 4   MAN   G O5  1 
HETATM 7937 O  O6  . MAN   D  2  .   ? 35.108  25.789  29.427 1.00 83.19  ? 4   MAN   G O6  1 
HETATM 7938 C  C1  . MAN   D  2  .   ? 25.998  19.608  23.801 1.00 149.42 ? 5   MAN   G C1  1 
HETATM 7939 C  C2  . MAN   D  2  .   ? 24.825  19.296  24.759 1.00 147.53 ? 5   MAN   G C2  1 
HETATM 7940 C  C3  . MAN   D  2  .   ? 24.816  17.867  25.316 1.00 139.37 ? 5   MAN   G C3  1 
HETATM 7941 C  C4  . MAN   D  2  .   ? 25.103  16.853  24.224 1.00 135.00 ? 5   MAN   G C4  1 
HETATM 7942 C  C5  . MAN   D  2  .   ? 26.441  17.165  23.559 1.00 140.23 ? 5   MAN   G C5  1 
HETATM 7943 C  C6  . MAN   D  2  .   ? 26.768  16.184  22.447 1.00 129.98 ? 5   MAN   G C6  1 
HETATM 7944 O  O2  . MAN   D  2  .   ? 23.596  19.590  24.100 1.00 138.59 ? 5   MAN   G O2  1 
HETATM 7945 O  O3  . MAN   D  2  .   ? 23.558  17.581  25.934 1.00 118.33 ? 5   MAN   G O3  1 
HETATM 7946 O  O4  . MAN   D  2  .   ? 25.142  15.540  24.777 1.00 128.10 ? 5   MAN   G O4  1 
HETATM 7947 O  O5  . MAN   D  2  .   ? 26.397  18.492  22.960 1.00 152.59 ? 5   MAN   G O5  1 
HETATM 7948 O  O6  . MAN   D  2  .   ? 28.122  16.304  21.982 1.00 114.44 ? 5   MAN   G O6  1 
HETATM 7949 C  C1  . NAG   E  3  .   ? 27.695  -8.888  19.963 1.00 43.68  ? 1   NAG   I C1  1 
HETATM 7950 C  C2  . NAG   E  3  .   ? 28.382  -9.831  18.977 1.00 45.66  ? 1   NAG   I C2  1 
HETATM 7951 C  C3  . NAG   E  3  .   ? 27.721  -9.751  17.603 1.00 46.32  ? 1   NAG   I C3  1 
HETATM 7952 C  C4  . NAG   E  3  .   ? 26.214  -9.952  17.736 1.00 47.70  ? 1   NAG   I C4  1 
HETATM 7953 C  C5  . NAG   E  3  .   ? 25.647  -8.949  18.743 1.00 49.66  ? 1   NAG   I C5  1 
HETATM 7954 C  C6  . NAG   E  3  .   ? 24.161  -9.119  18.989 1.00 46.29  ? 1   NAG   I C6  1 
HETATM 7955 C  C7  . NAG   E  3  .   ? 30.669  -10.612 19.211 1.00 46.67  ? 1   NAG   I C7  1 
HETATM 7956 C  C8  . NAG   E  3  .   ? 32.105  -10.362 18.876 1.00 45.84  ? 1   NAG   I C8  1 
HETATM 7957 N  N2  . NAG   E  3  .   ? 29.819  -9.631  18.888 1.00 43.95  ? 1   NAG   I N2  1 
HETATM 7958 O  O3  . NAG   E  3  .   ? 28.312  -10.758 16.790 1.00 38.91  ? 1   NAG   I O3  1 
HETATM 7959 O  O4  . NAG   E  3  .   ? 25.601  -9.744  16.470 1.00 48.35  ? 1   NAG   I O4  1 
HETATM 7960 O  O5  . NAG   E  3  .   ? 26.299  -9.143  20.010 1.00 45.76  ? 1   NAG   I O5  1 
HETATM 7961 O  O6  . NAG   E  3  .   ? 23.887  -10.393 19.565 1.00 39.09  ? 1   NAG   I O6  1 
HETATM 7962 O  O7  . NAG   E  3  .   ? 30.294  -11.667 19.728 1.00 39.94  ? 1   NAG   I O7  1 
HETATM 7963 C  C1  . NAG   E  3  .   ? 25.466  -10.798 15.576 1.00 54.74  ? 2   NAG   I C1  1 
HETATM 7964 C  C2  . NAG   E  3  .   ? 24.149  -10.590 14.845 1.00 58.40  ? 2   NAG   I C2  1 
HETATM 7965 C  C3  . NAG   E  3  .   ? 23.947  -11.736 13.862 1.00 66.68  ? 2   NAG   I C3  1 
HETATM 7966 C  C4  . NAG   E  3  .   ? 25.138  -11.822 12.916 1.00 74.37  ? 2   NAG   I C4  1 
HETATM 7967 C  C5  . NAG   E  3  .   ? 26.471  -11.878 13.671 1.00 73.92  ? 2   NAG   I C5  1 
HETATM 7968 C  C6  . NAG   E  3  .   ? 27.658  -11.654 12.758 1.00 73.15  ? 2   NAG   I C6  1 
HETATM 7969 C  C7  . NAG   E  3  .   ? 22.285  -9.451  15.970 1.00 51.82  ? 2   NAG   I C7  1 
HETATM 7970 C  C8  . NAG   E  3  .   ? 21.077  -9.662  16.841 1.00 49.62  ? 2   NAG   I C8  1 
HETATM 7971 N  N2  . NAG   E  3  .   ? 22.999  -10.547 15.718 1.00 50.62  ? 2   NAG   I N2  1 
HETATM 7972 O  O3  . NAG   E  3  .   ? 22.734  -11.499 13.158 1.00 49.50  ? 2   NAG   I O3  1 
HETATM 7973 O  O4  . NAG   E  3  .   ? 24.979  -12.972 12.082 1.00 75.89  ? 2   NAG   I O4  1 
HETATM 7974 O  O5  . NAG   E  3  .   ? 26.543  -10.813 14.644 1.00 63.64  ? 2   NAG   I O5  1 
HETATM 7975 O  O6  . NAG   E  3  .   ? 28.649  -10.844 13.370 1.00 81.54  ? 2   NAG   I O6  1 
HETATM 7976 O  O7  . NAG   E  3  .   ? 22.625  -8.342  15.562 1.00 42.89  ? 2   NAG   I O7  1 
HETATM 7977 C  C1  . BMA   E  3  .   ? 25.272  -12.614 10.768 1.00 84.21  ? 3   BMA   I C1  1 
HETATM 7978 C  C2  . BMA   E  3  .   ? 25.333  -13.897 9.962  1.00 85.50  ? 3   BMA   I C2  1 
HETATM 7979 C  C3  . BMA   E  3  .   ? 25.705  -13.553 8.516  1.00 96.90  ? 3   BMA   I C3  1 
HETATM 7980 C  C4  . BMA   E  3  .   ? 24.807  -12.463 7.941  1.00 92.42  ? 3   BMA   I C4  1 
HETATM 7981 C  C5  . BMA   E  3  .   ? 24.741  -11.241 8.868  1.00 97.12  ? 3   BMA   I C5  1 
HETATM 7982 C  C6  . BMA   E  3  .   ? 23.741  -10.189 8.416  1.00 101.89 ? 3   BMA   I C6  1 
HETATM 7983 O  O2  . BMA   E  3  .   ? 24.133  -14.637 10.157 1.00 63.76  ? 3   BMA   I O2  1 
HETATM 7984 O  O3  . BMA   E  3  .   ? 25.680  -14.737 7.713  1.00 110.12 ? 3   BMA   I O3  1 
HETATM 7985 O  O4  . BMA   E  3  .   ? 25.344  -12.040 6.691  1.00 80.80  ? 3   BMA   I O4  1 
HETATM 7986 O  O5  . BMA   E  3  .   ? 24.340  -11.702 10.183 1.00 93.44  ? 3   BMA   I O5  1 
HETATM 7987 O  O6  . BMA   E  3  .   ? 22.431  -10.765 8.257  1.00 106.15 ? 3   BMA   I O6  1 
HETATM 7988 C  C1  . MAN   E  3  .   ? 21.463  -10.116 7.465  1.00 109.59 ? 4   MAN   I C1  1 
HETATM 7989 C  C2  . MAN   E  3  .   ? 20.137  -10.780 7.830  1.00 106.69 ? 4   MAN   I C2  1 
HETATM 7990 C  C3  . MAN   E  3  .   ? 20.072  -12.244 7.328  1.00 110.42 ? 4   MAN   I C3  1 
HETATM 7991 C  C4  . MAN   E  3  .   ? 20.662  -12.463 5.930  1.00 116.91 ? 4   MAN   I C4  1 
HETATM 7992 C  C5  . MAN   E  3  .   ? 21.949  -11.671 5.713  1.00 131.72 ? 4   MAN   I C5  1 
HETATM 7993 C  C6  . MAN   E  3  .   ? 22.492  -11.734 4.291  1.00 146.40 ? 4   MAN   I C6  1 
HETATM 7994 O  O2  . MAN   E  3  .   ? 19.032  -9.981  7.411  1.00 89.16  ? 4   MAN   I O2  1 
HETATM 7995 O  O3  . MAN   E  3  .   ? 18.713  -12.671 7.325  1.00 107.60 ? 4   MAN   I O3  1 
HETATM 7996 O  O4  . MAN   E  3  .   ? 20.963  -13.850 5.771  1.00 106.86 ? 4   MAN   I O4  1 
HETATM 7997 O  O5  . MAN   E  3  .   ? 21.716  -10.279 6.067  1.00 118.03 ? 4   MAN   I O5  1 
HETATM 7998 O  O6  . MAN   E  3  .   ? 21.486  -11.572 3.253  1.00 170.87 ? 4   MAN   I O6  1 
HETATM 7999 C  C1  . MAN   E  3  .   ? 18.446  -13.906 7.918  1.00 110.99 ? 5   MAN   I C1  1 
HETATM 8000 C  C2  . MAN   E  3  .   ? 17.028  -14.270 7.567  1.00 113.88 ? 5   MAN   I C2  1 
HETATM 8001 C  C3  . MAN   E  3  .   ? 16.067  -13.171 8.065  1.00 109.84 ? 5   MAN   I C3  1 
HETATM 8002 C  C4  . MAN   E  3  .   ? 16.200  -13.006 9.575  1.00 108.47 ? 5   MAN   I C4  1 
HETATM 8003 C  C5  . MAN   E  3  .   ? 17.694  -12.808 9.933  1.00 108.30 ? 5   MAN   I C5  1 
HETATM 8004 C  C6  . MAN   E  3  .   ? 17.983  -12.797 11.420 1.00 98.26  ? 5   MAN   I C6  1 
HETATM 8005 O  O2  . MAN   E  3  .   ? 16.756  -15.554 8.124  1.00 107.22 ? 5   MAN   I O2  1 
HETATM 8006 O  O3  . MAN   E  3  .   ? 14.710  -13.452 7.712  1.00 103.87 ? 5   MAN   I O3  1 
HETATM 8007 O  O4  . MAN   E  3  .   ? 15.422  -11.876 10.012 1.00 83.04  ? 5   MAN   I O4  1 
HETATM 8008 O  O5  . MAN   E  3  .   ? 18.516  -13.870 9.348  1.00 109.73 ? 5   MAN   I O5  1 
HETATM 8009 O  O6  . MAN   E  3  .   ? 19.029  -11.856 11.691 1.00 69.07  ? 5   MAN   I O6  1 
HETATM 8010 C  C1  . MAN   E  3  .   ? 21.878  -11.977 1.962  1.00 169.35 ? 6   MAN   I C1  1 
HETATM 8011 C  C2  . MAN   E  3  .   ? 22.519  -10.774 1.255  1.00 168.64 ? 6   MAN   I C2  1 
HETATM 8012 C  C3  . MAN   E  3  .   ? 21.500  -9.738  0.748  1.00 156.71 ? 6   MAN   I C3  1 
HETATM 8013 C  C4  . MAN   E  3  .   ? 20.305  -10.391 0.059  1.00 149.02 ? 6   MAN   I C4  1 
HETATM 8014 C  C5  . MAN   E  3  .   ? 19.725  -11.506 0.941  1.00 142.90 ? 6   MAN   I C5  1 
HETATM 8015 C  C6  . MAN   E  3  .   ? 18.565  -12.246 0.308  1.00 130.11 ? 6   MAN   I C6  1 
HETATM 8016 O  O2  . MAN   E  3  .   ? 23.349  -11.238 0.194  1.00 172.53 ? 6   MAN   I O2  1 
HETATM 8017 O  O3  . MAN   E  3  .   ? 22.142  -8.833  -0.154 1.00 134.32 ? 6   MAN   I O3  1 
HETATM 8018 O  O4  . MAN   E  3  .   ? 19.301  -9.405  -0.187 1.00 132.51 ? 6   MAN   I O4  1 
HETATM 8019 O  O5  . MAN   E  3  .   ? 20.757  -12.486 1.209  1.00 152.84 ? 6   MAN   I O5  1 
HETATM 8020 O  O6  . MAN   E  3  .   ? 17.749  -12.894 1.309  1.00 105.73 ? 6   MAN   I O6  1 
HETATM 8021 C  C1  . MAN   E  3  .   ? 26.782  -15.587 7.854  1.00 126.29 ? 7   MAN   I C1  1 
HETATM 8022 C  C2  . MAN   E  3  .   ? 27.156  -16.079 6.428  1.00 134.04 ? 7   MAN   I C2  1 
HETATM 8023 C  C3  . MAN   E  3  .   ? 26.620  -17.477 6.047  1.00 139.82 ? 7   MAN   I C3  1 
HETATM 8024 C  C4  . MAN   E  3  .   ? 26.441  -18.398 7.255  1.00 135.31 ? 7   MAN   I C4  1 
HETATM 8025 C  C5  . MAN   E  3  .   ? 25.639  -17.671 8.311  1.00 123.37 ? 7   MAN   I C5  1 
HETATM 8026 C  C6  . MAN   E  3  .   ? 25.165  -18.536 9.467  1.00 107.15 ? 7   MAN   I C6  1 
HETATM 8027 O  O2  . MAN   E  3  .   ? 28.570  -16.013 6.241  1.00 125.95 ? 7   MAN   I O2  1 
HETATM 8028 O  O3  . MAN   E  3  .   ? 27.514  -18.073 5.094  1.00 144.05 ? 7   MAN   I O3  1 
HETATM 8029 O  O4  . MAN   E  3  .   ? 25.747  -19.588 6.900  1.00 136.05 ? 7   MAN   I O4  1 
HETATM 8030 O  O5  . MAN   E  3  .   ? 26.500  -16.638 8.818  1.00 118.99 ? 7   MAN   I O5  1 
HETATM 8031 O  O6  . MAN   E  3  .   ? 26.231  -19.171 10.150 1.00 96.26  ? 7   MAN   I O6  1 
HETATM 8032 C  C1  . NAG   F  4  .   ? 24.514  -11.145 69.349 1.00 68.25  ? 1   NAG   W C1  1 
HETATM 8033 C  C2  . NAG   F  4  .   ? 24.894  -10.281 70.549 1.00 74.58  ? 1   NAG   W C2  1 
HETATM 8034 C  C3  . NAG   F  4  .   ? 25.668  -11.177 71.506 1.00 77.37  ? 1   NAG   W C3  1 
HETATM 8035 C  C4  . NAG   F  4  .   ? 24.755  -12.290 71.995 1.00 87.80  ? 1   NAG   W C4  1 
HETATM 8036 C  C5  . NAG   F  4  .   ? 24.140  -13.049 70.815 1.00 82.86  ? 1   NAG   W C5  1 
HETATM 8037 C  C6  . NAG   F  4  .   ? 23.019  -14.007 71.221 1.00 75.64  ? 1   NAG   W C6  1 
HETATM 8038 C  C7  . NAG   F  4  .   ? 26.313  -8.635  69.349 1.00 79.66  ? 1   NAG   W C7  1 
HETATM 8039 C  C8  . NAG   F  4  .   ? 26.417  -7.151  69.129 1.00 76.35  ? 1   NAG   W C8  1 
HETATM 8040 N  N2  . NAG   F  4  .   ? 25.573  -9.009  70.391 1.00 77.28  ? 1   NAG   W N2  1 
HETATM 8041 O  O3  . NAG   F  4  .   ? 26.169  -10.443 72.607 1.00 77.73  ? 1   NAG   W O3  1 
HETATM 8042 O  O4  . NAG   F  4  .   ? 25.528  -13.184 72.795 1.00 102.36 ? 1   NAG   W O4  1 
HETATM 8043 O  O5  . NAG   F  4  .   ? 23.593  -12.128 69.844 1.00 76.77  ? 1   NAG   W O5  1 
HETATM 8044 O  O6  . NAG   F  4  .   ? 21.944  -13.387 71.965 1.00 57.59  ? 1   NAG   W O6  1 
HETATM 8045 O  O7  . NAG   F  4  .   ? 26.879  -9.457  68.629 1.00 75.98  ? 1   NAG   W O7  1 
HETATM 8046 C  C1  . NAG   F  4  .   ? 24.984  -13.427 74.053 1.00 101.21 ? 2   NAG   W C1  1 
HETATM 8047 C  C2  . NAG   F  4  .   ? 25.418  -14.780 74.604 1.00 102.78 ? 2   NAG   W C2  1 
HETATM 8048 C  C3  . NAG   F  4  .   ? 24.900  -14.930 76.032 1.00 108.55 ? 2   NAG   W C3  1 
HETATM 8049 C  C4  . NAG   F  4  .   ? 25.285  -13.724 76.888 1.00 118.24 ? 2   NAG   W C4  1 
HETATM 8050 C  C5  . NAG   F  4  .   ? 24.729  -12.475 76.207 1.00 111.65 ? 2   NAG   W C5  1 
HETATM 8051 C  C6  . NAG   F  4  .   ? 24.941  -11.162 76.941 1.00 108.94 ? 2   NAG   W C6  1 
HETATM 8052 C  C7  . NAG   F  4  .   ? 25.626  -16.503 72.821 1.00 111.24 ? 2   NAG   W C7  1 
HETATM 8053 C  C8  . NAG   F  4  .   ? 24.850  -17.494 71.998 1.00 111.80 ? 2   NAG   W C8  1 
HETATM 8054 N  N2  . NAG   F  4  .   ? 24.949  -15.901 73.810 1.00 111.75 ? 2   NAG   W N2  1 
HETATM 8055 O  O3  . NAG   F  4  .   ? 25.395  -16.150 76.568 1.00 102.29 ? 2   NAG   W O3  1 
HETATM 8056 O  O4  . NAG   F  4  .   ? 24.739  -13.864 78.215 1.00 130.42 ? 2   NAG   W O4  1 
HETATM 8057 O  O5  . NAG   F  4  .   ? 25.382  -12.374 74.929 1.00 102.51 ? 2   NAG   W O5  1 
HETATM 8058 O  O6  . NAG   F  4  .   ? 26.227  -11.061 77.529 1.00 105.56 ? 2   NAG   W O6  1 
HETATM 8059 O  O7  . NAG   F  4  .   ? 26.809  -16.255 72.596 1.00 88.20  ? 2   NAG   W O7  1 
HETATM 8060 C  C1  . BMA   F  4  .   ? 25.430  -14.409 79.305 1.00 130.09 ? 3   BMA   W C1  1 
HETATM 8061 C  C2  . BMA   F  4  .   ? 24.730  -13.826 80.537 1.00 131.47 ? 3   BMA   W C2  1 
HETATM 8062 C  C3  . BMA   F  4  .   ? 25.259  -14.440 81.824 1.00 133.45 ? 3   BMA   W C3  1 
HETATM 8063 C  C4  . BMA   F  4  .   ? 25.113  -15.950 81.742 1.00 135.60 ? 3   BMA   W C4  1 
HETATM 8064 C  C5  . BMA   F  4  .   ? 25.920  -16.474 80.549 1.00 132.33 ? 3   BMA   W C5  1 
HETATM 8065 C  C6  . BMA   F  4  .   ? 25.803  -17.976 80.383 1.00 128.97 ? 3   BMA   W C6  1 
HETATM 8066 O  O2  . BMA   F  4  .   ? 23.317  -14.012 80.435 1.00 112.66 ? 3   BMA   W O2  1 
HETATM 8067 O  O3  . BMA   F  4  .   ? 24.563  -13.926 82.964 1.00 116.65 ? 3   BMA   W O3  1 
HETATM 8068 O  O4  . BMA   F  4  .   ? 25.561  -16.560 82.958 1.00 124.39 ? 3   BMA   W O4  1 
HETATM 8069 O  O5  . BMA   F  4  .   ? 25.424  -15.859 79.322 1.00 126.56 ? 3   BMA   W O5  1 
HETATM 8070 O  O6  . BMA   F  4  .   ? 26.500  -18.447 79.233 1.00 127.09 ? 3   BMA   W O6  1 
HETATM 8071 C  C1  . NAG   G  5  .   ? 14.988  -30.282 54.845 1.00 44.95  ? 1   NAG   X C1  1 
HETATM 8072 C  C2  . NAG   G  5  .   ? 13.865  -31.236 54.441 1.00 48.26  ? 1   NAG   X C2  1 
HETATM 8073 C  C3  . NAG   G  5  .   ? 14.185  -32.654 54.888 1.00 47.00  ? 1   NAG   X C3  1 
HETATM 8074 C  C4  . NAG   G  5  .   ? 15.551  -33.053 54.344 1.00 44.57  ? 1   NAG   X C4  1 
HETATM 8075 C  C5  . NAG   G  5  .   ? 16.592  -32.060 54.839 1.00 47.52  ? 1   NAG   X C5  1 
HETATM 8076 C  C6  . NAG   G  5  .   ? 17.986  -32.380 54.350 1.00 41.86  ? 1   NAG   X C6  1 
HETATM 8077 C  C7  . NAG   G  5  .   ? 11.560  -30.442 54.124 1.00 57.42  ? 1   NAG   X C7  1 
HETATM 8078 C  C8  . NAG   G  5  .   ? 10.210  -30.342 54.773 1.00 57.10  ? 1   NAG   X C8  1 
HETATM 8079 N  N2  . NAG   G  5  .   ? 12.571  -30.804 54.932 1.00 51.31  ? 1   NAG   X N2  1 
HETATM 8080 O  O3  . NAG   G  5  .   ? 13.149  -33.498 54.417 1.00 45.12  ? 1   NAG   X O3  1 
HETATM 8081 O  O4  . NAG   G  5  .   ? 15.921  -34.315 54.866 1.00 44.19  ? 1   NAG   X O4  1 
HETATM 8082 O  O5  . NAG   G  5  .   ? 16.234  -30.757 54.341 1.00 45.63  ? 1   NAG   X O5  1 
HETATM 8083 O  O6  . NAG   G  5  .   ? 18.002  -32.346 52.936 1.00 41.06  ? 1   NAG   X O6  1 
HETATM 8084 O  O7  . NAG   G  5  .   ? 11.720  -30.199 52.925 1.00 50.05  ? 1   NAG   X O7  1 
HETATM 8085 C  C1  . NAG   G  5  .   ? 15.656  -35.411 54.065 1.00 55.58  ? 2   NAG   X C1  1 
HETATM 8086 C  C2  . NAG   G  5  .   ? 16.718  -36.470 54.325 1.00 58.27  ? 2   NAG   X C2  1 
HETATM 8087 C  C3  . NAG   G  5  .   ? 16.337  -37.813 53.716 1.00 62.77  ? 2   NAG   X C3  1 
HETATM 8088 C  C4  . NAG   G  5  .   ? 14.883  -38.150 54.010 1.00 75.82  ? 2   NAG   X C4  1 
HETATM 8089 C  C5  . NAG   G  5  .   ? 13.992  -36.993 53.556 1.00 74.62  ? 2   NAG   X C5  1 
HETATM 8090 C  C6  . NAG   G  5  .   ? 12.502  -37.195 53.745 1.00 72.88  ? 2   NAG   X C6  1 
HETATM 8091 C  C7  . NAG   G  5  .   ? 19.018  -35.665 54.500 1.00 55.58  ? 2   NAG   X C7  1 
HETATM 8092 C  C8  . NAG   G  5  .   ? 20.249  -35.243 53.745 1.00 48.21  ? 2   NAG   X C8  1 
HETATM 8093 N  N2  . NAG   G  5  .   ? 17.968  -36.025 53.755 1.00 55.07  ? 2   NAG   X N2  1 
HETATM 8094 O  O3  . NAG   G  5  .   ? 17.208  -38.764 54.298 1.00 58.48  ? 2   NAG   X O3  1 
HETATM 8095 O  O4  . NAG   G  5  .   ? 14.550  -39.388 53.363 1.00 91.78  ? 2   NAG   X O4  1 
HETATM 8096 O  O5  . NAG   G  5  .   ? 14.358  -35.884 54.394 1.00 59.67  ? 2   NAG   X O5  1 
HETATM 8097 O  O6  . NAG   G  5  .   ? 12.176  -37.141 55.139 1.00 67.82  ? 2   NAG   X O6  1 
HETATM 8098 O  O7  . NAG   G  5  .   ? 18.964  -35.663 55.728 1.00 46.29  ? 2   NAG   X O7  1 
HETATM 8099 C  C1  . BMA   G  5  .   ? 14.056  -40.331 54.263 1.00 100.56 ? 3   BMA   X C1  1 
HETATM 8100 C  C2  . BMA   G  5  .   ? 13.397  -41.437 53.459 1.00 103.12 ? 3   BMA   X C2  1 
HETATM 8101 C  C3  . BMA   G  5  .   ? 12.800  -42.468 54.427 1.00 115.99 ? 3   BMA   X C3  1 
HETATM 8102 C  C4  . BMA   G  5  .   ? 13.883  -42.976 55.377 1.00 109.76 ? 3   BMA   X C4  1 
HETATM 8103 C  C5  . BMA   G  5  .   ? 14.559  -41.796 56.088 1.00 109.34 ? 3   BMA   X C5  1 
HETATM 8104 C  C6  . BMA   G  5  .   ? 15.727  -42.198 56.963 1.00 117.09 ? 3   BMA   X C6  1 
HETATM 8105 O  O2  . BMA   G  5  .   ? 14.330  -41.945 52.510 1.00 92.95  ? 3   BMA   X O2  1 
HETATM 8106 O  O3  . BMA   G  5  .   ? 12.109  -43.549 53.766 1.00 132.21 ? 3   BMA   X O3  1 
HETATM 8107 O  O4  . BMA   G  5  .   ? 13.336  -43.828 56.395 1.00 94.26  ? 3   BMA   X O4  1 
HETATM 8108 O  O5  . BMA   G  5  .   ? 15.069  -40.880 55.105 1.00 103.61 ? 3   BMA   X O5  1 
HETATM 8109 O  O6  . BMA   G  5  .   ? 16.457  -43.304 56.414 1.00 127.10 ? 3   BMA   X O6  1 
HETATM 8110 C  C1  . MAN   G  5  .   ? 17.735  -43.520 56.953 1.00 123.32 ? 4   MAN   X C1  1 
HETATM 8111 C  C2  . MAN   G  5  .   ? 18.668  -43.787 55.785 1.00 118.50 ? 4   MAN   X C2  1 
HETATM 8112 C  C3  . MAN   G  5  .   ? 18.297  -45.063 55.032 1.00 115.74 ? 4   MAN   X C3  1 
HETATM 8113 C  C4  . MAN   G  5  .   ? 17.987  -46.252 55.954 1.00 118.59 ? 4   MAN   X C4  1 
HETATM 8114 C  C5  . MAN   G  5  .   ? 17.308  -45.897 57.316 1.00 126.08 ? 4   MAN   X C5  1 
HETATM 8115 C  C6  . MAN   G  5  .   ? 17.601  -46.907 58.415 1.00 125.94 ? 4   MAN   X C6  1 
HETATM 8116 O  O2  . MAN   G  5  .   ? 20.012  -43.804 56.260 1.00 103.17 ? 4   MAN   X O2  1 
HETATM 8117 O  O3  . MAN   G  5  .   ? 19.403  -45.404 54.191 1.00 114.34 ? 4   MAN   X O3  1 
HETATM 8118 O  O4  . MAN   G  5  .   ? 17.119  -47.123 55.237 1.00 112.64 ? 4   MAN   X O4  1 
HETATM 8119 O  O5  . MAN   G  5  .   ? 17.764  -44.627 57.852 1.00 124.29 ? 4   MAN   X O5  1 
HETATM 8120 O  O6  . MAN   G  5  .   ? 17.520  -48.276 57.965 1.00 130.26 ? 4   MAN   X O6  1 
HETATM 8121 C  C1  . MAN   G  5  .   ? 19.359  -45.254 52.801 1.00 114.06 ? 5   MAN   X C1  1 
HETATM 8122 C  C2  . MAN   G  5  .   ? 20.486  -46.128 52.276 1.00 112.05 ? 5   MAN   X C2  1 
HETATM 8123 C  C3  . MAN   G  5  .   ? 21.843  -45.592 52.740 1.00 108.81 ? 5   MAN   X C3  1 
HETATM 8124 C  C4  . MAN   G  5  .   ? 22.057  -44.171 52.226 1.00 111.56 ? 5   MAN   X C4  1 
HETATM 8125 C  C5  . MAN   G  5  .   ? 20.835  -43.268 52.556 1.00 114.73 ? 5   MAN   X C5  1 
HETATM 8126 C  C6  . MAN   G  5  .   ? 20.834  -41.990 51.747 1.00 109.84 ? 5   MAN   X C6  1 
HETATM 8127 O  O2  . MAN   G  5  .   ? 20.406  -46.207 50.854 1.00 89.47  ? 5   MAN   X O2  1 
HETATM 8128 O  O3  . MAN   G  5  .   ? 22.886  -46.462 52.287 1.00 96.76  ? 5   MAN   X O3  1 
HETATM 8129 O  O4  . MAN   G  5  .   ? 23.243  -43.617 52.818 1.00 90.39  ? 5   MAN   X O4  1 
HETATM 8130 O  O5  . MAN   G  5  .   ? 19.543  -43.917 52.281 1.00 112.10 ? 5   MAN   X O5  1 
HETATM 8131 O  O6  . MAN   G  5  .   ? 20.226  -40.935 52.480 1.00 105.73 ? 5   MAN   X O6  1 
HETATM 8132 C  C1  . MAN   G  5  .   ? 12.370  -43.986 52.463 1.00 146.63 ? 6   MAN   X C1  1 
HETATM 8133 C  C2  . MAN   G  5  .   ? 11.776  -43.043 51.379 1.00 142.84 ? 6   MAN   X C2  1 
HETATM 8134 C  C3  . MAN   G  5  .   ? 10.329  -43.322 50.983 1.00 144.99 ? 6   MAN   X C3  1 
HETATM 8135 C  C4  . MAN   G  5  .   ? 10.054  -44.811 50.882 1.00 150.63 ? 6   MAN   X C4  1 
HETATM 8136 C  C5  . MAN   G  5  .   ? 10.455  -45.467 52.190 1.00 153.54 ? 6   MAN   X C5  1 
HETATM 8137 C  C6  . MAN   G  5  .   ? 10.125  -46.941 52.259 1.00 150.05 ? 6   MAN   X C6  1 
HETATM 8138 O  O2  . MAN   G  5  .   ? 12.589  -43.078 50.208 1.00 132.22 ? 6   MAN   X O2  1 
HETATM 8139 O  O3  . MAN   G  5  .   ? 10.058  -42.677 49.731 1.00 136.10 ? 6   MAN   X O3  1 
HETATM 8140 O  O4  . MAN   G  5  .   ? 8.670   -45.044 50.630 1.00 144.29 ? 6   MAN   X O4  1 
HETATM 8141 O  O5  . MAN   G  5  .   ? 11.884  -45.340 52.332 1.00 155.10 ? 6   MAN   X O5  1 
HETATM 8142 O  O6  . MAN   G  5  .   ? 8.773   -47.142 52.661 1.00 157.50 ? 6   MAN   X O6  1 
HETATM 8143 C  C1  . NAG   H  6  .   ? -15.926 18.969  32.046 1.00 81.09  ? 1   NAG   j C1  1 
HETATM 8144 C  C2  . NAG   H  6  .   ? -15.596 18.656  33.505 1.00 83.87  ? 1   NAG   j C2  1 
HETATM 8145 C  C3  . NAG   H  6  .   ? -15.457 19.943  34.313 1.00 85.51  ? 1   NAG   j C3  1 
HETATM 8146 C  C4  . NAG   H  6  .   ? -14.636 21.016  33.600 1.00 85.95  ? 1   NAG   j C4  1 
HETATM 8147 C  C5  . NAG   H  6  .   ? -15.009 21.150  32.126 1.00 79.30  ? 1   NAG   j C5  1 
HETATM 8148 C  C6  . NAG   H  6  .   ? -14.072 22.052  31.357 1.00 73.50  ? 1   NAG   j C6  1 
HETATM 8149 C  C7  . NAG   H  6  .   ? -17.858 17.798  33.871 1.00 100.14 ? 1   NAG   j C7  1 
HETATM 8150 C  C8  . NAG   H  6  .   ? -18.476 16.460  33.595 1.00 98.05  ? 1   NAG   j C8  1 
HETATM 8151 N  N2  . NAG   H  6  .   ? -16.553 17.788  34.163 1.00 82.39  ? 1   NAG   j N2  1 
HETATM 8152 O  O3  . NAG   H  6  .   ? -14.828 19.562  35.527 1.00 88.61  ? 1   NAG   j O3  1 
HETATM 8153 O  O4  . NAG   H  6  .   ? -14.889 22.272  34.221 1.00 85.48  ? 1   NAG   j O4  1 
HETATM 8154 O  O5  . NAG   H  6  .   ? -14.937 19.852  31.514 1.00 67.24  ? 1   NAG   j O5  1 
HETATM 8155 O  O6  . NAG   H  6  .   ? -12.714 21.601  31.486 1.00 65.86  ? 1   NAG   j O6  1 
HETATM 8156 O  O7  . NAG   H  6  .   ? -18.506 18.842  33.802 1.00 101.83 ? 1   NAG   j O7  1 
HETATM 8157 C  C1  . NAG   H  6  .   ? -13.814 22.946  34.755 1.00 90.05  ? 2   NAG   j C1  1 
HETATM 8158 C  C2  . NAG   H  6  .   ? -13.902 24.459  34.708 1.00 88.87  ? 2   NAG   j C2  1 
HETATM 8159 C  C3  . NAG   H  6  .   ? -12.589 25.056  35.193 1.00 90.53  ? 2   NAG   j C3  1 
HETATM 8160 C  C4  . NAG   H  6  .   ? -12.282 24.498  36.574 1.00 97.85  ? 2   NAG   j C4  1 
HETATM 8161 C  C5  . NAG   H  6  .   ? -12.092 22.992  36.439 1.00 104.24 ? 2   NAG   j C5  1 
HETATM 8162 C  C6  . NAG   H  6  .   ? -11.706 22.284  37.728 1.00 99.47  ? 2   NAG   j C6  1 
HETATM 8163 C  C7  . NAG   H  6  .   ? -15.477 25.461  33.130 1.00 94.42  ? 2   NAG   j C7  1 
HETATM 8164 C  C8  . NAG   H  6  .   ? -15.550 26.749  32.365 1.00 85.92  ? 2   NAG   j C8  1 
HETATM 8165 N  N2  . NAG   H  6  .   ? -14.250 25.027  33.422 1.00 87.35  ? 2   NAG   j N2  1 
HETATM 8166 O  O3  . NAG   H  6  .   ? -12.697 26.470  35.195 1.00 85.28  ? 2   NAG   j O3  1 
HETATM 8167 O  O4  . NAG   H  6  .   ? -11.108 25.105  37.112 1.00 102.62 ? 2   NAG   j O4  1 
HETATM 8168 O  O5  . NAG   H  6  .   ? -13.348 22.438  35.993 1.00 102.26 ? 2   NAG   j O5  1 
HETATM 8169 O  O6  . NAG   H  6  .   ? -12.822 22.037  38.578 1.00 87.98  ? 2   NAG   j O6  1 
HETATM 8170 O  O7  . NAG   H  6  .   ? -16.483 24.839  33.469 1.00 89.58  ? 2   NAG   j O7  1 
HETATM 8171 C  C1  . BMA   H  6  .   ? -11.338 26.093  38.064 1.00 122.14 ? 3   BMA   j C1  1 
HETATM 8172 C  C2  . BMA   H  6  .   ? -9.999  26.347  38.747 1.00 125.01 ? 3   BMA   j C2  1 
HETATM 8173 C  C3  . BMA   H  6  .   ? -9.967  27.657  39.549 1.00 141.52 ? 3   BMA   j C3  1 
HETATM 8174 C  C4  . BMA   H  6  .   ? -10.623 28.801  38.781 1.00 145.02 ? 3   BMA   j C4  1 
HETATM 8175 C  C5  . BMA   H  6  .   ? -12.023 28.376  38.358 1.00 143.96 ? 3   BMA   j C5  1 
HETATM 8176 C  C6  . BMA   H  6  .   ? -12.841 29.457  37.667 1.00 133.49 ? 3   BMA   j C6  1 
HETATM 8177 O  O2  . BMA   H  6  .   ? -8.955  26.292  37.778 1.00 98.34  ? 3   BMA   j O2  1 
HETATM 8178 O  O3  . BMA   H  6  .   ? -8.610  27.989  39.862 1.00 150.11 ? 3   BMA   j O3  1 
HETATM 8179 O  O4  . BMA   H  6  .   ? -10.692 29.977  39.599 1.00 133.69 ? 3   BMA   j O4  1 
HETATM 8180 O  O5  . BMA   H  6  .   ? -11.859 27.271  37.444 1.00 139.62 ? 3   BMA   j O5  1 
HETATM 8181 O  O6  . BMA   H  6  .   ? -12.133 30.101  36.605 1.00 121.28 ? 3   BMA   j O6  1 
HETATM 8182 C  C1  . MAN   H  6  .   ? -8.156  27.782  41.166 1.00 140.85 ? 4   MAN   j C1  1 
HETATM 8183 C  C2  . MAN   H  6  .   ? -7.014  28.788  41.354 1.00 131.08 ? 4   MAN   j C2  1 
HETATM 8184 C  C3  . MAN   H  6  .   ? -5.700  28.317  40.707 1.00 122.94 ? 4   MAN   j C3  1 
HETATM 8185 C  C4  . MAN   H  6  .   ? -5.372  26.868  41.085 1.00 116.17 ? 4   MAN   j C4  1 
HETATM 8186 C  C5  . MAN   H  6  .   ? -6.563  25.975  40.693 1.00 121.65 ? 4   MAN   j C5  1 
HETATM 8187 C  C6  . MAN   H  6  .   ? -6.386  24.485  40.964 1.00 107.20 ? 4   MAN   j C6  1 
HETATM 8188 O  O2  . MAN   H  6  .   ? -6.866  29.090  42.741 1.00 126.55 ? 4   MAN   j O2  1 
HETATM 8189 O  O3  . MAN   H  6  .   ? -4.644  29.210  41.084 1.00 112.03 ? 4   MAN   j O3  1 
HETATM 8190 O  O4  . MAN   H  6  .   ? -4.188  26.421  40.414 1.00 88.44  ? 4   MAN   j O4  1 
HETATM 8191 O  O5  . MAN   H  6  .   ? -7.743  26.417  41.430 1.00 137.55 ? 4   MAN   j O5  1 
HETATM 8192 O  O6  . MAN   H  6  .   ? -5.323  24.172  41.863 1.00 90.08  ? 4   MAN   j O6  1 
HETATM 8193 C  C1  . NAG   I  4  .   ? -18.055 27.800  7.754  1.00 76.88  ? 1   NAG   l C1  1 
HETATM 8194 C  C2  . NAG   I  4  .   ? -17.314 28.432  6.583  1.00 75.78  ? 1   NAG   l C2  1 
HETATM 8195 C  C3  . NAG   I  4  .   ? -17.447 29.950  6.645  1.00 83.76  ? 1   NAG   l C3  1 
HETATM 8196 C  C4  . NAG   I  4  .   ? -18.921 30.342  6.727  1.00 89.56  ? 1   NAG   l C4  1 
HETATM 8197 C  C5  . NAG   I  4  .   ? -19.596 29.607  7.883  1.00 89.52  ? 1   NAG   l C5  1 
HETATM 8198 C  C6  . NAG   I  4  .   ? -21.082 29.864  7.977  1.00 83.97  ? 1   NAG   l C6  1 
HETATM 8199 C  C7  . NAG   I  4  .   ? -15.390 27.311  5.576  1.00 79.80  ? 1   NAG   l C7  1 
HETATM 8200 C  C8  . NAG   I  4  .   ? -14.002 27.700  5.170  1.00 81.76  ? 1   NAG   l C8  1 
HETATM 8201 N  N2  . NAG   I  4  .   ? -15.928 28.018  6.572  1.00 75.36  ? 1   NAG   l N2  1 
HETATM 8202 O  O3  . NAG   I  4  .   ? -16.796 30.527  5.516  1.00 65.47  ? 1   NAG   l O3  1 
HETATM 8203 O  O4  . NAG   I  4  .   ? -19.060 31.743  6.952  1.00 109.09 ? 1   NAG   l O4  1 
HETATM 8204 O  O5  . NAG   I  4  .   ? -19.427 28.185  7.705  1.00 83.98  ? 1   NAG   l O5  1 
HETATM 8205 O  O6  . NAG   I  4  .   ? -21.817 28.927  7.184  1.00 78.30  ? 1   NAG   l O6  1 
HETATM 8206 O  O7  . NAG   I  4  .   ? -15.996 26.392  5.030  1.00 71.23  ? 1   NAG   l O7  1 
HETATM 8207 C  C1  . NAG   I  4  .   ? -19.760 32.418  5.957  1.00 126.61 ? 2   NAG   l C1  1 
HETATM 8208 C  C2  . NAG   I  4  .   ? -20.390 33.685  6.550  1.00 130.63 ? 2   NAG   l C2  1 
HETATM 8209 C  C3  . NAG   I  4  .   ? -20.232 34.957  5.706  1.00 135.24 ? 2   NAG   l C3  1 
HETATM 8210 C  C4  . NAG   I  4  .   ? -19.144 34.907  4.636  1.00 144.81 ? 2   NAG   l C4  1 
HETATM 8211 C  C5  . NAG   I  4  .   ? -19.214 33.564  3.931  1.00 134.33 ? 2   NAG   l C5  1 
HETATM 8212 C  C6  . NAG   I  4  .   ? -18.290 33.431  2.740  1.00 122.54 ? 2   NAG   l C6  1 
HETATM 8213 C  C7  . NAG   I  4  .   ? -22.453 33.520  7.972  1.00 129.07 ? 2   NAG   l C7  1 
HETATM 8214 C  C8  . NAG   I  4  .   ? -23.798 32.851  8.046  1.00 115.04 ? 2   NAG   l C8  1 
HETATM 8215 N  N2  . NAG   I  4  .   ? -21.810 33.462  6.791  1.00 138.93 ? 2   NAG   l N2  1 
HETATM 8216 O  O3  . NAG   I  4  .   ? -19.959 35.995  6.635  1.00 130.92 ? 2   NAG   l O3  1 
HETATM 8217 O  O4  . NAG   I  4  .   ? -19.286 35.937  3.638  1.00 165.35 ? 2   NAG   l O4  1 
HETATM 8218 O  O5  . NAG   I  4  .   ? -18.792 32.627  4.929  1.00 132.04 ? 2   NAG   l O5  1 
HETATM 8219 O  O6  . NAG   I  4  .   ? -18.528 32.219  2.036  1.00 112.10 ? 2   NAG   l O6  1 
HETATM 8220 O  O7  . NAG   I  4  .   ? -21.976 34.095  8.945  1.00 108.00 ? 2   NAG   l O7  1 
HETATM 8221 C  C1  . BMA   I  4  .   ? -19.959 37.142  3.841  1.00 176.95 ? 3   BMA   l C1  1 
HETATM 8222 C  C2  . BMA   I  4  .   ? -19.022 38.304  3.595  1.00 172.86 ? 3   BMA   l C2  1 
HETATM 8223 C  C3  . BMA   I  4  .   ? -19.739 39.597  3.941  1.00 165.77 ? 3   BMA   l C3  1 
HETATM 8224 C  C4  . BMA   I  4  .   ? -21.040 39.723  3.148  1.00 173.71 ? 3   BMA   l C4  1 
HETATM 8225 C  C5  . BMA   I  4  .   ? -21.907 38.451  3.286  1.00 170.02 ? 3   BMA   l C5  1 
HETATM 8226 C  C6  . BMA   I  4  .   ? -23.084 38.406  2.333  1.00 156.82 ? 3   BMA   l C6  1 
HETATM 8227 O  O2  . BMA   I  4  .   ? -18.548 38.296  2.248  1.00 161.52 ? 3   BMA   l O2  1 
HETATM 8228 O  O3  . BMA   I  4  .   ? -18.882 40.705  3.677  1.00 141.75 ? 3   BMA   l O3  1 
HETATM 8229 O  O4  . BMA   I  4  .   ? -21.777 40.860  3.618  1.00 169.26 ? 3   BMA   l O4  1 
HETATM 8230 O  O5  . BMA   I  4  .   ? -21.108 37.278  2.992  1.00 175.88 ? 3   BMA   l O5  1 
HETATM 8231 O  O6  . BMA   I  4  .   ? -24.126 39.289  2.726  1.00 150.37 ? 3   BMA   l O6  1 
HETATM 8232 C  C2  . A1IUB J  7  .   ? 43.964  -0.975  32.085 0.80 73.45  ? 401 A1IUB A C2  1 
HETATM 8233 C  C4  . A1IUB J  7  .   ? 43.766  -1.322  34.525 0.80 67.78  ? 401 A1IUB A C4  1 
HETATM 8234 C  C5  . A1IUB J  7  .   ? 44.976  -2.215  34.284 0.80 70.01  ? 401 A1IUB A C5  1 
HETATM 8235 C  C6  . A1IUB J  7  .   ? 45.975  -1.696  33.230 0.80 79.82  ? 401 A1IUB A C6  1 
HETATM 8236 C  C8  . A1IUB J  7  .   ? 45.547  -2.433  30.964 0.80 71.86  ? 401 A1IUB A C8  1 
HETATM 8237 C  C9  . A1IUB J  7  .   ? 45.904  -2.303  29.709 0.80 60.40  ? 401 A1IUB A C9  1 
HETATM 8238 C  C10 . A1IUB J  7  .   ? 46.131  -3.477  28.887 0.80 60.42  ? 401 A1IUB A C10 1 
HETATM 8239 O  O11 . A1IUB J  7  .   ? 45.977  -3.398  27.674 0.80 71.62  ? 401 A1IUB A O11 1 
HETATM 8240 C  C12 . A1IUB J  7  .   ? 46.509  -4.791  29.533 0.80 57.81  ? 401 A1IUB A C12 1 
HETATM 8241 C  C1  . A1IUB J  7  .   ? 43.205  -1.111  30.798 0.80 76.19  ? 401 A1IUB A C1  1 
HETATM 8242 C  C3  . A1IUB J  7  .   ? 43.423  -0.667  33.254 0.80 65.03  ? 401 A1IUB A C3  1 
HETATM 8243 C  C7  . A1IUB J  7  .   ? 45.359  -1.324  31.957 0.80 75.26  ? 401 A1IUB A C7  1 
HETATM 8244 C  C13 . A1IUB J  7  .   ? 46.742  -0.489  33.792 0.80 86.75  ? 401 A1IUB A C13 1 
HETATM 8245 C  C14 . A1IUB J  7  .   ? 46.981  -2.819  32.945 0.80 84.48  ? 401 A1IUB A C14 1 
HETATM 8246 C  C2  . A1IUB K  7  .   ? 49.916  -5.135  27.837 0.80 79.48  ? 402 A1IUB A C2  1 
HETATM 8247 C  C4  . A1IUB K  7  .   ? 49.855  -5.821  25.404 0.80 73.33  ? 402 A1IUB A C4  1 
HETATM 8248 C  C5  . A1IUB K  7  .   ? 49.154  -4.505  25.084 0.80 70.79  ? 402 A1IUB A C5  1 
HETATM 8249 C  C6  . A1IUB K  7  .   ? 49.475  -3.399  26.097 0.80 74.44  ? 402 A1IUB A C6  1 
HETATM 8250 C  C8  . A1IUB K  7  .   ? 49.753  -2.720  28.511 0.80 66.36  ? 402 A1IUB A C8  1 
HETATM 8251 C  C9  . A1IUB K  7  .   ? 49.067  -2.352  29.582 0.80 67.80  ? 402 A1IUB A C9  1 
HETATM 8252 C  C10 . A1IUB K  7  .   ? 49.404  -1.243  30.482 0.80 70.59  ? 402 A1IUB A C10 1 
HETATM 8253 O  O11 . A1IUB K  7  .   ? 48.751  -1.064  31.532 0.80 77.38  ? 402 A1IUB A O11 1 
HETATM 8254 C  C12 . A1IUB K  7  .   ? 50.540  -0.319  30.148 0.80 65.98  ? 402 A1IUB A C12 1 
HETATM 8255 C  C1  . A1IUB K  7  .   ? 50.161  -5.428  29.298 0.80 70.62  ? 402 A1IUB A C1  1 
HETATM 8256 C  C3  . A1IUB K  7  .   ? 50.164  -6.020  26.871 0.80 74.31  ? 402 A1IUB A C3  1 
HETATM 8257 C  C7  . A1IUB K  7  .   ? 49.321  -3.799  27.554 0.80 68.43  ? 402 A1IUB A C7  1 
HETATM 8258 C  C13 . A1IUB K  7  .   ? 50.917  -2.967  25.842 0.80 84.37  ? 402 A1IUB A C13 1 
HETATM 8259 C  C14 . A1IUB K  7  .   ? 48.534  -2.238  25.782 0.80 77.75  ? 402 A1IUB A C14 1 
HETATM 8260 C  C1  . GOL   L  8  .   ? 24.367  9.214   19.175 1.00 66.08  ? 403 GOL   A C1  1 
HETATM 8261 O  O1  . GOL   L  8  .   ? 23.752  9.883   20.271 1.00 73.39  ? 403 GOL   A O1  1 
HETATM 8262 C  C2  . GOL   L  8  .   ? 25.545  8.374   19.616 1.00 55.70  ? 403 GOL   A C2  1 
HETATM 8263 O  O2  . GOL   L  8  .   ? 25.808  7.406   18.610 1.00 54.69  ? 403 GOL   A O2  1 
HETATM 8264 C  C3  . GOL   L  8  .   ? 26.840  9.127   19.784 1.00 60.51  ? 403 GOL   A C3  1 
HETATM 8265 O  O3  . GOL   L  8  .   ? 27.896  8.442   19.101 1.00 59.47  ? 403 GOL   A O3  1 
HETATM 8266 C  CHA . HEM   M  9  .   ? 40.253  1.435   35.139 1.00 26.82  ? 404 HEM   A CHA 1 
HETATM 8267 C  CHB . HEM   M  9  .   ? 44.251  0.790   37.694 1.00 26.85  ? 404 HEM   A CHB 1 
HETATM 8268 C  CHC . HEM   M  9  .   ? 43.529  -4.028  37.625 1.00 27.00  ? 404 HEM   A CHC 1 
HETATM 8269 C  CHD . HEM   M  9  .   ? 39.332  -3.342  35.332 1.00 24.72  ? 404 HEM   A CHD 1 
HETATM 8270 C  C1A . HEM   M  9  .   ? 41.409  1.655   35.863 1.00 24.11  ? 404 HEM   A C1A 1 
HETATM 8271 C  C2A . HEM   M  9  .   ? 41.952  2.931   36.094 1.00 27.02  ? 404 HEM   A C2A 1 
HETATM 8272 C  C3A . HEM   M  9  .   ? 43.083  2.770   36.803 1.00 28.84  ? 404 HEM   A C3A 1 
HETATM 8273 C  C4A . HEM   M  9  .   ? 43.244  1.372   37.011 1.00 29.06  ? 404 HEM   A C4A 1 
HETATM 8274 C  CMA . HEM   M  9  .   ? 44.001  3.865   37.252 1.00 29.56  ? 404 HEM   A CMA 1 
HETATM 8275 C  CAA . HEM   M  9  .   ? 41.374  4.244   35.640 1.00 27.06  ? 404 HEM   A CAA 1 
HETATM 8276 C  CBA . HEM   M  9  .   ? 41.786  4.468   34.234 1.00 30.18  ? 404 HEM   A CBA 1 
HETATM 8277 C  CGA . HEM   M  9  .   ? 41.573  5.912   33.798 1.00 36.22  ? 404 HEM   A CGA 1 
HETATM 8278 O  O1A . HEM   M  9  .   ? 42.362  6.378   32.909 1.00 38.27  ? 404 HEM   A O1A 1 
HETATM 8279 O  O2A . HEM   M  9  .   ? 40.675  6.695   34.196 1.00 32.06  ? 404 HEM   A O2A 1 
HETATM 8280 C  C1B . HEM   M  9  .   ? 44.378  -0.577  37.826 1.00 28.63  ? 404 HEM   A C1B 1 
HETATM 8281 C  C2B . HEM   M  9  .   ? 45.522  -1.168  38.437 1.00 28.51  ? 404 HEM   A C2B 1 
HETATM 8282 C  C3B . HEM   M  9  .   ? 45.337  -2.523  38.446 1.00 27.51  ? 404 HEM   A C3B 1 
HETATM 8283 C  C4B . HEM   M  9  .   ? 44.087  -2.770  37.760 1.00 27.59  ? 404 HEM   A C4B 1 
HETATM 8284 C  CMB . HEM   M  9  .   ? 46.717  -0.481  39.059 1.00 28.94  ? 404 HEM   A CMB 1 
HETATM 8285 C  CAB . HEM   M  9  .   ? 46.336  -3.428  38.981 1.00 30.93  ? 404 HEM   A CAB 1 
HETATM 8286 C  CBB . HEM   M  9  .   ? 46.386  -4.713  38.699 1.00 34.58  ? 404 HEM   A CBB 1 
HETATM 8287 C  C1C . HEM   M  9  .   ? 42.294  -4.264  37.038 1.00 26.89  ? 404 HEM   A C1C 1 
HETATM 8288 C  C2C . HEM   M  9  .   ? 41.624  -5.508  36.971 1.00 28.41  ? 404 HEM   A C2C 1 
HETATM 8289 C  C3C . HEM   M  9  .   ? 40.455  -5.265  36.279 1.00 28.08  ? 404 HEM   A C3C 1 
HETATM 8290 C  C4C . HEM   M  9  .   ? 40.370  -3.899  36.010 1.00 26.09  ? 404 HEM   A C4C 1 
HETATM 8291 C  CMC . HEM   M  9  .   ? 42.119  -6.847  37.460 1.00 27.49  ? 404 HEM   A CMC 1 
HETATM 8292 C  CAC . HEM   M  9  .   ? 39.352  -6.133  35.931 1.00 29.53  ? 404 HEM   A CAC 1 
HETATM 8293 C  CBC . HEM   M  9  .   ? 39.070  -7.138  36.705 1.00 37.46  ? 404 HEM   A CBC 1 
HETATM 8294 C  C1D . HEM   M  9  .   ? 39.310  -1.969  35.044 1.00 26.21  ? 404 HEM   A C1D 1 
HETATM 8295 C  C2D . HEM   M  9  .   ? 38.285  -1.378  34.193 1.00 24.36  ? 404 HEM   A C2D 1 
HETATM 8296 C  C3D . HEM   M  9  .   ? 38.521  -0.059  34.179 1.00 25.03  ? 404 HEM   A C3D 1 
HETATM 8297 C  C4D . HEM   M  9  .   ? 39.716  0.152   34.968 1.00 25.87  ? 404 HEM   A C4D 1 
HETATM 8298 C  CMD . HEM   M  9  .   ? 37.091  -2.051  33.487 1.00 25.04  ? 404 HEM   A CMD 1 
HETATM 8299 C  CAD . HEM   M  9  .   ? 37.710  0.989   33.418 1.00 25.07  ? 404 HEM   A CAD 1 
HETATM 8300 C  CBD . HEM   M  9  .   ? 36.661  1.680   34.286 1.00 26.47  ? 404 HEM   A CBD 1 
HETATM 8301 C  CGD . HEM   M  9  .   ? 35.795  2.638   33.483 1.00 27.63  ? 404 HEM   A CGD 1 
HETATM 8302 O  O1D . HEM   M  9  .   ? 36.236  3.229   32.457 1.00 30.54  ? 404 HEM   A O1D 1 
HETATM 8303 O  O2D . HEM   M  9  .   ? 34.588  2.831   33.824 1.00 28.85  ? 404 HEM   A O2D 1 
HETATM 8304 N  NA  . HEM   M  9  .   ? 42.189  0.716   36.464 1.00 26.65  ? 404 HEM   A NA  1 
HETATM 8305 N  NB  . HEM   M  9  .   ? 43.538  -1.541  37.477 1.00 26.85  ? 404 HEM   A NB  1 
HETATM 8306 N  NC  . HEM   M  9  .   ? 41.516  -3.321  36.461 1.00 26.74  ? 404 HEM   A NC  1 
HETATM 8307 N  ND  . HEM   M  9  .   ? 40.153  -1.022  35.494 1.00 24.71  ? 404 HEM   A ND  1 
HETATM 8308 FE FE  . HEM   M  9  .   ? 41.689  -1.233  36.591 1.00 25.41  ? 404 HEM   A FE  1 
HETATM 8309 MG MG  . MG    N  10 .   ? 39.260  7.887   33.587 1.00 49.86  ? 405 MG    A MG  1 
HETATM 8310 S  S   . SO4   O  11 .   ? 61.023  5.021   18.492 1.00 94.15  ? 406 SO4   A S   1 
HETATM 8311 O  O1  . SO4   O  11 .   ? 62.420  4.704   18.676 1.00 94.76  ? 406 SO4   A O1  1 
HETATM 8312 O  O2  . SO4   O  11 .   ? 60.775  5.271   17.082 1.00 87.36  ? 406 SO4   A O2  1 
HETATM 8313 O  O3  . SO4   O  11 .   ? 60.213  3.904   18.953 1.00 82.72  ? 406 SO4   A O3  1 
HETATM 8314 O  O4  . SO4   O  11 .   ? 60.709  6.213   19.261 1.00 81.52  ? 406 SO4   A O4  1 
HETATM 8315 C  C2  . A1IUB P  7  .   ? -0.471  -12.414 61.049 0.90 78.33  ? 401 A1IUB B C2  1 
HETATM 8316 C  C4  . A1IUB P  7  .   ? 1.129   -11.483 62.735 0.90 82.45  ? 401 A1IUB B C4  1 
HETATM 8317 C  C5  . A1IUB P  7  .   ? 1.641   -12.910 62.928 0.90 88.67  ? 401 A1IUB B C5  1 
HETATM 8318 C  C6  . A1IUB P  7  .   ? 1.494   -13.884 61.747 0.90 79.34  ? 401 A1IUB B C6  1 
HETATM 8319 C  C8  . A1IUB P  7  .   ? -0.996  -14.379 62.280 0.90 58.97  ? 401 A1IUB B C8  1 
HETATM 8320 C  C9  . A1IUB P  7  .   ? -1.703  -15.494 62.173 0.90 62.03  ? 401 A1IUB B C9  1 
HETATM 8321 C  C10 . A1IUB P  7  .   ? -2.357  -16.082 60.983 0.90 70.65  ? 401 A1IUB B C10 1 
HETATM 8322 O  O11 . A1IUB P  7  .   ? -2.690  -17.286 60.987 0.90 74.28  ? 401 A1IUB B O11 1 
HETATM 8323 C  C12 . A1IUB P  7  .   ? -2.654  -15.249 59.770 0.90 74.38  ? 401 A1IUB B C12 1 
HETATM 8324 C  C1  . A1IUB P  7  .   ? -1.430  -12.212 59.901 0.90 60.13  ? 401 A1IUB B C1  1 
HETATM 8325 C  C3  . A1IUB P  7  .   ? -0.054  -11.419 61.826 0.90 80.63  ? 401 A1IUB B C3  1 
HETATM 8326 C  C7  . A1IUB P  7  .   ? -0.032  -13.806 61.281 0.90 75.01  ? 401 A1IUB B C7  1 
HETATM 8327 C  C13 . A1IUB P  7  .   ? 2.476   -13.459 60.649 0.90 76.23  ? 401 A1IUB B C13 1 
HETATM 8328 C  C14 . A1IUB P  7  .   ? 1.863   -15.313 62.165 0.90 80.80  ? 401 A1IUB B C14 1 
HETATM 8329 C  C1  . GOL   Q  8  .   ? 22.622  -24.721 69.973 1.00 67.43  ? 402 GOL   B C1  1 
HETATM 8330 O  O1  . GOL   Q  8  .   ? 23.922  -24.462 69.438 1.00 54.90  ? 402 GOL   B O1  1 
HETATM 8331 C  C2  . GOL   Q  8  .   ? 22.157  -26.166 69.849 1.00 56.82  ? 402 GOL   B C2  1 
HETATM 8332 O  O2  . GOL   Q  8  .   ? 23.148  -27.066 70.325 1.00 57.19  ? 402 GOL   B O2  1 
HETATM 8333 C  C3  . GOL   Q  8  .   ? 20.857  -26.417 70.589 1.00 61.11  ? 402 GOL   B C3  1 
HETATM 8334 O  O3  . GOL   Q  8  .   ? 20.463  -27.780 70.520 1.00 60.79  ? 402 GOL   B O3  1 
HETATM 8335 C  C   . ACT   R  12 .   ? 5.363   -10.096 60.919 1.00 52.94  ? 403 ACT   B C   1 
HETATM 8336 O  O   . ACT   R  12 .   ? 5.322   -11.159 61.643 1.00 53.40  ? 403 ACT   B O   1 
HETATM 8337 O  OXT . ACT   R  12 .   ? 4.344   -9.431  60.617 1.00 54.27  ? 403 ACT   B OXT 1 
HETATM 8338 C  CH3 . ACT   R  12 .   ? 6.694   -9.608  60.316 1.00 45.98  ? 403 ACT   B CH3 1 
HETATM 8339 C  CHA . HEM   S  9  .   ? 10.521  -9.432  61.688 1.00 29.44  ? 404 HEM   B CHA 1 
HETATM 8340 C  CHB . HEM   S  9  .   ? 7.349   -5.863  61.034 1.00 31.75  ? 404 HEM   B CHB 1 
HETATM 8341 C  CHC . HEM   S  9  .   ? 6.508   -7.550  56.554 1.00 31.60  ? 404 HEM   B CHC 1 
HETATM 8342 C  CHD . HEM   S  9  .   ? 9.961   -10.894 57.166 1.00 32.09  ? 404 HEM   B CHD 1 
HETATM 8343 C  C1A . HEM   S  9  .   ? 9.717   -8.347  61.853 1.00 30.05  ? 404 HEM   B C1A 1 
HETATM 8344 C  C2A . HEM   S  9  .   ? 9.686   -7.584  63.047 1.00 28.06  ? 404 HEM   B C2A 1 
HETATM 8345 C  C3A . HEM   S  9  .   ? 8.807   -6.567  62.865 1.00 29.66  ? 404 HEM   B C3A 1 
HETATM 8346 C  C4A . HEM   S  9  .   ? 8.282   -6.697  61.566 1.00 30.66  ? 404 HEM   B C4A 1 
HETATM 8347 C  CMA . HEM   S  9  .   ? 8.454   -5.488  63.868 1.00 33.22  ? 404 HEM   B CMA 1 
HETATM 8348 C  CAA . HEM   S  9  .   ? 10.509  -7.817  64.288 1.00 31.72  ? 404 HEM   B CAA 1 
HETATM 8349 C  CBA . HEM   S  9  .   ? 9.813   -8.897  65.087 1.00 33.73  ? 404 HEM   B CBA 1 
HETATM 8350 C  CGA . HEM   S  9  .   ? 10.354  -9.045  66.495 1.00 37.51  ? 404 HEM   B CGA 1 
HETATM 8351 O  O1A . HEM   S  9  .   ? 11.561  -8.847  66.840 1.00 34.32  ? 404 HEM   B O1A 1 
HETATM 8352 O  O2A . HEM   S  9  .   ? 9.525   -9.441  67.390 1.00 38.96  ? 404 HEM   B O2A 1 
HETATM 8353 C  C1B . HEM   S  9  .   ? 6.833   -6.082  59.760 1.00 30.70  ? 404 HEM   B C1B 1 
HETATM 8354 C  C2B . HEM   S  9  .   ? 5.778   -5.273  59.254 1.00 29.82  ? 404 HEM   B C2B 1 
HETATM 8355 C  C3B . HEM   S  9  .   ? 5.550   -5.713  57.979 1.00 29.41  ? 404 HEM   B C3B 1 
HETATM 8356 C  C4B . HEM   S  9  .   ? 6.461   -6.862  57.745 1.00 29.43  ? 404 HEM   B C4B 1 
HETATM 8357 C  CMB . HEM   S  9  .   ? 5.132   -4.065  59.889 1.00 29.83  ? 404 HEM   B CMB 1 
HETATM 8358 C  CAB . HEM   S  9  .   ? 4.508   -5.174  57.118 1.00 32.26  ? 404 HEM   B CAB 1 
HETATM 8359 C  CBB . HEM   S  9  .   ? 3.880   -5.915  56.198 1.00 36.15  ? 404 HEM   B CBB 1 
HETATM 8360 C  C1C . HEM   S  9  .   ? 7.394   -8.571  56.300 1.00 32.52  ? 404 HEM   B C1C 1 
HETATM 8361 C  C2C . HEM   S  9  .   ? 7.616   -9.179  55.054 1.00 29.01  ? 404 HEM   B C2C 1 
HETATM 8362 C  C3C . HEM   S  9  .   ? 8.568   -10.158 55.274 1.00 28.25  ? 404 HEM   B C3C 1 
HETATM 8363 C  C4C . HEM   S  9  .   ? 8.984   -10.058 56.606 1.00 31.33  ? 404 HEM   B C4C 1 
HETATM 8364 C  CMC . HEM   S  9  .   ? 6.828   -8.892  53.794 1.00 33.84  ? 404 HEM   B CMC 1 
HETATM 8365 C  CAC . HEM   S  9  .   ? 9.245   -11.095 54.366 1.00 33.25  ? 404 HEM   B CAC 1 
HETATM 8366 C  CBC . HEM   S  9  .   ? 9.309   -10.826 53.076 1.00 38.17  ? 404 HEM   B CBC 1 
HETATM 8367 C  C1D . HEM   S  9  .   ? 10.329  -10.758 58.495 1.00 26.75  ? 404 HEM   B C1D 1 
HETATM 8368 C  C2D . HEM   S  9  .   ? 11.241  -11.690 59.085 1.00 28.05  ? 404 HEM   B C2D 1 
HETATM 8369 C  C3D . HEM   S  9  .   ? 11.426  -11.283 60.314 1.00 29.25  ? 404 HEM   B C3D 1 
HETATM 8370 C  C4D . HEM   S  9  .   ? 10.573  -10.097 60.486 1.00 29.00  ? 404 HEM   B C4D 1 
HETATM 8371 C  CMD . HEM   S  9  .   ? 11.927  -12.859 58.432 1.00 31.07  ? 404 HEM   B CMD 1 
HETATM 8372 C  CAD . HEM   S  9  .   ? 12.340  -11.936 61.330 1.00 28.31  ? 404 HEM   B CAD 1 
HETATM 8373 C  CBD . HEM   S  9  .   ? 13.735  -11.267 61.389 1.00 28.49  ? 404 HEM   B CBD 1 
HETATM 8374 C  CGD . HEM   S  9  .   ? 14.613  -12.063 62.307 1.00 29.90  ? 404 HEM   B CGD 1 
HETATM 8375 O  O1D . HEM   S  9  .   ? 15.805  -12.222 62.076 1.00 32.81  ? 404 HEM   B O1D 1 
HETATM 8376 O  O2D . HEM   S  9  .   ? 14.165  -12.633 63.312 1.00 32.62  ? 404 HEM   B O2D 1 
HETATM 8377 N  NA  . HEM   S  9  .   ? 8.867   -7.779  60.934 1.00 25.85  ? 404 HEM   B NA  1 
HETATM 8378 N  NB  . HEM   S  9  .   ? 7.217   -6.978  58.840 1.00 27.90  ? 404 HEM   B NB  1 
HETATM 8379 N  NC  . HEM   S  9  .   ? 8.245   -9.084  57.232 1.00 27.75  ? 404 HEM   B NC  1 
HETATM 8380 N  ND  . HEM   S  9  .   ? 9.948   -9.824  59.348 1.00 28.60  ? 404 HEM   B ND  1 
HETATM 8381 FE FE  . HEM   S  9  .   ? 8.717   -8.377  59.071 1.00 27.68  ? 404 HEM   B FE  1 
HETATM 8382 MG MG  . MG    T  10 .   ? 13.053  -9.348  68.142 1.00 49.86  ? 405 MG    B MG  1 
HETATM 8383 S  S   . SO4   U  11 .   ? -11.584 -16.761 75.349 1.00 98.43  ? 406 SO4   B S   1 
HETATM 8384 O  O1  . SO4   U  11 .   ? -10.969 -16.006 76.423 1.00 97.09  ? 406 SO4   B O1  1 
HETATM 8385 O  O2  . SO4   U  11 .   ? -12.806 -16.095 74.930 1.00 95.53  ? 406 SO4   B O2  1 
HETATM 8386 O  O3  . SO4   U  11 .   ? -10.670 -16.832 74.226 1.00 93.83  ? 406 SO4   B O3  1 
HETATM 8387 O  O4  . SO4   U  11 .   ? -11.878 -18.106 75.810 1.00 89.60  ? 406 SO4   B O4  1 
HETATM 8388 C  C2  . A1IUB V  7  .   ? -4.834  12.292  16.380 0.80 80.62  ? 401 A1IUB C C2  1 
HETATM 8389 C  C4  . A1IUB V  7  .   ? -5.720  9.984   16.628 0.80 73.84  ? 401 A1IUB C C4  1 
HETATM 8390 C  C5  . A1IUB V  7  .   ? -4.877  9.678   15.397 0.80 74.07  ? 401 A1IUB C C5  1 
HETATM 8391 C  C6  . A1IUB V  7  .   ? -3.661  10.612  15.255 0.80 79.94  ? 401 A1IUB C C6  1 
HETATM 8392 C  C8  . A1IUB V  7  .   ? -3.047  12.945  14.800 0.80 76.68  ? 401 A1IUB C C8  1 
HETATM 8393 C  C9  . A1IUB V  7  .   ? -3.112  13.899  13.877 0.80 73.98  ? 401 A1IUB C C9  1 
HETATM 8394 C  C10 . A1IUB V  7  .   ? -1.905  14.683  13.526 0.80 82.74  ? 401 A1IUB C C10 1 
HETATM 8395 O  O11 . A1IUB V  7  .   ? -0.784  14.261  13.867 0.80 99.62  ? 401 A1IUB C O11 1 
HETATM 8396 C  C12 . A1IUB V  7  .   ? -1.982  15.949  12.716 0.80 78.67  ? 401 A1IUB C C12 1 
HETATM 8397 C  C1  . A1IUB V  7  .   ? -4.484  13.636  16.929 0.80 88.67  ? 401 A1IUB C C1  1 
HETATM 8398 C  C3  . A1IUB V  7  .   ? -5.686  11.435  16.926 0.80 77.67  ? 401 A1IUB C C3  1 
HETATM 8399 C  C7  . A1IUB V  7  .   ? -4.130  11.985  15.210 0.80 78.96  ? 401 A1IUB C C7  1 
HETATM 8400 C  C13 . A1IUB V  7  .   ? -2.661  10.396  16.406 0.80 83.13  ? 401 A1IUB C C13 1 
HETATM 8401 C  C14 . A1IUB V  7  .   ? -2.946  10.319  13.954 0.80 81.61  ? 401 A1IUB C C14 1 
HETATM 8402 C  C1  . GOL   W  8  .   ? -15.365 31.043  25.207 1.00 80.52  ? 402 GOL   C C1  1 
HETATM 8403 O  O1  . GOL   W  8  .   ? -16.411 30.073  25.346 1.00 69.28  ? 402 GOL   C O1  1 
HETATM 8404 C  C2  . GOL   W  8  .   ? -15.793 32.263  24.398 1.00 83.33  ? 402 GOL   C C2  1 
HETATM 8405 O  O2  . GOL   W  8  .   ? -16.963 32.849  24.967 1.00 79.41  ? 402 GOL   C O2  1 
HETATM 8406 C  C3  . GOL   W  8  .   ? -14.736 33.343  24.274 1.00 82.87  ? 402 GOL   C C3  1 
HETATM 8407 O  O3  . GOL   W  8  .   ? -13.611 32.908  23.513 1.00 83.87  ? 402 GOL   C O3  1 
HETATM 8408 C  C2  . A1IUB X  7  .   ? -2.103  12.209  11.123 0.80 60.33  ? 403 A1IUB C C2  1 
HETATM 8409 C  C4  . A1IUB X  7  .   ? -1.917  9.840   11.900 0.80 54.20  ? 403 A1IUB C C4  1 
HETATM 8410 C  C5  . A1IUB X  7  .   ? -0.502  10.188  12.343 0.80 61.28  ? 403 A1IUB C C5  1 
HETATM 8411 C  C6  . A1IUB X  7  .   ? 0.206   11.174  11.395 0.80 69.52  ? 403 A1IUB C C6  1 
HETATM 8412 C  C8  . A1IUB X  7  .   ? 0.104   13.450  10.420 0.80 75.91  ? 403 A1IUB C C8  1 
HETATM 8413 C  C9  . A1IUB X  7  .   ? 0.806   14.523  10.770 0.80 76.38  ? 403 A1IUB C C9  1 
HETATM 8414 C  C10 . A1IUB X  7  .   ? 1.317   15.516  9.788  0.80 81.10  ? 403 A1IUB C C10 1 
HETATM 8415 O  O11 . A1IUB X  7  .   ? 1.580   16.685  10.136 0.80 69.60  ? 403 A1IUB C O11 1 
HETATM 8416 C  C12 . A1IUB X  7  .   ? 1.414   15.157  8.330  0.80 80.82  ? 403 A1IUB C C12 1 
HETATM 8417 C  C1  . A1IUB X  7  .   ? -2.906  13.270  10.453 0.80 61.45  ? 403 A1IUB C C1  1 
HETATM 8418 C  C3  . A1IUB X  7  .   ? -2.670  11.071  11.484 0.80 57.42  ? 403 A1IUB C C3  1 
HETATM 8419 C  C7  . A1IUB X  7  .   ? -0.559  12.463  11.344 0.80 74.44  ? 403 A1IUB C C7  1 
HETATM 8420 C  C13 . A1IUB X  7  .   ? 1.625   11.470  11.879 0.80 74.26  ? 403 A1IUB C C13 1 
HETATM 8421 C  C14 . A1IUB X  7  .   ? 0.300   10.546  10.000 0.80 64.65  ? 403 A1IUB C C14 1 
HETATM 8422 C  CHA . HEM   Y  9  .   ? -8.332  11.678  19.844 1.00 34.23  ? 404 HEM   C CHA 1 
HETATM 8423 C  CHB . HEM   Y  9  .   ? -5.757  7.627   19.360 1.00 31.91  ? 404 HEM   C CHB 1 
HETATM 8424 C  CHC . HEM   Y  9  .   ? -7.690  6.993   14.960 1.00 32.94  ? 404 HEM   C CHC 1 
HETATM 8425 C  CHD . HEM   Y  9  .   ? -10.589 10.830  15.664 1.00 32.77  ? 404 HEM   C CHD 1 
HETATM 8426 C  C1A . HEM   Y  9  .   ? -7.478  10.625  20.061 1.00 32.14  ? 404 HEM   C C1A 1 
HETATM 8427 C  C2A . HEM   Y  9  .   ? -6.751  10.465  21.258 1.00 31.36  ? 404 HEM   C C2A 1 
HETATM 8428 C  C3A . HEM   Y  9  .   ? -6.042  9.328   21.137 1.00 31.16  ? 404 HEM   C C3A 1 
HETATM 8429 C  C4A . HEM   Y  9  .   ? -6.312  8.778   19.853 1.00 32.32  ? 404 HEM   C C4A 1 
HETATM 8430 C  CMA . HEM   Y  9  .   ? -5.103  8.762   22.148 1.00 34.00  ? 404 HEM   C CMA 1 
HETATM 8431 C  CAA . HEM   Y  9  .   ? -6.766  11.380  22.448 1.00 34.03  ? 404 HEM   C CAA 1 
HETATM 8432 C  CBA . HEM   Y  9  .   ? -5.825  12.533  22.082 1.00 38.26  ? 404 HEM   C CBA 1 
HETATM 8433 C  CGA . HEM   Y  9  .   ? -5.560  13.388  23.308 1.00 42.19  ? 404 HEM   C CGA 1 
HETATM 8434 O  O1A . HEM   Y  9  .   ? -4.479  14.056  23.396 1.00 42.67  ? 404 HEM   C O1A 1 
HETATM 8435 O  O2A . HEM   Y  9  .   ? -6.313  13.430  24.329 1.00 41.55  ? 404 HEM   C O2A 1 
HETATM 8436 C  C1B . HEM   Y  9  .   ? -6.057  7.173   18.085 1.00 32.03  ? 404 HEM   C C1B 1 
HETATM 8437 C  C2B . HEM   Y  9  .   ? -5.421  6.023   17.561 1.00 30.26  ? 404 HEM   C C2B 1 
HETATM 8438 C  C3B . HEM   Y  9  .   ? -5.951  5.833   16.326 1.00 31.40  ? 404 HEM   C C3B 1 
HETATM 8439 C  C4B . HEM   Y  9  .   ? -6.901  6.916   16.087 1.00 31.58  ? 404 HEM   C C4B 1 
HETATM 8440 C  CMB . HEM   Y  9  .   ? -4.369  5.122   18.203 1.00 27.49  ? 404 HEM   C CMB 1 
HETATM 8441 C  CAB . HEM   Y  9  .   ? -5.469  4.759   15.455 1.00 39.37  ? 404 HEM   C CAB 1 
HETATM 8442 C  CBB . HEM   Y  9  .   ? -5.649  4.762   14.121 1.00 42.98  ? 404 HEM   C CBB 1 
HETATM 8443 C  C1C . HEM   Y  9  .   ? -8.707  7.943   14.771 1.00 33.94  ? 404 HEM   C C1C 1 
HETATM 8444 C  C2C . HEM   Y  9  .   ? -9.616  8.001   13.661 1.00 30.04  ? 404 HEM   C C2C 1 
HETATM 8445 C  C3C . HEM   Y  9  .   ? -10.416 9.114   13.872 1.00 32.58  ? 404 HEM   C C3C 1 
HETATM 8446 C  C4C . HEM   Y  9  .   ? -10.025 9.700   15.133 1.00 32.91  ? 404 HEM   C C4C 1 
HETATM 8447 C  CMC . HEM   Y  9  .   ? -9.667  7.011   12.540 1.00 33.35  ? 404 HEM   C CMC 1 
HETATM 8448 C  CAC . HEM   Y  9  .   ? -11.561 9.637   13.140 1.00 33.27  ? 404 HEM   C CAC 1 
HETATM 8449 C  CBC . HEM   Y  9  .   ? -12.227 8.830   12.337 1.00 38.26  ? 404 HEM   C CBC 1 
HETATM 8450 C  C1D . HEM   Y  9  .   ? -10.135 11.368  16.875 1.00 33.64  ? 404 HEM   C C1D 1 
HETATM 8451 C  C2D . HEM   Y  9  .   ? -10.690 12.628  17.366 1.00 32.86  ? 404 HEM   C C2D 1 
HETATM 8452 C  C3D . HEM   Y  9  .   ? -10.044 12.859  18.510 1.00 32.55  ? 404 HEM   C C3D 1 
HETATM 8453 C  C4D . HEM   Y  9  .   ? -9.116  11.742  18.717 1.00 31.85  ? 404 HEM   C C4D 1 
HETATM 8454 C  CMD . HEM   Y  9  .   ? -11.729 13.516  16.697 1.00 32.97  ? 404 HEM   C CMD 1 
HETATM 8455 C  CAD . HEM   Y  9  .   ? -10.245 14.043  19.397 1.00 35.17  ? 404 HEM   C CAD 1 
HETATM 8456 C  CBD . HEM   Y  9  .   ? -11.297 13.750  20.487 1.00 34.29  ? 404 HEM   C CBD 1 
HETATM 8457 C  CGD . HEM   Y  9  .   ? -11.585 15.055  21.221 1.00 35.80  ? 404 HEM   C CGD 1 
HETATM 8458 O  O1D . HEM   Y  9  .   ? -12.726 15.220  21.751 1.00 37.07  ? 404 HEM   C O1D 1 
HETATM 8459 O  O2D . HEM   Y  9  .   ? -10.751 15.993  21.292 1.00 34.93  ? 404 HEM   C O2D 1 
HETATM 8460 N  NA  . HEM   Y  9  .   ? -7.206  9.572   19.222 1.00 28.81  ? 404 HEM   C NA  1 
HETATM 8461 N  NB  . HEM   Y  9  .   ? -6.971  7.646   17.223 1.00 28.88  ? 404 HEM   C NB  1 
HETATM 8462 N  NC  . HEM   Y  9  .   ? -8.962  8.982   15.640 1.00 29.01  ? 404 HEM   C NC  1 
HETATM 8463 N  ND  . HEM   Y  9  .   ? -9.208  10.872  17.724 1.00 29.92  ? 404 HEM   C ND  1 
HETATM 8464 FE FE  . HEM   Y  9  .   ? -8.228  9.271   17.554 1.00 29.97  ? 404 HEM   C FE  1 
HETATM 8465 MG MG  . MG    Z  10 .   ? -7.059  14.783  25.959 1.00 52.43  ? 405 MG    C MG  1 
HETATM 8466 S  S   . SO4   AA 11 .   ? 16.461  19.819  14.285 1.00 104.70 ? 406 SO4   C S   1 
HETATM 8467 O  O1  . SO4   AA 11 .   ? 17.584  19.213  13.599 1.00 84.69  ? 406 SO4   C O1  1 
HETATM 8468 O  O2  . SO4   AA 11 .   ? 15.227  19.497  13.584 1.00 97.20  ? 406 SO4   C O2  1 
HETATM 8469 O  O3  . SO4   AA 11 .   ? 16.412  19.309  15.649 1.00 81.45  ? 406 SO4   C O3  1 
HETATM 8470 O  O4  . SO4   AA 11 .   ? 16.628  21.264  14.289 1.00 85.84  ? 406 SO4   C O4  1 
HETATM 8471 O  O   . HOH   BA 13 .   ? 45.430  -2.228  26.096 1.00 53.20  ? 501 HOH   A O   1 
HETATM 8472 O  O   . HOH   BA 13 .   ? 69.392  9.540   43.258 1.00 37.61  ? 502 HOH   A O   1 
HETATM 8473 O  O   . HOH   BA 13 .   ? 26.661  -13.319 36.425 1.00 49.03  ? 503 HOH   A O   1 
HETATM 8474 O  O   . HOH   BA 13 .   ? 51.485  -15.419 32.948 1.00 41.06  ? 504 HOH   A O   1 
HETATM 8475 O  O   . HOH   BA 13 .   ? 38.666  6.073   12.850 1.00 44.14  ? 505 HOH   A O   1 
HETATM 8476 O  O   . HOH   BA 13 .   ? 25.392  -19.700 39.217 1.00 42.22  ? 506 HOH   A O   1 
HETATM 8477 O  O   . HOH   BA 13 .   ? 57.539  -12.529 40.072 1.00 43.76  ? 507 HOH   A O   1 
HETATM 8478 O  O   . HOH   BA 13 .   ? 21.232  -15.120 43.264 1.00 53.32  ? 508 HOH   A O   1 
HETATM 8479 O  O   . HOH   BA 13 .   ? 62.961  0.163   34.826 1.00 35.44  ? 509 HOH   A O   1 
HETATM 8480 O  O   . HOH   BA 13 .   ? 74.308  5.795   41.069 1.00 37.56  ? 510 HOH   A O   1 
HETATM 8481 O  O   . HOH   BA 13 .   ? 54.587  14.544  49.078 1.00 40.72  ? 511 HOH   A O   1 
HETATM 8482 O  O   . HOH   BA 13 .   ? 43.178  15.423  30.252 1.00 44.56  ? 512 HOH   A O   1 
HETATM 8483 O  O   . HOH   BA 13 .   ? 38.343  -15.111 30.169 1.00 36.75  ? 513 HOH   A O   1 
HETATM 8484 O  O   . HOH   BA 13 .   ? 22.558  -1.444  42.502 1.00 36.43  ? 514 HOH   A O   1 
HETATM 8485 O  O   . HOH   BA 13 .   ? 26.654  -16.011 26.120 1.00 43.82  ? 515 HOH   A O   1 
HETATM 8486 O  O   . HOH   BA 13 .   ? 38.763  7.588   35.580 1.00 29.83  ? 516 HOH   A O   1 
HETATM 8487 O  O   . HOH   BA 13 .   ? 23.658  1.303   43.658 1.00 32.87  ? 517 HOH   A O   1 
HETATM 8488 O  O   . HOH   BA 13 .   ? 68.525  -5.288  35.691 1.00 50.59  ? 518 HOH   A O   1 
HETATM 8489 O  O   . HOH   BA 13 .   ? 37.340  -4.849  14.856 1.00 46.06  ? 519 HOH   A O   1 
HETATM 8490 O  O   . HOH   BA 13 .   ? 34.470  -1.932  54.251 1.00 32.41  ? 520 HOH   A O   1 
HETATM 8491 O  O   . HOH   BA 13 .   ? 33.160  10.404  37.427 1.00 32.70  ? 521 HOH   A O   1 
HETATM 8492 O  O   . HOH   BA 13 .   ? 40.279  12.094  33.350 1.00 31.82  ? 522 HOH   A O   1 
HETATM 8493 O  O   . HOH   BA 13 .   ? 38.987  3.902   18.705 1.00 35.46  ? 523 HOH   A O   1 
HETATM 8494 O  O   . HOH   BA 13 .   ? 43.684  11.494  29.403 1.00 35.52  ? 524 HOH   A O   1 
HETATM 8495 O  O   . HOH   BA 13 .   ? 50.269  9.826   38.401 1.00 40.99  ? 525 HOH   A O   1 
HETATM 8496 O  O   . HOH   BA 13 .   ? 60.627  13.561  45.250 1.00 45.23  ? 526 HOH   A O   1 
HETATM 8497 O  O   . HOH   BA 13 .   ? 47.795  14.014  30.480 1.00 45.21  ? 527 HOH   A O   1 
HETATM 8498 O  O   . HOH   BA 13 .   ? 30.353  -13.788 49.365 1.00 37.96  ? 528 HOH   A O   1 
HETATM 8499 O  O   . HOH   BA 13 .   ? 37.815  4.808   35.705 1.00 33.24  ? 529 HOH   A O   1 
HETATM 8500 O  O   . HOH   BA 13 .   ? 36.534  9.504   31.608 1.00 30.73  ? 530 HOH   A O   1 
HETATM 8501 O  O   . HOH   BA 13 .   ? 56.685  -5.557  45.426 1.00 33.06  ? 531 HOH   A O   1 
HETATM 8502 O  O   . HOH   BA 13 .   ? 56.012  -4.904  51.621 1.00 47.21  ? 532 HOH   A O   1 
HETATM 8503 O  O   . HOH   BA 13 .   ? 44.837  5.050   32.255 1.00 39.93  ? 533 HOH   A O   1 
HETATM 8504 O  O   . HOH   BA 13 .   ? 46.500  7.677   38.204 1.00 30.53  ? 534 HOH   A O   1 
HETATM 8505 O  O   . HOH   BA 13 .   ? 41.136  20.193  35.237 1.00 49.09  ? 535 HOH   A O   1 
HETATM 8506 O  O   . HOH   BA 13 .   ? 42.142  -10.155 18.970 1.00 45.42  ? 536 HOH   A O   1 
HETATM 8507 O  O   . HOH   BA 13 .   ? 65.224  7.966   51.600 1.00 36.56  ? 537 HOH   A O   1 
HETATM 8508 O  O   . HOH   BA 13 .   ? 48.095  8.809   50.102 1.00 36.12  ? 538 HOH   A O   1 
HETATM 8509 O  O   . HOH   BA 13 .   ? 24.280  -10.419 22.167 1.00 36.09  ? 539 HOH   A O   1 
HETATM 8510 O  O   . HOH   BA 13 .   ? 55.275  7.406   43.875 1.00 24.52  ? 540 HOH   A O   1 
HETATM 8511 O  O   . HOH   BA 13 .   ? 46.366  -12.282 29.118 1.00 37.14  ? 541 HOH   A O   1 
HETATM 8512 O  O   . HOH   BA 13 .   ? 68.135  2.835   38.475 1.00 35.42  ? 542 HOH   A O   1 
HETATM 8513 O  O   . HOH   BA 13 .   ? 70.367  -2.810  40.690 1.00 53.26  ? 543 HOH   A O   1 
HETATM 8514 O  O   . HOH   BA 13 .   ? 38.819  2.499   57.086 1.00 40.24  ? 544 HOH   A O   1 
HETATM 8515 O  O   . HOH   BA 13 .   ? 34.303  14.622  36.186 1.00 40.90  ? 545 HOH   A O   1 
HETATM 8516 O  O   . HOH   BA 13 .   ? 37.503  -13.168 35.935 1.00 27.36  ? 546 HOH   A O   1 
HETATM 8517 O  O   . HOH   BA 13 .   ? 65.313  -0.465  36.130 1.00 35.67  ? 547 HOH   A O   1 
HETATM 8518 O  O   . HOH   BA 13 .   ? 43.592  -15.376 28.136 1.00 38.37  ? 548 HOH   A O   1 
HETATM 8519 O  O   . HOH   BA 13 .   ? 46.192  -9.971  48.350 1.00 36.22  ? 549 HOH   A O   1 
HETATM 8520 O  O   . HOH   BA 13 .   ? 26.794  -11.384 32.633 1.00 29.94  ? 550 HOH   A O   1 
HETATM 8521 O  O   . HOH   BA 13 .   ? 57.419  7.467   47.692 1.00 31.19  ? 551 HOH   A O   1 
HETATM 8522 O  O   . HOH   BA 13 .   ? 57.134  -3.007  45.728 1.00 34.04  ? 552 HOH   A O   1 
HETATM 8523 O  O   . HOH   BA 13 .   ? 29.908  4.965   28.599 1.00 32.83  ? 553 HOH   A O   1 
HETATM 8524 O  O   . HOH   BA 13 .   ? 36.761  -13.375 26.871 1.00 32.24  ? 554 HOH   A O   1 
HETATM 8525 O  O   . HOH   BA 13 .   ? 45.658  -1.317  54.445 1.00 45.21  ? 555 HOH   A O   1 
HETATM 8526 O  O   . HOH   BA 13 .   ? 20.085  -10.426 22.838 1.00 33.07  ? 556 HOH   A O   1 
HETATM 8527 O  O   . HOH   BA 13 .   ? 57.839  0.162   47.438 1.00 34.10  ? 557 HOH   A O   1 
HETATM 8528 O  O   . HOH   BA 13 .   ? 48.246  10.355  36.721 1.00 45.70  ? 558 HOH   A O   1 
HETATM 8529 O  O   . HOH   BA 13 .   ? 23.697  9.045   28.806 1.00 48.68  ? 559 HOH   A O   1 
HETATM 8530 O  O   . HOH   BA 13 .   ? 34.860  7.294   44.093 1.00 38.89  ? 560 HOH   A O   1 
HETATM 8531 O  O   . HOH   BA 13 .   ? 32.750  -2.527  17.025 1.00 41.22  ? 561 HOH   A O   1 
HETATM 8532 O  O   . HOH   BA 13 .   ? 60.681  17.689  38.990 1.00 44.41  ? 562 HOH   A O   1 
HETATM 8533 O  O   . HOH   BA 13 .   ? 40.226  15.851  31.787 1.00 31.58  ? 563 HOH   A O   1 
HETATM 8534 O  O   . HOH   BA 13 .   ? 34.550  -22.830 32.234 1.00 47.40  ? 564 HOH   A O   1 
HETATM 8535 O  O   . HOH   BA 13 .   ? 49.104  5.958   47.237 1.00 30.16  ? 565 HOH   A O   1 
HETATM 8536 O  O   . HOH   BA 13 .   ? 65.269  8.019   31.488 1.00 48.99  ? 566 HOH   A O   1 
HETATM 8537 O  O   . HOH   BA 13 .   ? 51.918  8.609   52.002 1.00 25.95  ? 567 HOH   A O   1 
HETATM 8538 O  O   . HOH   BA 13 .   ? 29.072  -12.402 35.079 1.00 37.25  ? 568 HOH   A O   1 
HETATM 8539 O  O   . HOH   BA 13 .   ? 22.877  -11.356 34.605 1.00 47.83  ? 569 HOH   A O   1 
HETATM 8540 O  O   . HOH   BA 13 .   ? 40.007  2.103   42.354 1.00 23.81  ? 570 HOH   A O   1 
HETATM 8541 O  O   . HOH   BA 13 .   ? 34.868  5.002   43.024 1.00 31.10  ? 571 HOH   A O   1 
HETATM 8542 O  O   . HOH   BA 13 .   ? 32.534  -10.292 22.834 1.00 35.31  ? 572 HOH   A O   1 
HETATM 8543 O  O   . HOH   BA 13 .   ? 43.749  -9.958  21.085 1.00 46.09  ? 573 HOH   A O   1 
HETATM 8544 O  O   . HOH   BA 13 .   ? 40.769  10.361  49.825 1.00 41.24  ? 574 HOH   A O   1 
HETATM 8545 O  O   . HOH   BA 13 .   ? 33.728  12.774  27.937 1.00 34.42  ? 575 HOH   A O   1 
HETATM 8546 O  O   . HOH   BA 13 .   ? 43.869  -11.790 47.889 1.00 36.07  ? 576 HOH   A O   1 
HETATM 8547 O  O   . HOH   BA 13 .   ? 47.240  4.230   16.517 1.00 42.24  ? 577 HOH   A O   1 
HETATM 8548 O  O   . HOH   BA 13 .   ? 37.186  1.785   18.878 1.00 34.25  ? 578 HOH   A O   1 
HETATM 8549 O  O   . HOH   BA 13 .   ? 31.503  -1.597  49.663 1.00 30.15  ? 579 HOH   A O   1 
HETATM 8550 O  O   . HOH   BA 13 .   ? 41.473  7.116   54.681 1.00 38.73  ? 580 HOH   A O   1 
HETATM 8551 O  O   . HOH   BA 13 .   ? 26.103  -5.086  16.348 1.00 40.43  ? 581 HOH   A O   1 
HETATM 8552 O  O   . HOH   BA 13 .   ? 21.972  -4.960  19.319 1.00 36.42  ? 582 HOH   A O   1 
HETATM 8553 O  O   . HOH   BA 13 .   ? 56.363  -13.053 37.735 1.00 41.17  ? 583 HOH   A O   1 
HETATM 8554 O  O   . HOH   BA 13 .   ? 45.489  -24.737 37.039 1.00 41.70  ? 584 HOH   A O   1 
HETATM 8555 O  O   . HOH   BA 13 .   ? 44.116  -18.915 42.359 1.00 40.43  ? 585 HOH   A O   1 
HETATM 8556 O  O   . HOH   BA 13 .   ? 53.877  -18.099 41.703 1.00 50.93  ? 586 HOH   A O   1 
HETATM 8557 O  O   . HOH   BA 13 .   ? 60.966  -4.750  55.359 1.00 43.59  ? 587 HOH   A O   1 
HETATM 8558 O  O   . HOH   BA 13 .   ? 28.757  3.836   43.125 1.00 40.36  ? 588 HOH   A O   1 
HETATM 8559 O  O   . HOH   BA 13 .   ? 46.196  -15.319 36.813 1.00 27.55  ? 589 HOH   A O   1 
HETATM 8560 O  O   . HOH   BA 13 .   ? 54.776  -5.500  47.719 1.00 32.16  ? 590 HOH   A O   1 
HETATM 8561 O  O   . HOH   BA 13 .   ? 54.326  -14.479 34.400 1.00 43.32  ? 591 HOH   A O   1 
HETATM 8562 O  O   . HOH   BA 13 .   ? 52.002  11.858  39.046 1.00 43.91  ? 592 HOH   A O   1 
HETATM 8563 O  O   . HOH   BA 13 .   ? 36.481  -10.816 54.835 1.00 47.27  ? 593 HOH   A O   1 
HETATM 8564 O  O   . HOH   BA 13 .   ? 44.961  12.396  45.363 1.00 37.77  ? 594 HOH   A O   1 
HETATM 8565 O  O   . HOH   BA 13 .   ? 28.611  7.707   42.172 1.00 42.57  ? 595 HOH   A O   1 
HETATM 8566 O  O   . HOH   BA 13 .   ? 53.769  9.830   43.827 1.00 33.69  ? 596 HOH   A O   1 
HETATM 8567 O  O   . HOH   BA 13 .   ? 38.673  4.560   33.021 1.00 42.14  ? 597 HOH   A O   1 
HETATM 8568 O  O   . HOH   BA 13 .   ? 38.069  9.945   33.675 1.00 38.64  ? 598 HOH   A O   1 
HETATM 8569 O  O   . HOH   BA 13 .   ? 42.000  -12.917 50.150 1.00 51.56  ? 599 HOH   A O   1 
HETATM 8570 O  O   . HOH   BA 13 .   ? 67.970  -5.796  31.907 1.00 44.02  ? 600 HOH   A O   1 
HETATM 8571 O  O   . HOH   BA 13 .   ? 64.191  1.757   26.872 1.00 40.84  ? 601 HOH   A O   1 
HETATM 8572 O  O   . HOH   BA 13 .   ? 20.290  3.816   29.096 1.00 37.84  ? 602 HOH   A O   1 
HETATM 8573 O  O   . HOH   BA 13 .   ? 51.343  -16.279 43.161 1.00 49.99  ? 603 HOH   A O   1 
HETATM 8574 O  O   . HOH   BA 13 .   ? 35.262  8.182   54.859 1.00 48.94  ? 604 HOH   A O   1 
HETATM 8575 O  O   . HOH   BA 13 .   ? 30.950  11.913  37.318 1.00 37.17  ? 605 HOH   A O   1 
HETATM 8576 O  O   . HOH   BA 13 .   ? 48.609  -3.583  53.394 1.00 35.52  ? 606 HOH   A O   1 
HETATM 8577 O  O   . HOH   BA 13 .   ? 50.025  13.678  36.015 1.00 49.72  ? 607 HOH   A O   1 
HETATM 8578 O  O   . HOH   BA 13 .   ? 28.742  -24.331 38.559 1.00 44.27  ? 608 HOH   A O   1 
HETATM 8579 O  O   . HOH   BA 13 .   ? 34.161  -3.755  56.272 1.00 40.08  ? 609 HOH   A O   1 
HETATM 8580 O  O   . HOH   BA 13 .   ? 50.545  -21.591 37.060 1.00 47.18  ? 610 HOH   A O   1 
HETATM 8581 O  O   . HOH   BA 13 .   ? 28.414  -0.346  47.088 1.00 37.29  ? 611 HOH   A O   1 
HETATM 8582 O  O   . HOH   BA 13 .   ? 48.762  -15.438 35.560 1.00 33.86  ? 612 HOH   A O   1 
HETATM 8583 O  O   . HOH   BA 13 .   ? 31.079  5.651   42.776 1.00 38.47  ? 613 HOH   A O   1 
HETATM 8584 O  O   . HOH   BA 13 .   ? 44.710  14.719  39.834 1.00 43.46  ? 614 HOH   A O   1 
HETATM 8585 O  O   . HOH   BA 13 .   ? 23.550  -4.200  16.007 1.00 40.34  ? 615 HOH   A O   1 
HETATM 8586 O  O   . HOH   BA 13 .   ? 20.927  -1.270  37.814 1.00 42.52  ? 616 HOH   A O   1 
HETATM 8587 O  O   . HOH   BA 13 .   ? 48.417  -4.624  32.182 1.00 49.74  ? 617 HOH   A O   1 
HETATM 8588 O  O   . HOH   BA 13 .   ? 37.581  -9.733  24.391 1.00 42.21  ? 618 HOH   A O   1 
HETATM 8589 O  O   . HOH   BA 13 .   ? 50.878  9.166   30.070 1.00 42.80  ? 619 HOH   A O   1 
HETATM 8590 O  O   . HOH   BA 13 .   ? 22.281  -11.912 22.927 1.00 41.11  ? 620 HOH   A O   1 
HETATM 8591 O  O   . HOH   BA 13 .   ? 47.524  1.218   55.795 1.00 48.26  ? 621 HOH   A O   1 
HETATM 8592 O  O   . HOH   BA 13 .   ? 70.247  3.876   48.390 1.00 44.80  ? 622 HOH   A O   1 
HETATM 8593 O  O   . HOH   BA 13 .   ? 22.582  2.345   16.628 1.00 37.51  ? 623 HOH   A O   1 
HETATM 8594 O  O   . HOH   BA 13 .   ? 30.116  -10.090 56.339 1.00 37.13  ? 624 HOH   A O   1 
HETATM 8595 O  O   . HOH   BA 13 .   ? 66.295  -0.009  38.529 1.00 37.80  ? 625 HOH   A O   1 
HETATM 8596 O  O   . HOH   BA 13 .   ? 19.987  2.694   31.752 1.00 49.83  ? 626 HOH   A O   1 
HETATM 8597 O  O   . HOH   BA 13 .   ? 35.928  15.324  43.133 1.00 48.16  ? 627 HOH   A O   1 
HETATM 8598 O  O   . HOH   BA 13 .   ? 48.208  9.333   29.656 1.00 31.53  ? 628 HOH   A O   1 
HETATM 8599 O  O   . HOH   BA 13 .   ? 45.031  -8.536  50.472 1.00 34.15  ? 629 HOH   A O   1 
HETATM 8600 O  O   . HOH   BA 13 .   ? 31.734  2.295   42.098 1.00 34.93  ? 630 HOH   A O   1 
HETATM 8601 O  O   . HOH   BA 13 .   ? 72.959  4.375   35.582 1.00 48.12  ? 631 HOH   A O   1 
HETATM 8602 O  O   . HOH   BA 13 .   ? 29.210  10.927  39.149 1.00 40.01  ? 632 HOH   A O   1 
HETATM 8603 O  O   . HOH   BA 13 .   ? 63.209  8.171   29.844 1.00 44.51  ? 633 HOH   A O   1 
HETATM 8604 O  O   . HOH   BA 13 .   ? 31.510  -2.885  56.945 1.00 48.22  ? 634 HOH   A O   1 
HETATM 8605 O  O   . HOH   BA 13 .   ? 28.081  -15.026 37.772 1.00 39.72  ? 635 HOH   A O   1 
HETATM 8606 O  O   . HOH   BA 13 .   ? 43.601  -22.423 32.961 1.00 43.36  ? 636 HOH   A O   1 
HETATM 8607 O  O   . HOH   BA 13 .   ? 32.333  -24.247 41.892 1.00 53.22  ? 637 HOH   A O   1 
HETATM 8608 O  O   . HOH   BA 13 .   ? 36.597  -17.977 31.030 1.00 41.89  ? 638 HOH   A O   1 
HETATM 8609 O  O   . HOH   BA 13 .   ? 59.344  1.712   20.736 1.00 50.82  ? 639 HOH   A O   1 
HETATM 8610 O  O   . HOH   BA 13 .   ? 55.333  -2.256  20.236 1.00 50.78  ? 640 HOH   A O   1 
HETATM 8611 O  O   . HOH   BA 13 .   ? 53.930  -2.452  53.853 1.00 50.01  ? 641 HOH   A O   1 
HETATM 8612 O  O   . HOH   BA 13 .   ? 19.934  -8.965  30.835 1.00 39.15  ? 642 HOH   A O   1 
HETATM 8613 O  O   . HOH   BA 13 .   ? 47.747  -15.121 43.314 1.00 45.43  ? 643 HOH   A O   1 
HETATM 8614 O  O   . HOH   BA 13 .   ? 33.414  0.164   41.104 1.00 30.48  ? 644 HOH   A O   1 
HETATM 8615 O  O   . HOH   BA 13 .   ? 28.973  -11.305 48.985 1.00 32.86  ? 645 HOH   A O   1 
HETATM 8616 O  O   . HOH   BA 13 .   ? 38.679  -24.457 35.022 1.00 41.79  ? 646 HOH   A O   1 
HETATM 8617 O  O   . HOH   BA 13 .   ? 55.965  13.367  36.601 1.00 41.66  ? 647 HOH   A O   1 
HETATM 8618 O  O   . HOH   BA 13 .   ? 41.858  17.614  32.679 1.00 38.97  ? 648 HOH   A O   1 
HETATM 8619 O  O   . HOH   BA 13 .   ? 22.799  -5.133  39.733 1.00 44.05  ? 649 HOH   A O   1 
HETATM 8620 O  O   . HOH   BA 13 .   ? 34.899  -23.328 43.083 1.00 40.19  ? 650 HOH   A O   1 
HETATM 8621 O  O   . HOH   BA 13 .   ? 37.949  -8.829  56.081 1.00 56.98  ? 651 HOH   A O   1 
HETATM 8622 O  O   . HOH   BA 13 .   ? 48.389  2.169   17.676 1.00 38.51  ? 652 HOH   A O   1 
HETATM 8623 O  O   . HOH   BA 13 .   ? 46.925  11.191  27.917 1.00 41.79  ? 653 HOH   A O   1 
HETATM 8624 O  O   . HOH   BA 13 .   ? 33.534  12.295  30.599 1.00 28.15  ? 654 HOH   A O   1 
HETATM 8625 O  O   . HOH   BA 13 .   ? 58.370  11.792  30.516 1.00 41.68  ? 655 HOH   A O   1 
HETATM 8626 O  O   . HOH   BA 13 .   ? 37.503  6.951   48.611 1.00 36.65  ? 656 HOH   A O   1 
HETATM 8627 O  O   . HOH   BA 13 .   ? 34.284  -3.899  52.242 1.00 32.26  ? 657 HOH   A O   1 
HETATM 8628 O  O   . HOH   BA 13 .   ? 42.829  12.831  46.756 1.00 38.96  ? 658 HOH   A O   1 
HETATM 8629 O  O   . HOH   BA 13 .   ? 39.554  8.472   47.866 1.00 34.75  ? 659 HOH   A O   1 
HETATM 8630 O  O   . HOH   BA 13 .   ? 58.643  -0.922  18.155 1.00 52.21  ? 660 HOH   A O   1 
HETATM 8631 O  O   . HOH   BA 13 .   ? 26.812  1.508   45.702 1.00 39.26  ? 661 HOH   A O   1 
HETATM 8632 O  O   . HOH   BA 13 .   ? 46.765  10.035  31.713 1.00 40.93  ? 662 HOH   A O   1 
HETATM 8633 O  O   . HOH   BA 13 .   ? 47.477  -5.727  55.089 1.00 42.27  ? 663 HOH   A O   1 
HETATM 8634 O  O   . HOH   BA 13 .   ? 38.429  14.377  40.291 1.00 43.25  ? 664 HOH   A O   1 
HETATM 8635 O  O   . HOH   BA 13 .   ? 51.261  10.980  50.876 1.00 40.21  ? 665 HOH   A O   1 
HETATM 8636 O  O   . HOH   BA 13 .   ? 35.604  -6.561  58.282 1.00 48.14  ? 666 HOH   A O   1 
HETATM 8637 O  O   . HOH   BA 13 .   ? 39.810  -13.484 53.484 1.00 45.25  ? 667 HOH   A O   1 
HETATM 8638 O  O   . HOH   BA 13 .   ? 26.004  9.949   38.615 1.00 45.96  ? 668 HOH   A O   1 
HETATM 8639 O  O   . HOH   BA 13 .   ? 44.540  18.085  36.661 1.00 50.75  ? 669 HOH   A O   1 
HETATM 8640 O  O   . HOH   BA 13 .   ? 38.780  17.523  16.338 1.00 43.47  ? 670 HOH   A O   1 
HETATM 8641 O  O   . HOH   BA 13 .   ? 74.951  3.023   40.934 1.00 45.55  ? 671 HOH   A O   1 
HETATM 8642 O  O   . HOH   BA 13 .   ? 54.769  -16.487 43.859 1.00 46.35  ? 672 HOH   A O   1 
HETATM 8643 O  O   . HOH   BA 13 .   ? 21.514  1.476   36.014 1.00 43.46  ? 673 HOH   A O   1 
HETATM 8644 O  O   . HOH   BA 13 .   ? 32.898  -17.488 21.312 1.00 50.05  ? 674 HOH   A O   1 
HETATM 8645 O  O   . HOH   BA 13 .   ? 20.516  2.983   39.401 1.00 42.25  ? 675 HOH   A O   1 
HETATM 8646 O  O   . HOH   BA 13 .   ? 62.482  13.420  32.991 1.00 42.03  ? 676 HOH   A O   1 
HETATM 8647 O  O   . HOH   BA 13 .   ? 48.266  -10.226 52.492 1.00 46.21  ? 677 HOH   A O   1 
HETATM 8648 O  O   . HOH   BA 13 .   ? 42.866  10.053  15.186 1.00 48.89  ? 678 HOH   A O   1 
HETATM 8649 O  O   . HOH   BA 13 .   ? 25.335  11.530  36.360 1.00 53.89  ? 679 HOH   A O   1 
HETATM 8650 O  O   . HOH   BA 13 .   ? 28.396  1.142   51.622 1.00 32.00  ? 680 HOH   A O   1 
HETATM 8651 O  O   . HOH   BA 13 .   ? 68.431  -4.839  38.139 1.00 50.19  ? 681 HOH   A O   1 
HETATM 8652 O  O   . HOH   BA 13 .   ? 58.572  -0.802  20.965 1.00 49.80  ? 682 HOH   A O   1 
HETATM 8653 O  O   . HOH   BA 13 .   ? 53.194  16.835  45.993 1.00 46.14  ? 683 HOH   A O   1 
HETATM 8654 O  O   . HOH   BA 13 .   ? 24.346  3.961   14.411 1.00 48.50  ? 684 HOH   A O   1 
HETATM 8655 O  O   . HOH   BA 13 .   ? 58.131  8.036   50.181 1.00 43.59  ? 685 HOH   A O   1 
HETATM 8656 O  O   . HOH   BA 13 .   ? 65.283  11.095  49.182 1.00 40.26  ? 686 HOH   A O   1 
HETATM 8657 O  O   . HOH   BA 13 .   ? 63.833  13.294  45.193 1.00 47.28  ? 687 HOH   A O   1 
HETATM 8658 O  O   . HOH   BA 13 .   ? 44.953  -7.335  21.779 1.00 49.66  ? 688 HOH   A O   1 
HETATM 8659 O  O   . HOH   BA 13 .   ? 32.273  3.529   60.050 1.00 47.19  ? 689 HOH   A O   1 
HETATM 8660 O  O   . HOH   BA 13 .   ? 40.840  -5.358  55.927 1.00 38.12  ? 690 HOH   A O   1 
HETATM 8661 O  O   . HOH   BA 13 .   ? 41.332  -2.824  55.991 1.00 40.76  ? 691 HOH   A O   1 
HETATM 8662 O  O   . HOH   BA 13 .   ? 67.094  6.534   54.404 1.00 43.62  ? 692 HOH   A O   1 
HETATM 8663 O  O   . HOH   BA 13 .   ? 48.690  13.381  28.353 1.00 47.57  ? 693 HOH   A O   1 
HETATM 8664 O  O   . HOH   BA 13 .   ? 48.467  16.895  21.333 1.00 50.29  ? 694 HOH   A O   1 
HETATM 8665 O  O   . HOH   BA 13 .   ? 48.126  -11.225 49.746 1.00 42.08  ? 695 HOH   A O   1 
HETATM 8666 O  O   . HOH   BA 13 .   ? 50.668  -11.157 48.396 1.00 45.39  ? 696 HOH   A O   1 
HETATM 8667 O  O   . HOH   BA 13 .   ? 24.060  14.306  34.989 1.00 61.44  ? 697 HOH   A O   1 
HETATM 8668 O  O   . HOH   BA 13 .   ? 40.630  12.777  44.891 1.00 41.99  ? 698 HOH   A O   1 
HETATM 8669 O  O   . HOH   BA 13 .   ? 42.896  -11.539 52.092 1.00 46.33  ? 699 HOH   A O   1 
HETATM 8670 O  O   . HOH   BA 13 .   ? 62.840  7.558   55.503 1.00 48.74  ? 700 HOH   A O   1 
HETATM 8671 O  O   . HOH   BA 13 .   ? 48.316  22.935  23.994 1.00 50.63  ? 701 HOH   A O   1 
HETATM 8672 O  O   . HOH   BA 13 .   ? 49.511  -19.486 44.386 1.00 45.32  ? 702 HOH   A O   1 
HETATM 8673 O  O   . HOH   BA 13 .   ? 43.199  -8.821  52.202 1.00 50.88  ? 703 HOH   A O   1 
HETATM 8674 O  O   . HOH   BA 13 .   ? 42.001  -12.081 20.944 1.00 50.57  ? 704 HOH   A O   1 
HETATM 8675 O  O   . HOH   BA 13 .   ? 53.713  11.844  36.882 1.00 40.19  ? 705 HOH   A O   1 
HETATM 8676 O  O   . HOH   BA 13 .   ? 22.649  7.272   26.679 1.00 45.03  ? 706 HOH   A O   1 
HETATM 8677 O  O   . HOH   BA 13 .   ? 64.506  12.980  47.801 1.00 51.36  ? 707 HOH   A O   1 
HETATM 8678 O  O   . HOH   BA 13 .   ? 27.186  -18.286 34.904 1.00 50.10  ? 708 HOH   A O   1 
HETATM 8679 O  O   . HOH   BA 13 .   ? 54.913  -7.025  49.752 1.00 49.74  ? 709 HOH   A O   1 
HETATM 8680 O  O   . HOH   BA 13 .   ? 48.547  11.495  51.078 1.00 45.51  ? 710 HOH   A O   1 
HETATM 8681 O  O   . HOH   BA 13 .   ? 46.299  -4.725  22.060 1.00 51.61  ? 711 HOH   A O   1 
HETATM 8682 O  O   . HOH   BA 13 .   ? 47.665  18.869  22.472 1.00 61.31  ? 712 HOH   A O   1 
HETATM 8683 O  O   . HOH   BA 13 .   ? 25.072  -12.659 31.374 1.00 53.22  ? 713 HOH   A O   1 
HETATM 8684 O  O   . HOH   BA 13 .   ? 26.631  -21.090 34.844 1.00 59.01  ? 714 HOH   A O   1 
HETATM 8685 O  O   . HOH   BA 13 .   ? 51.226  14.458  38.984 1.00 45.79  ? 715 HOH   A O   1 
HETATM 8686 O  O   . HOH   BA 13 .   ? 22.392  -13.796 21.320 1.00 48.87  ? 716 HOH   A O   1 
HETATM 8687 O  O   . HOH   BA 13 .   ? 24.087  -16.820 44.983 1.00 53.59  ? 717 HOH   A O   1 
HETATM 8688 O  O   . HOH   BA 13 .   ? 50.928  19.272  24.028 1.00 52.52  ? 718 HOH   A O   1 
HETATM 8689 O  O   . HOH   BA 13 .   ? 67.862  -2.455  39.054 1.00 52.34  ? 719 HOH   A O   1 
HETATM 8690 O  O   . HOH   BA 13 .   ? 48.985  14.982  43.011 1.00 49.43  ? 720 HOH   A O   1 
HETATM 8691 O  O   . HOH   BA 13 .   ? 22.618  -15.902 40.438 1.00 47.10  ? 721 HOH   A O   1 
HETATM 8692 O  O   . HOH   BA 13 .   ? 38.614  -6.264  57.437 1.00 56.43  ? 722 HOH   A O   1 
HETATM 8693 O  O   . HOH   BA 13 .   ? 30.917  5.564   53.733 1.00 56.13  ? 723 HOH   A O   1 
HETATM 8694 O  O   . HOH   BA 13 .   ? 52.779  -21.727 38.111 1.00 54.62  ? 724 HOH   A O   1 
HETATM 8695 O  O   . HOH   BA 13 .   ? 43.119  -14.285 48.268 1.00 48.42  ? 725 HOH   A O   1 
HETATM 8696 O  O   . HOH   BA 13 .   ? 42.003  7.533   57.317 1.00 41.75  ? 726 HOH   A O   1 
HETATM 8697 O  O   . HOH   BA 13 .   ? 29.671  0.526   49.067 1.00 36.45  ? 727 HOH   A O   1 
HETATM 8698 O  O   . HOH   BA 13 .   ? 38.212  -26.854 37.999 1.00 54.55  ? 728 HOH   A O   1 
HETATM 8699 O  O   . HOH   BA 13 .   ? 49.185  -16.359 47.751 1.00 44.73  ? 729 HOH   A O   1 
HETATM 8700 O  O   . HOH   BA 13 .   ? 43.883  -7.476  54.821 1.00 58.46  ? 730 HOH   A O   1 
HETATM 8701 O  O   . HOH   BA 13 .   ? 24.108  3.966   44.028 1.00 39.96  ? 731 HOH   A O   1 
HETATM 8702 O  O   . HOH   BA 13 .   ? 55.880  -14.088 46.309 1.00 48.81  ? 732 HOH   A O   1 
HETATM 8703 O  O   . HOH   BA 13 .   ? 42.419  30.612  26.705 1.00 58.06  ? 733 HOH   A O   1 
HETATM 8704 O  O   . HOH   BA 13 .   ? 47.581  -20.745 31.629 1.00 47.60  ? 734 HOH   A O   1 
HETATM 8705 O  O   . HOH   BA 13 .   ? 33.217  -24.955 38.000 1.00 57.63  ? 735 HOH   A O   1 
HETATM 8706 O  O   . HOH   BA 13 .   ? 49.749  -17.309 33.663 1.00 31.06  ? 736 HOH   A O   1 
HETATM 8707 O  O   . HOH   BA 13 .   ? 25.967  -16.182 28.462 1.00 48.79  ? 737 HOH   A O   1 
HETATM 8708 O  O   . HOH   BA 13 .   ? 28.571  -24.230 34.163 1.00 53.63  ? 738 HOH   A O   1 
HETATM 8709 O  O   . HOH   BA 13 .   ? 60.583  9.467   51.447 1.00 47.52  ? 739 HOH   A O   1 
HETATM 8710 O  O   . HOH   BA 13 .   ? 63.514  10.513  51.271 1.00 53.33  ? 740 HOH   A O   1 
HETATM 8711 O  O   . HOH   BA 13 .   ? 50.448  -19.856 34.719 1.00 42.83  ? 741 HOH   A O   1 
HETATM 8712 O  O   . HOH   BA 13 .   ? 35.214  -11.351 22.785 1.00 55.17  ? 742 HOH   A O   1 
HETATM 8713 O  O   . HOH   BA 13 .   ? 48.585  -17.704 31.213 1.00 43.76  ? 743 HOH   A O   1 
HETATM 8714 O  O   . HOH   BA 13 .   ? 33.715  5.904   48.333 1.00 44.26  ? 744 HOH   A O   1 
HETATM 8715 O  O   . HOH   BA 13 .   ? 26.656  -15.876 33.954 1.00 50.99  ? 745 HOH   A O   1 
HETATM 8716 O  O   . HOH   BA 13 .   ? 26.868  5.437   42.935 1.00 44.74  ? 746 HOH   A O   1 
HETATM 8717 O  O   . HOH   BA 13 .   ? 35.159  -11.988 20.333 1.00 50.59  ? 747 HOH   A O   1 
HETATM 8718 O  O   . HOH   BA 13 .   ? 31.942  -25.322 34.575 1.00 61.04  ? 748 HOH   A O   1 
HETATM 8719 O  O   . HOH   BA 13 .   ? 45.659  -20.576 28.978 1.00 47.21  ? 749 HOH   A O   1 
HETATM 8720 O  O   . HOH   BA 13 .   ? 55.041  -10.082 49.673 1.00 40.48  ? 750 HOH   A O   1 
HETATM 8721 O  O   . HOH   BA 13 .   ? 29.670  3.289   47.847 1.00 40.61  ? 751 HOH   A O   1 
HETATM 8722 O  O   . HOH   BA 13 .   ? 32.178  4.673   46.860 1.00 40.84  ? 752 HOH   A O   1 
HETATM 8723 O  O   . HOH   BA 13 .   ? 26.760  18.078  33.237 1.00 49.32  ? 753 HOH   A O   1 
HETATM 8724 O  O   . HOH   CA 13 .   ? -13.301 -18.945 61.503 1.00 59.88  ? 501 HOH   B O   1 
HETATM 8725 O  O   . HOH   CA 13 .   ? -10.121 -2.697  75.597 1.00 42.01  ? 502 HOH   B O   1 
HETATM 8726 O  O   . HOH   CA 13 .   ? 22.039  -30.580 50.959 1.00 33.16  ? 503 HOH   B O   1 
HETATM 8727 O  O   . HOH   CA 13 .   ? 1.038   -26.128 57.210 1.00 44.28  ? 504 HOH   B O   1 
HETATM 8728 O  O   . HOH   CA 13 .   ? 11.067  -9.310  76.732 1.00 44.48  ? 505 HOH   B O   1 
HETATM 8729 O  O   . HOH   CA 13 .   ? -3.392  4.872   57.697 1.00 42.03  ? 506 HOH   B O   1 
HETATM 8730 O  O   . HOH   CA 13 .   ? 18.163  -19.612 47.885 1.00 34.23  ? 507 HOH   B O   1 
HETATM 8731 O  O   . HOH   CA 13 .   ? 20.311  -6.981  71.770 1.00 42.59  ? 508 HOH   B O   1 
HETATM 8732 O  O   . HOH   CA 13 .   ? 5.599   -18.976 47.963 1.00 40.26  ? 509 HOH   B O   1 
HETATM 8733 O  O   . HOH   CA 13 .   ? 27.613  -9.910  52.066 1.00 29.22  ? 510 HOH   B O   1 
HETATM 8734 O  O   . HOH   CA 13 .   ? 18.089  -3.838  40.586 1.00 45.60  ? 511 HOH   B O   1 
HETATM 8735 O  O   . HOH   CA 13 .   ? 25.280  -4.581  48.109 1.00 45.64  ? 512 HOH   B O   1 
HETATM 8736 O  O   . HOH   CA 13 .   ? 20.460  -7.341  67.366 1.00 37.62  ? 513 HOH   B O   1 
HETATM 8737 O  O   . HOH   CA 13 .   ? 18.645  -17.240 44.360 1.00 47.41  ? 514 HOH   B O   1 
HETATM 8738 O  O   . HOH   CA 13 .   ? 1.073   4.990   67.628 1.00 39.28  ? 515 HOH   B O   1 
HETATM 8739 O  O   . HOH   CA 13 .   ? -14.662 -1.360  55.708 1.00 54.47  ? 516 HOH   B O   1 
HETATM 8740 O  O   . HOH   CA 13 .   ? 27.937  -7.572  54.507 1.00 29.20  ? 517 HOH   B O   1 
HETATM 8741 O  O   . HOH   CA 13 .   ? -10.522 -2.402  65.571 1.00 31.97  ? 518 HOH   B O   1 
HETATM 8742 O  O   . HOH   CA 13 .   ? 2.092   -8.218  72.747 1.00 42.80  ? 519 HOH   B O   1 
HETATM 8743 O  O   . HOH   CA 13 .   ? 7.585   -2.990  67.741 1.00 39.75  ? 520 HOH   B O   1 
HETATM 8744 O  O   . HOH   CA 13 .   ? 18.261  -14.997 72.932 1.00 42.95  ? 521 HOH   B O   1 
HETATM 8745 O  O   . HOH   CA 13 .   ? 6.868   -9.565  67.008 1.00 38.16  ? 522 HOH   B O   1 
HETATM 8746 O  O   . HOH   CA 13 .   ? 5.900   -2.001  74.502 1.00 44.33  ? 523 HOH   B O   1 
HETATM 8747 O  O   . HOH   CA 13 .   ? 15.772  -11.824 69.440 1.00 33.51  ? 524 HOH   B O   1 
HETATM 8748 O  O   . HOH   CA 13 .   ? 16.722  -33.000 59.059 1.00 43.49  ? 525 HOH   B O   1 
HETATM 8749 O  O   . HOH   CA 13 .   ? -5.724  -11.501 49.598 1.00 44.85  ? 526 HOH   B O   1 
HETATM 8750 O  O   . HOH   CA 13 .   ? 23.309  -22.785 51.693 1.00 30.25  ? 527 HOH   B O   1 
HETATM 8751 O  O   . HOH   CA 13 .   ? 11.684  -29.373 62.676 1.00 41.53  ? 528 HOH   B O   1 
HETATM 8752 O  O   . HOH   CA 13 .   ? 16.289  -16.956 46.687 1.00 43.22  ? 529 HOH   B O   1 
HETATM 8753 O  O   . HOH   CA 13 .   ? 26.654  -18.878 66.624 1.00 37.89  ? 530 HOH   B O   1 
HETATM 8754 O  O   . HOH   CA 13 .   ? 14.068  -7.990  66.652 1.00 38.37  ? 531 HOH   B O   1 
HETATM 8755 O  O   . HOH   CA 13 .   ? -2.809  7.288   60.238 1.00 44.34  ? 532 HOH   B O   1 
HETATM 8756 O  O   . HOH   CA 13 .   ? 13.581  -8.032  72.019 1.00 31.21  ? 533 HOH   B O   1 
HETATM 8757 O  O   . HOH   CA 13 .   ? 9.782   -6.782  36.541 1.00 41.07  ? 534 HOH   B O   1 
HETATM 8758 O  O   . HOH   CA 13 .   ? 18.494  2.485   49.211 1.00 39.13  ? 535 HOH   B O   1 
HETATM 8759 O  O   . HOH   CA 13 .   ? -3.966  3.783   55.483 1.00 41.44  ? 536 HOH   B O   1 
HETATM 8760 O  O   . HOH   CA 13 .   ? 5.659   -30.381 61.827 1.00 55.09  ? 537 HOH   B O   1 
HETATM 8761 O  O   . HOH   CA 13 .   ? -0.926  -16.329 52.469 1.00 43.23  ? 538 HOH   B O   1 
HETATM 8762 O  O   . HOH   CA 13 .   ? 10.033  9.516   54.178 1.00 45.64  ? 539 HOH   B O   1 
HETATM 8763 O  O   . HOH   CA 13 .   ? -12.638 2.041   64.893 1.00 41.91  ? 540 HOH   B O   1 
HETATM 8764 O  O   . HOH   CA 13 .   ? 24.869  -9.197  39.550 1.00 38.11  ? 541 HOH   B O   1 
HETATM 8765 O  O   . HOH   CA 13 .   ? 6.925   5.728   63.658 1.00 47.79  ? 542 HOH   B O   1 
HETATM 8766 O  O   . HOH   CA 13 .   ? 15.239  -4.200  35.051 1.00 41.45  ? 543 HOH   B O   1 
HETATM 8767 O  O   . HOH   CA 13 .   ? 13.978  -8.838  64.107 1.00 36.14  ? 544 HOH   B O   1 
HETATM 8768 O  O   . HOH   CA 13 .   ? 24.680  -22.787 49.150 1.00 37.54  ? 545 HOH   B O   1 
HETATM 8769 O  O   . HOH   CA 13 .   ? 5.009   1.440   48.159 1.00 40.95  ? 546 HOH   B O   1 
HETATM 8770 O  O   . HOH   CA 13 .   ? -12.680 -0.685  64.922 1.00 38.17  ? 547 HOH   B O   1 
HETATM 8771 O  O   . HOH   CA 13 .   ? 8.592   -13.527 47.371 1.00 30.99  ? 548 HOH   B O   1 
HETATM 8772 O  O   . HOH   CA 13 .   ? -1.983  -12.516 78.338 1.00 45.86  ? 549 HOH   B O   1 
HETATM 8773 O  O   . HOH   CA 13 .   ? 14.425  -8.620  75.796 1.00 39.67  ? 550 HOH   B O   1 
HETATM 8774 O  O   . HOH   CA 13 .   ? 19.610  -17.941 64.911 1.00 32.86  ? 551 HOH   B O   1 
HETATM 8775 O  O   . HOH   CA 13 .   ? 0.219   -10.103 47.299 1.00 37.38  ? 552 HOH   B O   1 
HETATM 8776 O  O   . HOH   CA 13 .   ? 8.967   -10.535 73.769 1.00 49.31  ? 553 HOH   B O   1 
HETATM 8777 O  O   . HOH   CA 13 .   ? 15.622  8.451   47.524 1.00 49.47  ? 554 HOH   B O   1 
HETATM 8778 O  O   . HOH   CA 13 .   ? 8.436   -24.309 69.279 1.00 38.18  ? 555 HOH   B O   1 
HETATM 8779 O  O   . HOH   CA 13 .   ? 27.415  -27.151 61.247 1.00 37.32  ? 556 HOH   B O   1 
HETATM 8780 O  O   . HOH   CA 13 .   ? 10.818  -26.261 53.599 1.00 46.32  ? 557 HOH   B O   1 
HETATM 8781 O  O   . HOH   CA 13 .   ? 19.666  -34.080 59.739 1.00 44.33  ? 558 HOH   B O   1 
HETATM 8782 O  O   . HOH   CA 13 .   ? 21.146  -0.054  51.754 1.00 36.77  ? 559 HOH   B O   1 
HETATM 8783 O  O   . HOH   CA 13 .   ? 0.561   -19.093 49.408 1.00 36.55  ? 560 HOH   B O   1 
HETATM 8784 O  O   . HOH   CA 13 .   ? -17.681 -5.136  62.156 1.00 43.09  ? 561 HOH   B O   1 
HETATM 8785 O  O   . HOH   CA 13 .   ? 16.022  -27.743 68.564 1.00 51.85  ? 562 HOH   B O   1 
HETATM 8786 O  O   . HOH   CA 13 .   ? -11.713 7.999   74.827 1.00 45.79  ? 563 HOH   B O   1 
HETATM 8787 O  O   . HOH   CA 13 .   ? 7.059   -22.283 50.380 1.00 40.65  ? 564 HOH   B O   1 
HETATM 8788 O  O   . HOH   CA 13 .   ? -13.349 2.980   67.765 1.00 43.90  ? 565 HOH   B O   1 
HETATM 8789 O  O   . HOH   CA 13 .   ? -2.297  -18.557 56.119 1.00 49.31  ? 566 HOH   B O   1 
HETATM 8790 O  O   . HOH   CA 13 .   ? 6.110   -0.033  45.987 1.00 43.47  ? 567 HOH   B O   1 
HETATM 8791 O  O   . HOH   CA 13 .   ? 25.418  -13.297 50.007 1.00 36.85  ? 568 HOH   B O   1 
HETATM 8792 O  O   . HOH   CA 13 .   ? 2.266   -6.758  41.622 1.00 43.60  ? 569 HOH   B O   1 
HETATM 8793 O  O   . HOH   CA 13 .   ? -2.459  -16.984 47.710 1.00 49.29  ? 570 HOH   B O   1 
HETATM 8794 O  O   . HOH   CA 13 .   ? 16.860  -15.551 42.812 1.00 48.70  ? 571 HOH   B O   1 
HETATM 8795 O  O   . HOH   CA 13 .   ? -16.705 -9.966  62.525 1.00 45.75  ? 572 HOH   B O   1 
HETATM 8796 O  O   . HOH   CA 13 .   ? 14.876  -9.283  69.306 1.00 40.89  ? 573 HOH   B O   1 
HETATM 8797 O  O   . HOH   CA 13 .   ? 22.548  -31.887 65.082 1.00 48.52  ? 574 HOH   B O   1 
HETATM 8798 O  O   . HOH   CA 13 .   ? 6.104   -2.456  70.709 1.00 48.88  ? 575 HOH   B O   1 
HETATM 8799 O  O   . HOH   CA 13 .   ? 12.743  -2.942  59.691 1.00 33.30  ? 576 HOH   B O   1 
HETATM 8800 O  O   . HOH   CA 13 .   ? 23.970  -3.302  52.945 1.00 43.02  ? 577 HOH   B O   1 
HETATM 8801 O  O   . HOH   CA 13 .   ? 19.056  -12.793 71.613 1.00 38.57  ? 578 HOH   B O   1 
HETATM 8802 O  O   . HOH   CA 13 .   ? 6.973   10.600  67.152 1.00 52.87  ? 579 HOH   B O   1 
HETATM 8803 O  O   . HOH   CA 13 .   ? 22.297  -13.652 47.040 1.00 40.43  ? 580 HOH   B O   1 
HETATM 8804 O  O   . HOH   CA 13 .   ? 19.614  -30.035 49.796 1.00 40.08  ? 581 HOH   B O   1 
HETATM 8805 O  O   . HOH   CA 13 .   ? -1.778  4.945   54.428 1.00 43.18  ? 582 HOH   B O   1 
HETATM 8806 O  O   . HOH   CA 13 .   ? 7.310   0.534   43.414 1.00 50.06  ? 583 HOH   B O   1 
HETATM 8807 O  O   . HOH   CA 13 .   ? 4.291   -9.606  72.628 1.00 40.54  ? 584 HOH   B O   1 
HETATM 8808 O  O   . HOH   CA 13 .   ? -0.047  -23.677 57.263 1.00 45.93  ? 585 HOH   B O   1 
HETATM 8809 O  O   . HOH   CA 13 .   ? 22.953  -7.753  68.217 1.00 37.58  ? 586 HOH   B O   1 
HETATM 8810 O  O   . HOH   CA 13 .   ? 28.243  -14.335 53.583 1.00 39.55  ? 587 HOH   B O   1 
HETATM 8811 O  O   . HOH   CA 13 .   ? 5.966   8.769   52.918 1.00 40.11  ? 588 HOH   B O   1 
HETATM 8812 O  O   . HOH   CA 13 .   ? -7.888  -18.939 66.652 1.00 49.94  ? 589 HOH   B O   1 
HETATM 8813 O  O   . HOH   CA 13 .   ? -17.388 -7.650  63.608 1.00 41.02  ? 590 HOH   B O   1 
HETATM 8814 O  O   . HOH   CA 13 .   ? 20.031  -4.005  42.547 1.00 42.72  ? 591 HOH   B O   1 
HETATM 8815 O  O   . HOH   CA 13 .   ? 0.239   0.213   75.620 1.00 44.12  ? 592 HOH   B O   1 
HETATM 8816 O  O   . HOH   CA 13 .   ? 20.412  -5.780  57.946 1.00 36.10  ? 593 HOH   B O   1 
HETATM 8817 O  O   . HOH   CA 13 .   ? 0.888   -10.739 59.237 1.00 54.66  ? 594 HOH   B O   1 
HETATM 8818 O  O   . HOH   CA 13 .   ? 5.876   -11.209 74.400 1.00 39.16  ? 595 HOH   B O   1 
HETATM 8819 O  O   . HOH   CA 13 .   ? 17.568  -2.314  71.471 1.00 49.87  ? 596 HOH   B O   1 
HETATM 8820 O  O   . HOH   CA 13 .   ? 2.013   -0.573  73.571 1.00 40.25  ? 597 HOH   B O   1 
HETATM 8821 O  O   . HOH   CA 13 .   ? 20.571  -28.057 45.548 1.00 49.26  ? 598 HOH   B O   1 
HETATM 8822 O  O   . HOH   CA 13 .   ? -2.944  -2.945  45.261 1.00 48.15  ? 599 HOH   B O   1 
HETATM 8823 O  O   . HOH   CA 13 .   ? -0.946  -22.374 70.208 1.00 45.73  ? 600 HOH   B O   1 
HETATM 8824 O  O   . HOH   CA 13 .   ? 6.373   -19.730 44.266 1.00 39.53  ? 601 HOH   B O   1 
HETATM 8825 O  O   . HOH   CA 13 .   ? -2.590  -10.397 47.960 1.00 36.23  ? 602 HOH   B O   1 
HETATM 8826 O  O   . HOH   CA 13 .   ? 17.924  -6.579  56.709 1.00 33.58  ? 603 HOH   B O   1 
HETATM 8827 O  O   . HOH   CA 13 .   ? -3.512  -4.963  76.679 1.00 53.61  ? 604 HOH   B O   1 
HETATM 8828 O  O   . HOH   CA 13 .   ? -6.672  -1.554  45.612 1.00 48.75  ? 605 HOH   B O   1 
HETATM 8829 O  O   . HOH   CA 13 .   ? 5.997   -24.409 76.892 1.00 51.95  ? 606 HOH   B O   1 
HETATM 8830 O  O   . HOH   CA 13 .   ? -9.928  -4.777  74.318 1.00 41.15  ? 607 HOH   B O   1 
HETATM 8831 O  O   . HOH   CA 13 .   ? 16.832  3.672   64.077 1.00 45.17  ? 608 HOH   B O   1 
HETATM 8832 O  O   . HOH   CA 13 .   ? 22.317  -4.256  60.696 1.00 44.50  ? 609 HOH   B O   1 
HETATM 8833 O  O   . HOH   CA 13 .   ? 27.784  -15.075 56.767 1.00 40.31  ? 610 HOH   B O   1 
HETATM 8834 O  O   . HOH   CA 13 .   ? -7.520  -18.379 61.049 1.00 45.67  ? 611 HOH   B O   1 
HETATM 8835 O  O   . HOH   CA 13 .   ? -4.665  10.513  74.856 1.00 48.75  ? 612 HOH   B O   1 
HETATM 8836 O  O   . HOH   CA 13 .   ? 4.342   -15.297 82.088 1.00 47.83  ? 613 HOH   B O   1 
HETATM 8837 O  O   . HOH   CA 13 .   ? -7.711  18.318  65.337 1.00 55.38  ? 614 HOH   B O   1 
HETATM 8838 O  O   . HOH   CA 13 .   ? 12.932  7.390   48.220 1.00 51.40  ? 615 HOH   B O   1 
HETATM 8839 O  O   . HOH   CA 13 .   ? 15.064  4.981   68.601 1.00 56.49  ? 616 HOH   B O   1 
HETATM 8840 O  O   . HOH   CA 13 .   ? -7.673  -9.744  50.008 1.00 43.36  ? 617 HOH   B O   1 
HETATM 8841 O  O   . HOH   CA 13 .   ? 19.339  1.509   37.851 1.00 43.11  ? 618 HOH   B O   1 
HETATM 8842 O  O   . HOH   CA 13 .   ? 11.983  0.158   73.243 1.00 45.02  ? 619 HOH   B O   1 
HETATM 8843 O  O   . HOH   CA 13 .   ? 16.165  2.455   68.599 1.00 57.38  ? 620 HOH   B O   1 
HETATM 8844 O  O   . HOH   CA 13 .   ? 12.521  -22.723 82.626 1.00 47.88  ? 621 HOH   B O   1 
HETATM 8845 O  O   . HOH   CA 13 .   ? -10.264 -16.795 68.174 1.00 53.86  ? 622 HOH   B O   1 
HETATM 8846 O  O   . HOH   CA 13 .   ? -2.051  -3.276  41.507 1.00 48.41  ? 623 HOH   B O   1 
HETATM 8847 O  O   . HOH   CA 13 .   ? 5.557   -13.318 82.602 1.00 52.47  ? 624 HOH   B O   1 
HETATM 8848 O  O   . HOH   CA 13 .   ? 25.108  10.600  53.013 1.00 52.66  ? 625 HOH   B O   1 
HETATM 8849 O  O   . HOH   CA 13 .   ? 0.173   -22.211 59.436 1.00 49.09  ? 626 HOH   B O   1 
HETATM 8850 O  O   . HOH   CA 13 .   ? 25.487  1.159   52.974 1.00 34.47  ? 627 HOH   B O   1 
HETATM 8851 O  O   . HOH   CA 13 .   ? 4.961   -9.862  76.609 1.00 48.38  ? 628 HOH   B O   1 
HETATM 8852 O  O   . HOH   CA 13 .   ? 3.088   3.121   46.915 1.00 41.92  ? 629 HOH   B O   1 
HETATM 8853 O  O   . HOH   CA 13 .   ? 8.255   3.041   44.352 1.00 55.18  ? 630 HOH   B O   1 
HETATM 8854 O  O   . HOH   CA 13 .   ? 1.969   -17.556 62.500 1.00 57.05  ? 631 HOH   B O   1 
HETATM 8855 O  O   . HOH   CA 13 .   ? 24.235  -4.108  72.074 1.00 44.81  ? 632 HOH   B O   1 
HETATM 8856 O  O   . HOH   CA 13 .   ? 13.734  8.708   50.619 1.00 52.20  ? 633 HOH   B O   1 
HETATM 8857 O  O   . HOH   CA 13 .   ? 6.924   -11.687 86.906 1.00 45.74  ? 634 HOH   B O   1 
HETATM 8858 O  O   . HOH   CA 13 .   ? 19.247  -33.937 66.470 1.00 51.60  ? 635 HOH   B O   1 
HETATM 8859 O  O   . HOH   CA 13 .   ? 26.667  -16.676 53.569 1.00 54.74  ? 636 HOH   B O   1 
HETATM 8860 O  O   . HOH   CA 13 .   ? -10.351 -16.295 70.876 1.00 51.33  ? 637 HOH   B O   1 
HETATM 8861 O  O   . HOH   CA 13 .   ? 26.517  -21.360 65.994 1.00 41.34  ? 638 HOH   B O   1 
HETATM 8862 O  O   . HOH   CA 13 .   ? 18.186  -17.217 40.545 1.00 51.06  ? 639 HOH   B O   1 
HETATM 8863 O  O   . HOH   CA 13 .   ? 1.304   -27.941 67.719 1.00 50.88  ? 640 HOH   B O   1 
HETATM 8864 O  O   . HOH   CA 13 .   ? 27.805  -10.068 66.423 1.00 52.72  ? 641 HOH   B O   1 
HETATM 8865 O  O   . HOH   CA 13 .   ? 16.032  -19.430 40.603 1.00 46.63  ? 642 HOH   B O   1 
HETATM 8866 O  O   . HOH   CA 13 .   ? 28.385  -6.445  56.690 1.00 36.53  ? 643 HOH   B O   1 
HETATM 8867 O  O   . HOH   CA 13 .   ? 1.257   -13.520 58.436 1.00 45.95  ? 644 HOH   B O   1 
HETATM 8868 O  O   . HOH   CA 13 .   ? 7.401   -24.772 50.621 1.00 42.46  ? 645 HOH   B O   1 
HETATM 8869 O  O   . HOH   CA 13 .   ? 16.605  2.022   34.035 1.00 50.98  ? 646 HOH   B O   1 
HETATM 8870 O  O   . HOH   CA 13 .   ? 16.294  -24.881 44.932 1.00 46.27  ? 647 HOH   B O   1 
HETATM 8871 O  O   . HOH   CA 13 .   ? -4.245  -12.218 47.315 1.00 42.18  ? 648 HOH   B O   1 
HETATM 8872 O  O   . HOH   CA 13 .   ? -4.197  -14.912 47.451 1.00 44.86  ? 649 HOH   B O   1 
HETATM 8873 O  O   . HOH   CA 13 .   ? -5.642  -11.542 45.173 1.00 49.00  ? 650 HOH   B O   1 
HETATM 8874 O  O   . HOH   CA 13 .   ? 26.344  5.906   46.553 1.00 43.42  ? 651 HOH   B O   1 
HETATM 8875 O  O   . HOH   CA 13 .   ? 21.709  -10.958 84.058 1.00 47.83  ? 652 HOH   B O   1 
HETATM 8876 O  O   . HOH   CA 13 .   ? 21.867  -0.619  58.643 1.00 46.14  ? 653 HOH   B O   1 
HETATM 8877 O  O   . HOH   CA 13 .   ? -8.616  -11.721 46.029 1.00 46.20  ? 654 HOH   B O   1 
HETATM 8878 O  O   . HOH   DA 13 .   ? 18.353  -4.245  24.566 1.00 34.03  ? 501 HOH   C O   1 
HETATM 8879 O  O   . HOH   DA 13 .   ? -10.977 29.615  12.509 1.00 46.52  ? 502 HOH   C O   1 
HETATM 8880 O  O   . HOH   DA 13 .   ? -12.968 13.160  3.145  1.00 38.59  ? 503 HOH   C O   1 
HETATM 8881 O  O   . HOH   DA 13 .   ? -9.876  12.572  23.708 1.00 37.53  ? 504 HOH   C O   1 
HETATM 8882 O  O   . HOH   DA 13 .   ? 11.881  3.251   14.492 1.00 29.33  ? 505 HOH   C O   1 
HETATM 8883 O  O   . HOH   DA 13 .   ? -0.678  17.826  30.966 1.00 41.70  ? 506 HOH   C O   1 
HETATM 8884 O  O   . HOH   DA 13 .   ? -13.427 13.979  29.981 1.00 45.17  ? 507 HOH   C O   1 
HETATM 8885 O  O   . HOH   DA 13 .   ? 7.382   3.367   4.415  1.00 33.22  ? 508 HOH   C O   1 
HETATM 8886 O  O   . HOH   DA 13 .   ? -4.138  2.935   32.309 1.00 39.41  ? 509 HOH   C O   1 
HETATM 8887 O  O   . HOH   DA 13 .   ? -0.579  10.656  5.896  1.00 57.87  ? 510 HOH   C O   1 
HETATM 8888 O  O   . HOH   DA 13 .   ? -23.244 16.027  9.571  1.00 45.80  ? 511 HOH   C O   1 
HETATM 8889 O  O   . HOH   DA 13 .   ? -15.401 -1.324  4.730  1.00 61.01  ? 512 HOH   C O   1 
HETATM 8890 O  O   . HOH   DA 13 .   ? 4.323   -0.489  25.578 1.00 30.42  ? 513 HOH   C O   1 
HETATM 8891 O  O   . HOH   DA 13 .   ? 2.287   -2.247  5.528  1.00 42.10  ? 514 HOH   C O   1 
HETATM 8892 O  O   . HOH   DA 13 .   ? -21.561 -1.727  3.262  1.00 48.04  ? 515 HOH   C O   1 
HETATM 8893 O  O   . HOH   DA 13 .   ? 1.359   -5.457  13.612 1.00 33.08  ? 516 HOH   C O   1 
HETATM 8894 O  O   . HOH   DA 13 .   ? -1.056  -10.514 16.546 1.00 42.38  ? 517 HOH   C O   1 
HETATM 8895 O  O   . HOH   DA 13 .   ? -25.863 -0.966  11.012 1.00 46.01  ? 518 HOH   C O   1 
HETATM 8896 O  O   . HOH   DA 13 .   ? -2.321  13.338  21.651 1.00 50.84  ? 519 HOH   C O   1 
HETATM 8897 O  O   . HOH   DA 13 .   ? -8.628  17.820  27.226 1.00 47.46  ? 520 HOH   C O   1 
HETATM 8898 O  O   . HOH   DA 13 .   ? 2.512   -5.405  16.099 1.00 29.74  ? 521 HOH   C O   1 
HETATM 8899 O  O   . HOH   DA 13 .   ? -20.783 -4.206  23.418 1.00 37.97  ? 522 HOH   C O   1 
HETATM 8900 O  O   . HOH   DA 13 .   ? -5.018  15.492  29.364 1.00 43.04  ? 523 HOH   C O   1 
HETATM 8901 O  O   . HOH   DA 13 .   ? -14.956 8.604   6.872  1.00 34.98  ? 524 HOH   C O   1 
HETATM 8902 O  O   . HOH   DA 13 .   ? -0.888  17.745  27.093 1.00 47.53  ? 525 HOH   C O   1 
HETATM 8903 O  O   . HOH   DA 13 .   ? 1.819   6.878   27.033 1.00 37.64  ? 526 HOH   C O   1 
HETATM 8904 O  O   . HOH   DA 13 .   ? 3.846   5.846   28.654 1.00 44.83  ? 527 HOH   C O   1 
HETATM 8905 O  O   . HOH   DA 13 .   ? -9.980  -5.037  12.190 1.00 34.76  ? 528 HOH   C O   1 
HETATM 8906 O  O   . HOH   DA 13 .   ? 21.592  -7.023  29.933 1.00 33.13  ? 529 HOH   C O   1 
HETATM 8907 O  O   . HOH   DA 13 .   ? -10.413 19.700  6.363  1.00 45.48  ? 530 HOH   C O   1 
HETATM 8908 O  O   . HOH   DA 13 .   ? 10.344  -2.530  30.694 1.00 40.36  ? 531 HOH   C O   1 
HETATM 8909 O  O   . HOH   DA 13 .   ? -15.259 22.262  23.245 1.00 44.58  ? 532 HOH   C O   1 
HETATM 8910 O  O   . HOH   DA 13 .   ? 5.192   -1.260  7.164  1.00 43.26  ? 533 HOH   C O   1 
HETATM 8911 O  O   . HOH   DA 13 .   ? -4.562  -9.159  14.291 1.00 42.35  ? 534 HOH   C O   1 
HETATM 8912 O  O   . HOH   DA 13 .   ? 0.746   13.922  25.438 1.00 46.78  ? 535 HOH   C O   1 
HETATM 8913 O  O   . HOH   DA 13 .   ? -2.102  7.813   25.602 1.00 31.72  ? 536 HOH   C O   1 
HETATM 8914 O  O   . HOH   DA 13 .   ? -8.390  12.950  25.942 1.00 42.38  ? 537 HOH   C O   1 
HETATM 8915 O  O   . HOH   DA 13 .   ? 18.900  1.640   23.401 1.00 30.10  ? 538 HOH   C O   1 
HETATM 8916 O  O   . HOH   DA 13 .   ? 3.565   -6.496  19.480 1.00 30.91  ? 539 HOH   C O   1 
HETATM 8917 O  O   . HOH   DA 13 .   ? 13.566  4.254   32.567 1.00 40.57  ? 540 HOH   C O   1 
HETATM 8918 O  O   . HOH   DA 13 .   ? 0.696   9.216   27.218 1.00 46.03  ? 541 HOH   C O   1 
HETATM 8919 O  O   . HOH   DA 13 .   ? 15.856  2.807   7.404  1.00 40.19  ? 542 HOH   C O   1 
HETATM 8920 O  O   . HOH   DA 13 .   ? 2.840   -15.606 16.528 1.00 44.31  ? 543 HOH   C O   1 
HETATM 8921 O  O   . HOH   DA 13 .   ? -0.880  -6.358  29.637 1.00 36.40  ? 544 HOH   C O   1 
HETATM 8922 O  O   . HOH   DA 13 .   ? -9.135  22.794  29.544 1.00 47.44  ? 545 HOH   C O   1 
HETATM 8923 O  O   . HOH   DA 13 .   ? 1.807   0.322   4.799  1.00 32.57  ? 546 HOH   C O   1 
HETATM 8924 O  O   . HOH   DA 13 .   ? -3.011  -3.411  0.981  1.00 38.29  ? 547 HOH   C O   1 
HETATM 8925 O  O   . HOH   DA 13 .   ? -23.472 1.532   25.035 1.00 31.80  ? 548 HOH   C O   1 
HETATM 8926 O  O   . HOH   DA 13 .   ? -2.935  -1.491  26.447 1.00 27.59  ? 549 HOH   C O   1 
HETATM 8927 O  O   . HOH   DA 13 .   ? 14.136  8.504   4.758  1.00 34.11  ? 550 HOH   C O   1 
HETATM 8928 O  O   . HOH   DA 13 .   ? -7.847  13.063  1.622  1.00 41.02  ? 551 HOH   C O   1 
HETATM 8929 O  O   . HOH   DA 13 .   ? -0.842  -6.876  14.775 1.00 30.75  ? 552 HOH   C O   1 
HETATM 8930 O  O   . HOH   DA 13 .   ? -4.575  11.737  4.338  1.00 38.05  ? 553 HOH   C O   1 
HETATM 8931 O  O   . HOH   DA 13 .   ? -18.638 -2.294  5.848  1.00 48.36  ? 554 HOH   C O   1 
HETATM 8932 O  O   . HOH   DA 13 .   ? -26.949 11.357  13.655 1.00 52.78  ? 555 HOH   C O   1 
HETATM 8933 O  O   . HOH   DA 13 .   ? -13.030 17.350  4.097  1.00 46.27  ? 556 HOH   C O   1 
HETATM 8934 O  O   . HOH   DA 13 .   ? 16.105  -1.241  16.983 1.00 28.09  ? 557 HOH   C O   1 
HETATM 8935 O  O   . HOH   DA 13 .   ? 21.798  0.010   16.564 1.00 32.54  ? 558 HOH   C O   1 
HETATM 8936 O  O   . HOH   DA 13 .   ? 5.052   -4.869  26.318 1.00 30.72  ? 559 HOH   C O   1 
HETATM 8937 O  O   . HOH   DA 13 .   ? 13.773  -1.467  15.072 1.00 27.33  ? 560 HOH   C O   1 
HETATM 8938 O  O   . HOH   DA 13 .   ? 3.371   9.531   30.129 1.00 47.48  ? 561 HOH   C O   1 
HETATM 8939 O  O   . HOH   DA 13 .   ? 13.563  1.100   14.032 1.00 30.46  ? 562 HOH   C O   1 
HETATM 8940 O  O   . HOH   DA 13 .   ? 18.488  2.336   27.925 1.00 43.34  ? 563 HOH   C O   1 
HETATM 8941 O  O   . HOH   DA 13 .   ? -7.799  4.145   3.636  1.00 26.82  ? 564 HOH   C O   1 
HETATM 8942 O  O   . HOH   DA 13 .   ? 12.188  11.303  24.798 1.00 46.34  ? 565 HOH   C O   1 
HETATM 8943 O  O   . HOH   DA 13 .   ? 0.954   2.593   2.177  1.00 34.57  ? 566 HOH   C O   1 
HETATM 8944 O  O   . HOH   DA 13 .   ? 6.503   15.924  25.931 1.00 45.34  ? 567 HOH   C O   1 
HETATM 8945 O  O   . HOH   DA 13 .   ? -28.312 9.596   12.208 1.00 44.36  ? 568 HOH   C O   1 
HETATM 8946 O  O   . HOH   DA 13 .   ? 4.787   13.927  23.770 1.00 42.39  ? 569 HOH   C O   1 
HETATM 8947 O  O   . HOH   DA 13 .   ? -5.351  -3.602  3.867  1.00 47.03  ? 570 HOH   C O   1 
HETATM 8948 O  O   . HOH   DA 13 .   ? -9.409  1.439   -4.408 1.00 31.01  ? 571 HOH   C O   1 
HETATM 8949 O  O   . HOH   DA 13 .   ? -1.922  6.045   0.995  1.00 37.10  ? 572 HOH   C O   1 
HETATM 8950 O  O   . HOH   DA 13 .   ? -10.628 5.471   22.789 1.00 31.94  ? 573 HOH   C O   1 
HETATM 8951 O  O   . HOH   DA 13 .   ? -12.951 -0.960  2.241  1.00 44.94  ? 574 HOH   C O   1 
HETATM 8952 O  O   . HOH   DA 13 .   ? -27.250 3.345   1.406  1.00 51.41  ? 575 HOH   C O   1 
HETATM 8953 O  O   . HOH   DA 13 .   ? 0.495   11.918  14.799 1.00 54.38  ? 576 HOH   C O   1 
HETATM 8954 O  O   . HOH   DA 13 .   ? -10.297 20.408  29.951 1.00 45.74  ? 577 HOH   C O   1 
HETATM 8955 O  O   . HOH   DA 13 .   ? 3.755   1.937   5.742  1.00 35.73  ? 578 HOH   C O   1 
HETATM 8956 O  O   . HOH   DA 13 .   ? 11.367  -11.130 26.643 1.00 37.96  ? 579 HOH   C O   1 
HETATM 8957 O  O   . HOH   DA 13 .   ? -26.358 0.183   13.875 1.00 44.34  ? 580 HOH   C O   1 
HETATM 8958 O  O   . HOH   DA 13 .   ? -12.392 -3.964  10.561 1.00 38.40  ? 581 HOH   C O   1 
HETATM 8959 O  O   . HOH   DA 13 .   ? -22.212 17.571  -1.783 1.00 58.93  ? 582 HOH   C O   1 
HETATM 8960 O  O   . HOH   DA 13 .   ? -1.476  12.396  7.874  1.00 59.33  ? 583 HOH   C O   1 
HETATM 8961 O  O   . HOH   DA 13 .   ? -24.349 -5.492  23.649 1.00 41.00  ? 584 HOH   C O   1 
HETATM 8962 O  O   . HOH   DA 13 .   ? -15.130 12.374  1.085  1.00 40.57  ? 585 HOH   C O   1 
HETATM 8963 O  O   . HOH   DA 13 .   ? 15.749  -10.596 20.875 1.00 37.51  ? 586 HOH   C O   1 
HETATM 8964 O  O   . HOH   DA 13 .   ? 16.362  4.171   29.009 1.00 32.96  ? 587 HOH   C O   1 
HETATM 8965 O  O   . HOH   DA 13 .   ? -11.402 -2.908  0.285  1.00 42.16  ? 588 HOH   C O   1 
HETATM 8966 O  O   . HOH   DA 13 .   ? 3.828   0.567   28.142 1.00 29.67  ? 589 HOH   C O   1 
HETATM 8967 O  O   . HOH   DA 13 .   ? -14.689 23.001  6.423  1.00 52.23  ? 590 HOH   C O   1 
HETATM 8968 O  O   . HOH   DA 13 .   ? 0.946   8.863   33.042 1.00 49.04  ? 591 HOH   C O   1 
HETATM 8969 O  O   . HOH   DA 13 .   ? 11.645  17.154  10.321 1.00 50.32  ? 592 HOH   C O   1 
HETATM 8970 O  O   . HOH   DA 13 .   ? -8.089  10.224  33.506 1.00 46.50  ? 593 HOH   C O   1 
HETATM 8971 O  O   . HOH   DA 13 .   ? -8.130  -2.234  5.390  1.00 45.09  ? 594 HOH   C O   1 
HETATM 8972 O  O   . HOH   DA 13 .   ? -0.519  -4.471  31.521 1.00 42.08  ? 595 HOH   C O   1 
HETATM 8973 O  O   . HOH   DA 13 .   ? 20.316  4.221   16.183 1.00 42.38  ? 596 HOH   C O   1 
HETATM 8974 O  O   . HOH   DA 13 .   ? -16.817 8.406   21.645 1.00 42.21  ? 597 HOH   C O   1 
HETATM 8975 O  O   . HOH   DA 13 .   ? 15.720  7.885   26.246 1.00 42.13  ? 598 HOH   C O   1 
HETATM 8976 O  O   . HOH   DA 13 .   ? 16.025  -5.831  12.018 1.00 46.68  ? 599 HOH   C O   1 
HETATM 8977 O  O   . HOH   DA 13 .   ? 8.874   18.612  9.199  1.00 49.76  ? 600 HOH   C O   1 
HETATM 8978 O  O   . HOH   DA 13 .   ? -13.818 1.556   29.484 1.00 41.02  ? 601 HOH   C O   1 
HETATM 8979 O  O   . HOH   DA 13 .   ? -20.600 -2.842  20.892 1.00 41.06  ? 602 HOH   C O   1 
HETATM 8980 O  O   . HOH   DA 13 .   ? 21.697  -5.878  16.607 1.00 32.18  ? 603 HOH   C O   1 
HETATM 8981 O  O   . HOH   DA 13 .   ? -19.323 -8.630  16.863 1.00 46.06  ? 604 HOH   C O   1 
HETATM 8982 O  O   . HOH   DA 13 .   ? -5.175  4.320   2.739  1.00 29.90  ? 605 HOH   C O   1 
HETATM 8983 O  O   . HOH   DA 13 .   ? 17.917  -11.760 23.492 1.00 43.89  ? 606 HOH   C O   1 
HETATM 8984 O  O   . HOH   DA 13 .   ? -22.444 0.936   -0.046 1.00 47.40  ? 607 HOH   C O   1 
HETATM 8985 O  O   . HOH   DA 13 .   ? -11.160 2.098   30.430 1.00 43.91  ? 608 HOH   C O   1 
HETATM 8986 O  O   . HOH   DA 13 .   ? -2.011  -12.732 22.305 1.00 54.00  ? 609 HOH   C O   1 
HETATM 8987 O  O   . HOH   DA 13 .   ? 16.450  5.230   7.386  1.00 38.06  ? 610 HOH   C O   1 
HETATM 8988 O  O   . HOH   DA 13 .   ? -6.817  2.563   33.637 1.00 39.80  ? 611 HOH   C O   1 
HETATM 8989 O  O   . HOH   DA 13 .   ? 4.375   24.641  13.685 1.00 45.20  ? 612 HOH   C O   1 
HETATM 8990 O  O   . HOH   DA 13 .   ? 2.204   17.866  25.629 1.00 41.84  ? 613 HOH   C O   1 
HETATM 8991 O  O   . HOH   DA 13 .   ? 13.075  17.761  12.212 1.00 50.50  ? 614 HOH   C O   1 
HETATM 8992 O  O   . HOH   DA 13 .   ? 15.795  12.641  10.111 1.00 47.59  ? 615 HOH   C O   1 
HETATM 8993 O  O   . HOH   DA 13 .   ? -7.716  -9.479  19.342 1.00 42.51  ? 616 HOH   C O   1 
HETATM 8994 O  O   . HOH   DA 13 .   ? -9.003  -9.782  12.821 1.00 44.84  ? 617 HOH   C O   1 
HETATM 8995 O  O   . HOH   DA 13 .   ? 8.717   7.207   28.788 1.00 43.82  ? 618 HOH   C O   1 
HETATM 8996 O  O   . HOH   DA 13 .   ? -14.942 -8.463  21.951 1.00 47.51  ? 619 HOH   C O   1 
HETATM 8997 O  O   . HOH   DA 13 .   ? 3.693   3.564   2.060  1.00 32.79  ? 620 HOH   C O   1 
HETATM 8998 O  O   . HOH   DA 13 .   ? 5.225   -7.296  27.456 1.00 41.63  ? 621 HOH   C O   1 
HETATM 8999 O  O   . HOH   DA 13 .   ? -10.066 -10.879 17.847 1.00 42.86  ? 622 HOH   C O   1 
HETATM 9000 O  O   . HOH   DA 13 .   ? -16.255 6.664   -4.443 1.00 40.49  ? 623 HOH   C O   1 
HETATM 9001 O  O   . HOH   DA 13 .   ? -16.188 -8.773  19.253 1.00 43.80  ? 624 HOH   C O   1 
HETATM 9002 O  O   . HOH   DA 13 .   ? 12.286  -12.735 14.533 1.00 58.44  ? 625 HOH   C O   1 
HETATM 9003 O  O   . HOH   DA 13 .   ? -2.467  -5.688  3.133  1.00 37.40  ? 626 HOH   C O   1 
HETATM 9004 O  O   . HOH   DA 13 .   ? 14.386  -3.091  9.803  1.00 57.40  ? 627 HOH   C O   1 
HETATM 9005 O  O   . HOH   DA 13 .   ? 11.915  -14.661 25.691 1.00 48.48  ? 628 HOH   C O   1 
HETATM 9006 O  O   . HOH   DA 13 .   ? 2.759   12.640  3.197  1.00 51.82  ? 629 HOH   C O   1 
HETATM 9007 O  O   . HOH   DA 13 .   ? -1.835  19.777  7.366  1.00 45.31  ? 630 HOH   C O   1 
HETATM 9008 O  O   . HOH   DA 13 .   ? -7.934  5.035   33.377 1.00 42.32  ? 631 HOH   C O   1 
HETATM 9009 O  O   . HOH   DA 13 .   ? -2.149  -9.009  14.101 1.00 36.66  ? 632 HOH   C O   1 
HETATM 9010 O  O   . HOH   DA 13 .   ? -6.421  -7.110  10.112 1.00 44.27  ? 633 HOH   C O   1 
HETATM 9011 O  O   . HOH   DA 13 .   ? 19.138  4.869   18.784 1.00 44.76  ? 634 HOH   C O   1 
HETATM 9012 O  O   . HOH   DA 13 .   ? 14.199  13.717  21.915 1.00 52.75  ? 635 HOH   C O   1 
HETATM 9013 O  O   . HOH   DA 13 .   ? 1.266   10.418  4.312  1.00 47.89  ? 636 HOH   C O   1 
HETATM 9014 O  O   . HOH   DA 13 .   ? -5.997  -11.514 15.817 1.00 49.98  ? 637 HOH   C O   1 
HETATM 9015 O  O   . HOH   DA 13 .   ? -15.958 -11.194 24.921 1.00 60.54  ? 638 HOH   C O   1 
HETATM 9016 O  O   . HOH   DA 13 .   ? -26.603 12.221  1.781  1.00 63.07  ? 639 HOH   C O   1 
HETATM 9017 O  O   . HOH   DA 13 .   ? -1.383  8.419   -0.225 1.00 37.31  ? 640 HOH   C O   1 
HETATM 9018 O  O   . HOH   DA 13 .   ? 7.633   -3.712  7.428  1.00 48.17  ? 641 HOH   C O   1 
HETATM 9019 O  O   . HOH   DA 13 .   ? -25.205 13.127  3.921  1.00 56.92  ? 642 HOH   C O   1 
HETATM 9020 O  O   . HOH   DA 13 .   ? 12.354  -4.127  29.426 1.00 38.62  ? 643 HOH   C O   1 
HETATM 9021 O  O   . HOH   DA 13 .   ? 8.803   6.182   31.248 1.00 44.09  ? 644 HOH   C O   1 
HETATM 9022 O  O   . HOH   DA 13 .   ? 2.124   5.979   33.367 1.00 49.49  ? 645 HOH   C O   1 
HETATM 9023 O  O   . HOH   DA 13 .   ? 19.189  -12.878 18.899 1.00 45.72  ? 646 HOH   C O   1 
HETATM 9024 O  O   . HOH   DA 13 .   ? 12.589  -5.220  11.526 1.00 44.84  ? 647 HOH   C O   1 
HETATM 9025 O  O   . HOH   DA 13 .   ? 13.112  -5.070  34.117 1.00 35.35  ? 648 HOH   C O   1 
HETATM 9026 O  O   . HOH   DA 13 .   ? 0.360   4.207   33.910 1.00 51.81  ? 649 HOH   C O   1 
HETATM 9027 O  O   . HOH   DA 13 .   ? -5.326  -8.892  11.533 1.00 47.26  ? 650 HOH   C O   1 
HETATM 9028 O  O   . HOH   DA 13 .   ? -13.646 -4.387  -0.987 1.00 54.25  ? 651 HOH   C O   1 
HETATM 9029 O  O   . HOH   DA 13 .   ? 4.317   5.044   -0.331 1.00 35.52  ? 652 HOH   C O   1 
HETATM 9030 O  O   . HOH   DA 13 .   ? 18.654  -0.524  32.932 1.00 43.22  ? 653 HOH   C O   1 
HETATM 9031 O  O   . HOH   DA 13 .   ? 12.907  -7.214  32.986 1.00 38.15  ? 654 HOH   C O   1 
HETATM 9032 O  O   . HOH   DA 13 .   ? 21.813  -13.597 16.970 1.00 56.45  ? 655 HOH   C O   1 
# 
