data_9HED
# 
_entry.id   9HED 
# 
_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   9HED         pdb_00009hed 10.2210/pdb9hed/pdb 
WWPDB D_1292137858 ?            ?                   
# 
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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Source and taxonomy' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            entity_src_gen 
# 
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                        9HED 
_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 . 9HEC 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   2   ?        ? ? ? 
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 
;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   ?        ? ? ? 
5  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   ?        ? ? ? 
6  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   1   
?        ? ? ? 
7  non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
8  non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   5   ?        ? ? ? 
9  non-polymer syn GLYCEROL 92.094    3   ?        ? ? ? 
10 non-polymer syn alpha-damascone 192.297   3   ?        ? ? ? 
11 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
12 non-polymer syn 'SULFATE ION' 96.063    9   ?        ? ? ? 
13 water       nat water 18.015    310 ?        ? ? ? 
# 
_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  'PROTOPORPHYRIN IX CONTAINING FE'                     HEM   
8  '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE   
9  GLYCEROL                                              GOL   
10 alpha-damascone                                       A1IUA 
11 'MAGNESIUM ION'                                       MG    
12 'SULFATE ION'                                         SO4   
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 'DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
8  4 '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 
9  4 '[][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   ?     
10 5 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
11 5 '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 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   
?     
13 6 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 '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 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-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 4 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
14 4 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
15 4 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
16 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
17 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
18 5 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
19 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
20 6 3 BMA C1 O1 2 NAG O4 HO4 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 
A1IUA non-polymer                   . alpha-damascone                                       
'(~{E})-1-(2,6,6-trimethylcyclohex-2-en-1-yl)but-2-en-1-one' 'C13 H20 O'        192.297 
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 
EPE   non-polymer                   . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'   238.305 
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 H NAG 1 A NAG 402 n 
D 2 NAG 2 H NAG 2 A NAG 403 n 
D 2 BMA 3 H BMA 3 A BMA 425 n 
D 2 MAN 4 H MAN 4 A MAN 427 n 
D 2 MAN 5 H MAN 5 A MAN 426 n 
E 3 NAG 1 J NAG 1 A NAG 404 n 
E 3 NAG 2 J NAG 2 A NAG 405 n 
E 3 BMA 3 J BMA 3 A BMA 406 n 
E 3 MAN 4 J MAN 4 A MAN 407 n 
E 3 MAN 5 J MAN 5 A MAN 408 n 
E 3 MAN 6 J MAN 6 A MAN 409 n 
E 3 MAN 7 J MAN 7 A MAN 414 n 
F 2 NAG 1 Y NAG 1 B NAG 402 n 
F 2 NAG 2 Y NAG 2 B NAG 413 n 
F 2 BMA 3 Y BMA 3 B BMA 416 n 
F 2 MAN 4 Y MAN 4 B MAN 420 n 
F 2 MAN 5 Y MAN 5 B MAN 421 n 
G 4 NAG 1 Z NAG 1 B NAG 404 n 
G 4 NAG 2 Z NAG 2 B NAG 405 n 
G 4 BMA 3 Z BMA 3 B BMA 406 n 
G 4 MAN 4 Z MAN 4 B MAN 408 n 
G 4 MAN 5 Z MAN 5 B MAN 409 n 
G 4 MAN 6 Z MAN 6 B MAN 407 n 
H 5 NAG 1 m NAG 1 C NAG 402 n 
H 5 NAG 2 m NAG 2 C NAG 417 n 
H 5 BMA 3 m BMA 3 C BMA 418 n 
H 5 MAN 4 m MAN 4 C MAN 419 n 
I 6 NAG 1 n NAG 1 C NAG 404 n 
I 6 NAG 2 n NAG 2 C NAG 405 n 
I 6 BMA 3 n 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 A1IUA ? ? A1IUA ? ? '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  HEM   1   401 401 HEM   HEM A . 
K  8  EPE   1   402 430 EPE   EPE A . 
L  8  EPE   1   403 431 EPE   EPE A . 
M  9  GOL   1   404 432 GOL   GOL A . 
N  10 A1IUA 1   405 433 A1IUA DMC A . 
O  11 MG    1   406 1   MG    MG  A . 
P  12 SO4   1   407 2   SO4   SO4 A . 
Q  12 SO4   1   408 4   SO4   SO4 A . 
R  12 SO4   1   409 6   SO4   SO4 A . 
S  12 SO4   1   410 9   SO4   SO4 A . 
T  7  HEM   1   401 401 HEM   HEM B . 
U  9  GOL   1   402 418 GOL   GOL B . 
V  10 A1IUA 1   403 419 A1IUA DMC B . 
W  11 MG    1   404 2   MG    MG  B . 
X  12 SO4   1   405 1   SO4   SO4 B . 
Y  12 SO4   1   406 5   SO4   SO4 B . 
Z  12 SO4   1   407 7   SO4   SO4 B . 
AA 12 SO4   1   408 8   SO4   SO4 B . 
BA 12 SO4   1   409 11  SO4   SO4 B . 
CA 7  HEM   1   401 401 HEM   HEM C . 
DA 10 A1IUA 1   402 412 A1IUA DMC C . 
EA 8  EPE   1   403 413 EPE   EPE C . 
FA 8  EPE   1   404 414 EPE   EPE C . 
GA 8  EPE   1   405 415 EPE   EPE C . 
HA 9  GOL   1   406 416 GOL   GOL C . 
IA 11 MG    1   407 3   MG    MG  C . 
JA 13 HOH   1   501 289 HOH   HOH A . 
JA 13 HOH   2   502 69  HOH   HOH A . 
JA 13 HOH   3   503 201 HOH   HOH A . 
JA 13 HOH   4   504 178 HOH   HOH A . 
JA 13 HOH   5   505 198 HOH   HOH A . 
JA 13 HOH   6   506 91  HOH   HOH A . 
JA 13 HOH   7   507 252 HOH   HOH A . 
JA 13 HOH   8   508 128 HOH   HOH A . 
JA 13 HOH   9   509 55  HOH   HOH A . 
JA 13 HOH   10  510 186 HOH   HOH A . 
JA 13 HOH   11  511 293 HOH   HOH A . 
JA 13 HOH   12  512 28  HOH   HOH A . 
JA 13 HOH   13  513 77  HOH   HOH A . 
JA 13 HOH   14  514 220 HOH   HOH A . 
JA 13 HOH   15  515 114 HOH   HOH A . 
JA 13 HOH   16  516 107 HOH   HOH A . 
JA 13 HOH   17  517 156 HOH   HOH A . 
JA 13 HOH   18  518 165 HOH   HOH A . 
JA 13 HOH   19  519 129 HOH   HOH A . 
JA 13 HOH   20  520 172 HOH   HOH A . 
JA 13 HOH   21  521 121 HOH   HOH A . 
JA 13 HOH   22  522 150 HOH   HOH A . 
JA 13 HOH   23  523 67  HOH   HOH A . 
JA 13 HOH   24  524 6   HOH   HOH A . 
JA 13 HOH   25  525 151 HOH   HOH A . 
JA 13 HOH   26  526 290 HOH   HOH A . 
JA 13 HOH   27  527 144 HOH   HOH A . 
JA 13 HOH   28  528 86  HOH   HOH A . 
JA 13 HOH   29  529 21  HOH   HOH A . 
JA 13 HOH   30  530 39  HOH   HOH A . 
JA 13 HOH   31  531 25  HOH   HOH A . 
JA 13 HOH   32  532 188 HOH   HOH A . 
JA 13 HOH   33  533 246 HOH   HOH A . 
JA 13 HOH   34  534 4   HOH   HOH A . 
JA 13 HOH   35  535 236 HOH   HOH A . 
JA 13 HOH   36  536 93  HOH   HOH A . 
JA 13 HOH   37  537 57  HOH   HOH A . 
JA 13 HOH   38  538 48  HOH   HOH A . 
JA 13 HOH   39  539 143 HOH   HOH A . 
JA 13 HOH   40  540 81  HOH   HOH A . 
JA 13 HOH   41  541 41  HOH   HOH A . 
JA 13 HOH   42  542 195 HOH   HOH A . 
JA 13 HOH   43  543 166 HOH   HOH A . 
JA 13 HOH   44  544 63  HOH   HOH A . 
JA 13 HOH   45  545 19  HOH   HOH A . 
JA 13 HOH   46  546 285 HOH   HOH A . 
JA 13 HOH   47  547 251 HOH   HOH A . 
JA 13 HOH   48  548 250 HOH   HOH A . 
JA 13 HOH   49  549 249 HOH   HOH A . 
JA 13 HOH   50  550 259 HOH   HOH A . 
JA 13 HOH   51  551 142 HOH   HOH A . 
JA 13 HOH   52  552 194 HOH   HOH A . 
JA 13 HOH   53  553 49  HOH   HOH A . 
JA 13 HOH   54  554 44  HOH   HOH A . 
JA 13 HOH   55  555 8   HOH   HOH A . 
JA 13 HOH   56  556 68  HOH   HOH A . 
JA 13 HOH   57  557 32  HOH   HOH A . 
JA 13 HOH   58  558 287 HOH   HOH A . 
JA 13 HOH   59  559 24  HOH   HOH A . 
JA 13 HOH   60  560 199 HOH   HOH A . 
JA 13 HOH   61  561 82  HOH   HOH A . 
JA 13 HOH   62  562 254 HOH   HOH A . 
JA 13 HOH   63  563 126 HOH   HOH A . 
JA 13 HOH   64  564 13  HOH   HOH A . 
JA 13 HOH   65  565 286 HOH   HOH A . 
JA 13 HOH   66  566 248 HOH   HOH A . 
JA 13 HOH   67  567 197 HOH   HOH A . 
JA 13 HOH   68  568 206 HOH   HOH A . 
JA 13 HOH   69  569 15  HOH   HOH A . 
JA 13 HOH   70  570 161 HOH   HOH A . 
JA 13 HOH   71  571 18  HOH   HOH A . 
JA 13 HOH   72  572 101 HOH   HOH A . 
JA 13 HOH   73  573 20  HOH   HOH A . 
JA 13 HOH   74  574 96  HOH   HOH A . 
JA 13 HOH   75  575 148 HOH   HOH A . 
JA 13 HOH   76  576 146 HOH   HOH A . 
JA 13 HOH   77  577 83  HOH   HOH A . 
JA 13 HOH   78  578 116 HOH   HOH A . 
JA 13 HOH   79  579 54  HOH   HOH A . 
JA 13 HOH   80  580 120 HOH   HOH A . 
JA 13 HOH   81  581 29  HOH   HOH A . 
JA 13 HOH   82  582 200 HOH   HOH A . 
JA 13 HOH   83  583 52  HOH   HOH A . 
JA 13 HOH   84  584 261 HOH   HOH A . 
JA 13 HOH   85  585 153 HOH   HOH A . 
JA 13 HOH   86  586 73  HOH   HOH A . 
JA 13 HOH   87  587 237 HOH   HOH A . 
JA 13 HOH   88  588 37  HOH   HOH A . 
JA 13 HOH   89  589 88  HOH   HOH A . 
JA 13 HOH   90  590 33  HOH   HOH A . 
JA 13 HOH   91  591 5   HOH   HOH A . 
JA 13 HOH   92  592 42  HOH   HOH A . 
JA 13 HOH   93  593 80  HOH   HOH A . 
JA 13 HOH   94  594 113 HOH   HOH A . 
JA 13 HOH   95  595 87  HOH   HOH A . 
JA 13 HOH   96  596 118 HOH   HOH A . 
JA 13 HOH   97  597 260 HOH   HOH A . 
JA 13 HOH   98  598 75  HOH   HOH A . 
JA 13 HOH   99  599 247 HOH   HOH A . 
JA 13 HOH   100 600 12  HOH   HOH A . 
JA 13 HOH   101 601 157 HOH   HOH A . 
JA 13 HOH   102 602 103 HOH   HOH A . 
JA 13 HOH   103 603 97  HOH   HOH A . 
JA 13 HOH   104 604 288 HOH   HOH A . 
JA 13 HOH   105 605 35  HOH   HOH A . 
JA 13 HOH   106 606 214 HOH   HOH A . 
JA 13 HOH   107 607 100 HOH   HOH A . 
JA 13 HOH   108 608 184 HOH   HOH A . 
JA 13 HOH   109 609 17  HOH   HOH A . 
JA 13 HOH   110 610 84  HOH   HOH A . 
JA 13 HOH   111 611 30  HOH   HOH A . 
JA 13 HOH   112 612 127 HOH   HOH A . 
JA 13 HOH   113 613 85  HOH   HOH A . 
JA 13 HOH   114 614 135 HOH   HOH A . 
JA 13 HOH   115 615 179 HOH   HOH A . 
JA 13 HOH   116 616 190 HOH   HOH A . 
JA 13 HOH   117 617 189 HOH   HOH A . 
JA 13 HOH   118 618 284 HOH   HOH A . 
JA 13 HOH   119 619 217 HOH   HOH A . 
JA 13 HOH   120 620 253 HOH   HOH A . 
JA 13 HOH   121 621 177 HOH   HOH A . 
JA 13 HOH   122 622 163 HOH   HOH A . 
JA 13 HOH   123 623 185 HOH   HOH A . 
JA 13 HOH   124 624 191 HOH   HOH A . 
JA 13 HOH   125 625 164 HOH   HOH A . 
JA 13 HOH   126 626 136 HOH   HOH A . 
JA 13 HOH   127 627 171 HOH   HOH A . 
JA 13 HOH   128 628 292 HOH   HOH A . 
JA 13 HOH   129 629 108 HOH   HOH A . 
JA 13 HOH   130 630 291 HOH   HOH A . 
JA 13 HOH   131 631 256 HOH   HOH A . 
JA 13 HOH   132 632 162 HOH   HOH A . 
JA 13 HOH   133 633 169 HOH   HOH A . 
JA 13 HOH   134 634 102 HOH   HOH A . 
KA 13 HOH   1   501 302 HOH   HOH B . 
KA 13 HOH   2   502 124 HOH   HOH B . 
KA 13 HOH   3   503 170 HOH   HOH B . 
KA 13 HOH   4   504 90  HOH   HOH B . 
KA 13 HOH   5   505 123 HOH   HOH B . 
KA 13 HOH   6   506 64  HOH   HOH B . 
KA 13 HOH   7   507 71  HOH   HOH B . 
KA 13 HOH   8   508 134 HOH   HOH B . 
KA 13 HOH   9   509 154 HOH   HOH B . 
KA 13 HOH   10  510 130 HOH   HOH B . 
KA 13 HOH   11  511 283 HOH   HOH B . 
KA 13 HOH   12  512 137 HOH   HOH B . 
KA 13 HOH   13  513 66  HOH   HOH B . 
KA 13 HOH   14  514 38  HOH   HOH B . 
KA 13 HOH   15  515 9   HOH   HOH B . 
KA 13 HOH   16  516 14  HOH   HOH B . 
KA 13 HOH   17  517 301 HOH   HOH B . 
KA 13 HOH   18  518 176 HOH   HOH B . 
KA 13 HOH   19  519 117 HOH   HOH B . 
KA 13 HOH   20  520 31  HOH   HOH B . 
KA 13 HOH   21  521 152 HOH   HOH B . 
KA 13 HOH   22  522 138 HOH   HOH B . 
KA 13 HOH   23  523 274 HOH   HOH B . 
KA 13 HOH   24  524 175 HOH   HOH B . 
KA 13 HOH   25  525 234 HOH   HOH B . 
KA 13 HOH   26  526 207 HOH   HOH B . 
KA 13 HOH   27  527 43  HOH   HOH B . 
KA 13 HOH   28  528 47  HOH   HOH B . 
KA 13 HOH   29  529 50  HOH   HOH B . 
KA 13 HOH   30  530 79  HOH   HOH B . 
KA 13 HOH   31  531 40  HOH   HOH B . 
KA 13 HOH   32  532 7   HOH   HOH B . 
KA 13 HOH   33  533 139 HOH   HOH B . 
KA 13 HOH   34  534 74  HOH   HOH B . 
KA 13 HOH   35  535 122 HOH   HOH B . 
KA 13 HOH   36  536 140 HOH   HOH B . 
KA 13 HOH   37  537 277 HOH   HOH B . 
KA 13 HOH   38  538 70  HOH   HOH B . 
KA 13 HOH   39  539 300 HOH   HOH B . 
KA 13 HOH   40  540 72  HOH   HOH B . 
KA 13 HOH   41  541 278 HOH   HOH B . 
KA 13 HOH   42  542 202 HOH   HOH B . 
KA 13 HOH   43  543 76  HOH   HOH B . 
KA 13 HOH   44  544 131 HOH   HOH B . 
KA 13 HOH   45  545 155 HOH   HOH B . 
KA 13 HOH   46  546 264 HOH   HOH B . 
KA 13 HOH   47  547 34  HOH   HOH B . 
KA 13 HOH   48  548 203 HOH   HOH B . 
KA 13 HOH   49  549 168 HOH   HOH B . 
KA 13 HOH   50  550 115 HOH   HOH B . 
KA 13 HOH   51  551 304 HOH   HOH B . 
KA 13 HOH   52  552 275 HOH   HOH B . 
KA 13 HOH   53  553 141 HOH   HOH B . 
KA 13 HOH   54  554 95  HOH   HOH B . 
KA 13 HOH   55  555 78  HOH   HOH B . 
KA 13 HOH   56  556 149 HOH   HOH B . 
KA 13 HOH   57  557 307 HOH   HOH B . 
KA 13 HOH   58  558 62  HOH   HOH B . 
KA 13 HOH   59  559 26  HOH   HOH B . 
KA 13 HOH   60  560 23  HOH   HOH B . 
KA 13 HOH   61  561 65  HOH   HOH B . 
KA 13 HOH   62  562 1   HOH   HOH B . 
KA 13 HOH   63  563 22  HOH   HOH B . 
KA 13 HOH   64  564 180 HOH   HOH B . 
KA 13 HOH   65  565 133 HOH   HOH B . 
KA 13 HOH   66  566 258 HOH   HOH B . 
KA 13 HOH   67  567 110 HOH   HOH B . 
KA 13 HOH   68  568 51  HOH   HOH B . 
KA 13 HOH   69  569 59  HOH   HOH B . 
KA 13 HOH   70  570 213 HOH   HOH B . 
KA 13 HOH   71  571 56  HOH   HOH B . 
KA 13 HOH   72  572 53  HOH   HOH B . 
KA 13 HOH   73  573 262 HOH   HOH B . 
KA 13 HOH   74  574 271 HOH   HOH B . 
KA 13 HOH   75  575 257 HOH   HOH B . 
KA 13 HOH   76  576 208 HOH   HOH B . 
KA 13 HOH   77  577 311 HOH   HOH B . 
KA 13 HOH   78  578 209 HOH   HOH B . 
KA 13 HOH   79  579 310 HOH   HOH B . 
KA 13 HOH   80  580 159 HOH   HOH B . 
KA 13 HOH   81  581 312 HOH   HOH B . 
KA 13 HOH   82  582 211 HOH   HOH B . 
KA 13 HOH   83  583 215 HOH   HOH B . 
KA 13 HOH   84  584 219 HOH   HOH B . 
KA 13 HOH   85  585 299 HOH   HOH B . 
KA 13 HOH   86  586 3   HOH   HOH B . 
KA 13 HOH   87  587 309 HOH   HOH B . 
KA 13 HOH   88  588 218 HOH   HOH B . 
KA 13 HOH   89  589 210 HOH   HOH B . 
KA 13 HOH   90  590 181 HOH   HOH B . 
KA 13 HOH   91  591 212 HOH   HOH B . 
KA 13 HOH   92  592 160 HOH   HOH B . 
KA 13 HOH   93  593 263 HOH   HOH B . 
LA 13 HOH   1   501 298 HOH   HOH C . 
LA 13 HOH   2   502 294 HOH   HOH C . 
LA 13 HOH   3   503 280 HOH   HOH C . 
LA 13 HOH   4   504 296 HOH   HOH C . 
LA 13 HOH   5   505 112 HOH   HOH C . 
LA 13 HOH   6   506 173 HOH   HOH C . 
LA 13 HOH   7   507 109 HOH   HOH C . 
LA 13 HOH   8   508 235 HOH   HOH C . 
LA 13 HOH   9   509 239 HOH   HOH C . 
LA 13 HOH   10  510 187 HOH   HOH C . 
LA 13 HOH   11  511 227 HOH   HOH C . 
LA 13 HOH   12  512 61  HOH   HOH C . 
LA 13 HOH   13  513 279 HOH   HOH C . 
LA 13 HOH   14  514 243 HOH   HOH C . 
LA 13 HOH   15  515 273 HOH   HOH C . 
LA 13 HOH   16  516 58  HOH   HOH C . 
LA 13 HOH   17  517 46  HOH   HOH C . 
LA 13 HOH   18  518 265 HOH   HOH C . 
LA 13 HOH   19  519 132 HOH   HOH C . 
LA 13 HOH   20  520 281 HOH   HOH C . 
LA 13 HOH   21  521 174 HOH   HOH C . 
LA 13 HOH   22  522 233 HOH   HOH C . 
LA 13 HOH   23  523 104 HOH   HOH C . 
LA 13 HOH   24  524 60  HOH   HOH C . 
LA 13 HOH   25  525 111 HOH   HOH C . 
LA 13 HOH   26  526 119 HOH   HOH C . 
LA 13 HOH   27  527 270 HOH   HOH C . 
LA 13 HOH   28  528 167 HOH   HOH C . 
LA 13 HOH   29  529 2   HOH   HOH C . 
LA 13 HOH   30  530 11  HOH   HOH C . 
LA 13 HOH   31  531 10  HOH   HOH C . 
LA 13 HOH   32  532 305 HOH   HOH C . 
LA 13 HOH   33  533 269 HOH   HOH C . 
LA 13 HOH   34  534 92  HOH   HOH C . 
LA 13 HOH   35  535 229 HOH   HOH C . 
LA 13 HOH   36  536 205 HOH   HOH C . 
LA 13 HOH   37  537 147 HOH   HOH C . 
LA 13 HOH   38  538 105 HOH   HOH C . 
LA 13 HOH   39  539 106 HOH   HOH C . 
LA 13 HOH   40  540 89  HOH   HOH C . 
LA 13 HOH   41  541 98  HOH   HOH C . 
LA 13 HOH   42  542 231 HOH   HOH C . 
LA 13 HOH   43  543 306 HOH   HOH C . 
LA 13 HOH   44  544 226 HOH   HOH C . 
LA 13 HOH   45  545 94  HOH   HOH C . 
LA 13 HOH   46  546 45  HOH   HOH C . 
LA 13 HOH   47  547 267 HOH   HOH C . 
LA 13 HOH   48  548 27  HOH   HOH C . 
LA 13 HOH   49  549 125 HOH   HOH C . 
LA 13 HOH   50  550 145 HOH   HOH C . 
LA 13 HOH   51  551 99  HOH   HOH C . 
LA 13 HOH   52  552 36  HOH   HOH C . 
LA 13 HOH   53  553 297 HOH   HOH C . 
LA 13 HOH   54  554 303 HOH   HOH C . 
LA 13 HOH   55  555 282 HOH   HOH C . 
LA 13 HOH   56  556 308 HOH   HOH C . 
LA 13 HOH   57  557 272 HOH   HOH C . 
LA 13 HOH   58  558 16  HOH   HOH C . 
LA 13 HOH   59  559 245 HOH   HOH C . 
LA 13 HOH   60  560 192 HOH   HOH C . 
LA 13 HOH   61  561 232 HOH   HOH C . 
LA 13 HOH   62  562 216 HOH   HOH C . 
LA 13 HOH   63  563 222 HOH   HOH C . 
LA 13 HOH   64  564 196 HOH   HOH C . 
LA 13 HOH   65  565 224 HOH   HOH C . 
LA 13 HOH   66  566 204 HOH   HOH C . 
LA 13 HOH   67  567 158 HOH   HOH C . 
LA 13 HOH   68  568 183 HOH   HOH C . 
LA 13 HOH   69  569 241 HOH   HOH C . 
LA 13 HOH   70  570 182 HOH   HOH C . 
LA 13 HOH   71  571 295 HOH   HOH C . 
LA 13 HOH   72  572 242 HOH   HOH C . 
LA 13 HOH   73  573 221 HOH   HOH C . 
LA 13 HOH   74  574 230 HOH   HOH C . 
LA 13 HOH   75  575 240 HOH   HOH C . 
LA 13 HOH   76  576 225 HOH   HOH C . 
LA 13 HOH   77  577 244 HOH   HOH C . 
LA 13 HOH   78  578 193 HOH   HOH C . 
LA 13 HOH   79  579 268 HOH   HOH C . 
LA 13 HOH   80  580 223 HOH   HOH C . 
LA 13 HOH   81  581 228 HOH   HOH C . 
LA 13 HOH   82  582 238 HOH   HOH C . 
LA 13 HOH   83  583 255 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                   111.62 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HED 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     271.393 
_cell.length_a_esd                 ? 
_cell.length_b                     74.362 
_cell.length_b_esd                 ? 
_cell.length_c                     105.603 
_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                         9HED 
_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                   9HED 
_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             4.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.10 
_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    
;2.15M ammonium sulphate, 100mM HEPES pH 7.5; additive: cesium chloride

Soaking: 20 mM alpha-damascone 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                                       9HED 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.45 
_reflns.d_resolution_low                               49.14 
_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                                     72203 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.149 
_reflns.pdbx_Rpim_I_all                                0.063 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.135 
_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                                    2.45 
_reflns_shell.d_res_low                                     2.50 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4445 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              0.83 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.693 
_reflns_shell.pdbx_Rpim_I_all                               0.289 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.894 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.627 
_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]                            -2.56 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.68 
_refine.aniso_B[2][2]                            2.67 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.49 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               43.716 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.947 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_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                                 9HED 
_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                            2.45 
_refine.ls_d_res_low                             49.14 
_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                     68656 
_refine.ls_number_reflns_R_free                  3544 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.84 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18679 
_refine.ls_R_factor_R_free                       0.21531 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18530 
_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                       0.239 
_refine.pdbx_overall_ESU_R_Free                  0.193 
_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                             6.433 
_refine.overall_SU_ML                            0.145 
_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                       2.45 
_refine_hist.d_res_low                        49.14 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               8761 
_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        8403 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_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  8854  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7780  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.478  1.845  12222 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.531  1.754  18002 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.459  5.000  1037  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.100  5.000  53    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.702 10.000 1127  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200  1347  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  10418 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2102  ? 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' ? 3.471  4.208  4055  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.464  4.208  4055  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.113  7.557  5073  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.112  7.557  5074  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.597  4.981  4799  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.520  4.971  4764  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.909  8.962  7077  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.207  41.31  9768  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.217  41.26  9729  ? 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                       2.450 
_refine_ls_shell.d_res_low                        2.513 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             283 
_refine_ls_shell.number_reflns_R_work             5018 
_refine_ls_shell.percent_reflns_obs               99.81 
_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                  0.243 
_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                  0.275 
# 
_struct.entry_id                     9HED 
_struct.title                        
'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II) in complex with alpha-damascone' 
_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        9HED 
_struct_keywords.text            'Peroxygenase, peroxidase, complex, alpha-damascone, 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 2  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 6  ? 
J  N N 7  ? 
K  N N 8  ? 
L  N N 8  ? 
M  N N 9  ? 
N  N N 10 ? 
O  N N 11 ? 
P  N N 12 ? 
Q  N N 12 ? 
R  N N 12 ? 
S  N N 12 ? 
T  N N 7  ? 
U  N N 9  ? 
V  N N 10 ? 
W  N N 11 ? 
X  N N 12 ? 
Y  N N 12 ? 
Z  N N 12 ? 
AA N N 12 ? 
BA N N 12 ? 
CA N N 7  ? 
DA N N 10 ? 
EA N N 8  ? 
FA N N 8  ? 
GA N N 8  ? 
HA N N 9  ? 
IA N N 11 ? 
JA N N 13 ? 
KA N N 13 ? 
LA 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 9HED A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HED B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HED 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,P,Q,R,S,JA  
2 1 B,F,G,T,U,V,W,X,Y,Z,AA,BA,KA  
3 1 C,H,I,CA,DA,EA,FA,GA,HA,IA,LA 
# 
_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 ? PHE B 207 ? LYS B 202 PHE B 220 1 ? 19 
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 ? ? ? ? ? ? ? 2.142 ? ? 
disulf2  disulf ?    ? B  CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
disulf3  disulf ?    ? C  CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
covale1  covale one  ? A  ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 H NAG 1   1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 J NAG 1   1_555 ? ? ? ? ? ? ? 1.443 ? 
N-Glycosylation 
covale3  covale one  ? B  ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 Y NAG 1   1_555 ? ? ? ? ? ? ? 1.480 ? 
N-Glycosylation 
covale4  covale one  ? B  ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 Z NAG 1   1_555 ? ? ? ? ? ? ? 1.448 ? 
N-Glycosylation 
covale5  covale one  ? C  ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 m NAG 1   1_555 ? ? ? ? ? ? ? 1.461 ? 
N-Glycosylation 
covale6  covale one  ? C  ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 n NAG 1   1_555 ? ? ? ? ? ? ? 1.427 ? 
N-Glycosylation 
covale7  covale both ? D  NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale8  covale both ? D  NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.389 ? ? 
covale9  covale both ? D  BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? H BMA 3   H MAN 4   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale10 covale both ? D  BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? H BMA 3   H MAN 5   1_555 ? ? ? ? ? ? ? 1.403 ? ? 
covale11 covale both ? E  NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? J NAG 1   J NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale12 covale both ? E  NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? J NAG 2   J BMA 3   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale13 covale both ? E  BMA .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? J BMA 3   J MAN 4   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale14 covale both ? E  BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? J BMA 3   J MAN 7   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale15 covale both ? E  MAN .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? J MAN 4   J MAN 5   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale16 covale both ? E  MAN .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? J MAN 4   J MAN 6   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale17 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? Y NAG 1   Y NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale18 covale both ? F  NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? Y NAG 2   Y BMA 3   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale19 covale both ? F  BMA .   O3  ? ? ? 1_555 F  MAN .   C1 ? ? Y BMA 3   Y MAN 4   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale20 covale both ? F  BMA .   O6  ? ? ? 1_555 F  MAN .   C1 ? ? Y BMA 3   Y MAN 5   1_555 ? ? ? ? ? ? ? 1.409 ? ? 
covale21 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? Z NAG 1   Z NAG 2   1_555 ? ? ? ? ? ? ? 1.387 ? ? 
covale22 covale both ? G  NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? Z NAG 2   Z BMA 3   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale23 covale both ? G  BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? Z BMA 3   Z MAN 4   1_555 ? ? ? ? ? ? ? 1.410 ? ? 
covale24 covale both ? G  BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? Z BMA 3   Z MAN 6   1_555 ? ? ? ? ? ? ? 1.400 ? ? 
covale25 covale both ? G  MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? Z MAN 4   Z MAN 5   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale26 covale both ? H  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? m NAG 1   m NAG 2   1_555 ? ? ? ? ? ? ? 1.390 ? ? 
covale27 covale both ? H  NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? m NAG 2   m BMA 3   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale28 covale both ? H  BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? m BMA 3   m MAN 4   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale29 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? n NAG 1   n NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale30 covale both ? I  NAG .   O4  ? ? ? 1_555 I  BMA .   C1 ? ? n NAG 2   n BMA 3   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
metalc1  metalc ?    ? A  CYS 39  SG  ? ? ? 1_555 J  HEM .   FE ? ? A CYS 52  A HEM 401 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc2  metalc ?    ? A  GLU 125 OE2 ? ? ? 1_555 O  MG  .   MG ? ? A GLU 138 A MG  406 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc3  metalc ?    ? A  GLY 126 O   ? ? ? 1_555 O  MG  .   MG ? ? A GLY 139 A MG  406 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc4  metalc ?    ? J  HEM .   O2A ? ? ? 1_555 O  MG  .   MG ? ? A HEM 401 A MG  406 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc5  metalc ?    ? O  MG  .   MG  ? ? ? 1_555 JA HOH .   O  ? ? A MG  406 A HOH 519 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
metalc6  metalc ?    ? B  CYS 39  SG  ? ? ? 1_555 T  HEM .   FE ? ? B CYS 52  B HEM 401 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc7  metalc ?    ? B  GLU 125 OE2 ? ? ? 1_555 W  MG  .   MG ? ? B GLU 138 B MG  404 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc8  metalc ?    ? B  GLY 126 O   ? ? ? 1_555 W  MG  .   MG ? ? B GLY 139 B MG  404 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc9  metalc ?    ? T  HEM .   O2A ? ? ? 1_555 W  MG  .   MG ? ? B HEM 401 B MG  404 1_555 ? ? ? ? ? ? ? 1.958 ? ? 
metalc10 metalc ?    ? C  CYS 39  SG  ? ? ? 1_555 CA HEM .   FE ? ? C CYS 52  C HEM 401 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc11 metalc ?    ? C  GLU 125 OE2 ? ? ? 1_555 IA MG  .   MG ? ? C GLU 138 C MG  407 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc12 metalc ?    ? C  GLY 126 O   ? ? ? 1_555 IA MG  .   MG ? ? C GLY 139 C MG  407 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc13 metalc ?    ? CA HEM .   O1A ? ? ? 1_555 IA MG  .   MG ? ? C HEM 401 C MG  407 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
# 
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 ? J  HEM . ? A HEM 401 ? 1_555 NA  ? J  HEM .   ? A HEM 401 ? 1_555 101.3 ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NB  ? J  HEM .   ? A HEM 401 ? 1_555 92.3  ? 
3  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NB  ? J  HEM .   ? A HEM 401 ? 1_555 88.3  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 89.3  ? 
5  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 168.6 ? 
6  NB  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 87.1  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 95.6  ? 
8  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 92.7  ? 
9  NB  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 171.7 ? 
10 NC  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 90.4  ? 
11 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 76.8  ? 
12 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O2A ? J  HEM .   ? A HEM 401 ? 1_555 87.3  ? 
13 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O2A ? J  HEM .   ? A HEM 401 ? 1_555 89.3  ? 
14 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O   ? JA HOH .   ? A HOH 519 ? 1_555 82.8  ? 
15 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O   ? JA HOH .   ? A HOH 519 ? 1_555 155.1 ? 
16 O2A ? J  HEM .   ? A HEM 401 ? 1_555 MG ? O  MG  . ? A MG  406 ? 1_555 O   ? JA HOH .   ? A HOH 519 ? 1_555 75.4  ? 
17 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NA  ? T  HEM .   ? B HEM 401 ? 1_555 99.5  ? 
18 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NB  ? T  HEM .   ? B HEM 401 ? 1_555 91.2  ? 
19 NA  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NB  ? T  HEM .   ? B HEM 401 ? 1_555 87.4  ? 
20 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NC  ? T  HEM .   ? B HEM 401 ? 1_555 89.2  ? 
21 NA  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NC  ? T  HEM .   ? B HEM 401 ? 1_555 170.6 ? 
22 NB  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 NC  ? T  HEM .   ? B HEM 401 ? 1_555 88.8  ? 
23 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 ND  ? T  HEM .   ? B HEM 401 ? 1_555 96.2  ? 
24 NA  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 ND  ? T  HEM .   ? B HEM 401 ? 1_555 91.8  ? 
25 NB  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 ND  ? T  HEM .   ? B HEM 401 ? 1_555 172.6 ? 
26 NC  ? T  HEM .   ? B HEM 401 ? 1_555 FE ? T  HEM . ? B HEM 401 ? 1_555 ND  ? T  HEM .   ? B HEM 401 ? 1_555 90.8  ? 
27 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  404 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 75.2  ? 
28 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  404 ? 1_555 O2A ? T  HEM .   ? B HEM 401 ? 1_555 91.8  ? 
29 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? W  MG  . ? B MG  404 ? 1_555 O2A ? T  HEM .   ? B HEM 401 ? 1_555 95.8  ? 
30 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NA  ? CA HEM .   ? C HEM 401 ? 1_555 101.7 ? 
31 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NB  ? CA HEM .   ? C HEM 401 ? 1_555 90.8  ? 
32 NA  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NB  ? CA HEM .   ? C HEM 401 ? 1_555 88.3  ? 
33 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NC  ? CA HEM .   ? C HEM 401 ? 1_555 87.9  ? 
34 NA  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NC  ? CA HEM .   ? C HEM 401 ? 1_555 169.2 ? 
35 NB  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 NC  ? CA HEM .   ? C HEM 401 ? 1_555 86.5  ? 
36 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 ND  ? CA HEM .   ? C HEM 401 ? 1_555 96.7  ? 
37 NA  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 ND  ? CA HEM .   ? C HEM 401 ? 1_555 92.7  ? 
38 NB  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 ND  ? CA HEM .   ? C HEM 401 ? 1_555 172.0 ? 
39 NC  ? CA HEM .   ? C HEM 401 ? 1_555 FE ? CA HEM . ? C HEM 401 ? 1_555 ND  ? CA HEM .   ? C HEM 401 ? 1_555 91.2  ? 
40 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? IA MG  . ? C MG  407 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 72.7  ? 
41 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? IA MG  . ? C MG  407 ? 1_555 O1A ? CA HEM .   ? C HEM 401 ? 1_555 93.5  ? 
42 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? IA MG  . ? C MG  407 ? 1_555 O1A ? CA HEM .   ? C HEM 401 ? 1_555 86.3  ? 
# 
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 H 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG J 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG Y 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG Z 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG m 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG n 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 5.26 
2 PRO 111 B . ? PRO 124 B PRO 112 B ? PRO 125 B 1 6.64 
3 PRO 111 C . ? PRO 124 C PRO 112 C ? PRO 125 C 1 2.69 
# 
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                   9HED 
_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 N   C LEU 32  ? ? O1S C EPE 404 ? ? 2.02 
2 1 O   A ASN 169 ? ? NH2 C ARG 318 ? B 2.16 
3 1 NE2 A GLN 74  ? ? O2S A EPE 402 ? ? 2.16 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH1 A ARG 145 ? ? 117.05 120.30 -3.25 0.50 N 
2 1 NE A ARG 318 ? B CZ A ARG 318 ? B NH1 A ARG 318 ? B 124.21 120.30 3.91  0.50 N 
3 1 NE A ARG 318 ? B CZ A ARG 318 ? B NH2 A ARG 318 ? B 115.72 120.30 -4.58 0.50 N 
4 1 NE C ARG 318 ? B CZ C ARG 318 ? B NH2 C ARG 318 ? B 117.03 120.30 -3.27 0.50 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 ? ? -137.09 -32.13  
2  1 PHE A 137 ? ? -105.30 -83.07  
3  1 ALA A 141 ? ? 70.77   35.22   
4  1 ASN A 203 ? ? 55.76   -126.61 
5  1 ASP A 228 ? ? 61.28   60.20   
6  1 SER A 257 ? ? -155.60 -98.44  
7  1 ASN A 282 ? ? -146.31 50.69   
8  1 ASN A 312 ? ? -155.69 64.21   
9  1 HIS B 127 ? ? -135.96 -33.42  
10 1 PHE B 137 ? ? -103.18 -80.89  
11 1 ALA B 141 ? ? 70.50   36.06   
12 1 ASN B 203 ? ? 56.50   -125.82 
13 1 SER B 257 ? ? -155.02 -97.22  
14 1 ASN B 282 ? ? -144.60 53.04   
15 1 ASN B 312 ? ? -151.74 65.90   
16 1 HIS C 127 ? ? -137.61 -31.06  
17 1 PHE C 137 ? ? -105.45 -82.32  
18 1 ALA C 141 ? ? 71.63   37.10   
19 1 ASN C 203 ? ? 56.49   -126.04 
20 1 ASP C 228 ? ? 61.79   60.05   
21 1 SER C 257 ? ? -153.10 -97.57  
22 1 ASN C 282 ? ? -144.67 52.24   
23 1 ASN C 312 ? ? -156.61 61.85   
# 
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 633 ? 6.09 . 
2 1 O ? B HOH 593 ? 5.87 . 
# 
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 
A1IUA C1   C  N N 1   
A1IUA C2   C  N N 2   
A1IUA C3   C  N N 3   
A1IUA C4   C  N N 4   
A1IUA O5   O  N N 5   
A1IUA C6   C  N N 6   
A1IUA C7   C  N N 7   
A1IUA C8   C  N N 8   
A1IUA C9   C  N N 9   
A1IUA C10  C  N N 10  
A1IUA C11  C  N N 11  
A1IUA C12  C  N N 12  
A1IUA C13  C  N N 13  
A1IUA C14  C  N N 14  
A1IUA H1   H  N N 15  
A1IUA H2   H  N N 16  
A1IUA H3   H  N N 17  
A1IUA H4   H  N N 18  
A1IUA H5   H  N N 19  
A1IUA H6   H  N N 20  
A1IUA H7   H  N N 21  
A1IUA H8   H  N N 22  
A1IUA H9   H  N N 23  
A1IUA H10  H  N N 24  
A1IUA H11  H  N N 25  
A1IUA H12  H  N N 26  
A1IUA H13  H  N N 27  
A1IUA H14  H  N N 28  
A1IUA H15  H  N N 29  
A1IUA H16  H  N N 30  
A1IUA H17  H  N N 31  
A1IUA H18  H  N N 32  
A1IUA H19  H  N N 33  
A1IUA H20  H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
BMA   C1   C  N R 108 
BMA   C2   C  N S 109 
BMA   C3   C  N S 110 
BMA   C4   C  N S 111 
BMA   C5   C  N R 112 
BMA   C6   C  N N 113 
BMA   O1   O  N N 114 
BMA   O2   O  N N 115 
BMA   O3   O  N N 116 
BMA   O4   O  N N 117 
BMA   O5   O  N N 118 
BMA   O6   O  N N 119 
BMA   H1   H  N N 120 
BMA   H2   H  N N 121 
BMA   H3   H  N N 122 
BMA   H4   H  N N 123 
BMA   H5   H  N N 124 
BMA   H61  H  N N 125 
BMA   H62  H  N N 126 
BMA   HO1  H  N N 127 
BMA   HO2  H  N N 128 
BMA   HO3  H  N N 129 
BMA   HO4  H  N N 130 
BMA   HO6  H  N N 131 
CYS   N    N  N N 132 
CYS   CA   C  N R 133 
CYS   C    C  N N 134 
CYS   O    O  N N 135 
CYS   CB   C  N N 136 
CYS   SG   S  N N 137 
CYS   OXT  O  N N 138 
CYS   H    H  N N 139 
CYS   H2   H  N N 140 
CYS   HA   H  N N 141 
CYS   HB2  H  N N 142 
CYS   HB3  H  N N 143 
CYS   HG   H  N N 144 
CYS   HXT  H  N N 145 
EPE   N1   N  N N 146 
EPE   C2   C  N N 147 
EPE   C3   C  N N 148 
EPE   N4   N  N N 149 
EPE   C5   C  N N 150 
EPE   C6   C  N N 151 
EPE   C7   C  N N 152 
EPE   C8   C  N N 153 
EPE   O8   O  N N 154 
EPE   C9   C  N N 155 
EPE   C10  C  N N 156 
EPE   S    S  N N 157 
EPE   O1S  O  N N 158 
EPE   O2S  O  N N 159 
EPE   O3S  O  N N 160 
EPE   H21  H  N N 161 
EPE   H22  H  N N 162 
EPE   H31  H  N N 163 
EPE   H32  H  N N 164 
EPE   H51  H  N N 165 
EPE   H52  H  N N 166 
EPE   H61  H  N N 167 
EPE   H62  H  N N 168 
EPE   H71  H  N N 169 
EPE   H72  H  N N 170 
EPE   H81  H  N N 171 
EPE   H82  H  N N 172 
EPE   HO8  H  N N 173 
EPE   H91  H  N N 174 
EPE   H92  H  N N 175 
EPE   H101 H  N N 176 
EPE   H102 H  N N 177 
EPE   HOS3 H  N N 178 
GLN   N    N  N N 179 
GLN   CA   C  N S 180 
GLN   C    C  N N 181 
GLN   O    O  N N 182 
GLN   CB   C  N N 183 
GLN   CG   C  N N 184 
GLN   CD   C  N N 185 
GLN   OE1  O  N N 186 
GLN   NE2  N  N N 187 
GLN   OXT  O  N N 188 
GLN   H    H  N N 189 
GLN   H2   H  N N 190 
GLN   HA   H  N N 191 
GLN   HB2  H  N N 192 
GLN   HB3  H  N N 193 
GLN   HG2  H  N N 194 
GLN   HG3  H  N N 195 
GLN   HE21 H  N N 196 
GLN   HE22 H  N N 197 
GLN   HXT  H  N N 198 
GLU   N    N  N N 199 
GLU   CA   C  N S 200 
GLU   C    C  N N 201 
GLU   O    O  N N 202 
GLU   CB   C  N N 203 
GLU   CG   C  N N 204 
GLU   CD   C  N N 205 
GLU   OE1  O  N N 206 
GLU   OE2  O  N N 207 
GLU   OXT  O  N N 208 
GLU   H    H  N N 209 
GLU   H2   H  N N 210 
GLU   HA   H  N N 211 
GLU   HB2  H  N N 212 
GLU   HB3  H  N N 213 
GLU   HG2  H  N N 214 
GLU   HG3  H  N N 215 
GLU   HE2  H  N N 216 
GLU   HXT  H  N N 217 
GLY   N    N  N N 218 
GLY   CA   C  N N 219 
GLY   C    C  N N 220 
GLY   O    O  N N 221 
GLY   OXT  O  N N 222 
GLY   H    H  N N 223 
GLY   H2   H  N N 224 
GLY   HA2  H  N N 225 
GLY   HA3  H  N N 226 
GLY   HXT  H  N N 227 
GOL   C1   C  N N 228 
GOL   O1   O  N N 229 
GOL   C2   C  N N 230 
GOL   O2   O  N N 231 
GOL   C3   C  N N 232 
GOL   O3   O  N N 233 
GOL   H11  H  N N 234 
GOL   H12  H  N N 235 
GOL   HO1  H  N N 236 
GOL   H2   H  N N 237 
GOL   HO2  H  N N 238 
GOL   H31  H  N N 239 
GOL   H32  H  N N 240 
GOL   HO3  H  N N 241 
HEM   CHA  C  N N 242 
HEM   CHB  C  N N 243 
HEM   CHC  C  N N 244 
HEM   CHD  C  N N 245 
HEM   C1A  C  Y N 246 
HEM   C2A  C  Y N 247 
HEM   C3A  C  Y N 248 
HEM   C4A  C  Y N 249 
HEM   CMA  C  N N 250 
HEM   CAA  C  N N 251 
HEM   CBA  C  N N 252 
HEM   CGA  C  N N 253 
HEM   O1A  O  N N 254 
HEM   O2A  O  N N 255 
HEM   C1B  C  N N 256 
HEM   C2B  C  N N 257 
HEM   C3B  C  N N 258 
HEM   C4B  C  N N 259 
HEM   CMB  C  N N 260 
HEM   CAB  C  N N 261 
HEM   CBB  C  N N 262 
HEM   C1C  C  Y N 263 
HEM   C2C  C  Y N 264 
HEM   C3C  C  Y N 265 
HEM   C4C  C  Y N 266 
HEM   CMC  C  N N 267 
HEM   CAC  C  N N 268 
HEM   CBC  C  N N 269 
HEM   C1D  C  N N 270 
HEM   C2D  C  N N 271 
HEM   C3D  C  N N 272 
HEM   C4D  C  N N 273 
HEM   CMD  C  N N 274 
HEM   CAD  C  N N 275 
HEM   CBD  C  N N 276 
HEM   CGD  C  N N 277 
HEM   O1D  O  N N 278 
HEM   O2D  O  N N 279 
HEM   NA   N  Y N 280 
HEM   NB   N  N N 281 
HEM   NC   N  Y N 282 
HEM   ND   N  N N 283 
HEM   FE   FE N N 284 
HEM   HHB  H  N N 285 
HEM   HHC  H  N N 286 
HEM   HHD  H  N N 287 
HEM   HMA  H  N N 288 
HEM   HMAA H  N N 289 
HEM   HMAB H  N N 290 
HEM   HAA  H  N N 291 
HEM   HAAA H  N N 292 
HEM   HBA  H  N N 293 
HEM   HBAA H  N N 294 
HEM   HMB  H  N N 295 
HEM   HMBA H  N N 296 
HEM   HMBB H  N N 297 
HEM   HAB  H  N N 298 
HEM   HBB  H  N N 299 
HEM   HBBA H  N N 300 
HEM   HMC  H  N N 301 
HEM   HMCA H  N N 302 
HEM   HMCB H  N N 303 
HEM   HAC  H  N N 304 
HEM   HBC  H  N N 305 
HEM   HBCA H  N N 306 
HEM   HMD  H  N N 307 
HEM   HMDA H  N N 308 
HEM   HMDB H  N N 309 
HEM   HAD  H  N N 310 
HEM   HADA H  N N 311 
HEM   HBD  H  N N 312 
HEM   HBDA H  N N 313 
HEM   H2A  H  N N 314 
HEM   H2D  H  N N 315 
HEM   HHA  H  N N 316 
HIS   N    N  N N 317 
HIS   CA   C  N S 318 
HIS   C    C  N N 319 
HIS   O    O  N N 320 
HIS   CB   C  N N 321 
HIS   CG   C  Y N 322 
HIS   ND1  N  Y N 323 
HIS   CD2  C  Y N 324 
HIS   CE1  C  Y N 325 
HIS   NE2  N  Y N 326 
HIS   OXT  O  N N 327 
HIS   H    H  N N 328 
HIS   H2   H  N N 329 
HIS   HA   H  N N 330 
HIS   HB2  H  N N 331 
HIS   HB3  H  N N 332 
HIS   HD1  H  N N 333 
HIS   HD2  H  N N 334 
HIS   HE1  H  N N 335 
HIS   HE2  H  N N 336 
HIS   HXT  H  N N 337 
HOH   O    O  N N 338 
HOH   H1   H  N N 339 
HOH   H2   H  N N 340 
ILE   N    N  N N 341 
ILE   CA   C  N S 342 
ILE   C    C  N N 343 
ILE   O    O  N N 344 
ILE   CB   C  N S 345 
ILE   CG1  C  N N 346 
ILE   CG2  C  N N 347 
ILE   CD1  C  N N 348 
ILE   OXT  O  N N 349 
ILE   H    H  N N 350 
ILE   H2   H  N N 351 
ILE   HA   H  N N 352 
ILE   HB   H  N N 353 
ILE   HG12 H  N N 354 
ILE   HG13 H  N N 355 
ILE   HG21 H  N N 356 
ILE   HG22 H  N N 357 
ILE   HG23 H  N N 358 
ILE   HD11 H  N N 359 
ILE   HD12 H  N N 360 
ILE   HD13 H  N N 361 
ILE   HXT  H  N N 362 
LEU   N    N  N N 363 
LEU   CA   C  N S 364 
LEU   C    C  N N 365 
LEU   O    O  N N 366 
LEU   CB   C  N N 367 
LEU   CG   C  N N 368 
LEU   CD1  C  N N 369 
LEU   CD2  C  N N 370 
LEU   OXT  O  N N 371 
LEU   H    H  N N 372 
LEU   H2   H  N N 373 
LEU   HA   H  N N 374 
LEU   HB2  H  N N 375 
LEU   HB3  H  N N 376 
LEU   HG   H  N N 377 
LEU   HD11 H  N N 378 
LEU   HD12 H  N N 379 
LEU   HD13 H  N N 380 
LEU   HD21 H  N N 381 
LEU   HD22 H  N N 382 
LEU   HD23 H  N N 383 
LEU   HXT  H  N N 384 
LYS   N    N  N N 385 
LYS   CA   C  N S 386 
LYS   C    C  N N 387 
LYS   O    O  N N 388 
LYS   CB   C  N N 389 
LYS   CG   C  N N 390 
LYS   CD   C  N N 391 
LYS   CE   C  N N 392 
LYS   NZ   N  N N 393 
LYS   OXT  O  N N 394 
LYS   H    H  N N 395 
LYS   H2   H  N N 396 
LYS   HA   H  N N 397 
LYS   HB2  H  N N 398 
LYS   HB3  H  N N 399 
LYS   HG2  H  N N 400 
LYS   HG3  H  N N 401 
LYS   HD2  H  N N 402 
LYS   HD3  H  N N 403 
LYS   HE2  H  N N 404 
LYS   HE3  H  N N 405 
LYS   HZ1  H  N N 406 
LYS   HZ2  H  N N 407 
LYS   HZ3  H  N N 408 
LYS   HXT  H  N N 409 
MAN   C1   C  N S 410 
MAN   C2   C  N S 411 
MAN   C3   C  N S 412 
MAN   C4   C  N S 413 
MAN   C5   C  N R 414 
MAN   C6   C  N N 415 
MAN   O1   O  N N 416 
MAN   O2   O  N N 417 
MAN   O3   O  N N 418 
MAN   O4   O  N N 419 
MAN   O5   O  N N 420 
MAN   O6   O  N N 421 
MAN   H1   H  N N 422 
MAN   H2   H  N N 423 
MAN   H3   H  N N 424 
MAN   H4   H  N N 425 
MAN   H5   H  N N 426 
MAN   H61  H  N N 427 
MAN   H62  H  N N 428 
MAN   HO1  H  N N 429 
MAN   HO2  H  N N 430 
MAN   HO3  H  N N 431 
MAN   HO4  H  N N 432 
MAN   HO6  H  N N 433 
MET   N    N  N N 434 
MET   CA   C  N S 435 
MET   C    C  N N 436 
MET   O    O  N N 437 
MET   CB   C  N N 438 
MET   CG   C  N N 439 
MET   SD   S  N N 440 
MET   CE   C  N N 441 
MET   OXT  O  N N 442 
MET   H    H  N N 443 
MET   H2   H  N N 444 
MET   HA   H  N N 445 
MET   HB2  H  N N 446 
MET   HB3  H  N N 447 
MET   HG2  H  N N 448 
MET   HG3  H  N N 449 
MET   HE1  H  N N 450 
MET   HE2  H  N N 451 
MET   HE3  H  N N 452 
MET   HXT  H  N N 453 
MG    MG   MG N N 454 
NAG   C1   C  N R 455 
NAG   C2   C  N R 456 
NAG   C3   C  N R 457 
NAG   C4   C  N S 458 
NAG   C5   C  N R 459 
NAG   C6   C  N N 460 
NAG   C7   C  N N 461 
NAG   C8   C  N N 462 
NAG   N2   N  N N 463 
NAG   O1   O  N N 464 
NAG   O3   O  N N 465 
NAG   O4   O  N N 466 
NAG   O5   O  N N 467 
NAG   O6   O  N N 468 
NAG   O7   O  N N 469 
NAG   H1   H  N N 470 
NAG   H2   H  N N 471 
NAG   H3   H  N N 472 
NAG   H4   H  N N 473 
NAG   H5   H  N N 474 
NAG   H61  H  N N 475 
NAG   H62  H  N N 476 
NAG   H81  H  N N 477 
NAG   H82  H  N N 478 
NAG   H83  H  N N 479 
NAG   HN2  H  N N 480 
NAG   HO1  H  N N 481 
NAG   HO3  H  N N 482 
NAG   HO4  H  N N 483 
NAG   HO6  H  N N 484 
PHE   N    N  N N 485 
PHE   CA   C  N S 486 
PHE   C    C  N N 487 
PHE   O    O  N N 488 
PHE   CB   C  N N 489 
PHE   CG   C  Y N 490 
PHE   CD1  C  Y N 491 
PHE   CD2  C  Y N 492 
PHE   CE1  C  Y N 493 
PHE   CE2  C  Y N 494 
PHE   CZ   C  Y N 495 
PHE   OXT  O  N N 496 
PHE   H    H  N N 497 
PHE   H2   H  N N 498 
PHE   HA   H  N N 499 
PHE   HB2  H  N N 500 
PHE   HB3  H  N N 501 
PHE   HD1  H  N N 502 
PHE   HD2  H  N N 503 
PHE   HE1  H  N N 504 
PHE   HE2  H  N N 505 
PHE   HZ   H  N N 506 
PHE   HXT  H  N N 507 
PRO   N    N  N N 508 
PRO   CA   C  N S 509 
PRO   C    C  N N 510 
PRO   O    O  N N 511 
PRO   CB   C  N N 512 
PRO   CG   C  N N 513 
PRO   CD   C  N N 514 
PRO   OXT  O  N N 515 
PRO   H    H  N N 516 
PRO   HA   H  N N 517 
PRO   HB2  H  N N 518 
PRO   HB3  H  N N 519 
PRO   HG2  H  N N 520 
PRO   HG3  H  N N 521 
PRO   HD2  H  N N 522 
PRO   HD3  H  N N 523 
PRO   HXT  H  N N 524 
SER   N    N  N N 525 
SER   CA   C  N S 526 
SER   C    C  N N 527 
SER   O    O  N N 528 
SER   CB   C  N N 529 
SER   OG   O  N N 530 
SER   OXT  O  N N 531 
SER   H    H  N N 532 
SER   H2   H  N N 533 
SER   HA   H  N N 534 
SER   HB2  H  N N 535 
SER   HB3  H  N N 536 
SER   HG   H  N N 537 
SER   HXT  H  N N 538 
SO4   S    S  N N 539 
SO4   O1   O  N N 540 
SO4   O2   O  N N 541 
SO4   O3   O  N N 542 
SO4   O4   O  N N 543 
THR   N    N  N N 544 
THR   CA   C  N S 545 
THR   C    C  N N 546 
THR   O    O  N N 547 
THR   CB   C  N R 548 
THR   OG1  O  N N 549 
THR   CG2  C  N N 550 
THR   OXT  O  N N 551 
THR   H    H  N N 552 
THR   H2   H  N N 553 
THR   HA   H  N N 554 
THR   HB   H  N N 555 
THR   HG1  H  N N 556 
THR   HG21 H  N N 557 
THR   HG22 H  N N 558 
THR   HG23 H  N N 559 
THR   HXT  H  N N 560 
TRP   N    N  N N 561 
TRP   CA   C  N S 562 
TRP   C    C  N N 563 
TRP   O    O  N N 564 
TRP   CB   C  N N 565 
TRP   CG   C  Y N 566 
TRP   CD1  C  Y N 567 
TRP   CD2  C  Y N 568 
TRP   NE1  N  Y N 569 
TRP   CE2  C  Y N 570 
TRP   CE3  C  Y N 571 
TRP   CZ2  C  Y N 572 
TRP   CZ3  C  Y N 573 
TRP   CH2  C  Y N 574 
TRP   OXT  O  N N 575 
TRP   H    H  N N 576 
TRP   H2   H  N N 577 
TRP   HA   H  N N 578 
TRP   HB2  H  N N 579 
TRP   HB3  H  N N 580 
TRP   HD1  H  N N 581 
TRP   HE1  H  N N 582 
TRP   HE3  H  N N 583 
TRP   HZ2  H  N N 584 
TRP   HZ3  H  N N 585 
TRP   HH2  H  N N 586 
TRP   HXT  H  N N 587 
TYR   N    N  N N 588 
TYR   CA   C  N S 589 
TYR   C    C  N N 590 
TYR   O    O  N N 591 
TYR   CB   C  N N 592 
TYR   CG   C  Y N 593 
TYR   CD1  C  Y N 594 
TYR   CD2  C  Y N 595 
TYR   CE1  C  Y N 596 
TYR   CE2  C  Y N 597 
TYR   CZ   C  Y N 598 
TYR   OH   O  N N 599 
TYR   OXT  O  N N 600 
TYR   H    H  N N 601 
TYR   H2   H  N N 602 
TYR   HA   H  N N 603 
TYR   HB2  H  N N 604 
TYR   HB3  H  N N 605 
TYR   HD1  H  N N 606 
TYR   HD2  H  N N 607 
TYR   HE1  H  N N 608 
TYR   HE2  H  N N 609 
TYR   HH   H  N N 610 
TYR   HXT  H  N N 611 
VAL   N    N  N N 612 
VAL   CA   C  N S 613 
VAL   C    C  N N 614 
VAL   O    O  N N 615 
VAL   CB   C  N N 616 
VAL   CG1  C  N N 617 
VAL   CG2  C  N N 618 
VAL   OXT  O  N N 619 
VAL   H    H  N N 620 
VAL   H2   H  N N 621 
VAL   HA   H  N N 622 
VAL   HB   H  N N 623 
VAL   HG11 H  N N 624 
VAL   HG12 H  N N 625 
VAL   HG13 H  N N 626 
VAL   HG21 H  N N 627 
VAL   HG22 H  N N 628 
VAL   HG23 H  N N 629 
VAL   HXT  H  N N 630 
# 
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 
A1IUA C9  C10  sing N N 1   
A1IUA C9  C8   sing N N 2   
A1IUA C10 C11  sing N N 3   
A1IUA C8  C7   doub N N 4   
A1IUA C11 C13  sing N N 5   
A1IUA C11 C12  sing N N 6   
A1IUA C11 C6   sing N N 7   
A1IUA O5  C4   doub N N 8   
A1IUA C7  C6   sing N N 9   
A1IUA C7  C14  sing N N 10  
A1IUA C6  C4   sing N N 11  
A1IUA C4  C3   sing N N 12  
A1IUA C3  C2   doub N E 13  
A1IUA C2  C1   sing N N 14  
A1IUA C1  H1   sing N N 15  
A1IUA C1  H2   sing N N 16  
A1IUA C1  H3   sing N N 17  
A1IUA C2  H4   sing N N 18  
A1IUA C3  H5   sing N N 19  
A1IUA C6  H6   sing N N 20  
A1IUA C8  H7   sing N N 21  
A1IUA C9  H8   sing N N 22  
A1IUA C9  H9   sing N N 23  
A1IUA C10 H10  sing N N 24  
A1IUA C10 H11  sing N N 25  
A1IUA C12 H12  sing N N 26  
A1IUA C12 H13  sing N N 27  
A1IUA C12 H14  sing N N 28  
A1IUA C13 H15  sing N N 29  
A1IUA C13 H16  sing N N 30  
A1IUA C13 H17  sing N N 31  
A1IUA C14 H18  sing N N 32  
A1IUA C14 H19  sing N N 33  
A1IUA C14 H20  sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
BMA   C1  C2   sing N N 104 
BMA   C1  O1   sing N N 105 
BMA   C1  O5   sing N N 106 
BMA   C1  H1   sing N N 107 
BMA   C2  C3   sing N N 108 
BMA   C2  O2   sing N N 109 
BMA   C2  H2   sing N N 110 
BMA   C3  C4   sing N N 111 
BMA   C3  O3   sing N N 112 
BMA   C3  H3   sing N N 113 
BMA   C4  C5   sing N N 114 
BMA   C4  O4   sing N N 115 
BMA   C4  H4   sing N N 116 
BMA   C5  C6   sing N N 117 
BMA   C5  O5   sing N N 118 
BMA   C5  H5   sing N N 119 
BMA   C6  O6   sing N N 120 
BMA   C6  H61  sing N N 121 
BMA   C6  H62  sing N N 122 
BMA   O1  HO1  sing N N 123 
BMA   O2  HO2  sing N N 124 
BMA   O3  HO3  sing N N 125 
BMA   O4  HO4  sing N N 126 
BMA   O6  HO6  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
EPE   N1  C2   sing N N 141 
EPE   N1  C6   sing N N 142 
EPE   N1  C9   sing N N 143 
EPE   C2  C3   sing N N 144 
EPE   C2  H21  sing N N 145 
EPE   C2  H22  sing N N 146 
EPE   C3  N4   sing N N 147 
EPE   C3  H31  sing N N 148 
EPE   C3  H32  sing N N 149 
EPE   N4  C5   sing N N 150 
EPE   N4  C7   sing N N 151 
EPE   C5  C6   sing N N 152 
EPE   C5  H51  sing N N 153 
EPE   C5  H52  sing N N 154 
EPE   C6  H61  sing N N 155 
EPE   C6  H62  sing N N 156 
EPE   C7  C8   sing N N 157 
EPE   C7  H71  sing N N 158 
EPE   C7  H72  sing N N 159 
EPE   C8  O8   sing N N 160 
EPE   C8  H81  sing N N 161 
EPE   C8  H82  sing N N 162 
EPE   O8  HO8  sing N N 163 
EPE   C9  C10  sing N N 164 
EPE   C9  H91  sing N N 165 
EPE   C9  H92  sing N N 166 
EPE   C10 S    sing N N 167 
EPE   C10 H101 sing N N 168 
EPE   C10 H102 sing N N 169 
EPE   S   O1S  doub N N 170 
EPE   S   O2S  doub N N 171 
EPE   S   O3S  sing N N 172 
EPE   O3S HOS3 sing N N 173 
GLN   N   CA   sing N N 174 
GLN   N   H    sing N N 175 
GLN   N   H2   sing N N 176 
GLN   CA  C    sing N N 177 
GLN   CA  CB   sing N N 178 
GLN   CA  HA   sing N N 179 
GLN   C   O    doub N N 180 
GLN   C   OXT  sing N N 181 
GLN   CB  CG   sing N N 182 
GLN   CB  HB2  sing N N 183 
GLN   CB  HB3  sing N N 184 
GLN   CG  CD   sing N N 185 
GLN   CG  HG2  sing N N 186 
GLN   CG  HG3  sing N N 187 
GLN   CD  OE1  doub N N 188 
GLN   CD  NE2  sing N N 189 
GLN   NE2 HE21 sing N N 190 
GLN   NE2 HE22 sing N N 191 
GLN   OXT HXT  sing N N 192 
GLU   N   CA   sing N N 193 
GLU   N   H    sing N N 194 
GLU   N   H2   sing N N 195 
GLU   CA  C    sing N N 196 
GLU   CA  CB   sing N N 197 
GLU   CA  HA   sing N N 198 
GLU   C   O    doub N N 199 
GLU   C   OXT  sing N N 200 
GLU   CB  CG   sing N N 201 
GLU   CB  HB2  sing N N 202 
GLU   CB  HB3  sing N N 203 
GLU   CG  CD   sing N N 204 
GLU   CG  HG2  sing N N 205 
GLU   CG  HG3  sing N N 206 
GLU   CD  OE1  doub N N 207 
GLU   CD  OE2  sing N N 208 
GLU   OE2 HE2  sing N N 209 
GLU   OXT HXT  sing N N 210 
GLY   N   CA   sing N N 211 
GLY   N   H    sing N N 212 
GLY   N   H2   sing N N 213 
GLY   CA  C    sing N N 214 
GLY   CA  HA2  sing N N 215 
GLY   CA  HA3  sing N N 216 
GLY   C   O    doub N N 217 
GLY   C   OXT  sing N N 218 
GLY   OXT HXT  sing N N 219 
GOL   C1  O1   sing N N 220 
GOL   C1  C2   sing N N 221 
GOL   C1  H11  sing N N 222 
GOL   C1  H12  sing N N 223 
GOL   O1  HO1  sing N N 224 
GOL   C2  O2   sing N N 225 
GOL   C2  C3   sing N N 226 
GOL   C2  H2   sing N N 227 
GOL   O2  HO2  sing N N 228 
GOL   C3  O3   sing N N 229 
GOL   C3  H31  sing N N 230 
GOL   C3  H32  sing N N 231 
GOL   O3  HO3  sing N N 232 
HEM   CHA C1A  sing N N 233 
HEM   CHA C4D  doub N N 234 
HEM   CHA HHA  sing N N 235 
HEM   CHB C4A  sing N N 236 
HEM   CHB C1B  doub N N 237 
HEM   CHB HHB  sing N N 238 
HEM   CHC C4B  sing N N 239 
HEM   CHC C1C  doub N N 240 
HEM   CHC HHC  sing N N 241 
HEM   CHD C4C  doub N N 242 
HEM   CHD C1D  sing N N 243 
HEM   CHD HHD  sing N N 244 
HEM   C1A C2A  doub Y N 245 
HEM   C1A NA   sing Y N 246 
HEM   C2A C3A  sing Y N 247 
HEM   C2A CAA  sing N N 248 
HEM   C3A C4A  doub Y N 249 
HEM   C3A CMA  sing N N 250 
HEM   C4A NA   sing Y N 251 
HEM   CMA HMA  sing N N 252 
HEM   CMA HMAA sing N N 253 
HEM   CMA HMAB sing N N 254 
HEM   CAA CBA  sing N N 255 
HEM   CAA HAA  sing N N 256 
HEM   CAA HAAA sing N N 257 
HEM   CBA CGA  sing N N 258 
HEM   CBA HBA  sing N N 259 
HEM   CBA HBAA sing N N 260 
HEM   CGA O1A  doub N N 261 
HEM   CGA O2A  sing N N 262 
HEM   C1B C2B  sing N N 263 
HEM   C1B NB   sing N N 264 
HEM   C2B C3B  doub N N 265 
HEM   C2B CMB  sing N N 266 
HEM   C3B C4B  sing N N 267 
HEM   C3B CAB  sing N N 268 
HEM   C4B NB   doub N N 269 
HEM   CMB HMB  sing N N 270 
HEM   CMB HMBA sing N N 271 
HEM   CMB HMBB sing N N 272 
HEM   CAB CBB  doub N N 273 
HEM   CAB HAB  sing N N 274 
HEM   CBB HBB  sing N N 275 
HEM   CBB HBBA sing N N 276 
HEM   C1C C2C  sing Y N 277 
HEM   C1C NC   sing Y N 278 
HEM   C2C C3C  doub Y N 279 
HEM   C2C CMC  sing N N 280 
HEM   C3C C4C  sing Y N 281 
HEM   C3C CAC  sing N N 282 
HEM   C4C NC   sing Y N 283 
HEM   CMC HMC  sing N N 284 
HEM   CMC HMCA sing N N 285 
HEM   CMC HMCB sing N N 286 
HEM   CAC CBC  doub N N 287 
HEM   CAC HAC  sing N N 288 
HEM   CBC HBC  sing N N 289 
HEM   CBC HBCA sing N N 290 
HEM   C1D C2D  sing N N 291 
HEM   C1D ND   doub N N 292 
HEM   C2D C3D  doub N N 293 
HEM   C2D CMD  sing N N 294 
HEM   C3D C4D  sing N N 295 
HEM   C3D CAD  sing N N 296 
HEM   C4D ND   sing N N 297 
HEM   CMD HMD  sing N N 298 
HEM   CMD HMDA sing N N 299 
HEM   CMD HMDB sing N N 300 
HEM   CAD CBD  sing N N 301 
HEM   CAD HAD  sing N N 302 
HEM   CAD HADA sing N N 303 
HEM   CBD CGD  sing N N 304 
HEM   CBD HBD  sing N N 305 
HEM   CBD HBDA sing N N 306 
HEM   CGD O1D  doub N N 307 
HEM   CGD O2D  sing N N 308 
HEM   O2A H2A  sing N N 309 
HEM   O2D H2D  sing N N 310 
HEM   FE  NA   sing N N 311 
HEM   FE  NB   sing N N 312 
HEM   FE  NC   sing N N 313 
HEM   FE  ND   sing N N 314 
HIS   N   CA   sing N N 315 
HIS   N   H    sing N N 316 
HIS   N   H2   sing N N 317 
HIS   CA  C    sing N N 318 
HIS   CA  CB   sing N N 319 
HIS   CA  HA   sing N N 320 
HIS   C   O    doub N N 321 
HIS   C   OXT  sing N N 322 
HIS   CB  CG   sing N N 323 
HIS   CB  HB2  sing N N 324 
HIS   CB  HB3  sing N N 325 
HIS   CG  ND1  sing Y N 326 
HIS   CG  CD2  doub Y N 327 
HIS   ND1 CE1  doub Y N 328 
HIS   ND1 HD1  sing N N 329 
HIS   CD2 NE2  sing Y N 330 
HIS   CD2 HD2  sing N N 331 
HIS   CE1 NE2  sing Y N 332 
HIS   CE1 HE1  sing N N 333 
HIS   NE2 HE2  sing N N 334 
HIS   OXT HXT  sing N N 335 
HOH   O   H1   sing N N 336 
HOH   O   H2   sing N N 337 
ILE   N   CA   sing N N 338 
ILE   N   H    sing N N 339 
ILE   N   H2   sing N N 340 
ILE   CA  C    sing N N 341 
ILE   CA  CB   sing N N 342 
ILE   CA  HA   sing N N 343 
ILE   C   O    doub N N 344 
ILE   C   OXT  sing N N 345 
ILE   CB  CG1  sing N N 346 
ILE   CB  CG2  sing N N 347 
ILE   CB  HB   sing N N 348 
ILE   CG1 CD1  sing N N 349 
ILE   CG1 HG12 sing N N 350 
ILE   CG1 HG13 sing N N 351 
ILE   CG2 HG21 sing N N 352 
ILE   CG2 HG22 sing N N 353 
ILE   CG2 HG23 sing N N 354 
ILE   CD1 HD11 sing N N 355 
ILE   CD1 HD12 sing N N 356 
ILE   CD1 HD13 sing N N 357 
ILE   OXT HXT  sing N N 358 
LEU   N   CA   sing N N 359 
LEU   N   H    sing N N 360 
LEU   N   H2   sing N N 361 
LEU   CA  C    sing N N 362 
LEU   CA  CB   sing N N 363 
LEU   CA  HA   sing N N 364 
LEU   C   O    doub N N 365 
LEU   C   OXT  sing N N 366 
LEU   CB  CG   sing N N 367 
LEU   CB  HB2  sing N N 368 
LEU   CB  HB3  sing N N 369 
LEU   CG  CD1  sing N N 370 
LEU   CG  CD2  sing N N 371 
LEU   CG  HG   sing N N 372 
LEU   CD1 HD11 sing N N 373 
LEU   CD1 HD12 sing N N 374 
LEU   CD1 HD13 sing N N 375 
LEU   CD2 HD21 sing N N 376 
LEU   CD2 HD22 sing N N 377 
LEU   CD2 HD23 sing N N 378 
LEU   OXT HXT  sing N N 379 
LYS   N   CA   sing N N 380 
LYS   N   H    sing N N 381 
LYS   N   H2   sing N N 382 
LYS   CA  C    sing N N 383 
LYS   CA  CB   sing N N 384 
LYS   CA  HA   sing N N 385 
LYS   C   O    doub N N 386 
LYS   C   OXT  sing N N 387 
LYS   CB  CG   sing N N 388 
LYS   CB  HB2  sing N N 389 
LYS   CB  HB3  sing N N 390 
LYS   CG  CD   sing N N 391 
LYS   CG  HG2  sing N N 392 
LYS   CG  HG3  sing N N 393 
LYS   CD  CE   sing N N 394 
LYS   CD  HD2  sing N N 395 
LYS   CD  HD3  sing N N 396 
LYS   CE  NZ   sing N N 397 
LYS   CE  HE2  sing N N 398 
LYS   CE  HE3  sing N N 399 
LYS   NZ  HZ1  sing N N 400 
LYS   NZ  HZ2  sing N N 401 
LYS   NZ  HZ3  sing N N 402 
LYS   OXT HXT  sing N N 403 
MAN   C1  C2   sing N N 404 
MAN   C1  O1   sing N N 405 
MAN   C1  O5   sing N N 406 
MAN   C1  H1   sing N N 407 
MAN   C2  C3   sing N N 408 
MAN   C2  O2   sing N N 409 
MAN   C2  H2   sing N N 410 
MAN   C3  C4   sing N N 411 
MAN   C3  O3   sing N N 412 
MAN   C3  H3   sing N N 413 
MAN   C4  C5   sing N N 414 
MAN   C4  O4   sing N N 415 
MAN   C4  H4   sing N N 416 
MAN   C5  C6   sing N N 417 
MAN   C5  O5   sing N N 418 
MAN   C5  H5   sing N N 419 
MAN   C6  O6   sing N N 420 
MAN   C6  H61  sing N N 421 
MAN   C6  H62  sing N N 422 
MAN   O1  HO1  sing N N 423 
MAN   O2  HO2  sing N N 424 
MAN   O3  HO3  sing N N 425 
MAN   O4  HO4  sing N N 426 
MAN   O6  HO6  sing N N 427 
MET   N   CA   sing N N 428 
MET   N   H    sing N N 429 
MET   N   H2   sing N N 430 
MET   CA  C    sing N N 431 
MET   CA  CB   sing N N 432 
MET   CA  HA   sing N N 433 
MET   C   O    doub N N 434 
MET   C   OXT  sing N N 435 
MET   CB  CG   sing N N 436 
MET   CB  HB2  sing N N 437 
MET   CB  HB3  sing N N 438 
MET   CG  SD   sing N N 439 
MET   CG  HG2  sing N N 440 
MET   CG  HG3  sing N N 441 
MET   SD  CE   sing N N 442 
MET   CE  HE1  sing N N 443 
MET   CE  HE2  sing N N 444 
MET   CE  HE3  sing N N 445 
MET   OXT HXT  sing N N 446 
NAG   C1  C2   sing N N 447 
NAG   C1  O1   sing N N 448 
NAG   C1  O5   sing N N 449 
NAG   C1  H1   sing N N 450 
NAG   C2  C3   sing N N 451 
NAG   C2  N2   sing N N 452 
NAG   C2  H2   sing N N 453 
NAG   C3  C4   sing N N 454 
NAG   C3  O3   sing N N 455 
NAG   C3  H3   sing N N 456 
NAG   C4  C5   sing N N 457 
NAG   C4  O4   sing N N 458 
NAG   C4  H4   sing N N 459 
NAG   C5  C6   sing N N 460 
NAG   C5  O5   sing N N 461 
NAG   C5  H5   sing N N 462 
NAG   C6  O6   sing N N 463 
NAG   C6  H61  sing N N 464 
NAG   C6  H62  sing N N 465 
NAG   C7  C8   sing N N 466 
NAG   C7  N2   sing N N 467 
NAG   C7  O7   doub N N 468 
NAG   C8  H81  sing N N 469 
NAG   C8  H82  sing N N 470 
NAG   C8  H83  sing N N 471 
NAG   N2  HN2  sing N N 472 
NAG   O1  HO1  sing N N 473 
NAG   O3  HO3  sing N N 474 
NAG   O4  HO4  sing N N 475 
NAG   O6  HO6  sing N N 476 
PHE   N   CA   sing N N 477 
PHE   N   H    sing N N 478 
PHE   N   H2   sing N N 479 
PHE   CA  C    sing N N 480 
PHE   CA  CB   sing N N 481 
PHE   CA  HA   sing N N 482 
PHE   C   O    doub N N 483 
PHE   C   OXT  sing N N 484 
PHE   CB  CG   sing N N 485 
PHE   CB  HB2  sing N N 486 
PHE   CB  HB3  sing N N 487 
PHE   CG  CD1  doub Y N 488 
PHE   CG  CD2  sing Y N 489 
PHE   CD1 CE1  sing Y N 490 
PHE   CD1 HD1  sing N N 491 
PHE   CD2 CE2  doub Y N 492 
PHE   CD2 HD2  sing N N 493 
PHE   CE1 CZ   doub Y N 494 
PHE   CE1 HE1  sing N N 495 
PHE   CE2 CZ   sing Y N 496 
PHE   CE2 HE2  sing N N 497 
PHE   CZ  HZ   sing N N 498 
PHE   OXT HXT  sing N N 499 
PRO   N   CA   sing N N 500 
PRO   N   CD   sing N N 501 
PRO   N   H    sing N N 502 
PRO   CA  C    sing N N 503 
PRO   CA  CB   sing N N 504 
PRO   CA  HA   sing N N 505 
PRO   C   O    doub N N 506 
PRO   C   OXT  sing N N 507 
PRO   CB  CG   sing N N 508 
PRO   CB  HB2  sing N N 509 
PRO   CB  HB3  sing N N 510 
PRO   CG  CD   sing N N 511 
PRO   CG  HG2  sing N N 512 
PRO   CG  HG3  sing N N 513 
PRO   CD  HD2  sing N N 514 
PRO   CD  HD3  sing N N 515 
PRO   OXT HXT  sing N N 516 
SER   N   CA   sing N N 517 
SER   N   H    sing N N 518 
SER   N   H2   sing N N 519 
SER   CA  C    sing N N 520 
SER   CA  CB   sing N N 521 
SER   CA  HA   sing N N 522 
SER   C   O    doub N N 523 
SER   C   OXT  sing N N 524 
SER   CB  OG   sing N N 525 
SER   CB  HB2  sing N N 526 
SER   CB  HB3  sing N N 527 
SER   OG  HG   sing N N 528 
SER   OXT HXT  sing N N 529 
SO4   S   O1   doub N N 530 
SO4   S   O2   doub N N 531 
SO4   S   O3   sing N N 532 
SO4   S   O4   sing N N 533 
THR   N   CA   sing N N 534 
THR   N   H    sing N N 535 
THR   N   H2   sing N N 536 
THR   CA  C    sing N N 537 
THR   CA  CB   sing N N 538 
THR   CA  HA   sing N N 539 
THR   C   O    doub N N 540 
THR   C   OXT  sing N N 541 
THR   CB  OG1  sing N N 542 
THR   CB  CG2  sing N N 543 
THR   CB  HB   sing N N 544 
THR   OG1 HG1  sing N N 545 
THR   CG2 HG21 sing N N 546 
THR   CG2 HG22 sing N N 547 
THR   CG2 HG23 sing N N 548 
THR   OXT HXT  sing N N 549 
TRP   N   CA   sing N N 550 
TRP   N   H    sing N N 551 
TRP   N   H2   sing N N 552 
TRP   CA  C    sing N N 553 
TRP   CA  CB   sing N N 554 
TRP   CA  HA   sing N N 555 
TRP   C   O    doub N N 556 
TRP   C   OXT  sing N N 557 
TRP   CB  CG   sing N N 558 
TRP   CB  HB2  sing N N 559 
TRP   CB  HB3  sing N N 560 
TRP   CG  CD1  doub Y N 561 
TRP   CG  CD2  sing Y N 562 
TRP   CD1 NE1  sing Y N 563 
TRP   CD1 HD1  sing N N 564 
TRP   CD2 CE2  doub Y N 565 
TRP   CD2 CE3  sing Y N 566 
TRP   NE1 CE2  sing Y N 567 
TRP   NE1 HE1  sing N N 568 
TRP   CE2 CZ2  sing Y N 569 
TRP   CE3 CZ3  doub Y N 570 
TRP   CE3 HE3  sing N N 571 
TRP   CZ2 CH2  doub Y N 572 
TRP   CZ2 HZ2  sing N N 573 
TRP   CZ3 CH2  sing Y N 574 
TRP   CZ3 HZ3  sing N N 575 
TRP   CH2 HH2  sing N N 576 
TRP   OXT HXT  sing N N 577 
TYR   N   CA   sing N N 578 
TYR   N   H    sing N N 579 
TYR   N   H2   sing N N 580 
TYR   CA  C    sing N N 581 
TYR   CA  CB   sing N N 582 
TYR   CA  HA   sing N N 583 
TYR   C   O    doub N N 584 
TYR   C   OXT  sing N N 585 
TYR   CB  CG   sing N N 586 
TYR   CB  HB2  sing N N 587 
TYR   CB  HB3  sing N N 588 
TYR   CG  CD1  doub Y N 589 
TYR   CG  CD2  sing Y N 590 
TYR   CD1 CE1  sing Y N 591 
TYR   CD1 HD1  sing N N 592 
TYR   CD2 CE2  doub Y N 593 
TYR   CD2 HD2  sing N N 594 
TYR   CE1 CZ   doub Y N 595 
TYR   CE1 HE1  sing N N 596 
TYR   CE2 CZ   sing Y N 597 
TYR   CE2 HE2  sing N N 598 
TYR   CZ  OH   sing N N 599 
TYR   OH  HH   sing N N 600 
TYR   OXT HXT  sing N N 601 
VAL   N   CA   sing N N 602 
VAL   N   H    sing N N 603 
VAL   N   H2   sing N N 604 
VAL   CA  C    sing N N 605 
VAL   CA  CB   sing N N 606 
VAL   CA  HA   sing N N 607 
VAL   C   O    doub N N 608 
VAL   C   OXT  sing N N 609 
VAL   CB  CG1  sing N N 610 
VAL   CB  CG2  sing N N 611 
VAL   CB  HB   sing N N 612 
VAL   CG1 HG11 sing N N 613 
VAL   CG1 HG12 sing N N 614 
VAL   CG1 HG13 sing N N 615 
VAL   CG2 HG21 sing N N 616 
VAL   CG2 HG22 sing N N 617 
VAL   CG2 HG23 sing N N 618 
VAL   OXT HXT  sing N N 619 
# 
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 
4 MAN 4 n 
4 MAN 5 n 
4 MAN 6 n 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
5 MAN 4 n 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 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                    9HED 
_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]   0.003685 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001460 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013448 
_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]   0.010186 
_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   ? 60.987  3.709   59.370 1.00 107.29 ? 14  GLN   A N   1 
ATOM   2    C  CA  . GLN   A  1  1   ? 62.116  4.111   58.484 1.00 111.56 ? 14  GLN   A CA  1 
ATOM   3    C  C   . GLN   A  1  1   ? 62.062  3.451   57.097 1.00 103.50 ? 14  GLN   A C   1 
ATOM   4    O  O   . GLN   A  1  1   ? 62.761  3.929   56.204 1.00 88.79  ? 14  GLN   A O   1 
ATOM   5    C  CB  . GLN   A  1  1   ? 63.449  3.806   59.169 1.00 116.27 ? 14  GLN   A CB  1 
ATOM   6    C  CG  . GLN   A  1  1   ? 63.721  2.315   59.345 1.00 126.61 ? 14  GLN   A CG  1 
ATOM   7    C  CD  . GLN   A  1  1   ? 65.169  2.001   59.655 1.00 131.33 ? 14  GLN   A CD  1 
ATOM   8    O  OE1 . GLN   A  1  1   ? 66.043  2.880   59.650 1.00 129.06 ? 14  GLN   A OE1 1 
ATOM   9    N  NE2 . GLN   A  1  1   ? 65.436  0.727   59.898 1.00 126.01 ? 14  GLN   A NE2 1 
ATOM   10   N  N   . GLY   A  1  2   ? 61.321  2.332   56.929 1.00 90.54  ? 15  GLY   A N   1 
ATOM   11   C  CA  . GLY   A  1  2   ? 60.943  1.834   55.612 1.00 73.97  ? 15  GLY   A CA  1 
ATOM   12   C  C   . GLY   A  1  2   ? 60.971  0.307   55.486 1.00 62.06  ? 15  GLY   A C   1 
ATOM   13   O  O   . GLY   A  1  2   ? 61.300  -0.415  56.409 1.00 59.50  ? 15  GLY   A O   1 
ATOM   14   N  N   . VAL   A  1  3   ? 60.672  -0.175  54.284 1.00 54.83  ? 16  VAL   A N   1 
ATOM   15   C  CA  . VAL   A  1  3   ? 60.482  -1.583  53.983 1.00 49.97  ? 16  VAL   A CA  1 
ATOM   16   C  C   . VAL   A  1  3   ? 61.466  -1.964  52.880 1.00 48.77  ? 16  VAL   A C   1 
ATOM   17   O  O   . VAL   A  1  3   ? 61.847  -1.116  52.066 1.00 40.67  ? 16  VAL   A O   1 
ATOM   18   C  CB  . VAL   A  1  3   ? 59.008  -1.773  53.541 1.00 54.92  ? 16  VAL   A CB  1 
ATOM   19   C  CG1 . VAL   A  1  3   ? 58.724  -3.039  52.741 1.00 53.01  ? 16  VAL   A CG1 1 
ATOM   20   C  CG2 . VAL   A  1  3   ? 58.058  -1.690  54.722 1.00 56.97  ? 16  VAL   A CG2 1 
ATOM   21   N  N   . ASP   A  1  4   ? 61.848  -3.248  52.866 1.00 51.57  ? 17  ASP   A N   1 
ATOM   22   C  CA  . ASP   A  1  4   ? 62.628  -3.817  51.778 1.00 57.90  ? 17  ASP   A CA  1 
ATOM   23   C  C   . ASP   A  1  4   ? 61.686  -4.557  50.822 1.00 57.95  ? 17  ASP   A C   1 
ATOM   24   O  O   . ASP   A  1  4   ? 61.188  -5.621  51.176 1.00 57.81  ? 17  ASP   A O   1 
ATOM   25   C  CB  . ASP   A  1  4   ? 63.737  -4.714  52.305 1.00 63.71  ? 17  ASP   A CB  1 
ATOM   26   C  CG  . ASP   A  1  4   ? 64.929  -4.873  51.371 1.00 71.56  ? 17  ASP   A CG  1 
ATOM   27   O  OD1 . ASP   A  1  4   ? 64.871  -4.385  50.223 1.00 75.58  ? 17  ASP   A OD1 1 
ATOM   28   O  OD2 . ASP   A  1  4   ? 65.941  -5.443  51.802 1.00 91.37  ? 17  ASP   A OD2 1 
ATOM   29   N  N   . PRO   A  1  5   ? 61.392  -4.032  49.602 1.00 64.48  ? 18  PRO   A N   1 
ATOM   30   C  CA  . PRO   A  1  5   ? 60.280  -4.547  48.784 1.00 58.86  ? 18  PRO   A CA  1 
ATOM   31   C  C   . PRO   A  1  5   ? 60.572  -5.862  48.059 1.00 48.92  ? 18  PRO   A C   1 
ATOM   32   O  O   . PRO   A  1  5   ? 61.510  -5.942  47.266 1.00 45.21  ? 18  PRO   A O   1 
ATOM   33   C  CB  . PRO   A  1  5   ? 59.984  -3.421  47.781 1.00 56.01  ? 18  PRO   A CB  1 
ATOM   34   C  CG  . PRO   A  1  5   ? 61.229  -2.547  47.776 1.00 58.88  ? 18  PRO   A CG  1 
ATOM   35   C  CD  . PRO   A  1  5   ? 62.118  -2.927  48.950 1.00 56.89  ? 18  PRO   A CD  1 
ATOM   36   N  N   . PRO   A  1  6   ? 59.745  -6.913  48.251 1.00 44.49  ? 19  PRO   A N   1 
ATOM   37   C  CA  . PRO   A  1  6   ? 60.033  -8.223  47.666 1.00 46.97  ? 19  PRO   A CA  1 
ATOM   38   C  C   . PRO   A  1  6   ? 59.763  -8.204  46.165 1.00 44.00  ? 19  PRO   A C   1 
ATOM   39   O  O   . PRO   A  1  6   ? 59.004  -7.373  45.690 1.00 42.67  ? 19  PRO   A O   1 
ATOM   40   C  CB  . PRO   A  1  6   ? 59.090  -9.157  48.420 1.00 43.21  ? 19  PRO   A CB  1 
ATOM   41   C  CG  . PRO   A  1  6   ? 57.891  -8.272  48.718 1.00 47.93  ? 19  PRO   A CG  1 
ATOM   42   C  CD  . PRO   A  1  6   ? 58.478  -6.891  48.997 1.00 46.65  ? 19  PRO   A CD  1 
ATOM   43   N  N   . PRO   A  1  7   ? 60.401  -9.092  45.373 1.00 45.32  ? 20  PRO   A N   1 
ATOM   44   C  CA  . PRO   A  1  7   ? 60.079  -9.232  43.957 1.00 43.23  ? 20  PRO   A CA  1 
ATOM   45   C  C   . PRO   A  1  7   ? 58.633  -9.670  43.782 1.00 37.81  ? 20  PRO   A C   1 
ATOM   46   O  O   . PRO   A  1  7   ? 58.033  -10.206 44.708 1.00 35.29  ? 20  PRO   A O   1 
ATOM   47   C  CB  . PRO   A  1  7   ? 61.087  -10.258 43.412 1.00 45.95  ? 20  PRO   A CB  1 
ATOM   48   C  CG  . PRO   A  1  7   ? 61.607  -10.951 44.636 1.00 46.74  ? 20  PRO   A CG  1 
ATOM   49   C  CD  . PRO   A  1  7   ? 61.519  -9.956  45.772 1.00 48.03  ? 20  PRO   A CD  1 
ATOM   50   N  N   . PRO   A  1  8   ? 58.015  -9.386  42.613 1.00 34.41  ? 21  PRO   A N   1 
ATOM   51   C  CA  . PRO   A  1  8   ? 56.599  -9.673  42.415 1.00 35.97  ? 21  PRO   A CA  1 
ATOM   52   C  C   . PRO   A  1  8   ? 56.324  -11.169 42.469 1.00 36.40  ? 21  PRO   A C   1 
ATOM   53   O  O   . PRO   A  1  8   ? 57.152  -11.975 42.077 1.00 35.76  ? 21  PRO   A O   1 
ATOM   54   C  CB  . PRO   A  1  8   ? 56.277  -9.085  41.059 1.00 35.39  ? 21  PRO   A CB  1 
ATOM   55   C  CG  . PRO   A  1  8   ? 57.616  -9.096  40.350 1.00 36.94  ? 21  PRO   A CG  1 
ATOM   56   C  CD  . PRO   A  1  8   ? 58.633  -8.754  41.432 1.00 36.98  ? 21  PRO   A CD  1 
ATOM   57   N  N   . PRO   A  1  9   ? 55.144  -11.580 42.961 1.00 35.70  ? 22  PRO   A N   1 
ATOM   58   C  CA  . PRO   A  1  9   ? 54.719  -12.968 42.856 1.00 35.07  ? 22  PRO   A CA  1 
ATOM   59   C  C   . PRO   A  1  9   ? 54.742  -13.362 41.382 1.00 38.00  ? 22  PRO   A C   1 
ATOM   60   O  O   . PRO   A  1  9   ? 54.526  -12.527 40.509 1.00 31.84  ? 22  PRO   A O   1 
ATOM   61   C  CB  . PRO   A  1  9   ? 53.299  -12.964 43.409 1.00 32.90  ? 22  PRO   A CB  1 
ATOM   62   C  CG  . PRO   A  1  9   ? 53.214  -11.720 44.247 1.00 35.31  ? 22  PRO   A CG  1 
ATOM   63   C  CD  . PRO   A  1  9   ? 54.154  -10.718 43.619 1.00 38.62  ? 22  PRO   A CD  1 
ATOM   64   N  N   . GLY   A  1  10  ? 54.985  -14.652 41.145 1.00 36.04  ? 23  GLY   A N   1 
ATOM   65   C  CA  . GLY   A  1  10  ? 54.817  -15.274 39.848 1.00 34.44  ? 23  GLY   A CA  1 
ATOM   66   C  C   . GLY   A  1  10  ? 53.353  -15.682 39.633 1.00 39.32  ? 23  GLY   A C   1 
ATOM   67   O  O   . GLY   A  1  10  ? 52.472  -15.346 40.436 1.00 34.44  ? 23  GLY   A O   1 
ATOM   68   N  N   . PRO   A  1  11  ? 53.055  -16.378 38.513 1.00 38.36  ? 24  PRO   A N   1 
ATOM   69   C  CA  . PRO   A  1  11  ? 51.688  -16.806 38.201 1.00 38.35  ? 24  PRO   A CA  1 
ATOM   70   C  C   . PRO   A  1  11  ? 51.117  -17.676 39.313 1.00 35.69  ? 24  PRO   A C   1 
ATOM   71   O  O   . PRO   A  1  11  ? 51.875  -18.295 40.041 1.00 34.93  ? 24  PRO   A O   1 
ATOM   72   C  CB  . PRO   A  1  11  ? 51.828  -17.596 36.888 1.00 37.87  ? 24  PRO   A CB  1 
ATOM   73   C  CG  . PRO   A  1  11  ? 53.156  -17.098 36.292 1.00 40.66  ? 24  PRO   A CG  1 
ATOM   74   C  CD  . PRO   A  1  11  ? 54.035  -16.773 37.487 1.00 36.59  ? 24  PRO   A CD  1 
ATOM   75   N  N   . PRO   A  1  12  ? 49.784  -17.750 39.494 1.00 34.71  ? 25  PRO   A N   1 
ATOM   76   C  CA  . PRO   A  1  12  ? 49.225  -18.640 40.504 1.00 41.59  ? 25  PRO   A CA  1 
ATOM   77   C  C   . PRO   A  1  12  ? 49.508  -20.098 40.132 1.00 38.54  ? 25  PRO   A C   1 
ATOM   78   O  O   . PRO   A  1  12  ? 49.655  -20.454 38.967 1.00 34.55  ? 25  PRO   A O   1 
ATOM   79   C  CB  . PRO   A  1  12  ? 47.734  -18.275 40.552 1.00 42.72  ? 25  PRO   A CB  1 
ATOM   80   C  CG  . PRO   A  1  12  ? 47.456  -17.721 39.162 1.00 45.32  ? 25  PRO   A CG  1 
ATOM   81   C  CD  . PRO   A  1  12  ? 48.751  -17.049 38.719 1.00 40.68  ? 25  PRO   A CD  1 
ATOM   82   N  N   . SER   A  1  13  ? 49.685  -20.919 41.166 1.00 42.96  ? 26  SER   A N   1 
ATOM   83   C  CA  A SER   A  1  13  ? 49.893  -22.350 41.010 0.50 44.71  ? 26  SER   A CA  1 
ATOM   84   C  CA  B SER   A  1  13  ? 49.898  -22.348 41.002 0.50 46.15  ? 26  SER   A CA  1 
ATOM   85   C  C   . SER   A  1  13  ? 48.745  -22.966 40.214 1.00 43.16  ? 26  SER   A C   1 
ATOM   86   O  O   . SER   A  1  13  ? 48.981  -23.762 39.320 1.00 44.71  ? 26  SER   A O   1 
ATOM   87   C  CB  A SER   A  1  13  ? 50.023  -23.020 42.355 0.50 44.20  ? 26  SER   A CB  1 
ATOM   88   C  CB  B SER   A  1  13  ? 50.055  -23.033 42.334 0.50 47.59  ? 26  SER   A CB  1 
ATOM   89   O  OG  A SER   A  1  13  ? 51.148  -22.512 43.049 0.50 43.29  ? 26  SER   A OG  1 
ATOM   90   O  OG  B SER   A  1  13  ? 49.937  -24.438 42.161 0.50 50.23  ? 26  SER   A OG  1 
ATOM   91   N  N   . PHE   A  1  14  ? 47.509  -22.580 40.565 1.00 37.88  ? 27  PHE   A N   1 
ATOM   92   C  CA  . PHE   A  1  14  ? 46.306  -23.018 39.872 1.00 36.72  ? 27  PHE   A CA  1 
ATOM   93   C  C   . PHE   A  1  14  ? 45.751  -21.888 39.004 1.00 35.51  ? 27  PHE   A C   1 
ATOM   94   O  O   . PHE   A  1  14  ? 45.459  -20.809 39.520 1.00 34.09  ? 27  PHE   A O   1 
ATOM   95   C  CB  . PHE   A  1  14  ? 45.282  -23.454 40.925 1.00 33.38  ? 27  PHE   A CB  1 
ATOM   96   C  CG  . PHE   A  1  14  ? 43.955  -23.883 40.322 1.00 35.11  ? 27  PHE   A CG  1 
ATOM   97   C  CD1 . PHE   A  1  14  ? 43.867  -25.072 39.602 1.00 32.08  ? 27  PHE   A CD1 1 
ATOM   98   C  CD2 . PHE   A  1  14  ? 42.799  -23.114 40.489 1.00 33.60  ? 27  PHE   A CD2 1 
ATOM   99   C  CE1 . PHE   A  1  14  ? 42.664  -25.448 39.012 1.00 37.15  ? 27  PHE   A CE1 1 
ATOM   100  C  CE2 . PHE   A  1  14  ? 41.591  -23.511 39.923 1.00 36.71  ? 27  PHE   A CE2 1 
ATOM   101  C  CZ  . PHE   A  1  14  ? 41.525  -24.671 39.182 1.00 38.19  ? 27  PHE   A CZ  1 
ATOM   102  N  N   . THR   A  1  15  ? 45.563  -22.156 37.699 1.00 33.51  ? 28  THR   A N   1 
ATOM   103  C  CA  . THR   A  1  15  ? 45.164  -21.117 36.763 1.00 34.28  ? 28  THR   A CA  1 
ATOM   104  C  C   . THR   A  1  15  ? 43.816  -21.436 36.122 1.00 33.62  ? 28  THR   A C   1 
ATOM   105  O  O   . THR   A  1  15  ? 43.470  -20.811 35.116 1.00 33.38  ? 28  THR   A O   1 
ATOM   106  C  CB  . THR   A  1  15  ? 46.221  -20.920 35.677 1.00 38.78  ? 28  THR   A CB  1 
ATOM   107  O  OG1 . THR   A  1  15  ? 46.181  -22.074 34.848 1.00 38.31  ? 28  THR   A OG1 1 
ATOM   108  C  CG2 . THR   A  1  15  ? 47.613  -20.691 36.228 1.00 41.90  ? 28  THR   A CG2 1 
ATOM   109  N  N   . GLY   A  1  16  ? 43.053  -22.374 36.701 1.00 30.26  ? 29  GLY   A N   1 
ATOM   110  C  CA  . GLY   A  1  16  ? 41.730  -22.661 36.169 1.00 31.33  ? 29  GLY   A CA  1 
ATOM   111  C  C   . GLY   A  1  16  ? 40.651  -21.743 36.743 1.00 29.72  ? 29  GLY   A C   1 
ATOM   112  O  O   . GLY   A  1  16  ? 40.928  -20.838 37.514 1.00 30.00  ? 29  GLY   A O   1 
ATOM   113  N  N   . THR   A  1  17  ? 39.398  -22.003 36.371 1.00 33.38  ? 30  THR   A N   1 
ATOM   114  C  CA  . THR   A  1  17  ? 38.280  -21.271 36.930 1.00 34.83  ? 30  THR   A CA  1 
ATOM   115  C  C   . THR   A  1  17  ? 38.051  -21.727 38.366 1.00 36.81  ? 30  THR   A C   1 
ATOM   116  O  O   . THR   A  1  17  ? 38.446  -22.827 38.757 1.00 37.44  ? 30  THR   A O   1 
ATOM   117  C  CB  . THR   A  1  17  ? 37.014  -21.441 36.095 1.00 39.69  ? 30  THR   A CB  1 
ATOM   118  O  OG1 . THR   A  1  17  ? 36.173  -20.436 36.669 1.00 38.34  ? 30  THR   A OG1 1 
ATOM   119  C  CG2 . THR   A  1  17  ? 36.422  -22.839 36.209 1.00 36.86  ? 30  THR   A CG2 1 
ATOM   120  N  N   . LYS   A  1  18  ? 37.421  -20.840 39.136 1.00 33.00  ? 31  LYS   A N   1 
ATOM   121  C  CA  . LYS   A  1  18  ? 37.011  -21.153 40.490 1.00 32.49  ? 31  LYS   A CA  1 
ATOM   122  C  C   . LYS   A  1  18  ? 36.022  -20.089 40.943 1.00 31.32  ? 31  LYS   A C   1 
ATOM   123  O  O   . LYS   A  1  18  ? 35.936  -19.023 40.352 1.00 34.12  ? 31  LYS   A O   1 
ATOM   124  C  CB  . LYS   A  1  18  ? 38.201  -21.243 41.454 1.00 33.02  ? 31  LYS   A CB  1 
ATOM   125  C  CG  . LYS   A  1  18  ? 38.970  -19.966 41.704 1.00 40.87  ? 31  LYS   A CG  1 
ATOM   126  C  CD  . LYS   A  1  18  ? 40.090  -20.149 42.725 1.00 46.78  ? 31  LYS   A CD  1 
ATOM   127  C  CE  . LYS   A  1  18  ? 40.404  -18.867 43.428 1.00 60.61  ? 31  LYS   A CE  1 
ATOM   128  N  NZ  . LYS   A  1  18  ? 41.606  -18.924 44.262 1.00 65.35  ? 31  LYS   A NZ  1 
ATOM   129  N  N   . LEU   A  1  19  ? 35.293  -20.403 42.002 1.00 32.06  ? 32  LEU   A N   1 
ATOM   130  C  CA  . LEU   A  1  19  ? 34.408  -19.462 42.646 1.00 32.68  ? 32  LEU   A CA  1 
ATOM   131  C  C   . LEU   A  1  19  ? 35.255  -18.428 43.369 1.00 33.01  ? 32  LEU   A C   1 
ATOM   132  O  O   . LEU   A  1  19  ? 36.071  -18.804 44.203 1.00 34.27  ? 32  LEU   A O   1 
ATOM   133  C  CB  . LEU   A  1  19  ? 33.510  -20.208 43.631 1.00 34.52  ? 32  LEU   A CB  1 
ATOM   134  C  CG  . LEU   A  1  19  ? 32.587  -19.307 44.470 1.00 38.20  ? 32  LEU   A CG  1 
ATOM   135  C  CD1 . LEU   A  1  19  ? 31.569  -18.609 43.610 1.00 31.67  ? 32  LEU   A CD1 1 
ATOM   136  C  CD2 . LEU   A  1  19  ? 31.875  -20.111 45.563 1.00 35.44  ? 32  LEU   A CD2 1 
ATOM   137  N  N   . VAL   A  1  20  ? 35.052  -17.144 43.049 1.00 33.61  ? 33  VAL   A N   1 
ATOM   138  C  CA  . VAL   A  1  20  ? 35.820  -16.094 43.691 1.00 34.91  ? 33  VAL   A CA  1 
ATOM   139  C  C   . VAL   A  1  20  ? 34.908  -15.299 44.614 1.00 30.46  ? 33  VAL   A C   1 
ATOM   140  O  O   . VAL   A  1  20  ? 35.378  -14.736 45.591 1.00 34.26  ? 33  VAL   A O   1 
ATOM   141  C  CB  . VAL   A  1  20  ? 36.596  -15.189 42.715 1.00 34.22  ? 33  VAL   A CB  1 
ATOM   142  C  CG1 . VAL   A  1  20  ? 37.616  -15.965 41.898 1.00 36.69  ? 33  VAL   A CG1 1 
ATOM   143  C  CG2 . VAL   A  1  20  ? 35.674  -14.472 41.782 1.00 38.50  ? 33  VAL   A CG2 1 
ATOM   144  N  N   . ASN   A  1  21  ? 33.614  -15.272 44.332 1.00 28.94  ? 34  ASN   A N   1 
ATOM   145  C  CA  . ASN   A  1  21  ? 32.655  -14.673 45.241 1.00 30.26  ? 34  ASN   A CA  1 
ATOM   146  C  C   . ASN   A  1  21  ? 32.204  -15.723 46.254 1.00 30.48  ? 34  ASN   A C   1 
ATOM   147  O  O   . ASN   A  1  21  ? 31.137  -16.299 46.122 1.00 33.09  ? 34  ASN   A O   1 
ATOM   148  C  CB  . ASN   A  1  21  ? 31.465  -14.114 44.480 1.00 31.40  ? 34  ASN   A CB  1 
ATOM   149  C  CG  . ASN   A  1  21  ? 30.527  -13.328 45.369 1.00 31.49  ? 34  ASN   A CG  1 
ATOM   150  O  OD1 . ASN   A  1  21  ? 30.762  -13.170 46.575 1.00 34.07  ? 34  ASN   A OD1 1 
ATOM   151  N  ND2 . ASN   A  1  21  ? 29.475  -12.808 44.772 1.00 26.79  ? 34  ASN   A ND2 1 
ATOM   152  N  N   . ASP   A  1  22  ? 33.025  -15.964 47.272 1.00 33.23  ? 35  ASP   A N   1 
ATOM   153  C  CA  . ASP   A  1  22  ? 32.861  -17.105 48.158 1.00 33.02  ? 35  ASP   A CA  1 
ATOM   154  C  C   . ASP   A  1  22  ? 32.700  -16.591 49.580 1.00 33.93  ? 35  ASP   A C   1 
ATOM   155  O  O   . ASP   A  1  22  ? 32.759  -15.383 49.831 1.00 38.77  ? 35  ASP   A O   1 
ATOM   156  C  CB  . ASP   A  1  22  ? 34.010  -18.098 47.997 1.00 35.77  ? 35  ASP   A CB  1 
ATOM   157  C  CG  . ASP   A  1  22  ? 35.424  -17.613 48.312 1.00 38.99  ? 35  ASP   A CG  1 
ATOM   158  O  OD1 . ASP   A  1  22  ? 35.587  -16.464 48.738 1.00 49.48  ? 35  ASP   A OD1 1 
ATOM   159  O  OD2 . ASP   A  1  22  ? 36.383  -18.366 48.088 1.00 45.53  ? 35  ASP   A OD2 1 
ATOM   160  N  N   . ALA   A  1  23  ? 32.526  -17.524 50.512 1.00 35.57  ? 36  ALA   A N   1 
ATOM   161  C  CA  . ALA   A  1  23  ? 32.152  -17.189 51.880 1.00 36.48  ? 36  ALA   A CA  1 
ATOM   162  C  C   . ALA   A  1  23  ? 33.270  -16.397 52.557 1.00 34.12  ? 36  ALA   A C   1 
ATOM   163  O  O   . ALA   A  1  23  ? 33.009  -15.552 53.396 1.00 34.65  ? 36  ALA   A O   1 
ATOM   164  C  CB  . ALA   A  1  23  ? 31.832  -18.467 52.644 1.00 37.41  ? 36  ALA   A CB  1 
ATOM   165  N  N   . ASP   A  1  24  ? 34.523  -16.682 52.201 1.00 34.12  ? 37  ASP   A N   1 
ATOM   166  C  CA  . ASP   A  1  24  ? 35.652  -16.019 52.828 1.00 34.18  ? 37  ASP   A CA  1 
ATOM   167  C  C   . ASP   A  1  24  ? 35.868  -14.608 52.259 1.00 32.71  ? 37  ASP   A C   1 
ATOM   168  O  O   . ASP   A  1  24  ? 36.634  -13.849 52.832 1.00 27.55  ? 37  ASP   A O   1 
ATOM   169  C  CB  . ASP   A  1  24  ? 36.916  -16.842 52.656 1.00 36.12  ? 37  ASP   A CB  1 
ATOM   170  C  CG  . ASP   A  1  24  ? 38.030  -16.597 53.676 1.00 46.46  ? 37  ASP   A CG  1 
ATOM   171  O  OD1 . ASP   A  1  24  ? 37.731  -16.663 54.902 1.00 48.46  ? 37  ASP   A OD1 1 
ATOM   172  O  OD2 . ASP   A  1  24  ? 39.201  -16.367 53.244 1.00 48.22  ? 37  ASP   A OD2 1 
ATOM   173  N  N   . HIS   A  1  25  ? 35.217  -14.262 51.131 1.00 31.15  ? 38  HIS   A N   1 
ATOM   174  C  CA  . HIS   A  1  25  ? 35.415  -12.978 50.467 1.00 27.11  ? 38  HIS   A CA  1 
ATOM   175  C  C   . HIS   A  1  25  ? 34.080  -12.264 50.286 1.00 24.43  ? 38  HIS   A C   1 
ATOM   176  O  O   . HIS   A  1  25  ? 33.666  -11.978 49.181 1.00 27.21  ? 38  HIS   A O   1 
ATOM   177  C  CB  . HIS   A  1  25  ? 36.189  -13.194 49.161 1.00 28.93  ? 38  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A  1  25  ? 37.573  -13.707 49.395 1.00 32.24  ? 38  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A  1  25  ? 37.933  -15.023 49.231 1.00 35.04  ? 38  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A  1  25  ? 38.684  -13.079 49.784 1.00 33.86  ? 38  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A  1  25  ? 39.229  -15.170 49.516 1.00 36.66  ? 38  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A  1  25  ? 39.710  -14.002 49.844 1.00 35.38  ? 38  HIS   A NE2 1 
ATOM   183  N  N   . PRO   A  1  26  ? 33.329  -11.984 51.365 1.00 23.11  ? 39  PRO   A N   1 
ATOM   184  C  CA  . PRO   A  1  26  ? 32.025  -11.340 51.248 1.00 25.14  ? 39  PRO   A CA  1 
ATOM   185  C  C   . PRO   A  1  26  ? 32.140  -9.866  50.873 1.00 26.83  ? 39  PRO   A C   1 
ATOM   186  O  O   . PRO   A  1  26  ? 33.042  -9.184  51.322 1.00 27.63  ? 39  PRO   A O   1 
ATOM   187  C  CB  . PRO   A  1  26  ? 31.432  -11.527 52.667 1.00 23.37  ? 39  PRO   A CB  1 
ATOM   188  C  CG  . PRO   A  1  26  ? 32.651  -11.515 53.575 1.00 21.33  ? 39  PRO   A CG  1 
ATOM   189  C  CD  . PRO   A  1  26  ? 33.697  -12.247 52.767 1.00 21.87  ? 39  PRO   A CD  1 
ATOM   190  N  N   . TRP   A  1  27  ? 31.207  -9.378  50.061 1.00 29.20  ? 40  TRP   A N   1 
ATOM   191  C  CA  . TRP   A  1  27  ? 31.077  -7.949  49.873 1.00 27.73  ? 40  TRP   A CA  1 
ATOM   192  C  C   . TRP   A  1  27  ? 30.757  -7.310  51.221 1.00 28.43  ? 40  TRP   A C   1 
ATOM   193  O  O   . TRP   A  1  27  ? 29.978  -7.854  51.988 1.00 30.26  ? 40  TRP   A O   1 
ATOM   194  C  CB  . TRP   A  1  27  ? 30.011  -7.650  48.814 1.00 27.05  ? 40  TRP   A CB  1 
ATOM   195  C  CG  . TRP   A  1  27  ? 29.850  -6.186  48.509 1.00 27.14  ? 40  TRP   A CG  1 
ATOM   196  C  CD1 . TRP   A  1  27  ? 30.514  -5.467  47.565 1.00 30.68  ? 40  TRP   A CD1 1 
ATOM   197  C  CD2 . TRP   A  1  27  ? 29.011  -5.250  49.208 1.00 30.39  ? 40  TRP   A CD2 1 
ATOM   198  N  NE1 . TRP   A  1  27  ? 30.139  -4.152  47.614 1.00 32.19  ? 40  TRP   A NE1 1 
ATOM   199  C  CE2 . TRP   A  1  27  ? 29.227  -3.986  48.622 1.00 31.63  ? 40  TRP   A CE2 1 
ATOM   200  C  CE3 . TRP   A  1  27  ? 28.114  -5.362  50.278 1.00 29.60  ? 40  TRP   A CE3 1 
ATOM   201  C  CZ2 . TRP   A  1  27  ? 28.562  -2.844  49.070 1.00 31.80  ? 40  TRP   A CZ2 1 
ATOM   202  C  CZ3 . TRP   A  1  27  ? 27.466  -4.233  50.723 1.00 32.47  ? 40  TRP   A CZ3 1 
ATOM   203  C  CH2 . TRP   A  1  27  ? 27.703  -2.986  50.138 1.00 34.61  ? 40  TRP   A CH2 1 
ATOM   204  N  N   . GLN   A  1  28  ? 31.407  -6.182  51.515 1.00 29.53  ? 41  GLN   A N   1 
ATOM   205  C  CA  . GLN   A  1  28  ? 31.085  -5.401  52.691 1.00 29.15  ? 41  GLN   A CA  1 
ATOM   206  C  C   . GLN   A  1  28  ? 31.042  -3.934  52.304 1.00 29.36  ? 41  GLN   A C   1 
ATOM   207  O  O   . GLN   A  1  28  ? 31.744  -3.513  51.399 1.00 31.32  ? 41  GLN   A O   1 
ATOM   208  C  CB  . GLN   A  1  28  ? 32.060  -5.645  53.846 1.00 28.07  ? 41  GLN   A CB  1 
ATOM   209  C  CG  . GLN   A  1  28  ? 32.000  -7.062  54.398 1.00 28.30  ? 41  GLN   A CG  1 
ATOM   210  C  CD  . GLN   A  1  28  ? 33.049  -7.334  55.453 1.00 32.38  ? 41  GLN   A CD  1 
ATOM   211  O  OE1 . GLN   A  1  28  ? 33.889  -6.483  55.795 1.00 30.51  ? 41  GLN   A OE1 1 
ATOM   212  N  NE2 . GLN   A  1  28  ? 33.012  -8.551  55.970 1.00 30.39  ? 41  GLN   A NE2 1 
ATOM   213  N  N   . PRO   A  1  29  ? 30.203  -3.124  52.989 1.00 30.30  ? 42  PRO   A N   1 
ATOM   214  C  CA  . PRO   A  1  29  ? 30.140  -1.694  52.725 1.00 29.22  ? 42  PRO   A CA  1 
ATOM   215  C  C   . PRO   A  1  29  ? 31.394  -0.986  53.218 1.00 29.63  ? 42  PRO   A C   1 
ATOM   216  O  O   . PRO   A  1  29  ? 32.133  -1.499  54.049 1.00 30.61  ? 42  PRO   A O   1 
ATOM   217  C  CB  . PRO   A  1  29  ? 28.866  -1.223  53.461 1.00 32.73  ? 42  PRO   A CB  1 
ATOM   218  C  CG  . PRO   A  1  29  ? 28.612  -2.277  54.526 1.00 31.16  ? 42  PRO   A CG  1 
ATOM   219  C  CD  . PRO   A  1  29  ? 29.272  -3.560  54.047 1.00 29.33  ? 42  PRO   A CD  1 
ATOM   220  N  N   . LEU   A  1  30  ? 31.638  0.203   52.658 1.00 33.05  ? 43  LEU   A N   1 
ATOM   221  C  CA  . LEU   A  1  30  ? 32.774  1.021   53.041 1.00 32.49  ? 43  LEU   A CA  1 
ATOM   222  C  C   . LEU   A  1  30  ? 32.649  1.438   54.499 1.00 32.57  ? 43  LEU   A C   1 
ATOM   223  O  O   . LEU   A  1  30  ? 31.558  1.756   54.935 1.00 33.17  ? 43  LEU   A O   1 
ATOM   224  C  CB  . LEU   A  1  30  ? 32.803  2.249   52.141 1.00 33.40  ? 43  LEU   A CB  1 
ATOM   225  C  CG  . LEU   A  1  30  ? 33.012  1.991   50.646 1.00 35.81  ? 43  LEU   A CG  1 
ATOM   226  C  CD1 . LEU   A  1  30  ? 33.189  3.354   49.981 1.00 32.35  ? 43  LEU   A CD1 1 
ATOM   227  C  CD2 . LEU   A  1  30  ? 34.194  1.064   50.341 1.00 34.29  ? 43  LEU   A CD2 1 
ATOM   228  N  N   . ARG   A  1  31  ? 33.774  1.452   55.219 1.00 34.88  ? 44  ARG   A N   1 
ATOM   229  C  CA  . ARG   A  1  31  ? 33.885  2.109   56.511 1.00 40.80  ? 44  ARG   A CA  1 
ATOM   230  C  C   . ARG   A  1  31  ? 34.578  3.459   56.352 1.00 40.49  ? 44  ARG   A C   1 
ATOM   231  O  O   . ARG   A  1  31  ? 35.133  3.740   55.305 1.00 40.11  ? 44  ARG   A O   1 
ATOM   232  C  CB  . ARG   A  1  31  ? 34.755  1.292   57.466 1.00 44.32  ? 44  ARG   A CB  1 
ATOM   233  C  CG  . ARG   A  1  31  ? 34.348  -0.161  57.675 1.00 47.58  ? 44  ARG   A CG  1 
ATOM   234  C  CD  . ARG   A  1  31  ? 35.530  -0.951  58.222 1.00 58.47  ? 44  ARG   A CD  1 
ATOM   235  N  NE  . ARG   A  1  31  ? 36.700  -0.823  57.332 1.00 69.97  ? 44  ARG   A NE  1 
ATOM   236  C  CZ  . ARG   A  1  31  ? 37.819  -1.544  57.353 1.00 74.98  ? 44  ARG   A CZ  1 
ATOM   237  N  NH1 . ARG   A  1  31  ? 37.921  -2.577  58.176 1.00 79.11  ? 44  ARG   A NH1 1 
ATOM   238  N  NH2 . ARG   A  1  31  ? 38.814  -1.247  56.533 1.00 64.77  ? 44  ARG   A NH2 1 
ATOM   239  N  N   . GLU   A  1  32  ? 34.565  4.265   57.414 1.00 47.10  ? 45  GLU   A N   1 
ATOM   240  C  CA  . GLU   A  1  32  ? 35.284  5.529   57.446 1.00 51.35  ? 45  GLU   A CA  1 
ATOM   241  C  C   . GLU   A  1  32  ? 36.753  5.269   57.118 1.00 43.11  ? 45  GLU   A C   1 
ATOM   242  O  O   . GLU   A  1  32  ? 37.374  4.383   57.698 1.00 39.23  ? 45  GLU   A O   1 
ATOM   243  C  CB  . GLU   A  1  32  ? 35.057  6.180   58.814 1.00 65.79  ? 45  GLU   A CB  1 
ATOM   244  C  CG  . GLU   A  1  32  ? 35.750  7.528   59.031 1.00 80.31  ? 45  GLU   A CG  1 
ATOM   245  C  CD  . GLU   A  1  32  ? 37.045  7.507   59.845 1.00 101.13 ? 45  GLU   A CD  1 
ATOM   246  O  OE1 . GLU   A  1  32  ? 37.990  8.272   59.507 1.00 101.99 ? 45  GLU   A OE1 1 
ATOM   247  O  OE2 . GLU   A  1  32  ? 37.123  6.724   60.826 1.00 107.72 ? 45  GLU   A OE2 1 
ATOM   248  N  N   . GLY   A  1  33  ? 37.293  6.046   56.170 1.00 41.04  ? 46  GLY   A N   1 
ATOM   249  C  CA  . GLY   A  1  33  ? 38.696  5.961   55.784 1.00 41.12  ? 46  GLY   A CA  1 
ATOM   250  C  C   . GLY   A  1  33  ? 38.978  4.984   54.633 1.00 41.57  ? 46  GLY   A C   1 
ATOM   251  O  O   . GLY   A  1  33  ? 40.094  4.956   54.124 1.00 40.59  ? 46  GLY   A O   1 
ATOM   252  N  N   . ASP   A  1  34  ? 37.991  4.166   54.233 1.00 40.56  ? 47  ASP   A N   1 
ATOM   253  C  CA  . ASP   A  1  34  ? 38.204  3.205   53.157 1.00 40.16  ? 47  ASP   A CA  1 
ATOM   254  C  C   . ASP   A  1  34  ? 38.353  3.960   51.853 1.00 33.60  ? 47  ASP   A C   1 
ATOM   255  O  O   . ASP   A  1  34  ? 37.673  4.939   51.635 1.00 37.14  ? 47  ASP   A O   1 
ATOM   256  C  CB  . ASP   A  1  34  ? 37.123  2.138   53.091 1.00 42.12  ? 47  ASP   A CB  1 
ATOM   257  C  CG  . ASP   A  1  34  ? 37.181  1.076   54.189 1.00 43.81  ? 47  ASP   A CG  1 
ATOM   258  O  OD1 . ASP   A  1  34  ? 38.197  1.052   54.955 1.00 42.87  ? 47  ASP   A OD1 1 
ATOM   259  O  OD2 . ASP   A  1  34  ? 36.215  0.271   54.272 1.00 38.64  ? 47  ASP   A OD2 1 
ATOM   260  N  N   . ILE   A  1  35  ? 39.286  3.519   51.016 1.00 33.19  ? 48  ILE   A N   1 
ATOM   261  C  CA  . ILE   A  1  35  ? 39.606  4.226   49.791 1.00 28.83  ? 48  ILE   A CA  1 
ATOM   262  C  C   . ILE   A  1  35  ? 39.129  3.409   48.600 1.00 27.59  ? 48  ILE   A C   1 
ATOM   263  O  O   . ILE   A  1  35  ? 39.377  2.212   48.536 1.00 23.88  ? 48  ILE   A O   1 
ATOM   264  C  CB  . ILE   A  1  35  ? 41.117  4.501   49.703 1.00 29.01  ? 48  ILE   A CB  1 
ATOM   265  C  CG1 . ILE   A  1  35  ? 41.639  5.383   50.838 1.00 30.63  ? 48  ILE   A CG1 1 
ATOM   266  C  CG2 . ILE   A  1  35  ? 41.453  5.080   48.342 1.00 29.45  ? 48  ILE   A CG2 1 
ATOM   267  C  CD1 . ILE   A  1  35  ? 40.994  6.769   50.918 1.00 32.87  ? 48  ILE   A CD1 1 
ATOM   268  N  N   . ARG   A  1  36  ? 38.481  4.088   47.641 1.00 29.39  ? 49  ARG   A N   1 
ATOM   269  C  CA  . ARG   A  1  36  ? 38.157  3.497   46.354 1.00 25.65  ? 49  ARG   A CA  1 
ATOM   270  C  C   . ARG   A  1  36  ? 38.496  4.521   45.290 1.00 24.90  ? 49  ARG   A C   1 
ATOM   271  O  O   . ARG   A  1  36  ? 38.685  5.683   45.605 1.00 26.59  ? 49  ARG   A O   1 
ATOM   272  C  CB  . ARG   A  1  36  ? 36.682  3.103   46.337 1.00 25.55  ? 49  ARG   A CB  1 
ATOM   273  C  CG  . ARG   A  1  36  ? 36.298  2.028   47.352 1.00 25.74  ? 49  ARG   A CG  1 
ATOM   274  C  CD  . ARG   A  1  36  ? 36.930  0.677   47.020 1.00 24.04  ? 49  ARG   A CD  1 
ATOM   275  N  NE  . ARG   A  1  36  ? 36.469  -0.331  47.981 1.00 24.01  ? 49  ARG   A NE  1 
ATOM   276  C  CZ  . ARG   A  1  36  ? 36.994  -0.566  49.182 1.00 25.17  ? 49  ARG   A CZ  1 
ATOM   277  N  NH1 . ARG   A  1  36  ? 38.023  0.122   49.627 1.00 27.03  ? 49  ARG   A NH1 1 
ATOM   278  N  NH2 . ARG   A  1  36  ? 36.489  -1.511  49.950 1.00 25.55  ? 49  ARG   A NH2 1 
ATOM   279  N  N   . GLY   A  1  37  ? 38.595  4.086   44.037 1.00 27.05  ? 50  GLY   A N   1 
ATOM   280  C  CA  . GLY   A  1  37  ? 39.165  4.914   42.999 1.00 24.18  ? 50  GLY   A CA  1 
ATOM   281  C  C   . GLY   A  1  37  ? 38.619  4.596   41.621 1.00 23.99  ? 50  GLY   A C   1 
ATOM   282  O  O   . GLY   A  1  37  ? 37.520  4.079   41.472 1.00 26.93  ? 50  GLY   A O   1 
ATOM   283  N  N   . PRO   A  1  38  ? 39.395  4.886   40.560 1.00 23.53  ? 51  PRO   A N   1 
ATOM   284  C  CA  . PRO   A  1  38  ? 38.903  4.749   39.199 1.00 23.38  ? 51  PRO   A CA  1 
ATOM   285  C  C   . PRO   A  1  38  ? 38.897  3.339   38.614 1.00 25.99  ? 51  PRO   A C   1 
ATOM   286  O  O   . PRO   A  1  38  ? 38.372  3.159   37.511 1.00 29.10  ? 51  PRO   A O   1 
ATOM   287  C  CB  . PRO   A  1  38  ? 39.901  5.628   38.482 1.00 23.02  ? 51  PRO   A CB  1 
ATOM   288  C  CG  . PRO   A  1  38  ? 41.202  5.328   39.168 1.00 23.63  ? 51  PRO   A CG  1 
ATOM   289  C  CD  . PRO   A  1  38  ? 40.818  5.261   40.617 1.00 23.26  ? 51  PRO   A CD  1 
ATOM   290  N  N   . CYS   A  1  39  ? 39.519  2.370   39.308 1.00 26.01  ? 52  CYS   A N   1 
ATOM   291  C  CA  . CYS   A  1  39  ? 39.579  1.004   38.796 1.00 26.21  ? 52  CYS   A CA  1 
ATOM   292  C  C   . CYS   A  1  39  ? 38.497  0.117   39.408 1.00 23.62  ? 52  CYS   A C   1 
ATOM   293  O  O   . CYS   A  1  39  ? 38.515  -0.162  40.603 1.00 25.46  ? 52  CYS   A O   1 
ATOM   294  C  CB  . CYS   A  1  39  ? 40.916  0.337   39.063 1.00 27.47  ? 52  CYS   A CB  1 
ATOM   295  S  SG  . CYS   A  1  39  ? 40.991  -1.315  38.326 1.00 27.11  ? 52  CYS   A SG  1 
ATOM   296  N  N   . PRO   A  1  40  ? 37.533  -0.366  38.603 1.00 24.56  ? 53  PRO   A N   1 
ATOM   297  C  CA  . PRO   A  1  40  ? 36.475  -1.250  39.106 1.00 25.28  ? 53  PRO   A CA  1 
ATOM   298  C  C   . PRO   A  1  40  ? 36.979  -2.619  39.542 1.00 25.13  ? 53  PRO   A C   1 
ATOM   299  O  O   . PRO   A  1  40  ? 36.438  -3.215  40.464 1.00 27.04  ? 53  PRO   A O   1 
ATOM   300  C  CB  . PRO   A  1  40  ? 35.481  -1.351  37.957 1.00 25.56  ? 53  PRO   A CB  1 
ATOM   301  C  CG  . PRO   A  1  40  ? 36.323  -1.041  36.712 1.00 27.01  ? 53  PRO   A CG  1 
ATOM   302  C  CD  . PRO   A  1  40  ? 37.416  -0.088  37.164 1.00 24.00  ? 53  PRO   A CD  1 
ATOM   303  N  N   . GLY   A  1  41  ? 38.054  -3.090  38.910 1.00 26.87  ? 54  GLY   A N   1 
ATOM   304  C  CA  . GLY   A  1  41  ? 38.698  -4.336  39.302 1.00 23.94  ? 54  GLY   A CA  1 
ATOM   305  C  C   . GLY   A  1  41  ? 39.217  -4.281  40.734 1.00 22.96  ? 54  GLY   A C   1 
ATOM   306  O  O   . GLY   A  1  41  ? 38.815  -5.077  41.580 1.00 25.45  ? 54  GLY   A O   1 
ATOM   307  N  N   . LEU   A  1  42  ? 40.093  -3.316  41.002 1.00 22.99  ? 55  LEU   A N   1 
ATOM   308  C  CA  . LEU   A  1  42  ? 40.706  -3.178  42.311 1.00 23.44  ? 55  LEU   A CA  1 
ATOM   309  C  C   . LEU   A  1  42  ? 39.633  -2.835  43.335 1.00 22.67  ? 55  LEU   A C   1 
ATOM   310  O  O   . LEU   A  1  42  ? 39.691  -3.337  44.450 1.00 21.75  ? 55  LEU   A O   1 
ATOM   311  C  CB  . LEU   A  1  42  ? 41.806  -2.123  42.285 1.00 23.04  ? 55  LEU   A CB  1 
ATOM   312  C  CG  . LEU   A  1  42  ? 42.985  -2.424  41.365 1.00 24.38  ? 55  LEU   A CG  1 
ATOM   313  C  CD1 . LEU   A  1  42  ? 43.975  -1.269  41.338 1.00 24.48  ? 55  LEU   A CD1 1 
ATOM   314  C  CD2 . LEU   A  1  42  ? 43.677  -3.680  41.820 1.00 25.90  ? 55  LEU   A CD2 1 
ATOM   315  N  N   . ASN   A  1  43  ? 38.661  -1.997  42.944 1.00 23.00  ? 56  ASN   A N   1 
ATOM   316  C  CA  . ASN   A  1  43  ? 37.581  -1.616  43.837 1.00 24.45  ? 56  ASN   A CA  1 
ATOM   317  C  C   . ASN   A  1  43  ? 36.819  -2.852  44.316 1.00 25.05  ? 56  ASN   A C   1 
ATOM   318  O  O   . ASN   A  1  43  ? 36.535  -2.992  45.509 1.00 24.92  ? 56  ASN   A O   1 
ATOM   319  C  CB  . ASN   A  1  43  ? 36.617  -0.650  43.173 1.00 24.04  ? 56  ASN   A CB  1 
ATOM   320  C  CG  . ASN   A  1  43  ? 37.163  0.756   43.055 1.00 26.54  ? 56  ASN   A CG  1 
ATOM   321  O  OD1 . ASN   A  1  43  ? 38.138  1.149   43.716 1.00 27.98  ? 56  ASN   A OD1 1 
ATOM   322  N  ND2 . ASN   A  1  43  ? 36.518  1.536   42.206 1.00 28.00  ? 56  ASN   A ND2 1 
ATOM   323  N  N   . THR   A  1  44  ? 36.513  -3.749  43.384 1.00 23.97  ? 57  THR   A N   1 
ATOM   324  C  CA  . THR   A  1  44  ? 35.753  -4.940  43.707 1.00 25.38  ? 57  THR   A CA  1 
ATOM   325  C  C   . THR   A  1  44  ? 36.585  -5.862  44.603 1.00 24.26  ? 57  THR   A C   1 
ATOM   326  O  O   . THR   A  1  44  ? 36.060  -6.398  45.567 1.00 21.03  ? 57  THR   A O   1 
ATOM   327  C  CB  . THR   A  1  44  ? 35.295  -5.628  42.423 1.00 24.64  ? 57  THR   A CB  1 
ATOM   328  O  OG1 . THR   A  1  44  ? 34.436  -4.715  41.747 1.00 26.51  ? 57  THR   A OG1 1 
ATOM   329  C  CG2 . THR   A  1  44  ? 34.473  -6.866  42.690 1.00 24.97  ? 57  THR   A CG2 1 
ATOM   330  N  N   . LEU   A  1  45  ? 37.879  -6.016  44.307 1.00 25.06  ? 58  LEU   A N   1 
ATOM   331  C  CA  . LEU   A  1  45  ? 38.750  -6.855  45.113 1.00 22.51  ? 58  LEU   A CA  1 
ATOM   332  C  C   . LEU   A  1  45  ? 38.859  -6.293  46.531 1.00 24.19  ? 58  LEU   A C   1 
ATOM   333  O  O   . LEU   A  1  45  ? 38.904  -7.042  47.491 1.00 26.38  ? 58  LEU   A O   1 
ATOM   334  C  CB  . LEU   A  1  45  ? 40.117  -6.927  44.448 1.00 23.86  ? 58  LEU   A CB  1 
ATOM   335  C  CG  . LEU   A  1  45  ? 40.187  -7.625  43.093 1.00 24.09  ? 58  LEU   A CG  1 
ATOM   336  C  CD1 . LEU   A  1  45  ? 41.503  -7.343  42.358 1.00 23.02  ? 58  LEU   A CD1 1 
ATOM   337  C  CD2 . LEU   A  1  45  ? 40.029  -9.116  43.305 1.00 24.37  ? 58  LEU   A CD2 1 
ATOM   338  N  N   . ALA   A  1  46  ? 38.892  -4.973  46.681 1.00 25.47  ? 59  ALA   A N   1 
ATOM   339  C  CA  . ALA   A  1  46  ? 38.936  -4.394  48.013 1.00 25.64  ? 59  ALA   A CA  1 
ATOM   340  C  C   . ALA   A  1  46  ? 37.606  -4.613  48.735 1.00 23.22  ? 59  ALA   A C   1 
ATOM   341  O  O   . ALA   A  1  46  ? 37.587  -4.950  49.916 1.00 26.48  ? 59  ALA   A O   1 
ATOM   342  C  CB  . ALA   A  1  46  ? 39.292  -2.928  47.947 1.00 25.82  ? 59  ALA   A CB  1 
ATOM   343  N  N   . SER   A  1  47  ? 36.485  -4.454  48.036 1.00 23.61  ? 60  SER   A N   1 
ATOM   344  C  CA  . SER   A  1  47  ? 35.194  -4.551  48.709 1.00 26.63  ? 60  SER   A CA  1 
ATOM   345  C  C   . SER   A  1  47  ? 34.803  -6.004  49.012 1.00 28.33  ? 60  SER   A C   1 
ATOM   346  O  O   . SER   A  1  47  ? 33.875  -6.220  49.778 1.00 29.56  ? 60  SER   A O   1 
ATOM   347  C  CB  . SER   A  1  47  ? 34.123  -3.819  47.952 1.00 26.13  ? 60  SER   A CB  1 
ATOM   348  O  OG  . SER   A  1  47  ? 34.246  -2.416  48.167 1.00 26.61  ? 60  SER   A OG  1 
ATOM   349  N  N   . HIS   A  1  48  ? 35.530  -6.981  48.462 1.00 26.25  ? 61  HIS   A N   1 
ATOM   350  C  CA  . HIS   A  1  48  ? 35.375  -8.381  48.831 1.00 26.86  ? 61  HIS   A CA  1 
ATOM   351  C  C   . HIS   A  1  48  ? 36.543  -8.925  49.651 1.00 28.05  ? 61  HIS   A C   1 
ATOM   352  O  O   . HIS   A  1  48  ? 36.585  -10.121 49.906 1.00 26.22  ? 61  HIS   A O   1 
ATOM   353  C  CB  . HIS   A  1  48  ? 35.271  -9.281  47.593 1.00 23.99  ? 61  HIS   A CB  1 
ATOM   354  C  CG  . HIS   A  1  48  ? 33.928  -9.185  46.948 1.00 25.24  ? 61  HIS   A CG  1 
ATOM   355  N  ND1 . HIS   A  1  48  ? 32.935  -10.097 47.193 1.00 24.01  ? 61  HIS   A ND1 1 
ATOM   356  C  CD2 . HIS   A  1  48  ? 33.399  -8.309  46.095 1.00 27.47  ? 61  HIS   A CD2 1 
ATOM   357  C  CE1 . HIS   A  1  48  ? 31.869  -9.796  46.483 1.00 26.26  ? 61  HIS   A CE1 1 
ATOM   358  N  NE2 . HIS   A  1  48  ? 32.111  -8.694  45.832 1.00 27.43  ? 61  HIS   A NE2 1 
ATOM   359  N  N   . GLY   A  1  49  ? 37.498  -8.084  50.042 1.00 23.96  ? 62  GLY   A N   1 
ATOM   360  C  CA  . GLY   A  1  49  ? 38.559  -8.543  50.925 1.00 23.53  ? 62  GLY   A CA  1 
ATOM   361  C  C   . GLY   A  1  49  ? 39.665  -9.346  50.234 1.00 24.31  ? 62  GLY   A C   1 
ATOM   362  O  O   . GLY   A  1  49  ? 40.471  -9.962  50.902 1.00 24.53  ? 62  GLY   A O   1 
ATOM   363  N  N   . TYR   A  1  50  ? 39.747  -9.341  48.905 1.00 26.40  ? 63  TYR   A N   1 
ATOM   364  C  CA  . TYR   A  1  50  ? 40.924  -9.866  48.232 1.00 26.32  ? 63  TYR   A CA  1 
ATOM   365  C  C   . TYR   A  1  50  ? 42.120  -8.933  48.425 1.00 28.96  ? 63  TYR   A C   1 
ATOM   366  O  O   . TYR   A  1  50  ? 43.249  -9.398  48.457 1.00 31.55  ? 63  TYR   A O   1 
ATOM   367  C  CB  . TYR   A  1  50  ? 40.689  -10.063 46.734 1.00 27.08  ? 63  TYR   A CB  1 
ATOM   368  C  CG  . TYR   A  1  50  ? 39.960  -11.364 46.453 1.00 29.65  ? 63  TYR   A CG  1 
ATOM   369  C  CD1 . TYR   A  1  50  ? 40.643  -12.582 46.438 1.00 29.15  ? 63  TYR   A CD1 1 
ATOM   370  C  CD2 . TYR   A  1  50  ? 38.580  -11.375 46.270 1.00 29.64  ? 63  TYR   A CD2 1 
ATOM   371  C  CE1 . TYR   A  1  50  ? 39.971  -13.770 46.226 1.00 29.49  ? 63  TYR   A CE1 1 
ATOM   372  C  CE2 . TYR   A  1  50  ? 37.903  -12.553 46.040 1.00 28.41  ? 63  TYR   A CE2 1 
ATOM   373  C  CZ  . TYR   A  1  50  ? 38.600  -13.745 46.011 1.00 30.61  ? 63  TYR   A CZ  1 
ATOM   374  O  OH  . TYR   A  1  50  ? 37.902  -14.886 45.809 1.00 29.78  ? 63  TYR   A OH  1 
ATOM   375  N  N   . LEU   A  1  51  ? 41.862  -7.620  48.446 1.00 28.81  ? 64  LEU   A N   1 
ATOM   376  C  CA  . LEU   A  1  51  ? 42.815  -6.619  48.898 1.00 30.03  ? 64  LEU   A CA  1 
ATOM   377  C  C   . LEU   A  1  51  ? 42.377  -6.184  50.289 1.00 31.36  ? 64  LEU   A C   1 
ATOM   378  O  O   . LEU   A  1  51  ? 41.201  -6.351  50.633 1.00 32.89  ? 64  LEU   A O   1 
ATOM   379  C  CB  . LEU   A  1  51  ? 42.801  -5.403  47.973 1.00 30.53  ? 64  LEU   A CB  1 
ATOM   380  C  CG  . LEU   A  1  51  ? 43.332  -5.626  46.559 1.00 32.65  ? 64  LEU   A CG  1 
ATOM   381  C  CD1 . LEU   A  1  51  ? 42.975  -4.438  45.708 1.00 34.21  ? 64  LEU   A CD1 1 
ATOM   382  C  CD2 . LEU   A  1  51  ? 44.822  -5.854  46.602 1.00 33.61  ? 64  LEU   A CD2 1 
ATOM   383  N  N   . PRO   A  1  52  ? 43.260  -5.528  51.067 1.00 28.58  ? 65  PRO   A N   1 
ATOM   384  C  CA  . PRO   A  1  52  ? 42.821  -4.811  52.263 1.00 32.57  ? 65  PRO   A CA  1 
ATOM   385  C  C   . PRO   A  1  52  ? 41.601  -3.932  51.965 1.00 30.38  ? 65  PRO   A C   1 
ATOM   386  O  O   . PRO   A  1  52  ? 41.574  -3.239  50.950 1.00 32.53  ? 65  PRO   A O   1 
ATOM   387  C  CB  . PRO   A  1  52  ? 44.069  -4.008  52.650 1.00 33.02  ? 65  PRO   A CB  1 
ATOM   388  C  CG  . PRO   A  1  52  ? 45.235  -4.807  52.088 1.00 31.21  ? 65  PRO   A CG  1 
ATOM   389  C  CD  . PRO   A  1  52  ? 44.697  -5.373  50.795 1.00 29.83  ? 65  PRO   A CD  1 
ATOM   390  N  N   . ARG   A  1  53  ? 40.580  -3.998  52.826 1.00 27.08  ? 66  ARG   A N   1 
ATOM   391  C  CA  . ARG   A  1  53  ? 39.307  -3.350  52.571 1.00 29.73  ? 66  ARG   A CA  1 
ATOM   392  C  C   . ARG   A  1  53  ? 39.412  -1.828  52.602 1.00 29.18  ? 66  ARG   A C   1 
ATOM   393  O  O   . ARG   A  1  53  ? 38.523  -1.119  52.124 1.00 29.83  ? 66  ARG   A O   1 
ATOM   394  C  CB  . ARG   A  1  53  ? 38.270  -3.858  53.575 1.00 31.69  ? 66  ARG   A CB  1 
ATOM   395  C  CG  . ARG   A  1  53  ? 37.861  -5.285  53.247 1.00 32.11  ? 66  ARG   A CG  1 
ATOM   396  C  CD  . ARG   A  1  53  ? 36.761  -5.792  54.152 1.00 33.93  ? 66  ARG   A CD  1 
ATOM   397  N  NE  . ARG   A  1  53  ? 36.529  -7.214  53.903 1.00 33.74  ? 66  ARG   A NE  1 
ATOM   398  C  CZ  . ARG   A  1  53  ? 35.622  -7.686  53.053 1.00 33.14  ? 66  ARG   A CZ  1 
ATOM   399  N  NH1 . ARG   A  1  53  ? 34.928  -6.863  52.293 1.00 28.07  ? 66  ARG   A NH1 1 
ATOM   400  N  NH2 . ARG   A  1  53  ? 35.422  -8.987  52.961 1.00 36.56  ? 66  ARG   A NH2 1 
ATOM   401  N  N   . ASP   A  1  54  ? 40.511  -1.328  53.152 1.00 30.41  ? 67  ASP   A N   1 
ATOM   402  C  CA  . ASP   A  1  54  ? 40.746  0.104   53.213 1.00 31.85  ? 67  ASP   A CA  1 
ATOM   403  C  C   . ASP   A  1  54  ? 41.315  0.630   51.909 1.00 28.55  ? 67  ASP   A C   1 
ATOM   404  O  O   . ASP   A  1  54  ? 41.411  1.836   51.755 1.00 29.70  ? 67  ASP   A O   1 
ATOM   405  C  CB  . ASP   A  1  54  ? 41.586  0.498   54.414 1.00 34.20  ? 67  ASP   A CB  1 
ATOM   406  C  CG  . ASP   A  1  54  ? 43.038  0.054   54.416 1.00 40.95  ? 67  ASP   A CG  1 
ATOM   407  O  OD1 . ASP   A  1  54  ? 43.483  -0.553  53.407 1.00 39.40  ? 67  ASP   A OD1 1 
ATOM   408  O  OD2 . ASP   A  1  54  ? 43.716  0.340   55.441 1.00 48.51  ? 67  ASP   A OD2 1 
ATOM   409  N  N   . GLY   A  1  55  ? 41.654  -0.243  50.963 1.00 27.91  ? 68  GLY   A N   1 
ATOM   410  C  CA  . GLY   A  1  55  ? 41.975  0.210   49.616 1.00 28.63  ? 68  GLY   A CA  1 
ATOM   411  C  C   . GLY   A  1  55  ? 43.427  0.663   49.480 1.00 26.83  ? 68  GLY   A C   1 
ATOM   412  O  O   . GLY   A  1  55  ? 43.789  1.311   48.506 1.00 24.43  ? 68  GLY   A O   1 
ATOM   413  N  N   . VAL   A  1  56  ? 44.256  0.295   50.453 1.00 27.60  ? 69  VAL   A N   1 
ATOM   414  C  CA  . VAL   A  1  56  ? 45.678  0.567   50.411 1.00 32.82  ? 69  VAL   A CA  1 
ATOM   415  C  C   . VAL   A  1  56  ? 46.396  -0.772  50.523 1.00 29.38  ? 69  VAL   A C   1 
ATOM   416  O  O   . VAL   A  1  56  ? 46.164  -1.518  51.466 1.00 31.63  ? 69  VAL   A O   1 
ATOM   417  C  CB  . VAL   A  1  56  ? 46.058  1.527   51.561 1.00 38.48  ? 69  VAL   A CB  1 
ATOM   418  C  CG1 . VAL   A  1  56  ? 47.565  1.659   51.718 1.00 39.18  ? 69  VAL   A CG1 1 
ATOM   419  C  CG2 . VAL   A  1  56  ? 45.419  2.903   51.382 1.00 39.57  ? 69  VAL   A CG2 1 
ATOM   420  N  N   . ALA   A  1  57  ? 47.287  -1.044  49.579 1.00 27.27  ? 70  ALA   A N   1 
ATOM   421  C  CA  . ALA   A  1  57  ? 47.939  -2.335  49.506 1.00 27.91  ? 70  ALA   A CA  1 
ATOM   422  C  C   . ALA   A  1  57  ? 49.375  -2.246  48.989 1.00 29.86  ? 70  ALA   A C   1 
ATOM   423  O  O   . ALA   A  1  57  ? 49.764  -1.257  48.383 1.00 30.98  ? 70  ALA   A O   1 
ATOM   424  C  CB  . ALA   A  1  57  ? 47.117  -3.178  48.598 1.00 30.88  ? 70  ALA   A CB  1 
ATOM   425  N  N   . THR   A  1  58  ? 50.139  -3.328  49.197 1.00 26.77  ? 71  THR   A N   1 
ATOM   426  C  CA  . THR   A  1  58  ? 51.463  -3.470  48.627 1.00 25.78  ? 71  THR   A CA  1 
ATOM   427  C  C   . THR   A  1  58  ? 51.302  -3.881  47.178 1.00 25.90  ? 71  THR   A C   1 
ATOM   428  O  O   . THR   A  1  58  ? 50.285  -4.449  46.827 1.00 25.84  ? 71  THR   A O   1 
ATOM   429  C  CB  . THR   A  1  58  ? 52.336  -4.486  49.370 1.00 27.71  ? 71  THR   A CB  1 
ATOM   430  O  OG1 . THR   A  1  58  ? 51.754  -5.761  49.120 1.00 31.52  ? 71  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A  1  58  ? 52.419  -4.238  50.866 1.00 26.73  ? 71  THR   A CG2 1 
ATOM   432  N  N   . PRO   A  1  59  ? 52.293  -3.605  46.309 1.00 27.56  ? 72  PRO   A N   1 
ATOM   433  C  CA  . PRO   A  1  59  ? 52.313  -4.143  44.954 1.00 31.51  ? 72  PRO   A CA  1 
ATOM   434  C  C   . PRO   A  1  59  ? 52.081  -5.651  44.924 1.00 31.22  ? 72  PRO   A C   1 
ATOM   435  O  O   . PRO   A  1  59  ? 51.334  -6.144  44.094 1.00 29.55  ? 72  PRO   A O   1 
ATOM   436  C  CB  . PRO   A  1  59  ? 53.717  -3.767  44.435 1.00 30.58  ? 72  PRO   A CB  1 
ATOM   437  C  CG  . PRO   A  1  59  ? 53.993  -2.465  45.154 1.00 31.93  ? 72  PRO   A CG  1 
ATOM   438  C  CD  . PRO   A  1  59  ? 53.414  -2.687  46.546 1.00 31.36  ? 72  PRO   A CD  1 
ATOM   439  N  N   . ALA   A  1  60  ? 52.765  -6.369  45.813 1.00 32.69  ? 73  ALA   A N   1 
ATOM   440  C  CA  . ALA   A  1  60  ? 52.640  -7.816  45.863 1.00 32.00  ? 73  ALA   A CA  1 
ATOM   441  C  C   . ALA   A  1  60  ? 51.198  -8.207  46.159 1.00 29.45  ? 73  ALA   A C   1 
ATOM   442  O  O   . ALA   A  1  60  ? 50.683  -9.096  45.516 1.00 26.70  ? 73  ALA   A O   1 
ATOM   443  C  CB  . ALA   A  1  60  ? 53.563  -8.409  46.892 1.00 32.02  ? 73  ALA   A CB  1 
ATOM   444  N  N   . GLN   A  1  61  ? 50.536  -7.522  47.094 1.00 26.95  ? 74  GLN   A N   1 
ATOM   445  C  CA  . GLN   A  1  61  ? 49.164  -7.865  47.411 1.00 26.06  ? 74  GLN   A CA  1 
ATOM   446  C  C   . GLN   A  1  61  ? 48.257  -7.594  46.220 1.00 27.18  ? 74  GLN   A C   1 
ATOM   447  O  O   . GLN   A  1  61  ? 47.326  -8.353  45.986 1.00 31.80  ? 74  GLN   A O   1 
ATOM   448  C  CB  . GLN   A  1  61  ? 48.599  -7.107  48.600 1.00 26.95  ? 74  GLN   A CB  1 
ATOM   449  C  CG  . GLN   A  1  61  ? 49.211  -7.507  49.924 1.00 29.47  ? 74  GLN   A CG  1 
ATOM   450  C  CD  . GLN   A  1  61  ? 48.832  -6.543  51.024 1.00 34.68  ? 74  GLN   A CD  1 
ATOM   451  O  OE1 . GLN   A  1  61  ? 48.827  -5.321  50.845 1.00 37.43  ? 74  GLN   A OE1 1 
ATOM   452  N  NE2 . GLN   A  1  61  ? 48.503  -7.090  52.182 1.00 34.63  ? 74  GLN   A NE2 1 
ATOM   453  N  N   . ILE   A  1  62  ? 48.514  -6.517  45.481 1.00 28.84  ? 75  ILE   A N   1 
ATOM   454  C  CA  . ILE   A  1  62  ? 47.697  -6.169  44.329 1.00 31.05  ? 75  ILE   A CA  1 
ATOM   455  C  C   . ILE   A  1  62  ? 47.846  -7.248  43.264 1.00 30.19  ? 75  ILE   A C   1 
ATOM   456  O  O   . ILE   A  1  62  ? 46.861  -7.708  42.683 1.00 29.15  ? 75  ILE   A O   1 
ATOM   457  C  CB  . ILE   A  1  62  ? 48.047  -4.755  43.812 1.00 30.23  ? 75  ILE   A CB  1 
ATOM   458  C  CG1 . ILE   A  1  62  ? 47.555  -3.713  44.821 1.00 34.31  ? 75  ILE   A CG1 1 
ATOM   459  C  CG2 . ILE   A  1  62  ? 47.473  -4.502  42.420 1.00 27.05  ? 75  ILE   A CG2 1 
ATOM   460  C  CD1 . ILE   A  1  62  ? 48.024  -2.289  44.558 1.00 37.62  ? 75  ILE   A CD1 1 
ATOM   461  N  N   . ILE   A  1  63  ? 49.083  -7.677  43.028 1.00 30.56  ? 76  ILE   A N   1 
ATOM   462  C  CA  . ILE   A  1  63  ? 49.324  -8.674  41.998 1.00 30.48  ? 76  ILE   A CA  1 
ATOM   463  C  C   . ILE   A  1  63  ? 48.606  -9.966  42.366 1.00 27.33  ? 76  ILE   A C   1 
ATOM   464  O  O   . ILE   A  1  63  ? 47.885  -10.510 41.545 1.00 28.96  ? 76  ILE   A O   1 
ATOM   465  C  CB  . ILE   A  1  63  ? 50.823  -8.867  41.748 1.00 30.62  ? 76  ILE   A CB  1 
ATOM   466  C  CG1 . ILE   A  1  63  ? 51.382  -7.617  41.073 1.00 32.02  ? 76  ILE   A CG1 1 
ATOM   467  C  CG2 . ILE   A  1  63  ? 51.097  -10.121 40.917 1.00 29.89  ? 76  ILE   A CG2 1 
ATOM   468  C  CD1 . ILE   A  1  63  ? 52.861  -7.417  41.294 1.00 35.63  ? 76  ILE   A CD1 1 
ATOM   469  N  N   . THR   A  1  64  ? 48.764  -10.436 43.596 1.00 27.85  ? 77  THR   A N   1 
ATOM   470  C  CA  A THR   A  1  64  ? 48.182  -11.707 43.985 0.50 29.76  ? 77  THR   A CA  1 
ATOM   471  C  CA  B THR   A  1  64  ? 48.182  -11.706 43.997 0.50 29.07  ? 77  THR   A CA  1 
ATOM   472  C  C   . THR   A  1  64  ? 46.658  -11.602 43.937 1.00 29.20  ? 77  THR   A C   1 
ATOM   473  O  O   . THR   A  1  64  ? 46.010  -12.533 43.499 1.00 29.74  ? 77  THR   A O   1 
ATOM   474  C  CB  A THR   A  1  64  ? 48.682  -12.157 45.356 0.50 30.07  ? 77  THR   A CB  1 
ATOM   475  C  CB  B THR   A  1  64  ? 48.712  -12.200 45.352 0.50 29.71  ? 77  THR   A CB  1 
ATOM   476  O  OG1 A THR   A  1  64  ? 48.163  -11.160 46.229 0.50 45.87  ? 77  THR   A OG1 1 
ATOM   477  O  OG1 B THR   A  1  64  ? 47.780  -13.095 45.965 0.50 25.69  ? 77  THR   A OG1 1 
ATOM   478  C  CG2 A THR   A  1  64  ? 50.190  -12.283 45.425 0.50 25.07  ? 77  THR   A CG2 1 
ATOM   479  C  CG2 B THR   A  1  64  ? 48.916  -11.133 46.407 0.50 34.98  ? 77  THR   A CG2 1 
ATOM   480  N  N   . ALA   A  1  65  ? 46.093  -10.447 44.327 1.00 28.36  ? 78  ALA   A N   1 
ATOM   481  C  CA  . ALA   A  1  65  ? 44.647  -10.238 44.316 1.00 24.58  ? 78  ALA   A CA  1 
ATOM   482  C  C   . ALA   A  1  65  ? 44.072  -10.227 42.905 1.00 25.01  ? 78  ALA   A C   1 
ATOM   483  O  O   . ALA   A  1  65  ? 42.998  -10.792 42.684 1.00 27.16  ? 78  ALA   A O   1 
ATOM   484  C  CB  . ALA   A  1  65  ? 44.272  -8.968  45.030 1.00 26.35  ? 78  ALA   A CB  1 
ATOM   485  N  N   . THR   A  1  66  ? 44.737  -9.570  41.950 1.00 23.86  ? 79  THR   A N   1 
ATOM   486  C  CA  . THR   A  1  66  ? 44.219  -9.537  40.587 1.00 24.16  ? 79  THR   A CA  1 
ATOM   487  C  C   . THR   A  1  66  ? 44.271  -10.934 39.976 1.00 24.83  ? 79  THR   A C   1 
ATOM   488  O  O   . THR   A  1  66  ? 43.428  -11.288 39.160 1.00 23.59  ? 79  THR   A O   1 
ATOM   489  C  CB  . THR   A  1  66  ? 44.958  -8.525  39.707 1.00 27.03  ? 79  THR   A CB  1 
ATOM   490  O  OG1 . THR   A  1  66  ? 46.341  -8.872  39.675 1.00 30.19  ? 79  THR   A OG1 1 
ATOM   491  C  CG2 . THR   A  1  66  ? 44.777  -7.099  40.205 1.00 29.49  ? 79  THR   A CG2 1 
ATOM   492  N  N   . GLN   A  1  67  ? 45.269  -11.728 40.362 1.00 28.89  ? 80  GLN   A N   1 
ATOM   493  C  CA  . GLN   A  1  67  ? 45.391  -13.105 39.897 1.00 29.24  ? 80  GLN   A CA  1 
ATOM   494  C  C   . GLN   A  1  67  ? 44.353  -13.991 40.572 1.00 28.04  ? 80  GLN   A C   1 
ATOM   495  O  O   . GLN   A  1  67  ? 43.675  -14.726 39.894 1.00 28.55  ? 80  GLN   A O   1 
ATOM   496  C  CB  . GLN   A  1  67  ? 46.807  -13.643 40.112 1.00 29.77  ? 80  GLN   A CB  1 
ATOM   497  C  CG  . GLN   A  1  67  ? 47.837  -12.863 39.295 1.00 31.32  ? 80  GLN   A CG  1 
ATOM   498  C  CD  . GLN   A  1  67  ? 49.274  -13.331 39.408 1.00 30.07  ? 80  GLN   A CD  1 
ATOM   499  O  OE1 . GLN   A  1  67  ? 50.097  -13.054 38.535 1.00 34.00  ? 80  GLN   A OE1 1 
ATOM   500  N  NE2 . GLN   A  1  67  ? 49.612  -14.062 40.451 1.00 29.21  ? 80  GLN   A NE2 1 
ATOM   501  N  N   . GLU   A  1  68  ? 44.235  -13.943 41.895 1.00 33.40  ? 81  GLU   A N   1 
ATOM   502  C  CA  . GLU   A  1  68  ? 43.303  -14.803 42.617 1.00 34.83  ? 81  GLU   A CA  1 
ATOM   503  C  C   . GLU   A  1  68  ? 41.877  -14.485 42.197 1.00 31.80  ? 81  GLU   A C   1 
ATOM   504  O  O   . GLU   A  1  68  ? 41.109  -15.387 41.918 1.00 30.28  ? 81  GLU   A O   1 
ATOM   505  C  CB  . GLU   A  1  68  ? 43.391  -14.670 44.144 1.00 36.43  ? 81  GLU   A CB  1 
ATOM   506  C  CG  . GLU   A  1  68  ? 44.665  -15.272 44.732 1.00 46.03  ? 81  GLU   A CG  1 
ATOM   507  C  CD  . GLU   A  1  68  ? 44.961  -16.718 44.307 1.00 57.32  ? 81  GLU   A CD  1 
ATOM   508  O  OE1 . GLU   A  1  68  ? 46.087  -17.056 43.811 1.00 52.91  ? 81  GLU   A OE1 1 
ATOM   509  O  OE2 . GLU   A  1  68  ? 43.997  -17.512 44.447 1.00 58.42  ? 81  GLU   A OE2 1 
ATOM   510  N  N   . GLY   A  1  69  ? 41.538  -13.192 42.136 1.00 31.68  ? 82  GLY   A N   1 
ATOM   511  C  CA  . GLY   A  1  69  ? 40.156  -12.781 41.992 1.00 26.13  ? 82  GLY   A CA  1 
ATOM   512  C  C   . GLY   A  1  69  ? 39.672  -12.869 40.552 1.00 26.80  ? 82  GLY   A C   1 
ATOM   513  O  O   . GLY   A  1  69  ? 38.487  -13.091 40.341 1.00 24.99  ? 82  GLY   A O   1 
ATOM   514  N  N   . PHE   A  1  70  ? 40.558  -12.610 39.576 1.00 27.22  ? 83  PHE   A N   1 
ATOM   515  C  CA  . PHE   A  1  70  ? 40.123  -12.417 38.205 1.00 29.42  ? 83  PHE   A CA  1 
ATOM   516  C  C   . PHE   A  1  70  ? 40.954  -13.205 37.197 1.00 29.65  ? 83  PHE   A C   1 
ATOM   517  O  O   . PHE   A  1  70  ? 40.671  -13.148 36.002 1.00 28.15  ? 83  PHE   A O   1 
ATOM   518  C  CB  . PHE   A  1  70  ? 40.215  -10.945 37.792 1.00 28.80  ? 83  PHE   A CB  1 
ATOM   519  C  CG  . PHE   A  1  70  ? 39.131  -10.061 38.373 1.00 28.04  ? 83  PHE   A CG  1 
ATOM   520  C  CD1 . PHE   A  1  70  ? 37.841  -10.131 37.890 1.00 28.93  ? 83  PHE   A CD1 1 
ATOM   521  C  CD2 . PHE   A  1  70  ? 39.419  -9.123  39.347 1.00 29.54  ? 83  PHE   A CD2 1 
ATOM   522  C  CE1 . PHE   A  1  70  ? 36.844  -9.337  38.413 1.00 29.67  ? 83  PHE   A CE1 1 
ATOM   523  C  CE2 . PHE   A  1  70  ? 38.425  -8.302  39.829 1.00 29.99  ? 83  PHE   A CE2 1 
ATOM   524  C  CZ  . PHE   A  1  70  ? 37.140  -8.428  39.376 1.00 31.04  ? 83  PHE   A CZ  1 
ATOM   525  N  N   . ASN   A  1  71  ? 42.003  -13.880 37.669 1.00 29.74  ? 84  ASN   A N   1 
ATOM   526  C  CA  . ASN   A  1  71  ? 42.964  -14.548 36.809 1.00 27.68  ? 84  ASN   A CA  1 
ATOM   527  C  C   . ASN   A  1  71  ? 43.624  -13.561 35.861 1.00 26.89  ? 84  ASN   A C   1 
ATOM   528  O  O   . ASN   A  1  71  ? 43.854  -13.877 34.699 1.00 24.69  ? 84  ASN   A O   1 
ATOM   529  C  CB  . ASN   A  1  71  ? 42.296  -15.671 36.029 1.00 29.93  ? 84  ASN   A CB  1 
ATOM   530  C  CG  . ASN   A  1  71  ? 43.154  -16.912 35.941 1.00 28.88  ? 84  ASN   A CG  1 
ATOM   531  O  OD1 . ASN   A  1  71  ? 44.365  -16.872 36.178 1.00 29.36  ? 84  ASN   A OD1 1 
ATOM   532  N  ND2 . ASN   A  1  71  ? 42.535  -18.036 35.620 1.00 31.79  ? 84  ASN   A ND2 1 
ATOM   533  N  N   . PHE   A  1  72  ? 43.915  -12.351 36.344 1.00 27.74  ? 85  PHE   A N   1 
ATOM   534  C  CA  . PHE   A  1  72  ? 44.680  -11.410 35.544 1.00 27.61  ? 85  PHE   A CA  1 
ATOM   535  C  C   . PHE   A  1  72  ? 46.047  -12.038 35.278 1.00 27.18  ? 85  PHE   A C   1 
ATOM   536  O  O   . PHE   A  1  72  ? 46.679  -12.584 36.183 1.00 26.32  ? 85  PHE   A O   1 
ATOM   537  C  CB  . PHE   A  1  72  ? 44.798  -10.076 36.296 1.00 29.59  ? 85  PHE   A CB  1 
ATOM   538  C  CG  . PHE   A  1  72  ? 45.135  -8.854  35.456 1.00 29.95  ? 85  PHE   A CG  1 
ATOM   539  C  CD1 . PHE   A  1  72  ? 44.494  -8.620  34.249 1.00 31.62  ? 85  PHE   A CD1 1 
ATOM   540  C  CD2 . PHE   A  1  72  ? 46.061  -7.921  35.898 1.00 30.16  ? 85  PHE   A CD2 1 
ATOM   541  C  CE1 . PHE   A  1  72  ? 44.780  -7.488  33.506 1.00 36.07  ? 85  PHE   A CE1 1 
ATOM   542  C  CE2 . PHE   A  1  72  ? 46.331  -6.787  35.154 1.00 34.35  ? 85  PHE   A CE2 1 
ATOM   543  C  CZ  . PHE   A  1  72  ? 45.694  -6.569  33.962 1.00 31.97  ? 85  PHE   A CZ  1 
ATOM   544  N  N   . GLU   A  1  73  ? 46.497  -11.992 34.032 1.00 27.92  ? 86  GLU   A N   1 
ATOM   545  C  CA  . GLU   A  1  73  ? 47.784  -12.577 33.688 1.00 31.41  ? 86  GLU   A CA  1 
ATOM   546  C  C   . GLU   A  1  73  ? 48.929  -11.879 34.445 1.00 30.13  ? 86  GLU   A C   1 
ATOM   547  O  O   . GLU   A  1  73  ? 48.954  -10.658 34.617 1.00 30.78  ? 86  GLU   A O   1 
ATOM   548  C  CB  . GLU   A  1  73  ? 47.901  -12.498 32.167 1.00 35.91  ? 86  GLU   A CB  1 
ATOM   549  C  CG  . GLU   A  1  73  ? 49.056  -13.306 31.588 1.00 39.27  ? 86  GLU   A CG  1 
ATOM   550  C  CD  . GLU   A  1  73  ? 50.396  -12.575 31.562 1.00 54.55  ? 86  GLU   A CD  1 
ATOM   551  O  OE1 . GLU   A  1  73  ? 51.409  -13.204 32.000 1.00 52.75  ? 86  GLU   A OE1 1 
ATOM   552  O  OE2 . GLU   A  1  73  ? 50.425  -11.386 31.122 1.00 61.50  ? 86  GLU   A OE2 1 
ATOM   553  N  N   . ASN   A  1  74  ? 49.906  -12.683 34.863 1.00 30.12  ? 87  ASN   A N   1 
ATOM   554  C  CA  . ASN   A  1  74  ? 50.997  -12.262 35.734 1.00 31.31  ? 87  ASN   A CA  1 
ATOM   555  C  C   . ASN   A  1  74  ? 51.757  -11.037 35.207 1.00 31.63  ? 87  ASN   A C   1 
ATOM   556  O  O   . ASN   A  1  74  ? 51.973  -10.084 35.951 1.00 35.69  ? 87  ASN   A O   1 
ATOM   557  C  CB  . ASN   A  1  74  ? 51.963  -13.419 35.958 1.00 29.69  ? 87  ASN   A CB  1 
ATOM   558  C  CG  . ASN   A  1  74  ? 53.060  -13.121 36.950 1.00 28.39  ? 87  ASN   A CG  1 
ATOM   559  O  OD1 . ASN   A  1  74  ? 54.240  -13.227 36.592 1.00 34.96  ? 87  ASN   A OD1 1 
ATOM   560  N  ND2 . ASN   A  1  74  ? 52.712  -12.809 38.195 1.00 27.50  ? 87  ASN   A ND2 1 
ATOM   561  N  N   . ASN   A  1  75  ? 52.214  -11.082 33.951 1.00 29.70  ? 88  ASN   A N   1 
ATOM   562  C  CA  . ASN   A  1  75  ? 52.995  -9.996  33.400 1.00 33.46  ? 88  ASN   A CA  1 
ATOM   563  C  C   . ASN   A  1  75  ? 52.159  -8.726  33.287 1.00 31.73  ? 88  ASN   A C   1 
ATOM   564  O  O   . ASN   A  1  75  ? 52.692  -7.639  33.506 1.00 32.66  ? 88  ASN   A O   1 
ATOM   565  C  CB  . ASN   A  1  75  ? 53.672  -10.384 32.089 1.00 37.68  ? 88  ASN   A CB  1 
ATOM   566  C  CG  . ASN   A  1  75  ? 54.927  -11.179 32.377 1.00 44.90  ? 88  ASN   A CG  1 
ATOM   567  O  OD1 . ASN   A  1  75  ? 55.815  -10.717 33.112 1.00 42.90  ? 88  ASN   A OD1 1 
ATOM   568  N  ND2 . ASN   A  1  75  ? 55.034  -12.377 31.825 1.00 47.16  ? 88  ASN   A ND2 1 
ATOM   569  N  N   . ALA   A  1  76  ? 50.887  -8.881  32.916 1.00 28.56  ? 89  ALA   A N   1 
ATOM   570  C  CA  . ALA   A  1  76  ? 49.992  -7.756  32.807 1.00 28.94  ? 89  ALA   A CA  1 
ATOM   571  C  C   . ALA   A  1  76  ? 49.837  -7.106  34.184 1.00 29.20  ? 89  ALA   A C   1 
ATOM   572  O  O   . ALA   A  1  76  ? 49.871  -5.882  34.307 1.00 31.64  ? 89  ALA   A O   1 
ATOM   573  C  CB  . ALA   A  1  76  ? 48.677  -8.222  32.209 1.00 28.48  ? 89  ALA   A CB  1 
ATOM   574  N  N   . ALA   A  1  77  ? 49.727  -7.947  35.214 1.00 29.18  ? 90  ALA   A N   1 
ATOM   575  C  CA  . ALA   A  1  77  ? 49.578  -7.495  36.589 1.00 28.28  ? 90  ALA   A CA  1 
ATOM   576  C  C   . ALA   A  1  77  ? 50.832  -6.739  37.035 1.00 28.89  ? 90  ALA   A C   1 
ATOM   577  O  O   . ALA   A  1  77  ? 50.738  -5.732  37.737 1.00 29.14  ? 90  ALA   A O   1 
ATOM   578  C  CB  . ALA   A  1  77  ? 49.300  -8.670  37.489 1.00 24.93  ? 90  ALA   A CB  1 
ATOM   579  N  N   . ILE   A  1  78  ? 51.996  -7.226  36.593 1.00 28.00  ? 91  ILE   A N   1 
ATOM   580  C  CA  . ILE   A  1  78  ? 53.265  -6.617  36.948 1.00 29.59  ? 91  ILE   A CA  1 
ATOM   581  C  C   . ILE   A  1  78  ? 53.401  -5.257  36.263 1.00 27.89  ? 91  ILE   A C   1 
ATOM   582  O  O   . ILE   A  1  78  ? 53.685  -4.271  36.929 1.00 25.98  ? 91  ILE   A O   1 
ATOM   583  C  CB  . ILE   A  1  78  ? 54.418  -7.587  36.642 1.00 31.59  ? 91  ILE   A CB  1 
ATOM   584  C  CG1 . ILE   A  1  78  ? 54.443  -8.693  37.673 1.00 30.87  ? 91  ILE   A CG1 1 
ATOM   585  C  CG2 . ILE   A  1  78  ? 55.773  -6.864  36.592 1.00 35.37  ? 91  ILE   A CG2 1 
ATOM   586  C  CD1 . ILE   A  1  78  ? 55.346  -9.853  37.310 1.00 33.30  ? 91  ILE   A CD1 1 
ATOM   587  N  N   . VAL   A  1  79  ? 53.083  -5.191  34.968 1.00 26.69  ? 92  VAL   A N   1 
ATOM   588  C  CA  . VAL   A  1  79  ? 53.162  -3.947  34.228 1.00 28.65  ? 92  VAL   A CA  1 
ATOM   589  C  C   . VAL   A  1  79  ? 52.246  -2.898  34.845 1.00 30.67  ? 92  VAL   A C   1 
ATOM   590  O  O   . VAL   A  1  79  ? 52.690  -1.773  35.063 1.00 37.59  ? 92  VAL   A O   1 
ATOM   591  C  CB  . VAL   A  1  79  ? 52.853  -4.173  32.743 1.00 30.01  ? 92  VAL   A CB  1 
ATOM   592  C  CG1 . VAL   A  1  79  ? 52.651  -2.862  31.999 1.00 33.95  ? 92  VAL   A CG1 1 
ATOM   593  C  CG2 . VAL   A  1  79  ? 53.959  -4.992  32.086 1.00 30.35  ? 92  VAL   A CG2 1 
ATOM   594  N  N   . ALA   A  1  80  ? 50.987  -3.258  35.115 1.00 28.05  ? 93  ALA   A N   1 
ATOM   595  C  CA  . ALA   A  1  80  ? 50.029  -2.295  35.627 1.00 27.40  ? 93  ALA   A CA  1 
ATOM   596  C  C   . ALA   A  1  80  ? 50.384  -1.892  37.051 1.00 27.03  ? 93  ALA   A C   1 
ATOM   597  O  O   . ALA   A  1  80  ? 50.273  -0.719  37.405 1.00 29.18  ? 93  ALA   A O   1 
ATOM   598  C  CB  . ALA   A  1  80  ? 48.627  -2.865  35.579 1.00 29.52  ? 93  ALA   A CB  1 
ATOM   599  N  N   . THR   A  1  81  ? 50.807  -2.857  37.869 1.00 26.00  ? 94  THR   A N   1 
ATOM   600  C  CA  . THR   A  1  81  ? 50.943  -2.586  39.295 1.00 27.50  ? 94  THR   A CA  1 
ATOM   601  C  C   . THR   A  1  81  ? 52.111  -1.640  39.560 1.00 28.25  ? 94  THR   A C   1 
ATOM   602  O  O   . THR   A  1  81  ? 51.975  -0.696  40.328 1.00 26.15  ? 94  THR   A O   1 
ATOM   603  C  CB  . THR   A  1  81  ? 51.097  -3.874  40.103 1.00 25.87  ? 94  THR   A CB  1 
ATOM   604  O  OG1 . THR   A  1  81  ? 49.884  -4.625  40.025 1.00 27.58  ? 94  THR   A OG1 1 
ATOM   605  C  CG2 . THR   A  1  81  ? 51.302  -3.618  41.583 1.00 27.32  ? 94  THR   A CG2 1 
ATOM   606  N  N   . TYR   A  1  82  ? 53.270  -1.915  38.950 1.00 28.88  ? 95  TYR   A N   1 
ATOM   607  C  CA  . TYR   A  1  82  ? 54.469  -1.151  39.242 1.00 29.48  ? 95  TYR   A CA  1 
ATOM   608  C  C   . TYR   A  1  82  ? 54.429  0.186   38.496 1.00 27.39  ? 95  TYR   A C   1 
ATOM   609  O  O   . TYR   A  1  82  ? 55.018  1.142   38.944 1.00 30.05  ? 95  TYR   A O   1 
ATOM   610  C  CB  . TYR   A  1  82  ? 55.727  -1.986  38.976 1.00 28.73  ? 95  TYR   A CB  1 
ATOM   611  C  CG  . TYR   A  1  82  ? 55.930  -3.094  39.994 1.00 28.49  ? 95  TYR   A CG  1 
ATOM   612  C  CD1 . TYR   A  1  82  ? 56.378  -2.820  41.275 1.00 28.57  ? 95  TYR   A CD1 1 
ATOM   613  C  CD2 . TYR   A  1  82  ? 55.636  -4.419  39.690 1.00 32.73  ? 95  TYR   A CD2 1 
ATOM   614  C  CE1 . TYR   A  1  82  ? 56.518  -3.821  42.223 1.00 28.36  ? 95  TYR   A CE1 1 
ATOM   615  C  CE2 . TYR   A  1  82  ? 55.760  -5.431  40.630 1.00 31.95  ? 95  TYR   A CE2 1 
ATOM   616  C  CZ  . TYR   A  1  82  ? 56.224  -5.133  41.891 1.00 30.39  ? 95  TYR   A CZ  1 
ATOM   617  O  OH  . TYR   A  1  82  ? 56.375  -6.142  42.796 1.00 35.71  ? 95  TYR   A OH  1 
ATOM   618  N  N   . LEU   A  1  83  ? 53.703  0.274   37.391 1.00 28.36  ? 96  LEU   A N   1 
ATOM   619  C  CA  . LEU   A  1  83  ? 53.414  1.567   36.800 1.00 33.10  ? 96  LEU   A CA  1 
ATOM   620  C  C   . LEU   A  1  83  ? 52.668  2.428   37.825 1.00 32.04  ? 96  LEU   A C   1 
ATOM   621  O  O   . LEU   A  1  83  ? 53.074  3.544   38.111 1.00 33.36  ? 96  LEU   A O   1 
ATOM   622  C  CB  . LEU   A  1  83  ? 52.607  1.389   35.518 1.00 32.43  ? 96  LEU   A CB  1 
ATOM   623  C  CG  . LEU   A  1  83  ? 52.099  2.686   34.877 1.00 39.47  ? 96  LEU   A CG  1 
ATOM   624  C  CD1 . LEU   A  1  83  ? 53.259  3.586   34.461 1.00 38.63  ? 96  LEU   A CD1 1 
ATOM   625  C  CD2 . LEU   A  1  83  ? 51.202  2.386   33.691 1.00 42.65  ? 96  LEU   A CD2 1 
ATOM   626  N  N   . GLY   A  1  84  ? 51.563  1.902   38.354 1.00 27.87  ? 97  GLY   A N   1 
ATOM   627  C  CA  . GLY   A  1  84  ? 50.766  2.612   39.333 1.00 29.03  ? 97  GLY   A CA  1 
ATOM   628  C  C   . GLY   A  1  84  ? 51.581  2.963   40.581 1.00 27.77  ? 97  GLY   A C   1 
ATOM   629  O  O   . GLY   A  1  84  ? 51.455  4.059   41.121 1.00 31.70  ? 97  GLY   A O   1 
ATOM   630  N  N   . HIS   A  1  85  ? 52.435  2.047   41.015 1.00 26.93  ? 98  HIS   A N   1 
ATOM   631  C  CA  . HIS   A  1  85  ? 53.209  2.236   42.232 1.00 29.18  ? 98  HIS   A CA  1 
ATOM   632  C  C   . HIS   A  1  85  ? 54.339  3.254   42.040 1.00 28.99  ? 98  HIS   A C   1 
ATOM   633  O  O   . HIS   A  1  85  ? 54.553  4.100   42.915 1.00 27.93  ? 98  HIS   A O   1 
ATOM   634  C  CB  . HIS   A  1  85  ? 53.797  0.911   42.700 1.00 26.74  ? 98  HIS   A CB  1 
ATOM   635  C  CG  . HIS   A  1  85  ? 54.417  0.972   44.037 1.00 27.31  ? 98  HIS   A CG  1 
ATOM   636  N  ND1 . HIS   A  1  85  ? 53.787  1.525   45.133 1.00 29.13  ? 98  HIS   A ND1 1 
ATOM   637  C  CD2 . HIS   A  1  85  ? 55.596  0.499   44.455 1.00 25.73  ? 98  HIS   A CD2 1 
ATOM   638  C  CE1 . HIS   A  1  85  ? 54.582  1.388   46.192 1.00 30.87  ? 98  HIS   A CE1 1 
ATOM   639  N  NE2 . HIS   A  1  85  ? 55.694  0.772   45.795 1.00 28.34  ? 98  HIS   A NE2 1 
ATOM   640  N  N   . LEU   A  1  86  ? 55.067  3.151   40.924 1.00 27.01  ? 99  LEU   A N   1 
ATOM   641  C  CA  . LEU   A  1  86  ? 56.163  4.069   40.641 1.00 32.11  ? 99  LEU   A CA  1 
ATOM   642  C  C   . LEU   A  1  86  ? 55.661  5.515   40.633 1.00 30.96  ? 99  LEU   A C   1 
ATOM   643  O  O   . LEU   A  1  86  ? 56.263  6.368   41.268 1.00 32.89  ? 99  LEU   A O   1 
ATOM   644  C  CB  . LEU   A  1  86  ? 56.850  3.703   39.326 1.00 28.76  ? 99  LEU   A CB  1 
ATOM   645  C  CG  . LEU   A  1  86  ? 57.806  2.506   39.423 1.00 31.45  ? 99  LEU   A CG  1 
ATOM   646  C  CD1 . LEU   A  1  86  ? 58.181  1.959   38.080 1.00 29.71  ? 99  LEU   A CD1 1 
ATOM   647  C  CD2 . LEU   A  1  86  ? 59.072  2.832   40.179 1.00 34.31  ? 99  LEU   A CD2 1 
ATOM   648  N  N   . LEU   A  1  87  ? 54.526  5.750   39.965 1.00 29.13  ? 100 LEU   A N   1 
ATOM   649  C  CA  . LEU   A  1  87  ? 53.976  7.077   39.761 1.00 27.95  ? 100 LEU   A CA  1 
ATOM   650  C  C   . LEU   A  1  87  ? 53.175  7.553   40.965 1.00 27.72  ? 100 LEU   A C   1 
ATOM   651  O  O   . LEU   A  1  87  ? 53.195  8.739   41.279 1.00 30.21  ? 100 LEU   A O   1 
ATOM   652  C  CB  . LEU   A  1  87  ? 53.115  7.050   38.507 1.00 30.85  ? 100 LEU   A CB  1 
ATOM   653  C  CG  . LEU   A  1  87  ? 53.865  6.733   37.209 1.00 32.08  ? 100 LEU   A CG  1 
ATOM   654  C  CD1 . LEU   A  1  87  ? 52.908  6.664   36.056 1.00 34.80  ? 100 LEU   A CD1 1 
ATOM   655  C  CD2 . LEU   A  1  87  ? 54.944  7.756   36.902 1.00 34.79  ? 100 LEU   A CD2 1 
ATOM   656  N  N   . ASN   A  1  88  ? 52.488  6.636   41.653 1.00 30.64  ? 101 ASN   A N   1 
ATOM   657  C  CA  . ASN   A  1  88  ? 51.420  7.029   42.562 1.00 28.07  ? 101 ASN   A CA  1 
ATOM   658  C  C   . ASN   A  1  88  ? 51.550  6.426   43.953 1.00 27.34  ? 101 ASN   A C   1 
ATOM   659  O  O   . ASN   A  1  88  ? 50.726  6.730   44.821 1.00 27.89  ? 101 ASN   A O   1 
ATOM   660  C  CB  . ASN   A  1  88  ? 50.058  6.659   42.011 1.00 29.14  ? 101 ASN   A CB  1 
ATOM   661  C  CG  . ASN   A  1  88  ? 49.765  7.348   40.702 1.00 32.09  ? 101 ASN   A CG  1 
ATOM   662  O  OD1 . ASN   A  1  88  ? 50.081  8.531   40.511 1.00 35.85  ? 101 ASN   A OD1 1 
ATOM   663  N  ND2 . ASN   A  1  88  ? 49.149  6.627   39.784 1.00 37.33  ? 101 ASN   A ND2 1 
ATOM   664  N  N   . GLY   A  1  89  ? 52.556  5.573   44.163 1.00 25.55  ? 102 GLY   A N   1 
ATOM   665  C  CA  . GLY   A  1  89  ? 52.682  4.892   45.441 1.00 27.59  ? 102 GLY   A CA  1 
ATOM   666  C  C   . GLY   A  1  89  ? 53.799  5.464   46.304 1.00 25.77  ? 102 GLY   A C   1 
ATOM   667  O  O   . GLY   A  1  89  ? 54.589  6.278   45.853 1.00 27.13  ? 102 GLY   A O   1 
ATOM   668  N  N   . ASN   A  1  90  ? 53.844  5.028   47.560 1.00 24.54  ? 103 ASN   A N   1 
ATOM   669  C  CA  . ASN   A  1  90  ? 54.916  5.386   48.460 1.00 24.20  ? 103 ASN   A CA  1 
ATOM   670  C  C   . ASN   A  1  90  ? 55.948  4.266   48.403 1.00 29.26  ? 103 ASN   A C   1 
ATOM   671  O  O   . ASN   A  1  90  ? 55.690  3.172   48.893 1.00 29.53  ? 103 ASN   A O   1 
ATOM   672  C  CB  . ASN   A  1  90  ? 54.371  5.574   49.863 1.00 26.50  ? 103 ASN   A CB  1 
ATOM   673  C  CG  . ASN   A  1  90  ? 55.414  6.102   50.816 1.00 26.50  ? 103 ASN   A CG  1 
ATOM   674  O  OD1 . ASN   A  1  90  ? 56.561  5.648   50.810 1.00 25.41  ? 103 ASN   A OD1 1 
ATOM   675  N  ND2 . ASN   A  1  90  ? 55.048  7.082   51.620 1.00 29.65  ? 103 ASN   A ND2 1 
ATOM   676  N  N   . LEU   A  1  91  ? 57.115  4.542   47.823 1.00 33.10  ? 104 LEU   A N   1 
ATOM   677  C  CA  . LEU   A  1  91  ? 58.109  3.509   47.551 1.00 34.22  ? 104 LEU   A CA  1 
ATOM   678  C  C   . LEU   A  1  91  ? 58.861  3.114   48.816 1.00 31.56  ? 104 LEU   A C   1 
ATOM   679  O  O   . LEU   A  1  91  ? 59.439  2.042   48.876 1.00 31.51  ? 104 LEU   A O   1 
ATOM   680  C  CB  . LEU   A  1  91  ? 59.060  3.997   46.466 1.00 36.70  ? 104 LEU   A CB  1 
ATOM   681  C  CG  . LEU   A  1  91  ? 58.379  4.339   45.140 1.00 39.34  ? 104 LEU   A CG  1 
ATOM   682  C  CD1 . LEU   A  1  91  ? 59.273  5.127   44.245 1.00 43.21  ? 104 LEU   A CD1 1 
ATOM   683  C  CD2 . LEU   A  1  91  ? 57.977  3.097   44.427 1.00 43.39  ? 104 LEU   A CD2 1 
ATOM   684  N  N   . VAL   A  1  92  ? 58.829  3.963   49.839 1.00 30.97  ? 105 VAL   A N   1 
ATOM   685  C  CA  . VAL   A  1  92  ? 59.527  3.676   51.075 1.00 31.75  ? 105 VAL   A CA  1 
ATOM   686  C  C   . VAL   A  1  92  ? 58.694  2.721   51.925 1.00 33.67  ? 105 VAL   A C   1 
ATOM   687  O  O   . VAL   A  1  92  ? 59.231  1.735   52.408 1.00 33.63  ? 105 VAL   A O   1 
ATOM   688  C  CB  . VAL   A  1  92  ? 59.899  4.965   51.831 1.00 32.29  ? 105 VAL   A CB  1 
ATOM   689  C  CG1 . VAL   A  1  92  ? 60.389  4.696   53.252 1.00 32.35  ? 105 VAL   A CG1 1 
ATOM   690  C  CG2 . VAL   A  1  92  ? 60.965  5.723   51.067 1.00 30.79  ? 105 VAL   A CG2 1 
ATOM   691  N  N   . THR   A  1  93  ? 57.391  2.999   52.089 1.00 32.90  ? 106 THR   A N   1 
ATOM   692  C  CA  . THR   A  1  93  ? 56.526  2.122   52.859 1.00 34.00  ? 106 THR   A CA  1 
ATOM   693  C  C   . THR   A  1  93  ? 56.007  0.949   52.026 1.00 33.74  ? 106 THR   A C   1 
ATOM   694  O  O   . THR   A  1  93  ? 55.444  0.021   52.592 1.00 37.50  ? 106 THR   A O   1 
ATOM   695  C  CB  . THR   A  1  93  ? 55.354  2.902   53.439 1.00 36.76  ? 106 THR   A CB  1 
ATOM   696  O  OG1 . THR   A  1  93  ? 54.640  3.372   52.300 1.00 37.49  ? 106 THR   A OG1 1 
ATOM   697  C  CG2 . THR   A  1  93  ? 55.816  4.016   54.361 1.00 36.73  ? 106 THR   A CG2 1 
ATOM   698  N  N   . ASP   A  1  94  ? 56.148  1.020   50.699 1.00 32.27  ? 107 ASP   A N   1 
ATOM   699  C  CA  . ASP   A  1  94  ? 55.683  0.004   49.768 1.00 30.66  ? 107 ASP   A CA  1 
ATOM   700  C  C   . ASP   A  1  94  ? 54.155  -0.093  49.743 1.00 30.42  ? 107 ASP   A C   1 
ATOM   701  O  O   . ASP   A  1  94  ? 53.620  -1.182  49.633 1.00 27.81  ? 107 ASP   A O   1 
ATOM   702  C  CB  . ASP   A  1  94  ? 56.324  -1.340  50.070 1.00 33.70  ? 107 ASP   A CB  1 
ATOM   703  C  CG  . ASP   A  1  94  ? 56.327  -2.337  48.912 1.00 34.45  ? 107 ASP   A CG  1 
ATOM   704  O  OD1 . ASP   A  1  94  ? 56.603  -1.914  47.751 1.00 31.51  ? 107 ASP   A OD1 1 
ATOM   705  O  OD2 . ASP   A  1  94  ? 56.082  -3.536  49.182 1.00 40.93  ? 107 ASP   A OD2 1 
ATOM   706  N  N   . LEU   A  1  95  ? 53.452  1.040   49.823 1.00 31.31  ? 108 LEU   A N   1 
ATOM   707  C  CA  . LEU   A  1  95  ? 52.000  1.049   49.855 1.00 29.66  ? 108 LEU   A CA  1 
ATOM   708  C  C   . LEU   A  1  95  ? 51.462  1.964   48.757 1.00 27.21  ? 108 LEU   A C   1 
ATOM   709  O  O   . LEU   A  1  95  ? 51.983  3.048   48.544 1.00 29.50  ? 108 LEU   A O   1 
ATOM   710  C  CB  . LEU   A  1  95  ? 51.525  1.502   51.228 1.00 30.00  ? 108 LEU   A CB  1 
ATOM   711  C  CG  . LEU   A  1  95  ? 51.865  0.585   52.407 1.00 32.07  ? 108 LEU   A CG  1 
ATOM   712  C  CD1 . LEU   A  1  95  ? 51.532  1.299   53.718 1.00 32.57  ? 108 LEU   A CD1 1 
ATOM   713  C  CD2 . LEU   A  1  95  ? 51.101  -0.724  52.346 1.00 32.11  ? 108 LEU   A CD2 1 
ATOM   714  N  N   . LEU   A  1  96  ? 50.396  1.501   48.102 1.00 26.99  ? 109 LEU   A N   1 
ATOM   715  C  CA  . LEU   A  1  96  ? 49.713  2.212   47.037 1.00 26.77  ? 109 LEU   A CA  1 
ATOM   716  C  C   . LEU   A  1  96  ? 48.224  2.319   47.373 1.00 28.92  ? 109 LEU   A C   1 
ATOM   717  O  O   . LEU   A  1  96  ? 47.579  1.307   47.655 1.00 29.02  ? 109 LEU   A O   1 
ATOM   718  C  CB  . LEU   A  1  96  ? 49.945  1.455   45.734 1.00 24.61  ? 109 LEU   A CB  1 
ATOM   719  C  CG  . LEU   A  1  96  ? 49.097  1.918   44.550 1.00 27.38  ? 109 LEU   A CG  1 
ATOM   720  C  CD1 . LEU   A  1  96  ? 49.357  3.396   44.213 1.00 31.04  ? 109 LEU   A CD1 1 
ATOM   721  C  CD2 . LEU   A  1  96  ? 49.361  1.058   43.334 1.00 26.95  ? 109 LEU   A CD2 1 
ATOM   722  N  N   . SER   A  1  97  ? 47.706  3.560   47.347 1.00 26.45  ? 110 SER   A N   1 
ATOM   723  C  CA  . SER   A  1  97  ? 46.276  3.815   47.420 1.00 27.17  ? 110 SER   A CA  1 
ATOM   724  C  C   . SER   A  1  97  ? 45.634  3.561   46.066 1.00 24.38  ? 110 SER   A C   1 
ATOM   725  O  O   . SER   A  1  97  ? 46.089  4.086   45.059 1.00 25.89  ? 110 SER   A O   1 
ATOM   726  C  CB  . SER   A  1  97  ? 45.997  5.232   47.878 1.00 29.98  ? 110 SER   A CB  1 
ATOM   727  O  OG  . SER   A  1  97  ? 44.640  5.592   47.670 1.00 29.51  ? 110 SER   A OG  1 
ATOM   728  N  N   . ILE   A  1  98  ? 44.535  2.807   46.056 1.00 23.80  ? 111 ILE   A N   1 
ATOM   729  C  CA  . ILE   A  1  98  ? 43.860  2.519   44.809 1.00 26.74  ? 111 ILE   A CA  1 
ATOM   730  C  C   . ILE   A  1  98  ? 42.950  3.691   44.459 1.00 27.27  ? 111 ILE   A C   1 
ATOM   731  O  O   . ILE   A  1  98  ? 42.281  3.657   43.439 1.00 29.42  ? 111 ILE   A O   1 
ATOM   732  C  CB  . ILE   A  1  98  ? 43.096  1.181   44.852 1.00 26.79  ? 111 ILE   A CB  1 
ATOM   733  C  CG1 . ILE   A  1  98  ? 41.885  1.230   45.755 1.00 27.39  ? 111 ILE   A CG1 1 
ATOM   734  C  CG2 . ILE   A  1  98  ? 44.050  0.042   45.207 1.00 26.80  ? 111 ILE   A CG2 1 
ATOM   735  C  CD1 . ILE   A  1  98  ? 41.067  -0.051  45.779 1.00 28.07  ? 111 ILE   A CD1 1 
ATOM   736  N  N   . GLY   A  1  99  ? 42.919  4.702   45.326 1.00 28.29  ? 112 GLY   A N   1 
ATOM   737  C  CA  . GLY   A  1  99  ? 42.134  5.898   45.078 1.00 33.81  ? 112 GLY   A CA  1 
ATOM   738  C  C   . GLY   A  1  99  ? 42.941  7.168   45.277 1.00 32.11  ? 112 GLY   A C   1 
ATOM   739  O  O   . GLY   A  1  99  ? 43.877  7.409   44.535 1.00 30.27  ? 112 GLY   A O   1 
ATOM   740  N  N   . GLY   A  1  100 ? 42.521  7.972   46.249 1.00 36.28  ? 113 GLY   A N   1 
ATOM   741  C  CA  . GLY   A  1  100 ? 43.130  9.266   46.479 1.00 40.57  ? 113 GLY   A CA  1 
ATOM   742  C  C   . GLY   A  1  100 ? 44.093  9.227   47.658 1.00 36.94  ? 113 GLY   A C   1 
ATOM   743  O  O   . GLY   A  1  100 ? 44.433  8.167   48.160 1.00 33.16  ? 113 GLY   A O   1 
ATOM   744  N  N   . ALA   A  1  101 ? 44.495  10.423  48.086 1.00 40.51  ? 114 ALA   A N   1 
ATOM   745  C  CA  . ALA   A  1  101 ? 45.493  10.596  49.130 1.00 39.41  ? 114 ALA   A CA  1 
ATOM   746  C  C   . ALA   A  1  101 ? 44.945  10.076  50.447 1.00 30.41  ? 114 ALA   A C   1 
ATOM   747  O  O   . ALA   A  1  101 ? 43.761  10.175  50.717 1.00 29.94  ? 114 ALA   A O   1 
ATOM   748  C  CB  . ALA   A  1  101 ? 45.869  12.071  49.245 1.00 39.28  ? 114 ALA   A CB  1 
ATOM   749  N  N   . THR   A  1  102 ? 45.824  9.499   51.256 1.00 35.11  ? 115 THR   A N   1 
ATOM   750  C  CA  . THR   A  1  102 ? 45.414  8.949   52.535 1.00 36.53  ? 115 THR   A CA  1 
ATOM   751  C  C   . THR   A  1  102 ? 46.642  8.899   53.424 1.00 34.22  ? 115 THR   A C   1 
ATOM   752  O  O   . THR   A  1  102 ? 47.719  8.580   52.943 1.00 36.18  ? 115 THR   A O   1 
ATOM   753  C  CB  . THR   A  1  102 ? 44.782  7.561   52.353 1.00 34.78  ? 115 THR   A CB  1 
ATOM   754  O  OG1 . THR   A  1  102 ? 44.532  6.995   53.639 1.00 37.93  ? 115 THR   A OG1 1 
ATOM   755  C  CG2 . THR   A  1  102 ? 45.680  6.606   51.594 1.00 32.91  ? 115 THR   A CG2 1 
ATOM   756  N  N   . PRO   A  1  103 ? 46.497  9.164   54.739 1.00 38.23  ? 116 PRO   A N   1 
ATOM   757  C  CA  . PRO   A  1  103 ? 47.589  8.922   55.689 1.00 37.51  ? 116 PRO   A CA  1 
ATOM   758  C  C   . PRO   A  1  103 ? 48.055  7.468   55.757 1.00 35.51  ? 116 PRO   A C   1 
ATOM   759  O  O   . PRO   A  1  103 ? 49.179  7.205   56.174 1.00 39.11  ? 116 PRO   A O   1 
ATOM   760  C  CB  . PRO   A  1  103 ? 47.020  9.381   57.053 1.00 37.11  ? 116 PRO   A CB  1 
ATOM   761  C  CG  . PRO   A  1  103 ? 45.501  9.447   56.855 1.00 37.03  ? 116 PRO   A CG  1 
ATOM   762  C  CD  . PRO   A  1  103 ? 45.275  9.697   55.373 1.00 35.22  ? 116 PRO   A CD  1 
ATOM   763  N  N   . LYS   A  1  104 ? 47.196  6.537   55.329 1.00 33.75  ? 117 LYS   A N   1 
ATOM   764  C  CA  . LYS   A  1  104 ? 47.484  5.108   55.416 1.00 34.30  ? 117 LYS   A CA  1 
ATOM   765  C  C   . LYS   A  1  104 ? 48.682  4.683   54.556 1.00 33.25  ? 117 LYS   A C   1 
ATOM   766  O  O   . LYS   A  1  104 ? 49.182  3.587   54.745 1.00 31.36  ? 117 LYS   A O   1 
ATOM   767  C  CB  . LYS   A  1  104 ? 46.249  4.310   54.976 1.00 32.52  ? 117 LYS   A CB  1 
ATOM   768  C  CG  . LYS   A  1  104 ? 45.084  4.365   55.929 1.00 34.39  ? 117 LYS   A CG  1 
ATOM   769  C  CD  . LYS   A  1  104 ? 43.749  4.047   55.256 1.00 42.73  ? 117 LYS   A CD  1 
ATOM   770  C  CE  . LYS   A  1  104 ? 42.602  4.049   56.224 1.00 45.57  ? 117 LYS   A CE  1 
ATOM   771  N  NZ  . LYS   A  1  104 ? 42.696  2.934   57.173 1.00 47.69  ? 117 LYS   A NZ  1 
ATOM   772  N  N   . THR   A  1  105 ? 49.137  5.507   53.597 1.00 34.87  ? 118 THR   A N   1 
ATOM   773  C  CA  . THR   A  1  105 ? 50.318  5.142   52.821 1.00 34.89  ? 118 THR   A CA  1 
ATOM   774  C  C   . THR   A  1  105 ? 51.588  5.550   53.563 1.00 36.66  ? 118 THR   A C   1 
ATOM   775  O  O   . THR   A  1  105 ? 52.677  5.241   53.089 1.00 31.18  ? 118 THR   A O   1 
ATOM   776  C  CB  . THR   A  1  105 ? 50.287  5.733   51.410 1.00 36.21  ? 118 THR   A CB  1 
ATOM   777  O  OG1 . THR   A  1  105 ? 50.115  7.147   51.475 1.00 34.88  ? 118 THR   A OG1 1 
ATOM   778  C  CG2 . THR   A  1  105 ? 49.191  5.122   50.549 1.00 35.69  ? 118 THR   A CG2 1 
ATOM   779  N  N   . GLY   A  1  106 ? 51.436  6.230   54.718 1.00 37.72  ? 119 GLY   A N   1 
ATOM   780  C  CA  . GLY   A  1  106 ? 52.549  6.583   55.585 1.00 37.30  ? 119 GLY   A CA  1 
ATOM   781  C  C   . GLY   A  1  106 ? 53.102  7.987   55.301 1.00 42.53  ? 119 GLY   A C   1 
ATOM   782  O  O   . GLY   A  1  106 ? 52.498  8.760   54.548 1.00 38.15  ? 119 GLY   A O   1 
ATOM   783  N  N   . PRO   A  1  107 ? 54.279  8.337   55.887 1.00 45.78  ? 120 PRO   A N   1 
ATOM   784  C  CA  . PRO   A  1  107 ? 54.955  9.625   55.656 1.00 51.25  ? 120 PRO   A CA  1 
ATOM   785  C  C   . PRO   A  1  107 ? 55.154  10.019  54.194 1.00 46.06  ? 120 PRO   A C   1 
ATOM   786  O  O   . PRO   A  1  107 ? 55.752  9.276   53.437 1.00 44.97  ? 120 PRO   A O   1 
ATOM   787  C  CB  . PRO   A  1  107 ? 56.330  9.467   56.347 1.00 49.17  ? 120 PRO   A CB  1 
ATOM   788  C  CG  . PRO   A  1  107 ? 56.084  8.418   57.405 1.00 46.83  ? 120 PRO   A CG  1 
ATOM   789  C  CD  . PRO   A  1  107 ? 55.018  7.494   56.836 1.00 45.14  ? 120 PRO   A CD  1 
ATOM   790  N  N   . PRO   A  1  108 ? 54.683  11.208  53.765 1.00 50.10  ? 121 PRO   A N   1 
ATOM   791  C  CA  . PRO   A  1  108 ? 54.710  11.568  52.353 1.00 50.71  ? 121 PRO   A CA  1 
ATOM   792  C  C   . PRO   A  1  108 ? 56.136  11.565  51.812 1.00 43.66  ? 121 PRO   A C   1 
ATOM   793  O  O   . PRO   A  1  108 ? 57.094  11.793  52.540 1.00 41.79  ? 121 PRO   A O   1 
ATOM   794  C  CB  . PRO   A  1  108 ? 54.044  12.964  52.293 1.00 56.95  ? 121 PRO   A CB  1 
ATOM   795  C  CG  . PRO   A  1  108 ? 54.048  13.477  53.725 1.00 62.12  ? 121 PRO   A CG  1 
ATOM   796  C  CD  . PRO   A  1  108 ? 54.078  12.250  54.610 1.00 55.71  ? 121 PRO   A CD  1 
ATOM   797  N  N   . PRO   A  1  109 ? 56.323  11.253  50.515 1.00 43.31  ? 122 PRO   A N   1 
ATOM   798  C  CA  . PRO   A  1  109 ? 57.639  11.369  49.892 1.00 40.91  ? 122 PRO   A CA  1 
ATOM   799  C  C   . PRO   A  1  109 ? 58.006  12.827  49.624 1.00 40.80  ? 122 PRO   A C   1 
ATOM   800  O  O   . PRO   A  1  109 ? 57.144  13.698  49.664 1.00 40.83  ? 122 PRO   A O   1 
ATOM   801  C  CB  . PRO   A  1  109 ? 57.453  10.564  48.603 1.00 41.69  ? 122 PRO   A CB  1 
ATOM   802  C  CG  . PRO   A  1  109 ? 56.015  10.746  48.265 1.00 44.24  ? 122 PRO   A CG  1 
ATOM   803  C  CD  . PRO   A  1  109 ? 55.268  10.807  49.584 1.00 43.07  ? 122 PRO   A CD  1 
ATOM   804  N  N   . PRO   A  1  110 ? 59.285  13.134  49.321 1.00 44.00  ? 123 PRO   A N   1 
ATOM   805  C  CA  . PRO   A  1  110 ? 59.697  14.496  48.943 1.00 42.19  ? 123 PRO   A CA  1 
ATOM   806  C  C   . PRO   A  1  110 ? 59.051  14.974  47.646 1.00 40.79  ? 123 PRO   A C   1 
ATOM   807  O  O   . PRO   A  1  110 ? 59.074  14.262  46.649 1.00 38.82  ? 123 PRO   A O   1 
ATOM   808  C  CB  . PRO   A  1  110 ? 61.236  14.394  48.798 1.00 43.75  ? 123 PRO   A CB  1 
ATOM   809  C  CG  . PRO   A  1  110 ? 61.495  12.917  48.562 1.00 45.00  ? 123 PRO   A CG  1 
ATOM   810  C  CD  . PRO   A  1  110 ? 60.405  12.176  49.325 1.00 45.58  ? 123 PRO   A CD  1 
ATOM   811  N  N   . PRO   A  1  111 ? 58.432  16.171  47.606 1.00 43.08  ? 124 PRO   A N   1 
ATOM   812  C  CA  . PRO   A  1  111 ? 57.835  16.659  46.363 1.00 40.04  ? 124 PRO   A CA  1 
ATOM   813  C  C   . PRO   A  1  111 ? 58.936  16.737  45.308 1.00 36.28  ? 124 PRO   A C   1 
ATOM   814  O  O   . PRO   A  1  111 ? 60.096  16.852  45.663 1.00 34.47  ? 124 PRO   A O   1 
ATOM   815  C  CB  . PRO   A  1  111 ? 57.191  18.003  46.706 1.00 41.23  ? 124 PRO   A CB  1 
ATOM   816  C  CG  . PRO   A  1  111 ? 57.241  18.104  48.218 1.00 45.45  ? 124 PRO   A CG  1 
ATOM   817  C  CD  . PRO   A  1  111 ? 58.175  17.040  48.761 1.00 45.08  ? 124 PRO   A CD  1 
ATOM   818  N  N   . PRO   A  1  112 ? 58.642  16.663  43.988 1.00 34.06  ? 125 PRO   A N   1 
ATOM   819  C  CA  . PRO   A  1  112 ? 57.266  16.618  43.470 1.00 34.15  ? 125 PRO   A CA  1 
ATOM   820  C  C   . PRO   A  1  112 ? 56.518  15.290  43.493 1.00 36.53  ? 125 PRO   A C   1 
ATOM   821  O  O   . PRO   A  1  112 ? 55.366  15.222  43.053 1.00 38.39  ? 125 PRO   A O   1 
ATOM   822  C  CB  . PRO   A  1  112 ? 57.393  17.127  42.033 1.00 37.67  ? 125 PRO   A CB  1 
ATOM   823  C  CG  . PRO   A  1  112 ? 58.863  16.975  41.684 1.00 37.81  ? 125 PRO   A CG  1 
ATOM   824  C  CD  . PRO   A  1  112 ? 59.666  16.670  42.944 1.00 32.90  ? 125 PRO   A CD  1 
ATOM   825  N  N   . ALA   A  1  113 ? 57.141  14.245  44.050 1.00 36.79  ? 126 ALA   A N   1 
ATOM   826  C  CA  . ALA   A  1  113 ? 56.445  12.983  44.287 1.00 34.81  ? 126 ALA   A CA  1 
ATOM   827  C  C   . ALA   A  1  113 ? 55.393  13.166  45.376 1.00 34.91  ? 126 ALA   A C   1 
ATOM   828  O  O   . ALA   A  1  113 ? 55.537  14.012  46.248 1.00 38.24  ? 126 ALA   A O   1 
ATOM   829  C  CB  . ALA   A  1  113 ? 57.435  11.907  44.640 1.00 34.16  ? 126 ALA   A CB  1 
ATOM   830  N  N   . HIS   A  1  114 ? 54.330  12.354  45.327 1.00 37.08  ? 127 HIS   A N   1 
ATOM   831  C  CA  . HIS   A  1  114 ? 53.097  12.654  46.042 1.00 32.51  ? 127 HIS   A CA  1 
ATOM   832  C  C   . HIS   A  1  114 ? 52.518  11.418  46.731 1.00 31.87  ? 127 HIS   A C   1 
ATOM   833  O  O   . HIS   A  1  114 ? 51.879  11.550  47.777 1.00 33.32  ? 127 HIS   A O   1 
ATOM   834  C  CB  . HIS   A  1  114 ? 52.111  13.309  45.072 1.00 34.33  ? 127 HIS   A CB  1 
ATOM   835  C  CG  . HIS   A  1  114 ? 51.994  12.600  43.756 1.00 34.23  ? 127 HIS   A CG  1 
ATOM   836  N  ND1 . HIS   A  1  114 ? 51.307  11.417  43.619 1.00 32.84  ? 127 HIS   A ND1 1 
ATOM   837  C  CD2 . HIS   A  1  114 ? 52.484  12.879  42.540 1.00 34.60  ? 127 HIS   A CD2 1 
ATOM   838  C  CE1 . HIS   A  1  114 ? 51.359  11.025  42.354 1.00 37.21  ? 127 HIS   A CE1 1 
ATOM   839  N  NE2 . HIS   A  1  114 ? 52.076  11.898  41.676 1.00 34.87  ? 127 HIS   A NE2 1 
ATOM   840  N  N   . ALA   A  1  115 ? 52.709  10.223  46.148 1.00 35.39  ? 128 ALA   A N   1 
ATOM   841  C  CA  . ALA   A  1  115 ? 52.052  9.004   46.614 1.00 33.65  ? 128 ALA   A CA  1 
ATOM   842  C  C   . ALA   A  1  115 ? 50.546  9.228   46.775 1.00 31.45  ? 128 ALA   A C   1 
ATOM   843  O  O   . ALA   A  1  115 ? 49.938  8.823   47.762 1.00 33.97  ? 128 ALA   A O   1 
ATOM   844  C  CB  . ALA   A  1  115 ? 52.674  8.531   47.902 1.00 30.95  ? 128 ALA   A CB  1 
ATOM   845  N  N   . GLY   A  1  116 ? 49.941  9.860   45.770 1.00 30.21  ? 129 GLY   A N   1 
ATOM   846  C  CA  . GLY   A  1  116 ? 48.591  10.393  45.872 1.00 31.32  ? 129 GLY   A CA  1 
ATOM   847  C  C   . GLY   A  1  116 ? 47.550  9.409   45.365 1.00 29.02  ? 129 GLY   A C   1 
ATOM   848  O  O   . GLY   A  1  116 ? 46.375  9.703   45.426 1.00 29.98  ? 129 GLY   A O   1 
ATOM   849  N  N   . GLY   A  1  117 ? 48.005  8.253   44.873 1.00 29.92  ? 130 GLY   A N   1 
ATOM   850  C  CA  . GLY   A  1  117 ? 47.133  7.142   44.545 1.00 28.53  ? 130 GLY   A CA  1 
ATOM   851  C  C   . GLY   A  1  117 ? 46.727  7.168   43.083 1.00 28.34  ? 130 GLY   A C   1 
ATOM   852  O  O   . GLY   A  1  117 ? 47.097  8.081   42.354 1.00 28.14  ? 130 GLY   A O   1 
ATOM   853  N  N   . LEU   A  1  118 ? 45.936  6.164   42.678 1.00 29.62  ? 131 LEU   A N   1 
ATOM   854  C  CA  . LEU   A  1  118 ? 45.555  5.997   41.287 1.00 31.13  ? 131 LEU   A CA  1 
ATOM   855  C  C   . LEU   A  1  118 ? 44.644  7.124   40.797 1.00 31.28  ? 131 LEU   A C   1 
ATOM   856  O  O   . LEU   A  1  118 ? 44.455  7.242   39.586 1.00 28.91  ? 131 LEU   A O   1 
ATOM   857  C  CB  . LEU   A  1  118 ? 44.869  4.647   41.106 1.00 35.03  ? 131 LEU   A CB  1 
ATOM   858  C  CG  . LEU   A  1  118 ? 45.712  3.410   41.411 1.00 35.70  ? 131 LEU   A CG  1 
ATOM   859  C  CD1 . LEU   A  1  118 ? 44.877  2.177   41.157 1.00 37.33  ? 131 LEU   A CD1 1 
ATOM   860  C  CD2 . LEU   A  1  118 ? 46.993  3.385   40.605 1.00 35.16  ? 131 LEU   A CD2 1 
ATOM   861  N  N   . ASN   A  1  119 ? 44.063  7.914   41.715 1.00 29.93  ? 132 ASN   A N   1 
ATOM   862  C  CA  . ASN   A  1  119 ? 43.257  9.062   41.325 1.00 31.28  ? 132 ASN   A CA  1 
ATOM   863  C  C   . ASN   A  1  119 ? 44.060  10.145  40.625 1.00 28.91  ? 132 ASN   A C   1 
ATOM   864  O  O   . ASN   A  1  119 ? 43.483  10.877  39.848 1.00 33.73  ? 132 ASN   A O   1 
ATOM   865  C  CB  . ASN   A  1  119 ? 42.588  9.756   42.497 1.00 30.90  ? 132 ASN   A CB  1 
ATOM   866  C  CG  . ASN   A  1  119 ? 41.393  9.006   43.005 1.00 33.63  ? 132 ASN   A CG  1 
ATOM   867  O  OD1 . ASN   A  1  119 ? 41.052  7.940   42.488 1.00 33.88  ? 132 ASN   A OD1 1 
ATOM   868  N  ND2 . ASN   A  1  119 ? 40.755  9.545   44.024 1.00 39.03  ? 132 ASN   A ND2 1 
ATOM   869  N  N   . VAL   A  1  120 ? 45.372  10.222  40.862 1.00 31.20  ? 133 VAL   A N   1 
ATOM   870  C  CA  . VAL   A  1  120 ? 46.182  11.289  40.293 1.00 30.99  ? 133 VAL   A CA  1 
ATOM   871  C  C   . VAL   A  1  120 ? 46.125  11.278  38.766 1.00 32.63  ? 133 VAL   A C   1 
ATOM   872  O  O   . VAL   A  1  120 ? 46.463  10.290  38.141 1.00 34.72  ? 133 VAL   A O   1 
ATOM   873  C  CB  . VAL   A  1  120 ? 47.628  11.230  40.800 1.00 32.21  ? 133 VAL   A CB  1 
ATOM   874  C  CG1 . VAL   A  1  120 ? 48.540  12.218  40.052 1.00 33.13  ? 133 VAL   A CG1 1 
ATOM   875  C  CG2 . VAL   A  1  120 ? 47.683  11.443  42.317 1.00 30.37  ? 133 VAL   A CG2 1 
ATOM   876  N  N   . HIS   A  1  121 ? 45.774  12.433  38.184 1.00 36.56  ? 134 HIS   A N   1 
ATOM   877  C  CA  . HIS   A  1  121 ? 45.508  12.577  36.754 1.00 37.85  ? 134 HIS   A CA  1 
ATOM   878  C  C   . HIS   A  1  121 ? 46.773  12.889  35.966 1.00 36.24  ? 134 HIS   A C   1 
ATOM   879  O  O   . HIS   A  1  121 ? 47.647  13.574  36.463 1.00 34.65  ? 134 HIS   A O   1 
ATOM   880  C  CB  . HIS   A  1  121 ? 44.532  13.741  36.526 1.00 40.43  ? 134 HIS   A CB  1 
ATOM   881  C  CG  . HIS   A  1  121 ? 44.267  14.055  35.098 1.00 45.87  ? 134 HIS   A CG  1 
ATOM   882  N  ND1 . HIS   A  1  121 ? 43.603  13.191  34.247 1.00 43.79  ? 134 HIS   A ND1 1 
ATOM   883  C  CD2 . HIS   A  1  121 ? 44.625  15.127  34.353 1.00 44.29  ? 134 HIS   A CD2 1 
ATOM   884  C  CE1 . HIS   A  1  121 ? 43.528  13.750  33.038 1.00 41.64  ? 134 HIS   A CE1 1 
ATOM   885  N  NE2 . HIS   A  1  121 ? 44.137  14.922  33.085 1.00 39.35  ? 134 HIS   A NE2 1 
ATOM   886  N  N   . GLY   A  1  122 ? 46.865  12.383  34.731 1.00 42.62  ? 135 GLY   A N   1 
ATOM   887  C  CA  . GLY   A  1  122 ? 47.702  13.023  33.732 1.00 43.83  ? 135 GLY   A CA  1 
ATOM   888  C  C   . GLY   A  1  122 ? 48.869  12.182  33.229 1.00 42.87  ? 135 GLY   A C   1 
ATOM   889  O  O   . GLY   A  1  122 ? 49.370  12.476  32.150 1.00 42.99  ? 135 GLY   A O   1 
ATOM   890  N  N   . THR   A  1  123 ? 49.365  11.216  34.012 1.00 42.21  ? 136 THR   A N   1 
ATOM   891  C  CA  A THR   A  1  123 ? 50.456  10.359  33.572 0.50 45.49  ? 136 THR   A CA  1 
ATOM   892  C  CA  B THR   A  1  123 ? 50.448  10.359  33.527 0.50 42.16  ? 136 THR   A CA  1 
ATOM   893  C  C   . THR   A  1  123 ? 49.975  8.905   33.468 1.00 40.78  ? 136 THR   A C   1 
ATOM   894  O  O   . THR   A  1  123 ? 50.322  8.203   32.531 1.00 41.84  ? 136 THR   A O   1 
ATOM   895  C  CB  A THR   A  1  123 ? 51.625  10.530  34.545 0.50 51.96  ? 136 THR   A CB  1 
ATOM   896  C  CB  B THR   A  1  123 ? 51.742  10.524  34.334 0.50 44.27  ? 136 THR   A CB  1 
ATOM   897  O  OG1 A THR   A  1  123 ? 51.136  10.103  35.815 0.50 61.55  ? 136 THR   A OG1 1 
ATOM   898  O  OG1 B THR   A  1  123 ? 52.771  9.752   33.713 0.50 35.98  ? 136 THR   A OG1 1 
ATOM   899  C  CG2 A THR   A  1  123 ? 52.096  11.970  34.679 0.50 48.47  ? 136 THR   A CG2 1 
ATOM   900  C  CG2 B THR   A  1  123 ? 51.613  10.066  35.774 0.50 48.50  ? 136 THR   A CG2 1 
ATOM   901  N  N   . PHE   A  1  124 ? 49.174  8.449   34.449 1.00 39.31  ? 137 PHE   A N   1 
ATOM   902  C  CA  . PHE   A  1  124 ? 48.511  7.153   34.374 1.00 37.43  ? 137 PHE   A CA  1 
ATOM   903  C  C   . PHE   A  1  124 ? 47.019  7.332   34.071 1.00 41.80  ? 137 PHE   A C   1 
ATOM   904  O  O   . PHE   A  1  124 ? 46.619  7.153   32.922 1.00 43.99  ? 137 PHE   A O   1 
ATOM   905  C  CB  . PHE   A  1  124 ? 48.743  6.318   35.635 1.00 39.25  ? 137 PHE   A CB  1 
ATOM   906  C  CG  . PHE   A  1  124 ? 48.368  4.839   35.564 1.00 39.55  ? 137 PHE   A CG  1 
ATOM   907  C  CD1 . PHE   A  1  124 ? 47.664  4.299   34.492 1.00 41.57  ? 137 PHE   A CD1 1 
ATOM   908  C  CD2 . PHE   A  1  124 ? 48.738  3.973   36.588 1.00 40.34  ? 137 PHE   A CD2 1 
ATOM   909  C  CE1 . PHE   A  1  124 ? 47.345  2.948   34.459 1.00 38.67  ? 137 PHE   A CE1 1 
ATOM   910  C  CE2 . PHE   A  1  124 ? 48.415  2.621   36.546 1.00 36.86  ? 137 PHE   A CE2 1 
ATOM   911  C  CZ  . PHE   A  1  124 ? 47.725  2.113   35.480 1.00 36.86  ? 137 PHE   A CZ  1 
ATOM   912  N  N   . GLU   A  1  125 ? 46.184  7.599   35.096 1.00 40.24  ? 138 GLU   A N   1 
ATOM   913  C  CA  . GLU   A  1  125 ? 44.761  7.862   34.898 1.00 37.23  ? 138 GLU   A CA  1 
ATOM   914  C  C   . GLU   A  1  125 ? 44.585  8.977   33.865 1.00 34.72  ? 138 GLU   A C   1 
ATOM   915  O  O   . GLU   A  1  125 ? 45.348  9.933   33.825 1.00 40.99  ? 138 GLU   A O   1 
ATOM   916  C  CB  . GLU   A  1  125 ? 44.119  8.250   36.230 1.00 38.80  ? 138 GLU   A CB  1 
ATOM   917  C  CG  . GLU   A  1  125 ? 42.605  8.450   36.215 1.00 42.79  ? 138 GLU   A CG  1 
ATOM   918  C  CD  . GLU   A  1  125 ? 42.050  9.678   35.482 1.00 44.64  ? 138 GLU   A CD  1 
ATOM   919  O  OE1 . GLU   A  1  125 ? 42.601  10.785  35.697 1.00 43.07  ? 138 GLU   A OE1 1 
ATOM   920  O  OE2 . GLU   A  1  125 ? 41.068  9.517   34.696 1.00 39.80  ? 138 GLU   A OE2 1 
ATOM   921  N  N   . GLY   A  1  126 ? 43.582  8.844   33.006 1.00 32.70  ? 139 GLY   A N   1 
ATOM   922  C  CA  . GLY   A  1  126 ? 43.288  9.837   31.984 1.00 32.72  ? 139 GLY   A CA  1 
ATOM   923  C  C   . GLY   A  1  126 ? 41.871  9.699   31.418 1.00 31.84  ? 139 GLY   A C   1 
ATOM   924  O  O   . GLY   A  1  126 ? 40.999  9.095   32.041 1.00 33.95  ? 139 GLY   A O   1 
ATOM   925  N  N   . ASP   A  1  127 ? 41.690  10.207  30.190 1.00 35.54  ? 140 ASP   A N   1 
ATOM   926  C  CA  . ASP   A  1  127 ? 40.395  10.662  29.712 1.00 35.12  ? 140 ASP   A CA  1 
ATOM   927  C  C   . ASP   A  1  127 ? 39.712  9.602   28.850 1.00 30.00  ? 140 ASP   A C   1 
ATOM   928  O  O   . ASP   A  1  127 ? 40.329  8.657   28.385 1.00 32.96  ? 140 ASP   A O   1 
ATOM   929  C  CB  . ASP   A  1  127 ? 40.539  11.962  28.934 1.00 38.17  ? 140 ASP   A CB  1 
ATOM   930  C  CG  . ASP   A  1  127 ? 41.179  13.128  29.670 1.00 45.31  ? 140 ASP   A CG  1 
ATOM   931  O  OD1 . ASP   A  1  127 ? 40.898  13.286  30.876 1.00 44.43  ? 140 ASP   A OD1 1 
ATOM   932  O  OD2 . ASP   A  1  127 ? 41.947  13.885  29.017 1.00 54.36  ? 140 ASP   A OD2 1 
ATOM   933  N  N   . ALA   A  1  128 ? 38.421  9.810   28.603 1.00 30.39  ? 141 ALA   A N   1 
ATOM   934  C  CA  . ALA   A  1  128 ? 37.644  8.963   27.700 1.00 33.82  ? 141 ALA   A CA  1 
ATOM   935  C  C   . ALA   A  1  128 ? 37.404  7.582   28.305 1.00 31.08  ? 141 ALA   A C   1 
ATOM   936  O  O   . ALA   A  1  128 ? 37.334  6.595   27.596 1.00 33.70  ? 141 ALA   A O   1 
ATOM   937  C  CB  . ALA   A  1  128 ? 38.306  8.865   26.336 1.00 31.61  ? 141 ALA   A CB  1 
ATOM   938  N  N   . GLY   A  1  129 ? 37.224  7.525   29.622 1.00 29.99  ? 142 GLY   A N   1 
ATOM   939  C  CA  . GLY   A  1  129 ? 36.856  6.281   30.272 1.00 32.01  ? 142 GLY   A CA  1 
ATOM   940  C  C   . GLY   A  1  129 ? 35.405  5.909   29.986 1.00 32.86  ? 142 GLY   A C   1 
ATOM   941  O  O   . GLY   A  1  129 ? 34.658  6.715   29.450 1.00 39.47  ? 142 GLY   A O   1 
ATOM   942  N  N   . MET   A  1  130 ? 35.027  4.690   30.375 1.00 33.37  ? 143 MET   A N   1 
ATOM   943  C  CA  . MET   A  1  130 ? 33.715  4.140   30.093 1.00 32.17  ? 143 MET   A CA  1 
ATOM   944  C  C   . MET   A  1  130 ? 32.702  4.545   31.153 1.00 32.85  ? 143 MET   A C   1 
ATOM   945  O  O   . MET   A  1  130 ? 31.571  4.852   30.771 1.00 36.20  ? 143 MET   A O   1 
ATOM   946  C  CB  . MET   A  1  130 ? 33.749  2.610   30.054 1.00 37.32  ? 143 MET   A CB  1 
ATOM   947  C  CG  . MET   A  1  130 ? 34.482  2.029   28.849 1.00 41.21  ? 143 MET   A CG  1 
ATOM   948  S  SD  . MET   A  1  130 ? 34.618  0.228   28.940 1.00 42.86  ? 143 MET   A SD  1 
ATOM   949  C  CE  . MET   A  1  130 ? 35.737  -0.010  30.320 1.00 36.78  ? 143 MET   A CE  1 
ATOM   950  N  N   . THR   A  1  131 ? 33.073  4.492   32.453 1.00 29.64  ? 144 THR   A N   1 
ATOM   951  C  CA  . THR   A  1  131 ? 32.121  4.803   33.510 1.00 28.68  ? 144 THR   A CA  1 
ATOM   952  C  C   . THR   A  1  131 ? 32.589  5.938   34.414 1.00 30.48  ? 144 THR   A C   1 
ATOM   953  O  O   . THR   A  1  131 ? 31.889  6.282   35.367 1.00 33.72  ? 144 THR   A O   1 
ATOM   954  C  CB  . THR   A  1  131 ? 31.783  3.562   34.332 1.00 30.70  ? 144 THR   A CB  1 
ATOM   955  O  OG1 . THR   A  1  131 ? 32.894  3.245   35.162 1.00 27.99  ? 144 THR   A OG1 1 
ATOM   956  C  CG2 . THR   A  1  131 ? 31.378  2.400   33.437 1.00 32.43  ? 144 THR   A CG2 1 
ATOM   957  N  N   . ARG   A  1  132 ? 33.743  6.528   34.111 1.00 31.47  ? 145 ARG   A N   1 
ATOM   958  C  CA  . ARG   A  1  132 ? 34.262  7.663   34.853 1.00 31.89  ? 145 ARG   A CA  1 
ATOM   959  C  C   . ARG   A  1  132 ? 34.445  8.841   33.898 1.00 32.83  ? 145 ARG   A C   1 
ATOM   960  O  O   . ARG   A  1  132 ? 34.838  8.636   32.759 1.00 31.40  ? 145 ARG   A O   1 
ATOM   961  C  CB  . ARG   A  1  132 ? 35.585  7.291   35.534 1.00 34.38  ? 145 ARG   A CB  1 
ATOM   962  C  CG  . ARG   A  1  132 ? 35.466  6.671   36.923 1.00 35.57  ? 145 ARG   A CG  1 
ATOM   963  C  CD  . ARG   A  1  132 ? 34.944  5.245   36.967 1.00 34.92  ? 145 ARG   A CD  1 
ATOM   964  N  NE  . ARG   A  1  132 ? 34.801  4.841   38.371 1.00 37.61  ? 145 ARG   A NE  1 
ATOM   965  C  CZ  . ARG   A  1  132 ? 34.041  3.867   38.874 1.00 36.81  ? 145 ARG   A CZ  1 
ATOM   966  N  NH1 . ARG   A  1  132 ? 33.951  3.792   40.210 1.00 36.04  ? 145 ARG   A NH1 1 
ATOM   967  N  NH2 . ARG   A  1  132 ? 33.339  3.045   38.083 1.00 31.55  ? 145 ARG   A NH2 1 
ATOM   968  N  N   . ALA   A  1  133 ? 34.141  10.058  34.378 1.00 33.84  ? 146 ALA   A N   1 
ATOM   969  C  CA  . ALA   A  1  133 ? 34.197  11.289  33.605 1.00 29.06  ? 146 ALA   A CA  1 
ATOM   970  C  C   . ALA   A  1  133 ? 35.634  11.802  33.624 1.00 29.71  ? 146 ALA   A C   1 
ATOM   971  O  O   . ALA   A  1  133 ? 36.358  11.573  34.586 1.00 25.27  ? 146 ALA   A O   1 
ATOM   972  N  N   . ASP   A  1  134 ? 36.015  12.542  32.570 1.00 30.78  ? 147 ASP   A N   1 
ATOM   973  C  CA  . ASP   A  1  134 ? 37.315  13.191  32.488 1.00 32.28  ? 147 ASP   A CA  1 
ATOM   974  C  C   . ASP   A  1  134 ? 37.530  14.103  33.696 1.00 33.44  ? 147 ASP   A C   1 
ATOM   975  O  O   . ASP   A  1  134 ? 36.581  14.694  34.212 1.00 35.96  ? 147 ASP   A O   1 
ATOM   976  C  CB  . ASP   A  1  134 ? 37.474  13.971  31.193 1.00 31.41  ? 147 ASP   A CB  1 
ATOM   977  C  CG  . ASP   A  1  134 ? 37.373  13.160  29.912 1.00 34.02  ? 147 ASP   A CG  1 
ATOM   978  O  OD1 . ASP   A  1  134 ? 37.116  11.934  30.001 1.00 35.92  ? 147 ASP   A OD1 1 
ATOM   979  O  OD2 . ASP   A  1  134 ? 37.580  13.755  28.831 1.00 32.71  ? 147 ASP   A OD2 1 
ATOM   980  N  N   . GLU   A  1  135 ? 38.795  14.237  34.104 1.00 33.04  ? 148 GLU   A N   1 
ATOM   981  C  CA  . GLU   A  1  135 ? 39.190  15.015  35.273 1.00 38.90  ? 148 GLU   A CA  1 
ATOM   982  C  C   . GLU   A  1  135 ? 38.818  16.488  35.112 1.00 39.77  ? 148 GLU   A C   1 
ATOM   983  O  O   . GLU   A  1  135 ? 38.530  17.172  36.097 1.00 41.21  ? 148 GLU   A O   1 
ATOM   984  C  CB  . GLU   A  1  135 ? 40.698  14.872  35.488 1.00 43.73  ? 148 GLU   A CB  1 
ATOM   985  C  CG  . GLU   A  1  135 ? 41.229  15.563  36.744 1.00 54.67  ? 148 GLU   A CG  1 
ATOM   986  C  CD  . GLU   A  1  135 ? 41.721  17.000  36.590 1.00 65.63  ? 148 GLU   A CD  1 
ATOM   987  O  OE1 . GLU   A  1  135 ? 41.841  17.528  35.459 1.00 69.82  ? 148 GLU   A OE1 1 
ATOM   988  O  OE2 . GLU   A  1  135 ? 42.002  17.600  37.651 1.00 77.40  ? 148 GLU   A OE2 1 
ATOM   989  N  N   . PHE   A  1  136 ? 38.857  16.983  33.873 1.00 38.20  ? 149 PHE   A N   1 
ATOM   990  C  CA  . PHE   A  1  136 ? 38.487  18.355  33.583 1.00 42.31  ? 149 PHE   A CA  1 
ATOM   991  C  C   . PHE   A  1  136 ? 37.109  18.697  34.161 1.00 40.74  ? 149 PHE   A C   1 
ATOM   992  O  O   . PHE   A  1  136 ? 36.889  19.823  34.581 1.00 39.66  ? 149 PHE   A O   1 
ATOM   993  C  CB  . PHE   A  1  136 ? 38.487  18.602  32.072 1.00 47.76  ? 149 PHE   A CB  1 
ATOM   994  C  CG  . PHE   A  1  136 ? 38.032  20.014  31.723 1.00 55.27  ? 149 PHE   A CG  1 
ATOM   995  C  CD1 . PHE   A  1  136 ? 38.874  21.106  31.946 1.00 53.79  ? 149 PHE   A CD1 1 
ATOM   996  C  CD2 . PHE   A  1  136 ? 36.760  20.244  31.205 1.00 54.27  ? 149 PHE   A CD2 1 
ATOM   997  C  CE1 . PHE   A  1  136 ? 38.453  22.387  31.651 1.00 47.75  ? 149 PHE   A CE1 1 
ATOM   998  C  CE2 . PHE   A  1  136 ? 36.349  21.531  30.908 1.00 53.35  ? 149 PHE   A CE2 1 
ATOM   999  C  CZ  . PHE   A  1  136 ? 37.193  22.595  31.139 1.00 51.06  ? 149 PHE   A CZ  1 
ATOM   1000 N  N   . PHE   A  1  137 ? 36.182  17.736  34.197 1.00 38.70  ? 150 PHE   A N   1 
ATOM   1001 C  CA  . PHE   A  1  137 ? 34.822  18.006  34.638 1.00 39.90  ? 150 PHE   A CA  1 
ATOM   1002 C  C   . PHE   A  1  137 ? 34.692  17.933  36.161 1.00 36.52  ? 150 PHE   A C   1 
ATOM   1003 O  O   . PHE   A  1  137 ? 33.624  18.206  36.671 1.00 35.96  ? 150 PHE   A O   1 
ATOM   1004 C  CB  . PHE   A  1  137 ? 33.860  17.042  33.932 1.00 42.46  ? 150 PHE   A CB  1 
ATOM   1005 C  CG  . PHE   A  1  137 ? 33.939  17.098  32.412 1.00 46.90  ? 150 PHE   A CG  1 
ATOM   1006 C  CD1 . PHE   A  1  137 ? 33.823  18.311  31.734 1.00 51.80  ? 150 PHE   A CD1 1 
ATOM   1007 C  CD2 . PHE   A  1  137 ? 34.163  15.951  31.662 1.00 49.12  ? 150 PHE   A CD2 1 
ATOM   1008 C  CE1 . PHE   A  1  137 ? 33.895  18.362  30.347 1.00 50.30  ? 150 PHE   A CE1 1 
ATOM   1009 C  CE2 . PHE   A  1  137 ? 34.248  16.007  30.273 1.00 49.53  ? 150 PHE   A CE2 1 
ATOM   1010 C  CZ  . PHE   A  1  137 ? 34.103  17.208  29.619 1.00 51.02  ? 150 PHE   A CZ  1 
ATOM   1011 N  N   . GLY   A  1  138 ? 35.760  17.592  36.891 1.00 39.18  ? 151 GLY   A N   1 
ATOM   1012 C  CA  . GLY   A  1  138 ? 35.783  17.731  38.342 1.00 41.52  ? 151 GLY   A CA  1 
ATOM   1013 C  C   . GLY   A  1  138 ? 35.886  16.411  39.124 1.00 47.29  ? 151 GLY   A C   1 
ATOM   1014 O  O   . GLY   A  1  138 ? 36.073  16.459  40.337 1.00 46.65  ? 151 GLY   A O   1 
ATOM   1015 N  N   . ASP   A  1  139 ? 35.705  15.242  38.479 1.00 44.51  ? 152 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A  1  139 ? 35.649  13.985  39.217 1.00 43.03  ? 152 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A  1  139 ? 36.025  12.829  38.294 1.00 37.03  ? 152 ASP   A C   1 
ATOM   1018 O  O   . ASP   A  1  139 ? 35.222  12.392  37.460 1.00 34.04  ? 152 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A  1  139 ? 34.291  13.762  39.881 1.00 46.96  ? 152 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A  1  139 ? 34.182  12.509  40.745 1.00 51.63  ? 152 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A  1  139 ? 35.067  11.634  40.616 1.00 49.44  ? 152 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A  1  139 ? 33.247  12.432  41.575 1.00 55.90  ? 152 ASP   A OD2 1 
ATOM   1023 N  N   . ASN   A  1  140 ? 37.245  12.324  38.472 1.00 34.39  ? 153 ASN   A N   1 
ATOM   1024 C  CA  . ASN   A  1  140 ? 37.806  11.333  37.568 1.00 35.42  ? 153 ASN   A CA  1 
ATOM   1025 C  C   . ASN   A  1  140 ? 37.705  9.926   38.167 1.00 35.68  ? 153 ASN   A C   1 
ATOM   1026 O  O   . ASN   A  1  140 ? 38.209  8.982   37.565 1.00 33.33  ? 153 ASN   A O   1 
ATOM   1027 C  CB  . ASN   A  1  140 ? 39.256  11.647  37.225 1.00 31.62  ? 153 ASN   A CB  1 
ATOM   1028 C  CG  . ASN   A  1  140 ? 40.179  11.538  38.419 1.00 30.56  ? 153 ASN   A CG  1 
ATOM   1029 O  OD1 . ASN   A  1  140 ? 39.739  11.432  39.568 1.00 33.10  ? 153 ASN   A OD1 1 
ATOM   1030 N  ND2 . ASN   A  1  140 ? 41.475  11.553  38.178 1.00 32.98  ? 153 ASN   A ND2 1 
ATOM   1031 N  N   . HIS   A  1  141 ? 37.086  9.792   39.345 1.00 33.79  ? 154 HIS   A N   1 
ATOM   1032 C  CA  . HIS   A  1  141 ? 37.151  8.542   40.090 1.00 34.35  ? 154 HIS   A CA  1 
ATOM   1033 C  C   . HIS   A  1  141 ? 35.762  7.941   40.341 1.00 35.06  ? 154 HIS   A C   1 
ATOM   1034 O  O   . HIS   A  1  141 ? 35.648  6.722   40.435 1.00 33.35  ? 154 HIS   A O   1 
ATOM   1035 C  CB  . HIS   A  1  141 ? 37.950  8.697   41.388 1.00 30.67  ? 154 HIS   A CB  1 
ATOM   1036 C  CG  . HIS   A  1  141 ? 37.446  9.760   42.280 1.00 36.62  ? 154 HIS   A CG  1 
ATOM   1037 N  ND1 . HIS   A  1  141 ? 36.459  9.543   43.221 1.00 44.08  ? 154 HIS   A ND1 1 
ATOM   1038 C  CD2 . HIS   A  1  141 ? 37.781  11.074  42.358 1.00 38.70  ? 154 HIS   A CD2 1 
ATOM   1039 C  CE1 . HIS   A  1  141 ? 36.216  10.686  43.861 1.00 44.43  ? 154 HIS   A CE1 1 
ATOM   1040 N  NE2 . HIS   A  1  141 ? 37.022  11.624  43.364 1.00 44.25  ? 154 HIS   A NE2 1 
ATOM   1041 N  N   . SER   A  1  142 ? 34.724  8.778   40.481 1.00 32.81  ? 155 SER   A N   1 
ATOM   1042 C  CA  . SER   A  1  142 ? 33.398  8.295   40.829 1.00 34.56  ? 155 SER   A CA  1 
ATOM   1043 C  C   . SER   A  1  142 ? 32.719  7.659   39.622 1.00 33.06  ? 155 SER   A C   1 
ATOM   1044 O  O   . SER   A  1  142 ? 32.886  8.099   38.486 1.00 29.00  ? 155 SER   A O   1 
ATOM   1045 C  CB  . SER   A  1  142 ? 32.516  9.396   41.375 1.00 34.79  ? 155 SER   A CB  1 
ATOM   1046 O  OG  . SER   A  1  142 ? 32.952  9.765   42.677 1.00 42.85  ? 155 SER   A OG  1 
ATOM   1047 N  N   . PHE   A  1  143 ? 31.891  6.657   39.905 1.00 32.35  ? 156 PHE   A N   1 
ATOM   1048 C  CA  . PHE   A  1  143 ? 30.977  6.134   38.912 1.00 32.12  ? 156 PHE   A CA  1 
ATOM   1049 C  C   . PHE   A  1  143 ? 30.051  7.250   38.426 1.00 32.86  ? 156 PHE   A C   1 
ATOM   1050 O  O   . PHE   A  1  143 ? 29.567  8.036   39.226 1.00 32.53  ? 156 PHE   A O   1 
ATOM   1051 C  CB  . PHE   A  1  143 ? 30.185  4.985   39.536 1.00 30.06  ? 156 PHE   A CB  1 
ATOM   1052 C  CG  . PHE   A  1  143 ? 29.105  4.453   38.612 1.00 29.05  ? 156 PHE   A CG  1 
ATOM   1053 C  CD1 . PHE   A  1  143 ? 29.402  3.500   37.648 1.00 28.21  ? 156 PHE   A CD1 1 
ATOM   1054 C  CD2 . PHE   A  1  143 ? 27.802  4.925   38.702 1.00 27.28  ? 156 PHE   A CD2 1 
ATOM   1055 C  CE1 . PHE   A  1  143 ? 28.415  2.989   36.823 1.00 30.12  ? 156 PHE   A CE1 1 
ATOM   1056 C  CE2 . PHE   A  1  143 ? 26.821  4.426   37.858 1.00 27.85  ? 156 PHE   A CE2 1 
ATOM   1057 C  CZ  . PHE   A  1  143 ? 27.123  3.445   36.937 1.00 28.01  ? 156 PHE   A CZ  1 
ATOM   1058 N  N   . ASN   A  1  144 ? 29.799  7.270   37.114 1.00 33.06  ? 157 ASN   A N   1 
ATOM   1059 C  CA  . ASN   A  1  144 ? 28.991  8.287   36.479 1.00 31.99  ? 157 ASN   A CA  1 
ATOM   1060 C  C   . ASN   A  1  144 ? 27.826  7.633   35.744 1.00 27.35  ? 157 ASN   A C   1 
ATOM   1061 O  O   . ASN   A  1  144 ? 28.043  6.987   34.740 1.00 28.28  ? 157 ASN   A O   1 
ATOM   1062 C  CB  . ASN   A  1  144 ? 29.879  9.117   35.559 1.00 36.49  ? 157 ASN   A CB  1 
ATOM   1063 C  CG  . ASN   A  1  144 ? 29.124  10.200  34.825 1.00 36.74  ? 157 ASN   A CG  1 
ATOM   1064 O  OD1 . ASN   A  1  144 ? 28.172  9.889   34.091 1.00 35.00  ? 157 ASN   A OD1 1 
ATOM   1065 N  ND2 . ASN   A  1  144 ? 29.513  11.451  35.067 1.00 41.60  ? 157 ASN   A ND2 1 
ATOM   1066 N  N   . GLN   A  1  145 ? 26.594  7.851   36.215 1.00 29.76  ? 158 GLN   A N   1 
ATOM   1067 C  CA  . GLN   A  1  145 ? 25.423  7.143   35.713 1.00 31.04  ? 158 GLN   A CA  1 
ATOM   1068 C  C   . GLN   A  1  145 ? 25.172  7.489   34.242 1.00 31.45  ? 158 GLN   A C   1 
ATOM   1069 O  O   . GLN   A  1  145 ? 24.786  6.622   33.455 1.00 32.74  ? 158 GLN   A O   1 
ATOM   1070 C  CB  . GLN   A  1  145 ? 24.196  7.437   36.582 1.00 31.52  ? 158 GLN   A CB  1 
ATOM   1071 C  CG  . GLN   A  1  145 ? 22.942  6.630   36.237 1.00 32.00  ? 158 GLN   A CG  1 
ATOM   1072 C  CD  . GLN   A  1  145 ? 23.112  5.122   36.342 1.00 35.05  ? 158 GLN   A CD  1 
ATOM   1073 O  OE1 . GLN   A  1  145 ? 23.498  4.568   37.376 1.00 35.54  ? 158 GLN   A OE1 1 
ATOM   1074 N  NE2 . GLN   A  1  145 ? 22.802  4.419   35.267 1.00 36.31  ? 158 GLN   A NE2 1 
ATOM   1075 N  N   . THR   A  1  146 ? 25.382  8.752   33.870 1.00 31.10  ? 159 THR   A N   1 
ATOM   1076 C  CA  . THR   A  1  146 ? 25.178  9.180   32.497 1.00 34.10  ? 159 THR   A CA  1 
ATOM   1077 C  C   . THR   A  1  146 ? 26.100  8.395   31.568 1.00 33.61  ? 159 THR   A C   1 
ATOM   1078 O  O   . THR   A  1  146 ? 25.690  8.037   30.471 1.00 35.44  ? 159 THR   A O   1 
ATOM   1079 C  CB  . THR   A  1  146 ? 25.437  10.681  32.329 1.00 36.73  ? 159 THR   A CB  1 
ATOM   1080 O  OG1 . THR   A  1  146 ? 24.483  11.389  33.100 1.00 40.05  ? 159 THR   A OG1 1 
ATOM   1081 C  CG2 . THR   A  1  146 ? 25.274  11.173  30.904 1.00 36.34  ? 159 THR   A CG2 1 
ATOM   1082 N  N   . LEU   A  1  147 ? 27.351  8.178   31.988 1.00 32.04  ? 160 LEU   A N   1 
ATOM   1083 C  CA  . LEU   A  1  147 ? 28.287  7.421   31.163 1.00 31.52  ? 160 LEU   A CA  1 
ATOM   1084 C  C   . LEU   A  1  147 ? 27.896  5.945   31.097 1.00 30.76  ? 160 LEU   A C   1 
ATOM   1085 O  O   . LEU   A  1  147 ? 27.994  5.320   30.040 1.00 29.91  ? 160 LEU   A O   1 
ATOM   1086 C  CB  . LEU   A  1  147 ? 29.699  7.642   31.698 1.00 31.05  ? 160 LEU   A CB  1 
ATOM   1087 C  CG  . LEU   A  1  147 ? 30.320  9.005   31.369 1.00 30.49  ? 160 LEU   A CG  1 
ATOM   1088 C  CD1 . LEU   A  1  147 ? 31.754  9.082   31.837 1.00 31.57  ? 160 LEU   A CD1 1 
ATOM   1089 C  CD2 . LEU   A  1  147 ? 30.280  9.317   29.892 1.00 30.46  ? 160 LEU   A CD2 1 
ATOM   1090 N  N   . PHE   A  1  148 ? 27.423  5.397   32.221 1.00 28.84  ? 161 PHE   A N   1 
ATOM   1091 C  CA  . PHE   A  1  148 ? 26.956  4.025   32.229 1.00 28.91  ? 161 PHE   A CA  1 
ATOM   1092 C  C   . PHE   A  1  148 ? 25.718  3.887   31.338 1.00 31.41  ? 161 PHE   A C   1 
ATOM   1093 O  O   . PHE   A  1  148 ? 25.551  2.858   30.698 1.00 32.39  ? 161 PHE   A O   1 
ATOM   1094 C  CB  . PHE   A  1  148 ? 26.676  3.551   33.661 1.00 28.21  ? 161 PHE   A CB  1 
ATOM   1095 C  CG  . PHE   A  1  148 ? 26.322  2.077   33.718 1.00 25.99  ? 161 PHE   A CG  1 
ATOM   1096 C  CD1 . PHE   A  1  148 ? 27.308  1.123   33.509 1.00 27.82  ? 161 PHE   A CD1 1 
ATOM   1097 C  CD2 . PHE   A  1  148 ? 25.016  1.656   33.916 1.00 25.15  ? 161 PHE   A CD2 1 
ATOM   1098 C  CE1 . PHE   A  1  148 ? 27.008  -0.224  33.506 1.00 27.28  ? 161 PHE   A CE1 1 
ATOM   1099 C  CE2 . PHE   A  1  148 ? 24.706  0.309   33.914 1.00 26.69  ? 161 PHE   A CE2 1 
ATOM   1100 C  CZ  . PHE   A  1  148 ? 25.714  -0.630  33.727 1.00 31.33  ? 161 PHE   A CZ  1 
ATOM   1101 N  N   . ASP   A  1  149 ? 24.848  4.901   31.300 1.00 30.15  ? 162 ASP   A N   1 
ATOM   1102 C  CA  . ASP   A  1  149 ? 23.681  4.861   30.432 1.00 33.83  ? 162 ASP   A CA  1 
ATOM   1103 C  C   . ASP   A  1  149 ? 24.111  4.741   28.967 1.00 30.20  ? 162 ASP   A C   1 
ATOM   1104 O  O   . ASP   A  1  149 ? 23.463  4.068   28.181 1.00 32.61  ? 162 ASP   A O   1 
ATOM   1105 C  CB  . ASP   A  1  149 ? 22.779  6.072   30.661 1.00 35.54  ? 162 ASP   A CB  1 
ATOM   1106 C  CG  . ASP   A  1  149 ? 22.047  6.107   31.996 1.00 37.37  ? 162 ASP   A CG  1 
ATOM   1107 O  OD1 . ASP   A  1  149 ? 21.841  5.021   32.587 1.00 37.75  ? 162 ASP   A OD1 1 
ATOM   1108 O  OD2 . ASP   A  1  149 ? 21.697  7.227   32.435 1.00 41.90  ? 162 ASP   A OD2 1 
ATOM   1109 N  N   . LYS   A  1  150 ? 25.195  5.416   28.598 1.00 32.35  ? 163 LYS   A N   1 
ATOM   1110 C  CA  . LYS   A  1  150 ? 25.735  5.325   27.250 1.00 35.09  ? 163 LYS   A CA  1 
ATOM   1111 C  C   . LYS   A  1  150 ? 26.336  3.943   26.997 1.00 32.02  ? 163 LYS   A C   1 
ATOM   1112 O  O   . LYS   A  1  150 ? 26.221  3.416   25.901 1.00 30.76  ? 163 LYS   A O   1 
ATOM   1113 C  CB  . LYS   A  1  150 ? 26.759  6.440   27.028 1.00 34.42  ? 163 LYS   A CB  1 
ATOM   1114 C  CG  . LYS   A  1  150 ? 27.405  6.428   25.668 1.00 36.35  ? 163 LYS   A CG  1 
ATOM   1115 C  CD  . LYS   A  1  150 ? 28.449  7.525   25.568 1.00 39.93  ? 163 LYS   A CD  1 
ATOM   1116 C  CE  . LYS   A  1  150 ? 29.181  7.518   24.253 1.00 42.64  ? 163 LYS   A CE  1 
ATOM   1117 N  NZ  . LYS   A  1  150 ? 28.850  8.706   23.472 1.00 40.66  ? 163 LYS   A NZ  1 
ATOM   1118 N  N   . PHE   A  1  151 ? 26.963  3.360   28.018 1.00 31.78  ? 164 PHE   A N   1 
ATOM   1119 C  CA  . PHE   A  1  151 ? 27.447  1.989   27.938 1.00 32.39  ? 164 PHE   A CA  1 
ATOM   1120 C  C   . PHE   A  1  151 ? 26.284  1.055   27.624 1.00 33.46  ? 164 PHE   A C   1 
ATOM   1121 O  O   . PHE   A  1  151 ? 26.402  0.179   26.768 1.00 31.51  ? 164 PHE   A O   1 
ATOM   1122 C  CB  . PHE   A  1  151 ? 28.137  1.656   29.264 1.00 31.98  ? 164 PHE   A CB  1 
ATOM   1123 C  CG  . PHE   A  1  151 ? 28.683  0.248   29.412 1.00 31.42  ? 164 PHE   A CG  1 
ATOM   1124 C  CD1 . PHE   A  1  151 ? 27.891  -0.775  29.916 1.00 32.33  ? 164 PHE   A CD1 1 
ATOM   1125 C  CD2 . PHE   A  1  151 ? 30.020  -0.020  29.139 1.00 32.41  ? 164 PHE   A CD2 1 
ATOM   1126 C  CE1 . PHE   A  1  151 ? 28.406  -2.051  30.077 1.00 33.20  ? 164 PHE   A CE1 1 
ATOM   1127 C  CE2 . PHE   A  1  151 ? 30.541  -1.295  29.309 1.00 31.38  ? 164 PHE   A CE2 1 
ATOM   1128 C  CZ  . PHE   A  1  151 ? 29.730  -2.311  29.767 1.00 33.00  ? 164 PHE   A CZ  1 
ATOM   1129 N  N   . VAL   A  1  152 ? 25.155  1.262   28.313 1.00 33.20  ? 165 VAL   A N   1 
ATOM   1130 C  CA  . VAL   A  1  152 ? 23.969  0.441   28.133 1.00 34.78  ? 165 VAL   A CA  1 
ATOM   1131 C  C   . VAL   A  1  152 ? 23.436  0.656   26.717 1.00 31.50  ? 165 VAL   A C   1 
ATOM   1132 O  O   . VAL   A  1  152 ? 23.112  -0.296  26.008 1.00 28.20  ? 165 VAL   A O   1 
ATOM   1133 C  CB  . VAL   A  1  152 ? 22.886  0.743   29.192 1.00 34.99  ? 165 VAL   A CB  1 
ATOM   1134 C  CG1 . VAL   A  1  152 ? 21.562  0.074   28.867 1.00 37.68  ? 165 VAL   A CG1 1 
ATOM   1135 C  CG2 . VAL   A  1  152 ? 23.311  0.348   30.593 1.00 32.83  ? 165 VAL   A CG2 1 
ATOM   1136 N  N   . ASP   A  1  153 ? 23.360  1.920   26.313 1.00 31.67  ? 166 ASP   A N   1 
ATOM   1137 C  CA  . ASP   A  1  153 ? 22.835  2.276   25.005 1.00 35.29  ? 166 ASP   A CA  1 
ATOM   1138 C  C   . ASP   A  1  153 ? 23.635  1.572   23.909 1.00 36.47  ? 166 ASP   A C   1 
ATOM   1139 O  O   . ASP   A  1  153 ? 23.060  0.956   23.015 1.00 35.54  ? 166 ASP   A O   1 
ATOM   1140 C  CB  . ASP   A  1  153 ? 22.781  3.783   24.809 1.00 38.82  ? 166 ASP   A CB  1 
ATOM   1141 C  CG  . ASP   A  1  153 ? 22.197  4.267   23.483 1.00 44.03  ? 166 ASP   A CG  1 
ATOM   1142 O  OD1 . ASP   A  1  153 ? 21.088  3.807   23.108 1.00 46.05  ? 166 ASP   A OD1 1 
ATOM   1143 O  OD2 . ASP   A  1  153 ? 22.852  5.108   22.831 1.00 40.03  ? 166 ASP   A OD2 1 
ATOM   1144 N  N   . PHE   A  1  154 ? 24.962  1.669   23.977 1.00 33.43  ? 167 PHE   A N   1 
ATOM   1145 C  CA  . PHE   A  1  154 ? 25.799  1.079   22.948 1.00 34.64  ? 167 PHE   A CA  1 
ATOM   1146 C  C   . PHE   A  1  154 ? 25.709  -0.438  22.985 1.00 32.22  ? 167 PHE   A C   1 
ATOM   1147 O  O   . PHE   A  1  154 ? 25.814  -1.070  21.945 1.00 28.87  ? 167 PHE   A O   1 
ATOM   1148 C  CB  . PHE   A  1  154 ? 27.253  1.532   23.062 1.00 37.24  ? 167 PHE   A CB  1 
ATOM   1149 C  CG  . PHE   A  1  154 ? 27.520  2.835   22.318 1.00 36.53  ? 167 PHE   A CG  1 
ATOM   1150 C  CD1 . PHE   A  1  154 ? 26.884  4.014   22.690 1.00 38.26  ? 167 PHE   A CD1 1 
ATOM   1151 C  CD2 . PHE   A  1  154 ? 28.392  2.868   21.246 1.00 37.16  ? 167 PHE   A CD2 1 
ATOM   1152 C  CE1 . PHE   A  1  154 ? 27.137  5.196   22.019 1.00 40.74  ? 167 PHE   A CE1 1 
ATOM   1153 C  CE2 . PHE   A  1  154 ? 28.639  4.052   20.574 1.00 38.92  ? 167 PHE   A CE2 1 
ATOM   1154 C  CZ  . PHE   A  1  154 ? 28.021  5.210   20.968 1.00 41.36  ? 167 PHE   A CZ  1 
ATOM   1155 N  N   . SER   A  1  155 ? 25.514  -1.023  24.166 1.00 31.70  ? 168 SER   A N   1 
ATOM   1156 C  CA  . SER   A  1  155 ? 25.325  -2.466  24.260 1.00 32.63  ? 168 SER   A CA  1 
ATOM   1157 C  C   . SER   A  1  155 ? 24.011  -2.862  23.579 1.00 34.51  ? 168 SER   A C   1 
ATOM   1158 O  O   . SER   A  1  155 ? 23.935  -3.896  22.918 1.00 36.36  ? 168 SER   A O   1 
ATOM   1159 C  CB  . SER   A  1  155 ? 25.368  -2.933  25.708 1.00 31.86  ? 168 SER   A CB  1 
ATOM   1160 O  OG  . SER   A  1  155 ? 26.603  -2.597  26.321 1.00 31.68  ? 168 SER   A OG  1 
ATOM   1161 N  N   . ASN   A  1  156 ? 22.964  -2.034  23.744 1.00 34.78  ? 169 ASN   A N   1 
ATOM   1162 C  CA  . ASN   A  1  156 ? 21.686  -2.278  23.098 1.00 31.03  ? 169 ASN   A CA  1 
ATOM   1163 C  C   . ASN   A  1  156 ? 21.854  -2.184  21.582 1.00 35.16  ? 169 ASN   A C   1 
ATOM   1164 O  O   . ASN   A  1  156 ? 21.319  -3.000  20.842 1.00 34.13  ? 169 ASN   A O   1 
ATOM   1165 C  CB  . ASN   A  1  156 ? 20.619  -1.279  23.532 1.00 30.82  ? 169 ASN   A CB  1 
ATOM   1166 C  CG  . ASN   A  1  156 ? 20.142  -1.454  24.949 1.00 31.53  ? 169 ASN   A CG  1 
ATOM   1167 O  OD1 . ASN   A  1  156 ? 20.227  -2.537  25.532 1.00 35.24  ? 169 ASN   A OD1 1 
ATOM   1168 N  ND2 . ASN   A  1  156 ? 19.583  -0.393  25.492 1.00 33.60  ? 169 ASN   A ND2 1 
ATOM   1169 N  N   . ARG   A  1  157 ? 22.632  -1.198  21.123 1.00 34.12  ? 170 ARG   A N   1 
ATOM   1170 C  CA  . ARG   A  1  157 ? 22.711  -0.883  19.710 1.00 33.83  ? 170 ARG   A CA  1 
ATOM   1171 C  C   . ARG   A  1  157 ? 23.608  -1.855  18.957 1.00 34.37  ? 170 ARG   A C   1 
ATOM   1172 O  O   . ARG   A  1  157 ? 23.350  -2.106  17.790 1.00 43.52  ? 170 ARG   A O   1 
ATOM   1173 C  CB  . ARG   A  1  157 ? 23.232  0.547   19.521 1.00 34.90  ? 170 ARG   A CB  1 
ATOM   1174 C  CG  . ARG   A  1  157 ? 22.143  1.560   19.844 1.00 33.98  ? 170 ARG   A CG  1 
ATOM   1175 C  CD  . ARG   A  1  157 ? 22.652  2.940   20.135 1.00 33.54  ? 170 ARG   A CD  1 
ATOM   1176 N  NE  . ARG   A  1  157 ? 23.571  3.411   19.102 1.00 39.89  ? 170 ARG   A NE  1 
ATOM   1177 C  CZ  . ARG   A  1  157 ? 24.188  4.571   19.125 1.00 40.98  ? 170 ARG   A CZ  1 
ATOM   1178 N  NH1 . ARG   A  1  157 ? 24.918  4.910   18.089 1.00 40.79  ? 170 ARG   A NH1 1 
ATOM   1179 N  NH2 . ARG   A  1  157 ? 24.038  5.391   20.156 1.00 42.14  ? 170 ARG   A NH2 1 
ATOM   1180 N  N   . TYR   A  1  158 ? 24.661  -2.389  19.596 1.00 34.55  ? 171 TYR   A N   1 
ATOM   1181 C  CA  . TYR   A  1  158 ? 25.654  -3.180  18.882 1.00 31.37  ? 171 TYR   A CA  1 
ATOM   1182 C  C   . TYR   A  1  158 ? 25.854  -4.581  19.461 1.00 33.43  ? 171 TYR   A C   1 
ATOM   1183 O  O   . TYR   A  1  158 ? 26.560  -5.376  18.843 1.00 34.57  ? 171 TYR   A O   1 
ATOM   1184 C  CB  . TYR   A  1  158 ? 26.997  -2.441  18.854 1.00 33.54  ? 171 TYR   A CB  1 
ATOM   1185 C  CG  . TYR   A  1  158 ? 26.912  -1.073  18.196 1.00 34.25  ? 171 TYR   A CG  1 
ATOM   1186 C  CD1 . TYR   A  1  158 ? 26.765  -0.950  16.814 1.00 38.36  ? 171 TYR   A CD1 1 
ATOM   1187 C  CD2 . TYR   A  1  158 ? 26.924  0.093   18.950 1.00 35.88  ? 171 TYR   A CD2 1 
ATOM   1188 C  CE1 . TYR   A  1  158 ? 26.632  0.290   16.206 1.00 35.64  ? 171 TYR   A CE1 1 
ATOM   1189 C  CE2 . TYR   A  1  158 ? 26.816  1.344   18.354 1.00 36.13  ? 171 TYR   A CE2 1 
ATOM   1190 C  CZ  . TYR   A  1  158 ? 26.666  1.435   16.981 1.00 39.27  ? 171 TYR   A CZ  1 
ATOM   1191 O  OH  . TYR   A  1  158 ? 26.526  2.645   16.375 1.00 47.07  ? 171 TYR   A OH  1 
ATOM   1192 N  N   . GLY   A  1  159 ? 25.286  -4.898  20.639 1.00 32.35  ? 172 GLY   A N   1 
ATOM   1193 C  CA  . GLY   A  1  159 ? 25.612  -6.143  21.320 1.00 29.37  ? 172 GLY   A CA  1 
ATOM   1194 C  C   . GLY   A  1  159 ? 24.388  -6.934  21.785 1.00 33.18  ? 172 GLY   A C   1 
ATOM   1195 O  O   . GLY   A  1  159 ? 24.509  -7.809  22.641 1.00 36.76  ? 172 GLY   A O   1 
ATOM   1196 N  N   . GLY   A  1  160 ? 23.216  -6.654  21.211 1.00 34.62  ? 173 GLY   A N   1 
ATOM   1197 C  CA  . GLY   A  1  160 ? 22.007  -7.379  21.568 1.00 35.46  ? 173 GLY   A CA  1 
ATOM   1198 C  C   . GLY   A  1  160 ? 21.613  -7.170  23.031 1.00 37.26  ? 173 GLY   A C   1 
ATOM   1199 O  O   . GLY   A  1  160 ? 20.918  -8.023  23.587 1.00 41.48  ? 173 GLY   A O   1 
ATOM   1200 N  N   . GLY   A  1  161 ? 22.077  -6.061  23.642 1.00 33.77  ? 174 GLY   A N   1 
ATOM   1201 C  CA  . GLY   A  1  161 ? 21.800  -5.748  25.037 1.00 37.80  ? 174 GLY   A CA  1 
ATOM   1202 C  C   . GLY   A  1  161 ? 22.923  -6.187  25.982 1.00 37.41  ? 174 GLY   A C   1 
ATOM   1203 O  O   . GLY   A  1  161 ? 22.835  -5.972  27.190 1.00 35.96  ? 174 GLY   A O   1 
ATOM   1204 N  N   . PHE   A  1  162 ? 23.998  -6.736  25.399 1.00 34.96  ? 175 PHE   A N   1 
ATOM   1205 C  CA  . PHE   A  1  162 ? 25.163  -7.190  26.135 1.00 32.50  ? 175 PHE   A CA  1 
ATOM   1206 C  C   . PHE   A  1  162 ? 26.407  -6.454  25.655 1.00 34.39  ? 175 PHE   A C   1 
ATOM   1207 O  O   . PHE   A  1  162 ? 26.446  -5.954  24.532 1.00 30.73  ? 175 PHE   A O   1 
ATOM   1208 C  CB  . PHE   A  1  162 ? 25.323  -8.692  25.915 1.00 34.65  ? 175 PHE   A CB  1 
ATOM   1209 C  CG  . PHE   A  1  162 ? 24.159  -9.518  26.425 1.00 33.46  ? 175 PHE   A CG  1 
ATOM   1210 C  CD1 . PHE   A  1  162 ? 23.066  -9.788  25.603 1.00 31.08  ? 175 PHE   A CD1 1 
ATOM   1211 C  CD2 . PHE   A  1  162 ? 24.154  -9.990  27.733 1.00 33.36  ? 175 PHE   A CD2 1 
ATOM   1212 C  CE1 . PHE   A  1  162 ? 21.990  -10.528 26.088 1.00 32.69  ? 175 PHE   A CE1 1 
ATOM   1213 C  CE2 . PHE   A  1  162 ? 23.079  -10.733 28.213 1.00 34.70  ? 175 PHE   A CE2 1 
ATOM   1214 C  CZ  . PHE   A  1  162 ? 21.995  -10.991 27.396 1.00 34.84  ? 175 PHE   A CZ  1 
ATOM   1215 N  N   . TYR   A  1  163 ? 27.407  -6.354  26.533 1.00 33.15  ? 176 TYR   A N   1 
ATOM   1216 C  CA  . TYR   A  1  163 ? 28.661  -5.750  26.148 1.00 33.66  ? 176 TYR   A CA  1 
ATOM   1217 C  C   . TYR   A  1  163 ? 29.549  -6.850  25.579 1.00 35.39  ? 176 TYR   A C   1 
ATOM   1218 O  O   . TYR   A  1  163 ? 29.815  -7.845  26.257 1.00 37.33  ? 176 TYR   A O   1 
ATOM   1219 C  CB  . TYR   A  1  163 ? 29.337  -5.066  27.332 1.00 32.44  ? 176 TYR   A CB  1 
ATOM   1220 C  CG  . TYR   A  1  163 ? 30.591  -4.282  26.991 1.00 31.50  ? 176 TYR   A CG  1 
ATOM   1221 C  CD1 . TYR   A  1  163 ? 30.519  -3.014  26.434 1.00 31.01  ? 176 TYR   A CD1 1 
ATOM   1222 C  CD2 . TYR   A  1  163 ? 31.848  -4.805  27.245 1.00 31.72  ? 176 TYR   A CD2 1 
ATOM   1223 C  CE1 . TYR   A  1  163 ? 31.663  -2.300  26.121 1.00 30.94  ? 176 TYR   A CE1 1 
ATOM   1224 C  CE2 . TYR   A  1  163 ? 32.996  -4.086  26.965 1.00 29.96  ? 176 TYR   A CE2 1 
ATOM   1225 C  CZ  . TYR   A  1  163 ? 32.904  -2.844  26.382 1.00 29.51  ? 176 TYR   A CZ  1 
ATOM   1226 O  OH  . TYR   A  1  163 ? 34.041  -2.164  26.122 1.00 28.07  ? 176 TYR   A OH  1 
ATOM   1227 N  N   . ASN   A  1  164 ? 29.975  -6.652  24.331 1.00 31.72  ? 177 ASN   A N   1 
ATOM   1228 C  CA  . ASN   A  1  164 ? 30.879  -7.572  23.666 1.00 33.18  ? 177 ASN   A CA  1 
ATOM   1229 C  C   . ASN   A  1  164 ? 31.867  -6.777  22.825 1.00 32.54  ? 177 ASN   A C   1 
ATOM   1230 O  O   . ASN   A  1  164 ? 31.885  -5.544  22.857 1.00 36.67  ? 177 ASN   A O   1 
ATOM   1231 C  CB  . ASN   A  1  164 ? 30.099  -8.638  22.910 1.00 37.61  ? 177 ASN   A CB  1 
ATOM   1232 C  CG  . ASN   A  1  164 ? 29.518  -8.175  21.592 1.00 38.21  ? 177 ASN   A CG  1 
ATOM   1233 O  OD1 . ASN   A  1  164 ? 29.747  -7.042  21.137 1.00 34.77  ? 177 ASN   A OD1 1 
ATOM   1234 N  ND2 . ASN   A  1  164 ? 28.773  -9.083  20.971 1.00 39.02  ? 177 ASN   A ND2 1 
ATOM   1235 N  N   . LEU   A  1  165 ? 32.694  -7.484  22.066 1.00 33.20  ? 178 LEU   A N   1 
ATOM   1236 C  CA  . LEU   A  1  165 ? 33.839  -6.846  21.436 1.00 36.52  ? 178 LEU   A CA  1 
ATOM   1237 C  C   . LEU   A  1  165 ? 33.418  -5.823  20.379 1.00 36.85  ? 178 LEU   A C   1 
ATOM   1238 O  O   . LEU   A  1  165 ? 34.086  -4.807  20.203 1.00 32.07  ? 178 LEU   A O   1 
ATOM   1239 C  CB  . LEU   A  1  165 ? 34.747  -7.935  20.876 1.00 39.92  ? 178 LEU   A CB  1 
ATOM   1240 C  CG  . LEU   A  1  165 ? 36.149  -7.499  20.459 1.00 42.39  ? 178 LEU   A CG  1 
ATOM   1241 C  CD1 . LEU   A  1  165 ? 36.974  -7.035  21.627 1.00 41.63  ? 178 LEU   A CD1 1 
ATOM   1242 C  CD2 . LEU   A  1  165 ? 36.843  -8.694  19.820 1.00 47.09  ? 178 LEU   A CD2 1 
ATOM   1243 N  N   . THR   A  1  166 ? 32.282  -6.054  19.706 1.00 37.76  ? 179 THR   A N   1 
ATOM   1244 C  CA  . THR   A  1  166 ? 31.757  -5.092  18.741 1.00 34.76  ? 179 THR   A CA  1 
ATOM   1245 C  C   . THR   A  1  166 ? 31.353  -3.801  19.455 1.00 33.33  ? 179 THR   A C   1 
ATOM   1246 O  O   . THR   A  1  166 ? 31.661  -2.704  19.004 1.00 36.02  ? 179 THR   A O   1 
ATOM   1247 C  CB  . THR   A  1  166 ? 30.560  -5.704  18.008 1.00 40.61  ? 179 THR   A CB  1 
ATOM   1248 O  OG1 . THR   A  1  166 ? 30.908  -7.024  17.600 1.00 42.01  ? 179 THR   A OG1 1 
ATOM   1249 C  CG2 . THR   A  1  166 ? 30.110  -4.857  16.831 1.00 40.65  ? 179 THR   A CG2 1 
ATOM   1250 N  N   . VAL   A  1  167 ? 30.665  -3.929  20.595 1.00 33.55  ? 180 VAL   A N   1 
ATOM   1251 C  CA  . VAL   A  1  167 ? 30.273  -2.777  21.392 1.00 31.48  ? 180 VAL   A CA  1 
ATOM   1252 C  C   . VAL   A  1  167 ? 31.517  -1.998  21.799 1.00 31.51  ? 180 VAL   A C   1 
ATOM   1253 O  O   . VAL   A  1  167 ? 31.534  -0.778  21.713 1.00 33.34  ? 180 VAL   A O   1 
ATOM   1254 C  CB  . VAL   A  1  167 ? 29.481  -3.164  22.653 1.00 32.27  ? 180 VAL   A CB  1 
ATOM   1255 C  CG1 . VAL   A  1  167 ? 28.958  -1.938  23.389 1.00 29.28  ? 180 VAL   A CG1 1 
ATOM   1256 C  CG2 . VAL   A  1  167 ? 28.336  -4.117  22.336 1.00 33.26  ? 180 VAL   A CG2 1 
ATOM   1257 N  N   . ALA   A  1  168 ? 32.539  -2.713  22.290 1.00 33.47  ? 181 ALA   A N   1 
ATOM   1258 C  CA  . ALA   A  1  168 ? 33.767  -2.082  22.752 1.00 31.78  ? 181 ALA   A CA  1 
ATOM   1259 C  C   . ALA   A  1  168 ? 34.355  -1.181  21.660 1.00 35.16  ? 181 ALA   A C   1 
ATOM   1260 O  O   . ALA   A  1  168 ? 34.716  -0.037  21.922 1.00 34.70  ? 181 ALA   A O   1 
ATOM   1261 C  CB  . ALA   A  1  168 ? 34.753  -3.137  23.190 1.00 32.51  ? 181 ALA   A CB  1 
ATOM   1262 N  N   . GLY   A  1  169 ? 34.420  -1.676  20.418 1.00 36.88  ? 182 GLY   A N   1 
ATOM   1263 C  CA  . GLY   A  1  169 ? 34.977  -0.889  19.327 1.00 34.74  ? 182 GLY   A CA  1 
ATOM   1264 C  C   . GLY   A  1  169 ? 34.235  0.432   19.136 1.00 36.40  ? 182 GLY   A C   1 
ATOM   1265 O  O   . GLY   A  1  169 ? 34.850  1.491   18.977 1.00 35.54  ? 182 GLY   A O   1 
ATOM   1266 N  N   . GLU   A  1  170 ? 32.897  0.357   19.170 1.00 39.52  ? 183 GLU   A N   1 
ATOM   1267 C  CA  . GLU   A  1  170 ? 32.054  1.513   18.944 1.00 34.66  ? 183 GLU   A CA  1 
ATOM   1268 C  C   . GLU   A  1  170 ? 32.140  2.444   20.146 1.00 35.26  ? 183 GLU   A C   1 
ATOM   1269 O  O   . GLU   A  1  170 ? 32.300  3.652   19.972 1.00 40.20  ? 183 GLU   A O   1 
ATOM   1270 C  CB  . GLU   A  1  170 ? 30.611  1.077   18.697 1.00 39.06  ? 183 GLU   A CB  1 
ATOM   1271 C  CG  . GLU   A  1  170 ? 30.417  0.221   17.449 1.00 42.38  ? 183 GLU   A CG  1 
ATOM   1272 C  CD  . GLU   A  1  170 ? 30.910  0.882   16.167 1.00 50.45  ? 183 GLU   A CD  1 
ATOM   1273 O  OE1 . GLU   A  1  170 ? 30.631  2.082   15.968 1.00 47.09  ? 183 GLU   A OE1 1 
ATOM   1274 O  OE2 . GLU   A  1  170 ? 31.608  0.201   15.375 1.00 65.71  ? 183 GLU   A OE2 1 
ATOM   1275 N  N   . LEU   A  1  171 ? 32.043  1.896   21.366 1.00 33.60  ? 184 LEU   A N   1 
ATOM   1276 C  CA  . LEU   A  1  171 ? 31.981  2.747   22.540 1.00 31.53  ? 184 LEU   A CA  1 
ATOM   1277 C  C   . LEU   A  1  171 ? 33.289  3.521   22.672 1.00 30.66  ? 184 LEU   A C   1 
ATOM   1278 O  O   . LEU   A  1  171 ? 33.292  4.707   22.982 1.00 27.91  ? 184 LEU   A O   1 
ATOM   1279 C  CB  . LEU   A  1  171 ? 31.663  1.932   23.790 1.00 32.10  ? 184 LEU   A CB  1 
ATOM   1280 C  CG  . LEU   A  1  171 ? 31.542  2.723   25.094 1.00 32.38  ? 184 LEU   A CG  1 
ATOM   1281 C  CD1 . LEU   A  1  171 ? 30.426  3.745   25.020 1.00 34.48  ? 184 LEU   A CD1 1 
ATOM   1282 C  CD2 . LEU   A  1  171 ? 31.324  1.766   26.236 1.00 37.14  ? 184 LEU   A CD2 1 
ATOM   1283 N  N   . ARG   A  1  172 ? 34.411  2.859   22.411 1.00 32.39  ? 185 ARG   A N   1 
ATOM   1284 C  CA  . ARG   A  1  172 ? 35.712  3.464   22.664 1.00 33.95  ? 185 ARG   A CA  1 
ATOM   1285 C  C   . ARG   A  1  172 ? 35.853  4.721   21.809 1.00 33.44  ? 185 ARG   A C   1 
ATOM   1286 O  O   . ARG   A  1  172 ? 36.227  5.782   22.294 1.00 33.68  ? 185 ARG   A O   1 
ATOM   1287 C  CB  . ARG   A  1  172 ? 36.811  2.416   22.439 1.00 33.46  ? 185 ARG   A CB  1 
ATOM   1288 C  CG  . ARG   A  1  172 ? 38.198  2.931   22.097 1.00 34.59  ? 185 ARG   A CG  1 
ATOM   1289 C  CD  . ARG   A  1  172 ? 38.786  3.888   23.117 1.00 39.02  ? 185 ARG   A CD  1 
ATOM   1290 N  NE  . ARG   A  1  172 ? 38.651  3.461   24.518 1.00 38.35  ? 185 ARG   A NE  1 
ATOM   1291 C  CZ  . ARG   A  1  172 ? 38.271  4.235   25.518 1.00 40.77  ? 185 ARG   A CZ  1 
ATOM   1292 N  NH1 . ARG   A  1  172 ? 37.904  5.482   25.285 1.00 44.59  ? 185 ARG   A NH1 1 
ATOM   1293 N  NH2 . ARG   A  1  172 ? 38.256  3.764   26.757 1.00 44.26  ? 185 ARG   A NH2 1 
ATOM   1294 N  N   . TYR   A  1  173 ? 35.532  4.579   20.529 1.00 37.85  ? 186 TYR   A N   1 
ATOM   1295 C  CA  . TYR   A  1  173 ? 35.616  5.677   19.580 1.00 38.77  ? 186 TYR   A CA  1 
ATOM   1296 C  C   . TYR   A  1  173 ? 34.650  6.794   19.965 1.00 38.20  ? 186 TYR   A C   1 
ATOM   1297 O  O   . TYR   A  1  173 ? 35.020  7.961   19.975 1.00 34.36  ? 186 TYR   A O   1 
ATOM   1298 C  CB  . TYR   A  1  173 ? 35.252  5.133   18.199 1.00 42.51  ? 186 TYR   A CB  1 
ATOM   1299 C  CG  . TYR   A  1  173 ? 35.285  6.201   17.123 1.00 45.21  ? 186 TYR   A CG  1 
ATOM   1300 C  CD1 . TYR   A  1  173 ? 36.499  6.762   16.748 1.00 48.32  ? 186 TYR   A CD1 1 
ATOM   1301 C  CD2 . TYR   A  1  173 ? 34.132  6.624   16.469 1.00 48.75  ? 186 TYR   A CD2 1 
ATOM   1302 C  CE1 . TYR   A  1  173 ? 36.573  7.727   15.763 1.00 47.33  ? 186 TYR   A CE1 1 
ATOM   1303 C  CE2 . TYR   A  1  173 ? 34.193  7.584   15.471 1.00 52.17  ? 186 TYR   A CE2 1 
ATOM   1304 C  CZ  . TYR   A  1  173 ? 35.417  8.139   15.125 1.00 52.40  ? 186 TYR   A CZ  1 
ATOM   1305 O  OH  . TYR   A  1  173 ? 35.510  9.109   14.171 1.00 55.93  ? 186 TYR   A OH  1 
ATOM   1306 N  N   . SER   A  1  174 ? 33.404  6.437   20.291 1.00 36.41  ? 187 SER   A N   1 
ATOM   1307 C  CA  . SER   A  1  174 ? 32.422  7.449   20.632 1.00 35.33  ? 187 SER   A CA  1 
ATOM   1308 C  C   . SER   A  1  174 ? 32.868  8.246   21.853 1.00 34.74  ? 187 SER   A C   1 
ATOM   1309 O  O   . SER   A  1  174 ? 32.703  9.464   21.873 1.00 38.84  ? 187 SER   A O   1 
ATOM   1310 C  CB  . SER   A  1  174 ? 31.063  6.854   20.824 1.00 33.98  ? 187 SER   A CB  1 
ATOM   1311 O  OG  . SER   A  1  174 ? 30.137  7.867   21.202 1.00 36.80  ? 187 SER   A OG  1 
ATOM   1312 N  N   . ARG   A  1  175 ? 33.465  7.582   22.853 1.00 35.12  ? 188 ARG   A N   1 
ATOM   1313 C  CA  . ARG   A  1  175 ? 33.902  8.267   24.070 1.00 31.49  ? 188 ARG   A CA  1 
ATOM   1314 C  C   . ARG   A  1  175 ? 35.045  9.215   23.749 1.00 32.44  ? 188 ARG   A C   1 
ATOM   1315 O  O   . ARG   A  1  175 ? 35.148  10.279  24.355 1.00 36.64  ? 188 ARG   A O   1 
ATOM   1316 C  CB  . ARG   A  1  175 ? 34.283  7.301   25.199 1.00 31.65  ? 188 ARG   A CB  1 
ATOM   1317 C  CG  . ARG   A  1  175 ? 33.099  6.535   25.772 1.00 31.74  ? 188 ARG   A CG  1 
ATOM   1318 C  CD  . ARG   A  1  175 ? 32.173  7.433   26.556 1.00 31.92  ? 188 ARG   A CD  1 
ATOM   1319 N  NE  . ARG   A  1  175 ? 32.872  7.964   27.721 1.00 31.20  ? 188 ARG   A NE  1 
ATOM   1320 C  CZ  . ARG   A  1  175 ? 33.210  9.226   27.952 1.00 34.81  ? 188 ARG   A CZ  1 
ATOM   1321 N  NH1 . ARG   A  1  175 ? 32.711  10.194  27.210 1.00 35.47  ? 188 ARG   A NH1 1 
ATOM   1322 N  NH2 . ARG   A  1  175 ? 34.010  9.528   28.969 1.00 31.37  ? 188 ARG   A NH2 1 
ATOM   1323 N  N   . ILE   A  1  176 ? 35.896  8.828   22.791 1.00 32.77  ? 189 ILE   A N   1 
ATOM   1324 C  CA  . ILE   A  1  176 ? 36.948  9.709   22.324 1.00 33.19  ? 189 ILE   A CA  1 
ATOM   1325 C  C   . ILE   A  1  176 ? 36.317  10.969  21.739 1.00 34.86  ? 189 ILE   A C   1 
ATOM   1326 O  O   . ILE   A  1  176 ? 36.674  12.072  22.145 1.00 37.21  ? 189 ILE   A O   1 
ATOM   1327 C  CB  . ILE   A  1  176 ? 37.880  8.980   21.342 1.00 37.15  ? 189 ILE   A CB  1 
ATOM   1328 C  CG1 . ILE   A  1  176 ? 38.745  7.953   22.072 1.00 35.31  ? 189 ILE   A CG1 1 
ATOM   1329 C  CG2 . ILE   A  1  176 ? 38.743  9.968   20.551 1.00 39.38  ? 189 ILE   A CG2 1 
ATOM   1330 C  CD1 . ILE   A  1  176 ? 39.398  6.937   21.152 1.00 36.69  ? 189 ILE   A CD1 1 
ATOM   1331 N  N   . GLN   A  1  177 ? 35.336  10.798  20.844 1.00 38.37  ? 190 GLN   A N   1 
ATOM   1332 C  CA  . GLN   A  1  177 ? 34.600  11.921  20.265 1.00 40.33  ? 190 GLN   A CA  1 
ATOM   1333 C  C   . GLN   A  1  177 ? 33.951  12.808  21.337 1.00 39.26  ? 190 GLN   A C   1 
ATOM   1334 O  O   . GLN   A  1  177 ? 34.070  14.021  21.254 1.00 37.65  ? 190 GLN   A O   1 
ATOM   1335 C  CB  . GLN   A  1  177 ? 33.581  11.435  19.225 1.00 43.66  ? 190 GLN   A CB  1 
ATOM   1336 C  CG  . GLN   A  1  177 ? 34.201  10.720  18.024 1.00 44.81  ? 190 GLN   A CG  1 
ATOM   1337 C  CD  . GLN   A  1  177 ? 35.168  11.582  17.236 1.00 53.23  ? 190 GLN   A CD  1 
ATOM   1338 O  OE1 . GLN   A  1  177 ? 35.076  12.818  17.217 1.00 57.46  ? 190 GLN   A OE1 1 
ATOM   1339 N  NE2 . GLN   A  1  177 ? 36.096  10.933  16.547 1.00 59.72  ? 190 GLN   A NE2 1 
ATOM   1340 N  N   . ASP   A  1  178 ? 33.284  12.238  22.351 1.00 40.50  ? 191 ASP   A N   1 
ATOM   1341 C  CA  . ASP   A  1  178 ? 32.701  13.039  23.430 1.00 38.07  ? 191 ASP   A CA  1 
ATOM   1342 C  C   . ASP   A  1  178 ? 33.748  13.959  24.043 1.00 38.79  ? 191 ASP   A C   1 
ATOM   1343 O  O   . ASP   A  1  178 ? 33.473  15.123  24.310 1.00 43.36  ? 191 ASP   A O   1 
ATOM   1344 C  CB  . ASP   A  1  178 ? 32.118  12.199  24.557 1.00 38.77  ? 191 ASP   A CB  1 
ATOM   1345 C  CG  . ASP   A  1  178 ? 30.926  11.323  24.192 1.00 47.05  ? 191 ASP   A CG  1 
ATOM   1346 O  OD1 . ASP   A  1  178 ? 30.298  11.604  23.140 1.00 50.79  ? 191 ASP   A OD1 1 
ATOM   1347 O  OD2 . ASP   A  1  178 ? 30.628  10.379  24.972 1.00 49.33  ? 191 ASP   A OD2 1 
ATOM   1348 N  N   . SER   A  1  179 ? 34.950  13.431  24.277 1.00 40.06  ? 192 SER   A N   1 
ATOM   1349 C  CA  . SER   A  1  179 ? 35.987  14.173  24.978 1.00 40.48  ? 192 SER   A CA  1 
ATOM   1350 C  C   . SER   A  1  179 ? 36.585  15.244  24.064 1.00 37.51  ? 192 SER   A C   1 
ATOM   1351 O  O   . SER   A  1  179 ? 36.926  16.329  24.520 1.00 34.78  ? 192 SER   A O   1 
ATOM   1352 C  CB  . SER   A  1  179 ? 37.065  13.242  25.548 1.00 39.07  ? 192 SER   A CB  1 
ATOM   1353 O  OG  . SER   A  1  179 ? 36.686  12.699  26.807 1.00 36.44  ? 192 SER   A OG  1 
ATOM   1354 N  N   . ILE   A  1  180 ? 36.728  14.940  22.774 1.00 38.56  ? 193 ILE   A N   1 
ATOM   1355 C  CA  . ILE   A  1  180 ? 37.168  15.934  21.808 1.00 40.46  ? 193 ILE   A CA  1 
ATOM   1356 C  C   . ILE   A  1  180 ? 36.199  17.118  21.808 1.00 44.01  ? 193 ILE   A C   1 
ATOM   1357 O  O   . ILE   A  1  180 ? 36.625  18.267  21.847 1.00 42.62  ? 193 ILE   A O   1 
ATOM   1358 C  CB  . ILE   A  1  180 ? 37.289  15.317  20.403 1.00 43.75  ? 193 ILE   A CB  1 
ATOM   1359 C  CG1 . ILE   A  1  180 ? 38.478  14.360  20.327 1.00 43.44  ? 193 ILE   A CG1 1 
ATOM   1360 C  CG2 . ILE   A  1  180 ? 37.376  16.423  19.346 1.00 40.68  ? 193 ILE   A CG2 1 
ATOM   1361 C  CD1 . ILE   A  1  180 ? 38.565  13.590  19.025 1.00 43.72  ? 193 ILE   A CD1 1 
ATOM   1362 N  N   . ALA   A  1  181 ? 34.893  16.823  21.779 1.00 43.99  ? 194 ALA   A N   1 
ATOM   1363 C  CA  . ALA   A  1  181 ? 33.874  17.848  21.630 1.00 44.23  ? 194 ALA   A CA  1 
ATOM   1364 C  C   . ALA   A  1  181 ? 33.686  18.677  22.902 1.00 44.72  ? 194 ALA   A C   1 
ATOM   1365 O  O   . ALA   A  1  181 ? 33.230  19.812  22.809 1.00 46.85  ? 194 ALA   A O   1 
ATOM   1366 C  CB  . ALA   A  1  181 ? 32.568  17.208  21.206 1.00 44.12  ? 194 ALA   A CB  1 
ATOM   1367 N  N   . THR   A  1  182 ? 34.013  18.136  24.083 1.00 40.86  ? 195 THR   A N   1 
ATOM   1368 C  CA  . THR   A  1  182 ? 33.541  18.752  25.319 1.00 41.77  ? 195 THR   A CA  1 
ATOM   1369 C  C   . THR   A  1  182 ? 34.683  19.077  26.271 1.00 38.38  ? 195 THR   A C   1 
ATOM   1370 O  O   . THR   A  1  182 ? 34.466  19.783  27.247 1.00 41.19  ? 195 THR   A O   1 
ATOM   1371 C  CB  . THR   A  1  182 ? 32.515  17.862  26.038 1.00 48.03  ? 195 THR   A CB  1 
ATOM   1372 O  OG1 . THR   A  1  182 ? 33.145  16.623  26.358 1.00 44.42  ? 195 THR   A OG1 1 
ATOM   1373 C  CG2 . THR   A  1  182 ? 31.272  17.575  25.211 1.00 52.33  ? 195 THR   A CG2 1 
ATOM   1374 N  N   . ASN   A  1  183 ? 35.874  18.530  26.045 1.00 41.49  ? 196 ASN   A N   1 
ATOM   1375 C  CA  . ASN   A  1  183 ? 36.947  18.658  27.019 1.00 40.30  ? 196 ASN   A CA  1 
ATOM   1376 C  C   . ASN   A  1  183 ? 38.123  19.357  26.353 1.00 39.90  ? 196 ASN   A C   1 
ATOM   1377 O  O   . ASN   A  1  183 ? 38.871  18.748  25.595 1.00 36.59  ? 196 ASN   A O   1 
ATOM   1378 C  CB  . ASN   A  1  183 ? 37.354  17.310  27.606 1.00 40.31  ? 196 ASN   A CB  1 
ATOM   1379 C  CG  . ASN   A  1  183 ? 38.500  17.404  28.589 1.00 43.17  ? 196 ASN   A CG  1 
ATOM   1380 O  OD1 . ASN   A  1  183 ? 38.992  18.497  28.885 1.00 36.97  ? 196 ASN   A OD1 1 
ATOM   1381 N  ND2 . ASN   A  1  183 ? 38.947  16.265  29.103 1.00 43.05  ? 196 ASN   A ND2 1 
ATOM   1382 N  N   . PRO   A  1  184 ? 38.335  20.657  26.628 1.00 41.07  ? 197 PRO   A N   1 
ATOM   1383 C  CA  . PRO   A  1  184 ? 39.421  21.406  25.997 1.00 44.23  ? 197 PRO   A CA  1 
ATOM   1384 C  C   . PRO   A  1  184 ? 40.828  20.987  26.415 1.00 45.62  ? 197 PRO   A C   1 
ATOM   1385 O  O   . PRO   A  1  184 ? 41.790  21.323  25.730 1.00 56.54  ? 197 PRO   A O   1 
ATOM   1386 C  CB  . PRO   A  1  184 ? 39.106  22.841  26.416 1.00 43.50  ? 197 PRO   A CB  1 
ATOM   1387 C  CG  . PRO   A  1  184 ? 38.456  22.680  27.757 1.00 44.61  ? 197 PRO   A CG  1 
ATOM   1388 C  CD  . PRO   A  1  184 ? 37.577  21.457  27.596 1.00 43.63  ? 197 PRO   A CD  1 
ATOM   1389 N  N   . GLU   A  1  185 ? 40.950  20.251  27.529 1.00 51.71  ? 198 GLU   A N   1 
ATOM   1390 C  CA  . GLU   A  1  185 ? 42.242  19.745  27.987 1.00 50.18  ? 198 GLU   A CA  1 
ATOM   1391 C  C   . GLU   A  1  185 ? 42.424  18.259  27.639 1.00 46.79  ? 198 GLU   A C   1 
ATOM   1392 O  O   . GLU   A  1  185 ? 43.362  17.632  28.115 1.00 42.15  ? 198 GLU   A O   1 
ATOM   1393 C  CB  . GLU   A  1  185 ? 42.395  19.914  29.496 1.00 50.14  ? 198 GLU   A CB  1 
ATOM   1394 C  CG  . GLU   A  1  185 ? 42.458  21.361  29.975 1.00 56.36  ? 198 GLU   A CG  1 
ATOM   1395 C  CD  . GLU   A  1  185 ? 42.506  21.515  31.491 1.00 62.72  ? 198 GLU   A CD  1 
ATOM   1396 O  OE1 . GLU   A  1  185 ? 42.709  20.496  32.176 1.00 66.19  ? 198 GLU   A OE1 1 
ATOM   1397 O  OE2 . GLU   A  1  185 ? 42.326  22.632  32.013 1.00 70.59  ? 198 GLU   A OE2 1 
ATOM   1398 N  N   . PHE   A  1  186 ? 41.534  17.695  26.809 1.00 39.98  ? 199 PHE   A N   1 
ATOM   1399 C  CA  . PHE   A  1  186 ? 41.591  16.290  26.444 1.00 38.98  ? 199 PHE   A CA  1 
ATOM   1400 C  C   . PHE   A  1  186 ? 42.981  15.891  25.947 1.00 39.89  ? 199 PHE   A C   1 
ATOM   1401 O  O   . PHE   A  1  186 ? 43.483  16.456  24.990 1.00 41.99  ? 199 PHE   A O   1 
ATOM   1402 C  CB  . PHE   A  1  186 ? 40.571  15.988  25.347 1.00 37.74  ? 199 PHE   A CB  1 
ATOM   1403 C  CG  . PHE   A  1  186 ? 40.542  14.543  24.873 1.00 38.39  ? 199 PHE   A CG  1 
ATOM   1404 C  CD1 . PHE   A  1  186 ? 40.538  13.486  25.767 1.00 39.62  ? 199 PHE   A CD1 1 
ATOM   1405 C  CD2 . PHE   A  1  186 ? 40.510  14.249  23.521 1.00 38.93  ? 199 PHE   A CD2 1 
ATOM   1406 C  CE1 . PHE   A  1  186 ? 40.505  12.174  25.316 1.00 39.88  ? 199 PHE   A CE1 1 
ATOM   1407 C  CE2 . PHE   A  1  186 ? 40.490  12.943  23.081 1.00 39.18  ? 199 PHE   A CE2 1 
ATOM   1408 C  CZ  . PHE   A  1  186 ? 40.484  11.910  23.974 1.00 40.82  ? 199 PHE   A CZ  1 
ATOM   1409 N  N   . GLN   A  1  187 ? 43.552  14.878  26.600 1.00 44.73  ? 200 GLN   A N   1 
ATOM   1410 C  CA  . GLN   A  1  187 ? 44.797  14.235  26.216 1.00 43.19  ? 200 GLN   A CA  1 
ATOM   1411 C  C   . GLN   A  1  187 ? 44.528  12.749  25.995 1.00 42.46  ? 200 GLN   A C   1 
ATOM   1412 O  O   . GLN   A  1  187 ? 43.855  12.107  26.804 1.00 45.11  ? 200 GLN   A O   1 
ATOM   1413 C  CB  . GLN   A  1  187 ? 45.807  14.373  27.352 1.00 42.63  ? 200 GLN   A CB  1 
ATOM   1414 C  CG  . GLN   A  1  187 ? 46.319  15.792  27.551 1.00 48.46  ? 200 GLN   A CG  1 
ATOM   1415 C  CD  . GLN   A  1  187 ? 47.253  16.199  26.434 1.00 52.07  ? 200 GLN   A CD  1 
ATOM   1416 O  OE1 . GLN   A  1  187 ? 48.425  15.797  26.420 1.00 51.80  ? 200 GLN   A OE1 1 
ATOM   1417 N  NE2 . GLN   A  1  187 ? 46.737  16.964  25.479 1.00 51.93  ? 200 GLN   A NE2 1 
ATOM   1418 N  N   . PHE   A  1  188 ? 45.061  12.206  24.901 1.00 37.93  ? 201 PHE   A N   1 
ATOM   1419 C  CA  . PHE   A  1  188 ? 44.913  10.793  24.622 1.00 38.22  ? 201 PHE   A CA  1 
ATOM   1420 C  C   . PHE   A  1  188 ? 46.211  10.258  24.039 1.00 36.45  ? 201 PHE   A C   1 
ATOM   1421 O  O   . PHE   A  1  188 ? 46.238  9.838   22.888 1.00 33.67  ? 201 PHE   A O   1 
ATOM   1422 C  CB  . PHE   A  1  188 ? 43.733  10.593  23.669 1.00 38.83  ? 201 PHE   A CB  1 
ATOM   1423 C  CG  . PHE   A  1  188 ? 43.148  9.196   23.708 1.00 35.77  ? 201 PHE   A CG  1 
ATOM   1424 C  CD1 . PHE   A  1  188 ? 42.474  8.752   24.835 1.00 39.61  ? 201 PHE   A CD1 1 
ATOM   1425 C  CD2 . PHE   A  1  188 ? 43.229  8.358   22.615 1.00 36.09  ? 201 PHE   A CD2 1 
ATOM   1426 C  CE1 . PHE   A  1  188 ? 41.921  7.483   24.879 1.00 40.49  ? 201 PHE   A CE1 1 
ATOM   1427 C  CE2 . PHE   A  1  188 ? 42.677  7.088   22.667 1.00 37.25  ? 201 PHE   A CE2 1 
ATOM   1428 C  CZ  . PHE   A  1  188 ? 42.026  6.653   23.797 1.00 37.85  ? 201 PHE   A CZ  1 
ATOM   1429 N  N   . LYS   A  1  189 ? 47.270  10.264  24.853 1.00 39.22  ? 202 LYS   A N   1 
ATOM   1430 C  CA  . LYS   A  1  189 ? 48.589  9.867   24.379 1.00 43.10  ? 202 LYS   A CA  1 
ATOM   1431 C  C   . LYS   A  1  189 ? 49.373  9.134   25.474 1.00 41.25  ? 202 LYS   A C   1 
ATOM   1432 O  O   . LYS   A  1  189 ? 48.948  9.035   26.627 1.00 39.76  ? 202 LYS   A O   1 
ATOM   1433 C  CB  . LYS   A  1  189 ? 49.308  11.134  23.913 1.00 47.11  ? 202 LYS   A CB  1 
ATOM   1434 C  CG  . LYS   A  1  189 ? 49.562  12.146  25.025 1.00 54.59  ? 202 LYS   A CG  1 
ATOM   1435 C  CD  . LYS   A  1  189 ? 50.412  13.354  24.643 1.00 58.23  ? 202 LYS   A CD  1 
ATOM   1436 C  CE  . LYS   A  1  189 ? 49.694  14.254  23.679 1.00 65.46  ? 202 LYS   A CE  1 
ATOM   1437 N  NZ  . LYS   A  1  189 ? 50.419  15.501  23.426 1.00 71.07  ? 202 LYS   A NZ  1 
ATOM   1438 N  N   . ASN   A  1  190 ? 50.526  8.587   25.080 1.00 42.75  ? 203 ASN   A N   1 
ATOM   1439 C  CA  . ASN   A  1  190 ? 51.433  7.905   25.991 1.00 39.41  ? 203 ASN   A CA  1 
ATOM   1440 C  C   . ASN   A  1  190 ? 50.693  6.782   26.720 1.00 36.53  ? 203 ASN   A C   1 
ATOM   1441 O  O   . ASN   A  1  190 ? 50.084  5.937   26.092 1.00 36.92  ? 203 ASN   A O   1 
ATOM   1442 C  CB  . ASN   A  1  190 ? 52.145  8.945   26.845 1.00 38.86  ? 203 ASN   A CB  1 
ATOM   1443 C  CG  . ASN   A  1  190 ? 53.025  9.827   25.984 1.00 44.11  ? 203 ASN   A CG  1 
ATOM   1444 O  OD1 . ASN   A  1  190 ? 53.724  9.328   25.086 1.00 41.80  ? 203 ASN   A OD1 1 
ATOM   1445 N  ND2 . ASN   A  1  190 ? 52.995  11.128  26.220 1.00 45.02  ? 203 ASN   A ND2 1 
ATOM   1446 N  N   . VAL   A  1  191 ? 50.745  6.768   28.048 1.00 39.48  ? 204 VAL   A N   1 
ATOM   1447 C  CA  . VAL   A  1  191 ? 50.171  5.677   28.812 1.00 39.59  ? 204 VAL   A CA  1 
ATOM   1448 C  C   . VAL   A  1  191 ? 48.674  5.553   28.494 1.00 38.98  ? 204 VAL   A C   1 
ATOM   1449 O  O   . VAL   A  1  191 ? 48.161  4.460   28.276 1.00 36.63  ? 204 VAL   A O   1 
ATOM   1450 C  CB  . VAL   A  1  191 ? 50.401  5.886   30.322 1.00 41.80  ? 204 VAL   A CB  1 
ATOM   1451 C  CG1 . VAL   A  1  191 ? 49.647  4.860   31.165 1.00 41.49  ? 204 VAL   A CG1 1 
ATOM   1452 C  CG2 . VAL   A  1  191 ? 51.879  5.872   30.684 1.00 42.37  ? 204 VAL   A CG2 1 
ATOM   1453 N  N   . ARG   A  1  192 ? 47.959  6.673   28.484 1.00 35.99  ? 205 ARG   A N   1 
ATOM   1454 C  CA  . ARG   A  1  192 ? 46.516  6.632   28.399 1.00 32.81  ? 205 ARG   A CA  1 
ATOM   1455 C  C   . ARG   A  1  192 ? 46.076  6.031   27.075 1.00 33.54  ? 205 ARG   A C   1 
ATOM   1456 O  O   . ARG   A  1  192 ? 45.078  5.306   27.016 1.00 35.00  ? 205 ARG   A O   1 
ATOM   1457 C  CB  . ARG   A  1  192 ? 45.901  8.025   28.548 1.00 37.22  ? 205 ARG   A CB  1 
ATOM   1458 C  CG  . ARG   A  1  192 ? 44.379  8.002   28.478 1.00 37.07  ? 205 ARG   A CG  1 
ATOM   1459 C  CD  . ARG   A  1  192 ? 43.795  6.972   29.431 1.00 36.36  ? 205 ARG   A CD  1 
ATOM   1460 N  NE  . ARG   A  1  192 ? 42.339  6.872   29.328 1.00 35.92  ? 205 ARG   A NE  1 
ATOM   1461 C  CZ  . ARG   A  1  192 ? 41.620  5.859   29.772 1.00 34.41  ? 205 ARG   A CZ  1 
ATOM   1462 N  NH1 . ARG   A  1  192 ? 42.201  4.811   30.329 1.00 34.90  ? 205 ARG   A NH1 1 
ATOM   1463 N  NH2 . ARG   A  1  192 ? 40.312  5.892   29.637 1.00 37.97  ? 205 ARG   A NH2 1 
ATOM   1464 N  N   . PHE   A  1  193 ? 46.819  6.335   26.011 1.00 31.84  ? 206 PHE   A N   1 
ATOM   1465 C  CA  . PHE   A  1  193 ? 46.468  5.816   24.709 1.00 33.59  ? 206 PHE   A CA  1 
ATOM   1466 C  C   . PHE   A  1  193 ? 46.527  4.293   24.742 1.00 37.44  ? 206 PHE   A C   1 
ATOM   1467 O  O   . PHE   A  1  193 ? 45.660  3.628   24.187 1.00 43.61  ? 206 PHE   A O   1 
ATOM   1468 C  CB  . PHE   A  1  193 ? 47.371  6.384   23.616 1.00 35.50  ? 206 PHE   A CB  1 
ATOM   1469 C  CG  . PHE   A  1  193 ? 47.045  5.801   22.252 1.00 32.56  ? 206 PHE   A CG  1 
ATOM   1470 C  CD1 . PHE   A  1  193 ? 45.977  6.279   21.518 1.00 34.26  ? 206 PHE   A CD1 1 
ATOM   1471 C  CD2 . PHE   A  1  193 ? 47.800  4.777   21.720 1.00 34.57  ? 206 PHE   A CD2 1 
ATOM   1472 C  CE1 . PHE   A  1  193 ? 45.675  5.750   20.280 1.00 35.06  ? 206 PHE   A CE1 1 
ATOM   1473 C  CE2 . PHE   A  1  193 ? 47.495  4.247   20.482 1.00 36.25  ? 206 PHE   A CE2 1 
ATOM   1474 C  CZ  . PHE   A  1  193 ? 46.435  4.739   19.763 1.00 38.16  ? 206 PHE   A CZ  1 
ATOM   1475 N  N   . ILE   A  1  194 ? 47.533  3.736   25.420 1.00 37.68  ? 207 ILE   A N   1 
ATOM   1476 C  CA  . ILE   A  1  194 ? 47.690  2.291   25.459 1.00 36.19  ? 207 ILE   A CA  1 
ATOM   1477 C  C   . ILE   A  1  194 ? 46.648  1.665   26.394 1.00 33.66  ? 207 ILE   A C   1 
ATOM   1478 O  O   . ILE   A  1  194 ? 45.974  0.721   25.994 1.00 32.42  ? 207 ILE   A O   1 
ATOM   1479 C  CB  . ILE   A  1  194 ? 49.139  1.934   25.828 1.00 36.55  ? 207 ILE   A CB  1 
ATOM   1480 C  CG1 . ILE   A  1  194 ? 50.130  2.541   24.827 1.00 40.07  ? 207 ILE   A CG1 1 
ATOM   1481 C  CG2 . ILE   A  1  194 ? 49.309  0.425   25.917 1.00 38.03  ? 207 ILE   A CG2 1 
ATOM   1482 C  CD1 . ILE   A  1  194 ? 49.898  2.133   23.379 1.00 38.64  ? 207 ILE   A CD1 1 
ATOM   1483 N  N   . THR   A  1  195 ? 46.477  2.220   27.607 1.00 34.26  ? 208 THR   A N   1 
ATOM   1484 C  CA  . THR   A  1  195 ? 45.619  1.619   28.619 1.00 33.62  ? 208 THR   A CA  1 
ATOM   1485 C  C   . THR   A  1  195 ? 44.145  1.712   28.222 1.00 34.79  ? 208 THR   A C   1 
ATOM   1486 O  O   . THR   A  1  195 ? 43.339  0.895   28.654 1.00 39.71  ? 208 THR   A O   1 
ATOM   1487 C  CB  . THR   A  1  195 ? 45.859  2.230   29.997 1.00 34.92  ? 208 THR   A CB  1 
ATOM   1488 O  OG1 . THR   A  1  195 ? 45.533  3.616   29.979 1.00 39.33  ? 208 THR   A OG1 1 
ATOM   1489 C  CG2 . THR   A  1  195 ? 47.283  2.015   30.470 1.00 36.85  ? 208 THR   A CG2 1 
ATOM   1490 N  N   . ALA   A  1  196 ? 43.793  2.701   27.403 1.00 35.44  ? 209 ALA   A N   1 
ATOM   1491 C  CA  . ALA   A  1  196 ? 42.402  2.939   27.040 1.00 36.63  ? 209 ALA   A CA  1 
ATOM   1492 C  C   . ALA   A  1  196 ? 41.834  1.814   26.180 1.00 36.69  ? 209 ALA   A C   1 
ATOM   1493 O  O   . ALA   A  1  196 ? 40.636  1.574   26.232 1.00 37.10  ? 209 ALA   A O   1 
ATOM   1494 C  CB  . ALA   A  1  196 ? 42.254  4.255   26.333 1.00 38.83  ? 209 ALA   A CB  1 
ATOM   1495 N  N   . TYR   A  1  197 ? 42.675  1.129   25.400 1.00 35.23  ? 210 TYR   A N   1 
ATOM   1496 C  CA  . TYR   A  1  197 ? 42.184  0.051   24.563 1.00 32.94  ? 210 TYR   A CA  1 
ATOM   1497 C  C   . TYR   A  1  197 ? 42.044  -1.216  25.409 1.00 34.52  ? 210 TYR   A C   1 
ATOM   1498 O  O   . TYR   A  1  197 ? 41.015  -1.892  25.345 1.00 37.39  ? 210 TYR   A O   1 
ATOM   1499 C  CB  . TYR   A  1  197 ? 43.041  -0.048  23.302 1.00 32.57  ? 210 TYR   A CB  1 
ATOM   1500 C  CG  . TYR   A  1  197 ? 42.669  1.086   22.366 1.00 32.45  ? 210 TYR   A CG  1 
ATOM   1501 C  CD1 . TYR   A  1  197 ? 41.585  0.980   21.502 1.00 33.43  ? 210 TYR   A CD1 1 
ATOM   1502 C  CD2 . TYR   A  1  197 ? 43.323  2.307   22.435 1.00 36.49  ? 210 TYR   A CD2 1 
ATOM   1503 C  CE1 . TYR   A  1  197 ? 41.200  2.039   20.695 1.00 35.71  ? 210 TYR   A CE1 1 
ATOM   1504 C  CE2 . TYR   A  1  197 ? 42.951  3.381   21.640 1.00 36.67  ? 210 TYR   A CE2 1 
ATOM   1505 C  CZ  . TYR   A  1  197 ? 41.880  3.247   20.771 1.00 39.49  ? 210 TYR   A CZ  1 
ATOM   1506 O  OH  . TYR   A  1  197 ? 41.504  4.310   19.998 1.00 36.48  ? 210 TYR   A OH  1 
ATOM   1507 N  N   . GLY   A  1  198 ? 43.052  -1.503  26.235 1.00 33.27  ? 211 GLY   A N   1 
ATOM   1508 C  CA  . GLY   A  1  198 ? 42.986  -2.644  27.140 1.00 33.77  ? 211 GLY   A CA  1 
ATOM   1509 C  C   . GLY   A  1  198 ? 41.779  -2.598  28.084 1.00 28.78  ? 211 GLY   A C   1 
ATOM   1510 O  O   . GLY   A  1  198 ? 41.132  -3.612  28.300 1.00 27.78  ? 211 GLY   A O   1 
ATOM   1511 N  N   . GLU   A  1  199 ? 41.445  -1.415  28.609 1.00 30.61  ? 212 GLU   A N   1 
ATOM   1512 C  CA  A GLU   A  1  199 ? 40.407  -1.340  29.622 0.50 31.75  ? 212 GLU   A CA  1 
ATOM   1513 C  CA  B GLU   A  1  199 ? 40.401  -1.303  29.614 0.50 31.07  ? 212 GLU   A CA  1 
ATOM   1514 C  C   . GLU   A  1  199 ? 39.058  -1.677  28.988 1.00 31.77  ? 212 GLU   A C   1 
ATOM   1515 O  O   . GLU   A  1  199 ? 38.156  -2.131  29.682 1.00 31.86  ? 212 GLU   A O   1 
ATOM   1516 C  CB  A GLU   A  1  199 ? 40.493  -0.017  30.380 0.50 32.00  ? 212 GLU   A CB  1 
ATOM   1517 C  CB  B GLU   A  1  199 ? 40.385  0.107   30.220 0.50 30.47  ? 212 GLU   A CB  1 
ATOM   1518 C  CG  A GLU   A  1  199 ? 41.652  -0.001  31.376 0.50 31.87  ? 212 GLU   A CG  1 
ATOM   1519 C  CG  B GLU   A  1  199 ? 39.637  1.153   29.387 0.50 29.70  ? 212 GLU   A CG  1 
ATOM   1520 C  CD  A GLU   A  1  199 ? 42.116  1.377   31.798 0.50 31.24  ? 212 GLU   A CD  1 
ATOM   1521 C  CD  B GLU   A  1  199 ? 39.556  2.546   30.008 0.50 25.25  ? 212 GLU   A CD  1 
ATOM   1522 O  OE1 A GLU   A  1  199 ? 41.411  2.352   31.472 0.50 30.96  ? 212 GLU   A OE1 1 
ATOM   1523 O  OE1 B GLU   A  1  199 ? 40.288  2.807   30.955 0.50 24.58  ? 212 GLU   A OE1 1 
ATOM   1524 O  OE2 A GLU   A  1  199 ? 43.194  1.465   32.429 0.50 34.89  ? 212 GLU   A OE2 1 
ATOM   1525 O  OE2 B GLU   A  1  199 ? 38.789  3.402   29.579 0.50 24.12  ? 212 GLU   A OE2 1 
ATOM   1526 N  N   . THR   A  1  200 ? 38.935  -1.521  27.658 1.00 33.13  ? 213 THR   A N   1 
ATOM   1527 C  CA  . THR   A  1  200 ? 37.640  -1.740  27.033 1.00 32.49  ? 213 THR   A CA  1 
ATOM   1528 C  C   . THR   A  1  200 ? 37.399  -3.227  26.815 1.00 30.86  ? 213 THR   A C   1 
ATOM   1529 O  O   . THR   A  1  200 ? 36.252  -3.609  26.626 1.00 30.37  ? 213 THR   A O   1 
ATOM   1530 C  CB  . THR   A  1  200 ? 37.460  -0.958  25.729 1.00 37.78  ? 213 THR   A CB  1 
ATOM   1531 O  OG1 . THR   A  1  200 ? 38.242  -1.531  24.695 1.00 41.01  ? 213 THR   A OG1 1 
ATOM   1532 C  CG2 . THR   A  1  200 ? 37.823  0.506   25.868 1.00 41.75  ? 213 THR   A CG2 1 
ATOM   1533 N  N   . VAL   A  1  201 ? 38.449  -4.061  26.864 1.00 29.25  ? 214 VAL   A N   1 
ATOM   1534 C  CA  . VAL   A  1  201 ? 38.256  -5.500  26.722 1.00 28.23  ? 214 VAL   A CA  1 
ATOM   1535 C  C   . VAL   A  1  201 ? 38.322  -6.216  28.071 1.00 27.70  ? 214 VAL   A C   1 
ATOM   1536 O  O   . VAL   A  1  201 ? 37.892  -7.357  28.164 1.00 32.03  ? 214 VAL   A O   1 
ATOM   1537 C  CB  . VAL   A  1  201 ? 39.208  -6.141  25.694 1.00 28.71  ? 214 VAL   A CB  1 
ATOM   1538 C  CG1 . VAL   A  1  201 ? 38.978  -5.548  24.317 1.00 30.86  ? 214 VAL   A CG1 1 
ATOM   1539 C  CG2 . VAL   A  1  201 ? 40.673  -6.020  26.078 1.00 30.30  ? 214 VAL   A CG2 1 
ATOM   1540 N  N   . PHE   A  1  202 ? 38.827  -5.575  29.123 1.00 28.73  ? 215 PHE   A N   1 
ATOM   1541 C  CA  . PHE   A  1  202 ? 38.845  -6.216  30.431 1.00 29.57  ? 215 PHE   A CA  1 
ATOM   1542 C  C   . PHE   A  1  202 ? 37.445  -6.691  30.826 1.00 29.69  ? 215 PHE   A C   1 
ATOM   1543 O  O   . PHE   A  1  202 ? 37.288  -7.788  31.346 1.00 31.33  ? 215 PHE   A O   1 
ATOM   1544 C  CB  . PHE   A  1  202 ? 39.443  -5.324  31.520 1.00 29.40  ? 215 PHE   A CB  1 
ATOM   1545 C  CG  . PHE   A  1  202 ? 40.931  -5.058  31.378 1.00 31.43  ? 215 PHE   A CG  1 
ATOM   1546 C  CD1 . PHE   A  1  202 ? 41.733  -5.826  30.530 1.00 32.52  ? 215 PHE   A CD1 1 
ATOM   1547 C  CD2 . PHE   A  1  202 ? 41.537  -4.066  32.141 1.00 33.96  ? 215 PHE   A CD2 1 
ATOM   1548 C  CE1 . PHE   A  1  202 ? 43.089  -5.573  30.417 1.00 32.45  ? 215 PHE   A CE1 1 
ATOM   1549 C  CE2 . PHE   A  1  202 ? 42.896  -3.841  32.052 1.00 34.81  ? 215 PHE   A CE2 1 
ATOM   1550 C  CZ  . PHE   A  1  202 ? 43.669  -4.595  31.187 1.00 36.14  ? 215 PHE   A CZ  1 
ATOM   1551 N  N   . PRO   A  1  203 ? 36.358  -5.927  30.606 1.00 31.12  ? 216 PRO   A N   1 
ATOM   1552 C  CA  . PRO   A  1  203 ? 35.033  -6.418  30.985 1.00 30.65  ? 216 PRO   A CA  1 
ATOM   1553 C  C   . PRO   A  1  203 ? 34.686  -7.742  30.307 1.00 32.09  ? 216 PRO   A C   1 
ATOM   1554 O  O   . PRO   A  1  203 ? 34.009  -8.579  30.889 1.00 32.68  ? 216 PRO   A O   1 
ATOM   1555 C  CB  . PRO   A  1  203 ? 34.113  -5.272  30.561 1.00 30.53  ? 216 PRO   A CB  1 
ATOM   1556 C  CG  . PRO   A  1  203 ? 35.013  -4.063  30.631 1.00 30.85  ? 216 PRO   A CG  1 
ATOM   1557 C  CD  . PRO   A  1  203 ? 36.331  -4.563  30.058 1.00 29.91  ? 216 PRO   A CD  1 
ATOM   1558 N  N   . ILE   A  1  204 ? 35.156  -7.923  29.074 1.00 32.05  ? 217 ILE   A N   1 
ATOM   1559 C  CA  . ILE   A  1  204 ? 34.841  -9.101  28.288 1.00 32.34  ? 217 ILE   A CA  1 
ATOM   1560 C  C   . ILE   A  1  204 ? 35.669  -10.281 28.767 1.00 32.21  ? 217 ILE   A C   1 
ATOM   1561 O  O   . ILE   A  1  204 ? 35.149  -11.374 28.971 1.00 33.32  ? 217 ILE   A O   1 
ATOM   1562 C  CB  . ILE   A  1  204 ? 35.110  -8.834  26.801 1.00 37.09  ? 217 ILE   A CB  1 
ATOM   1563 C  CG1 . ILE   A  1  204 ? 34.225  -7.721  26.285 1.00 38.73  ? 217 ILE   A CG1 1 
ATOM   1564 C  CG2 . ILE   A  1  204 ? 34.958  -10.111 25.976 1.00 38.22  ? 217 ILE   A CG2 1 
ATOM   1565 C  CD1 . ILE   A  1  204 ? 34.677  -7.154  24.956 1.00 37.29  ? 217 ILE   A CD1 1 
ATOM   1566 N  N   . ASN   A  1  205 ? 36.975  -10.063 28.926 1.00 32.02  ? 218 ASN   A N   1 
ATOM   1567 C  CA  . ASN   A  1  205 ? 37.871  -11.154 29.243 1.00 31.26  ? 218 ASN   A CA  1 
ATOM   1568 C  C   . ASN   A  1  205 ? 37.854  -11.481 30.723 1.00 30.05  ? 218 ASN   A C   1 
ATOM   1569 O  O   . ASN   A  1  205 ? 38.190  -12.604 31.052 1.00 36.26  ? 218 ASN   A O   1 
ATOM   1570 C  CB  . ASN   A  1  205 ? 39.306  -10.872 28.820 1.00 35.60  ? 218 ASN   A CB  1 
ATOM   1571 C  CG  . ASN   A  1  205 ? 39.383  -10.521 27.358 1.00 35.80  ? 218 ASN   A CG  1 
ATOM   1572 O  OD1 . ASN   A  1  205 ? 38.591  -11.038 26.568 1.00 38.61  ? 218 ASN   A OD1 1 
ATOM   1573 N  ND2 . ASN   A  1  205 ? 40.261  -9.600  26.995 1.00 38.97  ? 218 ASN   A ND2 1 
ATOM   1574 N  N   . LEU   A  1  206 ? 37.498  -10.529 31.595 1.00 27.87  ? 219 LEU   A N   1 
ATOM   1575 C  CA  . LEU   A  1  206 ? 37.661  -10.738 33.024 1.00 28.79  ? 219 LEU   A CA  1 
ATOM   1576 C  C   . LEU   A  1  206 ? 36.353  -10.652 33.810 1.00 27.75  ? 219 LEU   A C   1 
ATOM   1577 O  O   . LEU   A  1  206 ? 36.283  -11.228 34.896 1.00 27.44  ? 219 LEU   A O   1 
ATOM   1578 C  CB  . LEU   A  1  206 ? 38.696  -9.753  33.550 1.00 29.02  ? 219 LEU   A CB  1 
ATOM   1579 C  CG  . LEU   A  1  206 ? 40.092  -9.898  32.955 1.00 31.63  ? 219 LEU   A CG  1 
ATOM   1580 C  CD1 . LEU   A  1  206 ? 40.948  -8.702  33.330 1.00 32.23  ? 219 LEU   A CD1 1 
ATOM   1581 C  CD2 . LEU   A  1  206 ? 40.766  -11.193 33.410 1.00 34.29  ? 219 LEU   A CD2 1 
ATOM   1582 N  N   . PHE   A  1  207 ? 35.361  -9.893  33.328 1.00 29.81  ? 220 PHE   A N   1 
ATOM   1583 C  CA  . PHE   A  1  207 ? 34.149  -9.676  34.114 1.00 29.35  ? 220 PHE   A CA  1 
ATOM   1584 C  C   . PHE   A  1  207 ? 33.077  -10.675 33.701 1.00 28.34  ? 220 PHE   A C   1 
ATOM   1585 O  O   . PHE   A  1  207 ? 32.083  -10.850 34.407 1.00 29.63  ? 220 PHE   A O   1 
ATOM   1586 C  CB  . PHE   A  1  207 ? 33.559  -8.267  34.026 1.00 27.73  ? 220 PHE   A CB  1 
ATOM   1587 C  CG  . PHE   A  1  207 ? 34.392  -7.159  34.640 1.00 29.03  ? 220 PHE   A CG  1 
ATOM   1588 C  CD1 . PHE   A  1  207 ? 35.452  -7.439  35.494 1.00 28.74  ? 220 PHE   A CD1 1 
ATOM   1589 C  CD2 . PHE   A  1  207 ? 34.094  -5.829  34.365 1.00 30.57  ? 220 PHE   A CD2 1 
ATOM   1590 C  CE1 . PHE   A  1  207 ? 36.187  -6.409  36.053 1.00 30.11  ? 220 PHE   A CE1 1 
ATOM   1591 C  CE2 . PHE   A  1  207 ? 34.856  -4.811  34.903 1.00 30.38  ? 220 PHE   A CE2 1 
ATOM   1592 C  CZ  . PHE   A  1  207 ? 35.903  -5.103  35.743 1.00 31.13  ? 220 PHE   A CZ  1 
ATOM   1593 N  N   . VAL   A  1  208 ? 33.286  -11.310 32.548 1.00 32.56  ? 221 VAL   A N   1 
ATOM   1594 C  CA  . VAL   A  1  208 ? 32.431  -12.399 32.109 1.00 35.86  ? 221 VAL   A CA  1 
ATOM   1595 C  C   . VAL   A  1  208 ? 32.838  -13.654 32.863 1.00 33.06  ? 221 VAL   A C   1 
ATOM   1596 O  O   . VAL   A  1  208 ? 34.014  -13.954 32.980 1.00 36.55  ? 221 VAL   A O   1 
ATOM   1597 C  CB  . VAL   A  1  208 ? 32.484  -12.615 30.585 1.00 34.40  ? 221 VAL   A CB  1 
ATOM   1598 C  CG1 . VAL   A  1  208 ? 31.700  -13.840 30.140 1.00 33.49  ? 221 VAL   A CG1 1 
ATOM   1599 C  CG2 . VAL   A  1  208 ? 31.971  -11.388 29.855 1.00 32.66  ? 221 VAL   A CG2 1 
ATOM   1600 N  N   . ASP   A  1  209 ? 31.833  -14.368 33.373 1.00 38.37  ? 222 ASP   A N   1 
ATOM   1601 C  CA  . ASP   A  1  209 ? 32.043  -15.567 34.162 1.00 36.24  ? 222 ASP   A CA  1 
ATOM   1602 C  C   . ASP   A  1  209 ? 32.886  -16.555 33.361 1.00 36.77  ? 222 ASP   A C   1 
ATOM   1603 O  O   . ASP   A  1  209 ? 32.698  -16.723 32.166 1.00 37.71  ? 222 ASP   A O   1 
ATOM   1604 C  CB  . ASP   A  1  209 ? 30.709  -16.169 34.553 1.00 36.01  ? 222 ASP   A CB  1 
ATOM   1605 C  CG  . ASP   A  1  209 ? 30.802  -17.268 35.588 1.00 35.73  ? 222 ASP   A CG  1 
ATOM   1606 O  OD1 . ASP   A  1  209 ? 31.251  -18.376 35.216 1.00 42.39  ? 222 ASP   A OD1 1 
ATOM   1607 O  OD2 . ASP   A  1  209 ? 30.458  -16.990 36.756 1.00 36.60  ? 222 ASP   A OD2 1 
ATOM   1608 N  N   . GLY   A  1  210 ? 33.805  -17.236 34.038 1.00 37.38  ? 223 GLY   A N   1 
ATOM   1609 C  CA  . GLY   A  1  210 ? 34.782  -18.067 33.358 1.00 37.37  ? 223 GLY   A CA  1 
ATOM   1610 C  C   . GLY   A  1  210 ? 34.204  -19.383 32.847 1.00 38.81  ? 223 GLY   A C   1 
ATOM   1611 O  O   . GLY   A  1  210 ? 34.835  -20.039 32.027 1.00 39.23  ? 223 GLY   A O   1 
ATOM   1612 N  N   . ARG   A  1  211 ? 33.035  -19.785 33.356 1.00 40.09  ? 224 ARG   A N   1 
ATOM   1613 C  CA  . ARG   A  1  211 ? 32.330  -20.956 32.851 1.00 39.23  ? 224 ARG   A CA  1 
ATOM   1614 C  C   . ARG   A  1  211 ? 31.710  -20.666 31.483 1.00 39.65  ? 224 ARG   A C   1 
ATOM   1615 O  O   . ARG   A  1  211 ? 31.339  -21.590 30.787 1.00 40.82  ? 224 ARG   A O   1 
ATOM   1616 C  CB  . ARG   A  1  211 ? 31.235  -21.419 33.813 1.00 40.33  ? 224 ARG   A CB  1 
ATOM   1617 C  CG  . ARG   A  1  211 ? 31.796  -21.932 35.136 1.00 43.39  ? 224 ARG   A CG  1 
ATOM   1618 C  CD  . ARG   A  1  211 ? 30.730  -21.995 36.238 1.00 41.79  ? 224 ARG   A CD  1 
ATOM   1619 N  NE  . ARG   A  1  211 ? 30.188  -20.670 36.569 1.00 42.38  ? 224 ARG   A NE  1 
ATOM   1620 C  CZ  . ARG   A  1  211 ? 29.348  -20.407 37.559 1.00 45.59  ? 224 ARG   A CZ  1 
ATOM   1621 N  NH1 . ARG   A  1  211 ? 28.912  -21.385 38.330 1.00 48.20  ? 224 ARG   A NH1 1 
ATOM   1622 N  NH2 . ARG   A  1  211 ? 28.949  -19.163 37.786 1.00 44.58  ? 224 ARG   A NH2 1 
ATOM   1623 N  N   . VAL   A  1  212 ? 31.579  -19.395 31.085 1.00 45.48  ? 225 VAL   A N   1 
ATOM   1624 C  CA  . VAL   A  1  212 ? 31.111  -19.060 29.746 1.00 47.74  ? 225 VAL   A CA  1 
ATOM   1625 C  C   . VAL   A  1  212 ? 32.292  -19.153 28.775 1.00 50.75  ? 225 VAL   A C   1 
ATOM   1626 O  O   . VAL   A  1  212 ? 33.153  -18.281 28.763 1.00 47.00  ? 225 VAL   A O   1 
ATOM   1627 C  CB  . VAL   A  1  212 ? 30.466  -17.658 29.696 1.00 48.64  ? 225 VAL   A CB  1 
ATOM   1628 C  CG1 . VAL   A  1  212 ? 30.042  -17.267 28.278 1.00 46.56  ? 225 VAL   A CG1 1 
ATOM   1629 C  CG2 . VAL   A  1  212 ? 29.282  -17.550 30.646 1.00 49.85  ? 225 VAL   A CG2 1 
ATOM   1630 N  N   . THR   A  1  213 ? 32.317  -20.189 27.931 1.00 63.00  ? 226 THR   A N   1 
ATOM   1631 C  CA  . THR   A  1  213 ? 33.468  -20.446 27.065 1.00 74.51  ? 226 THR   A CA  1 
ATOM   1632 C  C   . THR   A  1  213 ? 33.294  -19.769 25.699 1.00 77.43  ? 226 THR   A C   1 
ATOM   1633 O  O   . THR   A  1  213 ? 34.275  -19.404 25.055 1.00 63.20  ? 226 THR   A O   1 
ATOM   1634 C  CB  . THR   A  1  213 ? 33.688  -21.957 26.931 1.00 74.92  ? 226 THR   A CB  1 
ATOM   1635 O  OG1 . THR   A  1  213 ? 32.481  -22.525 26.429 1.00 72.76  ? 226 THR   A OG1 1 
ATOM   1636 C  CG2 . THR   A  1  213 ? 34.025  -22.615 28.260 1.00 76.45  ? 226 THR   A CG2 1 
ATOM   1637 N  N   . THR   A  1  214 ? 32.037  -19.557 25.290 1.00 83.67  ? 227 THR   A N   1 
ATOM   1638 C  CA  . THR   A  1  214 ? 31.712  -19.191 23.920 1.00 87.29  ? 227 THR   A CA  1 
ATOM   1639 C  C   . THR   A  1  214 ? 30.787  -17.969 23.899 1.00 83.95  ? 227 THR   A C   1 
ATOM   1640 O  O   . THR   A  1  214 ? 29.852  -17.889 24.693 1.00 79.26  ? 227 THR   A O   1 
ATOM   1641 C  CB  . THR   A  1  214 ? 31.073  -20.427 23.273 1.00 85.70  ? 227 THR   A CB  1 
ATOM   1642 O  OG1 . THR   A  1  214 ? 31.029  -20.134 21.882 1.00 84.20  ? 227 THR   A OG1 1 
ATOM   1643 C  CG2 . THR   A  1  214 ? 29.703  -20.779 23.840 1.00 83.00  ? 227 THR   A CG2 1 
ATOM   1644 N  N   . ASP   A  1  215 ? 31.024  -17.029 22.969 1.00 83.02  ? 228 ASP   A N   1 
ATOM   1645 C  CA  . ASP   A  1  215 ? 30.154  -15.871 22.800 1.00 86.64  ? 228 ASP   A CA  1 
ATOM   1646 C  C   . ASP   A  1  215 ? 30.180  -15.083 24.110 1.00 70.09  ? 228 ASP   A C   1 
ATOM   1647 O  O   . ASP   A  1  215 ? 29.164  -14.913 24.782 1.00 64.34  ? 228 ASP   A O   1 
ATOM   1648 C  CB  . ASP   A  1  215 ? 28.756  -16.280 22.341 1.00 101.43 ? 228 ASP   A CB  1 
ATOM   1649 C  CG  . ASP   A  1  215 ? 27.797  -15.157 21.935 1.00 116.82 ? 228 ASP   A CG  1 
ATOM   1650 O  OD1 . ASP   A  1  215 ? 28.269  -14.032 21.642 1.00 120.60 ? 228 ASP   A OD1 1 
ATOM   1651 O  OD2 . ASP   A  1  215 ? 26.562  -15.398 21.940 1.00 116.00 ? 228 ASP   A OD2 1 
ATOM   1652 N  N   . ARG   A  1  216 ? 31.381  -14.633 24.479 1.00 56.02  ? 229 ARG   A N   1 
ATOM   1653 C  CA  . ARG   A  1  216 ? 31.592  -13.998 25.761 1.00 50.54  ? 229 ARG   A CA  1 
ATOM   1654 C  C   . ARG   A  1  216 ? 31.004  -12.595 25.678 1.00 41.42  ? 229 ARG   A C   1 
ATOM   1655 O  O   . ARG   A  1  216 ? 31.335  -11.828 24.787 1.00 42.32  ? 229 ARG   A O   1 
ATOM   1656 C  CB  . ARG   A  1  216 ? 33.069  -14.099 26.163 1.00 52.09  ? 229 ARG   A CB  1 
ATOM   1657 C  CG  . ARG   A  1  216 ? 33.495  -15.490 26.631 1.00 54.36  ? 229 ARG   A CG  1 
ATOM   1658 C  CD  . ARG   A  1  216 ? 34.997  -15.599 26.925 1.00 50.91  ? 229 ARG   A CD  1 
ATOM   1659 N  NE  . ARG   A  1  216 ? 35.401  -14.814 28.099 1.00 55.33  ? 229 ARG   A NE  1 
ATOM   1660 C  CZ  . ARG   A  1  216 ? 35.168  -15.124 29.384 1.00 62.24  ? 229 ARG   A CZ  1 
ATOM   1661 N  NH1 . ARG   A  1  216 ? 34.555  -16.246 29.706 1.00 54.21  ? 229 ARG   A NH1 1 
ATOM   1662 N  NH2 . ARG   A  1  216 ? 35.584  -14.323 30.361 1.00 70.55  ? 229 ARG   A NH2 1 
ATOM   1663 N  N   . LYS   A  1  217 ? 30.111  -12.284 26.615 1.00 35.65  ? 230 LYS   A N   1 
ATOM   1664 C  CA  . LYS   A  1  217 ? 29.402  -11.023 26.605 1.00 35.51  ? 230 LYS   A CA  1 
ATOM   1665 C  C   . LYS   A  1  217 ? 28.977  -10.729 28.033 1.00 31.27  ? 230 LYS   A C   1 
ATOM   1666 O  O   . LYS   A  1  217 ? 28.658  -11.655 28.766 1.00 34.80  ? 230 LYS   A O   1 
ATOM   1667 C  CB  . LYS   A  1  217 ? 28.212  -11.153 25.648 1.00 38.94  ? 230 LYS   A CB  1 
ATOM   1668 C  CG  . LYS   A  1  217 ? 27.161  -12.169 26.080 1.00 38.93  ? 230 LYS   A CG  1 
ATOM   1669 C  CD  . LYS   A  1  217 ? 26.025  -12.366 25.084 1.00 43.09  ? 230 LYS   A CD  1 
ATOM   1670 C  CE  . LYS   A  1  217 ? 24.861  -13.099 25.718 1.00 48.10  ? 230 LYS   A CE  1 
ATOM   1671 N  NZ  . LYS   A  1  217 ? 23.839  -13.500 24.755 1.00 44.23  ? 230 LYS   A NZ  1 
ATOM   1672 N  N   . LEU   A  1  218 ? 28.979  -9.448  28.402 1.00 30.54  ? 231 LEU   A N   1 
ATOM   1673 C  CA  . LEU   A  1  218 ? 28.685  -9.054  29.766 1.00 30.53  ? 231 LEU   A CA  1 
ATOM   1674 C  C   . LEU   A  1  218 ? 27.271  -8.474  29.848 1.00 30.07  ? 231 LEU   A C   1 
ATOM   1675 O  O   . LEU   A  1  218 ? 26.936  -7.571  29.098 1.00 34.26  ? 231 LEU   A O   1 
ATOM   1676 C  CB  . LEU   A  1  218 ? 29.757  -8.041  30.160 1.00 29.53  ? 231 LEU   A CB  1 
ATOM   1677 C  CG  . LEU   A  1  218 ? 29.690  -7.559  31.614 1.00 31.93  ? 231 LEU   A CG  1 
ATOM   1678 C  CD1 . LEU   A  1  218 ? 29.964  -8.670  32.616 1.00 32.15  ? 231 LEU   A CD1 1 
ATOM   1679 C  CD2 . LEU   A  1  218 ? 30.614  -6.395  31.829 1.00 30.59  ? 231 LEU   A CD2 1 
ATOM   1680 N  N   . SER   A  1  219 ? 26.460  -8.956  30.792 1.00 32.26  ? 232 SER   A N   1 
ATOM   1681 C  CA  . SER   A  1  219 ? 25.137  -8.388  31.028 1.00 32.00  ? 232 SER   A CA  1 
ATOM   1682 C  C   . SER   A  1  219 ? 25.271  -7.030  31.714 1.00 28.57  ? 232 SER   A C   1 
ATOM   1683 O  O   . SER   A  1  219 ? 26.277  -6.739  32.347 1.00 28.28  ? 232 SER   A O   1 
ATOM   1684 C  CB  . SER   A  1  219 ? 24.267  -9.328  31.840 1.00 30.34  ? 232 SER   A CB  1 
ATOM   1685 O  OG  . SER   A  1  219 ? 24.738  -9.435  33.180 1.00 35.32  ? 232 SER   A OG  1 
ATOM   1686 N  N   . MET   A  1  220 ? 24.236  -6.207  31.598 1.00 32.05  ? 233 MET   A N   1 
ATOM   1687 C  CA  . MET   A  1  220 ? 24.236  -4.884  32.205 1.00 31.15  ? 233 MET   A CA  1 
ATOM   1688 C  C   . MET   A  1  220 ? 24.089  -4.967  33.720 1.00 32.34  ? 233 MET   A C   1 
ATOM   1689 O  O   . MET   A  1  220 ? 24.617  -4.107  34.418 1.00 38.96  ? 233 MET   A O   1 
ATOM   1690 C  CB  . MET   A  1  220 ? 23.134  -4.026  31.592 1.00 30.46  ? 233 MET   A CB  1 
ATOM   1691 C  CG  . MET   A  1  220 ? 23.324  -3.797  30.094 1.00 30.89  ? 233 MET   A CG  1 
ATOM   1692 S  SD  . MET   A  1  220 ? 24.880  -2.977  29.688 1.00 34.10  ? 233 MET   A SD  1 
ATOM   1693 C  CE  . MET   A  1  220 ? 25.807  -4.395  29.084 1.00 35.57  ? 233 MET   A CE  1 
ATOM   1694 N  N   . GLU   A  1  221 ? 23.432  -6.020  34.228 1.00 33.11  ? 234 GLU   A N   1 
ATOM   1695 C  CA  . GLU   A  1  221 ? 23.321  -6.243  35.667 1.00 36.04  ? 234 GLU   A CA  1 
ATOM   1696 C  C   . GLU   A  1  221 ? 24.711  -6.499  36.265 1.00 35.13  ? 234 GLU   A C   1 
ATOM   1697 O  O   . GLU   A  1  221 ? 25.048  -6.001  37.328 1.00 31.03  ? 234 GLU   A O   1 
ATOM   1698 C  CB  . GLU   A  1  221 ? 22.409  -7.431  35.984 1.00 37.98  ? 234 GLU   A CB  1 
ATOM   1699 C  CG  . GLU   A  1  221 ? 20.963  -7.254  35.517 1.00 45.44  ? 234 GLU   A CG  1 
ATOM   1700 C  CD  . GLU   A  1  221 ? 20.616  -7.493  34.031 1.00 53.07  ? 234 GLU   A CD  1 
ATOM   1701 O  OE1 . GLU   A  1  221 ? 21.469  -7.723  33.120 1.00 45.03  ? 234 GLU   A OE1 1 
ATOM   1702 O  OE2 . GLU   A  1  221 ? 19.386  -7.439  33.778 1.00 57.67  ? 234 GLU   A OE2 1 
ATOM   1703 N  N   . ASP   A  1  222 ? 25.498  -7.338  35.585 1.00 34.08  ? 235 ASP   A N   1 
ATOM   1704 C  CA  . ASP   A  1  222 ? 26.823  -7.708  36.041 1.00 32.05  ? 235 ASP   A CA  1 
ATOM   1705 C  C   . ASP   A  1  222 ? 27.759  -6.507  35.898 1.00 32.73  ? 235 ASP   A C   1 
ATOM   1706 O  O   . ASP   A  1  222 ? 28.543  -6.214  36.809 1.00 30.27  ? 235 ASP   A O   1 
ATOM   1707 C  CB  . ASP   A  1  222 ? 27.336  -8.950  35.335 1.00 35.04  ? 235 ASP   A CB  1 
ATOM   1708 C  CG  . ASP   A  1  222 ? 26.671  -10.279 35.701 1.00 36.74  ? 235 ASP   A CG  1 
ATOM   1709 O  OD1 . ASP   A  1  222 ? 25.778  -10.292 36.586 1.00 38.00  ? 235 ASP   A OD1 1 
ATOM   1710 O  OD2 . ASP   A  1  222 ? 27.063  -11.320 35.105 1.00 36.98  ? 235 ASP   A OD2 1 
ATOM   1711 N  N   . ALA   A  1  223 ? 27.634  -5.773  34.783 1.00 28.02  ? 236 ALA   A N   1 
ATOM   1712 C  CA  . ALA   A  1  223 ? 28.383  -4.542  34.634 1.00 28.96  ? 236 ALA   A CA  1 
ATOM   1713 C  C   . ALA   A  1  223 ? 28.062  -3.564  35.763 1.00 27.54  ? 236 ALA   A C   1 
ATOM   1714 O  O   . ALA   A  1  223 ? 28.974  -3.010  36.362 1.00 29.80  ? 236 ALA   A O   1 
ATOM   1715 C  CB  . ALA   A  1  223 ? 28.142  -3.941  33.279 1.00 30.06  ? 236 ALA   A CB  1 
ATOM   1716 N  N   . ALA   A  1  224 ? 26.784  -3.350  36.077 1.00 29.72  ? 237 ALA   A N   1 
ATOM   1717 C  CA  . ALA   A  1  224 ? 26.442  -2.371  37.107 1.00 31.22  ? 237 ALA   A CA  1 
ATOM   1718 C  C   . ALA   A  1  224 ? 27.015  -2.828  38.445 1.00 28.87  ? 237 ALA   A C   1 
ATOM   1719 O  O   . ALA   A  1  224 ? 27.552  -2.041  39.218 1.00 28.78  ? 237 ALA   A O   1 
ATOM   1720 C  CB  . ALA   A  1  224 ? 24.940  -2.166  37.206 1.00 29.45  ? 237 ALA   A CB  1 
ATOM   1721 N  N   . SER   A  1  225 ? 26.897  -4.122  38.694 1.00 25.86  ? 238 SER   A N   1 
ATOM   1722 C  CA  . SER   A  1  225 ? 27.334  -4.680  39.955 1.00 32.37  ? 238 SER   A CA  1 
ATOM   1723 C  C   . SER   A  1  225 ? 28.804  -4.334  40.198 1.00 27.89  ? 238 SER   A C   1 
ATOM   1724 O  O   . SER   A  1  225 ? 29.163  -3.900  41.292 1.00 28.05  ? 238 SER   A O   1 
ATOM   1725 C  CB  . SER   A  1  225 ? 27.069  -6.169  40.003 1.00 33.48  ? 238 SER   A CB  1 
ATOM   1726 O  OG  . SER   A  1  225 ? 27.470  -6.711  41.253 1.00 38.62  ? 238 SER   A OG  1 
ATOM   1727 N  N   . ILE   A  1  226 ? 29.627  -4.474  39.156 1.00 26.39  ? 239 ILE   A N   1 
ATOM   1728 C  CA  . ILE   A  1  226 ? 31.063  -4.293  39.302 1.00 29.01  ? 239 ILE   A CA  1 
ATOM   1729 C  C   . ILE   A  1  226 ? 31.431  -2.807  39.225 1.00 27.97  ? 239 ILE   A C   1 
ATOM   1730 O  O   . ILE   A  1  226 ? 32.105  -2.278  40.108 1.00 26.64  ? 239 ILE   A O   1 
ATOM   1731 C  CB  . ILE   A  1  226 ? 31.801  -5.150  38.259 1.00 28.31  ? 239 ILE   A CB  1 
ATOM   1732 C  CG1 . ILE   A  1  226 ? 31.615  -6.615  38.552 1.00 31.53  ? 239 ILE   A CG1 1 
ATOM   1733 C  CG2 . ILE   A  1  226 ? 33.279  -4.791  38.177 1.00 26.53  ? 239 ILE   A CG2 1 
ATOM   1734 C  CD1 . ILE   A  1  226 ? 31.918  -7.522  37.373 1.00 35.99  ? 239 ILE   A CD1 1 
ATOM   1735 N  N   . PHE   A  1  227 ? 30.971  -2.137  38.169 1.00 28.80  ? 240 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A  1  227 ? 31.362  -0.765  37.903 1.00 28.50  ? 240 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A  1  227 ? 30.779  0.203   38.931 1.00 24.87  ? 240 PHE   A C   1 
ATOM   1738 O  O   . PHE   A  1  227 ? 31.443  1.158   39.298 1.00 27.14  ? 240 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A  1  227 ? 30.886  -0.341  36.515 1.00 29.71  ? 240 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A  1  227 ? 31.730  -0.840  35.359 1.00 31.72  ? 240 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A  1  227 ? 32.962  -0.268  35.074 1.00 35.03  ? 240 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A  1  227 ? 31.255  -1.812  34.498 1.00 38.55  ? 240 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A  1  227 ? 33.708  -0.695  33.987 1.00 33.40  ? 240 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A  1  227 ? 32.013  -2.224  33.409 1.00 38.48  ? 240 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A  1  227 ? 33.226  -1.650  33.154 1.00 33.34  ? 240 PHE   A CZ  1 
ATOM   1746 N  N   . ARG   A  1  228 ? 29.547  -0.028  39.374 1.00 23.43  ? 241 ARG   A N   1 
ATOM   1747 C  CA  . ARG   A  1  228 ? 28.903  0.866   40.318 1.00 24.60  ? 241 ARG   A CA  1 
ATOM   1748 C  C   . ARG   A  1  228 ? 29.044  0.351   41.749 1.00 23.97  ? 241 ARG   A C   1 
ATOM   1749 O  O   . ARG   A  1  228 ? 29.424  1.117   42.613 1.00 23.35  ? 241 ARG   A O   1 
ATOM   1750 C  CB  . ARG   A  1  228 ? 27.435  1.119   39.968 1.00 26.06  ? 241 ARG   A CB  1 
ATOM   1751 C  CG  . ARG   A  1  228 ? 26.770  2.102   40.927 1.00 28.71  ? 241 ARG   A CG  1 
ATOM   1752 C  CD  . ARG   A  1  228 ? 25.364  2.528   40.544 1.00 27.90  ? 241 ARG   A CD  1 
ATOM   1753 N  NE  . ARG   A  1  228 ? 24.461  1.376   40.492 1.00 29.93  ? 241 ARG   A NE  1 
ATOM   1754 C  CZ  . ARG   A  1  228 ? 23.714  0.991   39.462 1.00 31.40  ? 241 ARG   A CZ  1 
ATOM   1755 N  NH1 . ARG   A  1  228 ? 23.773  1.629   38.308 1.00 32.71  ? 241 ARG   A NH1 1 
ATOM   1756 N  NH2 . ARG   A  1  228 ? 22.906  -0.062  39.595 1.00 32.36  ? 241 ARG   A NH2 1 
ATOM   1757 N  N   . ASP   A  1  229 ? 28.738  -0.924  42.012 1.00 26.19  ? 242 ASP   A N   1 
ATOM   1758 C  CA  . ASP   A  1  229 ? 28.620  -1.369  43.393 1.00 26.06  ? 242 ASP   A CA  1 
ATOM   1759 C  C   . ASP   A  1  229 ? 29.896  -2.017  43.925 1.00 25.00  ? 242 ASP   A C   1 
ATOM   1760 O  O   . ASP   A  1  229 ? 29.991  -2.266  45.122 1.00 28.09  ? 242 ASP   A O   1 
ATOM   1761 C  CB  . ASP   A  1  229 ? 27.391  -2.226  43.607 1.00 30.29  ? 242 ASP   A CB  1 
ATOM   1762 C  CG  . ASP   A  1  229 ? 26.048  -1.613  43.241 1.00 33.21  ? 242 ASP   A CG  1 
ATOM   1763 O  OD1 . ASP   A  1  229 ? 25.861  -0.389  43.413 1.00 39.46  ? 242 ASP   A OD1 1 
ATOM   1764 O  OD2 . ASP   A  1  229 ? 25.160  -2.391  42.872 1.00 37.20  ? 242 ASP   A OD2 1 
ATOM   1765 N  N   . MET   A  1  230 ? 30.888  -2.255  43.073 1.00 26.75  ? 243 MET   A N   1 
ATOM   1766 C  CA  A MET   A  1  230 ? 32.145  -2.872  43.480 0.50 26.65  ? 243 MET   A CA  1 
ATOM   1767 C  CA  B MET   A  1  230 ? 32.146  -2.871  43.481 0.50 28.25  ? 243 MET   A CA  1 
ATOM   1768 C  C   . MET   A  1  230 ? 31.881  -4.269  44.039 1.00 27.38  ? 243 MET   A C   1 
ATOM   1769 O  O   . MET   A  1  230 ? 32.514  -4.689  45.012 1.00 29.70  ? 243 MET   A O   1 
ATOM   1770 C  CB  A MET   A  1  230 ? 32.857  -2.024  44.538 0.50 26.57  ? 243 MET   A CB  1 
ATOM   1771 C  CB  B MET   A  1  230 ? 32.860  -2.022  44.539 0.50 30.65  ? 243 MET   A CB  1 
ATOM   1772 C  CG  A MET   A  1  230 ? 33.018  -0.578  44.136 0.50 25.65  ? 243 MET   A CG  1 
ATOM   1773 C  CG  B MET   A  1  230 ? 33.011  -0.565  44.150 0.50 32.14  ? 243 MET   A CG  1 
ATOM   1774 S  SD  A MET   A  1  230 ? 33.735  0.374   45.484 0.50 25.22  ? 243 MET   A SD  1 
ATOM   1775 S  SD  B MET   A  1  230 ? 33.701  0.419   45.494 0.50 36.20  ? 243 MET   A SD  1 
ATOM   1776 C  CE  A MET   A  1  230 ? 32.364  0.523   46.639 0.50 22.06  ? 243 MET   A CE  1 
ATOM   1777 C  CE  B MET   A  1  230 ? 33.221  2.093   45.018 0.50 38.05  ? 243 MET   A CE  1 
ATOM   1778 N  N   . ARG   A  1  231 ? 30.939  -4.968  43.403 1.00 27.86  ? 244 ARG   A N   1 
ATOM   1779 C  CA  A ARG   A  1  231 ? 30.429  -6.246  43.864 0.50 27.15  ? 244 ARG   A CA  1 
ATOM   1780 C  CA  B ARG   A  1  231 ? 30.436  -6.248  43.863 0.50 26.83  ? 244 ARG   A CA  1 
ATOM   1781 C  C   . ARG   A  1  231 ? 30.526  -7.268  42.734 1.00 26.48  ? 244 ARG   A C   1 
ATOM   1782 O  O   . ARG   A  1  231 ? 30.087  -7.018  41.621 1.00 26.35  ? 244 ARG   A O   1 
ATOM   1783 C  CB  A ARG   A  1  231 ? 28.974  -6.100  44.314 0.50 27.16  ? 244 ARG   A CB  1 
ATOM   1784 C  CB  B ARG   A  1  231 ? 28.983  -6.091  44.307 0.50 26.32  ? 244 ARG   A CB  1 
ATOM   1785 C  CG  A ARG   A  1  231 ? 28.390  -7.345  44.974 0.50 28.57  ? 244 ARG   A CG  1 
ATOM   1786 C  CG  B ARG   A  1  231 ? 28.357  -7.311  44.968 0.50 27.12  ? 244 ARG   A CG  1 
ATOM   1787 C  CD  A ARG   A  1  231 ? 26.943  -7.253  45.432 0.50 29.35  ? 244 ARG   A CD  1 
ATOM   1788 C  CD  B ARG   A  1  231 ? 26.955  -6.953  45.464 0.50 27.38  ? 244 ARG   A CD  1 
ATOM   1789 N  NE  A ARG   A  1  231 ? 26.038  -7.352  44.274 0.50 36.41  ? 244 ARG   A NE  1 
ATOM   1790 N  NE  B ARG   A  1  231 ? 26.071  -6.650  44.323 0.50 33.31  ? 244 ARG   A NE  1 
ATOM   1791 C  CZ  A ARG   A  1  231 ? 25.769  -8.452  43.557 0.50 35.41  ? 244 ARG   A CZ  1 
ATOM   1792 C  CZ  B ARG   A  1  231 ? 25.380  -5.532  44.035 0.50 31.64  ? 244 ARG   A CZ  1 
ATOM   1793 N  NH1 A ARG   A  1  231 ? 26.139  -9.643  44.005 0.50 37.73  ? 244 ARG   A NH1 1 
ATOM   1794 N  NH1 B ARG   A  1  231 ? 25.308  -4.517  44.883 0.50 33.31  ? 244 ARG   A NH1 1 
ATOM   1795 N  NH2 A ARG   A  1  231 ? 25.117  -8.346  42.410 0.50 30.81  ? 244 ARG   A NH2 1 
ATOM   1796 N  NH2 B ARG   A  1  231 ? 24.719  -5.465  42.898 0.50 30.08  ? 244 ARG   A NH2 1 
ATOM   1797 N  N   . PHE   A  1  232 ? 31.101  -8.428  43.039 1.00 28.84  ? 245 PHE   A N   1 
ATOM   1798 C  CA  . PHE   A  1  232 ? 31.090  -9.546  42.113 1.00 27.92  ? 245 PHE   A CA  1 
ATOM   1799 C  C   . PHE   A  1  232 ? 29.658  -10.014 41.899 1.00 27.21  ? 245 PHE   A C   1 
ATOM   1800 O  O   . PHE   A  1  232 ? 28.855  -10.018 42.827 1.00 26.80  ? 245 PHE   A O   1 
ATOM   1801 C  CB  . PHE   A  1  232 ? 31.830  -10.744 42.689 1.00 27.73  ? 245 PHE   A CB  1 
ATOM   1802 C  CG  . PHE   A  1  232 ? 33.339  -10.667 42.662 1.00 29.05  ? 245 PHE   A CG  1 
ATOM   1803 C  CD1 . PHE   A  1  232 ? 34.010  -10.632 41.450 1.00 28.74  ? 245 PHE   A CD1 1 
ATOM   1804 C  CD2 . PHE   A  1  232 ? 34.077  -10.701 43.837 1.00 30.00  ? 245 PHE   A CD2 1 
ATOM   1805 C  CE1 . PHE   A  1  232 ? 35.394  -10.588 41.423 1.00 32.03  ? 245 PHE   A CE1 1 
ATOM   1806 C  CE2 . PHE   A  1  232 ? 35.463  -10.651 43.797 1.00 29.91  ? 245 PHE   A CE2 1 
ATOM   1807 C  CZ  . PHE   A  1  232 ? 36.114  -10.604 42.594 1.00 29.60  ? 245 PHE   A CZ  1 
ATOM   1808 N  N   . PRO   A  1  233 ? 29.286  -10.434 40.676 1.00 27.78  ? 246 PRO   A N   1 
ATOM   1809 C  CA  . PRO   A  1  233 ? 28.016  -11.137 40.487 1.00 31.29  ? 246 PRO   A CA  1 
ATOM   1810 C  C   . PRO   A  1  233 ? 27.936  -12.335 41.434 1.00 30.38  ? 246 PRO   A C   1 
ATOM   1811 O  O   . PRO   A  1  233 ? 28.948  -12.882 41.863 1.00 30.15  ? 246 PRO   A O   1 
ATOM   1812 C  CB  . PRO   A  1  233 ? 28.014  -11.529 39.001 1.00 27.33  ? 246 PRO   A CB  1 
ATOM   1813 C  CG  . PRO   A  1  233 ? 28.994  -10.558 38.360 1.00 28.59  ? 246 PRO   A CG  1 
ATOM   1814 C  CD  . PRO   A  1  233 ? 30.016  -10.213 39.424 1.00 27.42  ? 246 PRO   A CD  1 
ATOM   1815 N  N   . ASP   A  1  234 ? 26.710  -12.721 41.776 1.00 32.05  ? 247 ASP   A N   1 
ATOM   1816 C  CA  . ASP   A  1  234 ? 26.502  -13.894 42.610 1.00 33.70  ? 247 ASP   A CA  1 
ATOM   1817 C  C   . ASP   A  1  234 ? 27.157  -15.097 41.941 1.00 32.06  ? 247 ASP   A C   1 
ATOM   1818 O  O   . ASP   A  1  234 ? 27.073  -15.270 40.733 1.00 30.05  ? 247 ASP   A O   1 
ATOM   1819 C  CB  . ASP   A  1  234 ? 25.034  -14.167 42.883 1.00 35.97  ? 247 ASP   A CB  1 
ATOM   1820 C  CG  . ASP   A  1  234 ? 24.314  -13.154 43.773 1.00 41.96  ? 247 ASP   A CG  1 
ATOM   1821 O  OD1 . ASP   A  1  234 ? 24.951  -12.151 44.221 1.00 37.62  ? 247 ASP   A OD1 1 
ATOM   1822 O  OD2 . ASP   A  1  234 ? 23.104  -13.379 44.015 1.00 42.78  ? 247 ASP   A OD2 1 
ATOM   1823 N  N   . ASP   A  1  235 ? 27.845  -15.901 42.744 1.00 31.25  ? 248 ASP   A N   1 
ATOM   1824 C  CA  . ASP   A  1  235 ? 28.429  -17.143 42.277 1.00 34.11  ? 248 ASP   A CA  1 
ATOM   1825 C  C   . ASP   A  1  235 ? 29.453  -16.902 41.161 1.00 30.83  ? 248 ASP   A C   1 
ATOM   1826 O  O   . ASP   A  1  235 ? 29.616  -17.733 40.273 1.00 31.40  ? 248 ASP   A O   1 
ATOM   1827 C  CB  . ASP   A  1  235 ? 27.325  -18.101 41.851 1.00 37.51  ? 248 ASP   A CB  1 
ATOM   1828 C  CG  . ASP   A  1  235 ? 27.803  -19.531 41.666 1.00 40.42  ? 248 ASP   A CG  1 
ATOM   1829 O  OD1 . ASP   A  1  235 ? 28.442  -20.054 42.603 1.00 47.53  ? 248 ASP   A OD1 1 
ATOM   1830 O  OD2 . ASP   A  1  235 ? 27.585  -20.087 40.573 1.00 42.19  ? 248 ASP   A OD2 1 
ATOM   1831 N  N   . PHE   A  1  236 ? 30.154  -15.768 41.192 1.00 28.07  ? 249 PHE   A N   1 
ATOM   1832 C  CA  . PHE   A  1  236 ? 31.048  -15.414 40.110 1.00 28.00  ? 249 PHE   A CA  1 
ATOM   1833 C  C   . PHE   A  1  236 ? 32.247  -16.342 40.070 1.00 27.18  ? 249 PHE   A C   1 
ATOM   1834 O  O   . PHE   A  1  236 ? 32.928  -16.538 41.073 1.00 26.65  ? 249 PHE   A O   1 
ATOM   1835 C  CB  . PHE   A  1  236 ? 31.571  -13.981 40.252 1.00 29.69  ? 249 PHE   A CB  1 
ATOM   1836 C  CG  . PHE   A  1  236 ? 32.475  -13.562 39.106 1.00 26.55  ? 249 PHE   A CG  1 
ATOM   1837 C  CD1 . PHE   A  1  236 ? 31.951  -13.325 37.852 1.00 26.79  ? 249 PHE   A CD1 1 
ATOM   1838 C  CD2 . PHE   A  1  236 ? 33.837  -13.396 39.309 1.00 28.18  ? 249 PHE   A CD2 1 
ATOM   1839 C  CE1 . PHE   A  1  236 ? 32.772  -12.936 36.815 1.00 30.32  ? 249 PHE   A CE1 1 
ATOM   1840 C  CE2 . PHE   A  1  236 ? 34.663  -13.011 38.273 1.00 29.39  ? 249 PHE   A CE2 1 
ATOM   1841 C  CZ  . PHE   A  1  236 ? 34.128  -12.762 37.034 1.00 29.15  ? 249 PHE   A CZ  1 
ATOM   1842 N  N   . HIS   A  1  237 ? 32.530  -16.864 38.876 1.00 28.33  ? 250 HIS   A N   1 
ATOM   1843 C  CA  . HIS   A  1  237 ? 33.711  -17.690 38.668 1.00 29.49  ? 250 HIS   A CA  1 
ATOM   1844 C  C   . HIS   A  1  237 ? 34.655  -16.952 37.735 1.00 27.32  ? 250 HIS   A C   1 
ATOM   1845 O  O   . HIS   A  1  237 ? 34.242  -16.491 36.677 1.00 28.16  ? 250 HIS   A O   1 
ATOM   1846 C  CB  . HIS   A  1  237 ? 33.357  -19.043 38.043 1.00 30.71  ? 250 HIS   A CB  1 
ATOM   1847 C  CG  . HIS   A  1  237 ? 32.692  -19.991 38.969 1.00 34.80  ? 250 HIS   A CG  1 
ATOM   1848 N  ND1 . HIS   A  1  237 ? 31.606  -19.640 39.743 1.00 35.74  ? 250 HIS   A ND1 1 
ATOM   1849 C  CD2 . HIS   A  1  237 ? 32.955  -21.292 39.235 1.00 36.32  ? 250 HIS   A CD2 1 
ATOM   1850 C  CE1 . HIS   A  1  237 ? 31.244  -20.704 40.465 1.00 40.47  ? 250 HIS   A CE1 1 
ATOM   1851 N  NE2 . HIS   A  1  237 ? 32.053  -21.714 40.172 1.00 36.75  ? 250 HIS   A NE2 1 
ATOM   1852 N  N   . ARG   A  1  238 ? 35.925  -16.886 38.113 1.00 26.79  ? 251 ARG   A N   1 
ATOM   1853 C  CA  . ARG   A  1  238 ? 36.884  -16.126 37.340 1.00 27.51  ? 251 ARG   A CA  1 
ATOM   1854 C  C   . ARG   A  1  238 ? 37.154  -16.816 36.008 1.00 26.67  ? 251 ARG   A C   1 
ATOM   1855 O  O   . ARG   A  1  238 ? 36.835  -17.981 35.817 1.00 25.79  ? 251 ARG   A O   1 
ATOM   1856 C  CB  . ARG   A  1  238 ? 38.187  -15.965 38.123 1.00 29.56  ? 251 ARG   A CB  1 
ATOM   1857 C  CG  . ARG   A  1  238 ? 38.942  -17.273 38.293 1.00 30.46  ? 251 ARG   A CG  1 
ATOM   1858 C  CD  . ARG   A  1  238 ? 40.200  -17.087 39.088 1.00 29.79  ? 251 ARG   A CD  1 
ATOM   1859 N  NE  . ARG   A  1  238 ? 41.061  -18.247 38.870 1.00 31.22  ? 251 ARG   A NE  1 
ATOM   1860 C  CZ  . ARG   A  1  238 ? 42.168  -18.528 39.539 1.00 35.91  ? 251 ARG   A CZ  1 
ATOM   1861 N  NH1 . ARG   A  1  238 ? 42.625  -17.684 40.446 1.00 34.80  ? 251 ARG   A NH1 1 
ATOM   1862 N  NH2 . ARG   A  1  238 ? 42.827  -19.652 39.282 1.00 37.29  ? 251 ARG   A NH2 1 
ATOM   1863 N  N   . SER   A  1  239 ? 37.752  -16.054 35.093 1.00 27.02  ? 252 SER   A N   1 
ATOM   1864 C  CA  . SER   A  1  239 ? 38.240  -16.566 33.825 1.00 28.98  ? 252 SER   A CA  1 
ATOM   1865 C  C   . SER   A  1  239 ? 38.954  -17.909 34.007 1.00 31.61  ? 252 SER   A C   1 
ATOM   1866 O  O   . SER   A  1  239 ? 39.617  -18.166 35.016 1.00 33.21  ? 252 SER   A O   1 
ATOM   1867 C  CB  . SER   A  1  239 ? 39.162  -15.555 33.213 1.00 28.65  ? 252 SER   A CB  1 
ATOM   1868 O  OG  . SER   A  1  239 ? 39.814  -16.071 32.061 1.00 31.73  ? 252 SER   A OG  1 
ATOM   1869 N  N   . ALA   A  1  240 ? 38.809  -18.777 33.014 1.00 32.40  ? 253 ALA   A N   1 
ATOM   1870 C  CA  . ALA   A  1  240 ? 39.310  -20.143 33.122 1.00 35.97  ? 253 ALA   A CA  1 
ATOM   1871 C  C   . ALA   A  1  240 ? 40.780  -20.198 32.712 1.00 33.95  ? 253 ALA   A C   1 
ATOM   1872 O  O   . ALA   A  1  240 ? 41.418  -21.219 32.922 1.00 34.40  ? 253 ALA   A O   1 
ATOM   1873 C  CB  . ALA   A  1  240 ? 38.479  -21.066 32.260 1.00 36.21  ? 253 ALA   A CB  1 
ATOM   1874 N  N   . VAL   A  1  241 ? 41.297  -19.101 32.132 1.00 33.52  ? 254 VAL   A N   1 
ATOM   1875 C  CA  . VAL   A  1  241 ? 42.704  -18.962 31.800 1.00 36.52  ? 254 VAL   A CA  1 
ATOM   1876 C  C   . VAL   A  1  241 ? 43.177  -17.577 32.213 1.00 35.95  ? 254 VAL   A C   1 
ATOM   1877 O  O   . VAL   A  1  241 ? 42.409  -16.619 32.174 1.00 40.71  ? 254 VAL   A O   1 
ATOM   1878 C  CB  . VAL   A  1  241 ? 42.969  -19.165 30.291 1.00 43.01  ? 254 VAL   A CB  1 
ATOM   1879 C  CG1 . VAL   A  1  241 ? 42.654  -20.589 29.842 1.00 44.12  ? 254 VAL   A CG1 1 
ATOM   1880 C  CG2 . VAL   A  1  241 ? 42.201  -18.172 29.433 1.00 39.94  ? 254 VAL   A CG2 1 
ATOM   1881 N  N   . PRO   A  1  242 ? 44.474  -17.410 32.552 1.00 35.32  ? 255 PRO   A N   1 
ATOM   1882 C  CA  . PRO   A  1  242 ? 45.041  -16.080 32.757 1.00 31.57  ? 255 PRO   A CA  1 
ATOM   1883 C  C   . PRO   A  1  242 ? 44.701  -15.225 31.549 1.00 31.56  ? 255 PRO   A C   1 
ATOM   1884 O  O   . PRO   A  1  242 ? 44.788  -15.700 30.423 1.00 33.40  ? 255 PRO   A O   1 
ATOM   1885 C  CB  . PRO   A  1  242 ? 46.535  -16.335 32.895 1.00 32.46  ? 255 PRO   A CB  1 
ATOM   1886 C  CG  . PRO   A  1  242 ? 46.612  -17.760 33.422 1.00 34.30  ? 255 PRO   A CG  1 
ATOM   1887 C  CD  . PRO   A  1  242 ? 45.471  -18.484 32.715 1.00 34.55  ? 255 PRO   A CD  1 
ATOM   1888 N  N   . ALA   A  1  243 ? 44.240  -13.994 31.789 1.00 31.80  ? 256 ALA   A N   1 
ATOM   1889 C  CA  . ALA   A  1  243 ? 43.866  -13.138 30.679 1.00 31.04  ? 256 ALA   A CA  1 
ATOM   1890 C  C   . ALA   A  1  243 ? 44.142  -11.681 31.012 1.00 28.29  ? 256 ALA   A C   1 
ATOM   1891 O  O   . ALA   A  1  243 ? 44.379  -11.324 32.158 1.00 31.94  ? 256 ALA   A O   1 
ATOM   1892 C  CB  . ALA   A  1  243 ? 42.419  -13.360 30.331 1.00 32.55  ? 256 ALA   A CB  1 
ATOM   1893 N  N   . SER   A  1  244 ? 44.090  -10.866 29.968 1.00 29.35  ? 257 SER   A N   1 
ATOM   1894 C  CA  . SER   A  1  244 ? 44.268  -9.436  30.098 1.00 31.94  ? 257 SER   A CA  1 
ATOM   1895 C  C   . SER   A  1  244 ? 43.577  -8.756  28.924 1.00 29.35  ? 257 SER   A C   1 
ATOM   1896 O  O   . SER   A  1  244 ? 42.365  -8.631  28.929 1.00 29.96  ? 257 SER   A O   1 
ATOM   1897 C  CB  . SER   A  1  244 ? 45.731  -9.094  30.197 1.00 32.65  ? 257 SER   A CB  1 
ATOM   1898 O  OG  . SER   A  1  244 ? 46.450  -9.662  29.109 1.00 32.98  ? 257 SER   A OG  1 
ATOM   1899 N  N   . ASN   A  1  245 ? 44.351  -8.398  27.895 1.00 31.95  ? 258 ASN   A N   1 
ATOM   1900 C  CA  . ASN   A  1  245 ? 43.912  -7.433  26.908 1.00 32.50  ? 258 ASN   A CA  1 
ATOM   1901 C  C   . ASN   A  1  245 ? 43.674  -8.065  25.535 1.00 33.20  ? 258 ASN   A C   1 
ATOM   1902 O  O   . ASN   A  1  245 ? 43.743  -7.351  24.534 1.00 31.61  ? 258 ASN   A O   1 
ATOM   1903 C  CB  . ASN   A  1  245 ? 44.926  -6.303  26.792 1.00 37.41  ? 258 ASN   A CB  1 
ATOM   1904 C  CG  . ASN   A  1  245 ? 46.208  -6.758  26.131 1.00 40.09  ? 258 ASN   A CG  1 
ATOM   1905 O  OD1 . ASN   A  1  245 ? 46.503  -7.955  26.057 1.00 40.36  ? 258 ASN   A OD1 1 
ATOM   1906 N  ND2 . ASN   A  1  245 ? 46.995  -5.805  25.671 1.00 45.14  ? 258 ASN   A ND2 1 
ATOM   1907 N  N   . GLU   A  1  246 ? 43.365  -9.376  25.494 1.00 33.95  ? 259 GLU   A N   1 
ATOM   1908 C  CA  . GLU   A  1  246 ? 43.013  -10.046 24.250 1.00 32.75  ? 259 GLU   A CA  1 
ATOM   1909 C  C   . GLU   A  1  246 ? 41.855  -9.310  23.575 1.00 34.25  ? 259 GLU   A C   1 
ATOM   1910 O  O   . GLU   A  1  246 ? 40.829  -9.040  24.207 1.00 31.05  ? 259 GLU   A O   1 
ATOM   1911 C  CB  . GLU   A  1  246 ? 42.600  -11.503 24.458 1.00 36.74  ? 259 GLU   A CB  1 
ATOM   1912 C  CG  . GLU   A  1  246 ? 43.733  -12.396 24.966 1.00 40.74  ? 259 GLU   A CG  1 
ATOM   1913 C  CD  . GLU   A  1  246 ? 44.096  -12.310 26.450 1.00 45.33  ? 259 GLU   A CD  1 
ATOM   1914 O  OE1 . GLU   A  1  246 ? 43.469  -11.529 27.210 1.00 39.89  ? 259 GLU   A OE1 1 
ATOM   1915 O  OE2 . GLU   A  1  246 ? 45.004  -13.080 26.855 1.00 45.05  ? 259 GLU   A OE2 1 
ATOM   1916 N  N   . GLY   A  1  247 ? 42.055  -8.965  22.290 1.00 34.11  ? 260 GLY   A N   1 
ATOM   1917 C  CA  . GLY   A  1  247 ? 41.039  -8.314  21.483 1.00 33.93  ? 260 GLY   A CA  1 
ATOM   1918 C  C   . GLY   A  1  247 ? 41.215  -6.797  21.411 1.00 36.90  ? 260 GLY   A C   1 
ATOM   1919 O  O   . GLY   A  1  247 ? 40.503  -6.139  20.664 1.00 44.47  ? 260 GLY   A O   1 
ATOM   1920 N  N   . ALA   A  1  248 ? 42.156  -6.225  22.163 1.00 37.72  ? 261 ALA   A N   1 
ATOM   1921 C  CA  . ALA   A  1  248 ? 42.342  -4.777  22.158 1.00 39.42  ? 261 ALA   A CA  1 
ATOM   1922 C  C   . ALA   A  1  248 ? 42.731  -4.279  20.766 1.00 39.68  ? 261 ALA   A C   1 
ATOM   1923 O  O   . ALA   A  1  248 ? 42.384  -3.164  20.384 1.00 44.68  ? 261 ALA   A O   1 
ATOM   1924 C  CB  . ALA   A  1  248 ? 43.387  -4.362  23.179 1.00 38.64  ? 261 ALA   A CB  1 
ATOM   1925 N  N   . ASP   A  1  249 ? 43.474  -5.105  20.030 1.00 38.15  ? 262 ASP   A N   1 
ATOM   1926 C  CA  . ASP   A  1  249 ? 43.857  -4.853  18.645 1.00 43.45  ? 262 ASP   A CA  1 
ATOM   1927 C  C   . ASP   A  1  249 ? 42.616  -4.637  17.774 1.00 42.48  ? 262 ASP   A C   1 
ATOM   1928 O  O   . ASP   A  1  249 ? 42.584  -3.731  16.948 1.00 44.28  ? 262 ASP   A O   1 
ATOM   1929 C  CB  . ASP   A  1  249 ? 44.743  -5.971  18.098 1.00 48.46  ? 262 ASP   A CB  1 
ATOM   1930 C  CG  . ASP   A  1  249 ? 44.200  -7.406  18.173 1.00 65.41  ? 262 ASP   A CG  1 
ATOM   1931 O  OD1 . ASP   A  1  249 ? 43.245  -7.676  18.964 1.00 60.03  ? 262 ASP   A OD1 1 
ATOM   1932 O  OD2 . ASP   A  1  249 ? 44.725  -8.275  17.432 1.00 76.18  ? 262 ASP   A OD2 1 
ATOM   1933 N  N   . GLN   A  1  250 ? 41.587  -5.469  17.960 1.00 40.79  ? 263 GLN   A N   1 
ATOM   1934 C  CA  . GLN   A  1  250 ? 40.377  -5.386  17.161 1.00 41.98  ? 263 GLN   A CA  1 
ATOM   1935 C  C   . GLN   A  1  250 ? 39.586  -4.129  17.501 1.00 41.98  ? 263 GLN   A C   1 
ATOM   1936 O  O   . GLN   A  1  250 ? 38.932  -3.583  16.623 1.00 47.92  ? 263 GLN   A O   1 
ATOM   1937 C  CB  . GLN   A  1  250 ? 39.498  -6.617  17.357 1.00 41.45  ? 263 GLN   A CB  1 
ATOM   1938 C  CG  . GLN   A  1  250 ? 40.104  -7.885  16.766 1.00 42.99  ? 263 GLN   A CG  1 
ATOM   1939 C  CD  . GLN   A  1  250 ? 39.204  -9.081  16.973 1.00 46.30  ? 263 GLN   A CD  1 
ATOM   1940 O  OE1 . GLN   A  1  250 ? 38.052  -9.074  16.539 1.00 48.46  ? 263 GLN   A OE1 1 
ATOM   1941 N  NE2 . GLN   A  1  250 ? 39.686  -10.090 17.692 1.00 47.92  ? 263 GLN   A NE2 1 
ATOM   1942 N  N   . VAL   A  1  251 ? 39.657  -3.678  18.761 1.00 39.29  ? 264 VAL   A N   1 
ATOM   1943 C  CA  . VAL   A  1  251 ? 38.958  -2.477  19.178 1.00 36.36  ? 264 VAL   A CA  1 
ATOM   1944 C  C   . VAL   A  1  251 ? 39.555  -1.281  18.445 1.00 35.95  ? 264 VAL   A C   1 
ATOM   1945 O  O   . VAL   A  1  251 ? 38.835  -0.412  17.974 1.00 41.76  ? 264 VAL   A O   1 
ATOM   1946 C  CB  . VAL   A  1  251 ? 39.003  -2.316  20.707 1.00 34.83  ? 264 VAL   A CB  1 
ATOM   1947 C  CG1 . VAL   A  1  251 ? 38.532  -0.953  21.166 1.00 35.66  ? 264 VAL   A CG1 1 
ATOM   1948 C  CG2 . VAL   A  1  251 ? 38.173  -3.382  21.391 1.00 37.47  ? 264 VAL   A CG2 1 
ATOM   1949 N  N   . LEU   A  1  252 ? 40.879  -1.241  18.355 1.00 41.07  ? 265 LEU   A N   1 
ATOM   1950 C  CA  . LEU   A  1  252 ? 41.556  -0.177  17.641 1.00 45.51  ? 265 LEU   A CA  1 
ATOM   1951 C  C   . LEU   A  1  252 ? 41.252  -0.265  16.148 1.00 45.56  ? 265 LEU   A C   1 
ATOM   1952 O  O   . LEU   A  1  252 ? 41.047  0.757   15.505 1.00 55.80  ? 265 LEU   A O   1 
ATOM   1953 C  CB  . LEU   A  1  252 ? 43.055  -0.219  17.883 1.00 45.90  ? 265 LEU   A CB  1 
ATOM   1954 C  CG  . LEU   A  1  252 ? 43.848  0.900   17.204 1.00 47.79  ? 265 LEU   A CG  1 
ATOM   1955 C  CD1 . LEU   A  1  252 ? 43.535  2.243   17.851 1.00 47.44  ? 265 LEU   A CD1 1 
ATOM   1956 C  CD2 . LEU   A  1  252 ? 45.344  0.580   17.258 1.00 43.34  ? 265 LEU   A CD2 1 
ATOM   1957 N  N   . ALA   A  1  253 ? 41.211  -1.480  15.603 1.00 44.07  ? 266 ALA   A N   1 
ATOM   1958 C  CA  . ALA   A  1  253 ? 41.014  -1.662  14.170 1.00 45.82  ? 266 ALA   A CA  1 
ATOM   1959 C  C   . ALA   A  1  253 ? 39.614  -1.207  13.738 1.00 47.80  ? 266 ALA   A C   1 
ATOM   1960 O  O   . ALA   A  1  253 ? 39.454  -0.692  12.640 1.00 49.59  ? 266 ALA   A O   1 
ATOM   1961 C  CB  . ALA   A  1  253 ? 41.280  -3.107  13.788 1.00 43.07  ? 266 ALA   A CB  1 
ATOM   1962 N  N   . ALA   A  1  254 ? 38.603  -1.354  14.602 1.00 49.80  ? 267 ALA   A N   1 
ATOM   1963 C  CA  . ALA   A  1  254 ? 37.241  -0.934  14.292 1.00 49.90  ? 267 ALA   A CA  1 
ATOM   1964 C  C   . ALA   A  1  254 ? 37.160  0.570   14.000 1.00 49.66  ? 267 ALA   A C   1 
ATOM   1965 O  O   . ALA   A  1  254 ? 36.316  0.991   13.205 1.00 55.21  ? 267 ALA   A O   1 
ATOM   1966 C  CB  . ALA   A  1  254 ? 36.311  -1.309  15.434 1.00 49.87  ? 267 ALA   A CB  1 
ATOM   1967 N  N   . HIS   A  1  255 ? 37.981  1.383   14.680 1.00 43.03  ? 268 HIS   A N   1 
ATOM   1968 C  CA  . HIS   A  1  255 ? 38.020  2.815   14.428 1.00 48.68  ? 268 HIS   A CA  1 
ATOM   1969 C  C   . HIS   A  1  255 ? 39.443  3.329   14.635 1.00 46.99  ? 268 HIS   A C   1 
ATOM   1970 O  O   . HIS   A  1  255 ? 39.762  3.884   15.684 1.00 51.14  ? 268 HIS   A O   1 
ATOM   1971 C  CB  . HIS   A  1  255 ? 37.009  3.583   15.283 1.00 47.98  ? 268 HIS   A CB  1 
ATOM   1972 C  CG  . HIS   A  1  255 ? 35.572  3.372   14.933 1.00 50.93  ? 268 HIS   A CG  1 
ATOM   1973 N  ND1 . HIS   A  1  255 ? 34.973  4.004   13.869 1.00 53.35  ? 268 HIS   A ND1 1 
ATOM   1974 C  CD2 . HIS   A  1  255 ? 34.620  2.624   15.513 1.00 49.28  ? 268 HIS   A CD2 1 
ATOM   1975 C  CE1 . HIS   A  1  255 ? 33.700  3.642   13.823 1.00 59.50  ? 268 HIS   A CE1 1 
ATOM   1976 N  NE2 . HIS   A  1  255 ? 33.462  2.812   14.824 1.00 55.48  ? 268 HIS   A NE2 1 
ATOM   1977 N  N   . PRO   A  1  256 ? 40.337  3.138   13.640 1.00 47.58  ? 269 PRO   A N   1 
ATOM   1978 C  CA  . PRO   A  1  256 ? 41.740  3.536   13.765 1.00 48.19  ? 269 PRO   A CA  1 
ATOM   1979 C  C   . PRO   A  1  256 ? 41.880  4.945   14.312 1.00 44.13  ? 269 PRO   A C   1 
ATOM   1980 O  O   . PRO   A  1  256 ? 41.143  5.849   13.931 1.00 44.19  ? 269 PRO   A O   1 
ATOM   1981 C  CB  . PRO   A  1  256 ? 42.287  3.403   12.341 1.00 52.52  ? 269 PRO   A CB  1 
ATOM   1982 C  CG  . PRO   A  1  256 ? 41.451  2.274   11.764 1.00 54.40  ? 269 PRO   A CG  1 
ATOM   1983 C  CD  . PRO   A  1  256 ? 40.053  2.471   12.361 1.00 49.26  ? 269 PRO   A CD  1 
ATOM   1984 N  N   . TRP   A  1  257 ? 42.824  5.101   15.238 1.00 41.87  ? 270 TRP   A N   1 
ATOM   1985 C  CA  . TRP   A  1  257 ? 42.983  6.355   15.946 1.00 40.09  ? 270 TRP   A CA  1 
ATOM   1986 C  C   . TRP   A  1  257 ? 44.447  6.549   16.333 1.00 39.71  ? 270 TRP   A C   1 
ATOM   1987 O  O   . TRP   A  1  257 ? 45.181  5.589   16.549 1.00 44.65  ? 270 TRP   A O   1 
ATOM   1988 C  CB  . TRP   A  1  257 ? 42.077  6.365   17.184 1.00 41.28  ? 270 TRP   A CB  1 
ATOM   1989 C  CG  . TRP   A  1  257 ? 41.960  7.741   17.766 1.00 40.32  ? 270 TRP   A CG  1 
ATOM   1990 C  CD1 . TRP   A  1  257 ? 42.604  8.240   18.851 1.00 39.87  ? 270 TRP   A CD1 1 
ATOM   1991 C  CD2 . TRP   A  1  257 ? 41.218  8.834   17.189 1.00 41.50  ? 270 TRP   A CD2 1 
ATOM   1992 N  NE1 . TRP   A  1  257 ? 42.273  9.556   19.021 1.00 42.04  ? 270 TRP   A NE1 1 
ATOM   1993 C  CE2 . TRP   A  1  257 ? 41.439  9.951   18.012 1.00 39.31  ? 270 TRP   A CE2 1 
ATOM   1994 C  CE3 . TRP   A  1  257 ? 40.388  8.969   16.069 1.00 44.67  ? 270 TRP   A CE3 1 
ATOM   1995 C  CZ2 . TRP   A  1  257 ? 40.867  11.190  17.745 1.00 45.10  ? 270 TRP   A CZ2 1 
ATOM   1996 C  CZ3 . TRP   A  1  257 ? 39.829  10.198  15.801 1.00 44.79  ? 270 TRP   A CZ3 1 
ATOM   1997 C  CH2 . TRP   A  1  257 ? 40.071  11.293  16.625 1.00 44.67  ? 270 TRP   A CH2 1 
ATOM   1998 N  N   . VAL   A  1  258 ? 44.839  7.812   16.452 1.00 41.98  ? 271 VAL   A N   1 
ATOM   1999 C  CA  . VAL   A  1  258 ? 46.225  8.197   16.600 1.00 43.52  ? 271 VAL   A CA  1 
ATOM   2000 C  C   . VAL   A  1  258 ? 46.362  9.000   17.884 1.00 42.34  ? 271 VAL   A C   1 
ATOM   2001 O  O   . VAL   A  1  258 ? 45.543  9.874   18.161 1.00 44.25  ? 271 VAL   A O   1 
ATOM   2002 C  CB  . VAL   A  1  258 ? 46.653  9.004   15.357 1.00 51.10  ? 271 VAL   A CB  1 
ATOM   2003 C  CG1 . VAL   A  1  258 ? 47.998  9.704   15.532 1.00 56.44  ? 271 VAL   A CG1 1 
ATOM   2004 C  CG2 . VAL   A  1  258 ? 46.687  8.108   14.127 1.00 53.43  ? 271 VAL   A CG2 1 
ATOM   2005 N  N   . PRO   A  1  259 ? 47.393  8.729   18.705 1.00 37.93  ? 272 PRO   A N   1 
ATOM   2006 C  CA  . PRO   A  1  259 ? 47.570  9.473   19.945 1.00 40.83  ? 272 PRO   A CA  1 
ATOM   2007 C  C   . PRO   A  1  259 ? 47.654  10.967  19.653 1.00 42.02  ? 272 PRO   A C   1 
ATOM   2008 O  O   . PRO   A  1  259 ? 48.086  11.370  18.585 1.00 44.75  ? 272 PRO   A O   1 
ATOM   2009 C  CB  . PRO   A  1  259 ? 48.855  8.904   20.569 1.00 39.74  ? 272 PRO   A CB  1 
ATOM   2010 C  CG  . PRO   A  1  259 ? 49.516  8.158   19.434 1.00 41.21  ? 272 PRO   A CG  1 
ATOM   2011 C  CD  . PRO   A  1  259 ? 48.401  7.674   18.525 1.00 39.06  ? 272 PRO   A CD  1 
ATOM   2012 N  N   . GLY   A  1  260 ? 47.224  11.772  20.625 1.00 43.59  ? 273 GLY   A N   1 
ATOM   2013 C  CA  . GLY   A  1  260 ? 47.259  13.218  20.510 1.00 46.56  ? 273 GLY   A CA  1 
ATOM   2014 C  C   . GLY   A  1  260 ? 46.408  13.857  21.602 1.00 50.79  ? 273 GLY   A C   1 
ATOM   2015 O  O   . GLY   A  1  260 ? 46.234  13.278  22.679 1.00 49.56  ? 273 GLY   A O   1 
ATOM   2016 N  N   . GLY   A  1  261 ? 45.864  15.038  21.294 1.00 50.11  ? 274 GLY   A N   1 
ATOM   2017 C  CA  . GLY   A  1  261 ? 45.071  15.786  22.250 1.00 49.47  ? 274 GLY   A CA  1 
ATOM   2018 C  C   . GLY   A  1  261 ? 44.446  17.031  21.619 1.00 50.91  ? 274 GLY   A C   1 
ATOM   2019 O  O   . GLY   A  1  261 ? 44.774  17.412  20.491 1.00 49.16  ? 274 GLY   A O   1 
ATOM   2020 N  N   . ASN   A  1  262 ? 43.527  17.657  22.366 1.00 43.79  ? 275 ASN   A N   1 
ATOM   2021 C  CA  . ASN   A  1  262 ? 43.027  18.970  22.014 1.00 44.44  ? 275 ASN   A CA  1 
ATOM   2022 C  C   . ASN   A  1  262 ? 44.134  19.996  22.267 1.00 47.47  ? 275 ASN   A C   1 
ATOM   2023 O  O   . ASN   A  1  262 ? 44.580  20.146  23.396 1.00 49.30  ? 275 ASN   A O   1 
ATOM   2024 C  CB  . ASN   A  1  262 ? 41.774  19.322  22.805 1.00 40.23  ? 275 ASN   A CB  1 
ATOM   2025 C  CG  . ASN   A  1  262 ? 40.499  18.865  22.136 1.00 40.70  ? 275 ASN   A CG  1 
ATOM   2026 O  OD1 . ASN   A  1  262 ? 40.493  18.613  20.936 1.00 38.13  ? 275 ASN   A OD1 1 
ATOM   2027 N  ND2 . ASN   A  1  262 ? 39.402  18.761  22.884 1.00 40.06  ? 275 ASN   A ND2 1 
ATOM   2028 N  N   . ALA   A  1  263 ? 44.535  20.739  21.225 1.00 53.96  ? 276 ALA   A N   1 
ATOM   2029 C  CA  . ALA   A  1  263 ? 45.554  21.771  21.372 1.00 54.95  ? 276 ALA   A CA  1 
ATOM   2030 C  C   . ALA   A  1  263 ? 44.925  23.106  21.770 1.00 57.71  ? 276 ALA   A C   1 
ATOM   2031 O  O   . ALA   A  1  263 ? 43.757  23.378  21.473 1.00 52.44  ? 276 ALA   A O   1 
ATOM   2032 C  CB  . ALA   A  1  263 ? 46.339  21.906  20.085 1.00 56.38  ? 276 ALA   A CB  1 
ATOM   2033 N  N   . ASP   A  1  264 ? 45.727  23.919  22.475 1.00 63.72  ? 277 ASP   A N   1 
ATOM   2034 C  CA  . ASP   A  1  264 ? 45.466  25.334  22.710 1.00 67.88  ? 277 ASP   A CA  1 
ATOM   2035 C  C   . ASP   A  1  264 ? 44.168  25.544  23.487 1.00 63.73  ? 277 ASP   A C   1 
ATOM   2036 O  O   . ASP   A  1  264 ? 43.461  26.508  23.229 1.00 61.84  ? 277 ASP   A O   1 
ATOM   2037 C  CB  . ASP   A  1  264 ? 45.427  26.134  21.411 1.00 78.23  ? 277 ASP   A CB  1 
ATOM   2038 C  CG  . ASP   A  1  264 ? 46.643  25.995  20.502 1.00 90.71  ? 277 ASP   A CG  1 
ATOM   2039 O  OD1 . ASP   A  1  264 ? 47.778  26.140  21.010 1.00 92.36  ? 277 ASP   A OD1 1 
ATOM   2040 O  OD2 . ASP   A  1  264 ? 46.451  25.755  19.285 1.00 91.01  ? 277 ASP   A OD2 1 
ATOM   2041 N  N   . ASN   A  1  265 ? 43.854  24.637  24.421 1.00 66.13  ? 278 ASN   A N   1 
ATOM   2042 C  CA  . ASN   A  1  265 ? 42.746  24.805  25.344 1.00 61.63  ? 278 ASN   A CA  1 
ATOM   2043 C  C   . ASN   A  1  265 ? 41.433  25.059  24.597 1.00 54.25  ? 278 ASN   A C   1 
ATOM   2044 O  O   . ASN   A  1  265 ? 40.647  25.899  25.011 1.00 50.80  ? 278 ASN   A O   1 
ATOM   2045 C  CB  . ASN   A  1  265 ? 43.076  25.895  26.358 1.00 61.49  ? 278 ASN   A CB  1 
ATOM   2046 C  CG  . ASN   A  1  265 ? 42.218  25.780  27.595 1.00 75.72  ? 278 ASN   A CG  1 
ATOM   2047 O  OD1 . ASN   A  1  265 ? 42.277  24.763  28.296 1.00 80.48  ? 278 ASN   A OD1 1 
ATOM   2048 N  ND2 . ASN   A  1  265 ? 41.404  26.788  27.875 1.00 82.02  ? 278 ASN   A ND2 1 
ATOM   2049 N  N   . GLN   A  1  266 ? 41.190  24.309  23.515 1.00 55.32  ? 279 GLN   A N   1 
ATOM   2050 C  CA  . GLN   A  1  266 ? 39.978  24.432  22.719 1.00 59.43  ? 279 GLN   A CA  1 
ATOM   2051 C  C   . GLN   A  1  266 ? 39.395  23.059  22.404 1.00 52.80  ? 279 GLN   A C   1 
ATOM   2052 O  O   . GLN   A  1  266 ? 40.137  22.129  22.131 1.00 56.74  ? 279 GLN   A O   1 
ATOM   2053 C  CB  . GLN   A  1  266 ? 40.288  25.082  21.370 1.00 70.90  ? 279 GLN   A CB  1 
ATOM   2054 C  CG  . GLN   A  1  266 ? 40.472  26.593  21.462 1.00 75.93  ? 279 GLN   A CG  1 
ATOM   2055 C  CD  . GLN   A  1  266 ? 40.840  27.237  20.145 1.00 82.19  ? 279 GLN   A CD  1 
ATOM   2056 O  OE1 . GLN   A  1  266 ? 41.055  26.577  19.118 1.00 72.95  ? 279 GLN   A OE1 1 
ATOM   2057 N  NE2 . GLN   A  1  266 ? 40.866  28.559  20.160 1.00 91.70  ? 279 GLN   A NE2 1 
ATOM   2058 N  N   . VAL   A  1  267 ? 38.066  22.960  22.371 1.00 42.16  ? 280 VAL   A N   1 
ATOM   2059 C  CA  . VAL   A  1  267 ? 37.404  21.749  21.929 1.00 46.15  ? 280 VAL   A CA  1 
ATOM   2060 C  C   . VAL   A  1  267 ? 37.489  21.641  20.404 1.00 49.00  ? 280 VAL   A C   1 
ATOM   2061 O  O   . VAL   A  1  267 ? 37.920  22.567  19.725 1.00 54.96  ? 280 VAL   A O   1 
ATOM   2062 C  CB  . VAL   A  1  267 ? 35.950  21.682  22.432 1.00 51.46  ? 280 VAL   A CB  1 
ATOM   2063 C  CG1 . VAL   A  1  267 ? 35.895  21.651  23.956 1.00 52.56  ? 280 VAL   A CG1 1 
ATOM   2064 C  CG2 . VAL   A  1  267 ? 35.097  22.830  21.894 1.00 53.96  ? 280 VAL   A CG2 1 
ATOM   2065 N  N   . ASN   A  1  268 ? 37.129  20.463  19.892 1.00 50.08  ? 281 ASN   A N   1 
ATOM   2066 C  CA  . ASN   A  1  268 ? 37.132  20.145  18.475 1.00 56.95  ? 281 ASN   A CA  1 
ATOM   2067 C  C   . ASN   A  1  268 ? 38.425  20.621  17.825 1.00 55.69  ? 281 ASN   A C   1 
ATOM   2068 O  O   . ASN   A  1  268 ? 38.397  21.209  16.751 1.00 53.87  ? 281 ASN   A O   1 
ATOM   2069 C  CB  . ASN   A  1  268 ? 35.879  20.663  17.779 1.00 55.80  ? 281 ASN   A CB  1 
ATOM   2070 C  CG  . ASN   A  1  268 ? 34.637  20.003  18.335 1.00 57.67  ? 281 ASN   A CG  1 
ATOM   2071 O  OD1 . ASN   A  1  268 ? 34.434  18.791  18.173 1.00 60.22  ? 281 ASN   A OD1 1 
ATOM   2072 N  ND2 . ASN   A  1  268 ? 33.803  20.783  18.997 1.00 55.06  ? 281 ASN   A ND2 1 
ATOM   2073 N  N   . ASN   A  1  269 ? 39.553  20.288  18.456 1.00 52.65  ? 282 ASN   A N   1 
ATOM   2074 C  CA  . ASN   A  1  269 ? 40.840  20.763  17.984 1.00 51.05  ? 282 ASN   A CA  1 
ATOM   2075 C  C   . ASN   A  1  269 ? 41.916  19.702  18.245 1.00 49.13  ? 282 ASN   A C   1 
ATOM   2076 O  O   . ASN   A  1  269 ? 42.981  19.998  18.796 1.00 41.06  ? 282 ASN   A O   1 
ATOM   2077 C  CB  . ASN   A  1  269 ? 41.113  22.134  18.593 1.00 52.40  ? 282 ASN   A CB  1 
ATOM   2078 C  CG  . ASN   A  1  269 ? 42.275  22.824  17.922 1.00 52.80  ? 282 ASN   A CG  1 
ATOM   2079 O  OD1 . ASN   A  1  269 ? 42.464  22.695  16.709 1.00 47.62  ? 282 ASN   A OD1 1 
ATOM   2080 N  ND2 . ASN   A  1  269 ? 43.091  23.506  18.709 1.00 54.48  ? 282 ASN   A ND2 1 
ATOM   2081 N  N   . TYR   A  1  270 ? 41.639  18.457  17.821 1.00 47.99  ? 283 TYR   A N   1 
ATOM   2082 C  CA  . TYR   A  1  270 ? 42.528  17.339  18.100 1.00 50.12  ? 283 TYR   A CA  1 
ATOM   2083 C  C   . TYR   A  1  270 ? 43.722  17.364  17.145 1.00 45.49  ? 283 TYR   A C   1 
ATOM   2084 O  O   . TYR   A  1  270 ? 43.554  17.269  15.935 1.00 44.75  ? 283 TYR   A O   1 
ATOM   2085 C  CB  . TYR   A  1  270 ? 41.762  16.011  18.018 1.00 48.42  ? 283 TYR   A CB  1 
ATOM   2086 C  CG  . TYR   A  1  270 ? 42.497  14.788  18.561 1.00 48.49  ? 283 TYR   A CG  1 
ATOM   2087 C  CD1 . TYR   A  1  270 ? 42.410  14.435  19.902 1.00 44.32  ? 283 TYR   A CD1 1 
ATOM   2088 C  CD2 . TYR   A  1  270 ? 43.265  13.971  17.732 1.00 48.05  ? 283 TYR   A CD2 1 
ATOM   2089 C  CE1 . TYR   A  1  270 ? 43.064  13.320  20.402 1.00 43.82  ? 283 TYR   A CE1 1 
ATOM   2090 C  CE2 . TYR   A  1  270 ? 43.922  12.850  18.219 1.00 43.41  ? 283 TYR   A CE2 1 
ATOM   2091 C  CZ  . TYR   A  1  270 ? 43.818  12.528  19.559 1.00 40.86  ? 283 TYR   A CZ  1 
ATOM   2092 O  OH  . TYR   A  1  270 ? 44.436  11.427  20.046 1.00 37.38  ? 283 TYR   A OH  1 
ATOM   2093 N  N   . VAL   A  1  271 ? 44.926  17.441  17.720 1.00 44.98  ? 284 VAL   A N   1 
ATOM   2094 C  CA  . VAL   A  1  271 ? 46.181  17.403  16.986 1.00 47.92  ? 284 VAL   A CA  1 
ATOM   2095 C  C   . VAL   A  1  271 ? 46.938  16.132  17.365 1.00 45.09  ? 284 VAL   A C   1 
ATOM   2096 O  O   . VAL   A  1  271 ? 47.048  15.796  18.543 1.00 46.74  ? 284 VAL   A O   1 
ATOM   2097 C  CB  . VAL   A  1  271 ? 47.024  18.650  17.324 1.00 51.69  ? 284 VAL   A CB  1 
ATOM   2098 C  CG1 . VAL   A  1  271 ? 48.399  18.623  16.665 1.00 48.40  ? 284 VAL   A CG1 1 
ATOM   2099 C  CG2 . VAL   A  1  271 ? 46.284  19.931  16.956 1.00 58.24  ? 284 VAL   A CG2 1 
ATOM   2100 N  N   . GLU   A  1  272 ? 47.521  15.473  16.366 1.00 45.49  ? 285 GLU   A N   1 
ATOM   2101 C  CA  . GLU   A  1  272 ? 48.227  14.218  16.570 1.00 50.62  ? 285 GLU   A CA  1 
ATOM   2102 C  C   . GLU   A  1  272 ? 49.588  14.477  17.215 1.00 52.98  ? 285 GLU   A C   1 
ATOM   2103 O  O   . GLU   A  1  272 ? 50.197  15.520  16.970 1.00 53.23  ? 285 GLU   A O   1 
ATOM   2104 C  CB  . GLU   A  1  272 ? 48.407  13.481  15.242 1.00 55.56  ? 285 GLU   A CB  1 
ATOM   2105 C  CG  . GLU   A  1  272 ? 47.111  13.303  14.446 1.00 64.87  ? 285 GLU   A CG  1 
ATOM   2106 C  CD  . GLU   A  1  272 ? 47.249  12.565  13.120 1.00 67.47  ? 285 GLU   A CD  1 
ATOM   2107 O  OE1 . GLU   A  1  272 ? 48.394  12.203  12.729 1.00 56.32  ? 285 GLU   A OE1 1 
ATOM   2108 O  OE2 . GLU   A  1  272 ? 46.182  12.304  12.507 1.00 59.67  ? 285 GLU   A OE2 1 
ATOM   2109 N  N   . ASP   A  1  273 ? 50.037  13.528  18.058 1.00 55.83  ? 286 ASP   A N   1 
ATOM   2110 C  CA  . ASP   A  1  273 ? 51.377  13.530  18.633 1.00 59.92  ? 286 ASP   A CA  1 
ATOM   2111 C  C   . ASP   A  1  273 ? 52.171  12.377  18.017 1.00 60.61  ? 286 ASP   A C   1 
ATOM   2112 O  O   . ASP   A  1  273 ? 51.944  11.214  18.342 1.00 55.75  ? 286 ASP   A O   1 
ATOM   2113 C  CB  . ASP   A  1  273 ? 51.374  13.442  20.155 1.00 61.79  ? 286 ASP   A CB  1 
ATOM   2114 C  CG  . ASP   A  1  273 ? 52.746  13.520  20.815 1.00 64.81  ? 286 ASP   A CG  1 
ATOM   2115 O  OD1 . ASP   A  1  273 ? 53.743  13.731  20.099 1.00 64.46  ? 286 ASP   A OD1 1 
ATOM   2116 O  OD2 . ASP   A  1  273 ? 52.820  13.420  22.049 1.00 64.19  ? 286 ASP   A OD2 1 
ATOM   2117 N  N   . PRO   A  1  274 ? 53.135  12.661  17.112 1.00 63.16  ? 287 PRO   A N   1 
ATOM   2118 C  CA  . PRO   A  1  274 ? 53.934  11.601  16.489 1.00 63.32  ? 287 PRO   A CA  1 
ATOM   2119 C  C   . PRO   A  1  274 ? 55.028  10.977  17.361 1.00 57.93  ? 287 PRO   A C   1 
ATOM   2120 O  O   . PRO   A  1  274 ? 55.570  9.940   16.987 1.00 51.15  ? 287 PRO   A O   1 
ATOM   2121 C  CB  . PRO   A  1  274 ? 54.512  12.346  15.262 1.00 63.73  ? 287 PRO   A CB  1 
ATOM   2122 C  CG  . PRO   A  1  274 ? 54.702  13.765  15.753 1.00 64.48  ? 287 PRO   A CG  1 
ATOM   2123 C  CD  . PRO   A  1  274 ? 53.514  14.014  16.661 1.00 66.13  ? 287 PRO   A CD  1 
ATOM   2124 N  N   . ASP   A  1  275 ? 55.329  11.598  18.516 1.00 56.17  ? 288 ASP   A N   1 
ATOM   2125 C  CA  . ASP   A  1  275 ? 56.316  11.104  19.474 1.00 56.52  ? 288 ASP   A CA  1 
ATOM   2126 C  C   . ASP   A  1  275 ? 55.727  10.130  20.502 1.00 54.69  ? 288 ASP   A C   1 
ATOM   2127 O  O   . ASP   A  1  275 ? 56.463  9.436   21.203 1.00 48.47  ? 288 ASP   A O   1 
ATOM   2128 C  CB  . ASP   A  1  275 ? 56.988  12.268  20.193 1.00 62.47  ? 288 ASP   A CB  1 
ATOM   2129 C  CG  . ASP   A  1  275 ? 57.847  13.157  19.300 1.00 70.33  ? 288 ASP   A CG  1 
ATOM   2130 O  OD1 . ASP   A  1  275 ? 58.100  12.742  18.130 1.00 62.98  ? 288 ASP   A OD1 1 
ATOM   2131 O  OD2 . ASP   A  1  275 ? 58.225  14.261  19.767 1.00 66.88  ? 288 ASP   A OD2 1 
ATOM   2132 N  N   . SER   A  1  276 ? 54.398  10.082  20.611 1.00 48.39  ? 289 SER   A N   1 
ATOM   2133 C  CA  . SER   A  1  276 ? 53.758  9.254   21.616 1.00 43.79  ? 289 SER   A CA  1 
ATOM   2134 C  C   . SER   A  1  276 ? 54.028  7.777   21.352 1.00 39.77  ? 289 SER   A C   1 
ATOM   2135 O  O   . SER   A  1  276 ? 54.187  7.341   20.221 1.00 41.85  ? 289 SER   A O   1 
ATOM   2136 C  CB  . SER   A  1  276 ? 52.281  9.535   21.631 1.00 46.03  ? 289 SER   A CB  1 
ATOM   2137 O  OG  . SER   A  1  276 ? 51.566  8.502   22.278 1.00 44.77  ? 289 SER   A OG  1 
ATOM   2138 N  N   . ALA   A  1  277 ? 54.012  6.991   22.418 1.00 40.36  ? 290 ALA   A N   1 
ATOM   2139 C  CA  . ALA   A  1  277 ? 53.868  5.553   22.282 1.00 38.00  ? 290 ALA   A CA  1 
ATOM   2140 C  C   . ALA   A  1  277 ? 52.594  5.217   21.516 1.00 34.79  ? 290 ALA   A C   1 
ATOM   2141 O  O   . ALA   A  1  277 ? 51.630  5.966   21.537 1.00 36.09  ? 290 ALA   A O   1 
ATOM   2142 C  CB  . ALA   A  1  277 ? 53.833  4.930   23.643 1.00 40.36  ? 290 ALA   A CB  1 
ATOM   2143 N  N   . ASP   A  1  278 ? 52.611  4.085   20.816 1.00 36.19  ? 291 ASP   A N   1 
ATOM   2144 C  CA  . ASP   A  1  278 ? 51.420  3.509   20.213 1.00 38.56  ? 291 ASP   A CA  1 
ATOM   2145 C  C   . ASP   A  1  278 ? 51.628  2.002   20.193 1.00 37.67  ? 291 ASP   A C   1 
ATOM   2146 O  O   . ASP   A  1  278 ? 52.592  1.532   20.796 1.00 39.84  ? 291 ASP   A O   1 
ATOM   2147 C  CB  . ASP   A  1  278 ? 51.079  4.133   18.871 1.00 43.33  ? 291 ASP   A CB  1 
ATOM   2148 C  CG  . ASP   A  1  278 ? 52.057  3.862   17.742 1.00 49.36  ? 291 ASP   A CG  1 
ATOM   2149 O  OD1 . ASP   A  1  278 ? 52.774  2.844   17.818 1.00 53.40  ? 291 ASP   A OD1 1 
ATOM   2150 O  OD2 . ASP   A  1  278 ? 52.111  4.709   16.821 1.00 57.46  ? 291 ASP   A OD2 1 
ATOM   2151 N  N   . PHE   A  1  279 ? 50.760  1.263   19.500 1.00 35.42  ? 292 PHE   A N   1 
ATOM   2152 C  CA  . PHE   A  1  279 ? 50.748  -0.187  19.641 1.00 41.71  ? 292 PHE   A CA  1 
ATOM   2153 C  C   . PHE   A  1  279 ? 51.887  -0.846  18.863 1.00 43.52  ? 292 PHE   A C   1 
ATOM   2154 O  O   . PHE   A  1  279 ? 52.189  -2.007  19.119 1.00 42.91  ? 292 PHE   A O   1 
ATOM   2155 C  CB  . PHE   A  1  279 ? 49.377  -0.786  19.307 1.00 40.80  ? 292 PHE   A CB  1 
ATOM   2156 C  CG  . PHE   A  1  279 ? 48.441  -0.614  20.490 1.00 41.67  ? 292 PHE   A CG  1 
ATOM   2157 C  CD1 . PHE   A  1  279 ? 48.534  -1.445  21.603 1.00 43.97  ? 292 PHE   A CD1 1 
ATOM   2158 C  CD2 . PHE   A  1  279 ? 47.534  0.431   20.520 1.00 45.92  ? 292 PHE   A CD2 1 
ATOM   2159 C  CE1 . PHE   A  1  279 ? 47.698  -1.264  22.699 1.00 47.44  ? 292 PHE   A CE1 1 
ATOM   2160 C  CE2 . PHE   A  1  279 ? 46.691  0.606   21.613 1.00 54.81  ? 292 PHE   A CE2 1 
ATOM   2161 C  CZ  . PHE   A  1  279 ? 46.773  -0.243  22.700 1.00 52.52  ? 292 PHE   A CZ  1 
ATOM   2162 N  N   . THR   A  1  280 ? 52.541  -0.117  17.954 1.00 49.08  ? 293 THR   A N   1 
ATOM   2163 C  CA  . THR   A  1  280 ? 53.734  -0.641  17.293 1.00 58.37  ? 293 THR   A CA  1 
ATOM   2164 C  C   . THR   A  1  280 ? 54.999  0.016   17.862 1.00 62.09  ? 293 THR   A C   1 
ATOM   2165 O  O   . THR   A  1  280 ? 56.093  -0.293  17.402 1.00 59.58  ? 293 THR   A O   1 
ATOM   2166 C  CB  . THR   A  1  280 ? 53.631  -0.452  15.775 1.00 60.07  ? 293 THR   A CB  1 
ATOM   2167 O  OG1 . THR   A  1  280 ? 53.573  0.952   15.521 1.00 66.65  ? 293 THR   A OG1 1 
ATOM   2168 C  CG2 . THR   A  1  280 ? 52.411  -1.133  15.181 1.00 59.17  ? 293 THR   A CG2 1 
ATOM   2169 N  N   . HIS   A  1  281 ? 54.851  0.897   18.869 1.00 58.13  ? 294 HIS   A N   1 
ATOM   2170 C  CA  . HIS   A  1  281 ? 55.969  1.604   19.472 1.00 51.49  ? 294 HIS   A CA  1 
ATOM   2171 C  C   . HIS   A  1  281 ? 55.859  1.575   21.001 1.00 48.99  ? 294 HIS   A C   1 
ATOM   2172 O  O   . HIS   A  1  281 ? 55.917  2.615   21.646 1.00 50.39  ? 294 HIS   A O   1 
ATOM   2173 C  CB  . HIS   A  1  281 ? 56.097  3.041   18.946 1.00 58.27  ? 294 HIS   A CB  1 
ATOM   2174 C  CG  . HIS   A  1  281 ? 56.351  3.167   17.480 1.00 70.12  ? 294 HIS   A CG  1 
ATOM   2175 N  ND1 . HIS   A  1  281 ? 57.618  3.143   16.929 1.00 81.93  ? 294 HIS   A ND1 1 
ATOM   2176 C  CD2 . HIS   A  1  281 ? 55.504  3.301   16.447 1.00 78.24  ? 294 HIS   A CD2 1 
ATOM   2177 C  CE1 . HIS   A  1  281 ? 57.527  3.275   15.614 1.00 84.82  ? 294 HIS   A CE1 1 
ATOM   2178 N  NE2 . HIS   A  1  281 ? 56.253  3.368   15.301 1.00 84.67  ? 294 HIS   A NE2 1 
ATOM   2179 N  N   . LEU   A  1  282 ? 55.711  0.379   21.575 1.00 47.64  ? 295 LEU   A N   1 
ATOM   2180 C  CA  . LEU   A  1  282 ? 55.403  0.216   22.984 1.00 48.43  ? 295 LEU   A CA  1 
ATOM   2181 C  C   . LEU   A  1  282 ? 56.563  0.639   23.883 1.00 46.11  ? 295 LEU   A C   1 
ATOM   2182 O  O   . LEU   A  1  282 ? 56.313  1.109   24.989 1.00 48.81  ? 295 LEU   A O   1 
ATOM   2183 C  CB  . LEU   A  1  282 ? 54.978  -1.220  23.270 1.00 45.35  ? 295 LEU   A CB  1 
ATOM   2184 C  CG  . LEU   A  1  282 ? 53.592  -1.626  22.771 1.00 46.11  ? 295 LEU   A CG  1 
ATOM   2185 C  CD1 . LEU   A  1  282 ? 53.351  -3.136  22.896 1.00 46.08  ? 295 LEU   A CD1 1 
ATOM   2186 C  CD2 . LEU   A  1  282 ? 52.545  -0.832  23.534 1.00 47.46  ? 295 LEU   A CD2 1 
ATOM   2187 N  N   . CYS   A  1  283 ? 57.809  0.488   23.434 1.00 46.10  ? 296 CYS   A N   1 
ATOM   2188 C  CA  . CYS   A  1  283 ? 58.956  0.805   24.281 1.00 48.52  ? 296 CYS   A CA  1 
ATOM   2189 C  C   . CYS   A  1  283 ? 59.032  2.288   24.604 1.00 44.19  ? 296 CYS   A C   1 
ATOM   2190 O  O   . CYS   A  1  283 ? 59.602  2.650   25.629 1.00 48.85  ? 296 CYS   A O   1 
ATOM   2191 C  CB  . CYS   A  1  283 ? 60.293  0.317   23.721 1.00 55.58  ? 296 CYS   A CB  1 
ATOM   2192 S  SG  . CYS   A  1  283 ? 60.508  -1.489  23.809 1.00 73.38  ? 296 CYS   A SG  1 
ATOM   2193 N  N   . ARG   A  1  284 ? 58.424  3.136   23.764 1.00 44.52  ? 297 ARG   A N   1 
ATOM   2194 C  CA  . ARG   A  1  284 ? 58.316  4.545   24.093 1.00 42.85  ? 297 ARG   A CA  1 
ATOM   2195 C  C   . ARG   A  1  284 ? 57.582  4.734   25.416 1.00 39.98  ? 297 ARG   A C   1 
ATOM   2196 O  O   . ARG   A  1  284 ? 57.913  5.651   26.164 1.00 41.86  ? 297 ARG   A O   1 
ATOM   2197 C  CB  . ARG   A  1  284 ? 57.585  5.339   23.013 1.00 46.89  ? 297 ARG   A CB  1 
ATOM   2198 C  CG  . ARG   A  1  284 ? 58.401  5.451   21.733 1.00 48.73  ? 297 ARG   A CG  1 
ATOM   2199 C  CD  . ARG   A  1  284 ? 57.624  6.316   20.752 1.00 55.34  ? 297 ARG   A CD  1 
ATOM   2200 N  NE  . ARG   A  1  284 ? 58.208  6.259   19.413 1.00 57.19  ? 297 ARG   A NE  1 
ATOM   2201 C  CZ  . ARG   A  1  284 ? 57.683  6.781   18.321 1.00 63.56  ? 297 ARG   A CZ  1 
ATOM   2202 N  NH1 . ARG   A  1  284 ? 56.552  7.465   18.376 1.00 59.52  ? 297 ARG   A NH1 1 
ATOM   2203 N  NH2 . ARG   A  1  284 ? 58.298  6.595   17.165 1.00 67.22  ? 297 ARG   A NH2 1 
ATOM   2204 N  N   . LEU   A  1  285 ? 56.585  3.883   25.689 1.00 36.44  ? 298 LEU   A N   1 
ATOM   2205 C  CA  . LEU   A  1  285 ? 55.827  3.989   26.922 1.00 39.11  ? 298 LEU   A CA  1 
ATOM   2206 C  C   . LEU   A  1  285 ? 56.786  3.774   28.092 1.00 36.82  ? 298 LEU   A C   1 
ATOM   2207 O  O   . LEU   A  1  285 ? 56.764  4.536   29.059 1.00 34.92  ? 298 LEU   A O   1 
ATOM   2208 C  CB  . LEU   A  1  285 ? 54.639  3.029   26.929 1.00 43.27  ? 298 LEU   A CB  1 
ATOM   2209 C  CG  . LEU   A  1  285 ? 53.667  3.147   28.108 1.00 51.97  ? 298 LEU   A CG  1 
ATOM   2210 C  CD1 . LEU   A  1  285 ? 52.320  2.538   27.766 1.00 58.46  ? 298 LEU   A CD1 1 
ATOM   2211 C  CD2 . LEU   A  1  285 ? 54.175  2.495   29.383 1.00 56.53  ? 298 LEU   A CD2 1 
ATOM   2212 N  N   . TYR   A  1  286 ? 57.675  2.786   27.959 1.00 38.69  ? 299 TYR   A N   1 
ATOM   2213 C  CA  . TYR   A  1  286 ? 58.650  2.472   29.001 1.00 38.87  ? 299 TYR   A CA  1 
ATOM   2214 C  C   . TYR   A  1  286 ? 59.575  3.662   29.238 1.00 36.49  ? 299 TYR   A C   1 
ATOM   2215 O  O   . TYR   A  1  286 ? 59.743  4.103   30.370 1.00 42.99  ? 299 TYR   A O   1 
ATOM   2216 C  CB  . TYR   A  1  286 ? 59.436  1.207   28.641 1.00 38.84  ? 299 TYR   A CB  1 
ATOM   2217 C  CG  . TYR   A  1  286 ? 60.580  0.912   29.593 1.00 38.02  ? 299 TYR   A CG  1 
ATOM   2218 C  CD1 . TYR   A  1  286 ? 60.340  0.566   30.921 1.00 36.04  ? 299 TYR   A CD1 1 
ATOM   2219 C  CD2 . TYR   A  1  286 ? 61.900  0.992   29.171 1.00 35.09  ? 299 TYR   A CD2 1 
ATOM   2220 C  CE1 . TYR   A  1  286 ? 61.377  0.308   31.802 1.00 31.71  ? 299 TYR   A CE1 1 
ATOM   2221 C  CE2 . TYR   A  1  286 ? 62.948  0.727   30.041 1.00 31.99  ? 299 TYR   A CE2 1 
ATOM   2222 C  CZ  . TYR   A  1  286 ? 62.689  0.397   31.361 1.00 31.89  ? 299 TYR   A CZ  1 
ATOM   2223 O  OH  . TYR   A  1  286 ? 63.743  0.174   32.205 1.00 28.72  ? 299 TYR   A OH  1 
ATOM   2224 N  N   . GLU   A  1  287 ? 60.132  4.220   28.166 1.00 42.73  ? 300 GLU   A N   1 
ATOM   2225 C  CA  . GLU   A  1  287 ? 61.037  5.357   28.268 1.00 47.27  ? 300 GLU   A CA  1 
ATOM   2226 C  C   . GLU   A  1  287 ? 60.313  6.571   28.851 1.00 43.31  ? 300 GLU   A C   1 
ATOM   2227 O  O   . GLU   A  1  287 ? 60.868  7.239   29.720 1.00 39.47  ? 300 GLU   A O   1 
ATOM   2228 C  CB  . GLU   A  1  287 ? 61.644  5.677   26.907 1.00 53.51  ? 300 GLU   A CB  1 
ATOM   2229 C  CG  . GLU   A  1  287 ? 62.566  4.566   26.405 1.00 66.79  ? 300 GLU   A CG  1 
ATOM   2230 C  CD  . GLU   A  1  287 ? 62.924  4.584   24.922 1.00 80.10  ? 300 GLU   A CD  1 
ATOM   2231 O  OE1 . GLU   A  1  287 ? 62.054  4.939   24.090 1.00 86.44  ? 300 GLU   A OE1 1 
ATOM   2232 O  OE2 . GLU   A  1  287 ? 64.079  4.211   24.583 1.00 89.78  ? 300 GLU   A OE2 1 
ATOM   2233 N  N   . PHE   A  1  288 ? 59.081  6.827   28.392 1.00 36.15  ? 301 PHE   A N   1 
ATOM   2234 C  CA  . PHE   A  1  288 ? 58.288  7.952   28.852 1.00 37.57  ? 301 PHE   A CA  1 
ATOM   2235 C  C   . PHE   A  1  288 ? 58.105  7.847   30.360 1.00 35.06  ? 301 PHE   A C   1 
ATOM   2236 O  O   . PHE   A  1  288 ? 58.345  8.806   31.081 1.00 36.07  ? 301 PHE   A O   1 
ATOM   2237 C  CB  . PHE   A  1  288 ? 56.943  8.022   28.107 1.00 41.73  ? 301 PHE   A CB  1 
ATOM   2238 C  CG  . PHE   A  1  288 ? 56.117  9.229   28.525 1.00 43.37  ? 301 PHE   A CG  1 
ATOM   2239 C  CD1 . PHE   A  1  288 ? 56.304  10.463  27.901 1.00 44.33  ? 301 PHE   A CD1 1 
ATOM   2240 C  CD2 . PHE   A  1  288 ? 55.208  9.141   29.572 1.00 41.30  ? 301 PHE   A CD2 1 
ATOM   2241 C  CE1 . PHE   A  1  288 ? 55.567  11.576  28.289 1.00 46.17  ? 301 PHE   A CE1 1 
ATOM   2242 C  CE2 . PHE   A  1  288 ? 54.497  10.263  29.978 1.00 47.68  ? 301 PHE   A CE2 1 
ATOM   2243 C  CZ  . PHE   A  1  288 ? 54.677  11.480  29.335 1.00 49.38  ? 301 PHE   A CZ  1 
ATOM   2244 N  N   . VAL   A  1  289 ? 57.730  6.659   30.841 1.00 32.99  ? 302 VAL   A N   1 
ATOM   2245 C  CA  . VAL   A  1  289 ? 57.429  6.464   32.252 1.00 32.34  ? 302 VAL   A CA  1 
ATOM   2246 C  C   . VAL   A  1  289 ? 58.688  6.607   33.096 1.00 30.30  ? 302 VAL   A C   1 
ATOM   2247 O  O   . VAL   A  1  289 ? 58.642  7.183   34.176 1.00 29.89  ? 302 VAL   A O   1 
ATOM   2248 C  CB  . VAL   A  1  289 ? 56.722  5.116   32.510 1.00 30.79  ? 302 VAL   A CB  1 
ATOM   2249 C  CG1 . VAL   A  1  289 ? 56.693  4.753   33.988 1.00 31.80  ? 302 VAL   A CG1 1 
ATOM   2250 C  CG2 . VAL   A  1  289 ? 55.311  5.117   31.950 1.00 29.77  ? 302 VAL   A CG2 1 
ATOM   2251 N  N   . VAL   A  1  290 ? 59.811  6.058   32.628 1.00 34.23  ? 303 VAL   A N   1 
ATOM   2252 C  CA  . VAL   A  1  290 ? 61.066  6.232   33.356 1.00 33.61  ? 303 VAL   A CA  1 
ATOM   2253 C  C   . VAL   A  1  290 ? 61.411  7.722   33.464 1.00 33.35  ? 303 VAL   A C   1 
ATOM   2254 O  O   . VAL   A  1  290 ? 61.794  8.181   34.534 1.00 34.17  ? 303 VAL   A O   1 
ATOM   2255 C  CB  . VAL   A  1  290 ? 62.212  5.432   32.723 1.00 34.78  ? 303 VAL   A CB  1 
ATOM   2256 C  CG1 . VAL   A  1  290 ? 63.554  5.783   33.343 1.00 35.72  ? 303 VAL   A CG1 1 
ATOM   2257 C  CG2 . VAL   A  1  290 ? 61.952  3.936   32.827 1.00 34.89  ? 303 VAL   A CG2 1 
ATOM   2258 N  N   . GLY   A  1  291 ? 61.258  8.477   32.367 1.00 33.74  ? 304 GLY   A N   1 
ATOM   2259 C  CA  . GLY   A  1  291 ? 61.328  9.936   32.377 1.00 33.58  ? 304 GLY   A CA  1 
ATOM   2260 C  C   . GLY   A  1  291 ? 60.440  10.540  33.464 1.00 34.62  ? 304 GLY   A C   1 
ATOM   2261 O  O   . GLY   A  1  291 ? 60.908  11.335  34.276 1.00 36.53  ? 304 GLY   A O   1 
ATOM   2262 N  N   . SER   A  1  292 ? 59.161  10.132  33.503 1.00 33.37  ? 305 SER   A N   1 
ATOM   2263 C  CA  . SER   A  1  292 ? 58.221  10.672  34.468 1.00 33.47  ? 305 SER   A CA  1 
ATOM   2264 C  C   . SER   A  1  292 ? 58.696  10.396  35.890 1.00 30.45  ? 305 SER   A C   1 
ATOM   2265 O  O   . SER   A  1  292 ? 58.548  11.231  36.761 1.00 36.58  ? 305 SER   A O   1 
ATOM   2266 C  CB  . SER   A  1  292 ? 56.836  10.146  34.238 1.00 33.62  ? 305 SER   A CB  1 
ATOM   2267 O  OG  . SER   A  1  292 ? 56.452  10.317  32.879 1.00 36.88  ? 305 SER   A OG  1 
ATOM   2268 N  N   . VAL   A  1  293 ? 59.263  9.220   36.124 1.00 33.64  ? 306 VAL   A N   1 
ATOM   2269 C  CA  . VAL   A  1  293 ? 59.769  8.857   37.442 1.00 36.44  ? 306 VAL   A CA  1 
ATOM   2270 C  C   . VAL   A  1  293 ? 60.928  9.772   37.824 1.00 34.27  ? 306 VAL   A C   1 
ATOM   2271 O  O   . VAL   A  1  293 ? 61.048  10.132  38.986 1.00 38.40  ? 306 VAL   A O   1 
ATOM   2272 C  CB  . VAL   A  1  293 ? 60.178  7.369   37.504 1.00 34.86  ? 306 VAL   A CB  1 
ATOM   2273 C  CG1 . VAL   A  1  293 ? 60.991  7.027   38.755 1.00 32.33  ? 306 VAL   A CG1 1 
ATOM   2274 C  CG2 . VAL   A  1  293 ? 58.942  6.493   37.398 1.00 34.82  ? 306 VAL   A CG2 1 
ATOM   2275 N  N   . GLN   A  1  294 ? 61.768  10.155  36.857 1.00 32.70  ? 307 GLN   A N   1 
ATOM   2276 C  CA  . GLN   A  1  294 ? 62.873  11.053  37.142 1.00 34.33  ? 307 GLN   A CA  1 
ATOM   2277 C  C   . GLN   A  1  294 ? 62.371  12.435  37.552 1.00 35.66  ? 307 GLN   A C   1 
ATOM   2278 O  O   . GLN   A  1  294 ? 62.974  13.058  38.424 1.00 40.15  ? 307 GLN   A O   1 
ATOM   2279 C  CB  . GLN   A  1  294 ? 63.811  11.122  35.949 1.00 34.86  ? 307 GLN   A CB  1 
ATOM   2280 C  CG  . GLN   A  1  294 ? 64.567  9.821   35.741 1.00 38.12  ? 307 GLN   A CG  1 
ATOM   2281 C  CD  . GLN   A  1  294 ? 65.365  9.823   34.461 1.00 40.19  ? 307 GLN   A CD  1 
ATOM   2282 O  OE1 . GLN   A  1  294 ? 64.851  9.525   33.377 1.00 47.09  ? 307 GLN   A OE1 1 
ATOM   2283 N  NE2 . GLN   A  1  294 ? 66.632  10.179  34.574 1.00 37.85  ? 307 GLN   A NE2 1 
ATOM   2284 N  N   . GLU   A  1  295 ? 61.273  12.901  36.936 1.00 37.25  ? 308 GLU   A N   1 
ATOM   2285 C  CA  . GLU   A  1  295 ? 60.674  14.168  37.306 1.00 39.71  ? 308 GLU   A CA  1 
ATOM   2286 C  C   . GLU   A  1  295 ? 60.160  14.090  38.740 1.00 38.33  ? 308 GLU   A C   1 
ATOM   2287 O  O   . GLU   A  1  295 ? 60.334  15.047  39.479 1.00 40.18  ? 308 GLU   A O   1 
ATOM   2288 C  CB  . GLU   A  1  295 ? 59.551  14.592  36.361 1.00 45.86  ? 308 GLU   A CB  1 
ATOM   2289 C  CG  . GLU   A  1  295 ? 60.006  14.880  34.935 1.00 55.32  ? 308 GLU   A CG  1 
ATOM   2290 C  CD  . GLU   A  1  295 ? 58.867  14.910  33.916 1.00 66.19  ? 308 GLU   A CD  1 
ATOM   2291 O  OE1 . GLU   A  1  295 ? 57.686  14.666  34.280 1.00 70.08  ? 308 GLU   A OE1 1 
ATOM   2292 O  OE2 . GLU   A  1  295 ? 59.174  15.172  32.728 1.00 75.69  ? 308 GLU   A OE2 1 
ATOM   2293 N  N   . LEU   A  1  296 ? 59.555  12.954  39.133 1.00 35.29  ? 309 LEU   A N   1 
ATOM   2294 C  CA  . LEU   A  1  296 ? 59.006  12.790  40.472 1.00 35.81  ? 309 LEU   A CA  1 
ATOM   2295 C  C   . LEU   A  1  296 ? 60.127  12.658  41.487 1.00 31.60  ? 309 LEU   A C   1 
ATOM   2296 O  O   . LEU   A  1  296 ? 59.969  13.089  42.625 1.00 32.03  ? 309 LEU   A O   1 
ATOM   2297 C  CB  . LEU   A  1  296 ? 58.066  11.587  40.604 1.00 35.95  ? 309 LEU   A CB  1 
ATOM   2298 C  CG  . LEU   A  1  296 ? 56.779  11.649  39.780 1.00 37.43  ? 309 LEU   A CG  1 
ATOM   2299 C  CD1 . LEU   A  1  296 ? 56.115  10.305  39.881 1.00 39.77  ? 309 LEU   A CD1 1 
ATOM   2300 C  CD2 . LEU   A  1  296 ? 55.821  12.769  40.193 1.00 35.89  ? 309 LEU   A CD2 1 
ATOM   2301 N  N   . TYR   A  1  297 ? 61.221  11.999  41.091 1.00 32.55  ? 310 TYR   A N   1 
ATOM   2302 C  CA  . TYR   A  1  297 ? 62.324  11.717  42.005 1.00 33.09  ? 310 TYR   A CA  1 
ATOM   2303 C  C   . TYR   A  1  297 ? 63.635  12.218  41.398 1.00 35.28  ? 310 TYR   A C   1 
ATOM   2304 O  O   . TYR   A  1  297 ? 64.404  11.439  40.849 1.00 34.16  ? 310 TYR   A O   1 
ATOM   2305 C  CB  . TYR   A  1  297 ? 62.380  10.213  42.291 1.00 29.99  ? 310 TYR   A CB  1 
ATOM   2306 C  CG  . TYR   A  1  297 ? 61.165  9.680   43.025 1.00 29.27  ? 310 TYR   A CG  1 
ATOM   2307 C  CD1 . TYR   A  1  297 ? 61.032  9.847   44.400 1.00 30.50  ? 310 TYR   A CD1 1 
ATOM   2308 C  CD2 . TYR   A  1  297 ? 60.146  9.021   42.348 1.00 29.68  ? 310 TYR   A CD2 1 
ATOM   2309 C  CE1 . TYR   A  1  297 ? 59.921  9.371   45.076 1.00 33.08  ? 310 TYR   A CE1 1 
ATOM   2310 C  CE2 . TYR   A  1  297 ? 59.025  8.545   43.016 1.00 28.21  ? 310 TYR   A CE2 1 
ATOM   2311 C  CZ  . TYR   A  1  297 ? 58.919  8.710   44.382 1.00 29.90  ? 310 TYR   A CZ  1 
ATOM   2312 O  OH  . TYR   A  1  297 ? 57.815  8.277   45.043 1.00 31.72  ? 310 TYR   A OH  1 
ATOM   2313 N  N   . PRO   A  1  298 ? 63.913  13.537  41.431 1.00 39.34  ? 311 PRO   A N   1 
ATOM   2314 C  CA  . PRO   A  1  298 ? 65.098  14.081  40.776 1.00 41.36  ? 311 PRO   A CA  1 
ATOM   2315 C  C   . PRO   A  1  298 ? 66.439  13.698  41.403 1.00 36.01  ? 311 PRO   A C   1 
ATOM   2316 O  O   . PRO   A  1  298 ? 67.416  13.641  40.677 1.00 39.61  ? 311 PRO   A O   1 
ATOM   2317 C  CB  . PRO   A  1  298 ? 64.866  15.611  40.750 1.00 42.93  ? 311 PRO   A CB  1 
ATOM   2318 C  CG  . PRO   A  1  298 ? 63.804  15.887  41.791 1.00 46.43  ? 311 PRO   A CG  1 
ATOM   2319 C  CD  . PRO   A  1  298 ? 63.085  14.575  42.056 1.00 42.58  ? 311 PRO   A CD  1 
ATOM   2320 N  N   . ASN   A  1  299 ? 66.510  13.443  42.713 1.00 37.51  ? 312 ASN   A N   1 
ATOM   2321 C  CA  . ASN   A  1  299 ? 67.800  13.127  43.324 1.00 33.17  ? 312 ASN   A CA  1 
ATOM   2322 C  C   . ASN   A  1  299 ? 67.636  12.315  44.603 1.00 31.25  ? 312 ASN   A C   1 
ATOM   2323 O  O   . ASN   A  1  299 ? 68.026  12.758  45.685 1.00 29.03  ? 312 ASN   A O   1 
ATOM   2324 C  CB  . ASN   A  1  299 ? 68.619  14.384  43.611 1.00 33.98  ? 312 ASN   A CB  1 
ATOM   2325 C  CG  . ASN   A  1  299 ? 69.990  14.073  44.164 1.00 35.15  ? 312 ASN   A CG  1 
ATOM   2326 O  OD1 . ASN   A  1  299 ? 70.712  13.206  43.632 1.00 32.42  ? 312 ASN   A OD1 1 
ATOM   2327 N  ND2 . ASN   A  1  299 ? 70.330  14.731  45.262 1.00 32.04  ? 312 ASN   A ND2 1 
ATOM   2328 N  N   . PRO   A  1  300 ? 67.103  11.079  44.526 1.00 32.53  ? 313 PRO   A N   1 
ATOM   2329 C  CA  . PRO   A  1  300 ? 66.885  10.272  45.728 1.00 32.96  ? 313 PRO   A CA  1 
ATOM   2330 C  C   . PRO   A  1  300 ? 68.180  9.657   46.241 1.00 31.21  ? 313 PRO   A C   1 
ATOM   2331 O  O   . PRO   A  1  300 ? 69.090  9.393   45.475 1.00 35.01  ? 313 PRO   A O   1 
ATOM   2332 C  CB  . PRO   A  1  300 ? 65.914  9.219   45.229 1.00 32.33  ? 313 PRO   A CB  1 
ATOM   2333 C  CG  . PRO   A  1  300 ? 66.375  8.985   43.811 1.00 32.92  ? 313 PRO   A CG  1 
ATOM   2334 C  CD  . PRO   A  1  300 ? 66.700  10.383  43.294 1.00 33.54  ? 313 PRO   A CD  1 
ATOM   2335 N  N   . THR   A  1  301 ? 68.227  9.431   47.552 1.00 35.14  ? 314 THR   A N   1 
ATOM   2336 C  CA  . THR   A  1  301 ? 69.315  8.722   48.203 1.00 40.06  ? 314 THR   A CA  1 
ATOM   2337 C  C   . THR   A  1  301 ? 68.692  7.753   49.212 1.00 36.56  ? 314 THR   A C   1 
ATOM   2338 O  O   . THR   A  1  301 ? 67.472  7.734   49.400 1.00 34.91  ? 314 THR   A O   1 
ATOM   2339 C  CB  . THR   A  1  301 ? 70.277  9.718   48.866 1.00 47.71  ? 314 THR   A CB  1 
ATOM   2340 O  OG1 . THR   A  1  301 ? 69.549  10.474  49.828 1.00 48.03  ? 314 THR   A OG1 1 
ATOM   2341 C  CG2 . THR   A  1  301 ? 70.896  10.709  47.892 1.00 50.68  ? 314 THR   A CG2 1 
ATOM   2342 N  N   . GLY   A  1  302 ? 69.539  6.954   49.875 1.00 36.06  ? 315 GLY   A N   1 
ATOM   2343 C  CA  . GLY   A  1  302 ? 69.121  6.075   50.954 1.00 33.08  ? 315 GLY   A CA  1 
ATOM   2344 C  C   . GLY   A  1  302 ? 68.107  5.022   50.487 1.00 36.66  ? 315 GLY   A C   1 
ATOM   2345 O  O   . GLY   A  1  302 ? 68.192  4.491   49.385 1.00 34.31  ? 315 GLY   A O   1 
ATOM   2346 N  N   . ILE   A  1  303 ? 67.142  4.736   51.362 1.00 40.53  ? 316 ILE   A N   1 
ATOM   2347 C  CA  . ILE   A  1  303 ? 66.157  3.683   51.178 1.00 42.09  ? 316 ILE   A CA  1 
ATOM   2348 C  C   . ILE   A  1  303 ? 65.287  4.027   49.973 1.00 37.08  ? 316 ILE   A C   1 
ATOM   2349 O  O   . ILE   A  1  303 ? 64.895  3.145   49.220 1.00 36.48  ? 316 ILE   A O   1 
ATOM   2350 C  CB  . ILE   A  1  303 ? 65.307  3.507   52.455 1.00 50.82  ? 316 ILE   A CB  1 
ATOM   2351 C  CG1 . ILE   A  1  303 ? 66.166  3.351   53.728 1.00 69.34  ? 316 ILE   A CG1 1 
ATOM   2352 C  CG2 . ILE   A  1  303 ? 64.322  2.352   52.300 1.00 54.11  ? 316 ILE   A CG2 1 
ATOM   2353 C  CD1 . ILE   A  1  303 ? 67.083  2.129   53.773 1.00 72.78  ? 316 ILE   A CD1 1 
ATOM   2354 N  N   . LEU   A  1  304 ? 64.986  5.318   49.789 1.00 35.09  ? 317 LEU   A N   1 
ATOM   2355 C  CA  . LEU   A  1  304 ? 64.149  5.735   48.683 1.00 33.67  ? 317 LEU   A CA  1 
ATOM   2356 C  C   . LEU   A  1  304 ? 64.836  5.350   47.376 1.00 32.36  ? 317 LEU   A C   1 
ATOM   2357 O  O   . LEU   A  1  304 ? 64.215  4.808   46.473 1.00 30.16  ? 317 LEU   A O   1 
ATOM   2358 C  CB  . LEU   A  1  304 ? 63.853  7.228   48.775 1.00 33.61  ? 317 LEU   A CB  1 
ATOM   2359 C  CG  . LEU   A  1  304 ? 63.104  7.825   47.586 1.00 34.62  ? 317 LEU   A CG  1 
ATOM   2360 C  CD1 . LEU   A  1  304 ? 61.778  7.119   47.379 1.00 33.20  ? 317 LEU   A CD1 1 
ATOM   2361 C  CD2 . LEU   A  1  304 ? 62.896  9.316   47.797 1.00 34.29  ? 317 LEU   A CD2 1 
ATOM   2362 N  N   . ARG   A  1  305 ? 66.132  5.629   47.273 1.00 31.58  ? 318 ARG   A N   1 
ATOM   2363 C  CA  A ARG   A  1  305 ? 66.868  5.329   46.062 0.50 30.35  ? 318 ARG   A CA  1 
ATOM   2364 C  CA  B ARG   A  1  305 ? 66.870  5.329   46.062 0.50 33.12  ? 318 ARG   A CA  1 
ATOM   2365 C  C   . ARG   A  1  305 ? 66.871  3.825   45.839 1.00 32.25  ? 318 ARG   A C   1 
ATOM   2366 O  O   . ARG   A  1  305 ? 66.651  3.365   44.732 1.00 36.79  ? 318 ARG   A O   1 
ATOM   2367 C  CB  A ARG   A  1  305 ? 68.305  5.859   46.132 0.50 27.42  ? 318 ARG   A CB  1 
ATOM   2368 C  CB  B ARG   A  1  305 ? 68.307  5.859   46.131 0.50 33.98  ? 318 ARG   A CB  1 
ATOM   2369 C  CG  A ARG   A  1  305 ? 69.184  5.430   44.969 0.50 23.23  ? 318 ARG   A CG  1 
ATOM   2370 C  CG  B ARG   A  1  305 ? 69.192  5.411   44.977 0.50 32.48  ? 318 ARG   A CG  1 
ATOM   2371 C  CD  A ARG   A  1  305 ? 70.618  5.827   45.244 0.50 22.20  ? 318 ARG   A CD  1 
ATOM   2372 C  CD  B ARG   A  1  305 ? 70.567  6.022   45.085 0.50 34.77  ? 318 ARG   A CD  1 
ATOM   2373 N  NE  A ARG   A  1  305 ? 71.483  5.332   44.168 0.50 19.35  ? 318 ARG   A NE  1 
ATOM   2374 N  NE  B ARG   A  1  305 ? 71.178  6.225   43.764 0.50 33.83  ? 318 ARG   A NE  1 
ATOM   2375 C  CZ  A ARG   A  1  305 ? 72.046  4.151   44.169 0.50 15.71  ? 318 ARG   A CZ  1 
ATOM   2376 C  CZ  B ARG   A  1  305 ? 71.024  7.272   42.943 0.50 29.99  ? 318 ARG   A CZ  1 
ATOM   2377 N  NH1 A ARG   A  1  305 ? 72.103  3.471   45.286 0.50 15.48  ? 318 ARG   A NH1 1 
ATOM   2378 N  NH1 B ARG   A  1  305 ? 70.275  8.362   43.232 0.50 31.64  ? 318 ARG   A NH1 1 
ATOM   2379 N  NH2 A ARG   A  1  305 ? 72.558  3.694   43.061 0.50 14.64  ? 318 ARG   A NH2 1 
ATOM   2380 N  NH2 B ARG   A  1  305 ? 71.651  7.191   41.793 0.50 23.14  ? 318 ARG   A NH2 1 
ATOM   2381 N  N   . ARG   A  1  306 ? 67.150  3.076   46.901 1.00 37.99  ? 319 ARG   A N   1 
ATOM   2382 C  CA  . ARG   A  1  306 ? 67.214  1.625   46.816 1.00 37.82  ? 319 ARG   A CA  1 
ATOM   2383 C  C   . ARG   A  1  306 ? 65.879  1.073   46.312 1.00 36.07  ? 319 ARG   A C   1 
ATOM   2384 O  O   . ARG   A  1  306 ? 65.864  0.233   45.409 1.00 31.75  ? 319 ARG   A O   1 
ATOM   2385 C  CB  . ARG   A  1  306 ? 67.592  1.060   48.190 1.00 40.84  ? 319 ARG   A CB  1 
ATOM   2386 C  CG  . ARG   A  1  306 ? 67.881  -0.437  48.188 1.00 51.63  ? 319 ARG   A CG  1 
ATOM   2387 C  CD  . ARG   A  1  306 ? 67.871  -1.095  49.568 1.00 60.75  ? 319 ARG   A CD  1 
ATOM   2388 N  NE  . ARG   A  1  306 ? 66.536  -1.083  50.181 1.00 75.59  ? 319 ARG   A NE  1 
ATOM   2389 C  CZ  . ARG   A  1  306 ? 66.261  -1.327  51.471 1.00 84.51  ? 319 ARG   A CZ  1 
ATOM   2390 N  NH1 . ARG   A  1  306 ? 67.220  -1.699  52.312 1.00 79.18  ? 319 ARG   A NH1 1 
ATOM   2391 N  NH2 . ARG   A  1  306 ? 65.026  -1.178  51.932 1.00 86.21  ? 319 ARG   A NH2 1 
ATOM   2392 N  N   . ASN   A  1  307 ? 64.761  1.563   46.885 1.00 29.12  ? 320 ASN   A N   1 
ATOM   2393 C  CA  . ASN   A  1  307 ? 63.467  1.010   46.549 1.00 31.42  ? 320 ASN   A CA  1 
ATOM   2394 C  C   . ASN   A  1  307 ? 63.060  1.437   45.145 1.00 31.04  ? 320 ASN   A C   1 
ATOM   2395 O  O   . ASN   A  1  307 ? 62.419  0.655   44.445 1.00 35.05  ? 320 ASN   A O   1 
ATOM   2396 C  CB  . ASN   A  1  307 ? 62.425  1.321   47.614 1.00 32.57  ? 320 ASN   A CB  1 
ATOM   2397 C  CG  . ASN   A  1  307 ? 62.707  0.577   48.903 1.00 33.04  ? 320 ASN   A CG  1 
ATOM   2398 O  OD1 . ASN   A  1  307 ? 63.727  -0.118  49.017 1.00 30.80  ? 320 ASN   A OD1 1 
ATOM   2399 N  ND2 . ASN   A  1  307 ? 61.829  0.711   49.886 1.00 34.37  ? 320 ASN   A ND2 1 
ATOM   2400 N  N   . LEU   A  1  308 ? 63.454  2.645   44.720 1.00 32.49  ? 321 LEU   A N   1 
ATOM   2401 C  CA  . LEU   A  1  308 ? 63.226  3.064   43.346 1.00 34.84  ? 321 LEU   A CA  1 
ATOM   2402 C  C   . LEU   A  1  308 ? 63.909  2.092   42.390 1.00 32.44  ? 321 LEU   A C   1 
ATOM   2403 O  O   . LEU   A  1  308 ? 63.332  1.684   41.399 1.00 31.52  ? 321 LEU   A O   1 
ATOM   2404 C  CB  . LEU   A  1  308 ? 63.744  4.473   43.078 1.00 38.63  ? 321 LEU   A CB  1 
ATOM   2405 C  CG  . LEU   A  1  308 ? 62.735  5.598   43.239 1.00 44.18  ? 321 LEU   A CG  1 
ATOM   2406 C  CD1 . LEU   A  1  308 ? 63.472  6.907   43.392 1.00 51.64  ? 321 LEU   A CD1 1 
ATOM   2407 C  CD2 . LEU   A  1  308 ? 61.808  5.627   42.032 1.00 44.87  ? 321 LEU   A CD2 1 
ATOM   2408 N  N   . ILE   A  1  309 ? 65.170  1.777   42.668 1.00 31.92  ? 322 ILE   A N   1 
ATOM   2409 C  CA  . ILE   A  1  309 ? 65.939  0.934   41.771 1.00 34.71  ? 322 ILE   A CA  1 
ATOM   2410 C  C   . ILE   A  1  309 ? 65.274  -0.431  41.630 1.00 34.17  ? 322 ILE   A C   1 
ATOM   2411 O  O   . ILE   A  1  309 ? 65.177  -0.966  40.540 1.00 31.98  ? 322 ILE   A O   1 
ATOM   2412 C  CB  . ILE   A  1  309 ? 67.391  0.827   42.247 1.00 31.15  ? 322 ILE   A CB  1 
ATOM   2413 C  CG1 . ILE   A  1  309 ? 68.130  2.159   42.013 1.00 34.57  ? 322 ILE   A CG1 1 
ATOM   2414 C  CG2 . ILE   A  1  309 ? 68.098  -0.321  41.536 1.00 32.16  ? 322 ILE   A CG2 1 
ATOM   2415 C  CD1 . ILE   A  1  309 ? 69.502  2.214   42.664 1.00 33.94  ? 322 ILE   A CD1 1 
ATOM   2416 N  N   . LYS   A  1  310 ? 64.827  -0.993  42.747 1.00 34.16  ? 323 LYS   A N   1 
ATOM   2417 C  CA  . LYS   A  1  310 ? 64.199  -2.306  42.733 1.00 35.87  ? 323 LYS   A CA  1 
ATOM   2418 C  C   . LYS   A  1  310 ? 62.848  -2.295  42.013 1.00 34.43  ? 323 LYS   A C   1 
ATOM   2419 O  O   . LYS   A  1  310 ? 62.595  -3.146  41.177 1.00 31.41  ? 323 LYS   A O   1 
ATOM   2420 C  CB  . LYS   A  1  310 ? 64.041  -2.796  44.172 1.00 39.05  ? 323 LYS   A CB  1 
ATOM   2421 C  CG  . LYS   A  1  310 ? 65.348  -3.261  44.786 1.00 39.73  ? 323 LYS   A CG  1 
ATOM   2422 C  CD  . LYS   A  1  310 ? 65.194  -3.616  46.255 1.00 46.48  ? 323 LYS   A CD  1 
ATOM   2423 C  CE  . LYS   A  1  310 ? 66.381  -4.379  46.782 1.00 51.70  ? 323 LYS   A CE  1 
ATOM   2424 N  NZ  . LYS   A  1  310 ? 66.252  -4.496  48.237 1.00 56.17  ? 323 LYS   A NZ  1 
ATOM   2425 N  N   . ASN   A  1  311 ? 61.984  -1.322  42.327 1.00 32.27  ? 324 ASN   A N   1 
ATOM   2426 C  CA  . ASN   A  1  311 ? 60.693  -1.229  41.685 1.00 28.87  ? 324 ASN   A CA  1 
ATOM   2427 C  C   . ASN   A  1  311 ? 60.857  -1.005  40.191 1.00 29.15  ? 324 ASN   A C   1 
ATOM   2428 O  O   . ASN   A  1  311 ? 60.103  -1.571  39.406 1.00 29.19  ? 324 ASN   A O   1 
ATOM   2429 C  CB  . ASN   A  1  311 ? 59.817  -0.187  42.355 1.00 31.07  ? 324 ASN   A CB  1 
ATOM   2430 C  CG  . ASN   A  1  311 ? 59.204  -0.721  43.621 1.00 33.58  ? 324 ASN   A CG  1 
ATOM   2431 O  OD1 . ASN   A  1  311 ? 58.197  -1.427  43.566 1.00 38.45  ? 324 ASN   A OD1 1 
ATOM   2432 N  ND2 . ASN   A  1  311 ? 59.752  -0.355  44.768 1.00 37.16  ? 324 ASN   A ND2 1 
ATOM   2433 N  N   . LEU   A  1  312 ? 61.853  -0.213  39.795 1.00 28.82  ? 325 LEU   A N   1 
ATOM   2434 C  CA  . LEU   A  1  312 ? 62.078  0.053   38.390 1.00 31.78  ? 325 LEU   A CA  1 
ATOM   2435 C  C   . LEU   A  1  312 ? 62.426  -1.256  37.705 1.00 32.48  ? 325 LEU   A C   1 
ATOM   2436 O  O   . LEU   A  1  312 ? 61.942  -1.538  36.619 1.00 32.26  ? 325 LEU   A O   1 
ATOM   2437 C  CB  . LEU   A  1  312 ? 63.158  1.111   38.167 1.00 35.16  ? 325 LEU   A CB  1 
ATOM   2438 C  CG  . LEU   A  1  312 ? 62.684  2.557   38.312 1.00 36.61  ? 325 LEU   A CG  1 
ATOM   2439 C  CD1 . LEU   A  1  312 ? 63.862  3.488   38.503 1.00 41.73  ? 325 LEU   A CD1 1 
ATOM   2440 C  CD2 . LEU   A  1  312 ? 61.859  2.960   37.101 1.00 36.92  ? 325 LEU   A CD2 1 
ATOM   2441 N  N   . HIS   A  1  313 ? 63.272  -2.048  38.360 1.00 33.73  ? 326 HIS   A N   1 
ATOM   2442 C  CA  . HIS   A  1  313 ? 63.691  -3.330  37.825 1.00 33.27  ? 326 HIS   A CA  1 
ATOM   2443 C  C   . HIS   A  1  313 ? 62.517  -4.306  37.773 1.00 31.17  ? 326 HIS   A C   1 
ATOM   2444 O  O   . HIS   A  1  313 ? 62.315  -4.972  36.775 1.00 29.12  ? 326 HIS   A O   1 
ATOM   2445 C  CB  . HIS   A  1  313 ? 64.838  -3.901  38.660 1.00 34.06  ? 326 HIS   A CB  1 
ATOM   2446 C  CG  . HIS   A  1  313 ? 65.292  -5.207  38.119 1.00 38.42  ? 326 HIS   A CG  1 
ATOM   2447 N  ND1 . HIS   A  1  313 ? 65.822  -5.310  36.850 1.00 40.27  ? 326 HIS   A ND1 1 
ATOM   2448 C  CD2 . HIS   A  1  313 ? 65.214  -6.457  38.607 1.00 40.22  ? 326 HIS   A CD2 1 
ATOM   2449 C  CE1 . HIS   A  1  313 ? 66.099  -6.587  36.614 1.00 39.63  ? 326 HIS   A CE1 1 
ATOM   2450 N  NE2 . HIS   A  1  313 ? 65.725  -7.299  37.655 1.00 38.33  ? 326 HIS   A NE2 1 
ATOM   2451 N  N   . TYR   A  1  314 ? 61.732  -4.396  38.844 1.00 33.20  ? 327 TYR   A N   1 
ATOM   2452 C  CA  . TYR   A  1  314 ? 60.560  -5.263  38.838 1.00 32.30  ? 327 TYR   A CA  1 
ATOM   2453 C  C   . TYR   A  1  314 ? 59.651  -4.890  37.668 1.00 33.60  ? 327 TYR   A C   1 
ATOM   2454 O  O   . TYR   A  1  314 ? 59.161  -5.762  36.967 1.00 33.93  ? 327 TYR   A O   1 
ATOM   2455 C  CB  . TYR   A  1  314 ? 59.744  -5.157  40.126 1.00 30.70  ? 327 TYR   A CB  1 
ATOM   2456 C  CG  . TYR   A  1  314 ? 60.511  -5.513  41.385 1.00 29.81  ? 327 TYR   A CG  1 
ATOM   2457 C  CD1 . TYR   A  1  314 ? 61.597  -6.379  41.361 1.00 30.82  ? 327 TYR   A CD1 1 
ATOM   2458 C  CD2 . TYR   A  1  314 ? 60.134  -4.984  42.607 1.00 33.64  ? 327 TYR   A CD2 1 
ATOM   2459 C  CE1 . TYR   A  1  314 ? 62.276  -6.719  42.524 1.00 30.82  ? 327 TYR   A CE1 1 
ATOM   2460 C  CE2 . TYR   A  1  314 ? 60.795  -5.309  43.776 1.00 35.66  ? 327 TYR   A CE2 1 
ATOM   2461 C  CZ  . TYR   A  1  314 ? 61.878  -6.171  43.732 1.00 35.32  ? 327 TYR   A CZ  1 
ATOM   2462 O  OH  . TYR   A  1  314 ? 62.521  -6.417  44.910 1.00 38.30  ? 327 TYR   A OH  1 
ATOM   2463 N  N   . TRP   A  1  315 ? 59.455  -3.589  37.446 1.00 34.60  ? 328 TRP   A N   1 
ATOM   2464 C  CA  . TRP   A  1  315 ? 58.558  -3.150  36.396 1.00 34.42  ? 328 TRP   A CA  1 
ATOM   2465 C  C   . TRP   A  1  315 ? 59.102  -3.637  35.070 1.00 33.89  ? 328 TRP   A C   1 
ATOM   2466 O  O   . TRP   A  1  315 ? 58.364  -4.185  34.261 1.00 32.01  ? 328 TRP   A O   1 
ATOM   2467 C  CB  . TRP   A  1  315 ? 58.376  -1.629  36.384 1.00 33.73  ? 328 TRP   A CB  1 
ATOM   2468 C  CG  . TRP   A  1  315 ? 57.270  -1.176  35.477 1.00 30.36  ? 328 TRP   A CG  1 
ATOM   2469 C  CD1 . TRP   A  1  315 ? 56.002  -1.668  35.406 1.00 29.87  ? 328 TRP   A CD1 1 
ATOM   2470 C  CD2 . TRP   A  1  315 ? 57.363  -0.139  34.487 1.00 32.17  ? 328 TRP   A CD2 1 
ATOM   2471 N  NE1 . TRP   A  1  315 ? 55.296  -1.017  34.436 1.00 31.79  ? 328 TRP   A NE1 1 
ATOM   2472 C  CE2 . TRP   A  1  315 ? 56.098  -0.066  33.862 1.00 33.72  ? 328 TRP   A CE2 1 
ATOM   2473 C  CE3 . TRP   A  1  315 ? 58.377  0.728   34.081 1.00 32.25  ? 328 TRP   A CE3 1 
ATOM   2474 C  CZ2 . TRP   A  1  315 ? 55.829  0.850   32.849 1.00 35.33  ? 328 TRP   A CZ2 1 
ATOM   2475 C  CZ3 . TRP   A  1  315 ? 58.106  1.628   33.074 1.00 34.33  ? 328 TRP   A CZ3 1 
ATOM   2476 C  CH2 . TRP   A  1  315 ? 56.862  1.669   32.454 1.00 35.61  ? 328 TRP   A CH2 1 
ATOM   2477 N  N   . TRP   A  1  316 ? 60.411  -3.476  34.896 1.00 33.39  ? 329 TRP   A N   1 
ATOM   2478 C  CA  . TRP   A  1  316 ? 61.043  -3.823  33.640 1.00 34.79  ? 329 TRP   A CA  1 
ATOM   2479 C  C   . TRP   A  1  316 ? 60.865  -5.316  33.370 1.00 35.47  ? 329 TRP   A C   1 
ATOM   2480 O  O   . TRP   A  1  316 ? 60.712  -5.702  32.223 1.00 31.41  ? 329 TRP   A O   1 
ATOM   2481 C  CB  . TRP   A  1  316 ? 62.530  -3.433  33.656 1.00 39.49  ? 329 TRP   A CB  1 
ATOM   2482 C  CG  . TRP   A  1  316 ? 63.247  -3.937  32.443 1.00 40.13  ? 329 TRP   A CG  1 
ATOM   2483 C  CD1 . TRP   A  1  316 ? 63.281  -3.364  31.207 1.00 44.27  ? 329 TRP   A CD1 1 
ATOM   2484 C  CD2 . TRP   A  1  316 ? 63.947  -5.185  32.324 1.00 42.25  ? 329 TRP   A CD2 1 
ATOM   2485 N  NE1 . TRP   A  1  316 ? 63.991  -4.148  30.339 1.00 42.19  ? 329 TRP   A NE1 1 
ATOM   2486 C  CE2 . TRP   A  1  316 ? 64.398  -5.279  30.990 1.00 40.05  ? 329 TRP   A CE2 1 
ATOM   2487 C  CE3 . TRP   A  1  316 ? 64.222  -6.232  33.203 1.00 46.61  ? 329 TRP   A CE3 1 
ATOM   2488 C  CZ2 . TRP   A  1  316 ? 65.116  -6.376  30.519 1.00 40.29  ? 329 TRP   A CZ2 1 
ATOM   2489 C  CZ3 . TRP   A  1  316 ? 64.947  -7.314  32.742 1.00 44.09  ? 329 TRP   A CZ3 1 
ATOM   2490 C  CH2 . TRP   A  1  316 ? 65.367  -7.395  31.411 1.00 39.03  ? 329 TRP   A CH2 1 
ATOM   2491 N  N   . THR   A  1  317 ? 60.883  -6.165  34.409 1.00 37.54  ? 330 THR   A N   1 
ATOM   2492 C  CA  . THR   A  1  317 ? 60.772  -7.599  34.165 1.00 38.35  ? 330 THR   A CA  1 
ATOM   2493 C  C   . THR   A  1  317 ? 59.462  -7.875  33.433 1.00 39.66  ? 330 THR   A C   1 
ATOM   2494 O  O   . THR   A  1  317 ? 59.418  -8.731  32.565 1.00 45.37  ? 330 THR   A O   1 
ATOM   2495 C  CB  . THR   A  1  317 ? 60.833  -8.462  35.428 1.00 37.60  ? 330 THR   A CB  1 
ATOM   2496 O  OG1 . THR   A  1  317 ? 59.717  -8.151  36.278 1.00 38.05  ? 330 THR   A OG1 1 
ATOM   2497 C  CG2 . THR   A  1  317 ? 62.170  -8.341  36.133 1.00 36.22  ? 330 THR   A CG2 1 
ATOM   2498 N  N   . GLY   A  1  318 ? 58.391  -7.174  33.810 1.00 35.49  ? 331 GLY   A N   1 
ATOM   2499 C  CA  . GLY   A  1  318 ? 57.106  -7.339  33.158 1.00 35.82  ? 331 GLY   A CA  1 
ATOM   2500 C  C   . GLY   A  1  318 ? 57.072  -6.675  31.783 1.00 36.10  ? 331 GLY   A C   1 
ATOM   2501 O  O   . GLY   A  1  318 ? 56.557  -7.240  30.837 1.00 35.01  ? 331 GLY   A O   1 
ATOM   2502 N  N   . VAL   A  1  319 ? 57.601  -5.453  31.696 1.00 39.65  ? 332 VAL   A N   1 
ATOM   2503 C  CA  . VAL   A  1  319 ? 57.562  -4.671  30.478 1.00 38.66  ? 332 VAL   A CA  1 
ATOM   2504 C  C   . VAL   A  1  319 ? 58.319  -5.421  29.394 1.00 39.74  ? 332 VAL   A C   1 
ATOM   2505 O  O   . VAL   A  1  319 ? 57.917  -5.413  28.233 1.00 40.38  ? 332 VAL   A O   1 
ATOM   2506 C  CB  . VAL   A  1  319 ? 58.197  -3.295  30.729 1.00 44.65  ? 332 VAL   A CB  1 
ATOM   2507 C  CG1 . VAL   A  1  319 ? 58.434  -2.523  29.446 1.00 43.95  ? 332 VAL   A CG1 1 
ATOM   2508 C  CG2 . VAL   A  1  319 ? 57.362  -2.470  31.692 1.00 48.17  ? 332 VAL   A CG2 1 
ATOM   2509 N  N   . ASN   A  1  320 ? 59.439  -6.040  29.778 1.00 43.64  ? 333 ASN   A N   1 
ATOM   2510 C  CA  . ASN   A  1  320 ? 60.325  -6.686  28.819 1.00 44.95  ? 333 ASN   A CA  1 
ATOM   2511 C  C   . ASN   A  1  320 ? 59.584  -7.786  28.069 1.00 42.78  ? 333 ASN   A C   1 
ATOM   2512 O  O   . ASN   A  1  320 ? 59.714  -7.902  26.856 1.00 40.64  ? 333 ASN   A O   1 
ATOM   2513 C  CB  . ASN   A  1  320 ? 61.570  -7.261  29.481 1.00 45.81  ? 333 ASN   A CB  1 
ATOM   2514 C  CG  . ASN   A  1  320 ? 62.601  -7.672  28.460 1.00 45.54  ? 333 ASN   A CG  1 
ATOM   2515 O  OD1 . ASN   A  1  320 ? 62.926  -6.903  27.549 1.00 49.99  ? 333 ASN   A OD1 1 
ATOM   2516 N  ND2 . ASN   A  1  320 ? 63.109  -8.884  28.572 1.00 40.31  ? 333 ASN   A ND2 1 
ATOM   2517 N  N   . VAL   A  1  321 ? 58.799  -8.573  28.805 1.00 42.81  ? 334 VAL   A N   1 
ATOM   2518 C  CA  . VAL   A  1  321 ? 57.970  -9.612  28.223 1.00 43.81  ? 334 VAL   A CA  1 
ATOM   2519 C  C   . VAL   A  1  321 ? 56.767  -8.986  27.519 1.00 44.79  ? 334 VAL   A C   1 
ATOM   2520 O  O   . VAL   A  1  321 ? 56.567  -9.236  26.337 1.00 44.51  ? 334 VAL   A O   1 
ATOM   2521 C  CB  . VAL   A  1  321 ? 57.541  -10.641 29.290 1.00 50.14  ? 334 VAL   A CB  1 
ATOM   2522 C  CG1 . VAL   A  1  321 ? 56.586  -11.699 28.737 1.00 47.75  ? 334 VAL   A CG1 1 
ATOM   2523 C  CG2 . VAL   A  1  321 ? 58.753  -11.292 29.948 1.00 47.92  ? 334 VAL   A CG2 1 
ATOM   2524 N  N   . ALA   A  1  322 ? 55.977  -8.154  28.214 1.00 47.57  ? 335 ALA   A N   1 
ATOM   2525 C  CA  . ALA   A  1  322 ? 54.719  -7.666  27.660 1.00 45.71  ? 335 ALA   A CA  1 
ATOM   2526 C  C   . ALA   A  1  322 ? 54.937  -6.846  26.387 1.00 44.95  ? 335 ALA   A C   1 
ATOM   2527 O  O   . ALA   A  1  322 ? 54.089  -6.870  25.501 1.00 43.43  ? 335 ALA   A O   1 
ATOM   2528 C  CB  . ALA   A  1  322 ? 53.939  -6.861  28.687 1.00 49.45  ? 335 ALA   A CB  1 
ATOM   2529 N  N   . PHE   A  1  323 ? 56.034  -6.084  26.301 1.00 46.37  ? 336 PHE   A N   1 
ATOM   2530 C  CA  . PHE   A  1  323 ? 56.226  -5.177  25.176 1.00 49.96  ? 336 PHE   A CA  1 
ATOM   2531 C  C   . PHE   A  1  323 ? 57.158  -5.796  24.133 1.00 49.53  ? 336 PHE   A C   1 
ATOM   2532 O  O   . PHE   A  1  323 ? 57.507  -5.127  23.163 1.00 53.54  ? 336 PHE   A O   1 
ATOM   2533 C  CB  . PHE   A  1  323 ? 56.792  -3.829  25.634 1.00 48.67  ? 336 PHE   A CB  1 
ATOM   2534 C  CG  . PHE   A  1  323 ? 55.893  -2.943  26.488 1.00 49.27  ? 336 PHE   A CG  1 
ATOM   2535 C  CD1 . PHE   A  1  323 ? 54.613  -3.340  26.862 1.00 54.25  ? 336 PHE   A CD1 1 
ATOM   2536 C  CD2 . PHE   A  1  323 ? 56.344  -1.706  26.933 1.00 51.17  ? 336 PHE   A CD2 1 
ATOM   2537 C  CE1 . PHE   A  1  323 ? 53.807  -2.527  27.642 1.00 54.56  ? 336 PHE   A CE1 1 
ATOM   2538 C  CE2 . PHE   A  1  323 ? 55.536  -0.896  27.716 1.00 56.05  ? 336 PHE   A CE2 1 
ATOM   2539 C  CZ  . PHE   A  1  323 ? 54.271  -1.308  28.071 1.00 56.72  ? 336 PHE   A CZ  1 
ATOM   2540 N  N   . GLY   A  1  324 ? 57.571  -7.054  24.334 1.00 48.52  ? 337 GLY   A N   1 
ATOM   2541 C  CA  . GLY   A  1  324 ? 58.373  -7.784  23.360 1.00 49.96  ? 337 GLY   A CA  1 
ATOM   2542 C  C   . GLY   A  1  324 ? 59.840  -7.346  23.297 1.00 51.37  ? 337 GLY   A C   1 
ATOM   2543 O  O   . GLY   A  1  324 ? 60.450  -7.448  22.237 1.00 54.80  ? 337 GLY   A O   1 
ATOM   2544 N  N   . GLY   A  1  325 ? 60.403  -6.883  24.426 1.00 50.34  ? 338 GLY   A N   1 
ATOM   2545 C  CA  . GLY   A  1  325 ? 61.825  -6.562  24.548 1.00 49.37  ? 338 GLY   A CA  1 
ATOM   2546 C  C   . GLY   A  1  325 ? 62.087  -5.055  24.549 1.00 50.03  ? 338 GLY   A C   1 
ATOM   2547 O  O   . GLY   A  1  325 ? 61.892  -4.413  23.524 1.00 55.23  ? 338 GLY   A O   1 
ATOM   2548 N  N   . CYS   A  1  326 ? 62.477  -4.494  25.711 1.00 48.92  ? 339 CYS   A N   1 
ATOM   2549 C  CA  . CYS   A  1  326 ? 62.887  -3.099  25.832 1.00 51.80  ? 339 CYS   A CA  1 
ATOM   2550 C  C   . CYS   A  1  326 ? 64.219  -3.069  26.572 1.00 48.74  ? 339 CYS   A C   1 
ATOM   2551 O  O   . CYS   A  1  326 ? 64.399  -3.847  27.502 1.00 50.07  ? 339 CYS   A O   1 
ATOM   2552 C  CB  . CYS   A  1  326 ? 61.886  -2.242  26.612 1.00 55.24  ? 339 CYS   A CB  1 
ATOM   2553 S  SG  . CYS   A  1  326 ? 60.245  -2.091  25.848 1.00 76.24  ? 339 CYS   A SG  1 
ATOM   2554 N  N   . ASP   A  1  327 ? 65.135  -2.184  26.174 1.00 47.64  ? 340 ASP   A N   1 
ATOM   2555 C  CA  . ASP   A  1  327 ? 66.409  -2.056  26.867 1.00 54.22  ? 340 ASP   A CA  1 
ATOM   2556 C  C   . ASP   A  1  327 ? 66.174  -1.430  28.234 1.00 49.69  ? 340 ASP   A C   1 
ATOM   2557 O  O   . ASP   A  1  327 ? 65.549  -0.374  28.332 1.00 54.45  ? 340 ASP   A O   1 
ATOM   2558 C  CB  . ASP   A  1  327 ? 67.411  -1.225  26.079 1.00 63.87  ? 340 ASP   A CB  1 
ATOM   2559 C  CG  . ASP   A  1  327 ? 67.831  -1.806  24.738 1.00 69.96  ? 340 ASP   A CG  1 
ATOM   2560 O  OD1 . ASP   A  1  327 ? 67.607  -3.019  24.535 1.00 66.62  ? 340 ASP   A OD1 1 
ATOM   2561 O  OD2 . ASP   A  1  327 ? 68.344  -1.033  23.900 1.00 74.86  ? 340 ASP   A OD2 1 
ATOM   2562 N  N   . GLU   A  1  328 ? 66.683  -2.088  29.280 1.00 44.88  ? 341 GLU   A N   1 
ATOM   2563 C  CA  . GLU   A  1  328 ? 66.502  -1.593  30.631 1.00 45.77  ? 341 GLU   A CA  1 
ATOM   2564 C  C   . GLU   A  1  328 ? 67.264  -0.276  30.805 1.00 44.36  ? 341 GLU   A C   1 
ATOM   2565 O  O   . GLU   A  1  328 ? 68.392  -0.154  30.359 1.00 40.73  ? 341 GLU   A O   1 
ATOM   2566 C  CB  . GLU   A  1  328 ? 66.888  -2.653  31.657 1.00 40.08  ? 341 GLU   A CB  1 
ATOM   2567 C  CG  . GLU   A  1  328 ? 66.497  -2.253  33.076 1.00 45.61  ? 341 GLU   A CG  1 
ATOM   2568 C  CD  . GLU   A  1  328 ? 66.702  -3.300  34.157 1.00 45.40  ? 341 GLU   A CD  1 
ATOM   2569 O  OE1 . GLU   A  1  328 ? 67.202  -4.398  33.827 1.00 48.27  ? 341 GLU   A OE1 1 
ATOM   2570 O  OE2 . GLU   A  1  328 ? 66.354  -3.014  35.331 1.00 43.40  ? 341 GLU   A OE2 1 
ATOM   2571 N  N   . LEU   A  1  329 ? 66.618  0.703   31.450 1.00 41.94  ? 342 LEU   A N   1 
ATOM   2572 C  CA  . LEU   A  1  329 ? 67.248  1.961   31.792 1.00 42.45  ? 342 LEU   A CA  1 
ATOM   2573 C  C   . LEU   A  1  329 ? 67.607  1.955   33.273 1.00 42.73  ? 342 LEU   A C   1 
ATOM   2574 O  O   . LEU   A  1  329 ? 66.902  1.325   34.083 1.00 40.69  ? 342 LEU   A O   1 
ATOM   2575 C  CB  . LEU   A  1  329 ? 66.288  3.099   31.453 1.00 43.59  ? 342 LEU   A CB  1 
ATOM   2576 C  CG  . LEU   A  1  329 ? 65.953  3.282   29.970 1.00 43.02  ? 342 LEU   A CG  1 
ATOM   2577 C  CD1 . LEU   A  1  329 ? 64.823  4.276   29.791 1.00 42.07  ? 342 LEU   A CD1 1 
ATOM   2578 C  CD2 . LEU   A  1  329 ? 67.179  3.759   29.217 1.00 41.41  ? 342 LEU   A CD2 1 
ATOM   2579 N  N   . PHE   A  1  330 ? 68.684  2.693   33.603 1.00 41.03  ? 343 PHE   A N   1 
ATOM   2580 C  CA  . PHE   A  1  330 ? 69.217  2.749   34.954 1.00 42.41  ? 343 PHE   A CA  1 
ATOM   2581 C  C   . PHE   A  1  330 ? 69.406  4.201   35.379 1.00 42.41  ? 343 PHE   A C   1 
ATOM   2582 O  O   . PHE   A  1  330 ? 70.530  4.628   35.637 1.00 42.38  ? 343 PHE   A O   1 
ATOM   2583 C  CB  . PHE   A  1  330 ? 70.539  1.977   35.025 1.00 43.75  ? 343 PHE   A CB  1 
ATOM   2584 C  CG  . PHE   A  1  330 ? 70.387  0.512   34.648 1.00 42.60  ? 343 PHE   A CG  1 
ATOM   2585 C  CD1 . PHE   A  1  330 ? 69.806  -0.405  35.533 1.00 46.86  ? 343 PHE   A CD1 1 
ATOM   2586 C  CD2 . PHE   A  1  330 ? 70.780  0.066   33.395 1.00 42.31  ? 343 PHE   A CD2 1 
ATOM   2587 C  CE1 . PHE   A  1  330 ? 69.622  -1.737  35.175 1.00 46.56  ? 343 PHE   A CE1 1 
ATOM   2588 C  CE2 . PHE   A  1  330 ? 70.625  -1.278  33.045 1.00 44.45  ? 343 PHE   A CE2 1 
ATOM   2589 C  CZ  . PHE   A  1  330 ? 70.046  -2.177  33.934 1.00 43.60  ? 343 PHE   A CZ  1 
ATOM   2590 N  N   . PRO   A  1  331 ? 68.322  4.992   35.531 1.00 41.09  ? 344 PRO   A N   1 
ATOM   2591 C  CA  . PRO   A  1  331 ? 68.469  6.407   35.875 1.00 40.58  ? 344 PRO   A CA  1 
ATOM   2592 C  C   . PRO   A  1  331 ? 69.131  6.637   37.232 1.00 33.45  ? 344 PRO   A C   1 
ATOM   2593 O  O   . PRO   A  1  331 ? 69.627  7.728   37.490 1.00 33.99  ? 344 PRO   A O   1 
ATOM   2594 C  CB  . PRO   A  1  331 ? 67.008  6.897   35.843 1.00 43.68  ? 344 PRO   A CB  1 
ATOM   2595 C  CG  . PRO   A  1  331 ? 66.206  5.650   36.209 1.00 42.26  ? 344 PRO   A CG  1 
ATOM   2596 C  CD  . PRO   A  1  331 ? 66.912  4.581   35.420 1.00 39.21  ? 344 PRO   A CD  1 
ATOM   2597 N  N   . TYR   A  1  332 ? 69.131  5.615   38.092 1.00 31.05  ? 345 TYR   A N   1 
ATOM   2598 C  CA  . TYR   A  1  332 ? 69.732  5.735   39.411 1.00 33.13  ? 345 TYR   A CA  1 
ATOM   2599 C  C   . TYR   A  1  332 ? 70.896  4.759   39.573 1.00 31.20  ? 345 TYR   A C   1 
ATOM   2600 O  O   . TYR   A  1  332 ? 71.382  4.545   40.680 1.00 30.05  ? 345 TYR   A O   1 
ATOM   2601 C  CB  . TYR   A  1  332 ? 68.680  5.586   40.510 1.00 32.67  ? 345 TYR   A CB  1 
ATOM   2602 C  CG  . TYR   A  1  332 ? 67.518  6.549   40.312 1.00 37.16  ? 345 TYR   A CG  1 
ATOM   2603 C  CD1 . TYR   A  1  332 ? 67.671  7.936   40.450 1.00 36.22  ? 345 TYR   A CD1 1 
ATOM   2604 C  CD2 . TYR   A  1  332 ? 66.278  6.067   39.920 1.00 36.73  ? 345 TYR   A CD2 1 
ATOM   2605 C  CE1 . TYR   A  1  332 ? 66.612  8.796   40.214 1.00 40.42  ? 345 TYR   A CE1 1 
ATOM   2606 C  CE2 . TYR   A  1  332 ? 65.214  6.923   39.691 1.00 40.11  ? 345 TYR   A CE2 1 
ATOM   2607 C  CZ  . TYR   A  1  332 ? 65.377  8.287   39.835 1.00 39.02  ? 345 TYR   A CZ  1 
ATOM   2608 O  OH  . TYR   A  1  332 ? 64.297  9.095   39.615 1.00 38.41  ? 345 TYR   A OH  1 
ATOM   2609 N  N   . GLY   A  1  333 ? 71.388  4.228   38.454 1.00 31.14  ? 346 GLY   A N   1 
ATOM   2610 C  CA  . GLY   A  1  333 ? 72.439  3.235   38.502 1.00 35.71  ? 346 GLY   A CA  1 
ATOM   2611 C  C   . GLY   A  1  333 ? 71.954  1.930   39.131 1.00 40.52  ? 346 GLY   A C   1 
ATOM   2612 O  O   . GLY   A  1  333 ? 70.771  1.591   39.042 1.00 44.74  ? 346 GLY   A O   1 
ATOM   2613 N  N   . GLN   A  1  334 ? 72.878  1.238   39.816 1.00 43.29  ? 347 GLN   A N   1 
ATOM   2614 C  CA  . GLN   A  1  334 ? 72.638  -0.104  40.322 1.00 47.07  ? 347 GLN   A CA  1 
ATOM   2615 C  C   . GLN   A  1  334 ? 72.762  -0.068  41.837 1.00 47.84  ? 347 GLN   A C   1 
ATOM   2616 O  O   . GLN   A  1  334 ? 73.271  0.914   42.374 1.00 46.05  ? 347 GLN   A O   1 
ATOM   2617 C  CB  . GLN   A  1  334 ? 73.632  -1.113  39.747 1.00 52.31  ? 347 GLN   A CB  1 
ATOM   2618 C  CG  . GLN   A  1  334 ? 73.991  -0.890  38.275 1.00 67.27  ? 347 GLN   A CG  1 
ATOM   2619 C  CD  . GLN   A  1  334 ? 73.140  -1.668  37.286 1.00 73.67  ? 347 GLN   A CD  1 
ATOM   2620 O  OE1 . GLN   A  1  334 ? 72.407  -2.606  37.632 1.00 68.89  ? 347 GLN   A OE1 1 
ATOM   2621 N  NE2 . GLN   A  1  334 ? 73.273  -1.311  36.017 1.00 74.46  ? 347 GLN   A NE2 1 
ATOM   2622 N  N   . LEU   A  1  335 ? 72.304  -1.145  42.499 1.00 52.44  ? 348 LEU   A N   1 
ATOM   2623 C  CA  . LEU   A  1  335 ? 72.330  -1.249  43.957 1.00 62.37  ? 348 LEU   A CA  1 
ATOM   2624 C  C   . LEU   A  1  335 ? 73.783  -1.308  44.487 1.00 62.86  ? 348 LEU   A C   1 
ATOM   2625 O  O   . LEU   A  1  335 ? 74.616  -1.951  43.809 1.00 69.48  ? 348 LEU   A O   1 
ATOM   2626 C  CB  . LEU   A  1  335 ? 71.512  -2.452  44.435 1.00 57.33  ? 348 LEU   A CB  1 
ATOM   2627 C  CG  . LEU   A  1  335 ? 69.993  -2.316  44.300 1.00 60.80  ? 348 LEU   A CG  1 
ATOM   2628 C  CD1 . LEU   A  1  335 ? 69.248  -3.592  44.656 1.00 54.64  ? 348 LEU   A CD1 1 
ATOM   2629 C  CD2 . LEU   A  1  335 ? 69.502  -1.140  45.133 1.00 57.04  ? 348 LEU   A CD2 1 
ATOM   2630 N  N   . GLN   B  1  1   ? 0.027   18.967  56.654 1.00 113.16 ? 14  GLN   B N   1 
ATOM   2631 C  CA  . GLN   B  1  1   ? 0.301   18.326  57.970 1.00 119.76 ? 14  GLN   B CA  1 
ATOM   2632 C  C   . GLN   B  1  1   ? -0.501  17.024  58.025 1.00 113.28 ? 14  GLN   B C   1 
ATOM   2633 O  O   . GLN   B  1  1   ? 0.040   15.950  57.750 1.00 96.83  ? 14  GLN   B O   1 
ATOM   2634 C  CB  . GLN   B  1  1   ? -0.038  19.255  59.143 1.00 132.51 ? 14  GLN   B CB  1 
ATOM   2635 C  CG  . GLN   B  1  1   ? 0.627   20.629  59.098 1.00 130.02 ? 14  GLN   B CG  1 
ATOM   2636 C  CD  . GLN   B  1  1   ? 0.091   21.579  60.147 1.00 126.06 ? 14  GLN   B CD  1 
ATOM   2637 O  OE1 . GLN   B  1  1   ? -0.711  21.213  61.016 1.00 117.51 ? 14  GLN   B OE1 1 
ATOM   2638 N  NE2 . GLN   B  1  1   ? 0.541   22.823  60.074 1.00 119.68 ? 14  GLN   B NE2 1 
ATOM   2639 N  N   . GLY   B  1  2   ? -1.814  17.158  58.288 1.00 104.14 ? 15  GLY   B N   1 
ATOM   2640 C  CA  . GLY   B  1  2   ? -2.711  16.028  58.480 1.00 87.00  ? 15  GLY   B CA  1 
ATOM   2641 C  C   . GLY   B  1  2   ? -3.198  15.457  57.148 1.00 74.73  ? 15  GLY   B C   1 
ATOM   2642 O  O   . GLY   B  1  2   ? -3.467  16.187  56.203 1.00 67.56  ? 15  GLY   B O   1 
ATOM   2643 N  N   . VAL   B  1  3   ? -3.343  14.132  57.103 1.00 71.06  ? 16  VAL   B N   1 
ATOM   2644 C  CA  . VAL   B  1  3   ? -3.670  13.404  55.893 1.00 71.37  ? 16  VAL   B CA  1 
ATOM   2645 C  C   . VAL   B  1  3   ? -4.940  12.612  56.170 1.00 58.90  ? 16  VAL   B C   1 
ATOM   2646 O  O   . VAL   B  1  3   ? -5.215  12.236  57.312 1.00 54.63  ? 16  VAL   B O   1 
ATOM   2647 C  CB  . VAL   B  1  3   ? -2.475  12.491  55.532 1.00 81.84  ? 16  VAL   B CB  1 
ATOM   2648 C  CG1 . VAL   B  1  3   ? -2.809  11.369  54.552 1.00 82.47  ? 16  VAL   B CG1 1 
ATOM   2649 C  CG2 . VAL   B  1  3   ? -1.296  13.298  55.002 1.00 83.61  ? 16  VAL   B CG2 1 
ATOM   2650 N  N   . ASP   B  1  4   ? -5.696  12.372  55.099 1.00 59.85  ? 17  ASP   B N   1 
ATOM   2651 C  CA  . ASP   B  1  4   ? -6.861  11.504  55.132 1.00 72.24  ? 17  ASP   B CA  1 
ATOM   2652 C  C   . ASP   B  1  4   ? -6.455  10.130  54.589 1.00 73.02  ? 17  ASP   B C   1 
ATOM   2653 O  O   . ASP   B  1  4   ? -6.237  9.998   53.387 1.00 70.38  ? 17  ASP   B O   1 
ATOM   2654 C  CB  . ASP   B  1  4   ? -7.985  12.160  54.345 1.00 72.95  ? 17  ASP   B CB  1 
ATOM   2655 C  CG  . ASP   B  1  4   ? -9.374  11.647  54.665 1.00 80.57  ? 17  ASP   B CG  1 
ATOM   2656 O  OD1 . ASP   B  1  4   ? -9.732  11.680  55.851 1.00 97.65  ? 17  ASP   B OD1 1 
ATOM   2657 O  OD2 . ASP   B  1  4   ? -10.062 11.196  53.721 1.00 86.82  ? 17  ASP   B OD2 1 
ATOM   2658 N  N   . PRO   B  1  5   ? -6.327  9.068   55.433 1.00 76.52  ? 18  PRO   B N   1 
ATOM   2659 C  CA  . PRO   B  1  5   ? -5.715  7.801   55.015 1.00 65.20  ? 18  PRO   B CA  1 
ATOM   2660 C  C   . PRO   B  1  5   ? -6.572  6.930   54.102 1.00 53.82  ? 18  PRO   B C   1 
ATOM   2661 O  O   . PRO   B  1  5   ? -7.676  6.531   54.473 1.00 51.20  ? 18  PRO   B O   1 
ATOM   2662 C  CB  . PRO   B  1  5   ? -5.433  7.042   56.330 1.00 72.96  ? 18  PRO   B CB  1 
ATOM   2663 C  CG  . PRO   B  1  5   ? -5.663  8.043   57.402 1.00 76.43  ? 18  PRO   B CG  1 
ATOM   2664 C  CD  . PRO   B  1  5   ? -6.709  9.010   56.851 1.00 72.61  ? 18  PRO   B CD  1 
ATOM   2665 N  N   . PRO   B  1  6   ? -6.055  6.525   52.920 1.00 53.67  ? 19  PRO   B N   1 
ATOM   2666 C  CA  . PRO   B  1  6   ? -6.820  5.692   51.996 1.00 51.69  ? 19  PRO   B CA  1 
ATOM   2667 C  C   . PRO   B  1  6   ? -6.937  4.272   52.536 1.00 50.48  ? 19  PRO   B C   1 
ATOM   2668 O  O   . PRO   B  1  6   ? -6.103  3.844   53.322 1.00 56.23  ? 19  PRO   B O   1 
ATOM   2669 C  CB  . PRO   B  1  6   ? -5.970  5.754   50.717 1.00 52.89  ? 19  PRO   B CB  1 
ATOM   2670 C  CG  . PRO   B  1  6   ? -4.543  5.902   51.226 1.00 56.28  ? 19  PRO   B CG  1 
ATOM   2671 C  CD  . PRO   B  1  6   ? -4.686  6.794   52.440 1.00 54.91  ? 19  PRO   B CD  1 
ATOM   2672 N  N   . PRO   B  1  7   ? -7.980  3.511   52.157 1.00 52.90  ? 20  PRO   B N   1 
ATOM   2673 C  CA  . PRO   B  1  7   ? -8.062  2.098   52.523 1.00 59.48  ? 20  PRO   B CA  1 
ATOM   2674 C  C   . PRO   B  1  7   ? -6.898  1.333   51.903 1.00 54.21  ? 20  PRO   B C   1 
ATOM   2675 O  O   . PRO   B  1  7   ? -6.302  1.793   50.932 1.00 46.29  ? 20  PRO   B O   1 
ATOM   2676 C  CB  . PRO   B  1  7   ? -9.444  1.636   52.012 1.00 58.71  ? 20  PRO   B CB  1 
ATOM   2677 C  CG  . PRO   B  1  7   ? -9.817  2.670   50.968 1.00 57.32  ? 20  PRO   B CG  1 
ATOM   2678 C  CD  . PRO   B  1  7   ? -9.144  3.975   51.389 1.00 56.91  ? 20  PRO   B CD  1 
ATOM   2679 N  N   . PRO   B  1  8   ? -6.524  0.160   52.465 1.00 50.88  ? 21  PRO   B N   1 
ATOM   2680 C  CA  . PRO   B  1  8   ? -5.375  -0.579  51.966 1.00 46.40  ? 21  PRO   B CA  1 
ATOM   2681 C  C   . PRO   B  1  8   ? -5.603  -1.055  50.540 1.00 43.11  ? 21  PRO   B C   1 
ATOM   2682 O  O   . PRO   B  1  8   ? -6.721  -1.367  50.150 1.00 45.64  ? 21  PRO   B O   1 
ATOM   2683 C  CB  . PRO   B  1  8   ? -5.226  -1.734  52.937 1.00 49.17  ? 21  PRO   B CB  1 
ATOM   2684 C  CG  . PRO   B  1  8   ? -6.616  -1.916  53.482 1.00 49.54  ? 21  PRO   B CG  1 
ATOM   2685 C  CD  . PRO   B  1  8   ? -7.169  -0.507  53.607 1.00 49.10  ? 21  PRO   B CD  1 
ATOM   2686 N  N   . PRO   B  1  9   ? -4.537  -1.122  49.723 1.00 39.07  ? 22  PRO   B N   1 
ATOM   2687 C  CA  . PRO   B  1  9   ? -4.629  -1.740  48.405 1.00 38.53  ? 22  PRO   B CA  1 
ATOM   2688 C  C   . PRO   B  1  9   ? -5.133  -3.156  48.587 1.00 37.91  ? 22  PRO   B C   1 
ATOM   2689 O  O   . PRO   B  1  9   ? -4.861  -3.775  49.618 1.00 39.24  ? 22  PRO   B O   1 
ATOM   2690 C  CB  . PRO   B  1  9   ? -3.191  -1.718  47.895 1.00 38.74  ? 22  PRO   B CB  1 
ATOM   2691 C  CG  . PRO   B  1  9   ? -2.558  -0.578  48.648 1.00 39.78  ? 22  PRO   B CG  1 
ATOM   2692 C  CD  . PRO   B  1  9   ? -3.210  -0.577  50.025 1.00 38.29  ? 22  PRO   B CD  1 
ATOM   2693 N  N   . GLY   B  1  10  ? -5.818  -3.662  47.555 1.00 39.22  ? 23  GLY   B N   1 
ATOM   2694 C  CA  . GLY   B  1  10  ? -6.153  -5.080  47.456 1.00 41.45  ? 23  GLY   B CA  1 
ATOM   2695 C  C   . GLY   B  1  10  ? -4.980  -5.880  46.879 1.00 44.34  ? 23  GLY   B C   1 
ATOM   2696 O  O   . GLY   B  1  10  ? -3.883  -5.344  46.691 1.00 40.63  ? 23  GLY   B O   1 
ATOM   2697 N  N   . PRO   B  1  11  ? -5.175  -7.185  46.587 1.00 44.18  ? 24  PRO   B N   1 
ATOM   2698 C  CA  . PRO   B  1  11  ? -4.119  -8.006  45.994 1.00 46.83  ? 24  PRO   B CA  1 
ATOM   2699 C  C   . PRO   B  1  11  ? -3.641  -7.412  44.671 1.00 48.07  ? 24  PRO   B C   1 
ATOM   2700 O  O   . PRO   B  1  11  ? -4.372  -6.675  44.026 1.00 48.75  ? 24  PRO   B O   1 
ATOM   2701 C  CB  . PRO   B  1  11  ? -4.769  -9.387  45.803 1.00 45.09  ? 24  PRO   B CB  1 
ATOM   2702 C  CG  . PRO   B  1  11  ? -5.962  -9.376  46.757 1.00 42.41  ? 24  PRO   B CG  1 
ATOM   2703 C  CD  . PRO   B  1  11  ? -6.425  -7.928  46.808 1.00 41.83  ? 24  PRO   B CD  1 
ATOM   2704 N  N   . PRO   B  1  12  ? -2.392  -7.682  44.230 1.00 54.52  ? 25  PRO   B N   1 
ATOM   2705 C  CA  . PRO   B  1  12  ? -1.936  -7.162  42.948 1.00 55.13  ? 25  PRO   B CA  1 
ATOM   2706 C  C   . PRO   B  1  12  ? -2.737  -7.817  41.819 1.00 55.41  ? 25  PRO   B C   1 
ATOM   2707 O  O   . PRO   B  1  12  ? -3.257  -8.935  41.951 1.00 43.42  ? 25  PRO   B O   1 
ATOM   2708 C  CB  . PRO   B  1  12  ? -0.433  -7.488  42.936 1.00 54.90  ? 25  PRO   B CB  1 
ATOM   2709 C  CG  . PRO   B  1  12  ? -0.298  -8.658  43.865 1.00 52.06  ? 25  PRO   B CG  1 
ATOM   2710 C  CD  . PRO   B  1  12  ? -1.379  -8.499  44.912 1.00 54.60  ? 25  PRO   B CD  1 
ATOM   2711 N  N   . SER   B  1  13  ? -2.874  -7.069  40.724 1.00 57.69  ? 26  SER   B N   1 
ATOM   2712 C  CA  A SER   B  1  13  ? -3.570  -7.544  39.535 0.50 59.89  ? 26  SER   B CA  1 
ATOM   2713 C  CA  B SER   B  1  13  ? -3.579  -7.551  39.546 0.50 59.03  ? 26  SER   B CA  1 
ATOM   2714 C  C   . SER   B  1  13  ? -2.932  -8.840  39.038 1.00 59.42  ? 26  SER   B C   1 
ATOM   2715 O  O   . SER   B  1  13  ? -3.625  -9.806  38.733 1.00 51.50  ? 26  SER   B O   1 
ATOM   2716 C  CB  A SER   B  1  13  ? -3.567  -6.506  38.433 0.50 59.34  ? 26  SER   B CB  1 
ATOM   2717 C  CB  B SER   B  1  13  ? -3.618  -6.494  38.474 0.50 57.63  ? 26  SER   B CB  1 
ATOM   2718 O  OG  A SER   B  1  13  ? -4.068  -5.250  38.871 0.50 60.38  ? 26  SER   B OG  1 
ATOM   2719 O  OG  B SER   B  1  13  ? -4.474  -6.887  37.414 0.50 56.65  ? 26  SER   B OG  1 
ATOM   2720 N  N   . PHE   B  1  14  ? -1.591  -8.849  38.965 1.00 57.95  ? 27  PHE   B N   1 
ATOM   2721 C  CA  . PHE   B  1  14  ? -0.831  -10.028 38.569 1.00 55.73  ? 27  PHE   B CA  1 
ATOM   2722 C  C   . PHE   B  1  14  ? -0.152  -10.642 39.793 1.00 44.85  ? 27  PHE   B C   1 
ATOM   2723 O  O   . PHE   B  1  14  ? 0.571   -9.949  40.490 1.00 43.65  ? 27  PHE   B O   1 
ATOM   2724 C  CB  . PHE   B  1  14  ? 0.200   -9.599  37.520 1.00 62.85  ? 27  PHE   B CB  1 
ATOM   2725 C  CG  . PHE   B  1  14  ? 1.141   -10.720 37.095 1.00 61.63  ? 27  PHE   B CG  1 
ATOM   2726 C  CD1 . PHE   B  1  14  ? 0.665   -11.774 36.318 1.00 61.47  ? 27  PHE   B CD1 1 
ATOM   2727 C  CD2 . PHE   B  1  14  ? 2.489   -10.716 37.455 1.00 58.46  ? 27  PHE   B CD2 1 
ATOM   2728 C  CE1 . PHE   B  1  14  ? 1.505   -12.804 35.925 1.00 59.66  ? 27  PHE   B CE1 1 
ATOM   2729 C  CE2 . PHE   B  1  14  ? 3.331   -11.751 37.061 1.00 54.42  ? 27  PHE   B CE2 1 
ATOM   2730 C  CZ  . PHE   B  1  14  ? 2.834   -12.790 36.299 1.00 59.63  ? 27  PHE   B CZ  1 
ATOM   2731 N  N   . THR   B  1  15  ? -0.373  -11.941 40.033 1.00 46.39  ? 28  THR   B N   1 
ATOM   2732 C  CA  . THR   B  1  15  ? 0.112   -12.606 41.237 1.00 49.22  ? 28  THR   B CA  1 
ATOM   2733 C  C   . THR   B  1  15  ? 1.070   -13.748 40.891 1.00 47.12  ? 28  THR   B C   1 
ATOM   2734 O  O   . THR   B  1  15  ? 1.334   -14.610 41.737 1.00 44.22  ? 28  THR   B O   1 
ATOM   2735 C  CB  . THR   B  1  15  ? -1.054  -13.147 42.067 1.00 51.36  ? 28  THR   B CB  1 
ATOM   2736 O  OG1 . THR   B  1  15  ? -1.619  -14.220 41.323 1.00 44.65  ? 28  THR   B OG1 1 
ATOM   2737 C  CG2 . THR   B  1  15  ? -2.127  -12.113 42.358 1.00 52.78  ? 28  THR   B CG2 1 
ATOM   2738 N  N   . GLY   B  1  16  ? 1.593   -13.776 39.658 1.00 40.43  ? 29  GLY   B N   1 
ATOM   2739 C  CA  . GLY   B  1  16  ? 2.570   -14.796 39.306 1.00 43.71  ? 29  GLY   B CA  1 
ATOM   2740 C  C   . GLY   B  1  16  ? 4.002   -14.374 39.668 1.00 40.32  ? 29  GLY   B C   1 
ATOM   2741 O  O   . GLY   B  1  16  ? 4.231   -13.325 40.253 1.00 36.82  ? 29  GLY   B O   1 
ATOM   2742 N  N   . THR   B  1  17  ? 4.976   -15.196 39.292 1.00 41.21  ? 30  THR   B N   1 
ATOM   2743 C  CA  . THR   B  1  17  ? 6.369   -14.860 39.505 1.00 40.71  ? 30  THR   B CA  1 
ATOM   2744 C  C   . THR   B  1  17  ? 6.769   -13.797 38.498 1.00 38.72  ? 30  THR   B C   1 
ATOM   2745 O  O   . THR   B  1  17  ? 6.150   -13.648 37.448 1.00 42.39  ? 30  THR   B O   1 
ATOM   2746 C  CB  . THR   B  1  17  ? 7.274   -16.087 39.395 1.00 43.55  ? 30  THR   B CB  1 
ATOM   2747 O  OG1 . THR   B  1  17  ? 8.504   -15.562 39.886 1.00 39.03  ? 30  THR   B OG1 1 
ATOM   2748 C  CG2 . THR   B  1  17  ? 7.376   -16.619 37.973 1.00 41.76  ? 30  THR   B CG2 1 
ATOM   2749 N  N   . LYS   B  1  18  ? 7.815   -13.057 38.858 1.00 39.93  ? 31  LYS   B N   1 
ATOM   2750 C  CA  . LYS   B  1  18  ? 8.409   -12.080 37.970 1.00 42.30  ? 31  LYS   B CA  1 
ATOM   2751 C  C   . LYS   B  1  18  ? 9.758   -11.689 38.543 1.00 38.97  ? 31  LYS   B C   1 
ATOM   2752 O  O   . LYS   B  1  18  ? 10.022  -11.932 39.724 1.00 33.34  ? 31  LYS   B O   1 
ATOM   2753 C  CB  . LYS   B  1  18  ? 7.516   -10.846 37.791 1.00 47.59  ? 31  LYS   B CB  1 
ATOM   2754 C  CG  . LYS   B  1  18  ? 7.283   -9.978  39.006 1.00 53.15  ? 31  LYS   B CG  1 
ATOM   2755 C  CD  . LYS   B  1  18  ? 6.619   -8.643  38.669 1.00 59.00  ? 31  LYS   B CD  1 
ATOM   2756 C  CE  . LYS   B  1  18  ? 6.870   -7.613  39.726 1.00 70.83  ? 31  LYS   B CE  1 
ATOM   2757 N  NZ  . LYS   B  1  18  ? 5.946   -6.480  39.648 1.00 78.03  ? 31  LYS   B NZ  1 
ATOM   2758 N  N   . LEU   B  1  19  ? 10.581  -11.076 37.687 1.00 36.90  ? 32  LEU   B N   1 
ATOM   2759 C  CA  . LEU   B  1  19  ? 11.850  -10.523 38.125 1.00 41.85  ? 32  LEU   B CA  1 
ATOM   2760 C  C   . LEU   B  1  19  ? 11.575  -9.291  38.974 1.00 41.65  ? 32  LEU   B C   1 
ATOM   2761 O  O   . LEU   B  1  19  ? 10.913  -8.376  38.494 1.00 38.33  ? 32  LEU   B O   1 
ATOM   2762 C  CB  . LEU   B  1  19  ? 12.690  -10.157 36.906 1.00 41.66  ? 32  LEU   B CB  1 
ATOM   2763 C  CG  . LEU   B  1  19  ? 14.008  -9.443  37.203 1.00 44.06  ? 32  LEU   B CG  1 
ATOM   2764 C  CD1 . LEU   B  1  19  ? 14.980  -10.352 37.942 1.00 40.39  ? 32  LEU   B CD1 1 
ATOM   2765 C  CD2 . LEU   B  1  19  ? 14.624  -8.908  35.910 1.00 45.32  ? 32  LEU   B CD2 1 
ATOM   2766 N  N   . VAL   B  1  20  ? 12.076  -9.281  40.222 1.00 39.35  ? 33  VAL   B N   1 
ATOM   2767 C  CA  . VAL   B  1  20  ? 11.849  -8.137  41.087 1.00 35.51  ? 33  VAL   B CA  1 
ATOM   2768 C  C   . VAL   B  1  20  ? 13.144  -7.356  41.246 1.00 36.35  ? 33  VAL   B C   1 
ATOM   2769 O  O   . VAL   B  1  20  ? 13.106  -6.158  41.509 1.00 41.32  ? 33  VAL   B O   1 
ATOM   2770 C  CB  . VAL   B  1  20  ? 11.233  -8.498  42.446 1.00 35.42  ? 33  VAL   B CB  1 
ATOM   2771 C  CG1 . VAL   B  1  20  ? 9.864   -9.131  42.276 1.00 38.68  ? 33  VAL   B CG1 1 
ATOM   2772 C  CG2 . VAL   B  1  20  ? 12.130  -9.400  43.265 1.00 37.88  ? 33  VAL   B CG2 1 
ATOM   2773 N  N   . ASN   B  1  21  ? 14.281  -8.033  41.078 1.00 33.52  ? 34  ASN   B N   1 
ATOM   2774 C  CA  . ASN   B  1  21  ? 15.567  -7.360  41.087 1.00 37.22  ? 34  ASN   B CA  1 
ATOM   2775 C  C   . ASN   B  1  21  ? 15.877  -6.871  39.671 1.00 37.06  ? 34  ASN   B C   1 
ATOM   2776 O  O   . ASN   B  1  21  ? 16.657  -7.487  38.958 1.00 41.11  ? 34  ASN   B O   1 
ATOM   2777 C  CB  . ASN   B  1  21  ? 16.642  -8.291  41.626 1.00 36.46  ? 34  ASN   B CB  1 
ATOM   2778 C  CG  . ASN   B  1  21  ? 17.973  -7.601  41.792 1.00 35.45  ? 34  ASN   B CG  1 
ATOM   2779 O  OD1 . ASN   B  1  21  ? 18.085  -6.396  41.562 1.00 37.41  ? 34  ASN   B OD1 1 
ATOM   2780 N  ND2 . ASN   B  1  21  ? 18.974  -8.345  42.242 1.00 33.30  ? 34  ASN   B ND2 1 
ATOM   2781 N  N   . ASP   B  1  22  ? 15.261  -5.760  39.274 1.00 39.80  ? 35  ASP   B N   1 
ATOM   2782 C  CA  . ASP   B  1  22  ? 15.193  -5.367  37.871 1.00 45.00  ? 35  ASP   B CA  1 
ATOM   2783 C  C   . ASP   B  1  22  ? 15.796  -3.978  37.720 1.00 40.39  ? 35  ASP   B C   1 
ATOM   2784 O  O   . ASP   B  1  22  ? 16.200  -3.369  38.708 1.00 43.53  ? 35  ASP   B O   1 
ATOM   2785 C  CB  . ASP   B  1  22  ? 13.776  -5.484  37.313 1.00 48.65  ? 35  ASP   B CB  1 
ATOM   2786 C  CG  . ASP   B  1  22  ? 12.693  -4.587  37.910 1.00 47.70  ? 35  ASP   B CG  1 
ATOM   2787 O  OD1 . ASP   B  1  22  ? 13.004  -3.806  38.823 1.00 47.59  ? 35  ASP   B OD1 1 
ATOM   2788 O  OD2 . ASP   B  1  22  ? 11.531  -4.664  37.446 1.00 54.74  ? 35  ASP   B OD2 1 
ATOM   2789 N  N   . ALA   B  1  23  ? 15.831  -3.481  36.483 1.00 43.35  ? 36  ALA   B N   1 
ATOM   2790 C  CA  . ALA   B  1  23  ? 16.565  -2.264  36.163 1.00 45.68  ? 36  ALA   B CA  1 
ATOM   2791 C  C   . ALA   B  1  23  ? 15.957  -1.062  36.883 1.00 42.85  ? 36  ALA   B C   1 
ATOM   2792 O  O   . ALA   B  1  23  ? 16.660  -0.127  37.260 1.00 39.35  ? 36  ALA   B O   1 
ATOM   2793 C  CB  . ALA   B  1  23  ? 16.579  -2.061  34.656 1.00 49.76  ? 36  ALA   B CB  1 
ATOM   2794 N  N   . ASP   B  1  24  ? 14.635  -1.091  37.077 1.00 40.95  ? 37  ASP   B N   1 
ATOM   2795 C  CA  . ASP   B  1  24  ? 13.965  0.015   37.724 1.00 42.27  ? 37  ASP   B CA  1 
ATOM   2796 C  C   . ASP   B  1  24  ? 14.129  -0.005  39.245 1.00 39.55  ? 37  ASP   B C   1 
ATOM   2797 O  O   . ASP   B  1  24  ? 13.822  0.989   39.893 1.00 36.48  ? 37  ASP   B O   1 
ATOM   2798 C  CB  . ASP   B  1  24  ? 12.495  0.033   37.347 1.00 51.39  ? 37  ASP   B CB  1 
ATOM   2799 C  CG  . ASP   B  1  24  ? 11.865  1.414   37.378 1.00 51.82  ? 37  ASP   B CG  1 
ATOM   2800 O  OD1 . ASP   B  1  24  ? 12.503  2.346   36.811 1.00 50.61  ? 37  ASP   B OD1 1 
ATOM   2801 O  OD2 . ASP   B  1  24  ? 10.751  1.523   37.955 1.00 52.69  ? 37  ASP   B OD2 1 
ATOM   2802 N  N   . HIS   B  1  25  ? 14.591  -1.131  39.815 1.00 37.87  ? 38  HIS   B N   1 
ATOM   2803 C  CA  . HIS   B  1  25  ? 14.693  -1.293  41.262 1.00 36.73  ? 38  HIS   B CA  1 
ATOM   2804 C  C   . HIS   B  1  25  ? 16.111  -1.699  41.668 1.00 35.89  ? 38  HIS   B C   1 
ATOM   2805 O  O   . HIS   B  1  25  ? 16.330  -2.760  42.252 1.00 34.06  ? 38  HIS   B O   1 
ATOM   2806 C  CB  . HIS   B  1  25  ? 13.618  -2.262  41.752 1.00 33.96  ? 38  HIS   B CB  1 
ATOM   2807 C  CG  . HIS   B  1  25  ? 12.240  -1.751  41.523 1.00 37.90  ? 38  HIS   B CG  1 
ATOM   2808 N  ND1 . HIS   B  1  25  ? 11.432  -2.157  40.479 1.00 43.95  ? 38  HIS   B ND1 1 
ATOM   2809 C  CD2 . HIS   B  1  25  ? 11.528  -0.841  42.206 1.00 38.60  ? 38  HIS   B CD2 1 
ATOM   2810 C  CE1 . HIS   B  1  25  ? 10.280  -1.495  40.538 1.00 41.64  ? 38  HIS   B CE1 1 
ATOM   2811 N  NE2 . HIS   B  1  25  ? 10.304  -0.703  41.597 1.00 36.14  ? 38  HIS   B NE2 1 
ATOM   2812 N  N   . PRO   B  1  26  ? 17.132  -0.871  41.362 1.00 34.30  ? 39  PRO   B N   1 
ATOM   2813 C  CA  . PRO   B  1  26  ? 18.513  -1.226  41.685 1.00 34.29  ? 39  PRO   B CA  1 
ATOM   2814 C  C   . PRO   B  1  26  ? 18.797  -1.090  43.170 1.00 31.53  ? 39  PRO   B C   1 
ATOM   2815 O  O   . PRO   B  1  26  ? 18.301  -0.173  43.808 1.00 33.49  ? 39  PRO   B O   1 
ATOM   2816 C  CB  . PRO   B  1  26  ? 19.325  -0.218  40.852 1.00 34.19  ? 39  PRO   B CB  1 
ATOM   2817 C  CG  . PRO   B  1  26  ? 18.425  1.012   40.795 1.00 33.43  ? 39  PRO   B CG  1 
ATOM   2818 C  CD  . PRO   B  1  26  ? 17.026  0.417   40.666 1.00 32.99  ? 39  PRO   B CD  1 
ATOM   2819 N  N   . TRP   B  1  27  ? 19.626  -1.988  43.710 1.00 29.60  ? 40  TRP   B N   1 
ATOM   2820 C  CA  . TRP   B  1  27  ? 20.150  -1.773  45.044 1.00 27.77  ? 40  TRP   B CA  1 
ATOM   2821 C  C   . TRP   B  1  27  ? 20.984  -0.490  45.030 1.00 29.15  ? 40  TRP   B C   1 
ATOM   2822 O  O   . TRP   B  1  27  ? 21.698  -0.217  44.065 1.00 33.02  ? 40  TRP   B O   1 
ATOM   2823 C  CB  . TRP   B  1  27  ? 20.963  -2.989  45.486 1.00 26.81  ? 40  TRP   B CB  1 
ATOM   2824 C  CG  . TRP   B  1  27  ? 21.527  -2.884  46.874 1.00 23.63  ? 40  TRP   B CG  1 
ATOM   2825 C  CD1 . TRP   B  1  27  ? 20.958  -3.300  48.035 1.00 24.14  ? 40  TRP   B CD1 1 
ATOM   2826 C  CD2 . TRP   B  1  27  ? 22.787  -2.292  47.232 1.00 25.29  ? 40  TRP   B CD2 1 
ATOM   2827 N  NE1 . TRP   B  1  27  ? 21.776  -3.017  49.096 1.00 27.58  ? 40  TRP   B NE1 1 
ATOM   2828 C  CE2 . TRP   B  1  27  ? 22.910  -2.398  48.635 1.00 23.39  ? 40  TRP   B CE2 1 
ATOM   2829 C  CE3 . TRP   B  1  27  ? 23.817  -1.676  46.508 1.00 28.29  ? 40  TRP   B CE3 1 
ATOM   2830 C  CZ2 . TRP   B  1  27  ? 24.010  -1.894  49.313 1.00 22.61  ? 40  TRP   B CZ2 1 
ATOM   2831 C  CZ3 . TRP   B  1  27  ? 24.907  -1.173  47.191 1.00 25.77  ? 40  TRP   B CZ3 1 
ATOM   2832 C  CH2 . TRP   B  1  27  ? 24.978  -1.251  48.578 1.00 25.20  ? 40  TRP   B CH2 1 
ATOM   2833 N  N   . GLN   B  1  28  ? 20.856  0.315   46.081 1.00 28.22  ? 41  GLN   B N   1 
ATOM   2834 C  CA  . GLN   B  1  28  ? 21.704  1.477   46.275 1.00 28.84  ? 41  GLN   B CA  1 
ATOM   2835 C  C   . GLN   B  1  28  ? 22.117  1.538   47.734 1.00 28.50  ? 41  GLN   B C   1 
ATOM   2836 O  O   . GLN   B  1  28  ? 21.391  1.070   48.606 1.00 27.51  ? 41  GLN   B O   1 
ATOM   2837 C  CB  . GLN   B  1  28  ? 21.010  2.769   45.858 1.00 29.79  ? 41  GLN   B CB  1 
ATOM   2838 C  CG  . GLN   B  1  28  ? 20.733  2.850   44.361 1.00 32.65  ? 41  GLN   B CG  1 
ATOM   2839 C  CD  . GLN   B  1  28  ? 19.908  4.063   43.986 1.00 35.73  ? 41  GLN   B CD  1 
ATOM   2840 O  OE1 . GLN   B  1  28  ? 19.516  4.868   44.842 1.00 37.99  ? 41  GLN   B OE1 1 
ATOM   2841 N  NE2 . GLN   B  1  28  ? 19.618  4.176   42.701 1.00 38.45  ? 41  GLN   B NE2 1 
ATOM   2842 N  N   . PRO   B  1  29  ? 23.307  2.098   48.039 1.00 29.68  ? 42  PRO   B N   1 
ATOM   2843 C  CA  . PRO   B  1  29  ? 23.755  2.242   49.420 1.00 30.97  ? 42  PRO   B CA  1 
ATOM   2844 C  C   . PRO   B  1  29  ? 22.934  3.299   50.156 1.00 34.04  ? 42  PRO   B C   1 
ATOM   2845 O  O   . PRO   B  1  29  ? 22.310  4.163   49.550 1.00 41.91  ? 42  PRO   B O   1 
ATOM   2846 C  CB  . PRO   B  1  29  ? 25.243  2.654   49.309 1.00 32.29  ? 42  PRO   B CB  1 
ATOM   2847 C  CG  . PRO   B  1  29  ? 25.400  3.202   47.914 1.00 30.48  ? 42  PRO   B CG  1 
ATOM   2848 C  CD  . PRO   B  1  29  ? 24.267  2.634   47.064 1.00 31.24  ? 42  PRO   B CD  1 
ATOM   2849 N  N   . LEU   B  1  30  ? 22.959  3.222   51.478 1.00 36.48  ? 43  LEU   B N   1 
ATOM   2850 C  CA  . LEU   B  1  30  ? 22.320  4.199   52.332 1.00 37.88  ? 43  LEU   B CA  1 
ATOM   2851 C  C   . LEU   B  1  30  ? 22.941  5.575   52.114 1.00 41.05  ? 43  LEU   B C   1 
ATOM   2852 O  O   . LEU   B  1  30  ? 24.153  5.694   51.981 1.00 37.90  ? 43  LEU   B O   1 
ATOM   2853 C  CB  . LEU   B  1  30  ? 22.524  3.737   53.772 1.00 38.70  ? 43  LEU   B CB  1 
ATOM   2854 C  CG  . LEU   B  1  30  ? 21.837  2.420   54.152 1.00 42.96  ? 43  LEU   B CG  1 
ATOM   2855 C  CD1 . LEU   B  1  30  ? 21.900  2.242   55.654 1.00 40.36  ? 43  LEU   B CD1 1 
ATOM   2856 C  CD2 . LEU   B  1  30  ? 20.378  2.303   53.682 1.00 42.61  ? 43  LEU   B CD2 1 
ATOM   2857 N  N   . ARG   B  1  31  ? 22.087  6.601   52.100 1.00 45.81  ? 44  ARG   B N   1 
ATOM   2858 C  CA  . ARG   B  1  31  ? 22.496  7.993   52.211 1.00 45.02  ? 44  ARG   B CA  1 
ATOM   2859 C  C   . ARG   B  1  31  ? 22.273  8.469   53.642 1.00 46.38  ? 44  ARG   B C   1 
ATOM   2860 O  O   . ARG   B  1  31  ? 21.620  7.793   54.432 1.00 45.83  ? 44  ARG   B O   1 
ATOM   2861 C  CB  . ARG   B  1  31  ? 21.637  8.884   51.311 1.00 46.60  ? 44  ARG   B CB  1 
ATOM   2862 C  CG  . ARG   B  1  31  ? 21.586  8.504   49.838 1.00 48.68  ? 44  ARG   B CG  1 
ATOM   2863 C  CD  . ARG   B  1  31  ? 20.368  9.103   49.150 1.00 60.89  ? 44  ARG   B CD  1 
ATOM   2864 N  NE  . ARG   B  1  31  ? 19.136  8.762   49.886 1.00 80.47  ? 44  ARG   B NE  1 
ATOM   2865 C  CZ  . ARG   B  1  31  ? 17.874  8.855   49.464 1.00 80.10  ? 44  ARG   B CZ  1 
ATOM   2866 N  NH1 . ARG   B  1  31  ? 17.599  9.078   48.188 1.00 88.45  ? 44  ARG   B NH1 1 
ATOM   2867 N  NH2 . ARG   B  1  31  ? 16.890  8.649   50.320 1.00 71.47  ? 44  ARG   B NH2 1 
ATOM   2868 N  N   . GLU   B  1  32  ? 22.802  9.652   53.949 1.00 54.07  ? 45  GLU   B N   1 
ATOM   2869 C  CA  . GLU   B  1  32  ? 22.563  10.303  55.229 1.00 65.14  ? 45  GLU   B CA  1 
ATOM   2870 C  C   . GLU   B  1  32  ? 21.054  10.418  55.456 1.00 56.86  ? 45  GLU   B C   1 
ATOM   2871 O  O   . GLU   B  1  32  ? 20.326  10.858  54.565 1.00 48.96  ? 45  GLU   B O   1 
ATOM   2872 C  CB  . GLU   B  1  32  ? 23.259  11.670  55.223 1.00 76.46  ? 45  GLU   B CB  1 
ATOM   2873 C  CG  . GLU   B  1  32  ? 23.172  12.433  56.543 1.00 91.07  ? 45  GLU   B CG  1 
ATOM   2874 C  CD  . GLU   B  1  32  ? 23.942  11.811  57.697 1.00 108.73 ? 45  GLU   B CD  1 
ATOM   2875 O  OE1 . GLU   B  1  32  ? 24.768  10.888  57.497 1.00 110.66 ? 45  GLU   B OE1 1 
ATOM   2876 O  OE2 . GLU   B  1  32  ? 23.724  12.291  58.827 1.00 122.86 ? 45  GLU   B OE2 1 
ATOM   2877 N  N   . GLY   B  1  33  ? 20.589  9.990   56.637 1.00 50.25  ? 46  GLY   B N   1 
ATOM   2878 C  CA  . GLY   B  1  33  ? 19.183  10.116  56.998 1.00 50.67  ? 46  GLY   B CA  1 
ATOM   2879 C  C   . GLY   B  1  33  ? 18.345  8.869   56.690 1.00 49.81  ? 46  GLY   B C   1 
ATOM   2880 O  O   . GLY   B  1  33  ? 17.205  8.785   57.144 1.00 52.63  ? 46  GLY   B O   1 
ATOM   2881 N  N   . ASP   B  1  34  ? 18.873  7.933   55.883 1.00 47.04  ? 47  ASP   B N   1 
ATOM   2882 C  CA  . ASP   B  1  34  ? 18.107  6.762   55.485 1.00 42.68  ? 47  ASP   B CA  1 
ATOM   2883 C  C   . ASP   B  1  34  ? 17.907  5.873   56.705 1.00 35.25  ? 47  ASP   B C   1 
ATOM   2884 O  O   . ASP   B  1  34  ? 18.790  5.743   57.527 1.00 35.24  ? 47  ASP   B O   1 
ATOM   2885 C  CB  . ASP   B  1  34  ? 18.746  6.036   54.312 1.00 46.07  ? 47  ASP   B CB  1 
ATOM   2886 C  CG  . ASP   B  1  34  ? 18.603  6.705   52.945 1.00 48.68  ? 47  ASP   B CG  1 
ATOM   2887 O  OD1 . ASP   B  1  34  ? 17.870  7.707   52.839 1.00 53.28  ? 47  ASP   B OD1 1 
ATOM   2888 O  OD2 . ASP   B  1  34  ? 19.235  6.217   51.977 1.00 47.71  ? 47  ASP   B OD2 1 
ATOM   2889 N  N   . ILE   B  1  35  ? 16.720  5.301   56.838 1.00 33.87  ? 48  ILE   B N   1 
ATOM   2890 C  CA  . ILE   B  1  35  ? 16.374  4.517   58.012 1.00 30.57  ? 48  ILE   B CA  1 
ATOM   2891 C  C   . ILE   B  1  35  ? 16.257  3.049   57.607 1.00 26.93  ? 48  ILE   B C   1 
ATOM   2892 O  O   . ILE   B  1  35  ? 15.626  2.723   56.613 1.00 24.56  ? 48  ILE   B O   1 
ATOM   2893 C  CB  . ILE   B  1  35  ? 15.050  5.012   58.620 1.00 33.68  ? 48  ILE   B CB  1 
ATOM   2894 C  CG1 . ILE   B  1  35  ? 15.096  6.485   59.079 1.00 36.12  ? 48  ILE   B CG1 1 
ATOM   2895 C  CG2 . ILE   B  1  35  ? 14.629  4.074   59.749 1.00 35.94  ? 48  ILE   B CG2 1 
ATOM   2896 C  CD1 . ILE   B  1  35  ? 16.125  6.783   60.166 1.00 37.36  ? 48  ILE   B CD1 1 
ATOM   2897 N  N   . ARG   B  1  36  ? 16.827  2.170   58.425 1.00 28.98  ? 49  ARG   B N   1 
ATOM   2898 C  CA  . ARG   B  1  36  ? 16.662  0.738   58.291 1.00 30.06  ? 49  ARG   B CA  1 
ATOM   2899 C  C   . ARG   B  1  36  ? 16.443  0.194   59.694 1.00 33.64  ? 49  ARG   B C   1 
ATOM   2900 O  O   . ARG   B  1  36  ? 16.767  0.875   60.663 1.00 34.03  ? 49  ARG   B O   1 
ATOM   2901 C  CB  . ARG   B  1  36  ? 17.886  0.114   57.603 1.00 26.49  ? 49  ARG   B CB  1 
ATOM   2902 C  CG  . ARG   B  1  36  ? 18.123  0.602   56.181 1.00 25.44  ? 49  ARG   B CG  1 
ATOM   2903 C  CD  . ARG   B  1  36  ? 17.040  0.131   55.230 1.00 27.99  ? 49  ARG   B CD  1 
ATOM   2904 N  NE  . ARG   B  1  36  ? 17.318  0.531   53.846 1.00 28.14  ? 49  ARG   B NE  1 
ATOM   2905 C  CZ  . ARG   B  1  36  ? 17.028  1.700   53.303 1.00 33.66  ? 49  ARG   B CZ  1 
ATOM   2906 N  NH1 . ARG   B  1  36  ? 16.405  2.641   54.006 1.00 32.39  ? 49  ARG   B NH1 1 
ATOM   2907 N  NH2 . ARG   B  1  36  ? 17.338  1.925   52.031 1.00 34.02  ? 49  ARG   B NH2 1 
ATOM   2908 N  N   . GLY   B  1  37  ? 15.889  -1.028  59.783 1.00 34.11  ? 50  GLY   B N   1 
ATOM   2909 C  CA  . GLY   B  1  37  ? 15.427  -1.529  61.057 1.00 30.59  ? 50  GLY   B CA  1 
ATOM   2910 C  C   . GLY   B  1  37  ? 15.490  -3.046  61.139 1.00 33.57  ? 50  GLY   B C   1 
ATOM   2911 O  O   . GLY   B  1  37  ? 16.313  -3.694  60.492 1.00 30.73  ? 50  GLY   B O   1 
ATOM   2912 N  N   . PRO   B  1  38  ? 14.616  -3.659  61.964 1.00 29.99  ? 51  PRO   B N   1 
ATOM   2913 C  CA  . PRO   B  1  38  ? 14.719  -5.080  62.272 1.00 27.47  ? 51  PRO   B CA  1 
ATOM   2914 C  C   . PRO   B  1  38  ? 14.156  -6.022  61.223 1.00 29.77  ? 51  PRO   B C   1 
ATOM   2915 O  O   . PRO   B  1  38  ? 14.318  -7.229  61.353 1.00 33.66  ? 51  PRO   B O   1 
ATOM   2916 C  CB  . PRO   B  1  38  ? 13.906  -5.157  63.538 1.00 28.35  ? 51  PRO   B CB  1 
ATOM   2917 C  CG  . PRO   B  1  38  ? 12.788  -4.184  63.313 1.00 30.94  ? 51  PRO   B CG  1 
ATOM   2918 C  CD  . PRO   B  1  38  ? 13.468  -3.019  62.618 1.00 30.22  ? 51  PRO   B CD  1 
ATOM   2919 N  N   . CYS   B  1  39  ? 13.456  -5.475  60.218 1.00 28.37  ? 52  CYS   B N   1 
ATOM   2920 C  CA  . CYS   B  1  39  ? 12.820  -6.299  59.207 1.00 27.32  ? 52  CYS   B CA  1 
ATOM   2921 C  C   . CYS   B  1  39  ? 13.669  -6.352  57.941 1.00 29.67  ? 52  CYS   B C   1 
ATOM   2922 O  O   . CYS   B  1  39  ? 13.828  -5.350  57.241 1.00 28.15  ? 52  CYS   B O   1 
ATOM   2923 C  CB  . CYS   B  1  39  ? 11.440  -5.794  58.831 1.00 27.19  ? 52  CYS   B CB  1 
ATOM   2924 S  SG  . CYS   B  1  39  ? 10.657  -6.893  57.635 1.00 31.96  ? 52  CYS   B SG  1 
ATOM   2925 N  N   . PRO   B  1  40  ? 14.205  -7.541  57.590 1.00 30.13  ? 53  PRO   B N   1 
ATOM   2926 C  CA  . PRO   B  1  40  ? 15.011  -7.689  56.376 1.00 28.78  ? 53  PRO   B CA  1 
ATOM   2927 C  C   . PRO   B  1  40  ? 14.188  -7.540  55.102 1.00 28.01  ? 53  PRO   B C   1 
ATOM   2928 O  O   . PRO   B  1  40  ? 14.694  -7.078  54.092 1.00 27.02  ? 53  PRO   B O   1 
ATOM   2929 C  CB  . PRO   B  1  40  ? 15.633  -9.085  56.508 1.00 28.59  ? 53  PRO   B CB  1 
ATOM   2930 C  CG  . PRO   B  1  40  ? 14.747  -9.816  57.485 1.00 29.15  ? 53  PRO   B CG  1 
ATOM   2931 C  CD  . PRO   B  1  40  ? 14.075  -8.787  58.352 1.00 28.64  ? 53  PRO   B CD  1 
ATOM   2932 N  N   . GLY   B  1  41  ? 12.908  -7.917  55.163 1.00 28.97  ? 54  GLY   B N   1 
ATOM   2933 C  CA  . GLY   B  1  41  ? 12.007  -7.705  54.044 1.00 30.14  ? 54  GLY   B CA  1 
ATOM   2934 C  C   . GLY   B  1  41  ? 11.865  -6.224  53.680 1.00 29.06  ? 54  GLY   B C   1 
ATOM   2935 O  O   . GLY   B  1  41  ? 12.152  -5.836  52.550 1.00 28.70  ? 54  GLY   B O   1 
ATOM   2936 N  N   . LEU   B  1  42  ? 11.426  -5.413  54.643 1.00 29.57  ? 55  LEU   B N   1 
ATOM   2937 C  CA  . LEU   B  1  42  ? 11.217  -3.993  54.410 1.00 30.86  ? 55  LEU   B CA  1 
ATOM   2938 C  C   . LEU   B  1  42  ? 12.554  -3.325  54.083 1.00 29.42  ? 55  LEU   B C   1 
ATOM   2939 O  O   . LEU   B  1  42  ? 12.600  -2.453  53.230 1.00 30.27  ? 55  LEU   B O   1 
ATOM   2940 C  CB  . LEU   B  1  42  ? 10.554  -3.324  55.613 1.00 29.01  ? 55  LEU   B CB  1 
ATOM   2941 C  CG  . LEU   B  1  42  ? 9.155   -3.821  55.966 1.00 32.27  ? 55  LEU   B CG  1 
ATOM   2942 C  CD1 . LEU   B  1  42  ? 8.624   -3.119  57.184 1.00 34.10  ? 55  LEU   B CD1 1 
ATOM   2943 C  CD2 . LEU   B  1  42  ? 8.200   -3.607  54.816 1.00 35.04  ? 55  LEU   B CD2 1 
ATOM   2944 N  N   . ASN   B  1  43  ? 13.632  -3.746  54.757 1.00 29.47  ? 56  ASN   B N   1 
ATOM   2945 C  CA  . ASN   B  1  43  ? 14.951  -3.181  54.511 1.00 27.56  ? 56  ASN   B CA  1 
ATOM   2946 C  C   . ASN   B  1  43  ? 15.353  -3.389  53.050 1.00 27.02  ? 56  ASN   B C   1 
ATOM   2947 O  O   . ASN   B  1  43  ? 15.841  -2.468  52.406 1.00 26.78  ? 56  ASN   B O   1 
ATOM   2948 C  CB  . ASN   B  1  43  ? 16.001  -3.803  55.403 1.00 26.65  ? 56  ASN   B CB  1 
ATOM   2949 C  CG  . ASN   B  1  43  ? 15.942  -3.343  56.831 1.00 28.80  ? 56  ASN   B CG  1 
ATOM   2950 O  OD1 . ASN   B  1  43  ? 15.332  -2.315  57.160 1.00 29.23  ? 56  ASN   B OD1 1 
ATOM   2951 N  ND2 . ASN   B  1  43  ? 16.623  -4.089  57.688 1.00 29.70  ? 56  ASN   B ND2 1 
ATOM   2952 N  N   . THR   B  1  44  ? 15.107  -4.588  52.526 1.00 24.88  ? 57  THR   B N   1 
ATOM   2953 C  CA  . THR   B  1  44  ? 15.498  -4.890  51.164 1.00 28.47  ? 57  THR   B CA  1 
ATOM   2954 C  C   . THR   B  1  44  ? 14.632  -4.086  50.191 1.00 28.16  ? 57  THR   B C   1 
ATOM   2955 O  O   . THR   B  1  44  ? 15.143  -3.562  49.208 1.00 30.20  ? 57  THR   B O   1 
ATOM   2956 C  CB  . THR   B  1  44  ? 15.405  -6.396  50.913 1.00 28.18  ? 57  THR   B CB  1 
ATOM   2957 O  OG1 . THR   B  1  44  ? 16.322  -7.022  51.801 1.00 27.32  ? 57  THR   B OG1 1 
ATOM   2958 C  CG2 . THR   B  1  44  ? 15.814  -6.764  49.500 1.00 29.14  ? 57  THR   B CG2 1 
ATOM   2959 N  N   . LEU   B  1  45  ? 13.327  -3.983  50.462 1.00 26.31  ? 58  LEU   B N   1 
ATOM   2960 C  CA  . LEU   B  1  45  ? 12.441  -3.217  49.603 1.00 28.67  ? 58  LEU   B CA  1 
ATOM   2961 C  C   . LEU   B  1  45  ? 12.839  -1.740  49.590 1.00 28.10  ? 58  LEU   B C   1 
ATOM   2962 O  O   . LEU   B  1  45  ? 12.780  -1.089  48.555 1.00 28.19  ? 58  LEU   B O   1 
ATOM   2963 C  CB  . LEU   B  1  45  ? 11.012  -3.403  50.089 1.00 30.42  ? 58  LEU   B CB  1 
ATOM   2964 C  CG  . LEU   B  1  45  ? 10.450  -4.817  49.955 1.00 30.95  ? 58  LEU   B CG  1 
ATOM   2965 C  CD1 . LEU   B  1  45  ? 9.180   -4.958  50.764 1.00 32.19  ? 58  LEU   B CD1 1 
ATOM   2966 C  CD2 . LEU   B  1  45  ? 10.185  -5.127  48.484 1.00 31.29  ? 58  LEU   B CD2 1 
ATOM   2967 N  N   . ALA   B  1  46  ? 13.286  -1.214  50.727 1.00 26.47  ? 59  ALA   B N   1 
ATOM   2968 C  CA  . ALA   B  1  46  ? 13.733  0.163   50.751 1.00 27.00  ? 59  ALA   B CA  1 
ATOM   2969 C  C   . ALA   B  1  46  ? 15.030  0.312   49.955 1.00 28.56  ? 59  ALA   B C   1 
ATOM   2970 O  O   . ALA   B  1  46  ? 15.189  1.266   49.193 1.00 30.80  ? 59  ALA   B O   1 
ATOM   2971 C  CB  . ALA   B  1  46  ? 13.871  0.633   52.180 1.00 26.50  ? 59  ALA   B CB  1 
ATOM   2972 N  N   . SER   B  1  47  ? 15.959  -0.634  50.101 1.00 26.41  ? 60  SER   B N   1 
ATOM   2973 C  CA  . SER   B  1  47  ? 17.263  -0.489  49.473 1.00 25.98  ? 60  SER   B CA  1 
ATOM   2974 C  C   . SER   B  1  47  ? 17.214  -0.765  47.968 1.00 28.14  ? 60  SER   B C   1 
ATOM   2975 O  O   . SER   B  1  47  ? 18.164  -0.430  47.275 1.00 29.26  ? 60  SER   B O   1 
ATOM   2976 C  CB  . SER   B  1  47  ? 18.301  -1.309  50.178 1.00 24.66  ? 60  SER   B CB  1 
ATOM   2977 O  OG  . SER   B  1  47  ? 18.692  -0.683  51.394 1.00 24.53  ? 60  SER   B OG  1 
ATOM   2978 N  N   . HIS   B  1  48  ? 16.096  -1.304  47.463 1.00 29.35  ? 61  HIS   B N   1 
ATOM   2979 C  CA  . HIS   B  1  48  ? 15.881  -1.433  46.032 1.00 32.01  ? 61  HIS   B CA  1 
ATOM   2980 C  C   . HIS   B  1  48  ? 14.827  -0.470  45.494 1.00 33.96  ? 61  HIS   B C   1 
ATOM   2981 O  O   . HIS   B  1  48  ? 14.466  -0.575  44.327 1.00 30.47  ? 61  HIS   B O   1 
ATOM   2982 C  CB  . HIS   B  1  48  ? 15.416  -2.839  45.656 1.00 31.88  ? 61  HIS   B CB  1 
ATOM   2983 C  CG  . HIS   B  1  48  ? 16.524  -3.830  45.690 1.00 30.29  ? 61  HIS   B CG  1 
ATOM   2984 N  ND1 . HIS   B  1  48  ? 17.147  -4.223  44.536 1.00 28.07  ? 61  HIS   B ND1 1 
ATOM   2985 C  CD2 . HIS   B  1  48  ? 17.123  -4.503  46.691 1.00 29.60  ? 61  HIS   B CD2 1 
ATOM   2986 C  CE1 . HIS   B  1  48  ? 18.084  -5.115  44.848 1.00 30.99  ? 61  HIS   B CE1 1 
ATOM   2987 N  NE2 . HIS   B  1  48  ? 18.087  -5.290  46.154 1.00 27.30  ? 61  HIS   B NE2 1 
ATOM   2988 N  N   . GLY   B  1  49  ? 14.335  0.456   46.318 1.00 34.14  ? 62  GLY   B N   1 
ATOM   2989 C  CA  . GLY   B  1  49  ? 13.407  1.468   45.834 1.00 36.24  ? 62  GLY   B CA  1 
ATOM   2990 C  C   . GLY   B  1  49  ? 11.977  0.958   45.612 1.00 33.05  ? 62  GLY   B C   1 
ATOM   2991 O  O   . GLY   B  1  49  ? 11.190  1.634   44.970 1.00 33.11  ? 62  GLY   B O   1 
ATOM   2992 N  N   . TYR   B  1  50  ? 11.606  -0.211  46.148 1.00 34.19  ? 63  TYR   B N   1 
ATOM   2993 C  CA  . TYR   B  1  50  ? 10.200  -0.586  46.193 1.00 32.34  ? 63  TYR   B CA  1 
ATOM   2994 C  C   . TYR   B  1  50  ? 9.447   0.269   47.210 1.00 32.88  ? 63  TYR   B C   1 
ATOM   2995 O  O   . TYR   B  1  50  ? 8.276   0.549   47.016 1.00 30.69  ? 63  TYR   B O   1 
ATOM   2996 C  CB  . TYR   B  1  50  ? 10.012  -2.065  46.512 1.00 34.17  ? 63  TYR   B CB  1 
ATOM   2997 C  CG  . TYR   B  1  50  ? 10.183  -2.924  45.269 1.00 35.16  ? 63  TYR   B CG  1 
ATOM   2998 C  CD1 . TYR   B  1  50  ? 9.159   -3.048  44.334 1.00 35.23  ? 63  TYR   B CD1 1 
ATOM   2999 C  CD2 . TYR   B  1  50  ? 11.392  -3.563  45.017 1.00 34.08  ? 63  TYR   B CD2 1 
ATOM   3000 C  CE1 . TYR   B  1  50  ? 9.329   -3.807  43.186 1.00 39.11  ? 63  TYR   B CE1 1 
ATOM   3001 C  CE2 . TYR   B  1  50  ? 11.563  -4.330  43.888 1.00 34.55  ? 63  TYR   B CE2 1 
ATOM   3002 C  CZ  . TYR   B  1  50  ? 10.535  -4.458  42.972 1.00 35.85  ? 63  TYR   B CZ  1 
ATOM   3003 O  OH  . TYR   B  1  50  ? 10.759  -5.210  41.863 1.00 34.76  ? 63  TYR   B OH  1 
ATOM   3004 N  N   . LEU   B  1  51  ? 10.112  0.600   48.319 1.00 35.57  ? 64  LEU   B N   1 
ATOM   3005 C  CA  . LEU   B  1  51  ? 9.675   1.608   49.267 1.00 34.56  ? 64  LEU   B CA  1 
ATOM   3006 C  C   . LEU   B  1  51  ? 10.548  2.828   49.055 1.00 39.44  ? 64  LEU   B C   1 
ATOM   3007 O  O   . LEU   B  1  51  ? 11.639  2.702   48.498 1.00 42.61  ? 64  LEU   B O   1 
ATOM   3008 C  CB  . LEU   B  1  51  ? 9.884   1.113   50.699 1.00 36.72  ? 64  LEU   B CB  1 
ATOM   3009 C  CG  . LEU   B  1  51  ? 8.989   -0.035  51.153 1.00 38.23  ? 64  LEU   B CG  1 
ATOM   3010 C  CD1 . LEU   B  1  51  ? 9.480   -0.609  52.444 1.00 40.25  ? 64  LEU   B CD1 1 
ATOM   3011 C  CD2 . LEU   B  1  51  ? 7.578   0.485   51.287 1.00 41.43  ? 64  LEU   B CD2 1 
ATOM   3012 N  N   . PRO   B  1  52  ? 10.148  4.012   49.573 1.00 40.26  ? 65  PRO   B N   1 
ATOM   3013 C  CA  . PRO   B  1  52  ? 11.063  5.149   49.659 1.00 39.19  ? 65  PRO   B CA  1 
ATOM   3014 C  C   . PRO   B  1  52  ? 12.392  4.724   50.285 1.00 35.64  ? 65  PRO   B C   1 
ATOM   3015 O  O   . PRO   B  1  52  ? 12.405  4.023   51.286 1.00 35.75  ? 65  PRO   B O   1 
ATOM   3016 C  CB  . PRO   B  1  52  ? 10.277  6.139   50.539 1.00 40.81  ? 65  PRO   B CB  1 
ATOM   3017 C  CG  . PRO   B  1  52  ? 8.823   5.804   50.290 1.00 39.26  ? 65  PRO   B CG  1 
ATOM   3018 C  CD  . PRO   B  1  52  ? 8.811   4.304   50.107 1.00 41.35  ? 65  PRO   B CD  1 
ATOM   3019 N  N   . ARG   B  1  53  ? 13.506  5.119   49.668 1.00 35.30  ? 66  ARG   B N   1 
ATOM   3020 C  CA  . ARG   B  1  53  ? 14.829  4.665   50.068 1.00 33.18  ? 66  ARG   B CA  1 
ATOM   3021 C  C   . ARG   B  1  53  ? 15.222  5.187   51.447 1.00 31.37  ? 66  ARG   B C   1 
ATOM   3022 O  O   . ARG   B  1  53  ? 16.146  4.679   52.073 1.00 33.18  ? 66  ARG   B O   1 
ATOM   3023 C  CB  . ARG   B  1  53  ? 15.866  5.040   49.008 1.00 34.42  ? 66  ARG   B CB  1 
ATOM   3024 C  CG  . ARG   B  1  53  ? 15.630  4.315   47.692 1.00 34.49  ? 66  ARG   B CG  1 
ATOM   3025 C  CD  . ARG   B  1  53  ? 16.733  4.557   46.690 1.00 33.53  ? 66  ARG   B CD  1 
ATOM   3026 N  NE  . ARG   B  1  53  ? 16.407  3.860   45.444 1.00 36.19  ? 66  ARG   B NE  1 
ATOM   3027 C  CZ  . ARG   B  1  53  ? 16.866  2.659   45.116 1.00 37.46  ? 66  ARG   B CZ  1 
ATOM   3028 N  NH1 . ARG   B  1  53  ? 17.599  1.969   45.977 1.00 37.98  ? 66  ARG   B NH1 1 
ATOM   3029 N  NH2 . ARG   B  1  53  ? 16.583  2.149   43.934 1.00 36.48  ? 66  ARG   B NH2 1 
ATOM   3030 N  N   . ASP   B  1  54  ? 14.518  6.192   51.936 1.00 34.97  ? 67  ASP   B N   1 
ATOM   3031 C  CA  . ASP   B  1  54  ? 14.795  6.741   53.252 1.00 35.09  ? 67  ASP   B CA  1 
ATOM   3032 C  C   . ASP   B  1  54  ? 14.114  5.933   54.347 1.00 31.87  ? 67  ASP   B C   1 
ATOM   3033 O  O   . ASP   B  1  54  ? 14.384  6.163   55.517 1.00 33.49  ? 67  ASP   B O   1 
ATOM   3034 C  CB  . ASP   B  1  54  ? 14.451  8.220   53.357 1.00 45.18  ? 67  ASP   B CB  1 
ATOM   3035 C  CG  . ASP   B  1  54  ? 12.977  8.597   53.285 1.00 49.25  ? 67  ASP   B CG  1 
ATOM   3036 O  OD1 . ASP   B  1  54  ? 12.123  7.669   53.207 1.00 46.99  ? 67  ASP   B OD1 1 
ATOM   3037 O  OD2 . ASP   B  1  54  ? 12.709  9.828   53.307 1.00 53.23  ? 67  ASP   B OD2 1 
ATOM   3038 N  N   . GLY   B  1  55  ? 13.287  4.951   53.989 1.00 31.57  ? 68  GLY   B N   1 
ATOM   3039 C  CA  . GLY   B  1  55  ? 12.817  3.980   54.971 1.00 33.52  ? 68  GLY   B CA  1 
ATOM   3040 C  C   . GLY   B  1  55  ? 11.603  4.484   55.756 1.00 32.77  ? 68  GLY   B C   1 
ATOM   3041 O  O   . GLY   B  1  55  ? 11.265  3.931   56.803 1.00 28.83  ? 68  GLY   B O   1 
ATOM   3042 N  N   . VAL   B  1  56  ? 10.954  5.523   55.231 1.00 33.40  ? 69  VAL   B N   1 
ATOM   3043 C  CA  . VAL   B  1  56  ? 9.753   6.081   55.826 1.00 35.25  ? 69  VAL   B CA  1 
ATOM   3044 C  C   . VAL   B  1  56  ? 8.660   6.031   54.771 1.00 36.89  ? 69  VAL   B C   1 
ATOM   3045 O  O   . VAL   B  1  56  ? 8.858   6.534   53.669 1.00 37.61  ? 69  VAL   B O   1 
ATOM   3046 C  CB  . VAL   B  1  56  ? 10.006  7.508   56.332 1.00 37.80  ? 69  VAL   B CB  1 
ATOM   3047 C  CG1 . VAL   B  1  56  ? 8.717   8.201   56.732 1.00 38.81  ? 69  VAL   B CG1 1 
ATOM   3048 C  CG2 . VAL   B  1  56  ? 10.988  7.508   57.500 1.00 37.78  ? 69  VAL   B CG2 1 
ATOM   3049 N  N   . ALA   B  1  57  ? 7.522   5.414   55.117 1.00 34.73  ? 70  ALA   B N   1 
ATOM   3050 C  CA  . ALA   B  1  57  ? 6.514   5.127   54.113 1.00 34.24  ? 70  ALA   B CA  1 
ATOM   3051 C  C   . ALA   B  1  57  ? 5.107   5.134   54.699 1.00 35.72  ? 70  ALA   B C   1 
ATOM   3052 O  O   . ALA   B  1  57  ? 4.926   4.970   55.909 1.00 40.14  ? 70  ALA   B O   1 
ATOM   3053 C  CB  . ALA   B  1  57  ? 6.814   3.789   53.494 1.00 35.23  ? 70  ALA   B CB  1 
ATOM   3054 N  N   . THR   B  1  58  ? 4.122   5.276   53.806 1.00 34.64  ? 71  THR   B N   1 
ATOM   3055 C  CA  . THR   B  1  58  ? 2.724   5.147   54.172 1.00 38.02  ? 71  THR   B CA  1 
ATOM   3056 C  C   . THR   B  1  58  ? 2.402   3.665   54.273 1.00 41.09  ? 71  THR   B C   1 
ATOM   3057 O  O   . THR   B  1  58  ? 3.070   2.850   53.650 1.00 43.10  ? 71  THR   B O   1 
ATOM   3058 C  CB  . THR   B  1  58  ? 1.776   5.802   53.163 1.00 38.72  ? 71  THR   B CB  1 
ATOM   3059 O  OG1 . THR   B  1  58  ? 1.843   5.007   51.984 1.00 42.48  ? 71  THR   B OG1 1 
ATOM   3060 C  CG2 . THR   B  1  58  ? 2.108   7.246   52.854 1.00 39.94  ? 71  THR   B CG2 1 
ATOM   3061 N  N   . PRO   B  1  59  ? 1.378   3.285   55.067 1.00 40.56  ? 72  PRO   B N   1 
ATOM   3062 C  CA  . PRO   B  1  59  ? 0.896   1.903   55.081 1.00 37.72  ? 72  PRO   B CA  1 
ATOM   3063 C  C   . PRO   B  1  59  ? 0.605   1.374   53.681 1.00 38.17  ? 72  PRO   B C   1 
ATOM   3064 O  O   . PRO   B  1  59  ? 0.923   0.237   53.362 1.00 41.10  ? 72  PRO   B O   1 
ATOM   3065 C  CB  . PRO   B  1  59  ? -0.381  2.000   55.933 1.00 40.29  ? 72  PRO   B CB  1 
ATOM   3066 C  CG  . PRO   B  1  59  ? -0.116  3.183   56.859 1.00 39.82  ? 72  PRO   B CG  1 
ATOM   3067 C  CD  . PRO   B  1  59  ? 0.684   4.157   56.032 1.00 37.11  ? 72  PRO   B CD  1 
ATOM   3068 N  N   . ALA   B  1  60  ? -0.027  2.197   52.852 1.00 37.51  ? 73  ALA   B N   1 
ATOM   3069 C  CA  . ALA   B  1  60  ? -0.390  1.783   51.509 1.00 38.92  ? 73  ALA   B CA  1 
ATOM   3070 C  C   . ALA   B  1  60  ? 0.863   1.467   50.709 1.00 35.11  ? 73  ALA   B C   1 
ATOM   3071 O  O   . ALA   B  1  60  ? 0.888   0.463   50.024 1.00 37.55  ? 73  ALA   B O   1 
ATOM   3072 C  CB  . ALA   B  1  60  ? -1.220  2.833   50.822 1.00 38.83  ? 73  ALA   B CB  1 
ATOM   3073 N  N   . GLN   B  1  61  ? 1.903   2.289   50.831 1.00 37.07  ? 74  GLN   B N   1 
ATOM   3074 C  CA  . GLN   B  1  61  ? 3.141   2.032   50.109 1.00 35.58  ? 74  GLN   B CA  1 
ATOM   3075 C  C   . GLN   B  1  61  ? 3.776   0.730   50.589 1.00 35.35  ? 74  GLN   B C   1 
ATOM   3076 O  O   . GLN   B  1  61  ? 4.322   -0.002  49.779 1.00 35.10  ? 74  GLN   B O   1 
ATOM   3077 C  CB  . GLN   B  1  61  ? 4.179   3.135   50.281 1.00 34.16  ? 74  GLN   B CB  1 
ATOM   3078 C  CG  . GLN   B  1  61  ? 3.802   4.423   49.571 1.00 36.34  ? 74  GLN   B CG  1 
ATOM   3079 C  CD  . GLN   B  1  61  ? 4.712   5.571   49.947 1.00 40.62  ? 74  GLN   B CD  1 
ATOM   3080 O  OE1 . GLN   B  1  61  ? 5.077   5.771   51.112 1.00 37.08  ? 74  GLN   B OE1 1 
ATOM   3081 N  NE2 . GLN   B  1  61  ? 5.122   6.313   48.935 1.00 44.35  ? 74  GLN   B NE2 1 
ATOM   3082 N  N   . ILE   B  1  62  ? 3.717   0.464   51.899 1.00 33.40  ? 75  ILE   B N   1 
ATOM   3083 C  CA  . ILE   B  1  62  ? 4.318   -0.739  52.450 1.00 35.60  ? 75  ILE   B CA  1 
ATOM   3084 C  C   . ILE   B  1  62  ? 3.588   -1.967  51.902 1.00 34.60  ? 75  ILE   B C   1 
ATOM   3085 O  O   . ILE   B  1  62  ? 4.207   -2.945  51.485 1.00 33.60  ? 75  ILE   B O   1 
ATOM   3086 C  CB  . ILE   B  1  62  ? 4.338   -0.683  53.986 1.00 30.26  ? 75  ILE   B CB  1 
ATOM   3087 C  CG1 . ILE   B  1  62  ? 5.329   0.362   54.466 1.00 28.05  ? 75  ILE   B CG1 1 
ATOM   3088 C  CG2 . ILE   B  1  62  ? 4.648   -2.057  54.576 1.00 31.56  ? 75  ILE   B CG2 1 
ATOM   3089 C  CD1 . ILE   B  1  62  ? 5.275   0.646   55.960 1.00 29.66  ? 75  ILE   B CD1 1 
ATOM   3090 N  N   . ILE   B  1  63  ? 2.268   -1.910  51.881 1.00 32.02  ? 76  ILE   B N   1 
ATOM   3091 C  CA  . ILE   B  1  63  ? 1.491   -3.039  51.408 1.00 32.01  ? 76  ILE   B CA  1 
ATOM   3092 C  C   . ILE   B  1  63  ? 1.813   -3.303  49.947 1.00 33.15  ? 76  ILE   B C   1 
ATOM   3093 O  O   . ILE   B  1  63  ? 2.113   -4.438  49.596 1.00 38.22  ? 76  ILE   B O   1 
ATOM   3094 C  CB  . ILE   B  1  63  ? -0.005  -2.832  51.667 1.00 33.51  ? 76  ILE   B CB  1 
ATOM   3095 C  CG1 . ILE   B  1  63  ? -0.272  -2.900  53.166 1.00 32.85  ? 76  ILE   B CG1 1 
ATOM   3096 C  CG2 . ILE   B  1  63  ? -0.862  -3.834  50.897 1.00 33.70  ? 76  ILE   B CG2 1 
ATOM   3097 C  CD1 . ILE   B  1  63  ? -1.506  -2.150  53.598 1.00 36.08  ? 76  ILE   B CD1 1 
ATOM   3098 N  N   . THR   B  1  64  ? 1.808   -2.272  49.104 1.00 35.78  ? 77  THR   B N   1 
ATOM   3099 C  CA  A THR   B  1  64  ? 2.015   -2.487  47.679 0.50 37.54  ? 77  THR   B CA  1 
ATOM   3100 C  CA  B THR   B  1  64  ? 2.011   -2.494  47.680 0.50 35.34  ? 77  THR   B CA  1 
ATOM   3101 C  C   . THR   B  1  64  ? 3.438   -3.005  47.448 1.00 33.80  ? 77  THR   B C   1 
ATOM   3102 O  O   . THR   B  1  64  ? 3.644   -3.866  46.602 1.00 34.20  ? 77  THR   B O   1 
ATOM   3103 C  CB  A THR   B  1  64  ? 1.734   -1.221  46.870 0.50 40.54  ? 77  THR   B CB  1 
ATOM   3104 C  CB  B THR   B  1  64  ? 1.646   -1.267  46.835 0.50 36.20  ? 77  THR   B CB  1 
ATOM   3105 O  OG1 A THR   B  1  64  ? 2.727   -0.317  47.345 0.50 57.10  ? 77  THR   B OG1 1 
ATOM   3106 O  OG1 B THR   B  1  64  ? 2.253   -1.416  45.552 0.50 31.76  ? 77  THR   B OG1 1 
ATOM   3107 C  CG2 A THR   B  1  64  ? 0.337   -0.676  47.073 0.50 37.70  ? 77  THR   B CG2 1 
ATOM   3108 C  CG2 B THR   B  1  64  ? 2.198   0.056   47.329 0.50 41.91  ? 77  THR   B CG2 1 
ATOM   3109 N  N   . ALA   B  1  65  ? 4.408   -2.518  48.234 1.00 30.89  ? 78  ALA   B N   1 
ATOM   3110 C  CA  . ALA   B  1  65  ? 5.808   -2.918  48.109 1.00 33.11  ? 78  ALA   B CA  1 
ATOM   3111 C  C   . ALA   B  1  65  ? 6.030   -4.379  48.497 1.00 33.99  ? 78  ALA   B C   1 
ATOM   3112 O  O   . ALA   B  1  65  ? 6.778   -5.078  47.820 1.00 31.01  ? 78  ALA   B O   1 
ATOM   3113 C  CB  . ALA   B  1  65  ? 6.700   -2.032  48.944 1.00 29.57  ? 78  ALA   B CB  1 
ATOM   3114 N  N   . THR   B  1  66  ? 5.413   -4.833  49.591 1.00 31.00  ? 79  THR   B N   1 
ATOM   3115 C  CA  . THR   B  1  66  ? 5.589   -6.214  50.015 1.00 30.80  ? 79  THR   B CA  1 
ATOM   3116 C  C   . THR   B  1  66  ? 4.947   -7.154  49.001 1.00 30.86  ? 79  THR   B C   1 
ATOM   3117 O  O   . THR   B  1  66  ? 5.419   -8.268  48.807 1.00 32.63  ? 79  THR   B O   1 
ATOM   3118 C  CB  . THR   B  1  66  ? 5.037   -6.466  51.421 1.00 30.43  ? 79  THR   B CB  1 
ATOM   3119 O  OG1 . THR   B  1  66  ? 3.652   -6.151  51.438 1.00 29.48  ? 79  THR   B OG1 1 
ATOM   3120 C  CG2 . THR   B  1  66  ? 5.748   -5.655  52.489 1.00 31.80  ? 79  THR   B CG2 1 
ATOM   3121 N  N   . GLN   B  1  67  ? 3.869   -6.707  48.355 1.00 36.46  ? 80  GLN   B N   1 
ATOM   3122 C  CA  . GLN   B  1  67  ? 3.207   -7.496  47.325 1.00 37.80  ? 80  GLN   B CA  1 
ATOM   3123 C  C   . GLN   B  1  67  ? 4.030   -7.493  46.042 1.00 36.53  ? 80  GLN   B C   1 
ATOM   3124 O  O   . GLN   B  1  67  ? 4.266   -8.548  45.480 1.00 38.72  ? 80  GLN   B O   1 
ATOM   3125 C  CB  . GLN   B  1  67  ? 1.784   -6.991  47.081 1.00 37.56  ? 80  GLN   B CB  1 
ATOM   3126 C  CG  . GLN   B  1  67  ? 0.898   -7.170  48.307 1.00 38.73  ? 80  GLN   B CG  1 
ATOM   3127 C  CD  . GLN   B  1  67  ? -0.543  -6.718  48.173 1.00 40.33  ? 80  GLN   B CD  1 
ATOM   3128 O  OE1 . GLN   B  1  67  ? -1.405  -7.160  48.937 1.00 43.73  ? 80  GLN   B OE1 1 
ATOM   3129 N  NE2 . GLN   B  1  67  ? -0.849  -5.863  47.209 1.00 40.45  ? 80  GLN   B NE2 1 
ATOM   3130 N  N   . GLU   B  1  68  ? 4.443   -6.321  45.559 1.00 37.13  ? 81  GLU   B N   1 
ATOM   3131 C  CA  . GLU   B  1  68  ? 5.195   -6.250  44.316 1.00 39.07  ? 81  GLU   B CA  1 
ATOM   3132 C  C   . GLU   B  1  68  ? 6.519   -7.000  44.454 1.00 37.89  ? 81  GLU   B C   1 
ATOM   3133 O  O   . GLU   B  1  68  ? 6.875   -7.770  43.579 1.00 40.56  ? 81  GLU   B O   1 
ATOM   3134 C  CB  . GLU   B  1  68  ? 5.460   -4.821  43.842 1.00 45.01  ? 81  GLU   B CB  1 
ATOM   3135 C  CG  . GLU   B  1  68  ? 4.212   -4.085  43.355 1.00 57.63  ? 81  GLU   B CG  1 
ATOM   3136 C  CD  . GLU   B  1  68  ? 3.406   -4.807  42.275 1.00 68.21  ? 81  GLU   B CD  1 
ATOM   3137 O  OE1 . GLU   B  1  68  ? 2.154   -4.884  42.381 1.00 62.57  ? 81  GLU   B OE1 1 
ATOM   3138 O  OE2 . GLU   B  1  68  ? 4.046   -5.333  41.334 1.00 72.24  ? 81  GLU   B OE2 1 
ATOM   3139 N  N   . GLY   B  1  69  ? 7.236   -6.785  45.558 1.00 34.15  ? 82  GLY   B N   1 
ATOM   3140 C  CA  . GLY   B  1  69  ? 8.600   -7.264  45.684 1.00 32.05  ? 82  GLY   B CA  1 
ATOM   3141 C  C   . GLY   B  1  69  ? 8.693   -8.737  46.071 1.00 31.00  ? 82  GLY   B C   1 
ATOM   3142 O  O   . GLY   B  1  69  ? 9.634   -9.398  45.661 1.00 30.25  ? 82  GLY   B O   1 
ATOM   3143 N  N   . PHE   B  1  70  ? 7.738   -9.236  46.868 1.00 29.75  ? 83  PHE   B N   1 
ATOM   3144 C  CA  . PHE   B  1  70  ? 7.866   -10.562 47.452 1.00 31.90  ? 83  PHE   B CA  1 
ATOM   3145 C  C   . PHE   B  1  70  ? 6.616   -11.419 47.290 1.00 33.13  ? 83  PHE   B C   1 
ATOM   3146 O  O   . PHE   B  1  70  ? 6.626   -12.584 47.699 1.00 34.03  ? 83  PHE   B O   1 
ATOM   3147 C  CB  . PHE   B  1  70  ? 8.149   -10.476 48.954 1.00 31.27  ? 83  PHE   B CB  1 
ATOM   3148 C  CG  . PHE   B  1  70  ? 9.581   -10.098 49.286 1.00 31.26  ? 83  PHE   B CG  1 
ATOM   3149 C  CD1 . PHE   B  1  70  ? 10.624  -10.987 49.077 1.00 31.95  ? 83  PHE   B CD1 1 
ATOM   3150 C  CD2 . PHE   B  1  70  ? 9.870   -8.869  49.852 1.00 34.00  ? 83  PHE   B CD2 1 
ATOM   3151 C  CE1 . PHE   B  1  70  ? 11.924  -10.641 49.393 1.00 32.25  ? 83  PHE   B CE1 1 
ATOM   3152 C  CE2 . PHE   B  1  70  ? 11.166  -8.533  50.199 1.00 31.68  ? 83  PHE   B CE2 1 
ATOM   3153 C  CZ  . PHE   B  1  70  ? 12.191  -9.412  49.950 1.00 35.11  ? 83  PHE   B CZ  1 
ATOM   3154 N  N   . ASN   B  1  71  ? 5.556   -10.848 46.711 1.00 33.26  ? 84  ASN   B N   1 
ATOM   3155 C  CA  . ASN   B  1  71  ? 4.252   -11.491 46.640 1.00 34.21  ? 84  ASN   B CA  1 
ATOM   3156 C  C   . ASN   B  1  71  ? 3.744   -11.843 48.033 1.00 30.37  ? 84  ASN   B C   1 
ATOM   3157 O  O   . ASN   B  1  71  ? 3.191   -12.912 48.244 1.00 32.92  ? 84  ASN   B O   1 
ATOM   3158 C  CB  . ASN   B  1  71  ? 4.293   -12.720 45.748 1.00 36.60  ? 84  ASN   B CB  1 
ATOM   3159 C  CG  . ASN   B  1  71  ? 3.076   -12.850 44.870 1.00 34.49  ? 84  ASN   B CG  1 
ATOM   3160 O  OD1 . ASN   B  1  71  ? 2.049   -12.215 45.113 1.00 37.46  ? 84  ASN   B OD1 1 
ATOM   3161 N  ND2 . ASN   B  1  71  ? 3.193   -13.662 43.833 1.00 41.11  ? 84  ASN   B ND2 1 
ATOM   3162 N  N   . PHE   B  1  72  ? 3.973   -10.957 49.000 1.00 31.68  ? 85  PHE   B N   1 
ATOM   3163 C  CA  . PHE   B  1  72  ? 3.408   -11.145 50.327 1.00 30.95  ? 85  PHE   B CA  1 
ATOM   3164 C  C   . PHE   B  1  72  ? 1.889   -11.109 50.182 1.00 33.23  ? 85  PHE   B C   1 
ATOM   3165 O  O   . PHE   B  1  72  ? 1.335   -10.255 49.492 1.00 33.43  ? 85  PHE   B O   1 
ATOM   3166 C  CB  . PHE   B  1  72  ? 3.899   -10.047 51.272 1.00 32.53  ? 85  PHE   B CB  1 
ATOM   3167 C  CG  . PHE   B  1  72  ? 3.809   -10.341 52.761 1.00 32.99  ? 85  PHE   B CG  1 
ATOM   3168 C  CD1 . PHE   B  1  72  ? 4.194   -11.567 53.277 1.00 36.16  ? 85  PHE   B CD1 1 
ATOM   3169 C  CD2 . PHE   B  1  72  ? 3.394   -9.364  53.650 1.00 34.39  ? 85  PHE   B CD2 1 
ATOM   3170 C  CE1 . PHE   B  1  72  ? 4.117   -11.824 54.637 1.00 37.45  ? 85  PHE   B CE1 1 
ATOM   3171 C  CE2 . PHE   B  1  72  ? 3.333   -9.621  55.016 1.00 34.53  ? 85  PHE   B CE2 1 
ATOM   3172 C  CZ  . PHE   B  1  72  ? 3.701   -10.843 55.506 1.00 34.52  ? 85  PHE   B CZ  1 
ATOM   3173 N  N   . GLU   B  1  73  ? 1.208   -12.075 50.787 1.00 33.17  ? 86  GLU   B N   1 
ATOM   3174 C  CA  . GLU   B  1  73  ? -0.239  -12.155 50.711 1.00 38.11  ? 86  GLU   B CA  1 
ATOM   3175 C  C   . GLU   B  1  73  ? -0.889  -10.884 51.279 1.00 35.05  ? 86  GLU   B C   1 
ATOM   3176 O  O   . GLU   B  1  73  ? -0.475  -10.348 52.303 1.00 35.55  ? 86  GLU   B O   1 
ATOM   3177 C  CB  . GLU   B  1  73  ? -0.652  -13.425 51.455 1.00 44.96  ? 86  GLU   B CB  1 
ATOM   3178 C  CG  . GLU   B  1  73  ? -2.092  -13.854 51.197 1.00 49.52  ? 86  GLU   B CG  1 
ATOM   3179 C  CD  . GLU   B  1  73  ? -3.120  -13.197 52.097 1.00 56.31  ? 86  GLU   B CD  1 
ATOM   3180 O  OE1 . GLU   B  1  73  ? -4.128  -12.654 51.562 1.00 55.24  ? 86  GLU   B OE1 1 
ATOM   3181 O  OE2 . GLU   B  1  73  ? -2.893  -13.224 53.339 1.00 60.86  ? 86  GLU   B OE2 1 
ATOM   3182 N  N   . ASN   B  1  74  ? -1.954  -10.438 50.619 1.00 33.85  ? 87  ASN   B N   1 
ATOM   3183 C  CA  . ASN   B  1  74  ? -2.603  -9.154  50.881 1.00 39.43  ? 87  ASN   B CA  1 
ATOM   3184 C  C   . ASN   B  1  74  ? -3.023  -9.001  52.343 1.00 34.78  ? 87  ASN   B C   1 
ATOM   3185 O  O   . ASN   B  1  74  ? -2.738  -7.988  52.969 1.00 35.87  ? 87  ASN   B O   1 
ATOM   3186 C  CB  . ASN   B  1  74  ? -3.806  -8.979  49.953 1.00 38.75  ? 87  ASN   B CB  1 
ATOM   3187 C  CG  . ASN   B  1  74  ? -4.516  -7.652  50.104 1.00 38.66  ? 87  ASN   B CG  1 
ATOM   3188 O  OD1 . ASN   B  1  74  ? -5.722  -7.635  50.388 1.00 43.14  ? 87  ASN   B OD1 1 
ATOM   3189 N  ND2 . ASN   B  1  74  ? -3.833  -6.540  49.857 1.00 34.54  ? 87  ASN   B ND2 1 
ATOM   3190 N  N   . ASN   B  1  75  ? -3.728  -9.991  52.879 1.00 34.65  ? 88  ASN   B N   1 
ATOM   3191 C  CA  . ASN   B  1  75  ? -4.230  -9.892  54.237 1.00 36.31  ? 88  ASN   B CA  1 
ATOM   3192 C  C   . ASN   B  1  75  ? -3.088  -9.905  55.233 1.00 37.35  ? 88  ASN   B C   1 
ATOM   3193 O  O   . ASN   B  1  75  ? -3.182  -9.215  56.246 1.00 34.21  ? 88  ASN   B O   1 
ATOM   3194 C  CB  . ASN   B  1  75  ? -5.284  -10.951 54.548 1.00 36.83  ? 88  ASN   B CB  1 
ATOM   3195 C  CG  . ASN   B  1  75  ? -6.595  -10.569 53.901 1.00 44.78  ? 88  ASN   B CG  1 
ATOM   3196 O  OD1 . ASN   B  1  75  ? -7.061  -9.426  54.021 1.00 43.75  ? 88  ASN   B OD1 1 
ATOM   3197 N  ND2 . ASN   B  1  75  ? -7.177  -11.495 53.163 1.00 50.90  ? 88  ASN   B ND2 1 
ATOM   3198 N  N   . ALA   B  1  76  ? -2.060  -10.724 54.957 1.00 35.29  ? 89  ALA   B N   1 
ATOM   3199 C  CA  . ALA   B  1  76  ? -0.905  -10.797 55.823 1.00 35.09  ? 89  ALA   B CA  1 
ATOM   3200 C  C   . ALA   B  1  76  ? -0.222  -9.435  55.851 1.00 33.63  ? 89  ALA   B C   1 
ATOM   3201 O  O   . ALA   B  1  76  ? 0.164   -8.965  56.917 1.00 34.09  ? 89  ALA   B O   1 
ATOM   3202 C  CB  . ALA   B  1  76  ? 0.007   -11.902 55.370 1.00 33.79  ? 89  ALA   B CB  1 
ATOM   3203 N  N   . ALA   B  1  77  ? -0.147  -8.793  54.680 1.00 30.72  ? 90  ALA   B N   1 
ATOM   3204 C  CA  . ALA   B  1  77  ? 0.459   -7.476  54.542 1.00 33.52  ? 90  ALA   B CA  1 
ATOM   3205 C  C   . ALA   B  1  77  ? -0.331  -6.435  55.329 1.00 32.93  ? 90  ALA   B C   1 
ATOM   3206 O  O   . ALA   B  1  77  ? 0.244   -5.546  55.951 1.00 34.88  ? 90  ALA   B O   1 
ATOM   3207 C  CB  . ALA   B  1  77  ? 0.539   -7.106  53.074 1.00 32.61  ? 90  ALA   B CB  1 
ATOM   3208 N  N   . ILE   B  1  78  ? -1.654  -6.569  55.300 1.00 34.78  ? 91  ILE   B N   1 
ATOM   3209 C  CA  . ILE   B  1  78  ? -2.537  -5.656  56.003 1.00 35.39  ? 91  ILE   B CA  1 
ATOM   3210 C  C   . ILE   B  1  78  ? -2.371  -5.835  57.512 1.00 31.16  ? 91  ILE   B C   1 
ATOM   3211 O  O   . ILE   B  1  78  ? -2.169  -4.856  58.218 1.00 33.92  ? 91  ILE   B O   1 
ATOM   3212 C  CB  . ILE   B  1  78  ? -3.986  -5.840  55.516 1.00 36.83  ? 91  ILE   B CB  1 
ATOM   3213 C  CG1 . ILE   B  1  78  ? -4.163  -5.270  54.116 1.00 35.45  ? 91  ILE   B CG1 1 
ATOM   3214 C  CG2 . ILE   B  1  78  ? -4.971  -5.204  56.487 1.00 35.71  ? 91  ILE   B CG2 1 
ATOM   3215 C  CD1 . ILE   B  1  78  ? -5.478  -5.641  53.449 1.00 35.44  ? 91  ILE   B CD1 1 
ATOM   3216 N  N   . VAL   B  1  79  ? -2.373  -7.081  57.986 1.00 27.48  ? 92  VAL   B N   1 
ATOM   3217 C  CA  . VAL   B  1  79  ? -2.214  -7.366  59.398 1.00 30.72  ? 92  VAL   B CA  1 
ATOM   3218 C  C   . VAL   B  1  79  ? -0.895  -6.811  59.917 1.00 31.58  ? 92  VAL   B C   1 
ATOM   3219 O  O   . VAL   B  1  79  ? -0.888  -6.156  60.955 1.00 34.32  ? 92  VAL   B O   1 
ATOM   3220 C  CB  . VAL   B  1  79  ? -2.336  -8.870  59.684 1.00 33.69  ? 92  VAL   B CB  1 
ATOM   3221 C  CG1 . VAL   B  1  79  ? -1.900  -9.230  61.100 1.00 34.39  ? 92  VAL   B CG1 1 
ATOM   3222 C  CG2 . VAL   B  1  79  ? -3.756  -9.341  59.408 1.00 31.64  ? 92  VAL   B CG2 1 
ATOM   3223 N  N   . ALA   B  1  80  ? 0.206   -7.080  59.209 1.00 31.77  ? 93  ALA   B N   1 
ATOM   3224 C  CA  . ALA   B  1  80  ? 1.518   -6.679  59.679 1.00 32.28  ? 93  ALA   B CA  1 
ATOM   3225 C  C   . ALA   B  1  80  ? 1.650   -5.164  59.591 1.00 31.83  ? 93  ALA   B C   1 
ATOM   3226 O  O   . ALA   B  1  80  ? 2.193   -4.542  60.503 1.00 33.17  ? 93  ALA   B O   1 
ATOM   3227 C  CB  . ALA   B  1  80  ? 2.611   -7.378  58.897 1.00 31.26  ? 93  ALA   B CB  1 
ATOM   3228 N  N   . THR   B  1  81  ? 1.158   -4.573  58.503 1.00 29.70  ? 94  THR   B N   1 
ATOM   3229 C  CA  . THR   B  1  81  ? 1.444   -3.164  58.254 1.00 32.35  ? 94  THR   B CA  1 
ATOM   3230 C  C   . THR   B  1  81  ? 0.722   -2.273  59.264 1.00 33.04  ? 94  THR   B C   1 
ATOM   3231 O  O   . THR   B  1  81  ? 1.327   -1.346  59.802 1.00 36.89  ? 94  THR   B O   1 
ATOM   3232 C  CB  . THR   B  1  81  ? 1.059   -2.771  56.825 1.00 34.59  ? 94  THR   B CB  1 
ATOM   3233 O  OG1 . THR   B  1  81  ? 1.899   -3.441  55.899 1.00 32.56  ? 94  THR   B OG1 1 
ATOM   3234 C  CG2 . THR   B  1  81  ? 1.240   -1.294  56.556 1.00 35.11  ? 94  THR   B CG2 1 
ATOM   3235 N  N   . TYR   B  1  82  ? -0.579  -2.516  59.490 1.00 35.70  ? 95  TYR   B N   1 
ATOM   3236 C  CA  . TYR   B  1  82  ? -1.369  -1.627  60.330 1.00 34.00  ? 95  TYR   B CA  1 
ATOM   3237 C  C   . TYR   B  1  82  ? -1.094  -1.934  61.802 1.00 34.18  ? 95  TYR   B C   1 
ATOM   3238 O  O   . TYR   B  1  82  ? -1.224  -1.052  62.636 1.00 37.25  ? 95  TYR   B O   1 
ATOM   3239 C  CB  . TYR   B  1  82  ? -2.854  -1.686  59.962 1.00 38.13  ? 95  TYR   B CB  1 
ATOM   3240 C  CG  . TYR   B  1  82  ? -3.170  -1.035  58.627 1.00 35.33  ? 95  TYR   B CG  1 
ATOM   3241 C  CD1 . TYR   B  1  82  ? -3.181  0.342   58.488 1.00 34.77  ? 95  TYR   B CD1 1 
ATOM   3242 C  CD2 . TYR   B  1  82  ? -3.447  -1.795  57.510 1.00 35.62  ? 95  TYR   B CD2 1 
ATOM   3243 C  CE1 . TYR   B  1  82  ? -3.450  0.942   57.271 1.00 33.30  ? 95  TYR   B CE1 1 
ATOM   3244 C  CE2 . TYR   B  1  82  ? -3.694  -1.213  56.275 1.00 37.19  ? 95  TYR   B CE2 1 
ATOM   3245 C  CZ  . TYR   B  1  82  ? -3.704  0.165   56.155 1.00 40.40  ? 95  TYR   B CZ  1 
ATOM   3246 O  OH  . TYR   B  1  82  ? -3.959  0.765   54.946 1.00 47.69  ? 95  TYR   B OH  1 
ATOM   3247 N  N   . LEU   B  1  83  ? -0.659  -3.151  62.133 1.00 34.98  ? 96  LEU   B N   1 
ATOM   3248 C  CA  . LEU   B  1  83  ? -0.135  -3.393  63.471 1.00 36.98  ? 96  LEU   B CA  1 
ATOM   3249 C  C   . LEU   B  1  83  ? 1.057   -2.470  63.714 1.00 37.96  ? 96  LEU   B C   1 
ATOM   3250 O  O   . LEU   B  1  83  ? 1.100   -1.752  64.716 1.00 33.60  ? 96  LEU   B O   1 
ATOM   3251 C  CB  . LEU   B  1  83  ? 0.262   -4.856  63.605 1.00 38.82  ? 96  LEU   B CB  1 
ATOM   3252 C  CG  . LEU   B  1  83  ? 0.971   -5.248  64.900 1.00 41.89  ? 96  LEU   B CG  1 
ATOM   3253 C  CD1 . LEU   B  1  83  ? 0.105   -4.993  66.132 1.00 44.04  ? 96  LEU   B CD1 1 
ATOM   3254 C  CD2 . LEU   B  1  83  ? 1.396   -6.707  64.828 1.00 42.64  ? 96  LEU   B CD2 1 
ATOM   3255 N  N   . GLY   B  1  84  ? 2.025   -2.502  62.789 1.00 34.96  ? 97  GLY   B N   1 
ATOM   3256 C  CA  . GLY   B  1  84  ? 3.212   -1.678  62.914 1.00 34.78  ? 97  GLY   B CA  1 
ATOM   3257 C  C   . GLY   B  1  84  ? 2.864   -0.190  62.955 1.00 31.73  ? 97  GLY   B C   1 
ATOM   3258 O  O   . GLY   B  1  84  ? 3.430   0.569   63.738 1.00 33.73  ? 97  GLY   B O   1 
ATOM   3259 N  N   . HIS   B  1  85  ? 1.916   0.216   62.116 1.00 30.52  ? 98  HIS   B N   1 
ATOM   3260 C  CA  . HIS   B  1  85  ? 1.552   1.623   62.017 1.00 35.70  ? 98  HIS   B CA  1 
ATOM   3261 C  C   . HIS   B  1  85  ? 0.771   2.115   63.245 1.00 35.75  ? 98  HIS   B C   1 
ATOM   3262 O  O   . HIS   B  1  85  ? 1.035   3.206   63.736 1.00 34.21  ? 98  HIS   B O   1 
ATOM   3263 C  CB  . HIS   B  1  85  ? 0.728   1.854   60.765 1.00 33.22  ? 98  HIS   B CB  1 
ATOM   3264 C  CG  . HIS   B  1  85  ? 0.450   3.277   60.470 1.00 36.00  ? 98  HIS   B CG  1 
ATOM   3265 N  ND1 . HIS   B  1  85  ? 1.447   4.221   60.407 1.00 39.60  ? 98  HIS   B ND1 1 
ATOM   3266 C  CD2 . HIS   B  1  85  ? -0.708  3.907   60.153 1.00 38.69  ? 98  HIS   B CD2 1 
ATOM   3267 C  CE1 . HIS   B  1  85  ? 0.909   5.385   60.092 1.00 42.04  ? 98  HIS   B CE1 1 
ATOM   3268 N  NE2 . HIS   B  1  85  ? -0.398  5.219   59.931 1.00 42.56  ? 98  HIS   B NE2 1 
ATOM   3269 N  N   . LEU   B  1  86  ? -0.187  1.324   63.730 1.00 34.28  ? 99  LEU   B N   1 
ATOM   3270 C  CA  . LEU   B  1  86  ? -0.984  1.722   64.884 1.00 36.27  ? 99  LEU   B CA  1 
ATOM   3271 C  C   . LEU   B  1  86  ? -0.086  1.956   66.090 1.00 33.16  ? 99  LEU   B C   1 
ATOM   3272 O  O   . LEU   B  1  86  ? -0.215  2.982   66.749 1.00 38.97  ? 99  LEU   B O   1 
ATOM   3273 C  CB  . LEU   B  1  86  ? -2.057  0.673   65.161 1.00 35.82  ? 99  LEU   B CB  1 
ATOM   3274 C  CG  . LEU   B  1  86  ? -3.276  0.733   64.226 1.00 36.47  ? 99  LEU   B CG  1 
ATOM   3275 C  CD1 . LEU   B  1  86  ? -4.097  -0.519  64.281 1.00 32.80  ? 99  LEU   B CD1 1 
ATOM   3276 C  CD2 . LEU   B  1  86  ? -4.147  1.910   64.587 1.00 37.61  ? 99  LEU   B CD2 1 
ATOM   3277 N  N   . LEU   B  1  87  ? 0.849   1.031   66.331 1.00 34.57  ? 100 LEU   B N   1 
ATOM   3278 C  CA  . LEU   B  1  87  ? 1.715   1.059   67.500 1.00 34.97  ? 100 LEU   B CA  1 
ATOM   3279 C  C   . LEU   B  1  87  ? 2.892   2.008   67.323 1.00 37.04  ? 100 LEU   B C   1 
ATOM   3280 O  O   . LEU   B  1  87  ? 3.326   2.609   68.303 1.00 38.63  ? 100 LEU   B O   1 
ATOM   3281 C  CB  . LEU   B  1  87  ? 2.217   -0.352  67.754 1.00 35.60  ? 100 LEU   B CB  1 
ATOM   3282 C  CG  . LEU   B  1  87  ? 1.142   -1.371  68.122 1.00 37.58  ? 100 LEU   B CG  1 
ATOM   3283 C  CD1 . LEU   B  1  87  ? 1.770   -2.737  68.250 1.00 42.24  ? 100 LEU   B CD1 1 
ATOM   3284 C  CD2 . LEU   B  1  87  ? 0.467   -0.999  69.429 1.00 41.25  ? 100 LEU   B CD2 1 
ATOM   3285 N  N   . ASN   B  1  88  ? 3.396   2.151   66.089 1.00 38.75  ? 101 ASN   B N   1 
ATOM   3286 C  CA  . ASN   B  1  88  ? 4.714   2.730   65.893 1.00 37.62  ? 101 ASN   B CA  1 
ATOM   3287 C  C   . ASN   B  1  88  ? 4.730   3.857   64.874 1.00 37.21  ? 101 ASN   B C   1 
ATOM   3288 O  O   . ASN   B  1  88  ? 5.781   4.451   64.656 1.00 38.39  ? 101 ASN   B O   1 
ATOM   3289 C  CB  . ASN   B  1  88  ? 5.707   1.669   65.442 1.00 37.08  ? 101 ASN   B CB  1 
ATOM   3290 C  CG  . ASN   B  1  88  ? 5.901   0.593   66.480 1.00 38.81  ? 101 ASN   B CG  1 
ATOM   3291 O  OD1 . ASN   B  1  88  ? 5.954   0.880   67.683 1.00 38.88  ? 101 ASN   B OD1 1 
ATOM   3292 N  ND2 . ASN   B  1  88  ? 6.021   -0.642  66.029 1.00 40.26  ? 101 ASN   B ND2 1 
ATOM   3293 N  N   . GLY   B  1  89  ? 3.594   4.127   64.223 1.00 35.90  ? 102 GLY   B N   1 
ATOM   3294 C  CA  . GLY   B  1  89  ? 3.564   5.101   63.143 1.00 35.51  ? 102 GLY   B CA  1 
ATOM   3295 C  C   . GLY   B  1  89  ? 2.930   6.412   63.598 1.00 38.34  ? 102 GLY   B C   1 
ATOM   3296 O  O   . GLY   B  1  89  ? 2.360   6.523   64.693 1.00 33.93  ? 102 GLY   B O   1 
ATOM   3297 N  N   . ASN   B  1  90  ? 3.038   7.411   62.735 1.00 38.23  ? 103 ASN   B N   1 
ATOM   3298 C  CA  . ASN   B  1  90  ? 2.390   8.682   62.968 1.00 39.12  ? 103 ASN   B CA  1 
ATOM   3299 C  C   . ASN   B  1  90  ? 1.068   8.654   62.222 1.00 39.42  ? 103 ASN   B C   1 
ATOM   3300 O  O   . ASN   B  1  90  ? 1.065   8.692   60.990 1.00 35.54  ? 103 ASN   B O   1 
ATOM   3301 C  CB  . ASN   B  1  90  ? 3.283   9.821   62.497 1.00 43.44  ? 103 ASN   B CB  1 
ATOM   3302 C  CG  . ASN   B  1  90  ? 2.717   11.167  62.863 1.00 44.17  ? 103 ASN   B CG  1 
ATOM   3303 O  OD1 . ASN   B  1  90  ? 1.520   11.417  62.684 1.00 43.47  ? 103 ASN   B OD1 1 
ATOM   3304 N  ND2 . ASN   B  1  90  ? 3.551   12.023  63.420 1.00 43.72  ? 103 ASN   B ND2 1 
ATOM   3305 N  N   . LEU   B  1  91  ? -0.046  8.622   62.968 1.00 42.41  ? 104 LEU   B N   1 
ATOM   3306 C  CA  . LEU   B  1  91  ? -1.347  8.374   62.363 1.00 43.24  ? 104 LEU   B CA  1 
ATOM   3307 C  C   . LEU   B  1  91  ? -1.885  9.638   61.705 1.00 40.76  ? 104 LEU   B C   1 
ATOM   3308 O  O   . LEU   B  1  91  ? -2.733  9.549   60.822 1.00 44.37  ? 104 LEU   B O   1 
ATOM   3309 C  CB  . LEU   B  1  91  ? -2.301  7.822   63.411 1.00 45.59  ? 104 LEU   B CB  1 
ATOM   3310 C  CG  . LEU   B  1  91  ? -1.833  6.515   64.060 1.00 50.10  ? 104 LEU   B CG  1 
ATOM   3311 C  CD1 . LEU   B  1  91  ? -2.552  6.229   65.356 1.00 60.33  ? 104 LEU   B CD1 1 
ATOM   3312 C  CD2 . LEU   B  1  91  ? -2.044  5.401   63.060 1.00 49.27  ? 104 LEU   B CD2 1 
ATOM   3313 N  N   . VAL   B  1  92  ? -1.354  10.798  62.083 1.00 41.93  ? 105 VAL   B N   1 
ATOM   3314 C  CA  . VAL   B  1  92  ? -1.794  12.060  61.506 1.00 43.79  ? 105 VAL   B CA  1 
ATOM   3315 C  C   . VAL   B  1  92  ? -1.134  12.264  60.144 1.00 42.95  ? 105 VAL   B C   1 
ATOM   3316 O  O   . VAL   B  1  92  ? -1.830  12.577  59.194 1.00 44.14  ? 105 VAL   B O   1 
ATOM   3317 C  CB  . VAL   B  1  92  ? -1.501  13.237  62.460 1.00 47.36  ? 105 VAL   B CB  1 
ATOM   3318 C  CG1 . VAL   B  1  92  ? -1.732  14.590  61.801 1.00 44.99  ? 105 VAL   B CG1 1 
ATOM   3319 C  CG2 . VAL   B  1  92  ? -2.290  13.112  63.755 1.00 52.13  ? 105 VAL   B CG2 1 
ATOM   3320 N  N   . THR   B  1  93  ? 0.189   12.061  60.034 1.00 47.03  ? 106 THR   B N   1 
ATOM   3321 C  CA  . THR   B  1  93  ? 0.880   12.218  58.754 1.00 46.48  ? 106 THR   B CA  1 
ATOM   3322 C  C   . THR   B  1  93  ? 0.780   10.957  57.900 1.00 43.50  ? 106 THR   B C   1 
ATOM   3323 O  O   . THR   B  1  93  ? 1.119   11.013  56.725 1.00 42.45  ? 106 THR   B O   1 
ATOM   3324 C  CB  . THR   B  1  93  ? 2.348   12.561  58.960 1.00 52.99  ? 106 THR   B CB  1 
ATOM   3325 O  OG1 . THR   B  1  93  ? 2.889   11.437  59.654 1.00 58.89  ? 106 THR   B OG1 1 
ATOM   3326 C  CG2 . THR   B  1  93  ? 2.518   13.858  59.732 1.00 57.56  ? 106 THR   B CG2 1 
ATOM   3327 N  N   . ASP   B  1  94  ? 0.363   9.830   58.501 1.00 36.59  ? 107 ASP   B N   1 
ATOM   3328 C  CA  . ASP   B  1  94  ? 0.227   8.562   57.805 1.00 38.36  ? 107 ASP   B CA  1 
ATOM   3329 C  C   . ASP   B  1  94  ? 1.595   8.007   57.379 1.00 38.63  ? 107 ASP   B C   1 
ATOM   3330 O  O   . ASP   B  1  94  ? 1.699   7.420   56.314 1.00 41.57  ? 107 ASP   B O   1 
ATOM   3331 C  CB  . ASP   B  1  94  ? -0.757  8.676   56.655 1.00 37.79  ? 107 ASP   B CB  1 
ATOM   3332 C  CG  . ASP   B  1  94  ? -1.336  7.356   56.152 1.00 43.68  ? 107 ASP   B CG  1 
ATOM   3333 O  OD1 . ASP   B  1  94  ? -1.742  6.525   57.014 1.00 43.58  ? 107 ASP   B OD1 1 
ATOM   3334 O  OD2 . ASP   B  1  94  ? -1.417  7.184   54.899 1.00 43.08  ? 107 ASP   B OD2 1 
ATOM   3335 N  N   . LEU   B  1  95  ? 2.630   8.166   58.211 1.00 33.53  ? 108 LEU   B N   1 
ATOM   3336 C  CA  . LEU   B  1  95  ? 3.970   7.726   57.883 1.00 35.72  ? 108 LEU   B CA  1 
ATOM   3337 C  C   . LEU   B  1  95  ? 4.523   6.867   59.015 1.00 35.95  ? 108 LEU   B C   1 
ATOM   3338 O  O   . LEU   B  1  95  ? 4.354   7.193   60.186 1.00 34.17  ? 108 LEU   B O   1 
ATOM   3339 C  CB  . LEU   B  1  95  ? 4.889   8.922   57.639 1.00 36.07  ? 108 LEU   B CB  1 
ATOM   3340 C  CG  . LEU   B  1  95  ? 4.544   9.829   56.458 1.00 37.44  ? 108 LEU   B CG  1 
ATOM   3341 C  CD1 . LEU   B  1  95  ? 5.425   11.069  56.571 1.00 40.24  ? 108 LEU   B CD1 1 
ATOM   3342 C  CD2 . LEU   B  1  95  ? 4.781   9.162   55.135 1.00 38.60  ? 108 LEU   B CD2 1 
ATOM   3343 N  N   . LEU   B  1  96  ? 5.238   5.797   58.631 1.00 34.82  ? 109 LEU   B N   1 
ATOM   3344 C  CA  . LEU   B  1  96  ? 5.861   4.859   59.546 1.00 33.51  ? 109 LEU   B CA  1 
ATOM   3345 C  C   . LEU   B  1  96  ? 7.326   4.707   59.165 1.00 34.09  ? 109 LEU   B C   1 
ATOM   3346 O  O   . LEU   B  1  96  ? 7.648   4.481   58.002 1.00 34.65  ? 109 LEU   B O   1 
ATOM   3347 C  CB  . LEU   B  1  96  ? 5.111   3.533   59.422 1.00 34.90  ? 109 LEU   B CB  1 
ATOM   3348 C  CG  . LEU   B  1  96  ? 5.762   2.311   60.069 1.00 35.87  ? 109 LEU   B CG  1 
ATOM   3349 C  CD1 . LEU   B  1  96  ? 5.891   2.501   61.556 1.00 34.94  ? 109 LEU   B CD1 1 
ATOM   3350 C  CD2 . LEU   B  1  96  ? 4.966   1.064   59.746 1.00 36.98  ? 109 LEU   B CD2 1 
ATOM   3351 N  N   . SER   B  1  97  ? 8.200   4.838   60.162 1.00 34.09  ? 110 SER   B N   1 
ATOM   3352 C  CA  . SER   B  1  97  ? 9.607   4.522   60.036 1.00 33.77  ? 110 SER   B CA  1 
ATOM   3353 C  C   . SER   B  1  97  ? 9.791   3.012   60.173 1.00 36.55  ? 110 SER   B C   1 
ATOM   3354 O  O   . SER   B  1  97  ? 9.315   2.406   61.133 1.00 36.05  ? 110 SER   B O   1 
ATOM   3355 C  CB  . SER   B  1  97  ? 10.403  5.227   61.099 1.00 33.73  ? 110 SER   B CB  1 
ATOM   3356 O  OG  . SER   B  1  97  ? 11.726  4.721   61.193 1.00 32.79  ? 110 SER   B OG  1 
ATOM   3357 N  N   . ILE   B  1  98  ? 10.535  2.415   59.241 1.00 34.94  ? 111 ILE   B N   1 
ATOM   3358 C  CA  . ILE   B  1  98  ? 10.774  0.986   59.297 1.00 33.35  ? 111 ILE   B CA  1 
ATOM   3359 C  C   . ILE   B  1  98  ? 11.903  0.708   60.277 1.00 31.68  ? 111 ILE   B C   1 
ATOM   3360 O  O   . ILE   B  1  98  ? 12.251  -0.448  60.477 1.00 34.30  ? 111 ILE   B O   1 
ATOM   3361 C  CB  . ILE   B  1  98  ? 11.048  0.380   57.913 1.00 31.28  ? 111 ILE   B CB  1 
ATOM   3362 C  CG1 . ILE   B  1  98  ? 12.379  0.804   57.347 1.00 29.23  ? 111 ILE   B CG1 1 
ATOM   3363 C  CG2 . ILE   B  1  98  ? 9.890   0.682   56.966 1.00 32.23  ? 111 ILE   B CG2 1 
ATOM   3364 C  CD1 . ILE   B  1  98  ? 12.726  0.144   56.035 1.00 32.54  ? 111 ILE   B CD1 1 
ATOM   3365 N  N   . GLY   B  1  99  ? 12.438  1.764   60.887 1.00 32.13  ? 112 GLY   B N   1 
ATOM   3366 C  CA  . GLY   B  1  99  ? 13.499  1.625   61.863 1.00 38.03  ? 112 GLY   B CA  1 
ATOM   3367 C  C   . GLY   B  1  99  ? 13.193  2.434   63.120 1.00 40.35  ? 112 GLY   B C   1 
ATOM   3368 O  O   . GLY   B  1  99  ? 12.234  2.145   63.836 1.00 38.81  ? 112 GLY   B O   1 
ATOM   3369 N  N   . GLY   B  1  100 ? 14.054  3.416   63.398 1.00 40.58  ? 113 GLY   B N   1 
ATOM   3370 C  CA  . GLY   B  1  100 ? 13.973  4.182   64.627 1.00 41.12  ? 113 GLY   B CA  1 
ATOM   3371 C  C   . GLY   B  1  100 ? 13.323  5.538   64.395 1.00 37.10  ? 113 GLY   B C   1 
ATOM   3372 O  O   . GLY   B  1  100 ? 12.762  5.799   63.337 1.00 34.32  ? 113 GLY   B O   1 
ATOM   3373 N  N   . ALA   B  1  101 ? 13.433  6.397   65.406 1.00 45.71  ? 114 ALA   B N   1 
ATOM   3374 C  CA  . ALA   B  1  101 ? 12.832  7.721   65.377 1.00 49.36  ? 114 ALA   B CA  1 
ATOM   3375 C  C   . ALA   B  1  101 ? 13.477  8.566   64.281 1.00 49.02  ? 114 ALA   B C   1 
ATOM   3376 O  O   . ALA   B  1  101 ? 14.670  8.444   64.013 1.00 49.31  ? 114 ALA   B O   1 
ATOM   3377 C  CB  . ALA   B  1  101 ? 12.965  8.382   66.738 1.00 52.19  ? 114 ALA   B CB  1 
ATOM   3378 N  N   . THR   B  1  102 ? 12.666  9.408   63.642 1.00 44.71  ? 115 THR   B N   1 
ATOM   3379 C  CA  . THR   B  1  102 ? 13.153  10.264  62.588 1.00 45.45  ? 115 THR   B CA  1 
ATOM   3380 C  C   . THR   B  1  102 ? 12.200  11.446  62.472 1.00 47.78  ? 115 THR   B C   1 
ATOM   3381 O  O   . THR   B  1  102 ? 10.998  11.275  62.592 1.00 46.62  ? 115 THR   B O   1 
ATOM   3382 C  CB  . THR   B  1  102 ? 13.273  9.495   61.267 1.00 43.07  ? 115 THR   B CB  1 
ATOM   3383 O  OG1 . THR   B  1  102 ? 13.601  10.398  60.212 1.00 39.14  ? 115 THR   B OG1 1 
ATOM   3384 C  CG2 . THR   B  1  102 ? 11.972  8.827   60.859 1.00 42.86  ? 115 THR   B CG2 1 
ATOM   3385 N  N   . PRO   B  1  103 ? 12.710  12.664  62.193 1.00 53.54  ? 116 PRO   B N   1 
ATOM   3386 C  CA  . PRO   B  1  103 ? 11.839  13.797  61.871 1.00 49.61  ? 116 PRO   B CA  1 
ATOM   3387 C  C   . PRO   B  1  103 ? 11.004  13.585  60.612 1.00 50.07  ? 116 PRO   B C   1 
ATOM   3388 O  O   . PRO   B  1  103 ? 9.998   14.260  60.423 1.00 54.71  ? 116 PRO   B O   1 
ATOM   3389 C  CB  . PRO   B  1  103 ? 12.788  15.006  61.706 1.00 50.71  ? 116 PRO   B CB  1 
ATOM   3390 C  CG  . PRO   B  1  103 ? 14.178  14.415  61.631 1.00 54.35  ? 116 PRO   B CG  1 
ATOM   3391 C  CD  . PRO   B  1  103 ? 14.146  13.002  62.188 1.00 51.98  ? 116 PRO   B CD  1 
ATOM   3392 N  N   . LYS   B  1  104 ? 11.413  12.648  59.749 1.00 48.53  ? 117 LYS   B N   1 
ATOM   3393 C  CA  . LYS   B  1  104 ? 10.723  12.398  58.493 1.00 46.80  ? 117 LYS   B CA  1 
ATOM   3394 C  C   . LYS   B  1  104 ? 9.294   11.874  58.695 1.00 45.60  ? 117 LYS   B C   1 
ATOM   3395 O  O   . LYS   B  1  104 ? 8.526   11.887  57.744 1.00 40.75  ? 117 LYS   B O   1 
ATOM   3396 C  CB  . LYS   B  1  104 ? 11.513  11.384  57.662 1.00 51.92  ? 117 LYS   B CB  1 
ATOM   3397 C  CG  . LYS   B  1  104 ? 12.841  11.862  57.103 1.00 56.10  ? 117 LYS   B CG  1 
ATOM   3398 C  CD  . LYS   B  1  104 ? 13.803  10.730  56.762 1.00 58.94  ? 117 LYS   B CD  1 
ATOM   3399 C  CE  . LYS   B  1  104 ? 15.071  11.241  56.140 1.00 58.85  ? 117 LYS   B CE  1 
ATOM   3400 N  NZ  . LYS   B  1  104 ? 14.873  11.771  54.791 1.00 54.35  ? 117 LYS   B NZ  1 
ATOM   3401 N  N   . THR   B  1  105 ? 8.918   11.394  59.894 1.00 47.38  ? 118 THR   B N   1 
ATOM   3402 C  CA  . THR   B  1  105 ? 7.535   10.975  60.108 1.00 47.68  ? 118 THR   B CA  1 
ATOM   3403 C  C   . THR   B  1  105 ? 6.674   12.175  60.491 1.00 52.51  ? 118 THR   B C   1 
ATOM   3404 O  O   . THR   B  1  105 ? 5.466   12.030  60.615 1.00 51.79  ? 118 THR   B O   1 
ATOM   3405 C  CB  . THR   B  1  105 ? 7.396   9.859   61.140 1.00 42.63  ? 118 THR   B CB  1 
ATOM   3406 O  OG1 . THR   B  1  105 ? 8.047   10.231  62.345 1.00 42.94  ? 118 THR   B OG1 1 
ATOM   3407 C  CG2 . THR   B  1  105 ? 8.034   8.570   60.676 1.00 47.20  ? 118 THR   B CG2 1 
ATOM   3408 N  N   . GLY   B  1  106 ? 7.301   13.345  60.682 1.00 61.92  ? 119 GLY   B N   1 
ATOM   3409 C  CA  . GLY   B  1  106 ? 6.590   14.592  60.936 1.00 60.13  ? 119 GLY   B CA  1 
ATOM   3410 C  C   . GLY   B  1  106 ? 6.487   14.913  62.428 1.00 59.83  ? 119 GLY   B C   1 
ATOM   3411 O  O   . GLY   B  1  106 ? 7.132   14.267  63.246 1.00 56.32  ? 119 GLY   B O   1 
ATOM   3412 N  N   . PRO   B  1  107 ? 5.656   15.919  62.808 1.00 71.14  ? 120 PRO   B N   1 
ATOM   3413 C  CA  . PRO   B  1  107 ? 5.446   16.304  64.213 1.00 70.23  ? 120 PRO   B CA  1 
ATOM   3414 C  C   . PRO   B  1  107 ? 5.041   15.171  65.154 1.00 60.34  ? 120 PRO   B C   1 
ATOM   3415 O  O   . PRO   B  1  107 ? 4.040   14.508  64.919 1.00 57.46  ? 120 PRO   B O   1 
ATOM   3416 C  CB  . PRO   B  1  107 ? 4.321   17.357  64.137 1.00 71.17  ? 120 PRO   B CB  1 
ATOM   3417 C  CG  . PRO   B  1  107 ? 4.411   17.911  62.727 1.00 76.59  ? 120 PRO   B CG  1 
ATOM   3418 C  CD  . PRO   B  1  107 ? 4.885   16.754  61.867 1.00 72.26  ? 120 PRO   B CD  1 
ATOM   3419 N  N   . PRO   B  1  108 ? 5.773   14.934  66.262 1.00 61.70  ? 121 PRO   B N   1 
ATOM   3420 C  CA  . PRO   B  1  108 ? 5.495   13.778  67.112 1.00 68.30  ? 121 PRO   B CA  1 
ATOM   3421 C  C   . PRO   B  1  108 ? 4.073   13.837  67.673 1.00 72.27  ? 121 PRO   B C   1 
ATOM   3422 O  O   . PRO   B  1  108 ? 3.503   14.912  67.845 1.00 63.91  ? 121 PRO   B O   1 
ATOM   3423 C  CB  . PRO   B  1  108 ? 6.583   13.810  68.207 1.00 72.10  ? 121 PRO   B CB  1 
ATOM   3424 C  CG  . PRO   B  1  108 ? 7.183   15.202  68.132 1.00 71.21  ? 121 PRO   B CG  1 
ATOM   3425 C  CD  . PRO   B  1  108 ? 6.886   15.765  66.748 1.00 69.17  ? 121 PRO   B CD  1 
ATOM   3426 N  N   . PRO   B  1  109 ? 3.435   12.676  67.933 1.00 71.80  ? 122 PRO   B N   1 
ATOM   3427 C  CA  . PRO   B  1  109 ? 2.135   12.651  68.595 1.00 70.28  ? 122 PRO   B CA  1 
ATOM   3428 C  C   . PRO   B  1  109 ? 2.262   12.951  70.088 1.00 69.93  ? 122 PRO   B C   1 
ATOM   3429 O  O   . PRO   B  1  109 ? 3.362   12.900  70.640 1.00 67.26  ? 122 PRO   B O   1 
ATOM   3430 C  CB  . PRO   B  1  109 ? 1.672   11.215  68.316 1.00 71.20  ? 122 PRO   B CB  1 
ATOM   3431 C  CG  . PRO   B  1  109 ? 2.956   10.407  68.307 1.00 70.73  ? 122 PRO   B CG  1 
ATOM   3432 C  CD  . PRO   B  1  109 ? 3.944   11.330  67.627 1.00 70.92  ? 122 PRO   B CD  1 
ATOM   3433 N  N   . PRO   B  1  110 ? 1.138   13.253  70.783 1.00 71.01  ? 123 PRO   B N   1 
ATOM   3434 C  CA  . PRO   B  1  110 ? 1.145   13.459  72.236 1.00 68.01  ? 123 PRO   B CA  1 
ATOM   3435 C  C   . PRO   B  1  110 ? 1.554   12.208  73.011 1.00 62.41  ? 123 PRO   B C   1 
ATOM   3436 O  O   . PRO   B  1  110 ? 1.041   11.123  72.753 1.00 55.99  ? 123 PRO   B O   1 
ATOM   3437 C  CB  . PRO   B  1  110 ? -0.304  13.873  72.555 1.00 69.50  ? 123 PRO   B CB  1 
ATOM   3438 C  CG  . PRO   B  1  110 ? -1.124  13.333  71.394 1.00 76.06  ? 123 PRO   B CG  1 
ATOM   3439 C  CD  . PRO   B  1  110 ? -0.200  13.421  70.188 1.00 75.91  ? 123 PRO   B CD  1 
ATOM   3440 N  N   . PRO   B  1  111 ? 2.518   12.294  73.956 1.00 63.99  ? 124 PRO   B N   1 
ATOM   3441 C  CA  . PRO   B  1  111 ? 2.886   11.128  74.769 1.00 68.46  ? 124 PRO   B CA  1 
ATOM   3442 C  C   . PRO   B  1  111 ? 1.636   10.618  75.478 1.00 61.75  ? 124 PRO   B C   1 
ATOM   3443 O  O   . PRO   B  1  111 ? 0.701   11.386  75.673 1.00 60.26  ? 124 PRO   B O   1 
ATOM   3444 C  CB  . PRO   B  1  111 ? 3.965   11.642  75.735 1.00 65.11  ? 124 PRO   B CB  1 
ATOM   3445 C  CG  . PRO   B  1  111 ? 4.531   12.858  75.002 1.00 65.85  ? 124 PRO   B CG  1 
ATOM   3446 C  CD  . PRO   B  1  111 ? 3.356   13.473  74.235 1.00 63.17  ? 124 PRO   B CD  1 
ATOM   3447 N  N   . PRO   B  1  112 ? 1.517   9.320   75.840 1.00 56.66  ? 125 PRO   B N   1 
ATOM   3448 C  CA  . PRO   B  1  112 ? 2.600   8.329   75.723 1.00 51.00  ? 125 PRO   B CA  1 
ATOM   3449 C  C   . PRO   B  1  112 ? 2.909   7.729   74.343 1.00 51.42  ? 125 PRO   B C   1 
ATOM   3450 O  O   . PRO   B  1  112 ? 3.785   6.869   74.215 1.00 52.00  ? 125 PRO   B O   1 
ATOM   3451 C  CB  . PRO   B  1  112 ? 2.119   7.218   76.707 1.00 51.31  ? 125 PRO   B CB  1 
ATOM   3452 C  CG  . PRO   B  1  112 ? 0.589   7.366   76.802 1.00 52.37  ? 125 PRO   B CG  1 
ATOM   3453 C  CD  . PRO   B  1  112 ? 0.245   8.763   76.332 1.00 54.04  ? 125 PRO   B CD  1 
ATOM   3454 N  N   . ALA   B  1  113 ? 2.166   8.147   73.311 1.00 48.38  ? 126 ALA   B N   1 
ATOM   3455 C  CA  . ALA   B  1  113 ? 2.425   7.703   71.953 1.00 48.70  ? 126 ALA   B CA  1 
ATOM   3456 C  C   . ALA   B  1  113 ? 3.720   8.337   71.444 1.00 50.02  ? 126 ALA   B C   1 
ATOM   3457 O  O   . ALA   B  1  113 ? 4.091   9.421   71.893 1.00 50.71  ? 126 ALA   B O   1 
ATOM   3458 C  CB  . ALA   B  1  113 ? 1.249   8.043   71.070 1.00 48.41  ? 126 ALA   B CB  1 
ATOM   3459 N  N   . HIS   B  1  114 ? 4.371   7.680   70.477 1.00 49.34  ? 127 HIS   B N   1 
ATOM   3460 C  CA  . HIS   B  1  114 ? 5.763   7.977   70.162 1.00 47.73  ? 127 HIS   B CA  1 
ATOM   3461 C  C   . HIS   B  1  114 ? 6.033   8.062   68.657 1.00 45.99  ? 127 HIS   B C   1 
ATOM   3462 O  O   . HIS   B  1  114 ? 6.876   8.846   68.246 1.00 53.88  ? 127 HIS   B O   1 
ATOM   3463 C  CB  . HIS   B  1  114 ? 6.663   6.954   70.862 1.00 45.83  ? 127 HIS   B CB  1 
ATOM   3464 C  CG  . HIS   B  1  114 ? 6.213   5.533   70.679 1.00 49.33  ? 127 HIS   B CG  1 
ATOM   3465 N  ND1 . HIS   B  1  114 ? 6.409   4.855   69.496 1.00 48.91  ? 127 HIS   B ND1 1 
ATOM   3466 C  CD2 . HIS   B  1  114 ? 5.574   4.672   71.485 1.00 49.65  ? 127 HIS   B CD2 1 
ATOM   3467 C  CE1 . HIS   B  1  114 ? 5.936   3.622   69.603 1.00 47.66  ? 127 HIS   B CE1 1 
ATOM   3468 N  NE2 . HIS   B  1  114 ? 5.415   3.482   70.800 1.00 48.18  ? 127 HIS   B NE2 1 
ATOM   3469 N  N   . ALA   B  1  115 ? 5.334   7.270   67.835 1.00 45.49  ? 128 ALA   B N   1 
ATOM   3470 C  CA  . ALA   B  1  115 ? 5.656   7.123   66.418 1.00 43.69  ? 128 ALA   B CA  1 
ATOM   3471 C  C   . ALA   B  1  115 ? 7.155   6.861   66.215 1.00 41.56  ? 128 ALA   B C   1 
ATOM   3472 O  O   . ALA   B  1  115 ? 7.788   7.442   65.342 1.00 39.29  ? 128 ALA   B O   1 
ATOM   3473 C  CB  . ALA   B  1  115 ? 5.202   8.342   65.647 1.00 46.55  ? 128 ALA   B CB  1 
ATOM   3474 N  N   . GLY   B  1  116 ? 7.702   5.936   67.003 1.00 42.60  ? 129 GLY   B N   1 
ATOM   3475 C  CA  . GLY   B  1  116 ? 9.140   5.756   67.110 1.00 43.94  ? 129 GLY   B CA  1 
ATOM   3476 C  C   . GLY   B  1  116 ? 9.672   4.684   66.153 1.00 41.89  ? 129 GLY   B C   1 
ATOM   3477 O  O   . GLY   B  1  116 ? 10.862  4.411   66.153 1.00 38.74  ? 129 GLY   B O   1 
ATOM   3478 N  N   . GLY   B  1  117 ? 8.771   4.062   65.380 1.00 38.48  ? 130 GLY   B N   1 
ATOM   3479 C  CA  . GLY   B  1  117 ? 9.149   3.160   64.307 1.00 38.94  ? 130 GLY   B CA  1 
ATOM   3480 C  C   . GLY   B  1  117 ? 9.186   1.710   64.773 1.00 36.96  ? 130 GLY   B C   1 
ATOM   3481 O  O   . GLY   B  1  117 ? 8.976   1.440   65.951 1.00 33.18  ? 130 GLY   B O   1 
ATOM   3482 N  N   . LEU   B  1  118 ? 9.527   0.801   63.847 1.00 35.64  ? 131 LEU   B N   1 
ATOM   3483 C  CA  . LEU   B  1  118 ? 9.503   -0.631  64.114 1.00 34.29  ? 131 LEU   B CA  1 
ATOM   3484 C  C   . LEU   B  1  118 ? 10.578  -1.053  65.109 1.00 34.12  ? 131 LEU   B C   1 
ATOM   3485 O  O   . LEU   B  1  118 ? 10.513  -2.168  65.607 1.00 41.18  ? 131 LEU   B O   1 
ATOM   3486 C  CB  . LEU   B  1  118 ? 9.657   -1.415  62.820 1.00 35.15  ? 131 LEU   B CB  1 
ATOM   3487 C  CG  . LEU   B  1  118 ? 8.577   -1.183  61.765 1.00 37.63  ? 131 LEU   B CG  1 
ATOM   3488 C  CD1 . LEU   B  1  118 ? 8.871   -2.053  60.557 1.00 37.69  ? 131 LEU   B CD1 1 
ATOM   3489 C  CD2 . LEU   B  1  118 ? 7.181   -1.400  62.310 1.00 39.01  ? 131 LEU   B CD2 1 
ATOM   3490 N  N   . ASN   B  1  119 ? 11.564  -0.197  65.379 1.00 35.05  ? 132 ASN   B N   1 
ATOM   3491 C  CA  . ASN   B  1  119 ? 12.584  -0.483  66.378 1.00 34.31  ? 132 ASN   B CA  1 
ATOM   3492 C  C   . ASN   B  1  119 ? 12.009  -0.522  67.786 1.00 35.95  ? 132 ASN   B C   1 
ATOM   3493 O  O   . ASN   B  1  119 ? 12.609  -1.156  68.644 1.00 34.88  ? 132 ASN   B O   1 
ATOM   3494 C  CB  . ASN   B  1  119 ? 13.699  0.552   66.412 1.00 35.80  ? 132 ASN   B CB  1 
ATOM   3495 C  CG  . ASN   B  1  119 ? 14.667  0.398   65.264 1.00 38.38  ? 132 ASN   B CG  1 
ATOM   3496 O  OD1 . ASN   B  1  119 ? 14.505  -0.484  64.420 1.00 42.39  ? 132 ASN   B OD1 1 
ATOM   3497 N  ND2 . ASN   B  1  119 ? 15.672  1.251   65.209 1.00 38.03  ? 132 ASN   B ND2 1 
ATOM   3498 N  N   . VAL   B  1  120 ? 10.869  0.137   68.045 1.00 35.37  ? 133 VAL   B N   1 
ATOM   3499 C  CA  . VAL   B  1  120 ? 10.346  0.206   69.405 1.00 37.83  ? 133 VAL   B CA  1 
ATOM   3500 C  C   . VAL   B  1  120 ? 10.032  -1.189  69.941 1.00 38.23  ? 133 VAL   B C   1 
ATOM   3501 O  O   . VAL   B  1  120 ? 9.239   -1.915  69.350 1.00 38.05  ? 133 VAL   B O   1 
ATOM   3502 C  CB  . VAL   B  1  120 ? 9.112   1.121   69.497 1.00 44.06  ? 133 VAL   B CB  1 
ATOM   3503 C  CG1 . VAL   B  1  120 ? 8.423   1.021   70.862 1.00 43.09  ? 133 VAL   B CG1 1 
ATOM   3504 C  CG2 . VAL   B  1  120 ? 9.462   2.569   69.156 1.00 43.28  ? 133 VAL   B CG2 1 
ATOM   3505 N  N   . HIS   B  1  121 ? 10.604  -1.505  71.113 1.00 40.22  ? 134 HIS   B N   1 
ATOM   3506 C  CA  . HIS   B  1  121 ? 10.565  -2.834  71.710 1.00 41.06  ? 134 HIS   B CA  1 
ATOM   3507 C  C   . HIS   B  1  121 ? 9.322   -3.021  72.573 1.00 41.68  ? 134 HIS   B C   1 
ATOM   3508 O  O   . HIS   B  1  121 ? 8.872   -2.084  73.227 1.00 39.83  ? 134 HIS   B O   1 
ATOM   3509 C  CB  . HIS   B  1  121 ? 11.787  -3.019  72.622 1.00 41.34  ? 134 HIS   B CB  1 
ATOM   3510 C  CG  . HIS   B  1  121 ? 11.796  -4.303  73.383 1.00 43.32  ? 134 HIS   B CG  1 
ATOM   3511 N  ND1 . HIS   B  1  121 ? 11.921  -5.533  72.769 1.00 42.69  ? 134 HIS   B ND1 1 
ATOM   3512 C  CD2 . HIS   B  1  121 ? 11.645  -4.552  74.698 1.00 41.75  ? 134 HIS   B CD2 1 
ATOM   3513 C  CE1 . HIS   B  1  121 ? 11.878  -6.489  73.694 1.00 43.20  ? 134 HIS   B CE1 1 
ATOM   3514 N  NE2 . HIS   B  1  121 ? 11.710  -5.913  74.867 1.00 43.90  ? 134 HIS   B NE2 1 
ATOM   3515 N  N   . GLY   B  1  122 ? 8.783   -4.247  72.599 1.00 49.70  ? 135 GLY   B N   1 
ATOM   3516 C  CA  . GLY   B  1  122 ? 7.986   -4.690  73.731 1.00 49.59  ? 135 GLY   B CA  1 
ATOM   3517 C  C   . GLY   B  1  122 ? 6.513   -4.957  73.416 1.00 47.93  ? 135 GLY   B C   1 
ATOM   3518 O  O   . GLY   B  1  122 ? 5.882   -5.669  74.183 1.00 47.29  ? 135 GLY   B O   1 
ATOM   3519 N  N   . THR   B  1  123 ? 5.955   -4.377  72.348 1.00 47.07  ? 136 THR   B N   1 
ATOM   3520 C  CA  . THR   B  1  123 ? 4.586   -4.697  71.964 1.00 52.49  ? 136 THR   B CA  1 
ATOM   3521 C  C   . THR   B  1  123 ? 4.570   -5.359  70.585 1.00 51.19  ? 136 THR   B C   1 
ATOM   3522 O  O   . THR   B  1  123 ? 3.836   -6.329  70.402 1.00 47.26  ? 136 THR   B O   1 
ATOM   3523 C  CB  . THR   B  1  123 ? 3.674   -3.471  71.991 1.00 57.75  ? 136 THR   B CB  1 
ATOM   3524 O  OG1 . THR   B  1  123 ? 3.903   -2.767  73.203 1.00 66.89  ? 136 THR   B OG1 1 
ATOM   3525 C  CG2 . THR   B  1  123 ? 2.208   -3.870  71.901 1.00 53.73  ? 136 THR   B CG2 1 
ATOM   3526 N  N   . PHE   B  1  124 ? 5.368   -4.845  69.624 1.00 46.76  ? 137 PHE   B N   1 
ATOM   3527 C  CA  . PHE   B  1  124 ? 5.540   -5.532  68.346 1.00 45.00  ? 137 PHE   B CA  1 
ATOM   3528 C  C   . PHE   B  1  124 ? 6.890   -6.257  68.289 1.00 44.32  ? 137 PHE   B C   1 
ATOM   3529 O  O   . PHE   B  1  124 ? 6.916   -7.481  68.475 1.00 44.91  ? 137 PHE   B O   1 
ATOM   3530 C  CB  . PHE   B  1  124 ? 5.351   -4.581  67.171 1.00 42.96  ? 137 PHE   B CB  1 
ATOM   3531 C  CG  . PHE   B  1  124 ? 5.202   -5.211  65.790 1.00 40.84  ? 137 PHE   B CG  1 
ATOM   3532 C  CD1 . PHE   B  1  124 ? 5.439   -6.561  65.557 1.00 41.61  ? 137 PHE   B CD1 1 
ATOM   3533 C  CD2 . PHE   B  1  124 ? 4.841   -4.424  64.705 1.00 40.19  ? 137 PHE   B CD2 1 
ATOM   3534 C  CE1 . PHE   B  1  124 ? 5.308   -7.099  64.281 1.00 42.68  ? 137 PHE   B CE1 1 
ATOM   3535 C  CE2 . PHE   B  1  124 ? 4.708   -4.965  63.433 1.00 39.67  ? 137 PHE   B CE2 1 
ATOM   3536 C  CZ  . PHE   B  1  124 ? 4.931   -6.302  63.224 1.00 39.57  ? 137 PHE   B CZ  1 
ATOM   3537 N  N   . GLU   B  1  125 ? 7.981   -5.527  67.988 1.00 37.87  ? 138 GLU   B N   1 
ATOM   3538 C  CA  . GLU   B  1  125 ? 9.322   -6.101  67.974 1.00 36.86  ? 138 GLU   B CA  1 
ATOM   3539 C  C   . GLU   B  1  125 ? 9.594   -6.780  69.317 1.00 35.29  ? 138 GLU   B C   1 
ATOM   3540 O  O   . GLU   B  1  125 ? 9.188   -6.282  70.367 1.00 42.88  ? 138 GLU   B O   1 
ATOM   3541 C  CB  . GLU   B  1  125 ? 10.350  -4.995  67.708 1.00 38.48  ? 138 GLU   B CB  1 
ATOM   3542 C  CG  . GLU   B  1  125 ? 11.796  -5.467  67.551 1.00 39.27  ? 138 GLU   B CG  1 
ATOM   3543 C  CD  . GLU   B  1  125 ? 12.525  -5.952  68.803 1.00 39.46  ? 138 GLU   B CD  1 
ATOM   3544 O  OE1 . GLU   B  1  125 ? 12.421  -5.265  69.843 1.00 43.21  ? 138 GLU   B OE1 1 
ATOM   3545 O  OE2 . GLU   B  1  125 ? 13.194  -7.018  68.743 1.00 43.34  ? 138 GLU   B OE2 1 
ATOM   3546 N  N   . GLY   B  1  126 ? 10.262  -7.932  69.280 1.00 35.30  ? 139 GLY   B N   1 
ATOM   3547 C  CA  . GLY   B  1  126 ? 10.614  -8.664  70.488 1.00 39.17  ? 139 GLY   B CA  1 
ATOM   3548 C  C   . GLY   B  1  126 ? 11.753  -9.666  70.270 1.00 37.39  ? 139 GLY   B C   1 
ATOM   3549 O  O   . GLY   B  1  126 ? 12.524  -9.556  69.319 1.00 37.62  ? 139 GLY   B O   1 
ATOM   3550 N  N   . ASP   B  1  127 ? 11.795  -10.673 71.143 1.00 37.52  ? 140 ASP   B N   1 
ATOM   3551 C  CA  . ASP   B  1  127 ? 13.015  -11.396 71.457 1.00 37.05  ? 140 ASP   B CA  1 
ATOM   3552 C  C   . ASP   B  1  127 ? 13.113  -12.710 70.673 1.00 36.18  ? 140 ASP   B C   1 
ATOM   3553 O  O   . ASP   B  1  127 ? 12.140  -13.199 70.115 1.00 37.54  ? 140 ASP   B O   1 
ATOM   3554 C  CB  . ASP   B  1  127 ? 13.093  -11.671 72.955 1.00 37.05  ? 140 ASP   B CB  1 
ATOM   3555 C  CG  . ASP   B  1  127 ? 13.049  -10.456 73.872 1.00 40.91  ? 140 ASP   B CG  1 
ATOM   3556 O  OD1 . ASP   B  1  127 ? 13.643  -9.412  73.511 1.00 44.47  ? 140 ASP   B OD1 1 
ATOM   3557 O  OD2 . ASP   B  1  127 ? 12.419  -10.555 74.954 1.00 50.99  ? 140 ASP   B OD2 1 
ATOM   3558 N  N   . ALA   B  1  128 ? 14.314  -13.296 70.668 1.00 33.91  ? 141 ALA   B N   1 
ATOM   3559 C  CA  . ALA   B  1  128 ? 14.549  -14.606 70.080 1.00 34.75  ? 141 ALA   B CA  1 
ATOM   3560 C  C   . ALA   B  1  128 ? 14.455  -14.543 68.554 1.00 32.18  ? 141 ALA   B C   1 
ATOM   3561 O  O   . ALA   B  1  128 ? 14.022  -15.484 67.892 1.00 38.23  ? 141 ALA   B O   1 
ATOM   3562 C  CB  . ALA   B  1  128 ? 13.586  -15.641 70.652 1.00 33.41  ? 141 ALA   B CB  1 
ATOM   3563 N  N   . GLY   B  1  129 ? 14.911  -13.446 67.974 1.00 30.12  ? 142 GLY   B N   1 
ATOM   3564 C  CA  . GLY   B  1  129 ? 14.993  -13.351 66.526 1.00 29.99  ? 142 GLY   B CA  1 
ATOM   3565 C  C   . GLY   B  1  129 ? 16.148  -14.182 65.989 1.00 31.20  ? 142 GLY   B C   1 
ATOM   3566 O  O   . GLY   B  1  129 ? 16.975  -14.670 66.759 1.00 30.23  ? 142 GLY   B O   1 
ATOM   3567 N  N   . MET   B  1  130 ? 16.199  -14.295 64.658 1.00 34.04  ? 143 MET   B N   1 
ATOM   3568 C  CA  . MET   B  1  130 ? 17.156  -15.134 63.964 1.00 33.28  ? 143 MET   B CA  1 
ATOM   3569 C  C   . MET   B  1  130 ? 18.497  -14.430 63.774 1.00 33.30  ? 143 MET   B C   1 
ATOM   3570 O  O   . MET   B  1  130 ? 19.537  -15.058 63.977 1.00 34.38  ? 143 MET   B O   1 
ATOM   3571 C  CB  . MET   B  1  130 ? 16.612  -15.548 62.597 1.00 37.25  ? 143 MET   B CB  1 
ATOM   3572 C  CG  . MET   B  1  130 ? 15.520  -16.617 62.669 1.00 45.01  ? 143 MET   B CG  1 
ATOM   3573 S  SD  . MET   B  1  130 ? 14.742  -17.036 61.089 1.00 43.76  ? 143 MET   B SD  1 
ATOM   3574 C  CE  . MET   B  1  130 ? 14.014  -15.457 60.632 1.00 39.33  ? 143 MET   B CE  1 
ATOM   3575 N  N   . THR   B  1  131 ? 18.474  -13.168 63.325 1.00 31.61  ? 144 THR   B N   1 
ATOM   3576 C  CA  . THR   B  1  131 ? 19.695  -12.445 62.994 1.00 30.93  ? 144 THR   B CA  1 
ATOM   3577 C  C   . THR   B  1  131 ? 19.794  -11.129 63.757 1.00 33.62  ? 144 THR   B C   1 
ATOM   3578 O  O   . THR   B  1  131 ? 20.744  -10.377 63.544 1.00 31.34  ? 144 THR   B O   1 
ATOM   3579 C  CB  . THR   B  1  131 ? 19.778  -12.194 61.489 1.00 31.89  ? 144 THR   B CB  1 
ATOM   3580 O  OG1 . THR   B  1  131 ? 18.831  -11.198 61.119 1.00 30.45  ? 144 THR   B OG1 1 
ATOM   3581 C  CG2 . THR   B  1  131 ? 19.523  -13.455 60.683 1.00 33.70  ? 144 THR   B CG2 1 
ATOM   3582 N  N   . ARG   B  1  132 ? 18.827  -10.845 64.636 1.00 34.60  ? 145 ARG   B N   1 
ATOM   3583 C  CA  . ARG   B  1  132 ? 18.883  -9.673  65.499 1.00 36.31  ? 145 ARG   B CA  1 
ATOM   3584 C  C   . ARG   B  1  132 ? 18.869  -10.129 66.955 1.00 34.56  ? 145 ARG   B C   1 
ATOM   3585 O  O   . ARG   B  1  132 ? 18.160  -11.078 67.285 1.00 34.82  ? 145 ARG   B O   1 
ATOM   3586 C  CB  . ARG   B  1  132 ? 17.711  -8.731  65.216 1.00 37.88  ? 145 ARG   B CB  1 
ATOM   3587 C  CG  . ARG   B  1  132 ? 17.927  -7.713  64.109 1.00 36.97  ? 145 ARG   B CG  1 
ATOM   3588 C  CD  . ARG   B  1  132 ? 17.962  -8.288  62.710 1.00 39.86  ? 145 ARG   B CD  1 
ATOM   3589 N  NE  . ARG   B  1  132 ? 18.288  -7.208  61.776 1.00 40.95  ? 145 ARG   B NE  1 
ATOM   3590 C  CZ  . ARG   B  1  132 ? 18.767  -7.353  60.548 1.00 44.74  ? 145 ARG   B CZ  1 
ATOM   3591 N  NH1 . ARG   B  1  132 ? 18.937  -8.569  60.027 1.00 40.11  ? 145 ARG   B NH1 1 
ATOM   3592 N  NH2 . ARG   B  1  132 ? 19.085  -6.273  59.848 1.00 46.07  ? 145 ARG   B NH2 1 
ATOM   3593 N  N   . ALA   B  1  133 ? 19.670  -9.455  67.792 1.00 34.58  ? 146 ALA   B N   1 
ATOM   3594 C  CA  . ALA   B  1  133 ? 19.799  -9.776  69.207 1.00 33.99  ? 146 ALA   B CA  1 
ATOM   3595 C  C   . ALA   B  1  133 ? 18.646  -9.126  69.976 1.00 32.71  ? 146 ALA   B C   1 
ATOM   3596 O  O   . ALA   B  1  133 ? 18.114  -8.091  69.563 1.00 25.75  ? 146 ALA   B O   1 
ATOM   3597 N  N   . ASP   B  1  134 ? 18.290  -9.738  71.116 1.00 34.86  ? 147 ASP   B N   1 
ATOM   3598 C  CA  . ASP   B  1  134 ? 17.289  -9.197  72.022 1.00 34.23  ? 147 ASP   B CA  1 
ATOM   3599 C  C   . ASP   B  1  134 ? 17.669  -7.775  72.420 1.00 35.60  ? 147 ASP   B C   1 
ATOM   3600 O  O   . ASP   B  1  134 ? 18.851  -7.475  72.566 1.00 38.05  ? 147 ASP   B O   1 
ATOM   3601 C  CB  . ASP   B  1  134 ? 17.095  -10.065 73.257 1.00 33.89  ? 147 ASP   B CB  1 
ATOM   3602 C  CG  . ASP   B  1  134 ? 16.618  -11.483 72.991 1.00 35.37  ? 147 ASP   B CG  1 
ATOM   3603 O  OD1 . ASP   B  1  134 ? 16.474  -11.843 71.802 1.00 35.79  ? 147 ASP   B OD1 1 
ATOM   3604 O  OD2 . ASP   B  1  134 ? 16.372  -12.214 73.970 1.00 37.47  ? 147 ASP   B OD2 1 
ATOM   3605 N  N   . GLU   B  1  135 ? 16.639  -6.935  72.630 1.00 39.46  ? 148 GLU   B N   1 
ATOM   3606 C  CA  . GLU   B  1  135 ? 16.800  -5.539  73.013 1.00 45.51  ? 148 GLU   B CA  1 
ATOM   3607 C  C   . GLU   B  1  135 ? 17.581  -5.389  74.320 1.00 44.03  ? 148 GLU   B C   1 
ATOM   3608 O  O   . GLU   B  1  135 ? 18.296  -4.406  74.492 1.00 48.56  ? 148 GLU   B O   1 
ATOM   3609 C  CB  . GLU   B  1  135 ? 15.422  -4.892  73.153 1.00 50.70  ? 148 GLU   B CB  1 
ATOM   3610 C  CG  . GLU   B  1  135 ? 15.451  -3.387  73.432 1.00 59.54  ? 148 GLU   B CG  1 
ATOM   3611 C  CD  . GLU   B  1  135 ? 15.447  -2.945  74.892 1.00 67.78  ? 148 GLU   B CD  1 
ATOM   3612 O  OE1 . GLU   B  1  135 ? 15.231  -3.777  75.806 1.00 69.54  ? 148 GLU   B OE1 1 
ATOM   3613 O  OE2 . GLU   B  1  135 ? 15.664  -1.728  75.104 1.00 73.12  ? 148 GLU   B OE2 1 
ATOM   3614 N  N   . PHE   B  1  136 ? 17.419  -6.341  75.244 1.00 44.89  ? 149 PHE   B N   1 
ATOM   3615 C  CA  . PHE   B  1  136 ? 18.123  -6.296  76.515 1.00 48.52  ? 149 PHE   B CA  1 
ATOM   3616 C  C   . PHE   B  1  136 ? 19.631  -6.118  76.306 1.00 49.27  ? 149 PHE   B C   1 
ATOM   3617 O  O   . PHE   B  1  136 ? 20.275  -5.465  77.113 1.00 45.91  ? 149 PHE   B O   1 
ATOM   3618 C  CB  . PHE   B  1  136 ? 17.847  -7.564  77.324 1.00 51.66  ? 149 PHE   B CB  1 
ATOM   3619 C  CG  . PHE   B  1  136 ? 18.649  -7.618  78.618 1.00 59.16  ? 149 PHE   B CG  1 
ATOM   3620 C  CD1 . PHE   B  1  136 ? 18.285  -6.819  79.705 1.00 57.75  ? 149 PHE   B CD1 1 
ATOM   3621 C  CD2 . PHE   B  1  136 ? 19.772  -8.438  78.732 1.00 55.89  ? 149 PHE   B CD2 1 
ATOM   3622 C  CE1 . PHE   B  1  136 ? 19.007  -6.855  80.881 1.00 54.46  ? 149 PHE   B CE1 1 
ATOM   3623 C  CE2 . PHE   B  1  136 ? 20.492  -8.471  79.916 1.00 57.47  ? 149 PHE   B CE2 1 
ATOM   3624 C  CZ  . PHE   B  1  136 ? 20.111  -7.678  80.983 1.00 57.14  ? 149 PHE   B CZ  1 
ATOM   3625 N  N   . PHE   B  1  137 ? 20.187  -6.687  75.229 1.00 45.15  ? 150 PHE   B N   1 
ATOM   3626 C  CA  . PHE   B  1  137 ? 21.623  -6.665  75.008 1.00 41.75  ? 150 PHE   B CA  1 
ATOM   3627 C  C   . PHE   B  1  137 ? 22.071  -5.373  74.326 1.00 36.57  ? 150 PHE   B C   1 
ATOM   3628 O  O   . PHE   B  1  137 ? 23.258  -5.220  74.087 1.00 38.59  ? 150 PHE   B O   1 
ATOM   3629 C  CB  . PHE   B  1  137 ? 22.022  -7.907  74.203 1.00 38.27  ? 150 PHE   B CB  1 
ATOM   3630 C  CG  . PHE   B  1  137 ? 21.621  -9.220  74.859 1.00 43.91  ? 150 PHE   B CG  1 
ATOM   3631 C  CD1 . PHE   B  1  137 ? 22.000  -9.505  76.164 1.00 49.42  ? 150 PHE   B CD1 1 
ATOM   3632 C  CD2 . PHE   B  1  137 ? 20.849  -10.160 74.186 1.00 44.34  ? 150 PHE   B CD2 1 
ATOM   3633 C  CE1 . PHE   B  1  137 ? 21.645  -10.714 76.754 1.00 53.57  ? 150 PHE   B CE1 1 
ATOM   3634 C  CE2 . PHE   B  1  137 ? 20.481  -11.352 74.787 1.00 45.07  ? 150 PHE   B CE2 1 
ATOM   3635 C  CZ  . PHE   B  1  137 ? 20.877  -11.633 76.061 1.00 48.93  ? 150 PHE   B CZ  1 
ATOM   3636 N  N   . GLY   B  1  138 ? 21.150  -4.469  73.973 1.00 37.42  ? 151 GLY   B N   1 
ATOM   3637 C  CA  . GLY   B  1  138 ? 21.531  -3.122  73.566 1.00 40.10  ? 151 GLY   B CA  1 
ATOM   3638 C  C   . GLY   B  1  138 ? 21.194  -2.745  72.115 1.00 42.94  ? 151 GLY   B C   1 
ATOM   3639 O  O   . GLY   B  1  138 ? 21.295  -1.571  71.766 1.00 41.72  ? 151 GLY   B O   1 
ATOM   3640 N  N   . ASP   B  1  139 ? 20.832  -3.706  71.255 1.00 41.55  ? 152 ASP   B N   1 
ATOM   3641 C  CA  . ASP   B  1  139 ? 20.617  -3.408  69.843 1.00 42.77  ? 152 ASP   B CA  1 
ATOM   3642 C  C   . ASP   B  1  139 ? 19.700  -4.471  69.237 1.00 39.70  ? 152 ASP   B C   1 
ATOM   3643 O  O   . ASP   B  1  139 ? 20.107  -5.624  69.002 1.00 37.05  ? 152 ASP   B O   1 
ATOM   3644 C  CB  . ASP   B  1  139 ? 21.935  -3.312  69.080 1.00 48.57  ? 152 ASP   B CB  1 
ATOM   3645 C  CG  . ASP   B  1  139 ? 21.833  -2.938  67.608 1.00 50.20  ? 152 ASP   B CG  1 
ATOM   3646 O  OD1 . ASP   B  1  139 ? 20.732  -3.023  67.067 1.00 51.00  ? 152 ASP   B OD1 1 
ATOM   3647 O  OD2 . ASP   B  1  139 ? 22.859  -2.539  67.022 1.00 53.48  ? 152 ASP   B OD2 1 
ATOM   3648 N  N   . ASN   B  1  140 ? 18.453  -4.059  68.988 1.00 32.50  ? 153 ASN   B N   1 
ATOM   3649 C  CA  . ASN   B  1  140 ? 17.418  -4.967  68.546 1.00 32.35  ? 153 ASN   B CA  1 
ATOM   3650 C  C   . ASN   B  1  140 ? 17.207  -4.872  67.036 1.00 34.74  ? 153 ASN   B C   1 
ATOM   3651 O  O   . ASN   B  1  140 ? 16.290  -5.517  66.525 1.00 38.05  ? 153 ASN   B O   1 
ATOM   3652 C  CB  . ASN   B  1  140 ? 16.115  -4.703  69.274 1.00 32.01  ? 153 ASN   B CB  1 
ATOM   3653 C  CG  . ASN   B  1  140 ? 15.499  -3.365  68.927 1.00 34.13  ? 153 ASN   B CG  1 
ATOM   3654 O  OD1 . ASN   B  1  140 ? 16.123  -2.509  68.293 1.00 35.99  ? 153 ASN   B OD1 1 
ATOM   3655 N  ND2 . ASN   B  1  140 ? 14.267  -3.152  69.355 1.00 36.70  ? 153 ASN   B ND2 1 
ATOM   3656 N  N   . HIS   B  1  141 ? 18.024  -4.068  66.337 1.00 33.22  ? 154 HIS   B N   1 
ATOM   3657 C  CA  . HIS   B  1  141 ? 17.743  -3.757  64.944 1.00 39.83  ? 154 HIS   B CA  1 
ATOM   3658 C  C   . HIS   B  1  141 ? 18.878  -4.172  63.997 1.00 35.69  ? 154 HIS   B C   1 
ATOM   3659 O  O   . HIS   B  1  141 ? 18.609  -4.501  62.849 1.00 35.62  ? 154 HIS   B O   1 
ATOM   3660 C  CB  . HIS   B  1  141 ? 17.337  -2.286  64.776 1.00 39.81  ? 154 HIS   B CB  1 
ATOM   3661 C  CG  . HIS   B  1  141 ? 18.364  -1.331  65.245 1.00 45.42  ? 154 HIS   B CG  1 
ATOM   3662 N  ND1 . HIS   B  1  141 ? 18.376  -0.844  66.530 1.00 49.80  ? 154 HIS   B ND1 1 
ATOM   3663 C  CD2 . HIS   B  1  141 ? 19.416  -0.774  64.623 1.00 53.39  ? 154 HIS   B CD2 1 
ATOM   3664 C  CE1 . HIS   B  1  141 ? 19.402  -0.021  66.676 1.00 50.98  ? 154 HIS   B CE1 1 
ATOM   3665 N  NE2 . HIS   B  1  141 ? 20.063  0.015   65.539 1.00 50.57  ? 154 HIS   B NE2 1 
ATOM   3666 N  N   . SER   B  1  142 ? 20.128  -4.125  64.455 1.00 34.04  ? 155 SER   B N   1 
ATOM   3667 C  CA  . SER   B  1  142 ? 21.280  -4.410  63.615 1.00 36.17  ? 155 SER   B CA  1 
ATOM   3668 C  C   . SER   B  1  142 ? 21.406  -5.904  63.342 1.00 36.14  ? 155 SER   B C   1 
ATOM   3669 O  O   . SER   B  1  142 ? 21.139  -6.734  64.206 1.00 34.90  ? 155 SER   B O   1 
ATOM   3670 C  CB  . SER   B  1  142 ? 22.569  -3.908  64.231 1.00 37.56  ? 155 SER   B CB  1 
ATOM   3671 O  OG  . SER   B  1  142 ? 22.638  -2.490  64.150 1.00 47.20  ? 155 SER   B OG  1 
ATOM   3672 N  N   . PHE   B  1  143 ? 21.914  -6.219  62.148 1.00 36.87  ? 156 PHE   B N   1 
ATOM   3673 C  CA  . PHE   B  1  143 ? 22.342  -7.567  61.839 1.00 33.50  ? 156 PHE   B CA  1 
ATOM   3674 C  C   . PHE   B  1  143 ? 23.446  -7.976  62.806 1.00 32.45  ? 156 PHE   B C   1 
ATOM   3675 O  O   . PHE   B  1  143 ? 24.324  -7.186  63.105 1.00 33.25  ? 156 PHE   B O   1 
ATOM   3676 C  CB  . PHE   B  1  143 ? 22.827  -7.615  60.394 1.00 35.47  ? 156 PHE   B CB  1 
ATOM   3677 C  CG  . PHE   B  1  143 ? 23.442  -8.944  60.007 1.00 32.16  ? 156 PHE   B CG  1 
ATOM   3678 C  CD1 . PHE   B  1  143 ? 22.638  -9.986  59.561 1.00 31.02  ? 156 PHE   B CD1 1 
ATOM   3679 C  CD2 . PHE   B  1  143 ? 24.811  -9.152  60.107 1.00 31.18  ? 156 PHE   B CD2 1 
ATOM   3680 C  CE1 . PHE   B  1  143 ? 23.180  -11.213 59.203 1.00 31.75  ? 156 PHE   B CE1 1 
ATOM   3681 C  CE2 . PHE   B  1  143 ? 25.354  -10.379 59.754 1.00 32.21  ? 156 PHE   B CE2 1 
ATOM   3682 C  CZ  . PHE   B  1  143 ? 24.530  -11.412 59.297 1.00 34.65  ? 156 PHE   B CZ  1 
ATOM   3683 N  N   . ASN   B  1  144 ? 23.392  -9.230  63.258 1.00 32.39  ? 157 ASN   B N   1 
ATOM   3684 C  CA  . ASN   B  1  144 ? 24.322  -9.773  64.227 1.00 31.61  ? 157 ASN   B CA  1 
ATOM   3685 C  C   . ASN   B  1  144 ? 24.967  -11.028 63.652 1.00 31.73  ? 157 ASN   B C   1 
ATOM   3686 O  O   . ASN   B  1  144 ? 24.314  -12.053 63.526 1.00 30.86  ? 157 ASN   B O   1 
ATOM   3687 C  CB  . ASN   B  1  144 ? 23.606  -10.004 65.550 1.00 33.74  ? 157 ASN   B CB  1 
ATOM   3688 C  CG  . ASN   B  1  144 ? 24.434  -10.671 66.622 1.00 35.49  ? 157 ASN   B CG  1 
ATOM   3689 O  OD1 . ASN   B  1  144 ? 25.046  -11.719 66.387 1.00 33.23  ? 157 ASN   B OD1 1 
ATOM   3690 N  ND2 . ASN   B  1  144 ? 24.446  -10.084 67.815 1.00 44.16  ? 157 ASN   B ND2 1 
ATOM   3691 N  N   . GLN   B  1  145 ? 26.276  -10.948 63.375 1.00 33.74  ? 158 GLN   B N   1 
ATOM   3692 C  CA  . GLN   B  1  145 ? 27.013  -11.994 62.683 1.00 33.62  ? 158 GLN   B CA  1 
ATOM   3693 C  C   . GLN   B  1  145 ? 27.029  -13.282 63.506 1.00 34.07  ? 158 GLN   B C   1 
ATOM   3694 O  O   . GLN   B  1  145 ? 26.936  -14.377 62.958 1.00 34.20  ? 158 GLN   B O   1 
ATOM   3695 C  CB  . GLN   B  1  145 ? 28.438  -11.515 62.355 1.00 33.14  ? 158 GLN   B CB  1 
ATOM   3696 C  CG  . GLN   B  1  145 ? 29.262  -12.463 61.483 1.00 31.14  ? 158 GLN   B CG  1 
ATOM   3697 C  CD  . GLN   B  1  145 ? 28.637  -12.786 60.132 1.00 35.21  ? 158 GLN   B CD  1 
ATOM   3698 O  OE1 . GLN   B  1  145 ? 28.310  -11.909 59.321 1.00 30.10  ? 158 GLN   B OE1 1 
ATOM   3699 N  NE2 . GLN   B  1  145 ? 28.471  -14.073 59.856 1.00 36.73  ? 158 GLN   B NE2 1 
ATOM   3700 N  N   . THR   B  1  146 ? 27.165  -13.161 64.827 1.00 34.83  ? 159 THR   B N   1 
ATOM   3701 C  CA  . THR   B  1  146 ? 27.199  -14.332 65.694 1.00 35.18  ? 159 THR   B CA  1 
ATOM   3702 C  C   . THR   B  1  146 ? 25.889  -15.111 65.571 1.00 35.31  ? 159 THR   B C   1 
ATOM   3703 O  O   . THR   B  1  146 ? 25.899  -16.341 65.569 1.00 36.68  ? 159 THR   B O   1 
ATOM   3704 C  CB  . THR   B  1  146 ? 27.422  -13.937 67.153 1.00 37.06  ? 159 THR   B CB  1 
ATOM   3705 O  OG1 . THR   B  1  146 ? 28.650  -13.231 67.253 1.00 40.75  ? 159 THR   B OG1 1 
ATOM   3706 C  CG2 . THR   B  1  146 ? 27.482  -15.129 68.088 1.00 35.91  ? 159 THR   B CG2 1 
ATOM   3707 N  N   . LEU   B  1  147 ? 24.761  -14.397 65.508 1.00 30.69  ? 160 LEU   B N   1 
ATOM   3708 C  CA  . LEU   B  1  147 ? 23.482  -15.065 65.347 1.00 31.42  ? 160 LEU   B CA  1 
ATOM   3709 C  C   . LEU   B  1  147 ? 23.343  -15.687 63.954 1.00 29.59  ? 160 LEU   B C   1 
ATOM   3710 O  O   . LEU   B  1  147 ? 22.797  -16.774 63.794 1.00 31.29  ? 160 LEU   B O   1 
ATOM   3711 C  CB  . LEU   B  1  147 ? 22.378  -14.066 65.671 1.00 33.04  ? 160 LEU   B CB  1 
ATOM   3712 C  CG  . LEU   B  1  147 ? 22.159  -13.759 67.157 1.00 34.62  ? 160 LEU   B CG  1 
ATOM   3713 C  CD1 . LEU   B  1  147 ? 20.955  -12.817 67.335 1.00 37.01  ? 160 LEU   B CD1 1 
ATOM   3714 C  CD2 . LEU   B  1  147 ? 21.930  -15.045 67.945 1.00 33.02  ? 160 LEU   B CD2 1 
ATOM   3715 N  N   . PHE   B  1  148 ? 23.845  -15.008 62.931 1.00 28.07  ? 161 PHE   B N   1 
ATOM   3716 C  CA  . PHE   B  1  148 ? 23.817  -15.553 61.590 1.00 27.00  ? 161 PHE   B CA  1 
ATOM   3717 C  C   . PHE   B  1  148 ? 24.712  -16.791 61.516 1.00 30.48  ? 161 PHE   B C   1 
ATOM   3718 O  O   . PHE   B  1  148 ? 24.385  -17.729 60.795 1.00 33.51  ? 161 PHE   B O   1 
ATOM   3719 C  CB  . PHE   B  1  148 ? 24.233  -14.497 60.561 1.00 29.04  ? 161 PHE   B CB  1 
ATOM   3720 C  CG  . PHE   B  1  148 ? 24.080  -14.990 59.136 1.00 27.70  ? 161 PHE   B CG  1 
ATOM   3721 C  CD1 . PHE   B  1  148 ? 22.818  -15.124 58.579 1.00 27.65  ? 161 PHE   B CD1 1 
ATOM   3722 C  CD2 . PHE   B  1  148 ? 25.183  -15.369 58.383 1.00 26.27  ? 161 PHE   B CD2 1 
ATOM   3723 C  CE1 . PHE   B  1  148 ? 22.668  -15.583 57.279 1.00 28.26  ? 161 PHE   B CE1 1 
ATOM   3724 C  CE2 . PHE   B  1  148 ? 25.025  -15.848 57.092 1.00 28.48  ? 161 PHE   B CE2 1 
ATOM   3725 C  CZ  . PHE   B  1  148 ? 23.771  -15.945 56.538 1.00 27.96  ? 161 PHE   B CZ  1 
ATOM   3726 N  N   . ASP   B  1  149 ? 25.826  -16.814 62.263 1.00 28.28  ? 162 ASP   B N   1 
ATOM   3727 C  CA  . ASP   B  1  149 ? 26.685  -17.989 62.292 1.00 31.33  ? 162 ASP   B CA  1 
ATOM   3728 C  C   . ASP   B  1  149 ? 25.904  -19.198 62.819 1.00 32.74  ? 162 ASP   B C   1 
ATOM   3729 O  O   . ASP   B  1  149 ? 26.103  -20.327 62.374 1.00 36.44  ? 162 ASP   B O   1 
ATOM   3730 C  CB  . ASP   B  1  149 ? 27.958  -17.728 63.085 1.00 35.36  ? 162 ASP   B CB  1 
ATOM   3731 C  CG  . ASP   B  1  149 ? 28.943  -16.738 62.469 1.00 42.60  ? 162 ASP   B CG  1 
ATOM   3732 O  OD1 . ASP   B  1  149 ? 28.919  -16.569 61.229 1.00 43.60  ? 162 ASP   B OD1 1 
ATOM   3733 O  OD2 . ASP   B  1  149 ? 29.723  -16.121 63.235 1.00 49.84  ? 162 ASP   B OD2 1 
ATOM   3734 N  N   . LYS   B  1  150 ? 25.035  -18.975 63.803 1.00 32.24  ? 163 LYS   B N   1 
ATOM   3735 C  CA  . LYS   B  1  150 ? 24.207  -20.039 64.350 1.00 31.92  ? 163 LYS   B CA  1 
ATOM   3736 C  C   . LYS   B  1  150 ? 23.155  -20.473 63.340 1.00 29.62  ? 163 LYS   B C   1 
ATOM   3737 O  O   . LYS   B  1  150 ? 22.851  -21.654 63.248 1.00 29.39  ? 163 LYS   B O   1 
ATOM   3738 C  CB  . LYS   B  1  150 ? 23.562  -19.569 65.650 1.00 33.47  ? 163 LYS   B CB  1 
ATOM   3739 C  CG  . LYS   B  1  150 ? 22.656  -20.581 66.298 1.00 38.12  ? 163 LYS   B CG  1 
ATOM   3740 C  CD  . LYS   B  1  150 ? 22.033  -20.013 67.563 1.00 44.64  ? 163 LYS   B CD  1 
ATOM   3741 C  CE  . LYS   B  1  150 ? 21.050  -20.954 68.207 1.00 48.27  ? 163 LYS   B CE  1 
ATOM   3742 N  NZ  . LYS   B  1  150 ? 21.559  -21.406 69.497 1.00 47.17  ? 163 LYS   B NZ  1 
ATOM   3743 N  N   . PHE   B  1  151 ? 22.609  -19.516 62.578 1.00 31.77  ? 164 PHE   B N   1 
ATOM   3744 C  CA  . PHE   B  1  151 ? 21.714  -19.833 61.476 1.00 32.61  ? 164 PHE   B CA  1 
ATOM   3745 C  C   . PHE   B  1  151 ? 22.409  -20.780 60.492 1.00 32.73  ? 164 PHE   B C   1 
ATOM   3746 O  O   . PHE   B  1  151 ? 21.830  -21.768 60.059 1.00 30.97  ? 164 PHE   B O   1 
ATOM   3747 C  CB  . PHE   B  1  151 ? 21.286  -18.515 60.828 1.00 31.94  ? 164 PHE   B CB  1 
ATOM   3748 C  CG  . PHE   B  1  151 ? 20.371  -18.627 59.618 1.00 31.49  ? 164 PHE   B CG  1 
ATOM   3749 C  CD1 . PHE   B  1  151 ? 20.892  -18.707 58.333 1.00 31.14  ? 164 PHE   B CD1 1 
ATOM   3750 C  CD2 . PHE   B  1  151 ? 18.994  -18.535 59.762 1.00 33.58  ? 164 PHE   B CD2 1 
ATOM   3751 C  CE1 . PHE   B  1  151 ? 20.051  -18.754 57.234 1.00 30.18  ? 164 PHE   B CE1 1 
ATOM   3752 C  CE2 . PHE   B  1  151 ? 18.154  -18.608 58.661 1.00 31.90  ? 164 PHE   B CE2 1 
ATOM   3753 C  CZ  . PHE   B  1  151 ? 18.679  -18.741 57.410 1.00 31.34  ? 164 PHE   B CZ  1 
ATOM   3754 N  N   . VAL   B  1  152 ? 23.667  -20.477 60.159 1.00 35.07  ? 165 VAL   B N   1 
ATOM   3755 C  CA  . VAL   B  1  152 ? 24.450  -21.273 59.226 1.00 33.42  ? 165 VAL   B CA  1 
ATOM   3756 C  C   . VAL   B  1  152 ? 24.678  -22.651 59.847 1.00 33.06  ? 165 VAL   B C   1 
ATOM   3757 O  O   . VAL   B  1  152 ? 24.502  -23.673 59.193 1.00 30.39  ? 165 VAL   B O   1 
ATOM   3758 C  CB  . VAL   B  1  152 ? 25.791  -20.578 58.881 1.00 30.86  ? 165 VAL   B CB  1 
ATOM   3759 C  CG1 . VAL   B  1  152 ? 26.772  -21.518 58.176 1.00 30.90  ? 165 VAL   B CG1 1 
ATOM   3760 C  CG2 . VAL   B  1  152 ? 25.592  -19.302 58.066 1.00 28.67  ? 165 VAL   B CG2 1 
ATOM   3761 N  N   . ASP   B  1  153 ? 25.063  -22.671 61.124 1.00 34.76  ? 166 ASP   B N   1 
ATOM   3762 C  CA  . ASP   B  1  153 ? 25.378  -23.919 61.806 1.00 35.80  ? 166 ASP   B CA  1 
ATOM   3763 C  C   . ASP   B  1  153 ? 24.165  -24.848 61.763 1.00 34.56  ? 166 ASP   B C   1 
ATOM   3764 O  O   . ASP   B  1  153 ? 24.293  -26.021 61.422 1.00 31.60  ? 166 ASP   B O   1 
ATOM   3765 C  CB  . ASP   B  1  153 ? 25.872  -23.672 63.226 1.00 37.16  ? 166 ASP   B CB  1 
ATOM   3766 C  CG  . ASP   B  1  153 ? 26.221  -24.914 64.041 1.00 39.47  ? 166 ASP   B CG  1 
ATOM   3767 O  OD1 . ASP   B  1  153 ? 27.010  -25.746 63.531 1.00 45.05  ? 166 ASP   B OD1 1 
ATOM   3768 O  OD2 . ASP   B  1  153 ? 25.718  -25.027 65.191 1.00 39.86  ? 166 ASP   B OD2 1 
ATOM   3769 N  N   . PHE   B  1  154 ? 22.991  -24.322 62.137 1.00 33.55  ? 167 PHE   B N   1 
ATOM   3770 C  CA  . PHE   B  1  154 ? 21.796  -25.138 62.179 1.00 31.09  ? 167 PHE   B CA  1 
ATOM   3771 C  C   . PHE   B  1  154 ? 21.405  -25.582 60.785 1.00 28.69  ? 167 PHE   B C   1 
ATOM   3772 O  O   . PHE   B  1  154 ? 20.854  -26.662 60.628 1.00 31.78  ? 167 PHE   B O   1 
ATOM   3773 C  CB  . PHE   B  1  154 ? 20.641  -24.412 62.866 1.00 33.09  ? 167 PHE   B CB  1 
ATOM   3774 C  CG  . PHE   B  1  154 ? 20.634  -24.617 64.374 1.00 33.71  ? 167 PHE   B CG  1 
ATOM   3775 C  CD1 . PHE   B  1  154 ? 21.679  -24.158 65.166 1.00 37.08  ? 167 PHE   B CD1 1 
ATOM   3776 C  CD2 . PHE   B  1  154 ? 19.587  -25.278 64.991 1.00 35.45  ? 167 PHE   B CD2 1 
ATOM   3777 C  CE1 . PHE   B  1  154 ? 21.662  -24.336 66.537 1.00 36.70  ? 167 PHE   B CE1 1 
ATOM   3778 C  CE2 . PHE   B  1  154 ? 19.575  -25.461 66.362 1.00 37.15  ? 167 PHE   B CE2 1 
ATOM   3779 C  CZ  . PHE   B  1  154 ? 20.615  -24.991 67.129 1.00 38.06  ? 167 PHE   B CZ  1 
ATOM   3780 N  N   . SER   B  1  155 ? 21.650  -24.753 59.773 1.00 31.88  ? 168 SER   B N   1 
ATOM   3781 C  CA  . SER   B  1  155 ? 21.372  -25.160 58.396 1.00 32.85  ? 168 SER   B CA  1 
ATOM   3782 C  C   . SER   B  1  155 ? 22.285  -26.320 57.997 1.00 32.09  ? 168 SER   B C   1 
ATOM   3783 O  O   . SER   B  1  155 ? 21.873  -27.240 57.302 1.00 35.18  ? 168 SER   B O   1 
ATOM   3784 C  CB  . SER   B  1  155 ? 21.501  -23.981 57.444 1.00 36.46  ? 168 SER   B CB  1 
ATOM   3785 O  OG  . SER   B  1  155 ? 20.604  -22.935 57.800 1.00 31.21  ? 168 SER   B OG  1 
ATOM   3786 N  N   . ASN   B  1  156 ? 23.548  -26.265 58.429 1.00 33.97  ? 169 ASN   B N   1 
ATOM   3787 C  CA  . ASN   B  1  156 ? 24.495  -27.340 58.170 1.00 32.94  ? 169 ASN   B CA  1 
ATOM   3788 C  C   . ASN   B  1  156 ? 24.022  -28.622 58.871 1.00 33.50  ? 169 ASN   B C   1 
ATOM   3789 O  O   . ASN   B  1  156 ? 24.093  -29.709 58.310 1.00 29.36  ? 169 ASN   B O   1 
ATOM   3790 C  CB  . ASN   B  1  156 ? 25.906  -27.002 58.644 1.00 31.53  ? 169 ASN   B CB  1 
ATOM   3791 C  CG  . ASN   B  1  156 ? 26.583  -25.901 57.867 1.00 34.50  ? 169 ASN   B CG  1 
ATOM   3792 O  OD1 . ASN   B  1  156 ? 26.252  -25.596 56.707 1.00 35.84  ? 169 ASN   B OD1 1 
ATOM   3793 N  ND2 . ASN   B  1  156 ? 27.568  -25.312 58.520 1.00 35.81  ? 169 ASN   B ND2 1 
ATOM   3794 N  N   . ARG   B  1  157 ? 23.542  -28.488 60.111 1.00 30.88  ? 170 ARG   B N   1 
ATOM   3795 C  CA  . ARG   B  1  157 ? 23.252  -29.630 60.955 1.00 30.89  ? 170 ARG   B CA  1 
ATOM   3796 C  C   . ARG   B  1  157 ? 21.932  -30.301 60.575 1.00 35.26  ? 170 ARG   B C   1 
ATOM   3797 O  O   . ARG   B  1  157 ? 21.817  -31.500 60.744 1.00 36.61  ? 170 ARG   B O   1 
ATOM   3798 C  CB  . ARG   B  1  157 ? 23.194  -29.203 62.426 1.00 29.62  ? 170 ARG   B CB  1 
ATOM   3799 C  CG  . ARG   B  1  157 ? 24.581  -29.052 63.012 1.00 33.84  ? 170 ARG   B CG  1 
ATOM   3800 C  CD  . ARG   B  1  157 ? 24.645  -28.190 64.261 1.00 37.25  ? 170 ARG   B CD  1 
ATOM   3801 N  NE  . ARG   B  1  157 ? 23.684  -28.658 65.259 1.00 39.20  ? 170 ARG   B NE  1 
ATOM   3802 C  CZ  . ARG   B  1  157 ? 23.499  -28.069 66.434 1.00 44.87  ? 170 ARG   B CZ  1 
ATOM   3803 N  NH1 . ARG   B  1  157 ? 22.625  -28.581 67.284 1.00 47.20  ? 170 ARG   B NH1 1 
ATOM   3804 N  NH2 . ARG   B  1  157 ? 24.174  -26.971 66.767 1.00 43.02  ? 170 ARG   B NH2 1 
ATOM   3805 N  N   . TYR   B  1  158 ? 20.939  -29.541 60.084 1.00 39.12  ? 171 TYR   B N   1 
ATOM   3806 C  CA  . TYR   B  1  158 ? 19.607  -30.084 59.861 1.00 35.76  ? 171 TYR   B CA  1 
ATOM   3807 C  C   . TYR   B  1  158 ? 19.102  -29.921 58.430 1.00 34.01  ? 171 TYR   B C   1 
ATOM   3808 O  O   . TYR   B  1  158 ? 18.070  -30.515 58.116 1.00 37.98  ? 171 TYR   B O   1 
ATOM   3809 C  CB  . TYR   B  1  158 ? 18.596  -29.437 60.813 1.00 36.24  ? 171 TYR   B CB  1 
ATOM   3810 C  CG  . TYR   B  1  158 ? 18.955  -29.665 62.271 1.00 35.99  ? 171 TYR   B CG  1 
ATOM   3811 C  CD1 . TYR   B  1  158 ? 18.791  -30.927 62.863 1.00 38.79  ? 171 TYR   B CD1 1 
ATOM   3812 C  CD2 . TYR   B  1  158 ? 19.508  -28.646 63.037 1.00 34.70  ? 171 TYR   B CD2 1 
ATOM   3813 C  CE1 . TYR   B  1  158 ? 19.157  -31.156 64.178 1.00 37.81  ? 171 TYR   B CE1 1 
ATOM   3814 C  CE2 . TYR   B  1  158 ? 19.866  -28.866 64.359 1.00 37.63  ? 171 TYR   B CE2 1 
ATOM   3815 C  CZ  . TYR   B  1  158 ? 19.691  -30.122 64.930 1.00 39.05  ? 171 TYR   B CZ  1 
ATOM   3816 O  OH  . TYR   B  1  158 ? 20.068  -30.328 66.226 1.00 39.20  ? 171 TYR   B OH  1 
ATOM   3817 N  N   . GLY   B  1  159 ? 19.791  -29.152 57.575 1.00 30.55  ? 172 GLY   B N   1 
ATOM   3818 C  CA  . GLY   B  1  159 ? 19.258  -28.824 56.262 1.00 29.03  ? 172 GLY   B CA  1 
ATOM   3819 C  C   . GLY   B  1  159 ? 20.242  -29.019 55.115 1.00 29.16  ? 172 GLY   B C   1 
ATOM   3820 O  O   . GLY   B  1  159 ? 20.047  -28.467 54.026 1.00 31.97  ? 172 GLY   B O   1 
ATOM   3821 N  N   . GLY   B  1  160 ? 21.278  -29.835 55.332 1.00 32.12  ? 173 GLY   B N   1 
ATOM   3822 C  CA  . GLY   B  1  160 ? 22.241  -30.130 54.285 1.00 32.98  ? 173 GLY   B CA  1 
ATOM   3823 C  C   . GLY   B  1  160 ? 22.990  -28.888 53.806 1.00 32.65  ? 173 GLY   B C   1 
ATOM   3824 O  O   . GLY   B  1  160 ? 23.454  -28.885 52.678 1.00 39.63  ? 173 GLY   B O   1 
ATOM   3825 N  N   . GLY   B  1  161 ? 23.070  -27.847 54.658 1.00 32.91  ? 174 GLY   B N   1 
ATOM   3826 C  CA  . GLY   B  1  161 ? 23.744  -26.598 54.341 1.00 32.95  ? 174 GLY   B CA  1 
ATOM   3827 C  C   . GLY   B  1  161 ? 22.789  -25.506 53.848 1.00 35.78  ? 174 GLY   B C   1 
ATOM   3828 O  O   . GLY   B  1  161 ? 23.225  -24.391 53.535 1.00 29.95  ? 174 GLY   B O   1 
ATOM   3829 N  N   . PHE   B  1  162 ? 21.488  -25.839 53.822 1.00 36.15  ? 175 PHE   B N   1 
ATOM   3830 C  CA  . PHE   B  1  162 ? 20.442  -24.939 53.374 1.00 34.40  ? 175 PHE   B CA  1 
ATOM   3831 C  C   . PHE   B  1  162 ? 19.435  -24.725 54.499 1.00 34.76  ? 175 PHE   B C   1 
ATOM   3832 O  O   . PHE   B  1  162 ? 19.298  -25.568 55.383 1.00 35.15  ? 175 PHE   B O   1 
ATOM   3833 C  CB  . PHE   B  1  162 ? 19.777  -25.541 52.137 1.00 34.16  ? 175 PHE   B CB  1 
ATOM   3834 C  CG  . PHE   B  1  162 ? 20.700  -25.658 50.938 1.00 34.38  ? 175 PHE   B CG  1 
ATOM   3835 C  CD1 . PHE   B  1  162 ? 20.855  -24.589 50.052 1.00 37.68  ? 175 PHE   B CD1 1 
ATOM   3836 C  CD2 . PHE   B  1  162 ? 21.438  -26.815 50.719 1.00 35.79  ? 175 PHE   B CD2 1 
ATOM   3837 C  CE1 . PHE   B  1  162 ? 21.709  -24.694 48.953 1.00 39.30  ? 175 PHE   B CE1 1 
ATOM   3838 C  CE2 . PHE   B  1  162 ? 22.297  -26.916 49.625 1.00 37.93  ? 175 PHE   B CE2 1 
ATOM   3839 C  CZ  . PHE   B  1  162 ? 22.443  -25.849 48.748 1.00 37.86  ? 175 PHE   B CZ  1 
ATOM   3840 N  N   . TYR   B  1  163 ? 18.751  -23.578 54.469 1.00 29.69  ? 176 TYR   B N   1 
ATOM   3841 C  CA  . TYR   B  1  163 ? 17.711  -23.315 55.432 1.00 28.62  ? 176 TYR   B CA  1 
ATOM   3842 C  C   . TYR   B  1  163 ? 16.413  -23.840 54.843 1.00 31.44  ? 176 TYR   B C   1 
ATOM   3843 O  O   . TYR   B  1  163 ? 16.018  -23.445 53.746 1.00 31.33  ? 176 TYR   B O   1 
ATOM   3844 C  CB  . TYR   B  1  163 ? 17.553  -21.832 55.749 1.00 30.22  ? 176 TYR   B CB  1 
ATOM   3845 C  CG  . TYR   B  1  163 ? 16.568  -21.500 56.856 1.00 30.44  ? 176 TYR   B CG  1 
ATOM   3846 C  CD1 . TYR   B  1  163 ? 16.907  -21.665 58.201 1.00 30.79  ? 176 TYR   B CD1 1 
ATOM   3847 C  CD2 . TYR   B  1  163 ? 15.316  -20.992 56.557 1.00 30.70  ? 176 TYR   B CD2 1 
ATOM   3848 C  CE1 . TYR   B  1  163 ? 16.027  -21.331 59.215 1.00 30.08  ? 176 TYR   B CE1 1 
ATOM   3849 C  CE2 . TYR   B  1  163 ? 14.430  -20.636 57.566 1.00 29.69  ? 176 TYR   B CE2 1 
ATOM   3850 C  CZ  . TYR   B  1  163 ? 14.782  -20.816 58.891 1.00 31.22  ? 176 TYR   B CZ  1 
ATOM   3851 O  OH  . TYR   B  1  163 ? 13.873  -20.482 59.844 1.00 29.52  ? 176 TYR   B OH  1 
ATOM   3852 N  N   . ASN   B  1  164 ? 15.783  -24.752 55.588 1.00 30.31  ? 177 ASN   B N   1 
ATOM   3853 C  CA  . ASN   B  1  164 ? 14.513  -25.321 55.191 1.00 34.50  ? 177 ASN   B CA  1 
ATOM   3854 C  C   . ASN   B  1  164 ? 13.666  -25.503 56.443 1.00 33.18  ? 177 ASN   B C   1 
ATOM   3855 O  O   . ASN   B  1  164 ? 14.064  -25.114 57.542 1.00 31.86  ? 177 ASN   B O   1 
ATOM   3856 C  CB  . ASN   B  1  164 ? 14.724  -26.581 54.355 1.00 37.61  ? 177 ASN   B CB  1 
ATOM   3857 C  CG  . ASN   B  1  164 ? 15.094  -27.806 55.162 1.00 37.81  ? 177 ASN   B CG  1 
ATOM   3858 O  OD1 . ASN   B  1  164 ? 15.140  -27.792 56.398 1.00 34.92  ? 177 ASN   B OD1 1 
ATOM   3859 N  ND2 . ASN   B  1  164 ? 15.320  -28.904 54.467 1.00 44.44  ? 177 ASN   B ND2 1 
ATOM   3860 N  N   . LEU   B  1  165 ? 12.496  -26.120 56.269 1.00 33.92  ? 178 LEU   B N   1 
ATOM   3861 C  CA  . LEU   B  1  165 ? 11.499  -26.107 57.323 1.00 35.41  ? 178 LEU   B CA  1 
ATOM   3862 C  C   . LEU   B  1  165 ? 11.963  -26.892 58.548 1.00 33.48  ? 178 LEU   B C   1 
ATOM   3863 O  O   . LEU   B  1  165 ? 11.630  -26.530 59.670 1.00 33.46  ? 178 LEU   B O   1 
ATOM   3864 C  CB  . LEU   B  1  165 ? 10.187  -26.614 56.732 1.00 43.24  ? 178 LEU   B CB  1 
ATOM   3865 C  CG  . LEU   B  1  165 ? 8.942   -26.413 57.603 1.00 48.05  ? 178 LEU   B CG  1 
ATOM   3866 C  CD1 . LEU   B  1  165 ? 8.584   -24.948 57.769 1.00 45.57  ? 178 LEU   B CD1 1 
ATOM   3867 C  CD2 . LEU   B  1  165 ? 7.777   -27.153 56.978 1.00 52.66  ? 178 LEU   B CD2 1 
ATOM   3868 N  N   . THR   B  1  166 ? 12.767  -27.944 58.349 1.00 33.78  ? 179 THR   B N   1 
ATOM   3869 C  CA  . THR   B  1  166 ? 13.317  -28.709 59.459 1.00 32.11  ? 179 THR   B CA  1 
ATOM   3870 C  C   . THR   B  1  166 ? 14.271  -27.832 60.279 1.00 35.02  ? 179 THR   B C   1 
ATOM   3871 O  O   . THR   B  1  166 ? 14.222  -27.814 61.503 1.00 33.97  ? 179 THR   B O   1 
ATOM   3872 C  CB  . THR   B  1  166 ? 14.032  -29.947 58.910 1.00 34.99  ? 179 THR   B CB  1 
ATOM   3873 O  OG1 . THR   B  1  166 ? 13.191  -30.598 57.957 1.00 36.74  ? 179 THR   B OG1 1 
ATOM   3874 C  CG2 . THR   B  1  166 ? 14.420  -30.923 60.006 1.00 32.51  ? 179 THR   B CG2 1 
ATOM   3875 N  N   . VAL   B  1  167 ? 15.146  -27.091 59.596 1.00 36.16  ? 180 VAL   B N   1 
ATOM   3876 C  CA  . VAL   B  1  167 ? 16.070  -26.174 60.245 1.00 33.71  ? 180 VAL   B CA  1 
ATOM   3877 C  C   . VAL   B  1  167 ? 15.278  -25.150 61.047 1.00 32.01  ? 180 VAL   B C   1 
ATOM   3878 O  O   . VAL   B  1  167 ? 15.640  -24.844 62.177 1.00 32.30  ? 180 VAL   B O   1 
ATOM   3879 C  CB  . VAL   B  1  167 ? 16.990  -25.430 59.253 1.00 33.90  ? 180 VAL   B CB  1 
ATOM   3880 C  CG1 . VAL   B  1  167 ? 18.026  -24.588 59.983 1.00 31.59  ? 180 VAL   B CG1 1 
ATOM   3881 C  CG2 . VAL   B  1  167 ? 17.654  -26.375 58.269 1.00 36.71  ? 180 VAL   B CG2 1 
ATOM   3882 N  N   . ALA   B  1  168 ? 14.230  -24.583 60.437 1.00 33.61  ? 181 ALA   B N   1 
ATOM   3883 C  CA  . ALA   B  1  168 ? 13.409  -23.570 61.093 1.00 34.49  ? 181 ALA   B CA  1 
ATOM   3884 C  C   . ALA   B  1  168 ? 12.911  -24.074 62.448 1.00 34.49  ? 181 ALA   B C   1 
ATOM   3885 O  O   . ALA   B  1  168 ? 13.026  -23.379 63.457 1.00 32.64  ? 181 ALA   B O   1 
ATOM   3886 C  CB  . ALA   B  1  168 ? 12.269  -23.150 60.196 1.00 35.12  ? 181 ALA   B CB  1 
ATOM   3887 N  N   . GLY   B  1  169 ? 12.393  -25.303 62.481 1.00 36.24  ? 182 GLY   B N   1 
ATOM   3888 C  CA  . GLY   B  1  169 ? 11.887  -25.863 63.730 1.00 36.98  ? 182 GLY   B CA  1 
ATOM   3889 C  C   . GLY   B  1  169 ? 12.957  -25.910 64.816 1.00 37.95  ? 182 GLY   B C   1 
ATOM   3890 O  O   . GLY   B  1  169 ? 12.707  -25.555 65.962 1.00 39.04  ? 182 GLY   B O   1 
ATOM   3891 N  N   . GLU   B  1  170 ? 14.163  -26.351 64.435 1.00 39.88  ? 183 GLU   B N   1 
ATOM   3892 C  CA  . GLU   B  1  170 ? 15.256  -26.488 65.381 1.00 36.20  ? 183 GLU   B CA  1 
ATOM   3893 C  C   . GLU   B  1  170 ? 15.756  -25.113 65.800 1.00 33.63  ? 183 GLU   B C   1 
ATOM   3894 O  O   . GLU   B  1  170 ? 15.956  -24.863 66.983 1.00 35.23  ? 183 GLU   B O   1 
ATOM   3895 C  CB  . GLU   B  1  170 ? 16.381  -27.320 64.768 1.00 45.14  ? 183 GLU   B CB  1 
ATOM   3896 C  CG  . GLU   B  1  170 ? 15.987  -28.758 64.443 1.00 46.88  ? 183 GLU   B CG  1 
ATOM   3897 C  CD  . GLU   B  1  170 ? 15.476  -29.527 65.647 1.00 55.15  ? 183 GLU   B CD  1 
ATOM   3898 O  OE1 . GLU   B  1  170 ? 16.040  -29.409 66.751 1.00 55.36  ? 183 GLU   B OE1 1 
ATOM   3899 O  OE2 . GLU   B  1  170 ? 14.468  -30.237 65.467 1.00 72.46  ? 183 GLU   B OE2 1 
ATOM   3900 N  N   . LEU   B  1  171 ? 15.960  -24.213 64.834 1.00 33.18  ? 184 LEU   B N   1 
ATOM   3901 C  CA  . LEU   B  1  171 ? 16.563  -22.932 65.152 1.00 33.74  ? 184 LEU   B CA  1 
ATOM   3902 C  C   . LEU   B  1  171 ? 15.635  -22.158 66.081 1.00 29.99  ? 184 LEU   B C   1 
ATOM   3903 O  O   . LEU   B  1  171 ? 16.082  -21.530 67.029 1.00 34.76  ? 184 LEU   B O   1 
ATOM   3904 C  CB  . LEU   B  1  171 ? 16.887  -22.148 63.878 1.00 34.95  ? 184 LEU   B CB  1 
ATOM   3905 C  CG  . LEU   B  1  171 ? 17.567  -20.794 64.085 1.00 34.30  ? 184 LEU   B CG  1 
ATOM   3906 C  CD1 . LEU   B  1  171 ? 18.904  -20.954 64.804 1.00 35.31  ? 184 LEU   B CD1 1 
ATOM   3907 C  CD2 . LEU   B  1  171 ? 17.738  -20.112 62.748 1.00 36.04  ? 184 LEU   B CD2 1 
ATOM   3908 N  N   . ARG   B  1  172 ? 14.332  -22.217 65.826 1.00 33.00  ? 185 ARG   B N   1 
ATOM   3909 C  CA  . ARG   B  1  172 ? 13.388  -21.374 66.553 1.00 34.85  ? 185 ARG   B CA  1 
ATOM   3910 C  C   . ARG   B  1  172 ? 13.444  -21.728 68.037 1.00 36.39  ? 185 ARG   B C   1 
ATOM   3911 O  O   . ARG   B  1  172 ? 13.546  -20.853 68.902 1.00 34.35  ? 185 ARG   B O   1 
ATOM   3912 C  CB  . ARG   B  1  172 ? 11.995  -21.524 65.926 1.00 35.49  ? 185 ARG   B CB  1 
ATOM   3913 C  CG  . ARG   B  1  172 ? 10.793  -21.199 66.799 1.00 37.10  ? 185 ARG   B CG  1 
ATOM   3914 C  CD  . ARG   B  1  172 ? 10.792  -19.822 67.440 1.00 37.30  ? 185 ARG   B CD  1 
ATOM   3915 N  NE  . ARG   B  1  172 ? 11.115  -18.734 66.510 1.00 37.45  ? 185 ARG   B NE  1 
ATOM   3916 C  CZ  . ARG   B  1  172 ? 11.958  -17.738 66.740 1.00 39.16  ? 185 ARG   B CZ  1 
ATOM   3917 N  NH1 . ARG   B  1  172 ? 12.649  -17.708 67.867 1.00 42.67  ? 185 ARG   B NH1 1 
ATOM   3918 N  NH2 . ARG   B  1  172 ? 12.100  -16.757 65.854 1.00 41.40  ? 185 ARG   B NH2 1 
ATOM   3919 N  N   . TYR   B  1  173 ? 13.397  -23.031 68.307 1.00 34.97  ? 186 TYR   B N   1 
ATOM   3920 C  CA  . TYR   B  1  173 ? 13.449  -23.542 69.663 1.00 39.13  ? 186 TYR   B CA  1 
ATOM   3921 C  C   . TYR   B  1  173 ? 14.771  -23.175 70.331 1.00 36.79  ? 186 TYR   B C   1 
ATOM   3922 O  O   . TYR   B  1  173 ? 14.800  -22.706 71.468 1.00 34.66  ? 186 TYR   B O   1 
ATOM   3923 C  CB  . TYR   B  1  173 ? 13.260  -25.059 69.603 1.00 42.63  ? 186 TYR   B CB  1 
ATOM   3924 C  CG  . TYR   B  1  173 ? 13.294  -25.691 70.978 1.00 45.70  ? 186 TYR   B CG  1 
ATOM   3925 C  CD1 . TYR   B  1  173 ? 12.274  -25.442 71.881 1.00 51.12  ? 186 TYR   B CD1 1 
ATOM   3926 C  CD2 . TYR   B  1  173 ? 14.319  -26.543 71.368 1.00 53.03  ? 186 TYR   B CD2 1 
ATOM   3927 C  CE1 . TYR   B  1  173 ? 12.276  -26.001 73.147 1.00 52.66  ? 186 TYR   B CE1 1 
ATOM   3928 C  CE2 . TYR   B  1  173 ? 14.330  -27.119 72.629 1.00 55.78  ? 186 TYR   B CE2 1 
ATOM   3929 C  CZ  . TYR   B  1  173 ? 13.304  -26.845 73.520 1.00 56.36  ? 186 TYR   B CZ  1 
ATOM   3930 O  OH  . TYR   B  1  173 ? 13.278  -27.378 74.775 1.00 56.99  ? 186 TYR   B OH  1 
ATOM   3931 N  N   . SER   B  1  174 ? 15.878  -23.412 69.625 1.00 35.89  ? 187 SER   B N   1 
ATOM   3932 C  CA  . SER   B  1  174 ? 17.186  -23.130 70.200 1.00 37.86  ? 187 SER   B CA  1 
ATOM   3933 C  C   . SER   B  1  174 ? 17.315  -21.652 70.563 1.00 38.23  ? 187 SER   B C   1 
ATOM   3934 O  O   . SER   B  1  174 ? 17.847  -21.340 71.630 1.00 37.54  ? 187 SER   B O   1 
ATOM   3935 C  CB  . SER   B  1  174 ? 18.288  -23.571 69.295 1.00 39.59  ? 187 SER   B CB  1 
ATOM   3936 O  OG  . SER   B  1  174 ? 19.542  -23.267 69.873 1.00 44.77  ? 187 SER   B OG  1 
ATOM   3937 N  N   . ARG   B  1  175 ? 16.795  -20.749 69.711 1.00 35.61  ? 188 ARG   B N   1 
ATOM   3938 C  CA  . ARG   B  1  175 ? 16.898  -19.314 69.972 1.00 35.96  ? 188 ARG   B CA  1 
ATOM   3939 C  C   . ARG   B  1  175 ? 16.079  -18.936 71.203 1.00 35.85  ? 188 ARG   B C   1 
ATOM   3940 O  O   . ARG   B  1  175 ? 16.463  -18.047 71.965 1.00 34.61  ? 188 ARG   B O   1 
ATOM   3941 C  CB  . ARG   B  1  175 ? 16.512  -18.454 68.759 1.00 35.31  ? 188 ARG   B CB  1 
ATOM   3942 C  CG  . ARG   B  1  175 ? 17.492  -18.555 67.598 1.00 33.18  ? 188 ARG   B CG  1 
ATOM   3943 C  CD  . ARG   B  1  175 ? 18.823  -17.893 67.917 1.00 34.16  ? 188 ARG   B CD  1 
ATOM   3944 N  NE  . ARG   B  1  175 ? 18.600  -16.461 68.115 1.00 34.23  ? 188 ARG   B NE  1 
ATOM   3945 C  CZ  . ARG   B  1  175 ? 18.747  -15.776 69.248 1.00 37.78  ? 188 ARG   B CZ  1 
ATOM   3946 N  NH1 . ARG   B  1  175 ? 19.315  -16.336 70.305 1.00 39.67  ? 188 ARG   B NH1 1 
ATOM   3947 N  NH2 . ARG   B  1  175 ? 18.363  -14.503 69.311 1.00 33.93  ? 188 ARG   B NH2 1 
ATOM   3948 N  N   . ILE   B  1  176 ? 14.949  -19.620 71.395 1.00 37.94  ? 189 ILE   B N   1 
ATOM   3949 C  CA  . ILE   B  1  176 ? 14.157  -19.432 72.596 1.00 36.76  ? 189 ILE   B CA  1 
ATOM   3950 C  C   . ILE   B  1  176 ? 14.998  -19.802 73.821 1.00 39.03  ? 189 ILE   B C   1 
ATOM   3951 O  O   . ILE   B  1  176 ? 15.108  -19.009 74.757 1.00 37.68  ? 189 ILE   B O   1 
ATOM   3952 C  CB  . ILE   B  1  176 ? 12.836  -20.218 72.511 1.00 37.20  ? 189 ILE   B CB  1 
ATOM   3953 C  CG1 . ILE   B  1  176 ? 11.889  -19.569 71.503 1.00 36.19  ? 189 ILE   B CG1 1 
ATOM   3954 C  CG2 . ILE   B  1  176 ? 12.174  -20.335 73.895 1.00 37.53  ? 189 ILE   B CG2 1 
ATOM   3955 C  CD1 . ILE   B  1  176 ? 10.751  -20.469 71.069 1.00 38.76  ? 189 ILE   B CD1 1 
ATOM   3956 N  N   . GLN   B  1  177 ? 15.631  -20.979 73.782 1.00 40.21  ? 190 GLN   B N   1 
ATOM   3957 C  CA  . GLN   B  1  177 ? 16.509  -21.420 74.861 1.00 43.72  ? 190 GLN   B CA  1 
ATOM   3958 C  C   . GLN   B  1  177 ? 17.650  -20.421 75.119 1.00 43.95  ? 190 GLN   B C   1 
ATOM   3959 O  O   . GLN   B  1  177 ? 17.910  -20.097 76.274 1.00 46.26  ? 190 GLN   B O   1 
ATOM   3960 C  CB  . GLN   B  1  177 ? 17.017  -22.839 74.605 1.00 48.65  ? 190 GLN   B CB  1 
ATOM   3961 C  CG  . GLN   B  1  177 ? 15.916  -23.895 74.544 1.00 55.95  ? 190 GLN   B CG  1 
ATOM   3962 C  CD  . GLN   B  1  177 ? 15.115  -24.022 75.827 1.00 73.79  ? 190 GLN   B CD  1 
ATOM   3963 O  OE1 . GLN   B  1  177 ? 15.544  -23.665 76.933 1.00 76.21  ? 190 GLN   B OE1 1 
ATOM   3964 N  NE2 . GLN   B  1  177 ? 13.927  -24.581 75.695 1.00 83.07  ? 190 GLN   B NE2 1 
ATOM   3965 N  N   . ASP   B  1  178 ? 18.320  -19.905 74.074 1.00 43.43  ? 191 ASP   B N   1 
ATOM   3966 C  CA  . ASP   B  1  178 ? 19.359  -18.895 74.262 1.00 44.82  ? 191 ASP   B CA  1 
ATOM   3967 C  C   . ASP   B  1  178 ? 18.837  -17.727 75.100 1.00 45.67  ? 191 ASP   B C   1 
ATOM   3968 O  O   . ASP   B  1  178 ? 19.528  -17.225 75.990 1.00 48.57  ? 191 ASP   B O   1 
ATOM   3969 C  CB  . ASP   B  1  178 ? 19.901  -18.330 72.956 1.00 45.91  ? 191 ASP   B CB  1 
ATOM   3970 C  CG  . ASP   B  1  178 ? 20.630  -19.310 72.041 1.00 55.25  ? 191 ASP   B CG  1 
ATOM   3971 O  OD1 . ASP   B  1  178 ? 21.028  -20.393 72.539 1.00 54.96  ? 191 ASP   B OD1 1 
ATOM   3972 O  OD2 . ASP   B  1  178 ? 20.796  -18.979 70.832 1.00 52.76  ? 191 ASP   B OD2 1 
ATOM   3973 N  N   . SER   B  1  179 ? 17.621  -17.271 74.791 1.00 39.53  ? 192 SER   B N   1 
ATOM   3974 C  CA  . SER   B  1  179 ? 17.074  -16.080 75.424 1.00 41.55  ? 192 SER   B CA  1 
ATOM   3975 C  C   . SER   B  1  179 ? 16.657  -16.380 76.868 1.00 39.12  ? 192 SER   B C   1 
ATOM   3976 O  O   . SER   B  1  179 ? 16.791  -15.528 77.738 1.00 35.70  ? 192 SER   B O   1 
ATOM   3977 C  CB  . SER   B  1  179 ? 15.929  -15.481 74.608 1.00 39.50  ? 192 SER   B CB  1 
ATOM   3978 O  OG  . SER   B  1  179 ? 16.416  -14.621 73.590 1.00 37.35  ? 192 SER   B OG  1 
ATOM   3979 N  N   . ILE   B  1  180 ? 16.127  -17.582 77.110 1.00 40.06  ? 193 ILE   B N   1 
ATOM   3980 C  CA  . ILE   B  1  180 ? 15.815  -18.016 78.461 1.00 43.59  ? 193 ILE   B CA  1 
ATOM   3981 C  C   . ILE   B  1  180 ? 17.080  -17.984 79.317 1.00 44.25  ? 193 ILE   B C   1 
ATOM   3982 O  O   . ILE   B  1  180 ? 17.059  -17.470 80.431 1.00 38.39  ? 193 ILE   B O   1 
ATOM   3983 C  CB  . ILE   B  1  180 ? 15.174  -19.412 78.458 1.00 46.77  ? 193 ILE   B CB  1 
ATOM   3984 C  CG1 . ILE   B  1  180 ? 13.750  -19.360 77.913 1.00 47.71  ? 193 ILE   B CG1 1 
ATOM   3985 C  CG2 . ILE   B  1  180 ? 15.219  -20.031 79.850 1.00 46.93  ? 193 ILE   B CG2 1 
ATOM   3986 C  CD1 . ILE   B  1  180 ? 13.104  -20.722 77.715 1.00 50.25  ? 193 ILE   B CD1 1 
ATOM   3987 N  N   . ALA   B  1  181 ? 18.180  -18.516 78.781 1.00 42.90  ? 194 ALA   B N   1 
ATOM   3988 C  CA  . ALA   B  1  181 ? 19.405  -18.695 79.541 1.00 41.80  ? 194 ALA   B CA  1 
ATOM   3989 C  C   . ALA   B  1  181 ? 20.129  -17.374 79.780 1.00 42.82  ? 194 ALA   B C   1 
ATOM   3990 O  O   . ALA   B  1  181 ? 20.883  -17.276 80.743 1.00 47.92  ? 194 ALA   B O   1 
ATOM   3991 C  CB  . ALA   B  1  181 ? 20.310  -19.681 78.835 1.00 39.87  ? 194 ALA   B CB  1 
ATOM   3992 N  N   . THR   B  1  182 ? 19.927  -16.360 78.924 1.00 40.37  ? 195 THR   B N   1 
ATOM   3993 C  CA  . THR   B  1  182 ? 20.843  -15.226 78.919 1.00 42.03  ? 195 THR   B CA  1 
ATOM   3994 C  C   . THR   B  1  182 ? 20.115  -13.899 79.109 1.00 45.04  ? 195 THR   B C   1 
ATOM   3995 O  O   . THR   B  1  182 ? 20.768  -12.883 79.337 1.00 42.60  ? 195 THR   B O   1 
ATOM   3996 C  CB  . THR   B  1  182 ? 21.663  -15.187 77.622 1.00 46.86  ? 195 THR   B CB  1 
ATOM   3997 O  OG1 . THR   B  1  182 ? 20.752  -15.048 76.533 1.00 49.29  ? 195 THR   B OG1 1 
ATOM   3998 C  CG2 . THR   B  1  182 ? 22.532  -16.418 77.412 1.00 47.10  ? 195 THR   B CG2 1 
ATOM   3999 N  N   . ASN   B  1  183 ? 18.785  -13.872 78.949 1.00 42.99  ? 196 ASN   B N   1 
ATOM   4000 C  CA  . ASN   B  1  183 ? 18.076  -12.603 78.928 1.00 42.56  ? 196 ASN   B CA  1 
ATOM   4001 C  C   . ASN   B  1  183 ? 17.066  -12.605 80.064 1.00 46.24  ? 196 ASN   B C   1 
ATOM   4002 O  O   . ASN   B  1  183 ? 16.011  -13.215 79.958 1.00 48.42  ? 196 ASN   B O   1 
ATOM   4003 C  CB  . ASN   B  1  183 ? 17.414  -12.326 77.583 1.00 42.73  ? 196 ASN   B CB  1 
ATOM   4004 C  CG  . ASN   B  1  183 ? 16.622  -11.028 77.555 1.00 40.56  ? 196 ASN   B CG  1 
ATOM   4005 O  OD1 . ASN   B  1  183 ? 16.576  -10.281 78.536 1.00 38.82  ? 196 ASN   B OD1 1 
ATOM   4006 N  ND2 . ASN   B  1  183 ? 15.970  -10.732 76.441 1.00 40.15  ? 196 ASN   B ND2 1 
ATOM   4007 N  N   . PRO   B  1  184 ? 17.352  -11.908 81.178 1.00 51.57  ? 197 PRO   B N   1 
ATOM   4008 C  CA  . PRO   B  1  184 ? 16.445  -11.913 82.328 1.00 58.25  ? 197 PRO   B CA  1 
ATOM   4009 C  C   . PRO   B  1  184 ? 15.116  -11.189 82.106 1.00 51.61  ? 197 PRO   B C   1 
ATOM   4010 O  O   . PRO   B  1  184 ? 14.193  -11.384 82.878 1.00 52.02  ? 197 PRO   B O   1 
ATOM   4011 C  CB  . PRO   B  1  184 ? 17.300  -11.228 83.400 1.00 57.16  ? 197 PRO   B CB  1 
ATOM   4012 C  CG  . PRO   B  1  184 ? 18.154  -10.254 82.602 1.00 57.28  ? 197 PRO   B CG  1 
ATOM   4013 C  CD  . PRO   B  1  184 ? 18.527  -11.044 81.364 1.00 52.28  ? 197 PRO   B CD  1 
ATOM   4014 N  N   . GLU   B  1  185 ? 15.021  -10.368 81.056 1.00 49.57  ? 198 GLU   B N   1 
ATOM   4015 C  CA  . GLU   B  1  185 ? 13.777  -9.688  80.716 1.00 50.29  ? 198 GLU   B CA  1 
ATOM   4016 C  C   . GLU   B  1  185 ? 13.068  -10.363 79.534 1.00 44.32  ? 198 GLU   B C   1 
ATOM   4017 O  O   . GLU   B  1  185 ? 12.126  -9.811  78.978 1.00 45.21  ? 198 GLU   B O   1 
ATOM   4018 C  CB  . GLU   B  1  185 ? 14.032  -8.221  80.352 1.00 55.17  ? 198 GLU   B CB  1 
ATOM   4019 C  CG  . GLU   B  1  185 ? 14.614  -7.351  81.465 1.00 54.43  ? 198 GLU   B CG  1 
ATOM   4020 C  CD  . GLU   B  1  185 ? 14.961  -5.934  81.015 1.00 61.69  ? 198 GLU   B CD  1 
ATOM   4021 O  OE1 . GLU   B  1  185 ? 14.620  -5.569  79.873 1.00 60.58  ? 198 GLU   B OE1 1 
ATOM   4022 O  OE2 . GLU   B  1  185 ? 15.601  -5.176  81.779 1.00 65.48  ? 198 GLU   B OE2 1 
ATOM   4023 N  N   . PHE   B  1  186 ? 13.509  -11.561 79.140 1.00 43.18  ? 199 PHE   B N   1 
ATOM   4024 C  CA  . PHE   B  1  186 ? 12.938  -12.275 78.006 1.00 41.74  ? 199 PHE   B CA  1 
ATOM   4025 C  C   . PHE   B  1  186 ? 11.420  -12.390 78.131 1.00 43.49  ? 199 PHE   B C   1 
ATOM   4026 O  O   . PHE   B  1  186 ? 10.917  -12.937 79.103 1.00 44.89  ? 199 PHE   B O   1 
ATOM   4027 C  CB  . PHE   B  1  186 ? 13.522  -13.688 77.926 1.00 41.26  ? 199 PHE   B CB  1 
ATOM   4028 C  CG  . PHE   B  1  186 ? 12.984  -14.558 76.801 1.00 36.45  ? 199 PHE   B CG  1 
ATOM   4029 C  CD1 . PHE   B  1  186 ? 12.852  -14.065 75.510 1.00 37.37  ? 199 PHE   B CD1 1 
ATOM   4030 C  CD2 . PHE   B  1  186 ? 12.610  -15.869 77.044 1.00 36.32  ? 199 PHE   B CD2 1 
ATOM   4031 C  CE1 . PHE   B  1  186 ? 12.370  -14.865 74.492 1.00 35.19  ? 199 PHE   B CE1 1 
ATOM   4032 C  CE2 . PHE   B  1  186 ? 12.110  -16.660 76.031 1.00 37.76  ? 199 PHE   B CE2 1 
ATOM   4033 C  CZ  . PHE   B  1  186 ? 12.005  -16.161 74.752 1.00 37.51  ? 199 PHE   B CZ  1 
ATOM   4034 N  N   . GLN   B  1  187 ? 10.717  -11.907 77.104 1.00 46.74  ? 200 GLN   B N   1 
ATOM   4035 C  CA  . GLN   B  1  187 ? 9.276   -12.054 76.953 1.00 45.70  ? 200 GLN   B CA  1 
ATOM   4036 C  C   . GLN   B  1  187 ? 8.989   -12.771 75.638 1.00 46.66  ? 200 GLN   B C   1 
ATOM   4037 O  O   . GLN   B  1  187 ? 9.591   -12.447 74.615 1.00 41.01  ? 200 GLN   B O   1 
ATOM   4038 C  CB  . GLN   B  1  187 ? 8.633   -10.670 76.900 1.00 47.96  ? 200 GLN   B CB  1 
ATOM   4039 C  CG  . GLN   B  1  187 ? 8.661   -9.911  78.224 1.00 53.48  ? 200 GLN   B CG  1 
ATOM   4040 C  CD  . GLN   B  1  187 ? 7.728   -10.527 79.245 1.00 55.21  ? 200 GLN   B CD  1 
ATOM   4041 O  OE1 . GLN   B  1  187 ? 6.505   -10.376 79.164 1.00 64.97  ? 200 GLN   B OE1 1 
ATOM   4042 N  NE2 . GLN   B  1  187 ? 8.295   -11.273 80.182 1.00 54.46  ? 200 GLN   B NE2 1 
ATOM   4043 N  N   . PHE   B  1  188 ? 8.089   -13.763 75.674 1.00 43.51  ? 201 PHE   B N   1 
ATOM   4044 C  CA  . PHE   B  1  188 ? 7.716   -14.480 74.465 1.00 37.38  ? 201 PHE   B CA  1 
ATOM   4045 C  C   . PHE   B  1  188 ? 6.214   -14.739 74.470 1.00 34.83  ? 201 PHE   B C   1 
ATOM   4046 O  O   . PHE   B  1  188 ? 5.779   -15.879 74.537 1.00 33.02  ? 201 PHE   B O   1 
ATOM   4047 C  CB  . PHE   B  1  188 ? 8.524   -15.773 74.388 1.00 33.30  ? 201 PHE   B CB  1 
ATOM   4048 C  CG  . PHE   B  1  188 ? 8.631   -16.329 72.979 1.00 35.23  ? 201 PHE   B CG  1 
ATOM   4049 C  CD1 . PHE   B  1  188 ? 9.382   -15.668 72.017 1.00 37.86  ? 201 PHE   B CD1 1 
ATOM   4050 C  CD2 . PHE   B  1  188 ? 8.036   -17.523 72.633 1.00 36.45  ? 201 PHE   B CD2 1 
ATOM   4051 C  CE1 . PHE   B  1  188 ? 9.469   -16.146 70.732 1.00 38.34  ? 201 PHE   B CE1 1 
ATOM   4052 C  CE2 . PHE   B  1  188 ? 8.146   -18.007 71.348 1.00 38.54  ? 201 PHE   B CE2 1 
ATOM   4053 C  CZ  . PHE   B  1  188 ? 8.857   -17.318 70.402 1.00 39.94  ? 201 PHE   B CZ  1 
ATOM   4054 N  N   . LYS   B  1  189 ? 5.429   -13.670 74.399 1.00 37.82  ? 202 LYS   B N   1 
ATOM   4055 C  CA  . LYS   B  1  189 ? 3.980   -13.783 74.522 1.00 44.07  ? 202 LYS   B CA  1 
ATOM   4056 C  C   . LYS   B  1  189 ? 3.272   -12.761 73.624 1.00 43.87  ? 202 LYS   B C   1 
ATOM   4057 O  O   . LYS   B  1  189 ? 3.895   -11.898 73.016 1.00 43.73  ? 202 LYS   B O   1 
ATOM   4058 C  CB  . LYS   B  1  189 ? 3.593   -13.591 75.990 1.00 41.72  ? 202 LYS   B CB  1 
ATOM   4059 C  CG  . LYS   B  1  189 ? 3.974   -12.236 76.548 1.00 46.68  ? 202 LYS   B CG  1 
ATOM   4060 C  CD  . LYS   B  1  189 ? 3.461   -11.955 77.961 1.00 53.66  ? 202 LYS   B CD  1 
ATOM   4061 C  CE  . LYS   B  1  189 ? 4.131   -12.780 78.994 1.00 57.41  ? 202 LYS   B CE  1 
ATOM   4062 N  NZ  . LYS   B  1  189 ? 3.726   -12.359 80.337 1.00 62.55  ? 202 LYS   B NZ  1 
ATOM   4063 N  N   . ASN   B  1  190 ? 1.949   -12.897 73.519 1.00 44.78  ? 203 ASN   B N   1 
ATOM   4064 C  CA  . ASN   B  1  190 ? 1.125   -11.958 72.782 1.00 43.20  ? 203 ASN   B CA  1 
ATOM   4065 C  C   . ASN   B  1  190 ? 1.627   -11.856 71.342 1.00 38.97  ? 203 ASN   B C   1 
ATOM   4066 O  O   . ASN   B  1  190 ? 1.733   -12.865 70.656 1.00 41.76  ? 203 ASN   B O   1 
ATOM   4067 C  CB  . ASN   B  1  190 ? 1.000   -10.655 73.569 1.00 45.07  ? 203 ASN   B CB  1 
ATOM   4068 C  CG  . ASN   B  1  190 ? 0.283   -10.894 74.882 1.00 49.53  ? 203 ASN   B CG  1 
ATOM   4069 O  OD1 . ASN   B  1  190 ? -0.708  -11.640 74.933 1.00 41.83  ? 203 ASN   B OD1 1 
ATOM   4070 N  ND2 . ASN   B  1  190 ? 0.784   -10.292 75.950 1.00 50.33  ? 203 ASN   B ND2 1 
ATOM   4071 N  N   . VAL   B  1  191 ? 1.919   -10.641 70.871 1.00 35.55  ? 204 VAL   B N   1 
ATOM   4072 C  CA  . VAL   B  1  191 ? 2.253   -10.440 69.482 1.00 35.36  ? 204 VAL   B CA  1 
ATOM   4073 C  C   . VAL   B  1  191 ? 3.493   -11.260 69.136 1.00 37.29  ? 204 VAL   B C   1 
ATOM   4074 O  O   . VAL   B  1  191 ? 3.541   -11.942 68.109 1.00 38.10  ? 204 VAL   B O   1 
ATOM   4075 C  CB  . VAL   B  1  191 ? 2.463   -8.950  69.169 1.00 40.26  ? 204 VAL   B CB  1 
ATOM   4076 C  CG1 . VAL   B  1  191 ? 2.990   -8.721  67.749 1.00 38.63  ? 204 VAL   B CG1 1 
ATOM   4077 C  CG2 . VAL   B  1  191 ? 1.202   -8.130  69.413 1.00 39.34  ? 204 VAL   B CG2 1 
ATOM   4078 N  N   . ARG   B  1  192 ? 4.504   -11.190 70.001 1.00 37.99  ? 205 ARG   B N   1 
ATOM   4079 C  CA  . ARG   B  1  192 ? 5.794   -11.766 69.675 1.00 35.95  ? 205 ARG   B CA  1 
ATOM   4080 C  C   . ARG   B  1  192 ? 5.686   -13.276 69.515 1.00 35.55  ? 205 ARG   B C   1 
ATOM   4081 O  O   . ARG   B  1  192 ? 6.349   -13.876 68.673 1.00 34.00  ? 205 ARG   B O   1 
ATOM   4082 C  CB  . ARG   B  1  192 ? 6.841   -11.429 70.736 1.00 39.57  ? 205 ARG   B CB  1 
ATOM   4083 C  CG  . ARG   B  1  192 ? 8.208   -12.005 70.389 1.00 44.54  ? 205 ARG   B CG  1 
ATOM   4084 C  CD  . ARG   B  1  192 ? 8.644   -11.637 68.987 1.00 38.09  ? 205 ARG   B CD  1 
ATOM   4085 N  NE  . ARG   B  1  192 ? 9.926   -12.238 68.631 1.00 38.29  ? 205 ARG   B NE  1 
ATOM   4086 C  CZ  . ARG   B  1  192 ? 10.381  -12.352 67.388 1.00 38.77  ? 205 ARG   B CZ  1 
ATOM   4087 N  NH1 . ARG   B  1  192 ? 9.654   -11.971 66.357 1.00 37.77  ? 205 ARG   B NH1 1 
ATOM   4088 N  NH2 . ARG   B  1  192 ? 11.563  -12.874 67.173 1.00 39.86  ? 205 ARG   B NH2 1 
ATOM   4089 N  N   . PHE   B  1  193 ? 4.846   -13.896 70.331 1.00 36.47  ? 206 PHE   B N   1 
ATOM   4090 C  CA  . PHE   B  1  193 ? 4.698   -15.335 70.267 1.00 37.40  ? 206 PHE   B CA  1 
ATOM   4091 C  C   . PHE   B  1  193 ? 4.166   -15.721 68.896 1.00 38.21  ? 206 PHE   B C   1 
ATOM   4092 O  O   . PHE   B  1  193 ? 4.628   -16.695 68.311 1.00 45.26  ? 206 PHE   B O   1 
ATOM   4093 C  CB  . PHE   B  1  193 ? 3.806   -15.863 71.388 1.00 36.56  ? 206 PHE   B CB  1 
ATOM   4094 C  CG  . PHE   B  1  193 ? 3.627   -17.364 71.296 1.00 38.16  ? 206 PHE   B CG  1 
ATOM   4095 C  CD1 . PHE   B  1  193 ? 4.605   -18.222 71.769 1.00 37.64  ? 206 PHE   B CD1 1 
ATOM   4096 C  CD2 . PHE   B  1  193 ? 2.479   -17.906 70.739 1.00 40.63  ? 206 PHE   B CD2 1 
ATOM   4097 C  CE1 . PHE   B  1  193 ? 4.439   -19.592 71.673 1.00 41.64  ? 206 PHE   B CE1 1 
ATOM   4098 C  CE2 . PHE   B  1  193 ? 2.305   -19.273 70.653 1.00 39.10  ? 206 PHE   B CE2 1 
ATOM   4099 C  CZ  . PHE   B  1  193 ? 3.289   -20.113 71.111 1.00 44.14  ? 206 PHE   B CZ  1 
ATOM   4100 N  N   . ILE   B  1  194 ? 3.223   -14.940 68.365 1.00 37.16  ? 207 ILE   B N   1 
ATOM   4101 C  CA  . ILE   B  1  194 ? 2.632   -15.274 67.081 1.00 34.56  ? 207 ILE   B CA  1 
ATOM   4102 C  C   . ILE   B  1  194 ? 3.612   -14.944 65.950 1.00 34.50  ? 207 ILE   B C   1 
ATOM   4103 O  O   . ILE   B  1  194 ? 3.836   -15.786 65.087 1.00 38.29  ? 207 ILE   B O   1 
ATOM   4104 C  CB  . ILE   B  1  194 ? 1.268   -14.578 66.928 1.00 36.16  ? 207 ILE   B CB  1 
ATOM   4105 C  CG1 . ILE   B  1  194 ? 0.305   -14.967 68.050 1.00 38.90  ? 207 ILE   B CG1 1 
ATOM   4106 C  CG2 . ILE   B  1  194 ? 0.664   -14.856 65.556 1.00 35.60  ? 207 ILE   B CG2 1 
ATOM   4107 C  CD1 . ILE   B  1  194 ? 0.068   -16.466 68.160 1.00 37.89  ? 207 ILE   B CD1 1 
ATOM   4108 N  N   . THR   B  1  195 ? 4.227   -13.751 65.972 1.00 33.74  ? 208 THR   B N   1 
ATOM   4109 C  CA  . THR   B  1  195 ? 5.062   -13.296 64.870 1.00 35.45  ? 208 THR   B CA  1 
ATOM   4110 C  C   . THR   B  1  195 ? 6.353   -14.109 64.780 1.00 36.86  ? 208 THR   B C   1 
ATOM   4111 O  O   . THR   B  1  195 ? 6.924   -14.223 63.701 1.00 39.68  ? 208 THR   B O   1 
ATOM   4112 C  CB  . THR   B  1  195 ? 5.364   -11.806 64.985 1.00 36.56  ? 208 THR   B CB  1 
ATOM   4113 O  OG1 . THR   B  1  195 ? 6.117   -11.539 66.166 1.00 42.37  ? 208 THR   B OG1 1 
ATOM   4114 C  CG2 . THR   B  1  195 ? 4.096   -10.974 64.928 1.00 40.61  ? 208 THR   B CG2 1 
ATOM   4115 N  N   . ALA   B  1  196 ? 6.808   -14.679 65.900 1.00 38.13  ? 209 ALA   B N   1 
ATOM   4116 C  CA  . ALA   B  1  196 ? 8.080   -15.383 65.943 1.00 37.91  ? 209 ALA   B CA  1 
ATOM   4117 C  C   . ALA   B  1  196 ? 8.050   -16.663 65.118 1.00 42.68  ? 209 ALA   B C   1 
ATOM   4118 O  O   . ALA   B  1  196 ? 9.088   -17.068 64.619 1.00 46.40  ? 209 ALA   B O   1 
ATOM   4119 C  CB  . ALA   B  1  196 ? 8.470   -15.701 67.355 1.00 36.09  ? 209 ALA   B CB  1 
ATOM   4120 N  N   . TYR   B  1  197 ? 6.876   -17.289 64.976 1.00 38.02  ? 210 TYR   B N   1 
ATOM   4121 C  CA  . TYR   B  1  197 ? 6.794   -18.514 64.214 1.00 37.03  ? 210 TYR   B CA  1 
ATOM   4122 C  C   . TYR   B  1  197 ? 6.703   -18.167 62.734 1.00 38.03  ? 210 TYR   B C   1 
ATOM   4123 O  O   . TYR   B  1  197 ? 7.394   -18.778 61.919 1.00 44.11  ? 210 TYR   B O   1 
ATOM   4124 C  CB  . TYR   B  1  197 ? 5.689   -19.407 64.775 1.00 35.69  ? 210 TYR   B CB  1 
ATOM   4125 C  CG  . TYR   B  1  197 ? 6.178   -20.037 66.066 1.00 34.98  ? 210 TYR   B CG  1 
ATOM   4126 C  CD1 . TYR   B  1  197 ? 6.910   -21.213 66.055 1.00 33.30  ? 210 TYR   B CD1 1 
ATOM   4127 C  CD2 . TYR   B  1  197 ? 5.994   -19.401 67.284 1.00 36.67  ? 210 TYR   B CD2 1 
ATOM   4128 C  CE1 . TYR   B  1  197 ? 7.413   -21.759 67.224 1.00 31.24  ? 210 TYR   B CE1 1 
ATOM   4129 C  CE2 . TYR   B  1  197 ? 6.498   -19.933 68.457 1.00 35.11  ? 210 TYR   B CE2 1 
ATOM   4130 C  CZ  . TYR   B  1  197 ? 7.210   -21.115 68.426 1.00 32.91  ? 210 TYR   B CZ  1 
ATOM   4131 O  OH  . TYR   B  1  197 ? 7.713   -21.617 69.596 1.00 40.04  ? 210 TYR   B OH  1 
ATOM   4132 N  N   . GLY   B  1  198 ? 5.885   -17.172 62.394 1.00 34.78  ? 211 GLY   B N   1 
ATOM   4133 C  CA  . GLY   B  1  198 ? 5.765   -16.721 61.017 1.00 33.79  ? 211 GLY   B CA  1 
ATOM   4134 C  C   . GLY   B  1  198 ? 7.101   -16.272 60.431 1.00 30.24  ? 211 GLY   B C   1 
ATOM   4135 O  O   . GLY   B  1  198 ? 7.417   -16.592 59.294 1.00 29.23  ? 211 GLY   B O   1 
ATOM   4136 N  N   . GLU   B  1  199 ? 7.900   -15.549 61.219 1.00 33.27  ? 212 GLU   B N   1 
ATOM   4137 C  CA  A GLU   B  1  199 ? 9.123   -14.972 60.694 0.50 33.47  ? 212 GLU   B CA  1 
ATOM   4138 C  CA  B GLU   B  1  199 ? 9.139   -14.966 60.730 0.50 33.55  ? 212 GLU   B CA  1 
ATOM   4139 C  C   . GLU   B  1  199 ? 10.103  -16.088 60.327 1.00 34.12  ? 212 GLU   B C   1 
ATOM   4140 O  O   . GLU   B  1  199 ? 10.960  -15.894 59.476 1.00 32.31  ? 212 GLU   B O   1 
ATOM   4141 C  CB  A GLU   B  1  199 ? 9.646   -13.879 61.622 0.50 32.81  ? 212 GLU   B CB  1 
ATOM   4142 C  CB  B GLU   B  1  199 ? 9.726   -13.975 61.751 0.50 33.14  ? 212 GLU   B CB  1 
ATOM   4143 C  CG  A GLU   B  1  199 ? 8.830   -12.594 61.524 0.50 32.19  ? 212 GLU   B CG  1 
ATOM   4144 C  CG  B GLU   B  1  199 ? 10.465  -14.615 62.935 0.50 32.70  ? 212 GLU   B CG  1 
ATOM   4145 C  CD  A GLU   B  1  199 ? 8.944   -11.676 62.718 0.50 32.64  ? 212 GLU   B CD  1 
ATOM   4146 C  CD  B GLU   B  1  199 ? 11.233  -13.721 63.916 0.50 27.84  ? 212 GLU   B CD  1 
ATOM   4147 O  OE1 A GLU   B  1  199 ? 9.823   -11.940 63.556 0.50 31.11  ? 212 GLU   B OE1 1 
ATOM   4148 O  OE1 B GLU   B  1  199 ? 11.100  -12.493 63.929 0.50 25.60  ? 212 GLU   B OE1 1 
ATOM   4149 O  OE2 A GLU   B  1  199 ? 8.136   -10.726 62.812 0.50 38.24  ? 212 GLU   B OE2 1 
ATOM   4150 O  OE2 B GLU   B  1  199 ? 12.015  -14.271 64.697 0.50 27.91  ? 212 GLU   B OE2 1 
ATOM   4151 N  N   . THR   B  1  200 ? 9.955   -17.273 60.931 1.00 34.95  ? 213 THR   B N   1 
ATOM   4152 C  CA  . THR   B  1  200 ? 10.926  -18.326 60.685 1.00 37.37  ? 213 THR   B CA  1 
ATOM   4153 C  C   . THR   B  1  200 ? 10.626  -19.033 59.372 1.00 33.17  ? 213 THR   B C   1 
ATOM   4154 O  O   . THR   B  1  200 ? 11.518  -19.706 58.852 1.00 35.36  ? 213 THR   B O   1 
ATOM   4155 C  CB  . THR   B  1  200 ? 11.043  -19.332 61.833 1.00 42.35  ? 213 THR   B CB  1 
ATOM   4156 O  OG1 . THR   B  1  200 ? 9.902   -20.180 61.857 1.00 47.44  ? 213 THR   B OG1 1 
ATOM   4157 C  CG2 . THR   B  1  200 ? 11.213  -18.660 63.177 1.00 41.00  ? 213 THR   B CG2 1 
ATOM   4158 N  N   . VAL   B  1  201 ? 9.403   -18.881 58.836 1.00 30.91  ? 214 VAL   B N   1 
ATOM   4159 C  CA  . VAL   B  1  201 ? 9.089   -19.497 57.557 1.00 31.40  ? 214 VAL   B CA  1 
ATOM   4160 C  C   . VAL   B  1  201 ? 9.125   -18.478 56.413 1.00 31.64  ? 214 VAL   B C   1 
ATOM   4161 O  O   . VAL   B  1  201 ? 9.179   -18.873 55.249 1.00 34.72  ? 214 VAL   B O   1 
ATOM   4162 C  CB  . VAL   B  1  201 ? 7.771   -20.288 57.579 1.00 32.59  ? 214 VAL   B CB  1 
ATOM   4163 C  CG1 . VAL   B  1  201 ? 7.860   -21.433 58.574 1.00 31.82  ? 214 VAL   B CG1 1 
ATOM   4164 C  CG2 . VAL   B  1  201 ? 6.547   -19.419 57.846 1.00 34.69  ? 214 VAL   B CG2 1 
ATOM   4165 N  N   . PHE   B  1  202 ? 9.124   -17.181 56.712 1.00 31.85  ? 215 PHE   B N   1 
ATOM   4166 C  CA  . PHE   B  1  202 ? 9.212   -16.181 55.658 1.00 32.85  ? 215 PHE   B CA  1 
ATOM   4167 C  C   . PHE   B  1  202 ? 10.424  -16.441 54.762 1.00 30.77  ? 215 PHE   B C   1 
ATOM   4168 O  O   . PHE   B  1  202 ? 10.325  -16.345 53.534 1.00 30.44  ? 215 PHE   B O   1 
ATOM   4169 C  CB  . PHE   B  1  202 ? 9.198   -14.753 56.211 1.00 31.20  ? 215 PHE   B CB  1 
ATOM   4170 C  CG  . PHE   B  1  202 ? 7.872   -14.308 56.816 1.00 32.04  ? 215 PHE   B CG  1 
ATOM   4171 C  CD1 . PHE   B  1  202 ? 6.696   -15.026 56.624 1.00 37.50  ? 215 PHE   B CD1 1 
ATOM   4172 C  CD2 . PHE   B  1  202 ? 7.796   -13.143 57.559 1.00 34.99  ? 215 PHE   B CD2 1 
ATOM   4173 C  CE1 . PHE   B  1  202 ? 5.489   -14.599 57.184 1.00 37.70  ? 215 PHE   B CE1 1 
ATOM   4174 C  CE2 . PHE   B  1  202 ? 6.595   -12.720 58.111 1.00 35.50  ? 215 PHE   B CE2 1 
ATOM   4175 C  CZ  . PHE   B  1  202 ? 5.442   -13.442 57.914 1.00 35.97  ? 215 PHE   B CZ  1 
ATOM   4176 N  N   . PRO   B  1  203 ? 11.611  -16.777 55.297 1.00 29.43  ? 216 PRO   B N   1 
ATOM   4177 C  CA  . PRO   B  1  203 ? 12.758  -17.015 54.424 1.00 30.56  ? 216 PRO   B CA  1 
ATOM   4178 C  C   . PRO   B  1  203 ? 12.505  -18.129 53.409 1.00 30.03  ? 216 PRO   B C   1 
ATOM   4179 O  O   . PRO   B  1  203 ? 12.986  -18.073 52.284 1.00 36.40  ? 216 PRO   B O   1 
ATOM   4180 C  CB  . PRO   B  1  203 ? 13.869  -17.371 55.420 1.00 33.54  ? 216 PRO   B CB  1 
ATOM   4181 C  CG  . PRO   B  1  203 ? 13.451  -16.719 56.724 1.00 31.26  ? 216 PRO   B CG  1 
ATOM   4182 C  CD  . PRO   B  1  203 ? 11.946  -16.889 56.723 1.00 31.73  ? 216 PRO   B CD  1 
ATOM   4183 N  N   . ILE   B  1  204 ? 11.732  -19.132 53.801 1.00 30.11  ? 217 ILE   B N   1 
ATOM   4184 C  CA  . ILE   B  1  204 ? 11.450  -20.281 52.953 1.00 32.74  ? 217 ILE   B CA  1 
ATOM   4185 C  C   . ILE   B  1  204 ? 10.422  -19.917 51.893 1.00 30.45  ? 217 ILE   B C   1 
ATOM   4186 O  O   . ILE   B  1  204 ? 10.601  -20.229 50.729 1.00 39.85  ? 217 ILE   B O   1 
ATOM   4187 C  CB  . ILE   B  1  204 ? 10.945  -21.459 53.806 1.00 34.24  ? 217 ILE   B CB  1 
ATOM   4188 C  CG1 . ILE   B  1  204 ? 11.996  -21.892 54.787 1.00 33.99  ? 217 ILE   B CG1 1 
ATOM   4189 C  CG2 . ILE   B  1  204 ? 10.474  -22.611 52.922 1.00 34.50  ? 217 ILE   B CG2 1 
ATOM   4190 C  CD1 . ILE   B  1  204 ? 11.466  -22.769 55.895 1.00 36.43  ? 217 ILE   B CD1 1 
ATOM   4191 N  N   . ASN   B  1  205 ? 9.334   -19.275 52.311 1.00 32.10  ? 218 ASN   B N   1 
ATOM   4192 C  CA  . ASN   B  1  205 ? 8.226   -19.016 51.413 1.00 30.41  ? 218 ASN   B CA  1 
ATOM   4193 C  C   . ASN   B  1  205 ? 8.478   -17.800 50.548 1.00 30.42  ? 218 ASN   B C   1 
ATOM   4194 O  O   . ASN   B  1  205 ? 7.878   -17.732 49.478 1.00 37.57  ? 218 ASN   B O   1 
ATOM   4195 C  CB  . ASN   B  1  205 ? 6.917   -18.813 52.158 1.00 32.38  ? 218 ASN   B CB  1 
ATOM   4196 C  CG  . ASN   B  1  205 ? 6.613   -19.992 53.044 1.00 31.92  ? 218 ASN   B CG  1 
ATOM   4197 O  OD1 . ASN   B  1  205 ? 6.981   -21.108 52.696 1.00 31.92  ? 218 ASN   B OD1 1 
ATOM   4198 N  ND2 . ASN   B  1  205 ? 5.998   -19.769 54.195 1.00 35.02  ? 218 ASN   B ND2 1 
ATOM   4199 N  N   . LEU   B  1  206 ? 9.326   -16.856 50.999 1.00 32.50  ? 219 LEU   B N   1 
ATOM   4200 C  CA  . LEU   B  1  206 ? 9.438   -15.580 50.310 1.00 30.06  ? 219 LEU   B CA  1 
ATOM   4201 C  C   . LEU   B  1  206 ? 10.856  -15.284 49.832 1.00 30.40  ? 219 LEU   B C   1 
ATOM   4202 O  O   . LEU   B  1  206 ? 11.003  -14.501 48.903 1.00 30.83  ? 219 LEU   B O   1 
ATOM   4203 C  CB  . LEU   B  1  206 ? 8.911   -14.482 51.223 1.00 29.52  ? 219 LEU   B CB  1 
ATOM   4204 C  CG  . LEU   B  1  206 ? 7.444   -14.617 51.640 1.00 31.68  ? 219 LEU   B CG  1 
ATOM   4205 C  CD1 . LEU   B  1  206 ? 7.127   -13.703 52.790 1.00 34.68  ? 219 LEU   B CD1 1 
ATOM   4206 C  CD2 . LEU   B  1  206 ? 6.544   -14.306 50.468 1.00 34.83  ? 219 LEU   B CD2 1 
ATOM   4207 N  N   . PHE   B  1  207 ? 11.892  -15.822 50.484 1.00 32.87  ? 220 PHE   B N   1 
ATOM   4208 C  CA  . PHE   B  1  207 ? 13.255  -15.445 50.127 1.00 33.29  ? 220 PHE   B CA  1 
ATOM   4209 C  C   . PHE   B  1  207 ? 13.824  -16.448 49.132 1.00 33.59  ? 220 PHE   B C   1 
ATOM   4210 O  O   . PHE   B  1  207 ? 14.829  -16.174 48.495 1.00 38.20  ? 220 PHE   B O   1 
ATOM   4211 C  CB  . PHE   B  1  207 ? 14.231  -15.322 51.297 1.00 32.90  ? 220 PHE   B CB  1 
ATOM   4212 C  CG  . PHE   B  1  207 ? 13.966  -14.174 52.252 1.00 33.74  ? 220 PHE   B CG  1 
ATOM   4213 C  CD1 . PHE   B  1  207 ? 13.079  -13.149 51.931 1.00 36.38  ? 220 PHE   B CD1 1 
ATOM   4214 C  CD2 . PHE   B  1  207 ? 14.612  -14.131 53.480 1.00 32.52  ? 220 PHE   B CD2 1 
ATOM   4215 C  CE1 . PHE   B  1  207 ? 12.844  -12.113 52.825 1.00 34.42  ? 220 PHE   B CE1 1 
ATOM   4216 C  CE2 . PHE   B  1  207 ? 14.346  -13.116 54.373 1.00 32.58  ? 220 PHE   B CE2 1 
ATOM   4217 C  CZ  . PHE   B  1  207 ? 13.464  -12.115 54.048 1.00 33.60  ? 220 PHE   B CZ  1 
ATOM   4218 N  N   . VAL   B  1  208 ? 13.179  -17.612 49.034 1.00 35.07  ? 221 VAL   B N   1 
ATOM   4219 C  CA  . VAL   B  1  208 ? 13.512  -18.591 48.022 1.00 30.90  ? 221 VAL   B CA  1 
ATOM   4220 C  C   . VAL   B  1  208 ? 12.881  -18.140 46.712 1.00 30.54  ? 221 VAL   B C   1 
ATOM   4221 O  O   . VAL   B  1  208 ? 11.723  -17.746 46.666 1.00 36.37  ? 221 VAL   B O   1 
ATOM   4222 C  CB  . VAL   B  1  208 ? 13.031  -19.996 48.426 1.00 30.25  ? 221 VAL   B CB  1 
ATOM   4223 C  CG1 . VAL   B  1  208 ? 13.229  -21.016 47.315 1.00 29.46  ? 221 VAL   B CG1 1 
ATOM   4224 C  CG2 . VAL   B  1  208 ? 13.720  -20.474 49.691 1.00 29.58  ? 221 VAL   B CG2 1 
ATOM   4225 N  N   . ASP   B  1  209 ? 13.672  -18.203 45.649 1.00 29.20  ? 222 ASP   B N   1 
ATOM   4226 C  CA  . ASP   B  1  209 ? 13.262  -17.771 44.334 1.00 29.91  ? 222 ASP   B CA  1 
ATOM   4227 C  C   . ASP   B  1  209 ? 11.983  -18.497 43.934 1.00 30.25  ? 222 ASP   B C   1 
ATOM   4228 O  O   . ASP   B  1  209 ? 11.835  -19.680 44.179 1.00 27.91  ? 222 ASP   B O   1 
ATOM   4229 C  CB  . ASP   B  1  209 ? 14.385  -18.023 43.344 1.00 31.66  ? 222 ASP   B CB  1 
ATOM   4230 C  CG  . ASP   B  1  209 ? 14.170  -17.394 41.987 1.00 31.91  ? 222 ASP   B CG  1 
ATOM   4231 O  OD1 . ASP   B  1  209 ? 13.327  -17.923 41.235 1.00 31.47  ? 222 ASP   B OD1 1 
ATOM   4232 O  OD2 . ASP   B  1  209 ? 14.831  -16.390 41.717 1.00 36.63  ? 222 ASP   B OD2 1 
ATOM   4233 N  N   . GLY   B  1  210 ? 11.074  -17.781 43.276 1.00 38.09  ? 223 GLY   B N   1 
ATOM   4234 C  CA  . GLY   B  1  210 ? 9.755   -18.309 42.963 1.00 41.74  ? 223 GLY   B CA  1 
ATOM   4235 C  C   . GLY   B  1  210 ? 9.764   -19.383 41.874 1.00 43.65  ? 223 GLY   B C   1 
ATOM   4236 O  O   . GLY   B  1  210 ? 8.798   -20.135 41.745 1.00 44.22  ? 223 GLY   B O   1 
ATOM   4237 N  N   . ARG   B  1  211 ? 10.841  -19.427 41.077 1.00 44.08  ? 224 ARG   B N   1 
ATOM   4238 C  CA  . ARG   B  1  211 ? 10.993  -20.443 40.049 1.00 41.91  ? 224 ARG   B CA  1 
ATOM   4239 C  C   . ARG   B  1  211 ? 11.375  -21.781 40.671 1.00 41.95  ? 224 ARG   B C   1 
ATOM   4240 O  O   . ARG   B  1  211 ? 11.271  -22.801 40.008 1.00 43.84  ? 224 ARG   B O   1 
ATOM   4241 C  CB  . ARG   B  1  211 ? 12.032  -20.057 38.996 1.00 42.25  ? 224 ARG   B CB  1 
ATOM   4242 C  CG  . ARG   B  1  211 ? 11.653  -18.830 38.182 1.00 42.83  ? 224 ARG   B CG  1 
ATOM   4243 C  CD  . ARG   B  1  211 ? 12.875  -18.241 37.479 1.00 45.47  ? 224 ARG   B CD  1 
ATOM   4244 N  NE  . ARG   B  1  211 ? 13.870  -17.728 38.428 1.00 47.68  ? 224 ARG   B NE  1 
ATOM   4245 C  CZ  . ARG   B  1  211 ? 14.972  -17.054 38.100 1.00 49.01  ? 224 ARG   B CZ  1 
ATOM   4246 N  NH1 . ARG   B  1  211 ? 15.247  -16.798 36.830 1.00 39.12  ? 224 ARG   B NH1 1 
ATOM   4247 N  NH2 . ARG   B  1  211 ? 15.793  -16.626 39.055 1.00 44.32  ? 224 ARG   B NH2 1 
ATOM   4248 N  N   . VAL   B  1  212 ? 11.801  -21.799 41.936 1.00 45.73  ? 225 VAL   B N   1 
ATOM   4249 C  CA  . VAL   B  1  212 ? 12.035  -23.056 42.637 1.00 48.16  ? 225 VAL   B CA  1 
ATOM   4250 C  C   . VAL   B  1  212 ? 10.696  -23.574 43.174 1.00 58.43  ? 225 VAL   B C   1 
ATOM   4251 O  O   . VAL   B  1  212 ? 10.188  -23.079 44.173 1.00 55.14  ? 225 VAL   B O   1 
ATOM   4252 C  CB  . VAL   B  1  212 ? 13.062  -22.902 43.776 1.00 47.91  ? 225 VAL   B CB  1 
ATOM   4253 C  CG1 . VAL   B  1  212 ? 13.271  -24.206 44.540 1.00 44.66  ? 225 VAL   B CG1 1 
ATOM   4254 C  CG2 . VAL   B  1  212 ? 14.400  -22.355 43.290 1.00 48.46  ? 225 VAL   B CG2 1 
ATOM   4255 N  N   . THR   B  1  213 ? 10.127  -24.599 42.529 1.00 66.04  ? 226 THR   B N   1 
ATOM   4256 C  CA  . THR   B  1  213 ? 8.792   -25.084 42.876 1.00 74.29  ? 226 THR   B CA  1 
ATOM   4257 C  C   . THR   B  1  213 ? 8.895   -26.236 43.880 1.00 76.16  ? 226 THR   B C   1 
ATOM   4258 O  O   . THR   B  1  213 ? 7.980   -26.463 44.668 1.00 66.92  ? 226 THR   B O   1 
ATOM   4259 C  CB  . THR   B  1  213 ? 8.031   -25.495 41.609 1.00 74.66  ? 226 THR   B CB  1 
ATOM   4260 O  OG1 . THR   B  1  213 ? 8.805   -26.491 40.943 1.00 72.03  ? 226 THR   B OG1 1 
ATOM   4261 C  CG2 . THR   B  1  213 ? 7.803   -24.324 40.666 1.00 76.83  ? 226 THR   B CG2 1 
ATOM   4262 N  N   . THR   B  1  214 ? 10.044  -26.919 43.888 1.00 84.79  ? 227 THR   B N   1 
ATOM   4263 C  CA  . THR   B  1  214 ? 10.207  -28.172 44.603 1.00 90.44  ? 227 THR   B CA  1 
ATOM   4264 C  C   . THR   B  1  214 ? 11.383  -28.094 45.588 1.00 83.43  ? 227 THR   B C   1 
ATOM   4265 O  O   . THR   B  1  214 ? 12.464  -27.616 45.238 1.00 79.65  ? 227 THR   B O   1 
ATOM   4266 C  CB  . THR   B  1  214 ? 10.395  -29.238 43.523 1.00 96.81  ? 227 THR   B CB  1 
ATOM   4267 O  OG1 . THR   B  1  214 ? 10.291  -30.478 44.217 1.00 93.11  ? 227 THR   B OG1 1 
ATOM   4268 C  CG2 . THR   B  1  214 ? 11.722  -29.142 42.783 1.00 92.46  ? 227 THR   B CG2 1 
ATOM   4269 N  N   . ASP   B  1  215 ? 11.160  -28.585 46.816 1.00 71.75  ? 228 ASP   B N   1 
ATOM   4270 C  CA  . ASP   B  1  215 ? 12.243  -28.744 47.780 1.00 81.00  ? 228 ASP   B CA  1 
ATOM   4271 C  C   . ASP   B  1  215 ? 12.817  -27.357 48.089 1.00 61.85  ? 228 ASP   B C   1 
ATOM   4272 O  O   . ASP   B  1  215 ? 13.984  -27.078 47.824 1.00 53.75  ? 228 ASP   B O   1 
ATOM   4273 C  CB  . ASP   B  1  215 ? 13.254  -29.759 47.248 1.00 98.66  ? 228 ASP   B CB  1 
ATOM   4274 C  CG  . ASP   B  1  215 ? 14.383  -30.205 48.169 1.00 114.52 ? 228 ASP   B CG  1 
ATOM   4275 O  OD1 . ASP   B  1  215 ? 14.237  -30.055 49.398 1.00 127.23 ? 228 ASP   B OD1 1 
ATOM   4276 O  OD2 . ASP   B  1  215 ? 15.416  -30.687 47.640 1.00 110.76 ? 228 ASP   B OD2 1 
ATOM   4277 N  N   . ARG   B  1  216 ? 11.954  -26.475 48.604 1.00 50.13  ? 229 ARG   B N   1 
ATOM   4278 C  CA  . ARG   B  1  216 ? 12.289  -25.072 48.756 1.00 42.70  ? 229 ARG   B CA  1 
ATOM   4279 C  C   . ARG   B  1  216 ? 13.256  -24.948 49.933 1.00 44.76  ? 229 ARG   B C   1 
ATOM   4280 O  O   . ARG   B  1  216 ? 13.005  -25.451 51.033 1.00 44.91  ? 229 ARG   B O   1 
ATOM   4281 C  CB  . ARG   B  1  216 ? 11.030  -24.195 48.863 1.00 43.11  ? 229 ARG   B CB  1 
ATOM   4282 C  CG  . ARG   B  1  216 ? 10.289  -24.014 47.541 1.00 49.25  ? 229 ARG   B CG  1 
ATOM   4283 C  CD  . ARG   B  1  216 ? 8.926   -23.328 47.683 1.00 54.11  ? 229 ARG   B CD  1 
ATOM   4284 N  NE  . ARG   B  1  216 ? 9.044   -21.906 48.032 1.00 60.30  ? 229 ARG   B NE  1 
ATOM   4285 C  CZ  . ARG   B  1  216 ? 9.450   -20.923 47.211 1.00 67.52  ? 229 ARG   B CZ  1 
ATOM   4286 N  NH1 . ARG   B  1  216 ? 9.701   -21.151 45.927 1.00 63.91  ? 229 ARG   B NH1 1 
ATOM   4287 N  NH2 . ARG   B  1  216 ? 9.578   -19.683 47.661 1.00 72.71  ? 229 ARG   B NH2 1 
ATOM   4288 N  N   . LYS   B  1  217 ? 14.380  -24.287 49.665 1.00 37.65  ? 230 LYS   B N   1 
ATOM   4289 C  CA  . LYS   B  1  217 ? 15.430  -24.161 50.650 1.00 39.71  ? 230 LYS   B CA  1 
ATOM   4290 C  C   . LYS   B  1  217 ? 16.233  -22.918 50.302 1.00 35.97  ? 230 LYS   B C   1 
ATOM   4291 O  O   . LYS   B  1  217 ? 16.394  -22.605 49.121 1.00 36.14  ? 230 LYS   B O   1 
ATOM   4292 C  CB  . LYS   B  1  217 ? 16.281  -25.438 50.617 1.00 40.89  ? 230 LYS   B CB  1 
ATOM   4293 C  CG  . LYS   B  1  217 ? 17.023  -25.677 49.305 1.00 42.33  ? 230 LYS   B CG  1 
ATOM   4294 C  CD  . LYS   B  1  217 ? 17.764  -27.014 49.238 1.00 45.39  ? 230 LYS   B CD  1 
ATOM   4295 C  CE  . LYS   B  1  217 ? 18.753  -27.029 48.096 1.00 48.63  ? 230 LYS   B CE  1 
ATOM   4296 N  NZ  . LYS   B  1  217 ? 19.355  -28.342 47.847 1.00 49.57  ? 230 LYS   B NZ  1 
ATOM   4297 N  N   . LEU   B  1  218 ? 16.746  -22.245 51.335 1.00 31.31  ? 231 LEU   B N   1 
ATOM   4298 C  CA  . LEU   B  1  218 ? 17.469  -21.007 51.127 1.00 30.37  ? 231 LEU   B CA  1 
ATOM   4299 C  C   . LEU   B  1  218 ? 18.968  -21.247 51.282 1.00 27.65  ? 231 LEU   B C   1 
ATOM   4300 O  O   . LEU   B  1  218 ? 19.400  -21.805 52.282 1.00 28.71  ? 231 LEU   B O   1 
ATOM   4301 C  CB  . LEU   B  1  218 ? 16.921  -20.008 52.144 1.00 27.11  ? 231 LEU   B CB  1 
ATOM   4302 C  CG  . LEU   B  1  218 ? 17.445  -18.583 51.987 1.00 29.85  ? 231 LEU   B CG  1 
ATOM   4303 C  CD1 . LEU   B  1  218 ? 17.028  -17.941 50.660 1.00 29.30  ? 231 LEU   B CD1 1 
ATOM   4304 C  CD2 . LEU   B  1  218 ? 17.001  -17.756 53.168 1.00 31.01  ? 231 LEU   B CD2 1 
ATOM   4305 N  N   . SER   B  1  219 ? 19.764  -20.776 50.314 1.00 29.09  ? 232 SER   B N   1 
ATOM   4306 C  CA  . SER   B  1  219 ? 21.220  -20.823 50.439 1.00 30.52  ? 232 SER   B CA  1 
ATOM   4307 C  C   . SER   B  1  219 ? 21.673  -19.773 51.444 1.00 29.81  ? 232 SER   B C   1 
ATOM   4308 O  O   . SER   B  1  219 ? 20.974  -18.788 51.705 1.00 37.07  ? 232 SER   B O   1 
ATOM   4309 C  CB  . SER   B  1  219 ? 21.893  -20.646 49.114 1.00 29.95  ? 232 SER   B CB  1 
ATOM   4310 O  OG  . SER   B  1  219 ? 21.699  -19.334 48.609 1.00 31.42  ? 232 SER   B OG  1 
ATOM   4311 N  N   . MET   B  1  220 ? 22.858  -19.979 52.002 1.00 30.50  ? 233 MET   B N   1 
ATOM   4312 C  CA  . MET   B  1  220 ? 23.419  -19.045 52.964 1.00 32.27  ? 233 MET   B CA  1 
ATOM   4313 C  C   . MET   B  1  220 ? 23.876  -17.749 52.287 1.00 30.40  ? 233 MET   B C   1 
ATOM   4314 O  O   . MET   B  1  220 ? 23.819  -16.689 52.911 1.00 33.31  ? 233 MET   B O   1 
ATOM   4315 C  CB  . MET   B  1  220 ? 24.574  -19.710 53.713 1.00 32.48  ? 233 MET   B CB  1 
ATOM   4316 C  CG  . MET   B  1  220 ? 24.126  -20.925 54.531 1.00 32.31  ? 233 MET   B CG  1 
ATOM   4317 S  SD  . MET   B  1  220 ? 22.848  -20.589 55.764 1.00 33.82  ? 233 MET   B SD  1 
ATOM   4318 C  CE  . MET   B  1  220 ? 21.432  -21.258 54.903 1.00 31.95  ? 233 MET   B CE  1 
ATOM   4319 N  N   . GLU   B  1  221 ? 24.275  -17.822 51.012 1.00 31.68  ? 234 GLU   B N   1 
ATOM   4320 C  CA  . GLU   B  1  221 ? 24.610  -16.645 50.216 1.00 32.77  ? 234 GLU   B CA  1 
ATOM   4321 C  C   . GLU   B  1  221 ? 23.390  -15.723 50.076 1.00 34.73  ? 234 GLU   B C   1 
ATOM   4322 O  O   . GLU   B  1  221 ? 23.493  -14.505 50.202 1.00 29.97  ? 234 GLU   B O   1 
ATOM   4323 C  CB  . GLU   B  1  221 ? 25.086  -17.034 48.811 1.00 35.31  ? 234 GLU   B CB  1 
ATOM   4324 C  CG  . GLU   B  1  221 ? 26.362  -17.879 48.785 1.00 45.62  ? 234 GLU   B CG  1 
ATOM   4325 C  CD  . GLU   B  1  221 ? 26.317  -19.383 49.143 1.00 53.46  ? 234 GLU   B CD  1 
ATOM   4326 O  OE1 . GLU   B  1  221 ? 25.260  -19.995 49.480 1.00 42.08  ? 234 GLU   B OE1 1 
ATOM   4327 O  OE2 . GLU   B  1  221 ? 27.422  -19.978 49.035 1.00 51.61  ? 234 GLU   B OE2 1 
ATOM   4328 N  N   . ASP   B  1  222 ? 22.234  -16.320 49.765 1.00 35.90  ? 235 ASP   B N   1 
ATOM   4329 C  CA  . ASP   B  1  222 ? 21.002  -15.574 49.555 1.00 36.95  ? 235 ASP   B CA  1 
ATOM   4330 C  C   . ASP   B  1  222 ? 20.512  -15.028 50.888 1.00 32.40  ? 235 ASP   B C   1 
ATOM   4331 O  O   . ASP   B  1  222 ? 20.104  -13.873 50.964 1.00 31.91  ? 235 ASP   B O   1 
ATOM   4332 C  CB  . ASP   B  1  222 ? 19.948  -16.408 48.839 1.00 38.62  ? 235 ASP   B CB  1 
ATOM   4333 C  CG  . ASP   B  1  222 ? 20.186  -16.685 47.353 1.00 42.24  ? 235 ASP   B CG  1 
ATOM   4334 O  OD1 . ASP   B  1  222 ? 21.212  -16.187 46.791 1.00 35.14  ? 235 ASP   B OD1 1 
ATOM   4335 O  OD2 . ASP   B  1  222 ? 19.327  -17.395 46.762 1.00 43.67  ? 235 ASP   B OD2 1 
ATOM   4336 N  N   . ALA   B  1  223 ? 20.591  -15.854 51.937 1.00 30.31  ? 236 ALA   B N   1 
ATOM   4337 C  CA  . ALA   B  1  223 ? 20.269  -15.370 53.272 1.00 31.50  ? 236 ALA   B CA  1 
ATOM   4338 C  C   . ALA   B  1  223 ? 21.156  -14.171 53.646 1.00 30.36  ? 236 ALA   B C   1 
ATOM   4339 O  O   . ALA   B  1  223 ? 20.650  -13.163 54.116 1.00 30.67  ? 236 ALA   B O   1 
ATOM   4340 C  CB  . ALA   B  1  223 ? 20.376  -16.486 54.285 1.00 28.99  ? 236 ALA   B CB  1 
ATOM   4341 N  N   . ALA   B  1  224 ? 22.473  -14.250 53.431 1.00 28.69  ? 237 ALA   B N   1 
ATOM   4342 C  CA  . ALA   B  1  224 ? 23.332  -13.156 53.855 1.00 29.36  ? 237 ALA   B CA  1 
ATOM   4343 C  C   . ALA   B  1  224 ? 22.977  -11.900 53.065 1.00 26.94  ? 237 ALA   B C   1 
ATOM   4344 O  O   . ALA   B  1  224 ? 22.922  -10.794 53.610 1.00 26.13  ? 237 ALA   B O   1 
ATOM   4345 C  CB  . ALA   B  1  224 ? 24.792  -13.510 53.675 1.00 29.85  ? 237 ALA   B CB  1 
ATOM   4346 N  N   . SER   B  1  225 ? 22.730  -12.094 51.767 1.00 26.10  ? 238 SER   B N   1 
ATOM   4347 C  CA  . SER   B  1  225 ? 22.430  -10.983 50.890 1.00 28.20  ? 238 SER   B CA  1 
ATOM   4348 C  C   . SER   B  1  225 ? 21.251  -10.175 51.447 1.00 28.56  ? 238 SER   B C   1 
ATOM   4349 O  O   . SER   B  1  225 ? 21.311  -8.947  51.516 1.00 28.72  ? 238 SER   B O   1 
ATOM   4350 C  CB  . SER   B  1  225 ? 22.182  -11.457 49.486 1.00 30.13  ? 238 SER   B CB  1 
ATOM   4351 O  OG  . SER   B  1  225 ? 21.945  -10.362 48.611 1.00 35.21  ? 238 SER   B OG  1 
ATOM   4352 N  N   . ILE   B  1  226 ? 20.208  -10.876 51.895 1.00 27.98  ? 239 ILE   B N   1 
ATOM   4353 C  CA  . ILE   B  1  226 ? 18.975  -10.235 52.322 1.00 32.24  ? 239 ILE   B CA  1 
ATOM   4354 C  C   . ILE   B  1  226 ? 19.085  -9.754  53.772 1.00 31.06  ? 239 ILE   B C   1 
ATOM   4355 O  O   . ILE   B  1  226 ? 18.837  -8.578  54.066 1.00 34.64  ? 239 ILE   B O   1 
ATOM   4356 C  CB  . ILE   B  1  226 ? 17.791  -11.187 52.104 1.00 31.97  ? 239 ILE   B CB  1 
ATOM   4357 C  CG1 . ILE   B  1  226 ? 17.573  -11.406 50.615 1.00 34.22  ? 239 ILE   B CG1 1 
ATOM   4358 C  CG2 . ILE   B  1  226 ? 16.528  -10.673 52.788 1.00 33.03  ? 239 ILE   B CG2 1 
ATOM   4359 C  CD1 . ILE   B  1  226 ? 16.681  -12.592 50.291 1.00 36.99  ? 239 ILE   B CD1 1 
ATOM   4360 N  N   . PHE   B  1  227 ? 19.492  -10.652 54.666 1.00 28.70  ? 240 PHE   B N   1 
ATOM   4361 C  CA  . PHE   B  1  227 ? 19.528  -10.351 56.092 1.00 30.12  ? 240 PHE   B CA  1 
ATOM   4362 C  C   . PHE   B  1  227 ? 20.606  -9.324  56.434 1.00 29.53  ? 240 PHE   B C   1 
ATOM   4363 O  O   . PHE   B  1  227 ? 20.394  -8.489  57.306 1.00 32.13  ? 240 PHE   B O   1 
ATOM   4364 C  CB  . PHE   B  1  227 ? 19.779  -11.613 56.902 1.00 29.87  ? 240 PHE   B CB  1 
ATOM   4365 C  CG  . PHE   B  1  227 ? 18.587  -12.533 57.084 1.00 31.61  ? 240 PHE   B CG  1 
ATOM   4366 C  CD1 . PHE   B  1  227 ? 17.604  -12.246 58.012 1.00 33.45  ? 240 PHE   B CD1 1 
ATOM   4367 C  CD2 . PHE   B  1  227 ? 18.497  -13.736 56.406 1.00 38.61  ? 240 PHE   B CD2 1 
ATOM   4368 C  CE1 . PHE   B  1  227 ? 16.540  -13.117 58.221 1.00 32.39  ? 240 PHE   B CE1 1 
ATOM   4369 C  CE2 . PHE   B  1  227 ? 17.431  -14.598 56.617 1.00 40.99  ? 240 PHE   B CE2 1 
ATOM   4370 C  CZ  . PHE   B  1  227 ? 16.449  -14.279 57.522 1.00 34.26  ? 240 PHE   B CZ  1 
ATOM   4371 N  N   . ARG   B  1  228 ? 21.759  -9.389  55.767 1.00 29.33  ? 241 ARG   B N   1 
ATOM   4372 C  CA  . ARG   B  1  228 ? 22.869  -8.509  56.099 1.00 31.44  ? 241 ARG   B CA  1 
ATOM   4373 C  C   . ARG   B  1  228 ? 22.914  -7.329  55.134 1.00 29.55  ? 241 ARG   B C   1 
ATOM   4374 O  O   . ARG   B  1  228 ? 22.994  -6.203  55.585 1.00 30.24  ? 241 ARG   B O   1 
ATOM   4375 C  CB  . ARG   B  1  228 ? 24.215  -9.247  56.132 1.00 32.18  ? 241 ARG   B CB  1 
ATOM   4376 C  CG  . ARG   B  1  228 ? 25.366  -8.324  56.499 1.00 34.09  ? 241 ARG   B CG  1 
ATOM   4377 C  CD  . ARG   B  1  228 ? 26.688  -9.033  56.724 1.00 33.85  ? 241 ARG   B CD  1 
ATOM   4378 N  NE  . ARG   B  1  228 ? 27.175  -9.699  55.518 1.00 34.93  ? 241 ARG   B NE  1 
ATOM   4379 C  CZ  . ARG   B  1  228 ? 27.489  -10.984 55.392 1.00 35.90  ? 241 ARG   B CZ  1 
ATOM   4380 N  NH1 . ARG   B  1  228 ? 27.353  -11.821 56.410 1.00 39.31  ? 241 ARG   B NH1 1 
ATOM   4381 N  NH2 . ARG   B  1  228 ? 27.920  -11.452 54.218 1.00 32.80  ? 241 ARG   B NH2 1 
ATOM   4382 N  N   . ASP   B  1  229 ? 22.850  -7.571  53.821 1.00 30.47  ? 242 ASP   B N   1 
ATOM   4383 C  CA  . ASP   B  1  229 ? 23.130  -6.499  52.882 1.00 27.99  ? 242 ASP   B CA  1 
ATOM   4384 C  C   . ASP   B  1  229 ? 21.870  -5.790  52.380 1.00 27.42  ? 242 ASP   B C   1 
ATOM   4385 O  O   . ASP   B  1  229 ? 21.983  -4.765  51.710 1.00 29.35  ? 242 ASP   B O   1 
ATOM   4386 C  CB  . ASP   B  1  229 ? 24.015  -6.969  51.749 1.00 29.64  ? 242 ASP   B CB  1 
ATOM   4387 C  CG  . ASP   B  1  229 ? 25.367  -7.545  52.134 1.00 33.75  ? 242 ASP   B CG  1 
ATOM   4388 O  OD1 . ASP   B  1  229 ? 25.980  -7.090  53.147 1.00 35.62  ? 242 ASP   B OD1 1 
ATOM   4389 O  OD2 . ASP   B  1  229 ? 25.828  -8.406  51.356 1.00 36.04  ? 242 ASP   B OD2 1 
ATOM   4390 N  N   . MET   B  1  230 ? 20.674  -6.309  52.711 1.00 28.50  ? 243 MET   B N   1 
ATOM   4391 C  CA  A MET   B  1  230 ? 19.425  -5.696  52.285 0.50 29.04  ? 243 MET   B CA  1 
ATOM   4392 C  CA  B MET   B  1  230 ? 19.424  -5.700  52.282 0.50 27.96  ? 243 MET   B CA  1 
ATOM   4393 C  C   . MET   B  1  230 ? 19.344  -5.690  50.761 1.00 28.35  ? 243 MET   B C   1 
ATOM   4394 O  O   . MET   B  1  230 ? 18.853  -4.724  50.161 1.00 28.27  ? 243 MET   B O   1 
ATOM   4395 C  CB  A MET   B  1  230 ? 19.304  -4.255  52.798 0.50 30.62  ? 243 MET   B CB  1 
ATOM   4396 C  CB  B MET   B  1  230 ? 19.303  -4.258  52.783 0.50 27.87  ? 243 MET   B CB  1 
ATOM   4397 C  CG  A MET   B  1  230 ? 19.549  -4.106  54.282 0.50 33.35  ? 243 MET   B CG  1 
ATOM   4398 C  CG  B MET   B  1  230 ? 19.517  -4.114  54.263 0.50 28.67  ? 243 MET   B CG  1 
ATOM   4399 S  SD  A MET   B  1  230 ? 19.555  -2.382  54.817 0.50 37.13  ? 243 MET   B SD  1 
ATOM   4400 S  SD  B MET   B  1  230 ? 19.477  -2.372  54.723 0.50 29.25  ? 243 MET   B SD  1 
ATOM   4401 C  CE  A MET   B  1  230 ? 20.221  -2.596  56.484 0.50 38.45  ? 243 MET   B CE  1 
ATOM   4402 C  CE  B MET   B  1  230 ? 21.090  -1.849  54.130 0.50 25.86  ? 243 MET   B CE  1 
ATOM   4403 N  N   . ARG   B  1  231 ? 19.821  -6.790  50.161 1.00 28.76  ? 244 ARG   B N   1 
ATOM   4404 C  CA  A ARG   B  1  231 ? 19.983  -6.903  48.722 0.50 26.94  ? 244 ARG   B CA  1 
ATOM   4405 C  CA  B ARG   B  1  231 ? 19.975  -6.902  48.724 0.50 27.24  ? 244 ARG   B CA  1 
ATOM   4406 C  C   . ARG   B  1  231 ? 19.306  -8.183  48.246 1.00 26.63  ? 244 ARG   B C   1 
ATOM   4407 O  O   . ARG   B  1  231 ? 19.544  -9.251  48.790 1.00 26.48  ? 244 ARG   B O   1 
ATOM   4408 C  CB  A ARG   B  1  231 ? 21.472  -6.929  48.357 0.50 28.48  ? 244 ARG   B CB  1 
ATOM   4409 C  CB  B ARG   B  1  231 ? 21.466  -6.918  48.384 0.50 29.26  ? 244 ARG   B CB  1 
ATOM   4410 C  CG  A ARG   B  1  231 ? 21.754  -6.881  46.857 0.50 30.55  ? 244 ARG   B CG  1 
ATOM   4411 C  CG  B ARG   B  1  231 ? 21.803  -6.879  46.900 0.50 31.94  ? 244 ARG   B CG  1 
ATOM   4412 C  CD  A ARG   B  1  231 ? 23.216  -6.957  46.408 0.50 31.29  ? 244 ARG   B CD  1 
ATOM   4413 C  CD  B ARG   B  1  231 ? 23.324  -6.782  46.745 0.50 33.21  ? 244 ARG   B CD  1 
ATOM   4414 N  NE  A ARG   B  1  231 ? 23.747  -8.319  46.559 0.50 35.17  ? 244 ARG   B NE  1 
ATOM   4415 N  NE  B ARG   B  1  231 ? 23.931  -8.009  47.280 0.50 37.65  ? 244 ARG   B NE  1 
ATOM   4416 C  CZ  A ARG   B  1  231 ? 23.472  -9.360  45.783 0.50 32.57  ? 244 ARG   B CZ  1 
ATOM   4417 C  CZ  B ARG   B  1  231 ? 24.920  -8.155  48.165 0.50 33.52  ? 244 ARG   B CZ  1 
ATOM   4418 N  NH1 A ARG   B  1  231 ? 22.881  -9.163  44.620 0.50 35.58  ? 244 ARG   B NH1 1 
ATOM   4419 N  NH1 B ARG   B  1  231 ? 25.594  -7.129  48.639 0.50 32.68  ? 244 ARG   B NH1 1 
ATOM   4420 N  NH2 A ARG   B  1  231 ? 23.807  -10.584 46.162 0.50 28.78  ? 244 ARG   B NH2 1 
ATOM   4421 N  NH2 B ARG   B  1  231 ? 25.247  -9.372  48.540 0.50 34.52  ? 244 ARG   B NH2 1 
ATOM   4422 N  N   . PHE   B  1  232 ? 18.475  -8.063  47.211 1.00 27.19  ? 245 PHE   B N   1 
ATOM   4423 C  CA  . PHE   B  1  232 ? 17.916  -9.217  46.543 1.00 27.88  ? 245 PHE   B CA  1 
ATOM   4424 C  C   . PHE   B  1  232 ? 19.035  -10.020 45.891 1.00 30.54  ? 245 PHE   B C   1 
ATOM   4425 O  O   . PHE   B  1  232 ? 19.983  -9.450  45.359 1.00 32.24  ? 245 PHE   B O   1 
ATOM   4426 C  CB  . PHE   B  1  232 ? 16.974  -8.805  45.411 1.00 29.14  ? 245 PHE   B CB  1 
ATOM   4427 C  CG  . PHE   B  1  232 ? 15.612  -8.301  45.857 1.00 29.65  ? 245 PHE   B CG  1 
ATOM   4428 C  CD1 . PHE   B  1  232 ? 14.726  -9.148  46.502 1.00 28.84  ? 245 PHE   B CD1 1 
ATOM   4429 C  CD2 . PHE   B  1  232 ? 15.188  -7.014  45.551 1.00 30.62  ? 245 PHE   B CD2 1 
ATOM   4430 C  CE1 . PHE   B  1  232 ? 13.464  -8.704  46.850 1.00 31.12  ? 245 PHE   B CE1 1 
ATOM   4431 C  CE2 . PHE   B  1  232 ? 13.917  -6.571  45.905 1.00 32.58  ? 245 PHE   B CE2 1 
ATOM   4432 C  CZ  . PHE   B  1  232 ? 13.061  -7.411  46.570 1.00 31.56  ? 245 PHE   B CZ  1 
ATOM   4433 N  N   . PRO   B  1  233 ? 18.965  -11.366 45.891 1.00 27.43  ? 246 PRO   B N   1 
ATOM   4434 C  CA  . PRO   B  1  233 ? 19.868  -12.160 45.066 1.00 28.75  ? 246 PRO   B CA  1 
ATOM   4435 C  C   . PRO   B  1  233 ? 19.790  -11.697 43.617 1.00 29.23  ? 246 PRO   B C   1 
ATOM   4436 O  O   . PRO   B  1  233 ? 18.778  -11.141 43.178 1.00 31.93  ? 246 PRO   B O   1 
ATOM   4437 C  CB  . PRO   B  1  233 ? 19.372  -13.610 45.266 1.00 29.85  ? 246 PRO   B CB  1 
ATOM   4438 C  CG  . PRO   B  1  233 ? 18.654  -13.578 46.618 1.00 29.41  ? 246 PRO   B CG  1 
ATOM   4439 C  CD  . PRO   B  1  233 ? 18.070  -12.181 46.718 1.00 28.21  ? 246 PRO   B CD  1 
ATOM   4440 N  N   . ASP   B  1  234 ? 20.880  -11.905 42.883 1.00 28.85  ? 247 ASP   B N   1 
ATOM   4441 C  CA  . ASP   B  1  234 ? 20.891  -11.582 41.467 1.00 33.27  ? 247 ASP   B CA  1 
ATOM   4442 C  C   . ASP   B  1  234 ? 19.740  -12.319 40.788 1.00 33.81  ? 247 ASP   B C   1 
ATOM   4443 O  O   . ASP   B  1  234 ? 19.479  -13.484 41.083 1.00 31.54  ? 247 ASP   B O   1 
ATOM   4444 C  CB  . ASP   B  1  234 ? 22.212  -11.928 40.792 1.00 34.60  ? 247 ASP   B CB  1 
ATOM   4445 C  CG  . ASP   B  1  234 ? 23.413  -11.066 41.171 1.00 39.39  ? 247 ASP   B CG  1 
ATOM   4446 O  OD1 . ASP   B  1  234 ? 23.281  -10.173 42.065 1.00 40.21  ? 247 ASP   B OD1 1 
ATOM   4447 O  OD2 . ASP   B  1  234 ? 24.484  -11.300 40.558 1.00 38.31  ? 247 ASP   B OD2 1 
ATOM   4448 N  N   . ASP   B  1  235 ? 19.045  -11.612 39.894 1.00 35.38  ? 248 ASP   B N   1 
ATOM   4449 C  CA  . ASP   B  1  235 ? 18.010  -12.220 39.090 1.00 37.92  ? 248 ASP   B CA  1 
ATOM   4450 C  C   . ASP   B  1  235 ? 16.872  -12.793 39.949 1.00 34.94  ? 248 ASP   B C   1 
ATOM   4451 O  O   . ASP   B  1  235 ? 16.233  -13.767 39.569 1.00 31.33  ? 248 ASP   B O   1 
ATOM   4452 C  CB  . ASP   B  1  235 ? 18.606  -13.285 38.173 1.00 38.78  ? 248 ASP   B CB  1 
ATOM   4453 C  CG  . ASP   B  1  235 ? 17.668  -13.653 37.030 1.00 43.81  ? 248 ASP   B CG  1 
ATOM   4454 O  OD1 . ASP   B  1  235 ? 17.157  -12.711 36.364 1.00 46.55  ? 248 ASP   B OD1 1 
ATOM   4455 O  OD2 . ASP   B  1  235 ? 17.405  -14.860 36.866 1.00 39.33  ? 248 ASP   B OD2 1 
ATOM   4456 N  N   . PHE   B  1  236 ? 16.596  -12.194 41.107 1.00 33.49  ? 249 PHE   B N   1 
ATOM   4457 C  CA  . PHE   B  1  236 ? 15.629  -12.768 42.023 1.00 32.10  ? 249 PHE   B CA  1 
ATOM   4458 C  C   . PHE   B  1  236 ? 14.213  -12.642 41.471 1.00 31.81  ? 249 PHE   B C   1 
ATOM   4459 O  O   . PHE   B  1  236 ? 13.766  -11.573 41.061 1.00 31.26  ? 249 PHE   B O   1 
ATOM   4460 C  CB  . PHE   B  1  236 ? 15.665  -12.061 43.376 1.00 33.96  ? 249 PHE   B CB  1 
ATOM   4461 C  CG  . PHE   B  1  236 ? 14.698  -12.643 44.385 1.00 31.93  ? 249 PHE   B CG  1 
ATOM   4462 C  CD1 . PHE   B  1  236 ? 14.947  -13.883 44.949 1.00 29.77  ? 249 PHE   B CD1 1 
ATOM   4463 C  CD2 . PHE   B  1  236 ? 13.561  -11.950 44.769 1.00 32.79  ? 249 PHE   B CD2 1 
ATOM   4464 C  CE1 . PHE   B  1  236 ? 14.073  -14.405 45.878 1.00 30.94  ? 249 PHE   B CE1 1 
ATOM   4465 C  CE2 . PHE   B  1  236 ? 12.674  -12.491 45.678 1.00 30.65  ? 249 PHE   B CE2 1 
ATOM   4466 C  CZ  . PHE   B  1  236 ? 12.941  -13.708 46.243 1.00 30.59  ? 249 PHE   B CZ  1 
ATOM   4467 N  N   . HIS   B  1  237 ? 13.494  -13.757 41.506 1.00 33.89  ? 250 HIS   B N   1 
ATOM   4468 C  CA  . HIS   B  1  237 ? 12.099  -13.786 41.094 1.00 34.55  ? 250 HIS   B CA  1 
ATOM   4469 C  C   . HIS   B  1  237 ? 11.259  -14.093 42.324 1.00 30.06  ? 250 HIS   B C   1 
ATOM   4470 O  O   . HIS   B  1  237 ? 11.531  -15.043 43.050 1.00 25.43  ? 250 HIS   B O   1 
ATOM   4471 C  CB  . HIS   B  1  237 ? 11.837  -14.863 40.031 1.00 36.70  ? 250 HIS   B CB  1 
ATOM   4472 C  CG  . HIS   B  1  237 ? 12.376  -14.543 38.683 1.00 41.71  ? 250 HIS   B CG  1 
ATOM   4473 N  ND1 . HIS   B  1  237 ? 13.667  -14.107 38.469 1.00 48.07  ? 250 HIS   B ND1 1 
ATOM   4474 C  CD2 . HIS   B  1  237 ? 11.791  -14.601 37.475 1.00 43.41  ? 250 HIS   B CD2 1 
ATOM   4475 C  CE1 . HIS   B  1  237 ? 13.843  -13.895 37.166 1.00 50.27  ? 250 HIS   B CE1 1 
ATOM   4476 N  NE2 . HIS   B  1  237 ? 12.713  -14.185 36.545 1.00 48.11  ? 250 HIS   B NE2 1 
ATOM   4477 N  N   . ARG   B  1  238 ? 10.215  -13.302 42.528 1.00 31.29  ? 251 ARG   B N   1 
ATOM   4478 C  CA  . ARG   B  1  238 ? 9.391   -13.462 43.705 1.00 32.03  ? 251 ARG   B CA  1 
ATOM   4479 C  C   . ARG   B  1  238 ? 8.605   -14.768 43.630 1.00 34.34  ? 251 ARG   B C   1 
ATOM   4480 O  O   . ARG   B  1  238 ? 8.488   -15.396 42.577 1.00 32.25  ? 251 ARG   B O   1 
ATOM   4481 C  CB  . ARG   B  1  238 ? 8.417   -12.295 43.824 1.00 34.13  ? 251 ARG   B CB  1 
ATOM   4482 C  CG  . ARG   B  1  238 ? 7.358   -12.273 42.736 1.00 35.25  ? 251 ARG   B CG  1 
ATOM   4483 C  CD  . ARG   B  1  238 ? 6.475   -11.065 42.858 1.00 35.97  ? 251 ARG   B CD  1 
ATOM   4484 N  NE  . ARG   B  1  238 ? 5.267   -11.306 42.074 1.00 38.10  ? 251 ARG   B NE  1 
ATOM   4485 C  CZ  . ARG   B  1  238 ? 4.321   -10.413 41.826 1.00 40.55  ? 251 ARG   B CZ  1 
ATOM   4486 N  NH1 . ARG   B  1  238 ? 4.381   -9.211  42.348 1.00 39.42  ? 251 ARG   B NH1 1 
ATOM   4487 N  NH2 . ARG   B  1  238 ? 3.320   -10.735 41.038 1.00 46.14  ? 251 ARG   B NH2 1 
ATOM   4488 N  N   . SER   B  1  239 ? 8.069   -15.160 44.788 1.00 32.51  ? 252 SER   B N   1 
ATOM   4489 C  CA  . SER   B  1  239 ? 7.165   -16.290 44.891 1.00 33.72  ? 252 SER   B CA  1 
ATOM   4490 C  C   . SER   B  1  239 ? 6.134   -16.291 43.759 1.00 34.40  ? 252 SER   B C   1 
ATOM   4491 O  O   . SER   B  1  239 ? 5.677   -15.240 43.312 1.00 31.85  ? 252 SER   B O   1 
ATOM   4492 C  CB  . SER   B  1  239 ? 6.499   -16.277 46.223 1.00 30.95  ? 252 SER   B CB  1 
ATOM   4493 O  OG  . SER   B  1  239 ? 5.519   -17.298 46.301 1.00 32.47  ? 252 SER   B OG  1 
ATOM   4494 N  N   . ALA   B  1  240 ? 5.770   -17.495 43.304 1.00 35.30  ? 253 ALA   B N   1 
ATOM   4495 C  CA  . ALA   B  1  240 ? 4.902   -17.629 42.146 1.00 42.57  ? 253 ALA   B CA  1 
ATOM   4496 C  C   . ALA   B  1  240 ? 3.440   -17.500 42.566 1.00 44.74  ? 253 ALA   B C   1 
ATOM   4497 O  O   . ALA   B  1  240 ? 2.581   -17.391 41.702 1.00 48.15  ? 253 ALA   B O   1 
ATOM   4498 C  CB  . ALA   B  1  240 ? 5.163   -18.951 41.459 1.00 44.73  ? 253 ALA   B CB  1 
ATOM   4499 N  N   . VAL   B  1  241 ? 3.184   -17.533 43.885 1.00 41.97  ? 254 VAL   B N   1 
ATOM   4500 C  CA  . VAL   B  1  241 ? 1.864   -17.317 44.446 1.00 45.64  ? 254 VAL   B CA  1 
ATOM   4501 C  C   . VAL   B  1  241 ? 1.988   -16.404 45.657 1.00 43.57  ? 254 VAL   B C   1 
ATOM   4502 O  O   . VAL   B  1  241 ? 2.985   -16.441 46.372 1.00 47.23  ? 254 VAL   B O   1 
ATOM   4503 C  CB  . VAL   B  1  241 ? 1.190   -18.642 44.866 1.00 51.23  ? 254 VAL   B CB  1 
ATOM   4504 C  CG1 . VAL   B  1  241 ? 0.908   -19.550 43.671 1.00 50.63  ? 254 VAL   B CG1 1 
ATOM   4505 C  CG2 . VAL   B  1  241 ? 2.002   -19.399 45.913 1.00 47.99  ? 254 VAL   B CG2 1 
ATOM   4506 N  N   . PRO   B  1  242 ? 0.941   -15.615 45.981 1.00 43.17  ? 255 PRO   B N   1 
ATOM   4507 C  CA  . PRO   B  1  242 ? 0.909   -14.870 47.238 1.00 38.63  ? 255 PRO   B CA  1 
ATOM   4508 C  C   . PRO   B  1  242 ? 1.218   -15.842 48.370 1.00 39.68  ? 255 PRO   B C   1 
ATOM   4509 O  O   . PRO   B  1  242 ? 0.737   -16.972 48.367 1.00 34.79  ? 255 PRO   B O   1 
ATOM   4510 C  CB  . PRO   B  1  242 ? -0.507  -14.317 47.306 1.00 37.18  ? 255 PRO   B CB  1 
ATOM   4511 C  CG  . PRO   B  1  242 ? -0.936  -14.241 45.854 1.00 39.34  ? 255 PRO   B CG  1 
ATOM   4512 C  CD  . PRO   B  1  242 ? -0.280  -15.426 45.174 1.00 40.51  ? 255 PRO   B CD  1 
ATOM   4513 N  N   . ALA   B  1  243 ? 2.069   -15.420 49.314 1.00 39.28  ? 256 ALA   B N   1 
ATOM   4514 C  CA  . ALA   B  1  243 ? 2.431   -16.305 50.403 1.00 35.70  ? 256 ALA   B CA  1 
ATOM   4515 C  C   . ALA   B  1  243 ? 2.712   -15.499 51.661 1.00 34.11  ? 256 ALA   B C   1 
ATOM   4516 O  O   . ALA   B  1  243 ? 2.904   -14.282 51.604 1.00 33.81  ? 256 ALA   B O   1 
ATOM   4517 C  CB  . ALA   B  1  243 ? 3.621   -17.136 49.999 1.00 39.26  ? 256 ALA   B CB  1 
ATOM   4518 N  N   . SER   B  1  244 ? 2.768   -16.216 52.782 1.00 34.18  ? 257 SER   B N   1 
ATOM   4519 C  CA  . SER   B  1  244 ? 3.106   -15.622 54.062 1.00 38.38  ? 257 SER   B CA  1 
ATOM   4520 C  C   . SER   B  1  244 ? 3.685   -16.690 54.980 1.00 35.98  ? 257 SER   B C   1 
ATOM   4521 O  O   . SER   B  1  244 ? 4.843   -17.046 54.824 1.00 36.88  ? 257 SER   B O   1 
ATOM   4522 C  CB  . SER   B  1  244 ? 1.903   -14.946 54.659 1.00 36.71  ? 257 SER   B CB  1 
ATOM   4523 O  OG  . SER   B  1  244 ? 0.816   -15.856 54.711 1.00 37.48  ? 257 SER   B OG  1 
ATOM   4524 N  N   . ASN   B  1  245 ? 2.848   -17.259 55.855 1.00 37.22  ? 258 ASN   B N   1 
ATOM   4525 C  CA  . ASN   B  1  245 ? 3.331   -18.033 56.986 1.00 35.49  ? 258 ASN   B CA  1 
ATOM   4526 C  C   . ASN   B  1  245 ? 2.995   -19.522 56.861 1.00 35.15  ? 258 ASN   B C   1 
ATOM   4527 O  O   . ASN   B  1  245 ? 2.902   -20.212 57.869 1.00 35.00  ? 258 ASN   B O   1 
ATOM   4528 C  CB  . ASN   B  1  245 ? 2.767   -17.508 58.303 1.00 36.45  ? 258 ASN   B CB  1 
ATOM   4529 C  CG  . ASN   B  1  245 ? 1.290   -17.778 58.453 1.00 38.05  ? 258 ASN   B CG  1 
ATOM   4530 O  OD1 . ASN   B  1  245 ? 0.583   -18.024 57.469 1.00 34.98  ? 258 ASN   B OD1 1 
ATOM   4531 N  ND2 . ASN   B  1  245 ? 0.801   -17.730 59.681 1.00 40.85  ? 258 ASN   B ND2 1 
ATOM   4532 N  N   . GLU   B  1  246 ? 2.850   -20.027 55.635 1.00 39.61  ? 259 GLU   B N   1 
ATOM   4533 C  CA  . GLU   B  1  246 ? 2.687   -21.461 55.410 1.00 44.05  ? 259 GLU   B CA  1 
ATOM   4534 C  C   . GLU   B  1  246 ? 3.840   -22.230 56.067 1.00 43.84  ? 259 GLU   B C   1 
ATOM   4535 O  O   . GLU   B  1  246 ? 5.010   -21.906 55.860 1.00 44.71  ? 259 GLU   B O   1 
ATOM   4536 C  CB  . GLU   B  1  246 ? 2.628   -21.837 53.928 1.00 44.04  ? 259 GLU   B CB  1 
ATOM   4537 C  CG  . GLU   B  1  246 ? 1.419   -21.248 53.204 1.00 46.62  ? 259 GLU   B CG  1 
ATOM   4538 C  CD  . GLU   B  1  246 ? 1.518   -19.785 52.770 1.00 50.79  ? 259 GLU   B CD  1 
ATOM   4539 O  OE1 . GLU   B  1  246 ? 2.532   -19.086 53.050 1.00 43.04  ? 259 GLU   B OE1 1 
ATOM   4540 O  OE2 . GLU   B  1  246 ? 0.526   -19.333 52.145 1.00 51.86  ? 259 GLU   B OE2 1 
ATOM   4541 N  N   . GLY   B  1  247 ? 3.482   -23.232 56.886 1.00 41.47  ? 260 GLY   B N   1 
ATOM   4542 C  CA  . GLY   B  1  247 ? 4.426   -24.100 57.565 1.00 33.59  ? 260 GLY   B CA  1 
ATOM   4543 C  C   . GLY   B  1  247 ? 4.715   -23.660 59.001 1.00 37.21  ? 260 GLY   B C   1 
ATOM   4544 O  O   . GLY   B  1  247 ? 5.400   -24.370 59.730 1.00 42.26  ? 260 GLY   B O   1 
ATOM   4545 N  N   . ALA   B  1  248 ? 4.215   -22.498 59.434 1.00 36.28  ? 261 ALA   B N   1 
ATOM   4546 C  CA  . ALA   B  1  248 ? 4.517   -22.020 60.777 1.00 40.02  ? 261 ALA   B CA  1 
ATOM   4547 C  C   . ALA   B  1  248 ? 3.998   -22.994 61.840 1.00 41.07  ? 261 ALA   B C   1 
ATOM   4548 O  O   . ALA   B  1  248 ? 4.593   -23.130 62.909 1.00 38.53  ? 261 ALA   B O   1 
ATOM   4549 C  CB  . ALA   B  1  248 ? 3.949   -20.628 60.979 1.00 41.11  ? 261 ALA   B CB  1 
ATOM   4550 N  N   . ASP   B  1  249 ? 2.860   -23.631 61.541 1.00 46.45  ? 262 ASP   B N   1 
ATOM   4551 C  CA  . ASP   B  1  249 ? 2.266   -24.671 62.373 1.00 56.49  ? 262 ASP   B CA  1 
ATOM   4552 C  C   . ASP   B  1  249 ? 3.261   -25.815 62.622 1.00 49.10  ? 262 ASP   B C   1 
ATOM   4553 O  O   . ASP   B  1  249 ? 3.386   -26.309 63.738 1.00 46.75  ? 262 ASP   B O   1 
ATOM   4554 C  CB  . ASP   B  1  249 ? 0.961   -25.185 61.763 1.00 64.92  ? 262 ASP   B CB  1 
ATOM   4555 C  CG  . ASP   B  1  249 ? 1.002   -25.708 60.321 1.00 76.10  ? 262 ASP   B CG  1 
ATOM   4556 O  OD1 . ASP   B  1  249 ? 1.975   -25.400 59.572 1.00 68.91  ? 262 ASP   B OD1 1 
ATOM   4557 O  OD2 . ASP   B  1  249 ? 0.052   -26.435 59.939 1.00 75.59  ? 262 ASP   B OD2 1 
ATOM   4558 N  N   . GLN   B  1  250 ? 3.969   -26.243 61.573 1.00 42.71  ? 263 GLN   B N   1 
ATOM   4559 C  CA  . GLN   B  1  250 ? 4.909   -27.342 61.685 1.00 43.32  ? 263 GLN   B CA  1 
ATOM   4560 C  C   . GLN   B  1  250 ? 6.135   -26.946 62.504 1.00 43.00  ? 263 GLN   B C   1 
ATOM   4561 O  O   . GLN   B  1  250 ? 6.713   -27.801 63.169 1.00 38.71  ? 263 GLN   B O   1 
ATOM   4562 C  CB  . GLN   B  1  250 ? 5.367   -27.809 60.310 1.00 44.65  ? 263 GLN   B CB  1 
ATOM   4563 C  CG  . GLN   B  1  250 ? 4.274   -28.483 59.490 1.00 46.53  ? 263 GLN   B CG  1 
ATOM   4564 C  CD  . GLN   B  1  250 ? 4.831   -29.038 58.200 1.00 51.96  ? 263 GLN   B CD  1 
ATOM   4565 O  OE1 . GLN   B  1  250 ? 5.824   -29.782 58.201 1.00 53.05  ? 263 GLN   B OE1 1 
ATOM   4566 N  NE2 . GLN   B  1  250 ? 4.260   -28.594 57.088 1.00 50.96  ? 263 GLN   B NE2 1 
ATOM   4567 N  N   . VAL   B  1  251 ? 6.524   -25.660 62.451 1.00 38.68  ? 264 VAL   B N   1 
ATOM   4568 C  CA  . VAL   B  1  251 ? 7.664   -25.187 63.212 1.00 37.89  ? 264 VAL   B CA  1 
ATOM   4569 C  C   . VAL   B  1  251 ? 7.335   -25.301 64.695 1.00 41.03  ? 264 VAL   B C   1 
ATOM   4570 O  O   . VAL   B  1  251 ? 8.169   -25.725 65.493 1.00 40.98  ? 264 VAL   B O   1 
ATOM   4571 C  CB  . VAL   B  1  251 ? 8.051   -23.753 62.798 1.00 36.86  ? 264 VAL   B CB  1 
ATOM   4572 C  CG1 . VAL   B  1  251 ? 9.014   -23.085 63.763 1.00 35.37  ? 264 VAL   B CG1 1 
ATOM   4573 C  CG2 . VAL   B  1  251 ? 8.639   -23.734 61.400 1.00 37.94  ? 264 VAL   B CG2 1 
ATOM   4574 N  N   . LEU   B  1  252 ? 6.113   -24.914 65.063 1.00 48.96  ? 265 LEU   B N   1 
ATOM   4575 C  CA  . LEU   B  1  252 ? 5.669   -25.031 66.442 1.00 48.61  ? 265 LEU   B CA  1 
ATOM   4576 C  C   . LEU   B  1  252 ? 5.566   -26.504 66.844 1.00 46.94  ? 265 LEU   B C   1 
ATOM   4577 O  O   . LEU   B  1  252 ? 5.928   -26.860 67.958 1.00 49.43  ? 265 LEU   B O   1 
ATOM   4578 C  CB  . LEU   B  1  252 ? 4.332   -24.326 66.644 1.00 43.57  ? 265 LEU   B CB  1 
ATOM   4579 C  CG  . LEU   B  1  252 ? 3.816   -24.351 68.084 1.00 45.17  ? 265 LEU   B CG  1 
ATOM   4580 C  CD1 . LEU   B  1  252 ? 4.706   -23.507 68.993 1.00 43.87  ? 265 LEU   B CD1 1 
ATOM   4581 C  CD2 . LEU   B  1  252 ? 2.371   -23.891 68.146 1.00 42.75  ? 265 LEU   B CD2 1 
ATOM   4582 N  N   . ALA   B  1  253 ? 5.069   -27.354 65.943 1.00 45.02  ? 266 ALA   B N   1 
ATOM   4583 C  CA  . ALA   B  1  253 ? 4.853   -28.760 66.256 1.00 48.80  ? 266 ALA   B CA  1 
ATOM   4584 C  C   . ALA   B  1  253 ? 6.177   -29.493 66.529 1.00 52.50  ? 266 ALA   B C   1 
ATOM   4585 O  O   . ALA   B  1  253 ? 6.217   -30.384 67.368 1.00 53.20  ? 266 ALA   B O   1 
ATOM   4586 C  CB  . ALA   B  1  253 ? 4.046   -29.430 65.153 1.00 41.33  ? 266 ALA   B CB  1 
ATOM   4587 N  N   . ALA   B  1  254 ? 7.270   -29.102 65.858 1.00 54.89  ? 267 ALA   B N   1 
ATOM   4588 C  CA  . ALA   B  1  254 ? 8.577   -29.714 66.076 1.00 54.69  ? 267 ALA   B CA  1 
ATOM   4589 C  C   . ALA   B  1  254 ? 9.044   -29.594 67.534 1.00 54.56  ? 267 ALA   B C   1 
ATOM   4590 O  O   . ALA   B  1  254 ? 9.759   -30.463 68.037 1.00 46.87  ? 267 ALA   B O   1 
ATOM   4591 C  CB  . ALA   B  1  254 ? 9.597   -29.095 65.133 1.00 51.77  ? 267 ALA   B CB  1 
ATOM   4592 N  N   . HIS   B  1  255 ? 8.706   -28.477 68.196 1.00 54.25  ? 268 HIS   B N   1 
ATOM   4593 C  CA  . HIS   B  1  255 ? 9.076   -28.263 69.590 1.00 56.84  ? 268 HIS   B CA  1 
ATOM   4594 C  C   . HIS   B  1  255 ? 7.979   -27.443 70.270 1.00 58.20  ? 268 HIS   B C   1 
ATOM   4595 O  O   . HIS   B  1  255 ? 8.101   -26.227 70.437 1.00 53.43  ? 268 HIS   B O   1 
ATOM   4596 C  CB  . HIS   B  1  255 ? 10.448  -27.587 69.729 1.00 57.77  ? 268 HIS   B CB  1 
ATOM   4597 C  CG  . HIS   B  1  255 ? 11.620  -28.414 69.329 1.00 59.91  ? 268 HIS   B CG  1 
ATOM   4598 N  ND1 . HIS   B  1  255 ? 12.138  -29.376 70.164 1.00 59.38  ? 268 HIS   B ND1 1 
ATOM   4599 C  CD2 . HIS   B  1  255 ? 12.381  -28.429 68.216 1.00 64.34  ? 268 HIS   B CD2 1 
ATOM   4600 C  CE1 . HIS   B  1  255 ? 13.169  -29.958 69.565 1.00 66.94  ? 268 HIS   B CE1 1 
ATOM   4601 N  NE2 . HIS   B  1  255 ? 13.339  -29.396 68.384 1.00 67.95  ? 268 HIS   B NE2 1 
ATOM   4602 N  N   . PRO   B  1  256 ? 6.856   -28.092 70.659 1.00 53.41  ? 269 PRO   B N   1 
ATOM   4603 C  CA  . PRO   B  1  256 ? 5.731   -27.393 71.274 1.00 49.71  ? 269 PRO   B CA  1 
ATOM   4604 C  C   . PRO   B  1  256 ? 6.189   -26.453 72.378 1.00 46.63  ? 269 PRO   B C   1 
ATOM   4605 O  O   . PRO   B  1  256 ? 7.060   -26.785 73.173 1.00 48.41  ? 269 PRO   B O   1 
ATOM   4606 C  CB  . PRO   B  1  256 ? 4.870   -28.538 71.805 1.00 51.85  ? 269 PRO   B CB  1 
ATOM   4607 C  CG  . PRO   B  1  256 ? 5.109   -29.635 70.791 1.00 55.95  ? 269 PRO   B CG  1 
ATOM   4608 C  CD  . PRO   B  1  256 ? 6.597   -29.529 70.475 1.00 52.03  ? 269 PRO   B CD  1 
ATOM   4609 N  N   . TRP   B  1  257 ? 5.592   -25.264 72.395 1.00 47.77  ? 270 TRP   B N   1 
ATOM   4610 C  CA  . TRP   B  1  257 ? 6.041   -24.198 73.273 1.00 46.27  ? 270 TRP   B CA  1 
ATOM   4611 C  C   . TRP   B  1  257 ? 4.859   -23.301 73.622 1.00 44.57  ? 270 TRP   B C   1 
ATOM   4612 O  O   . TRP   B  1  257 ? 3.927   -23.140 72.838 1.00 45.83  ? 270 TRP   B O   1 
ATOM   4613 C  CB  . TRP   B  1  257 ? 7.182   -23.399 72.624 1.00 40.74  ? 270 TRP   B CB  1 
ATOM   4614 C  CG  . TRP   B  1  257 ? 7.858   -22.500 73.612 1.00 38.59  ? 270 TRP   B CG  1 
ATOM   4615 C  CD1 . TRP   B  1  257 ? 7.682   -21.157 73.786 1.00 42.73  ? 270 TRP   B CD1 1 
ATOM   4616 C  CD2 . TRP   B  1  257 ? 8.751   -22.932 74.655 1.00 39.13  ? 270 TRP   B CD2 1 
ATOM   4617 N  NE1 . TRP   B  1  257 ? 8.451   -20.717 74.829 1.00 47.45  ? 270 TRP   B NE1 1 
ATOM   4618 C  CE2 . TRP   B  1  257 ? 9.102   -21.787 75.390 1.00 40.22  ? 270 TRP   B CE2 1 
ATOM   4619 C  CE3 . TRP   B  1  257 ? 9.275   -24.171 75.035 1.00 43.41  ? 270 TRP   B CE3 1 
ATOM   4620 C  CZ2 . TRP   B  1  257 ? 9.961   -21.844 76.481 1.00 47.34  ? 270 TRP   B CZ2 1 
ATOM   4621 C  CZ3 . TRP   B  1  257 ? 10.109  -24.229 76.130 1.00 44.61  ? 270 TRP   B CZ3 1 
ATOM   4622 C  CH2 . TRP   B  1  257 ? 10.444  -23.081 76.844 1.00 46.10  ? 270 TRP   B CH2 1 
ATOM   4623 N  N   . VAL   B  1  258 ? 4.937   -22.706 74.810 1.00 44.66  ? 271 VAL   B N   1 
ATOM   4624 C  CA  . VAL   B  1  258 ? 3.811   -22.013 75.395 1.00 48.81  ? 271 VAL   B CA  1 
ATOM   4625 C  C   . VAL   B  1  258 ? 4.236   -20.577 75.657 1.00 45.01  ? 271 VAL   B C   1 
ATOM   4626 O  O   . VAL   B  1  258 ? 5.330   -20.332 76.150 1.00 44.92  ? 271 VAL   B O   1 
ATOM   4627 C  CB  . VAL   B  1  258 ? 3.360   -22.724 76.686 1.00 57.54  ? 271 VAL   B CB  1 
ATOM   4628 C  CG1 . VAL   B  1  258 ? 2.239   -21.974 77.393 1.00 62.29  ? 271 VAL   B CG1 1 
ATOM   4629 C  CG2 . VAL   B  1  258 ? 2.944   -24.168 76.423 1.00 58.79  ? 271 VAL   B CG2 1 
ATOM   4630 N  N   . PRO   B  1  259 ? 3.399   -19.578 75.312 1.00 41.79  ? 272 PRO   B N   1 
ATOM   4631 C  CA  . PRO   B  1  259 ? 3.752   -18.191 75.576 1.00 42.38  ? 272 PRO   B CA  1 
ATOM   4632 C  C   . PRO   B  1  259 ? 4.078   -17.993 77.051 1.00 41.28  ? 272 PRO   B C   1 
ATOM   4633 O  O   . PRO   B  1  259 ? 3.541   -18.679 77.900 1.00 39.03  ? 272 PRO   B O   1 
ATOM   4634 C  CB  . PRO   B  1  259 ? 2.522   -17.390 75.109 1.00 42.23  ? 272 PRO   B CB  1 
ATOM   4635 C  CG  . PRO   B  1  259 ? 1.413   -18.421 75.011 1.00 41.37  ? 272 PRO   B CG  1 
ATOM   4636 C  CD  . PRO   B  1  259 ? 2.102   -19.716 74.630 1.00 41.81  ? 272 PRO   B CD  1 
ATOM   4637 N  N   . GLY   B  1  260 ? 4.972   -17.041 77.321 1.00 42.17  ? 273 GLY   B N   1 
ATOM   4638 C  CA  . GLY   B  1  260 ? 5.357   -16.693 78.670 1.00 40.85  ? 273 GLY   B CA  1 
ATOM   4639 C  C   . GLY   B  1  260 ? 6.588   -15.800 78.654 1.00 43.33  ? 273 GLY   B C   1 
ATOM   4640 O  O   . GLY   B  1  260 ? 6.807   -15.068 77.700 1.00 44.10  ? 273 GLY   B O   1 
ATOM   4641 N  N   . GLY   B  1  261 ? 7.392   -15.889 79.718 1.00 47.40  ? 274 GLY   B N   1 
ATOM   4642 C  CA  . GLY   B  1  261 ? 8.581   -15.070 79.860 1.00 47.00  ? 274 GLY   B CA  1 
ATOM   4643 C  C   . GLY   B  1  261 ? 9.394   -15.457 81.096 1.00 52.26  ? 274 GLY   B C   1 
ATOM   4644 O  O   . GLY   B  1  261 ? 8.953   -16.244 81.935 1.00 50.07  ? 274 GLY   B O   1 
ATOM   4645 N  N   . ASN   B  1  262 ? 10.612  -14.914 81.172 1.00 47.84  ? 275 ASN   B N   1 
ATOM   4646 C  CA  . ASN   B  1  262 ? 11.427  -15.021 82.364 1.00 49.21  ? 275 ASN   B CA  1 
ATOM   4647 C  C   . ASN   B  1  262 ? 10.832  -14.109 83.431 1.00 51.50  ? 275 ASN   B C   1 
ATOM   4648 O  O   . ASN   B  1  262 ? 10.781  -12.904 83.233 1.00 47.22  ? 275 ASN   B O   1 
ATOM   4649 C  CB  . ASN   B  1  262 ? 12.882  -14.635 82.097 1.00 46.41  ? 275 ASN   B CB  1 
ATOM   4650 C  CG  . ASN   B  1  262 ? 13.734  -15.796 81.645 1.00 40.35  ? 275 ASN   B CG  1 
ATOM   4651 O  OD1 . ASN   B  1  262 ? 13.374  -16.957 81.852 1.00 36.80  ? 275 ASN   B OD1 1 
ATOM   4652 N  ND2 . ASN   B  1  262 ? 14.891  -15.501 81.069 1.00 43.17  ? 275 ASN   B ND2 1 
ATOM   4653 N  N   . ALA   B  1  263 ? 10.446  -14.677 84.582 1.00 56.73  ? 276 ALA   B N   1 
ATOM   4654 C  CA  . ALA   B  1  263 ? 9.880   -13.885 85.666 1.00 60.37  ? 276 ALA   B CA  1 
ATOM   4655 C  C   . ALA   B  1  263 ? 10.976  -13.354 86.591 1.00 61.93  ? 276 ALA   B C   1 
ATOM   4656 O  O   . ALA   B  1  263 ? 12.038  -13.954 86.721 1.00 60.38  ? 276 ALA   B O   1 
ATOM   4657 C  CB  . ALA   B  1  263 ? 8.867   -14.713 86.429 1.00 66.03  ? 276 ALA   B CB  1 
ATOM   4658 N  N   . ASP   B  1  264 ? 10.687  -12.206 87.213 1.00 70.64  ? 277 ASP   B N   1 
ATOM   4659 C  CA  . ASP   B  1  264 ? 11.417  -11.680 88.361 1.00 81.38  ? 277 ASP   B CA  1 
ATOM   4660 C  C   . ASP   B  1  264 ? 12.871  -11.371 88.006 1.00 79.40  ? 277 ASP   B C   1 
ATOM   4661 O  O   . ASP   B  1  264 ? 13.750  -11.579 88.835 1.00 87.34  ? 277 ASP   B O   1 
ATOM   4662 C  CB  . ASP   B  1  264 ? 11.356  -12.609 89.571 1.00 88.13  ? 277 ASP   B CB  1 
ATOM   4663 C  CG  . ASP   B  1  264 ? 9.965   -13.043 90.021 1.00 93.94  ? 277 ASP   B CG  1 
ATOM   4664 O  OD1 . ASP   B  1  264 ? 9.072   -12.170 90.152 1.00 87.18  ? 277 ASP   B OD1 1 
ATOM   4665 O  OD2 . ASP   B  1  264 ? 9.780   -14.264 90.228 1.00 91.38  ? 277 ASP   B OD2 1 
ATOM   4666 N  N   . ASN   B  1  265 ? 13.118  -10.884 86.785 1.00 70.76  ? 278 ASN   B N   1 
ATOM   4667 C  CA  . ASN   B  1  265 ? 14.436  -10.411 86.377 1.00 67.53  ? 278 ASN   B CA  1 
ATOM   4668 C  C   . ASN   B  1  265 ? 15.498  -11.490 86.594 1.00 59.69  ? 278 ASN   B C   1 
ATOM   4669 O  O   . ASN   B  1  265 ? 16.603  -11.169 87.015 1.00 56.20  ? 278 ASN   B O   1 
ATOM   4670 C  CB  . ASN   B  1  265 ? 14.859  -9.129  87.096 1.00 74.85  ? 278 ASN   B CB  1 
ATOM   4671 C  CG  . ASN   B  1  265 ? 14.174  -7.878  86.599 1.00 91.54  ? 278 ASN   B CG  1 
ATOM   4672 O  OD1 . ASN   B  1  265 ? 13.811  -7.756  85.422 1.00 90.18  ? 278 ASN   B OD1 1 
ATOM   4673 N  ND2 . ASN   B  1  265 ? 14.048  -6.894  87.476 1.00 105.60 ? 278 ASN   B ND2 1 
ATOM   4674 N  N   . GLN   B  1  266 ? 15.182  -12.751 86.262 1.00 54.52  ? 279 GLN   B N   1 
ATOM   4675 C  CA  . GLN   B  1  266 ? 16.124  -13.847 86.400 1.00 57.96  ? 279 GLN   B CA  1 
ATOM   4676 C  C   . GLN   B  1  266 ? 16.136  -14.698 85.136 1.00 54.56  ? 279 GLN   B C   1 
ATOM   4677 O  O   . GLN   B  1  266 ? 15.097  -14.963 84.548 1.00 55.61  ? 279 GLN   B O   1 
ATOM   4678 C  CB  . GLN   B  1  266 ? 15.709  -14.774 87.540 1.00 70.12  ? 279 GLN   B CB  1 
ATOM   4679 C  CG  . GLN   B  1  266 ? 15.971  -14.217 88.932 1.00 81.15  ? 279 GLN   B CG  1 
ATOM   4680 C  CD  . GLN   B  1  266 ? 15.396  -15.073 90.042 1.00 89.95  ? 279 GLN   B CD  1 
ATOM   4681 O  OE1 . GLN   B  1  266 ? 14.783  -16.130 89.834 1.00 76.67  ? 279 GLN   B OE1 1 
ATOM   4682 N  NE2 . GLN   B  1  266 ? 15.607  -14.614 91.264 1.00 96.03  ? 279 GLN   B NE2 1 
ATOM   4683 N  N   . VAL   B  1  267 ? 17.322  -15.184 84.773 1.00 52.42  ? 280 VAL   B N   1 
ATOM   4684 C  CA  . VAL   B  1  267 ? 17.452  -16.158 83.708 1.00 54.78  ? 280 VAL   B CA  1 
ATOM   4685 C  C   . VAL   B  1  267 ? 16.971  -17.530 84.187 1.00 51.82  ? 280 VAL   B C   1 
ATOM   4686 O  O   . VAL   B  1  267 ? 16.709  -17.742 85.359 1.00 56.37  ? 280 VAL   B O   1 
ATOM   4687 C  CB  . VAL   B  1  267 ? 18.893  -16.185 83.166 1.00 54.88  ? 280 VAL   B CB  1 
ATOM   4688 C  CG1 . VAL   B  1  267 ? 19.281  -14.835 82.557 1.00 57.30  ? 280 VAL   B CG1 1 
ATOM   4689 C  CG2 . VAL   B  1  267 ? 19.900  -16.618 84.225 1.00 56.88  ? 280 VAL   B CG2 1 
ATOM   4690 N  N   . ASN   B  1  268 ? 16.816  -18.443 83.233 1.00 54.39  ? 281 ASN   B N   1 
ATOM   4691 C  CA  . ASN   B  1  268 ? 16.364  -19.811 83.453 1.00 60.66  ? 281 ASN   B CA  1 
ATOM   4692 C  C   . ASN   B  1  268 ? 15.165  -19.835 84.394 1.00 59.19  ? 281 ASN   B C   1 
ATOM   4693 O  O   . ASN   B  1  268 ? 15.111  -20.664 85.291 1.00 52.84  ? 281 ASN   B O   1 
ATOM   4694 C  CB  . ASN   B  1  268 ? 17.505  -20.717 83.905 1.00 62.02  ? 281 ASN   B CB  1 
ATOM   4695 C  CG  . ASN   B  1  268 ? 18.594  -20.797 82.860 1.00 61.76  ? 281 ASN   B CG  1 
ATOM   4696 O  OD1 . ASN   B  1  268 ? 18.383  -21.355 81.775 1.00 60.61  ? 281 ASN   B OD1 1 
ATOM   4697 N  ND2 . ASN   B  1  268 ? 19.756  -20.234 83.159 1.00 58.31  ? 281 ASN   B ND2 1 
ATOM   4698 N  N   . ASN   B  1  269 ? 14.182  -18.966 84.134 1.00 60.86  ? 282 ASN   B N   1 
ATOM   4699 C  CA  . ASN   B  1  269 ? 13.040  -18.826 85.015 1.00 55.92  ? 282 ASN   B CA  1 
ATOM   4700 C  C   . ASN   B  1  269 ? 11.774  -18.537 84.199 1.00 53.11  ? 282 ASN   B C   1 
ATOM   4701 O  O   . ASN   B  1  269 ? 11.032  -17.594 84.484 1.00 51.32  ? 282 ASN   B O   1 
ATOM   4702 C  CB  . ASN   B  1  269 ? 13.366  -17.806 86.097 1.00 53.93  ? 282 ASN   B CB  1 
ATOM   4703 C  CG  . ASN   B  1  269 ? 12.337  -17.817 87.209 1.00 54.74  ? 282 ASN   B CG  1 
ATOM   4704 O  OD1 . ASN   B  1  269 ? 11.830  -18.890 87.577 1.00 49.87  ? 282 ASN   B OD1 1 
ATOM   4705 N  ND2 . ASN   B  1  269 ? 11.983  -16.638 87.709 1.00 49.08  ? 282 ASN   B ND2 1 
ATOM   4706 N  N   . TYR   B  1  270 ? 11.506  -19.392 83.207 1.00 52.99  ? 283 TYR   B N   1 
ATOM   4707 C  CA  . TYR   B  1  270 ? 10.403  -19.171 82.279 1.00 54.58  ? 283 TYR   B CA  1 
ATOM   4708 C  C   . TYR   B  1  270 ? 9.083   -19.612 82.917 1.00 56.05  ? 283 TYR   B C   1 
ATOM   4709 O  O   . TYR   B  1  270 ? 8.919   -20.771 83.281 1.00 55.22  ? 283 TYR   B O   1 
ATOM   4710 C  CB  . TYR   B  1  270 ? 10.664  -19.924 80.971 1.00 48.86  ? 283 TYR   B CB  1 
ATOM   4711 C  CG  . TYR   B  1  270 ? 9.747   -19.550 79.815 1.00 53.05  ? 283 TYR   B CG  1 
ATOM   4712 C  CD1 . TYR   B  1  270 ? 10.038  -18.465 78.983 1.00 54.46  ? 283 TYR   B CD1 1 
ATOM   4713 C  CD2 . TYR   B  1  270 ? 8.607   -20.297 79.539 1.00 52.13  ? 283 TYR   B CD2 1 
ATOM   4714 C  CE1 . TYR   B  1  270 ? 9.213   -18.132 77.925 1.00 55.24  ? 283 TYR   B CE1 1 
ATOM   4715 C  CE2 . TYR   B  1  270 ? 7.779   -19.978 78.474 1.00 54.91  ? 283 TYR   B CE2 1 
ATOM   4716 C  CZ  . TYR   B  1  270 ? 8.081   -18.888 77.674 1.00 57.30  ? 283 TYR   B CZ  1 
ATOM   4717 O  OH  . TYR   B  1  270 ? 7.272   -18.567 76.632 1.00 55.03  ? 283 TYR   B OH  1 
ATOM   4718 N  N   . VAL   B  1  271 ? 8.140   -18.668 83.012 1.00 58.25  ? 284 VAL   B N   1 
ATOM   4719 C  CA  . VAL   B  1  271 ? 6.800   -18.902 83.529 1.00 55.27  ? 284 VAL   B CA  1 
ATOM   4720 C  C   . VAL   B  1  271 ? 5.796   -18.689 82.402 1.00 53.02  ? 284 VAL   B C   1 
ATOM   4721 O  O   . VAL   B  1  271 ? 5.866   -17.695 81.680 1.00 51.42  ? 284 VAL   B O   1 
ATOM   4722 C  CB  . VAL   B  1  271 ? 6.502   -17.936 84.693 1.00 59.57  ? 284 VAL   B CB  1 
ATOM   4723 C  CG1 . VAL   B  1  271 ? 5.073   -18.080 85.211 1.00 59.12  ? 284 VAL   B CG1 1 
ATOM   4724 C  CG2 . VAL   B  1  271 ? 7.520   -18.083 85.824 1.00 63.86  ? 284 VAL   B CG2 1 
ATOM   4725 N  N   . GLU   B  1  272 ? 4.818   -19.594 82.301 1.00 52.13  ? 285 GLU   B N   1 
ATOM   4726 C  CA  . GLU   B  1  272 ? 3.821   -19.533 81.247 1.00 55.22  ? 285 GLU   B CA  1 
ATOM   4727 C  C   . GLU   B  1  272 ? 2.798   -18.432 81.527 1.00 57.68  ? 285 GLU   B C   1 
ATOM   4728 O  O   . GLU   B  1  272 ? 2.511   -18.151 82.684 1.00 59.35  ? 285 GLU   B O   1 
ATOM   4729 C  CB  . GLU   B  1  272 ? 3.141   -20.890 81.085 1.00 56.32  ? 285 GLU   B CB  1 
ATOM   4730 C  CG  . GLU   B  1  272 ? 4.128   -22.012 80.768 1.00 62.74  ? 285 GLU   B CG  1 
ATOM   4731 C  CD  . GLU   B  1  272 ? 3.519   -23.415 80.712 1.00 68.37  ? 285 GLU   B CD  1 
ATOM   4732 O  OE1 . GLU   B  1  272 ? 2.272   -23.524 80.841 1.00 64.29  ? 285 GLU   B OE1 1 
ATOM   4733 O  OE2 . GLU   B  1  272 ? 4.283   -24.403 80.527 1.00 56.03  ? 285 GLU   B OE2 1 
ATOM   4734 N  N   . ASP   B  1  273 ? 2.280   -17.809 80.452 1.00 61.66  ? 286 ASP   B N   1 
ATOM   4735 C  CA  . ASP   B  1  273 ? 1.158   -16.880 80.521 1.00 62.51  ? 286 ASP   B CA  1 
ATOM   4736 C  C   . ASP   B  1  273 ? -0.068  -17.534 79.889 1.00 61.50  ? 286 ASP   B C   1 
ATOM   4737 O  O   . ASP   B  1  273 ? -0.140  -17.671 78.670 1.00 58.71  ? 286 ASP   B O   1 
ATOM   4738 C  CB  . ASP   B  1  273 ? 1.459   -15.541 79.864 1.00 60.98  ? 286 ASP   B CB  1 
ATOM   4739 C  CG  . ASP   B  1  273 ? 0.361   -14.488 79.955 1.00 62.32  ? 286 ASP   B CG  1 
ATOM   4740 O  OD1 . ASP   B  1  273 ? -0.648  -14.742 80.642 1.00 68.26  ? 286 ASP   B OD1 1 
ATOM   4741 O  OD2 . ASP   B  1  273 ? 0.517   -13.426 79.321 1.00 66.89  ? 286 ASP   B OD2 1 
ATOM   4742 N  N   . PRO   B  1  274 ? -1.071  -17.955 80.691 1.00 67.43  ? 287 PRO   B N   1 
ATOM   4743 C  CA  . PRO   B  1  274 ? -2.274  -18.590 80.138 1.00 66.85  ? 287 PRO   B CA  1 
ATOM   4744 C  C   . PRO   B  1  274 ? -3.275  -17.651 79.447 1.00 61.02  ? 287 PRO   B C   1 
ATOM   4745 O  O   . PRO   B  1  274 ? -4.172  -18.131 78.750 1.00 61.15  ? 287 PRO   B O   1 
ATOM   4746 C  CB  . PRO   B  1  274 ? -2.863  -19.245 81.411 1.00 70.55  ? 287 PRO   B CB  1 
ATOM   4747 C  CG  . PRO   B  1  274 ? -2.515  -18.262 82.522 1.00 72.56  ? 287 PRO   B CG  1 
ATOM   4748 C  CD  . PRO   B  1  274 ? -1.104  -17.816 82.160 1.00 70.89  ? 287 PRO   B CD  1 
ATOM   4749 N  N   . ASP   B  1  275 ? -3.121  -16.327 79.646 1.00 53.01  ? 288 ASP   B N   1 
ATOM   4750 C  CA  . ASP   B  1  275 ? -3.980  -15.309 79.047 1.00 55.40  ? 288 ASP   B CA  1 
ATOM   4751 C  C   . ASP   B  1  275 ? -3.484  -14.840 77.671 1.00 53.59  ? 288 ASP   B C   1 
ATOM   4752 O  O   . ASP   B  1  275 ? -4.206  -14.163 76.941 1.00 53.77  ? 288 ASP   B O   1 
ATOM   4753 C  CB  . ASP   B  1  275 ? -4.113  -14.109 79.969 1.00 60.06  ? 288 ASP   B CB  1 
ATOM   4754 C  CG  . ASP   B  1  275 ? -4.898  -14.359 81.250 1.00 72.01  ? 288 ASP   B CG  1 
ATOM   4755 O  OD1 . ASP   B  1  275 ? -5.241  -15.530 81.541 1.00 73.05  ? 288 ASP   B OD1 1 
ATOM   4756 O  OD2 . ASP   B  1  275 ? -5.189  -13.360 81.940 1.00 79.31  ? 288 ASP   B OD2 1 
ATOM   4757 N  N   . SER   B  1  276 ? -2.245  -15.183 77.311 1.00 51.49  ? 289 SER   B N   1 
ATOM   4758 C  CA  . SER   B  1  276 ? -1.659  -14.747 76.060 1.00 47.61  ? 289 SER   B CA  1 
ATOM   4759 C  C   . SER   B  1  276 ? -2.421  -15.327 74.879 1.00 44.41  ? 289 SER   B C   1 
ATOM   4760 O  O   . SER   B  1  276 ? -2.957  -16.436 74.948 1.00 44.38  ? 289 SER   B O   1 
ATOM   4761 C  CB  . SER   B  1  276 ? -0.204  -15.141 75.997 1.00 48.35  ? 289 SER   B CB  1 
ATOM   4762 O  OG  . SER   B  1  276 ? 0.290   -15.100 74.670 1.00 43.98  ? 289 SER   B OG  1 
ATOM   4763 N  N   . ALA   B  1  277 ? -2.400  -14.598 73.771 1.00 41.48  ? 290 ALA   B N   1 
ATOM   4764 C  CA  . ALA   B  1  277 ? -2.739  -15.199 72.486 1.00 43.14  ? 290 ALA   B CA  1 
ATOM   4765 C  C   . ALA   B  1  277 ? -1.870  -16.424 72.217 1.00 43.37  ? 290 ALA   B C   1 
ATOM   4766 O  O   . ALA   B  1  277 ? -0.731  -16.488 72.669 1.00 43.85  ? 290 ALA   B O   1 
ATOM   4767 C  CB  . ALA   B  1  277 ? -2.527  -14.188 71.393 1.00 45.31  ? 290 ALA   B CB  1 
ATOM   4768 N  N   . ASP   B  1  278 ? -2.417  -17.387 71.476 1.00 44.78  ? 291 ASP   B N   1 
ATOM   4769 C  CA  . ASP   B  1  278 ? -1.628  -18.461 70.897 1.00 49.67  ? 291 ASP   B CA  1 
ATOM   4770 C  C   . ASP   B  1  278 ? -2.280  -18.837 69.568 1.00 46.42  ? 291 ASP   B C   1 
ATOM   4771 O  O   . ASP   B  1  278 ? -3.144  -18.099 69.091 1.00 41.80  ? 291 ASP   B O   1 
ATOM   4772 C  CB  . ASP   B  1  278 ? -1.443  -19.596 71.889 1.00 53.85  ? 291 ASP   B CB  1 
ATOM   4773 C  CG  . ASP   B  1  278 ? -2.696  -20.392 72.212 1.00 56.59  ? 291 ASP   B CG  1 
ATOM   4774 O  OD1 . ASP   B  1  278 ? -3.675  -20.311 71.427 1.00 54.38  ? 291 ASP   B OD1 1 
ATOM   4775 O  OD2 . ASP   B  1  278 ? -2.671  -21.093 73.238 1.00 58.54  ? 291 ASP   B OD2 1 
ATOM   4776 N  N   . PHE   B  1  279 ? -1.875  -19.963 68.964 1.00 46.67  ? 292 PHE   B N   1 
ATOM   4777 C  CA  . PHE   B  1  279 ? -2.272  -20.236 67.589 1.00 48.12  ? 292 PHE   B CA  1 
ATOM   4778 C  C   . PHE   B  1  279 ? -3.706  -20.751 67.503 1.00 54.03  ? 292 PHE   B C   1 
ATOM   4779 O  O   . PHE   B  1  279 ? -4.281  -20.739 66.412 1.00 51.75  ? 292 PHE   B O   1 
ATOM   4780 C  CB  . PHE   B  1  279 ? -1.282  -21.147 66.866 1.00 49.10  ? 292 PHE   B CB  1 
ATOM   4781 C  CG  . PHE   B  1  279 ? -0.084  -20.336 66.406 1.00 52.78  ? 292 PHE   B CG  1 
ATOM   4782 C  CD1 . PHE   B  1  279 ? -0.162  -19.557 65.254 1.00 53.56  ? 292 PHE   B CD1 1 
ATOM   4783 C  CD2 . PHE   B  1  279 ? 1.081   -20.295 67.167 1.00 49.16  ? 292 PHE   B CD2 1 
ATOM   4784 C  CE1 . PHE   B  1  279 ? 0.914   -18.784 64.849 1.00 52.65  ? 292 PHE   B CE1 1 
ATOM   4785 C  CE2 . PHE   B  1  279 ? 2.153   -19.534 66.751 1.00 54.24  ? 292 PHE   B CE2 1 
ATOM   4786 C  CZ  . PHE   B  1  279 ? 2.067   -18.780 65.594 1.00 55.74  ? 292 PHE   B CZ  1 
ATOM   4787 N  N   . THR   B  1  280 ? -4.301  -21.147 68.637 1.00 55.60  ? 293 THR   B N   1 
ATOM   4788 C  CA  . THR   B  1  280 ? -5.714  -21.504 68.648 1.00 60.03  ? 293 THR   B CA  1 
ATOM   4789 C  C   . THR   B  1  280 ? -6.550  -20.388 69.283 1.00 56.46  ? 293 THR   B C   1 
ATOM   4790 O  O   . THR   B  1  280 ? -7.764  -20.541 69.406 1.00 51.93  ? 293 THR   B O   1 
ATOM   4791 C  CB  . THR   B  1  280 ? -5.911  -22.850 69.355 1.00 58.09  ? 293 THR   B CB  1 
ATOM   4792 O  OG1 . THR   B  1  280 ? -5.533  -22.676 70.719 1.00 57.19  ? 293 THR   B OG1 1 
ATOM   4793 C  CG2 . THR   B  1  280 ? -5.103  -23.973 68.721 1.00 55.67  ? 293 THR   B CG2 1 
ATOM   4794 N  N   . HIS   B  1  281 ? -5.910  -19.272 69.670 1.00 53.86  ? 294 HIS   B N   1 
ATOM   4795 C  CA  . HIS   B  1  281 ? -6.592  -18.142 70.287 1.00 56.86  ? 294 HIS   B CA  1 
ATOM   4796 C  C   . HIS   B  1  281 ? -6.084  -16.841 69.660 1.00 48.36  ? 294 HIS   B C   1 
ATOM   4797 O  O   . HIS   B  1  281 ? -5.632  -15.944 70.365 1.00 52.57  ? 294 HIS   B O   1 
ATOM   4798 C  CB  . HIS   B  1  281 ? -6.407  -18.132 71.816 1.00 62.50  ? 294 HIS   B CB  1 
ATOM   4799 C  CG  . HIS   B  1  281 ? -6.933  -19.330 72.546 1.00 70.53  ? 294 HIS   B CG  1 
ATOM   4800 N  ND1 . HIS   B  1  281 ? -6.176  -20.461 72.773 1.00 76.83  ? 294 HIS   B ND1 1 
ATOM   4801 C  CD2 . HIS   B  1  281 ? -8.111  -19.547 73.155 1.00 66.13  ? 294 HIS   B CD2 1 
ATOM   4802 C  CE1 . HIS   B  1  281 ? -6.893  -21.336 73.467 1.00 75.94  ? 294 HIS   B CE1 1 
ATOM   4803 N  NE2 . HIS   B  1  281 ? -8.070  -20.798 73.715 1.00 69.10  ? 294 HIS   B NE2 1 
ATOM   4804 N  N   . LEU   B  1  282 ? -6.182  -16.726 68.334 1.00 45.23  ? 295 LEU   B N   1 
ATOM   4805 C  CA  . LEU   B  1  282 ? -5.596  -15.614 67.605 1.00 46.90  ? 295 LEU   B CA  1 
ATOM   4806 C  C   . LEU   B  1  282 ? -6.305  -14.293 67.894 1.00 49.09  ? 295 LEU   B C   1 
ATOM   4807 O  O   . LEU   B  1  282 ? -5.663  -13.237 67.873 1.00 49.13  ? 295 LEU   B O   1 
ATOM   4808 C  CB  . LEU   B  1  282 ? -5.569  -15.909 66.110 1.00 46.78  ? 295 LEU   B CB  1 
ATOM   4809 C  CG  . LEU   B  1  282 ? -4.488  -16.891 65.656 1.00 51.67  ? 295 LEU   B CG  1 
ATOM   4810 C  CD1 . LEU   B  1  282 ? -4.631  -17.216 64.173 1.00 53.99  ? 295 LEU   B CD1 1 
ATOM   4811 C  CD2 . LEU   B  1  282 ? -3.124  -16.298 65.929 1.00 54.09  ? 295 LEU   B CD2 1 
ATOM   4812 N  N   . CYS   B  1  283 ? -7.608  -14.341 68.188 1.00 50.70  ? 296 CYS   B N   1 
ATOM   4813 C  CA  . CYS   B  1  283 ? -8.359  -13.114 68.411 1.00 55.28  ? 296 CYS   B CA  1 
ATOM   4814 C  C   . CYS   B  1  283 ? -7.898  -12.398 69.678 1.00 53.31  ? 296 CYS   B C   1 
ATOM   4815 O  O   . CYS   B  1  283 ? -8.073  -11.191 69.779 1.00 53.64  ? 296 CYS   B O   1 
ATOM   4816 C  CB  . CYS   B  1  283 ? -9.866  -13.347 68.403 1.00 60.54  ? 296 CYS   B CB  1 
ATOM   4817 S  SG  . CYS   B  1  283 ? -10.527 -13.758 66.756 1.00 77.57  ? 296 CYS   B SG  1 
ATOM   4818 N  N   . ARG   B  1  284 ? -7.268  -13.114 70.617 1.00 50.46  ? 297 ARG   B N   1 
ATOM   4819 C  CA  . ARG   B  1  284 ? -6.668  -12.453 71.763 1.00 50.45  ? 297 ARG   B CA  1 
ATOM   4820 C  C   . ARG   B  1  284 ? -5.608  -11.453 71.318 1.00 48.48  ? 297 ARG   B C   1 
ATOM   4821 O  O   . ARG   B  1  284 ? -5.458  -10.409 71.953 1.00 51.43  ? 297 ARG   B O   1 
ATOM   4822 C  CB  . ARG   B  1  284 ? -6.028  -13.424 72.745 1.00 51.18  ? 297 ARG   B CB  1 
ATOM   4823 C  CG  . ARG   B  1  284 ? -7.031  -14.309 73.459 1.00 54.63  ? 297 ARG   B CG  1 
ATOM   4824 C  CD  . ARG   B  1  284 ? -6.319  -15.126 74.506 1.00 59.80  ? 297 ARG   B CD  1 
ATOM   4825 N  NE  . ARG   B  1  284 ? -7.191  -16.163 75.060 1.00 63.92  ? 297 ARG   B NE  1 
ATOM   4826 C  CZ  . ARG   B  1  284 ? -6.791  -17.173 75.820 1.00 65.22  ? 297 ARG   B CZ  1 
ATOM   4827 N  NH1 . ARG   B  1  284 ? -5.530  -17.283 76.205 1.00 63.73  ? 297 ARG   B NH1 1 
ATOM   4828 N  NH2 . ARG   B  1  284 ? -7.670  -18.075 76.202 1.00 62.60  ? 297 ARG   B NH2 1 
ATOM   4829 N  N   . LEU   B  1  285 ? -4.884  -11.772 70.238 1.00 40.90  ? 298 LEU   B N   1 
ATOM   4830 C  CA  . LEU   B  1  285 ? -3.869  -10.864 69.740 1.00 44.81  ? 298 LEU   B CA  1 
ATOM   4831 C  C   . LEU   B  1  285 ? -4.553  -9.551  69.348 1.00 43.30  ? 298 LEU   B C   1 
ATOM   4832 O  O   . LEU   B  1  285 ? -4.085  -8.457  69.692 1.00 43.35  ? 298 LEU   B O   1 
ATOM   4833 C  CB  . LEU   B  1  285 ? -3.066  -11.481 68.591 1.00 46.78  ? 298 LEU   B CB  1 
ATOM   4834 C  CG  . LEU   B  1  285 ? -1.852  -10.670 68.109 1.00 48.38  ? 298 LEU   B CG  1 
ATOM   4835 C  CD1 . LEU   B  1  285 ? -0.843  -11.529 67.404 1.00 50.53  ? 298 LEU   B CD1 1 
ATOM   4836 C  CD2 . LEU   B  1  285 ? -2.237  -9.548  67.167 1.00 49.59  ? 298 LEU   B CD2 1 
ATOM   4837 N  N   . TYR   B  1  286 ? -5.699  -9.674  68.671 1.00 42.66  ? 299 TYR   B N   1 
ATOM   4838 C  CA  . TYR   B  1  286 ? -6.448  -8.514  68.213 1.00 44.58  ? 299 TYR   B CA  1 
ATOM   4839 C  C   . TYR   B  1  286 ? -6.913  -7.668  69.399 1.00 39.07  ? 299 TYR   B C   1 
ATOM   4840 O  O   . TYR   B  1  286 ? -6.669  -6.473  69.424 1.00 41.84  ? 299 TYR   B O   1 
ATOM   4841 C  CB  . TYR   B  1  286 ? -7.595  -8.990  67.318 1.00 42.43  ? 299 TYR   B CB  1 
ATOM   4842 C  CG  . TYR   B  1  286 ? -8.533  -7.865  66.931 1.00 40.25  ? 299 TYR   B CG  1 
ATOM   4843 C  CD1 . TYR   B  1  286 ? -8.105  -6.828  66.118 1.00 38.48  ? 299 TYR   B CD1 1 
ATOM   4844 C  CD2 . TYR   B  1  286 ? -9.837  -7.827  67.407 1.00 42.00  ? 299 TYR   B CD2 1 
ATOM   4845 C  CE1 . TYR   B  1  286 ? -8.955  -5.794  65.765 1.00 40.60  ? 299 TYR   B CE1 1 
ATOM   4846 C  CE2 . TYR   B  1  286 ? -10.703 -6.804  67.045 1.00 36.49  ? 299 TYR   B CE2 1 
ATOM   4847 C  CZ  . TYR   B  1  286 ? -10.265 -5.791  66.222 1.00 37.50  ? 299 TYR   B CZ  1 
ATOM   4848 O  OH  . TYR   B  1  286 ? -11.120 -4.783  65.902 1.00 33.26  ? 299 TYR   B OH  1 
ATOM   4849 N  N   . GLU   B  1  287 ? -7.527  -8.302  70.395 1.00 41.14  ? 300 GLU   B N   1 
ATOM   4850 C  CA  . GLU   B  1  287 ? -7.988  -7.612  71.596 1.00 44.57  ? 300 GLU   B CA  1 
ATOM   4851 C  C   . GLU   B  1  287 ? -6.819  -6.967  72.340 1.00 41.92  ? 300 GLU   B C   1 
ATOM   4852 O  O   . GLU   B  1  287 ? -6.928  -5.816  72.772 1.00 48.87  ? 300 GLU   B O   1 
ATOM   4853 C  CB  . GLU   B  1  287 ? -8.735  -8.575  72.519 1.00 44.04  ? 300 GLU   B CB  1 
ATOM   4854 C  CG  . GLU   B  1  287 ? -10.050 -9.064  71.926 1.00 56.77  ? 300 GLU   B CG  1 
ATOM   4855 C  CD  . GLU   B  1  287 ? -10.621 -10.384 72.443 1.00 69.94  ? 300 GLU   B CD  1 
ATOM   4856 O  OE1 . GLU   B  1  287 ? -9.901  -11.223 73.038 1.00 70.60  ? 300 GLU   B OE1 1 
ATOM   4857 O  OE2 . GLU   B  1  287 ? -11.844 -10.573 72.241 1.00 74.79  ? 300 GLU   B OE2 1 
ATOM   4858 N  N   . PHE   B  1  288 ? -5.709  -7.710  72.489 1.00 38.58  ? 301 PHE   B N   1 
ATOM   4859 C  CA  . PHE   B  1  288 ? -4.534  -7.210  73.188 1.00 39.62  ? 301 PHE   B CA  1 
ATOM   4860 C  C   . PHE   B  1  288 ? -4.063  -5.912  72.530 1.00 39.23  ? 301 PHE   B C   1 
ATOM   4861 O  O   . PHE   B  1  288 ? -3.856  -4.904  73.205 1.00 39.56  ? 301 PHE   B O   1 
ATOM   4862 C  CB  . PHE   B  1  288 ? -3.437  -8.281  73.228 1.00 41.59  ? 301 PHE   B CB  1 
ATOM   4863 C  CG  . PHE   B  1  288 ? -2.231  -7.820  74.030 1.00 45.13  ? 301 PHE   B CG  1 
ATOM   4864 C  CD1 . PHE   B  1  288 ? -2.197  -7.996  75.414 1.00 42.97  ? 301 PHE   B CD1 1 
ATOM   4865 C  CD2 . PHE   B  1  288 ? -1.174  -7.157  73.408 1.00 42.68  ? 301 PHE   B CD2 1 
ATOM   4866 C  CE1 . PHE   B  1  288 ? -1.114  -7.536  76.152 1.00 49.85  ? 301 PHE   B CE1 1 
ATOM   4867 C  CE2 . PHE   B  1  288 ? -0.101  -6.690  74.156 1.00 45.07  ? 301 PHE   B CE2 1 
ATOM   4868 C  CZ  . PHE   B  1  288 ? -0.071  -6.876  75.524 1.00 46.38  ? 301 PHE   B CZ  1 
ATOM   4869 N  N   . VAL   B  1  289 ? -3.947  -5.933  71.193 1.00 39.14  ? 302 VAL   B N   1 
ATOM   4870 C  CA  . VAL   B  1  289 ? -3.408  -4.805  70.457 1.00 39.25  ? 302 VAL   B CA  1 
ATOM   4871 C  C   . VAL   B  1  289 ? -4.352  -3.611  70.535 1.00 39.19  ? 302 VAL   B C   1 
ATOM   4872 O  O   . VAL   B  1  289 ? -3.892  -2.476  70.657 1.00 35.84  ? 302 VAL   B O   1 
ATOM   4873 C  CB  . VAL   B  1  289 ? -3.081  -5.173  68.997 1.00 40.14  ? 302 VAL   B CB  1 
ATOM   4874 C  CG1 . VAL   B  1  289 ? -2.813  -3.946  68.141 1.00 37.05  ? 302 VAL   B CG1 1 
ATOM   4875 C  CG2 . VAL   B  1  289 ? -1.890  -6.116  68.917 1.00 39.55  ? 302 VAL   B CG2 1 
ATOM   4876 N  N   . VAL   B  1  290 ? -5.663  -3.848  70.441 1.00 40.20  ? 303 VAL   B N   1 
ATOM   4877 C  CA  . VAL   B  1  290 ? -6.625  -2.758  70.586 1.00 42.67  ? 303 VAL   B CA  1 
ATOM   4878 C  C   . VAL   B  1  290 ? -6.466  -2.086  71.957 1.00 42.55  ? 303 VAL   B C   1 
ATOM   4879 O  O   . VAL   B  1  290 ? -6.401  -0.845  72.031 1.00 40.91  ? 303 VAL   B O   1 
ATOM   4880 C  CB  . VAL   B  1  290 ? -8.064  -3.248  70.332 1.00 43.89  ? 303 VAL   B CB  1 
ATOM   4881 C  CG1 . VAL   B  1  290 ? -9.105  -2.240  70.780 1.00 41.12  ? 303 VAL   B CG1 1 
ATOM   4882 C  CG2 . VAL   B  1  290 ? -8.273  -3.639  68.871 1.00 42.89  ? 303 VAL   B CG2 1 
ATOM   4883 N  N   . GLY   B  1  291 ? -6.347  -2.903  73.023 1.00 43.06  ? 304 GLY   B N   1 
ATOM   4884 C  CA  . GLY   B  1  291 ? -5.968  -2.408  74.341 1.00 41.40  ? 304 GLY   B CA  1 
ATOM   4885 C  C   . GLY   B  1  291 ? -4.694  -1.552  74.296 1.00 44.32  ? 304 GLY   B C   1 
ATOM   4886 O  O   . GLY   B  1  291 ? -4.684  -0.441  74.802 1.00 43.20  ? 304 GLY   B O   1 
ATOM   4887 N  N   . SER   B  1  292 ? -3.622  -2.065  73.676 1.00 41.77  ? 305 SER   B N   1 
ATOM   4888 C  CA  . SER   B  1  292 ? -2.349  -1.357  73.628 1.00 36.75  ? 305 SER   B CA  1 
ATOM   4889 C  C   . SER   B  1  292 ? -2.507  -0.007  72.943 1.00 35.35  ? 305 SER   B C   1 
ATOM   4890 O  O   . SER   B  1  292 ? -1.893  0.973   73.362 1.00 37.84  ? 305 SER   B O   1 
ATOM   4891 C  CB  . SER   B  1  292 ? -1.286  -2.178  72.931 1.00 38.20  ? 305 SER   B CB  1 
ATOM   4892 O  OG  . SER   B  1  292 ? -1.196  -3.456  73.540 1.00 40.56  ? 305 SER   B OG  1 
ATOM   4893 N  N   . VAL   B  1  293 ? -3.330  0.048   71.888 1.00 35.15  ? 306 VAL   B N   1 
ATOM   4894 C  CA  . VAL   B  1  293 ? -3.551  1.300   71.187 1.00 37.87  ? 306 VAL   B CA  1 
ATOM   4895 C  C   . VAL   B  1  293 ? -4.237  2.310   72.108 1.00 41.94  ? 306 VAL   B C   1 
ATOM   4896 O  O   . VAL   B  1  293 ? -3.945  3.508   72.062 1.00 43.43  ? 306 VAL   B O   1 
ATOM   4897 C  CB  . VAL   B  1  293 ? -4.337  1.083   69.886 1.00 40.36  ? 306 VAL   B CB  1 
ATOM   4898 C  CG1 . VAL   B  1  293 ? -4.775  2.396   69.265 1.00 39.10  ? 306 VAL   B CG1 1 
ATOM   4899 C  CG2 . VAL   B  1  293 ? -3.510  0.306   68.874 1.00 44.98  ? 306 VAL   B CG2 1 
ATOM   4900 N  N   . GLN   B  1  294 ? -5.147  1.831   72.957 1.00 46.09  ? 307 GLN   B N   1 
ATOM   4901 C  CA  . GLN   B  1  294 ? -5.826  2.714   73.894 1.00 45.81  ? 307 GLN   B CA  1 
ATOM   4902 C  C   . GLN   B  1  294 ? -4.861  3.272   74.932 1.00 45.67  ? 307 GLN   B C   1 
ATOM   4903 O  O   . GLN   B  1  294 ? -5.018  4.416   75.325 1.00 50.94  ? 307 GLN   B O   1 
ATOM   4904 C  CB  . GLN   B  1  294 ? -6.978  1.991   74.570 1.00 47.93  ? 307 GLN   B CB  1 
ATOM   4905 C  CG  . GLN   B  1  294 ? -8.080  1.659   73.579 1.00 53.07  ? 307 GLN   B CG  1 
ATOM   4906 C  CD  . GLN   B  1  294 ? -9.159  0.834   74.217 1.00 53.67  ? 307 GLN   B CD  1 
ATOM   4907 O  OE1 . GLN   B  1  294 ? -9.088  -0.401  74.285 1.00 59.48  ? 307 GLN   B OE1 1 
ATOM   4908 N  NE2 . GLN   B  1  294 ? -10.122 1.562   74.740 1.00 56.59  ? 307 GLN   B NE2 1 
ATOM   4909 N  N   . GLU   B  1  295 ? -3.875  2.480   75.367 1.00 45.02  ? 308 GLU   B N   1 
ATOM   4910 C  CA  . GLU   B  1  295 ? -2.859  2.971   76.291 1.00 47.03  ? 308 GLU   B CA  1 
ATOM   4911 C  C   . GLU   B  1  295 ? -2.027  4.066   75.624 1.00 46.97  ? 308 GLU   B C   1 
ATOM   4912 O  O   . GLU   B  1  295 ? -1.715  5.042   76.278 1.00 50.87  ? 308 GLU   B O   1 
ATOM   4913 C  CB  . GLU   B  1  295 ? -1.992  1.842   76.843 1.00 53.66  ? 308 GLU   B CB  1 
ATOM   4914 C  CG  . GLU   B  1  295 ? -2.776  0.903   77.758 1.00 65.85  ? 308 GLU   B CG  1 
ATOM   4915 C  CD  . GLU   B  1  295 ? -2.134  -0.448  78.039 1.00 77.74  ? 308 GLU   B CD  1 
ATOM   4916 O  OE1 . GLU   B  1  295 ? -1.083  -0.762  77.425 1.00 76.84  ? 308 GLU   B OE1 1 
ATOM   4917 O  OE2 . GLU   B  1  295 ? -2.715  -1.190  78.868 1.00 79.73  ? 308 GLU   B OE2 1 
ATOM   4918 N  N   . LEU   B  1  296 ? -1.716  3.933   74.326 1.00 48.54  ? 309 LEU   B N   1 
ATOM   4919 C  CA  . LEU   B  1  296 ? -0.934  4.938   73.609 1.00 46.48  ? 309 LEU   B CA  1 
ATOM   4920 C  C   . LEU   B  1  296 ? -1.768  6.189   73.378 1.00 43.22  ? 309 LEU   B C   1 
ATOM   4921 O  O   . LEU   B  1  296 ? -1.230  7.297   73.360 1.00 44.53  ? 309 LEU   B O   1 
ATOM   4922 C  CB  . LEU   B  1  296 ? -0.386  4.450   72.267 1.00 44.84  ? 309 LEU   B CB  1 
ATOM   4923 C  CG  . LEU   B  1  296 ? 0.614   3.290   72.330 1.00 50.16  ? 309 LEU   B CG  1 
ATOM   4924 C  CD1 . LEU   B  1  296 ? 0.855   2.773   70.923 1.00 50.75  ? 309 LEU   B CD1 1 
ATOM   4925 C  CD2 . LEU   B  1  296 ? 1.936   3.705   73.020 1.00 49.58  ? 309 LEU   B CD2 1 
ATOM   4926 N  N   . TYR   B  1  297 ? -3.062  5.997   73.118 1.00 45.05  ? 310 TYR   B N   1 
ATOM   4927 C  CA  . TYR   B  1  297 ? -3.940  7.109   72.772 1.00 50.25  ? 310 TYR   B CA  1 
ATOM   4928 C  C   . TYR   B  1  297 ? -5.176  7.095   73.676 1.00 52.71  ? 310 TYR   B C   1 
ATOM   4929 O  O   . TYR   B  1  297 ? -6.230  6.641   73.254 1.00 49.10  ? 310 TYR   B O   1 
ATOM   4930 C  CB  . TYR   B  1  297 ? -4.345  6.998   71.300 1.00 45.95  ? 310 TYR   B CB  1 
ATOM   4931 C  CG  . TYR   B  1  297 ? -3.199  7.104   70.316 1.00 42.19  ? 310 TYR   B CG  1 
ATOM   4932 C  CD1 . TYR   B  1  297 ? -2.684  8.336   69.961 1.00 42.80  ? 310 TYR   B CD1 1 
ATOM   4933 C  CD2 . TYR   B  1  297 ? -2.637  5.977   69.738 1.00 44.16  ? 310 TYR   B CD2 1 
ATOM   4934 C  CE1 . TYR   B  1  297 ? -1.622  8.442   69.080 1.00 42.97  ? 310 TYR   B CE1 1 
ATOM   4935 C  CE2 . TYR   B  1  297 ? -1.586  6.071   68.836 1.00 42.49  ? 310 TYR   B CE2 1 
ATOM   4936 C  CZ  . TYR   B  1  297 ? -1.081  7.308   68.498 1.00 42.20  ? 310 TYR   B CZ  1 
ATOM   4937 O  OH  . TYR   B  1  297 ? -0.052  7.404   67.611 1.00 37.88  ? 310 TYR   B OH  1 
ATOM   4938 N  N   . PRO   B  1  298 ? -5.085  7.547   74.948 1.00 49.54  ? 311 PRO   B N   1 
ATOM   4939 C  CA  . PRO   B  1  298 ? -6.214  7.435   75.873 1.00 53.01  ? 311 PRO   B CA  1 
ATOM   4940 C  C   . PRO   B  1  298 ? -7.409  8.338   75.570 1.00 52.37  ? 311 PRO   B C   1 
ATOM   4941 O  O   . PRO   B  1  298 ? -8.546  7.946   75.800 1.00 55.66  ? 311 PRO   B O   1 
ATOM   4942 C  CB  . PRO   B  1  298 ? -5.652  7.711   77.269 1.00 55.64  ? 311 PRO   B CB  1 
ATOM   4943 C  CG  . PRO   B  1  298 ? -4.249  8.254   77.041 1.00 55.23  ? 311 PRO   B CG  1 
ATOM   4944 C  CD  . PRO   B  1  298 ? -3.881  8.114   75.570 1.00 54.91  ? 311 PRO   B CD  1 
ATOM   4945 N  N   . ASN   B  1  299 ? -7.169  9.517   74.990 1.00 50.96  ? 312 ASN   B N   1 
ATOM   4946 C  CA  . ASN   B  1  299 ? -8.245  10.465  74.731 1.00 54.30  ? 312 ASN   B CA  1 
ATOM   4947 C  C   . ASN   B  1  299 ? -7.889  11.324  73.522 1.00 56.14  ? 312 ASN   B C   1 
ATOM   4948 O  O   . ASN   B  1  299 ? -7.727  12.539  73.646 1.00 58.67  ? 312 ASN   B O   1 
ATOM   4949 C  CB  . ASN   B  1  299 ? -8.515  11.400  75.911 1.00 52.74  ? 312 ASN   B CB  1 
ATOM   4950 C  CG  . ASN   B  1  299 ? -8.756  10.689  77.221 1.00 58.93  ? 312 ASN   B CG  1 
ATOM   4951 O  OD1 . ASN   B  1  299 ? -7.953  10.822  78.156 1.00 61.33  ? 312 ASN   B OD1 1 
ATOM   4952 N  ND2 . ASN   B  1  299 ? -9.843  9.931   77.305 1.00 53.19  ? 312 ASN   B ND2 1 
ATOM   4953 N  N   . PRO   B  1  300 ? -7.793  10.739  72.304 1.00 52.60  ? 313 PRO   B N   1 
ATOM   4954 C  CA  . PRO   B  1  300 ? -7.463  11.528  71.120 1.00 53.30  ? 313 PRO   B CA  1 
ATOM   4955 C  C   . PRO   B  1  300 ? -8.660  12.353  70.648 1.00 56.76  ? 313 PRO   B C   1 
ATOM   4956 O  O   . PRO   B  1  300 ? -9.812  11.991  70.897 1.00 53.54  ? 313 PRO   B O   1 
ATOM   4957 C  CB  . PRO   B  1  300 ? -7.097  10.417  70.137 1.00 50.03  ? 313 PRO   B CB  1 
ATOM   4958 C  CG  . PRO   B  1  300 ? -8.073  9.295   70.482 1.00 49.18  ? 313 PRO   B CG  1 
ATOM   4959 C  CD  . PRO   B  1  300 ? -8.074  9.323   71.994 1.00 51.57  ? 313 PRO   B CD  1 
ATOM   4960 N  N   . THR   B  1  301 ? -8.375  13.442  69.935 1.00 61.68  ? 314 THR   B N   1 
ATOM   4961 C  CA  . THR   B  1  301 ? -9.417  14.256  69.324 1.00 67.78  ? 314 THR   B CA  1 
ATOM   4962 C  C   . THR   B  1  301 ? -8.989  14.595  67.898 1.00 64.50  ? 314 THR   B C   1 
ATOM   4963 O  O   . THR   B  1  301 ? -7.871  14.297  67.503 1.00 60.45  ? 314 THR   B O   1 
ATOM   4964 C  CB  . THR   B  1  301 ? -9.672  15.524  70.159 1.00 71.44  ? 314 THR   B CB  1 
ATOM   4965 O  OG1 . THR   B  1  301 ? -8.471  16.291  70.199 1.00 74.24  ? 314 THR   B OG1 1 
ATOM   4966 C  CG2 . THR   B  1  301 ? -10.069 15.249  71.600 1.00 68.08  ? 314 THR   B CG2 1 
ATOM   4967 N  N   . GLY   B  1  302 ? -9.888  15.233  67.147 1.00 64.53  ? 315 GLY   B N   1 
ATOM   4968 C  CA  . GLY   B  1  302 ? -9.571  15.776  65.834 1.00 63.90  ? 315 GLY   B CA  1 
ATOM   4969 C  C   . GLY   B  1  302 ? -9.151  14.695  64.834 1.00 65.30  ? 315 GLY   B C   1 
ATOM   4970 O  O   . GLY   B  1  302 ? -9.691  13.585  64.837 1.00 60.58  ? 315 GLY   B O   1 
ATOM   4971 N  N   . ILE   B  1  303 ? -8.165  15.043  63.995 1.00 66.08  ? 316 ILE   B N   1 
ATOM   4972 C  CA  . ILE   B  1  303 ? -7.710  14.188  62.908 1.00 65.41  ? 316 ILE   B CA  1 
ATOM   4973 C  C   . ILE   B  1  303 ? -7.093  12.918  63.488 1.00 52.49  ? 316 ILE   B C   1 
ATOM   4974 O  O   . ILE   B  1  303 ? -7.270  11.853  62.925 1.00 54.46  ? 316 ILE   B O   1 
ATOM   4975 C  CB  . ILE   B  1  303 ? -6.726  14.925  61.983 1.00 75.11  ? 316 ILE   B CB  1 
ATOM   4976 C  CG1 . ILE   B  1  303 ? -7.280  16.269  61.510 1.00 98.56  ? 316 ILE   B CG1 1 
ATOM   4977 C  CG2 . ILE   B  1  303 ? -6.374  14.053  60.783 1.00 76.13  ? 316 ILE   B CG2 1 
ATOM   4978 C  CD1 . ILE   B  1  303 ? -6.234  17.204  60.923 1.00 105.43 ? 316 ILE   B CD1 1 
ATOM   4979 N  N   . LEU   B  1  304 ? -6.402  13.025  64.619 1.00 44.65  ? 317 LEU   B N   1 
ATOM   4980 C  CA  . LEU   B  1  304 ? -5.785  11.869  65.246 1.00 45.88  ? 317 LEU   B CA  1 
ATOM   4981 C  C   . LEU   B  1  304 ? -6.862  10.846  65.585 1.00 48.33  ? 317 LEU   B C   1 
ATOM   4982 O  O   . LEU   B  1  304 ? -6.707  9.673   65.287 1.00 49.18  ? 317 LEU   B O   1 
ATOM   4983 C  CB  . LEU   B  1  304 ? -4.990  12.291  66.479 1.00 42.68  ? 317 LEU   B CB  1 
ATOM   4984 C  CG  . LEU   B  1  304 ? -4.415  11.165  67.334 1.00 48.10  ? 317 LEU   B CG  1 
ATOM   4985 C  CD1 . LEU   B  1  304 ? -3.488  10.319  66.473 1.00 47.05  ? 317 LEU   B CD1 1 
ATOM   4986 C  CD2 . LEU   B  1  304 ? -3.701  11.811  68.538 1.00 54.13  ? 317 LEU   B CD2 1 
ATOM   4987 N  N   . ARG   B  1  305 ? -7.964  11.301  66.191 1.00 50.50  ? 318 ARG   B N   1 
ATOM   4988 C  CA  . ARG   B  1  305 ? -9.042  10.406  66.569 1.00 50.02  ? 318 ARG   B CA  1 
ATOM   4989 C  C   . ARG   B  1  305 ? -9.608  9.745   65.313 1.00 44.53  ? 318 ARG   B C   1 
ATOM   4990 O  O   . ARG   B  1  305 ? -9.849  8.538   65.259 1.00 47.99  ? 318 ARG   B O   1 
ATOM   4991 C  CB  . ARG   B  1  305 ? -10.135 11.144  67.364 1.00 52.69  ? 318 ARG   B CB  1 
ATOM   4992 C  CG  . ARG   B  1  305 ? -11.366 10.259  67.604 1.00 52.03  ? 318 ARG   B CG  1 
ATOM   4993 C  CD  . ARG   B  1  305 ? -12.490 10.751  68.536 1.00 52.95  ? 318 ARG   B CD  1 
ATOM   4994 N  NE  . ARG   B  1  305 ? -12.099 10.564  69.942 1.00 54.57  ? 318 ARG   B NE  1 
ATOM   4995 C  CZ  . ARG   B  1  305 ? -12.614 9.729   70.847 1.00 52.21  ? 318 ARG   B CZ  1 
ATOM   4996 N  NH1 . ARG   B  1  305 ? -11.996 9.566   72.012 1.00 55.83  ? 318 ARG   B NH1 1 
ATOM   4997 N  NH2 . ARG   B  1  305 ? -13.695 9.017   70.592 1.00 46.42  ? 318 ARG   B NH2 1 
ATOM   4998 N  N   . ARG   B  1  306 ? -9.856  10.568  64.307 1.00 41.73  ? 319 ARG   B N   1 
ATOM   4999 C  CA  . ARG   B  1  306 ? -10.461 10.093  63.079 1.00 48.38  ? 319 ARG   B CA  1 
ATOM   5000 C  C   . ARG   B  1  306 ? -9.556  9.056   62.408 1.00 47.39  ? 319 ARG   B C   1 
ATOM   5001 O  O   . ARG   B  1  306 ? -10.037 8.020   61.956 1.00 47.00  ? 319 ARG   B O   1 
ATOM   5002 C  CB  . ARG   B  1  306 ? -10.701 11.323  62.205 1.00 58.11  ? 319 ARG   B CB  1 
ATOM   5003 C  CG  . ARG   B  1  306 ? -11.692 11.170  61.067 1.00 78.12  ? 319 ARG   B CG  1 
ATOM   5004 C  CD  . ARG   B  1  306 ? -11.641 12.433  60.195 1.00 94.12  ? 319 ARG   B CD  1 
ATOM   5005 N  NE  . ARG   B  1  306 ? -10.411 12.435  59.391 1.00 112.94 ? 319 ARG   B NE  1 
ATOM   5006 C  CZ  . ARG   B  1  306 ? -9.889  13.450  58.711 1.00 122.33 ? 319 ARG   B CZ  1 
ATOM   5007 N  NH1 . ARG   B  1  306 ? -10.513 14.614  58.685 1.00 123.11 ? 319 ARG   B NH1 1 
ATOM   5008 N  NH2 . ARG   B  1  306 ? -8.744  13.282  58.057 1.00 125.33 ? 319 ARG   B NH2 1 
ATOM   5009 N  N   . ASN   B  1  307 ? -8.245  9.320   62.366 1.00 43.62  ? 320 ASN   B N   1 
ATOM   5010 C  CA  . ASN   B  1  307 ? -7.319  8.427   61.685 1.00 45.11  ? 320 ASN   B CA  1 
ATOM   5011 C  C   . ASN   B  1  307 ? -7.136  7.155   62.496 1.00 43.58  ? 320 ASN   B C   1 
ATOM   5012 O  O   . ASN   B  1  307 ? -6.959  6.101   61.894 1.00 41.01  ? 320 ASN   B O   1 
ATOM   5013 C  CB  . ASN   B  1  307 ? -6.004  9.115   61.326 1.00 44.72  ? 320 ASN   B CB  1 
ATOM   5014 C  CG  . ASN   B  1  307 ? -6.198  10.123  60.215 1.00 44.89  ? 320 ASN   B CG  1 
ATOM   5015 O  OD1 . ASN   B  1  307 ? -7.326  10.305  59.751 1.00 48.54  ? 320 ASN   B OD1 1 
ATOM   5016 N  ND2 . ASN   B  1  307 ? -5.128  10.779  59.772 1.00 48.23  ? 320 ASN   B ND2 1 
ATOM   5017 N  N   . LEU   B  1  308 ? -7.205  7.239   63.831 1.00 39.42  ? 321 LEU   B N   1 
ATOM   5018 C  CA  . LEU   B  1  308 ? -7.187  6.039   64.656 1.00 42.87  ? 321 LEU   B CA  1 
ATOM   5019 C  C   . LEU   B  1  308 ? -8.345  5.128   64.263 1.00 44.35  ? 321 LEU   B C   1 
ATOM   5020 O  O   . LEU   B  1  308 ? -8.175  3.928   64.092 1.00 43.61  ? 321 LEU   B O   1 
ATOM   5021 C  CB  . LEU   B  1  308 ? -7.254  6.351   66.144 1.00 43.13  ? 321 LEU   B CB  1 
ATOM   5022 C  CG  . LEU   B  1  308 ? -5.914  6.543   66.844 1.00 46.38  ? 321 LEU   B CG  1 
ATOM   5023 C  CD1 . LEU   B  1  308 ? -6.129  7.297   68.146 1.00 50.32  ? 321 LEU   B CD1 1 
ATOM   5024 C  CD2 . LEU   B  1  308 ? -5.269  5.206   67.081 1.00 46.49  ? 321 LEU   B CD2 1 
ATOM   5025 N  N   . ILE   B  1  309 ? -9.534  5.704   64.144 1.00 42.97  ? 322 ILE   B N   1 
ATOM   5026 C  CA  . ILE   B  1  309 ? -10.723 4.927   63.871 1.00 41.44  ? 322 ILE   B CA  1 
ATOM   5027 C  C   . ILE   B  1  309 ? -10.582 4.204   62.532 1.00 39.52  ? 322 ILE   B C   1 
ATOM   5028 O  O   . ILE   B  1  309 ? -10.934 3.032   62.400 1.00 41.40  ? 322 ILE   B O   1 
ATOM   5029 C  CB  . ILE   B  1  309 ? -11.962 5.834   63.929 1.00 39.18  ? 322 ILE   B CB  1 
ATOM   5030 C  CG1 . ILE   B  1  309 ? -12.246 6.263   65.370 1.00 42.22  ? 322 ILE   B CG1 1 
ATOM   5031 C  CG2 . ILE   B  1  309 ? -13.156 5.131   63.295 1.00 36.37  ? 322 ILE   B CG2 1 
ATOM   5032 C  CD1 . ILE   B  1  309 ? -13.292 7.354   65.506 1.00 41.12  ? 322 ILE   B CD1 1 
ATOM   5033 N  N   . LYS   B  1  310 ? -10.088 4.922   61.529 1.00 42.31  ? 323 LYS   B N   1 
ATOM   5034 C  CA  . LYS   B  1  310 ? -9.934  4.358   60.195 1.00 45.18  ? 323 LYS   B CA  1 
ATOM   5035 C  C   . LYS   B  1  310 ? -8.856  3.263   60.148 1.00 41.30  ? 323 LYS   B C   1 
ATOM   5036 O  O   . LYS   B  1  310 ? -9.081  2.190   59.603 1.00 37.39  ? 323 LYS   B O   1 
ATOM   5037 C  CB  . LYS   B  1  310 ? -9.594  5.472   59.209 1.00 46.72  ? 323 LYS   B CB  1 
ATOM   5038 C  CG  . LYS   B  1  310 ? -10.765 6.349   58.865 1.00 55.65  ? 323 LYS   B CG  1 
ATOM   5039 C  CD  . LYS   B  1  310 ? -10.343 7.543   58.019 1.00 62.68  ? 323 LYS   B CD  1 
ATOM   5040 C  CE  . LYS   B  1  310 ? -11.453 8.205   57.274 1.00 70.33  ? 323 LYS   B CE  1 
ATOM   5041 N  NZ  . LYS   B  1  310 ? -11.003 9.522   56.825 1.00 77.50  ? 323 LYS   B NZ  1 
ATOM   5042 N  N   . ASN   B  1  311 ? -7.684  3.538   60.723 1.00 38.39  ? 324 ASN   B N   1 
ATOM   5043 C  CA  . ASN   B  1  311 ? -6.603  2.573   60.728 1.00 38.22  ? 324 ASN   B CA  1 
ATOM   5044 C  C   . ASN   B  1  311 ? -7.015  1.332   61.505 1.00 37.91  ? 324 ASN   B C   1 
ATOM   5045 O  O   . ASN   B  1  311 ? -6.680  0.228   61.110 1.00 38.73  ? 324 ASN   B O   1 
ATOM   5046 C  CB  . ASN   B  1  311 ? -5.314  3.200   61.232 1.00 38.08  ? 324 ASN   B CB  1 
ATOM   5047 C  CG  . ASN   B  1  311 ? -4.646  4.016   60.151 1.00 40.08  ? 324 ASN   B CG  1 
ATOM   5048 O  OD1 . ASN   B  1  311 ? -4.656  5.252   60.182 1.00 42.25  ? 324 ASN   B OD1 1 
ATOM   5049 N  ND2 . ASN   B  1  311 ? -4.104  3.343   59.156 1.00 42.36  ? 324 ASN   B ND2 1 
ATOM   5050 N  N   . LEU   B  1  312 ? -7.764  1.505   62.594 1.00 42.63  ? 325 LEU   B N   1 
ATOM   5051 C  CA  . LEU   B  1  312 ? -8.211  0.363   63.370 1.00 39.06  ? 325 LEU   B CA  1 
ATOM   5052 C  C   . LEU   B  1  312 ? -9.111  -0.509  62.504 1.00 38.04  ? 325 LEU   B C   1 
ATOM   5053 O  O   . LEU   B  1  312 ? -8.992  -1.737  62.524 1.00 37.59  ? 325 LEU   B O   1 
ATOM   5054 C  CB  . LEU   B  1  312 ? -8.898  0.802   64.655 1.00 38.84  ? 325 LEU   B CB  1 
ATOM   5055 C  CG  . LEU   B  1  312 ? -7.943  1.169   65.792 1.00 36.26  ? 325 LEU   B CG  1 
ATOM   5056 C  CD1 . LEU   B  1  312 ? -8.677  1.979   66.826 1.00 40.14  ? 325 LEU   B CD1 1 
ATOM   5057 C  CD2 . LEU   B  1  312 ? -7.368  -0.078  66.416 1.00 34.83  ? 325 LEU   B CD2 1 
ATOM   5058 N  N   . HIS   B  1  313 ? -9.993  0.147   61.743 1.00 36.15  ? 326 HIS   B N   1 
ATOM   5059 C  CA  . HIS   B  1  313 ? -10.892 -0.548  60.841 1.00 36.29  ? 326 HIS   B CA  1 
ATOM   5060 C  C   . HIS   B  1  313 ? -10.113 -1.257  59.730 1.00 35.01  ? 326 HIS   B C   1 
ATOM   5061 O  O   . HIS   B  1  313 ? -10.371 -2.412  59.411 1.00 35.10  ? 326 HIS   B O   1 
ATOM   5062 C  CB  . HIS   B  1  313 ? -11.938 0.418   60.263 1.00 36.28  ? 326 HIS   B CB  1 
ATOM   5063 C  CG  . HIS   B  1  313 ? -12.867 -0.271  59.326 1.00 37.85  ? 326 HIS   B CG  1 
ATOM   5064 N  ND1 . HIS   B  1  313 ? -13.668 -1.325  59.728 1.00 41.78  ? 326 HIS   B ND1 1 
ATOM   5065 C  CD2 . HIS   B  1  313 ? -13.034 -0.148  58.007 1.00 40.22  ? 326 HIS   B CD2 1 
ATOM   5066 C  CE1 . HIS   B  1  313 ? -14.335 -1.790  58.679 1.00 42.46  ? 326 HIS   B CE1 1 
ATOM   5067 N  NE2 . HIS   B  1  313 ? -13.953 -1.087  57.612 1.00 40.89  ? 326 HIS   B NE2 1 
ATOM   5068 N  N   . TYR   B  1  314 ? -9.167  -0.551  59.108 1.00 33.77  ? 327 TYR   B N   1 
ATOM   5069 C  CA  . TYR   B  1  314 ? -8.361  -1.165  58.059 1.00 34.99  ? 327 TYR   B CA  1 
ATOM   5070 C  C   . TYR   B  1  314 ? -7.659  -2.407  58.598 1.00 34.17  ? 327 TYR   B C   1 
ATOM   5071 O  O   . TYR   B  1  314 ? -7.653  -3.435  57.930 1.00 32.62  ? 327 TYR   B O   1 
ATOM   5072 C  CB  . TYR   B  1  314 ? -7.315  -0.195  57.546 1.00 34.01  ? 327 TYR   B CB  1 
ATOM   5073 C  CG  . TYR   B  1  314 ? -7.860  1.070   56.914 1.00 34.39  ? 327 TYR   B CG  1 
ATOM   5074 C  CD1 . TYR   B  1  314 ? -9.144  1.126   56.386 1.00 37.64  ? 327 TYR   B CD1 1 
ATOM   5075 C  CD2 . TYR   B  1  314 ? -7.083  2.212   56.865 1.00 37.87  ? 327 TYR   B CD2 1 
ATOM   5076 C  CE1 . TYR   B  1  314 ? -9.631  2.278   55.791 1.00 38.14  ? 327 TYR   B CE1 1 
ATOM   5077 C  CE2 . TYR   B  1  314 ? -7.559  3.374   56.277 1.00 45.47  ? 327 TYR   B CE2 1 
ATOM   5078 C  CZ  . TYR   B  1  314 ? -8.836  3.409   55.743 1.00 42.11  ? 327 TYR   B CZ  1 
ATOM   5079 O  OH  . TYR   B  1  314 ? -9.265  4.568   55.159 1.00 42.70  ? 327 TYR   B OH  1 
ATOM   5080 N  N   . TRP   B  1  315 ? -7.127  -2.314  59.825 1.00 30.28  ? 328 TRP   B N   1 
ATOM   5081 C  CA  . TRP   B  1  315 ? -6.417  -3.425  60.411 1.00 33.08  ? 328 TRP   B CA  1 
ATOM   5082 C  C   . TRP   B  1  315 ? -7.373  -4.601  60.516 1.00 35.35  ? 328 TRP   B C   1 
ATOM   5083 O  O   . TRP   B  1  315 ? -7.036  -5.726  60.135 1.00 36.49  ? 328 TRP   B O   1 
ATOM   5084 C  CB  . TRP   B  1  315 ? -5.808  -3.074  61.773 1.00 32.06  ? 328 TRP   B CB  1 
ATOM   5085 C  CG  . TRP   B  1  315 ? -4.862  -4.126  62.278 1.00 33.15  ? 328 TRP   B CG  1 
ATOM   5086 C  CD1 . TRP   B  1  315 ? -3.860  -4.744  61.587 1.00 32.94  ? 328 TRP   B CD1 1 
ATOM   5087 C  CD2 . TRP   B  1  315 ? -4.839  -4.691  63.600 1.00 34.84  ? 328 TRP   B CD2 1 
ATOM   5088 N  NE1 . TRP   B  1  315 ? -3.239  -5.668  62.378 1.00 36.11  ? 328 TRP   B NE1 1 
ATOM   5089 C  CE2 . TRP   B  1  315 ? -3.804  -5.651  63.620 1.00 33.92  ? 328 TRP   B CE2 1 
ATOM   5090 C  CE3 . TRP   B  1  315 ? -5.570  -4.466  64.764 1.00 32.77  ? 328 TRP   B CE3 1 
ATOM   5091 C  CZ2 . TRP   B  1  315 ? -3.494  -6.387  64.752 1.00 34.18  ? 328 TRP   B CZ2 1 
ATOM   5092 C  CZ3 . TRP   B  1  315 ? -5.248  -5.176  65.895 1.00 35.26  ? 328 TRP   B CZ3 1 
ATOM   5093 C  CH2 . TRP   B  1  315 ? -4.226  -6.126  65.888 1.00 36.44  ? 328 TRP   B CH2 1 
ATOM   5094 N  N   . TRP   B  1  316 ? -8.581  -4.311  60.997 1.00 35.78  ? 329 TRP   B N   1 
ATOM   5095 C  CA  . TRP   B  1  316 ? -9.554  -5.359  61.224 1.00 33.56  ? 329 TRP   B CA  1 
ATOM   5096 C  C   . TRP   B  1  316 ? -9.900  -6.068  59.917 1.00 31.62  ? 329 TRP   B C   1 
ATOM   5097 O  O   . TRP   B  1  316 ? -10.137 -7.274  59.917 1.00 28.48  ? 329 TRP   B O   1 
ATOM   5098 C  CB  . TRP   B  1  316 ? -10.810 -4.792  61.885 1.00 38.22  ? 329 TRP   B CB  1 
ATOM   5099 C  CG  . TRP   B  1  316 ? -11.895 -5.825  61.990 1.00 36.82  ? 329 TRP   B CG  1 
ATOM   5100 C  CD1 . TRP   B  1  316 ? -12.028 -6.767  62.961 1.00 36.14  ? 329 TRP   B CD1 1 
ATOM   5101 C  CD2 . TRP   B  1  316 ? -12.939 -6.068  61.032 1.00 34.33  ? 329 TRP   B CD2 1 
ATOM   5102 N  NE1 . TRP   B  1  316 ? -13.108 -7.554  62.697 1.00 38.83  ? 329 TRP   B NE1 1 
ATOM   5103 C  CE2 . TRP   B  1  316 ? -13.683 -7.153  61.521 1.00 34.56  ? 329 TRP   B CE2 1 
ATOM   5104 C  CE3 . TRP   B  1  316 ? -13.319 -5.466  59.826 1.00 42.21  ? 329 TRP   B CE3 1 
ATOM   5105 C  CZ2 . TRP   B  1  316 ? -14.796 -7.653  60.849 1.00 39.98  ? 329 TRP   B CZ2 1 
ATOM   5106 C  CZ3 . TRP   B  1  316 ? -14.435 -5.951  59.165 1.00 39.71  ? 329 TRP   B CZ3 1 
ATOM   5107 C  CH2 . TRP   B  1  316 ? -15.146 -7.047  59.662 1.00 37.19  ? 329 TRP   B CH2 1 
ATOM   5108 N  N   . THR   B  1  317 ? -9.931  -5.340  58.796 1.00 33.17  ? 330 THR   B N   1 
ATOM   5109 C  CA  . THR   B  1  317 ? -10.306 -5.987  57.543 1.00 40.97  ? 330 THR   B CA  1 
ATOM   5110 C  C   . THR   B  1  317 ? -9.358  -7.154  57.276 1.00 39.06  ? 330 THR   B C   1 
ATOM   5111 O  O   . THR   B  1  317 ? -9.792  -8.193  56.801 1.00 42.40  ? 330 THR   B O   1 
ATOM   5112 C  CB  . THR   B  1  317 ? -10.336 -5.054  56.328 1.00 42.96  ? 330 THR   B CB  1 
ATOM   5113 O  OG1 . THR   B  1  317 ? -9.016  -4.553  56.111 1.00 42.64  ? 330 THR   B OG1 1 
ATOM   5114 C  CG2 . THR   B  1  317 ? -11.352 -3.935  56.482 1.00 41.96  ? 330 THR   B CG2 1 
ATOM   5115 N  N   . GLY   B  1  318 ? -8.072  -6.967  57.564 1.00 36.22  ? 331 GLY   B N   1 
ATOM   5116 C  CA  . GLY   B  1  318 ? -7.103  -8.029  57.374 1.00 38.80  ? 331 GLY   B CA  1 
ATOM   5117 C  C   . GLY   B  1  318 ? -7.175  -9.082  58.471 1.00 37.57  ? 331 GLY   B C   1 
ATOM   5118 O  O   . GLY   B  1  318 ? -7.082  -10.269 58.174 1.00 42.38  ? 331 GLY   B O   1 
ATOM   5119 N  N   . VAL   B  1  319 ? -7.302  -8.631  59.727 1.00 36.05  ? 332 VAL   B N   1 
ATOM   5120 C  CA  . VAL   B  1  319 ? -7.324  -9.520  60.875 1.00 36.87  ? 332 VAL   B CA  1 
ATOM   5121 C  C   . VAL   B  1  319 ? -8.474  -10.502 60.716 1.00 37.11  ? 332 VAL   B C   1 
ATOM   5122 O  O   . VAL   B  1  319 ? -8.345  -11.679 61.046 1.00 40.10  ? 332 VAL   B O   1 
ATOM   5123 C  CB  . VAL   B  1  319 ? -7.476  -8.714  62.180 1.00 39.88  ? 332 VAL   B CB  1 
ATOM   5124 C  CG1 . VAL   B  1  319 ? -7.724  -9.605  63.380 1.00 42.90  ? 332 VAL   B CG1 1 
ATOM   5125 C  CG2 . VAL   B  1  319 ? -6.273  -7.840  62.467 1.00 41.05  ? 332 VAL   B CG2 1 
ATOM   5126 N  N   . ASN   B  1  320 ? -9.613  -9.988  60.248 1.00 36.58  ? 333 ASN   B N   1 
ATOM   5127 C  CA  . ASN   B  1  320 ? -10.833 -10.774 60.200 1.00 39.29  ? 333 ASN   B CA  1 
ATOM   5128 C  C   . ASN   B  1  320 ? -10.646 -11.997 59.317 1.00 41.14  ? 333 ASN   B C   1 
ATOM   5129 O  O   . ASN   B  1  320 ? -11.070 -13.091 59.691 1.00 36.74  ? 333 ASN   B O   1 
ATOM   5130 C  CB  . ASN   B  1  320 ? -12.014 -9.961  59.684 1.00 44.83  ? 333 ASN   B CB  1 
ATOM   5131 C  CG  . ASN   B  1  320 ? -13.323 -10.678 59.912 1.00 43.93  ? 333 ASN   B CG  1 
ATOM   5132 O  OD1 . ASN   B  1  320 ? -13.579 -11.182 61.009 1.00 47.32  ? 333 ASN   B OD1 1 
ATOM   5133 N  ND2 . ASN   B  1  320 ? -14.148 -10.766 58.889 1.00 40.89  ? 333 ASN   B ND2 1 
ATOM   5134 N  N   . VAL   B  1  321 ? -9.996  -11.797 58.162 1.00 43.69  ? 334 VAL   B N   1 
ATOM   5135 C  CA  . VAL   B  1  321 ? -9.687  -12.900 57.268 1.00 45.28  ? 334 VAL   B CA  1 
ATOM   5136 C  C   . VAL   B  1  321 ? -8.529  -13.726 57.832 1.00 46.28  ? 334 VAL   B C   1 
ATOM   5137 O  O   . VAL   B  1  321 ? -8.672  -14.925 58.023 1.00 49.25  ? 334 VAL   B O   1 
ATOM   5138 C  CB  . VAL   B  1  321 ? -9.376  -12.413 55.841 1.00 52.48  ? 334 VAL   B CB  1 
ATOM   5139 C  CG1 . VAL   B  1  321 ? -9.092  -13.592 54.909 1.00 49.91  ? 334 VAL   B CG1 1 
ATOM   5140 C  CG2 . VAL   B  1  321 ? -10.473 -11.511 55.276 1.00 45.34  ? 334 VAL   B CG2 1 
ATOM   5141 N  N   . ALA   B  1  322 ? -7.391  -13.099 58.149 1.00 49.30  ? 335 ALA   B N   1 
ATOM   5142 C  CA  . ALA   B  1  322 ? -6.204  -13.851 58.539 1.00 49.41  ? 335 ALA   B CA  1 
ATOM   5143 C  C   . ALA   B  1  322 ? -6.423  -14.676 59.809 1.00 47.42  ? 335 ALA   B C   1 
ATOM   5144 O  O   . ALA   B  1  322 ? -5.833  -15.742 59.937 1.00 49.94  ? 335 ALA   B O   1 
ATOM   5145 C  CB  . ALA   B  1  322 ? -5.012  -12.931 58.713 1.00 51.60  ? 335 ALA   B CB  1 
ATOM   5146 N  N   . PHE   B  1  323 ? -7.224  -14.183 60.765 1.00 46.84  ? 336 PHE   B N   1 
ATOM   5147 C  CA  . PHE   B  1  323 ? -7.370  -14.873 62.038 1.00 46.77  ? 336 PHE   B CA  1 
ATOM   5148 C  C   . PHE   B  1  323 ? -8.652  -15.706 62.065 1.00 48.22  ? 336 PHE   B C   1 
ATOM   5149 O  O   . PHE   B  1  323 ? -8.984  -16.269 63.101 1.00 47.47  ? 336 PHE   B O   1 
ATOM   5150 C  CB  . PHE   B  1  323 ? -7.384  -13.906 63.222 1.00 45.68  ? 336 PHE   B CB  1 
ATOM   5151 C  CG  . PHE   B  1  323 ? -6.098  -13.157 63.536 1.00 47.54  ? 336 PHE   B CG  1 
ATOM   5152 C  CD1 . PHE   B  1  323 ? -4.960  -13.273 62.745 1.00 49.57  ? 336 PHE   B CD1 1 
ATOM   5153 C  CD2 . PHE   B  1  323 ? -6.049  -12.284 64.618 1.00 47.39  ? 336 PHE   B CD2 1 
ATOM   5154 C  CE1 . PHE   B  1  323 ? -3.814  -12.539 63.038 1.00 47.05  ? 336 PHE   B CE1 1 
ATOM   5155 C  CE2 . PHE   B  1  323 ? -4.898  -11.568 64.915 1.00 47.18  ? 336 PHE   B CE2 1 
ATOM   5156 C  CZ  . PHE   B  1  323 ? -3.782  -11.702 64.125 1.00 47.82  ? 336 PHE   B CZ  1 
ATOM   5157 N  N   . GLY   B  1  324 ? -9.371  -15.776 60.939 1.00 49.66  ? 337 GLY   B N   1 
ATOM   5158 C  CA  . GLY   B  1  324 ? -10.532 -16.648 60.808 1.00 50.47  ? 337 GLY   B CA  1 
ATOM   5159 C  C   . GLY   B  1  324 ? -11.781 -16.130 61.527 1.00 48.14  ? 337 GLY   B C   1 
ATOM   5160 O  O   . GLY   B  1  324 ? -12.598 -16.937 61.954 1.00 49.10  ? 337 GLY   B O   1 
ATOM   5161 N  N   . GLY   B  1  325 ? -11.938 -14.798 61.631 1.00 47.32  ? 338 GLY   B N   1 
ATOM   5162 C  CA  . GLY   B  1  325 ? -13.144 -14.161 62.167 1.00 43.75  ? 338 GLY   B CA  1 
ATOM   5163 C  C   . GLY   B  1  325 ? -12.933 -13.641 63.595 1.00 44.39  ? 338 GLY   B C   1 
ATOM   5164 O  O   . GLY   B  1  325 ? -12.793 -14.439 64.523 1.00 42.08  ? 338 GLY   B O   1 
ATOM   5165 N  N   . CYS   B  1  326 ? -12.867 -12.308 63.755 1.00 45.36  ? 339 CYS   B N   1 
ATOM   5166 C  CA  . CYS   B  1  326 ? -12.780 -11.657 65.058 1.00 50.51  ? 339 CYS   B CA  1 
ATOM   5167 C  C   . CYS   B  1  326 ? -13.849 -10.572 65.101 1.00 50.93  ? 339 CYS   B C   1 
ATOM   5168 O  O   . CYS   B  1  326 ? -14.068 -9.894  64.091 1.00 47.68  ? 339 CYS   B O   1 
ATOM   5169 C  CB  . CYS   B  1  326 ? -11.416 -11.002 65.306 1.00 54.49  ? 339 CYS   B CB  1 
ATOM   5170 S  SG  . CYS   B  1  326 ? -10.033 -12.172 65.428 1.00 79.23  ? 339 CYS   B SG  1 
ATOM   5171 N  N   . ASP   B  1  327 ? -14.481 -10.395 66.266 1.00 51.68  ? 340 ASP   B N   1 
ATOM   5172 C  CA  . ASP   B  1  327 ? -15.476 -9.343  66.425 1.00 52.36  ? 340 ASP   B CA  1 
ATOM   5173 C  C   . ASP   B  1  327 ? -14.777 -7.986  66.413 1.00 46.43  ? 340 ASP   B C   1 
ATOM   5174 O  O   . ASP   B  1  327 ? -13.833 -7.769  67.168 1.00 47.19  ? 340 ASP   B O   1 
ATOM   5175 C  CB  . ASP   B  1  327 ? -16.269 -9.502  67.713 1.00 63.40  ? 340 ASP   B CB  1 
ATOM   5176 C  CG  . ASP   B  1  327 ? -17.043 -10.803 67.887 1.00 64.76  ? 340 ASP   B CG  1 
ATOM   5177 O  OD1 . ASP   B  1  327 ? -17.236 -11.519 66.889 1.00 65.11  ? 340 ASP   B OD1 1 
ATOM   5178 O  OD2 . ASP   B  1  327 ? -17.426 -11.095 69.032 1.00 72.32  ? 340 ASP   B OD2 1 
ATOM   5179 N  N   . GLU   B  1  328 ? -15.222 -7.081  65.539 1.00 45.08  ? 341 GLU   B N   1 
ATOM   5180 C  CA  . GLU   B  1  328 ? -14.594 -5.778  65.426 1.00 40.62  ? 341 GLU   B CA  1 
ATOM   5181 C  C   . GLU   B  1  328 ? -14.847 -4.975  66.699 1.00 41.48  ? 341 GLU   B C   1 
ATOM   5182 O  O   . GLU   B  1  328 ? -15.954 -4.960  67.214 1.00 41.23  ? 341 GLU   B O   1 
ATOM   5183 C  CB  . GLU   B  1  328 ? -15.053 -5.027  64.177 1.00 38.44  ? 341 GLU   B CB  1 
ATOM   5184 C  CG  . GLU   B  1  328 ? -14.244 -3.753  63.947 1.00 38.42  ? 341 GLU   B CG  1 
ATOM   5185 C  CD  . GLU   B  1  328 ? -14.472 -3.019  62.648 1.00 37.49  ? 341 GLU   B CD  1 
ATOM   5186 O  OE1 . GLU   B  1  328 ? -15.333 -3.455  61.875 1.00 44.83  ? 341 GLU   B OE1 1 
ATOM   5187 O  OE2 . GLU   B  1  328 ? -13.782 -2.011  62.423 1.00 40.68  ? 341 GLU   B OE2 1 
ATOM   5188 N  N   . LEU   B  1  329 ? -13.793 -4.315  67.189 1.00 38.76  ? 342 LEU   B N   1 
ATOM   5189 C  CA  . LEU   B  1  329 ? -13.890 -3.445  68.338 1.00 40.86  ? 342 LEU   B CA  1 
ATOM   5190 C  C   . LEU   B  1  329 ? -13.813 -2.003  67.848 1.00 41.19  ? 342 LEU   B C   1 
ATOM   5191 O  O   . LEU   B  1  329 ? -13.142 -1.712  66.861 1.00 44.62  ? 342 LEU   B O   1 
ATOM   5192 C  CB  . LEU   B  1  329 ? -12.773 -3.782  69.326 1.00 45.58  ? 342 LEU   B CB  1 
ATOM   5193 C  CG  . LEU   B  1  329 ? -12.789 -5.204  69.902 1.00 49.94  ? 342 LEU   B CG  1 
ATOM   5194 C  CD1 . LEU   B  1  329 ? -11.547 -5.447  70.747 1.00 52.44  ? 342 LEU   B CD1 1 
ATOM   5195 C  CD2 . LEU   B  1  329 ? -14.067 -5.530  70.688 1.00 49.48  ? 342 LEU   B CD2 1 
ATOM   5196 N  N   . PHE   B  1  330 ? -14.490 -1.106  68.571 1.00 41.58  ? 343 PHE   B N   1 
ATOM   5197 C  CA  . PHE   B  1  330 ? -14.564 0.305   68.221 1.00 41.50  ? 343 PHE   B CA  1 
ATOM   5198 C  C   . PHE   B  1  330 ? -14.239 1.127   69.468 1.00 45.36  ? 343 PHE   B C   1 
ATOM   5199 O  O   . PHE   B  1  330 ? -15.111 1.776   70.040 1.00 47.85  ? 343 PHE   B O   1 
ATOM   5200 C  CB  . PHE   B  1  330 ? -15.955 0.670   67.709 1.00 40.22  ? 343 PHE   B CB  1 
ATOM   5201 C  CG  . PHE   B  1  330 ? -16.418 -0.175  66.546 1.00 39.65  ? 343 PHE   B CG  1 
ATOM   5202 C  CD1 . PHE   B  1  330 ? -15.988 0.119   65.259 1.00 42.62  ? 343 PHE   B CD1 1 
ATOM   5203 C  CD2 . PHE   B  1  330 ? -17.252 -1.272  66.740 1.00 43.68  ? 343 PHE   B CD2 1 
ATOM   5204 C  CE1 . PHE   B  1  330 ? -16.420 -0.650  64.183 1.00 43.00  ? 343 PHE   B CE1 1 
ATOM   5205 C  CE2 . PHE   B  1  330 ? -17.649 -2.059  65.670 1.00 49.11  ? 343 PHE   B CE2 1 
ATOM   5206 C  CZ  . PHE   B  1  330 ? -17.241 -1.744  64.390 1.00 43.55  ? 343 PHE   B CZ  1 
ATOM   5207 N  N   . PRO   B  1  331 ? -12.975 1.112   69.948 1.00 48.40  ? 344 PRO   B N   1 
ATOM   5208 C  CA  . PRO   B  1  331 ? -12.638 1.783   71.200 1.00 51.03  ? 344 PRO   B CA  1 
ATOM   5209 C  C   . PRO   B  1  331 ? -12.873 3.290   71.170 1.00 47.86  ? 344 PRO   B C   1 
ATOM   5210 O  O   . PRO   B  1  331 ? -12.929 3.919   72.215 1.00 51.57  ? 344 PRO   B O   1 
ATOM   5211 C  CB  . PRO   B  1  331 ? -11.149 1.428   71.362 1.00 55.27  ? 344 PRO   B CB  1 
ATOM   5212 C  CG  . PRO   B  1  331 ? -10.674 1.219   69.957 1.00 52.70  ? 344 PRO   B CG  1 
ATOM   5213 C  CD  . PRO   B  1  331 ? -11.816 0.457   69.319 1.00 48.17  ? 344 PRO   B CD  1 
ATOM   5214 N  N   . TYR   B  1  332 ? -13.001 3.867   69.978 1.00 40.84  ? 345 TYR   B N   1 
ATOM   5215 C  CA  . TYR   B  1  332 ? -13.243 5.292   69.850 1.00 44.96  ? 345 TYR   B CA  1 
ATOM   5216 C  C   . TYR   B  1  332 ? -14.575 5.550   69.147 1.00 45.17  ? 345 TYR   B C   1 
ATOM   5217 O  O   . TYR   B  1  332 ? -14.821 6.651   68.662 1.00 47.94  ? 345 TYR   B O   1 
ATOM   5218 C  CB  . TYR   B  1  332 ? -12.078 5.948   69.105 1.00 47.86  ? 345 TYR   B CB  1 
ATOM   5219 C  CG  . TYR   B  1  332 ? -10.730 5.649   69.728 1.00 49.72  ? 345 TYR   B CG  1 
ATOM   5220 C  CD1 . TYR   B  1  332 ? -10.362 6.262   70.914 1.00 43.74  ? 345 TYR   B CD1 1 
ATOM   5221 C  CD2 . TYR   B  1  332 ? -9.833  4.763   69.133 1.00 49.22  ? 345 TYR   B CD2 1 
ATOM   5222 C  CE1 . TYR   B  1  332 ? -9.133  6.009   71.496 1.00 49.44  ? 345 TYR   B CE1 1 
ATOM   5223 C  CE2 . TYR   B  1  332 ? -8.610  4.486   69.719 1.00 49.18  ? 345 TYR   B CE2 1 
ATOM   5224 C  CZ  . TYR   B  1  332 ? -8.247  5.133   70.885 1.00 49.88  ? 345 TYR   B CZ  1 
ATOM   5225 O  OH  . TYR   B  1  332 ? -7.041  4.867   71.448 1.00 44.09  ? 345 TYR   B OH  1 
ATOM   5226 N  N   . GLY   B  1  333 ? -15.449 4.548   69.128 1.00 48.76  ? 346 GLY   B N   1 
ATOM   5227 C  CA  . GLY   B  1  333 ? -16.709 4.676   68.418 1.00 52.23  ? 346 GLY   B CA  1 
ATOM   5228 C  C   . GLY   B  1  333 ? -16.496 4.705   66.906 1.00 56.80  ? 346 GLY   B C   1 
ATOM   5229 O  O   . GLY   B  1  333 ? -15.486 4.204   66.397 1.00 57.75  ? 346 GLY   B O   1 
ATOM   5230 N  N   . GLN   B  1  334 ? -17.463 5.302   66.202 1.00 63.97  ? 347 GLN   B N   1 
ATOM   5231 C  CA  . GLN   B  1  334 ? -17.512 5.261   64.743 1.00 64.88  ? 347 GLN   B CA  1 
ATOM   5232 C  C   . GLN   B  1  334 ? -17.410 6.685   64.214 1.00 68.80  ? 347 GLN   B C   1 
ATOM   5233 O  O   . GLN   B  1  334 ? -17.576 7.632   64.977 1.00 68.36  ? 347 GLN   B O   1 
ATOM   5234 C  CB  . GLN   B  1  334 ? -18.779 4.618   64.186 1.00 68.57  ? 347 GLN   B CB  1 
ATOM   5235 C  CG  . GLN   B  1  334 ? -19.243 3.390   64.968 1.00 73.87  ? 347 GLN   B CG  1 
ATOM   5236 C  CD  . GLN   B  1  334 ? -19.304 2.123   64.144 1.00 72.16  ? 347 GLN   B CD  1 
ATOM   5237 O  OE1 . GLN   B  1  334 ? -18.776 2.049   63.029 1.00 65.98  ? 347 GLN   B OE1 1 
ATOM   5238 N  NE2 . GLN   B  1  334 ? -19.881 1.078   64.722 1.00 71.52  ? 347 GLN   B NE2 1 
ATOM   5239 N  N   . LEU   B  1  335 ? -17.128 6.817   62.909 1.00 79.54  ? 348 LEU   B N   1 
ATOM   5240 C  CA  . LEU   B  1  335 ? -16.964 8.119   62.272 1.00 87.58  ? 348 LEU   B CA  1 
ATOM   5241 C  C   . LEU   B  1  335 ? -18.304 8.879   62.218 1.00 84.77  ? 348 LEU   B C   1 
ATOM   5242 O  O   . LEU   B  1  335 ? -19.327 8.215   61.981 1.00 83.27  ? 348 LEU   B O   1 
ATOM   5243 C  CB  . LEU   B  1  335 ? -16.346 7.946   60.882 1.00 89.06  ? 348 LEU   B CB  1 
ATOM   5244 C  CG  . LEU   B  1  335 ? -14.840 7.665   60.848 1.00 92.07  ? 348 LEU   B CG  1 
ATOM   5245 C  CD1 . LEU   B  1  335 ? -14.354 7.747   59.416 1.00 89.57  ? 348 LEU   B CD1 1 
ATOM   5246 C  CD2 . LEU   B  1  335 ? -14.002 8.610   61.720 1.00 94.28  ? 348 LEU   B CD2 1 
ATOM   5247 N  N   . GLN   C  1  1   ? 4.682   -16.784 27.047 1.00 119.90 ? 14  GLN   C N   1 
ATOM   5248 C  CA  . GLN   C  1  1   ? 5.525   -17.038 25.846 1.00 126.37 ? 14  GLN   C CA  1 
ATOM   5249 C  C   . GLN   C  1  1   ? 5.683   -15.733 25.061 1.00 124.63 ? 14  GLN   C C   1 
ATOM   5250 O  O   . GLN   C  1  1   ? 6.620   -14.975 25.319 1.00 113.40 ? 14  GLN   C O   1 
ATOM   5251 C  CB  . GLN   C  1  1   ? 4.962   -18.196 25.013 1.00 122.73 ? 14  GLN   C CB  1 
ATOM   5252 C  CG  . GLN   C  1  1   ? 6.014   -18.923 24.179 1.00 120.19 ? 14  GLN   C CG  1 
ATOM   5253 C  CD  . GLN   C  1  1   ? 7.157   -19.456 25.020 1.00 121.70 ? 14  GLN   C CD  1 
ATOM   5254 O  OE1 . GLN   C  1  1   ? 6.952   -20.256 25.938 1.00 118.68 ? 14  GLN   C OE1 1 
ATOM   5255 N  NE2 . GLN   C  1  1   ? 8.372   -18.999 24.744 1.00 117.57 ? 14  GLN   C NE2 1 
ATOM   5256 N  N   . GLY   C  1  2   ? 4.759   -15.487 24.115 1.00 112.82 ? 15  GLY   C N   1 
ATOM   5257 C  CA  . GLY   C  1  2   ? 4.791   -14.316 23.252 1.00 91.49  ? 15  GLY   C CA  1 
ATOM   5258 C  C   . GLY   C  1  2   ? 4.252   -14.595 21.848 1.00 73.31  ? 15  GLY   C C   1 
ATOM   5259 O  O   . GLY   C  1  2   ? 3.861   -15.708 21.507 1.00 67.37  ? 15  GLY   C O   1 
ATOM   5260 N  N   . VAL   C  1  3   ? 4.243   -13.545 21.031 1.00 69.84  ? 16  VAL   C N   1 
ATOM   5261 C  CA  . VAL   C  1  3   ? 3.717   -13.604 19.677 1.00 68.04  ? 16  VAL   C CA  1 
ATOM   5262 C  C   . VAL   C  1  3   ? 4.742   -12.988 18.742 1.00 61.59  ? 16  VAL   C C   1 
ATOM   5263 O  O   . VAL   C  1  3   ? 5.479   -12.129 19.194 1.00 53.50  ? 16  VAL   C O   1 
ATOM   5264 C  CB  . VAL   C  1  3   ? 2.377   -12.847 19.620 1.00 75.60  ? 16  VAL   C CB  1 
ATOM   5265 C  CG1 . VAL   C  1  3   ? 1.822   -12.845 18.206 1.00 77.80  ? 16  VAL   C CG1 1 
ATOM   5266 C  CG2 . VAL   C  1  3   ? 1.379   -13.430 20.625 1.00 76.83  ? 16  VAL   C CG2 1 
ATOM   5267 N  N   . ASP   C  1  4   ? 4.778   -13.428 17.472 1.00 65.70  ? 17  ASP   C N   1 
ATOM   5268 C  CA  . ASP   C  1  4   ? 5.572   -12.795 16.425 1.00 69.96  ? 17  ASP   C CA  1 
ATOM   5269 C  C   . ASP   C  1  4   ? 4.712   -11.771 15.676 1.00 66.71  ? 17  ASP   C C   1 
ATOM   5270 O  O   . ASP   C  1  4   ? 3.804   -12.162 14.942 1.00 72.38  ? 17  ASP   C O   1 
ATOM   5271 C  CB  . ASP   C  1  4   ? 6.133   -13.804 15.433 1.00 80.01  ? 17  ASP   C CB  1 
ATOM   5272 C  CG  . ASP   C  1  4   ? 7.183   -14.774 15.941 1.00 102.23 ? 17  ASP   C CG  1 
ATOM   5273 O  OD1 . ASP   C  1  4   ? 7.659   -14.588 17.080 1.00 130.36 ? 17  ASP   C OD1 1 
ATOM   5274 O  OD2 . ASP   C  1  4   ? 7.497   -15.718 15.191 1.00 101.26 ? 17  ASP   C OD2 1 
ATOM   5275 N  N   . PRO   C  1  5   ? 4.952   -10.439 15.824 1.00 58.41  ? 18  PRO   C N   1 
ATOM   5276 C  CA  . PRO   C  1  5   ? 4.036   -9.429  15.274 1.00 51.33  ? 18  PRO   C CA  1 
ATOM   5277 C  C   . PRO   C  1  5   ? 4.139   -9.215  13.763 1.00 43.92  ? 18  PRO   C C   1 
ATOM   5278 O  O   . PRO   C  1  5   ? 5.200   -8.870  13.261 1.00 40.54  ? 18  PRO   C O   1 
ATOM   5279 C  CB  . PRO   C  1  5   ? 4.386   -8.149  16.041 1.00 53.22  ? 18  PRO   C CB  1 
ATOM   5280 C  CG  . PRO   C  1  5   ? 5.785   -8.383  16.636 1.00 56.52  ? 18  PRO   C CG  1 
ATOM   5281 C  CD  . PRO   C  1  5   ? 6.117   -9.853  16.511 1.00 53.04  ? 18  PRO   C CD  1 
ATOM   5282 N  N   . PRO   C  1  6   ? 3.031   -9.342  12.997 1.00 43.34  ? 19  PRO   C N   1 
ATOM   5283 C  CA  . PRO   C  1  6   ? 3.092   -9.219  11.536 1.00 47.38  ? 19  PRO   C CA  1 
ATOM   5284 C  C   . PRO   C  1  6   ? 3.273   -7.756  11.139 1.00 46.11  ? 19  PRO   C C   1 
ATOM   5285 O  O   . PRO   C  1  6   ? 2.946   -6.861  11.918 1.00 38.93  ? 19  PRO   C O   1 
ATOM   5286 C  CB  . PRO   C  1  6   ? 1.733   -9.777  11.084 1.00 45.44  ? 19  PRO   C CB  1 
ATOM   5287 C  CG  . PRO   C  1  6   ? 0.802   -9.418  12.225 1.00 47.46  ? 19  PRO   C CG  1 
ATOM   5288 C  CD  . PRO   C  1  6   ? 1.658   -9.545  13.494 1.00 46.05  ? 19  PRO   C CD  1 
ATOM   5289 N  N   . PRO   C  1  7   ? 3.812   -7.461  9.940  1.00 44.22  ? 20  PRO   C N   1 
ATOM   5290 C  CA  . PRO   C  1  7   ? 3.869   -6.088  9.449  1.00 43.18  ? 20  PRO   C CA  1 
ATOM   5291 C  C   . PRO   C  1  7   ? 2.465   -5.519  9.302  1.00 39.48  ? 20  PRO   C C   1 
ATOM   5292 O  O   . PRO   C  1  7   ? 1.498   -6.263  9.190  1.00 37.22  ? 20  PRO   C O   1 
ATOM   5293 C  CB  . PRO   C  1  7   ? 4.643   -6.158  8.111  1.00 43.60  ? 20  PRO   C CB  1 
ATOM   5294 C  CG  . PRO   C  1  7   ? 4.529   -7.613  7.709  1.00 49.24  ? 20  PRO   C CG  1 
ATOM   5295 C  CD  . PRO   C  1  7   ? 4.440   -8.415  9.012  1.00 48.24  ? 20  PRO   C CD  1 
ATOM   5296 N  N   . PRO   C  1  8   ? 2.314   -4.174  9.339  1.00 38.21  ? 21  PRO   C N   1 
ATOM   5297 C  CA  . PRO   C  1  8   ? 1.003   -3.554  9.242  1.00 35.18  ? 21  PRO   C CA  1 
ATOM   5298 C  C   . PRO   C  1  8   ? 0.369   -3.831  7.877  1.00 37.81  ? 21  PRO   C C   1 
ATOM   5299 O  O   . PRO   C  1  8   ? 1.037   -3.966  6.860  1.00 40.98  ? 21  PRO   C O   1 
ATOM   5300 C  CB  . PRO   C  1  8   ? 1.298   -2.082  9.442  1.00 33.83  ? 21  PRO   C CB  1 
ATOM   5301 C  CG  . PRO   C  1  8   ? 2.719   -1.928  8.982  1.00 35.73  ? 21  PRO   C CG  1 
ATOM   5302 C  CD  . PRO   C  1  8   ? 3.395   -3.186  9.451  1.00 36.26  ? 21  PRO   C CD  1 
ATOM   5303 N  N   . PRO   C  1  9   ? -0.966  -3.899  7.832  1.00 36.06  ? 22  PRO   C N   1 
ATOM   5304 C  CA  . PRO   C  1  9   ? -1.691  -3.917  6.573  1.00 36.25  ? 22  PRO   C CA  1 
ATOM   5305 C  C   . PRO   C  1  9   ? -1.270  -2.727  5.726  1.00 32.58  ? 22  PRO   C C   1 
ATOM   5306 O  O   . PRO   C  1  9   ? -0.929  -1.687  6.268  1.00 30.59  ? 22  PRO   C O   1 
ATOM   5307 C  CB  . PRO   C  1  9   ? -3.154  -3.790  7.026  1.00 36.69  ? 22  PRO   C CB  1 
ATOM   5308 C  CG  . PRO   C  1  9   ? -3.142  -4.336  8.417  1.00 38.32  ? 22  PRO   C CG  1 
ATOM   5309 C  CD  . PRO   C  1  9   ? -1.845  -3.930  9.006  1.00 36.69  ? 22  PRO   C CD  1 
ATOM   5310 N  N   . GLY   C  1  10  ? -1.368  -2.900  4.408  1.00 32.18  ? 23  GLY   C N   1 
ATOM   5311 C  CA  . GLY   C  1  10  ? -1.350  -1.809  3.451  1.00 34.17  ? 23  GLY   C CA  1 
ATOM   5312 C  C   . GLY   C  1  10  ? -2.724  -1.156  3.310  1.00 34.87  ? 23  GLY   C C   1 
ATOM   5313 O  O   . GLY   C  1  10  ? -3.654  -1.486  4.036  1.00 31.29  ? 23  GLY   C O   1 
ATOM   5314 N  N   . PRO   C  1  11  ? -2.879  -0.193  2.374  1.00 39.59  ? 24  PRO   C N   1 
ATOM   5315 C  CA  . PRO   C  1  11  ? -4.160  0.485   2.163  1.00 41.04  ? 24  PRO   C CA  1 
ATOM   5316 C  C   . PRO   C  1  11  ? -5.257  -0.515  1.821  1.00 38.36  ? 24  PRO   C C   1 
ATOM   5317 O  O   . PRO   C  1  11  ? -4.960  -1.603  1.344  1.00 33.62  ? 24  PRO   C O   1 
ATOM   5318 C  CB  . PRO   C  1  11  ? -3.884  1.473   1.019  1.00 41.10  ? 24  PRO   C CB  1 
ATOM   5319 C  CG  . PRO   C  1  11  ? -2.387  1.673   1.054  1.00 38.20  ? 24  PRO   C CG  1 
ATOM   5320 C  CD  . PRO   C  1  11  ? -1.818  0.317   1.483  1.00 39.34  ? 24  PRO   C CD  1 
ATOM   5321 N  N   . PRO   C  1  12  ? -6.547  -0.199  2.061  1.00 36.78  ? 25  PRO   C N   1 
ATOM   5322 C  CA  . PRO   C  1  12  ? -7.606  -1.124  1.678  1.00 41.36  ? 25  PRO   C CA  1 
ATOM   5323 C  C   . PRO   C  1  12  ? -7.646  -1.252  0.151  1.00 41.59  ? 25  PRO   C C   1 
ATOM   5324 O  O   . PRO   C  1  12  ? -7.240  -0.346  -0.585 1.00 36.68  ? 25  PRO   C O   1 
ATOM   5325 C  CB  . PRO   C  1  12  ? -8.886  -0.514  2.290  1.00 44.58  ? 25  PRO   C CB  1 
ATOM   5326 C  CG  . PRO   C  1  12  ? -8.564  0.962   2.421  1.00 44.74  ? 25  PRO   C CG  1 
ATOM   5327 C  CD  . PRO   C  1  12  ? -7.049  1.063   2.631  1.00 39.59  ? 25  PRO   C CD  1 
ATOM   5328 N  N   . SER   C  1  13  ? -8.078  -2.435  -0.302 1.00 43.35  ? 26  SER   C N   1 
ATOM   5329 C  CA  A SER   C  1  13  ? -8.215  -2.721  -1.720 0.50 43.57  ? 26  SER   C CA  1 
ATOM   5330 C  CA  B SER   C  1  13  ? -8.254  -2.754  -1.710 0.50 44.07  ? 26  SER   C CA  1 
ATOM   5331 C  C   . SER   C  1  13  ? -9.130  -1.698  -2.387 1.00 39.23  ? 26  SER   C C   1 
ATOM   5332 O  O   . SER   C  1  13  ? -8.809  -1.192  -3.455 1.00 39.57  ? 26  SER   C O   1 
ATOM   5333 C  CB  A SER   C  1  13  ? -8.722  -4.117  -1.938 0.50 45.59  ? 26  SER   C CB  1 
ATOM   5334 C  CB  B SER   C  1  13  ? -8.843  -4.154  -1.821 0.50 46.61  ? 26  SER   C CB  1 
ATOM   5335 O  OG  A SER   C  1  13  ? -7.740  -5.046  -1.509 0.50 46.26  ? 26  SER   C OG  1 
ATOM   5336 O  OG  B SER   C  1  13  ? -9.135  -4.534  -3.158 0.50 48.16  ? 26  SER   C OG  1 
ATOM   5337 N  N   . PHE   C  1  14  ? -10.250 -1.380  -1.734 1.00 39.82  ? 27  PHE   C N   1 
ATOM   5338 C  CA  . PHE   C  1  14  ? -11.191 -0.379  -2.214 1.00 38.10  ? 27  PHE   C CA  1 
ATOM   5339 C  C   . PHE   C  1  14  ? -11.124 0.851   -1.319 1.00 35.73  ? 27  PHE   C C   1 
ATOM   5340 O  O   . PHE   C  1  14  ? -11.295 0.728   -0.113 1.00 36.33  ? 27  PHE   C O   1 
ATOM   5341 C  CB  . PHE   C  1  14  ? -12.594 -1.004  -2.217 1.00 39.50  ? 27  PHE   C CB  1 
ATOM   5342 C  CG  . PHE   C  1  14  ? -13.680 -0.024  -2.622 1.00 39.10  ? 27  PHE   C CG  1 
ATOM   5343 C  CD1 . PHE   C  1  14  ? -13.774 0.431   -3.937 1.00 40.27  ? 27  PHE   C CD1 1 
ATOM   5344 C  CD2 . PHE   C  1  14  ? -14.613 0.419   -1.694 1.00 41.13  ? 27  PHE   C CD2 1 
ATOM   5345 C  CE1 . PHE   C  1  14  ? -14.758 1.343   -4.301 1.00 39.03  ? 27  PHE   C CE1 1 
ATOM   5346 C  CE2 . PHE   C  1  14  ? -15.613 1.311   -2.069 1.00 44.01  ? 27  PHE   C CE2 1 
ATOM   5347 C  CZ  . PHE   C  1  14  ? -15.684 1.776   -3.373 1.00 36.25  ? 27  PHE   C CZ  1 
ATOM   5348 N  N   . THR   C  1  15  ? -10.921 2.035   -1.909 1.00 36.92  ? 28  THR   C N   1 
ATOM   5349 C  CA  . THR   C  1  15  ? -10.734 3.258   -1.136 1.00 35.44  ? 28  THR   C CA  1 
ATOM   5350 C  C   . THR   C  1  15  ? -11.823 4.280   -1.432 1.00 33.18  ? 28  THR   C C   1 
ATOM   5351 O  O   . THR   C  1  15  ? -11.659 5.449   -1.124 1.00 31.44  ? 28  THR   C O   1 
ATOM   5352 C  CB  . THR   C  1  15  ? -9.359  3.869   -1.429 1.00 39.87  ? 28  THR   C CB  1 
ATOM   5353 O  OG1 . THR   C  1  15  ? -9.374  4.406   -2.749 1.00 45.16  ? 28  THR   C OG1 1 
ATOM   5354 C  CG2 . THR   C  1  15  ? -8.212  2.883   -1.265 1.00 44.18  ? 28  THR   C CG2 1 
ATOM   5355 N  N   . GLY   C  1  16  ? -12.938 3.866   -2.029 1.00 33.78  ? 29  GLY   C N   1 
ATOM   5356 C  CA  . GLY   C  1  16  ? -14.047 4.782   -2.242 1.00 33.38  ? 29  GLY   C CA  1 
ATOM   5357 C  C   . GLY   C  1  16  ? -14.997 4.822   -1.039 1.00 39.02  ? 29  GLY   C C   1 
ATOM   5358 O  O   . GLY   C  1  16  ? -14.745 4.226   0.007  1.00 37.63  ? 29  GLY   C O   1 
ATOM   5359 N  N   . THR   C  1  17  ? -16.111 5.543   -1.196 1.00 42.89  ? 30  THR   C N   1 
ATOM   5360 C  CA  . THR   C  1  17  ? -17.112 5.605   -0.147 1.00 44.62  ? 30  THR   C CA  1 
ATOM   5361 C  C   . THR   C  1  17  ? -17.883 4.297   -0.105 1.00 42.20  ? 30  THR   C C   1 
ATOM   5362 O  O   . THR   C  1  17  ? -17.923 3.553   -1.083 1.00 39.97  ? 30  THR   C O   1 
ATOM   5363 C  CB  . THR   C  1  17  ? -18.060 6.788   -0.336 1.00 51.12  ? 30  THR   C CB  1 
ATOM   5364 O  OG1 . THR   C  1  17  ? -18.720 6.784   0.930  1.00 48.41  ? 30  THR   C OG1 1 
ATOM   5365 C  CG2 . THR   C  1  17  ? -18.986 6.617   -1.533 1.00 46.39  ? 30  THR   C CG2 1 
ATOM   5366 N  N   . LYS   C  1  18  ? -18.459 4.032   1.064  1.00 39.88  ? 31  LYS   C N   1 
ATOM   5367 C  CA  . LYS   C  1  18  ? -19.343 2.900   1.256  1.00 42.26  ? 31  LYS   C CA  1 
ATOM   5368 C  C   . LYS   C  1  18  ? -20.094 3.082   2.572  1.00 41.01  ? 31  LYS   C C   1 
ATOM   5369 O  O   . LYS   C  1  18  ? -19.709 3.881   3.408  1.00 39.80  ? 31  LYS   C O   1 
ATOM   5370 C  CB  . LYS   C  1  18  ? -18.585 1.573   1.251  1.00 42.86  ? 31  LYS   C CB  1 
ATOM   5371 C  CG  . LYS   C  1  18  ? -17.620 1.347   2.399  1.00 49.24  ? 31  LYS   C CG  1 
ATOM   5372 C  CD  . LYS   C  1  18  ? -16.948 -0.016  2.326  1.00 54.58  ? 31  LYS   C CD  1 
ATOM   5373 C  CE  . LYS   C  1  18  ? -17.571 -1.075  3.166  1.00 56.25  ? 31  LYS   C CE  1 
ATOM   5374 N  NZ  . LYS   C  1  18  ? -16.873 -2.335  2.876  1.00 60.82  ? 31  LYS   C NZ  1 
ATOM   5375 N  N   . LEU   C  1  19  ? -21.169 2.324   2.737  1.00 43.83  ? 32  LEU   C N   1 
ATOM   5376 C  CA  . LEU   C  1  19  ? -21.930 2.280   3.967  1.00 43.14  ? 32  LEU   C CA  1 
ATOM   5377 C  C   . LEU   C  1  19  ? -21.095 1.534   4.987  1.00 43.77  ? 32  LEU   C C   1 
ATOM   5378 O  O   . LEU   C  1  19  ? -20.721 0.384   4.741  1.00 48.12  ? 32  LEU   C O   1 
ATOM   5379 C  CB  . LEU   C  1  19  ? -23.257 1.561   3.742  1.00 44.39  ? 32  LEU   C CB  1 
ATOM   5380 C  CG  . LEU   C  1  19  ? -24.103 1.308   4.992  1.00 44.54  ? 32  LEU   C CG  1 
ATOM   5381 C  CD1 . LEU   C  1  19  ? -24.608 2.621   5.570  1.00 40.82  ? 32  LEU   C CD1 1 
ATOM   5382 C  CD2 . LEU   C  1  19  ? -25.257 0.358   4.701  1.00 47.02  ? 32  LEU   C CD2 1 
ATOM   5383 N  N   . VAL   C  1  20  ? -20.819 2.189   6.125  1.00 43.00  ? 33  VAL   C N   1 
ATOM   5384 C  CA  . VAL   C  1  20  ? -20.010 1.547   7.148  1.00 46.57  ? 33  VAL   C CA  1 
ATOM   5385 C  C   . VAL   C  1  20  ? -20.896 1.183   8.332  1.00 44.81  ? 33  VAL   C C   1 
ATOM   5386 O  O   . VAL   C  1  20  ? -20.590 0.257   9.065  1.00 43.65  ? 33  VAL   C O   1 
ATOM   5387 C  CB  . VAL   C  1  20  ? -18.780 2.367   7.575  1.00 46.39  ? 33  VAL   C CB  1 
ATOM   5388 C  CG1 . VAL   C  1  20  ? -17.795 2.517   6.421  1.00 47.10  ? 33  VAL   C CG1 1 
ATOM   5389 C  CG2 . VAL   C  1  20  ? -19.170 3.721   8.140  1.00 45.33  ? 33  VAL   C CG2 1 
ATOM   5390 N  N   . ASN   C  1  21  ? -22.000 1.897   8.489  1.00 47.01  ? 34  ASN   C N   1 
ATOM   5391 C  CA  . ASN   C  1  21  ? -22.987 1.553   9.496  1.00 49.37  ? 34  ASN   C CA  1 
ATOM   5392 C  C   . ASN   C  1  21  ? -23.975 0.531   8.926  1.00 49.29  ? 34  ASN   C C   1 
ATOM   5393 O  O   . ASN   C  1  21  ? -25.084 0.891   8.562  1.00 52.50  ? 34  ASN   C O   1 
ATOM   5394 C  CB  . ASN   C  1  21  ? -23.682 2.825   9.964  1.00 44.35  ? 34  ASN   C CB  1 
ATOM   5395 C  CG  . ASN   C  1  21  ? -24.564 2.564   11.152 1.00 45.31  ? 34  ASN   C CG  1 
ATOM   5396 O  OD1 . ASN   C  1  21  ? -24.675 1.426   11.642 1.00 42.00  ? 34  ASN   C OD1 1 
ATOM   5397 N  ND2 . ASN   C  1  21  ? -25.186 3.636   11.617 1.00 45.29  ? 34  ASN   C ND2 1 
ATOM   5398 N  N   . ASP   C  1  22  ? -23.574 -0.735  8.866  1.00 46.73  ? 35  ASP   C N   1 
ATOM   5399 C  CA  . ASP   C  1  22  ? -24.271 -1.737  8.074  1.00 55.95  ? 35  ASP   C CA  1 
ATOM   5400 C  C   . ASP   C  1  22  ? -24.676 -2.904  8.971  1.00 60.96  ? 35  ASP   C C   1 
ATOM   5401 O  O   . ASP   C  1  22  ? -24.375 -2.907  10.155 1.00 61.63  ? 35  ASP   C O   1 
ATOM   5402 C  CB  . ASP   C  1  22  ? -23.442 -2.169  6.864  1.00 60.64  ? 35  ASP   C CB  1 
ATOM   5403 C  CG  . ASP   C  1  22  ? -22.105 -2.860  7.121  1.00 62.40  ? 35  ASP   C CG  1 
ATOM   5404 O  OD1 . ASP   C  1  22  ? -21.743 -3.045  8.300  1.00 67.19  ? 35  ASP   C OD1 1 
ATOM   5405 O  OD2 . ASP   C  1  22  ? -21.433 -3.227  6.127  1.00 63.02  ? 35  ASP   C OD2 1 
ATOM   5406 N  N   . ALA   C  1  23  ? -25.330 -3.907  8.382  1.00 63.04  ? 36  ALA   C N   1 
ATOM   5407 C  CA  . ALA   C  1  23  ? -25.948 -4.990  9.130  1.00 66.30  ? 36  ALA   C CA  1 
ATOM   5408 C  C   . ALA   C  1  23  ? -24.893 -5.812  9.867  1.00 62.57  ? 36  ALA   C C   1 
ATOM   5409 O  O   . ALA   C  1  23  ? -25.149 -6.312  10.965 1.00 54.01  ? 36  ALA   C O   1 
ATOM   5410 C  CB  . ALA   C  1  23  ? -26.767 -5.872  8.194  1.00 67.68  ? 36  ALA   C CB  1 
ATOM   5411 N  N   . ASP   C  1  24  ? -23.714 -5.950  9.254  1.00 61.25  ? 37  ASP   C N   1 
ATOM   5412 C  CA  . ASP   C  1  24  ? -22.647 -6.744  9.842  1.00 64.78  ? 37  ASP   C CA  1 
ATOM   5413 C  C   . ASP   C  1  24  ? -21.949 -5.992  10.989 1.00 53.09  ? 37  ASP   C C   1 
ATOM   5414 O  O   . ASP   C  1  24  ? -21.217 -6.614  11.747 1.00 51.26  ? 37  ASP   C O   1 
ATOM   5415 C  CB  . ASP   C  1  24  ? -21.594 -7.155  8.820  1.00 74.02  ? 37  ASP   C CB  1 
ATOM   5416 C  CG  . ASP   C  1  24  ? -21.986 -8.141  7.731  1.00 78.87  ? 37  ASP   C CG  1 
ATOM   5417 O  OD1 . ASP   C  1  24  ? -22.632 -9.149  8.062  1.00 83.79  ? 37  ASP   C OD1 1 
ATOM   5418 O  OD2 . ASP   C  1  24  ? -21.574 -7.923  6.577  1.00 85.46  ? 37  ASP   C OD2 1 
ATOM   5419 N  N   . HIS   C  1  25  ? -22.149 -4.668  11.111 1.00 43.46  ? 38  HIS   C N   1 
ATOM   5420 C  CA  . HIS   C  1  25  ? -21.442 -3.850  12.084 1.00 40.65  ? 38  HIS   C CA  1 
ATOM   5421 C  C   . HIS   C  1  25  ? -22.429 -3.035  12.920 1.00 36.98  ? 38  HIS   C C   1 
ATOM   5422 O  O   . HIS   C  1  25  ? -22.404 -1.793  12.930 1.00 34.45  ? 38  HIS   C O   1 
ATOM   5423 C  CB  . HIS   C  1  25  ? -20.412 -2.963  11.375 1.00 44.62  ? 38  HIS   C CB  1 
ATOM   5424 C  CG  . HIS   C  1  25  ? -19.338 -3.762  10.718 1.00 48.90  ? 38  HIS   C CG  1 
ATOM   5425 N  ND1 . HIS   C  1  25  ? -19.312 -4.006  9.361  1.00 52.07  ? 38  HIS   C ND1 1 
ATOM   5426 C  CD2 . HIS   C  1  25  ? -18.261 -4.373  11.236 1.00 50.23  ? 38  HIS   C CD2 1 
ATOM   5427 C  CE1 . HIS   C  1  25  ? -18.250 -4.752  9.082  1.00 58.31  ? 38  HIS   C CE1 1 
ATOM   5428 N  NE2 . HIS   C  1  25  ? -17.598 -4.986  10.204 1.00 52.66  ? 38  HIS   C NE2 1 
ATOM   5429 N  N   . PRO   C  1  26  ? -23.343 -3.701  13.656 1.00 37.77  ? 39  PRO   C N   1 
ATOM   5430 C  CA  . PRO   C  1  26  ? -24.347 -2.975  14.440 1.00 39.46  ? 39  PRO   C CA  1 
ATOM   5431 C  C   . PRO   C  1  26  ? -23.722 -2.341  15.679 1.00 40.82  ? 39  PRO   C C   1 
ATOM   5432 O  O   . PRO   C  1  26  ? -22.848 -2.926  16.303 1.00 38.69  ? 39  PRO   C O   1 
ATOM   5433 C  CB  . PRO   C  1  26  ? -25.361 -4.071  14.815 1.00 36.95  ? 39  PRO   C CB  1 
ATOM   5434 C  CG  . PRO   C  1  26  ? -24.511 -5.330  14.877 1.00 40.48  ? 39  PRO   C CG  1 
ATOM   5435 C  CD  . PRO   C  1  26  ? -23.478 -5.167  13.754 1.00 40.22  ? 39  PRO   C CD  1 
ATOM   5436 N  N   . TRP   C  1  27  ? -24.185 -1.149  16.043 1.00 40.12  ? 40  TRP   C N   1 
ATOM   5437 C  CA  . TRP   C  1  27  ? -23.862 -0.615  17.345 1.00 43.37  ? 40  TRP   C CA  1 
ATOM   5438 C  C   . TRP   C  1  27  ? -24.424 -1.550  18.411 1.00 49.89  ? 40  TRP   C C   1 
ATOM   5439 O  O   . TRP   C  1  27  ? -25.527 -2.068  18.271 1.00 55.89  ? 40  TRP   C O   1 
ATOM   5440 C  CB  . TRP   C  1  27  ? -24.408 0.804   17.479 1.00 46.27  ? 40  TRP   C CB  1 
ATOM   5441 C  CG  . TRP   C  1  27  ? -24.047 1.464   18.780 1.00 55.26  ? 40  TRP   C CG  1 
ATOM   5442 C  CD1 . TRP   C  1  27  ? -22.972 2.249   19.046 1.00 52.32  ? 40  TRP   C CD1 1 
ATOM   5443 C  CD2 . TRP   C  1  27  ? -24.796 1.386   20.007 1.00 61.33  ? 40  TRP   C CD2 1 
ATOM   5444 N  NE1 . TRP   C  1  27  ? -23.009 2.683   20.338 1.00 54.27  ? 40  TRP   C NE1 1 
ATOM   5445 C  CE2 . TRP   C  1  27  ? -24.103 2.159   20.959 1.00 61.25  ? 40  TRP   C CE2 1 
ATOM   5446 C  CE3 . TRP   C  1  27  ? -25.971 0.739   20.391 1.00 61.55  ? 40  TRP   C CE3 1 
ATOM   5447 C  CZ2 . TRP   C  1  27  ? -24.546 2.313   22.269 1.00 60.17  ? 40  TRP   C CZ2 1 
ATOM   5448 C  CZ3 . TRP   C  1  27  ? -26.388 0.859   21.695 1.00 61.18  ? 40  TRP   C CZ3 1 
ATOM   5449 C  CH2 . TRP   C  1  27  ? -25.685 1.633   22.621 1.00 57.00  ? 40  TRP   C CH2 1 
ATOM   5450 N  N   . GLN   C  1  28  ? -23.631 -1.807  19.451 1.00 49.80  ? 41  GLN   C N   1 
ATOM   5451 C  CA  . GLN   C  1  28  ? -24.096 -2.557  20.601 1.00 48.83  ? 41  GLN   C CA  1 
ATOM   5452 C  C   . GLN   C  1  28  ? -23.604 -1.860  21.864 1.00 50.52  ? 41  GLN   C C   1 
ATOM   5453 O  O   . GLN   C  1  28  ? -22.572 -1.181  21.857 1.00 49.13  ? 41  GLN   C O   1 
ATOM   5454 C  CB  . GLN   C  1  28  ? -23.640 -4.007  20.565 1.00 46.66  ? 41  GLN   C CB  1 
ATOM   5455 C  CG  . GLN   C  1  28  ? -24.226 -4.805  19.410 1.00 44.27  ? 41  GLN   C CG  1 
ATOM   5456 C  CD  . GLN   C  1  28  ? -23.633 -6.192  19.317 1.00 45.76  ? 41  GLN   C CD  1 
ATOM   5457 O  OE1 . GLN   C  1  28  ? -22.762 -6.566  20.107 1.00 46.69  ? 41  GLN   C OE1 1 
ATOM   5458 N  NE2 . GLN   C  1  28  ? -24.090 -6.965  18.341 1.00 47.56  ? 41  GLN   C NE2 1 
ATOM   5459 N  N   . PRO   C  1  29  ? -24.380 -1.949  22.967 1.00 53.13  ? 42  PRO   C N   1 
ATOM   5460 C  CA  . PRO   C  1  29  ? -24.023 -1.256  24.203 1.00 50.89  ? 42  PRO   C CA  1 
ATOM   5461 C  C   . PRO   C  1  29  ? -22.847 -1.934  24.882 1.00 45.73  ? 42  PRO   C C   1 
ATOM   5462 O  O   . PRO   C  1  29  ? -22.593 -3.121  24.670 1.00 40.80  ? 42  PRO   C O   1 
ATOM   5463 C  CB  . PRO   C  1  29  ? -25.303 -1.259  25.052 1.00 53.91  ? 42  PRO   C CB  1 
ATOM   5464 C  CG  . PRO   C  1  29  ? -26.132 -2.403  24.489 1.00 58.09  ? 42  PRO   C CG  1 
ATOM   5465 C  CD  . PRO   C  1  29  ? -25.664 -2.660  23.058 1.00 58.66  ? 42  PRO   C CD  1 
ATOM   5466 N  N   . LEU   C  1  30  ? -22.125 -1.144  25.681 1.00 41.71  ? 43  LEU   C N   1 
ATOM   5467 C  CA  . LEU   C  1  30  ? -20.984 -1.647  26.420 1.00 41.91  ? 43  LEU   C CA  1 
ATOM   5468 C  C   . LEU   C  1  30  ? -21.434 -2.719  27.395 1.00 43.85  ? 43  LEU   C C   1 
ATOM   5469 O  O   . LEU   C  1  30  ? -22.479 -2.566  28.036 1.00 47.09  ? 43  LEU   C O   1 
ATOM   5470 C  CB  . LEU   C  1  30  ? -20.363 -0.474  27.165 1.00 47.46  ? 43  LEU   C CB  1 
ATOM   5471 C  CG  . LEU   C  1  30  ? -19.795 0.651   26.296 1.00 52.68  ? 43  LEU   C CG  1 
ATOM   5472 C  CD1 . LEU   C  1  30  ? -19.233 1.786   27.133 1.00 49.65  ? 43  LEU   C CD1 1 
ATOM   5473 C  CD2 . LEU   C  1  30  ? -18.742 0.051   25.391 1.00 51.22  ? 43  LEU   C CD2 1 
ATOM   5474 N  N   . ARG   C  1  31  ? -20.640 -3.794  27.466 1.00 45.73  ? 44  ARG   C N   1 
ATOM   5475 C  CA  . ARG   C  1  31  ? -20.770 -4.807  28.493 1.00 46.04  ? 44  ARG   C CA  1 
ATOM   5476 C  C   . ARG   C  1  31  ? -19.757 -4.490  29.591 1.00 48.22  ? 44  ARG   C C   1 
ATOM   5477 O  O   . ARG   C  1  31  ? -18.807 -3.754  29.370 1.00 53.30  ? 44  ARG   C O   1 
ATOM   5478 C  CB  . ARG   C  1  31  ? -20.519 -6.208  27.940 1.00 46.46  ? 44  ARG   C CB  1 
ATOM   5479 C  CG  . ARG   C  1  31  ? -21.388 -6.615  26.761 1.00 53.61  ? 44  ARG   C CG  1 
ATOM   5480 C  CD  . ARG   C  1  31  ? -20.762 -7.786  26.010 1.00 64.07  ? 44  ARG   C CD  1 
ATOM   5481 N  NE  . ARG   C  1  31  ? -19.428 -7.410  25.517 1.00 82.53  ? 44  ARG   C NE  1 
ATOM   5482 C  CZ  . ARG   C  1  31  ? -18.569 -8.162  24.811 1.00 88.26  ? 44  ARG   C CZ  1 
ATOM   5483 N  NH1 . ARG   C  1  31  ? -18.909 -9.385  24.443 1.00 89.57  ? 44  ARG   C NH1 1 
ATOM   5484 N  NH2 . ARG   C  1  31  ? -17.366 -7.691  24.478 1.00 89.12  ? 44  ARG   C NH2 1 
ATOM   5485 N  N   . GLU   C  1  32  ? -19.988 -5.015  30.795 1.00 51.84  ? 45  GLU   C N   1 
ATOM   5486 C  CA  . GLU   C  1  32  ? -18.993 -5.020  31.857 1.00 53.09  ? 45  GLU   C CA  1 
ATOM   5487 C  C   . GLU   C  1  32  ? -17.673 -5.558  31.295 1.00 52.84  ? 45  GLU   C C   1 
ATOM   5488 O  O   . GLU   C  1  32  ? -17.646 -6.609  30.651 1.00 52.59  ? 45  GLU   C O   1 
ATOM   5489 C  CB  . GLU   C  1  32  ? -19.524 -5.865  33.023 1.00 52.63  ? 45  GLU   C CB  1 
ATOM   5490 C  CG  . GLU   C  1  32  ? -18.600 -5.957  34.239 1.00 50.30  ? 45  GLU   C CG  1 
ATOM   5491 C  CD  . GLU   C  1  32  ? -18.312 -4.659  34.987 1.00 52.15  ? 45  GLU   C CD  1 
ATOM   5492 O  OE1 . GLU   C  1  32  ? -19.231 -3.851  35.237 1.00 54.41  ? 45  GLU   C OE1 1 
ATOM   5493 O  OE2 . GLU   C  1  32  ? -17.127 -4.442  35.329 1.00 61.55  ? 45  GLU   C OE2 1 
ATOM   5494 N  N   . GLY   C  1  33  ? -16.581 -4.820  31.526 1.00 50.97  ? 46  GLY   C N   1 
ATOM   5495 C  CA  . GLY   C  1  33  ? -15.269 -5.269  31.080 1.00 61.09  ? 46  GLY   C CA  1 
ATOM   5496 C  C   . GLY   C  1  33  ? -14.825 -4.663  29.748 1.00 53.42  ? 46  GLY   C C   1 
ATOM   5497 O  O   . GLY   C  1  33  ? -13.632 -4.603  29.485 1.00 64.45  ? 46  GLY   C O   1 
ATOM   5498 N  N   . ASP   C  1  34  ? -15.768 -4.166  28.947 1.00 53.52  ? 47  ASP   C N   1 
ATOM   5499 C  CA  . ASP   C  1  34  ? -15.447 -3.512  27.687 1.00 52.95  ? 47  ASP   C CA  1 
ATOM   5500 C  C   . ASP   C  1  34  ? -14.713 -2.212  27.988 1.00 50.99  ? 47  ASP   C C   1 
ATOM   5501 O  O   . ASP   C  1  34  ? -15.064 -1.493  28.920 1.00 43.07  ? 47  ASP   C O   1 
ATOM   5502 C  CB  . ASP   C  1  34  ? -16.687 -3.243  26.843 1.00 47.14  ? 47  ASP   C CB  1 
ATOM   5503 C  CG  . ASP   C  1  34  ? -17.322 -4.458  26.186 1.00 47.14  ? 47  ASP   C CG  1 
ATOM   5504 O  OD1 . ASP   C  1  34  ? -16.687 -5.549  26.212 1.00 46.17  ? 47  ASP   C OD1 1 
ATOM   5505 O  OD2 . ASP   C  1  34  ? -18.444 -4.304  25.649 1.00 46.71  ? 47  ASP   C OD2 1 
ATOM   5506 N  N   . ILE   C  1  35  ? -13.674 -1.937  27.190 1.00 50.35  ? 48  ILE   C N   1 
ATOM   5507 C  CA  . ILE   C  1  35  ? -12.837 -0.780  27.421 1.00 43.23  ? 48  ILE   C CA  1 
ATOM   5508 C  C   . ILE   C  1  35  ? -13.069 0.249   26.326 1.00 37.50  ? 48  ILE   C C   1 
ATOM   5509 O  O   . ILE   C  1  35  ? -13.166 -0.074  25.155 1.00 43.96  ? 48  ILE   C O   1 
ATOM   5510 C  CB  . ILE   C  1  35  ? -11.367 -1.210  27.547 1.00 50.09  ? 48  ILE   C CB  1 
ATOM   5511 C  CG1 . ILE   C  1  35  ? -11.160 -1.936  28.896 1.00 50.61  ? 48  ILE   C CG1 1 
ATOM   5512 C  CG2 . ILE   C  1  35  ? -10.424 -0.008  27.410 1.00 50.87  ? 48  ILE   C CG2 1 
ATOM   5513 C  CD1 . ILE   C  1  35  ? -10.229 -3.124  28.822 1.00 57.38  ? 48  ILE   C CD1 1 
ATOM   5514 N  N   . ARG   C  1  36  ? -13.163 1.504   26.744 1.00 35.65  ? 49  ARG   C N   1 
ATOM   5515 C  CA  . ARG   C  1  36  ? -13.253 2.641   25.852 1.00 37.26  ? 49  ARG   C CA  1 
ATOM   5516 C  C   . ARG   C  1  36  ? -12.334 3.717   26.420 1.00 38.47  ? 49  ARG   C C   1 
ATOM   5517 O  O   . ARG   C  1  36  ? -11.932 3.640   27.577 1.00 37.51  ? 49  ARG   C O   1 
ATOM   5518 C  CB  . ARG   C  1  36  ? -14.707 3.114   25.729 1.00 40.71  ? 49  ARG   C CB  1 
ATOM   5519 C  CG  . ARG   C  1  36  ? -15.634 2.078   25.104 1.00 42.34  ? 49  ARG   C CG  1 
ATOM   5520 C  CD  . ARG   C  1  36  ? -15.332 1.833   23.638 1.00 39.82  ? 49  ARG   C CD  1 
ATOM   5521 N  NE  . ARG   C  1  36  ? -16.291 0.912   23.022 1.00 38.78  ? 49  ARG   C NE  1 
ATOM   5522 C  CZ  . ARG   C  1  36  ? -16.254 -0.412  23.094 1.00 39.50  ? 49  ARG   C CZ  1 
ATOM   5523 N  NH1 . ARG   C  1  36  ? -15.275 -1.036  23.727 1.00 40.22  ? 49  ARG   C NH1 1 
ATOM   5524 N  NH2 . ARG   C  1  36  ? -17.193 -1.129  22.507 1.00 42.13  ? 49  ARG   C NH2 1 
ATOM   5525 N  N   . GLY   C  1  37  ? -11.982 4.709   25.597 1.00 37.73  ? 50  GLY   C N   1 
ATOM   5526 C  CA  . GLY   C  1  37  ? -10.947 5.638   25.992 1.00 36.34  ? 50  GLY   C CA  1 
ATOM   5527 C  C   . GLY   C  1  37  ? -11.117 7.007   25.357 1.00 35.53  ? 50  GLY   C C   1 
ATOM   5528 O  O   . GLY   C  1  37  ? -12.216 7.434   25.032 1.00 39.45  ? 50  GLY   C O   1 
ATOM   5529 N  N   . PRO   C  1  38  ? -10.007 7.736   25.162 1.00 35.21  ? 51  PRO   C N   1 
ATOM   5530 C  CA  . PRO   C  1  38  ? -10.077 9.128   24.729 1.00 34.90  ? 51  PRO   C CA  1 
ATOM   5531 C  C   . PRO   C  1  38  ? -10.276 9.357   23.238 1.00 37.57  ? 51  PRO   C C   1 
ATOM   5532 O  O   . PRO   C  1  38  ? -10.456 10.502  22.826 1.00 36.70  ? 51  PRO   C O   1 
ATOM   5533 C  CB  . PRO   C  1  38  ? -8.725  9.638   25.163 1.00 32.67  ? 51  PRO   C CB  1 
ATOM   5534 C  CG  . PRO   C  1  38  ? -7.824  8.464   24.927 1.00 35.70  ? 51  PRO   C CG  1 
ATOM   5535 C  CD  . PRO   C  1  38  ? -8.630  7.239   25.305 1.00 35.11  ? 51  PRO   C CD  1 
ATOM   5536 N  N   . CYS   C  1  39  ? -10.210 8.289   22.438 1.00 37.34  ? 52  CYS   C N   1 
ATOM   5537 C  CA  . CYS   C  1  39  ? -10.373 8.420   20.997 1.00 38.51  ? 52  CYS   C CA  1 
ATOM   5538 C  C   . CYS   C  1  39  ? -11.791 8.050   20.567 1.00 38.79  ? 52  CYS   C C   1 
ATOM   5539 O  O   . CYS   C  1  39  ? -12.204 6.892   20.666 1.00 37.84  ? 52  CYS   C O   1 
ATOM   5540 C  CB  . CYS   C  1  39  ? -9.413  7.536   20.217 1.00 36.25  ? 52  CYS   C CB  1 
ATOM   5541 S  SG  . CYS   C  1  39  ? -9.524  7.844   18.435 1.00 39.95  ? 52  CYS   C SG  1 
ATOM   5542 N  N   . PRO   C  1  40  ? -12.579 9.019   20.058 1.00 38.19  ? 53  PRO   C N   1 
ATOM   5543 C  CA  . PRO   C  1  40  ? -13.932 8.741   19.573 1.00 38.83  ? 53  PRO   C CA  1 
ATOM   5544 C  C   . PRO   C  1  40  ? -13.954 7.853   18.329 1.00 41.27  ? 53  PRO   C C   1 
ATOM   5545 O  O   . PRO   C  1  40  ? -14.881 7.067   18.152 1.00 39.41  ? 53  PRO   C O   1 
ATOM   5546 C  CB  . PRO   C  1  40  ? -14.522 10.126  19.319 1.00 38.26  ? 53  PRO   C CB  1 
ATOM   5547 C  CG  . PRO   C  1  40  ? -13.332 11.035  19.112 1.00 38.82  ? 53  PRO   C CG  1 
ATOM   5548 C  CD  . PRO   C  1  40  ? -12.191 10.424  19.896 1.00 38.70  ? 53  PRO   C CD  1 
ATOM   5549 N  N   . GLY   C  1  41  ? -12.903 7.952   17.496 1.00 39.29  ? 54  GLY   C N   1 
ATOM   5550 C  CA  . GLY   C  1  41  ? -12.750 7.067   16.359 1.00 32.63  ? 54  GLY   C CA  1 
ATOM   5551 C  C   . GLY   C  1  41  ? -12.692 5.599   16.764 1.00 34.04  ? 54  GLY   C C   1 
ATOM   5552 O  O   . GLY   C  1  41  ? -13.509 4.795   16.324 1.00 34.90  ? 54  GLY   C O   1 
ATOM   5553 N  N   . LEU   C  1  42  ? -11.713 5.253   17.600 1.00 34.52  ? 55  LEU   C N   1 
ATOM   5554 C  CA  . LEU   C  1  42  ? -11.516 3.875   18.013 1.00 36.58  ? 55  LEU   C CA  1 
ATOM   5555 C  C   . LEU   C  1  42  ? -12.706 3.396   18.838 1.00 36.17  ? 55  LEU   C C   1 
ATOM   5556 O  O   . LEU   C  1  42  ? -13.127 2.248   18.711 1.00 35.08  ? 55  LEU   C O   1 
ATOM   5557 C  CB  . LEU   C  1  42  ? -10.208 3.741   18.789 1.00 39.61  ? 55  LEU   C CB  1 
ATOM   5558 C  CG  . LEU   C  1  42  ? -8.941  4.104   18.008 1.00 40.35  ? 55  LEU   C CG  1 
ATOM   5559 C  CD1 . LEU   C  1  42  ? -7.736  3.988   18.912 1.00 44.20  ? 55  LEU   C CD1 1 
ATOM   5560 C  CD2 . LEU   C  1  42  ? -8.792  3.186   16.812 1.00 38.45  ? 55  LEU   C CD2 1 
ATOM   5561 N  N   . ASN   C  1  43  ? -13.262 4.288   19.649 1.00 35.08  ? 56  ASN   C N   1 
ATOM   5562 C  CA  . ASN   C  1  43  ? -14.431 3.959   20.454 1.00 40.33  ? 56  ASN   C CA  1 
ATOM   5563 C  C   . ASN   C  1  43  ? -15.591 3.524   19.562 1.00 40.19  ? 56  ASN   C C   1 
ATOM   5564 O  O   . ASN   C  1  43  ? -16.241 2.513   19.827 1.00 38.87  ? 56  ASN   C O   1 
ATOM   5565 C  CB  . ASN   C  1  43  ? -14.870 5.128   21.331 1.00 39.24  ? 56  ASN   C CB  1 
ATOM   5566 C  CG  . ASN   C  1  43  ? -13.924 5.373   22.484 1.00 40.85  ? 56  ASN   C CG  1 
ATOM   5567 O  OD1 . ASN   C  1  43  ? -13.123 4.505   22.874 1.00 39.53  ? 56  ASN   C OD1 1 
ATOM   5568 N  ND2 . ASN   C  1  43  ? -14.041 6.547   23.074 1.00 39.22  ? 56  ASN   C ND2 1 
ATOM   5569 N  N   . THR   C  1  44  ? -15.827 4.290   18.490 1.00 39.35  ? 57  THR   C N   1 
ATOM   5570 C  CA  . THR   C  1  44  ? -16.927 3.996   17.584 1.00 36.73  ? 57  THR   C CA  1 
ATOM   5571 C  C   . THR   C  1  44  ? -16.680 2.679   16.862 1.00 36.92  ? 57  THR   C C   1 
ATOM   5572 O  O   . THR   C  1  44  ? -17.598 1.870   16.721 1.00 39.36  ? 57  THR   C O   1 
ATOM   5573 C  CB  . THR   C  1  44  ? -17.152 5.153   16.623 1.00 39.22  ? 57  THR   C CB  1 
ATOM   5574 O  OG1 . THR   C  1  44  ? -17.460 6.284   17.428 1.00 35.79  ? 57  THR   C OG1 1 
ATOM   5575 C  CG2 . THR   C  1  44  ? -18.315 4.909   15.676 1.00 43.20  ? 57  THR   C CG2 1 
ATOM   5576 N  N   . LEU   C  1  45  ? -15.433 2.446   16.441 1.00 35.17  ? 58  LEU   C N   1 
ATOM   5577 C  CA  . LEU   C  1  45  ? -15.104 1.222   15.739 1.00 33.83  ? 58  LEU   C CA  1 
ATOM   5578 C  C   . LEU   C  1  45  ? -15.318 0.023   16.651 1.00 32.04  ? 58  LEU   C C   1 
ATOM   5579 O  O   . LEU   C  1  45  ? -15.789 -1.029  16.220 1.00 31.54  ? 58  LEU   C O   1 
ATOM   5580 C  CB  . LEU   C  1  45  ? -13.669 1.310   15.221 1.00 35.72  ? 58  LEU   C CB  1 
ATOM   5581 C  CG  . LEU   C  1  45  ? -13.441 2.381   14.149 1.00 37.77  ? 58  LEU   C CG  1 
ATOM   5582 C  CD1 . LEU   C  1  45  ? -11.960 2.673   13.989 1.00 39.65  ? 58  LEU   C CD1 1 
ATOM   5583 C  CD2 . LEU   C  1  45  ? -14.076 1.942   12.839 1.00 35.96  ? 58  LEU   C CD2 1 
ATOM   5584 N  N   . ALA   C  1  46  ? -14.975 0.167   17.929 1.00 32.54  ? 59  ALA   C N   1 
ATOM   5585 C  CA  . ALA   C  1  46  ? -15.176 -0.942  18.846 1.00 33.89  ? 59  ALA   C CA  1 
ATOM   5586 C  C   . ALA   C  1  46  ? -16.674 -1.174  19.064 1.00 33.84  ? 59  ALA   C C   1 
ATOM   5587 O  O   . ALA   C  1  46  ? -17.137 -2.305  19.081 1.00 34.82  ? 59  ALA   C O   1 
ATOM   5588 C  CB  . ALA   C  1  46  ? -14.431 -0.683  20.129 1.00 33.85  ? 59  ALA   C CB  1 
ATOM   5589 N  N   . SER   C  1  47  ? -17.451 -0.101  19.194 1.00 36.83  ? 60  SER   C N   1 
ATOM   5590 C  CA  . SER   C  1  47  ? -18.863 -0.256  19.513 1.00 45.97  ? 60  SER   C CA  1 
ATOM   5591 C  C   . SER   C  1  47  ? -19.692 -0.721  18.306 1.00 48.33  ? 60  SER   C C   1 
ATOM   5592 O  O   . SER   C  1  47  ? -20.824 -1.160  18.495 1.00 43.42  ? 60  SER   C O   1 
ATOM   5593 C  CB  . SER   C  1  47  ? -19.408 0.991   20.143 1.00 41.81  ? 60  SER   C CB  1 
ATOM   5594 O  OG  . SER   C  1  47  ? -18.953 1.085   21.487 1.00 43.55  ? 60  SER   C OG  1 
ATOM   5595 N  N   . HIS   C  1  48  ? -19.111 -0.698  17.095 1.00 44.58  ? 61  HIS   C N   1 
ATOM   5596 C  CA  . HIS   C  1  48  ? -19.748 -1.282  15.918 1.00 42.11  ? 61  HIS   C CA  1 
ATOM   5597 C  C   . HIS   C  1  48  ? -19.086 -2.573  15.456 1.00 39.62  ? 61  HIS   C C   1 
ATOM   5598 O  O   . HIS   C  1  48  ? -19.462 -3.101  14.416 1.00 41.04  ? 61  HIS   C O   1 
ATOM   5599 C  CB  . HIS   C  1  48  ? -19.731 -0.334  14.728 1.00 35.92  ? 61  HIS   C CB  1 
ATOM   5600 C  CG  . HIS   C  1  48  ? -20.722 0.759   14.863 1.00 39.30  ? 61  HIS   C CG  1 
ATOM   5601 N  ND1 . HIS   C  1  48  ? -21.943 0.677   14.220 1.00 37.80  ? 61  HIS   C ND1 1 
ATOM   5602 C  CD2 . HIS   C  1  48  ? -20.698 1.937   15.519 1.00 33.21  ? 61  HIS   C CD2 1 
ATOM   5603 C  CE1 . HIS   C  1  48  ? -22.616 1.805   14.481 1.00 39.09  ? 61  HIS   C CE1 1 
ATOM   5604 N  NE2 . HIS   C  1  48  ? -21.887 2.577   15.267 1.00 34.55  ? 61  HIS   C NE2 1 
ATOM   5605 N  N   . GLY   C  1  49  ? -18.118 -3.094  16.216 1.00 37.75  ? 62  GLY   C N   1 
ATOM   5606 C  CA  . GLY   C  1  49  ? -17.532 -4.382  15.881 1.00 37.59  ? 62  GLY   C CA  1 
ATOM   5607 C  C   . GLY   C  1  49  ? -16.527 -4.315  14.726 1.00 34.72  ? 62  GLY   C C   1 
ATOM   5608 O  O   . GLY   C  1  49  ? -16.141 -5.349  14.208 1.00 37.56  ? 62  GLY   C O   1 
ATOM   5609 N  N   . TYR   C  1  50  ? -16.059 -3.126  14.341 1.00 35.71  ? 63  TYR   C N   1 
ATOM   5610 C  CA  . TYR   C  1  50  ? -14.903 -3.024  13.458 1.00 40.22  ? 63  TYR   C CA  1 
ATOM   5611 C  C   . TYR   C  1  50  ? -13.631 -3.437  14.203 1.00 40.34  ? 63  TYR   C C   1 
ATOM   5612 O  O   . TYR   C  1  50  ? -12.730 -3.998  13.599 1.00 48.27  ? 63  TYR   C O   1 
ATOM   5613 C  CB  . TYR   C  1  50  ? -14.764 -1.627  12.861 1.00 38.40  ? 63  TYR   C CB  1 
ATOM   5614 C  CG  . TYR   C  1  50  ? -15.714 -1.390  11.698 1.00 45.25  ? 63  TYR   C CG  1 
ATOM   5615 C  CD1 . TYR   C  1  50  ? -15.423 -1.885  10.429 1.00 47.88  ? 63  TYR   C CD1 1 
ATOM   5616 C  CD2 . TYR   C  1  50  ? -16.916 -0.727  11.872 1.00 43.51  ? 63  TYR   C CD2 1 
ATOM   5617 C  CE1 . TYR   C  1  50  ? -16.284 -1.697  9.362  1.00 45.71  ? 63  TYR   C CE1 1 
ATOM   5618 C  CE2 . TYR   C  1  50  ? -17.793 -0.539  10.818 1.00 46.51  ? 63  TYR   C CE2 1 
ATOM   5619 C  CZ  . TYR   C  1  50  ? -17.470 -1.015  9.560  1.00 47.82  ? 63  TYR   C CZ  1 
ATOM   5620 O  OH  . TYR   C  1  50  ? -18.360 -0.833  8.551  1.00 48.56  ? 63  TYR   C OH  1 
ATOM   5621 N  N   . LEU   C  1  51  ? -13.537 -3.081  15.484 1.00 39.29  ? 64  LEU   C N   1 
ATOM   5622 C  CA  . LEU   C  1  51  ? -12.552 -3.620  16.414 1.00 43.37  ? 64  LEU   C CA  1 
ATOM   5623 C  C   . LEU   C  1  51  ? -13.242 -4.625  17.319 1.00 43.31  ? 64  LEU   C C   1 
ATOM   5624 O  O   . LEU   C  1  51  ? -14.464 -4.583  17.440 1.00 53.21  ? 64  LEU   C O   1 
ATOM   5625 C  CB  . LEU   C  1  51  ? -11.956 -2.515  17.287 1.00 39.70  ? 64  LEU   C CB  1 
ATOM   5626 C  CG  . LEU   C  1  51  ? -11.067 -1.498  16.585 1.00 40.79  ? 64  LEU   C CG  1 
ATOM   5627 C  CD1 . LEU   C  1  51  ? -10.772 -0.295  17.430 1.00 40.01  ? 64  LEU   C CD1 1 
ATOM   5628 C  CD2 . LEU   C  1  51  ? -9.797  -2.191  16.200 1.00 41.13  ? 64  LEU   C CD2 1 
ATOM   5629 N  N   . PRO   C  1  52  ? -12.483 -5.487  18.031 1.00 45.94  ? 65  PRO   C N   1 
ATOM   5630 C  CA  . PRO   C  1  52  ? -13.037 -6.245  19.156 1.00 44.30  ? 65  PRO   C CA  1 
ATOM   5631 C  C   . PRO   C  1  52  ? -13.825 -5.336  20.090 1.00 44.09  ? 65  PRO   C C   1 
ATOM   5632 O  O   . PRO   C  1  52  ? -13.343 -4.270  20.451 1.00 44.99  ? 65  PRO   C O   1 
ATOM   5633 C  CB  . PRO   C  1  52  ? -11.799 -6.850  19.828 1.00 45.47  ? 65  PRO   C CB  1 
ATOM   5634 C  CG  . PRO   C  1  52  ? -10.799 -6.975  18.705 1.00 46.76  ? 65  PRO   C CG  1 
ATOM   5635 C  CD  . PRO   C  1  52  ? -11.049 -5.752  17.823 1.00 43.75  ? 65  PRO   C CD  1 
ATOM   5636 N  N   . ARG   C  1  53  ? -15.043 -5.751  20.461 1.00 46.47  ? 66  ARG   C N   1 
ATOM   5637 C  CA  . ARG   C  1  53  ? -15.959 -4.894  21.193 1.00 43.05  ? 66  ARG   C CA  1 
ATOM   5638 C  C   . ARG   C  1  53  ? -15.466 -4.661  22.626 1.00 42.85  ? 66  ARG   C C   1 
ATOM   5639 O  O   . ARG   C  1  53  ? -15.917 -3.723  23.302 1.00 37.04  ? 66  ARG   C O   1 
ATOM   5640 C  CB  . ARG   C  1  53  ? -17.356 -5.526  21.161 1.00 53.55  ? 66  ARG   C CB  1 
ATOM   5641 C  CG  . ARG   C  1  53  ? -18.001 -5.442  19.786 1.00 53.08  ? 66  ARG   C CG  1 
ATOM   5642 C  CD  . ARG   C  1  53  ? -19.445 -5.896  19.787 1.00 51.54  ? 66  ARG   C CD  1 
ATOM   5643 N  NE  . ARG   C  1  53  ? -19.954 -6.013  18.414 1.00 49.64  ? 66  ARG   C NE  1 
ATOM   5644 C  CZ  . ARG   C  1  53  ? -20.641 -5.064  17.818 1.00 44.45  ? 66  ARG   C CZ  1 
ATOM   5645 N  NH1 . ARG   C  1  53  ? -20.850 -3.919  18.434 1.00 41.55  ? 66  ARG   C NH1 1 
ATOM   5646 N  NH2 . ARG   C  1  53  ? -21.110 -5.234  16.595 1.00 51.87  ? 66  ARG   C NH2 1 
ATOM   5647 N  N   . ASP   C  1  54  ? -14.524 -5.486  23.092 1.00 39.09  ? 67  ASP   C N   1 
ATOM   5648 C  CA  . ASP   C  1  54  ? -13.956 -5.287  24.416 1.00 45.92  ? 67  ASP   C CA  1 
ATOM   5649 C  C   . ASP   C  1  54  ? -12.873 -4.201  24.429 1.00 42.00  ? 67  ASP   C C   1 
ATOM   5650 O  O   . ASP   C  1  54  ? -12.424 -3.815  25.499 1.00 44.48  ? 67  ASP   C O   1 
ATOM   5651 C  CB  . ASP   C  1  54  ? -13.459 -6.591  25.019 1.00 48.39  ? 67  ASP   C CB  1 
ATOM   5652 C  CG  . ASP   C  1  54  ? -12.212 -7.209  24.390 1.00 58.20  ? 67  ASP   C CG  1 
ATOM   5653 O  OD1 . ASP   C  1  54  ? -11.658 -6.616  23.419 1.00 63.32  ? 67  ASP   C OD1 1 
ATOM   5654 O  OD2 . ASP   C  1  54  ? -11.778 -8.263  24.911 1.00 62.89  ? 67  ASP   C OD2 1 
ATOM   5655 N  N   . GLY   C  1  55  ? -12.476 -3.678  23.268 1.00 41.69  ? 68  GLY   C N   1 
ATOM   5656 C  CA  . GLY   C  1  55  ? -11.643 -2.479  23.239 1.00 43.30  ? 68  GLY   C CA  1 
ATOM   5657 C  C   . GLY   C  1  55  ? -10.146 -2.773  23.413 1.00 41.14  ? 68  GLY   C C   1 
ATOM   5658 O  O   . GLY   C  1  55  ? -9.342  -1.881  23.694 1.00 42.56  ? 68  GLY   C O   1 
ATOM   5659 N  N   . VAL   C  1  56  ? -9.776  -4.035  23.208 1.00 38.64  ? 69  VAL   C N   1 
ATOM   5660 C  CA  . VAL   C  1  56  ? -8.397  -4.472  23.226 1.00 38.18  ? 69  VAL   C CA  1 
ATOM   5661 C  C   . VAL   C  1  56  ? -8.123  -5.131  21.884 1.00 36.70  ? 69  VAL   C C   1 
ATOM   5662 O  O   . VAL   C  1  56  ? -8.868  -6.010  21.468 1.00 37.57  ? 69  VAL   C O   1 
ATOM   5663 C  CB  . VAL   C  1  56  ? -8.151  -5.448  24.392 1.00 41.96  ? 69  VAL   C CB  1 
ATOM   5664 C  CG1 . VAL   C  1  56  ? -6.782  -6.116  24.309 1.00 44.15  ? 69  VAL   C CG1 1 
ATOM   5665 C  CG2 . VAL   C  1  56  ? -8.312  -4.749  25.739 1.00 44.23  ? 69  VAL   C CG2 1 
ATOM   5666 N  N   . ALA   C  1  57  ? -7.059  -4.690  21.203 1.00 36.75  ? 70  ALA   C N   1 
ATOM   5667 C  CA  . ALA   C  1  57  ? -6.842  -5.091  19.827 1.00 33.41  ? 70  ALA   C CA  1 
ATOM   5668 C  C   . ALA   C  1  57  ? -5.359  -5.137  19.486 1.00 33.97  ? 70  ALA   C C   1 
ATOM   5669 O  O   . ALA   C  1  57  ? -4.542  -4.512  20.148 1.00 38.10  ? 70  ALA   C O   1 
ATOM   5670 C  CB  . ALA   C  1  57  ? -7.577  -4.138  18.939 1.00 33.93  ? 70  ALA   C CB  1 
ATOM   5671 N  N   . THR   C  1  58  ? -5.035  -5.851  18.400 1.00 34.05  ? 71  THR   C N   1 
ATOM   5672 C  CA  . THR   C  1  58  ? -3.699  -5.838  17.837 1.00 33.62  ? 71  THR   C CA  1 
ATOM   5673 C  C   . THR   C  1  58  ? -3.542  -4.559  17.033 1.00 33.45  ? 71  THR   C C   1 
ATOM   5674 O  O   . THR   C  1  58  ? -4.526  -3.986  16.584 1.00 36.81  ? 71  THR   C O   1 
ATOM   5675 C  CB  . THR   C  1  58  ? -3.419  -7.050  16.958 1.00 34.98  ? 71  THR   C CB  1 
ATOM   5676 O  OG1 . THR   C  1  58  ? -4.227  -6.843  15.803 1.00 39.11  ? 71  THR   C OG1 1 
ATOM   5677 C  CG2 . THR   C  1  58  ? -3.690  -8.374  17.656 1.00 36.28  ? 71  THR   C CG2 1 
ATOM   5678 N  N   . PRO   C  1  59  ? -2.302  -4.059  16.862 1.00 34.95  ? 72  PRO   C N   1 
ATOM   5679 C  CA  . PRO   C  1  59  ? -2.056  -2.935  15.958 1.00 36.76  ? 72  PRO   C CA  1 
ATOM   5680 C  C   . PRO   C  1  59  ? -2.659  -3.164  14.574 1.00 34.38  ? 72  PRO   C C   1 
ATOM   5681 O  O   . PRO   C  1  59  ? -3.249  -2.258  13.998 1.00 32.39  ? 72  PRO   C O   1 
ATOM   5682 C  CB  . PRO   C  1  59  ? -0.518  -2.851  15.920 1.00 33.39  ? 72  PRO   C CB  1 
ATOM   5683 C  CG  . PRO   C  1  59  ? -0.075  -3.432  17.251 1.00 35.67  ? 72  PRO   C CG  1 
ATOM   5684 C  CD  . PRO   C  1  59  ? -1.086  -4.530  17.551 1.00 35.22  ? 72  PRO   C CD  1 
ATOM   5685 N  N   . ALA   C  1  60  ? -2.480  -4.374  14.041 1.00 33.85  ? 73  ALA   C N   1 
ATOM   5686 C  CA  . ALA   C  1  60  ? -2.988  -4.697  12.720 1.00 34.61  ? 73  ALA   C CA  1 
ATOM   5687 C  C   . ALA   C  1  60  ? -4.502  -4.533  12.685 1.00 33.03  ? 73  ALA   C C   1 
ATOM   5688 O  O   . ALA   C  1  60  ? -5.016  -3.968  11.736 1.00 31.38  ? 73  ALA   C O   1 
ATOM   5689 C  CB  . ALA   C  1  60  ? -2.602  -6.104  12.323 1.00 34.39  ? 73  ALA   C CB  1 
ATOM   5690 N  N   . GLN   C  1  61  ? -5.203  -4.986  13.729 1.00 33.22  ? 74  GLN   C N   1 
ATOM   5691 C  CA  . GLN   C  1  61  ? -6.648  -4.852  13.748 1.00 34.75  ? 74  GLN   C CA  1 
ATOM   5692 C  C   . GLN   C  1  61  ? -7.055  -3.389  13.785 1.00 33.67  ? 74  GLN   C C   1 
ATOM   5693 O  O   . GLN   C  1  61  ? -8.048  -3.013  13.171 1.00 37.76  ? 74  GLN   C O   1 
ATOM   5694 C  CB  . GLN   C  1  61  ? -7.292  -5.546  14.943 1.00 36.73  ? 74  GLN   C CB  1 
ATOM   5695 C  CG  . GLN   C  1  61  ? -7.251  -7.063  14.848 1.00 38.99  ? 74  GLN   C CG  1 
ATOM   5696 C  CD  . GLN   C  1  61  ? -7.654  -7.707  16.155 1.00 44.05  ? 74  GLN   C CD  1 
ATOM   5697 O  OE1 . GLN   C  1  61  ? -7.290  -7.262  17.251 1.00 46.85  ? 74  GLN   C OE1 1 
ATOM   5698 N  NE2 . GLN   C  1  61  ? -8.430  -8.766  16.046 1.00 49.62  ? 74  GLN   C NE2 1 
ATOM   5699 N  N   . ILE   C  1  62  ? -6.311  -2.572  14.529 1.00 33.93  ? 75  ILE   C N   1 
ATOM   5700 C  CA  . ILE   C  1  62  ? -6.637  -1.157  14.642 1.00 36.02  ? 75  ILE   C CA  1 
ATOM   5701 C  C   . ILE   C  1  62  ? -6.476  -0.489  13.270 1.00 34.61  ? 75  ILE   C C   1 
ATOM   5702 O  O   . ILE   C  1  62  ? -7.322  0.294   12.825 1.00 33.06  ? 75  ILE   C O   1 
ATOM   5703 C  CB  . ILE   C  1  62  ? -5.786  -0.494  15.738 1.00 30.83  ? 75  ILE   C CB  1 
ATOM   5704 C  CG1 . ILE   C  1  62  ? -6.198  -0.995  17.113 1.00 30.20  ? 75  ILE   C CG1 1 
ATOM   5705 C  CG2 . ILE   C  1  62  ? -5.855  1.022   15.634 1.00 29.15  ? 75  ILE   C CG2 1 
ATOM   5706 C  CD1 . ILE   C  1  62  ? -5.296  -0.543  18.246 1.00 30.74  ? 75  ILE   C CD1 1 
ATOM   5707 N  N   . ILE   C  1  63  ? -5.385  -0.816  12.584 1.00 29.77  ? 76  ILE   C N   1 
ATOM   5708 C  CA  . ILE   C  1  63  ? -5.127  -0.202  11.297 1.00 31.75  ? 76  ILE   C CA  1 
ATOM   5709 C  C   . ILE   C  1  63  ? -6.233  -0.578  10.319 1.00 30.63  ? 76  ILE   C C   1 
ATOM   5710 O  O   . ILE   C  1  63  ? -6.793  0.306   9.695  1.00 29.15  ? 76  ILE   C O   1 
ATOM   5711 C  CB  . ILE   C  1  63  ? -3.726  -0.566  10.790 1.00 31.38  ? 76  ILE   C CB  1 
ATOM   5712 C  CG1 . ILE   C  1  63  ? -2.684  0.106   11.641 1.00 33.33  ? 76  ILE   C CG1 1 
ATOM   5713 C  CG2 . ILE   C  1  63  ? -3.557  -0.209  9.312  1.00 33.47  ? 76  ILE   C CG2 1 
ATOM   5714 C  CD1 . ILE   C  1  63  ? -1.375  -0.631  11.655 1.00 34.90  ? 76  ILE   C CD1 1 
ATOM   5715 N  N   . THR   C  1  64  ? -6.588  -1.868  10.231 1.00 34.07  ? 77  THR   C N   1 
ATOM   5716 C  CA  A THR   C  1  64  ? -7.583  -2.294  9.266  0.50 33.74  ? 77  THR   C CA  1 
ATOM   5717 C  CA  B THR   C  1  64  ? -7.580  -2.280  9.247  0.50 34.81  ? 77  THR   C CA  1 
ATOM   5718 C  C   . THR   C  1  64  ? -8.934  -1.659  9.602  1.00 31.88  ? 77  THR   C C   1 
ATOM   5719 O  O   . THR   C  1  64  ? -9.652  -1.252  8.703  1.00 29.12  ? 77  THR   C O   1 
ATOM   5720 C  CB  A THR   C  1  64  ? -7.676  -3.818  9.192  0.50 33.94  ? 77  THR   C CB  1 
ATOM   5721 C  CB  B THR   C  1  64  ? -7.630  -3.793  8.984  0.50 37.39  ? 77  THR   C CB  1 
ATOM   5722 O  OG1 A THR   C  1  64  ? -8.133  -4.164  10.492 0.50 41.02  ? 77  THR   C OG1 1 
ATOM   5723 O  OG1 B THR   C  1  64  ? -8.990  -4.196  8.781  0.50 35.61  ? 77  THR   C OG1 1 
ATOM   5724 C  CG2 A THR   C  1  64  ? -6.365  -4.501  8.882  0.50 28.81  ? 77  THR   C CG2 1 
ATOM   5725 C  CG2 B THR   C  1  64  ? -7.038  -4.657  10.078 0.50 39.48  ? 77  THR   C CG2 1 
ATOM   5726 N  N   . ALA   C  1  65  ? -9.248  -1.516  10.899 1.00 33.32  ? 78  ALA   C N   1 
ATOM   5727 C  CA  . ALA   C  1  65  ? -10.514 -0.946  11.355 1.00 31.21  ? 78  ALA   C CA  1 
ATOM   5728 C  C   . ALA   C  1  65  ? -10.626 0.534   11.025 1.00 29.58  ? 78  ALA   C C   1 
ATOM   5729 O  O   . ALA   C  1  65  ? -11.692 0.986   10.614 1.00 30.81  ? 78  ALA   C O   1 
ATOM   5730 C  CB  . ALA   C  1  65  ? -10.691 -1.152  12.848 1.00 34.33  ? 78  ALA   C CB  1 
ATOM   5731 N  N   . THR   C  1  66  ? -9.555  1.309   11.229 1.00 32.40  ? 79  THR   C N   1 
ATOM   5732 C  CA  . THR   C  1  66  ? -9.604  2.736   10.918 1.00 31.93  ? 79  THR   C CA  1 
ATOM   5733 C  C   . THR   C  1  66  ? -9.752  2.943   9.412  1.00 29.89  ? 79  THR   C C   1 
ATOM   5734 O  O   . THR   C  1  66  ? -10.360 3.907   8.976  1.00 28.53  ? 79  THR   C O   1 
ATOM   5735 C  CB  . THR   C  1  66  ? -8.386  3.491   11.446 1.00 35.04  ? 79  THR   C CB  1 
ATOM   5736 O  OG1 . THR   C  1  66  ? -7.218  2.933   10.860 1.00 33.64  ? 79  THR   C OG1 1 
ATOM   5737 C  CG2 . THR   C  1  66  ? -8.262  3.410   12.953 1.00 37.07  ? 79  THR   C CG2 1 
ATOM   5738 N  N   . GLN   C  1  67  ? -9.191  2.033   8.613  1.00 31.10  ? 80  GLN   C N   1 
ATOM   5739 C  CA  . GLN   C  1  67  ? -9.308  2.113   7.165  1.00 32.99  ? 80  GLN   C CA  1 
ATOM   5740 C  C   . GLN   C  1  67  ? -10.701 1.678   6.716  1.00 30.25  ? 80  GLN   C C   1 
ATOM   5741 O  O   . GLN   C  1  67  ? -11.322 2.371   5.942  1.00 29.57  ? 80  GLN   C O   1 
ATOM   5742 C  CB  . GLN   C  1  67  ? -8.218  1.260   6.526  1.00 31.67  ? 80  GLN   C CB  1 
ATOM   5743 C  CG  . GLN   C  1  67  ? -6.829  1.815   6.789  1.00 32.06  ? 80  GLN   C CG  1 
ATOM   5744 C  CD  . GLN   C  1  67  ? -5.685  1.042   6.172  1.00 33.45  ? 80  GLN   C CD  1 
ATOM   5745 O  OE1 . GLN   C  1  67  ? -4.592  1.582   6.037  1.00 35.79  ? 80  GLN   C OE1 1 
ATOM   5746 N  NE2 . GLN   C  1  67  ? -5.891  -0.212  5.803  1.00 31.86  ? 80  GLN   C NE2 1 
ATOM   5747 N  N   . GLU   C  1  68  ? -11.192 0.530   7.199  1.00 32.29  ? 81  GLU   C N   1 
ATOM   5748 C  CA  . GLU   C  1  68  ? -12.485 0.030   6.772  1.00 34.55  ? 81  GLU   C CA  1 
ATOM   5749 C  C   . GLU   C  1  68  ? -13.581 1.000   7.214  1.00 36.25  ? 81  GLU   C C   1 
ATOM   5750 O  O   . GLU   C  1  68  ? -14.453 1.347   6.429  1.00 39.79  ? 81  GLU   C O   1 
ATOM   5751 C  CB  . GLU   C  1  68  ? -12.808 -1.352  7.328  1.00 40.81  ? 81  GLU   C CB  1 
ATOM   5752 C  CG  . GLU   C  1  68  ? -11.967 -2.485  6.752  1.00 53.68  ? 81  GLU   C CG  1 
ATOM   5753 C  CD  . GLU   C  1  68  ? -11.964 -2.591  5.235  1.00 64.40  ? 81  GLU   C CD  1 
ATOM   5754 O  OE1 . GLU   C  1  68  ? -10.854 -2.829  4.679  1.00 53.06  ? 81  GLU   C OE1 1 
ATOM   5755 O  OE2 . GLU   C  1  68  ? -13.059 -2.421  4.618  1.00 76.09  ? 81  GLU   C OE2 1 
ATOM   5756 N  N   . GLY   C  1  69  ? -13.514 1.473   8.461  1.00 33.26  ? 82  GLY   C N   1 
ATOM   5757 C  CA  . GLY   C  1  69  ? -14.627 2.210   9.023  1.00 33.54  ? 82  GLY   C CA  1 
ATOM   5758 C  C   . GLY   C  1  69  ? -14.653 3.680   8.621  1.00 31.50  ? 82  GLY   C C   1 
ATOM   5759 O  O   . GLY   C  1  69  ? -15.726 4.256   8.533  1.00 34.99  ? 82  GLY   C O   1 
ATOM   5760 N  N   . PHE   C  1  70  ? -13.482 4.291   8.414  1.00 30.81  ? 83  PHE   C N   1 
ATOM   5761 C  CA  . PHE   C  1  70  ? -13.408 5.734   8.239  1.00 32.17  ? 83  PHE   C CA  1 
ATOM   5762 C  C   . PHE   C  1  70  ? -12.567 6.152   7.045  1.00 31.71  ? 83  PHE   C C   1 
ATOM   5763 O  O   . PHE   C  1  70  ? -12.472 7.340   6.777  1.00 29.91  ? 83  PHE   C O   1 
ATOM   5764 C  CB  . PHE   C  1  70  ? -12.762 6.394   9.459  1.00 36.43  ? 83  PHE   C CB  1 
ATOM   5765 C  CG  . PHE   C  1  70  ? -13.685 6.507   10.656 1.00 40.01  ? 83  PHE   C CG  1 
ATOM   5766 C  CD1 . PHE   C  1  70  ? -14.731 7.419   10.651 1.00 39.56  ? 83  PHE   C CD1 1 
ATOM   5767 C  CD2 . PHE   C  1  70  ? -13.481 5.726   11.781 1.00 43.64  ? 83  PHE   C CD2 1 
ATOM   5768 C  CE1 . PHE   C  1  70  ? -15.578 7.513   11.739 1.00 42.40  ? 83  PHE   C CE1 1 
ATOM   5769 C  CE2 . PHE   C  1  70  ? -14.320 5.840   12.866 1.00 45.30  ? 83  PHE   C CE2 1 
ATOM   5770 C  CZ  . PHE   C  1  70  ? -15.365 6.738   12.844 1.00 45.91  ? 83  PHE   C CZ  1 
ATOM   5771 N  N   . ASN   C  1  71  ? -11.930 5.187   6.370  1.00 33.45  ? 84  ASN   C N   1 
ATOM   5772 C  CA  . ASN   C  1  71  ? -10.984 5.479   5.309  1.00 32.66  ? 84  ASN   C CA  1 
ATOM   5773 C  C   . ASN   C  1  71  ? -9.830  6.327   5.828  1.00 31.00  ? 84  ASN   C C   1 
ATOM   5774 O  O   . ASN   C  1  71  ? -9.367  7.235   5.152  1.00 30.71  ? 84  ASN   C O   1 
ATOM   5775 C  CB  . ASN   C  1  71  ? -11.668 6.187   4.142  1.00 36.31  ? 84  ASN   C CB  1 
ATOM   5776 C  CG  . ASN   C  1  71  ? -11.192 5.668   2.810  1.00 36.60  ? 84  ASN   C CG  1 
ATOM   5777 O  OD1 . ASN   C  1  71  ? -10.152 5.013   2.704  1.00 38.85  ? 84  ASN   C OD1 1 
ATOM   5778 N  ND2 . ASN   C  1  71  ? -11.966 5.927   1.780  1.00 38.94  ? 84  ASN   C ND2 1 
ATOM   5779 N  N   . PHE   C  1  72  ? -9.377  6.047   7.048  1.00 32.40  ? 85  PHE   C N   1 
ATOM   5780 C  CA  . PHE   C  1  72  ? -8.190  6.707   7.563  1.00 32.18  ? 85  PHE   C CA  1 
ATOM   5781 C  C   . PHE   C  1  72  ? -7.019  6.289   6.679  1.00 30.28  ? 85  PHE   C C   1 
ATOM   5782 O  O   . PHE   C  1  72  ? -6.872  5.121   6.351  1.00 29.52  ? 85  PHE   C O   1 
ATOM   5783 C  CB  . PHE   C  1  72  ? -7.977  6.308   9.029  1.00 34.11  ? 85  PHE   C CB  1 
ATOM   5784 C  CG  . PHE   C  1  72  ? -7.094  7.221   9.866  1.00 32.46  ? 85  PHE   C CG  1 
ATOM   5785 C  CD1 . PHE   C  1  72  ? -7.264  8.592   9.827  1.00 34.48  ? 85  PHE   C CD1 1 
ATOM   5786 C  CD2 . PHE   C  1  72  ? -6.107  6.706   10.697 1.00 34.69  ? 85  PHE   C CD2 1 
ATOM   5787 C  CE1 . PHE   C  1  72  ? -6.475  9.429   10.597 1.00 35.82  ? 85  PHE   C CE1 1 
ATOM   5788 C  CE2 . PHE   C  1  72  ? -5.313  7.550   11.458 1.00 37.63  ? 85  PHE   C CE2 1 
ATOM   5789 C  CZ  . PHE   C  1  72  ? -5.493  8.909   11.404 1.00 36.75  ? 85  PHE   C CZ  1 
ATOM   5790 N  N   . GLU   C  1  73  ? -6.213  7.252   6.252  1.00 30.24  ? 86  GLU   C N   1 
ATOM   5791 C  CA  . GLU   C  1  73  ? -5.083  6.966   5.380  1.00 32.41  ? 86  GLU   C CA  1 
ATOM   5792 C  C   . GLU   C  1  73  ? -4.089  6.014   6.060  1.00 30.39  ? 86  GLU   C C   1 
ATOM   5793 O  O   . GLU   C  1  73  ? -3.782  6.135   7.233  1.00 28.74  ? 86  GLU   C O   1 
ATOM   5794 C  CB  . GLU   C  1  73  ? -4.483  8.300   4.939  1.00 34.88  ? 86  GLU   C CB  1 
ATOM   5795 C  CG  . GLU   C  1  73  ? -3.476  8.173   3.793  1.00 43.73  ? 86  GLU   C CG  1 
ATOM   5796 C  CD  . GLU   C  1  73  ? -2.045  7.842   4.220  1.00 48.55  ? 86  GLU   C CD  1 
ATOM   5797 O  OE1 . GLU   C  1  73  ? -1.442  6.914   3.619  1.00 47.03  ? 86  GLU   C OE1 1 
ATOM   5798 O  OE2 . GLU   C  1  73  ? -1.548  8.503   5.178  1.00 52.16  ? 86  GLU   C OE2 1 
ATOM   5799 N  N   . ASN   C  1  74  ? -3.567  5.069   5.283  1.00 30.58  ? 87  ASN   C N   1 
ATOM   5800 C  CA  . ASN   C  1  74  ? -2.740  3.968   5.761  1.00 31.79  ? 87  ASN   C CA  1 
ATOM   5801 C  C   . ASN   C  1  74  ? -1.540  4.432   6.584  1.00 30.81  ? 87  ASN   C C   1 
ATOM   5802 O  O   . ASN   C  1  74  ? -1.307  3.915   7.664  1.00 30.81  ? 87  ASN   C O   1 
ATOM   5803 C  CB  . ASN   C  1  74  ? -2.263  3.141   4.574  1.00 31.57  ? 87  ASN   C CB  1 
ATOM   5804 C  CG  . ASN   C  1  74  ? -1.442  1.929   4.921  1.00 28.16  ? 87  ASN   C CG  1 
ATOM   5805 O  OD1 . ASN   C  1  74  ? -0.296  1.800   4.477  1.00 35.58  ? 87  ASN   C OD1 1 
ATOM   5806 N  ND2 . ASN   C  1  74  ? -2.031  1.000   5.641  1.00 30.98  ? 87  ASN   C ND2 1 
ATOM   5807 N  N   . ASN   C  1  75  ? -0.751  5.369   6.066  1.00 29.56  ? 88  ASN   C N   1 
ATOM   5808 C  CA  . ASN   C  1  75  ? 0.438   5.797   6.771  1.00 31.59  ? 88  ASN   C CA  1 
ATOM   5809 C  C   . ASN   C  1  75  ? 0.068   6.553   8.039  1.00 30.27  ? 88  ASN   C C   1 
ATOM   5810 O  O   . ASN   C  1  75  ? 0.775   6.417   9.031  1.00 28.69  ? 88  ASN   C O   1 
ATOM   5811 C  CB  . ASN   C  1  75  ? 1.394   6.552   5.864  1.00 32.51  ? 88  ASN   C CB  1 
ATOM   5812 C  CG  . ASN   C  1  75  ? 2.155   5.589   4.979  1.00 38.30  ? 88  ASN   C CG  1 
ATOM   5813 O  OD1 . ASN   C  1  75  ? 2.717   4.580   5.433  1.00 34.22  ? 88  ASN   C OD1 1 
ATOM   5814 N  ND2 . ASN   C  1  75  ? 2.149   5.858   3.686  1.00 46.74  ? 88  ASN   C ND2 1 
ATOM   5815 N  N   . ALA   C  1  76  ? -1.008  7.352   7.987  1.00 30.52  ? 89  ALA   C N   1 
ATOM   5816 C  CA  . ALA   C  1  76  ? -1.493  8.047   9.165  1.00 30.73  ? 89  ALA   C CA  1 
ATOM   5817 C  C   . ALA   C  1  76  ? -1.893  7.024   10.238 1.00 29.40  ? 89  ALA   C C   1 
ATOM   5818 O  O   . ALA   C  1  76  ? -1.572  7.175   11.414 1.00 29.93  ? 89  ALA   C O   1 
ATOM   5819 C  CB  . ALA   C  1  76  ? -2.626  8.966   8.777  1.00 29.34  ? 89  ALA   C CB  1 
ATOM   5820 N  N   . ALA   C  1  77  ? -2.545  5.949   9.799  1.00 30.23  ? 90  ALA   C N   1 
ATOM   5821 C  CA  . ALA   C  1  77  ? -2.987  4.883   10.684 1.00 30.33  ? 90  ALA   C CA  1 
ATOM   5822 C  C   . ALA   C  1  77  ? -1.793  4.174   11.310 1.00 29.36  ? 90  ALA   C C   1 
ATOM   5823 O  O   . ALA   C  1  77  ? -1.826  3.802   12.489 1.00 26.43  ? 90  ALA   C O   1 
ATOM   5824 C  CB  . ALA   C  1  77  ? -3.843  3.901   9.918  1.00 29.71  ? 90  ALA   C CB  1 
ATOM   5825 N  N   . ILE   C  1  78  ? -0.739  4.002   10.502 1.00 26.12  ? 91  ILE   C N   1 
ATOM   5826 C  CA  . ILE   C  1  78  ? 0.467   3.344   10.966 1.00 26.98  ? 91  ILE   C CA  1 
ATOM   5827 C  C   . ILE   C  1  78  ? 1.173   4.223   11.992 1.00 26.19  ? 91  ILE   C C   1 
ATOM   5828 O  O   . ILE   C  1  78  ? 1.505   3.738   13.067 1.00 27.09  ? 91  ILE   C O   1 
ATOM   5829 C  CB  . ILE   C  1  78  ? 1.351   2.947   9.784  1.00 29.63  ? 91  ILE   C CB  1 
ATOM   5830 C  CG1 . ILE   C  1  78  ? 0.750   1.755   9.063  1.00 32.07  ? 91  ILE   C CG1 1 
ATOM   5831 C  CG2 . ILE   C  1  78  ? 2.778   2.650   10.224 1.00 31.02  ? 91  ILE   C CG2 1 
ATOM   5832 C  CD1 . ILE   C  1  78  ? 1.383   1.480   7.706  1.00 31.28  ? 91  ILE   C CD1 1 
ATOM   5833 N  N   . VAL   C  1  79  ? 1.302   5.520   11.705 1.00 24.60  ? 92  VAL   C N   1 
ATOM   5834 C  CA  . VAL   C  1  79  ? 1.942   6.445   12.615 1.00 27.33  ? 92  VAL   C CA  1 
ATOM   5835 C  C   . VAL   C  1  79  ? 1.226   6.468   13.957 1.00 32.35  ? 92  VAL   C C   1 
ATOM   5836 O  O   . VAL   C  1  79  ? 1.898   6.379   14.988 1.00 31.51  ? 92  VAL   C O   1 
ATOM   5837 C  CB  . VAL   C  1  79  ? 2.047   7.851   12.004 1.00 30.90  ? 92  VAL   C CB  1 
ATOM   5838 C  CG1 . VAL   C  1  79  ? 2.466   8.898   13.009 1.00 31.89  ? 92  VAL   C CG1 1 
ATOM   5839 C  CG2 . VAL   C  1  79  ? 3.029   7.855   10.849 1.00 31.68  ? 92  VAL   C CG2 1 
ATOM   5840 N  N   . ALA   C  1  80  ? -0.113  6.601   13.937 1.00 29.76  ? 93  ALA   C N   1 
ATOM   5841 C  CA  . ALA   C  1  80  ? -0.865  6.724   15.167 1.00 29.64  ? 93  ALA   C CA  1 
ATOM   5842 C  C   . ALA   C  1  80  ? -0.831  5.408   15.928 1.00 31.25  ? 93  ALA   C C   1 
ATOM   5843 O  O   . ALA   C  1  80  ? -0.692  5.396   17.147 1.00 31.86  ? 93  ALA   C O   1 
ATOM   5844 C  CB  . ALA   C  1  80  ? -2.289  7.141   14.880 1.00 32.74  ? 93  ALA   C CB  1 
ATOM   5845 N  N   . THR   C  1  81  ? -0.978  4.291   15.206 1.00 31.04  ? 94  THR   C N   1 
ATOM   5846 C  CA  . THR   C  1  81  ? -1.216  3.024   15.876 1.00 28.73  ? 94  THR   C CA  1 
ATOM   5847 C  C   . THR   C  1  81  ? 0.036   2.566   16.620 1.00 30.60  ? 94  THR   C C   1 
ATOM   5848 O  O   . THR   C  1  81  ? -0.051  2.134   17.776 1.00 32.05  ? 94  THR   C O   1 
ATOM   5849 C  CB  . THR   C  1  81  ? -1.704  1.962   14.898 1.00 29.11  ? 94  THR   C CB  1 
ATOM   5850 O  OG1 . THR   C  1  81  ? -2.999  2.322   14.414 1.00 26.26  ? 94  THR   C OG1 1 
ATOM   5851 C  CG2 . THR   C  1  81  ? -1.854  0.598   15.542 1.00 29.74  ? 94  THR   C CG2 1 
ATOM   5852 N  N   . TYR   C  1  82  ? 1.192   2.617   15.951 1.00 31.44  ? 95  TYR   C N   1 
ATOM   5853 C  CA  . TYR   C  1  82  ? 2.415   2.080   16.521 1.00 29.78  ? 95  TYR   C CA  1 
ATOM   5854 C  C   . TYR   C  1  82  ? 3.007   3.059   17.533 1.00 26.59  ? 95  TYR   C C   1 
ATOM   5855 O  O   . TYR   C  1  82  ? 3.681   2.654   18.460 1.00 28.75  ? 95  TYR   C O   1 
ATOM   5856 C  CB  . TYR   C  1  82  ? 3.395   1.654   15.424 1.00 28.82  ? 95  TYR   C CB  1 
ATOM   5857 C  CG  . TYR   C  1  82  ? 2.936   0.403   14.702 1.00 28.74  ? 95  TYR   C CG  1 
ATOM   5858 C  CD1 . TYR   C  1  82  ? 3.022   -0.846  15.303 1.00 28.45  ? 95  TYR   C CD1 1 
ATOM   5859 C  CD2 . TYR   C  1  82  ? 2.388   0.478   13.426 1.00 32.62  ? 95  TYR   C CD2 1 
ATOM   5860 C  CE1 . TYR   C  1  82  ? 2.655   -1.993  14.628 1.00 28.04  ? 95  TYR   C CE1 1 
ATOM   5861 C  CE2 . TYR   C  1  82  ? 1.977   -0.657  12.759 1.00 30.73  ? 95  TYR   C CE2 1 
ATOM   5862 C  CZ  . TYR   C  1  82  ? 2.109   -1.898  13.357 1.00 33.03  ? 95  TYR   C CZ  1 
ATOM   5863 O  OH  . TYR   C  1  82  ? 1.667   -3.030  12.713 1.00 33.74  ? 95  TYR   C OH  1 
ATOM   5864 N  N   . LEU   C  1  83  ? 2.722   4.344   17.399 1.00 29.71  ? 96  LEU   C N   1 
ATOM   5865 C  CA  . LEU   C  1  83  ? 3.007   5.278   18.472 1.00 30.27  ? 96  LEU   C CA  1 
ATOM   5866 C  C   . LEU   C  1  83  ? 2.269   4.828   19.729 1.00 30.35  ? 96  LEU   C C   1 
ATOM   5867 O  O   . LEU   C  1  83  ? 2.870   4.681   20.779 1.00 34.07  ? 96  LEU   C O   1 
ATOM   5868 C  CB  . LEU   C  1  83  ? 2.594   6.683   18.047 1.00 29.19  ? 96  LEU   C CB  1 
ATOM   5869 C  CG  . LEU   C  1  83  ? 2.693   7.765   19.124 1.00 33.27  ? 96  LEU   C CG  1 
ATOM   5870 C  CD1 . LEU   C  1  83  ? 4.119   7.933   19.598 1.00 34.07  ? 96  LEU   C CD1 1 
ATOM   5871 C  CD2 . LEU   C  1  83  ? 2.157   9.070   18.588 1.00 35.23  ? 96  LEU   C CD2 1 
ATOM   5872 N  N   . GLY   C  1  84  ? 0.956   4.628   19.617 1.00 31.65  ? 97  GLY   C N   1 
ATOM   5873 C  CA  . GLY   C  1  84  ? 0.134   4.210   20.749 1.00 32.09  ? 97  GLY   C CA  1 
ATOM   5874 C  C   . GLY   C  1  84  ? 0.613   2.879   21.322 1.00 30.62  ? 97  GLY   C C   1 
ATOM   5875 O  O   . GLY   C  1  84  ? 0.675   2.714   22.531 1.00 28.91  ? 97  GLY   C O   1 
ATOM   5876 N  N   . HIS   C  1  85  ? 0.975   1.945   20.438 1.00 29.48  ? 98  HIS   C N   1 
ATOM   5877 C  CA  . HIS   C  1  85  ? 1.373   0.611   20.857 1.00 31.04  ? 98  HIS   C CA  1 
ATOM   5878 C  C   . HIS   C  1  85  ? 2.753   0.613   21.524 1.00 31.43  ? 98  HIS   C C   1 
ATOM   5879 O  O   . HIS   C  1  85  ? 2.943   -0.057  22.536 1.00 31.89  ? 98  HIS   C O   1 
ATOM   5880 C  CB  . HIS   C  1  85  ? 1.399   -0.334  19.660 1.00 30.61  ? 98  HIS   C CB  1 
ATOM   5881 C  CG  . HIS   C  1  85  ? 1.595   -1.756  20.028 1.00 31.16  ? 98  HIS   C CG  1 
ATOM   5882 N  ND1 . HIS   C  1  85  ? 0.845   -2.394  20.994 1.00 30.30  ? 98  HIS   C ND1 1 
ATOM   5883 C  CD2 . HIS   C  1  85  ? 2.426   -2.679  19.511 1.00 29.68  ? 98  HIS   C CD2 1 
ATOM   5884 C  CE1 . HIS   C  1  85  ? 1.231   -3.665  21.055 1.00 32.81  ? 98  HIS   C CE1 1 
ATOM   5885 N  NE2 . HIS   C  1  85  ? 2.195   -3.867  20.167 1.00 32.56  ? 98  HIS   C NE2 1 
ATOM   5886 N  N   . LEU   C  1  86  ? 3.723   1.325   20.940 1.00 30.55  ? 99  LEU   C N   1 
ATOM   5887 C  CA  . LEU   C  1  86  ? 5.067   1.372   21.501 1.00 32.22  ? 99  LEU   C CA  1 
ATOM   5888 C  C   . LEU   C  1  86  ? 5.031   1.907   22.930 1.00 30.79  ? 99  LEU   C C   1 
ATOM   5889 O  O   . LEU   C  1  86  ? 5.638   1.328   23.808 1.00 34.70  ? 99  LEU   C O   1 
ATOM   5890 C  CB  . LEU   C  1  86  ? 5.975   2.208   20.601 1.00 31.30  ? 99  LEU   C CB  1 
ATOM   5891 C  CG  . LEU   C  1  86  ? 6.489   1.493   19.350 1.00 31.89  ? 99  LEU   C CG  1 
ATOM   5892 C  CD1 . LEU   C  1  86  ? 7.042   2.474   18.345 1.00 31.90  ? 99  LEU   C CD1 1 
ATOM   5893 C  CD2 . LEU   C  1  86  ? 7.541   0.475   19.702 1.00 35.74  ? 99  LEU   C CD2 1 
ATOM   5894 N  N   . LEU   C  1  87  ? 4.292   2.999   23.147 1.00 34.51  ? 100 LEU   C N   1 
ATOM   5895 C  CA  . LEU   C  1  87  ? 4.229   3.700   24.418 1.00 32.31  ? 100 LEU   C CA  1 
ATOM   5896 C  C   . LEU   C  1  87  ? 3.281   3.028   25.402 1.00 35.13  ? 100 LEU   C C   1 
ATOM   5897 O  O   . LEU   C  1  87  ? 3.551   3.049   26.596 1.00 37.49  ? 100 LEU   C O   1 
ATOM   5898 C  CB  . LEU   C  1  87  ? 3.780   5.127   24.133 1.00 31.84  ? 100 LEU   C CB  1 
ATOM   5899 C  CG  . LEU   C  1  87  ? 4.772   5.964   23.322 1.00 31.57  ? 100 LEU   C CG  1 
ATOM   5900 C  CD1 . LEU   C  1  87  ? 4.197   7.317   23.047 1.00 33.58  ? 100 LEU   C CD1 1 
ATOM   5901 C  CD2 . LEU   C  1  87  ? 6.120   6.107   24.006 1.00 30.79  ? 100 LEU   C CD2 1 
ATOM   5902 N  N   . ASN   C  1  88  ? 2.193   2.428   24.903 1.00 35.19  ? 101 ASN   C N   1 
ATOM   5903 C  CA  . ASN   C  1  88  ? 1.067   2.097   25.758 1.00 35.42  ? 101 ASN   C CA  1 
ATOM   5904 C  C   . ASN   C  1  88  ? 0.600   0.655   25.592 1.00 35.52  ? 101 ASN   C C   1 
ATOM   5905 O  O   . ASN   C  1  88  ? -0.319  0.245   26.288 1.00 37.79  ? 101 ASN   C O   1 
ATOM   5906 C  CB  . ASN   C  1  88  ? -0.124  2.996   25.470 1.00 35.15  ? 101 ASN   C CB  1 
ATOM   5907 C  CG  . ASN   C  1  88  ? 0.175   4.449   25.735 1.00 39.01  ? 101 ASN   C CG  1 
ATOM   5908 O  OD1 . ASN   C  1  88  ? 0.865   4.799   26.701 1.00 38.60  ? 101 ASN   C OD1 1 
ATOM   5909 N  ND2 . ASN   C  1  88  ? -0.332  5.322   24.882 1.00 42.70  ? 101 ASN   C ND2 1 
ATOM   5910 N  N   . GLY   C  1  89  ? 1.213   -0.116  24.694 1.00 35.30  ? 102 GLY   C N   1 
ATOM   5911 C  CA  . GLY   C  1  89  ? 0.740   -1.469  24.428 1.00 33.14  ? 102 GLY   C CA  1 
ATOM   5912 C  C   . GLY   C  1  89  ? 1.659   -2.520  25.035 1.00 33.20  ? 102 GLY   C C   1 
ATOM   5913 O  O   . GLY   C  1  89  ? 2.761   -2.220  25.496 1.00 33.51  ? 102 GLY   C O   1 
ATOM   5914 N  N   . ASN   C  1  90  ? 1.201   -3.767  25.002 1.00 31.68  ? 103 ASN   C N   1 
ATOM   5915 C  CA  . ASN   C  1  90  ? 2.033   -4.875  25.412 1.00 31.62  ? 103 ASN   C CA  1 
ATOM   5916 C  C   . ASN   C  1  90  ? 2.682   -5.461  24.173 1.00 31.89  ? 103 ASN   C C   1 
ATOM   5917 O  O   . ASN   C  1  90  ? 1.998   -6.058  23.357 1.00 37.08  ? 103 ASN   C O   1 
ATOM   5918 C  CB  . ASN   C  1  90  ? 1.202   -5.904  26.155 1.00 34.28  ? 103 ASN   C CB  1 
ATOM   5919 C  CG  . ASN   C  1  90  ? 2.047   -6.991  26.775 1.00 37.03  ? 103 ASN   C CG  1 
ATOM   5920 O  OD1 . ASN   C  1  90  ? 2.948   -7.534  26.119 1.00 35.40  ? 103 ASN   C OD1 1 
ATOM   5921 N  ND2 . ASN   C  1  90  ? 1.777   -7.289  28.045 1.00 36.84  ? 103 ASN   C ND2 1 
ATOM   5922 N  N   . LEU   C  1  91  ? 4.002   -5.309  24.045 1.00 34.12  ? 104 LEU   C N   1 
ATOM   5923 C  CA  . LEU   C  1  91  ? 4.696   -5.649  22.815 1.00 34.33  ? 104 LEU   C CA  1 
ATOM   5924 C  C   . LEU   C  1  91  ? 4.889   -7.149  22.688 1.00 33.27  ? 104 LEU   C C   1 
ATOM   5925 O  O   . LEU   C  1  91  ? 5.095   -7.655  21.596 1.00 34.20  ? 104 LEU   C O   1 
ATOM   5926 C  CB  . LEU   C  1  91  ? 6.020   -4.894  22.788 1.00 40.61  ? 104 LEU   C CB  1 
ATOM   5927 C  CG  . LEU   C  1  91  ? 5.876   -3.372  22.808 1.00 44.77  ? 104 LEU   C CG  1 
ATOM   5928 C  CD1 . LEU   C  1  91  ? 7.176   -2.704  23.105 1.00 47.25  ? 104 LEU   C CD1 1 
ATOM   5929 C  CD2 . LEU   C  1  91  ? 5.346   -2.881  21.483 1.00 50.39  ? 104 LEU   C CD2 1 
ATOM   5930 N  N   . VAL   C  1  92  ? 4.812   -7.863  23.812 1.00 38.10  ? 105 VAL   C N   1 
ATOM   5931 C  CA  . VAL   C  1  92  ? 5.013   -9.301  23.803 1.00 41.16  ? 105 VAL   C CA  1 
ATOM   5932 C  C   . VAL   C  1  92  ? 3.728   -10.003 23.366 1.00 43.01  ? 105 VAL   C C   1 
ATOM   5933 O  O   . VAL   C  1  92  ? 3.791   -10.885 22.507 1.00 44.75  ? 105 VAL   C O   1 
ATOM   5934 C  CB  . VAL   C  1  92  ? 5.539   -9.784  25.165 1.00 44.05  ? 105 VAL   C CB  1 
ATOM   5935 C  CG1 . VAL   C  1  92  ? 5.477   -11.302 25.307 1.00 43.64  ? 105 VAL   C CG1 1 
ATOM   5936 C  CG2 . VAL   C  1  92  ? 6.968   -9.282  25.378 1.00 43.05  ? 105 VAL   C CG2 1 
ATOM   5937 N  N   . THR   C  1  93  ? 2.568   -9.590  23.909 1.00 39.93  ? 106 THR   C N   1 
ATOM   5938 C  CA  . THR   C  1  93  ? 1.295   -10.175 23.503 1.00 39.40  ? 106 THR   C CA  1 
ATOM   5939 C  C   . THR   C  1  93  ? 0.735   -9.521  22.242 1.00 40.12  ? 106 THR   C C   1 
ATOM   5940 O  O   . THR   C  1  93  ? -0.205  -10.059 21.668 1.00 46.17  ? 106 THR   C O   1 
ATOM   5941 C  CB  . THR   C  1  93  ? 0.272   -10.070 24.628 1.00 41.83  ? 106 THR   C CB  1 
ATOM   5942 O  OG1 . THR   C  1  93  ? 0.094   -8.668  24.831 1.00 36.36  ? 106 THR   C OG1 1 
ATOM   5943 C  CG2 . THR   C  1  93  ? 0.725   -10.813 25.873 1.00 45.66  ? 106 THR   C CG2 1 
ATOM   5944 N  N   . ASP   C  1  94  ? 1.267   -8.352  21.856 1.00 36.28  ? 107 ASP   C N   1 
ATOM   5945 C  CA  . ASP   C  1  94  ? 0.814   -7.616  20.683 1.00 36.91  ? 107 ASP   C CA  1 
ATOM   5946 C  C   . ASP   C  1  94  ? -0.598  -7.055  20.867 1.00 35.78  ? 107 ASP   C C   1 
ATOM   5947 O  O   . ASP   C  1  94  ? -1.376  -7.002  19.922 1.00 41.06  ? 107 ASP   C O   1 
ATOM   5948 C  CB  . ASP   C  1  94  ? 0.932   -8.454  19.414 1.00 37.18  ? 107 ASP   C CB  1 
ATOM   5949 C  CG  . ASP   C  1  94  ? 0.973   -7.663  18.109 1.00 43.02  ? 107 ASP   C CG  1 
ATOM   5950 O  OD1 . ASP   C  1  94  ? 1.695   -6.626  18.074 1.00 43.94  ? 107 ASP   C OD1 1 
ATOM   5951 O  OD2 . ASP   C  1  94  ? 0.298   -8.099  17.124 1.00 42.90  ? 107 ASP   C OD2 1 
ATOM   5952 N  N   . LEU   C  1  95  ? -0.940  -6.610  22.078 1.00 39.17  ? 108 LEU   C N   1 
ATOM   5953 C  CA  . LEU   C  1  95  ? -2.277  -6.106  22.358 1.00 35.59  ? 108 LEU   C CA  1 
ATOM   5954 C  C   . LEU   C  1  95  ? -2.173  -4.714  22.964 1.00 34.23  ? 108 LEU   C C   1 
ATOM   5955 O  O   . LEU   C  1  95  ? -1.332  -4.470  23.828 1.00 35.64  ? 108 LEU   C O   1 
ATOM   5956 C  CB  . LEU   C  1  95  ? -3.011  -7.058  23.293 1.00 36.56  ? 108 LEU   C CB  1 
ATOM   5957 C  CG  . LEU   C  1  95  ? -3.278  -8.466  22.756 1.00 38.83  ? 108 LEU   C CG  1 
ATOM   5958 C  CD1 . LEU   C  1  95  ? -3.724  -9.385  23.874 1.00 40.86  ? 108 LEU   C CD1 1 
ATOM   5959 C  CD2 . LEU   C  1  95  ? -4.344  -8.443  21.666 1.00 38.35  ? 108 LEU   C CD2 1 
ATOM   5960 N  N   . LEU   C  1  96  ? -3.059  -3.832  22.495 1.00 34.72  ? 109 LEU   C N   1 
ATOM   5961 C  CA  . LEU   C  1  96  ? -3.181  -2.472  22.978 1.00 32.20  ? 109 LEU   C CA  1 
ATOM   5962 C  C   . LEU   C  1  96  ? -4.615  -2.230  23.455 1.00 36.95  ? 109 LEU   C C   1 
ATOM   5963 O  O   . LEU   C  1  96  ? -5.582  -2.526  22.749 1.00 37.32  ? 109 LEU   C O   1 
ATOM   5964 C  CB  . LEU   C  1  96  ? -2.824  -1.555  21.815 1.00 29.55  ? 109 LEU   C CB  1 
ATOM   5965 C  CG  . LEU   C  1  96  ? -3.115  -0.066  22.024 1.00 29.29  ? 109 LEU   C CG  1 
ATOM   5966 C  CD1 . LEU   C  1  96  ? -2.330  0.478   23.225 1.00 36.12  ? 109 LEU   C CD1 1 
ATOM   5967 C  CD2 . LEU   C  1  96  ? -2.784  0.766   20.812 1.00 26.16  ? 109 LEU   C CD2 1 
ATOM   5968 N  N   . SER   C  1  97  ? -4.737  -1.704  24.677 1.00 34.59  ? 110 SER   C N   1 
ATOM   5969 C  CA  . SER   C  1  97  ? -6.006  -1.220  25.187 1.00 35.45  ? 110 SER   C CA  1 
ATOM   5970 C  C   . SER   C  1  97  ? -6.263  0.174   24.632 1.00 33.05  ? 110 SER   C C   1 
ATOM   5971 O  O   . SER   C  1  97  ? -5.400  1.050   24.733 1.00 32.08  ? 110 SER   C O   1 
ATOM   5972 C  CB  . SER   C  1  97  ? -6.017  -1.206  26.693 1.00 37.10  ? 110 SER   C CB  1 
ATOM   5973 O  OG  . SER   C  1  97  ? -7.123  -0.464  27.180 1.00 40.63  ? 110 SER   C OG  1 
ATOM   5974 N  N   . ILE   C  1  98  ? -7.470  0.395   24.096 1.00 31.65  ? 111 ILE   C N   1 
ATOM   5975 C  CA  . ILE   C  1  98  ? -7.791  1.697   23.541 1.00 33.40  ? 111 ILE   C CA  1 
ATOM   5976 C  C   . ILE   C  1  98  ? -8.210  2.618   24.675 1.00 32.34  ? 111 ILE   C C   1 
ATOM   5977 O  O   . ILE   C  1  98  ? -8.542  3.773   24.437 1.00 39.14  ? 111 ILE   C O   1 
ATOM   5978 C  CB  . ILE   C  1  98  ? -8.861  1.610   22.439 1.00 35.81  ? 111 ILE   C CB  1 
ATOM   5979 C  CG1 . ILE   C  1  98  ? -10.258 1.267   22.987 1.00 39.48  ? 111 ILE   C CG1 1 
ATOM   5980 C  CG2 . ILE   C  1  98  ? -8.451  0.623   21.353 1.00 34.40  ? 111 ILE   C CG2 1 
ATOM   5981 C  CD1 . ILE   C  1  98  ? -11.342 1.269   21.927 1.00 37.40  ? 111 ILE   C CD1 1 
ATOM   5982 N  N   . GLY   C  1  99  ? -8.200  2.094   25.901 1.00 36.49  ? 112 GLY   C N   1 
ATOM   5983 C  CA  . GLY   C  1  99  ? -8.546  2.877   27.073 1.00 39.12  ? 112 GLY   C CA  1 
ATOM   5984 C  C   . GLY   C  1  99  ? -7.510  2.684   28.176 1.00 39.55  ? 112 GLY   C C   1 
ATOM   5985 O  O   . GLY   C  1  99  ? -6.353  3.081   28.016 1.00 35.58  ? 112 GLY   C O   1 
ATOM   5986 N  N   . GLY   C  1  100 ? -7.952  2.130   29.311 1.00 41.17  ? 113 GLY   C N   1 
ATOM   5987 C  CA  . GLY   C  1  100 ? -7.103  2.015   30.487 1.00 42.12  ? 113 GLY   C CA  1 
ATOM   5988 C  C   . GLY   C  1  100 ? -6.526  0.609   30.642 1.00 43.45  ? 113 GLY   C C   1 
ATOM   5989 O  O   . GLY   C  1  100 ? -6.658  -0.231  29.765 1.00 42.84  ? 113 GLY   C O   1 
ATOM   5990 N  N   . ALA   C  1  101 ? -5.902  0.374   31.797 1.00 48.02  ? 114 ALA   C N   1 
ATOM   5991 C  CA  . ALA   C  1  101 ? -5.225  -0.877  32.085 1.00 47.31  ? 114 ALA   C CA  1 
ATOM   5992 C  C   . ALA   C  1  101 ? -6.248  -1.999  32.198 1.00 46.63  ? 114 ALA   C C   1 
ATOM   5993 O  O   . ALA   C  1  101 ? -7.381  -1.784  32.624 1.00 53.17  ? 114 ALA   C O   1 
ATOM   5994 C  CB  . ALA   C  1  101 ? -4.402  -0.736  33.352 1.00 48.41  ? 114 ALA   C CB  1 
ATOM   5995 N  N   . THR   C  1  102 ? -5.839  -3.199  31.791 1.00 44.27  ? 115 THR   C N   1 
ATOM   5996 C  CA  . THR   C  1  102 ? -6.731  -4.336  31.778 1.00 53.99  ? 115 THR   C CA  1 
ATOM   5997 C  C   . THR   C  1  102 ? -5.877  -5.591  31.761 1.00 53.88  ? 115 THR   C C   1 
ATOM   5998 O  O   . THR   C  1  102 ? -4.843  -5.616  31.113 1.00 56.69  ? 115 THR   C O   1 
ATOM   5999 C  CB  . THR   C  1  102 ? -7.681  -4.272  30.575 1.00 61.04  ? 115 THR   C CB  1 
ATOM   6000 O  OG1 . THR   C  1  102 ? -8.436  -5.481  30.514 1.00 59.21  ? 115 THR   C OG1 1 
ATOM   6001 C  CG2 . THR   C  1  102 ? -6.955  -4.134  29.248 1.00 63.42  ? 115 THR   C CG2 1 
ATOM   6002 N  N   . PRO   C  1  103 ? -6.296  -6.675  32.450 1.00 59.96  ? 116 PRO   C N   1 
ATOM   6003 C  CA  . PRO   C  1  103 ? -5.623  -7.970  32.306 1.00 61.22  ? 116 PRO   C CA  1 
ATOM   6004 C  C   . PRO   C  1  103 ? -5.689  -8.538  30.889 1.00 54.67  ? 116 PRO   C C   1 
ATOM   6005 O  O   . PRO   C  1  103 ? -4.902  -9.406  30.551 1.00 54.00  ? 116 PRO   C O   1 
ATOM   6006 C  CB  . PRO   C  1  103 ? -6.340  -8.883  33.327 1.00 64.81  ? 116 PRO   C CB  1 
ATOM   6007 C  CG  . PRO   C  1  103 ? -7.678  -8.187  33.605 1.00 63.41  ? 116 PRO   C CG  1 
ATOM   6008 C  CD  . PRO   C  1  103 ? -7.412  -6.697  33.412 1.00 58.11  ? 116 PRO   C CD  1 
ATOM   6009 N  N   . LYS   C  1  104 ? -6.622  -8.049  30.063 1.00 59.20  ? 117 LYS   C N   1 
ATOM   6010 C  CA  . LYS   C  1  104 ? -6.805  -8.547  28.706 1.00 58.18  ? 117 LYS   C CA  1 
ATOM   6011 C  C   . LYS   C  1  104 ? -5.584  -8.290  27.815 1.00 54.86  ? 117 LYS   C C   1 
ATOM   6012 O  O   . LYS   C  1  104 ? -5.467  -8.919  26.767 1.00 52.88  ? 117 LYS   C O   1 
ATOM   6013 C  CB  . LYS   C  1  104 ? -8.029  -7.893  28.058 1.00 63.85  ? 117 LYS   C CB  1 
ATOM   6014 C  CG  . LYS   C  1  104 ? -9.399  -8.209  28.633 1.00 65.20  ? 117 LYS   C CG  1 
ATOM   6015 C  CD  . LYS   C  1  104 ? -10.419 -7.152  28.215 1.00 72.45  ? 117 LYS   C CD  1 
ATOM   6016 C  CE  . LYS   C  1  104 ? -11.815 -7.354  28.744 1.00 78.18  ? 117 LYS   C CE  1 
ATOM   6017 N  NZ  . LYS   C  1  104 ? -12.407 -8.561  28.155 1.00 79.97  ? 117 LYS   C NZ  1 
ATOM   6018 N  N   . THR   C  1  105 ? -4.673  -7.372  28.199 1.00 52.83  ? 118 THR   C N   1 
ATOM   6019 C  CA  . THR   C  1  105 ? -3.464  -7.166  27.415 1.00 50.85  ? 118 THR   C CA  1 
ATOM   6020 C  C   . THR   C  1  105 ? -2.392  -8.163  27.832 1.00 49.68  ? 118 THR   C C   1 
ATOM   6021 O  O   . THR   C  1  105 ? -1.344  -8.217  27.206 1.00 50.56  ? 118 THR   C O   1 
ATOM   6022 C  CB  . THR   C  1  105 ? -2.938  -5.733  27.461 1.00 44.13  ? 118 THR   C CB  1 
ATOM   6023 O  OG1 . THR   C  1  105 ? -2.684  -5.361  28.805 1.00 43.45  ? 118 THR   C OG1 1 
ATOM   6024 C  CG2 . THR   C  1  105 ? -3.910  -4.735  26.857 1.00 41.99  ? 118 THR   C CG2 1 
ATOM   6025 N  N   . GLY   C  1  106 ? -2.660  -8.965  28.865 1.00 55.97  ? 119 GLY   C N   1 
ATOM   6026 C  CA  . GLY   C  1  106 ? -1.757  -10.031 29.283 1.00 57.61  ? 119 GLY   C CA  1 
ATOM   6027 C  C   . GLY   C  1  106 ? -0.844  -9.608  30.436 1.00 56.78  ? 119 GLY   C C   1 
ATOM   6028 O  O   . GLY   C  1  106 ? -1.014  -8.525  31.009 1.00 52.85  ? 119 GLY   C O   1 
ATOM   6029 N  N   . PRO   C  1  107 ? 0.146   -10.462 30.803 1.00 56.15  ? 120 PRO   C N   1 
ATOM   6030 C  CA  . PRO   C  1  107 ? 1.144   -10.145 31.838 1.00 61.99  ? 120 PRO   C CA  1 
ATOM   6031 C  C   . PRO   C  1  107 ? 1.861   -8.808  31.662 1.00 61.21  ? 120 PRO   C C   1 
ATOM   6032 O  O   . PRO   C  1  107 ? 2.457   -8.558  30.620 1.00 68.35  ? 120 PRO   C O   1 
ATOM   6033 C  CB  . PRO   C  1  107 ? 2.158   -11.305 31.749 1.00 61.51  ? 120 PRO   C CB  1 
ATOM   6034 C  CG  . PRO   C  1  107 ? 1.380   -12.442 31.136 1.00 63.72  ? 120 PRO   C CG  1 
ATOM   6035 C  CD  . PRO   C  1  107 ? 0.339   -11.802 30.231 1.00 61.53  ? 120 PRO   C CD  1 
ATOM   6036 N  N   . PRO   C  1  108 ? 1.861   -7.927  32.683 1.00 64.35  ? 121 PRO   C N   1 
ATOM   6037 C  CA  . PRO   C  1  108 ? 2.432   -6.591  32.529 1.00 64.21  ? 121 PRO   C CA  1 
ATOM   6038 C  C   . PRO   C  1  108 ? 3.910   -6.662  32.146 1.00 65.46  ? 121 PRO   C C   1 
ATOM   6039 O  O   . PRO   C  1  108 ? 4.612   -7.603  32.510 1.00 58.12  ? 121 PRO   C O   1 
ATOM   6040 C  CB  . PRO   C  1  108 ? 2.201   -5.876  33.878 1.00 61.96  ? 121 PRO   C CB  1 
ATOM   6041 C  CG  . PRO   C  1  108 ? 1.825   -6.987  34.847 1.00 66.51  ? 121 PRO   C CG  1 
ATOM   6042 C  CD  . PRO   C  1  108 ? 1.319   -8.169  34.027 1.00 67.20  ? 121 PRO   C CD  1 
ATOM   6043 N  N   . PRO   C  1  109 ? 4.415   -5.689  31.355 1.00 59.08  ? 122 PRO   C N   1 
ATOM   6044 C  CA  . PRO   C  1  109 ? 5.832   -5.636  31.022 1.00 56.27  ? 122 PRO   C CA  1 
ATOM   6045 C  C   . PRO   C  1  109 ? 6.663   -5.126  32.199 1.00 50.01  ? 122 PRO   C C   1 
ATOM   6046 O  O   . PRO   C  1  109 ? 6.120   -4.576  33.155 1.00 58.22  ? 122 PRO   C O   1 
ATOM   6047 C  CB  . PRO   C  1  109 ? 5.832   -4.673  29.827 1.00 51.62  ? 122 PRO   C CB  1 
ATOM   6048 C  CG  . PRO   C  1  109 ? 4.717   -3.715  30.133 1.00 53.11  ? 122 PRO   C CG  1 
ATOM   6049 C  CD  . PRO   C  1  109 ? 3.654   -4.589  30.758 1.00 53.28  ? 122 PRO   C CD  1 
ATOM   6050 N  N   . PRO   C  1  110 ? 8.001   -5.287  32.153 1.00 50.48  ? 123 PRO   C N   1 
ATOM   6051 C  CA  . PRO   C  1  110 ? 8.899   -4.757  33.188 1.00 53.46  ? 123 PRO   C CA  1 
ATOM   6052 C  C   . PRO   C  1  110 ? 8.858   -3.240  33.296 1.00 49.26  ? 123 PRO   C C   1 
ATOM   6053 O  O   . PRO   C  1  110 ? 8.960   -2.554  32.289 1.00 45.36  ? 123 PRO   C O   1 
ATOM   6054 C  CB  . PRO   C  1  110 ? 10.301  -5.255  32.772 1.00 52.27  ? 123 PRO   C CB  1 
ATOM   6055 C  CG  . PRO   C  1  110 ? 10.156  -5.584  31.294 1.00 55.28  ? 123 PRO   C CG  1 
ATOM   6056 C  CD  . PRO   C  1  110 ? 8.719   -6.032  31.109 1.00 52.03  ? 123 PRO   C CD  1 
ATOM   6057 N  N   . PRO   C  1  111 ? 8.671   -2.667  34.508 1.00 53.35  ? 124 PRO   C N   1 
ATOM   6058 C  CA  . PRO   C  1  111 ? 8.642   -1.209  34.656 1.00 48.84  ? 124 PRO   C CA  1 
ATOM   6059 C  C   . PRO   C  1  111 ? 9.970   -0.651  34.150 1.00 45.00  ? 124 PRO   C C   1 
ATOM   6060 O  O   . PRO   C  1  111 ? 10.958  -1.377  34.094 1.00 37.87  ? 124 PRO   C O   1 
ATOM   6061 C  CB  . PRO   C  1  111 ? 8.392   -0.954  36.152 1.00 54.29  ? 124 PRO   C CB  1 
ATOM   6062 C  CG  . PRO   C  1  111 ? 8.628   -2.304  36.820 1.00 59.32  ? 124 PRO   C CG  1 
ATOM   6063 C  CD  . PRO   C  1  111 ? 8.385   -3.376  35.765 1.00 54.79  ? 124 PRO   C CD  1 
ATOM   6064 N  N   . PRO   C  1  112 ? 10.054  0.628   33.727 1.00 38.57  ? 125 PRO   C N   1 
ATOM   6065 C  CA  . PRO   C  1  112 ? 8.943   1.588   33.763 1.00 40.48  ? 125 PRO   C CA  1 
ATOM   6066 C  C   . PRO   C  1  112 ? 7.870   1.516   32.672 1.00 42.38  ? 125 PRO   C C   1 
ATOM   6067 O  O   . PRO   C  1  112 ? 6.941   2.331   32.653 1.00 42.11  ? 125 PRO   C O   1 
ATOM   6068 C  CB  . PRO   C  1  112 ? 9.630   2.953   33.733 1.00 41.78  ? 125 PRO   C CB  1 
ATOM   6069 C  CG  . PRO   C  1  112 ? 11.014  2.696   33.195 1.00 43.34  ? 125 PRO   C CG  1 
ATOM   6070 C  CD  . PRO   C  1  112 ? 11.292  1.206   33.224 1.00 40.27  ? 125 PRO   C CD  1 
ATOM   6071 N  N   . ALA   C  1  113 ? 7.964   0.512   31.797 1.00 40.59  ? 126 ALA   C N   1 
ATOM   6072 C  CA  . ALA   C  1  113 ? 6.902   0.236   30.839 1.00 44.22  ? 126 ALA   C CA  1 
ATOM   6073 C  C   . ALA   C  1  113 ? 5.662   -0.286  31.570 1.00 46.45  ? 126 ALA   C C   1 
ATOM   6074 O  O   . ALA   C  1  113 ? 5.785   -0.902  32.623 1.00 50.33  ? 126 ALA   C O   1 
ATOM   6075 C  CB  . ALA   C  1  113 ? 7.406   -0.752  29.822 1.00 42.09  ? 126 ALA   C CB  1 
ATOM   6076 N  N   . HIS   C  1  114 ? 4.474   -0.067  30.992 1.00 43.53  ? 127 HIS   C N   1 
ATOM   6077 C  CA  . HIS   C  1  114 ? 3.227   -0.214  31.736 1.00 41.56  ? 127 HIS   C CA  1 
ATOM   6078 C  C   . HIS   C  1  114 ? 2.131   -0.926  30.934 1.00 42.40  ? 127 HIS   C C   1 
ATOM   6079 O  O   . HIS   C  1  114 ? 1.296   -1.610  31.516 1.00 47.34  ? 127 HIS   C O   1 
ATOM   6080 C  CB  . HIS   C  1  114 ? 2.756   1.162   32.231 1.00 41.78  ? 127 HIS   C CB  1 
ATOM   6081 C  CG  . HIS   C  1  114 ? 2.820   2.227   31.188 1.00 44.22  ? 127 HIS   C CG  1 
ATOM   6082 N  ND1 . HIS   C  1  114 ? 1.901   2.297   30.160 1.00 42.05  ? 127 HIS   C ND1 1 
ATOM   6083 C  CD2 . HIS   C  1  114 ? 3.697   3.238   30.983 1.00 40.43  ? 127 HIS   C CD2 1 
ATOM   6084 C  CE1 . HIS   C  1  114 ? 2.206   3.328   29.383 1.00 38.43  ? 127 HIS   C CE1 1 
ATOM   6085 N  NE2 . HIS   C  1  114 ? 3.295   3.909   29.849 1.00 39.07  ? 127 HIS   C NE2 1 
ATOM   6086 N  N   . ALA   C  1  115 ? 2.124   -0.768  29.602 1.00 42.75  ? 128 ALA   C N   1 
ATOM   6087 C  CA  . ALA   C  1  115 ? 1.053   -1.263  28.748 1.00 38.67  ? 128 ALA   C CA  1 
ATOM   6088 C  C   . ALA   C  1  115 ? -0.308  -0.831  29.290 1.00 34.96  ? 128 ALA   C C   1 
ATOM   6089 O  O   . ALA   C  1  115 ? -1.242  -1.616  29.323 1.00 33.93  ? 128 ALA   C O   1 
ATOM   6090 C  CB  . ALA   C  1  115 ? 1.131   -2.769  28.592 1.00 37.95  ? 128 ALA   C CB  1 
ATOM   6091 N  N   . GLY   C  1  116 ? -0.421  0.446   29.653 1.00 36.00  ? 129 GLY   C N   1 
ATOM   6092 C  CA  . GLY   C  1  116 ? -1.562  0.934   30.403 1.00 38.44  ? 129 GLY   C CA  1 
ATOM   6093 C  C   . GLY   C  1  116 ? -2.650  1.520   29.511 1.00 42.16  ? 129 GLY   C C   1 
ATOM   6094 O  O   . GLY   C  1  116 ? -3.655  2.024   30.022 1.00 42.23  ? 129 GLY   C O   1 
ATOM   6095 N  N   . GLY   C  1  117 ? -2.415  1.499   28.188 1.00 37.00  ? 130 GLY   C N   1 
ATOM   6096 C  CA  . GLY   C  1  117 ? -3.421  1.854   27.206 1.00 31.60  ? 130 GLY   C CA  1 
ATOM   6097 C  C   . GLY   C  1  117 ? -3.363  3.331   26.850 1.00 29.43  ? 130 GLY   C C   1 
ATOM   6098 O  O   . GLY   C  1  117 ? -2.568  4.073   27.416 1.00 28.78  ? 130 GLY   C O   1 
ATOM   6099 N  N   . LEU   C  1  118 ? -4.243  3.744   25.928 1.00 31.40  ? 131 LEU   C N   1 
ATOM   6100 C  CA  . LEU   C  1  118 ? -4.253  5.099   25.407 1.00 33.66  ? 131 LEU   C CA  1 
ATOM   6101 C  C   . LEU   C  1  118 ? -4.624  6.125   26.469 1.00 36.78  ? 131 LEU   C C   1 
ATOM   6102 O  O   . LEU   C  1  118 ? -4.452  7.315   26.223 1.00 33.93  ? 131 LEU   C O   1 
ATOM   6103 C  CB  . LEU   C  1  118 ? -5.218  5.204   24.226 1.00 35.20  ? 131 LEU   C CB  1 
ATOM   6104 C  CG  . LEU   C  1  118 ? -4.870  4.371   22.994 1.00 37.55  ? 131 LEU   C CG  1 
ATOM   6105 C  CD1 . LEU   C  1  118 ? -5.894  4.574   21.908 1.00 37.83  ? 131 LEU   C CD1 1 
ATOM   6106 C  CD2 . LEU   C  1  118 ? -3.479  4.769   22.510 1.00 35.63  ? 131 LEU   C CD2 1 
ATOM   6107 N  N   . ASN   C  1  119 ? -5.198  5.685   27.602 1.00 41.17  ? 132 ASN   C N   1 
ATOM   6108 C  CA  . ASN   C  1  119 ? -5.531  6.596   28.689 1.00 46.21  ? 132 ASN   C CA  1 
ATOM   6109 C  C   . ASN   C  1  119 ? -4.290  7.213   29.328 1.00 43.80  ? 132 ASN   C C   1 
ATOM   6110 O  O   . ASN   C  1  119 ? -4.381  8.307   29.851 1.00 40.91  ? 132 ASN   C O   1 
ATOM   6111 C  CB  . ASN   C  1  119 ? -6.307  5.924   29.810 1.00 51.67  ? 132 ASN   C CB  1 
ATOM   6112 C  CG  . ASN   C  1  119 ? -7.758  5.718   29.446 1.00 60.08  ? 132 ASN   C CG  1 
ATOM   6113 O  OD1 . ASN   C  1  119 ? -8.190  6.079   28.341 1.00 53.96  ? 132 ASN   C OD1 1 
ATOM   6114 N  ND2 . ASN   C  1  119 ? -8.525  5.138   30.358 1.00 59.98  ? 132 ASN   C ND2 1 
ATOM   6115 N  N   . VAL   C  1  120 ? -3.142  6.533   29.269 1.00 44.75  ? 133 VAL   C N   1 
ATOM   6116 C  CA  . VAL   C  1  120 ? -1.938  7.002   29.950 1.00 42.22  ? 133 VAL   C CA  1 
ATOM   6117 C  C   . VAL   C  1  120 ? -1.533  8.387   29.438 1.00 39.95  ? 133 VAL   C C   1 
ATOM   6118 O  O   . VAL   C  1  120 ? -1.298  8.579   28.248 1.00 43.20  ? 133 VAL   C O   1 
ATOM   6119 C  CB  . VAL   C  1  120 ? -0.767  6.015   29.790 1.00 40.62  ? 133 VAL   C CB  1 
ATOM   6120 C  CG1 . VAL   C  1  120 ? 0.548   6.595   30.307 1.00 41.78  ? 133 VAL   C CG1 1 
ATOM   6121 C  CG2 . VAL   C  1  120 ? -1.066  4.685   30.446 1.00 38.00  ? 133 VAL   C CG2 1 
ATOM   6122 N  N   . HIS   C  1  121 ? -1.360  9.316   30.383 1.00 38.88  ? 134 HIS   C N   1 
ATOM   6123 C  CA  . HIS   C  1  121 ? -1.135  10.725  30.101 1.00 40.40  ? 134 HIS   C CA  1 
ATOM   6124 C  C   . HIS   C  1  121 ? 0.345   11.042  29.910 1.00 43.08  ? 134 HIS   C C   1 
ATOM   6125 O  O   . HIS   C  1  121 ? 1.183   10.444  30.564 1.00 41.08  ? 134 HIS   C O   1 
ATOM   6126 C  CB  . HIS   C  1  121 ? -1.646  11.550  31.288 1.00 40.31  ? 134 HIS   C CB  1 
ATOM   6127 C  CG  . HIS   C  1  121 ? -1.366  13.009  31.178 1.00 45.14  ? 134 HIS   C CG  1 
ATOM   6128 N  ND1 . HIS   C  1  121 ? -1.964  13.807  30.219 1.00 55.00  ? 134 HIS   C ND1 1 
ATOM   6129 C  CD2 . HIS   C  1  121 ? -0.530  13.802  31.858 1.00 45.68  ? 134 HIS   C CD2 1 
ATOM   6130 C  CE1 . HIS   C  1  121 ? -1.519  15.047  30.341 1.00 51.23  ? 134 HIS   C CE1 1 
ATOM   6131 N  NE2 . HIS   C  1  121 ? -0.640  15.070  31.320 1.00 53.53  ? 134 HIS   C NE2 1 
ATOM   6132 N  N   . GLY   C  1  122 ? 0.664   11.998  29.028 1.00 45.73  ? 135 GLY   C N   1 
ATOM   6133 C  CA  . GLY   C  1  122 ? 1.900   12.746  29.174 1.00 45.75  ? 135 GLY   C CA  1 
ATOM   6134 C  C   . GLY   C  1  122 ? 2.897   12.588  28.030 1.00 50.46  ? 135 GLY   C C   1 
ATOM   6135 O  O   . GLY   C  1  122 ? 3.750   13.452  27.868 1.00 46.06  ? 135 GLY   C O   1 
ATOM   6136 N  N   . THR   C  1  123 ? 2.845   11.497  27.263 1.00 52.40  ? 136 THR   C N   1 
ATOM   6137 C  CA  A THR   C  1  123 ? 3.727   11.324  26.116 0.50 55.32  ? 136 THR   C CA  1 
ATOM   6138 C  CA  B THR   C  1  123 ? 3.721   11.410  26.103 0.50 52.73  ? 136 THR   C CA  1 
ATOM   6139 C  C   . THR   C  1  123 ? 2.900   11.238  24.827 1.00 50.29  ? 136 THR   C C   1 
ATOM   6140 O  O   . THR   C  1  123 ? 3.306   11.752  23.797 1.00 46.73  ? 136 THR   C O   1 
ATOM   6141 C  CB  A THR   C  1  123 ? 4.600   10.082  26.327 0.50 63.57  ? 136 THR   C CB  1 
ATOM   6142 C  CB  B THR   C  1  123 ? 4.799   10.335  26.268 0.50 58.65  ? 136 THR   C CB  1 
ATOM   6143 O  OG1 A THR   C  1  123 ? 3.689   8.998   26.497 0.50 76.60  ? 136 THR   C OG1 1 
ATOM   6144 O  OG1 B THR   C  1  123 ? 5.542   10.317  25.050 0.50 49.77  ? 136 THR   C OG1 1 
ATOM   6145 C  CG2 A THR   C  1  123 ? 5.507   10.177  27.545 0.50 58.21  ? 136 THR   C CG2 1 
ATOM   6146 C  CG2 B THR   C  1  123 ? 4.237   8.947   26.509 0.50 64.98  ? 136 THR   C CG2 1 
ATOM   6147 N  N   . PHE   C  1  124 ? 1.760   10.530  24.873 1.00 46.31  ? 137 PHE   C N   1 
ATOM   6148 C  CA  . PHE   C  1  124 ? 0.820   10.523  23.756 1.00 46.35  ? 137 PHE   C CA  1 
ATOM   6149 C  C   . PHE   C  1  124 ? -0.405  11.381  24.103 1.00 45.28  ? 137 PHE   C C   1 
ATOM   6150 O  O   . PHE   C  1  124 ? -0.484  12.518  23.658 1.00 43.16  ? 137 PHE   C O   1 
ATOM   6151 C  CB  . PHE   C  1  124 ? 0.428   9.106   23.327 1.00 45.91  ? 137 PHE   C CB  1 
ATOM   6152 C  CG  . PHE   C  1  124 ? -0.298  8.984   21.990 1.00 46.79  ? 137 PHE   C CG  1 
ATOM   6153 C  CD1 . PHE   C  1  124 ? -0.756  10.091  21.280 1.00 47.27  ? 137 PHE   C CD1 1 
ATOM   6154 C  CD2 . PHE   C  1  124 ? -0.531  7.731   21.442 1.00 47.12  ? 137 PHE   C CD2 1 
ATOM   6155 C  CE1 . PHE   C  1  124 ? -1.403  9.942   20.062 1.00 48.04  ? 137 PHE   C CE1 1 
ATOM   6156 C  CE2 . PHE   C  1  124 ? -1.180  7.586   20.228 1.00 45.51  ? 137 PHE   C CE2 1 
ATOM   6157 C  CZ  . PHE   C  1  124 ? -1.608  8.692   19.533 1.00 47.22  ? 137 PHE   C CZ  1 
ATOM   6158 N  N   . GLU   C  1  125 ? -1.378  10.818  24.843 1.00 49.48  ? 138 GLU   C N   1 
ATOM   6159 C  CA  . GLU   C  1  125 ? -2.560  11.552  25.283 1.00 46.33  ? 138 GLU   C CA  1 
ATOM   6160 C  C   . GLU   C  1  125 ? -2.124  12.822  26.009 1.00 42.49  ? 138 GLU   C C   1 
ATOM   6161 O  O   . GLU   C  1  125 ? -1.151  12.813  26.752 1.00 52.49  ? 138 GLU   C O   1 
ATOM   6162 C  CB  . GLU   C  1  125 ? -3.439  10.678  26.180 1.00 44.36  ? 138 GLU   C CB  1 
ATOM   6163 C  CG  . GLU   C  1  125 ? -4.770  11.301  26.603 1.00 47.85  ? 138 GLU   C CG  1 
ATOM   6164 C  CD  . GLU   C  1  125 ? -4.735  12.440  27.617 1.00 48.34  ? 138 GLU   C CD  1 
ATOM   6165 O  OE1 . GLU   C  1  125 ? -3.998  12.312  28.626 1.00 52.61  ? 138 GLU   C OE1 1 
ATOM   6166 O  OE2 . GLU   C  1  125 ? -5.451  13.453  27.397 1.00 44.25  ? 138 GLU   C OE2 1 
ATOM   6167 N  N   . GLY   C  1  126 ? -2.835  13.922  25.771 1.00 40.63  ? 139 GLY   C N   1 
ATOM   6168 C  CA  . GLY   C  1  126 ? -2.530  15.187  26.411 1.00 41.34  ? 139 GLY   C CA  1 
ATOM   6169 C  C   . GLY   C  1  126 ? -3.704  16.167  26.374 1.00 41.74  ? 139 GLY   C C   1 
ATOM   6170 O  O   . GLY   C  1  126 ? -4.870  15.783  26.206 1.00 43.43  ? 139 GLY   C O   1 
ATOM   6171 N  N   . ASP   C  1  127 ? -3.355  17.455  26.500 1.00 47.75  ? 140 ASP   C N   1 
ATOM   6172 C  CA  . ASP   C  1  127 ? -4.268  18.457  27.038 1.00 54.30  ? 140 ASP   C CA  1 
ATOM   6173 C  C   . ASP   C  1  127 ? -4.943  19.246  25.922 1.00 56.83  ? 140 ASP   C C   1 
ATOM   6174 O  O   . ASP   C  1  127 ? -4.501  19.242  24.773 1.00 56.79  ? 140 ASP   C O   1 
ATOM   6175 C  CB  . ASP   C  1  127 ? -3.535  19.398  27.980 1.00 52.85  ? 140 ASP   C CB  1 
ATOM   6176 C  CG  . ASP   C  1  127 ? -2.850  18.740  29.173 1.00 55.83  ? 140 ASP   C CG  1 
ATOM   6177 O  OD1 . ASP   C  1  127 ? -3.453  17.778  29.735 1.00 51.51  ? 140 ASP   C OD1 1 
ATOM   6178 O  OD2 . ASP   C  1  127 ? -1.719  19.197  29.536 1.00 55.99  ? 140 ASP   C OD2 1 
ATOM   6179 N  N   . ALA   C  1  128 ? -6.014  19.950  26.291 1.00 54.96  ? 141 ALA   C N   1 
ATOM   6180 C  CA  . ALA   C  1  128 ? -6.701  20.863  25.389 1.00 53.21  ? 141 ALA   C CA  1 
ATOM   6181 C  C   . ALA   C  1  128 ? -7.467  20.088  24.320 1.00 48.75  ? 141 ALA   C C   1 
ATOM   6182 O  O   . ALA   C  1  128 ? -7.583  20.534  23.190 1.00 54.20  ? 141 ALA   C O   1 
ATOM   6183 C  CB  . ALA   C  1  128 ? -5.729  21.854  24.788 1.00 48.56  ? 141 ALA   C CB  1 
ATOM   6184 N  N   . GLY   C  1  129 ? -8.046  18.955  24.698 1.00 50.22  ? 142 GLY   C N   1 
ATOM   6185 C  CA  . GLY   C  1  129 ? -8.936  18.234  23.804 1.00 58.20  ? 142 GLY   C CA  1 
ATOM   6186 C  C   . GLY   C  1  129 ? -10.270 18.961  23.635 1.00 63.15  ? 142 GLY   C C   1 
ATOM   6187 O  O   . GLY   C  1  129 ? -10.564 19.906  24.363 1.00 63.48  ? 142 GLY   C O   1 
ATOM   6188 N  N   . MET   C  1  130 ? -11.074 18.485  22.676 1.00 64.42  ? 143 MET   C N   1 
ATOM   6189 C  CA  . MET   C  1  130 ? -12.340 19.105  22.312 1.00 58.22  ? 143 MET   C CA  1 
ATOM   6190 C  C   . MET   C  1  130 ? -13.478 18.652  23.225 1.00 54.20  ? 143 MET   C C   1 
ATOM   6191 O  O   . MET   C  1  130 ? -14.297 19.472  23.635 1.00 60.39  ? 143 MET   C O   1 
ATOM   6192 C  CB  . MET   C  1  130 ? -12.710 18.754  20.867 1.00 67.19  ? 143 MET   C CB  1 
ATOM   6193 C  CG  . MET   C  1  130 ? -11.849 19.463  19.826 1.00 71.17  ? 143 MET   C CG  1 
ATOM   6194 S  SD  . MET   C  1  130 ? -12.174 18.925  18.137 1.00 74.02  ? 143 MET   C SD  1 
ATOM   6195 C  CE  . MET   C  1  130 ? -11.671 17.199  18.170 1.00 63.92  ? 143 MET   C CE  1 
ATOM   6196 N  N   . THR   C  1  131 ? -13.555 17.346  23.505 1.00 46.79  ? 144 THR   C N   1 
ATOM   6197 C  CA  . THR   C  1  131 ? -14.642 16.789  24.288 1.00 51.41  ? 144 THR   C CA  1 
ATOM   6198 C  C   . THR   C  1  131 ? -14.141 16.043  25.526 1.00 49.98  ? 144 THR   C C   1 
ATOM   6199 O  O   . THR   C  1  131 ? -14.966 15.457  26.240 1.00 51.35  ? 144 THR   C O   1 
ATOM   6200 C  CB  . THR   C  1  131 ? -15.481 15.864  23.408 1.00 51.64  ? 144 THR   C CB  1 
ATOM   6201 O  OG1 . THR   C  1  131 ? -14.744 14.670  23.139 1.00 48.44  ? 144 THR   C OG1 1 
ATOM   6202 C  CG2 . THR   C  1  131 ? -15.925 16.573  22.142 1.00 53.73  ? 144 THR   C CG2 1 
ATOM   6203 N  N   . ARG   C  1  132 ? -12.820 16.052  25.762 1.00 44.95  ? 145 ARG   C N   1 
ATOM   6204 C  CA  . ARG   C  1  132 ? -12.263 15.426  26.957 1.00 50.67  ? 145 ARG   C CA  1 
ATOM   6205 C  C   . ARG   C  1  132 ? -11.507 16.481  27.765 1.00 50.89  ? 145 ARG   C C   1 
ATOM   6206 O  O   . ARG   C  1  132 ? -10.855 17.332  27.171 1.00 44.06  ? 145 ARG   C O   1 
ATOM   6207 C  CB  . ARG   C  1  132 ? -11.342 14.254  26.610 1.00 45.79  ? 145 ARG   C CB  1 
ATOM   6208 C  CG  . ARG   C  1  132 ? -12.031 12.904  26.477 1.00 48.78  ? 145 ARG   C CG  1 
ATOM   6209 C  CD  . ARG   C  1  132 ? -12.871 12.748  25.222 1.00 47.22  ? 145 ARG   C CD  1 
ATOM   6210 N  NE  . ARG   C  1  132 ? -13.526 11.437  25.283 1.00 50.69  ? 145 ARG   C NE  1 
ATOM   6211 C  CZ  . ARG   C  1  132 ? -14.629 11.098  24.644 1.00 49.58  ? 145 ARG   C CZ  1 
ATOM   6212 N  NH1 . ARG   C  1  132 ? -15.189 11.955  23.810 1.00 49.05  ? 145 ARG   C NH1 1 
ATOM   6213 N  NH2 . ARG   C  1  132 ? -15.155 9.904   24.849 1.00 49.52  ? 145 ARG   C NH2 1 
ATOM   6214 N  N   . ALA   C  1  133 ? -11.610 16.408  29.105 1.00 50.88  ? 146 ALA   C N   1 
ATOM   6215 C  CA  . ALA   C  1  133 ? -10.962 17.361  29.993 1.00 53.71  ? 146 ALA   C CA  1 
ATOM   6216 C  C   . ALA   C  1  133 ? -9.512  16.937  30.217 1.00 55.07  ? 146 ALA   C C   1 
ATOM   6217 O  O   . ALA   C  1  133 ? -9.203  15.746  30.160 1.00 50.53  ? 146 ALA   C O   1 
ATOM   6218 N  N   . ASP   C  1  134 ? -8.636  17.925  30.484 1.00 54.78  ? 147 ASP   C N   1 
ATOM   6219 C  CA  . ASP   C  1  134 ? -7.246  17.666  30.834 1.00 51.74  ? 147 ASP   C CA  1 
ATOM   6220 C  C   . ASP   C  1  134 ? -7.164  16.711  32.023 1.00 54.04  ? 147 ASP   C C   1 
ATOM   6221 O  O   . ASP   C  1  134 ? -8.022  16.736  32.907 1.00 56.38  ? 147 ASP   C O   1 
ATOM   6222 C  CB  . ASP   C  1  134 ? -6.480  18.937  31.146 1.00 46.82  ? 147 ASP   C CB  1 
ATOM   6223 C  CG  . ASP   C  1  134 ? -6.380  19.932  30.005 1.00 52.31  ? 147 ASP   C CG  1 
ATOM   6224 O  OD1 . ASP   C  1  134 ? -7.014  19.679  28.957 1.00 49.07  ? 147 ASP   C OD1 1 
ATOM   6225 O  OD2 . ASP   C  1  134 ? -5.654  20.946  30.172 1.00 50.47  ? 147 ASP   C OD2 1 
ATOM   6226 N  N   . GLU   C  1  135 ? -6.101  15.893  32.020 1.00 51.14  ? 148 GLU   C N   1 
ATOM   6227 C  CA  . GLU   C  1  135 ? -5.863  14.858  33.013 1.00 53.82  ? 148 GLU   C CA  1 
ATOM   6228 C  C   . GLU   C  1  135 ? -5.765  15.450  34.422 1.00 55.72  ? 148 GLU   C C   1 
ATOM   6229 O  O   . GLU   C  1  135 ? -6.144  14.807  35.399 1.00 54.80  ? 148 GLU   C O   1 
ATOM   6230 C  CB  . GLU   C  1  135 ? -4.572  14.108  32.663 1.00 52.22  ? 148 GLU   C CB  1 
ATOM   6231 C  CG  . GLU   C  1  135 ? -4.306  12.905  33.568 1.00 59.10  ? 148 GLU   C CG  1 
ATOM   6232 C  CD  . GLU   C  1  135 ? -3.441  13.143  34.793 1.00 68.48  ? 148 GLU   C CD  1 
ATOM   6233 O  OE1 . GLU   C  1  135 ? -2.824  14.234  34.923 1.00 70.82  ? 148 GLU   C OE1 1 
ATOM   6234 O  OE2 . GLU   C  1  135 ? -3.391  12.192  35.612 1.00 78.04  ? 148 GLU   C OE2 1 
ATOM   6235 N  N   . PHE   C  1  136 ? -5.220  16.662  34.524 1.00 54.81  ? 149 PHE   C N   1 
ATOM   6236 C  CA  . PHE   C  1  136 ? -5.076  17.324  35.806 1.00 66.36  ? 149 PHE   C CA  1 
ATOM   6237 C  C   . PHE   C  1  136 ? -6.405  17.383  36.558 1.00 64.11  ? 149 PHE   C C   1 
ATOM   6238 O  O   . PHE   C  1  136 ? -6.407  17.304  37.776 1.00 63.84  ? 149 PHE   C O   1 
ATOM   6239 C  CB  . PHE   C  1  136 ? -4.525  18.734  35.603 1.00 76.75  ? 149 PHE   C CB  1 
ATOM   6240 C  CG  . PHE   C  1  136 ? -4.418  19.504  36.910 1.00 85.49  ? 149 PHE   C CG  1 
ATOM   6241 C  CD1 . PHE   C  1  136 ? -3.424  19.212  37.843 1.00 88.77  ? 149 PHE   C CD1 1 
ATOM   6242 C  CD2 . PHE   C  1  136 ? -5.331  20.502  37.212 1.00 90.84  ? 149 PHE   C CD2 1 
ATOM   6243 C  CE1 . PHE   C  1  136 ? -3.340  19.922  39.033 1.00 85.39  ? 149 PHE   C CE1 1 
ATOM   6244 C  CE2 . PHE   C  1  136 ? -5.243  21.211  38.401 1.00 87.54  ? 149 PHE   C CE2 1 
ATOM   6245 C  CZ  . PHE   C  1  136 ? -4.244  20.925  39.305 1.00 85.38  ? 149 PHE   C CZ  1 
ATOM   6246 N  N   . PHE   C  1  137 ? -7.527  17.514  35.843 1.00 59.83  ? 150 PHE   C N   1 
ATOM   6247 C  CA  . PHE   C  1  137 ? -8.822  17.678  36.485 1.00 55.20  ? 150 PHE   C CA  1 
ATOM   6248 C  C   . PHE   C  1  137 ? -9.448  16.331  36.858 1.00 57.37  ? 150 PHE   C C   1 
ATOM   6249 O  O   . PHE   C  1  137 ? -10.554 16.324  37.398 1.00 56.36  ? 150 PHE   C O   1 
ATOM   6250 C  CB  . PHE   C  1  137 ? -9.754  18.485  35.577 1.00 51.65  ? 150 PHE   C CB  1 
ATOM   6251 C  CG  . PHE   C  1  137 ? -9.191  19.823  35.122 1.00 57.56  ? 150 PHE   C CG  1 
ATOM   6252 C  CD1 . PHE   C  1  137 ? -8.660  20.730  36.028 1.00 62.51  ? 150 PHE   C CD1 1 
ATOM   6253 C  CD2 . PHE   C  1  137 ? -9.165  20.158  33.772 1.00 63.23  ? 150 PHE   C CD2 1 
ATOM   6254 C  CE1 . PHE   C  1  137 ? -8.114  21.928  35.592 1.00 63.77  ? 150 PHE   C CE1 1 
ATOM   6255 C  CE2 . PHE   C  1  137 ? -8.650  21.376  33.341 1.00 58.90  ? 150 PHE   C CE2 1 
ATOM   6256 C  CZ  . PHE   C  1  137 ? -8.109  22.252  34.252 1.00 63.78  ? 150 PHE   C CZ  1 
ATOM   6257 N  N   . GLY   C  1  138 ? -8.793  15.197  36.548 1.00 57.29  ? 151 GLY   C N   1 
ATOM   6258 C  CA  . GLY   C  1  138 ? -9.185  13.913  37.117 1.00 52.79  ? 151 GLY   C CA  1 
ATOM   6259 C  C   . GLY   C  1  138 ? -9.653  12.864  36.103 1.00 57.65  ? 151 GLY   C C   1 
ATOM   6260 O  O   . GLY   C  1  138 ? -9.708  11.681  36.434 1.00 64.25  ? 151 GLY   C O   1 
ATOM   6261 N  N   . ASP   C  1  139 ? -10.006 13.264  34.878 1.00 59.24  ? 152 ASP   C N   1 
ATOM   6262 C  CA  . ASP   C  1  139 ? -10.586 12.320  33.929 1.00 66.07  ? 152 ASP   C CA  1 
ATOM   6263 C  C   . ASP   C  1  139 ? -10.278 12.766  32.504 1.00 57.36  ? 152 ASP   C C   1 
ATOM   6264 O  O   . ASP   C  1  139 ? -10.870 13.722  32.018 1.00 51.30  ? 152 ASP   C O   1 
ATOM   6265 C  CB  . ASP   C  1  139 ? -12.075 12.114  34.162 1.00 70.12  ? 152 ASP   C CB  1 
ATOM   6266 C  CG  . ASP   C  1  139 ? -12.728 11.043  33.294 1.00 72.05  ? 152 ASP   C CG  1 
ATOM   6267 O  OD1 . ASP   C  1  139 ? -12.119 10.659  32.283 1.00 74.71  ? 152 ASP   C OD1 1 
ATOM   6268 O  OD2 . ASP   C  1  139 ? -13.838 10.584  33.649 1.00 69.74  ? 152 ASP   C OD2 1 
ATOM   6269 N  N   . ASN   C  1  140 ? -9.339  12.055  31.868 1.00 52.58  ? 153 ASN   C N   1 
ATOM   6270 C  CA  . ASN   C  1  140 ? -8.837  12.449  30.567 1.00 51.78  ? 153 ASN   C CA  1 
ATOM   6271 C  C   . ASN   C  1  140 ? -9.491  11.632  29.459 1.00 49.44  ? 153 ASN   C C   1 
ATOM   6272 O  O   . ASN   C  1  140 ? -9.120  11.811  28.305 1.00 59.06  ? 153 ASN   C O   1 
ATOM   6273 C  CB  . ASN   C  1  140 ? -7.319  12.314  30.475 1.00 47.11  ? 153 ASN   C CB  1 
ATOM   6274 C  CG  . ASN   C  1  140 ? -6.847  10.884  30.559 1.00 43.67  ? 153 ASN   C CG  1 
ATOM   6275 O  OD1 . ASN   C  1  140 ? -7.613  9.969   30.873 1.00 47.77  ? 153 ASN   C OD1 1 
ATOM   6276 N  ND2 . ASN   C  1  140 ? -5.569  10.666  30.305 1.00 50.20  ? 153 ASN   C ND2 1 
ATOM   6277 N  N   . HIS   C  1  141 ? -10.434 10.744  29.800 1.00 52.97  ? 154 HIS   C N   1 
ATOM   6278 C  CA  . HIS   C  1  141 ? -10.934 9.779   28.831 1.00 60.11  ? 154 HIS   C CA  1 
ATOM   6279 C  C   . HIS   C  1  141 ? -12.437 9.918   28.596 1.00 62.99  ? 154 HIS   C C   1 
ATOM   6280 O  O   . HIS   C  1  141 ? -12.896 9.636   27.495 1.00 64.71  ? 154 HIS   C O   1 
ATOM   6281 C  CB  . HIS   C  1  141 ? -10.522 8.356   29.216 1.00 66.05  ? 154 HIS   C CB  1 
ATOM   6282 C  CG  . HIS   C  1  141 ? -10.992 7.930   30.553 1.00 71.88  ? 154 HIS   C CG  1 
ATOM   6283 N  ND1 . HIS   C  1  141 ? -10.226 8.102   31.683 1.00 75.76  ? 154 HIS   C ND1 1 
ATOM   6284 C  CD2 . HIS   C  1  141 ? -12.124 7.337   30.948 1.00 76.79  ? 154 HIS   C CD2 1 
ATOM   6285 C  CE1 . HIS   C  1  141 ? -10.889 7.627   32.728 1.00 80.50  ? 154 HIS   C CE1 1 
ATOM   6286 N  NE2 . HIS   C  1  141 ? -12.051 7.180   32.308 1.00 74.62  ? 154 HIS   C NE2 1 
ATOM   6287 N  N   . SER   C  1  142 ? -13.196 10.337  29.619 1.00 60.72  ? 155 SER   C N   1 
ATOM   6288 C  CA  . SER   C  1  142 ? -14.644 10.398  29.520 1.00 60.23  ? 155 SER   C CA  1 
ATOM   6289 C  C   . SER   C  1  142 ? -15.080 11.591  28.684 1.00 58.33  ? 155 SER   C C   1 
ATOM   6290 O  O   . SER   C  1  142 ? -14.471 12.663  28.721 1.00 51.22  ? 155 SER   C O   1 
ATOM   6291 C  CB  . SER   C  1  142 ? -15.297 10.459  30.873 1.00 61.25  ? 155 SER   C CB  1 
ATOM   6292 O  OG  . SER   C  1  142 ? -15.229 9.186   31.508 1.00 65.27  ? 155 SER   C OG  1 
ATOM   6293 N  N   . PHE   C  1  143 ? -16.200 11.400  27.979 1.00 59.61  ? 156 PHE   C N   1 
ATOM   6294 C  CA  . PHE   C  1  143 ? -16.877 12.522  27.358 1.00 59.89  ? 156 PHE   C CA  1 
ATOM   6295 C  C   . PHE   C  1  143 ? -17.285 13.530  28.430 1.00 57.99  ? 156 PHE   C C   1 
ATOM   6296 O  O   . PHE   C  1  143 ? -17.765 13.155  29.496 1.00 54.16  ? 156 PHE   C O   1 
ATOM   6297 C  CB  . PHE   C  1  143 ? -18.085 11.990  26.597 1.00 63.18  ? 156 PHE   C CB  1 
ATOM   6298 C  CG  . PHE   C  1  143 ? -18.955 13.093  26.027 1.00 62.23  ? 156 PHE   C CG  1 
ATOM   6299 C  CD1 . PHE   C  1  143 ? -18.673 13.651  24.788 1.00 57.45  ? 156 PHE   C CD1 1 
ATOM   6300 C  CD2 . PHE   C  1  143 ? -20.065 13.550  26.737 1.00 65.14  ? 156 PHE   C CD2 1 
ATOM   6301 C  CE1 . PHE   C  1  143 ? -19.498 14.628  24.262 1.00 61.66  ? 156 PHE   C CE1 1 
ATOM   6302 C  CE2 . PHE   C  1  143 ? -20.881 14.533  26.207 1.00 66.30  ? 156 PHE   C CE2 1 
ATOM   6303 C  CZ  . PHE   C  1  143 ? -20.598 15.066  24.971 1.00 64.53  ? 156 PHE   C CZ  1 
ATOM   6304 N  N   . ASN   C  1  144 ? -17.123 14.812  28.113 1.00 57.85  ? 157 ASN   C N   1 
ATOM   6305 C  CA  . ASN   C  1  144 ? -17.365 15.897  29.043 1.00 62.59  ? 157 ASN   C CA  1 
ATOM   6306 C  C   . ASN   C  1  144 ? -18.402 16.823  28.415 1.00 64.95  ? 157 ASN   C C   1 
ATOM   6307 O  O   . ASN   C  1  144 ? -18.088 17.537  27.469 1.00 56.46  ? 157 ASN   C O   1 
ATOM   6308 C  CB  . ASN   C  1  144 ? -16.048 16.595  29.342 1.00 77.45  ? 157 ASN   C CB  1 
ATOM   6309 C  CG  . ASN   C  1  144 ? -16.143 17.862  30.165 1.00 87.17  ? 157 ASN   C CG  1 
ATOM   6310 O  OD1 . ASN   C  1  144 ? -17.021 18.700  29.955 1.00 80.29  ? 157 ASN   C OD1 1 
ATOM   6311 N  ND2 . ASN   C  1  144 ? -15.205 18.054  31.081 1.00 96.54  ? 157 ASN   C ND2 1 
ATOM   6312 N  N   . GLN   C  1  145 ? -19.616 16.842  28.984 1.00 73.74  ? 158 GLN   C N   1 
ATOM   6313 C  CA  . GLN   C  1  145 ? -20.753 17.547  28.402 1.00 73.39  ? 158 GLN   C CA  1 
ATOM   6314 C  C   . GLN   C  1  145 ? -20.480 19.052  28.339 1.00 62.96  ? 158 GLN   C C   1 
ATOM   6315 O  O   . GLN   C  1  145 ? -20.856 19.718  27.378 1.00 67.67  ? 158 GLN   C O   1 
ATOM   6316 C  CB  . GLN   C  1  145 ? -22.024 17.215  29.194 1.00 77.62  ? 158 GLN   C CB  1 
ATOM   6317 C  CG  . GLN   C  1  145 ? -23.317 17.813  28.634 1.00 73.42  ? 158 GLN   C CG  1 
ATOM   6318 C  CD  . GLN   C  1  145 ? -23.655 17.348  27.232 1.00 63.63  ? 158 GLN   C CD  1 
ATOM   6319 O  OE1 . GLN   C  1  145 ? -23.760 16.145  26.952 1.00 64.16  ? 158 GLN   C OE1 1 
ATOM   6320 N  NE2 . GLN   C  1  145 ? -23.832 18.301  26.324 1.00 58.64  ? 158 GLN   C NE2 1 
ATOM   6321 N  N   . THR   C  1  146 ? -19.823 19.591  29.368 1.00 62.83  ? 159 THR   C N   1 
ATOM   6322 C  CA  . THR   C  1  146 ? -19.516 21.014  29.415 1.00 62.47  ? 159 THR   C CA  1 
ATOM   6323 C  C   . THR   C  1  146 ? -18.640 21.401  28.226 1.00 63.97  ? 159 THR   C C   1 
ATOM   6324 O  O   . THR   C  1  146 ? -18.810 22.466  27.642 1.00 60.36  ? 159 THR   C O   1 
ATOM   6325 C  CB  . THR   C  1  146 ? -18.827 21.390  30.730 1.00 62.62  ? 159 THR   C CB  1 
ATOM   6326 O  OG1 . THR   C  1  146 ? -19.656 20.989  31.823 1.00 64.45  ? 159 THR   C OG1 1 
ATOM   6327 C  CG2 . THR   C  1  146 ? -18.530 22.880  30.808 1.00 59.87  ? 159 THR   C CG2 1 
ATOM   6328 N  N   . LEU   C  1  147 ? -17.663 20.552  27.898 1.00 72.38  ? 160 LEU   C N   1 
ATOM   6329 C  CA  . LEU   C  1  147 ? -16.783 20.818  26.771 1.00 71.84  ? 160 LEU   C CA  1 
ATOM   6330 C  C   . LEU   C  1  147 ? -17.532 20.665  25.446 1.00 66.96  ? 160 LEU   C C   1 
ATOM   6331 O  O   . LEU   C  1  147 ? -17.313 21.440  24.517 1.00 54.81  ? 160 LEU   C O   1 
ATOM   6332 C  CB  . LEU   C  1  147 ? -15.560 19.906  26.861 1.00 77.03  ? 160 LEU   C CB  1 
ATOM   6333 C  CG  . LEU   C  1  147 ? -14.521 20.301  27.915 1.00 72.00  ? 160 LEU   C CG  1 
ATOM   6334 C  CD1 . LEU   C  1  147 ? -13.335 19.349  27.896 1.00 68.54  ? 160 LEU   C CD1 1 
ATOM   6335 C  CD2 . LEU   C  1  147 ? -14.043 21.731  27.698 1.00 67.66  ? 160 LEU   C CD2 1 
ATOM   6336 N  N   . PHE   C  1  148 ? -18.433 19.683  25.359 1.00 63.74  ? 161 PHE   C N   1 
ATOM   6337 C  CA  . PHE   C  1  148 ? -19.247 19.523  24.167 1.00 65.40  ? 161 PHE   C CA  1 
ATOM   6338 C  C   . PHE   C  1  148 ? -20.166 20.732  24.003 1.00 66.44  ? 161 PHE   C C   1 
ATOM   6339 O  O   . PHE   C  1  148 ? -20.416 21.141  22.876 1.00 68.65  ? 161 PHE   C O   1 
ATOM   6340 C  CB  . PHE   C  1  148 ? -20.047 18.220  24.191 1.00 73.71  ? 161 PHE   C CB  1 
ATOM   6341 C  CG  . PHE   C  1  148 ? -20.794 17.977  22.888 1.00 80.41  ? 161 PHE   C CG  1 
ATOM   6342 C  CD1 . PHE   C  1  148 ? -20.103 17.625  21.732 1.00 86.44  ? 161 PHE   C CD1 1 
ATOM   6343 C  CD2 . PHE   C  1  148 ? -22.173 18.123  22.815 1.00 80.69  ? 161 PHE   C CD2 1 
ATOM   6344 C  CE1 . PHE   C  1  148 ? -20.770 17.428  20.535 1.00 85.31  ? 161 PHE   C CE1 1 
ATOM   6345 C  CE2 . PHE   C  1  148 ? -22.839 17.901  21.615 1.00 82.71  ? 161 PHE   C CE2 1 
ATOM   6346 C  CZ  . PHE   C  1  148 ? -22.136 17.554  20.477 1.00 82.98  ? 161 PHE   C CZ  1 
ATOM   6347 N  N   . ASP   C  1  149 ? -20.659 21.309  25.108 1.00 68.30  ? 162 ASP   C N   1 
ATOM   6348 C  CA  . ASP   C  1  149 ? -21.498 22.501  25.033 1.00 65.49  ? 162 ASP   C CA  1 
ATOM   6349 C  C   . ASP   C  1  149 ? -20.723 23.647  24.381 1.00 57.62  ? 162 ASP   C C   1 
ATOM   6350 O  O   . ASP   C  1  149 ? -21.281 24.428  23.614 1.00 60.24  ? 162 ASP   C O   1 
ATOM   6351 C  CB  . ASP   C  1  149 ? -22.054 22.887  26.398 1.00 70.13  ? 162 ASP   C CB  1 
ATOM   6352 C  CG  . ASP   C  1  149 ? -23.064 21.922  27.011 1.00 75.48  ? 162 ASP   C CG  1 
ATOM   6353 O  OD1 . ASP   C  1  149 ? -23.707 21.172  26.251 1.00 79.93  ? 162 ASP   C OD1 1 
ATOM   6354 O  OD2 . ASP   C  1  149 ? -23.191 21.896  28.256 1.00 82.49  ? 162 ASP   C OD2 1 
ATOM   6355 N  N   . LYS   C  1  150 ? -19.430 23.755  24.691 1.00 61.48  ? 163 LYS   C N   1 
ATOM   6356 C  CA  . LYS   C  1  150 ? -18.581 24.778  24.095 1.00 63.23  ? 163 LYS   C CA  1 
ATOM   6357 C  C   . LYS   C  1  150 ? -18.342 24.478  22.615 1.00 66.05  ? 163 LYS   C C   1 
ATOM   6358 O  O   . LYS   C  1  150 ? -18.275 25.393  21.802 1.00 62.71  ? 163 LYS   C O   1 
ATOM   6359 C  CB  . LYS   C  1  150 ? -17.260 24.847  24.862 1.00 63.89  ? 163 LYS   C CB  1 
ATOM   6360 C  CG  . LYS   C  1  150 ? -16.265 25.852  24.338 1.00 66.99  ? 163 LYS   C CG  1 
ATOM   6361 C  CD  . LYS   C  1  150 ? -14.996 25.897  25.196 1.00 68.75  ? 163 LYS   C CD  1 
ATOM   6362 C  CE  . LYS   C  1  150 ? -13.892 26.737  24.630 1.00 69.24  ? 163 LYS   C CE  1 
ATOM   6363 N  NZ  . LYS   C  1  150 ? -13.812 28.089  25.184 1.00 71.07  ? 163 LYS   C NZ  1 
ATOM   6364 N  N   . PHE   C  1  151 ? -18.218 23.193  22.268 1.00 64.25  ? 164 PHE   C N   1 
ATOM   6365 C  CA  . PHE   C  1  151 ? -18.113 22.780  20.879 1.00 72.71  ? 164 PHE   C CA  1 
ATOM   6366 C  C   . PHE   C  1  151 ? -19.343 23.255  20.110 1.00 72.01  ? 164 PHE   C C   1 
ATOM   6367 O  O   . PHE   C  1  151 ? -19.220 23.801  19.011 1.00 61.15  ? 164 PHE   C O   1 
ATOM   6368 C  CB  . PHE   C  1  151 ? -17.937 21.257  20.846 1.00 72.68  ? 164 PHE   C CB  1 
ATOM   6369 C  CG  . PHE   C  1  151 ? -17.833 20.638  19.462 1.00 72.47  ? 164 PHE   C CG  1 
ATOM   6370 C  CD1 . PHE   C  1  151 ? -16.632 20.641  18.762 1.00 69.04  ? 164 PHE   C CD1 1 
ATOM   6371 C  CD2 . PHE   C  1  151 ? -18.943 20.029  18.883 1.00 72.99  ? 164 PHE   C CD2 1 
ATOM   6372 C  CE1 . PHE   C  1  151 ? -16.549 20.066  17.510 1.00 69.54  ? 164 PHE   C CE1 1 
ATOM   6373 C  CE2 . PHE   C  1  151 ? -18.852 19.450  17.628 1.00 73.93  ? 164 PHE   C CE2 1 
ATOM   6374 C  CZ  . PHE   C  1  151 ? -17.655 19.466  16.947 1.00 75.02  ? 164 PHE   C CZ  1 
ATOM   6375 N  N   . VAL   C  1  152 ? -20.525 23.045  20.712 1.00 68.20  ? 165 VAL   C N   1 
ATOM   6376 C  CA  . VAL   C  1  152 ? -21.791 23.435  20.106 1.00 68.84  ? 165 VAL   C CA  1 
ATOM   6377 C  C   . VAL   C  1  152 ? -21.820 24.953  19.968 1.00 62.45  ? 165 VAL   C C   1 
ATOM   6378 O  O   . VAL   C  1  152 ? -22.172 25.490  18.916 1.00 59.79  ? 165 VAL   C O   1 
ATOM   6379 C  CB  . VAL   C  1  152 ? -23.001 22.924  20.918 1.00 76.98  ? 165 VAL   C CB  1 
ATOM   6380 C  CG1 . VAL   C  1  152 ? -24.316 23.528  20.456 1.00 77.69  ? 165 VAL   C CG1 1 
ATOM   6381 C  CG2 . VAL   C  1  152 ? -23.122 21.410  20.866 1.00 82.41  ? 165 VAL   C CG2 1 
ATOM   6382 N  N   . ASP   C  1  153 ? -21.436 25.634  21.046 1.00 68.27  ? 166 ASP   C N   1 
ATOM   6383 C  CA  . ASP   C  1  153 ? -21.468 27.084  21.067 1.00 80.02  ? 166 ASP   C CA  1 
ATOM   6384 C  C   . ASP   C  1  153 ? -20.613 27.650  19.937 1.00 65.28  ? 166 ASP   C C   1 
ATOM   6385 O  O   . ASP   C  1  153 ? -21.068 28.506  19.188 1.00 67.09  ? 166 ASP   C O   1 
ATOM   6386 C  CB  . ASP   C  1  153 ? -21.081 27.651  22.428 1.00 85.64  ? 166 ASP   C CB  1 
ATOM   6387 C  CG  . ASP   C  1  153 ? -21.309 29.155  22.555 1.00 88.19  ? 166 ASP   C CG  1 
ATOM   6388 O  OD1 . ASP   C  1  153 ? -22.419 29.611  22.200 1.00 94.15  ? 166 ASP   C OD1 1 
ATOM   6389 O  OD2 . ASP   C  1  153 ? -20.398 29.872  23.016 1.00 83.28  ? 166 ASP   C OD2 1 
ATOM   6390 N  N   . PHE   C  1  154 ? -19.374 27.177  19.819 1.00 68.02  ? 167 PHE   C N   1 
ATOM   6391 C  CA  . PHE   C  1  154 ? -18.465 27.695  18.806 1.00 71.66  ? 167 PHE   C CA  1 
ATOM   6392 C  C   . PHE   C  1  154 ? -18.967 27.336  17.408 1.00 68.81  ? 167 PHE   C C   1 
ATOM   6393 O  O   . PHE   C  1  154 ? -18.743 28.096  16.476 1.00 66.84  ? 167 PHE   C O   1 
ATOM   6394 C  CB  . PHE   C  1  154 ? -17.036 27.184  18.987 1.00 71.98  ? 167 PHE   C CB  1 
ATOM   6395 C  CG  . PHE   C  1  154 ? -16.193 28.045  19.907 1.00 72.15  ? 167 PHE   C CG  1 
ATOM   6396 C  CD1 . PHE   C  1  154 ? -16.521 28.165  21.250 1.00 75.13  ? 167 PHE   C CD1 1 
ATOM   6397 C  CD2 . PHE   C  1  154 ? -15.048 28.691  19.443 1.00 72.95  ? 167 PHE   C CD2 1 
ATOM   6398 C  CE1 . PHE   C  1  154 ? -15.754 28.955  22.102 1.00 77.76  ? 167 PHE   C CE1 1 
ATOM   6399 C  CE2 . PHE   C  1  154 ? -14.275 29.469  20.302 1.00 73.06  ? 167 PHE   C CE2 1 
ATOM   6400 C  CZ  . PHE   C  1  154 ? -14.635 29.607  21.626 1.00 74.60  ? 167 PHE   C CZ  1 
ATOM   6401 N  N   . SER   C  1  155 ? -19.629 26.185  17.246 1.00 69.02  ? 168 SER   C N   1 
ATOM   6402 C  CA  . SER   C  1  155 ? -20.209 25.843  15.954 1.00 75.68  ? 168 SER   C CA  1 
ATOM   6403 C  C   . SER   C  1  155 ? -21.338 26.820  15.608 1.00 81.72  ? 168 SER   C C   1 
ATOM   6404 O  O   . SER   C  1  155 ? -21.497 27.223  14.453 1.00 78.68  ? 168 SER   C O   1 
ATOM   6405 C  CB  . SER   C  1  155 ? -20.702 24.418  15.929 1.00 76.71  ? 168 SER   C CB  1 
ATOM   6406 O  OG  . SER   C  1  155 ? -19.653 23.502  16.211 1.00 72.04  ? 168 SER   C OG  1 
ATOM   6407 N  N   . ASN   C  1  156 ? -22.130 27.203  16.623 1.00 81.68  ? 169 ASN   C N   1 
ATOM   6408 C  CA  . ASN   C  1  156 ? -23.199 28.174  16.428 1.00 74.80  ? 169 ASN   C CA  1 
ATOM   6409 C  C   . ASN   C  1  156 ? -22.603 29.527  16.060 1.00 69.85  ? 169 ASN   C C   1 
ATOM   6410 O  O   . ASN   C  1  156 ? -23.113 30.209  15.188 1.00 70.23  ? 169 ASN   C O   1 
ATOM   6411 C  CB  . ASN   C  1  156 ? -24.113 28.276  17.643 1.00 68.46  ? 169 ASN   C CB  1 
ATOM   6412 C  CG  . ASN   C  1  156 ? -24.992 27.049  17.820 1.00 70.47  ? 169 ASN   C CG  1 
ATOM   6413 O  OD1 . ASN   C  1  156 ? -25.235 26.258  16.894 1.00 68.99  ? 169 ASN   C OD1 1 
ATOM   6414 N  ND2 . ASN   C  1  156 ? -25.507 26.868  19.021 1.00 64.70  ? 169 ASN   C ND2 1 
ATOM   6415 N  N   . ARG   C  1  157 ? -21.500 29.894  16.711 1.00 76.67  ? 170 ARG   C N   1 
ATOM   6416 C  CA  . ARG   C  1  157 ? -20.934 31.230  16.590 1.00 81.42  ? 170 ARG   C CA  1 
ATOM   6417 C  C   . ARG   C  1  157 ? -20.160 31.408  15.284 1.00 73.86  ? 170 ARG   C C   1 
ATOM   6418 O  O   . ARG   C  1  157 ? -20.130 32.510  14.759 1.00 64.85  ? 170 ARG   C O   1 
ATOM   6419 C  CB  . ARG   C  1  157 ? -20.007 31.533  17.772 1.00 87.07  ? 170 ARG   C CB  1 
ATOM   6420 C  CG  . ARG   C  1  157 ? -19.785 33.022  18.020 1.00 89.45  ? 170 ARG   C CG  1 
ATOM   6421 C  CD  . ARG   C  1  157 ? -18.690 33.328  19.023 1.00 86.09  ? 170 ARG   C CD  1 
ATOM   6422 N  NE  . ARG   C  1  157 ? -18.820 32.527  20.246 1.00 87.59  ? 170 ARG   C NE  1 
ATOM   6423 C  CZ  . ARG   C  1  157 ? -17.925 32.419  21.222 1.00 82.85  ? 170 ARG   C CZ  1 
ATOM   6424 N  NH1 . ARG   C  1  157 ? -16.767 33.064  21.145 1.00 77.53  ? 170 ARG   C NH1 1 
ATOM   6425 N  NH2 . ARG   C  1  157 ? -18.200 31.650  22.265 1.00 80.43  ? 170 ARG   C NH2 1 
ATOM   6426 N  N   . TYR   C  1  158 ? -19.515 30.350  14.770 1.00 78.65  ? 171 TYR   C N   1 
ATOM   6427 C  CA  . TYR   C  1  158 ? -18.619 30.507  13.632 1.00 73.91  ? 171 TYR   C CA  1 
ATOM   6428 C  C   . TYR   C  1  158 ? -18.987 29.627  12.436 1.00 72.01  ? 171 TYR   C C   1 
ATOM   6429 O  O   . TYR   C  1  158 ? -18.426 29.849  11.365 1.00 62.50  ? 171 TYR   C O   1 
ATOM   6430 C  CB  . TYR   C  1  158 ? -17.186 30.193  14.059 1.00 81.91  ? 171 TYR   C CB  1 
ATOM   6431 C  CG  . TYR   C  1  158 ? -16.680 31.119  15.151 1.00 84.65  ? 171 TYR   C CG  1 
ATOM   6432 C  CD1 . TYR   C  1  158 ? -16.326 32.421  14.845 1.00 86.66  ? 171 TYR   C CD1 1 
ATOM   6433 C  CD2 . TYR   C  1  158 ? -16.556 30.697  16.470 1.00 86.75  ? 171 TYR   C CD2 1 
ATOM   6434 C  CE1 . TYR   C  1  158 ? -15.846 33.288  15.815 1.00 89.40  ? 171 TYR   C CE1 1 
ATOM   6435 C  CE2 . TYR   C  1  158 ? -16.091 31.553  17.455 1.00 90.15  ? 171 TYR   C CE2 1 
ATOM   6436 C  CZ  . TYR   C  1  158 ? -15.740 32.856  17.126 1.00 92.52  ? 171 TYR   C CZ  1 
ATOM   6437 O  OH  . TYR   C  1  158 ? -15.267 33.726  18.063 1.00 96.60  ? 171 TYR   C OH  1 
ATOM   6438 N  N   . GLY   C  1  159 ? -19.913 28.663  12.597 1.00 66.72  ? 172 GLY   C N   1 
ATOM   6439 C  CA  . GLY   C  1  159 ? -20.148 27.681  11.548 1.00 67.47  ? 172 GLY   C CA  1 
ATOM   6440 C  C   . GLY   C  1  159 ? -21.623 27.488  11.192 1.00 67.76  ? 172 GLY   C C   1 
ATOM   6441 O  O   . GLY   C  1  159 ? -21.983 26.470  10.600 1.00 59.45  ? 172 GLY   C O   1 
ATOM   6442 N  N   . GLY   C  1  160 ? -22.472 28.467  11.532 1.00 70.70  ? 173 GLY   C N   1 
ATOM   6443 C  CA  . GLY   C  1  160 ? -23.890 28.406  11.208 1.00 59.87  ? 173 GLY   C CA  1 
ATOM   6444 C  C   . GLY   C  1  160 ? -24.589 27.223  11.875 1.00 63.66  ? 173 GLY   C C   1 
ATOM   6445 O  O   . GLY   C  1  160 ? -25.610 26.769  11.364 1.00 64.37  ? 173 GLY   C O   1 
ATOM   6446 N  N   . GLY   C  1  161 ? -24.021 26.724  12.990 1.00 59.25  ? 174 GLY   C N   1 
ATOM   6447 C  CA  . GLY   C  1  161 ? -24.578 25.600  13.732 1.00 61.88  ? 174 GLY   C CA  1 
ATOM   6448 C  C   . GLY   C  1  161 ? -23.940 24.263  13.356 1.00 63.20  ? 174 GLY   C C   1 
ATOM   6449 O  O   . GLY   C  1  161 ? -24.384 23.209  13.820 1.00 58.09  ? 174 GLY   C O   1 
ATOM   6450 N  N   . PHE   C  1  162 ? -22.923 24.335  12.491 1.00 69.96  ? 175 PHE   C N   1 
ATOM   6451 C  CA  . PHE   C  1  162 ? -22.175 23.178  12.034 1.00 77.23  ? 175 PHE   C CA  1 
ATOM   6452 C  C   . PHE   C  1  162 ? -20.705 23.360  12.405 1.00 77.85  ? 175 PHE   C C   1 
ATOM   6453 O  O   . PHE   C  1  162 ? -20.209 24.485  12.512 1.00 68.89  ? 175 PHE   C O   1 
ATOM   6454 C  CB  . PHE   C  1  162 ? -22.363 23.021  10.523 1.00 77.67  ? 175 PHE   C CB  1 
ATOM   6455 C  CG  . PHE   C  1  162 ? -23.797 22.728  10.105 1.00 77.80  ? 175 PHE   C CG  1 
ATOM   6456 C  CD1 . PHE   C  1  162 ? -24.254 21.412  10.030 1.00 83.00  ? 175 PHE   C CD1 1 
ATOM   6457 C  CD2 . PHE   C  1  162 ? -24.690 23.754  9.812  1.00 75.36  ? 175 PHE   C CD2 1 
ATOM   6458 C  CE1 . PHE   C  1  162 ? -25.558 21.123  9.644  1.00 82.07  ? 175 PHE   C CE1 1 
ATOM   6459 C  CE2 . PHE   C  1  162 ? -25.996 23.463  9.436  1.00 84.04  ? 175 PHE   C CE2 1 
ATOM   6460 C  CZ  . PHE   C  1  162 ? -26.430 22.147  9.355  1.00 83.32  ? 175 PHE   C CZ  1 
ATOM   6461 N  N   . TYR   C  1  163 ? -20.003 22.236  12.593 1.00 68.33  ? 176 TYR   C N   1 
ATOM   6462 C  CA  . TYR   C  1  163 ? -18.569 22.290  12.807 1.00 59.00  ? 176 TYR   C CA  1 
ATOM   6463 C  C   . TYR   C  1  163 ? -17.901 22.257  11.445 1.00 54.07  ? 176 TYR   C C   1 
ATOM   6464 O  O   . TYR   C  1  163 ? -18.133 21.333  10.666 1.00 63.54  ? 176 TYR   C O   1 
ATOM   6465 C  CB  . TYR   C  1  163 ? -18.088 21.129  13.673 1.00 62.77  ? 176 TYR   C CB  1 
ATOM   6466 C  CG  . TYR   C  1  163 ? -16.612 21.180  14.053 1.00 58.77  ? 176 TYR   C CG  1 
ATOM   6467 C  CD1 . TYR   C  1  163 ? -16.158 21.981  15.092 1.00 58.86  ? 176 TYR   C CD1 1 
ATOM   6468 C  CD2 . TYR   C  1  163 ? -15.681 20.382  13.400 1.00 61.51  ? 176 TYR   C CD2 1 
ATOM   6469 C  CE1 . TYR   C  1  163 ? -14.821 21.998  15.460 1.00 58.73  ? 176 TYR   C CE1 1 
ATOM   6470 C  CE2 . TYR   C  1  163 ? -14.342 20.390  13.754 1.00 61.95  ? 176 TYR   C CE2 1 
ATOM   6471 C  CZ  . TYR   C  1  163 ? -13.915 21.184  14.800 1.00 55.74  ? 176 TYR   C CZ  1 
ATOM   6472 O  OH  . TYR   C  1  163 ? -12.598 21.172  15.127 1.00 47.49  ? 176 TYR   C OH  1 
ATOM   6473 N  N   . ASN   C  1  164 ? -17.098 23.282  11.175 1.00 50.47  ? 177 ASN   C N   1 
ATOM   6474 C  CA  . ASN   C  1  164 ? -16.335 23.359  9.946  1.00 57.32  ? 177 ASN   C CA  1 
ATOM   6475 C  C   . ASN   C  1  164 ? -14.959 23.949  10.249 1.00 57.90  ? 177 ASN   C C   1 
ATOM   6476 O  O   . ASN   C  1  164 ? -14.621 24.171  11.413 1.00 53.03  ? 177 ASN   C O   1 
ATOM   6477 C  CB  . ASN   C  1  164 ? -17.141 24.085  8.880  1.00 68.87  ? 177 ASN   C CB  1 
ATOM   6478 C  CG  . ASN   C  1  164 ? -17.122 25.591  9.004  1.00 76.68  ? 177 ASN   C CG  1 
ATOM   6479 O  OD1 . ASN   C  1  164 ? -16.478 26.177  9.894  1.00 73.25  ? 177 ASN   C OD1 1 
ATOM   6480 N  ND2 . ASN   C  1  164 ? -17.790 26.225  8.053  1.00 85.59  ? 177 ASN   C ND2 1 
ATOM   6481 N  N   . LEU   C  1  165 ? -14.174 24.207  9.196  1.00 58.18  ? 178 LEU   C N   1 
ATOM   6482 C  CA  . LEU   C  1  165 ? -12.761 24.502  9.365  1.00 61.98  ? 178 LEU   C CA  1 
ATOM   6483 C  C   . LEU   C  1  165 ? -12.564 25.815  10.126 1.00 64.39  ? 178 LEU   C C   1 
ATOM   6484 O  O   . LEU   C  1  165 ? -11.609 25.946  10.898 1.00 62.45  ? 178 LEU   C O   1 
ATOM   6485 C  CB  . LEU   C  1  165 ? -12.085 24.485  7.996  1.00 65.96  ? 178 LEU   C CB  1 
ATOM   6486 C  CG  . LEU   C  1  165 ? -10.554 24.595  7.984  1.00 72.54  ? 178 LEU   C CG  1 
ATOM   6487 C  CD1 . LEU   C  1  165 ? -9.880  23.346  8.552  1.00 68.21  ? 178 LEU   C CD1 1 
ATOM   6488 C  CD2 . LEU   C  1  165 ? -10.027 24.925  6.589  1.00 74.41  ? 178 LEU   C CD2 1 
ATOM   6489 N  N   . THR   C  1  166 ? -13.477 26.781  9.941  1.00 68.09  ? 179 THR   C N   1 
ATOM   6490 C  CA  . THR   C  1  166 ? -13.401 28.047  10.660 1.00 69.90  ? 179 THR   C CA  1 
ATOM   6491 C  C   . THR   C  1  166 ? -13.617 27.810  12.157 1.00 52.73  ? 179 THR   C C   1 
ATOM   6492 O  O   . THR   C  1  166 ? -12.884 28.329  12.986 1.00 49.85  ? 179 THR   C O   1 
ATOM   6493 C  CB  . THR   C  1  166 ? -14.437 29.016  10.082 1.00 79.76  ? 179 THR   C CB  1 
ATOM   6494 O  OG1 . THR   C  1  166 ? -14.178 29.087  8.682  1.00 77.92  ? 179 THR   C OG1 1 
ATOM   6495 C  CG2 . THR   C  1  166 ? -14.362 30.403  10.703 1.00 81.13  ? 179 THR   C CG2 1 
ATOM   6496 N  N   . VAL   C  1  167 ? -14.623 27.008  12.501 1.00 51.55  ? 180 VAL   C N   1 
ATOM   6497 C  CA  . VAL   C  1  167 ? -14.898 26.675  13.889 1.00 54.99  ? 180 VAL   C CA  1 
ATOM   6498 C  C   . VAL   C  1  167 ? -13.666 26.008  14.499 1.00 67.61  ? 180 VAL   C C   1 
ATOM   6499 O  O   . VAL   C  1  167 ? -13.293 26.324  15.624 1.00 67.21  ? 180 VAL   C O   1 
ATOM   6500 C  CB  . VAL   C  1  167 ? -16.114 25.744  14.043 1.00 55.07  ? 180 VAL   C CB  1 
ATOM   6501 C  CG1 . VAL   C  1  167 ? -16.470 25.522  15.508 1.00 52.90  ? 180 VAL   C CG1 1 
ATOM   6502 C  CG2 . VAL   C  1  167 ? -17.338 26.230  13.266 1.00 61.50  ? 180 VAL   C CG2 1 
ATOM   6503 N  N   . ALA   C  1  168 ? -13.067 25.056  13.768 1.00 80.61  ? 181 ALA   C N   1 
ATOM   6504 C  CA  . ALA   C  1  168 ? -11.904 24.318  14.253 1.00 77.38  ? 181 ALA   C CA  1 
ATOM   6505 C  C   . ALA   C  1  168 ? -10.796 25.273  14.685 1.00 72.12  ? 181 ALA   C C   1 
ATOM   6506 O  O   . ALA   C  1  168 ? -10.234 25.132  15.772 1.00 72.85  ? 181 ALA   C O   1 
ATOM   6507 C  CB  . ALA   C  1  168 ? -11.399 23.341  13.206 1.00 76.83  ? 181 ALA   C CB  1 
ATOM   6508 N  N   . GLY   C  1  169 ? -10.501 26.265  13.841 1.00 67.35  ? 182 GLY   C N   1 
ATOM   6509 C  CA  . GLY   C  1  169 ? -9.451  27.221  14.152 1.00 72.93  ? 182 GLY   C CA  1 
ATOM   6510 C  C   . GLY   C  1  169 ? -9.725  27.949  15.469 1.00 76.27  ? 182 GLY   C C   1 
ATOM   6511 O  O   . GLY   C  1  169 ? -8.825  28.109  16.289 1.00 82.55  ? 182 GLY   C O   1 
ATOM   6512 N  N   . GLU   C  1  170 ? -10.978 28.368  15.663 1.00 70.97  ? 183 GLU   C N   1 
ATOM   6513 C  CA  . GLU   C  1  170 ? -11.367 29.127  16.834 1.00 66.46  ? 183 GLU   C CA  1 
ATOM   6514 C  C   . GLU   C  1  170 ? -11.370 28.210  18.050 1.00 61.50  ? 183 GLU   C C   1 
ATOM   6515 O  O   . GLU   C  1  170 ? -10.828 28.572  19.086 1.00 68.03  ? 183 GLU   C O   1 
ATOM   6516 C  CB  . GLU   C  1  170 ? -12.736 29.793  16.634 1.00 73.44  ? 183 GLU   C CB  1 
ATOM   6517 C  CG  . GLU   C  1  170 ? -12.779 30.823  15.508 1.00 74.89  ? 183 GLU   C CG  1 
ATOM   6518 C  CD  . GLU   C  1  170 ? -11.697 31.899  15.605 1.00 75.52  ? 183 GLU   C CD  1 
ATOM   6519 O  OE1 . GLU   C  1  170 ? -11.520 32.436  16.712 1.00 76.63  ? 183 GLU   C OE1 1 
ATOM   6520 O  OE2 . GLU   C  1  170 ? -11.030 32.205  14.593 1.00 80.63  ? 183 GLU   C OE2 1 
ATOM   6521 N  N   . LEU   C  1  171 ? -11.974 27.026  17.928 1.00 57.08  ? 184 LEU   C N   1 
ATOM   6522 C  CA  . LEU   C  1  171 ? -12.131 26.163  19.083 1.00 61.84  ? 184 LEU   C CA  1 
ATOM   6523 C  C   . LEU   C  1  171 ? -10.752 25.747  19.597 1.00 60.82  ? 184 LEU   C C   1 
ATOM   6524 O  O   . LEU   C  1  171 ? -10.510 25.742  20.802 1.00 59.82  ? 184 LEU   C O   1 
ATOM   6525 C  CB  . LEU   C  1  171 ? -13.009 24.952  18.768 1.00 65.42  ? 184 LEU   C CB  1 
ATOM   6526 C  CG  . LEU   C  1  171 ? -13.322 24.055  19.972 1.00 69.44  ? 184 LEU   C CG  1 
ATOM   6527 C  CD1 . LEU   C  1  171 ? -14.020 24.801  21.101 1.00 70.68  ? 184 LEU   C CD1 1 
ATOM   6528 C  CD2 . LEU   C  1  171 ? -14.158 22.860  19.576 1.00 73.97  ? 184 LEU   C CD2 1 
ATOM   6529 N  N   . ARG   C  1  172 ? -9.836  25.427  18.677 1.00 57.79  ? 185 ARG   C N   1 
ATOM   6530 C  CA  . ARG   C  1  172 ? -8.545  24.876  19.066 1.00 61.40  ? 185 ARG   C CA  1 
ATOM   6531 C  C   . ARG   C  1  172 ? -7.813  25.883  19.955 1.00 61.73  ? 185 ARG   C C   1 
ATOM   6532 O  O   . ARG   C  1  172 ? -7.309  25.549  21.032 1.00 58.05  ? 185 ARG   C O   1 
ATOM   6533 C  CB  . ARG   C  1  172 ? -7.754  24.471  17.815 1.00 57.31  ? 185 ARG   C CB  1 
ATOM   6534 C  CG  . ARG   C  1  172 ? -6.236  24.373  17.924 1.00 54.07  ? 185 ARG   C CG  1 
ATOM   6535 C  CD  . ARG   C  1  172 ? -5.710  23.486  19.041 1.00 48.59  ? 185 ARG   C CD  1 
ATOM   6536 N  NE  . ARG   C  1  172 ? -6.354  22.173  19.100 1.00 50.71  ? 185 ARG   C NE  1 
ATOM   6537 C  CZ  . ARG   C  1  172 ? -6.801  21.571  20.200 1.00 59.00  ? 185 ARG   C CZ  1 
ATOM   6538 N  NH1 . ARG   C  1  172 ? -6.733  22.195  21.368 1.00 54.08  ? 185 ARG   C NH1 1 
ATOM   6539 N  NH2 . ARG   C  1  172 ? -7.304  20.341  20.129 1.00 60.04  ? 185 ARG   C NH2 1 
ATOM   6540 N  N   . TYR   C  1  173 ? -7.778  27.128  19.483 1.00 62.66  ? 186 TYR   C N   1 
ATOM   6541 C  CA  . TYR   C  1  173 ? -7.124  28.207  20.201 1.00 65.53  ? 186 TYR   C CA  1 
ATOM   6542 C  C   . TYR   C  1  173 ? -7.784  28.464  21.555 1.00 60.85  ? 186 TYR   C C   1 
ATOM   6543 O  O   . TYR   C  1  173 ? -7.111  28.578  22.575 1.00 59.37  ? 186 TYR   C O   1 
ATOM   6544 C  CB  . TYR   C  1  173 ? -7.190  29.457  19.330 1.00 67.38  ? 186 TYR   C CB  1 
ATOM   6545 C  CG  . TYR   C  1  173 ? -6.467  30.624  19.970 1.00 82.47  ? 186 TYR   C CG  1 
ATOM   6546 C  CD1 . TYR   C  1  173 ? -5.086  30.593  20.133 1.00 87.70  ? 186 TYR   C CD1 1 
ATOM   6547 C  CD2 . TYR   C  1  173 ? -7.155  31.754  20.391 1.00 92.30  ? 186 TYR   C CD2 1 
ATOM   6548 C  CE1 . TYR   C  1  173 ? -4.402  31.658  20.690 1.00 92.55  ? 186 TYR   C CE1 1 
ATOM   6549 C  CE2 . TYR   C  1  173 ? -6.483  32.826  20.959 1.00 92.25  ? 186 TYR   C CE2 1 
ATOM   6550 C  CZ  . TYR   C  1  173 ? -5.106  32.780  21.097 1.00 94.25  ? 186 TYR   C CZ  1 
ATOM   6551 O  OH  . TYR   C  1  173 ? -4.451  33.824  21.675 1.00 89.86  ? 186 TYR   C OH  1 
ATOM   6552 N  N   . SER   C  1  174 ? -9.111  28.545  21.563 1.00 59.91  ? 187 SER   C N   1 
ATOM   6553 C  CA  . SER   C  1  174 ? -9.828  28.809  22.798 1.00 64.81  ? 187 SER   C CA  1 
ATOM   6554 C  C   . SER   C  1  174 ? -9.541  27.724  23.840 1.00 62.88  ? 187 SER   C C   1 
ATOM   6555 O  O   . SER   C  1  174 ? -9.359  28.035  25.019 1.00 63.23  ? 187 SER   C O   1 
ATOM   6556 C  CB  . SER   C  1  174 ? -11.311 28.966  22.545 1.00 69.87  ? 187 SER   C CB  1 
ATOM   6557 O  OG  . SER   C  1  174 ? -11.999 29.168  23.768 1.00 62.29  ? 187 SER   C OG  1 
ATOM   6558 N  N   . ARG   C  1  175 ? -9.474  26.452  23.409 1.00 59.40  ? 188 ARG   C N   1 
ATOM   6559 C  CA  . ARG   C  1  175 ? -9.250  25.352  24.341 1.00 55.42  ? 188 ARG   C CA  1 
ATOM   6560 C  C   . ARG   C  1  175 ? -7.837  25.439  24.913 1.00 57.87  ? 188 ARG   C C   1 
ATOM   6561 O  O   . ARG   C  1  175 ? -7.619  25.087  26.078 1.00 63.31  ? 188 ARG   C O   1 
ATOM   6562 C  CB  . ARG   C  1  175 ? -9.530  23.983  23.711 1.00 53.97  ? 188 ARG   C CB  1 
ATOM   6563 C  CG  . ARG   C  1  175 ? -11.013 23.766  23.427 1.00 51.72  ? 188 ARG   C CG  1 
ATOM   6564 C  CD  . ARG   C  1  175 ? -11.843 23.580  24.675 1.00 53.94  ? 188 ARG   C CD  1 
ATOM   6565 N  NE  . ARG   C  1  175 ? -11.379 22.376  25.371 1.00 63.27  ? 188 ARG   C NE  1 
ATOM   6566 C  CZ  . ARG   C  1  175 ? -10.779 22.317  26.550 1.00 65.85  ? 188 ARG   C CZ  1 
ATOM   6567 N  NH1 . ARG   C  1  175 ? -10.698 23.380  27.326 1.00 64.68  ? 188 ARG   C NH1 1 
ATOM   6568 N  NH2 . ARG   C  1  175 ? -10.273 21.168  26.958 1.00 74.24  ? 188 ARG   C NH2 1 
ATOM   6569 N  N   . ILE   C  1  176 ? -6.890  25.916  24.096 1.00 56.77  ? 189 ILE   C N   1 
ATOM   6570 C  CA  . ILE   C  1  176 ? -5.535  26.161  24.567 1.00 64.22  ? 189 ILE   C CA  1 
ATOM   6571 C  C   . ILE   C  1  176 ? -5.586  27.188  25.699 1.00 66.59  ? 189 ILE   C C   1 
ATOM   6572 O  O   . ILE   C  1  176 ? -5.031  26.955  26.778 1.00 69.31  ? 189 ILE   C O   1 
ATOM   6573 C  CB  . ILE   C  1  176 ? -4.598  26.579  23.413 1.00 58.57  ? 189 ILE   C CB  1 
ATOM   6574 C  CG1 . ILE   C  1  176 ? -4.333  25.408  22.468 1.00 59.73  ? 189 ILE   C CG1 1 
ATOM   6575 C  CG2 . ILE   C  1  176 ? -3.282  27.157  23.945 1.00 55.50  ? 189 ILE   C CG2 1 
ATOM   6576 C  CD1 . ILE   C  1  176 ? -3.701  25.791  21.140 1.00 56.10  ? 189 ILE   C CD1 1 
ATOM   6577 N  N   . GLN   C  1  177 ? -6.296  28.299  25.462 1.00 71.98  ? 190 GLN   C N   1 
ATOM   6578 C  CA  . GLN   C  1  177 ? -6.459  29.347  26.465 1.00 74.46  ? 190 GLN   C CA  1 
ATOM   6579 C  C   . GLN   C  1  177 ? -7.087  28.812  27.758 1.00 64.80  ? 190 GLN   C C   1 
ATOM   6580 O  O   . GLN   C  1  177 ? -6.572  29.105  28.840 1.00 69.18  ? 190 GLN   C O   1 
ATOM   6581 C  CB  . GLN   C  1  177 ? -7.220  30.546  25.892 1.00 80.79  ? 190 GLN   C CB  1 
ATOM   6582 C  CG  . GLN   C  1  177 ? -6.522  31.240  24.720 1.00 81.13  ? 190 GLN   C CG  1 
ATOM   6583 C  CD  . GLN   C  1  177 ? -5.140  31.780  25.048 1.00 85.16  ? 190 GLN   C CD  1 
ATOM   6584 O  OE1 . GLN   C  1  177 ? -4.807  32.068  26.206 1.00 84.22  ? 190 GLN   C OE1 1 
ATOM   6585 N  NE2 . GLN   C  1  177 ? -4.290  31.908  24.039 1.00 85.15  ? 190 GLN   C NE2 1 
ATOM   6586 N  N   . ASP   C  1  178 ? -8.166  28.015  27.663 1.00 59.47  ? 191 ASP   C N   1 
ATOM   6587 C  CA  . ASP   C  1  178 ? -8.773  27.416  28.848 1.00 61.04  ? 191 ASP   C CA  1 
ATOM   6588 C  C   . ASP   C  1  178 ? -7.719  26.693  29.693 1.00 70.88  ? 191 ASP   C C   1 
ATOM   6589 O  O   . ASP   C  1  178 ? -7.706  26.812  30.923 1.00 64.06  ? 191 ASP   C O   1 
ATOM   6590 C  CB  . ASP   C  1  178 ? -9.888  26.432  28.516 1.00 71.00  ? 191 ASP   C CB  1 
ATOM   6591 C  CG  . ASP   C  1  178 ? -11.126 26.998  27.821 1.00 78.18  ? 191 ASP   C CG  1 
ATOM   6592 O  OD1 . ASP   C  1  178 ? -11.295 28.233  27.835 1.00 92.77  ? 191 ASP   C OD1 1 
ATOM   6593 O  OD2 . ASP   C  1  178 ? -11.923 26.205  27.252 1.00 74.19  ? 191 ASP   C OD2 1 
ATOM   6594 N  N   . SER   C  1  179 ? -6.847  25.920  29.030 1.00 72.20  ? 192 SER   C N   1 
ATOM   6595 C  CA  . SER   C  1  179 ? -5.884  25.076  29.722 1.00 66.48  ? 192 SER   C CA  1 
ATOM   6596 C  C   . SER   C  1  179 ? -4.760  25.916  30.339 1.00 62.23  ? 192 SER   C C   1 
ATOM   6597 O  O   . SER   C  1  179 ? -4.267  25.605  31.425 1.00 55.87  ? 192 SER   C O   1 
ATOM   6598 C  CB  . SER   C  1  179 ? -5.334  23.988  28.803 1.00 61.02  ? 192 SER   C CB  1 
ATOM   6599 O  OG  . SER   C  1  179 ? -6.197  22.859  28.770 1.00 53.38  ? 192 SER   C OG  1 
ATOM   6600 N  N   . ILE   C  1  180 ? -4.336  26.968  29.633 1.00 55.23  ? 193 ILE   C N   1 
ATOM   6601 C  CA  . ILE   C  1  180 ? -3.360  27.893  30.188 1.00 62.51  ? 193 ILE   C CA  1 
ATOM   6602 C  C   . ILE   C  1  180 ? -3.888  28.498  31.490 1.00 68.73  ? 193 ILE   C C   1 
ATOM   6603 O  O   . ILE   C  1  180 ? -3.174  28.559  32.491 1.00 70.59  ? 193 ILE   C O   1 
ATOM   6604 C  CB  . ILE   C  1  180 ? -3.004  28.991  29.174 1.00 61.40  ? 193 ILE   C CB  1 
ATOM   6605 C  CG1 . ILE   C  1  180 ? -2.164  28.425  28.033 1.00 65.69  ? 193 ILE   C CG1 1 
ATOM   6606 C  CG2 . ILE   C  1  180 ? -2.292  30.152  29.870 1.00 60.29  ? 193 ILE   C CG2 1 
ATOM   6607 C  CD1 . ILE   C  1  180 ? -1.893  29.398  26.903 1.00 65.33  ? 193 ILE   C CD1 1 
ATOM   6608 N  N   . ALA   C  1  181 ? -5.153  28.933  31.466 1.00 76.57  ? 194 ALA   C N   1 
ATOM   6609 C  CA  . ALA   C  1  181 ? -5.727  29.676  32.575 1.00 76.46  ? 194 ALA   C CA  1 
ATOM   6610 C  C   . ALA   C  1  181 ? -6.022  28.778  33.777 1.00 75.16  ? 194 ALA   C C   1 
ATOM   6611 O  O   . ALA   C  1  181 ? -6.075  29.278  34.899 1.00 83.82  ? 194 ALA   C O   1 
ATOM   6612 C  CB  . ALA   C  1  181 ? -6.982  30.389  32.113 1.00 73.37  ? 194 ALA   C CB  1 
ATOM   6613 N  N   . THR   C  1  182 ? -6.247  27.473  33.561 1.00 70.69  ? 195 THR   C N   1 
ATOM   6614 C  CA  . THR   C  1  182 ? -6.864  26.661  34.600 1.00 75.16  ? 195 THR   C CA  1 
ATOM   6615 C  C   . THR   C  1  182 ? -6.017  25.444  34.961 1.00 75.33  ? 195 THR   C C   1 
ATOM   6616 O  O   . THR   C  1  182 ? -6.301  24.795  35.963 1.00 78.25  ? 195 THR   C O   1 
ATOM   6617 C  CB  . THR   C  1  182 ? -8.268  26.211  34.190 1.00 90.80  ? 195 THR   C CB  1 
ATOM   6618 O  OG1 . THR   C  1  182 ? -8.141  25.429  33.005 1.00 101.91 ? 195 THR   C OG1 1 
ATOM   6619 C  CG2 . THR   C  1  182 ? -9.228  27.364  33.952 1.00 93.51  ? 195 THR   C CG2 1 
ATOM   6620 N  N   . ASN   C  1  183 ? -5.020  25.097  34.144 1.00 70.95  ? 196 ASN   C N   1 
ATOM   6621 C  CA  . ASN   C  1  183 ? -4.302  23.851  34.354 1.00 71.03  ? 196 ASN   C CA  1 
ATOM   6622 C  C   . ASN   C  1  183 ? -2.836  24.184  34.586 1.00 64.74  ? 196 ASN   C C   1 
ATOM   6623 O  O   . ASN   C  1  183 ? -2.108  24.463  33.646 1.00 59.58  ? 196 ASN   C O   1 
ATOM   6624 C  CB  . ASN   C  1  183 ? -4.485  22.868  33.201 1.00 72.33  ? 196 ASN   C CB  1 
ATOM   6625 C  CG  . ASN   C  1  183 ? -3.729  21.571  33.393 1.00 69.33  ? 196 ASN   C CG  1 
ATOM   6626 O  OD1 . ASN   C  1  183 ? -3.075  21.366  34.424 1.00 69.72  ? 196 ASN   C OD1 1 
ATOM   6627 N  ND2 . ASN   C  1  183 ? -3.805  20.680  32.411 1.00 66.93  ? 196 ASN   C ND2 1 
ATOM   6628 N  N   . PRO   C  1  184 ? -2.358  24.143  35.845 1.00 63.27  ? 197 PRO   C N   1 
ATOM   6629 C  CA  . PRO   C  1  184 ? -0.965  24.480  36.133 1.00 66.13  ? 197 PRO   C CA  1 
ATOM   6630 C  C   . PRO   C  1  184 ? 0.065   23.486  35.593 1.00 70.65  ? 197 PRO   C C   1 
ATOM   6631 O  O   . PRO   C  1  184 ? 1.235   23.824  35.497 1.00 70.54  ? 197 PRO   C O   1 
ATOM   6632 C  CB  . PRO   C  1  184 ? -0.978  24.526  37.670 1.00 65.93  ? 197 PRO   C CB  1 
ATOM   6633 C  CG  . PRO   C  1  184 ? -2.006  23.488  38.059 1.00 68.37  ? 197 PRO   C CG  1 
ATOM   6634 C  CD  . PRO   C  1  184 ? -3.111  23.705  37.034 1.00 69.03  ? 197 PRO   C CD  1 
ATOM   6635 N  N   . GLU   C  1  185 ? -0.370  22.267  35.239 1.00 73.65  ? 198 GLU   C N   1 
ATOM   6636 C  CA  . GLU   C  1  185 ? 0.513   21.258  34.667 1.00 78.36  ? 198 GLU   C CA  1 
ATOM   6637 C  C   . GLU   C  1  185 ? 0.369   21.189  33.140 1.00 72.45  ? 198 GLU   C C   1 
ATOM   6638 O  O   . GLU   C  1  185 ? 0.931   20.299  32.516 1.00 80.31  ? 198 GLU   C O   1 
ATOM   6639 C  CB  . GLU   C  1  185 ? 0.238   19.876  35.270 1.00 79.39  ? 198 GLU   C CB  1 
ATOM   6640 C  CG  . GLU   C  1  185 ? 0.505   19.762  36.771 1.00 77.02  ? 198 GLU   C CG  1 
ATOM   6641 C  CD  . GLU   C  1  185 ? 0.139   18.411  37.381 1.00 87.47  ? 198 GLU   C CD  1 
ATOM   6642 O  OE1 . GLU   C  1  185 ? -0.191  17.471  36.623 1.00 89.98  ? 198 GLU   C OE1 1 
ATOM   6643 O  OE2 . GLU   C  1  185 ? 0.155   18.288  38.627 1.00 85.66  ? 198 GLU   C OE2 1 
ATOM   6644 N  N   . PHE   C  1  186 ? -0.350  22.140  32.533 1.00 67.06  ? 199 PHE   C N   1 
ATOM   6645 C  CA  . PHE   C  1  186 ? -0.588  22.156  31.100 1.00 62.78  ? 199 PHE   C CA  1 
ATOM   6646 C  C   . PHE   C  1  186 ? 0.711   22.023  30.310 1.00 60.35  ? 199 PHE   C C   1 
ATOM   6647 O  O   . PHE   C  1  186 ? 1.613   22.837  30.454 1.00 56.80  ? 199 PHE   C O   1 
ATOM   6648 C  CB  . PHE   C  1  186 ? -1.264  23.464  30.687 1.00 62.23  ? 199 PHE   C CB  1 
ATOM   6649 C  CG  . PHE   C  1  186 ? -1.569  23.613  29.202 1.00 59.03  ? 199 PHE   C CG  1 
ATOM   6650 C  CD1 . PHE   C  1  186 ? -2.148  22.579  28.477 1.00 59.33  ? 199 PHE   C CD1 1 
ATOM   6651 C  CD2 . PHE   C  1  186 ? -1.264  24.790  28.536 1.00 55.56  ? 199 PHE   C CD2 1 
ATOM   6652 C  CE1 . PHE   C  1  186 ? -2.418  22.727  27.124 1.00 57.69  ? 199 PHE   C CE1 1 
ATOM   6653 C  CE2 . PHE   C  1  186 ? -1.529  24.928  27.184 1.00 58.38  ? 199 PHE   C CE2 1 
ATOM   6654 C  CZ  . PHE   C  1  186 ? -2.102  23.898  26.482 1.00 60.36  ? 199 PHE   C CZ  1 
ATOM   6655 N  N   . GLN   C  1  187 ? 0.750   20.998  29.444 1.00 62.11  ? 200 GLN   C N   1 
ATOM   6656 C  CA  . GLN   C  1  187 ? 1.816   20.778  28.478 1.00 57.38  ? 200 GLN   C CA  1 
ATOM   6657 C  C   . GLN   C  1  187 ? 1.217   20.767  27.073 1.00 55.02  ? 200 GLN   C C   1 
ATOM   6658 O  O   . GLN   C  1  187 ? 0.177   20.144  26.841 1.00 57.52  ? 200 GLN   C O   1 
ATOM   6659 C  CB  . GLN   C  1  187 ? 2.459   19.420  28.756 1.00 64.03  ? 200 GLN   C CB  1 
ATOM   6660 C  CG  . GLN   C  1  187 ? 3.287   19.375  30.035 1.00 71.27  ? 200 GLN   C CG  1 
ATOM   6661 C  CD  . GLN   C  1  187 ? 4.566   20.172  29.897 1.00 70.86  ? 200 GLN   C CD  1 
ATOM   6662 O  OE1 . GLN   C  1  187 ? 5.543   19.717  29.295 1.00 76.30  ? 200 GLN   C OE1 1 
ATOM   6663 N  NE2 . GLN   C  1  187 ? 4.574   21.382  30.432 1.00 68.98  ? 200 GLN   C NE2 1 
ATOM   6664 N  N   . PHE   C  1  188 ? 1.879   21.447  26.134 1.00 49.18  ? 201 PHE   C N   1 
ATOM   6665 C  CA  . PHE   C  1  188 ? 1.421   21.460  24.755 1.00 47.68  ? 201 PHE   C CA  1 
ATOM   6666 C  C   . PHE   C  1  188 ? 2.622   21.388  23.821 1.00 43.76  ? 201 PHE   C C   1 
ATOM   6667 O  O   . PHE   C  1  188 ? 2.880   22.318  23.078 1.00 47.34  ? 201 PHE   C O   1 
ATOM   6668 C  CB  . PHE   C  1  188 ? 0.575   22.708  24.510 1.00 46.95  ? 201 PHE   C CB  1 
ATOM   6669 C  CG  . PHE   C  1  188 ? -0.380  22.589  23.334 1.00 47.65  ? 201 PHE   C CG  1 
ATOM   6670 C  CD1 . PHE   C  1  188 ? -1.483  21.752  23.409 1.00 48.71  ? 201 PHE   C CD1 1 
ATOM   6671 C  CD2 . PHE   C  1  188 ? -0.204  23.329  22.176 1.00 45.85  ? 201 PHE   C CD2 1 
ATOM   6672 C  CE1 . PHE   C  1  188 ? -2.382  21.662  22.361 1.00 48.42  ? 201 PHE   C CE1 1 
ATOM   6673 C  CE2 . PHE   C  1  188 ? -1.113  23.237  21.136 1.00 41.76  ? 201 PHE   C CE2 1 
ATOM   6674 C  CZ  . PHE   C  1  188 ? -2.179  22.388  21.219 1.00 43.34  ? 201 PHE   C CZ  1 
ATOM   6675 N  N   . LYS   C  1  189 ? 3.358   20.277  23.866 1.00 47.98  ? 202 LYS   C N   1 
ATOM   6676 C  CA  . LYS   C  1  189 ? 4.590   20.147  23.096 1.00 51.24  ? 202 LYS   C CA  1 
ATOM   6677 C  C   . LYS   C  1  189 ? 4.776   18.710  22.595 1.00 47.01  ? 202 LYS   C C   1 
ATOM   6678 O  O   . LYS   C  1  189 ? 4.026   17.803  22.948 1.00 44.42  ? 202 LYS   C O   1 
ATOM   6679 C  CB  . LYS   C  1  189 ? 5.761   20.573  23.984 1.00 55.01  ? 202 LYS   C CB  1 
ATOM   6680 C  CG  . LYS   C  1  189 ? 5.927   19.717  25.243 1.00 59.07  ? 202 LYS   C CG  1 
ATOM   6681 C  CD  . LYS   C  1  189 ? 7.151   20.037  26.090 1.00 64.43  ? 202 LYS   C CD  1 
ATOM   6682 C  CE  . LYS   C  1  189 ? 7.027   21.368  26.747 1.00 76.85  ? 202 LYS   C CE  1 
ATOM   6683 N  NZ  . LYS   C  1  189 ? 8.119   21.703  27.656 1.00 82.52  ? 202 LYS   C NZ  1 
ATOM   6684 N  N   . ASN   C  1  190 ? 5.775   18.526  21.732 1.00 47.36  ? 203 ASN   C N   1 
ATOM   6685 C  CA  . ASN   C  1  190 ? 6.141   17.216  21.227 1.00 48.28  ? 203 ASN   C CA  1 
ATOM   6686 C  C   . ASN   C  1  190 ? 4.929   16.558  20.566 1.00 47.55  ? 203 ASN   C C   1 
ATOM   6687 O  O   . ASN   C  1  190 ? 4.329   17.148  19.671 1.00 41.47  ? 203 ASN   C O   1 
ATOM   6688 C  CB  . ASN   C  1  190 ? 6.841   16.431  22.327 1.00 53.41  ? 203 ASN   C CB  1 
ATOM   6689 C  CG  . ASN   C  1  190 ? 8.146   17.097  22.701 1.00 56.92  ? 203 ASN   C CG  1 
ATOM   6690 O  OD1 . ASN   C  1  190 ? 8.886   17.528  21.806 1.00 56.07  ? 203 ASN   C OD1 1 
ATOM   6691 N  ND2 . ASN   C  1  190 ? 8.431   17.191  23.993 1.00 53.73  ? 203 ASN   C ND2 1 
ATOM   6692 N  N   . VAL   C  1  191 ? 4.575   15.338  20.985 1.00 42.87  ? 204 VAL   C N   1 
ATOM   6693 C  CA  . VAL   C  1  191 ? 3.525   14.604  20.310 1.00 42.39  ? 204 VAL   C CA  1 
ATOM   6694 C  C   . VAL   C  1  191 ? 2.224   15.411  20.374 1.00 43.51  ? 204 VAL   C C   1 
ATOM   6695 O  O   . VAL   C  1  191 ? 1.515   15.545  19.378 1.00 45.51  ? 204 VAL   C O   1 
ATOM   6696 C  CB  . VAL   C  1  191 ? 3.353   13.206  20.933 1.00 42.45  ? 204 VAL   C CB  1 
ATOM   6697 C  CG1 . VAL   C  1  191 ? 2.114   12.497  20.394 1.00 43.01  ? 204 VAL   C CG1 1 
ATOM   6698 C  CG2 . VAL   C  1  191 ? 4.592   12.340  20.747 1.00 41.61  ? 204 VAL   C CG2 1 
ATOM   6699 N  N   . ARG   C  1  192 ? 1.900   15.944  21.553 1.00 45.94  ? 205 ARG   C N   1 
ATOM   6700 C  CA  . ARG   C  1  192 ? 0.597   16.553  21.757 1.00 45.08  ? 205 ARG   C CA  1 
ATOM   6701 C  C   . ARG   C  1  192 ? 0.420   17.767  20.855 1.00 43.56  ? 205 ARG   C C   1 
ATOM   6702 O  O   . ARG   C  1  192 ? -0.666  18.030  20.350 1.00 43.50  ? 205 ARG   C O   1 
ATOM   6703 C  CB  . ARG   C  1  192 ? 0.368   16.976  23.210 1.00 48.96  ? 205 ARG   C CB  1 
ATOM   6704 C  CG  . ARG   C  1  192 ? -1.009  17.585  23.420 1.00 50.87  ? 205 ARG   C CG  1 
ATOM   6705 C  CD  . ARG   C  1  192 ? -2.109  16.692  22.870 1.00 53.38  ? 205 ARG   C CD  1 
ATOM   6706 N  NE  . ARG   C  1  192 ? -3.441  17.277  23.015 1.00 56.61  ? 205 ARG   C NE  1 
ATOM   6707 C  CZ  . ARG   C  1  192 ? -4.522  16.880  22.360 1.00 57.56  ? 205 ARG   C CZ  1 
ATOM   6708 N  NH1 . ARG   C  1  192 ? -4.447  15.927  21.452 1.00 58.57  ? 205 ARG   C NH1 1 
ATOM   6709 N  NH2 . ARG   C  1  192 ? -5.681  17.455  22.611 1.00 61.08  ? 205 ARG   C NH2 1 
ATOM   6710 N  N   . PHE   C  1  193 ? 1.501   18.512  20.652 1.00 45.83  ? 206 PHE   C N   1 
ATOM   6711 C  CA  . PHE   C  1  193 ? 1.422   19.697  19.829 1.00 42.71  ? 206 PHE   C CA  1 
ATOM   6712 C  C   . PHE   C  1  193 ? 1.041   19.301  18.411 1.00 45.07  ? 206 PHE   C C   1 
ATOM   6713 O  O   . PHE   C  1  193 ? 0.229   19.977  17.796 1.00 46.14  ? 206 PHE   C O   1 
ATOM   6714 C  CB  . PHE   C  1  193 ? 2.730   20.475  19.853 1.00 43.28  ? 206 PHE   C CB  1 
ATOM   6715 C  CG  . PHE   C  1  193 ? 2.672   21.700  18.964 1.00 47.99  ? 206 PHE   C CG  1 
ATOM   6716 C  CD1 . PHE   C  1  193 ? 2.039   22.860  19.397 1.00 48.80  ? 206 PHE   C CD1 1 
ATOM   6717 C  CD2 . PHE   C  1  193 ? 3.246   21.678  17.699 1.00 54.21  ? 206 PHE   C CD2 1 
ATOM   6718 C  CE1 . PHE   C  1  193 ? 1.984   23.973  18.579 1.00 52.21  ? 206 PHE   C CE1 1 
ATOM   6719 C  CE2 . PHE   C  1  193 ? 3.190   22.797  16.884 1.00 54.93  ? 206 PHE   C CE2 1 
ATOM   6720 C  CZ  . PHE   C  1  193 ? 2.554   23.939  17.324 1.00 53.49  ? 206 PHE   C CZ  1 
ATOM   6721 N  N   . ILE   C  1  194 ? 1.592   18.184  17.915 1.00 45.60  ? 207 ILE   C N   1 
ATOM   6722 C  CA  . ILE   C  1  194 ? 1.307   17.759  16.557 1.00 43.75  ? 207 ILE   C CA  1 
ATOM   6723 C  C   . ILE   C  1  194 ? -0.103  17.169  16.475 1.00 44.04  ? 207 ILE   C C   1 
ATOM   6724 O  O   . ILE   C  1  194 ? -0.870  17.562  15.601 1.00 45.42  ? 207 ILE   C O   1 
ATOM   6725 C  CB  . ILE   C  1  194 ? 2.399   16.806  16.049 1.00 45.81  ? 207 ILE   C CB  1 
ATOM   6726 C  CG1 . ILE   C  1  194 ? 3.777   17.479  16.098 1.00 50.45  ? 207 ILE   C CG1 1 
ATOM   6727 C  CG2 . ILE   C  1  194 ? 2.076   16.298  14.645 1.00 45.95  ? 207 ILE   C CG2 1 
ATOM   6728 C  CD1 . ILE   C  1  194 ? 3.891   18.762  15.298 1.00 50.66  ? 207 ILE   C CD1 1 
ATOM   6729 N  N   . THR   C  1  195 ? -0.459  16.269  17.404 1.00 46.07  ? 208 THR   C N   1 
ATOM   6730 C  CA  . THR   C  1  195 ? -1.716  15.539  17.323 1.00 46.22  ? 208 THR   C CA  1 
ATOM   6731 C  C   . THR   C  1  195 ? -2.909  16.455  17.572 1.00 47.79  ? 208 THR   C C   1 
ATOM   6732 O  O   . THR   C  1  195 ? -4.004  16.168  17.092 1.00 47.52  ? 208 THR   C O   1 
ATOM   6733 C  CB  . THR   C  1  195 ? -1.728  14.347  18.276 1.00 45.37  ? 208 THR   C CB  1 
ATOM   6734 O  OG1 . THR   C  1  195 ? -1.621  14.805  19.624 1.00 48.45  ? 208 THR   C OG1 1 
ATOM   6735 C  CG2 . THR   C  1  195 ? -0.634  13.349  17.927 1.00 44.79  ? 208 THR   C CG2 1 
ATOM   6736 N  N   . ALA   C  1  196 ? -2.697  17.557  18.302 1.00 52.75  ? 209 ALA   C N   1 
ATOM   6737 C  CA  . ALA   C  1  196 ? -3.790  18.436  18.688 1.00 53.36  ? 209 ALA   C CA  1 
ATOM   6738 C  C   . ALA   C  1  196 ? -4.371  19.167  17.486 1.00 49.00  ? 209 ALA   C C   1 
ATOM   6739 O  O   . ALA   C  1  196 ? -5.547  19.507  17.502 1.00 50.73  ? 209 ALA   C O   1 
ATOM   6740 C  CB  . ALA   C  1  196 ? -3.347  19.432  19.734 1.00 57.93  ? 209 ALA   C CB  1 
ATOM   6741 N  N   . TYR   C  1  197 ? -3.564  19.417  16.457 1.00 46.50  ? 210 TYR   C N   1 
ATOM   6742 C  CA  . TYR   C  1  197 ? -4.067  20.125  15.291 1.00 48.93  ? 210 TYR   C CA  1 
ATOM   6743 C  C   . TYR   C  1  197 ? -4.800  19.142  14.389 1.00 48.00  ? 210 TYR   C C   1 
ATOM   6744 O  O   . TYR   C  1  197 ? -5.888  19.444  13.912 1.00 51.17  ? 210 TYR   C O   1 
ATOM   6745 C  CB  . TYR   C  1  197 ? -2.935  20.922  14.641 1.00 52.45  ? 210 TYR   C CB  1 
ATOM   6746 C  CG  . TYR   C  1  197 ? -2.681  22.159  15.482 1.00 59.65  ? 210 TYR   C CG  1 
ATOM   6747 C  CD1 . TYR   C  1  197 ? -3.447  23.310  15.312 1.00 63.04  ? 210 TYR   C CD1 1 
ATOM   6748 C  CD2 . TYR   C  1  197 ? -1.770  22.132  16.525 1.00 62.84  ? 210 TYR   C CD2 1 
ATOM   6749 C  CE1 . TYR   C  1  197 ? -3.270  24.417  16.124 1.00 61.71  ? 210 TYR   C CE1 1 
ATOM   6750 C  CE2 . TYR   C  1  197 ? -1.582  23.233  17.340 1.00 62.50  ? 210 TYR   C CE2 1 
ATOM   6751 C  CZ  . TYR   C  1  197 ? -2.342  24.373  17.147 1.00 61.57  ? 210 TYR   C CZ  1 
ATOM   6752 O  OH  . TYR   C  1  197 ? -2.139  25.458  17.949 1.00 69.06  ? 210 TYR   C OH  1 
ATOM   6753 N  N   . GLY   C  1  198 ? -4.214  17.961  14.189 1.00 44.17  ? 211 GLY   C N   1 
ATOM   6754 C  CA  . GLY   C  1  198 ? -4.850  16.947  13.373 1.00 42.65  ? 211 GLY   C CA  1 
ATOM   6755 C  C   . GLY   C  1  198 ? -6.207  16.536  13.928 1.00 41.60  ? 211 GLY   C C   1 
ATOM   6756 O  O   . GLY   C  1  198 ? -7.131  16.330  13.158 1.00 47.73  ? 211 GLY   C O   1 
ATOM   6757 N  N   . GLU   C  1  199 ? -6.338  16.415  15.252 1.00 41.28  ? 212 GLU   C N   1 
ATOM   6758 C  CA  A GLU   C  1  199 ? -7.567  15.894  15.825 0.50 41.81  ? 212 GLU   C CA  1 
ATOM   6759 C  CA  B GLU   C  1  199 ? -7.562  15.910  15.850 0.50 43.29  ? 212 GLU   C CA  1 
ATOM   6760 C  C   . GLU   C  1  199 ? -8.707  16.872  15.551 1.00 42.56  ? 212 GLU   C C   1 
ATOM   6761 O  O   . GLU   C  1  199 ? -9.861  16.469  15.514 1.00 41.45  ? 212 GLU   C O   1 
ATOM   6762 C  CB  A GLU   C  1  199 ? -7.364  15.462  17.279 0.50 41.05  ? 212 GLU   C CB  1 
ATOM   6763 C  CB  B GLU   C  1  199 ? -7.433  15.705  17.361 0.50 44.87  ? 212 GLU   C CB  1 
ATOM   6764 C  CG  A GLU   C  1  199 ? -6.612  14.136  17.397 0.50 40.14  ? 212 GLU   C CG  1 
ATOM   6765 C  CG  B GLU   C  1  199 ? -7.597  16.988  18.177 0.50 46.45  ? 212 GLU   C CG  1 
ATOM   6766 C  CD  A GLU   C  1  199 ? -5.910  13.868  18.718 0.50 41.19  ? 212 GLU   C CD  1 
ATOM   6767 C  CD  B GLU   C  1  199 ? -7.452  16.811  19.679 0.50 44.28  ? 212 GLU   C CD  1 
ATOM   6768 O  OE1 A GLU   C  1  199 ? -6.203  14.643  19.646 0.50 36.96  ? 212 GLU   C OE1 1 
ATOM   6769 O  OE1 B GLU   C  1  199 ? -7.029  15.716  20.100 0.50 44.15  ? 212 GLU   C OE1 1 
ATOM   6770 O  OE2 A GLU   C  1  199 ? -5.082  12.919  18.816 0.50 40.84  ? 212 GLU   C OE2 1 
ATOM   6771 O  OE2 B GLU   C  1  199 ? -7.781  17.749  20.427 0.50 38.88  ? 212 GLU   C OE2 1 
ATOM   6772 N  N   . THR   C  1  200 ? -8.381  18.152  15.324 1.00 43.92  ? 213 THR   C N   1 
ATOM   6773 C  CA  . THR   C  1  200 ? -9.435  19.142  15.164 1.00 52.27  ? 213 THR   C CA  1 
ATOM   6774 C  C   . THR   C  1  200 ? -9.997  19.106  13.751 1.00 53.34  ? 213 THR   C C   1 
ATOM   6775 O  O   . THR   C  1  200 ? -11.099 19.606  13.554 1.00 50.01  ? 213 THR   C O   1 
ATOM   6776 C  CB  . THR   C  1  200 ? -8.994  20.558  15.545 1.00 61.61  ? 213 THR   C CB  1 
ATOM   6777 O  OG1 . THR   C  1  200 ? -8.152  21.108  14.537 1.00 58.61  ? 213 THR   C OG1 1 
ATOM   6778 C  CG2 . THR   C  1  200 ? -8.312  20.595  16.901 1.00 63.61  ? 213 THR   C CG2 1 
ATOM   6779 N  N   . VAL   C  1  201 ? -9.273  18.499  12.795 1.00 51.72  ? 214 VAL   C N   1 
ATOM   6780 C  CA  . VAL   C  1  201 ? -9.794  18.378  11.441 1.00 47.57  ? 214 VAL   C CA  1 
ATOM   6781 C  C   . VAL   C  1  201 ? -10.353 16.985  11.168 1.00 44.87  ? 214 VAL   C C   1 
ATOM   6782 O  O   . VAL   C  1  201 ? -11.093 16.820  10.206 1.00 47.66  ? 214 VAL   C O   1 
ATOM   6783 C  CB  . VAL   C  1  201 ? -8.788  18.800  10.361 1.00 50.52  ? 214 VAL   C CB  1 
ATOM   6784 C  CG1 . VAL   C  1  201 ? -8.443  20.274  10.537 1.00 51.00  ? 214 VAL   C CG1 1 
ATOM   6785 C  CG2 . VAL   C  1  201 ? -7.533  17.930  10.328 1.00 49.50  ? 214 VAL   C CG2 1 
ATOM   6786 N  N   . PHE   C  1  202 ? -10.049 15.995  12.013 1.00 46.16  ? 215 PHE   C N   1 
ATOM   6787 C  CA  . PHE   C  1  202 ? -10.585 14.666  11.783 1.00 48.80  ? 215 PHE   C CA  1 
ATOM   6788 C  C   . PHE   C  1  202 ? -12.113 14.713  11.707 1.00 48.78  ? 215 PHE   C C   1 
ATOM   6789 O  O   . PHE   C  1  202 ? -12.708 14.035  10.874 1.00 54.12  ? 215 PHE   C O   1 
ATOM   6790 C  CB  . PHE   C  1  202 ? -10.112 13.675  12.843 1.00 48.71  ? 215 PHE   C CB  1 
ATOM   6791 C  CG  . PHE   C  1  202 ? -8.642  13.308  12.786 1.00 49.52  ? 215 PHE   C CG  1 
ATOM   6792 C  CD1 . PHE   C  1  202 ? -7.848  13.623  11.691 1.00 42.85  ? 215 PHE   C CD1 1 
ATOM   6793 C  CD2 . PHE   C  1  202 ? -8.068  12.604  13.836 1.00 48.74  ? 215 PHE   C CD2 1 
ATOM   6794 C  CE1 . PHE   C  1  202 ? -6.509  13.268  11.675 1.00 43.56  ? 215 PHE   C CE1 1 
ATOM   6795 C  CE2 . PHE   C  1  202 ? -6.731  12.251  13.803 1.00 46.36  ? 215 PHE   C CE2 1 
ATOM   6796 C  CZ  . PHE   C  1  202 ? -5.953  12.595  12.735 1.00 45.68  ? 215 PHE   C CZ  1 
ATOM   6797 N  N   . PRO   C  1  203 ? -12.831 15.481  12.550 1.00 47.55  ? 216 PRO   C N   1 
ATOM   6798 C  CA  . PRO   C  1  203 ? -14.287 15.510  12.448 1.00 46.76  ? 216 PRO   C CA  1 
ATOM   6799 C  C   . PRO   C  1  203 ? -14.770 15.953  11.071 1.00 43.56  ? 216 PRO   C C   1 
ATOM   6800 O  O   . PRO   C  1  203 ? -15.781 15.474  10.587 1.00 49.97  ? 216 PRO   C O   1 
ATOM   6801 C  CB  . PRO   C  1  203 ? -14.699 16.475  13.567 1.00 46.95  ? 216 PRO   C CB  1 
ATOM   6802 C  CG  . PRO   C  1  203 ? -13.553 16.392  14.556 1.00 47.57  ? 216 PRO   C CG  1 
ATOM   6803 C  CD  . PRO   C  1  203 ? -12.322 16.288  13.669 1.00 48.84  ? 216 PRO   C CD  1 
ATOM   6804 N  N   . ILE   C  1  204 ? -14.032 16.865  10.446 1.00 42.16  ? 217 ILE   C N   1 
ATOM   6805 C  CA  . ILE   C  1  204 ? -14.398 17.388  9.144  1.00 43.55  ? 217 ILE   C CA  1 
ATOM   6806 C  C   . ILE   C  1  204 ? -14.086 16.379  8.045  1.00 44.74  ? 217 ILE   C C   1 
ATOM   6807 O  O   . ILE   C  1  204 ? -14.927 16.125  7.187  1.00 46.24  ? 217 ILE   C O   1 
ATOM   6808 C  CB  . ILE   C  1  204 ? -13.664 18.704  8.878  1.00 46.36  ? 217 ILE   C CB  1 
ATOM   6809 C  CG1 . ILE   C  1  204 ? -14.052 19.745  9.909  1.00 46.23  ? 217 ILE   C CG1 1 
ATOM   6810 C  CG2 . ILE   C  1  204 ? -13.913 19.187  7.449  1.00 47.19  ? 217 ILE   C CG2 1 
ATOM   6811 C  CD1 . ILE   C  1  204 ? -13.116 20.941  9.928  1.00 50.78  ? 217 ILE   C CD1 1 
ATOM   6812 N  N   . ASN   C  1  205 ? -12.870 15.823  8.067  1.00 42.61  ? 218 ASN   C N   1 
ATOM   6813 C  CA  . ASN   C  1  205 ? -12.431 14.953  6.992  1.00 39.56  ? 218 ASN   C CA  1 
ATOM   6814 C  C   . ASN   C  1  205 ? -12.995 13.551  7.121  1.00 37.20  ? 218 ASN   C C   1 
ATOM   6815 O  O   . ASN   C  1  205 ? -13.108 12.892  6.094  1.00 40.06  ? 218 ASN   C O   1 
ATOM   6816 C  CB  . ASN   C  1  205 ? -10.916 14.854  6.898  1.00 40.07  ? 218 ASN   C CB  1 
ATOM   6817 C  CG  . ASN   C  1  205 ? -10.291 16.214  6.767  1.00 35.89  ? 218 ASN   C CG  1 
ATOM   6818 O  OD1 . ASN   C  1  205 ? -10.908 17.122  6.208  1.00 40.64  ? 218 ASN   C OD1 1 
ATOM   6819 N  ND2 . ASN   C  1  205 ? -9.117  16.403  7.350  1.00 36.91  ? 218 ASN   C ND2 1 
ATOM   6820 N  N   . LEU   C  1  206 ? -13.343 13.108  8.343  1.00 34.39  ? 219 LEU   C N   1 
ATOM   6821 C  CA  . LEU   C  1  206 ? -13.685 11.711  8.546  1.00 34.48  ? 219 LEU   C CA  1 
ATOM   6822 C  C   . LEU   C  1  206 ? -15.088 11.509  9.115  1.00 36.83  ? 219 LEU   C C   1 
ATOM   6823 O  O   . LEU   C  1  206 ? -15.640 10.419  8.962  1.00 36.29  ? 219 LEU   C O   1 
ATOM   6824 C  CB  . LEU   C  1  206 ? -12.620 11.078  9.436  1.00 33.22  ? 219 LEU   C CB  1 
ATOM   6825 C  CG  . LEU   C  1  206 ? -11.199 11.101  8.872  1.00 38.47  ? 219 LEU   C CG  1 
ATOM   6826 C  CD1 . LEU   C  1  206 ? -10.184 10.765  9.925  1.00 41.11  ? 219 LEU   C CD1 1 
ATOM   6827 C  CD2 . LEU   C  1  206 ? -11.071 10.115  7.734  1.00 41.82  ? 219 LEU   C CD2 1 
ATOM   6828 N  N   . PHE   C  1  207 ? -15.630 12.481  9.863  1.00 40.71  ? 220 PHE   C N   1 
ATOM   6829 C  CA  . PHE   C  1  207 ? -16.908 12.264  10.526 1.00 41.83  ? 220 PHE   C CA  1 
ATOM   6830 C  C   . PHE   C  1  207 ? -18.038 12.802  9.656  1.00 39.30  ? 220 PHE   C C   1 
ATOM   6831 O  O   . PHE   C  1  207 ? -19.193 12.479  9.882  1.00 45.64  ? 220 PHE   C O   1 
ATOM   6832 C  CB  . PHE   C  1  207 ? -17.031 12.880  11.919 1.00 44.91  ? 220 PHE   C CB  1 
ATOM   6833 C  CG  . PHE   C  1  207 ? -16.140 12.294  12.998 1.00 48.07  ? 220 PHE   C CG  1 
ATOM   6834 C  CD1 . PHE   C  1  207 ? -15.464 11.092  12.811 1.00 50.81  ? 220 PHE   C CD1 1 
ATOM   6835 C  CD2 . PHE   C  1  207 ? -15.996 12.959  14.212 1.00 46.89  ? 220 PHE   C CD2 1 
ATOM   6836 C  CE1 . PHE   C  1  207 ? -14.660 10.575  13.814 1.00 50.48  ? 220 PHE   C CE1 1 
ATOM   6837 C  CE2 . PHE   C  1  207 ? -15.167 12.457  15.200 1.00 46.20  ? 220 PHE   C CE2 1 
ATOM   6838 C  CZ  . PHE   C  1  207 ? -14.496 11.270  14.994 1.00 48.66  ? 220 PHE   C CZ  1 
ATOM   6839 N  N   . VAL   C  1  208 ? -17.700 13.632  8.679  1.00 40.65  ? 221 VAL   C N   1 
ATOM   6840 C  CA  . VAL   C  1  208 ? -18.652 14.088  7.683  1.00 44.46  ? 221 VAL   C CA  1 
ATOM   6841 C  C   . VAL   C  1  208 ? -18.828 12.979  6.654  1.00 49.37  ? 221 VAL   C C   1 
ATOM   6842 O  O   . VAL   C  1  208 ? -17.858 12.374  6.198  1.00 51.85  ? 221 VAL   C O   1 
ATOM   6843 C  CB  . VAL   C  1  208 ? -18.199 15.395  7.018  1.00 45.50  ? 221 VAL   C CB  1 
ATOM   6844 C  CG1 . VAL   C  1  208 ? -19.109 15.803  5.871  1.00 52.24  ? 221 VAL   C CG1 1 
ATOM   6845 C  CG2 . VAL   C  1  208 ? -18.110 16.514  8.039  1.00 43.55  ? 221 VAL   C CG2 1 
ATOM   6846 N  N   . ASP   C  1  209 ? -20.090 12.730  6.309  1.00 51.57  ? 222 ASP   C N   1 
ATOM   6847 C  CA  . ASP   C  1  209 ? -20.453 11.669  5.396  1.00 52.98  ? 222 ASP   C CA  1 
ATOM   6848 C  C   . ASP   C  1  209 ? -19.699 11.846  4.077  1.00 49.33  ? 222 ASP   C C   1 
ATOM   6849 O  O   . ASP   C  1  209 ? -19.552 12.956  3.587  1.00 43.37  ? 222 ASP   C O   1 
ATOM   6850 C  CB  . ASP   C  1  209 ? -21.955 11.663  5.198  1.00 51.23  ? 222 ASP   C CB  1 
ATOM   6851 C  CG  . ASP   C  1  209 ? -22.464 10.443  4.457  1.00 52.03  ? 222 ASP   C CG  1 
ATOM   6852 O  OD1 . ASP   C  1  209 ? -22.232 10.370  3.232  1.00 51.85  ? 222 ASP   C OD1 1 
ATOM   6853 O  OD2 . ASP   C  1  209 ? -23.055 9.573   5.120  1.00 50.85  ? 222 ASP   C OD2 1 
ATOM   6854 N  N   . GLY   C  1  210 ? -19.247 10.734  3.495  1.00 42.44  ? 223 GLY   C N   1 
ATOM   6855 C  CA  . GLY   C  1  210 ? -18.362 10.790  2.340  1.00 52.95  ? 223 GLY   C CA  1 
ATOM   6856 C  C   . GLY   C  1  210 ? -19.077 11.193  1.046  1.00 53.76  ? 223 GLY   C C   1 
ATOM   6857 O  O   . GLY   C  1  210 ? -18.416 11.608  0.091  1.00 50.45  ? 223 GLY   C O   1 
ATOM   6858 N  N   . ARG   C  1  211 ? -20.416 11.071  1.028  1.00 47.34  ? 224 ARG   C N   1 
ATOM   6859 C  CA  . ARG   C  1  211 ? -21.221 11.513  -0.093 1.00 47.56  ? 224 ARG   C CA  1 
ATOM   6860 C  C   . ARG   C  1  211 ? -21.295 13.038  -0.144 1.00 49.71  ? 224 ARG   C C   1 
ATOM   6861 O  O   . ARG   C  1  211 ? -21.668 13.583  -1.175 1.00 54.59  ? 224 ARG   C O   1 
ATOM   6862 C  CB  . ARG   C  1  211 ? -22.640 10.938  -0.019 1.00 47.16  ? 224 ARG   C CB  1 
ATOM   6863 C  CG  . ARG   C  1  211 ? -22.684 9.428   -0.194 1.00 47.99  ? 224 ARG   C CG  1 
ATOM   6864 C  CD  . ARG   C  1  211 ? -24.001 8.838   0.258  1.00 53.95  ? 224 ARG   C CD  1 
ATOM   6865 N  NE  . ARG   C  1  211 ? -24.249 9.032   1.693  1.00 59.78  ? 224 ARG   C NE  1 
ATOM   6866 C  CZ  . ARG   C  1  211 ? -25.260 8.508   2.386  1.00 59.23  ? 224 ARG   C CZ  1 
ATOM   6867 N  NH1 . ARG   C  1  211 ? -26.161 7.750   1.787  1.00 57.47  ? 224 ARG   C NH1 1 
ATOM   6868 N  NH2 . ARG   C  1  211 ? -25.360 8.738   3.683  1.00 62.30  ? 224 ARG   C NH2 1 
ATOM   6869 N  N   . VAL   C  1  212 ? -20.968 13.730  0.957  1.00 49.21  ? 225 VAL   C N   1 
ATOM   6870 C  CA  . VAL   C  1  212 ? -20.934 15.189  0.958  1.00 56.24  ? 225 VAL   C CA  1 
ATOM   6871 C  C   . VAL   C  1  212 ? -19.612 15.669  0.349  1.00 65.01  ? 225 VAL   C C   1 
ATOM   6872 O  O   . VAL   C  1  212 ? -18.563 15.578  0.979  1.00 72.18  ? 225 VAL   C O   1 
ATOM   6873 C  CB  . VAL   C  1  212 ? -21.136 15.760  2.375  1.00 57.38  ? 225 VAL   C CB  1 
ATOM   6874 C  CG1 . VAL   C  1  212 ? -20.983 17.279  2.432  1.00 53.65  ? 225 VAL   C CG1 1 
ATOM   6875 C  CG2 . VAL   C  1  212 ? -22.478 15.326  2.964  1.00 58.41  ? 225 VAL   C CG2 1 
ATOM   6876 N  N   . THR   C  1  213 ? -19.674 16.203  -0.875 1.00 75.83  ? 226 THR   C N   1 
ATOM   6877 C  CA  . THR   C  1  213 ? -18.480 16.528  -1.644 1.00 81.21  ? 226 THR   C CA  1 
ATOM   6878 C  C   . THR   C  1  213 ? -18.066 17.980  -1.407 1.00 80.05  ? 226 THR   C C   1 
ATOM   6879 O  O   . THR   C  1  213 ? -16.886 18.303  -1.507 1.00 66.33  ? 226 THR   C O   1 
ATOM   6880 C  CB  . THR   C  1  213 ? -18.738 16.241  -3.128 1.00 86.76  ? 226 THR   C CB  1 
ATOM   6881 O  OG1 . THR   C  1  213 ? -19.871 17.008  -3.542 1.00 84.55  ? 226 THR   C OG1 1 
ATOM   6882 C  CG2 . THR   C  1  213 ? -18.983 14.764  -3.403 1.00 81.32  ? 226 THR   C CG2 1 
ATOM   6883 N  N   . THR   C  1  214 ? -19.036 18.838  -1.063 1.00 95.64  ? 227 THR   C N   1 
ATOM   6884 C  CA  . THR   C  1  214 ? -18.843 20.279  -1.076 1.00 102.81 ? 227 THR   C CA  1 
ATOM   6885 C  C   . THR   C  1  214 ? -19.284 20.879  0.262  1.00 99.40  ? 227 THR   C C   1 
ATOM   6886 O  O   . THR   C  1  214 ? -20.340 20.515  0.787  1.00 103.49 ? 227 THR   C O   1 
ATOM   6887 C  CB  . THR   C  1  214 ? -19.630 20.844  -2.263 1.00 106.64 ? 227 THR   C CB  1 
ATOM   6888 O  OG1 . THR   C  1  214 ? -19.200 22.195  -2.381 1.00 102.76 ? 227 THR   C OG1 1 
ATOM   6889 C  CG2 . THR   C  1  214 ? -21.140 20.734  -2.106 1.00 103.53 ? 227 THR   C CG2 1 
ATOM   6890 N  N   . ASP   C  1  215 ? -18.482 21.814  0.802  1.00 94.30  ? 228 ASP   C N   1 
ATOM   6891 C  CA  . ASP   C  1  215 ? -18.863 22.560  1.992  1.00 96.96  ? 228 ASP   C CA  1 
ATOM   6892 C  C   . ASP   C  1  215 ? -19.032 21.559  3.133  1.00 81.54  ? 228 ASP   C C   1 
ATOM   6893 O  O   . ASP   C  1  215 ? -20.119 21.399  3.687  1.00 88.31  ? 228 ASP   C O   1 
ATOM   6894 C  CB  . ASP   C  1  215 ? -20.096 23.417  1.714  1.00 112.60 ? 228 ASP   C CB  1 
ATOM   6895 C  CG  . ASP   C  1  215 ? -20.526 24.408  2.793  1.00 117.46 ? 228 ASP   C CG  1 
ATOM   6896 O  OD1 . ASP   C  1  215 ? -19.692 24.751  3.654  1.00 127.06 ? 228 ASP   C OD1 1 
ATOM   6897 O  OD2 . ASP   C  1  215 ? -21.707 24.823  2.777  1.00 106.81 ? 228 ASP   C OD2 1 
ATOM   6898 N  N   . ARG   C  1  216 ? -17.945 20.848  3.440  1.00 70.57  ? 229 ARG   C N   1 
ATOM   6899 C  CA  . ARG   C  1  216 ? -17.991 19.759  4.398  1.00 68.01  ? 229 ARG   C CA  1 
ATOM   6900 C  C   . ARG   C  1  216 ? -18.102 20.360  5.797  1.00 57.38  ? 229 ARG   C C   1 
ATOM   6901 O  O   . ARG   C  1  216 ? -17.328 21.234  6.176  1.00 57.49  ? 229 ARG   C O   1 
ATOM   6902 C  CB  . ARG   C  1  216 ? -16.797 18.815  4.189  1.00 74.55  ? 229 ARG   C CB  1 
ATOM   6903 C  CG  . ARG   C  1  216 ? -16.890 17.933  2.949  1.00 72.28  ? 229 ARG   C CG  1 
ATOM   6904 C  CD  . ARG   C  1  216 ? -15.622 17.129  2.671  1.00 64.09  ? 229 ARG   C CD  1 
ATOM   6905 N  NE  . ARG   C  1  216 ? -15.377 16.074  3.659  1.00 60.23  ? 229 ARG   C NE  1 
ATOM   6906 C  CZ  . ARG   C  1  216 ? -16.062 14.935  3.793  1.00 68.66  ? 229 ARG   C CZ  1 
ATOM   6907 N  NH1 . ARG   C  1  216 ? -17.029 14.618  2.946  1.00 63.61  ? 229 ARG   C NH1 1 
ATOM   6908 N  NH2 . ARG   C  1  216 ? -15.756 14.092  4.776  1.00 78.01  ? 229 ARG   C NH2 1 
ATOM   6909 N  N   . LYS   C  1  217 ? -19.110 19.906  6.542  1.00 56.89  ? 230 LYS   C N   1 
ATOM   6910 C  CA  . LYS   C  1  217 ? -19.418 20.446  7.853  1.00 55.19  ? 230 LYS   C CA  1 
ATOM   6911 C  C   . LYS   C  1  217 ? -20.166 19.374  8.636  1.00 52.87  ? 230 LYS   C C   1 
ATOM   6912 O  O   . LYS   C  1  217 ? -20.925 18.608  8.049  1.00 54.64  ? 230 LYS   C O   1 
ATOM   6913 C  CB  . LYS   C  1  217 ? -20.259 21.707  7.636  1.00 63.82  ? 230 LYS   C CB  1 
ATOM   6914 C  CG  . LYS   C  1  217 ? -21.619 21.457  6.985  1.00 70.27  ? 230 LYS   C CG  1 
ATOM   6915 C  CD  . LYS   C  1  217 ? -22.440 22.710  6.706  1.00 80.73  ? 230 LYS   C CD  1 
ATOM   6916 C  CE  . LYS   C  1  217 ? -23.873 22.381  6.395  1.00 78.99  ? 230 LYS   C CE  1 
ATOM   6917 N  NZ  . LYS   C  1  217 ? -24.621 23.565  5.970  1.00 73.54  ? 230 LYS   C NZ  1 
ATOM   6918 N  N   . LEU   C  1  218 ? -19.960 19.337  9.953  1.00 52.85  ? 231 LEU   C N   1 
ATOM   6919 C  CA  . LEU   C  1  218 ? -20.514 18.281  10.782 1.00 58.21  ? 231 LEU   C CA  1 
ATOM   6920 C  C   . LEU   C  1  218 ? -21.688 18.816  11.606 1.00 61.99  ? 231 LEU   C C   1 
ATOM   6921 O  O   . LEU   C  1  218 ? -21.545 19.821  12.286 1.00 62.75  ? 231 LEU   C O   1 
ATOM   6922 C  CB  . LEU   C  1  218 ? -19.375 17.766  11.663 1.00 52.63  ? 231 LEU   C CB  1 
ATOM   6923 C  CG  . LEU   C  1  218 ? -19.721 16.573  12.556 1.00 57.48  ? 231 LEU   C CG  1 
ATOM   6924 C  CD1 . LEU   C  1  218 ? -20.031 15.329  11.740 1.00 64.29  ? 231 LEU   C CD1 1 
ATOM   6925 C  CD2 . LEU   C  1  218 ? -18.614 16.311  13.546 1.00 58.02  ? 231 LEU   C CD2 1 
ATOM   6926 N  N   . SER   C  1  219 ? -22.830 18.116  11.583 1.00 64.81  ? 232 SER   C N   1 
ATOM   6927 C  CA  . SER   C  1  219 ? -23.962 18.474  12.425 1.00 66.34  ? 232 SER   C CA  1 
ATOM   6928 C  C   . SER   C  1  219 ? -23.674 18.111  13.882 1.00 72.20  ? 232 SER   C C   1 
ATOM   6929 O  O   . SER   C  1  219 ? -22.831 17.261  14.168 1.00 70.69  ? 232 SER   C O   1 
ATOM   6930 C  CB  . SER   C  1  219 ? -25.240 17.821  11.951 1.00 61.63  ? 232 SER   C CB  1 
ATOM   6931 O  OG  . SER   C  1  219 ? -25.233 16.420  12.176 1.00 62.69  ? 232 SER   C OG  1 
ATOM   6932 N  N   . MET   C  1  220 ? -24.398 18.751  14.799 1.00 66.36  ? 233 MET   C N   1 
ATOM   6933 C  CA  . MET   C  1  220 ? -24.212 18.508  16.218 1.00 60.16  ? 233 MET   C CA  1 
ATOM   6934 C  C   . MET   C  1  220 ? -24.762 17.149  16.630 1.00 61.35  ? 233 MET   C C   1 
ATOM   6935 O  O   . MET   C  1  220 ? -24.235 16.540  17.561 1.00 74.82  ? 233 MET   C O   1 
ATOM   6936 C  CB  . MET   C  1  220 ? -24.868 19.626  17.029 1.00 66.66  ? 233 MET   C CB  1 
ATOM   6937 C  CG  . MET   C  1  220 ? -24.278 21.002  16.764 1.00 65.64  ? 233 MET   C CG  1 
ATOM   6938 S  SD  . MET   C  1  220 ? -22.508 21.108  17.109 1.00 69.58  ? 233 MET   C SD  1 
ATOM   6939 C  CE  . MET   C  1  220 ? -21.774 20.942  15.471 1.00 70.99  ? 233 MET   C CE  1 
ATOM   6940 N  N   . GLU   C  1  221 ? -25.796 16.666  15.929 1.00 62.35  ? 234 GLU   C N   1 
ATOM   6941 C  CA  . GLU   C  1  221 ? -26.355 15.340  16.173 1.00 69.70  ? 234 GLU   C CA  1 
ATOM   6942 C  C   . GLU   C  1  221 ? -25.305 14.271  15.863 1.00 61.51  ? 234 GLU   C C   1 
ATOM   6943 O  O   . GLU   C  1  221 ? -25.153 13.305  16.606 1.00 59.30  ? 234 GLU   C O   1 
ATOM   6944 C  CB  . GLU   C  1  221 ? -27.595 15.068  15.310 1.00 81.51  ? 234 GLU   C CB  1 
ATOM   6945 C  CG  . GLU   C  1  221 ? -28.774 16.017  15.545 1.00 93.54  ? 234 GLU   C CG  1 
ATOM   6946 C  CD  . GLU   C  1  221 ? -28.717 17.465  15.034 1.00 102.44 ? 234 GLU   C CD  1 
ATOM   6947 O  OE1 . GLU   C  1  221 ? -27.771 17.921  14.332 1.00 97.71  ? 234 GLU   C OE1 1 
ATOM   6948 O  OE2 . GLU   C  1  221 ? -29.673 18.182  15.397 1.00 111.60 ? 234 GLU   C OE2 1 
ATOM   6949 N  N   . ASP   C  1  222 ? -24.608 14.443  14.737 1.00 56.86  ? 235 ASP   C N   1 
ATOM   6950 C  CA  . ASP   C  1  222 ? -23.599 13.498  14.287 1.00 61.52  ? 235 ASP   C CA  1 
ATOM   6951 C  C   . ASP   C  1  222 ? -22.388 13.579  15.214 1.00 53.97  ? 235 ASP   C C   1 
ATOM   6952 O  O   . ASP   C  1  222 ? -21.855 12.555  15.619 1.00 48.15  ? 235 ASP   C O   1 
ATOM   6953 C  CB  . ASP   C  1  222 ? -23.244 13.716  12.820 1.00 62.96  ? 235 ASP   C CB  1 
ATOM   6954 C  CG  . ASP   C  1  222 ? -24.321 13.378  11.792 1.00 64.44  ? 235 ASP   C CG  1 
ATOM   6955 O  OD1 . ASP   C  1  222 ? -25.366 12.788  12.181 1.00 62.44  ? 235 ASP   C OD1 1 
ATOM   6956 O  OD2 . ASP   C  1  222 ? -24.111 13.736  10.615 1.00 55.29  ? 235 ASP   C OD2 1 
ATOM   6957 N  N   . ALA   C  1  223 ? -21.984 14.795  15.580 1.00 50.37  ? 236 ALA   C N   1 
ATOM   6958 C  CA  . ALA   C  1  223 ? -20.929 14.957  16.566 1.00 54.27  ? 236 ALA   C CA  1 
ATOM   6959 C  C   . ALA   C  1  223 ? -21.286 14.253  17.880 1.00 58.37  ? 236 ALA   C C   1 
ATOM   6960 O  O   . ALA   C  1  223 ? -20.464 13.514  18.418 1.00 62.19  ? 236 ALA   C O   1 
ATOM   6961 C  CB  . ALA   C  1  223 ? -20.626 16.419  16.778 1.00 52.23  ? 236 ALA   C CB  1 
ATOM   6962 N  N   . ALA   C  1  224 ? -22.504 14.443  18.401 1.00 52.95  ? 237 ALA   C N   1 
ATOM   6963 C  CA  . ALA   C  1  224 ? -22.831 13.854  19.693 1.00 52.97  ? 237 ALA   C CA  1 
ATOM   6964 C  C   . ALA   C  1  224 ? -22.792 12.340  19.568 1.00 53.36  ? 237 ALA   C C   1 
ATOM   6965 O  O   . ALA   C  1  224 ? -22.302 11.627  20.445 1.00 49.67  ? 237 ALA   C O   1 
ATOM   6966 C  CB  . ALA   C  1  224 ? -24.196 14.299  20.180 1.00 58.34  ? 237 ALA   C CB  1 
ATOM   6967 N  N   . SER   C  1  225 ? -23.343 11.865  18.451 1.00 50.87  ? 238 SER   C N   1 
ATOM   6968 C  CA  . SER   C  1  225 ? -23.453 10.441  18.215 1.00 49.23  ? 238 SER   C CA  1 
ATOM   6969 C  C   . SER   C  1  225 ? -22.070 9.796   18.333 1.00 48.82  ? 238 SER   C C   1 
ATOM   6970 O  O   . SER   C  1  225 ? -21.937 8.770   18.981 1.00 43.27  ? 238 SER   C O   1 
ATOM   6971 C  CB  . SER   C  1  225 ? -24.097 10.188  16.873 1.00 45.31  ? 238 SER   C CB  1 
ATOM   6972 O  OG  . SER   C  1  225 ? -24.278 8.806   16.657 1.00 49.56  ? 238 SER   C OG  1 
ATOM   6973 N  N   . ILE   C  1  226 ? -21.042 10.428  17.759 1.00 44.42  ? 239 ILE   C N   1 
ATOM   6974 C  CA  . ILE   C  1  226 ? -19.717 9.838   17.682 1.00 50.70  ? 239 ILE   C CA  1 
ATOM   6975 C  C   . ILE   C  1  226 ? -18.946 10.104  18.978 1.00 50.38  ? 239 ILE   C C   1 
ATOM   6976 O  O   . ILE   C  1  226 ? -18.442 9.172   19.610 1.00 47.31  ? 239 ILE   C O   1 
ATOM   6977 C  CB  . ILE   C  1  226 ? -18.978 10.348  16.428 1.00 49.67  ? 239 ILE   C CB  1 
ATOM   6978 C  CG1 . ILE   C  1  226 ? -19.648 9.822   15.169 1.00 54.71  ? 239 ILE   C CG1 1 
ATOM   6979 C  CG2 . ILE   C  1  226 ? -17.505 9.962   16.455 1.00 50.30  ? 239 ILE   C CG2 1 
ATOM   6980 C  CD1 . ILE   C  1  226 ? -19.282 10.576  13.907 1.00 51.30  ? 239 ILE   C CD1 1 
ATOM   6981 N  N   . PHE   C  1  227 ? -18.878 11.377  19.373 1.00 49.88  ? 240 PHE   C N   1 
ATOM   6982 C  CA  . PHE   C  1  227 ? -18.078 11.788  20.514 1.00 50.81  ? 240 PHE   C CA  1 
ATOM   6983 C  C   . PHE   C  1  227 ? -18.630 11.251  21.831 1.00 52.25  ? 240 PHE   C C   1 
ATOM   6984 O  O   . PHE   C  1  227 ? -17.856 10.887  22.716 1.00 56.30  ? 240 PHE   C O   1 
ATOM   6985 C  CB  . PHE   C  1  227 ? -17.995 13.307  20.615 1.00 48.39  ? 240 PHE   C CB  1 
ATOM   6986 C  CG  . PHE   C  1  227 ? -17.045 13.978  19.637 1.00 46.26  ? 240 PHE   C CG  1 
ATOM   6987 C  CD1 . PHE   C  1  227 ? -15.670 13.947  19.841 1.00 50.47  ? 240 PHE   C CD1 1 
ATOM   6988 C  CD2 . PHE   C  1  227 ? -17.523 14.719  18.571 1.00 48.97  ? 240 PHE   C CD2 1 
ATOM   6989 C  CE1 . PHE   C  1  227 ? -14.807 14.610  18.986 1.00 50.10  ? 240 PHE   C CE1 1 
ATOM   6990 C  CE2 . PHE   C  1  227 ? -16.656 15.380  17.715 1.00 51.58  ? 240 PHE   C CE2 1 
ATOM   6991 C  CZ  . PHE   C  1  227 ? -15.303 15.338  17.931 1.00 50.13  ? 240 PHE   C CZ  1 
ATOM   6992 N  N   . ARG   C  1  228 ? -19.959 11.214  21.979 1.00 54.67  ? 241 ARG   C N   1 
ATOM   6993 C  CA  . ARG   C  1  228 ? -20.549 10.760  23.225 1.00 49.64  ? 241 ARG   C CA  1 
ATOM   6994 C  C   . ARG   C  1  228 ? -20.974 9.302   23.123 1.00 51.15  ? 241 ARG   C C   1 
ATOM   6995 O  O   . ARG   C  1  228 ? -20.645 8.512   24.001 1.00 54.34  ? 241 ARG   C O   1 
ATOM   6996 C  CB  . ARG   C  1  228 ? -21.734 11.626  23.648 1.00 61.06  ? 241 ARG   C CB  1 
ATOM   6997 C  CG  . ARG   C  1  228 ? -22.354 11.202  24.973 1.00 66.53  ? 241 ARG   C CG  1 
ATOM   6998 C  CD  . ARG   C  1  228 ? -23.487 12.163  25.322 1.00 73.01  ? 241 ARG   C CD  1 
ATOM   6999 N  NE  . ARG   C  1  228 ? -24.653 11.795  24.506 1.00 72.49  ? 241 ARG   C NE  1 
ATOM   7000 C  CZ  . ARG   C  1  228 ? -25.363 12.571  23.693 1.00 75.74  ? 241 ARG   C CZ  1 
ATOM   7001 N  NH1 . ARG   C  1  228 ? -25.107 13.867  23.620 1.00 68.83  ? 241 ARG   C NH1 1 
ATOM   7002 N  NH2 . ARG   C  1  228 ? -26.337 12.035  22.974 1.00 74.77  ? 241 ARG   C NH2 1 
ATOM   7003 N  N   . ASP   C  1  229 ? -21.718 8.927   22.071 1.00 46.99  ? 242 ASP   C N   1 
ATOM   7004 C  CA  . ASP   C  1  229 ? -22.380 7.631   22.082 1.00 46.85  ? 242 ASP   C CA  1 
ATOM   7005 C  C   . ASP   C  1  229 ? -21.577 6.548   21.376 1.00 45.79  ? 242 ASP   C C   1 
ATOM   7006 O  O   . ASP   C  1  229 ? -21.945 5.381   21.463 1.00 36.16  ? 242 ASP   C O   1 
ATOM   7007 C  CB  . ASP   C  1  229 ? -23.819 7.766   21.614 1.00 59.51  ? 242 ASP   C CB  1 
ATOM   7008 C  CG  . ASP   C  1  229 ? -24.694 8.564   22.583 1.00 66.47  ? 242 ASP   C CG  1 
ATOM   7009 O  OD1 . ASP   C  1  229 ? -24.691 8.184   23.786 1.00 65.92  ? 242 ASP   C OD1 1 
ATOM   7010 O  OD2 . ASP   C  1  229 ? -25.273 9.609   22.160 1.00 63.90  ? 242 ASP   C OD2 1 
ATOM   7011 N  N   . MET   C  1  230 ? -20.458 6.920   20.722 1.00 46.68  ? 243 MET   C N   1 
ATOM   7012 C  CA  A MET   C  1  230 ? -19.594 5.959   20.060 0.50 41.39  ? 243 MET   C CA  1 
ATOM   7013 C  CA  B MET   C  1  230 ? -19.597 5.949   20.067 0.50 44.68  ? 243 MET   C CA  1 
ATOM   7014 C  C   . MET   C  1  230 ? -20.376 5.257   18.954 1.00 41.02  ? 243 MET   C C   1 
ATOM   7015 O  O   . MET   C  1  230 ? -20.209 4.046   18.740 1.00 37.88  ? 243 MET   C O   1 
ATOM   7016 C  CB  A MET   C  1  230 ? -19.070 4.925   21.058 0.50 41.79  ? 243 MET   C CB  1 
ATOM   7017 C  CB  B MET   C  1  230 ? -19.117 4.872   21.051 0.50 50.28  ? 243 MET   C CB  1 
ATOM   7018 C  CG  A MET   C  1  230 ? -18.445 5.521   22.309 0.50 39.39  ? 243 MET   C CG  1 
ATOM   7019 C  CG  B MET   C  1  230 ? -18.503 5.409   22.334 0.50 53.18  ? 243 MET   C CG  1 
ATOM   7020 S  SD  A MET   C  1  230 ? -17.972 4.253   23.501 0.50 38.52  ? 243 MET   C SD  1 
ATOM   7021 S  SD  B MET   C  1  230 ? -18.160 4.061   23.483 0.50 60.86  ? 243 MET   C SD  1 
ATOM   7022 C  CE  A MET   C  1  230 ? -17.675 5.312   24.926 0.50 36.85  ? 243 MET   C CE  1 
ATOM   7023 C  CE  B MET   C  1  230 ? -19.848 3.612   23.913 0.50 69.25  ? 243 MET   C CE  1 
ATOM   7024 N  N   . ARG   C  1  231 ? -21.219 6.033   18.254 1.00 37.60  ? 244 ARG   C N   1 
ATOM   7025 C  CA  A ARG   C  1  231 ? -22.168 5.499   17.288 0.50 42.26  ? 244 ARG   C CA  1 
ATOM   7026 C  CA  B ARG   C  1  231 ? -22.135 5.476   17.277 0.50 41.04  ? 244 ARG   C CA  1 
ATOM   7027 C  C   . ARG   C  1  231 ? -22.041 6.266   15.980 1.00 39.17  ? 244 ARG   C C   1 
ATOM   7028 O  O   . ARG   C  1  231 ? -22.058 7.499   15.972 1.00 36.10  ? 244 ARG   C O   1 
ATOM   7029 C  CB  A ARG   C  1  231 ? -23.602 5.642   17.823 0.50 45.38  ? 244 ARG   C CB  1 
ATOM   7030 C  CB  B ARG   C  1  231 ? -23.568 5.467   17.824 0.50 42.32  ? 244 ARG   C CB  1 
ATOM   7031 C  CG  A ARG   C  1  231 ? -24.695 4.980   16.996 0.50 46.92  ? 244 ARG   C CG  1 
ATOM   7032 C  CG  B ARG   C  1  231 ? -24.568 4.716   16.956 0.50 41.69  ? 244 ARG   C CG  1 
ATOM   7033 C  CD  A ARG   C  1  231 ? -26.085 5.142   17.645 0.50 49.35  ? 244 ARG   C CD  1 
ATOM   7034 C  CD  B ARG   C  1  231 ? -25.854 4.405   17.719 0.50 42.23  ? 244 ARG   C CD  1 
ATOM   7035 N  NE  A ARG   C  1  231 ? -26.992 3.995   17.464 0.50 50.00  ? 244 ARG   C NE  1 
ATOM   7036 N  NE  B ARG   C  1  231 ? -26.444 5.573   18.392 0.50 41.17  ? 244 ARG   C NE  1 
ATOM   7037 C  CZ  A ARG   C  1  231 ? -27.704 3.400   18.427 0.50 48.05  ? 244 ARG   C CZ  1 
ATOM   7038 C  CZ  B ARG   C  1  231 ? -26.752 5.643   19.690 0.50 40.41  ? 244 ARG   C CZ  1 
ATOM   7039 N  NH1 A ARG   C  1  231 ? -27.713 3.881   19.663 0.50 51.05  ? 244 ARG   C NH1 1 
ATOM   7040 N  NH1 B ARG   C  1  231 ? -26.538 4.620   20.501 0.50 40.72  ? 244 ARG   C NH1 1 
ATOM   7041 N  NH2 A ARG   C  1  231 ? -28.417 2.326   18.153 0.50 42.40  ? 244 ARG   C NH2 1 
ATOM   7042 N  NH2 B ARG   C  1  231 ? -27.294 6.741   20.180 0.50 41.57  ? 244 ARG   C NH2 1 
ATOM   7043 N  N   . PHE   C  1  232 ? -21.941 5.529   14.877 1.00 42.36  ? 245 PHE   C N   1 
ATOM   7044 C  CA  . PHE   C  1  232 ? -22.015 6.148   13.559 1.00 41.75  ? 245 PHE   C CA  1 
ATOM   7045 C  C   . PHE   C  1  232 ? -23.390 6.772   13.347 1.00 44.28  ? 245 PHE   C C   1 
ATOM   7046 O  O   . PHE   C  1  232 ? -24.397 6.213   13.770 1.00 42.96  ? 245 PHE   C O   1 
ATOM   7047 C  CB  . PHE   C  1  232 ? -21.829 5.096   12.467 1.00 39.47  ? 245 PHE   C CB  1 
ATOM   7048 C  CG  . PHE   C  1  232 ? -20.406 4.602   12.282 1.00 37.78  ? 245 PHE   C CG  1 
ATOM   7049 C  CD1 . PHE   C  1  232 ? -19.412 5.476   11.862 1.00 36.28  ? 245 PHE   C CD1 1 
ATOM   7050 C  CD2 . PHE   C  1  232 ? -20.090 3.257   12.457 1.00 41.48  ? 245 PHE   C CD2 1 
ATOM   7051 C  CE1 . PHE   C  1  232 ? -18.128 5.020   11.664 1.00 39.88  ? 245 PHE   C CE1 1 
ATOM   7052 C  CE2 . PHE   C  1  232 ? -18.797 2.811   12.251 1.00 41.65  ? 245 PHE   C CE2 1 
ATOM   7053 C  CZ  . PHE   C  1  232 ? -17.825 3.690   11.855 1.00 38.25  ? 245 PHE   C CZ  1 
ATOM   7054 N  N   . PRO   C  1  233 ? -23.493 7.927   12.665 1.00 47.59  ? 246 PRO   C N   1 
ATOM   7055 C  CA  . PRO   C  1  233 ? -24.781 8.407   12.166 1.00 51.80  ? 246 PRO   C CA  1 
ATOM   7056 C  C   . PRO   C  1  233 ? -25.498 7.314   11.384 1.00 51.47  ? 246 PRO   C C   1 
ATOM   7057 O  O   . PRO   C  1  233 ? -24.860 6.414   10.826 1.00 45.88  ? 246 PRO   C O   1 
ATOM   7058 C  CB  . PRO   C  1  233 ? -24.405 9.608   11.283 1.00 53.56  ? 246 PRO   C CB  1 
ATOM   7059 C  CG  . PRO   C  1  233 ? -23.087 10.084  11.857 1.00 53.67  ? 246 PRO   C CG  1 
ATOM   7060 C  CD  . PRO   C  1  233 ? -22.388 8.841   12.365 1.00 52.02  ? 246 PRO   C CD  1 
ATOM   7061 N  N   . ASP   C  1  234 ? -26.832 7.380   11.362 1.00 56.20  ? 247 ASP   C N   1 
ATOM   7062 C  CA  . ASP   C  1  234 ? -27.612 6.444   10.562 1.00 62.40  ? 247 ASP   C CA  1 
ATOM   7063 C  C   . ASP   C  1  234 ? -27.156 6.533   9.111  1.00 50.25  ? 247 ASP   C C   1 
ATOM   7064 O  O   . ASP   C  1  234 ? -26.912 7.623   8.606  1.00 39.59  ? 247 ASP   C O   1 
ATOM   7065 C  CB  . ASP   C  1  234 ? -29.113 6.695   10.655 1.00 72.14  ? 247 ASP   C CB  1 
ATOM   7066 C  CG  . ASP   C  1  234 ? -29.689 6.670   12.066 1.00 85.04  ? 247 ASP   C CG  1 
ATOM   7067 O  OD1 . ASP   C  1  234 ? -29.169 5.874   12.873 1.00 93.61  ? 247 ASP   C OD1 1 
ATOM   7068 O  OD2 . ASP   C  1  234 ? -30.630 7.452   12.352 1.00 88.80  ? 247 ASP   C OD2 1 
ATOM   7069 N  N   . ASP   C  1  235 ? -26.995 5.370   8.473  1.00 50.64  ? 248 ASP   C N   1 
ATOM   7070 C  CA  . ASP   C  1  235 ? -26.664 5.320   7.058  1.00 62.60  ? 248 ASP   C CA  1 
ATOM   7071 C  C   . ASP   C  1  235 ? -25.324 6.018   6.758  1.00 54.80  ? 248 ASP   C C   1 
ATOM   7072 O  O   . ASP   C  1  235 ? -25.132 6.575   5.682  1.00 45.04  ? 248 ASP   C O   1 
ATOM   7073 C  CB  . ASP   C  1  235 ? -27.810 5.900   6.237  1.00 59.85  ? 248 ASP   C CB  1 
ATOM   7074 C  CG  . ASP   C  1  235 ? -27.712 5.584   4.753  1.00 61.92  ? 248 ASP   C CG  1 
ATOM   7075 O  OD1 . ASP   C  1  235 ? -27.577 4.378   4.451  1.00 53.46  ? 248 ASP   C OD1 1 
ATOM   7076 O  OD2 . ASP   C  1  235 ? -27.716 6.542   3.935  1.00 58.14  ? 248 ASP   C OD2 1 
ATOM   7077 N  N   . PHE   C  1  236 ? -24.382 5.994   7.703  1.00 49.58  ? 249 PHE   C N   1 
ATOM   7078 C  CA  . PHE   C  1  236 ? -23.143 6.733   7.530  1.00 46.21  ? 249 PHE   C CA  1 
ATOM   7079 C  C   . PHE   C  1  236 ? -22.272 6.090   6.449  1.00 41.53  ? 249 PHE   C C   1 
ATOM   7080 O  O   . PHE   C  1  236 ? -22.013 4.881   6.456  1.00 36.17  ? 249 PHE   C O   1 
ATOM   7081 C  CB  . PHE   C  1  236 ? -22.317 6.736   8.813  1.00 45.36  ? 249 PHE   C CB  1 
ATOM   7082 C  CG  . PHE   C  1  236 ? -21.031 7.525   8.704  1.00 38.76  ? 249 PHE   C CG  1 
ATOM   7083 C  CD1 . PHE   C  1  236 ? -21.069 8.903   8.625  1.00 40.07  ? 249 PHE   C CD1 1 
ATOM   7084 C  CD2 . PHE   C  1  236 ? -19.796 6.891   8.692  1.00 42.96  ? 249 PHE   C CD2 1 
ATOM   7085 C  CE1 . PHE   C  1  236 ? -19.901 9.635   8.551  1.00 40.26  ? 249 PHE   C CE1 1 
ATOM   7086 C  CE2 . PHE   C  1  236 ? -18.626 7.630   8.602  1.00 38.04  ? 249 PHE   C CE2 1 
ATOM   7087 C  CZ  . PHE   C  1  236 ? -18.681 8.998   8.526  1.00 35.79  ? 249 PHE   C CZ  1 
ATOM   7088 N  N   . HIS   C  1  237 ? -21.799 6.935   5.537  1.00 40.96  ? 250 HIS   C N   1 
ATOM   7089 C  CA  . HIS   C  1  237 ? -20.871 6.509   4.506  1.00 43.84  ? 250 HIS   C CA  1 
ATOM   7090 C  C   . HIS   C  1  237 ? -19.524 7.162   4.761  1.00 38.42  ? 250 HIS   C C   1 
ATOM   7091 O  O   . HIS   C  1  237 ? -19.448 8.379   4.919  1.00 34.09  ? 250 HIS   C O   1 
ATOM   7092 C  CB  . HIS   C  1  237 ? -21.367 6.899   3.108  1.00 50.78  ? 250 HIS   C CB  1 
ATOM   7093 C  CG  . HIS   C  1  237 ? -22.528 6.098   2.629  1.00 58.45  ? 250 HIS   C CG  1 
ATOM   7094 N  ND1 . HIS   C  1  237 ? -23.659 5.875   3.383  1.00 62.40  ? 250 HIS   C ND1 1 
ATOM   7095 C  CD2 . HIS   C  1  237 ? -22.725 5.470   1.470  1.00 64.20  ? 250 HIS   C CD2 1 
ATOM   7096 C  CE1 . HIS   C  1  237 ? -24.502 5.124   2.695  1.00 70.03  ? 250 HIS   C CE1 1 
ATOM   7097 N  NE2 . HIS   C  1  237 ? -23.951 4.863   1.536  1.00 69.62  ? 250 HIS   C NE2 1 
ATOM   7098 N  N   . ARG   C  1  238 ? -18.463 6.353   4.759  1.00 37.75  ? 251 ARG   C N   1 
ATOM   7099 C  CA  . ARG   C  1  238 ? -17.143 6.875   5.072  1.00 33.54  ? 251 ARG   C CA  1 
ATOM   7100 C  C   . ARG   C  1  238 ? -16.670 7.819   3.973  1.00 34.05  ? 251 ARG   C C   1 
ATOM   7101 O  O   . ARG   C  1  238 ? -17.217 7.846   2.872  1.00 34.12  ? 251 ARG   C O   1 
ATOM   7102 C  CB  . ARG   C  1  238 ? -16.132 5.739   5.239  1.00 36.36  ? 251 ARG   C CB  1 
ATOM   7103 C  CG  . ARG   C  1  238 ? -15.870 4.993   3.938  1.00 39.07  ? 251 ARG   C CG  1 
ATOM   7104 C  CD  . ARG   C  1  238 ? -14.894 3.857   4.131  1.00 38.81  ? 251 ARG   C CD  1 
ATOM   7105 N  NE  . ARG   C  1  238 ? -14.368 3.466   2.823  1.00 39.78  ? 251 ARG   C NE  1 
ATOM   7106 C  CZ  . ARG   C  1  238 ? -13.661 2.400   2.568  1.00 36.92  ? 251 ARG   C CZ  1 
ATOM   7107 N  NH1 . ARG   C  1  238 ? -13.318 1.572   3.537  1.00 39.83  ? 251 ARG   C NH1 1 
ATOM   7108 N  NH2 . ARG   C  1  238 ? -13.343 2.138   1.309  1.00 41.98  ? 251 ARG   C NH2 1 
ATOM   7109 N  N   . SER   C  1  239 ? -15.627 8.584   4.297  1.00 35.92  ? 252 SER   C N   1 
ATOM   7110 C  CA  . SER   C  1  239 ? -14.928 9.431   3.349  1.00 35.70  ? 252 SER   C CA  1 
ATOM   7111 C  C   . SER   C  1  239 ? -14.713 8.715   2.016  1.00 37.80  ? 252 SER   C C   1 
ATOM   7112 O  O   . SER   C  1  239 ? -14.489 7.506   1.975  1.00 38.66  ? 252 SER   C O   1 
ATOM   7113 C  CB  . SER   C  1  239 ? -13.613 9.852   3.921  1.00 34.80  ? 252 SER   C CB  1 
ATOM   7114 O  OG  . SER   C  1  239 ? -12.850 10.580  2.966  1.00 34.68  ? 252 SER   C OG  1 
ATOM   7115 N  N   . ALA   C  1  240 ? -14.783 9.479   0.924  1.00 36.65  ? 253 ALA   C N   1 
ATOM   7116 C  CA  . ALA   C  1  240 ? -14.711 8.907   -0.407 1.00 38.03  ? 253 ALA   C CA  1 
ATOM   7117 C  C   . ALA   C  1  240 ? -13.256 8.723   -0.824 1.00 37.93  ? 253 ALA   C C   1 
ATOM   7118 O  O   . ALA   C  1  240 ? -13.017 8.102   -1.845 1.00 42.02  ? 253 ALA   C O   1 
ATOM   7119 C  CB  . ALA   C  1  240 ? -15.459 9.766   -1.398 1.00 34.07  ? 253 ALA   C CB  1 
ATOM   7120 N  N   . VAL   C  1  241 ? -12.311 9.290   -0.059 1.00 38.42  ? 254 VAL   C N   1 
ATOM   7121 C  CA  . VAL   C  1  241 ? -10.882 9.108   -0.290 1.00 37.78  ? 254 VAL   C CA  1 
ATOM   7122 C  C   . VAL   C  1  241 ? -10.192 8.867   1.048  1.00 38.79  ? 254 VAL   C C   1 
ATOM   7123 O  O   . VAL   C  1  241 ? -10.617 9.405   2.071  1.00 37.50  ? 254 VAL   C O   1 
ATOM   7124 C  CB  . VAL   C  1  241 ? -10.218 10.307  -0.988 1.00 39.74  ? 254 VAL   C CB  1 
ATOM   7125 C  CG1 . VAL   C  1  241 ? -10.775 10.534  -2.371 1.00 48.44  ? 254 VAL   C CG1 1 
ATOM   7126 C  CG2 . VAL   C  1  241 ? -10.380 11.589  -0.192 1.00 43.25  ? 254 VAL   C CG2 1 
ATOM   7127 N  N   . PRO   C  1  242 ? -9.075  8.109   1.078  1.00 38.67  ? 255 PRO   C N   1 
ATOM   7128 C  CA  . PRO   C  1  242 ? -8.259  8.009   2.283  1.00 38.40  ? 255 PRO   C CA  1 
ATOM   7129 C  C   . PRO   C  1  242 ? -7.950  9.423   2.755  1.00 37.18  ? 255 PRO   C C   1 
ATOM   7130 O  O   . PRO   C  1  242 ? -7.659  10.300  1.946  1.00 36.08  ? 255 PRO   C O   1 
ATOM   7131 C  CB  . PRO   C  1  242 ? -7.003  7.260   1.845  1.00 37.22  ? 255 PRO   C CB  1 
ATOM   7132 C  CG  . PRO   C  1  242 ? -7.461  6.471   0.658  1.00 38.36  ? 255 PRO   C CG  1 
ATOM   7133 C  CD  . PRO   C  1  242 ? -8.492  7.363   -0.043 1.00 37.92  ? 255 PRO   C CD  1 
ATOM   7134 N  N   . ALA   C  1  243 ? -8.089  9.654   4.062  1.00 39.73  ? 256 ALA   C N   1 
ATOM   7135 C  CA  . ALA   C  1  243 ? -7.871  10.985  4.581  1.00 39.36  ? 256 ALA   C CA  1 
ATOM   7136 C  C   . ALA   C  1  243 ? -7.312  10.906  5.990  1.00 36.83  ? 256 ALA   C C   1 
ATOM   7137 O  O   . ALA   C  1  243 ? -7.379  9.869   6.641  1.00 34.42  ? 256 ALA   C O   1 
ATOM   7138 C  CB  . ALA   C  1  243 ? -9.168  11.752  4.538  1.00 42.81  ? 256 ALA   C CB  1 
ATOM   7139 N  N   . SER   C  1  244 ? -6.793  12.046  6.435  1.00 34.76  ? 257 SER   C N   1 
ATOM   7140 C  CA  . SER   C  1  244 ? -6.322  12.208  7.787  1.00 34.65  ? 257 SER   C CA  1 
ATOM   7141 C  C   . SER   C  1  244 ? -6.426  13.678  8.176  1.00 36.67  ? 257 SER   C C   1 
ATOM   7142 O  O   . SER   C  1  244 ? -7.501  14.153  8.487  1.00 36.98  ? 257 SER   C O   1 
ATOM   7143 C  CB  . SER   C  1  244 ? -4.931  11.676  7.907  1.00 34.34  ? 257 SER   C CB  1 
ATOM   7144 O  OG  . SER   C  1  244 ? -4.091  12.270  6.926  1.00 30.95  ? 257 SER   C OG  1 
ATOM   7145 N  N   . ASN   C  1  245 ? -5.315  14.412  8.069  1.00 42.89  ? 258 ASN   C N   1 
ATOM   7146 C  CA  . ASN   C  1  245 ? -5.169  15.691  8.740  1.00 40.03  ? 258 ASN   C CA  1 
ATOM   7147 C  C   . ASN   C  1  245 ? -5.120  16.850  7.749  1.00 41.77  ? 258 ASN   C C   1 
ATOM   7148 O  O   . ASN   C  1  245 ? -4.556  17.889  8.074  1.00 42.11  ? 258 ASN   C O   1 
ATOM   7149 C  CB  . ASN   C  1  245 ? -3.916  15.691  9.603  1.00 38.77  ? 258 ASN   C CB  1 
ATOM   7150 C  CG  . ASN   C  1  245 ? -2.648  15.692  8.785  1.00 39.79  ? 258 ASN   C CG  1 
ATOM   7151 O  OD1 . ASN   C  1  245 ? -2.652  15.355  7.599  1.00 36.77  ? 258 ASN   C OD1 1 
ATOM   7152 N  ND2 . ASN   C  1  245 ? -1.545  16.057  9.408  1.00 37.80  ? 258 ASN   C ND2 1 
ATOM   7153 N  N   . GLU   C  1  246 ? -5.728  16.688  6.565  1.00 47.28  ? 259 GLU   C N   1 
ATOM   7154 C  CA  . GLU   C  1  246 ? -5.878  17.783  5.617  1.00 51.33  ? 259 GLU   C CA  1 
ATOM   7155 C  C   . GLU   C  1  246 ? -6.547  18.969  6.312  1.00 51.44  ? 259 GLU   C C   1 
ATOM   7156 O  O   . GLU   C  1  246 ? -7.591  18.815  6.941  1.00 48.92  ? 259 GLU   C O   1 
ATOM   7157 C  CB  . GLU   C  1  246 ? -6.719  17.410  4.390  1.00 51.82  ? 259 GLU   C CB  1 
ATOM   7158 C  CG  . GLU   C  1  246 ? -6.100  16.324  3.510  1.00 55.15  ? 259 GLU   C CG  1 
ATOM   7159 C  CD  . GLU   C  1  246 ? -6.180  14.880  4.001  1.00 53.56  ? 259 GLU   C CD  1 
ATOM   7160 O  OE1 . GLU   C  1  246 ? -6.786  14.610  5.068  1.00 52.47  ? 259 GLU   C OE1 1 
ATOM   7161 O  OE2 . GLU   C  1  246 ? -5.594  14.022  3.324  1.00 47.65  ? 259 GLU   C OE2 1 
ATOM   7162 N  N   . GLY   C  1  247 ? -5.915  20.146  6.197  1.00 50.22  ? 260 GLY   C N   1 
ATOM   7163 C  CA  . GLY   C  1  247 ? -6.453  21.384  6.739  1.00 49.98  ? 260 GLY   C CA  1 
ATOM   7164 C  C   . GLY   C  1  247 ? -5.853  21.755  8.096  1.00 52.17  ? 260 GLY   C C   1 
ATOM   7165 O  O   . GLY   C  1  247 ? -6.098  22.855  8.590  1.00 50.77  ? 260 GLY   C O   1 
ATOM   7166 N  N   . ALA   C  1  248 ? -5.061  20.861  8.703  1.00 52.98  ? 261 ALA   C N   1 
ATOM   7167 C  CA  . ALA   C  1  248 ? -4.496  21.133  10.020 1.00 53.40  ? 261 ALA   C CA  1 
ATOM   7168 C  C   . ALA   C  1  248 ? -3.597  22.368  9.974  1.00 52.28  ? 261 ALA   C C   1 
ATOM   7169 O  O   . ALA   C  1  248 ? -3.507  23.093  10.962 1.00 51.05  ? 261 ALA   C O   1 
ATOM   7170 C  CB  . ALA   C  1  248 ? -3.722  19.935  10.543 1.00 53.00  ? 261 ALA   C CB  1 
ATOM   7171 N  N   . ASP   C  1  249 ? -2.910  22.559  8.839  1.00 49.40  ? 262 ASP   C N   1 
ATOM   7172 C  CA  . ASP   C  1  249 ? -2.076  23.725  8.571  1.00 62.73  ? 262 ASP   C CA  1 
ATOM   7173 C  C   . ASP   C  1  249 ? -2.877  25.024  8.739  1.00 66.63  ? 262 ASP   C C   1 
ATOM   7174 O  O   . ASP   C  1  249 ? -2.409  25.983  9.345  1.00 63.00  ? 262 ASP   C O   1 
ATOM   7175 C  CB  . ASP   C  1  249 ? -1.433  23.649  7.186  1.00 67.10  ? 262 ASP   C CB  1 
ATOM   7176 C  CG  . ASP   C  1  249 ? -2.351  23.426  5.977  1.00 78.07  ? 262 ASP   C CG  1 
ATOM   7177 O  OD1 . ASP   C  1  249 ? -3.519  23.018  6.153  1.00 78.44  ? 262 ASP   C OD1 1 
ATOM   7178 O  OD2 . ASP   C  1  249 ? -1.898  23.658  4.834  1.00 80.55  ? 262 ASP   C OD2 1 
ATOM   7179 N  N   . GLN   C  1  250 ? -4.097  25.054  8.202  1.00 68.84  ? 263 GLN   C N   1 
ATOM   7180 C  CA  . GLN   C  1  250 ? -4.918  26.249  8.251  1.00 65.89  ? 263 GLN   C CA  1 
ATOM   7181 C  C   . GLN   C  1  250 ? -5.426  26.507  9.663  1.00 61.22  ? 263 GLN   C C   1 
ATOM   7182 O  O   . GLN   C  1  250 ? -5.624  27.657  10.026 1.00 62.03  ? 263 GLN   C O   1 
ATOM   7183 C  CB  . GLN   C  1  250 ? -6.095  26.138  7.288  1.00 71.17  ? 263 GLN   C CB  1 
ATOM   7184 C  CG  . GLN   C  1  250 ? -5.674  26.183  5.823  1.00 67.81  ? 263 GLN   C CG  1 
ATOM   7185 C  CD  . GLN   C  1  250 ? -6.850  25.929  4.914  1.00 75.01  ? 263 GLN   C CD  1 
ATOM   7186 O  OE1 . GLN   C  1  250 ? -7.848  26.656  4.961  1.00 71.53  ? 263 GLN   C OE1 1 
ATOM   7187 N  NE2 . GLN   C  1  250 ? -6.758  24.870  4.119  1.00 77.65  ? 263 GLN   C NE2 1 
ATOM   7188 N  N   . VAL   C  1  251 ? -5.640  25.449  10.448 1.00 59.81  ? 264 VAL   C N   1 
ATOM   7189 C  CA  . VAL   C  1  251 ? -6.094  25.605  11.819 1.00 58.86  ? 264 VAL   C CA  1 
ATOM   7190 C  C   . VAL   C  1  251 ? -4.999  26.306  12.619 1.00 58.01  ? 264 VAL   C C   1 
ATOM   7191 O  O   . VAL   C  1  251 ? -5.281  27.195  13.416 1.00 65.27  ? 264 VAL   C O   1 
ATOM   7192 C  CB  . VAL   C  1  251 ? -6.506  24.251  12.430 1.00 59.72  ? 264 VAL   C CB  1 
ATOM   7193 C  CG1 . VAL   C  1  251 ? -6.691  24.313  13.947 1.00 63.94  ? 264 VAL   C CG1 1 
ATOM   7194 C  CG2 . VAL   C  1  251 ? -7.776  23.723  11.777 1.00 59.67  ? 264 VAL   C CG2 1 
ATOM   7195 N  N   . LEU   C  1  252 ? -3.746  25.904  12.401 1.00 62.22  ? 265 LEU   C N   1 
ATOM   7196 C  CA  . LEU   C  1  252 ? -2.622  26.544  13.061 1.00 61.19  ? 265 LEU   C CA  1 
ATOM   7197 C  C   . LEU   C  1  252 ? -2.478  27.986  12.581 1.00 69.87  ? 265 LEU   C C   1 
ATOM   7198 O  O   . LEU   C  1  252 ? -2.194  28.874  13.381 1.00 68.31  ? 265 LEU   C O   1 
ATOM   7199 C  CB  . LEU   C  1  252 ? -1.327  25.778  12.823 1.00 53.28  ? 265 LEU   C CB  1 
ATOM   7200 C  CG  . LEU   C  1  252 ? -0.089  26.365  13.507 1.00 55.00  ? 265 LEU   C CG  1 
ATOM   7201 C  CD1 . LEU   C  1  252 ? -0.214  26.195  15.016 1.00 58.91  ? 265 LEU   C CD1 1 
ATOM   7202 C  CD2 . LEU   C  1  252 ? 1.185   25.729  12.992 1.00 56.84  ? 265 LEU   C CD2 1 
ATOM   7203 N  N   . ALA   C  1  253 ? -2.663  28.218  11.277 1.00 73.92  ? 266 ALA   C N   1 
ATOM   7204 C  CA  . ALA   C  1  253 ? -2.457  29.542  10.708 1.00 78.29  ? 266 ALA   C CA  1 
ATOM   7205 C  C   . ALA   C  1  253 ? -3.480  30.554  11.249 1.00 75.86  ? 266 ALA   C C   1 
ATOM   7206 O  O   . ALA   C  1  253 ? -3.153  31.720  11.422 1.00 71.89  ? 266 ALA   C O   1 
ATOM   7207 C  CB  . ALA   C  1  253 ? -2.479  29.457  9.196  1.00 75.87  ? 266 ALA   C CB  1 
ATOM   7208 N  N   . ALA   C  1  254 ? -4.708  30.117  11.552 1.00 77.58  ? 267 ALA   C N   1 
ATOM   7209 C  CA  . ALA   C  1  254 ? -5.741  30.993  12.097 1.00 80.31  ? 267 ALA   C CA  1 
ATOM   7210 C  C   . ALA   C  1  254 ? -5.325  31.621  13.431 1.00 83.14  ? 267 ALA   C C   1 
ATOM   7211 O  O   . ALA   C  1  254 ? -5.745  32.731  13.743 1.00 85.13  ? 267 ALA   C O   1 
ATOM   7212 C  CB  . ALA   C  1  254 ? -7.039  30.224  12.256 1.00 79.11  ? 267 ALA   C CB  1 
ATOM   7213 N  N   . HIS   C  1  255 ? -4.551  30.898  14.250 1.00 87.25  ? 268 HIS   C N   1 
ATOM   7214 C  CA  . HIS   C  1  255 ? -4.065  31.419  15.523 1.00 82.92  ? 268 HIS   C CA  1 
ATOM   7215 C  C   . HIS   C  1  255 ? -2.681  30.838  15.814 1.00 77.68  ? 268 HIS   C C   1 
ATOM   7216 O  O   . HIS   C  1  255 ? -2.540  29.888  16.588 1.00 87.07  ? 268 HIS   C O   1 
ATOM   7217 C  CB  . HIS   C  1  255 ? -5.057  31.121  16.655 1.00 90.00  ? 268 HIS   C CB  1 
ATOM   7218 C  CG  . HIS   C  1  255 ? -6.328  31.906  16.618 1.00 98.45  ? 268 HIS   C CG  1 
ATOM   7219 N  ND1 . HIS   C  1  255 ? -6.399  33.228  17.002 1.00 93.99  ? 268 HIS   C ND1 1 
ATOM   7220 C  CD2 . HIS   C  1  255 ? -7.576  31.555  16.255 1.00 105.12 ? 268 HIS   C CD2 1 
ATOM   7221 C  CE1 . HIS   C  1  255 ? -7.649  33.648  16.874 1.00 97.88  ? 268 HIS   C CE1 1 
ATOM   7222 N  NE2 . HIS   C  1  255 ? -8.384  32.649  16.426 1.00 99.53  ? 268 HIS   C NE2 1 
ATOM   7223 N  N   . PRO   C  1  256 ? -1.620  31.367  15.167 1.00 66.25  ? 269 PRO   C N   1 
ATOM   7224 C  CA  . PRO   C  1  256 ? -0.269  30.827  15.309 1.00 65.33  ? 269 PRO   C CA  1 
ATOM   7225 C  C   . PRO   C  1  256 ? 0.096   30.583  16.763 1.00 70.18  ? 269 PRO   C C   1 
ATOM   7226 O  O   . PRO   C  1  256 ? -0.212  31.393  17.632 1.00 79.51  ? 269 PRO   C O   1 
ATOM   7227 C  CB  . PRO   C  1  256 ? 0.622   31.874  14.654 1.00 61.39  ? 269 PRO   C CB  1 
ATOM   7228 C  CG  . PRO   C  1  256 ? -0.272  32.431  13.571 1.00 65.03  ? 269 PRO   C CG  1 
ATOM   7229 C  CD  . PRO   C  1  256 ? -1.673  32.475  14.206 1.00 65.47  ? 269 PRO   C CD  1 
ATOM   7230 N  N   . TRP   C  1  257 ? 0.744   29.442  16.998 1.00 66.04  ? 270 TRP   C N   1 
ATOM   7231 C  CA  . TRP   C  1  257 ? 1.025   29.002  18.346 1.00 66.24  ? 270 TRP   C CA  1 
ATOM   7232 C  C   . TRP   C  1  257 ? 2.302   28.175  18.367 1.00 63.66  ? 270 TRP   C C   1 
ATOM   7233 O  O   . TRP   C  1  257 ? 2.638   27.508  17.388 1.00 63.63  ? 270 TRP   C O   1 
ATOM   7234 C  CB  . TRP   C  1  257 ? -0.162  28.217  18.905 1.00 69.86  ? 270 TRP   C CB  1 
ATOM   7235 C  CG  . TRP   C  1  257 ? -0.051  28.041  20.388 1.00 76.31  ? 270 TRP   C CG  1 
ATOM   7236 C  CD1 . TRP   C  1  257 ? 0.337   26.926  21.062 1.00 81.10  ? 270 TRP   C CD1 1 
ATOM   7237 C  CD2 . TRP   C  1  257 ? -0.257  29.066  21.378 1.00 80.83  ? 270 TRP   C CD2 1 
ATOM   7238 N  NE1 . TRP   C  1  257 ? 0.337   27.167  22.408 1.00 85.01  ? 270 TRP   C NE1 1 
ATOM   7239 C  CE2 . TRP   C  1  257 ? -0.019  28.471  22.632 1.00 85.46  ? 270 TRP   C CE2 1 
ATOM   7240 C  CE3 . TRP   C  1  257 ? -0.638  30.409  21.326 1.00 80.01  ? 270 TRP   C CE3 1 
ATOM   7241 C  CZ2 . TRP   C  1  257 ? -0.136  29.185  23.820 1.00 90.66  ? 270 TRP   C CZ2 1 
ATOM   7242 C  CZ3 . TRP   C  1  257 ? -0.760  31.113  22.501 1.00 83.00  ? 270 TRP   C CZ3 1 
ATOM   7243 C  CH2 . TRP   C  1  257 ? -0.505  30.508  23.730 1.00 88.17  ? 270 TRP   C CH2 1 
ATOM   7244 N  N   . VAL   C  1  258 ? 2.988   28.224  19.511 1.00 63.59  ? 271 VAL   C N   1 
ATOM   7245 C  CA  . VAL   C  1  258 ? 4.315   27.653  19.628 1.00 67.47  ? 271 VAL   C CA  1 
ATOM   7246 C  C   . VAL   C  1  258 ? 4.280   26.618  20.743 1.00 64.13  ? 271 VAL   C C   1 
ATOM   7247 O  O   . VAL   C  1  258 ? 3.701   26.869  21.804 1.00 63.66  ? 271 VAL   C O   1 
ATOM   7248 C  CB  . VAL   C  1  258 ? 5.355   28.758  19.890 1.00 72.06  ? 271 VAL   C CB  1 
ATOM   7249 C  CG1 . VAL   C  1  258 ? 6.748   28.198  20.165 1.00 78.45  ? 271 VAL   C CG1 1 
ATOM   7250 C  CG2 . VAL   C  1  258 ? 5.403   29.744  18.730 1.00 72.81  ? 271 VAL   C CG2 1 
ATOM   7251 N  N   . PRO   C  1  259 ? 4.874   25.422  20.534 1.00 58.61  ? 272 PRO   C N   1 
ATOM   7252 C  CA  . PRO   C  1  259 ? 4.872   24.400  21.575 1.00 63.80  ? 272 PRO   C CA  1 
ATOM   7253 C  C   . PRO   C  1  259 ? 5.461   24.962  22.864 1.00 59.53  ? 272 PRO   C C   1 
ATOM   7254 O  O   . PRO   C  1  259 ? 6.306   25.845  22.821 1.00 54.89  ? 272 PRO   C O   1 
ATOM   7255 C  CB  . PRO   C  1  259 ? 5.714   23.252  20.977 1.00 66.81  ? 272 PRO   C CB  1 
ATOM   7256 C  CG  . PRO   C  1  259 ? 6.448   23.880  19.809 1.00 61.00  ? 272 PRO   C CG  1 
ATOM   7257 C  CD  . PRO   C  1  259 ? 5.543   24.978  19.304 1.00 58.01  ? 272 PRO   C CD  1 
ATOM   7258 N  N   . GLY   C  1  260 ? 4.993   24.440  23.993 1.00 54.14  ? 273 GLY   C N   1 
ATOM   7259 C  CA  . GLY   C  1  260 ? 5.480   24.838  25.297 1.00 55.04  ? 273 GLY   C CA  1 
ATOM   7260 C  C   . GLY   C  1  260 ? 4.555   24.304  26.389 1.00 58.63  ? 273 GLY   C C   1 
ATOM   7261 O  O   . GLY   C  1  260 ? 3.916   23.262  26.220 1.00 64.00  ? 273 GLY   C O   1 
ATOM   7262 N  N   . GLY   C  1  261 ? 4.494   25.031  27.507 1.00 54.45  ? 274 GLY   C N   1 
ATOM   7263 C  CA  . GLY   C  1  261 ? 3.690   24.612  28.643 1.00 62.74  ? 274 GLY   C CA  1 
ATOM   7264 C  C   . GLY   C  1  261 ? 3.677   25.670  29.744 1.00 63.76  ? 274 GLY   C C   1 
ATOM   7265 O  O   . GLY   C  1  261 ? 4.427   26.645  29.698 1.00 53.61  ? 274 GLY   C O   1 
ATOM   7266 N  N   . ASN   C  1  262 ? 2.788   25.472  30.717 1.00 66.40  ? 275 ASN   C N   1 
ATOM   7267 C  CA  . ASN   C  1  262 ? 2.810   26.246  31.946 1.00 63.63  ? 275 ASN   C CA  1 
ATOM   7268 C  C   . ASN   C  1  262 ? 4.009   25.802  32.781 1.00 69.48  ? 275 ASN   C C   1 
ATOM   7269 O  O   . ASN   C  1  262 ? 4.086   24.641  33.169 1.00 70.01  ? 275 ASN   C O   1 
ATOM   7270 C  CB  . ASN   C  1  262 ? 1.525   26.063  32.749 1.00 63.59  ? 275 ASN   C CB  1 
ATOM   7271 C  CG  . ASN   C  1  262 ? 0.430   27.028  32.351 1.00 62.36  ? 275 ASN   C CG  1 
ATOM   7272 O  OD1 . ASN   C  1  262 ? 0.711   28.060  31.726 1.00 47.16  ? 275 ASN   C OD1 1 
ATOM   7273 N  ND2 . ASN   C  1  262 ? -0.812  26.722  32.714 1.00 60.26  ? 275 ASN   C ND2 1 
ATOM   7274 N  N   . ALA   C  1  263 ? 4.925   26.728  33.084 1.00 72.59  ? 276 ALA   C N   1 
ATOM   7275 C  CA  . ALA   C  1  263 ? 6.099   26.406  33.886 1.00 77.87  ? 276 ALA   C CA  1 
ATOM   7276 C  C   . ALA   C  1  263 ? 5.801   26.531  35.382 1.00 85.11  ? 276 ALA   C C   1 
ATOM   7277 O  O   . ALA   C  1  263 ? 4.949   27.322  35.799 1.00 74.34  ? 276 ALA   C O   1 
ATOM   7278 C  CB  . ALA   C  1  263 ? 7.259   27.290  33.487 1.00 74.40  ? 276 ALA   C CB  1 
ATOM   7279 N  N   . ASP   C  1  264 ? 6.504   25.698  36.166 1.00 93.99  ? 277 ASP   C N   1 
ATOM   7280 C  CA  . ASP   C  1  264 ? 6.626   25.837  37.611 1.00 98.28  ? 277 ASP   C CA  1 
ATOM   7281 C  C   . ASP   C  1  264 ? 5.271   25.727  38.305 1.00 91.78  ? 277 ASP   C C   1 
ATOM   7282 O  O   . ASP   C  1  264 ? 5.020   26.437  39.271 1.00 95.49  ? 277 ASP   C O   1 
ATOM   7283 C  CB  . ASP   C  1  264 ? 7.307   27.142  38.001 1.00 100.62 ? 277 ASP   C CB  1 
ATOM   7284 C  CG  . ASP   C  1  264 ? 8.663   27.401  37.358 1.00 105.81 ? 277 ASP   C CG  1 
ATOM   7285 O  OD1 . ASP   C  1  264 ? 9.515   26.483  37.390 1.00 111.60 ? 277 ASP   C OD1 1 
ATOM   7286 O  OD2 . ASP   C  1  264 ? 8.864   28.524  36.846 1.00 98.47  ? 277 ASP   C OD2 1 
ATOM   7287 N  N   . ASN   C  1  265 ? 4.407   24.835  37.813 1.00 91.13  ? 278 ASN   C N   1 
ATOM   7288 C  CA  . ASN   C  1  265 ? 3.158   24.497  38.485 1.00 90.71  ? 278 ASN   C CA  1 
ATOM   7289 C  C   . ASN   C  1  265 ? 2.319   25.757  38.745 1.00 79.72  ? 278 ASN   C C   1 
ATOM   7290 O  O   . ASN   C  1  265 ? 1.727   25.894  39.811 1.00 66.54  ? 278 ASN   C O   1 
ATOM   7291 C  CB  . ASN   C  1  265 ? 3.457   23.685  39.743 1.00 92.11  ? 278 ASN   C CB  1 
ATOM   7292 C  CG  . ASN   C  1  265 ? 2.245   22.969  40.284 1.00 98.10  ? 278 ASN   C CG  1 
ATOM   7293 O  OD1 . ASN   C  1  265 ? 1.675   22.111  39.601 1.00 103.04 ? 278 ASN   C OD1 1 
ATOM   7294 N  ND2 . ASN   C  1  265 ? 1.844   23.294  41.504 1.00 102.99 ? 278 ASN   C ND2 1 
ATOM   7295 N  N   . GLN   C  1  266 ? 2.244   26.660  37.757 1.00 78.77  ? 279 GLN   C N   1 
ATOM   7296 C  CA  . GLN   C  1  266 ? 1.439   27.869  37.860 1.00 82.83  ? 279 GLN   C CA  1 
ATOM   7297 C  C   . GLN   C  1  266 ? 0.607   28.083  36.599 1.00 82.43  ? 279 GLN   C C   1 
ATOM   7298 O  O   . GLN   C  1  266 ? 1.091   27.850  35.493 1.00 87.23  ? 279 GLN   C O   1 
ATOM   7299 C  CB  . GLN   C  1  266 ? 2.325   29.105  37.980 1.00 89.59  ? 279 GLN   C CB  1 
ATOM   7300 C  CG  . GLN   C  1  266 ? 3.041   29.269  39.317 1.00 95.74  ? 279 GLN   C CG  1 
ATOM   7301 C  CD  . GLN   C  1  266 ? 4.164   30.290  39.247 1.00 96.79  ? 279 GLN   C CD  1 
ATOM   7302 O  OE1 . GLN   C  1  266 ? 4.077   31.290  38.522 1.00 81.40  ? 279 GLN   C OE1 1 
ATOM   7303 N  NE2 . GLN   C  1  266 ? 5.264   30.013  39.940 1.00 95.19  ? 279 GLN   C NE2 1 
ATOM   7304 N  N   . VAL   C  1  267 ? -0.621  28.588  36.764 1.00 79.63  ? 280 VAL   C N   1 
ATOM   7305 C  CA  . VAL   C  1  267 ? -1.454  28.952  35.626 1.00 76.60  ? 280 VAL   C CA  1 
ATOM   7306 C  C   . VAL   C  1  267 ? -0.951  30.267  35.031 1.00 69.66  ? 280 VAL   C C   1 
ATOM   7307 O  O   . VAL   C  1  267 ? -0.087  30.929  35.603 1.00 66.78  ? 280 VAL   C O   1 
ATOM   7308 C  CB  . VAL   C  1  267 ? -2.945  29.026  36.005 1.00 86.41  ? 280 VAL   C CB  1 
ATOM   7309 C  CG1 . VAL   C  1  267 ? -3.475  27.664  36.439 1.00 88.32  ? 280 VAL   C CG1 1 
ATOM   7310 C  CG2 . VAL   C  1  267 ? -3.225  30.074  37.080 1.00 90.20  ? 280 VAL   C CG2 1 
ATOM   7311 N  N   . ASN   C  1  268 ? -1.479  30.601  33.850 1.00 69.28  ? 281 ASN   C N   1 
ATOM   7312 C  CA  . ASN   C  1  268 ? -1.127  31.799  33.101 1.00 75.98  ? 281 ASN   C CA  1 
ATOM   7313 C  C   . ASN   C  1  268 ? 0.382   32.024  33.101 1.00 74.47  ? 281 ASN   C C   1 
ATOM   7314 O  O   . ASN   C  1  268 ? 0.843   33.135  33.320 1.00 75.58  ? 281 ASN   C O   1 
ATOM   7315 C  CB  . ASN   C  1  268 ? -1.901  33.014  33.598 1.00 73.93  ? 281 ASN   C CB  1 
ATOM   7316 C  CG  . ASN   C  1  268 ? -3.393  32.833  33.437 1.00 77.76  ? 281 ASN   C CG  1 
ATOM   7317 O  OD1 . ASN   C  1  268 ? -3.905  32.790  32.314 1.00 78.07  ? 281 ASN   C OD1 1 
ATOM   7318 N  ND2 . ASN   C  1  268 ? -4.111  32.712  34.540 1.00 80.10  ? 281 ASN   C ND2 1 
ATOM   7319 N  N   . ASN   C  1  269 ? 1.140   30.974  32.788 1.00 75.39  ? 282 ASN   C N   1 
ATOM   7320 C  CA  . ASN   C  1  269 ? 2.590   31.035  32.840 1.00 80.66  ? 282 ASN   C CA  1 
ATOM   7321 C  C   . ASN   C  1  269 ? 3.190   30.185  31.711 1.00 83.46  ? 282 ASN   C C   1 
ATOM   7322 O  O   . ASN   C  1  269 ? 4.064   29.348  31.940 1.00 80.63  ? 282 ASN   C O   1 
ATOM   7323 C  CB  . ASN   C  1  269 ? 3.046   30.666  34.248 1.00 78.98  ? 282 ASN   C CB  1 
ATOM   7324 C  CG  . ASN   C  1  269 ? 4.509   30.961  34.468 1.00 75.47  ? 282 ASN   C CG  1 
ATOM   7325 O  OD1 . ASN   C  1  269 ? 5.029   31.955  33.951 1.00 65.61  ? 282 ASN   C OD1 1 
ATOM   7326 N  ND2 . ASN   C  1  269 ? 5.199   30.091  35.189 1.00 76.82  ? 282 ASN   C ND2 1 
ATOM   7327 N  N   . TYR   C  1  270 ? 2.731   30.435  30.477 1.00 81.44  ? 283 TYR   C N   1 
ATOM   7328 C  CA  . TYR   C  1  270 ? 3.104   29.624  29.331 1.00 80.00  ? 283 TYR   C CA  1 
ATOM   7329 C  C   . TYR   C  1  270 ? 4.491   30.040  28.834 1.00 79.81  ? 283 TYR   C C   1 
ATOM   7330 O  O   . TYR   C  1  270 ? 4.694   31.183  28.447 1.00 63.68  ? 283 TYR   C O   1 
ATOM   7331 C  CB  . TYR   C  1  270 ? 2.040   29.723  28.228 1.00 77.07  ? 283 TYR   C CB  1 
ATOM   7332 C  CG  . TYR   C  1  270 ? 2.178   28.702  27.103 1.00 77.51  ? 283 TYR   C CG  1 
ATOM   7333 C  CD1 . TYR   C  1  270 ? 1.603   27.439  27.203 1.00 80.86  ? 283 TYR   C CD1 1 
ATOM   7334 C  CD2 . TYR   C  1  270 ? 2.880   28.999  25.938 1.00 75.44  ? 283 TYR   C CD2 1 
ATOM   7335 C  CE1 . TYR   C  1  270 ? 1.733   26.503  26.187 1.00 78.72  ? 283 TYR   C CE1 1 
ATOM   7336 C  CE2 . TYR   C  1  270 ? 3.017   28.072  24.917 1.00 77.31  ? 283 TYR   C CE2 1 
ATOM   7337 C  CZ  . TYR   C  1  270 ? 2.446   26.821  25.045 1.00 72.21  ? 283 TYR   C CZ  1 
ATOM   7338 O  OH  . TYR   C  1  270 ? 2.566   25.917  24.036 1.00 67.91  ? 283 TYR   C OH  1 
ATOM   7339 N  N   . VAL   C  1  271 ? 5.424   29.078  28.815 1.00 87.06  ? 284 VAL   C N   1 
ATOM   7340 C  CA  . VAL   C  1  271 ? 6.779   29.266  28.312 1.00 81.86  ? 284 VAL   C CA  1 
ATOM   7341 C  C   . VAL   C  1  271 ? 6.975   28.387  27.078 1.00 80.04  ? 284 VAL   C C   1 
ATOM   7342 O  O   . VAL   C  1  271 ? 6.626   27.212  27.102 1.00 85.65  ? 284 VAL   C O   1 
ATOM   7343 C  CB  . VAL   C  1  271 ? 7.811   28.886  29.395 1.00 79.94  ? 284 VAL   C CB  1 
ATOM   7344 C  CG1 . VAL   C  1  271 ? 9.248   29.013  28.903 1.00 73.52  ? 284 VAL   C CG1 1 
ATOM   7345 C  CG2 . VAL   C  1  271 ? 7.604   29.670  30.683 1.00 85.06  ? 284 VAL   C CG2 1 
ATOM   7346 N  N   . GLU   C  1  272 ? 7.612   28.939  26.042 1.00 76.53  ? 285 GLU   C N   1 
ATOM   7347 C  CA  . GLU   C  1  272 ? 7.842   28.225  24.796 1.00 76.75  ? 285 GLU   C CA  1 
ATOM   7348 C  C   . GLU   C  1  272 ? 8.971   27.208  24.970 1.00 81.06  ? 285 GLU   C C   1 
ATOM   7349 O  O   . GLU   C  1  272 ? 9.893   27.445  25.744 1.00 74.87  ? 285 GLU   C O   1 
ATOM   7350 C  CB  . GLU   C  1  272 ? 8.173   29.197  23.662 1.00 76.44  ? 285 GLU   C CB  1 
ATOM   7351 C  CG  . GLU   C  1  272 ? 7.105   30.271  23.451 1.00 76.50  ? 285 GLU   C CG  1 
ATOM   7352 C  CD  . GLU   C  1  272 ? 7.399   31.293  22.353 1.00 77.62  ? 285 GLU   C CD  1 
ATOM   7353 O  OE1 . GLU   C  1  272 ? 8.474   31.195  21.704 1.00 67.61  ? 285 GLU   C OE1 1 
ATOM   7354 O  OE2 . GLU   C  1  272 ? 6.546   32.198  22.142 1.00 68.98  ? 285 GLU   C OE2 1 
ATOM   7355 N  N   . ASP   C  1  273 ? 8.857   26.067  24.259 1.00 84.84  ? 286 ASP   C N   1 
ATOM   7356 C  CA  . ASP   C  1  273 ? 9.911   25.066  24.166 1.00 75.87  ? 286 ASP   C CA  1 
ATOM   7357 C  C   . ASP   C  1  273 ? 10.482  25.089  22.752 1.00 76.11  ? 286 ASP   C C   1 
ATOM   7358 O  O   . ASP   C  1  273 ? 9.846   24.623  21.814 1.00 82.35  ? 286 ASP   C O   1 
ATOM   7359 C  CB  . ASP   C  1  273 ? 9.427   23.674  24.543 1.00 72.01  ? 286 ASP   C CB  1 
ATOM   7360 C  CG  . ASP   C  1  273 ? 10.505  22.595  24.555 1.00 75.68  ? 286 ASP   C CG  1 
ATOM   7361 O  OD1 . ASP   C  1  273 ? 11.695  22.932  24.347 1.00 70.52  ? 286 ASP   C OD1 1 
ATOM   7362 O  OD2 . ASP   C  1  273 ? 10.142  21.413  24.756 1.00 83.41  ? 286 ASP   C OD2 1 
ATOM   7363 N  N   . PRO   C  1  274 ? 11.705  25.625  22.549 1.00 83.37  ? 287 PRO   C N   1 
ATOM   7364 C  CA  . PRO   C  1  274 ? 12.303  25.677  21.210 1.00 82.67  ? 287 PRO   C CA  1 
ATOM   7365 C  C   . PRO   C  1  274 ? 12.866  24.353  20.679 1.00 82.71  ? 287 PRO   C C   1 
ATOM   7366 O  O   . PRO   C  1  274 ? 13.189  24.260  19.494 1.00 74.20  ? 287 PRO   C O   1 
ATOM   7367 C  CB  . PRO   C  1  274 ? 13.400  26.742  21.415 1.00 83.57  ? 287 PRO   C CB  1 
ATOM   7368 C  CG  . PRO   C  1  274 ? 13.851  26.531  22.850 1.00 83.61  ? 287 PRO   C CG  1 
ATOM   7369 C  CD  . PRO   C  1  274 ? 12.575  26.192  23.599 1.00 82.78  ? 287 PRO   C CD  1 
ATOM   7370 N  N   . ASP   C  1  275 ? 12.992  23.340  21.559 1.00 80.23  ? 288 ASP   C N   1 
ATOM   7371 C  CA  . ASP   C  1  275 ? 13.500  22.016  21.203 1.00 80.16  ? 288 ASP   C CA  1 
ATOM   7372 C  C   . ASP   C  1  275 ? 12.382  21.068  20.743 1.00 67.82  ? 288 ASP   C C   1 
ATOM   7373 O  O   . ASP   C  1  275 ? 12.650  20.025  20.163 1.00 56.17  ? 288 ASP   C O   1 
ATOM   7374 C  CB  . ASP   C  1  275 ? 14.268  21.402  22.366 1.00 82.01  ? 288 ASP   C CB  1 
ATOM   7375 C  CG  . ASP   C  1  275 ? 15.526  22.153  22.794 1.00 87.53  ? 288 ASP   C CG  1 
ATOM   7376 O  OD1 . ASP   C  1  275 ? 15.933  23.094  22.080 1.00 86.04  ? 288 ASP   C OD1 1 
ATOM   7377 O  OD2 . ASP   C  1  275 ? 16.076  21.825  23.860 1.00 85.29  ? 288 ASP   C OD2 1 
ATOM   7378 N  N   . SER   C  1  276 ? 11.123  21.427  21.003 1.00 60.23  ? 289 SER   C N   1 
ATOM   7379 C  CA  . SER   C  1  276 ? 9.988   20.593  20.664 1.00 56.28  ? 289 SER   C CA  1 
ATOM   7380 C  C   . SER   C  1  276 ? 9.881   20.442  19.154 1.00 56.04  ? 289 SER   C C   1 
ATOM   7381 O  O   . SER   C  1  276 ? 10.234  21.330  18.385 1.00 54.76  ? 289 SER   C O   1 
ATOM   7382 C  CB  . SER   C  1  276 ? 8.706   21.174  21.218 1.00 59.37  ? 289 SER   C CB  1 
ATOM   7383 O  OG  . SER   C  1  276 ? 7.556   20.639  20.577 1.00 60.70  ? 289 SER   C OG  1 
ATOM   7384 N  N   . ALA   C  1  277 ? 9.337   19.301  18.742 1.00 54.43  ? 290 ALA   C N   1 
ATOM   7385 C  CA  . ALA   C  1  277 ? 8.829   19.147  17.397 1.00 52.27  ? 290 ALA   C CA  1 
ATOM   7386 C  C   . ALA   C  1  277 ? 7.832   20.261  17.081 1.00 47.69  ? 290 ALA   C C   1 
ATOM   7387 O  O   . ALA   C  1  277 ? 7.152   20.756  17.970 1.00 46.79  ? 290 ALA   C O   1 
ATOM   7388 C  CB  . ALA   C  1  277 ? 8.184   17.785  17.285 1.00 48.57  ? 290 ALA   C CB  1 
ATOM   7389 N  N   . ASP   C  1  278 ? 7.742   20.620  15.803 1.00 44.53  ? 291 ASP   C N   1 
ATOM   7390 C  CA  . ASP   C  1  278 ? 6.636   21.425  15.304 1.00 52.34  ? 291 ASP   C CA  1 
ATOM   7391 C  C   . ASP   C  1  278 ? 6.382   20.986  13.860 1.00 51.91  ? 291 ASP   C C   1 
ATOM   7392 O  O   . ASP   C  1  278 ? 6.927   19.973  13.425 1.00 51.69  ? 291 ASP   C O   1 
ATOM   7393 C  CB  . ASP   C  1  278 ? 6.910   22.913  15.493 1.00 57.12  ? 291 ASP   C CB  1 
ATOM   7394 C  CG  . ASP   C  1  278 ? 8.044   23.490  14.651 1.00 62.80  ? 291 ASP   C CG  1 
ATOM   7395 O  OD1 . ASP   C  1  278 ? 8.413   22.854  13.640 1.00 71.75  ? 291 ASP   C OD1 1 
ATOM   7396 O  OD2 . ASP   C  1  278 ? 8.576   24.562  15.012 1.00 65.86  ? 291 ASP   C OD2 1 
ATOM   7397 N  N   . PHE   C  1  279 ? 5.584   21.755  13.113 1.00 49.79  ? 292 PHE   C N   1 
ATOM   7398 C  CA  . PHE   C  1  279 ? 5.097   21.295  11.828 1.00 52.61  ? 292 PHE   C CA  1 
ATOM   7399 C  C   . PHE   C  1  279 ? 6.165   21.414  10.742 1.00 57.38  ? 292 PHE   C C   1 
ATOM   7400 O  O   . PHE   C  1  279 ? 6.008   20.796  9.691  1.00 61.98  ? 292 PHE   C O   1 
ATOM   7401 C  CB  . PHE   C  1  279 ? 3.779   21.973  11.443 1.00 51.20  ? 292 PHE   C CB  1 
ATOM   7402 C  CG  . PHE   C  1  279 ? 2.625   21.301  12.168 1.00 57.11  ? 292 PHE   C CG  1 
ATOM   7403 C  CD1 . PHE   C  1  279 ? 2.116   20.081  11.715 1.00 57.30  ? 292 PHE   C CD1 1 
ATOM   7404 C  CD2 . PHE   C  1  279 ? 2.101   21.854  13.336 1.00 56.38  ? 292 PHE   C CD2 1 
ATOM   7405 C  CE1 . PHE   C  1  279 ? 1.080   19.450  12.387 1.00 57.49  ? 292 PHE   C CE1 1 
ATOM   7406 C  CE2 . PHE   C  1  279 ? 1.066   21.222  14.009 1.00 57.29  ? 292 PHE   C CE2 1 
ATOM   7407 C  CZ  . PHE   C  1  279 ? 0.557   20.022  13.534 1.00 63.44  ? 292 PHE   C CZ  1 
ATOM   7408 N  N   . THR   C  1  280 ? 7.256   22.149  10.991 1.00 56.62  ? 293 THR   C N   1 
ATOM   7409 C  CA  . THR   C  1  280 ? 8.374   22.169  10.055 1.00 56.48  ? 293 THR   C CA  1 
ATOM   7410 C  C   . THR   C  1  280 ? 9.540   21.333  10.589 1.00 55.95  ? 293 THR   C C   1 
ATOM   7411 O  O   . THR   C  1  280 ? 10.575  21.251  9.938  1.00 60.07  ? 293 THR   C O   1 
ATOM   7412 C  CB  . THR   C  1  280 ? 8.796   23.614  9.763  1.00 61.59  ? 293 THR   C CB  1 
ATOM   7413 O  OG1 . THR   C  1  280 ? 9.273   24.185  10.979 1.00 57.86  ? 293 THR   C OG1 1 
ATOM   7414 C  CG2 . THR   C  1  280 ? 7.664   24.468  9.213  1.00 58.72  ? 293 THR   C CG2 1 
ATOM   7415 N  N   . HIS   C  1  281 ? 9.370   20.692  11.757 1.00 58.69  ? 294 HIS   C N   1 
ATOM   7416 C  CA  . HIS   C  1  281 ? 10.414  19.872  12.366 1.00 58.50  ? 294 HIS   C CA  1 
ATOM   7417 C  C   . HIS   C  1  281 ? 9.806   18.565  12.870 1.00 54.28  ? 294 HIS   C C   1 
ATOM   7418 O  O   . HIS   C  1  281 ? 9.934   18.216  14.045 1.00 57.90  ? 294 HIS   C O   1 
ATOM   7419 C  CB  . HIS   C  1  281 ? 11.138  20.610  13.503 1.00 60.49  ? 294 HIS   C CB  1 
ATOM   7420 C  CG  . HIS   C  1  281 ? 11.834  21.867  13.106 1.00 74.00  ? 294 HIS   C CG  1 
ATOM   7421 N  ND1 . HIS   C  1  281 ? 13.143  21.878  12.669 1.00 84.33  ? 294 HIS   C ND1 1 
ATOM   7422 C  CD2 . HIS   C  1  281 ? 11.417  23.147  13.085 1.00 78.75  ? 294 HIS   C CD2 1 
ATOM   7423 C  CE1 . HIS   C  1  281 ? 13.499  23.125  12.388 1.00 86.65  ? 294 HIS   C CE1 1 
ATOM   7424 N  NE2 . HIS   C  1  281 ? 12.465  23.909  12.632 1.00 84.25  ? 294 HIS   C NE2 1 
ATOM   7425 N  N   . LEU   C  1  282 ? 9.183   17.822  11.952 1.00 48.63  ? 295 LEU   C N   1 
ATOM   7426 C  CA  . LEU   C  1  282 ? 8.429   16.630  12.314 1.00 48.35  ? 295 LEU   C CA  1 
ATOM   7427 C  C   . LEU   C  1  282 ? 9.347   15.501  12.776 1.00 41.24  ? 295 LEU   C C   1 
ATOM   7428 O  O   . LEU   C  1  282 ? 8.947   14.703  13.610 1.00 43.48  ? 295 LEU   C O   1 
ATOM   7429 C  CB  . LEU   C  1  282 ? 7.548   16.205  11.142 1.00 48.70  ? 295 LEU   C CB  1 
ATOM   7430 C  CG  . LEU   C  1  282 ? 6.302   17.066  10.921 1.00 51.47  ? 295 LEU   C CG  1 
ATOM   7431 C  CD1 . LEU   C  1  282 ? 5.545   16.662  9.664  1.00 53.57  ? 295 LEU   C CD1 1 
ATOM   7432 C  CD2 . LEU   C  1  282 ? 5.379   16.984  12.120 1.00 52.25  ? 295 LEU   C CD2 1 
ATOM   7433 N  N   . CYS   C  1  283 ? 10.571  15.437  12.263 1.00 41.90  ? 296 CYS   C N   1 
ATOM   7434 C  CA  . CYS   C  1  283 ? 11.461  14.333  12.590 1.00 48.20  ? 296 CYS   C CA  1 
ATOM   7435 C  C   . CYS   C  1  283 ? 11.896  14.395  14.047 1.00 47.39  ? 296 CYS   C C   1 
ATOM   7436 O  O   . CYS   C  1  283 ? 12.235  13.354  14.607 1.00 53.28  ? 296 CYS   C O   1 
ATOM   7437 C  CB  . CYS   C  1  283 ? 12.652  14.238  11.644 1.00 59.18  ? 296 CYS   C CB  1 
ATOM   7438 S  SG  . CYS   C  1  283 ? 12.206  13.672  9.969  1.00 71.77  ? 296 CYS   C SG  1 
ATOM   7439 N  N   . ARG   C  1  284 ? 11.833  15.576  14.678 1.00 42.75  ? 297 ARG   C N   1 
ATOM   7440 C  CA  . ARG   C  1  284 ? 12.053  15.649  16.115 1.00 48.98  ? 297 ARG   C CA  1 
ATOM   7441 C  C   . ARG   C  1  284 ? 11.050  14.774  16.867 1.00 45.05  ? 297 ARG   C C   1 
ATOM   7442 O  O   . ARG   C  1  284 ? 11.389  14.191  17.894 1.00 44.98  ? 297 ARG   C O   1 
ATOM   7443 C  CB  . ARG   C  1  284 ? 11.900  17.064  16.676 1.00 55.14  ? 297 ARG   C CB  1 
ATOM   7444 C  CG  . ARG   C  1  284 ? 13.024  17.972  16.222 1.00 62.11  ? 297 ARG   C CG  1 
ATOM   7445 C  CD  . ARG   C  1  284 ? 12.888  19.311  16.894 1.00 67.70  ? 297 ARG   C CD  1 
ATOM   7446 N  NE  . ARG   C  1  284 ? 13.805  20.288  16.304 1.00 71.62  ? 297 ARG   C NE  1 
ATOM   7447 C  CZ  . ARG   C  1  284 ? 13.787  21.589  16.522 1.00 72.68  ? 297 ARG   C CZ  1 
ATOM   7448 N  NH1 . ARG   C  1  284 ? 12.966  22.110  17.425 1.00 75.43  ? 297 ARG   C NH1 1 
ATOM   7449 N  NH2 . ARG   C  1  284 ? 14.632  22.343  15.847 1.00 69.13  ? 297 ARG   C NH2 1 
ATOM   7450 N  N   . LEU   C  1  285 ? 9.813   14.697  16.364 1.00 44.49  ? 298 LEU   C N   1 
ATOM   7451 C  CA  . LEU   C  1  285 ? 8.800   13.883  17.017 1.00 44.15  ? 298 LEU   C CA  1 
ATOM   7452 C  C   . LEU   C  1  285 ? 9.279   12.434  17.000 1.00 36.78  ? 298 LEU   C C   1 
ATOM   7453 O  O   . LEU   C  1  285 ? 9.203   11.744  18.019 1.00 38.98  ? 298 LEU   C O   1 
ATOM   7454 C  CB  . LEU   C  1  285 ? 7.428   14.086  16.371 1.00 44.53  ? 298 LEU   C CB  1 
ATOM   7455 C  CG  . LEU   C  1  285 ? 6.241   13.414  17.063 1.00 48.07  ? 298 LEU   C CG  1 
ATOM   7456 C  CD1 . LEU   C  1  285 ? 4.929   14.051  16.644 1.00 49.44  ? 298 LEU   C CD1 1 
ATOM   7457 C  CD2 . LEU   C  1  285 ? 6.142   11.922  16.788 1.00 52.13  ? 298 LEU   C CD2 1 
ATOM   7458 N  N   . TYR   C  1  286 ? 9.832   12.005  15.859 1.00 33.82  ? 299 TYR   C N   1 
ATOM   7459 C  CA  . TYR   C  1  286 ? 10.326  10.641  15.696 1.00 37.50  ? 299 TYR   C CA  1 
ATOM   7460 C  C   . TYR   C  1  286 ? 11.439  10.356  16.708 1.00 38.15  ? 299 TYR   C C   1 
ATOM   7461 O  O   . TYR   C  1  286 ? 11.370  9.375   17.455 1.00 38.06  ? 299 TYR   C O   1 
ATOM   7462 C  CB  . TYR   C  1  286 ? 10.773  10.388  14.253 1.00 33.88  ? 299 TYR   C CB  1 
ATOM   7463 C  CG  . TYR   C  1  286 ? 11.431  9.033   14.067 1.00 31.74  ? 299 TYR   C CG  1 
ATOM   7464 C  CD1 . TYR   C  1  286 ? 10.710  7.851   14.223 1.00 29.95  ? 299 TYR   C CD1 1 
ATOM   7465 C  CD2 . TYR   C  1  286 ? 12.777  8.936   13.767 1.00 29.48  ? 299 TYR   C CD2 1 
ATOM   7466 C  CE1 . TYR   C  1  286 ? 11.318  6.615   14.094 1.00 30.49  ? 299 TYR   C CE1 1 
ATOM   7467 C  CE2 . TYR   C  1  286 ? 13.393  7.708   13.609 1.00 30.01  ? 299 TYR   C CE2 1 
ATOM   7468 C  CZ  . TYR   C  1  286 ? 12.661  6.547   13.767 1.00 31.75  ? 299 TYR   C CZ  1 
ATOM   7469 O  OH  . TYR   C  1  286 ? 13.273  5.342   13.613 1.00 33.18  ? 299 TYR   C OH  1 
ATOM   7470 N  N   . GLU   C  1  287 ? 12.433  11.248  16.763 1.00 39.40  ? 300 GLU   C N   1 
ATOM   7471 C  CA  . GLU   C  1  287 ? 13.548  11.103  17.686 1.00 44.63  ? 300 GLU   C CA  1 
ATOM   7472 C  C   . GLU   C  1  287 ? 13.067  11.118  19.137 1.00 39.66  ? 300 GLU   C C   1 
ATOM   7473 O  O   . GLU   C  1  287 ? 13.504  10.291  19.921 1.00 39.16  ? 300 GLU   C O   1 
ATOM   7474 C  CB  . GLU   C  1  287 ? 14.583  12.192  17.405 1.00 50.82  ? 300 GLU   C CB  1 
ATOM   7475 C  CG  . GLU   C  1  287 ? 15.278  12.004  16.057 1.00 63.46  ? 300 GLU   C CG  1 
ATOM   7476 C  CD  . GLU   C  1  287 ? 15.739  13.241  15.284 1.00 79.37  ? 300 GLU   C CD  1 
ATOM   7477 O  OE1 . GLU   C  1  287 ? 15.582  14.398  15.741 1.00 96.71  ? 300 GLU   C OE1 1 
ATOM   7478 O  OE2 . GLU   C  1  287 ? 16.232  13.032  14.159 1.00 86.65  ? 300 GLU   C OE2 1 
ATOM   7479 N  N   . PHE   C  1  288 ? 12.175  12.058  19.478 1.00 37.46  ? 301 PHE   C N   1 
ATOM   7480 C  CA  . PHE   C  1  288 ? 11.631  12.176  20.822 1.00 38.51  ? 301 PHE   C CA  1 
ATOM   7481 C  C   . PHE   C  1  288 ? 10.990  10.850  21.244 1.00 33.28  ? 301 PHE   C C   1 
ATOM   7482 O  O   . PHE   C  1  288 ? 11.282  10.332  22.307 1.00 36.44  ? 301 PHE   C O   1 
ATOM   7483 C  CB  . PHE   C  1  288 ? 10.641  13.350  20.902 1.00 42.21  ? 301 PHE   C CB  1 
ATOM   7484 C  CG  . PHE   C  1  288 ? 10.091  13.551  22.303 1.00 42.84  ? 301 PHE   C CG  1 
ATOM   7485 C  CD1 . PHE   C  1  288 ? 10.786  14.328  23.227 1.00 45.73  ? 301 PHE   C CD1 1 
ATOM   7486 C  CD2 . PHE   C  1  288 ? 8.931   12.903  22.716 1.00 45.11  ? 301 PHE   C CD2 1 
ATOM   7487 C  CE1 . PHE   C  1  288 ? 10.311  14.473  24.526 1.00 46.48  ? 301 PHE   C CE1 1 
ATOM   7488 C  CE2 . PHE   C  1  288 ? 8.471   13.034  24.026 1.00 47.44  ? 301 PHE   C CE2 1 
ATOM   7489 C  CZ  . PHE   C  1  288 ? 9.156   13.826  24.926 1.00 42.89  ? 301 PHE   C CZ  1 
ATOM   7490 N  N   . VAL   C  1  289 ? 10.148  10.280  20.383 1.00 33.14  ? 302 VAL   C N   1 
ATOM   7491 C  CA  . VAL   C  1  289 ? 9.412   9.071   20.712 1.00 33.45  ? 302 VAL   C CA  1 
ATOM   7492 C  C   . VAL   C  1  289 ? 10.357  7.877   20.850 1.00 30.14  ? 302 VAL   C C   1 
ATOM   7493 O  O   . VAL   C  1  289 ? 10.177  7.053   21.745 1.00 33.65  ? 302 VAL   C O   1 
ATOM   7494 C  CB  . VAL   C  1  289 ? 8.292   8.785   19.689 1.00 34.79  ? 302 VAL   C CB  1 
ATOM   7495 C  CG1 . VAL   C  1  289 ? 7.713   7.384   19.851 1.00 34.55  ? 302 VAL   C CG1 1 
ATOM   7496 C  CG2 . VAL   C  1  289 ? 7.175   9.809   19.786 1.00 32.88  ? 302 VAL   C CG2 1 
ATOM   7497 N  N   . VAL   C  1  290 ? 11.353  7.771   19.968 1.00 29.73  ? 303 VAL   C N   1 
ATOM   7498 C  CA  . VAL   C  1  290 ? 12.353  6.717   20.117 1.00 33.66  ? 303 VAL   C CA  1 
ATOM   7499 C  C   . VAL   C  1  290 ? 13.068  6.829   21.472 1.00 31.45  ? 303 VAL   C C   1 
ATOM   7500 O  O   . VAL   C  1  290 ? 13.232  5.823   22.159 1.00 30.62  ? 303 VAL   C O   1 
ATOM   7501 C  CB  . VAL   C  1  290 ? 13.350  6.678   18.950 1.00 34.98  ? 303 VAL   C CB  1 
ATOM   7502 C  CG1 . VAL   C  1  290 ? 14.495  5.701   19.215 1.00 36.85  ? 303 VAL   C CG1 1 
ATOM   7503 C  CG2 . VAL   C  1  290 ? 12.649  6.313   17.649 1.00 35.17  ? 303 VAL   C CG2 1 
ATOM   7504 N  N   . GLY   C  1  291 ? 13.457  8.051   21.856 1.00 34.48  ? 304 GLY   C N   1 
ATOM   7505 C  CA  . GLY   C  1  291 ? 13.938  8.354   23.201 1.00 37.21  ? 304 GLY   C CA  1 
ATOM   7506 C  C   . GLY   C  1  291 ? 12.993  7.831   24.287 1.00 38.39  ? 304 GLY   C C   1 
ATOM   7507 O  O   . GLY   C  1  291 ? 13.420  7.093   25.185 1.00 43.12  ? 304 GLY   C O   1 
ATOM   7508 N  N   . SER   C  1  292 ? 11.697  8.164   24.166 1.00 34.79  ? 305 SER   C N   1 
ATOM   7509 C  CA  . SER   C  1  292 ? 10.718  7.757   25.165 1.00 36.46  ? 305 SER   C CA  1 
ATOM   7510 C  C   . SER   C  1  292 ? 10.656  6.233   25.269 1.00 34.96  ? 305 SER   C C   1 
ATOM   7511 O  O   . SER   C  1  292 ? 10.528  5.695   26.357 1.00 38.44  ? 305 SER   C O   1 
ATOM   7512 C  CB  . SER   C  1  292 ? 9.373   8.343   24.869 1.00 36.62  ? 305 SER   C CB  1 
ATOM   7513 O  OG  . SER   C  1  292 ? 9.460   9.750   24.655 1.00 37.55  ? 305 SER   C OG  1 
ATOM   7514 N  N   . VAL   C  1  293 ? 10.763  5.541   24.129 1.00 32.77  ? 306 VAL   C N   1 
ATOM   7515 C  CA  . VAL   C  1  293 ? 10.716  4.092   24.129 1.00 34.58  ? 306 VAL   C CA  1 
ATOM   7516 C  C   . VAL   C  1  293 ? 11.927  3.523   24.866 1.00 35.83  ? 306 VAL   C C   1 
ATOM   7517 O  O   . VAL   C  1  293 ? 11.801  2.523   25.568 1.00 35.68  ? 306 VAL   C O   1 
ATOM   7518 C  CB  . VAL   C  1  293 ? 10.596  3.538   22.701 1.00 32.82  ? 306 VAL   C CB  1 
ATOM   7519 C  CG1 . VAL   C  1  293 ? 10.821  2.027   22.643 1.00 31.97  ? 306 VAL   C CG1 1 
ATOM   7520 C  CG2 . VAL   C  1  293 ? 9.237   3.885   22.117 1.00 32.54  ? 306 VAL   C CG2 1 
ATOM   7521 N  N   . GLN   C  1  294 ? 13.087  4.167   24.723 1.00 39.60  ? 307 GLN   C N   1 
ATOM   7522 C  CA  . GLN   C  1  294 ? 14.280  3.713   25.418 1.00 45.16  ? 307 GLN   C CA  1 
ATOM   7523 C  C   . GLN   C  1  294 ? 14.124  3.856   26.932 1.00 40.89  ? 307 GLN   C C   1 
ATOM   7524 O  O   . GLN   C  1  294 ? 14.605  2.998   27.671 1.00 45.35  ? 307 GLN   C O   1 
ATOM   7525 C  CB  . GLN   C  1  294 ? 15.514  4.457   24.921 1.00 46.52  ? 307 GLN   C CB  1 
ATOM   7526 C  CG  . GLN   C  1  294 ? 15.887  4.090   23.488 1.00 48.75  ? 307 GLN   C CG  1 
ATOM   7527 C  CD  . GLN   C  1  294 ? 16.972  4.989   22.923 1.00 44.66  ? 307 GLN   C CD  1 
ATOM   7528 O  OE1 . GLN   C  1  294 ? 16.731  6.131   22.520 1.00 41.40  ? 307 GLN   C OE1 1 
ATOM   7529 N  NE2 . GLN   C  1  294 ? 18.195  4.491   22.890 1.00 42.69  ? 307 GLN   C NE2 1 
ATOM   7530 N  N   . GLU   C  1  295 ? 13.462  4.927   27.386 1.00 42.76  ? 308 GLU   C N   1 
ATOM   7531 C  CA  . GLU   C  1  295 ? 13.205  5.115   28.809 1.00 44.79  ? 308 GLU   C CA  1 
ATOM   7532 C  C   . GLU   C  1  295 ? 12.298  4.007   29.334 1.00 38.34  ? 308 GLU   C C   1 
ATOM   7533 O  O   . GLU   C  1  295 ? 12.580  3.484   30.407 1.00 40.41  ? 308 GLU   C O   1 
ATOM   7534 C  CB  . GLU   C  1  295 ? 12.624  6.487   29.144 1.00 50.32  ? 308 GLU   C CB  1 
ATOM   7535 C  CG  . GLU   C  1  295 ? 13.610  7.625   28.886 1.00 55.36  ? 308 GLU   C CG  1 
ATOM   7536 C  CD  . GLU   C  1  295 ? 13.004  9.022   28.999 1.00 70.31  ? 308 GLU   C CD  1 
ATOM   7537 O  OE1 . GLU   C  1  295 ? 11.755  9.145   29.092 1.00 72.17  ? 308 GLU   C OE1 1 
ATOM   7538 O  OE2 . GLU   C  1  295 ? 13.784  10.008  28.992 1.00 76.15  ? 308 GLU   C OE2 1 
ATOM   7539 N  N   . LEU   C  1  296 ? 11.280  3.609   28.550 1.00 34.40  ? 309 LEU   C N   1 
ATOM   7540 C  CA  . LEU   C  1  296 ? 10.348  2.568   28.959 1.00 31.90  ? 309 LEU   C CA  1 
ATOM   7541 C  C   . LEU   C  1  296 ? 11.039  1.210   28.938 1.00 33.36  ? 309 LEU   C C   1 
ATOM   7542 O  O   . LEU   C  1  296 ? 10.711  0.342   29.754 1.00 34.11  ? 309 LEU   C O   1 
ATOM   7543 C  CB  . LEU   C  1  296 ? 9.096   2.502   28.085 1.00 32.89  ? 309 LEU   C CB  1 
ATOM   7544 C  CG  . LEU   C  1  296 ? 8.189   3.735   28.046 1.00 33.77  ? 309 LEU   C CG  1 
ATOM   7545 C  CD1 . LEU   C  1  296 ? 7.115   3.509   27.018 1.00 35.06  ? 309 LEU   C CD1 1 
ATOM   7546 C  CD2 . LEU   C  1  296 ? 7.533   4.078   29.380 1.00 33.58  ? 309 LEU   C CD2 1 
ATOM   7547 N  N   . TYR   C  1  297 ? 11.939  1.007   27.962 1.00 34.38  ? 310 TYR   C N   1 
ATOM   7548 C  CA  . TYR   C  1  297 ? 12.583  -0.287  27.760 1.00 36.27  ? 310 TYR   C CA  1 
ATOM   7549 C  C   . TYR   C  1  297 ? 14.099  -0.114  27.720 1.00 38.12  ? 310 TYR   C C   1 
ATOM   7550 O  O   . TYR   C  1  297 ? 14.692  -0.091  26.652 1.00 36.38  ? 310 TYR   C O   1 
ATOM   7551 C  CB  . TYR   C  1  297 ? 12.073  -0.929  26.471 1.00 34.15  ? 310 TYR   C CB  1 
ATOM   7552 C  CG  . TYR   C  1  297 ? 10.589  -1.252  26.494 1.00 33.48  ? 310 TYR   C CG  1 
ATOM   7553 C  CD1 . TYR   C  1  297 ? 10.121  -2.392  27.128 1.00 33.91  ? 310 TYR   C CD1 1 
ATOM   7554 C  CD2 . TYR   C  1  297 ? 9.662   -0.419  25.879 1.00 30.73  ? 310 TYR   C CD2 1 
ATOM   7555 C  CE1 . TYR   C  1  297 ? 8.773   -2.701  27.147 1.00 36.87  ? 310 TYR   C CE1 1 
ATOM   7556 C  CE2 . TYR   C  1  297 ? 8.314   -0.718  25.883 1.00 32.63  ? 310 TYR   C CE2 1 
ATOM   7557 C  CZ  . TYR   C  1  297 ? 7.863   -1.853  26.537 1.00 33.55  ? 310 TYR   C CZ  1 
ATOM   7558 O  OH  . TYR   C  1  297 ? 6.529   -2.146  26.580 1.00 29.67  ? 310 TYR   C OH  1 
ATOM   7559 N  N   . PRO   C  1  298 ? 14.762  0.059   28.884 1.00 41.41  ? 311 PRO   C N   1 
ATOM   7560 C  CA  . PRO   C  1  298 ? 16.181  0.413   28.921 1.00 39.90  ? 311 PRO   C CA  1 
ATOM   7561 C  C   . PRO   C  1  298 ? 17.151  -0.655  28.439 1.00 35.65  ? 311 PRO   C C   1 
ATOM   7562 O  O   . PRO   C  1  298 ? 18.197  -0.307  27.922 1.00 34.05  ? 311 PRO   C O   1 
ATOM   7563 C  CB  . PRO   C  1  298 ? 16.475  0.778   30.393 1.00 43.59  ? 311 PRO   C CB  1 
ATOM   7564 C  CG  . PRO   C  1  298 ? 15.167  0.641   31.125 1.00 46.31  ? 311 PRO   C CG  1 
ATOM   7565 C  CD  . PRO   C  1  298 ? 14.159  -0.032  30.216 1.00 42.80  ? 311 PRO   C CD  1 
ATOM   7566 N  N   . ASN   C  1  299 ? 16.839  -1.942  28.618 1.00 39.20  ? 312 ASN   C N   1 
ATOM   7567 C  CA  . ASN   C  1  299 ? 17.778  -2.993  28.244 1.00 35.63  ? 312 ASN   C CA  1 
ATOM   7568 C  C   . ASN   C  1  299 ? 17.061  -4.312  27.986 1.00 35.94  ? 312 ASN   C C   1 
ATOM   7569 O  O   . ASN   C  1  299 ? 17.345  -5.307  28.641 1.00 34.18  ? 312 ASN   C O   1 
ATOM   7570 C  CB  . ASN   C  1  299 ? 18.829  -3.195  29.331 1.00 39.76  ? 312 ASN   C CB  1 
ATOM   7571 C  CG  . ASN   C  1  299 ? 19.916  -4.166  28.940 1.00 37.46  ? 312 ASN   C CG  1 
ATOM   7572 O  OD1 . ASN   C  1  299 ? 20.272  -5.031  29.741 1.00 35.43  ? 312 ASN   C OD1 1 
ATOM   7573 N  ND2 . ASN   C  1  299 ? 20.483  -4.026  27.750 1.00 35.40  ? 312 ASN   C ND2 1 
ATOM   7574 N  N   . PRO   C  1  300 ? 16.150  -4.386  26.988 1.00 37.11  ? 313 PRO   C N   1 
ATOM   7575 C  CA  . PRO   C  1  300 ? 15.390  -5.606  26.733 1.00 34.98  ? 313 PRO   C CA  1 
ATOM   7576 C  C   . PRO   C  1  300 ? 16.221  -6.679  26.034 1.00 36.44  ? 313 PRO   C C   1 
ATOM   7577 O  O   . PRO   C  1  300 ? 17.171  -6.366  25.312 1.00 36.45  ? 313 PRO   C O   1 
ATOM   7578 C  CB  . PRO   C  1  300 ? 14.277  -5.061  25.830 1.00 36.20  ? 313 PRO   C CB  1 
ATOM   7579 C  CG  . PRO   C  1  300 ? 14.996  -4.027  24.986 1.00 35.54  ? 313 PRO   C CG  1 
ATOM   7580 C  CD  . PRO   C  1  300 ? 15.855  -3.322  26.018 1.00 35.32  ? 313 PRO   C CD  1 
ATOM   7581 N  N   . THR   C  1  301 ? 15.816  -7.938  26.234 1.00 37.69  ? 314 THR   C N   1 
ATOM   7582 C  CA  . THR   C  1  301 ? 16.395  -9.072  25.531 1.00 42.56  ? 314 THR   C CA  1 
ATOM   7583 C  C   . THR   C  1  301 ? 15.245  -9.990  25.100 1.00 42.49  ? 314 THR   C C   1 
ATOM   7584 O  O   . THR   C  1  301 ? 14.075  -9.727  25.409 1.00 40.52  ? 314 THR   C O   1 
ATOM   7585 C  CB  . THR   C  1  301 ? 17.418  -9.794  26.425 1.00 51.66  ? 314 THR   C CB  1 
ATOM   7586 O  OG1 . THR   C  1  301 ? 16.740  -10.318 27.566 1.00 48.92  ? 314 THR   C OG1 1 
ATOM   7587 C  CG2 . THR   C  1  301 ? 18.550  -8.899  26.922 1.00 49.22  ? 314 THR   C CG2 1 
ATOM   7588 N  N   . GLY   C  1  302 ? 15.584  -11.078 24.391 1.00 41.52  ? 315 GLY   C N   1 
ATOM   7589 C  CA  . GLY   C  1  302 ? 14.621  -12.106 24.029 1.00 42.21  ? 315 GLY   C CA  1 
ATOM   7590 C  C   . GLY   C  1  302 ? 13.500  -11.576 23.128 1.00 43.69  ? 315 GLY   C C   1 
ATOM   7591 O  O   . GLY   C  1  302 ? 13.726  -10.733 22.268 1.00 38.04  ? 315 GLY   C O   1 
ATOM   7592 N  N   . ILE   C  1  303 ? 12.288  -12.091 23.356 1.00 43.69  ? 316 ILE   C N   1 
ATOM   7593 C  CA  . ILE   C  1  303 ? 11.125  -11.804 22.532 1.00 49.40  ? 316 ILE   C CA  1 
ATOM   7594 C  C   . ILE   C  1  303 ? 10.777  -10.322 22.647 1.00 41.11  ? 316 ILE   C C   1 
ATOM   7595 O  O   . ILE   C  1  303 ? 10.373  -9.710  21.666 1.00 42.88  ? 316 ILE   C O   1 
ATOM   7596 C  CB  . ILE   C  1  303 ? 9.952   -12.719 22.935 1.00 57.94  ? 316 ILE   C CB  1 
ATOM   7597 C  CG1 . ILE   C  1  303 ? 10.354  -14.196 22.812 1.00 82.36  ? 316 ILE   C CG1 1 
ATOM   7598 C  CG2 . ILE   C  1  303 ? 8.691   -12.433 22.121 1.00 56.42  ? 316 ILE   C CG2 1 
ATOM   7599 C  CD1 . ILE   C  1  303 ? 9.494   -15.150 23.622 1.00 97.11  ? 316 ILE   C CD1 1 
ATOM   7600 N  N   . LEU   C  1  304 ? 10.949  -9.747  23.841 1.00 38.47  ? 317 LEU   C N   1 
ATOM   7601 C  CA  . LEU   C  1  304 ? 10.619  -8.351  24.045 1.00 34.94  ? 317 LEU   C CA  1 
ATOM   7602 C  C   . LEU   C  1  304 ? 11.499  -7.502  23.132 1.00 34.86  ? 317 LEU   C C   1 
ATOM   7603 O  O   . LEU   C  1  304 ? 11.018  -6.595  22.463 1.00 38.06  ? 317 LEU   C O   1 
ATOM   7604 C  CB  . LEU   C  1  304 ? 10.767  -7.966  25.509 1.00 35.26  ? 317 LEU   C CB  1 
ATOM   7605 C  CG  . LEU   C  1  304 ? 10.595  -6.474  25.819 1.00 37.84  ? 317 LEU   C CG  1 
ATOM   7606 C  CD1 . LEU   C  1  304 ? 9.251   -5.941  25.353 1.00 36.23  ? 317 LEU   C CD1 1 
ATOM   7607 C  CD2 . LEU   C  1  304 ? 10.761  -6.230  27.312 1.00 37.53  ? 317 LEU   C CD2 1 
ATOM   7608 N  N   . ARG   C  1  305 ? 12.797  -7.805  23.097 1.00 34.43  ? 318 ARG   C N   1 
ATOM   7609 C  CA  A ARG   C  1  305 ? 13.716  -7.047  22.267 0.50 31.60  ? 318 ARG   C CA  1 
ATOM   7610 C  CA  B ARG   C  1  305 ? 13.738  -7.076  22.265 0.50 33.55  ? 318 ARG   C CA  1 
ATOM   7611 C  C   . ARG   C  1  305 ? 13.327  -7.202  20.801 1.00 32.23  ? 318 ARG   C C   1 
ATOM   7612 O  O   . ARG   C  1  305 ? 13.314  -6.234  20.062 1.00 33.01  ? 318 ARG   C O   1 
ATOM   7613 C  CB  A ARG   C  1  305 ? 15.160  -7.509  22.469 0.50 27.97  ? 318 ARG   C CB  1 
ATOM   7614 C  CB  B ARG   C  1  305 ? 15.156  -7.619  22.464 0.50 32.49  ? 318 ARG   C CB  1 
ATOM   7615 C  CG  A ARG   C  1  305 ? 16.179  -6.971  21.484 0.50 26.29  ? 318 ARG   C CG  1 
ATOM   7616 C  CG  B ARG   C  1  305 ? 16.229  -6.731  21.853 0.50 33.59  ? 318 ARG   C CG  1 
ATOM   7617 C  CD  A ARG   C  1  305 ? 17.510  -7.697  21.597 0.50 24.64  ? 318 ARG   C CD  1 
ATOM   7618 C  CD  B ARG   C  1  305 ? 17.634  -7.302  21.965 0.50 34.47  ? 318 ARG   C CD  1 
ATOM   7619 N  NE  A ARG   C  1  305 ? 18.398  -7.128  20.583 0.50 21.08  ? 318 ARG   C NE  1 
ATOM   7620 N  NE  B ARG   C  1  305 ? 18.650  -6.352  21.491 0.50 33.82  ? 318 ARG   C NE  1 
ATOM   7621 C  CZ  A ARG   C  1  305 ? 18.572  -7.629  19.407 0.50 16.68  ? 318 ARG   C CZ  1 
ATOM   7622 C  CZ  B ARG   C  1  305 ? 19.064  -5.267  22.144 0.50 29.71  ? 318 ARG   C CZ  1 
ATOM   7623 N  NH1 A ARG   C  1  305 ? 18.120  -8.822  19.159 0.50 16.02  ? 318 ARG   C NH1 1 
ATOM   7624 N  NH1 B ARG   C  1  305 ? 18.670  -4.975  23.399 0.50 32.41  ? 318 ARG   C NH1 1 
ATOM   7625 N  NH2 A ARG   C  1  305 ? 19.216  -6.940  18.509 0.50 16.14  ? 318 ARG   C NH2 1 
ATOM   7626 N  NH2 B ARG   C  1  305 ? 19.920  -4.498  21.532 0.50 23.06  ? 318 ARG   C NH2 1 
ATOM   7627 N  N   . ARG   C  1  306 ? 13.025  -8.425  20.391 1.00 34.58  ? 319 ARG   C N   1 
ATOM   7628 C  CA  . ARG   C  1  306 ? 12.701  -8.714  19.008 1.00 38.07  ? 319 ARG   C CA  1 
ATOM   7629 C  C   . ARG   C  1  306 ? 11.449  -7.934  18.610 1.00 38.22  ? 319 ARG   C C   1 
ATOM   7630 O  O   . ARG   C  1  306 ? 11.437  -7.316  17.547 1.00 34.44  ? 319 ARG   C O   1 
ATOM   7631 C  CB  . ARG   C  1  306 ? 12.527  -10.227 18.868 1.00 46.77  ? 319 ARG   C CB  1 
ATOM   7632 C  CG  . ARG   C  1  306 ? 12.365  -10.712 17.433 1.00 58.71  ? 319 ARG   C CG  1 
ATOM   7633 C  CD  . ARG   C  1  306 ? 11.752  -12.108 17.338 1.00 65.16  ? 319 ARG   C CD  1 
ATOM   7634 N  NE  . ARG   C  1  306 ? 10.355  -12.114 17.797 1.00 75.64  ? 319 ARG   C NE  1 
ATOM   7635 C  CZ  . ARG   C  1  306 ? 9.639   -13.191 18.098 1.00 88.82  ? 319 ARG   C CZ  1 
ATOM   7636 N  NH1 . ARG   C  1  306 ? 10.126  -14.407 17.911 1.00 87.76  ? 319 ARG   C NH1 1 
ATOM   7637 N  NH2 . ARG   C  1  306 ? 8.412   -13.043 18.567 1.00 94.18  ? 319 ARG   C NH2 1 
ATOM   7638 N  N   . ASN   C  1  307 ? 10.423  -7.932  19.478 1.00 34.54  ? 320 ASN   C N   1 
ATOM   7639 C  CA  . ASN   C  1  307 ? 9.166   -7.280  19.144 1.00 33.43  ? 320 ASN   C CA  1 
ATOM   7640 C  C   . ASN   C  1  307 ? 9.331   -5.757  19.164 1.00 32.56  ? 320 ASN   C C   1 
ATOM   7641 O  O   . ASN   C  1  307 ? 8.709   -5.052  18.366 1.00 34.04  ? 320 ASN   C O   1 
ATOM   7642 C  CB  . ASN   C  1  307 ? 8.026   -7.792  20.011 1.00 33.36  ? 320 ASN   C CB  1 
ATOM   7643 C  CG  . ASN   C  1  307 ? 7.671   -9.218  19.680 1.00 33.03  ? 320 ASN   C CG  1 
ATOM   7644 O  OD1 . ASN   C  1  307 ? 8.334   -9.852  18.867 1.00 35.04  ? 320 ASN   C OD1 1 
ATOM   7645 N  ND2 . ASN   C  1  307 ? 6.616   -9.744  20.272 1.00 38.24  ? 320 ASN   C ND2 1 
ATOM   7646 N  N   . LEU   C  1  308 ? 10.198  -5.243  20.039 1.00 32.09  ? 321 LEU   C N   1 
ATOM   7647 C  CA  . LEU   C  1  308 ? 10.519  -3.823  20.021 1.00 31.47  ? 321 LEU   C CA  1 
ATOM   7648 C  C   . LEU   C  1  308 ? 11.114  -3.436  18.677 1.00 30.51  ? 321 LEU   C C   1 
ATOM   7649 O  O   . LEU   C  1  308 ? 10.745  -2.431  18.089 1.00 32.71  ? 321 LEU   C O   1 
ATOM   7650 C  CB  . LEU   C  1  308 ? 11.467  -3.431  21.145 1.00 34.73  ? 321 LEU   C CB  1 
ATOM   7651 C  CG  . LEU   C  1  308 ? 10.790  -3.001  22.447 1.00 39.86  ? 321 LEU   C CG  1 
ATOM   7652 C  CD1 . LEU   C  1  308 ? 11.790  -3.103  23.600 1.00 41.82  ? 321 LEU   C CD1 1 
ATOM   7653 C  CD2 . LEU   C  1  308 ? 10.256  -1.574  22.296 1.00 39.07  ? 321 LEU   C CD2 1 
ATOM   7654 N  N   . ILE   C  1  309 ? 12.070  -4.225  18.205 1.00 31.26  ? 322 ILE   C N   1 
ATOM   7655 C  CA  . ILE   C  1  309 ? 12.777  -3.888  16.981 1.00 33.26  ? 322 ILE   C CA  1 
ATOM   7656 C  C   . ILE   C  1  309 ? 11.793  -3.843  15.816 1.00 32.82  ? 322 ILE   C C   1 
ATOM   7657 O  O   . ILE   C  1  309 ? 11.867  -2.947  14.975 1.00 29.96  ? 322 ILE   C O   1 
ATOM   7658 C  CB  . ILE   C  1  309 ? 13.913  -4.891  16.728 1.00 33.81  ? 322 ILE   C CB  1 
ATOM   7659 C  CG1 . ILE   C  1  309 ? 15.046  -4.680  17.710 1.00 31.78  ? 322 ILE   C CG1 1 
ATOM   7660 C  CG2 . ILE   C  1  309 ? 14.397  -4.834  15.275 1.00 33.32  ? 322 ILE   C CG2 1 
ATOM   7661 C  CD1 . ILE   C  1  309 ? 16.066  -5.799  17.713 1.00 31.26  ? 322 ILE   C CD1 1 
ATOM   7662 N  N   . LYS   C  1  310 ? 10.879  -4.814  15.781 1.00 31.27  ? 323 LYS   C N   1 
ATOM   7663 C  CA  . LYS   C  1  310 ? 9.906   -4.898  14.708 1.00 34.41  ? 323 LYS   C CA  1 
ATOM   7664 C  C   . LYS   C  1  310 ? 8.924   -3.730  14.743 1.00 31.46  ? 323 LYS   C C   1 
ATOM   7665 O  O   . LYS   C  1  310 ? 8.694   -3.083  13.718 1.00 30.10  ? 323 LYS   C O   1 
ATOM   7666 C  CB  . LYS   C  1  310 ? 9.215   -6.256  14.777 1.00 35.96  ? 323 LYS   C CB  1 
ATOM   7667 C  CG  . LYS   C  1  310 ? 10.108  -7.380  14.239 1.00 40.30  ? 323 LYS   C CG  1 
ATOM   7668 C  CD  . LYS   C  1  310 ? 9.475   -8.750  14.396 1.00 48.68  ? 323 LYS   C CD  1 
ATOM   7669 C  CE  . LYS   C  1  310 ? 10.252  -9.810  13.691 1.00 55.29  ? 323 LYS   C CE  1 
ATOM   7670 N  NZ  . LYS   C  1  310 ? 9.736   -11.131 14.057 1.00 59.18  ? 323 LYS   C NZ  1 
ATOM   7671 N  N   . ASN   C  1  311 ? 8.342   -3.469  15.910 1.00 28.18  ? 324 ASN   C N   1 
ATOM   7672 C  CA  . ASN   C  1  311 ? 7.365   -2.405  16.033 1.00 30.10  ? 324 ASN   C CA  1 
ATOM   7673 C  C   . ASN   C  1  311 ? 8.014   -1.065  15.726 1.00 31.00  ? 324 ASN   C C   1 
ATOM   7674 O  O   . ASN   C  1  311 ? 7.391   -0.223  15.084 1.00 36.39  ? 324 ASN   C O   1 
ATOM   7675 C  CB  . ASN   C  1  311 ? 6.681   -2.427  17.394 1.00 32.84  ? 324 ASN   C CB  1 
ATOM   7676 C  CG  . ASN   C  1  311 ? 5.600   -3.472  17.453 1.00 32.17  ? 324 ASN   C CG  1 
ATOM   7677 O  OD1 . ASN   C  1  311 ? 4.480   -3.220  16.998 1.00 36.88  ? 324 ASN   C OD1 1 
ATOM   7678 N  ND2 . ASN   C  1  311 ? 5.881   -4.615  18.057 1.00 31.79  ? 324 ASN   C ND2 1 
ATOM   7679 N  N   . LEU   C  1  312 ? 9.265   -0.881  16.148 1.00 31.66  ? 325 LEU   C N   1 
ATOM   7680 C  CA  . LEU   C  1  312 ? 9.961   0.365   15.872 1.00 32.61  ? 325 LEU   C CA  1 
ATOM   7681 C  C   . LEU   C  1  312 ? 10.095  0.558   14.366 1.00 28.47  ? 325 LEU   C C   1 
ATOM   7682 O  O   . LEU   C  1  312 ? 9.876   1.653   13.860 1.00 27.95  ? 325 LEU   C O   1 
ATOM   7683 C  CB  . LEU   C  1  312 ? 11.317  0.414   16.568 1.00 31.65  ? 325 LEU   C CB  1 
ATOM   7684 C  CG  . LEU   C  1  312 ? 11.265  0.783   18.049 1.00 33.02  ? 325 LEU   C CG  1 
ATOM   7685 C  CD1 . LEU   C  1  312 ? 12.557  0.395   18.685 1.00 32.28  ? 325 LEU   C CD1 1 
ATOM   7686 C  CD2 . LEU   C  1  312 ? 10.994  2.264   18.246 1.00 35.61  ? 325 LEU   C CD2 1 
ATOM   7687 N  N   . HIS   C  1  313 ? 10.446  -0.522  13.672 1.00 30.05  ? 326 HIS   C N   1 
ATOM   7688 C  CA  . HIS   C  1  313 ? 10.620  -0.496  12.230 1.00 28.88  ? 326 HIS   C CA  1 
ATOM   7689 C  C   . HIS   C  1  313 ? 9.280   -0.262  11.539 1.00 26.60  ? 326 HIS   C C   1 
ATOM   7690 O  O   . HIS   C  1  313 ? 9.189   0.548   10.628 1.00 26.84  ? 326 HIS   C O   1 
ATOM   7691 C  CB  . HIS   C  1  313 ? 11.264  -1.797  11.735 1.00 29.68  ? 326 HIS   C CB  1 
ATOM   7692 C  CG  . HIS   C  1  313 ? 11.431  -1.794  10.256 1.00 36.93  ? 326 HIS   C CG  1 
ATOM   7693 N  ND1 . HIS   C  1  313 ? 12.203  -0.850  9.608  1.00 37.13  ? 326 HIS   C ND1 1 
ATOM   7694 C  CD2 . HIS   C  1  313 ? 10.831  -2.524  9.289  1.00 37.51  ? 326 HIS   C CD2 1 
ATOM   7695 C  CE1 . HIS   C  1  313 ? 12.117  -1.057  8.302  1.00 41.07  ? 326 HIS   C CE1 1 
ATOM   7696 N  NE2 . HIS   C  1  313 ? 11.279  -2.057  8.089  1.00 40.23  ? 326 HIS   C NE2 1 
ATOM   7697 N  N   . TYR   C  1  314 ? 8.229   -0.963  11.970 1.00 29.99  ? 327 TYR   C N   1 
ATOM   7698 C  CA  . TYR   C  1  314 ? 6.911   -0.757  11.385 1.00 28.27  ? 327 TYR   C CA  1 
ATOM   7699 C  C   . TYR   C  1  314 ? 6.518   0.703   11.525 1.00 27.42  ? 327 TYR   C C   1 
ATOM   7700 O  O   . TYR   C  1  314 ? 6.012   1.289   10.575 1.00 25.85  ? 327 TYR   C O   1 
ATOM   7701 C  CB  . TYR   C  1  314 ? 5.835   -1.602  12.062 1.00 27.80  ? 327 TYR   C CB  1 
ATOM   7702 C  CG  . TYR   C  1  314 ? 6.083   -3.097  11.987 1.00 25.16  ? 327 TYR   C CG  1 
ATOM   7703 C  CD1 . TYR   C  1  314 ? 6.832   -3.659  10.966 1.00 27.24  ? 327 TYR   C CD1 1 
ATOM   7704 C  CD2 . TYR   C  1  314 ? 5.521   -3.937  12.929 1.00 26.34  ? 327 TYR   C CD2 1 
ATOM   7705 C  CE1 . TYR   C  1  314 ? 7.040   -5.031  10.899 1.00 28.42  ? 327 TYR   C CE1 1 
ATOM   7706 C  CE2 . TYR   C  1  314 ? 5.711   -5.306  12.874 1.00 28.22  ? 327 TYR   C CE2 1 
ATOM   7707 C  CZ  . TYR   C  1  314 ? 6.474   -5.855  11.857 1.00 29.60  ? 327 TYR   C CZ  1 
ATOM   7708 O  OH  . TYR   C  1  314 ? 6.660   -7.207  11.843 1.00 33.09  ? 327 TYR   C OH  1 
ATOM   7709 N  N   . TRP   C  1  315 ? 6.781   1.284   12.700 1.00 26.70  ? 328 TRP   C N   1 
ATOM   7710 C  CA  . TRP   C  1  315 ? 6.393   2.662   12.942 1.00 28.78  ? 328 TRP   C CA  1 
ATOM   7711 C  C   . TRP   C  1  315 ? 7.120   3.538   11.947 1.00 27.33  ? 328 TRP   C C   1 
ATOM   7712 O  O   . TRP   C  1  315 ? 6.521   4.398   11.325 1.00 30.80  ? 328 TRP   C O   1 
ATOM   7713 C  CB  . TRP   C  1  315 ? 6.677   3.095   14.384 1.00 29.65  ? 328 TRP   C CB  1 
ATOM   7714 C  CG  . TRP   C  1  315 ? 6.093   4.430   14.726 1.00 31.12  ? 328 TRP   C CG  1 
ATOM   7715 C  CD1 . TRP   C  1  315 ? 4.820   4.851   14.507 1.00 34.36  ? 328 TRP   C CD1 1 
ATOM   7716 C  CD2 . TRP   C  1  315 ? 6.781   5.537   15.336 1.00 33.90  ? 328 TRP   C CD2 1 
ATOM   7717 N  NE1 . TRP   C  1  315 ? 4.661   6.141   14.938 1.00 33.82  ? 328 TRP   C NE1 1 
ATOM   7718 C  CE2 . TRP   C  1  315 ? 5.839   6.585   15.460 1.00 34.44  ? 328 TRP   C CE2 1 
ATOM   7719 C  CE3 . TRP   C  1  315 ? 8.081   5.733   15.798 1.00 32.79  ? 328 TRP   C CE3 1 
ATOM   7720 C  CZ2 . TRP   C  1  315 ? 6.158   7.807   16.037 1.00 37.28  ? 328 TRP   C CZ2 1 
ATOM   7721 C  CZ3 . TRP   C  1  315 ? 8.395   6.941   16.379 1.00 36.40  ? 328 TRP   C CZ3 1 
ATOM   7722 C  CH2 . TRP   C  1  315 ? 7.456   7.970   16.470 1.00 38.87  ? 328 TRP   C CH2 1 
ATOM   7723 N  N   . TRP   C  1  316 ? 8.410   3.263   11.766 1.00 30.51  ? 329 TRP   C N   1 
ATOM   7724 C  CA  . TRP   C  1  316 ? 9.226   4.089   10.897 1.00 29.46  ? 329 TRP   C CA  1 
ATOM   7725 C  C   . TRP   C  1  316 ? 8.692   4.046   9.467  1.00 29.42  ? 329 TRP   C C   1 
ATOM   7726 O  O   . TRP   C  1  316 ? 8.757   5.043   8.753  1.00 28.62  ? 329 TRP   C O   1 
ATOM   7727 C  CB  . TRP   C  1  316 ? 10.695  3.662   10.960 1.00 30.61  ? 329 TRP   C CB  1 
ATOM   7728 C  CG  . TRP   C  1  316 ? 11.524  4.398   9.948  1.00 31.18  ? 329 TRP   C CG  1 
ATOM   7729 C  CD1 . TRP   C  1  316 ? 12.066  5.642   10.074 1.00 29.98  ? 329 TRP   C CD1 1 
ATOM   7730 C  CD2 . TRP   C  1  316 ? 11.814  3.965   8.607  1.00 30.76  ? 329 TRP   C CD2 1 
ATOM   7731 N  NE1 . TRP   C  1  316 ? 12.700  5.993   8.915  1.00 29.73  ? 329 TRP   C NE1 1 
ATOM   7732 C  CE2 . TRP   C  1  316 ? 12.550  4.996   7.989  1.00 31.71  ? 329 TRP   C CE2 1 
ATOM   7733 C  CE3 . TRP   C  1  316 ? 11.502  2.827   7.865  1.00 36.69  ? 329 TRP   C CE3 1 
ATOM   7734 C  CZ2 . TRP   C  1  316 ? 12.985  4.917   6.668  1.00 30.61  ? 329 TRP   C CZ2 1 
ATOM   7735 C  CZ3 . TRP   C  1  316 ? 11.902  2.763   6.550  1.00 37.05  ? 329 TRP   C CZ3 1 
ATOM   7736 C  CH2 . TRP   C  1  316 ? 12.637  3.791   5.966  1.00 35.03  ? 329 TRP   C CH2 1 
ATOM   7737 N  N   . THR   C  1  317 ? 8.167   2.895   9.022  1.00 32.49  ? 330 THR   C N   1 
ATOM   7738 C  CA  . THR   C  1  317 ? 7.678   2.812   7.643  1.00 30.20  ? 330 THR   C CA  1 
ATOM   7739 C  C   . THR   C  1  317 ? 6.615   3.884   7.416  1.00 31.17  ? 330 THR   C C   1 
ATOM   7740 O  O   . THR   C  1  317 ? 6.558   4.486   6.343  1.00 38.73  ? 330 THR   C O   1 
ATOM   7741 C  CB  . THR   C  1  317 ? 7.115   1.448   7.252  1.00 29.67  ? 330 THR   C CB  1 
ATOM   7742 O  OG1 . THR   C  1  317 ? 5.977   1.180   8.059  1.00 33.07  ? 330 THR   C OG1 1 
ATOM   7743 C  CG2 . THR   C  1  317 ? 8.115   0.309   7.364  1.00 31.36  ? 330 THR   C CG2 1 
ATOM   7744 N  N   . GLY   C  1  318 ? 5.769   4.114   8.424  1.00 30.12  ? 331 GLY   C N   1 
ATOM   7745 C  CA  . GLY   C  1  318 ? 4.740   5.132   8.339  1.00 30.16  ? 331 GLY   C CA  1 
ATOM   7746 C  C   . GLY   C  1  318 ? 5.308   6.536   8.496  1.00 29.52  ? 331 GLY   C C   1 
ATOM   7747 O  O   . GLY   C  1  318 ? 4.923   7.447   7.772  1.00 28.21  ? 331 GLY   C O   1 
ATOM   7748 N  N   . VAL   C  1  319 ? 6.194   6.699   9.474  1.00 30.13  ? 332 VAL   C N   1 
ATOM   7749 C  CA  . VAL   C  1  319 ? 6.768   7.992   9.795  1.00 33.57  ? 332 VAL   C CA  1 
ATOM   7750 C  C   . VAL   C  1  319 ? 7.508   8.528   8.572  1.00 31.82  ? 332 VAL   C C   1 
ATOM   7751 O  O   . VAL   C  1  319 ? 7.466   9.715   8.277  1.00 33.15  ? 332 VAL   C O   1 
ATOM   7752 C  CB  . VAL   C  1  319 ? 7.710   7.860   11.005 1.00 34.22  ? 332 VAL   C CB  1 
ATOM   7753 C  CG1 . VAL   C  1  319 ? 8.567   9.098   11.214 1.00 33.72  ? 332 VAL   C CG1 1 
ATOM   7754 C  CG2 . VAL   C  1  319 ? 6.932   7.497   12.266 1.00 34.56  ? 332 VAL   C CG2 1 
ATOM   7755 N  N   . ASN   C  1  320 ? 8.203   7.640   7.873  1.00 33.00  ? 333 ASN   C N   1 
ATOM   7756 C  CA  . ASN   C  1  320 ? 9.060   8.057   6.780  1.00 34.47  ? 333 ASN   C CA  1 
ATOM   7757 C  C   . ASN   C  1  320 ? 8.242   8.746   5.694  1.00 33.62  ? 333 ASN   C C   1 
ATOM   7758 O  O   . ASN   C  1  320 ? 8.652   9.760   5.135  1.00 32.16  ? 333 ASN   C O   1 
ATOM   7759 C  CB  . ASN   C  1  320 ? 9.818   6.878   6.191  1.00 36.23  ? 333 ASN   C CB  1 
ATOM   7760 C  CG  . ASN   C  1  320 ? 10.897  7.342   5.247  1.00 35.44  ? 333 ASN   C CG  1 
ATOM   7761 O  OD1 . ASN   C  1  320 ? 11.680  8.233   5.602  1.00 37.65  ? 333 ASN   C OD1 1 
ATOM   7762 N  ND2 . ASN   C  1  320 ? 10.938  6.759   4.056  1.00 36.03  ? 333 ASN   C ND2 1 
ATOM   7763 N  N   . VAL   C  1  321 ? 7.079   8.167   5.384  1.00 34.47  ? 334 VAL   C N   1 
ATOM   7764 C  CA  . VAL   C  1  321 ? 6.187   8.751   4.400  1.00 34.03  ? 334 VAL   C CA  1 
ATOM   7765 C  C   . VAL   C  1  321 ? 5.465   9.952   5.015  1.00 38.71  ? 334 VAL   C C   1 
ATOM   7766 O  O   . VAL   C  1  321 ? 5.540   11.055  4.476  1.00 39.88  ? 334 VAL   C O   1 
ATOM   7767 C  CB  . VAL   C  1  321 ? 5.211   7.719   3.821  1.00 36.99  ? 334 VAL   C CB  1 
ATOM   7768 C  CG1 . VAL   C  1  321 ? 4.310   8.356   2.768  1.00 34.80  ? 334 VAL   C CG1 1 
ATOM   7769 C  CG2 . VAL   C  1  321 ? 5.948   6.511   3.228  1.00 35.29  ? 334 VAL   C CG2 1 
ATOM   7770 N  N   . ALA   C  1  322 ? 4.808   9.775   6.168  1.00 39.54  ? 335 ALA   C N   1 
ATOM   7771 C  CA  . ALA   C  1  322 ? 3.966   10.835  6.708  1.00 40.01  ? 335 ALA   C CA  1 
ATOM   7772 C  C   . ALA   C  1  322 ? 4.770   12.087  7.068  1.00 38.86  ? 335 ALA   C C   1 
ATOM   7773 O  O   . ALA   C  1  322 ? 4.242   13.186  6.958  1.00 39.56  ? 335 ALA   C O   1 
ATOM   7774 C  CB  . ALA   C  1  322 ? 3.157   10.354  7.887  1.00 38.64  ? 335 ALA   C CB  1 
ATOM   7775 N  N   . PHE   C  1  323 ? 6.021   11.948  7.503  1.00 39.05  ? 336 PHE   C N   1 
ATOM   7776 C  CA  . PHE   C  1  323 ? 6.793   13.104  7.948  1.00 39.85  ? 336 PHE   C CA  1 
ATOM   7777 C  C   . PHE   C  1  323 ? 7.755   13.585  6.866  1.00 41.24  ? 336 PHE   C C   1 
ATOM   7778 O  O   . PHE   C  1  323 ? 8.582   14.453  7.139  1.00 46.49  ? 336 PHE   C O   1 
ATOM   7779 C  CB  . PHE   C  1  323 ? 7.617   12.796  9.206  1.00 45.54  ? 336 PHE   C CB  1 
ATOM   7780 C  CG  . PHE   C  1  323 ? 6.841   12.557  10.496 1.00 43.88  ? 336 PHE   C CG  1 
ATOM   7781 C  CD1 . PHE   C  1  323 ? 5.451   12.572  10.531 1.00 45.25  ? 336 PHE   C CD1 1 
ATOM   7782 C  CD2 . PHE   C  1  323 ? 7.530   12.290  11.672 1.00 45.67  ? 336 PHE   C CD2 1 
ATOM   7783 C  CE1 . PHE   C  1  323 ? 4.772   12.342  11.714 1.00 48.52  ? 336 PHE   C CE1 1 
ATOM   7784 C  CE2 . PHE   C  1  323 ? 6.846   12.033  12.850 1.00 44.95  ? 336 PHE   C CE2 1 
ATOM   7785 C  CZ  . PHE   C  1  323 ? 5.467   12.055  12.865 1.00 47.12  ? 336 PHE   C CZ  1 
ATOM   7786 N  N   . GLY   C  1  324 ? 7.690   12.981  5.669  1.00 40.28  ? 337 GLY   C N   1 
ATOM   7787 C  CA  . GLY   C  1  324 ? 8.440   13.470  4.525  1.00 38.76  ? 337 GLY   C CA  1 
ATOM   7788 C  C   . GLY   C  1  324 ? 9.924   13.102  4.563  1.00 44.21  ? 337 GLY   C C   1 
ATOM   7789 O  O   . GLY   C  1  324 ? 10.727  13.833  3.996  1.00 48.09  ? 337 GLY   C O   1 
ATOM   7790 N  N   . GLY   C  1  325 ? 10.276  11.968  5.200  1.00 47.48  ? 338 GLY   C N   1 
ATOM   7791 C  CA  . GLY   C  1  325 ? 11.630  11.424  5.210  1.00 45.95  ? 338 GLY   C CA  1 
ATOM   7792 C  C   . GLY   C  1  325 ? 12.359  11.670  6.534  1.00 44.53  ? 338 GLY   C C   1 
ATOM   7793 O  O   . GLY   C  1  325 ? 12.644  12.809  6.853  1.00 43.79  ? 338 GLY   C O   1 
ATOM   7794 N  N   . CYS   C  1  326 ? 12.631  10.604  7.301  1.00 40.90  ? 339 CYS   C N   1 
ATOM   7795 C  CA  . CYS   C  1  326 ? 13.378  10.667  8.548  1.00 44.13  ? 339 CYS   C CA  1 
ATOM   7796 C  C   . CYS   C  1  326 ? 14.373  9.515   8.522  1.00 42.03  ? 339 CYS   C C   1 
ATOM   7797 O  O   . CYS   C  1  326 ? 14.023  8.425   8.074  1.00 39.31  ? 339 CYS   C O   1 
ATOM   7798 C  CB  . CYS   C  1  326 ? 12.514  10.496  9.813  1.00 48.24  ? 339 CYS   C CB  1 
ATOM   7799 S  SG  . CYS   C  1  326 ? 11.275  11.795  10.095 1.00 71.46  ? 339 CYS   C SG  1 
ATOM   7800 N  N   . ASP   C  1  327 ? 15.594  9.732   9.035  1.00 38.52  ? 340 ASP   C N   1 
ATOM   7801 C  CA  . ASP   C  1  327 ? 16.550  8.645   9.155  1.00 42.31  ? 340 ASP   C CA  1 
ATOM   7802 C  C   . ASP   C  1  327 ? 16.112  7.700   10.265 1.00 43.24  ? 340 ASP   C C   1 
ATOM   7803 O  O   . ASP   C  1  327 ? 15.828  8.113   11.385 1.00 45.82  ? 340 ASP   C O   1 
ATOM   7804 C  CB  . ASP   C  1  327 ? 17.965  9.154   9.366  1.00 50.94  ? 340 ASP   C CB  1 
ATOM   7805 C  CG  . ASP   C  1  327 ? 18.631  9.725   8.115  1.00 55.56  ? 340 ASP   C CG  1 
ATOM   7806 O  OD1 . ASP   C  1  327 ? 17.966  9.851   7.079  1.00 58.07  ? 340 ASP   C OD1 1 
ATOM   7807 O  OD2 . ASP   C  1  327 ? 19.834  10.016  8.168  1.00 67.21  ? 340 ASP   C OD2 1 
ATOM   7808 N  N   . GLU   C  1  328 ? 16.064  6.416   9.929  1.00 38.96  ? 341 GLU   C N   1 
ATOM   7809 C  CA  . GLU   C  1  328 ? 15.659  5.406   10.887 1.00 40.79  ? 341 GLU   C CA  1 
ATOM   7810 C  C   . GLU   C  1  328 ? 16.717  5.291   11.988 1.00 38.82  ? 341 GLU   C C   1 
ATOM   7811 O  O   . GLU   C  1  328 ? 17.902  5.274   11.706 1.00 39.01  ? 341 GLU   C O   1 
ATOM   7812 C  CB  . GLU   C  1  328 ? 15.410  4.084   10.156 1.00 37.83  ? 341 GLU   C CB  1 
ATOM   7813 C  CG  . GLU   C  1  328 ? 14.786  3.026   11.061 1.00 36.61  ? 341 GLU   C CG  1 
ATOM   7814 C  CD  . GLU   C  1  328 ? 14.344  1.746   10.386 1.00 36.97  ? 341 GLU   C CD  1 
ATOM   7815 O  OE1 . GLU   C  1  328 ? 14.551  1.601   9.146  1.00 38.82  ? 341 GLU   C OE1 1 
ATOM   7816 O  OE2 . GLU   C  1  328 ? 13.791  0.895   11.132 1.00 33.93  ? 341 GLU   C OE2 1 
ATOM   7817 N  N   . LEU   C  1  329 ? 16.265  5.164   13.233 1.00 38.85  ? 342 LEU   C N   1 
ATOM   7818 C  CA  . LEU   C  1  329 ? 17.114  4.869   14.374 1.00 41.79  ? 342 LEU   C CA  1 
ATOM   7819 C  C   . LEU   C  1  329 ? 16.985  3.398   14.757 1.00 38.28  ? 342 LEU   C C   1 
ATOM   7820 O  O   . LEU   C  1  329 ? 15.925  2.797   14.560 1.00 41.55  ? 342 LEU   C O   1 
ATOM   7821 C  CB  . LEU   C  1  329 ? 16.681  5.778   15.520 1.00 45.30  ? 342 LEU   C CB  1 
ATOM   7822 C  CG  . LEU   C  1  329 ? 16.928  7.276   15.327 1.00 49.46  ? 342 LEU   C CG  1 
ATOM   7823 C  CD1 . LEU   C  1  329 ? 16.255  8.060   16.434 1.00 50.27  ? 342 LEU   C CD1 1 
ATOM   7824 C  CD2 . LEU   C  1  329 ? 18.415  7.559   15.335 1.00 48.41  ? 342 LEU   C CD2 1 
ATOM   7825 N  N   . PHE   C  1  330 ? 18.063  2.847   15.333 1.00 37.33  ? 343 PHE   C N   1 
ATOM   7826 C  CA  . PHE   C  1  330 ? 18.146  1.436   15.677 1.00 35.45  ? 343 PHE   C CA  1 
ATOM   7827 C  C   . PHE   C  1  330 ? 18.613  1.283   17.117 1.00 38.25  ? 343 PHE   C C   1 
ATOM   7828 O  O   . PHE   C  1  330 ? 19.693  0.739   17.358 1.00 37.32  ? 343 PHE   C O   1 
ATOM   7829 C  CB  . PHE   C  1  330 ? 19.106  0.707   14.726 1.00 36.73  ? 343 PHE   C CB  1 
ATOM   7830 C  CG  . PHE   C  1  330 ? 18.665  0.793   13.275 1.00 38.01  ? 343 PHE   C CG  1 
ATOM   7831 C  CD1 . PHE   C  1  330 ? 17.606  0.007   12.810 1.00 37.75  ? 343 PHE   C CD1 1 
ATOM   7832 C  CD2 . PHE   C  1  330 ? 19.264  1.697   12.403 1.00 36.62  ? 343 PHE   C CD2 1 
ATOM   7833 C  CE1 . PHE   C  1  330 ? 17.162  0.109   11.504 1.00 39.68  ? 343 PHE   C CE1 1 
ATOM   7834 C  CE2 . PHE   C  1  330 ? 18.848  1.773   11.074 1.00 42.83  ? 343 PHE   C CE2 1 
ATOM   7835 C  CZ  . PHE   C  1  330 ? 17.789  0.987   10.626 1.00 42.99  ? 343 PHE   C CZ  1 
ATOM   7836 N  N   . PRO   C  1  331 ? 17.824  1.733   18.122 1.00 39.03  ? 344 PRO   C N   1 
ATOM   7837 C  CA  . PRO   C  1  331 ? 18.293  1.728   19.505 1.00 34.04  ? 344 PRO   C CA  1 
ATOM   7838 C  C   . PRO   C  1  331 ? 18.597  0.328   20.022 1.00 30.24  ? 344 PRO   C C   1 
ATOM   7839 O  O   . PRO   C  1  331 ? 19.307  0.196   21.007 1.00 33.76  ? 344 PRO   C O   1 
ATOM   7840 C  CB  . PRO   C  1  331 ? 17.132  2.401   20.259 1.00 35.58  ? 344 PRO   C CB  1 
ATOM   7841 C  CG  . PRO   C  1  331 ? 15.925  2.074   19.415 1.00 36.89  ? 344 PRO   C CG  1 
ATOM   7842 C  CD  . PRO   C  1  331 ? 16.459  2.277   17.999 1.00 36.76  ? 344 PRO   C CD  1 
ATOM   7843 N  N   . TYR   C  1  332 ? 18.045  -0.706  19.374 1.00 29.70  ? 345 TYR   C N   1 
ATOM   7844 C  CA  . TYR   C  1  332 ? 18.267  -2.073  19.818 1.00 28.52  ? 345 TYR   C CA  1 
ATOM   7845 C  C   . TYR   C  1  332 ? 18.978  -2.883  18.735 1.00 27.73  ? 345 TYR   C C   1 
ATOM   7846 O  O   . TYR   C  1  332 ? 19.030  -4.121  18.811 1.00 27.47  ? 345 TYR   C O   1 
ATOM   7847 C  CB  . TYR   C  1  332 ? 16.952  -2.714  20.270 1.00 30.00  ? 345 TYR   C CB  1 
ATOM   7848 C  CG  . TYR   C  1  332 ? 16.219  -1.882  21.306 1.00 31.43  ? 345 TYR   C CG  1 
ATOM   7849 C  CD1 . TYR   C  1  332 ? 16.713  -1.723  22.594 1.00 36.24  ? 345 TYR   C CD1 1 
ATOM   7850 C  CD2 . TYR   C  1  332 ? 15.057  -1.215  20.985 1.00 32.55  ? 345 TYR   C CD2 1 
ATOM   7851 C  CE1 . TYR   C  1  332 ? 16.069  -0.920  23.529 1.00 39.07  ? 345 TYR   C CE1 1 
ATOM   7852 C  CE2 . TYR   C  1  332 ? 14.384  -0.436  21.915 1.00 38.20  ? 345 TYR   C CE2 1 
ATOM   7853 C  CZ  . TYR   C  1  332 ? 14.892  -0.275  23.191 1.00 37.60  ? 345 TYR   C CZ  1 
ATOM   7854 O  OH  . TYR   C  1  332 ? 14.215  0.492   24.095 1.00 37.11  ? 345 TYR   C OH  1 
ATOM   7855 N  N   . GLY   C  1  333 ? 19.560  -2.181  17.755 1.00 29.89  ? 346 GLY   C N   1 
ATOM   7856 C  CA  . GLY   C  1  333 ? 20.202  -2.848  16.626 1.00 36.41  ? 346 GLY   C CA  1 
ATOM   7857 C  C   . GLY   C  1  333 ? 19.188  -3.589  15.751 1.00 35.91  ? 346 GLY   C C   1 
ATOM   7858 O  O   . GLY   C  1  333 ? 18.046  -3.165  15.654 1.00 35.13  ? 346 GLY   C O   1 
ATOM   7859 N  N   . GLN   C  1  334 ? 19.614  -4.700  15.149 1.00 40.85  ? 347 GLN   C N   1 
ATOM   7860 C  CA  . GLN   C  1  334 ? 18.854  -5.399  14.124 1.00 45.96  ? 347 GLN   C CA  1 
ATOM   7861 C  C   . GLN   C  1  334 ? 18.529  -6.802  14.618 1.00 43.92  ? 347 GLN   C C   1 
ATOM   7862 O  O   . GLN   C  1  334 ? 19.128  -7.253  15.597 1.00 41.80  ? 347 GLN   C O   1 
ATOM   7863 C  CB  . GLN   C  1  334 ? 19.678  -5.517  12.839 1.00 52.87  ? 347 GLN   C CB  1 
ATOM   7864 C  CG  . GLN   C  1  334 ? 20.431  -4.249  12.432 1.00 63.04  ? 347 GLN   C CG  1 
ATOM   7865 C  CD  . GLN   C  1  334 ? 19.618  -3.255  11.614 1.00 68.49  ? 347 GLN   C CD  1 
ATOM   7866 O  OE1 . GLN   C  1  334 ? 18.503  -3.533  11.159 1.00 66.75  ? 347 GLN   C OE1 1 
ATOM   7867 N  NE2 . GLN   C  1  334 ? 20.178  -2.071  11.396 1.00 67.46  ? 347 GLN   C NE2 1 
ATOM   7868 N  N   . LEU   C  1  335 ? 17.591  -7.474  13.930 1.00 42.95  ? 348 LEU   C N   1 
ATOM   7869 C  CA  . LEU   C  1  335 ? 17.107  -8.799  14.307 1.00 48.71  ? 348 LEU   C CA  1 
ATOM   7870 C  C   . LEU   C  1  335 ? 18.232  -9.850  14.197 1.00 50.67  ? 348 LEU   C C   1 
ATOM   7871 O  O   . LEU   C  1  335 ? 19.013  -9.752  13.222 1.00 64.77  ? 348 LEU   C O   1 
ATOM   7872 C  CB  . LEU   C  1  335 ? 15.914  -9.214  13.443 1.00 48.31  ? 348 LEU   C CB  1 
ATOM   7873 C  CG  . LEU   C  1  335 ? 14.608  -8.456  13.680 1.00 51.47  ? 348 LEU   C CG  1 
ATOM   7874 C  CD1 . LEU   C  1  335 ? 13.580  -8.795  12.601 1.00 49.22  ? 348 LEU   C CD1 1 
ATOM   7875 C  CD2 . LEU   C  1  335 ? 14.122  -8.786  15.084 1.00 48.88  ? 348 LEU   C CD2 1 
HETATM 7876 C  C1  . NAG   D  2  .   ? 28.924  12.595  34.405 1.00 50.41  ? 1   NAG   H C1  1 
HETATM 7877 C  C2  . NAG   D  2  .   ? 28.829  13.984  35.045 1.00 56.64  ? 1   NAG   H C2  1 
HETATM 7878 C  C3  . NAG   D  2  .   ? 28.419  15.060  34.027 1.00 58.32  ? 1   NAG   H C3  1 
HETATM 7879 C  C4  . NAG   D  2  .   ? 29.041  14.866  32.642 1.00 57.81  ? 1   NAG   H C4  1 
HETATM 7880 C  C5  . NAG   D  2  .   ? 28.914  13.408  32.224 1.00 54.09  ? 1   NAG   H C5  1 
HETATM 7881 C  C6  . NAG   D  2  .   ? 29.468  13.093  30.850 1.00 52.38  ? 1   NAG   H C6  1 
HETATM 7882 C  C7  . NAG   D  2  .   ? 28.175  14.280  37.392 1.00 70.39  ? 1   NAG   H C7  1 
HETATM 7883 C  C8  . NAG   D  2  .   ? 27.027  14.673  38.282 1.00 75.36  ? 1   NAG   H C8  1 
HETATM 7884 N  N2  . NAG   D  2  .   ? 27.877  13.905  36.141 1.00 65.45  ? 1   NAG   H N2  1 
HETATM 7885 O  O3  . NAG   D  2  .   ? 28.780  16.329  34.544 1.00 63.00  ? 1   NAG   H O3  1 
HETATM 7886 O  O4  . NAG   D  2  .   ? 28.361  15.620  31.640 1.00 61.72  ? 1   NAG   H O4  1 
HETATM 7887 O  O5  . NAG   D  2  .   ? 29.655  12.641  33.187 1.00 45.69  ? 1   NAG   H O5  1 
HETATM 7888 O  O6  . NAG   D  2  .   ? 30.874  13.445  30.727 1.00 45.39  ? 1   NAG   H O6  1 
HETATM 7889 O  O7  . NAG   D  2  .   ? 29.340  14.346  37.772 1.00 55.94  ? 1   NAG   H O7  1 
HETATM 7890 C  C1  . NAG   D  2  .   ? 29.046  16.346  30.669 1.00 59.64  ? 2   NAG   H C1  1 
HETATM 7891 C  C2  . NAG   D  2  .   ? 28.224  16.556  29.399 1.00 63.76  ? 2   NAG   H C2  1 
HETATM 7892 C  C3  . NAG   D  2  .   ? 28.961  17.488  28.447 1.00 73.97  ? 2   NAG   H C3  1 
HETATM 7893 C  C4  . NAG   D  2  .   ? 29.319  18.795  29.154 1.00 77.17  ? 2   NAG   H C4  1 
HETATM 7894 C  C5  . NAG   D  2  .   ? 30.103  18.483  30.426 1.00 73.24  ? 2   NAG   H C5  1 
HETATM 7895 C  C6  . NAG   D  2  .   ? 30.428  19.715  31.245 1.00 70.30  ? 2   NAG   H C6  1 
HETATM 7896 C  C7  . NAG   D  2  .   ? 26.669  14.812  28.704 1.00 59.04  ? 2   NAG   H C7  1 
HETATM 7897 C  C8  . NAG   D  2  .   ? 26.501  13.542  27.924 1.00 55.72  ? 2   NAG   H C8  1 
HETATM 7898 N  N2  . NAG   D  2  .   ? 27.870  15.389  28.618 1.00 62.30  ? 2   NAG   H N2  1 
HETATM 7899 O  O3  . NAG   D  2  .   ? 28.113  17.651  27.312 1.00 63.99  ? 2   NAG   H O3  1 
HETATM 7900 O  O4  . NAG   D  2  .   ? 30.176  19.617  28.359 1.00 86.46  ? 2   NAG   H O4  1 
HETATM 7901 O  O5  . NAG   D  2  .   ? 29.330  17.605  31.265 1.00 64.53  ? 2   NAG   H O5  1 
HETATM 7902 O  O6  . NAG   D  2  .   ? 29.256  20.286  31.789 1.00 65.39  ? 2   NAG   H O6  1 
HETATM 7903 O  O7  . NAG   D  2  .   ? 25.769  15.286  29.396 1.00 48.61  ? 2   NAG   H O7  1 
HETATM 7904 C  C1  . BMA   D  2  .   ? 29.668  20.736  27.711 1.00 90.97  ? 3   BMA   H C1  1 
HETATM 7905 C  C2  . BMA   D  2  .   ? 30.812  21.715  27.513 1.00 94.83  ? 3   BMA   H C2  1 
HETATM 7906 C  C3  . BMA   D  2  .   ? 30.368  22.920  26.674 1.00 102.72 ? 3   BMA   H C3  1 
HETATM 7907 C  C4  . BMA   D  2  .   ? 29.564  22.517  25.434 1.00 109.57 ? 3   BMA   H C4  1 
HETATM 7908 C  C5  . BMA   D  2  .   ? 28.553  21.391  25.697 1.00 110.63 ? 3   BMA   H C5  1 
HETATM 7909 C  C6  . BMA   D  2  .   ? 28.033  20.745  24.429 1.00 107.83 ? 3   BMA   H C6  1 
HETATM 7910 O  O2  . BMA   D  2  .   ? 31.930  21.020  26.964 1.00 80.49  ? 3   BMA   H O2  1 
HETATM 7911 O  O3  . BMA   D  2  .   ? 31.527  23.659  26.269 1.00 97.47  ? 3   BMA   H O3  1 
HETATM 7912 O  O4  . BMA   D  2  .   ? 28.834  23.663  24.981 1.00 105.09 ? 3   BMA   H O4  1 
HETATM 7913 O  O5  . BMA   D  2  .   ? 29.151  20.331  26.449 1.00 98.58  ? 3   BMA   H O5  1 
HETATM 7914 O  O6  . BMA   D  2  .   ? 26.924  19.908  24.745 1.00 112.07 ? 3   BMA   H O6  1 
HETATM 7915 C  C1  . MAN   D  2  .   ? 31.741  24.937  26.791 1.00 91.01  ? 4   MAN   H C1  1 
HETATM 7916 C  C2  . MAN   D  2  .   ? 32.249  25.750  25.599 1.00 88.73  ? 4   MAN   H C2  1 
HETATM 7917 C  C3  . MAN   D  2  .   ? 33.707  25.322  25.234 1.00 83.23  ? 4   MAN   H C3  1 
HETATM 7918 C  C4  . MAN   D  2  .   ? 34.622  25.341  26.463 1.00 81.93  ? 4   MAN   H C4  1 
HETATM 7919 C  C5  . MAN   D  2  .   ? 34.002  24.473  27.572 1.00 75.22  ? 4   MAN   H C5  1 
HETATM 7920 C  C6  . MAN   D  2  .   ? 34.811  24.435  28.854 1.00 69.11  ? 4   MAN   H C6  1 
HETATM 7921 O  O2  . MAN   D  2  .   ? 32.036  27.142  25.860 1.00 77.60  ? 4   MAN   H O2  1 
HETATM 7922 O  O3  . MAN   D  2  .   ? 34.260  26.149  24.197 1.00 80.58  ? 4   MAN   H O3  1 
HETATM 7923 O  O4  . MAN   D  2  .   ? 35.931  24.863  26.120 1.00 69.50  ? 4   MAN   H O4  1 
HETATM 7924 O  O5  . MAN   D  2  .   ? 32.682  24.985  27.896 1.00 81.08  ? 4   MAN   H O5  1 
HETATM 7925 O  O6  . MAN   D  2  .   ? 35.145  25.718  29.368 1.00 59.98  ? 4   MAN   H O6  1 
HETATM 7926 C  C1  . MAN   D  2  .   ? 26.080  19.520  23.693 1.00 104.13 ? 5   MAN   H C1  1 
HETATM 7927 C  C2  . MAN   D  2  .   ? 24.770  19.035  24.322 1.00 96.74  ? 5   MAN   H C2  1 
HETATM 7928 C  C3  . MAN   D  2  .   ? 24.976  17.735  25.093 1.00 93.52  ? 5   MAN   H C3  1 
HETATM 7929 C  C4  . MAN   D  2  .   ? 25.560  16.696  24.157 1.00 99.03  ? 5   MAN   H C4  1 
HETATM 7930 C  C5  . MAN   D  2  .   ? 26.897  17.198  23.567 1.00 107.76 ? 5   MAN   H C5  1 
HETATM 7931 C  C6  . MAN   D  2  .   ? 27.469  16.234  22.543 1.00 98.33  ? 5   MAN   H C6  1 
HETATM 7932 O  O2  . MAN   D  2  .   ? 23.783  18.898  23.307 1.00 88.65  ? 5   MAN   H O2  1 
HETATM 7933 O  O3  . MAN   D  2  .   ? 23.761  17.268  25.676 1.00 77.94  ? 5   MAN   H O3  1 
HETATM 7934 O  O4  . MAN   D  2  .   ? 25.769  15.486  24.868 1.00 99.62  ? 5   MAN   H O4  1 
HETATM 7935 O  O5  . MAN   D  2  .   ? 26.715  18.492  22.902 1.00 111.20 ? 5   MAN   H O5  1 
HETATM 7936 O  O6  . MAN   D  2  .   ? 28.389  16.868  21.637 1.00 89.75  ? 5   MAN   H O6  1 
HETATM 7937 C  C1  . NAG   E  3  .   ? 28.101  -8.878  19.711 1.00 43.68  ? 1   NAG   J C1  1 
HETATM 7938 C  C2  . NAG   E  3  .   ? 28.720  -9.809  18.677 1.00 44.82  ? 1   NAG   J C2  1 
HETATM 7939 C  C3  . NAG   E  3  .   ? 28.068  -9.600  17.322 1.00 43.47  ? 1   NAG   J C3  1 
HETATM 7940 C  C4  . NAG   E  3  .   ? 26.560  -9.738  17.439 1.00 50.19  ? 1   NAG   J C4  1 
HETATM 7941 C  C5  . NAG   E  3  .   ? 26.038  -8.775  18.509 1.00 48.63  ? 1   NAG   J C5  1 
HETATM 7942 C  C6  . NAG   E  3  .   ? 24.548  -8.901  18.749 1.00 42.06  ? 1   NAG   J C6  1 
HETATM 7943 C  C7  . NAG   E  3  .   ? 31.017  -10.576 18.941 1.00 45.47  ? 1   NAG   J C7  1 
HETATM 7944 C  C8  . NAG   E  3  .   ? 32.473  -10.272 18.746 1.00 45.14  ? 1   NAG   J C8  1 
HETATM 7945 N  N2  . NAG   E  3  .   ? 30.153  -9.617  18.590 1.00 44.91  ? 1   NAG   J N2  1 
HETATM 7946 O  O3  . NAG   E  3  .   ? 28.600  -10.584 16.460 1.00 38.88  ? 1   NAG   J O3  1 
HETATM 7947 O  O4  . NAG   E  3  .   ? 25.988  -9.466  16.162 1.00 53.62  ? 1   NAG   J O4  1 
HETATM 7948 O  O5  . NAG   E  3  .   ? 26.691  -9.075  19.758 1.00 42.22  ? 1   NAG   J O5  1 
HETATM 7949 O  O6  . NAG   E  3  .   ? 24.188  -10.239 19.107 1.00 39.19  ? 1   NAG   J O6  1 
HETATM 7950 O  O7  . NAG   E  3  .   ? 30.643  -11.655 19.388 1.00 40.33  ? 1   NAG   J O7  1 
HETATM 7951 C  C1  . NAG   E  3  .   ? 25.717  -10.591 15.388 1.00 56.87  ? 2   NAG   J C1  1 
HETATM 7952 C  C2  . NAG   E  3  .   ? 24.401  -10.416 14.647 1.00 54.79  ? 2   NAG   J C2  1 
HETATM 7953 C  C3  . NAG   E  3  .   ? 24.214  -11.490 13.584 1.00 63.63  ? 2   NAG   J C3  1 
HETATM 7954 C  C4  . NAG   E  3  .   ? 25.454  -11.643 12.720 1.00 71.77  ? 2   NAG   J C4  1 
HETATM 7955 C  C5  . NAG   E  3  .   ? 26.712  -11.803 13.566 1.00 68.20  ? 2   NAG   J C5  1 
HETATM 7956 C  C6  . NAG   E  3  .   ? 27.962  -11.737 12.728 1.00 63.53  ? 2   NAG   J C6  1 
HETATM 7957 C  C7  . NAG   E  3  .   ? 22.565  -9.351  15.803 1.00 49.94  ? 2   NAG   J C7  1 
HETATM 7958 C  C8  . NAG   E  3  .   ? 21.375  -9.533  16.704 1.00 48.40  ? 2   NAG   J C8  1 
HETATM 7959 N  N2  . NAG   E  3  .   ? 23.260  -10.457 15.529 1.00 49.26  ? 2   NAG   J N2  1 
HETATM 7960 O  O3  . NAG   E  3  .   ? 23.125  -11.090 12.770 1.00 49.94  ? 2   NAG   J O3  1 
HETATM 7961 O  O4  . NAG   E  3  .   ? 25.269  -12.772 11.860 1.00 72.59  ? 2   NAG   J O4  1 
HETATM 7962 O  O5  . NAG   E  3  .   ? 26.811  -10.702 14.487 1.00 63.09  ? 2   NAG   J O5  1 
HETATM 7963 O  O6  . NAG   E  3  .   ? 29.093  -12.057 13.499 1.00 73.19  ? 2   NAG   J O6  1 
HETATM 7964 O  O7  . NAG   E  3  .   ? 22.906  -8.251  15.361 1.00 42.00  ? 2   NAG   J O7  1 
HETATM 7965 C  C1  . BMA   E  3  .   ? 25.606  -12.426 10.554 1.00 84.14  ? 3   BMA   J C1  1 
HETATM 7966 C  C2  . BMA   E  3  .   ? 25.758  -13.711 9.758  1.00 88.45  ? 3   BMA   J C2  1 
HETATM 7967 C  C3  . BMA   E  3  .   ? 26.148  -13.369 8.324  1.00 97.85  ? 3   BMA   J C3  1 
HETATM 7968 C  C4  . BMA   E  3  .   ? 25.225  -12.315 7.712  1.00 96.88  ? 3   BMA   J C4  1 
HETATM 7969 C  C5  . BMA   E  3  .   ? 25.107  -11.095 8.631  1.00 92.06  ? 3   BMA   J C5  1 
HETATM 7970 C  C6  . BMA   E  3  .   ? 24.110  -10.062 8.142  1.00 94.72  ? 3   BMA   J C6  1 
HETATM 7971 O  O2  . BMA   E  3  .   ? 24.585  -14.512 9.872  1.00 66.21  ? 3   BMA   J O2  1 
HETATM 7972 O  O3  . BMA   E  3  .   ? 26.136  -14.569 7.558  1.00 102.74 ? 3   BMA   J O3  1 
HETATM 7973 O  O4  . BMA   E  3  .   ? 25.737  -11.893 6.443  1.00 92.56  ? 3   BMA   J O4  1 
HETATM 7974 O  O5  . BMA   E  3  .   ? 24.658  -11.567 9.920  1.00 88.35  ? 3   BMA   J O5  1 
HETATM 7975 O  O6  . BMA   E  3  .   ? 22.841  -10.678 7.909  1.00 102.32 ? 3   BMA   J O6  1 
HETATM 7976 C  C1  . MAN   E  3  .   ? 21.899  -10.018 7.101  1.00 103.48 ? 4   MAN   J C1  1 
HETATM 7977 C  C2  . MAN   E  3  .   ? 20.544  -10.539 7.567  1.00 101.74 ? 4   MAN   J C2  1 
HETATM 7978 C  C3  . MAN   E  3  .   ? 20.314  -12.000 7.145  1.00 108.48 ? 4   MAN   J C3  1 
HETATM 7979 C  C4  . MAN   E  3  .   ? 20.724  -12.295 5.703  1.00 116.07 ? 4   MAN   J C4  1 
HETATM 7980 C  C5  . MAN   E  3  .   ? 22.108  -11.722 5.399  1.00 126.18 ? 4   MAN   J C5  1 
HETATM 7981 C  C6  . MAN   E  3  .   ? 22.549  -11.901 3.952  1.00 135.06 ? 4   MAN   J C6  1 
HETATM 7982 O  O2  . MAN   E  3  .   ? 19.497  -9.663  7.159  1.00 86.35  ? 4   MAN   J O2  1 
HETATM 7983 O  O3  . MAN   E  3  .   ? 18.936  -12.305 7.311  1.00 107.58 ? 4   MAN   J O3  1 
HETATM 7984 O  O4  . MAN   E  3  .   ? 20.748  -13.710 5.499  1.00 109.31 ? 4   MAN   J O4  1 
HETATM 7985 O  O5  . MAN   E  3  .   ? 22.099  -10.299 5.710  1.00 113.81 ? 4   MAN   J O5  1 
HETATM 7986 O  O6  . MAN   E  3  .   ? 21.484  -11.658 2.997  1.00 155.17 ? 4   MAN   J O6  1 
HETATM 7987 C  C1  . MAN   E  3  .   ? 18.654  -13.562 7.846  1.00 111.97 ? 5   MAN   J C1  1 
HETATM 7988 C  C2  . MAN   E  3  .   ? 17.280  -13.923 7.364  1.00 116.16 ? 5   MAN   J C2  1 
HETATM 7989 C  C3  . MAN   E  3  .   ? 16.257  -12.891 7.840  1.00 116.26 ? 5   MAN   J C3  1 
HETATM 7990 C  C4  . MAN   E  3  .   ? 16.304  -12.750 9.362  1.00 115.72 ? 5   MAN   J C4  1 
HETATM 7991 C  C5  . MAN   E  3  .   ? 17.752  -12.601 9.880  1.00 114.18 ? 5   MAN   J C5  1 
HETATM 7992 C  C6  . MAN   E  3  .   ? 17.853  -12.786 11.380 1.00 108.64 ? 5   MAN   J C6  1 
HETATM 7993 O  O2  . MAN   E  3  .   ? 16.968  -15.235 7.821  1.00 103.08 ? 5   MAN   J O2  1 
HETATM 7994 O  O3  . MAN   E  3  .   ? 14.944  -13.272 7.401  1.00 111.09 ? 5   MAN   J O3  1 
HETATM 7995 O  O4  . MAN   E  3  .   ? 15.567  -11.593 9.770  1.00 95.33  ? 5   MAN   J O4  1 
HETATM 7996 O  O5  . MAN   E  3  .   ? 18.635  -13.588 9.278  1.00 114.28 ? 5   MAN   J O5  1 
HETATM 7997 O  O6  . MAN   E  3  .   ? 18.877  -11.961 11.927 1.00 96.31  ? 5   MAN   J O6  1 
HETATM 7998 C  C1  . MAN   E  3  .   ? 21.805  -11.872 1.645  1.00 150.44 ? 6   MAN   J C1  1 
HETATM 7999 C  C2  . MAN   E  3  .   ? 22.374  -10.560 1.080  1.00 147.66 ? 6   MAN   J C2  1 
HETATM 8000 C  C3  . MAN   E  3  .   ? 21.291  -9.498  0.880  1.00 142.79 ? 6   MAN   J C3  1 
HETATM 8001 C  C4  . MAN   E  3  .   ? 20.128  -10.072 0.083  1.00 143.85 ? 6   MAN   J C4  1 
HETATM 8002 C  C5  . MAN   E  3  .   ? 19.580  -11.293 0.825  1.00 137.84 ? 6   MAN   J C5  1 
HETATM 8003 C  C6  . MAN   E  3  .   ? 18.394  -11.939 0.144  1.00 124.74 ? 6   MAN   J C6  1 
HETATM 8004 O  O2  . MAN   E  3  .   ? 23.079  -10.817 -0.132 1.00 137.10 ? 6   MAN   J O2  1 
HETATM 8005 O  O3  . MAN   E  3  .   ? 21.838  -8.351  0.231  1.00 125.59 ? 6   MAN   J O3  1 
HETATM 8006 O  O4  . MAN   E  3  .   ? 19.102  -9.098  -0.070 1.00 143.90 ? 6   MAN   J O4  1 
HETATM 8007 O  O5  . MAN   E  3  .   ? 20.624  -12.300 0.928  1.00 142.77 ? 6   MAN   J O5  1 
HETATM 8008 O  O6  . MAN   E  3  .   ? 17.541  -12.561 1.120  1.00 108.33 ? 6   MAN   J O6  1 
HETATM 8009 C  C1  . MAN   E  3  .   ? 27.338  -15.277 7.548  1.00 117.72 ? 7   MAN   J C1  1 
HETATM 8010 C  C2  . MAN   E  3  .   ? 27.508  -15.771 6.116  1.00 126.64 ? 7   MAN   J C2  1 
HETATM 8011 C  C3  . MAN   E  3  .   ? 26.615  -16.986 5.796  1.00 130.09 ? 7   MAN   J C3  1 
HETATM 8012 C  C4  . MAN   E  3  .   ? 26.565  -18.022 6.928  1.00 119.12 ? 7   MAN   J C4  1 
HETATM 8013 C  C5  . MAN   E  3  .   ? 26.345  -17.365 8.292  1.00 110.69 ? 7   MAN   J C5  1 
HETATM 8014 C  C6  . MAN   E  3  .   ? 26.418  -18.357 9.438  1.00 98.58  ? 7   MAN   J C6  1 
HETATM 8015 O  O2  . MAN   E  3  .   ? 28.888  -16.021 5.850  1.00 119.94 ? 7   MAN   J O2  1 
HETATM 8016 O  O3  . MAN   E  3  .   ? 27.092  -17.595 4.585  1.00 133.68 ? 7   MAN   J O3  1 
HETATM 8017 O  O4  . MAN   E  3  .   ? 25.484  -18.938 6.717  1.00 101.46 ? 7   MAN   J O4  1 
HETATM 8018 O  O5  . MAN   E  3  .   ? 27.359  -16.356 8.506  1.00 115.35 ? 7   MAN   J O5  1 
HETATM 8019 O  O6  . MAN   E  3  .   ? 27.655  -18.283 10.132 1.00 102.64 ? 7   MAN   J O6  1 
HETATM 8020 C  C1  . NAG   F  2  .   ? 25.054  -10.701 69.015 1.00 53.34  ? 1   NAG   Y C1  1 
HETATM 8021 C  C2  . NAG   F  2  .   ? 25.290  -9.815  70.222 1.00 62.62  ? 1   NAG   Y C2  1 
HETATM 8022 C  C3  . NAG   F  2  .   ? 26.179  -10.619 71.156 1.00 63.65  ? 1   NAG   Y C3  1 
HETATM 8023 C  C4  . NAG   F  2  .   ? 25.331  -11.747 71.718 1.00 64.77  ? 1   NAG   Y C4  1 
HETATM 8024 C  C5  . NAG   F  2  .   ? 24.706  -12.566 70.578 1.00 61.78  ? 1   NAG   Y C5  1 
HETATM 8025 C  C6  . NAG   F  2  .   ? 23.533  -13.434 71.029 1.00 58.14  ? 1   NAG   Y C6  1 
HETATM 8026 C  C7  . NAG   F  2  .   ? 26.709  -8.121  69.204 1.00 67.74  ? 1   NAG   Y C7  1 
HETATM 8027 C  C8  . NAG   F  2  .   ? 26.952  -6.647  69.070 1.00 63.22  ? 1   NAG   Y C8  1 
HETATM 8028 N  N2  . NAG   F  2  .   ? 25.718  -8.450  70.018 1.00 71.94  ? 1   NAG   Y N2  1 
HETATM 8029 O  O3  . NAG   F  2  .   ? 26.712  -9.821  72.196 1.00 60.78  ? 1   NAG   Y O3  1 
HETATM 8030 O  O4  . NAG   F  2  .   ? 26.169  -12.540 72.557 1.00 72.38  ? 1   NAG   Y O4  1 
HETATM 8031 O  O5  . NAG   F  2  .   ? 24.194  -11.733 69.508 1.00 58.24  ? 1   NAG   Y O5  1 
HETATM 8032 O  O6  . NAG   F  2  .   ? 22.588  -12.749 71.874 1.00 53.48  ? 1   NAG   Y O6  1 
HETATM 8033 O  O7  . NAG   F  2  .   ? 27.372  -8.977  68.621 1.00 68.01  ? 1   NAG   Y O7  1 
HETATM 8034 C  C1  . NAG   F  2  .   ? 25.617  -12.802 73.812 1.00 73.78  ? 2   NAG   Y C1  1 
HETATM 8035 C  C2  . NAG   F  2  .   ? 26.121  -14.124 74.366 1.00 73.42  ? 2   NAG   Y C2  1 
HETATM 8036 C  C3  . NAG   F  2  .   ? 25.488  -14.355 75.738 1.00 79.32  ? 2   NAG   Y C3  1 
HETATM 8037 C  C4  . NAG   F  2  .   ? 25.715  -13.150 76.655 1.00 84.12  ? 2   NAG   Y C4  1 
HETATM 8038 C  C5  . NAG   F  2  .   ? 25.217  -11.879 75.973 1.00 79.50  ? 2   NAG   Y C5  1 
HETATM 8039 C  C6  . NAG   F  2  .   ? 25.449  -10.606 76.767 1.00 77.81  ? 2   NAG   Y C6  1 
HETATM 8040 C  C7  . NAG   F  2  .   ? 26.787  -15.688 72.576 1.00 70.88  ? 2   NAG   Y C7  1 
HETATM 8041 C  C8  . NAG   F  2  .   ? 26.330  -16.734 71.601 1.00 66.63  ? 2   NAG   Y C8  1 
HETATM 8042 N  N2  . NAG   F  2  .   ? 25.872  -15.212 73.437 1.00 77.23  ? 2   NAG   Y N2  1 
HETATM 8043 O  O3  . NAG   F  2  .   ? 26.033  -15.553 76.282 1.00 73.88  ? 2   NAG   Y O3  1 
HETATM 8044 O  O4  . NAG   F  2  .   ? 25.007  -13.286 77.898 1.00 91.72  ? 2   NAG   Y O4  1 
HETATM 8045 O  O5  . NAG   F  2  .   ? 25.922  -11.749 74.724 1.00 77.39  ? 2   NAG   Y O5  1 
HETATM 8046 O  O6  . NAG   F  2  .   ? 26.811  -10.190 76.755 1.00 85.83  ? 2   NAG   Y O6  1 
HETATM 8047 O  O7  . NAG   F  2  .   ? 27.942  -15.275 72.575 1.00 70.32  ? 2   NAG   Y O7  1 
HETATM 8048 C  C1  . BMA   F  2  .   ? 25.709  -13.777 79.001 1.00 98.78  ? 3   BMA   Y C1  1 
HETATM 8049 C  C2  . BMA   F  2  .   ? 24.892  -13.530 80.274 1.00 96.98  ? 3   BMA   Y C2  1 
HETATM 8050 C  C3  . BMA   F  2  .   ? 25.558  -14.191 81.473 1.00 101.10 ? 3   BMA   Y C3  1 
HETATM 8051 C  C4  . BMA   F  2  .   ? 25.918  -15.643 81.203 1.00 104.99 ? 3   BMA   Y C4  1 
HETATM 8052 C  C5  . BMA   F  2  .   ? 26.756  -15.757 79.928 1.00 105.50 ? 3   BMA   Y C5  1 
HETATM 8053 C  C6  . BMA   F  2  .   ? 27.037  -17.191 79.541 1.00 103.60 ? 3   BMA   Y C6  1 
HETATM 8054 O  O2  . BMA   F  2  .   ? 23.534  -13.944 80.132 1.00 86.78  ? 3   BMA   Y O2  1 
HETATM 8055 O  O3  . BMA   F  2  .   ? 24.682  -14.119 82.605 1.00 92.15  ? 3   BMA   Y O3  1 
HETATM 8056 O  O4  . BMA   F  2  .   ? 26.645  -16.167 82.325 1.00 98.91  ? 3   BMA   Y O4  1 
HETATM 8057 O  O5  . BMA   F  2  .   ? 26.027  -15.170 78.829 1.00 100.16 ? 3   BMA   Y O5  1 
HETATM 8058 O  O6  . BMA   F  2  .   ? 28.187  -17.296 78.671 1.00 98.92  ? 3   BMA   Y O6  1 
HETATM 8059 C  C1  . MAN   F  2  .   ? 25.085  -13.202 83.581 1.00 81.37  ? 4   MAN   Y C1  1 
HETATM 8060 C  C2  . MAN   F  2  .   ? 24.474  -13.591 84.933 1.00 76.21  ? 4   MAN   Y C2  1 
HETATM 8061 C  C3  . MAN   F  2  .   ? 22.930  -13.436 84.921 1.00 69.85  ? 4   MAN   Y C3  1 
HETATM 8062 C  C4  . MAN   F  2  .   ? 22.545  -11.996 84.568 1.00 64.44  ? 4   MAN   Y C4  1 
HETATM 8063 C  C5  . MAN   F  2  .   ? 23.245  -11.573 83.241 1.00 71.50  ? 4   MAN   Y C5  1 
HETATM 8064 C  C6  . MAN   F  2  .   ? 23.096  -10.087 82.994 1.00 71.35  ? 4   MAN   Y C6  1 
HETATM 8065 O  O2  . MAN   F  2  .   ? 25.088  -12.814 85.970 1.00 58.33  ? 4   MAN   Y O2  1 
HETATM 8066 O  O3  . MAN   F  2  .   ? 22.370  -13.786 86.193 1.00 61.86  ? 4   MAN   Y O3  1 
HETATM 8067 O  O4  . MAN   F  2  .   ? 21.095  -11.879 84.466 1.00 49.92  ? 4   MAN   Y O4  1 
HETATM 8068 O  O5  . MAN   F  2  .   ? 24.706  -11.862 83.237 1.00 70.95  ? 4   MAN   Y O5  1 
HETATM 8069 O  O6  . MAN   F  2  .   ? 21.740  -9.699  83.266 1.00 76.82  ? 4   MAN   Y O6  1 
HETATM 8070 C  C1  . MAN   F  2  .   ? 28.510  -18.631 78.359 1.00 92.09  ? 5   MAN   Y C1  1 
HETATM 8071 C  C2  . MAN   F  2  .   ? 29.866  -18.628 77.641 1.00 84.10  ? 5   MAN   Y C2  1 
HETATM 8072 C  C3  . MAN   F  2  .   ? 29.787  -17.975 76.265 1.00 77.44  ? 5   MAN   Y C3  1 
HETATM 8073 C  C4  . MAN   F  2  .   ? 28.772  -18.750 75.415 1.00 72.55  ? 5   MAN   Y C4  1 
HETATM 8074 C  C5  . MAN   F  2  .   ? 27.382  -18.711 76.155 1.00 80.02  ? 5   MAN   Y C5  1 
HETATM 8075 C  C6  . MAN   F  2  .   ? 26.276  -19.500 75.459 1.00 80.96  ? 5   MAN   Y C6  1 
HETATM 8076 O  O2  . MAN   F  2  .   ? 30.337  -19.973 77.467 1.00 77.02  ? 5   MAN   Y O2  1 
HETATM 8077 O  O3  . MAN   F  2  .   ? 31.081  -17.971 75.640 1.00 62.72  ? 5   MAN   Y O3  1 
HETATM 8078 O  O4  . MAN   F  2  .   ? 28.762  -18.174 74.089 1.00 61.45  ? 5   MAN   Y O4  1 
HETATM 8079 O  O5  . MAN   F  2  .   ? 27.503  -19.257 77.540 1.00 81.54  ? 5   MAN   Y O5  1 
HETATM 8080 O  O6  . MAN   F  2  .   ? 25.751  -18.780 74.301 1.00 76.42  ? 5   MAN   Y O6  1 
HETATM 8081 C  C1  . NAG   G  4  .   ? 15.696  -30.156 55.090 1.00 46.19  ? 1   NAG   Z C1  1 
HETATM 8082 C  C2  . NAG   G  4  .   ? 14.612  -31.147 54.673 1.00 49.21  ? 1   NAG   Z C2  1 
HETATM 8083 C  C3  . NAG   G  4  .   ? 14.978  -32.525 55.194 1.00 48.35  ? 1   NAG   Z C3  1 
HETATM 8084 C  C4  . NAG   G  4  .   ? 16.348  -32.918 54.656 1.00 45.80  ? 1   NAG   Z C4  1 
HETATM 8085 C  C5  . NAG   G  4  .   ? 17.394  -31.898 55.076 1.00 45.32  ? 1   NAG   Z C5  1 
HETATM 8086 C  C6  . NAG   G  4  .   ? 18.755  -32.197 54.470 1.00 39.37  ? 1   NAG   Z C6  1 
HETATM 8087 C  C7  . NAG   G  4  .   ? 12.286  -30.432 54.293 1.00 54.68  ? 1   NAG   Z C7  1 
HETATM 8088 C  C8  . NAG   G  4  .   ? 10.922  -30.280 54.896 1.00 56.73  ? 1   NAG   Z C8  1 
HETATM 8089 N  N2  . NAG   G  4  .   ? 13.279  -30.791 55.124 1.00 50.26  ? 1   NAG   Z N2  1 
HETATM 8090 O  O3  . NAG   G  4  .   ? 13.948  -33.407 54.775 1.00 44.99  ? 1   NAG   Z O3  1 
HETATM 8091 O  O4  . NAG   G  4  .   ? 16.752  -34.156 55.213 1.00 49.44  ? 1   NAG   Z O4  1 
HETATM 8092 O  O5  . NAG   G  4  .   ? 16.983  -30.585 54.643 1.00 45.68  ? 1   NAG   Z O5  1 
HETATM 8093 O  O6  . NAG   G  4  .   ? 18.695  -32.193 53.052 1.00 38.86  ? 1   NAG   Z O6  1 
HETATM 8094 O  O7  . NAG   G  4  .   ? 12.473  -30.222 53.101 1.00 49.07  ? 1   NAG   Z O7  1 
HETATM 8095 C  C1  . NAG   G  4  .   ? 16.480  -35.257 54.414 1.00 58.74  ? 2   NAG   Z C1  1 
HETATM 8096 C  C2  . NAG   G  4  .   ? 17.557  -36.311 54.609 1.00 58.18  ? 2   NAG   Z C2  1 
HETATM 8097 C  C3  . NAG   G  4  .   ? 17.171  -37.637 53.966 1.00 67.95  ? 2   NAG   Z C3  1 
HETATM 8098 C  C4  . NAG   G  4  .   ? 15.736  -37.995 54.316 1.00 76.84  ? 2   NAG   Z C4  1 
HETATM 8099 C  C5  . NAG   G  4  .   ? 14.825  -36.840 53.908 1.00 79.57  ? 2   NAG   Z C5  1 
HETATM 8100 C  C6  . NAG   G  4  .   ? 13.334  -37.079 54.071 1.00 76.45  ? 2   NAG   Z C6  1 
HETATM 8101 C  C7  . NAG   G  4  .   ? 19.861  -35.542 54.683 1.00 53.83  ? 2   NAG   Z C7  1 
HETATM 8102 C  C8  . NAG   G  4  .   ? 21.065  -35.148 53.877 1.00 55.04  ? 2   NAG   Z C8  1 
HETATM 8103 N  N2  . NAG   G  4  .   ? 18.775  -35.865 53.983 1.00 55.11  ? 2   NAG   Z N2  1 
HETATM 8104 O  O3  . NAG   G  4  .   ? 18.075  -38.643 54.401 1.00 57.02  ? 2   NAG   Z O3  1 
HETATM 8105 O  O4  . NAG   G  4  .   ? 15.399  -39.204 53.640 1.00 92.92  ? 2   NAG   Z O4  1 
HETATM 8106 O  O5  . NAG   G  4  .   ? 15.198  -35.755 54.774 1.00 67.49  ? 2   NAG   Z O5  1 
HETATM 8107 O  O6  . NAG   G  4  .   ? 12.957  -37.081 55.440 1.00 76.73  ? 2   NAG   Z O6  1 
HETATM 8108 O  O7  . NAG   G  4  .   ? 19.849  -35.544 55.912 1.00 43.06  ? 2   NAG   Z O7  1 
HETATM 8109 C  C1  . BMA   G  4  .   ? 14.880  -40.164 54.504 1.00 97.59  ? 3   BMA   Z C1  1 
HETATM 8110 C  C2  . BMA   G  4  .   ? 14.160  -41.178 53.633 1.00 94.40  ? 3   BMA   Z C2  1 
HETATM 8111 C  C3  . BMA   G  4  .   ? 13.565  -42.237 54.554 1.00 103.76 ? 3   BMA   Z C3  1 
HETATM 8112 C  C4  . BMA   G  4  .   ? 14.697  -42.882 55.351 1.00 97.93  ? 3   BMA   Z C4  1 
HETATM 8113 C  C5  . BMA   G  4  .   ? 15.386  -41.796 56.184 1.00 98.06  ? 3   BMA   Z C5  1 
HETATM 8114 C  C6  . BMA   G  4  .   ? 16.555  -42.284 57.029 1.00 105.38 ? 3   BMA   Z C6  1 
HETATM 8115 O  O2  . BMA   G  4  .   ? 15.056  -41.636 52.621 1.00 75.32  ? 3   BMA   Z O2  1 
HETATM 8116 O  O3  . BMA   G  4  .   ? 12.712  -43.173 53.855 1.00 122.20 ? 3   BMA   Z O3  1 
HETATM 8117 O  O4  . BMA   G  4  .   ? 14.208  -43.888 56.242 1.00 89.27  ? 3   BMA   Z O4  1 
HETATM 8118 O  O5  . BMA   G  4  .   ? 15.894  -40.799 55.284 1.00 95.50  ? 3   BMA   Z O5  1 
HETATM 8119 O  O6  . BMA   G  4  .   ? 17.446  -43.176 56.322 1.00 105.80 ? 3   BMA   Z O6  1 
HETATM 8120 C  C1  . MAN   G  4  .   ? 18.606  -43.557 57.027 1.00 102.70 ? 4   MAN   Z C1  1 
HETATM 8121 C  C2  . MAN   G  4  .   ? 19.702  -43.823 56.007 1.00 105.63 ? 4   MAN   Z C2  1 
HETATM 8122 C  C3  . MAN   G  4  .   ? 19.300  -44.929 55.041 1.00 107.48 ? 4   MAN   Z C3  1 
HETATM 8123 C  C4  . MAN   G  4  .   ? 18.784  -46.175 55.771 1.00 107.50 ? 4   MAN   Z C4  1 
HETATM 8124 C  C5  . MAN   G  4  .   ? 17.941  -45.886 57.046 1.00 106.19 ? 4   MAN   Z C5  1 
HETATM 8125 C  C6  . MAN   G  4  .   ? 17.961  -47.042 58.023 1.00 103.51 ? 4   MAN   Z C6  1 
HETATM 8126 O  O2  . MAN   G  4  .   ? 20.915  -44.148 56.681 1.00 97.44  ? 4   MAN   Z O2  1 
HETATM 8127 O  O3  . MAN   G  4  .   ? 20.434  -45.280 54.241 1.00 104.30 ? 4   MAN   Z O3  1 
HETATM 8128 O  O4  . MAN   G  4  .   ? 17.965  -46.912 54.864 1.00 100.89 ? 4   MAN   Z O4  1 
HETATM 8129 O  O5  . MAN   G  4  .   ? 18.423  -44.744 57.798 1.00 101.89 ? 4   MAN   Z O5  1 
HETATM 8130 O  O6  . MAN   G  4  .   ? 17.212  -48.167 57.535 1.00 106.70 ? 4   MAN   Z O6  1 
HETATM 8131 C  C1  . MAN   G  4  .   ? 20.316  -45.143 52.858 1.00 100.15 ? 5   MAN   Z C1  1 
HETATM 8132 C  C2  . MAN   G  4  .   ? 21.444  -45.957 52.268 1.00 100.92 ? 5   MAN   Z C2  1 
HETATM 8133 C  C3  . MAN   G  4  .   ? 22.796  -45.353 52.617 1.00 108.21 ? 5   MAN   Z C3  1 
HETATM 8134 C  C4  . MAN   G  4  .   ? 22.863  -43.906 52.147 1.00 109.19 ? 5   MAN   Z C4  1 
HETATM 8135 C  C5  . MAN   G  4  .   ? 21.670  -43.112 52.715 1.00 115.09 ? 5   MAN   Z C5  1 
HETATM 8136 C  C6  . MAN   G  4  .   ? 21.578  -41.704 52.160 1.00 114.19 ? 5   MAN   Z C6  1 
HETATM 8137 O  O2  . MAN   G  4  .   ? 21.271  -46.037 50.856 1.00 88.14  ? 5   MAN   Z O2  1 
HETATM 8138 O  O3  . MAN   G  4  .   ? 23.838  -46.128 52.015 1.00 111.67 ? 5   MAN   Z O3  1 
HETATM 8139 O  O4  . MAN   G  4  .   ? 24.092  -43.319 52.574 1.00 92.62  ? 5   MAN   Z O4  1 
HETATM 8140 O  O5  . MAN   G  4  .   ? 20.410  -43.784 52.397 1.00 106.28 ? 5   MAN   Z O5  1 
HETATM 8141 O  O6  . MAN   G  4  .   ? 20.833  -40.853 53.027 1.00 114.54 ? 5   MAN   Z O6  1 
HETATM 8142 C  C1  . MAN   G  4  .   ? 13.058  -43.871 52.692 1.00 140.82 ? 6   MAN   Z C1  1 
HETATM 8143 C  C2  . MAN   G  4  .   ? 12.788  -43.105 51.365 1.00 142.13 ? 6   MAN   Z C2  1 
HETATM 8144 C  C3  . MAN   G  4  .   ? 11.347  -43.175 50.852 1.00 144.39 ? 6   MAN   Z C3  1 
HETATM 8145 C  C4  . MAN   G  4  .   ? 10.780  -44.581 50.971 1.00 146.16 ? 6   MAN   Z C4  1 
HETATM 8146 C  C5  . MAN   G  4  .   ? 10.939  -45.060 52.408 1.00 139.85 ? 6   MAN   Z C5  1 
HETATM 8147 C  C6  . MAN   G  4  .   ? 10.356  -46.433 52.666 1.00 125.55 ? 6   MAN   Z C6  1 
HETATM 8148 O  O2  . MAN   G  4  .   ? 13.662  -43.585 50.344 1.00 128.17 ? 6   MAN   Z O2  1 
HETATM 8149 O  O3  . MAN   G  4  .   ? 11.317  -42.737 49.484 1.00 134.04 ? 6   MAN   Z O3  1 
HETATM 8150 O  O4  . MAN   G  4  .   ? 9.399   -44.591 50.611 1.00 148.80 ? 6   MAN   Z O4  1 
HETATM 8151 O  O5  . MAN   G  4  .   ? 12.353  -45.134 52.710 1.00 145.67 ? 6   MAN   Z O5  1 
HETATM 8152 O  O6  . MAN   G  4  .   ? 9.572   -46.438 53.854 1.00 116.53 ? 6   MAN   Z O6  1 
HETATM 8153 C  C1  . NAG   H  5  .   ? -15.081 19.267  31.886 1.00 90.21  ? 1   NAG   m C1  1 
HETATM 8154 C  C2  . NAG   H  5  .   ? -14.624 19.069  33.337 1.00 91.03  ? 1   NAG   m C2  1 
HETATM 8155 C  C3  . NAG   H  5  .   ? -14.966 20.324  34.120 1.00 84.44  ? 1   NAG   m C3  1 
HETATM 8156 C  C4  . NAG   H  5  .   ? -14.219 21.482  33.486 1.00 80.22  ? 1   NAG   m C4  1 
HETATM 8157 C  C5  . NAG   H  5  .   ? -14.609 21.638  32.019 1.00 81.95  ? 1   NAG   m C5  1 
HETATM 8158 C  C6  . NAG   H  5  .   ? -13.787 22.705  31.313 1.00 81.84  ? 1   NAG   m C6  1 
HETATM 8159 C  C7  . NAG   H  5  .   ? -16.201 17.431  34.448 1.00 78.94  ? 1   NAG   m C7  1 
HETATM 8160 C  C8  . NAG   H  5  .   ? -17.411 18.218  34.046 1.00 76.59  ? 1   NAG   m C8  1 
HETATM 8161 N  N2  . NAG   H  5  .   ? -15.008 17.846  34.019 1.00 92.79  ? 1   NAG   m N2  1 
HETATM 8162 O  O3  . NAG   H  5  .   ? -14.610 20.172  35.486 1.00 86.80  ? 1   NAG   m O3  1 
HETATM 8163 O  O4  . NAG   H  5  .   ? -14.572 22.659  34.197 1.00 73.51  ? 1   NAG   m O4  1 
HETATM 8164 O  O5  . NAG   H  5  .   ? -14.399 20.392  31.324 1.00 80.57  ? 1   NAG   m O5  1 
HETATM 8165 O  O6  . NAG   H  5  .   ? -12.379 22.463  31.423 1.00 71.43  ? 1   NAG   m O6  1 
HETATM 8166 O  O7  . NAG   H  5  .   ? -16.293 16.414  35.125 1.00 78.38  ? 1   NAG   m O7  1 
HETATM 8167 C  C1  . NAG   H  5  .   ? -13.445 23.305  34.691 1.00 68.08  ? 2   NAG   m C1  1 
HETATM 8168 C  C2  . NAG   H  5  .   ? -13.611 24.812  34.865 1.00 66.70  ? 2   NAG   m C2  1 
HETATM 8169 C  C3  . NAG   H  5  .   ? -12.268 25.342  35.371 1.00 67.47  ? 2   NAG   m C3  1 
HETATM 8170 C  C4  . NAG   H  5  .   ? -11.857 24.612  36.655 1.00 66.58  ? 2   NAG   m C4  1 
HETATM 8171 C  C5  . NAG   H  5  .   ? -11.845 23.105  36.430 1.00 70.45  ? 2   NAG   m C5  1 
HETATM 8172 C  C6  . NAG   H  5  .   ? -11.535 22.332  37.702 1.00 67.78  ? 2   NAG   m C6  1 
HETATM 8173 C  C7  . NAG   H  5  .   ? -15.382 25.467  33.245 1.00 74.62  ? 2   NAG   m C7  1 
HETATM 8174 C  C8  . NAG   H  5  .   ? -15.653 26.139  31.928 1.00 71.70  ? 2   NAG   m C8  1 
HETATM 8175 N  N2  . NAG   H  5  .   ? -14.099 25.517  33.687 1.00 65.14  ? 2   NAG   m N2  1 
HETATM 8176 O  O3  . NAG   H  5  .   ? -12.315 26.753  35.564 1.00 61.49  ? 2   NAG   m O3  1 
HETATM 8177 O  O4  . NAG   H  5  .   ? -10.514 24.939  37.055 1.00 67.18  ? 2   NAG   m O4  1 
HETATM 8178 O  O5  . NAG   H  5  .   ? -13.145 22.693  35.950 1.00 69.08  ? 2   NAG   m O5  1 
HETATM 8179 O  O6  . NAG   H  5  .   ? -12.505 22.626  38.697 1.00 62.74  ? 2   NAG   m O6  1 
HETATM 8180 O  O7  . NAG   H  5  .   ? -16.289 24.889  33.859 1.00 63.27  ? 2   NAG   m O7  1 
HETATM 8181 C  C1  . BMA   H  5  .   ? -10.425 26.025  37.932 1.00 79.48  ? 3   BMA   m C1  1 
HETATM 8182 C  C2  . BMA   H  5  .   ? -9.080  26.022  38.665 1.00 78.22  ? 3   BMA   m C2  1 
HETATM 8183 C  C3  . BMA   H  5  .   ? -8.954  27.256  39.614 1.00 81.06  ? 3   BMA   m C3  1 
HETATM 8184 C  C4  . BMA   H  5  .   ? -9.236  28.532  38.837 1.00 79.59  ? 3   BMA   m C4  1 
HETATM 8185 C  C5  . BMA   H  5  .   ? -10.589 28.447  38.090 1.00 82.79  ? 3   BMA   m C5  1 
HETATM 8186 C  C6  . BMA   H  5  .   ? -10.823 29.676  37.225 1.00 82.09  ? 3   BMA   m C6  1 
HETATM 8187 O  O2  . BMA   H  5  .   ? -8.016  26.022  37.706 1.00 64.32  ? 3   BMA   m O2  1 
HETATM 8188 O  O3  . BMA   H  5  .   ? -7.620  27.423  40.146 1.00 71.91  ? 3   BMA   m O3  1 
HETATM 8189 O  O4  . BMA   H  5  .   ? -9.203  29.645  39.746 1.00 81.36  ? 3   BMA   m O4  1 
HETATM 8190 O  O5  . BMA   H  5  .   ? -10.590 27.252  37.206 1.00 69.34  ? 3   BMA   m O5  1 
HETATM 8191 O  O6  . BMA   H  5  .   ? -9.617  30.014  36.485 1.00 70.27  ? 3   BMA   m O6  1 
HETATM 8192 C  C1  . MAN   H  5  .   ? -7.312  27.133  41.479 1.00 78.96  ? 4   MAN   m C1  1 
HETATM 8193 C  C2  . MAN   H  5  .   ? -6.438  28.342  41.809 1.00 76.28  ? 4   MAN   m C2  1 
HETATM 8194 C  C3  . MAN   H  5  .   ? -5.242  28.329  40.815 1.00 68.61  ? 4   MAN   m C3  1 
HETATM 8195 C  C4  . MAN   H  5  .   ? -4.469  26.991  40.936 1.00 67.11  ? 4   MAN   m C4  1 
HETATM 8196 C  C5  . MAN   H  5  .   ? -5.433  25.814  40.672 1.00 66.82  ? 4   MAN   m C5  1 
HETATM 8197 C  C6  . MAN   H  5  .   ? -4.801  24.444  40.856 1.00 62.92  ? 4   MAN   m C6  1 
HETATM 8198 O  O2  . MAN   H  5  .   ? -6.093  28.362  43.207 1.00 64.22  ? 4   MAN   m O2  1 
HETATM 8199 O  O3  . MAN   H  5  .   ? -4.413  29.470  41.053 1.00 65.82  ? 4   MAN   m O3  1 
HETATM 8200 O  O4  . MAN   H  5  .   ? -3.363  26.901  40.018 1.00 59.88  ? 4   MAN   m O4  1 
HETATM 8201 O  O5  . MAN   H  5  .   ? -6.570  25.910  41.616 1.00 76.17  ? 4   MAN   m O5  1 
HETATM 8202 O  O6  . MAN   H  5  .   ? -4.312  24.244  42.183 1.00 59.97  ? 4   MAN   m O6  1 
HETATM 8203 C  C1  . NAG   I  6  .   ? -17.898 27.647  8.012  1.00 91.03  ? 1   NAG   n C1  1 
HETATM 8204 C  C2  . NAG   I  6  .   ? -17.245 28.226  6.764  1.00 89.28  ? 1   NAG   n C2  1 
HETATM 8205 C  C3  . NAG   I  6  .   ? -17.381 29.746  6.775  1.00 91.20  ? 1   NAG   n C3  1 
HETATM 8206 C  C4  . NAG   I  6  .   ? -18.835 30.148  7.011  1.00 97.73  ? 1   NAG   n C4  1 
HETATM 8207 C  C5  . NAG   I  6  .   ? -19.334 29.495  8.295  1.00 100.01 ? 1   NAG   n C5  1 
HETATM 8208 C  C6  . NAG   I  6  .   ? -20.763 29.829  8.656  1.00 98.17  ? 1   NAG   n C6  1 
HETATM 8209 C  C7  . NAG   I  6  .   ? -15.293 27.251  5.616  1.00 86.03  ? 1   NAG   n C7  1 
HETATM 8210 C  C8  . NAG   I  6  .   ? -13.975 27.824  5.194  1.00 84.64  ? 1   NAG   n C8  1 
HETATM 8211 N  N2  . NAG   I  6  .   ? -15.857 27.816  6.687  1.00 89.00  ? 1   NAG   n N2  1 
HETATM 8212 O  O3  . NAG   I  6  .   ? -16.877 30.251  5.545  1.00 72.66  ? 1   NAG   n O3  1 
HETATM 8213 O  O4  . NAG   I  6  .   ? -18.964 31.561  7.140  1.00 114.83 ? 1   NAG   n O4  1 
HETATM 8214 O  O5  . NAG   I  6  .   ? -19.255 28.072  8.102  1.00 94.12  ? 1   NAG   n O5  1 
HETATM 8215 O  O6  . NAG   I  6  .   ? -21.679 29.079  7.866  1.00 92.48  ? 1   NAG   n O6  1 
HETATM 8216 O  O7  . NAG   I  6  .   ? -15.810 26.311  5.023  1.00 73.78  ? 1   NAG   n O7  1 
HETATM 8217 C  C1  . NAG   I  6  .   ? -19.640 32.180  6.092  1.00 133.11 ? 2   NAG   n C1  1 
HETATM 8218 C  C2  . NAG   I  6  .   ? -20.327 33.459  6.590  1.00 127.92 ? 2   NAG   n C2  1 
HETATM 8219 C  C3  . NAG   I  6  .   ? -20.451 34.551  5.524  1.00 134.51 ? 2   NAG   n C3  1 
HETATM 8220 C  C4  . NAG   I  6  .   ? -19.300 34.565  4.524  1.00 145.57 ? 2   NAG   n C4  1 
HETATM 8221 C  C5  . NAG   I  6  .   ? -19.154 33.159  3.970  1.00 143.60 ? 2   NAG   n C5  1 
HETATM 8222 C  C6  . NAG   I  6  .   ? -18.196 33.046  2.801  1.00 131.90 ? 2   NAG   n C6  1 
HETATM 8223 C  C7  . NAG   I  6  .   ? -22.161 33.369  8.293  1.00 105.29 ? 2   NAG   n C7  1 
HETATM 8224 C  C8  . NAG   I  6  .   ? -23.587 32.955  8.528  1.00 91.01  ? 2   NAG   n C8  1 
HETATM 8225 N  N2  . NAG   I  6  .   ? -21.669 33.153  7.061  1.00 119.42 ? 2   NAG   n N2  1 
HETATM 8226 O  O3  . NAG   I  6  .   ? -20.532 35.783  6.224  1.00 133.52 ? 2   NAG   n O3  1 
HETATM 8227 O  O4  . NAG   I  6  .   ? -19.532 35.456  3.418  1.00 157.23 ? 2   NAG   n O4  1 
HETATM 8228 O  O5  . NAG   I  6  .   ? -18.656 32.392  5.077  1.00 147.97 ? 2   NAG   n O5  1 
HETATM 8229 O  O6  . NAG   I  6  .   ? -17.305 31.949  2.932  1.00 130.71 ? 2   NAG   n O6  1 
HETATM 8230 O  O7  . NAG   I  6  .   ? -21.482 33.867  9.186  1.00 98.15  ? 2   NAG   n O7  1 
HETATM 8231 C  C1  . BMA   I  6  .   ? -19.895 36.791  3.594  1.00 164.55 ? 3   BMA   n C1  1 
HETATM 8232 C  C2  . BMA   I  6  .   ? -18.867 37.725  2.969  1.00 154.85 ? 3   BMA   n C2  1 
HETATM 8233 C  C3  . BMA   I  6  .   ? -19.285 39.177  3.145  1.00 151.58 ? 3   BMA   n C3  1 
HETATM 8234 C  C4  . BMA   I  6  .   ? -20.733 39.416  2.702  1.00 158.63 ? 3   BMA   n C4  1 
HETATM 8235 C  C5  . BMA   I  6  .   ? -21.693 38.372  3.310  1.00 161.11 ? 3   BMA   n C5  1 
HETATM 8236 C  C6  . BMA   I  6  .   ? -23.098 38.425  2.742  1.00 146.07 ? 3   BMA   n C6  1 
HETATM 8237 O  O2  . BMA   I  6  .   ? -18.659 37.429  1.589  1.00 136.63 ? 3   BMA   n O2  1 
HETATM 8238 O  O3  . BMA   I  6  .   ? -18.395 39.990  2.384  1.00 124.19 ? 3   BMA   n O3  1 
HETATM 8239 O  O4  . BMA   I  6  .   ? -21.147 40.733  3.097  1.00 150.33 ? 3   BMA   n O4  1 
HETATM 8240 O  O5  . BMA   I  6  .   ? -21.192 37.043  3.031  1.00 168.35 ? 3   BMA   n O5  1 
HETATM 8241 O  O6  . BMA   I  6  .   ? -23.681 39.720  2.865  1.00 131.69 ? 3   BMA   n O6  1 
HETATM 8242 C  CHA . HEM   J  7  .   ? 40.615  1.401   34.896 1.00 29.15  ? 401 HEM   A CHA 1 
HETATM 8243 C  CHB . HEM   J  7  .   ? 44.686  0.673   37.452 1.00 29.77  ? 401 HEM   A CHB 1 
HETATM 8244 C  CHC . HEM   J  7  .   ? 43.826  -4.111  37.380 1.00 30.50  ? 401 HEM   A CHC 1 
HETATM 8245 C  CHD . HEM   J  7  .   ? 39.701  -3.326  35.072 1.00 27.43  ? 401 HEM   A CHD 1 
HETATM 8246 C  C1A . HEM   J  7  .   ? 41.793  1.603   35.614 1.00 31.41  ? 401 HEM   A C1A 1 
HETATM 8247 C  C2A . HEM   J  7  .   ? 42.344  2.858   35.904 1.00 32.89  ? 401 HEM   A C2A 1 
HETATM 8248 C  C3A . HEM   J  7  .   ? 43.479  2.667   36.622 1.00 35.33  ? 401 HEM   A C3A 1 
HETATM 8249 C  C4A . HEM   J  7  .   ? 43.659  1.281   36.778 1.00 32.80  ? 401 HEM   A C4A 1 
HETATM 8250 C  CMA . HEM   J  7  .   ? 44.406  3.752   37.143 1.00 32.90  ? 401 HEM   A CMA 1 
HETATM 8251 C  CAA . HEM   J  7  .   ? 41.764  4.189   35.524 1.00 34.66  ? 401 HEM   A CAA 1 
HETATM 8252 C  CBA . HEM   J  7  .   ? 41.860  4.364   34.030 1.00 38.53  ? 401 HEM   A CBA 1 
HETATM 8253 C  CGA . HEM   J  7  .   ? 41.825  5.812   33.576 1.00 44.14  ? 401 HEM   A CGA 1 
HETATM 8254 O  O1A . HEM   J  7  .   ? 42.709  6.085   32.719 1.00 46.19  ? 401 HEM   A O1A 1 
HETATM 8255 O  O2A . HEM   J  7  .   ? 40.973  6.701   33.946 1.00 41.58  ? 401 HEM   A O2A 1 
HETATM 8256 C  C1B . HEM   J  7  .   ? 44.779  -0.706  37.603 1.00 30.45  ? 401 HEM   A C1B 1 
HETATM 8257 C  C2B . HEM   J  7  .   ? 45.902  -1.312  38.228 1.00 31.94  ? 401 HEM   A C2B 1 
HETATM 8258 C  C3B . HEM   J  7  .   ? 45.673  -2.652  38.262 1.00 32.69  ? 401 HEM   A C3B 1 
HETATM 8259 C  C4B . HEM   J  7  .   ? 44.395  -2.857  37.559 1.00 31.42  ? 401 HEM   A C4B 1 
HETATM 8260 C  CMB . HEM   J  7  .   ? 47.099  -0.633  38.876 1.00 29.55  ? 401 HEM   A CMB 1 
HETATM 8261 C  CAB . HEM   J  7  .   ? 46.666  -3.610  38.771 1.00 34.86  ? 401 HEM   A CAB 1 
HETATM 8262 C  CBB . HEM   J  7  .   ? 46.781  -4.808  38.231 1.00 39.72  ? 401 HEM   A CBB 1 
HETATM 8263 C  C1C . HEM   J  7  .   ? 42.618  -4.351  36.761 1.00 28.71  ? 401 HEM   A C1C 1 
HETATM 8264 C  C2C . HEM   J  7  .   ? 41.986  -5.594  36.656 1.00 29.79  ? 401 HEM   A C2C 1 
HETATM 8265 C  C3C . HEM   J  7  .   ? 40.808  -5.333  35.956 1.00 31.60  ? 401 HEM   A C3C 1 
HETATM 8266 C  C4C . HEM   J  7  .   ? 40.730  -3.940  35.719 1.00 28.42  ? 401 HEM   A C4C 1 
HETATM 8267 C  CMC . HEM   J  7  .   ? 42.518  -6.945  37.134 1.00 28.08  ? 401 HEM   A CMC 1 
HETATM 8268 C  CAC . HEM   J  7  .   ? 39.698  -6.223  35.613 1.00 35.65  ? 401 HEM   A CAC 1 
HETATM 8269 C  CBC . HEM   J  7  .   ? 39.391  -7.193  36.471 1.00 43.38  ? 401 HEM   A CBC 1 
HETATM 8270 C  C1D . HEM   J  7  .   ? 39.650  -1.953  34.832 1.00 29.47  ? 401 HEM   A C1D 1 
HETATM 8271 C  C2D . HEM   J  7  .   ? 38.617  -1.353  33.972 1.00 30.56  ? 401 HEM   A C2D 1 
HETATM 8272 C  C3D . HEM   J  7  .   ? 38.873  -0.046  33.956 1.00 29.81  ? 401 HEM   A C3D 1 
HETATM 8273 C  C4D . HEM   J  7  .   ? 40.080  0.143   34.728 1.00 28.29  ? 401 HEM   A C4D 1 
HETATM 8274 C  CMD . HEM   J  7  .   ? 37.430  -2.038  33.287 1.00 29.54  ? 401 HEM   A CMD 1 
HETATM 8275 C  CAD . HEM   J  7  .   ? 38.100  1.009   33.219 1.00 29.64  ? 401 HEM   A CAD 1 
HETATM 8276 C  CBD . HEM   J  7  .   ? 37.062  1.761   34.067 1.00 30.29  ? 401 HEM   A CBD 1 
HETATM 8277 C  CGD . HEM   J  7  .   ? 36.235  2.743   33.217 1.00 32.31  ? 401 HEM   A CGD 1 
HETATM 8278 O  O1D . HEM   J  7  .   ? 35.008  2.940   33.504 1.00 34.11  ? 401 HEM   A O1D 1 
HETATM 8279 O  O2D . HEM   J  7  .   ? 36.732  3.318   32.202 1.00 35.12  ? 401 HEM   A O2D 1 
HETATM 8280 N  NA  . HEM   J  7  .   ? 42.600  0.646   36.209 1.00 35.23  ? 401 HEM   A NA  1 
HETATM 8281 N  NB  . HEM   J  7  .   ? 43.914  -1.637  37.232 1.00 30.46  ? 401 HEM   A NB  1 
HETATM 8282 N  NC  . HEM   J  7  .   ? 41.859  -3.374  36.188 1.00 30.30  ? 401 HEM   A NC  1 
HETATM 8283 N  ND  . HEM   J  7  .   ? 40.519  -1.013  35.257 1.00 31.56  ? 401 HEM   A ND  1 
HETATM 8284 FE FE  . HEM   J  7  .   ? 42.089  -1.271  36.330 1.00 27.55  ? 401 HEM   A FE  1 
HETATM 8285 N  N1  . EPE   K  8  .   ? 43.322  -6.518  55.798 0.80 51.53  ? 402 EPE   A N1  1 
HETATM 8286 C  C2  . EPE   K  8  .   ? 43.482  -5.130  56.285 0.80 56.27  ? 402 EPE   A C2  1 
HETATM 8287 C  C3  . EPE   K  8  .   ? 42.208  -4.593  56.885 0.80 53.94  ? 402 EPE   A C3  1 
HETATM 8288 N  N4  . EPE   K  8  .   ? 41.063  -4.710  55.974 0.80 48.23  ? 402 EPE   A N4  1 
HETATM 8289 C  C5  . EPE   K  8  .   ? 40.924  -6.100  55.518 0.80 46.13  ? 402 EPE   A C5  1 
HETATM 8290 C  C6  . EPE   K  8  .   ? 42.191  -6.560  54.854 0.80 52.05  ? 402 EPE   A C6  1 
HETATM 8291 C  C7  . EPE   K  8  .   ? 39.858  -4.290  56.714 0.80 52.91  ? 402 EPE   A C7  1 
HETATM 8292 C  C8  . EPE   K  8  .   ? 39.004  -5.377  57.399 0.80 47.19  ? 402 EPE   A C8  1 
HETATM 8293 O  O8  . EPE   K  8  .   ? 37.641  -4.949  57.534 0.80 46.57  ? 402 EPE   A O8  1 
HETATM 8294 C  C9  . EPE   K  8  .   ? 44.584  -7.029  55.168 0.80 51.64  ? 402 EPE   A C9  1 
HETATM 8295 C  C10 . EPE   K  8  .   ? 45.854  -6.652  55.962 0.80 54.58  ? 402 EPE   A C10 1 
HETATM 8296 S  S   . EPE   K  8  .   ? 47.270  -6.312  54.933 0.80 62.28  ? 402 EPE   A S   1 
HETATM 8297 O  O1S . EPE   K  8  .   ? 47.245  -4.876  54.713 0.80 56.87  ? 402 EPE   A O1S 1 
HETATM 8298 O  O2S . EPE   K  8  .   ? 47.099  -7.224  53.824 0.80 63.67  ? 402 EPE   A O2S 1 
HETATM 8299 O  O3S . EPE   K  8  .   ? 48.609  -6.738  55.736 0.80 48.36  ? 402 EPE   A O3S 1 
HETATM 8300 N  N1  . EPE   L  8  .   ? 60.196  1.396   20.139 0.80 58.44  ? 403 EPE   A N1  1 
HETATM 8301 C  C2  . EPE   L  8  .   ? 58.878  1.251   20.753 0.80 55.62  ? 403 EPE   A C2  1 
HETATM 8302 C  C3  . EPE   L  8  .   ? 58.102  0.166   20.037 0.80 59.23  ? 403 EPE   A C3  1 
HETATM 8303 N  N4  . EPE   L  8  .   ? 58.657  -1.187  20.173 0.80 55.50  ? 403 EPE   A N4  1 
HETATM 8304 C  C5  . EPE   L  8  .   ? 60.037  -1.062  20.636 0.80 54.85  ? 403 EPE   A C5  1 
HETATM 8305 C  C6  . EPE   L  8  .   ? 60.753  0.037   19.882 0.80 57.70  ? 403 EPE   A C6  1 
HETATM 8306 C  C7  . EPE   L  8  .   ? 57.815  -2.057  21.024 0.80 59.60  ? 403 EPE   A C7  1 
HETATM 8307 C  C8  . EPE   L  8  .   ? 56.378  -2.359  20.507 0.80 55.88  ? 403 EPE   A C8  1 
HETATM 8308 O  O8  . EPE   L  8  .   ? 56.356  -2.892  19.203 0.80 51.63  ? 403 EPE   A O8  1 
HETATM 8309 C  C9  . EPE   L  8  .   ? 60.153  2.265   18.909 0.80 59.35  ? 403 EPE   A C9  1 
HETATM 8310 C  C10 . EPE   L  8  .   ? 61.460  3.035   18.614 0.80 57.07  ? 403 EPE   A C10 1 
HETATM 8311 S  S   . EPE   L  8  .   ? 61.174  4.713   18.061 0.80 53.78  ? 403 EPE   A S   1 
HETATM 8312 O  O1S . EPE   L  8  .   ? 60.452  5.386   19.113 0.80 52.29  ? 403 EPE   A O1S 1 
HETATM 8313 O  O2S . EPE   L  8  .   ? 60.675  4.589   16.710 0.80 54.88  ? 403 EPE   A O2S 1 
HETATM 8314 O  O3S . EPE   L  8  .   ? 62.502  5.547   17.999 0.80 47.04  ? 403 EPE   A O3S 1 
HETATM 8315 C  C1  . GOL   M  9  .   ? 33.386  1.038   60.954 1.00 62.69  ? 404 GOL   A C1  1 
HETATM 8316 O  O1  . GOL   M  9  .   ? 32.476  0.087   60.380 1.00 56.98  ? 404 GOL   A O1  1 
HETATM 8317 C  C2  . GOL   M  9  .   ? 32.886  2.474   60.817 1.00 57.88  ? 404 GOL   A C2  1 
HETATM 8318 O  O2  . GOL   M  9  .   ? 33.995  3.345   60.587 1.00 53.92  ? 404 GOL   A O2  1 
HETATM 8319 C  C3  . GOL   M  9  .   ? 31.865  2.691   59.712 1.00 52.62  ? 404 GOL   A C3  1 
HETATM 8320 O  O3  . GOL   M  9  .   ? 31.902  4.041   59.229 1.00 47.50  ? 404 GOL   A O3  1 
HETATM 8321 C  C1  . A1IUA N  10 .   ? 45.096  -1.201  33.655 1.00 50.49  ? 405 A1IUA A C1  1 
HETATM 8322 C  C2  . A1IUA N  10 .   ? 45.649  -1.561  32.206 1.00 54.26  ? 405 A1IUA A C2  1 
HETATM 8323 C  C3  . A1IUA N  10 .   ? 46.910  -1.951  31.899 1.00 47.93  ? 405 A1IUA A C3  1 
HETATM 8324 C  C4  . A1IUA N  10 .   ? 47.280  -2.305  30.421 1.00 51.99  ? 405 A1IUA A C4  1 
HETATM 8325 O  O5  . A1IUA N  10 .   ? 46.454  -2.238  29.504 1.00 47.86  ? 405 A1IUA A O5  1 
HETATM 8326 C  C6  . A1IUA N  10 .   ? 48.688  -2.885  30.204 1.00 48.78  ? 405 A1IUA A C6  1 
HETATM 8327 C  C7  . A1IUA N  10 .   ? 49.664  -1.909  29.563 1.00 52.44  ? 405 A1IUA A C7  1 
HETATM 8328 C  C8  . A1IUA N  10 .   ? 50.133  -2.089  28.332 1.00 51.23  ? 405 A1IUA A C8  1 
HETATM 8329 C  C9  . A1IUA N  10 .   ? 50.025  -3.373  27.550 1.00 48.38  ? 405 A1IUA A C9  1 
HETATM 8330 C  C10 . A1IUA N  10 .   ? 48.764  -4.120  27.971 1.00 50.81  ? 405 A1IUA A C10 1 
HETATM 8331 C  C11 . A1IUA N  10 .   ? 48.669  -4.287  29.503 1.00 47.77  ? 405 A1IUA A C11 1 
HETATM 8332 C  C12 . A1IUA N  10 .   ? 49.874  -5.111  30.007 1.00 47.96  ? 405 A1IUA A C12 1 
HETATM 8333 C  C13 . A1IUA N  10 .   ? 47.358  -5.040  29.837 1.00 43.96  ? 405 A1IUA A C13 1 
HETATM 8334 C  C14 . A1IUA N  10 .   ? 50.120  -0.772  30.433 1.00 55.50  ? 405 A1IUA A C14 1 
HETATM 8335 MG MG  . MG    O  11 .   ? 39.664  8.350   33.662 1.00 41.04  ? 406 MG    A MG  1 
HETATM 8336 S  S   . SO4   P  12 .   ? 26.319  8.550   19.183 1.00 63.81  ? 407 SO4   A S   1 
HETATM 8337 O  O1  . SO4   P  12 .   ? 27.201  7.627   18.434 1.00 52.30  ? 407 SO4   A O1  1 
HETATM 8338 O  O2  . SO4   P  12 .   ? 25.264  9.089   18.340 1.00 53.56  ? 407 SO4   A O2  1 
HETATM 8339 O  O3  . SO4   P  12 .   ? 25.658  7.902   20.333 1.00 54.16  ? 407 SO4   A O3  1 
HETATM 8340 O  O4  . SO4   P  12 .   ? 27.189  9.639   19.662 1.00 60.07  ? 407 SO4   A O4  1 
HETATM 8341 S  S   . SO4   Q  12 .   ? 37.608  -9.742  56.120 1.00 75.09  ? 408 SO4   A S   1 
HETATM 8342 O  O1  . SO4   Q  12 .   ? 38.600  -9.221  55.121 1.00 51.59  ? 408 SO4   A O1  1 
HETATM 8343 O  O2  . SO4   Q  12 .   ? 36.478  -10.397 55.387 1.00 51.32  ? 408 SO4   A O2  1 
HETATM 8344 O  O3  . SO4   Q  12 .   ? 38.235  -10.718 57.052 1.00 59.68  ? 408 SO4   A O3  1 
HETATM 8345 O  O4  . SO4   Q  12 .   ? 37.112  -8.604  56.961 1.00 69.84  ? 408 SO4   A O4  1 
HETATM 8346 S  S   . SO4   R  12 .   ? 45.753  -8.119  21.265 1.00 61.79  ? 409 SO4   A S   1 
HETATM 8347 O  O1  . SO4   R  12 .   ? 46.750  -8.067  20.184 1.00 57.09  ? 409 SO4   A O1  1 
HETATM 8348 O  O2  . SO4   R  12 .   ? 46.440  -8.396  22.542 1.00 55.95  ? 409 SO4   A O2  1 
HETATM 8349 O  O3  . SO4   R  12 .   ? 44.730  -9.168  20.968 1.00 48.63  ? 409 SO4   A O3  1 
HETATM 8350 O  O4  . SO4   R  12 .   ? 45.135  -6.804  21.381 1.00 51.73  ? 409 SO4   A O4  1 
HETATM 8351 S  S   . SO4   S  12 .   ? 55.443  -16.789 43.766 1.00 66.78  ? 410 SO4   A S   1 
HETATM 8352 O  O1  . SO4   S  12 .   ? 56.528  -16.037 43.114 1.00 62.25  ? 410 SO4   A O1  1 
HETATM 8353 O  O2  . SO4   S  12 .   ? 54.257  -16.898 42.905 1.00 66.70  ? 410 SO4   A O2  1 
HETATM 8354 O  O3  . SO4   S  12 .   ? 55.968  -18.131 44.037 1.00 65.98  ? 410 SO4   A O3  1 
HETATM 8355 O  O4  . SO4   S  12 .   ? 55.034  -16.127 45.037 1.00 56.74  ? 410 SO4   A O4  1 
HETATM 8356 C  CHA . HEM   T  7  .   ? 11.011  -9.328  61.277 1.00 28.34  ? 401 HEM   B CHA 1 
HETATM 8357 C  CHB . HEM   T  7  .   ? 7.722   -5.888  60.598 1.00 28.99  ? 401 HEM   B CHB 1 
HETATM 8358 C  CHC . HEM   T  7  .   ? 6.947   -7.627  56.130 1.00 29.19  ? 401 HEM   B CHC 1 
HETATM 8359 C  CHD . HEM   T  7  .   ? 10.368  -10.893 56.782 1.00 30.55  ? 401 HEM   B CHD 1 
HETATM 8360 C  C1A . HEM   T  7  .   ? 10.199  -8.240  61.431 1.00 27.68  ? 401 HEM   B C1A 1 
HETATM 8361 C  C2A . HEM   T  7  .   ? 10.168  -7.473  62.601 1.00 31.95  ? 401 HEM   B C2A 1 
HETATM 8362 C  C3A . HEM   T  7  .   ? 9.263   -6.501  62.415 1.00 30.42  ? 401 HEM   B C3A 1 
HETATM 8363 C  C4A . HEM   T  7  .   ? 8.700   -6.687  61.143 1.00 29.17  ? 401 HEM   B C4A 1 
HETATM 8364 C  CMA . HEM   T  7  .   ? 8.909   -5.445  63.423 1.00 29.41  ? 401 HEM   B CMA 1 
HETATM 8365 C  CAA . HEM   T  7  .   ? 11.013  -7.622  63.840 1.00 34.31  ? 401 HEM   B CAA 1 
HETATM 8366 C  CBA . HEM   T  7  .   ? 10.451  -8.753  64.645 1.00 39.91  ? 401 HEM   B CBA 1 
HETATM 8367 C  CGA . HEM   T  7  .   ? 11.028  -8.825  66.054 1.00 47.80  ? 401 HEM   B CGA 1 
HETATM 8368 O  O1A . HEM   T  7  .   ? 10.154  -9.097  66.926 1.00 54.90  ? 401 HEM   B O1A 1 
HETATM 8369 O  O2A . HEM   T  7  .   ? 12.259  -8.688  66.401 1.00 51.74  ? 401 HEM   B O2A 1 
HETATM 8370 C  C1B . HEM   T  7  .   ? 7.204   -6.106  59.325 1.00 29.46  ? 401 HEM   B C1B 1 
HETATM 8371 C  C2B . HEM   T  7  .   ? 6.133   -5.334  58.799 1.00 30.56  ? 401 HEM   B C2B 1 
HETATM 8372 C  C3B . HEM   T  7  .   ? 5.917   -5.771  57.526 1.00 29.92  ? 401 HEM   B C3B 1 
HETATM 8373 C  C4B . HEM   T  7  .   ? 6.844   -6.906  57.314 1.00 30.61  ? 401 HEM   B C4B 1 
HETATM 8374 C  CMB . HEM   T  7  .   ? 5.434   -4.134  59.442 1.00 27.71  ? 401 HEM   B CMB 1 
HETATM 8375 C  CAB . HEM   T  7  .   ? 4.841   -5.225  56.695 1.00 32.51  ? 401 HEM   B CAB 1 
HETATM 8376 C  CBB . HEM   T  7  .   ? 4.240   -5.953  55.776 1.00 37.26  ? 401 HEM   B CBB 1 
HETATM 8377 C  C1C . HEM   T  7  .   ? 7.825   -8.638  55.876 1.00 29.73  ? 401 HEM   B C1C 1 
HETATM 8378 C  C2C . HEM   T  7  .   ? 7.997   -9.322  54.640 1.00 28.95  ? 401 HEM   B C2C 1 
HETATM 8379 C  C3C . HEM   T  7  .   ? 8.968   -10.280 54.875 1.00 28.83  ? 401 HEM   B C3C 1 
HETATM 8380 C  C4C . HEM   T  7  .   ? 9.406   -10.121 56.217 1.00 30.85  ? 401 HEM   B C4C 1 
HETATM 8381 C  CMC . HEM   T  7  .   ? 7.187   -9.087  53.370 1.00 30.29  ? 401 HEM   B CMC 1 
HETATM 8382 C  CAC . HEM   T  7  .   ? 9.609   -11.225 53.976 1.00 33.23  ? 401 HEM   B CAC 1 
HETATM 8383 C  CBC . HEM   T  7  .   ? 9.631   -10.990 52.682 1.00 40.07  ? 401 HEM   B CBC 1 
HETATM 8384 C  C1D . HEM   T  7  .   ? 10.784  -10.731 58.095 1.00 30.23  ? 401 HEM   B C1D 1 
HETATM 8385 C  C2D . HEM   T  7  .   ? 11.742  -11.630 58.706 1.00 30.05  ? 401 HEM   B C2D 1 
HETATM 8386 C  C3D . HEM   T  7  .   ? 11.919  -11.200 59.940 1.00 31.59  ? 401 HEM   B C3D 1 
HETATM 8387 C  C4D . HEM   T  7  .   ? 11.058  -10.049 60.094 1.00 28.78  ? 401 HEM   B C4D 1 
HETATM 8388 C  CMD . HEM   T  7  .   ? 12.418  -12.811 58.078 1.00 29.66  ? 401 HEM   B CMD 1 
HETATM 8389 C  CAD . HEM   T  7  .   ? 12.826  -11.821 60.959 1.00 32.60  ? 401 HEM   B CAD 1 
HETATM 8390 C  CBD . HEM   T  7  .   ? 14.207  -11.171 61.029 1.00 32.79  ? 401 HEM   B CBD 1 
HETATM 8391 C  CGD . HEM   T  7  .   ? 15.076  -11.938 62.002 1.00 33.91  ? 401 HEM   B CGD 1 
HETATM 8392 O  O1D . HEM   T  7  .   ? 14.599  -12.432 63.045 1.00 40.27  ? 401 HEM   B O1D 1 
HETATM 8393 O  O2D . HEM   T  7  .   ? 16.277  -12.077 61.763 1.00 38.69  ? 401 HEM   B O2D 1 
HETATM 8394 N  NA  . HEM   T  7  .   ? 9.289   -7.750  60.537 1.00 27.23  ? 401 HEM   B NA  1 
HETATM 8395 N  NB  . HEM   T  7  .   ? 7.590   -7.004  58.418 1.00 32.35  ? 401 HEM   B NB  1 
HETATM 8396 N  NC  . HEM   T  7  .   ? 8.693   -9.122  56.806 1.00 29.33  ? 401 HEM   B NC  1 
HETATM 8397 N  ND  . HEM   T  7  .   ? 10.405  -9.789  58.947 1.00 32.11  ? 401 HEM   B ND  1 
HETATM 8398 FE FE  . HEM   T  7  .   ? 9.141   -8.370  58.646 1.00 27.51  ? 401 HEM   B FE  1 
HETATM 8399 C  C1  . GOL   U  9  .   ? 12.925  7.912   49.014 1.00 48.68  ? 402 GOL   B C1  1 
HETATM 8400 O  O1  . GOL   U  9  .   ? 13.827  8.803   49.675 1.00 43.25  ? 402 GOL   B O1  1 
HETATM 8401 C  C2  . GOL   U  9  .   ? 12.942  8.059   47.497 1.00 46.50  ? 402 GOL   B C2  1 
HETATM 8402 O  O2  . GOL   U  9  .   ? 14.154  7.498   46.999 1.00 48.43  ? 402 GOL   B O2  1 
HETATM 8403 C  C3  . GOL   U  9  .   ? 11.769  7.407   46.779 1.00 52.37  ? 402 GOL   B C3  1 
HETATM 8404 O  O3  . GOL   U  9  .   ? 12.053  6.044   46.433 1.00 54.08  ? 402 GOL   B O3  1 
HETATM 8405 C  C1  . A1IUA V  10 .   ? 5.666   -9.924  60.609 1.00 55.92  ? 403 A1IUA B C1  1 
HETATM 8406 C  C2  . A1IUA V  10 .   ? 4.781   -11.156 60.972 1.00 56.51  ? 403 A1IUA B C2  1 
HETATM 8407 C  C3  . A1IUA V  10 .   ? 3.455   -11.227 60.839 1.00 56.82  ? 403 A1IUA B C3  1 
HETATM 8408 C  C4  . A1IUA V  10 .   ? 2.603   -12.639 61.291 1.00 57.63  ? 403 A1IUA B C4  1 
HETATM 8409 O  O5  . A1IUA V  10 .   ? 3.124   -13.680 61.693 1.00 49.74  ? 403 A1IUA B O5  1 
HETATM 8410 C  C6  . A1IUA V  10 .   ? 1.096   -12.427 61.112 1.00 51.14  ? 403 A1IUA B C6  1 
HETATM 8411 C  C7  . A1IUA V  10 .   ? 0.331   -12.840 62.337 1.00 51.41  ? 403 A1IUA B C7  1 
HETATM 8412 C  C8  . A1IUA V  10 .   ? -0.325  -13.995 62.395 1.00 52.40  ? 403 A1IUA B C8  1 
HETATM 8413 C  C9  . A1IUA V  10 .   ? -0.912  -14.693 61.218 1.00 52.77  ? 403 A1IUA B C9  1 
HETATM 8414 C  C10 . A1IUA V  10 .   ? -0.845  -13.747 60.014 1.00 57.75  ? 403 A1IUA B C10 1 
HETATM 8415 C  C11 . A1IUA V  10 .   ? 0.462   -12.950 59.778 1.00 55.63  ? 403 A1IUA B C11 1 
HETATM 8416 C  C12 . A1IUA V  10 .   ? 0.140   -11.720 58.916 1.00 54.66  ? 403 A1IUA B C12 1 
HETATM 8417 C  C13 . A1IUA V  10 .   ? 1.491   -13.813 59.015 1.00 54.88  ? 403 A1IUA B C13 1 
HETATM 8418 C  C14 . A1IUA V  10 .   ? 0.336   -11.801 63.429 1.00 55.57  ? 403 A1IUA B C14 1 
HETATM 8419 MG MG  . MG    W  11 .   ? 13.742  -8.906  67.660 1.00 49.50  ? 404 MG    B MG  1 
HETATM 8420 S  S   . SO4   X  12 .   ? 22.858  -26.328 70.412 1.00 66.43  ? 405 SO4   B S   1 
HETATM 8421 O  O1  . SO4   X  12 .   ? 23.972  -26.123 69.484 1.00 58.90  ? 405 SO4   B O1  1 
HETATM 8422 O  O2  . SO4   X  12 .   ? 21.565  -26.443 69.737 1.00 55.72  ? 405 SO4   B O2  1 
HETATM 8423 O  O3  . SO4   X  12 .   ? 23.070  -27.563 71.162 1.00 70.76  ? 405 SO4   B O3  1 
HETATM 8424 O  O4  . SO4   X  12 .   ? 22.821  -25.173 71.302 1.00 65.95  ? 405 SO4   B O4  1 
HETATM 8425 S  S   . SO4   Y  12 .   ? 14.772  5.409   42.723 1.00 75.30  ? 406 SO4   B S   1 
HETATM 8426 O  O1  . SO4   Y  12 .   ? 15.644  4.579   41.829 1.00 60.72  ? 406 SO4   B O1  1 
HETATM 8427 O  O2  . SO4   Y  12 .   ? 13.763  6.151   41.919 1.00 60.73  ? 406 SO4   B O2  1 
HETATM 8428 O  O3  . SO4   Y  12 .   ? 14.052  4.524   43.682 1.00 61.56  ? 406 SO4   B O3  1 
HETATM 8429 O  O4  . SO4   Y  12 .   ? 15.617  6.372   43.482 1.00 59.36  ? 406 SO4   B O4  1 
HETATM 8430 S  S   . SO4   Z  12 .   ? -10.769 -16.785 75.163 1.00 75.82  ? 407 SO4   B S   1 
HETATM 8431 O  O1  . SO4   Z  12 .   ? -9.686  -16.711 74.167 1.00 65.65  ? 407 SO4   B O1  1 
HETATM 8432 O  O2  . SO4   Z  12 .   ? -12.065 -16.981 74.494 1.00 64.52  ? 407 SO4   B O2  1 
HETATM 8433 O  O3  . SO4   Z  12 .   ? -10.557 -17.922 76.088 1.00 63.85  ? 407 SO4   B O3  1 
HETATM 8434 O  O4  . SO4   Z  12 .   ? -10.777 -15.521 75.933 1.00 65.28  ? 407 SO4   B O4  1 
HETATM 8435 S  S   . SO4   AA 12 .   ? -6.646  -2.058  44.585 1.00 72.37  ? 408 SO4   B S   1 
HETATM 8436 O  O1  . SO4   AA 12 .   ? -5.405  -2.708  45.036 1.00 63.08  ? 408 SO4   B O1  1 
HETATM 8437 O  O2  . SO4   AA 12 .   ? -6.380  -1.330  43.330 1.00 69.56  ? 408 SO4   B O2  1 
HETATM 8438 O  O3  . SO4   AA 12 .   ? -7.701  -3.075  44.350 1.00 61.85  ? 408 SO4   B O3  1 
HETATM 8439 O  O4  . SO4   AA 12 .   ? -7.121  -1.106  45.611 1.00 71.54  ? 408 SO4   B O4  1 
HETATM 8440 S  S   . SO4   BA 12 .   ? 25.231  0.477   52.618 1.00 57.05  ? 409 SO4   B S   1 
HETATM 8441 O  O1  . SO4   BA 12 .   ? 26.092  0.053   51.525 1.00 59.13  ? 409 SO4   B O1  1 
HETATM 8442 O  O2  . SO4   BA 12 .   ? 23.876  -0.147  52.491 1.00 46.29  ? 409 SO4   B O2  1 
HETATM 8443 O  O3  . SO4   BA 12 .   ? 25.852  0.078   53.892 1.00 57.15  ? 409 SO4   B O3  1 
HETATM 8444 O  O4  . SO4   BA 12 .   ? 25.121  1.944   52.567 1.00 53.00  ? 409 SO4   B O4  1 
HETATM 8445 C  CHA . HEM   CA 7  .   ? -8.099  11.680  20.040 1.00 36.20  ? 401 HEM   C CHA 1 
HETATM 8446 C  CHB . HEM   CA 7  .   ? -5.407  7.723   19.487 1.00 38.60  ? 401 HEM   C CHB 1 
HETATM 8447 C  CHC . HEM   CA 7  .   ? -7.356  7.031   15.104 1.00 36.80  ? 401 HEM   C CHC 1 
HETATM 8448 C  CHD . HEM   CA 7  .   ? -10.258 10.785  15.816 1.00 37.71  ? 401 HEM   C CHD 1 
HETATM 8449 C  C1A . HEM   CA 7  .   ? -7.212  10.668  20.251 1.00 38.27  ? 401 HEM   C C1A 1 
HETATM 8450 C  C2A . HEM   CA 7  .   ? -6.472  10.503  21.435 1.00 43.69  ? 401 HEM   C C2A 1 
HETATM 8451 C  C3A . HEM   CA 7  .   ? -5.710  9.392   21.277 1.00 44.21  ? 401 HEM   C C3A 1 
HETATM 8452 C  C4A . HEM   CA 7  .   ? -5.982  8.856   20.006 1.00 39.65  ? 401 HEM   C C4A 1 
HETATM 8453 C  CMA . HEM   CA 7  .   ? -4.770  8.808   22.292 1.00 43.75  ? 401 HEM   C CMA 1 
HETATM 8454 C  CAA . HEM   CA 7  .   ? -6.523  11.361  22.664 1.00 46.18  ? 401 HEM   C CAA 1 
HETATM 8455 C  CBA . HEM   CA 7  .   ? -5.937  12.743  22.415 1.00 57.05  ? 401 HEM   C CBA 1 
HETATM 8456 C  CGA . HEM   CA 7  .   ? -5.593  13.535  23.683 1.00 63.61  ? 401 HEM   C CGA 1 
HETATM 8457 O  O1A . HEM   CA 7  .   ? -6.412  13.881  24.605 1.00 69.30  ? 401 HEM   C O1A 1 
HETATM 8458 O  O2A . HEM   CA 7  .   ? -4.403  13.898  23.776 1.00 58.60  ? 401 HEM   C O2A 1 
HETATM 8459 C  C1B . HEM   CA 7  .   ? -5.699  7.227   18.203 1.00 37.86  ? 401 HEM   C C1B 1 
HETATM 8460 C  C2B . HEM   CA 7  .   ? -5.023  6.111   17.661 1.00 34.05  ? 401 HEM   C C2B 1 
HETATM 8461 C  C3B . HEM   CA 7  .   ? -5.562  5.902   16.436 1.00 38.96  ? 401 HEM   C C3B 1 
HETATM 8462 C  C4B . HEM   CA 7  .   ? -6.572  6.948   16.234 1.00 35.22  ? 401 HEM   C C4B 1 
HETATM 8463 C  CMB . HEM   CA 7  .   ? -3.965  5.263   18.309 1.00 31.53  ? 401 HEM   C CMB 1 
HETATM 8464 C  CAB . HEM   CA 7  .   ? -5.100  4.863   15.498 1.00 42.73  ? 401 HEM   C CAB 1 
HETATM 8465 C  CBB . HEM   CA 7  .   ? -5.274  4.947   14.191 1.00 43.66  ? 401 HEM   C CBB 1 
HETATM 8466 C  C1C . HEM   CA 7  .   ? -8.369  7.961   14.912 1.00 38.21  ? 401 HEM   C C1C 1 
HETATM 8467 C  C2C . HEM   CA 7  .   ? -9.248  8.013   13.812 1.00 40.24  ? 401 HEM   C C2C 1 
HETATM 8468 C  C3C . HEM   CA 7  .   ? -10.050 9.115   14.026 1.00 42.95  ? 401 HEM   C C3C 1 
HETATM 8469 C  C4C . HEM   CA 7  .   ? -9.671  9.688   15.268 1.00 39.97  ? 401 HEM   C C4C 1 
HETATM 8470 C  CMC . HEM   CA 7  .   ? -9.253  7.056   12.635 1.00 38.64  ? 401 HEM   C CMC 1 
HETATM 8471 C  CAC . HEM   CA 7  .   ? -11.197 9.618   13.262 1.00 43.09  ? 401 HEM   C CAC 1 
HETATM 8472 C  CBC . HEM   CA 7  .   ? -11.813 8.859   12.380 1.00 47.31  ? 401 HEM   C CBC 1 
HETATM 8473 C  C1D . HEM   CA 7  .   ? -9.846  11.323  17.038 1.00 41.01  ? 401 HEM   C C1D 1 
HETATM 8474 C  C2D . HEM   CA 7  .   ? -10.413 12.596  17.527 1.00 42.25  ? 401 HEM   C C2D 1 
HETATM 8475 C  C3D . HEM   CA 7  .   ? -9.816  12.833  18.682 1.00 44.08  ? 401 HEM   C C3D 1 
HETATM 8476 C  C4D . HEM   CA 7  .   ? -8.890  11.720  18.899 1.00 38.49  ? 401 HEM   C C4D 1 
HETATM 8477 C  CMD . HEM   CA 7  .   ? -11.472 13.459  16.889 1.00 42.19  ? 401 HEM   C CMD 1 
HETATM 8478 C  CAD . HEM   CA 7  .   ? -10.060 14.025  19.569 1.00 47.76  ? 401 HEM   C CAD 1 
HETATM 8479 C  CBD . HEM   CA 7  .   ? -11.067 13.780  20.693 1.00 48.77  ? 401 HEM   C CBD 1 
HETATM 8480 C  CGD . HEM   CA 7  .   ? -11.213 15.116  21.422 1.00 51.01  ? 401 HEM   C CGD 1 
HETATM 8481 O  O1D . HEM   CA 7  .   ? -12.279 15.274  22.050 1.00 54.74  ? 401 HEM   C O1D 1 
HETATM 8482 O  O2D . HEM   CA 7  .   ? -10.331 16.044  21.409 1.00 46.54  ? 401 HEM   C O2D 1 
HETATM 8483 N  NA  . HEM   CA 7  .   ? -6.917  9.635   19.388 1.00 39.73  ? 401 HEM   C NA  1 
HETATM 8484 N  NB  . HEM   CA 7  .   ? -6.618  7.680   17.340 1.00 37.05  ? 401 HEM   C NB  1 
HETATM 8485 N  NC  . HEM   CA 7  .   ? -8.641  8.975   15.773 1.00 40.77  ? 401 HEM   C NC  1 
HETATM 8486 N  ND  . HEM   CA 7  .   ? -8.942  10.846  17.885 1.00 37.40  ? 401 HEM   C ND  1 
HETATM 8487 FE FE  . HEM   CA 7  .   ? -7.925  9.277   17.712 1.00 35.89  ? 401 HEM   C FE  1 
HETATM 8488 C  C1  . A1IUA DA 10 .   ? -4.364  10.650  16.273 1.00 49.04  ? 402 A1IUA C C1  1 
HETATM 8489 C  C2  . A1IUA DA 10 .   ? -3.269  11.201  15.368 1.00 55.73  ? 402 A1IUA C C2  1 
HETATM 8490 C  C3  . A1IUA DA 10 .   ? -3.087  12.495  15.098 1.00 53.85  ? 402 A1IUA C C3  1 
HETATM 8491 C  C4  . A1IUA DA 10 .   ? -1.908  13.046  14.110 1.00 55.17  ? 402 A1IUA C C4  1 
HETATM 8492 O  O5  . A1IUA DA 10 .   ? -1.718  14.247  13.915 1.00 54.81  ? 402 A1IUA C O5  1 
HETATM 8493 C  C6  . A1IUA DA 10 .   ? -1.032  11.981  13.436 1.00 50.30  ? 402 A1IUA C C6  1 
HETATM 8494 C  C7  . A1IUA DA 10 .   ? 0.353   12.060  14.032 1.00 53.72  ? 402 A1IUA C C7  1 
HETATM 8495 C  C8  . A1IUA DA 10 .   ? 1.303   12.780  13.455 1.00 54.12  ? 402 A1IUA C C8  1 
HETATM 8496 C  C9  . A1IUA DA 10 .   ? 1.271   13.258  12.022 1.00 55.72  ? 402 A1IUA C C9  1 
HETATM 8497 C  C10 . A1IUA DA 10 .   ? -0.131  13.203  11.411 1.00 55.73  ? 402 A1IUA C C10 1 
HETATM 8498 C  C11 . A1IUA DA 10 .   ? -1.006  12.024  11.874 1.00 53.65  ? 402 A1IUA C C11 1 
HETATM 8499 C  C12 . A1IUA DA 10 .   ? -0.400  10.712  11.339 1.00 60.34  ? 402 A1IUA C C12 1 
HETATM 8500 C  C13 . A1IUA DA 10 .   ? -2.431  12.174  11.315 1.00 46.15  ? 402 A1IUA C C13 1 
HETATM 8501 C  C14 . A1IUA DA 10 .   ? 0.569   11.301  15.314 1.00 54.52  ? 402 A1IUA C C14 1 
HETATM 8502 N  N1  . EPE   EA 8  .   ? 15.431  18.505  11.927 0.80 62.78  ? 403 EPE   C N1  1 
HETATM 8503 C  C2  . EPE   EA 8  .   ? 15.632  19.968  11.808 0.80 59.34  ? 403 EPE   C C2  1 
HETATM 8504 C  C3  . EPE   EA 8  .   ? 16.870  20.439  12.550 0.80 59.19  ? 403 EPE   C C3  1 
HETATM 8505 N  N4  . EPE   EA 8  .   ? 16.740  20.252  14.019 0.80 56.75  ? 403 EPE   C N4  1 
HETATM 8506 C  C5  . EPE   EA 8  .   ? 15.961  19.022  14.276 0.80 60.83  ? 403 EPE   C C5  1 
HETATM 8507 C  C6  . EPE   EA 8  .   ? 16.118  18.020  13.153 0.80 67.22  ? 403 EPE   C C6  1 
HETATM 8508 C  C7  . EPE   EA 8  .   ? 18.068  20.165  14.650 0.80 59.88  ? 403 EPE   C C7  1 
HETATM 8509 C  C8  . EPE   EA 8  .   ? 18.059  19.816  16.137 0.80 60.38  ? 403 EPE   C C8  1 
HETATM 8510 O  O8  . EPE   EA 8  .   ? 19.374  19.691  16.658 0.80 56.45  ? 403 EPE   C O8  1 
HETATM 8511 C  C9  . EPE   EA 8  .   ? 13.968  18.128  11.909 0.80 57.65  ? 403 EPE   C C9  1 
HETATM 8512 C  C10 . EPE   EA 8  .   ? 13.265  18.744  10.705 0.80 57.10  ? 403 EPE   C C10 1 
HETATM 8513 S  S   . EPE   EA 8  .   ? 12.474  17.517  9.694  0.80 60.53  ? 403 EPE   C S   1 
HETATM 8514 O  O1S . EPE   EA 8  .   ? 11.377  17.005  10.483 0.80 52.20  ? 403 EPE   C O1S 1 
HETATM 8515 O  O2S . EPE   EA 8  .   ? 13.536  16.639  9.232  0.80 54.01  ? 403 EPE   C O2S 1 
HETATM 8516 O  O3S . EPE   EA 8  .   ? 11.873  18.385  8.484  0.80 53.43  ? 403 EPE   C O3S 1 
HETATM 8517 N  N1  . EPE   FA 8  .   ? -25.833 2.806   -1.469 0.80 60.88  ? 404 EPE   C N1  1 
HETATM 8518 C  C2  . EPE   FA 8  .   ? -26.644 3.338   -0.340 0.80 65.87  ? 404 EPE   C C2  1 
HETATM 8519 C  C3  . EPE   FA 8  .   ? -27.351 4.615   -0.749 0.80 61.61  ? 404 EPE   C C3  1 
HETATM 8520 N  N4  . EPE   FA 8  .   ? -26.359 5.680   -1.073 0.80 63.60  ? 404 EPE   C N4  1 
HETATM 8521 C  C5  . EPE   FA 8  .   ? -24.992 5.119   -1.217 0.80 57.85  ? 404 EPE   C C5  1 
HETATM 8522 C  C6  . EPE   FA 8  .   ? -25.005 3.880   -2.079 0.80 59.08  ? 404 EPE   C C6  1 
HETATM 8523 C  C7  . EPE   FA 8  .   ? -26.727 6.449   -2.270 0.80 62.64  ? 404 EPE   C C7  1 
HETATM 8524 C  C8  . EPE   FA 8  .   ? -27.603 7.646   -1.961 0.80 60.65  ? 404 EPE   C C8  1 
HETATM 8525 O  O8  . EPE   FA 8  .   ? -26.802 8.800   -1.815 0.80 50.89  ? 404 EPE   C O8  1 
HETATM 8526 C  C9  . EPE   FA 8  .   ? -25.033 1.596   -1.092 0.80 60.74  ? 404 EPE   C C9  1 
HETATM 8527 C  C10 . EPE   FA 8  .   ? -24.172 1.756   0.159  0.80 55.31  ? 404 EPE   C C10 1 
HETATM 8528 S  S   . EPE   FA 8  .   ? -22.514 1.182   -0.145 0.80 60.41  ? 404 EPE   C S   1 
HETATM 8529 O  O1S . EPE   FA 8  .   ? -21.792 1.315   1.096  0.80 59.80  ? 404 EPE   C O1S 1 
HETATM 8530 O  O2S . EPE   FA 8  .   ? -22.055 1.888   -1.332 0.80 53.17  ? 404 EPE   C O2S 1 
HETATM 8531 O  O3S . EPE   FA 8  .   ? -22.703 -0.409  -0.258 0.80 48.52  ? 404 EPE   C O3S 1 
HETATM 8532 N  N1  . EPE   GA 8  .   ? -16.837 -9.238  18.954 0.80 63.90  ? 405 EPE   C N1  1 
HETATM 8533 C  C2  . EPE   GA 8  .   ? -15.839 -8.213  18.594 0.80 60.75  ? 405 EPE   C C2  1 
HETATM 8534 C  C3  . EPE   GA 8  .   ? -14.639 -8.873  17.955 0.80 62.91  ? 405 EPE   C C3  1 
HETATM 8535 N  N4  . EPE   GA 8  .   ? -13.985 -9.807  18.908 0.80 59.86  ? 405 EPE   C N4  1 
HETATM 8536 C  C5  . EPE   GA 8  .   ? -14.993 -10.822 19.315 0.80 61.14  ? 405 EPE   C C5  1 
HETATM 8537 C  C6  . EPE   GA 8  .   ? -16.217 -10.164 19.915 0.80 62.99  ? 405 EPE   C C6  1 
HETATM 8538 C  C7  . EPE   GA 8  .   ? -12.766 -10.406 18.314 0.80 57.21  ? 405 EPE   C C7  1 
HETATM 8539 C  C8  . EPE   GA 8  .   ? -11.590 -10.674 19.285 0.80 62.52  ? 405 EPE   C C8  1 
HETATM 8540 O  O8  . EPE   GA 8  .   ? -10.286 -10.562 18.689 0.80 51.10  ? 405 EPE   C O8  1 
HETATM 8541 C  C9  . EPE   GA 8  .   ? -18.066 -8.644  19.538 0.80 69.93  ? 405 EPE   C C9  1 
HETATM 8542 C  C10 . EPE   GA 8  .   ? -19.373 -9.309  19.099 0.80 60.85  ? 405 EPE   C C10 1 
HETATM 8543 S  S   . EPE   GA 8  .   ? -19.356 -9.303  17.318 0.80 59.35  ? 405 EPE   C S   1 
HETATM 8544 O  O1S . EPE   GA 8  .   ? -20.733 -9.490  16.896 0.80 51.56  ? 405 EPE   C O1S 1 
HETATM 8545 O  O2S . EPE   GA 8  .   ? -18.338 -10.270 16.957 0.80 56.68  ? 405 EPE   C O2S 1 
HETATM 8546 O  O3S . EPE   GA 8  .   ? -18.799 -7.847  16.913 0.80 48.22  ? 405 EPE   C O3S 1 
HETATM 8547 C  C1  . GOL   HA 9  .   ? 2.013   3.470   2.298  1.00 52.76  ? 406 GOL   C C1  1 
HETATM 8548 O  O1  . GOL   HA 9  .   ? 1.095   2.401   1.988  1.00 44.00  ? 406 GOL   C O1  1 
HETATM 8549 C  C2  . GOL   HA 9  .   ? 3.468   3.225   1.887  1.00 41.05  ? 406 GOL   C C2  1 
HETATM 8550 O  O2  . GOL   HA 9  .   ? 3.934   4.288   1.039  1.00 48.71  ? 406 GOL   C O2  1 
HETATM 8551 C  C3  . GOL   HA 9  .   ? 4.448   3.022   3.027  1.00 47.67  ? 406 GOL   C C3  1 
HETATM 8552 O  O3  . GOL   HA 9  .   ? 5.336   1.901   2.843  1.00 47.13  ? 406 GOL   C O3  1 
HETATM 8553 MG MG  . MG    IA 11 .   ? -6.907  14.633  26.293 1.00 58.64  ? 407 MG    C MG  1 
HETATM 8554 O  O   . HOH   JA 13 .   ? 48.755  13.920  30.525 1.00 43.60  ? 501 HOH   A O   1 
HETATM 8555 O  O   . HOH   JA 13 .   ? 55.040  14.494  49.047 1.00 32.52  ? 502 HOH   A O   1 
HETATM 8556 O  O   . HOH   JA 13 .   ? 39.081  4.184   32.463 1.00 45.88  ? 503 HOH   A O   1 
HETATM 8557 O  O   . HOH   JA 13 .   ? 50.655  9.690   38.169 1.00 40.66  ? 504 HOH   A O   1 
HETATM 8558 O  O   . HOH   JA 13 .   ? 60.860  13.522  44.859 1.00 39.39  ? 505 HOH   A O   1 
HETATM 8559 O  O   . HOH   JA 13 .   ? 63.362  0.050   34.627 1.00 29.78  ? 506 HOH   A O   1 
HETATM 8560 O  O   . HOH   JA 13 .   ? 42.704  -10.078 18.895 1.00 47.46  ? 507 HOH   A O   1 
HETATM 8561 O  O   . HOH   JA 13 .   ? 22.854  -1.822  42.218 1.00 32.96  ? 508 HOH   A O   1 
HETATM 8562 O  O   . HOH   JA 13 .   ? 40.558  15.637  31.563 1.00 31.97  ? 509 HOH   A O   1 
HETATM 8563 O  O   . HOH   JA 13 .   ? 36.717  9.564   31.445 1.00 43.18  ? 510 HOH   A O   1 
HETATM 8564 O  O   . HOH   JA 13 .   ? 68.628  13.042  48.084 1.00 41.27  ? 511 HOH   A O   1 
HETATM 8565 O  O   . HOH   JA 13 .   ? 35.075  -1.940  54.081 1.00 29.24  ? 512 HOH   A O   1 
HETATM 8566 O  O   . HOH   JA 13 .   ? 55.693  7.313   43.833 1.00 34.96  ? 513 HOH   A O   1 
HETATM 8567 O  O   . HOH   JA 13 .   ? 45.168  5.091   31.999 1.00 37.54  ? 514 HOH   A O   1 
HETATM 8568 O  O   . HOH   JA 13 .   ? 33.530  10.261  37.331 1.00 33.09  ? 515 HOH   A O   1 
HETATM 8569 O  O   . HOH   JA 13 .   ? 23.875  1.197   43.270 1.00 34.62  ? 516 HOH   A O   1 
HETATM 8570 O  O   . HOH   JA 13 .   ? 46.374  -1.736  53.999 1.00 44.52  ? 517 HOH   A O   1 
HETATM 8571 O  O   . HOH   JA 13 .   ? 50.712  -21.741 37.033 1.00 45.49  ? 518 HOH   A O   1 
HETATM 8572 O  O   . HOH   JA 13 .   ? 39.213  7.639   35.616 1.00 26.89  ? 519 HOH   A O   1 
HETATM 8573 O  O   . HOH   JA 13 .   ? 57.059  -5.729  45.286 1.00 29.11  ? 520 HOH   A O   1 
HETATM 8574 O  O   . HOH   JA 13 .   ? 58.199  0.089   47.338 1.00 33.43  ? 521 HOH   A O   1 
HETATM 8575 O  O   . HOH   JA 13 .   ? 56.165  -10.868 46.399 1.00 42.60  ? 522 HOH   A O   1 
HETATM 8576 O  O   . HOH   JA 13 .   ? 30.566  -13.935 49.058 1.00 34.49  ? 523 HOH   A O   1 
HETATM 8577 O  O   . HOH   JA 13 .   ? 48.640  10.249  36.567 1.00 32.61  ? 524 HOH   A O   1 
HETATM 8578 O  O   . HOH   JA 13 .   ? 33.029  -2.563  16.769 1.00 41.57  ? 525 HOH   A O   1 
HETATM 8579 O  O   . HOH   JA 13 .   ? 48.358  8.454   50.026 1.00 36.56  ? 526 HOH   A O   1 
HETATM 8580 O  O   . HOH   JA 13 .   ? 46.506  -10.082 47.961 1.00 32.93  ? 527 HOH   A O   1 
HETATM 8581 O  O   . HOH   JA 13 .   ? 38.541  -17.510 46.841 1.00 35.83  ? 528 HOH   A O   1 
HETATM 8582 O  O   . HOH   JA 13 .   ? 52.406  8.402   51.831 1.00 26.96  ? 529 HOH   A O   1 
HETATM 8583 O  O   . HOH   JA 13 .   ? 48.920  -3.574  53.143 1.00 33.94  ? 530 HOH   A O   1 
HETATM 8584 O  O   . HOH   JA 13 .   ? 29.485  -12.362 34.972 1.00 35.36  ? 531 HOH   A O   1 
HETATM 8585 O  O   . HOH   JA 13 .   ? 34.204  12.679  27.708 1.00 37.42  ? 532 HOH   A O   1 
HETATM 8586 O  O   . HOH   JA 13 .   ? 52.597  -7.679  50.729 1.00 42.73  ? 533 HOH   A O   1 
HETATM 8587 O  O   . HOH   JA 13 .   ? 57.568  -3.066  45.546 1.00 33.84  ? 534 HOH   A O   1 
HETATM 8588 O  O   . HOH   JA 13 .   ? 19.418  1.750   23.241 1.00 40.63  ? 535 HOH   A O   1 
HETATM 8589 O  O   . HOH   JA 13 .   ? 32.949  -10.092 22.505 1.00 32.13  ? 536 HOH   A O   1 
HETATM 8590 O  O   . HOH   JA 13 .   ? 40.487  12.142  33.241 1.00 29.43  ? 537 HOH   A O   1 
HETATM 8591 O  O   . HOH   JA 13 .   ? 46.779  7.649   38.059 1.00 30.30  ? 538 HOH   A O   1 
HETATM 8592 O  O   . HOH   JA 13 .   ? 42.041  7.151   54.566 1.00 38.85  ? 539 HOH   A O   1 
HETATM 8593 O  O   . HOH   JA 13 .   ? 46.034  -24.613 36.772 1.00 41.22  ? 540 HOH   A O   1 
HETATM 8594 O  O   . HOH   JA 13 .   ? 57.765  7.314   47.541 1.00 31.39  ? 541 HOH   A O   1 
HETATM 8595 O  O   . HOH   JA 13 .   ? 39.406  3.941   18.366 1.00 37.51  ? 542 HOH   A O   1 
HETATM 8596 O  O   . HOH   JA 13 .   ? 37.967  -13.240 35.525 1.00 31.78  ? 543 HOH   A O   1 
HETATM 8597 O  O   . HOH   JA 13 .   ? 30.280  5.120   28.415 1.00 31.55  ? 544 HOH   A O   1 
HETATM 8598 O  O   . HOH   JA 13 .   ? 31.983  -1.631  49.420 1.00 29.11  ? 545 HOH   A O   1 
HETATM 8599 O  O   . HOH   JA 13 .   ? 44.199  11.579  29.434 1.00 39.61  ? 546 HOH   A O   1 
HETATM 8600 O  O   . HOH   JA 13 .   ? 52.171  -15.626 32.934 1.00 44.26  ? 547 HOH   A O   1 
HETATM 8601 O  O   . HOH   JA 13 .   ? 56.819  -13.173 37.471 1.00 33.00  ? 548 HOH   A O   1 
HETATM 8602 O  O   . HOH   JA 13 .   ? 47.996  -15.269 43.042 1.00 41.99  ? 549 HOH   A O   1 
HETATM 8603 O  O   . HOH   JA 13 .   ? 25.111  -9.064  38.928 1.00 36.74  ? 550 HOH   A O   1 
HETATM 8604 O  O   . HOH   JA 13 .   ? 73.074  4.619   34.650 1.00 44.35  ? 551 HOH   A O   1 
HETATM 8605 O  O   . HOH   JA 13 .   ? 37.656  1.975   18.582 1.00 37.62  ? 552 HOH   A O   1 
HETATM 8606 O  O   . HOH   JA 13 .   ? 46.835  -15.282 36.595 1.00 26.30  ? 553 HOH   A O   1 
HETATM 8607 O  O   . HOH   JA 13 .   ? 39.248  2.466   57.049 1.00 35.88  ? 554 HOH   A O   1 
HETATM 8608 O  O   . HOH   JA 13 .   ? 40.461  2.125   42.085 1.00 23.71  ? 555 HOH   A O   1 
HETATM 8609 O  O   . HOH   JA 13 .   ? 20.054  -10.474 22.715 1.00 43.20  ? 556 HOH   A O   1 
HETATM 8610 O  O   . HOH   JA 13 .   ? 37.105  -18.326 30.906 1.00 35.50  ? 557 HOH   A O   1 
HETATM 8611 O  O   . HOH   JA 13 .   ? 43.690  15.636  30.220 1.00 35.17  ? 558 HOH   A O   1 
HETATM 8612 O  O   . HOH   JA 13 .   ? 49.507  5.859   47.130 1.00 27.48  ? 559 HOH   A O   1 
HETATM 8613 O  O   . HOH   JA 13 .   ? 71.086  -2.978  40.827 1.00 45.31  ? 560 HOH   A O   1 
HETATM 8614 O  O   . HOH   JA 13 .   ? 34.699  -3.836  55.845 1.00 34.44  ? 561 HOH   A O   1 
HETATM 8615 O  O   . HOH   JA 13 .   ? 37.282  -13.479 26.500 1.00 44.59  ? 562 HOH   A O   1 
HETATM 8616 O  O   . HOH   JA 13 .   ? 32.241  2.332   41.840 1.00 33.81  ? 563 HOH   A O   1 
HETATM 8617 O  O   . HOH   JA 13 .   ? 54.102  9.599   43.826 1.00 32.19  ? 564 HOH   A O   1 
HETATM 8618 O  O   . HOH   JA 13 .   ? 47.123  9.969   31.682 1.00 43.35  ? 565 HOH   A O   1 
HETATM 8619 O  O   . HOH   JA 13 .   ? 54.868  -0.549  55.262 1.00 42.70  ? 566 HOH   A O   1 
HETATM 8620 O  O   . HOH   JA 13 .   ? 66.685  -0.163  38.329 1.00 37.53  ? 567 HOH   A O   1 
HETATM 8621 O  O   . HOH   JA 13 .   ? 20.548  2.731   31.641 1.00 45.54  ? 568 HOH   A O   1 
HETATM 8622 O  O   . HOH   JA 13 .   ? 65.698  -0.361  35.960 1.00 30.75  ? 569 HOH   A O   1 
HETATM 8623 O  O   . HOH   JA 13 .   ? 35.126  7.299   44.223 1.00 37.87  ? 570 HOH   A O   1 
HETATM 8624 O  O   . HOH   JA 13 .   ? 27.349  -11.360 32.323 1.00 32.12  ? 571 HOH   A O   1 
HETATM 8625 O  O   . HOH   JA 13 .   ? 38.942  -14.935 29.655 1.00 33.27  ? 572 HOH   A O   1 
HETATM 8626 O  O   . HOH   JA 13 .   ? 44.421  -11.772 47.541 1.00 34.31  ? 573 HOH   A O   1 
HETATM 8627 O  O   . HOH   JA 13 .   ? 31.397  12.008  37.070 1.00 31.16  ? 574 HOH   A O   1 
HETATM 8628 O  O   . HOH   JA 13 .   ? 38.197  5.029   35.425 1.00 31.40  ? 575 HOH   A O   1 
HETATM 8629 O  O   . HOH   JA 13 .   ? 25.465  3.264   13.851 1.00 41.51  ? 576 HOH   A O   1 
HETATM 8630 O  O   . HOH   JA 13 .   ? 70.607  3.803   48.098 1.00 39.05  ? 577 HOH   A O   1 
HETATM 8631 O  O   . HOH   JA 13 .   ? 65.687  7.600   51.584 1.00 35.55  ? 578 HOH   A O   1 
HETATM 8632 O  O   . HOH   JA 13 .   ? 22.405  -4.933  19.087 1.00 34.48  ? 579 HOH   A O   1 
HETATM 8633 O  O   . HOH   JA 13 .   ? 35.267  4.974   42.933 1.00 32.98  ? 580 HOH   A O   1 
HETATM 8634 O  O   . HOH   JA 13 .   ? 30.629  -10.093 56.192 1.00 34.57  ? 581 HOH   A O   1 
HETATM 8635 O  O   . HOH   JA 13 .   ? 68.286  2.685   38.167 1.00 37.25  ? 582 HOH   A O   1 
HETATM 8636 O  O   . HOH   JA 13 .   ? 49.165  -15.422 35.279 1.00 27.86  ? 583 HOH   A O   1 
HETATM 8637 O  O   . HOH   JA 13 .   ? 28.755  -0.315  46.836 1.00 35.17  ? 584 HOH   A O   1 
HETATM 8638 O  O   . HOH   JA 13 .   ? 44.145  -22.527 32.864 1.00 39.13  ? 585 HOH   A O   1 
HETATM 8639 O  O   . HOH   JA 13 .   ? 45.339  12.401  45.273 1.00 31.41  ? 586 HOH   A O   1 
HETATM 8640 O  O   . HOH   JA 13 .   ? 20.594  3.818   28.512 1.00 41.98  ? 587 HOH   A O   1 
HETATM 8641 O  O   . HOH   JA 13 .   ? 48.754  9.384   29.500 1.00 27.54  ? 588 HOH   A O   1 
HETATM 8642 O  O   . HOH   JA 13 .   ? 51.363  9.479   30.138 1.00 34.36  ? 589 HOH   A O   1 
HETATM 8643 O  O   . HOH   JA 13 .   ? 55.215  -5.678  47.407 1.00 29.59  ? 590 HOH   A O   1 
HETATM 8644 O  O   . HOH   JA 13 .   ? 22.343  -0.012  16.031 1.00 31.60  ? 591 HOH   A O   1 
HETATM 8645 O  O   . HOH   JA 13 .   ? 31.397  5.719   42.632 1.00 31.06  ? 592 HOH   A O   1 
HETATM 8646 O  O   . HOH   JA 13 .   ? 34.047  12.296  30.418 1.00 31.73  ? 593 HOH   A O   1 
HETATM 8647 O  O   . HOH   JA 13 .   ? 58.410  1.987   57.012 1.00 43.73  ? 594 HOH   A O   1 
HETATM 8648 O  O   . HOH   JA 13 .   ? 28.573  -14.787 37.311 1.00 42.55  ? 595 HOH   A O   1 
HETATM 8649 O  O   . HOH   JA 13 .   ? 49.731  5.940   15.582 1.00 41.46  ? 596 HOH   A O   1 
HETATM 8650 O  O   . HOH   JA 13 .   ? 27.209  1.453   45.289 1.00 37.08  ? 597 HOH   A O   1 
HETATM 8651 O  O   . HOH   JA 13 .   ? 66.083  10.865  48.996 1.00 34.76  ? 598 HOH   A O   1 
HETATM 8652 O  O   . HOH   JA 13 .   ? 54.252  -2.544  53.538 1.00 40.74  ? 599 HOH   A O   1 
HETATM 8653 O  O   . HOH   JA 13 .   ? 61.317  -4.875  55.312 1.00 36.58  ? 600 HOH   A O   1 
HETATM 8654 O  O   . HOH   JA 13 .   ? 29.239  -11.251 48.813 1.00 31.59  ? 601 HOH   A O   1 
HETATM 8655 O  O   . HOH   JA 13 .   ? 47.411  11.304  27.841 1.00 36.71  ? 602 HOH   A O   1 
HETATM 8656 O  O   . HOH   JA 13 .   ? 75.353  2.844   40.448 1.00 31.56  ? 603 HOH   A O   1 
HETATM 8657 O  O   . HOH   JA 13 .   ? 48.980  13.342  28.098 1.00 39.70  ? 604 HOH   A O   1 
HETATM 8658 O  O   . HOH   JA 13 .   ? 39.963  8.621   47.731 1.00 29.61  ? 605 HOH   A O   1 
HETATM 8659 O  O   . HOH   JA 13 .   ? 28.954  -13.799 32.622 1.00 41.12  ? 606 HOH   A O   1 
HETATM 8660 O  O   . HOH   JA 13 .   ? 36.136  15.124  43.065 1.00 42.96  ? 607 HOH   A O   1 
HETATM 8661 O  O   . HOH   JA 13 .   ? 43.105  12.779  46.764 1.00 36.95  ? 608 HOH   A O   1 
HETATM 8662 O  O   . HOH   JA 13 .   ? 34.733  -3.729  51.927 1.00 25.52  ? 609 HOH   A O   1 
HETATM 8663 O  O   . HOH   JA 13 .   ? 39.064  -24.581 34.740 1.00 38.13  ? 610 HOH   A O   1 
HETATM 8664 O  O   . HOH   JA 13 .   ? 37.658  6.955   48.374 1.00 33.78  ? 611 HOH   A O   1 
HETATM 8665 O  O   . HOH   JA 13 .   ? 33.950  0.053   40.881 1.00 36.90  ? 612 HOH   A O   1 
HETATM 8666 O  O   . HOH   JA 13 .   ? 48.471  -11.254 49.379 1.00 33.40  ? 613 HOH   A O   1 
HETATM 8667 O  O   . HOH   JA 13 .   ? 51.664  10.964  50.941 1.00 35.66  ? 614 HOH   A O   1 
HETATM 8668 O  O   . HOH   JA 13 .   ? 62.977  13.529  32.981 1.00 42.59  ? 615 HOH   A O   1 
HETATM 8669 O  O   . HOH   JA 13 .   ? 24.302  14.307  34.654 1.00 38.59  ? 616 HOH   A O   1 
HETATM 8670 O  O   . HOH   JA 13 .   ? 26.311  9.882   38.843 1.00 32.10  ? 617 HOH   A O   1 
HETATM 8671 O  O   . HOH   JA 13 .   ? 45.457  15.016  40.360 1.00 43.62  ? 618 HOH   A O   1 
HETATM 8672 O  O   . HOH   JA 13 .   ? 48.320  18.049  22.504 1.00 56.32  ? 619 HOH   A O   1 
HETATM 8673 O  O   . HOH   JA 13 .   ? 42.831  -6.597  14.950 1.00 46.86  ? 620 HOH   A O   1 
HETATM 8674 O  O   . HOH   JA 13 .   ? 48.585  -10.538 52.481 1.00 41.18  ? 621 HOH   A O   1 
HETATM 8675 O  O   . HOH   JA 13 .   ? 67.555  6.655   54.281 1.00 38.57  ? 622 HOH   A O   1 
HETATM 8676 O  O   . HOH   JA 13 .   ? 40.967  12.868  45.223 1.00 36.51  ? 623 HOH   A O   1 
HETATM 8677 O  O   . HOH   JA 13 .   ? 25.678  11.324  36.454 1.00 42.88  ? 624 HOH   A O   1 
HETATM 8678 O  O   . HOH   JA 13 .   ? 49.719  -19.473 44.494 1.00 40.70  ? 625 HOH   A O   1 
HETATM 8679 O  O   . HOH   JA 13 .   ? 24.268  3.758   43.694 1.00 41.54  ? 626 HOH   A O   1 
HETATM 8680 O  O   . HOH   JA 13 .   ? 34.798  8.742   54.477 1.00 47.02  ? 627 HOH   A O   1 
HETATM 8681 O  O   . HOH   JA 13 .   ? 44.032  6.659   58.836 1.00 40.62  ? 628 HOH   A O   1 
HETATM 8682 O  O   . HOH   JA 13 .   ? 50.203  -17.141 33.344 1.00 35.21  ? 629 HOH   A O   1 
HETATM 8683 O  O   . HOH   JA 13 .   ? 42.196  7.781   57.382 1.00 41.69  ? 630 HOH   A O   1 
HETATM 8684 O  O   . HOH   JA 13 .   ? 27.025  -15.864 33.227 1.00 41.56  ? 631 HOH   A O   1 
HETATM 8685 O  O   . HOH   JA 13 .   ? 55.508  -10.651 48.950 1.00 38.83  ? 632 HOH   A O   1 
HETATM 8686 O  O   . HOH   JA 13 .   ? 29.663  4.099   48.416 1.00 46.10  ? 633 HOH   A O   1 
HETATM 8687 O  O   . HOH   JA 13 .   ? 22.649  15.299  26.535 1.00 47.85  ? 634 HOH   A O   1 
HETATM 8688 O  O   . HOH   KA 13 .   ? 22.752  -30.331 50.981 1.00 35.66  ? 501 HOH   B O   1 
HETATM 8689 O  O   . HOH   KA 13 .   ? 1.779   -26.397 57.412 1.00 45.97  ? 502 HOH   B O   1 
HETATM 8690 O  O   . HOH   KA 13 .   ? 25.342  0.076   56.277 1.00 42.69  ? 503 HOH   B O   1 
HETATM 8691 O  O   . HOH   KA 13 .   ? 1.282   5.286   66.507 1.00 30.76  ? 504 HOH   B O   1 
HETATM 8692 O  O   . HOH   KA 13 .   ? 28.281  -7.334  53.995 1.00 28.79  ? 505 HOH   B O   1 
HETATM 8693 O  O   . HOH   KA 13 .   ? 19.535  4.931   49.789 1.00 34.05  ? 506 HOH   B O   1 
HETATM 8694 O  O   . HOH   KA 13 .   ? 16.285  -11.233 69.023 1.00 36.08  ? 507 HOH   B O   1 
HETATM 8695 O  O   . HOH   KA 13 .   ? -10.319 -2.548  64.933 1.00 35.88  ? 508 HOH   B O   1 
HETATM 8696 O  O   . HOH   KA 13 .   ? 0.125   9.302   65.436 1.00 43.81  ? 509 HOH   B O   1 
HETATM 8697 O  O   . HOH   KA 13 .   ? 9.652   -10.281 73.235 1.00 41.43  ? 510 HOH   B O   1 
HETATM 8698 O  O   . HOH   KA 13 .   ? 12.285  4.604   68.290 1.00 41.13  ? 511 HOH   B O   1 
HETATM 8699 O  O   . HOH   KA 13 .   ? 22.878  -14.221 46.815 1.00 36.95  ? 512 HOH   B O   1 
HETATM 8700 O  O   . HOH   KA 13 .   ? 20.964  -7.005  66.782 1.00 34.05  ? 513 HOH   B O   1 
HETATM 8701 O  O   . HOH   KA 13 .   ? 7.088   5.751   62.826 1.00 31.68  ? 514 HOH   B O   1 
HETATM 8702 O  O   . HOH   KA 13 .   ? 23.995  -22.740 51.679 1.00 24.51  ? 515 HOH   B O   1 
HETATM 8703 O  O   . HOH   KA 13 .   ? 6.778   -2.801  70.446 1.00 32.94  ? 516 HOH   B O   1 
HETATM 8704 O  O   . HOH   KA 13 .   ? 22.948  -17.588 70.366 1.00 46.67  ? 517 HOH   B O   1 
HETATM 8705 O  O   . HOH   KA 13 .   ? -3.411  4.515   56.743 1.00 46.01  ? 518 HOH   B O   1 
HETATM 8706 O  O   . HOH   KA 13 .   ? 14.121  -7.637  71.632 1.00 30.70  ? 519 HOH   B O   1 
HETATM 8707 O  O   . HOH   KA 13 .   ? 22.126  -31.407 57.271 1.00 31.84  ? 520 HOH   B O   1 
HETATM 8708 O  O   . HOH   KA 13 .   ? -15.952 1.752   72.568 1.00 38.39  ? 521 HOH   B O   1 
HETATM 8709 O  O   . HOH   KA 13 .   ? 28.023  -9.851  51.818 1.00 30.35  ? 522 HOH   B O   1 
HETATM 8710 O  O   . HOH   KA 13 .   ? 11.432  -26.302 53.815 1.00 37.75  ? 523 HOH   B O   1 
HETATM 8711 O  O   . HOH   KA 13 .   ? -2.618  7.204   59.522 1.00 37.73  ? 524 HOH   B O   1 
HETATM 8712 O  O   . HOH   KA 13 .   ? -12.388 -0.793  64.368 1.00 39.87  ? 525 HOH   B O   1 
HETATM 8713 O  O   . HOH   KA 13 .   ? 8.330   0.718   42.741 1.00 50.31  ? 526 HOH   B O   1 
HETATM 8714 O  O   . HOH   KA 13 .   ? 20.103  -17.591 64.686 1.00 31.30  ? 527 HOH   B O   1 
HETATM 8715 O  O   . HOH   KA 13 .   ? 14.989  -7.883  75.278 1.00 37.04  ? 528 HOH   B O   1 
HETATM 8716 O  O   . HOH   KA 13 .   ? 14.587  -8.684  63.625 1.00 28.88  ? 529 HOH   B O   1 
HETATM 8717 O  O   . HOH   KA 13 .   ? 18.720  -19.788 47.896 1.00 31.78  ? 530 HOH   B O   1 
HETATM 8718 O  O   . HOH   KA 13 .   ? 9.018   -14.005 47.112 1.00 23.76  ? 531 HOH   B O   1 
HETATM 8719 O  O   . HOH   KA 13 .   ? 27.175  -18.478 66.693 1.00 34.04  ? 532 HOH   B O   1 
HETATM 8720 O  O   . HOH   KA 13 .   ? 0.481   -10.630 46.924 1.00 37.30  ? 533 HOH   B O   1 
HETATM 8721 O  O   . HOH   KA 13 .   ? 21.394  -0.013  51.115 1.00 29.97  ? 534 HOH   B O   1 
HETATM 8722 O  O   . HOH   KA 13 .   ? 6.241   -19.373 47.931 1.00 33.80  ? 535 HOH   B O   1 
HETATM 8723 O  O   . HOH   KA 13 .   ? 21.618  -14.671 73.958 1.00 40.21  ? 536 HOH   B O   1 
HETATM 8724 O  O   . HOH   KA 13 .   ? 17.395  -32.914 59.274 1.00 40.80  ? 537 HOH   B O   1 
HETATM 8725 O  O   . HOH   KA 13 .   ? 13.037  -2.709  59.118 1.00 28.95  ? 538 HOH   B O   1 
HETATM 8726 O  O   . HOH   KA 13 .   ? 25.114  -22.748 49.361 1.00 36.95  ? 539 HOH   B O   1 
HETATM 8727 O  O   . HOH   KA 13 .   ? 3.023   5.335   68.633 1.00 38.19  ? 540 HOH   B O   1 
HETATM 8728 O  O   . HOH   KA 13 .   ? 12.546  -29.447 62.976 1.00 36.41  ? 541 HOH   B O   1 
HETATM 8729 O  O   . HOH   KA 13 .   ? -1.664  4.888   53.351 1.00 44.47  ? 542 HOH   B O   1 
HETATM 8730 O  O   . HOH   KA 13 .   ? 18.970  -2.893  60.241 1.00 38.52  ? 543 HOH   B O   1 
HETATM 8731 O  O   . HOH   KA 13 .   ? 8.099   -2.728  66.894 1.00 34.67  ? 544 HOH   B O   1 
HETATM 8732 O  O   . HOH   KA 13 .   ? 6.081   8.327   51.620 1.00 40.88  ? 545 HOH   B O   1 
HETATM 8733 O  O   . HOH   KA 13 .   ? 16.746  3.844   62.767 1.00 41.06  ? 546 HOH   B O   1 
HETATM 8734 O  O   . HOH   KA 13 .   ? 19.096  -14.488 72.771 1.00 31.52  ? 547 HOH   B O   1 
HETATM 8735 O  O   . HOH   KA 13 .   ? 1.033   -19.642 49.207 1.00 39.14  ? 548 HOH   B O   1 
HETATM 8736 O  O   . HOH   KA 13 .   ? 25.787  -12.912 49.751 1.00 36.15  ? 549 HOH   B O   1 
HETATM 8737 O  O   . HOH   KA 13 .   ? 22.985  5.943   47.454 1.00 36.41  ? 550 HOH   B O   1 
HETATM 8738 O  O   . HOH   KA 13 .   ? 2.771   -16.384 62.521 1.00 46.00  ? 551 HOH   B O   1 
HETATM 8739 O  O   . HOH   KA 13 .   ? 21.302  -28.365 45.739 1.00 45.31  ? 552 HOH   B O   1 
HETATM 8740 O  O   . HOH   KA 13 .   ? 20.464  -33.907 59.948 1.00 39.18  ? 553 HOH   B O   1 
HETATM 8741 O  O   . HOH   KA 13 .   ? -7.751  -5.651  50.864 1.00 35.51  ? 554 HOH   B O   1 
HETATM 8742 O  O   . HOH   KA 13 .   ? 20.728  -5.601  57.534 1.00 33.22  ? 555 HOH   B O   1 
HETATM 8743 O  O   . HOH   KA 13 .   ? 28.761  -14.204 53.689 1.00 39.16  ? 556 HOH   B O   1 
HETATM 8744 O  O   . HOH   KA 13 .   ? -13.606 -12.311 68.301 1.00 40.91  ? 557 HOH   B O   1 
HETATM 8745 O  O   . HOH   KA 13 .   ? 23.379  -7.327  67.708 1.00 31.64  ? 558 HOH   B O   1 
HETATM 8746 O  O   . HOH   KA 13 .   ? 6.978   -20.001 44.321 1.00 37.22  ? 559 HOH   B O   1 
HETATM 8747 O  O   . HOH   KA 13 .   ? 6.608   2.967   47.440 1.00 37.20  ? 560 HOH   B O   1 
HETATM 8748 O  O   . HOH   KA 13 .   ? 19.614  -12.396 71.199 1.00 34.29  ? 561 HOH   B O   1 
HETATM 8749 O  O   . HOH   KA 13 .   ? 0.477   -22.944 58.816 1.00 31.97  ? 562 HOH   B O   1 
HETATM 8750 O  O   . HOH   KA 13 .   ? 22.615  -4.142  60.135 1.00 35.88  ? 563 HOH   B O   1 
HETATM 8751 O  O   . HOH   KA 13 .   ? 15.151  5.381   67.614 1.00 42.94  ? 564 HOH   B O   1 
HETATM 8752 O  O   . HOH   KA 13 .   ? 6.893   -7.755  71.650 1.00 41.13  ? 565 HOH   B O   1 
HETATM 8753 O  O   . HOH   KA 13 .   ? 20.788  -4.361  42.236 1.00 40.28  ? 566 HOH   B O   1 
HETATM 8754 O  O   . HOH   KA 13 .   ? 6.542   -10.832 74.073 1.00 37.19  ? 567 HOH   B O   1 
HETATM 8755 O  O   . HOH   KA 13 .   ? -17.106 -8.035  63.339 1.00 35.90  ? 568 HOH   B O   1 
HETATM 8756 O  O   . HOH   KA 13 .   ? -2.163  -11.130 47.649 1.00 33.32  ? 569 HOH   B O   1 
HETATM 8757 O  O   . HOH   KA 13 .   ? 11.784  -27.314 40.777 1.00 53.20  ? 570 HOH   B O   1 
HETATM 8758 O  O   . HOH   KA 13 .   ? 18.132  -6.485  56.236 1.00 32.07  ? 571 HOH   B O   1 
HETATM 8759 O  O   . HOH   KA 13 .   ? 18.646  2.492   48.847 1.00 30.65  ? 572 HOH   B O   1 
HETATM 8760 O  O   . HOH   KA 13 .   ? 25.560  -4.146  54.043 1.00 40.12  ? 573 HOH   B O   1 
HETATM 8761 O  O   . HOH   KA 13 .   ? -1.905  -4.018  40.794 1.00 47.96  ? 574 HOH   B O   1 
HETATM 8762 O  O   . HOH   KA 13 .   ? 20.627  -9.039  38.988 1.00 38.09  ? 575 HOH   B O   1 
HETATM 8763 O  O   . HOH   KA 13 .   ? 8.488   3.093   44.223 1.00 42.03  ? 576 HOH   B O   1 
HETATM 8764 O  O   . HOH   KA 13 .   ? 24.869  10.752  51.766 1.00 45.44  ? 577 HOH   B O   1 
HETATM 8765 O  O   . HOH   KA 13 .   ? 9.783   -11.638 34.605 1.00 43.11  ? 578 HOH   B O   1 
HETATM 8766 O  O   . HOH   KA 13 .   ? 22.519  8.700   58.998 1.00 46.39  ? 579 HOH   B O   1 
HETATM 8767 O  O   . HOH   KA 13 .   ? 28.385  -14.990 56.495 1.00 38.50  ? 580 HOH   B O   1 
HETATM 8768 O  O   . HOH   KA 13 .   ? 28.978  1.076   50.107 1.00 27.71  ? 581 HOH   B O   1 
HETATM 8769 O  O   . HOH   KA 13 .   ? 29.769  -10.906 69.458 1.00 38.75  ? 582 HOH   B O   1 
HETATM 8770 O  O   . HOH   KA 13 .   ? 6.275   -13.045 82.489 1.00 48.55  ? 583 HOH   B O   1 
HETATM 8771 O  O   . HOH   KA 13 .   ? -6.702  -18.888 61.376 1.00 52.26  ? 584 HOH   B O   1 
HETATM 8772 O  O   . HOH   KA 13 .   ? 27.085  -20.942 65.967 1.00 36.65  ? 585 HOH   B O   1 
HETATM 8773 O  O   . HOH   KA 13 .   ? 28.363  -9.821  66.135 1.00 38.40  ? 586 HOH   B O   1 
HETATM 8774 O  O   . HOH   KA 13 .   ? 17.056  1.699   34.151 1.00 44.04  ? 587 HOH   B O   1 
HETATM 8775 O  O   . HOH   KA 13 .   ? -10.202 -16.706 69.178 1.00 50.46  ? 588 HOH   B O   1 
HETATM 8776 O  O   . HOH   KA 13 .   ? -4.942  14.305  71.021 1.00 39.07  ? 589 HOH   B O   1 
HETATM 8777 O  O   . HOH   KA 13 .   ? 16.957  3.355   67.987 1.00 48.95  ? 590 HOH   B O   1 
HETATM 8778 O  O   . HOH   KA 13 .   ? 8.831   -28.185 49.937 1.00 44.74  ? 591 HOH   B O   1 
HETATM 8779 O  O   . HOH   KA 13 .   ? 28.872  -6.230  56.446 1.00 37.83  ? 592 HOH   B O   1 
HETATM 8780 O  O   . HOH   KA 13 .   ? 21.982  -0.644  58.309 1.00 44.77  ? 593 HOH   B O   1 
HETATM 8781 O  O   . HOH   LA 13 .   ? -10.926 29.407  12.349 1.00 44.99  ? 501 HOH   C O   1 
HETATM 8782 O  O   . HOH   LA 13 .   ? 10.857  -2.006  30.554 1.00 41.60  ? 502 HOH   C O   1 
HETATM 8783 O  O   . HOH   LA 13 .   ? 2.329   6.980   27.047 1.00 40.07  ? 503 HOH   C O   1 
HETATM 8784 O  O   . HOH   LA 13 .   ? -23.066 15.970  10.096 1.00 43.07  ? 504 HOH   C O   1 
HETATM 8785 O  O   . HOH   LA 13 .   ? -21.004 0.973   22.980 1.00 38.76  ? 505 HOH   C O   1 
HETATM 8786 O  O   . HOH   LA 13 .   ? 1.656   -5.526  13.663 1.00 38.31  ? 506 HOH   C O   1 
HETATM 8787 O  O   . HOH   LA 13 .   ? 1.239   9.187   27.174 1.00 42.18  ? 507 HOH   C O   1 
HETATM 8788 O  O   . HOH   LA 13 .   ? 12.051  3.238   14.434 1.00 31.40  ? 508 HOH   C O   1 
HETATM 8789 O  O   . HOH   LA 13 .   ? 2.315   -15.033 24.775 1.00 52.29  ? 509 HOH   C O   1 
HETATM 8790 O  O   . HOH   LA 13 .   ? -8.415  18.123  27.380 1.00 49.52  ? 510 HOH   C O   1 
HETATM 8791 O  O   . HOH   LA 13 .   ? 4.739   -0.569  25.567 1.00 34.90  ? 511 HOH   C O   1 
HETATM 8792 O  O   . HOH   LA 13 .   ? -9.522  12.722  23.811 1.00 38.98  ? 512 HOH   C O   1 
HETATM 8793 O  O   . HOH   LA 13 .   ? 5.556   -4.566  26.419 1.00 40.39  ? 513 HOH   C O   1 
HETATM 8794 O  O   . HOH   LA 13 .   ? -4.488  -9.084  14.438 1.00 36.02  ? 514 HOH   C O   1 
HETATM 8795 O  O   . HOH   LA 13 .   ? -12.652 13.193  3.306  1.00 36.90  ? 515 HOH   C O   1 
HETATM 8796 O  O   . HOH   LA 13 .   ? 2.796   -5.319  16.041 1.00 33.57  ? 516 HOH   C O   1 
HETATM 8797 O  O   . HOH   LA 13 .   ? 21.982  -7.058  29.561 1.00 29.59  ? 517 HOH   C O   1 
HETATM 8798 O  O   . HOH   LA 13 .   ? -1.758  5.697   1.276  1.00 37.79  ? 518 HOH   C O   1 
HETATM 8799 O  O   . HOH   LA 13 .   ? -20.276 -3.997  23.702 1.00 38.22  ? 519 HOH   C O   1 
HETATM 8800 O  O   . HOH   LA 13 .   ? -9.744  -5.088  12.418 1.00 36.30  ? 520 HOH   C O   1 
HETATM 8801 O  O   . HOH   LA 13 .   ? 3.984   -6.353  19.487 1.00 32.25  ? 521 HOH   C O   1 
HETATM 8802 O  O   . HOH   LA 13 .   ? 14.019  -1.318  14.767 1.00 33.60  ? 522 HOH   C O   1 
HETATM 8803 O  O   . HOH   LA 13 .   ? -1.799  7.963   25.646 1.00 34.78  ? 523 HOH   C O   1 
HETATM 8804 O  O   . HOH   LA 13 .   ? -4.412  11.738  4.273  1.00 37.79  ? 524 HOH   C O   1 
HETATM 8805 O  O   . HOH   LA 13 .   ? -2.428  -1.478  26.505 1.00 36.71  ? 525 HOH   C O   1 
HETATM 8806 O  O   . HOH   LA 13 .   ? -10.204 5.585   22.848 1.00 35.56  ? 526 HOH   C O   1 
HETATM 8807 O  O   . HOH   LA 13 .   ? 3.843   2.074   5.427  1.00 36.32  ? 527 HOH   C O   1 
HETATM 8808 O  O   . HOH   LA 13 .   ? -14.938 8.536   7.024  1.00 35.57  ? 528 HOH   C O   1 
HETATM 8809 O  O   . HOH   LA 13 .   ? 13.726  1.215   13.867 1.00 25.18  ? 529 HOH   C O   1 
HETATM 8810 O  O   . HOH   LA 13 .   ? -9.373  1.360   -4.341 1.00 35.96  ? 530 HOH   C O   1 
HETATM 8811 O  O   . HOH   LA 13 .   ? 4.238   0.805   28.060 1.00 30.58  ? 531 HOH   C O   1 
HETATM 8812 O  O   . HOH   LA 13 .   ? 16.201  9.614   20.073 1.00 39.30  ? 532 HOH   C O   1 
HETATM 8813 O  O   . HOH   LA 13 .   ? 2.175   -0.165  2.137  1.00 36.33  ? 533 HOH   C O   1 
HETATM 8814 O  O   . HOH   LA 13 .   ? 16.454  -1.218  16.859 1.00 34.65  ? 534 HOH   C O   1 
HETATM 8815 O  O   . HOH   LA 13 .   ? -0.095  -6.175  29.813 1.00 39.43  ? 535 HOH   C O   1 
HETATM 8816 O  O   . HOH   LA 13 .   ? 14.563  4.008   32.326 1.00 38.74  ? 536 HOH   C O   1 
HETATM 8817 O  O   . HOH   LA 13 .   ? 19.200  5.061   9.219  1.00 44.34  ? 537 HOH   C O   1 
HETATM 8818 O  O   . HOH   LA 13 .   ? -11.245 -2.823  0.483  1.00 36.72  ? 538 HOH   C O   1 
HETATM 8819 O  O   . HOH   LA 13 .   ? -0.514  -6.768  14.755 1.00 39.47  ? 539 HOH   C O   1 
HETATM 8820 O  O   . HOH   LA 13 .   ? -7.694  4.065   3.845  1.00 32.59  ? 540 HOH   C O   1 
HETATM 8821 O  O   . HOH   LA 13 .   ? 1.986   0.061   4.665  1.00 31.78  ? 541 HOH   C O   1 
HETATM 8822 O  O   . HOH   LA 13 .   ? -7.928  13.101  1.350  1.00 40.60  ? 542 HOH   C O   1 
HETATM 8823 O  O   . HOH   LA 13 .   ? -22.853 20.424  3.754  1.00 44.45  ? 543 HOH   C O   1 
HETATM 8824 O  O   . HOH   LA 13 .   ? 5.471   -7.054  27.508 1.00 40.42  ? 544 HOH   C O   1 
HETATM 8825 O  O   . HOH   LA 13 .   ? -12.111 -3.987  10.741 1.00 34.13  ? 545 HOH   C O   1 
HETATM 8826 O  O   . HOH   LA 13 .   ? 22.111  -5.773  16.280 1.00 29.90  ? 546 HOH   C O   1 
HETATM 8827 O  O   . HOH   LA 13 .   ? -8.216  -2.187  5.860  1.00 44.31  ? 547 HOH   C O   1 
HETATM 8828 O  O   . HOH   LA 13 .   ? -22.196 17.779  -1.866 1.00 52.75  ? 548 HOH   C O   1 
HETATM 8829 O  O   . HOH   LA 13 .   ? 11.674  -11.079 26.524 1.00 42.26  ? 549 HOH   C O   1 
HETATM 8830 O  O   . HOH   LA 13 .   ? 17.053  4.440   28.576 1.00 38.65  ? 550 HOH   C O   1 
HETATM 8831 O  O   . HOH   LA 13 .   ? -20.057 -2.720  21.198 1.00 33.30  ? 551 HOH   C O   1 
HETATM 8832 O  O   . HOH   LA 13 .   ? -5.157  4.234   2.844  1.00 31.25  ? 552 HOH   C O   1 
HETATM 8833 O  O   . HOH   LA 13 .   ? -24.457 10.053  7.766  1.00 44.39  ? 553 HOH   C O   1 
HETATM 8834 O  O   . HOH   LA 13 .   ? 2.784   17.950  25.729 1.00 42.64  ? 554 HOH   C O   1 
HETATM 8835 O  O   . HOH   LA 13 .   ? -10.786 -6.268  14.296 1.00 38.60  ? 555 HOH   C O   1 
HETATM 8836 O  O   . HOH   LA 13 .   ? 15.755  12.652  9.998  1.00 42.62  ? 556 HOH   C O   1 
HETATM 8837 O  O   . HOH   LA 13 .   ? -12.143 -4.388  -3.897 1.00 43.82  ? 557 HOH   C O   1 
HETATM 8838 O  O   . HOH   LA 13 .   ? 20.672  4.206   16.375 1.00 39.05  ? 558 HOH   C O   1 
HETATM 8839 O  O   . HOH   LA 13 .   ? -7.465  -9.493  19.630 1.00 46.31  ? 559 HOH   C O   1 
HETATM 8840 O  O   . HOH   LA 13 .   ? 13.949  -8.286  28.774 1.00 41.13  ? 560 HOH   C O   1 
HETATM 8841 O  O   . HOH   LA 13 .   ? 8.721   18.693  8.751  1.00 52.01  ? 561 HOH   C O   1 
HETATM 8842 O  O   . HOH   LA 13 .   ? 7.385   23.776  29.981 1.00 48.99  ? 562 HOH   C O   1 
HETATM 8843 O  O   . HOH   LA 13 .   ? -8.696  -5.033  1.579  1.00 50.43  ? 563 HOH   C O   1 
HETATM 8844 O  O   . HOH   LA 13 .   ? -2.261  20.047  6.577  1.00 49.05  ? 564 HOH   C O   1 
HETATM 8845 O  O   . HOH   LA 13 .   ? -26.488 0.869   14.323 1.00 39.35  ? 565 HOH   C O   1 
HETATM 8846 O  O   . HOH   LA 13 .   ? -26.509 -4.067  5.213  1.00 47.55  ? 566 HOH   C O   1 
HETATM 8847 O  O   . HOH   LA 13 .   ? -2.236  -8.915  13.943 1.00 38.51  ? 567 HOH   C O   1 
HETATM 8848 O  O   . HOH   LA 13 .   ? -6.271  3.019   33.986 1.00 37.27  ? 568 HOH   C O   1 
HETATM 8849 O  O   . HOH   LA 13 .   ? -21.704 -11.385 24.070 1.00 48.24  ? 569 HOH   C O   1 
HETATM 8850 O  O   . HOH   LA 13 .   ? -7.439  5.349   33.635 1.00 40.16  ? 570 HOH   C O   1 
HETATM 8851 O  O   . HOH   LA 13 .   ? -19.890 17.515  32.371 1.00 53.23  ? 571 HOH   C O   1 
HETATM 8852 O  O   . HOH   LA 13 .   ? -14.862 -8.904  22.395 1.00 50.44  ? 572 HOH   C O   1 
HETATM 8853 O  O   . HOH   LA 13 .   ? -2.380  -6.011  3.080  1.00 35.52  ? 573 HOH   C O   1 
HETATM 8854 O  O   . HOH   LA 13 .   ? -15.087 32.876  24.277 1.00 46.94  ? 574 HOH   C O   1 
HETATM 8855 O  O   . HOH   LA 13 .   ? -15.545 -10.768 24.544 1.00 45.02  ? 575 HOH   C O   1 
HETATM 8856 O  O   . HOH   LA 13 .   ? -8.965  -9.959  12.692 1.00 45.75  ? 576 HOH   C O   1 
HETATM 8857 O  O   . HOH   LA 13 .   ? -8.903  -7.512  11.636 1.00 39.83  ? 577 HOH   C O   1 
HETATM 8858 O  O   . HOH   LA 13 .   ? 12.284  -14.507 26.065 1.00 42.01  ? 578 HOH   C O   1 
HETATM 8859 O  O   . HOH   LA 13 .   ? -6.640  -4.598  6.016  1.00 38.34  ? 579 HOH   C O   1 
HETATM 8860 O  O   . HOH   LA 13 .   ? -13.168 -4.601  -1.124 1.00 48.11  ? 580 HOH   C O   1 
HETATM 8861 O  O   . HOH   LA 13 .   ? 8.343   -11.767 27.992 1.00 45.32  ? 581 HOH   C O   1 
HETATM 8862 O  O   . HOH   LA 13 .   ? 19.987  -1.431  32.933 1.00 47.51  ? 582 HOH   C O   1 
HETATM 8863 O  O   . HOH   LA 13 .   ? 22.412  -13.760 16.751 1.00 46.10  ? 583 HOH   C O   1 
# 
