data_9HE6
# 
_entry.id   9HE6 
# 
_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   9HE6         pdb_00009he6 10.2210/pdb9he6/pdb 
WWPDB D_1292143183 ?            ?                   
# 
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                        9HE6 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xjulia@iqfr.csic.es 
_pdbx_contact_author.name_first         Julia 
_pdbx_contact_author.name_last          Sanz-Aparicio 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6849-8621 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fernandez-Garcia, A.' 1 0000-0003-2052-6483 
'Sanz-Aparicio, J.'    2 0000-0002-6849-8621 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Characterization of Recombinant Unspecific Peroxygenase from Candolleomyces aberdarensis through Crystallographic and Substrate Selectivity Studies
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202402015 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Menes-Rubio, A.'      1 ? 
primary 'Fernandez-Garcia, A.' 2 ? 
primary 'Monterrey, D.T.'      3 ? 
primary 'de Santos, P.G.'      4 ? 
primary 'Sanchez-Moreno, I.'   5 ? 
primary 'Sanz-Aparicio, J.'    6 ? 
primary 'Alcalde, M.'          7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Heme-thiolate peroxidase' 36630.445 3   1.11.2.1 ? ? ? 
2  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1   ?        ? ? ? 
3  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1235.105  1   ?        ? ? ? 
4  branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2   ? ? ? ? 
5  branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1   ?        ? ? ? 
6  branched    man 
;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1   ?        ? ? ? 
7  non-polymer syn GLYCEROL 92.094    11  ?        ? ? ? 
8  non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   12  ?        ? ? ? 
9  non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
10 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
11 non-polymer syn 'SULFATE ION' 96.063    8   ?        ? ? ? 
12 water       nat water 18.015    395 ?        ? ? ? 
# 
_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  GLYCEROL                                              GOL 
8  '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
9  'PROTOPORPHYRIN IX CONTAINING FE'                     HEM 
10 'MAGNESIUM ION'                                       MG  
11 'SULFATE ION'                                         SO4 
12 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 DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
8  4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
9  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}' LINUCS                      PDB-CARE   ?     
10 5 'DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1' WURCS 
PDB2Glycan 1.1.0 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
13 6 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1' WURCS PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   
?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3  2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4  2 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
5  3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
7  3 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
8  3 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
9  3 6 MAN C1 O1 4 MAN O6 HO6 sing ? 
10 3 7 MAN C1 O1 3 BMA O3 HO3 sing ? 
11 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
12 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
13 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
14 5 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
15 5 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
16 5 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
17 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
18 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
19 6 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 G NAG 1 A NAG 402 n 
D 2 NAG 2 G NAG 2 A NAG 403 n 
D 2 BMA 3 G BMA 3 A BMA 426 n 
D 2 MAN 4 G MAN 4 A MAN 427 n 
D 2 MAN 5 G MAN 5 A MAN 428 n 
E 3 NAG 1 I NAG 1 A NAG 404 n 
E 3 NAG 2 I NAG 2 A NAG 405 n 
E 3 BMA 3 I BMA 3 A BMA 406 n 
E 3 MAN 4 I MAN 4 A MAN 407 n 
E 3 MAN 5 I MAN 5 A MAN 408 n 
E 3 MAN 6 I MAN 6 A MAN 409 n 
E 3 MAN 7 I MAN 7 A MAN 414 n 
F 4 NAG 1 b NAG 1 B NAG 402 n 
F 4 NAG 2 b NAG 2 B NAG 419 n 
G 5 NAG 1 c NAG 1 B NAG 404 n 
G 5 NAG 2 c NAG 2 B NAG 405 n 
G 5 BMA 3 c BMA 3 B BMA 406 n 
G 5 MAN 4 c MAN 4 B MAN 408 n 
G 5 MAN 5 c MAN 5 B MAN 409 n 
G 5 MAN 6 c MAN 6 B MAN 407 n 
H 6 NAG 1 s NAG 1 C NAG 402 n 
H 6 NAG 2 s NAG 2 C NAG 419 n 
H 6 BMA 3 s BMA 3 C BMA 420 n 
H 6 MAN 4 s MAN 4 C MAN 421 n 
I 4 NAG 1 t NAG 1 C NAG 404 n 
I 4 NAG 2 t NAG 2 C NAG 418 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
J  7  GOL 1   401 411 GOL GOL A . 
K  7  GOL 1   402 413 GOL GOL A . 
L  7  GOL 1   403 415 GOL GOL A . 
M  8  EPE 1   404 416 EPE EPE A . 
N  8  EPE 1   405 418 EPE EPE A . 
O  8  EPE 1   406 420 EPE EPE A . 
P  7  GOL 1   407 421 GOL GOL A . 
Q  8  EPE 1   408 422 EPE EPE A . 
R  9  HEM 1   409 425 HEM HEM A . 
S  10 MG  1   410 2   MG  MG  A . 
T  11 SO4 1   411 3   SO4 SO4 A . 
U  11 SO4 1   412 4   SO4 SO4 A . 
V  11 SO4 1   413 8   SO4 SO4 A . 
W  11 SO4 1   414 10  SO4 SO4 A . 
X  7  GOL 1   401 410 GOL GOL B . 
Y  7  GOL 1   402 411 GOL GOL B . 
Z  7  GOL 1   403 412 GOL GOL B . 
AA 8  EPE 1   404 413 EPE EPE B . 
BA 8  EPE 1   405 414 EPE EPE B . 
CA 7  GOL 1   406 415 GOL GOL B . 
DA 8  EPE 1   407 416 EPE EPE B . 
EA 7  GOL 1   408 417 GOL GOL B . 
FA 9  HEM 1   409 418 HEM HEM B . 
GA 10 MG  1   410 3   MG  MG  B . 
HA 11 SO4 1   411 5   SO4 SO4 B . 
IA 11 SO4 1   412 6   SO4 SO4 B . 
JA 7  GOL 1   401 408 GOL GOL C . 
KA 7  GOL 1   402 410 GOL GOL C . 
LA 8  EPE 1   403 412 EPE EPE C . 
MA 8  EPE 1   404 413 EPE EPE C . 
NA 8  EPE 1   405 414 EPE EPE C . 
OA 8  EPE 1   406 415 EPE EPE C . 
PA 8  EPE 1   407 416 EPE EPE C . 
QA 9  HEM 1   408 417 HEM HEM C . 
RA 10 MG  1   409 1   MG  MG  C . 
SA 11 SO4 1   410 7   SO4 SO4 C . 
TA 11 SO4 1   411 9   SO4 SO4 C . 
UA 12 HOH 1   501 143 HOH HOH A . 
UA 12 HOH 2   502 228 HOH HOH A . 
UA 12 HOH 3   503 141 HOH HOH A . 
UA 12 HOH 4   504 353 HOH HOH A . 
UA 12 HOH 5   505 191 HOH HOH A . 
UA 12 HOH 6   506 30  HOH HOH A . 
UA 12 HOH 7   507 181 HOH HOH A . 
UA 12 HOH 8   508 170 HOH HOH A . 
UA 12 HOH 9   509 358 HOH HOH A . 
UA 12 HOH 10  510 110 HOH HOH A . 
UA 12 HOH 11  511 343 HOH HOH A . 
UA 12 HOH 12  512 113 HOH HOH A . 
UA 12 HOH 13  513 79  HOH HOH A . 
UA 12 HOH 14  514 127 HOH HOH A . 
UA 12 HOH 15  515 180 HOH HOH A . 
UA 12 HOH 16  516 162 HOH HOH A . 
UA 12 HOH 17  517 281 HOH HOH A . 
UA 12 HOH 18  518 186 HOH HOH A . 
UA 12 HOH 19  519 242 HOH HOH A . 
UA 12 HOH 20  520 9   HOH HOH A . 
UA 12 HOH 21  521 35  HOH HOH A . 
UA 12 HOH 22  522 357 HOH HOH A . 
UA 12 HOH 23  523 183 HOH HOH A . 
UA 12 HOH 24  524 12  HOH HOH A . 
UA 12 HOH 25  525 76  HOH HOH A . 
UA 12 HOH 26  526 20  HOH HOH A . 
UA 12 HOH 27  527 259 HOH HOH A . 
UA 12 HOH 28  528 213 HOH HOH A . 
UA 12 HOH 29  529 132 HOH HOH A . 
UA 12 HOH 30  530 24  HOH HOH A . 
UA 12 HOH 31  531 72  HOH HOH A . 
UA 12 HOH 32  532 243 HOH HOH A . 
UA 12 HOH 33  533 134 HOH HOH A . 
UA 12 HOH 34  534 10  HOH HOH A . 
UA 12 HOH 35  535 247 HOH HOH A . 
UA 12 HOH 36  536 92  HOH HOH A . 
UA 12 HOH 37  537 3   HOH HOH A . 
UA 12 HOH 38  538 125 HOH HOH A . 
UA 12 HOH 39  539 211 HOH HOH A . 
UA 12 HOH 40  540 77  HOH HOH A . 
UA 12 HOH 41  541 64  HOH HOH A . 
UA 12 HOH 42  542 121 HOH HOH A . 
UA 12 HOH 43  543 47  HOH HOH A . 
UA 12 HOH 44  544 252 HOH HOH A . 
UA 12 HOH 45  545 96  HOH HOH A . 
UA 12 HOH 46  546 114 HOH HOH A . 
UA 12 HOH 47  547 246 HOH HOH A . 
UA 12 HOH 48  548 195 HOH HOH A . 
UA 12 HOH 49  549 102 HOH HOH A . 
UA 12 HOH 50  550 5   HOH HOH A . 
UA 12 HOH 51  551 236 HOH HOH A . 
UA 12 HOH 52  552 182 HOH HOH A . 
UA 12 HOH 53  553 50  HOH HOH A . 
UA 12 HOH 54  554 137 HOH HOH A . 
UA 12 HOH 55  555 215 HOH HOH A . 
UA 12 HOH 56  556 216 HOH HOH A . 
UA 12 HOH 57  557 131 HOH HOH A . 
UA 12 HOH 58  558 174 HOH HOH A . 
UA 12 HOH 59  559 351 HOH HOH A . 
UA 12 HOH 60  560 33  HOH HOH A . 
UA 12 HOH 61  561 52  HOH HOH A . 
UA 12 HOH 62  562 231 HOH HOH A . 
UA 12 HOH 63  563 328 HOH HOH A . 
UA 12 HOH 64  564 123 HOH HOH A . 
UA 12 HOH 65  565 178 HOH HOH A . 
UA 12 HOH 66  566 185 HOH HOH A . 
UA 12 HOH 67  567 187 HOH HOH A . 
UA 12 HOH 68  568 200 HOH HOH A . 
UA 12 HOH 69  569 271 HOH HOH A . 
UA 12 HOH 70  570 184 HOH HOH A . 
UA 12 HOH 71  571 327 HOH HOH A . 
UA 12 HOH 72  572 45  HOH HOH A . 
UA 12 HOH 73  573 41  HOH HOH A . 
UA 12 HOH 74  574 89  HOH HOH A . 
UA 12 HOH 75  575 229 HOH HOH A . 
UA 12 HOH 76  576 74  HOH HOH A . 
UA 12 HOH 77  577 21  HOH HOH A . 
UA 12 HOH 78  578 46  HOH HOH A . 
UA 12 HOH 79  579 139 HOH HOH A . 
UA 12 HOH 80  580 97  HOH HOH A . 
UA 12 HOH 81  581 208 HOH HOH A . 
UA 12 HOH 82  582 95  HOH HOH A . 
UA 12 HOH 83  583 245 HOH HOH A . 
UA 12 HOH 84  584 179 HOH HOH A . 
UA 12 HOH 85  585 83  HOH HOH A . 
UA 12 HOH 86  586 268 HOH HOH A . 
UA 12 HOH 87  587 238 HOH HOH A . 
UA 12 HOH 88  588 153 HOH HOH A . 
UA 12 HOH 89  589 218 HOH HOH A . 
UA 12 HOH 90  590 198 HOH HOH A . 
UA 12 HOH 91  591 133 HOH HOH A . 
UA 12 HOH 92  592 44  HOH HOH A . 
UA 12 HOH 93  593 189 HOH HOH A . 
UA 12 HOH 94  594 161 HOH HOH A . 
UA 12 HOH 95  595 333 HOH HOH A . 
UA 12 HOH 96  596 65  HOH HOH A . 
UA 12 HOH 97  597 227 HOH HOH A . 
UA 12 HOH 98  598 53  HOH HOH A . 
UA 12 HOH 99  599 34  HOH HOH A . 
UA 12 HOH 100 600 140 HOH HOH A . 
UA 12 HOH 101 601 164 HOH HOH A . 
UA 12 HOH 102 602 71  HOH HOH A . 
UA 12 HOH 103 603 58  HOH HOH A . 
UA 12 HOH 104 604 28  HOH HOH A . 
UA 12 HOH 105 605 23  HOH HOH A . 
UA 12 HOH 106 606 57  HOH HOH A . 
UA 12 HOH 107 607 244 HOH HOH A . 
UA 12 HOH 108 608 350 HOH HOH A . 
UA 12 HOH 109 609 8   HOH HOH A . 
UA 12 HOH 110 610 260 HOH HOH A . 
UA 12 HOH 111 611 341 HOH HOH A . 
UA 12 HOH 112 612 330 HOH HOH A . 
UA 12 HOH 113 613 230 HOH HOH A . 
UA 12 HOH 114 614 219 HOH HOH A . 
UA 12 HOH 115 615 155 HOH HOH A . 
UA 12 HOH 116 616 197 HOH HOH A . 
UA 12 HOH 117 617 135 HOH HOH A . 
UA 12 HOH 118 618 168 HOH HOH A . 
UA 12 HOH 119 619 54  HOH HOH A . 
UA 12 HOH 120 620 107 HOH HOH A . 
UA 12 HOH 121 621 373 HOH HOH A . 
UA 12 HOH 122 622 210 HOH HOH A . 
UA 12 HOH 123 623 339 HOH HOH A . 
UA 12 HOH 124 624 345 HOH HOH A . 
UA 12 HOH 125 625 207 HOH HOH A . 
UA 12 HOH 126 626 152 HOH HOH A . 
UA 12 HOH 127 627 262 HOH HOH A . 
UA 12 HOH 128 628 86  HOH HOH A . 
UA 12 HOH 129 629 156 HOH HOH A . 
UA 12 HOH 130 630 269 HOH HOH A . 
UA 12 HOH 131 631 237 HOH HOH A . 
UA 12 HOH 132 632 349 HOH HOH A . 
UA 12 HOH 133 633 160 HOH HOH A . 
UA 12 HOH 134 634 241 HOH HOH A . 
UA 12 HOH 135 635 196 HOH HOH A . 
UA 12 HOH 136 636 175 HOH HOH A . 
UA 12 HOH 137 637 154 HOH HOH A . 
UA 12 HOH 138 638 265 HOH HOH A . 
UA 12 HOH 139 639 251 HOH HOH A . 
UA 12 HOH 140 640 342 HOH HOH A . 
UA 12 HOH 141 641 340 HOH HOH A . 
UA 12 HOH 142 642 239 HOH HOH A . 
UA 12 HOH 143 643 149 HOH HOH A . 
UA 12 HOH 144 644 2   HOH HOH A . 
UA 12 HOH 145 645 165 HOH HOH A . 
UA 12 HOH 146 646 212 HOH HOH A . 
UA 12 HOH 147 647 177 HOH HOH A . 
UA 12 HOH 148 648 263 HOH HOH A . 
VA 12 HOH 1   501 62  HOH HOH B . 
VA 12 HOH 2   502 163 HOH HOH B . 
VA 12 HOH 3   503 294 HOH HOH B . 
VA 12 HOH 4   504 217 HOH HOH B . 
VA 12 HOH 5   505 368 HOH HOH B . 
VA 12 HOH 6   506 320 HOH HOH B . 
VA 12 HOH 7   507 119 HOH HOH B . 
VA 12 HOH 8   508 226 HOH HOH B . 
VA 12 HOH 9   509 305 HOH HOH B . 
VA 12 HOH 10  510 108 HOH HOH B . 
VA 12 HOH 11  511 347 HOH HOH B . 
VA 12 HOH 12  512 159 HOH HOH B . 
VA 12 HOH 13  513 75  HOH HOH B . 
VA 12 HOH 14  514 25  HOH HOH B . 
VA 12 HOH 15  515 292 HOH HOH B . 
VA 12 HOH 16  516 16  HOH HOH B . 
VA 12 HOH 17  517 190 HOH HOH B . 
VA 12 HOH 18  518 48  HOH HOH B . 
VA 12 HOH 19  519 272 HOH HOH B . 
VA 12 HOH 20  520 286 HOH HOH B . 
VA 12 HOH 21  521 367 HOH HOH B . 
VA 12 HOH 22  522 171 HOH HOH B . 
VA 12 HOH 23  523 145 HOH HOH B . 
VA 12 HOH 24  524 130 HOH HOH B . 
VA 12 HOH 25  525 129 HOH HOH B . 
VA 12 HOH 26  526 273 HOH HOH B . 
VA 12 HOH 27  527 55  HOH HOH B . 
VA 12 HOH 28  528 118 HOH HOH B . 
VA 12 HOH 29  529 37  HOH HOH B . 
VA 12 HOH 30  530 193 HOH HOH B . 
VA 12 HOH 31  531 63  HOH HOH B . 
VA 12 HOH 32  532 126 HOH HOH B . 
VA 12 HOH 33  533 98  HOH HOH B . 
VA 12 HOH 34  534 284 HOH HOH B . 
VA 12 HOH 35  535 296 HOH HOH B . 
VA 12 HOH 36  536 258 HOH HOH B . 
VA 12 HOH 37  537 199 HOH HOH B . 
VA 12 HOH 38  538 267 HOH HOH B . 
VA 12 HOH 39  539 253 HOH HOH B . 
VA 12 HOH 40  540 6   HOH HOH B . 
VA 12 HOH 41  541 117 HOH HOH B . 
VA 12 HOH 42  542 88  HOH HOH B . 
VA 12 HOH 43  543 49  HOH HOH B . 
VA 12 HOH 44  544 232 HOH HOH B . 
VA 12 HOH 45  545 371 HOH HOH B . 
VA 12 HOH 46  546 256 HOH HOH B . 
VA 12 HOH 47  547 80  HOH HOH B . 
VA 12 HOH 48  548 148 HOH HOH B . 
VA 12 HOH 49  549 18  HOH HOH B . 
VA 12 HOH 50  550 87  HOH HOH B . 
VA 12 HOH 51  551 254 HOH HOH B . 
VA 12 HOH 52  552 250 HOH HOH B . 
VA 12 HOH 53  553 369 HOH HOH B . 
VA 12 HOH 54  554 7   HOH HOH B . 
VA 12 HOH 55  555 106 HOH HOH B . 
VA 12 HOH 56  556 138 HOH HOH B . 
VA 12 HOH 57  557 100 HOH HOH B . 
VA 12 HOH 58  558 372 HOH HOH B . 
VA 12 HOH 59  559 38  HOH HOH B . 
VA 12 HOH 60  560 293 HOH HOH B . 
VA 12 HOH 61  561 115 HOH HOH B . 
VA 12 HOH 62  562 289 HOH HOH B . 
VA 12 HOH 63  563 84  HOH HOH B . 
VA 12 HOH 64  564 206 HOH HOH B . 
VA 12 HOH 65  565 105 HOH HOH B . 
VA 12 HOH 66  566 142 HOH HOH B . 
VA 12 HOH 67  567 67  HOH HOH B . 
VA 12 HOH 68  568 93  HOH HOH B . 
VA 12 HOH 69  569 94  HOH HOH B . 
VA 12 HOH 70  570 120 HOH HOH B . 
VA 12 HOH 71  571 297 HOH HOH B . 
VA 12 HOH 72  572 304 HOH HOH B . 
VA 12 HOH 73  573 31  HOH HOH B . 
VA 12 HOH 74  574 116 HOH HOH B . 
VA 12 HOH 75  575 285 HOH HOH B . 
VA 12 HOH 76  576 19  HOH HOH B . 
VA 12 HOH 77  577 144 HOH HOH B . 
VA 12 HOH 78  578 306 HOH HOH B . 
VA 12 HOH 79  579 172 HOH HOH B . 
VA 12 HOH 80  580 257 HOH HOH B . 
VA 12 HOH 81  581 248 HOH HOH B . 
VA 12 HOH 82  582 40  HOH HOH B . 
VA 12 HOH 83  583 205 HOH HOH B . 
VA 12 HOH 84  584 147 HOH HOH B . 
VA 12 HOH 85  585 365 HOH HOH B . 
VA 12 HOH 86  586 303 HOH HOH B . 
VA 12 HOH 87  587 26  HOH HOH B . 
VA 12 HOH 88  588 101 HOH HOH B . 
VA 12 HOH 89  589 348 HOH HOH B . 
VA 12 HOH 90  590 68  HOH HOH B . 
VA 12 HOH 91  591 14  HOH HOH B . 
VA 12 HOH 92  592 90  HOH HOH B . 
VA 12 HOH 93  593 337 HOH HOH B . 
VA 12 HOH 94  594 275 HOH HOH B . 
VA 12 HOH 95  595 309 HOH HOH B . 
VA 12 HOH 96  596 233 HOH HOH B . 
VA 12 HOH 97  597 300 HOH HOH B . 
VA 12 HOH 98  598 1   HOH HOH B . 
VA 12 HOH 99  599 336 HOH HOH B . 
VA 12 HOH 100 600 60  HOH HOH B . 
VA 12 HOH 101 601 32  HOH HOH B . 
VA 12 HOH 102 602 311 HOH HOH B . 
VA 12 HOH 103 603 124 HOH HOH B . 
VA 12 HOH 104 604 363 HOH HOH B . 
VA 12 HOH 105 605 234 HOH HOH B . 
VA 12 HOH 106 606 157 HOH HOH B . 
VA 12 HOH 107 607 338 HOH HOH B . 
VA 12 HOH 108 608 176 HOH HOH B . 
VA 12 HOH 109 609 308 HOH HOH B . 
VA 12 HOH 110 610 276 HOH HOH B . 
VA 12 HOH 111 611 299 HOH HOH B . 
VA 12 HOH 112 612 298 HOH HOH B . 
VA 12 HOH 113 613 282 HOH HOH B . 
VA 12 HOH 114 614 331 HOH HOH B . 
VA 12 HOH 115 615 354 HOH HOH B . 
VA 12 HOH 116 616 355 HOH HOH B . 
VA 12 HOH 117 617 291 HOH HOH B . 
VA 12 HOH 118 618 188 HOH HOH B . 
VA 12 HOH 119 619 99  HOH HOH B . 
VA 12 HOH 120 620 356 HOH HOH B . 
VA 12 HOH 121 621 395 HOH HOH B . 
VA 12 HOH 122 622 362 HOH HOH B . 
VA 12 HOH 123 623 375 HOH HOH B . 
VA 12 HOH 124 624 364 HOH HOH B . 
VA 12 HOH 125 625 151 HOH HOH B . 
VA 12 HOH 126 626 374 HOH HOH B . 
VA 12 HOH 127 627 310 HOH HOH B . 
VA 12 HOH 128 628 204 HOH HOH B . 
VA 12 HOH 129 629 283 HOH HOH B . 
VA 12 HOH 130 630 389 HOH HOH B . 
VA 12 HOH 131 631 290 HOH HOH B . 
VA 12 HOH 132 632 366 HOH HOH B . 
VA 12 HOH 133 633 280 HOH HOH B . 
VA 12 HOH 134 634 370 HOH HOH B . 
VA 12 HOH 135 635 307 HOH HOH B . 
VA 12 HOH 136 636 150 HOH HOH B . 
VA 12 HOH 137 637 346 HOH HOH B . 
VA 12 HOH 138 638 288 HOH HOH B . 
VA 12 HOH 139 639 344 HOH HOH B . 
VA 12 HOH 140 640 264 HOH HOH B . 
VA 12 HOH 141 641 235 HOH HOH B . 
VA 12 HOH 142 642 301 HOH HOH B . 
VA 12 HOH 143 643 302 HOH HOH B . 
VA 12 HOH 144 644 81  HOH HOH B . 
VA 12 HOH 145 645 287 HOH HOH B . 
VA 12 HOH 146 646 249 HOH HOH B . 
VA 12 HOH 147 647 295 HOH HOH B . 
WA 12 HOH 1   501 112 HOH HOH C . 
WA 12 HOH 2   502 321 HOH HOH C . 
WA 12 HOH 3   503 382 HOH HOH C . 
WA 12 HOH 4   504 255 HOH HOH C . 
WA 12 HOH 5   505 319 HOH HOH C . 
WA 12 HOH 6   506 42  HOH HOH C . 
WA 12 HOH 7   507 352 HOH HOH C . 
WA 12 HOH 8   508 225 HOH HOH C . 
WA 12 HOH 9   509 22  HOH HOH C . 
WA 12 HOH 10  510 169 HOH HOH C . 
WA 12 HOH 11  511 109 HOH HOH C . 
WA 12 HOH 12  512 70  HOH HOH C . 
WA 12 HOH 13  513 4   HOH HOH C . 
WA 12 HOH 14  514 111 HOH HOH C . 
WA 12 HOH 15  515 122 HOH HOH C . 
WA 12 HOH 16  516 56  HOH HOH C . 
WA 12 HOH 17  517 91  HOH HOH C . 
WA 12 HOH 18  518 194 HOH HOH C . 
WA 12 HOH 19  519 82  HOH HOH C . 
WA 12 HOH 20  520 73  HOH HOH C . 
WA 12 HOH 21  521 279 HOH HOH C . 
WA 12 HOH 22  522 43  HOH HOH C . 
WA 12 HOH 23  523 36  HOH HOH C . 
WA 12 HOH 24  524 223 HOH HOH C . 
WA 12 HOH 25  525 203 HOH HOH C . 
WA 12 HOH 26  526 11  HOH HOH C . 
WA 12 HOH 27  527 27  HOH HOH C . 
WA 12 HOH 28  528 222 HOH HOH C . 
WA 12 HOH 29  529 61  HOH HOH C . 
WA 12 HOH 30  530 261 HOH HOH C . 
WA 12 HOH 31  531 173 HOH HOH C . 
WA 12 HOH 32  532 78  HOH HOH C . 
WA 12 HOH 33  533 128 HOH HOH C . 
WA 12 HOH 34  534 386 HOH HOH C . 
WA 12 HOH 35  535 325 HOH HOH C . 
WA 12 HOH 36  536 332 HOH HOH C . 
WA 12 HOH 37  537 317 HOH HOH C . 
WA 12 HOH 38  538 214 HOH HOH C . 
WA 12 HOH 39  539 103 HOH HOH C . 
WA 12 HOH 40  540 329 HOH HOH C . 
WA 12 HOH 41  541 224 HOH HOH C . 
WA 12 HOH 42  542 104 HOH HOH C . 
WA 12 HOH 43  543 59  HOH HOH C . 
WA 12 HOH 44  544 39  HOH HOH C . 
WA 12 HOH 45  545 146 HOH HOH C . 
WA 12 HOH 46  546 380 HOH HOH C . 
WA 12 HOH 47  547 361 HOH HOH C . 
WA 12 HOH 48  548 387 HOH HOH C . 
WA 12 HOH 49  549 69  HOH HOH C . 
WA 12 HOH 50  550 278 HOH HOH C . 
WA 12 HOH 51  551 66  HOH HOH C . 
WA 12 HOH 52  552 391 HOH HOH C . 
WA 12 HOH 53  553 29  HOH HOH C . 
WA 12 HOH 54  554 274 HOH HOH C . 
WA 12 HOH 55  555 314 HOH HOH C . 
WA 12 HOH 56  556 277 HOH HOH C . 
WA 12 HOH 57  557 15  HOH HOH C . 
WA 12 HOH 58  558 394 HOH HOH C . 
WA 12 HOH 59  559 136 HOH HOH C . 
WA 12 HOH 60  560 51  HOH HOH C . 
WA 12 HOH 61  561 221 HOH HOH C . 
WA 12 HOH 62  562 379 HOH HOH C . 
WA 12 HOH 63  563 318 HOH HOH C . 
WA 12 HOH 64  564 378 HOH HOH C . 
WA 12 HOH 65  565 392 HOH HOH C . 
WA 12 HOH 66  566 17  HOH HOH C . 
WA 12 HOH 67  567 322 HOH HOH C . 
WA 12 HOH 68  568 324 HOH HOH C . 
WA 12 HOH 69  569 240 HOH HOH C . 
WA 12 HOH 70  570 384 HOH HOH C . 
WA 12 HOH 71  571 360 HOH HOH C . 
WA 12 HOH 72  572 334 HOH HOH C . 
WA 12 HOH 73  573 220 HOH HOH C . 
WA 12 HOH 74  574 166 HOH HOH C . 
WA 12 HOH 75  575 201 HOH HOH C . 
WA 12 HOH 76  576 312 HOH HOH C . 
WA 12 HOH 77  577 393 HOH HOH C . 
WA 12 HOH 78  578 158 HOH HOH C . 
WA 12 HOH 79  579 376 HOH HOH C . 
WA 12 HOH 80  580 85  HOH HOH C . 
WA 12 HOH 81  581 359 HOH HOH C . 
WA 12 HOH 82  582 316 HOH HOH C . 
WA 12 HOH 83  583 167 HOH HOH C . 
WA 12 HOH 84  584 388 HOH HOH C . 
WA 12 HOH 85  585 13  HOH HOH C . 
WA 12 HOH 86  586 315 HOH HOH C . 
WA 12 HOH 87  587 192 HOH HOH C . 
WA 12 HOH 88  588 326 HOH HOH C . 
WA 12 HOH 89  589 381 HOH HOH C . 
WA 12 HOH 90  590 313 HOH HOH C . 
WA 12 HOH 91  591 383 HOH HOH C . 
WA 12 HOH 92  592 270 HOH HOH C . 
WA 12 HOH 93  593 390 HOH HOH C . 
WA 12 HOH 94  594 335 HOH HOH C . 
WA 12 HOH 95  595 385 HOH HOH C . 
WA 12 HOH 96  596 202 HOH HOH C . 
WA 12 HOH 97  597 209 HOH HOH C . 
WA 12 HOH 98  598 323 HOH HOH C . 
WA 12 HOH 99  599 377 HOH HOH C . 
WA 12 HOH 100 600 266 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                   111.61 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HE6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     272.859 
_cell.length_a_esd                 ? 
_cell.length_b                     74.840 
_cell.length_b_esd                 ? 
_cell.length_c                     105.579 
_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                         9HE6 
_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                   9HE6 
_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             4.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.19 
_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, HANGING 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    
;2M ammonium sulphate, 100 mM HEPES pH 7.5

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         2021-03-05 
_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                                       9HE6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               49.08 
_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                                     88037 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_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                                0.088 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.077 
_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                                    2.30 
_reflns_shell.d_res_low                                     2.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4524 
_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                               4.7 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.792 
_reflns_shell.pdbx_Rpim_I_all                               0.367 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.699 
_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]                            -2.55 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.73 
_refine.aniso_B[2][2]                            3.45 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.13 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               46.727 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_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                                 9HE6 
_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                            2.30 
_refine.ls_d_res_low                             48.43 
_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                     83573 
_refine.ls_number_reflns_R_free                  4443 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19500 
_refine.ls_R_factor_R_free                       0.22169 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19359 
_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                       0.197 
_refine.pdbx_overall_ESU_R_Free                  0.170 
_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                             6.482 
_refine.overall_SU_ML                            0.149 
_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                       2.30 
_refine_hist.d_res_low                        48.43 
_refine_hist.number_atoms_solvent             395 
_refine_hist.number_atoms_total               8908 
_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        8470 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_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' ? 0.007  0.012  8866  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7767  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.349  1.843  12205 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.484  1.738  18009 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.164  5.000  1028  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.128  5.000  50    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.692 10.000 1111  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.066  0.200  1344  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  10268 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2054  ? 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' ? 3.052  4.611  4043  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.050  4.611  4043  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.351  8.304  5055  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.351  8.304  5056  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.401  5.281  4823  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.109  5.266  4792  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.023  9.522  7090  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.136  45.61  9615  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.135  45.57  9555  ? 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                       2.300 
_refine_ls_shell.d_res_low                        2.360 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             335 
_refine_ls_shell.number_reflns_R_work             6161 
_refine_ls_shell.percent_reflns_obs               99.69 
_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                  0.289 
_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                  0.324 
# 
_struct.entry_id                     9HE6 
_struct.title                        'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II)' 
_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        9HE6 
_struct_keywords.text            'Peroxygenase, peroxidase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 1  ? 
D  N N 2  ? 
E  N N 3  ? 
F  N N 4  ? 
G  N N 5  ? 
H  N N 6  ? 
I  N N 4  ? 
J  N N 7  ? 
K  N N 7  ? 
L  N N 7  ? 
M  N N 8  ? 
N  N N 8  ? 
O  N N 8  ? 
P  N N 7  ? 
Q  N N 8  ? 
R  N N 9  ? 
S  N N 10 ? 
T  N N 11 ? 
U  N N 11 ? 
V  N N 11 ? 
W  N N 11 ? 
X  N N 7  ? 
Y  N N 7  ? 
Z  N N 7  ? 
AA N N 8  ? 
BA N N 8  ? 
CA N N 7  ? 
DA N N 8  ? 
EA N N 7  ? 
FA N N 9  ? 
GA N N 10 ? 
HA N N 11 ? 
IA N N 11 ? 
JA N N 7  ? 
KA N N 7  ? 
LA N N 8  ? 
MA N N 8  ? 
NA N N 8  ? 
OA N N 8  ? 
PA N N 8  ? 
QA N N 9  ? 
RA N N 10 ? 
SA N N 11 ? 
TA N N 11 ? 
UA N N 12 ? 
VA N N 12 ? 
WA N N 12 ? 
# 
_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 9HE6 A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HE6 B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HE6 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,T,U,V,W,UA      
2 1 B,F,G,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,VA 
3 1 C,H,I,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,WA 
# 
_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 ASN A 190 ? LEU A 206 ? ASN A 203 LEU A 219 1 ? 17 
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 ASN B 190 ? LEU B 206 ? ASN B 203 LEU B 219 1 ? 17 
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 GLY B 302 ? PHE B 323 ? GLY B 315 PHE B 336 1 ? 22 
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 ? LEU C 206 ? LYS C 202 LEU C 219 1 ? 18 
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 ? ? ? ? ? ? ? 2.105 ? ? 
disulf2  disulf ?    ? B  CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf3  disulf ?    ? C  CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
covale1  covale one  ? A  ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 G NAG 1   1_555 ? ? ? ? ? ? ? 1.457 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 I NAG 1   1_555 ? ? ? ? ? ? ? 1.505 ? 
N-Glycosylation 
covale3  covale one  ? B  ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 b NAG 1   1_555 ? ? ? ? ? ? ? 1.431 ? 
N-Glycosylation 
covale4  covale one  ? B  ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 c NAG 1   1_555 ? ? ? ? ? ? ? 1.443 ? 
N-Glycosylation 
covale5  covale one  ? C  ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 s NAG 1   1_555 ? ? ? ? ? ? ? 1.448 ? 
N-Glycosylation 
covale6  covale one  ? C  ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 t NAG 1   1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale7  covale both ? D  NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale8  covale both ? D  NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale9  covale both ? D  BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 4   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale10 covale both ? D  BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 5   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale11 covale both ? E  NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale12 covale both ? E  NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? I NAG 2   I BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale13 covale both ? E  BMA .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 4   1_555 ? ? ? ? ? ? ? 1.408 ? ? 
covale14 covale both ? E  BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 7   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale15 covale both ? E  MAN .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 5   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale16 covale both ? E  MAN .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 6   1_555 ? ? ? ? ? ? ? 1.405 ? ? 
covale17 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? b NAG 1   b NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale18 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? c NAG 1   c NAG 2   1_555 ? ? ? ? ? ? ? 1.391 ? ? 
covale19 covale both ? G  NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? c NAG 2   c BMA 3   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale20 covale both ? G  BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? c BMA 3   c MAN 4   1_555 ? ? ? ? ? ? ? 1.412 ? ? 
covale21 covale both ? G  BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? c BMA 3   c MAN 6   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale22 covale both ? G  MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? c MAN 4   c MAN 5   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale23 covale both ? H  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? s NAG 1   s NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale24 covale both ? H  NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? s NAG 2   s BMA 3   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale25 covale both ? H  BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? s BMA 3   s MAN 4   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale26 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? t NAG 1   t NAG 2   1_555 ? ? ? ? ? ? ? 1.403 ? ? 
metalc1  metalc ?    ? A  CYS 39  SG  ? ? ? 1_555 R  HEM .   FE ? ? A CYS 52  A HEM 409 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc2  metalc ?    ? A  GLU 125 OE2 ? ? ? 1_555 S  MG  .   MG ? ? A GLU 138 A MG  410 1_555 ? ? ? ? ? ? ? 2.274 ? ? 
metalc3  metalc ?    ? A  GLY 126 O   ? ? ? 1_555 S  MG  .   MG ? ? A GLY 139 A MG  410 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc4  metalc ?    ? R  HEM .   O1A ? ? ? 1_555 S  MG  .   MG ? ? A HEM 409 A MG  410 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc5  metalc ?    ? R  HEM .   O2A ? ? ? 1_555 S  MG  .   MG ? ? A HEM 409 A MG  410 1_555 ? ? ? ? ? ? ? 2.986 ? ? 
metalc6  metalc ?    ? S  MG  .   MG  ? ? ? 1_555 UA HOH .   O  ? ? A MG  410 A HOH 518 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc7  metalc ?    ? S  MG  .   MG  ? ? ? 1_555 UA HOH .   O  ? ? A MG  410 A HOH 567 1_555 ? ? ? ? ? ? ? 2.376 ? ? 
metalc8  metalc ?    ? B  CYS 39  SG  ? ? ? 1_555 FA HEM .   FE ? ? B CYS 52  B HEM 409 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc9  metalc ?    ? B  GLU 125 OE2 ? ? ? 1_555 GA MG  .   MG ? ? B GLU 138 B MG  410 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc10 metalc ?    ? B  GLY 126 O   ? ? ? 1_555 GA MG  .   MG ? ? B GLY 139 B MG  410 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc11 metalc ?    ? FA HEM .   O1A ? ? ? 1_555 GA MG  .   MG ? ? B HEM 409 B MG  410 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc12 metalc ?    ? GA MG  .   MG  ? ? ? 1_555 VA HOH .   O  ? ? B MG  410 B HOH 505 1_555 ? ? ? ? ? ? ? 1.935 ? ? 
metalc13 metalc ?    ? C  CYS 39  SG  ? ? ? 1_555 QA HEM .   FE ? ? C CYS 52  C HEM 408 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc14 metalc ?    ? C  GLU 125 OE2 ? ? ? 1_555 RA MG  .   MG ? ? C GLU 138 C MG  409 1_555 ? ? ? ? ? ? ? 2.713 ? ? 
metalc15 metalc ?    ? C  GLY 126 O   ? ? ? 1_555 RA MG  .   MG ? ? C GLY 139 C MG  409 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc16 metalc ?    ? QA HEM .   O1A ? ? ? 1_555 RA MG  .   MG ? ? C HEM 408 C MG  409 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc17 metalc ?    ? QA HEM .   O2A ? ? ? 1_555 RA MG  .   MG ? ? C HEM 408 C MG  409 1_555 ? ? ? ? ? ? ? 2.901 ? ? 
metalc18 metalc ?    ? RA MG  .   MG  ? ? ? 1_555 WA HOH .   O  ? ? C MG  409 C HOH 508 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
metalc19 metalc ?    ? RA MG  .   MG  ? ? ? 1_555 WA HOH .   O  ? ? C MG  409 C HOH 524 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
# 
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 ? R  HEM . ? A HEM 409 ? 1_555 NA  ? R  HEM .   ? A HEM 409 ? 1_555 102.4 ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 NB  ? R  HEM .   ? A HEM 409 ? 1_555 90.2  ? 
3  NA  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 NB  ? R  HEM .   ? A HEM 409 ? 1_555 87.8  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 NC  ? R  HEM .   ? A HEM 409 ? 1_555 87.8  ? 
5  NA  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 NC  ? R  HEM .   ? A HEM 409 ? 1_555 168.5 ? 
6  NB  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 NC  ? R  HEM .   ? A HEM 409 ? 1_555 86.8  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 ND  ? R  HEM .   ? A HEM 409 ? 1_555 97.0  ? 
8  NA  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 ND  ? R  HEM .   ? A HEM 409 ? 1_555 92.6  ? 
9  NB  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 ND  ? R  HEM .   ? A HEM 409 ? 1_555 172.6 ? 
10 NC  ? R  HEM .   ? A HEM 409 ? 1_555 FE ? R  HEM . ? A HEM 409 ? 1_555 ND  ? R  HEM .   ? A HEM 409 ? 1_555 91.5  ? 
11 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 70.8  ? 
12 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O1A ? R  HEM .   ? A HEM 409 ? 1_555 79.4  ? 
13 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O1A ? R  HEM .   ? A HEM 409 ? 1_555 90.3  ? 
14 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O2A ? R  HEM .   ? A HEM 409 ? 1_555 127.0 ? 
15 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O2A ? R  HEM .   ? A HEM 409 ? 1_555 116.1 ? 
16 O1A ? R  HEM .   ? A HEM 409 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O2A ? R  HEM .   ? A HEM 409 ? 1_555 49.5  ? 
17 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 518 ? 1_555 72.7  ? 
18 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 518 ? 1_555 143.4 ? 
19 O1A ? R  HEM .   ? A HEM 409 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 518 ? 1_555 84.7  ? 
20 O2A ? R  HEM .   ? A HEM 409 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 518 ? 1_555 87.5  ? 
21 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 567 ? 1_555 77.0  ? 
22 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 567 ? 1_555 83.4  ? 
23 O1A ? R  HEM .   ? A HEM 409 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 567 ? 1_555 156.3 ? 
24 O2A ? R  HEM .   ? A HEM 409 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 567 ? 1_555 152.0 ? 
25 O   ? UA HOH .   ? A HOH 518 ? 1_555 MG ? S  MG  . ? A MG  410 ? 1_555 O   ? UA HOH .   ? A HOH 567 ? 1_555 86.8  ? 
26 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NA  ? FA HEM .   ? B HEM 409 ? 1_555 101.2 ? 
27 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NB  ? FA HEM .   ? B HEM 409 ? 1_555 90.4  ? 
28 NA  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NB  ? FA HEM .   ? B HEM 409 ? 1_555 88.3  ? 
29 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NC  ? FA HEM .   ? B HEM 409 ? 1_555 88.0  ? 
30 NA  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NC  ? FA HEM .   ? B HEM 409 ? 1_555 170.2 ? 
31 NB  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 NC  ? FA HEM .   ? B HEM 409 ? 1_555 88.1  ? 
32 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 ND  ? FA HEM .   ? B HEM 409 ? 1_555 96.3  ? 
33 NA  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 ND  ? FA HEM .   ? B HEM 409 ? 1_555 90.9  ? 
34 NB  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 ND  ? FA HEM .   ? B HEM 409 ? 1_555 173.3 ? 
35 NC  ? FA HEM .   ? B HEM 409 ? 1_555 FE ? FA HEM . ? B HEM 409 ? 1_555 ND  ? FA HEM .   ? B HEM 409 ? 1_555 91.7  ? 
36 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 78.2  ? 
37 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O1A ? FA HEM .   ? B HEM 409 ? 1_555 92.9  ? 
38 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O1A ? FA HEM .   ? B HEM 409 ? 1_555 95.6  ? 
39 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O   ? VA HOH .   ? B HOH 505 ? 1_555 75.8  ? 
40 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O   ? VA HOH .   ? B HOH 505 ? 1_555 153.7 ? 
41 O1A ? FA HEM .   ? B HEM 409 ? 1_555 MG ? GA MG  . ? B MG  410 ? 1_555 O   ? VA HOH .   ? B HOH 505 ? 1_555 89.6  ? 
42 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NA  ? QA HEM .   ? C HEM 408 ? 1_555 99.9  ? 
43 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NB  ? QA HEM .   ? C HEM 408 ? 1_555 87.5  ? 
44 NA  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NB  ? QA HEM .   ? C HEM 408 ? 1_555 86.6  ? 
45 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NC  ? QA HEM .   ? C HEM 408 ? 1_555 86.8  ? 
46 NA  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NC  ? QA HEM .   ? C HEM 408 ? 1_555 170.8 ? 
47 NB  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 NC  ? QA HEM .   ? C HEM 408 ? 1_555 87.3  ? 
48 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 ND  ? QA HEM .   ? C HEM 408 ? 1_555 97.2  ? 
49 NA  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 ND  ? QA HEM .   ? C HEM 408 ? 1_555 94.3  ? 
50 NB  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 ND  ? QA HEM .   ? C HEM 408 ? 1_555 175.0 ? 
51 NC  ? QA HEM .   ? C HEM 408 ? 1_555 FE ? QA HEM . ? C HEM 408 ? 1_555 ND  ? QA HEM .   ? C HEM 408 ? 1_555 91.2  ? 
52 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 62.2  ? 
53 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O1A ? QA HEM .   ? C HEM 408 ? 1_555 67.1  ? 
54 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O1A ? QA HEM .   ? C HEM 408 ? 1_555 76.6  ? 
55 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O2A ? QA HEM .   ? C HEM 408 ? 1_555 112.4 ? 
56 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O2A ? QA HEM .   ? C HEM 408 ? 1_555 113.4 ? 
57 O1A ? QA HEM .   ? C HEM 408 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O2A ? QA HEM .   ? C HEM 408 ? 1_555 49.0  ? 
58 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 508 ? 1_555 61.3  ? 
59 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 508 ? 1_555 123.5 ? 
60 O1A ? QA HEM .   ? C HEM 408 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 508 ? 1_555 81.9  ? 
61 O2A ? QA HEM .   ? C HEM 408 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 508 ? 1_555 87.8  ? 
62 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 524 ? 1_555 67.0  ? 
63 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 524 ? 1_555 81.5  ? 
64 O1A ? QA HEM .   ? C HEM 408 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 524 ? 1_555 134.1 ? 
65 O2A ? QA HEM .   ? C HEM 408 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 524 ? 1_555 163.4 ? 
66 O   ? WA HOH .   ? C HOH 508 ? 1_555 MG ? RA MG  . ? C MG  409 ? 1_555 O   ? WA HOH .   ? C HOH 524 ? 1_555 77.4  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG D .   ? ASN A 144 ? NAG G 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG I 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG b 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG c 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG s 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG t 1   ? 1_555 ASN C 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 283 ? CYS A 326 ? CYS A 296 ? 1_555 CYS A 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 283 ? CYS B 326 ? CYS B 296 ? 1_555 CYS B 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS C 283 ? CYS C 326 ? CYS C 296 ? 1_555 CYS C 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 111 A . ? PRO 124 A PRO 112 A ? PRO 125 A 1 7.96 
2 PRO 111 B . ? PRO 124 B PRO 112 B ? PRO 125 B 1 2.71 
3 PRO 111 C . ? PRO 124 C PRO 112 C ? PRO 125 C 1 3.30 
# 
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                   9HE6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 623 ? ? O A HOH 641 ? ? 2.01 
2 1 O B HOH 593 ? ? O B HOH 599 ? ? 2.12 
3 1 O C HOH 572 ? ? O C HOH 594 ? ? 2.15 
# 
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 PHE A 137 ? ? -101.14 -79.35  
2  1 ASN A 203 ? ? 53.51   -122.70 
3  1 SER A 257 ? ? -153.77 -109.95 
4  1 ASN A 282 ? ? -141.67 53.59   
5  1 HIS B 127 ? ? -138.06 -30.97  
6  1 PHE B 137 ? ? -100.73 -80.10  
7  1 ASN B 203 ? ? 54.08   -122.31 
8  1 SER B 257 ? ? -154.30 -107.88 
9  1 ASN B 282 ? ? -140.86 54.00   
10 1 PHE C 137 ? ? -105.84 -81.13  
11 1 ASN C 203 ? ? 52.32   -121.69 
12 1 PRO C 246 ? ? -49.87  151.62  
13 1 SER C 257 ? ? -148.42 -109.86 
14 1 ASN C 282 ? ? -140.73 53.79   
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       600 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   . 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          7.58 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BMA C1   C  N R 74  
BMA C2   C  N S 75  
BMA C3   C  N S 76  
BMA C4   C  N S 77  
BMA C5   C  N R 78  
BMA C6   C  N N 79  
BMA O1   O  N N 80  
BMA O2   O  N N 81  
BMA O3   O  N N 82  
BMA O4   O  N N 83  
BMA O5   O  N N 84  
BMA O6   O  N N 85  
BMA H1   H  N N 86  
BMA H2   H  N N 87  
BMA H3   H  N N 88  
BMA H4   H  N N 89  
BMA H5   H  N N 90  
BMA H61  H  N N 91  
BMA H62  H  N N 92  
BMA HO1  H  N N 93  
BMA HO2  H  N N 94  
BMA HO3  H  N N 95  
BMA HO4  H  N N 96  
BMA HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
EPE N1   N  N N 112 
EPE C2   C  N N 113 
EPE C3   C  N N 114 
EPE N4   N  N N 115 
EPE C5   C  N N 116 
EPE C6   C  N N 117 
EPE C7   C  N N 118 
EPE C8   C  N N 119 
EPE O8   O  N N 120 
EPE C9   C  N N 121 
EPE C10  C  N N 122 
EPE S    S  N N 123 
EPE O1S  O  N N 124 
EPE O2S  O  N N 125 
EPE O3S  O  N N 126 
EPE H21  H  N N 127 
EPE H22  H  N N 128 
EPE H31  H  N N 129 
EPE H32  H  N N 130 
EPE H51  H  N N 131 
EPE H52  H  N N 132 
EPE H61  H  N N 133 
EPE H62  H  N N 134 
EPE H71  H  N N 135 
EPE H72  H  N N 136 
EPE H81  H  N N 137 
EPE H82  H  N N 138 
EPE HO8  H  N N 139 
EPE H91  H  N N 140 
EPE H92  H  N N 141 
EPE H101 H  N N 142 
EPE H102 H  N N 143 
EPE HOS3 H  N N 144 
GLN N    N  N N 145 
GLN CA   C  N S 146 
GLN C    C  N N 147 
GLN O    O  N N 148 
GLN CB   C  N N 149 
GLN CG   C  N N 150 
GLN CD   C  N N 151 
GLN OE1  O  N N 152 
GLN NE2  N  N N 153 
GLN OXT  O  N N 154 
GLN H    H  N N 155 
GLN H2   H  N N 156 
GLN HA   H  N N 157 
GLN HB2  H  N N 158 
GLN HB3  H  N N 159 
GLN HG2  H  N N 160 
GLN HG3  H  N N 161 
GLN HE21 H  N N 162 
GLN HE22 H  N N 163 
GLN HXT  H  N N 164 
GLU N    N  N N 165 
GLU CA   C  N S 166 
GLU C    C  N N 167 
GLU O    O  N N 168 
GLU CB   C  N N 169 
GLU CG   C  N N 170 
GLU CD   C  N N 171 
GLU OE1  O  N N 172 
GLU OE2  O  N N 173 
GLU OXT  O  N N 174 
GLU H    H  N N 175 
GLU H2   H  N N 176 
GLU HA   H  N N 177 
GLU HB2  H  N N 178 
GLU HB3  H  N N 179 
GLU HG2  H  N N 180 
GLU HG3  H  N N 181 
GLU HE2  H  N N 182 
GLU HXT  H  N N 183 
GLY N    N  N N 184 
GLY CA   C  N N 185 
GLY C    C  N N 186 
GLY O    O  N N 187 
GLY OXT  O  N N 188 
GLY H    H  N N 189 
GLY H2   H  N N 190 
GLY HA2  H  N N 191 
GLY HA3  H  N N 192 
GLY HXT  H  N N 193 
GOL C1   C  N N 194 
GOL O1   O  N N 195 
GOL C2   C  N N 196 
GOL O2   O  N N 197 
GOL C3   C  N N 198 
GOL O3   O  N N 199 
GOL H11  H  N N 200 
GOL H12  H  N N 201 
GOL HO1  H  N N 202 
GOL H2   H  N N 203 
GOL HO2  H  N N 204 
GOL H31  H  N N 205 
GOL H32  H  N N 206 
GOL HO3  H  N N 207 
HEM CHA  C  N N 208 
HEM CHB  C  N N 209 
HEM CHC  C  N N 210 
HEM CHD  C  N N 211 
HEM C1A  C  Y N 212 
HEM C2A  C  Y N 213 
HEM C3A  C  Y N 214 
HEM C4A  C  Y N 215 
HEM CMA  C  N N 216 
HEM CAA  C  N N 217 
HEM CBA  C  N N 218 
HEM CGA  C  N N 219 
HEM O1A  O  N N 220 
HEM O2A  O  N N 221 
HEM C1B  C  N N 222 
HEM C2B  C  N N 223 
HEM C3B  C  N N 224 
HEM C4B  C  N N 225 
HEM CMB  C  N N 226 
HEM CAB  C  N N 227 
HEM CBB  C  N N 228 
HEM C1C  C  Y N 229 
HEM C2C  C  Y N 230 
HEM C3C  C  Y N 231 
HEM C4C  C  Y N 232 
HEM CMC  C  N N 233 
HEM CAC  C  N N 234 
HEM CBC  C  N N 235 
HEM C1D  C  N N 236 
HEM C2D  C  N N 237 
HEM C3D  C  N N 238 
HEM C4D  C  N N 239 
HEM CMD  C  N N 240 
HEM CAD  C  N N 241 
HEM CBD  C  N N 242 
HEM CGD  C  N N 243 
HEM O1D  O  N N 244 
HEM O2D  O  N N 245 
HEM NA   N  Y N 246 
HEM NB   N  N N 247 
HEM NC   N  Y N 248 
HEM ND   N  N N 249 
HEM FE   FE N N 250 
HEM HHB  H  N N 251 
HEM HHC  H  N N 252 
HEM HHD  H  N N 253 
HEM HMA  H  N N 254 
HEM HMAA H  N N 255 
HEM HMAB H  N N 256 
HEM HAA  H  N N 257 
HEM HAAA H  N N 258 
HEM HBA  H  N N 259 
HEM HBAA H  N N 260 
HEM HMB  H  N N 261 
HEM HMBA H  N N 262 
HEM HMBB H  N N 263 
HEM HAB  H  N N 264 
HEM HBB  H  N N 265 
HEM HBBA H  N N 266 
HEM HMC  H  N N 267 
HEM HMCA H  N N 268 
HEM HMCB H  N N 269 
HEM HAC  H  N N 270 
HEM HBC  H  N N 271 
HEM HBCA H  N N 272 
HEM HMD  H  N N 273 
HEM HMDA H  N N 274 
HEM HMDB H  N N 275 
HEM HAD  H  N N 276 
HEM HADA H  N N 277 
HEM HBD  H  N N 278 
HEM HBDA H  N N 279 
HEM H2A  H  N N 280 
HEM H2D  H  N N 281 
HEM HHA  H  N N 282 
HIS N    N  N N 283 
HIS CA   C  N S 284 
HIS C    C  N N 285 
HIS O    O  N N 286 
HIS CB   C  N N 287 
HIS CG   C  Y N 288 
HIS ND1  N  Y N 289 
HIS CD2  C  Y N 290 
HIS CE1  C  Y N 291 
HIS NE2  N  Y N 292 
HIS OXT  O  N N 293 
HIS H    H  N N 294 
HIS H2   H  N N 295 
HIS HA   H  N N 296 
HIS HB2  H  N N 297 
HIS HB3  H  N N 298 
HIS HD1  H  N N 299 
HIS HD2  H  N N 300 
HIS HE1  H  N N 301 
HIS HE2  H  N N 302 
HIS HXT  H  N N 303 
HOH O    O  N N 304 
HOH H1   H  N N 305 
HOH H2   H  N N 306 
ILE N    N  N N 307 
ILE CA   C  N S 308 
ILE C    C  N N 309 
ILE O    O  N N 310 
ILE CB   C  N S 311 
ILE CG1  C  N N 312 
ILE CG2  C  N N 313 
ILE CD1  C  N N 314 
ILE OXT  O  N N 315 
ILE H    H  N N 316 
ILE H2   H  N N 317 
ILE HA   H  N N 318 
ILE HB   H  N N 319 
ILE HG12 H  N N 320 
ILE HG13 H  N N 321 
ILE HG21 H  N N 322 
ILE HG22 H  N N 323 
ILE HG23 H  N N 324 
ILE HD11 H  N N 325 
ILE HD12 H  N N 326 
ILE HD13 H  N N 327 
ILE HXT  H  N N 328 
LEU N    N  N N 329 
LEU CA   C  N S 330 
LEU C    C  N N 331 
LEU O    O  N N 332 
LEU CB   C  N N 333 
LEU CG   C  N N 334 
LEU CD1  C  N N 335 
LEU CD2  C  N N 336 
LEU OXT  O  N N 337 
LEU H    H  N N 338 
LEU H2   H  N N 339 
LEU HA   H  N N 340 
LEU HB2  H  N N 341 
LEU HB3  H  N N 342 
LEU HG   H  N N 343 
LEU HD11 H  N N 344 
LEU HD12 H  N N 345 
LEU HD13 H  N N 346 
LEU HD21 H  N N 347 
LEU HD22 H  N N 348 
LEU HD23 H  N N 349 
LEU HXT  H  N N 350 
LYS N    N  N N 351 
LYS CA   C  N S 352 
LYS C    C  N N 353 
LYS O    O  N N 354 
LYS CB   C  N N 355 
LYS CG   C  N N 356 
LYS CD   C  N N 357 
LYS CE   C  N N 358 
LYS NZ   N  N N 359 
LYS OXT  O  N N 360 
LYS H    H  N N 361 
LYS H2   H  N N 362 
LYS HA   H  N N 363 
LYS HB2  H  N N 364 
LYS HB3  H  N N 365 
LYS HG2  H  N N 366 
LYS HG3  H  N N 367 
LYS HD2  H  N N 368 
LYS HD3  H  N N 369 
LYS HE2  H  N N 370 
LYS HE3  H  N N 371 
LYS HZ1  H  N N 372 
LYS HZ2  H  N N 373 
LYS HZ3  H  N N 374 
LYS HXT  H  N N 375 
MAN C1   C  N S 376 
MAN C2   C  N S 377 
MAN C3   C  N S 378 
MAN C4   C  N S 379 
MAN C5   C  N R 380 
MAN C6   C  N N 381 
MAN O1   O  N N 382 
MAN O2   O  N N 383 
MAN O3   O  N N 384 
MAN O4   O  N N 385 
MAN O5   O  N N 386 
MAN O6   O  N N 387 
MAN H1   H  N N 388 
MAN H2   H  N N 389 
MAN H3   H  N N 390 
MAN H4   H  N N 391 
MAN H5   H  N N 392 
MAN H61  H  N N 393 
MAN H62  H  N N 394 
MAN HO1  H  N N 395 
MAN HO2  H  N N 396 
MAN HO3  H  N N 397 
MAN HO4  H  N N 398 
MAN HO6  H  N N 399 
MET N    N  N N 400 
MET CA   C  N S 401 
MET C    C  N N 402 
MET O    O  N N 403 
MET CB   C  N N 404 
MET CG   C  N N 405 
MET SD   S  N N 406 
MET CE   C  N N 407 
MET OXT  O  N N 408 
MET H    H  N N 409 
MET H2   H  N N 410 
MET HA   H  N N 411 
MET HB2  H  N N 412 
MET HB3  H  N N 413 
MET HG2  H  N N 414 
MET HG3  H  N N 415 
MET HE1  H  N N 416 
MET HE2  H  N N 417 
MET HE3  H  N N 418 
MET HXT  H  N N 419 
MG  MG   MG N N 420 
NAG C1   C  N R 421 
NAG C2   C  N R 422 
NAG C3   C  N R 423 
NAG C4   C  N S 424 
NAG C5   C  N R 425 
NAG C6   C  N N 426 
NAG C7   C  N N 427 
NAG C8   C  N N 428 
NAG N2   N  N N 429 
NAG O1   O  N N 430 
NAG O3   O  N N 431 
NAG O4   O  N N 432 
NAG O5   O  N N 433 
NAG O6   O  N N 434 
NAG O7   O  N N 435 
NAG H1   H  N N 436 
NAG H2   H  N N 437 
NAG H3   H  N N 438 
NAG H4   H  N N 439 
NAG H5   H  N N 440 
NAG H61  H  N N 441 
NAG H62  H  N N 442 
NAG H81  H  N N 443 
NAG H82  H  N N 444 
NAG H83  H  N N 445 
NAG HN2  H  N N 446 
NAG HO1  H  N N 447 
NAG HO3  H  N N 448 
NAG HO4  H  N N 449 
NAG HO6  H  N N 450 
PHE N    N  N N 451 
PHE CA   C  N S 452 
PHE C    C  N N 453 
PHE O    O  N N 454 
PHE CB   C  N N 455 
PHE CG   C  Y N 456 
PHE CD1  C  Y N 457 
PHE CD2  C  Y N 458 
PHE CE1  C  Y N 459 
PHE CE2  C  Y N 460 
PHE CZ   C  Y N 461 
PHE OXT  O  N N 462 
PHE H    H  N N 463 
PHE H2   H  N N 464 
PHE HA   H  N N 465 
PHE HB2  H  N N 466 
PHE HB3  H  N N 467 
PHE HD1  H  N N 468 
PHE HD2  H  N N 469 
PHE HE1  H  N N 470 
PHE HE2  H  N N 471 
PHE HZ   H  N N 472 
PHE HXT  H  N N 473 
PRO N    N  N N 474 
PRO CA   C  N S 475 
PRO C    C  N N 476 
PRO O    O  N N 477 
PRO CB   C  N N 478 
PRO CG   C  N N 479 
PRO CD   C  N N 480 
PRO OXT  O  N N 481 
PRO H    H  N N 482 
PRO HA   H  N N 483 
PRO HB2  H  N N 484 
PRO HB3  H  N N 485 
PRO HG2  H  N N 486 
PRO HG3  H  N N 487 
PRO HD2  H  N N 488 
PRO HD3  H  N N 489 
PRO HXT  H  N N 490 
SER N    N  N N 491 
SER CA   C  N S 492 
SER C    C  N N 493 
SER O    O  N N 494 
SER CB   C  N N 495 
SER OG   O  N N 496 
SER OXT  O  N N 497 
SER H    H  N N 498 
SER H2   H  N N 499 
SER HA   H  N N 500 
SER HB2  H  N N 501 
SER HB3  H  N N 502 
SER HG   H  N N 503 
SER HXT  H  N N 504 
SO4 S    S  N N 505 
SO4 O1   O  N N 506 
SO4 O2   O  N N 507 
SO4 O3   O  N N 508 
SO4 O4   O  N N 509 
THR N    N  N N 510 
THR CA   C  N S 511 
THR C    C  N N 512 
THR O    O  N N 513 
THR CB   C  N R 514 
THR OG1  O  N N 515 
THR CG2  C  N N 516 
THR OXT  O  N N 517 
THR H    H  N N 518 
THR H2   H  N N 519 
THR HA   H  N N 520 
THR HB   H  N N 521 
THR HG1  H  N N 522 
THR HG21 H  N N 523 
THR HG22 H  N N 524 
THR HG23 H  N N 525 
THR HXT  H  N N 526 
TRP N    N  N N 527 
TRP CA   C  N S 528 
TRP C    C  N N 529 
TRP O    O  N N 530 
TRP CB   C  N N 531 
TRP CG   C  Y N 532 
TRP CD1  C  Y N 533 
TRP CD2  C  Y N 534 
TRP NE1  N  Y N 535 
TRP CE2  C  Y N 536 
TRP CE3  C  Y N 537 
TRP CZ2  C  Y N 538 
TRP CZ3  C  Y N 539 
TRP CH2  C  Y N 540 
TRP OXT  O  N N 541 
TRP H    H  N N 542 
TRP H2   H  N N 543 
TRP HA   H  N N 544 
TRP HB2  H  N N 545 
TRP HB3  H  N N 546 
TRP HD1  H  N N 547 
TRP HE1  H  N N 548 
TRP HE3  H  N N 549 
TRP HZ2  H  N N 550 
TRP HZ3  H  N N 551 
TRP HH2  H  N N 552 
TRP HXT  H  N N 553 
TYR N    N  N N 554 
TYR CA   C  N S 555 
TYR C    C  N N 556 
TYR O    O  N N 557 
TYR CB   C  N N 558 
TYR CG   C  Y N 559 
TYR CD1  C  Y N 560 
TYR CD2  C  Y N 561 
TYR CE1  C  Y N 562 
TYR CE2  C  Y N 563 
TYR CZ   C  Y N 564 
TYR OH   O  N N 565 
TYR OXT  O  N N 566 
TYR H    H  N N 567 
TYR H2   H  N N 568 
TYR HA   H  N N 569 
TYR HB2  H  N N 570 
TYR HB3  H  N N 571 
TYR HD1  H  N N 572 
TYR HD2  H  N N 573 
TYR HE1  H  N N 574 
TYR HE2  H  N N 575 
TYR HH   H  N N 576 
TYR HXT  H  N N 577 
VAL N    N  N N 578 
VAL CA   C  N S 579 
VAL C    C  N N 580 
VAL O    O  N N 581 
VAL CB   C  N N 582 
VAL CG1  C  N N 583 
VAL CG2  C  N N 584 
VAL OXT  O  N N 585 
VAL H    H  N N 586 
VAL H2   H  N N 587 
VAL HA   H  N N 588 
VAL HB   H  N N 589 
VAL HG11 H  N N 590 
VAL HG12 H  N N 591 
VAL HG13 H  N N 592 
VAL HG21 H  N N 593 
VAL HG22 H  N N 594 
VAL HG23 H  N N 595 
VAL HXT  H  N N 596 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
EPE N1  C2   sing N N 107 
EPE N1  C6   sing N N 108 
EPE N1  C9   sing N N 109 
EPE C2  C3   sing N N 110 
EPE C2  H21  sing N N 111 
EPE C2  H22  sing N N 112 
EPE C3  N4   sing N N 113 
EPE C3  H31  sing N N 114 
EPE C3  H32  sing N N 115 
EPE N4  C5   sing N N 116 
EPE N4  C7   sing N N 117 
EPE C5  C6   sing N N 118 
EPE C5  H51  sing N N 119 
EPE C5  H52  sing N N 120 
EPE C6  H61  sing N N 121 
EPE C6  H62  sing N N 122 
EPE C7  C8   sing N N 123 
EPE C7  H71  sing N N 124 
EPE C7  H72  sing N N 125 
EPE C8  O8   sing N N 126 
EPE C8  H81  sing N N 127 
EPE C8  H82  sing N N 128 
EPE O8  HO8  sing N N 129 
EPE C9  C10  sing N N 130 
EPE C9  H91  sing N N 131 
EPE C9  H92  sing N N 132 
EPE C10 S    sing N N 133 
EPE C10 H101 sing N N 134 
EPE C10 H102 sing N N 135 
EPE S   O1S  doub N N 136 
EPE S   O2S  doub N N 137 
EPE S   O3S  sing N N 138 
EPE O3S HOS3 sing N N 139 
GLN N   CA   sing N N 140 
GLN N   H    sing N N 141 
GLN N   H2   sing N N 142 
GLN CA  C    sing N N 143 
GLN CA  CB   sing N N 144 
GLN CA  HA   sing N N 145 
GLN C   O    doub N N 146 
GLN C   OXT  sing N N 147 
GLN CB  CG   sing N N 148 
GLN CB  HB2  sing N N 149 
GLN CB  HB3  sing N N 150 
GLN CG  CD   sing N N 151 
GLN CG  HG2  sing N N 152 
GLN CG  HG3  sing N N 153 
GLN CD  OE1  doub N N 154 
GLN CD  NE2  sing N N 155 
GLN NE2 HE21 sing N N 156 
GLN NE2 HE22 sing N N 157 
GLN OXT HXT  sing N N 158 
GLU N   CA   sing N N 159 
GLU N   H    sing N N 160 
GLU N   H2   sing N N 161 
GLU CA  C    sing N N 162 
GLU CA  CB   sing N N 163 
GLU CA  HA   sing N N 164 
GLU C   O    doub N N 165 
GLU C   OXT  sing N N 166 
GLU CB  CG   sing N N 167 
GLU CB  HB2  sing N N 168 
GLU CB  HB3  sing N N 169 
GLU CG  CD   sing N N 170 
GLU CG  HG2  sing N N 171 
GLU CG  HG3  sing N N 172 
GLU CD  OE1  doub N N 173 
GLU CD  OE2  sing N N 174 
GLU OE2 HE2  sing N N 175 
GLU OXT HXT  sing N N 176 
GLY N   CA   sing N N 177 
GLY N   H    sing N N 178 
GLY N   H2   sing N N 179 
GLY CA  C    sing N N 180 
GLY CA  HA2  sing N N 181 
GLY CA  HA3  sing N N 182 
GLY C   O    doub N N 183 
GLY C   OXT  sing N N 184 
GLY OXT HXT  sing N N 185 
GOL C1  O1   sing N N 186 
GOL C1  C2   sing N N 187 
GOL C1  H11  sing N N 188 
GOL C1  H12  sing N N 189 
GOL O1  HO1  sing N N 190 
GOL C2  O2   sing N N 191 
GOL C2  C3   sing N N 192 
GOL C2  H2   sing N N 193 
GOL O2  HO2  sing N N 194 
GOL C3  O3   sing N N 195 
GOL C3  H31  sing N N 196 
GOL C3  H32  sing N N 197 
GOL O3  HO3  sing N N 198 
HEM CHA C1A  sing N N 199 
HEM CHA C4D  doub N N 200 
HEM CHA HHA  sing N N 201 
HEM CHB C4A  sing N N 202 
HEM CHB C1B  doub N N 203 
HEM CHB HHB  sing N N 204 
HEM CHC C4B  sing N N 205 
HEM CHC C1C  doub N N 206 
HEM CHC HHC  sing N N 207 
HEM CHD C4C  doub N N 208 
HEM CHD C1D  sing N N 209 
HEM CHD HHD  sing N N 210 
HEM C1A C2A  doub Y N 211 
HEM C1A NA   sing Y N 212 
HEM C2A C3A  sing Y N 213 
HEM C2A CAA  sing N N 214 
HEM C3A C4A  doub Y N 215 
HEM C3A CMA  sing N N 216 
HEM C4A NA   sing Y N 217 
HEM CMA HMA  sing N N 218 
HEM CMA HMAA sing N N 219 
HEM CMA HMAB sing N N 220 
HEM CAA CBA  sing N N 221 
HEM CAA HAA  sing N N 222 
HEM CAA HAAA sing N N 223 
HEM CBA CGA  sing N N 224 
HEM CBA HBA  sing N N 225 
HEM CBA HBAA sing N N 226 
HEM CGA O1A  doub N N 227 
HEM CGA O2A  sing N N 228 
HEM C1B C2B  sing N N 229 
HEM C1B NB   sing N N 230 
HEM C2B C3B  doub N N 231 
HEM C2B CMB  sing N N 232 
HEM C3B C4B  sing N N 233 
HEM C3B CAB  sing N N 234 
HEM C4B NB   doub N N 235 
HEM CMB HMB  sing N N 236 
HEM CMB HMBA sing N N 237 
HEM CMB HMBB sing N N 238 
HEM CAB CBB  doub N N 239 
HEM CAB HAB  sing N N 240 
HEM CBB HBB  sing N N 241 
HEM CBB HBBA sing N N 242 
HEM C1C C2C  sing Y N 243 
HEM C1C NC   sing Y N 244 
HEM C2C C3C  doub Y N 245 
HEM C2C CMC  sing N N 246 
HEM C3C C4C  sing Y N 247 
HEM C3C CAC  sing N N 248 
HEM C4C NC   sing Y N 249 
HEM CMC HMC  sing N N 250 
HEM CMC HMCA sing N N 251 
HEM CMC HMCB sing N N 252 
HEM CAC CBC  doub N N 253 
HEM CAC HAC  sing N N 254 
HEM CBC HBC  sing N N 255 
HEM CBC HBCA sing N N 256 
HEM C1D C2D  sing N N 257 
HEM C1D ND   doub N N 258 
HEM C2D C3D  doub N N 259 
HEM C2D CMD  sing N N 260 
HEM C3D C4D  sing N N 261 
HEM C3D CAD  sing N N 262 
HEM C4D ND   sing N N 263 
HEM CMD HMD  sing N N 264 
HEM CMD HMDA sing N N 265 
HEM CMD HMDB sing N N 266 
HEM CAD CBD  sing N N 267 
HEM CAD HAD  sing N N 268 
HEM CAD HADA sing N N 269 
HEM CBD CGD  sing N N 270 
HEM CBD HBD  sing N N 271 
HEM CBD HBDA sing N N 272 
HEM CGD O1D  doub N N 273 
HEM CGD O2D  sing N N 274 
HEM O2A H2A  sing N N 275 
HEM O2D H2D  sing N N 276 
HEM FE  NA   sing N N 277 
HEM FE  NB   sing N N 278 
HEM FE  NC   sing N N 279 
HEM FE  ND   sing N N 280 
HIS N   CA   sing N N 281 
HIS N   H    sing N N 282 
HIS N   H2   sing N N 283 
HIS CA  C    sing N N 284 
HIS CA  CB   sing N N 285 
HIS CA  HA   sing N N 286 
HIS C   O    doub N N 287 
HIS C   OXT  sing N N 288 
HIS CB  CG   sing N N 289 
HIS CB  HB2  sing N N 290 
HIS CB  HB3  sing N N 291 
HIS CG  ND1  sing Y N 292 
HIS CG  CD2  doub Y N 293 
HIS ND1 CE1  doub Y N 294 
HIS ND1 HD1  sing N N 295 
HIS CD2 NE2  sing Y N 296 
HIS CD2 HD2  sing N N 297 
HIS CE1 NE2  sing Y N 298 
HIS CE1 HE1  sing N N 299 
HIS NE2 HE2  sing N N 300 
HIS OXT HXT  sing N N 301 
HOH O   H1   sing N N 302 
HOH O   H2   sing N N 303 
ILE N   CA   sing N N 304 
ILE N   H    sing N N 305 
ILE N   H2   sing N N 306 
ILE CA  C    sing N N 307 
ILE CA  CB   sing N N 308 
ILE CA  HA   sing N N 309 
ILE C   O    doub N N 310 
ILE C   OXT  sing N N 311 
ILE CB  CG1  sing N N 312 
ILE CB  CG2  sing N N 313 
ILE CB  HB   sing N N 314 
ILE CG1 CD1  sing N N 315 
ILE CG1 HG12 sing N N 316 
ILE CG1 HG13 sing N N 317 
ILE CG2 HG21 sing N N 318 
ILE CG2 HG22 sing N N 319 
ILE CG2 HG23 sing N N 320 
ILE CD1 HD11 sing N N 321 
ILE CD1 HD12 sing N N 322 
ILE CD1 HD13 sing N N 323 
ILE OXT HXT  sing N N 324 
LEU N   CA   sing N N 325 
LEU N   H    sing N N 326 
LEU N   H2   sing N N 327 
LEU CA  C    sing N N 328 
LEU CA  CB   sing N N 329 
LEU CA  HA   sing N N 330 
LEU C   O    doub N N 331 
LEU C   OXT  sing N N 332 
LEU CB  CG   sing N N 333 
LEU CB  HB2  sing N N 334 
LEU CB  HB3  sing N N 335 
LEU CG  CD1  sing N N 336 
LEU CG  CD2  sing N N 337 
LEU CG  HG   sing N N 338 
LEU CD1 HD11 sing N N 339 
LEU CD1 HD12 sing N N 340 
LEU CD1 HD13 sing N N 341 
LEU CD2 HD21 sing N N 342 
LEU CD2 HD22 sing N N 343 
LEU CD2 HD23 sing N N 344 
LEU OXT HXT  sing N N 345 
LYS N   CA   sing N N 346 
LYS N   H    sing N N 347 
LYS N   H2   sing N N 348 
LYS CA  C    sing N N 349 
LYS CA  CB   sing N N 350 
LYS CA  HA   sing N N 351 
LYS C   O    doub N N 352 
LYS C   OXT  sing N N 353 
LYS CB  CG   sing N N 354 
LYS CB  HB2  sing N N 355 
LYS CB  HB3  sing N N 356 
LYS CG  CD   sing N N 357 
LYS CG  HG2  sing N N 358 
LYS CG  HG3  sing N N 359 
LYS CD  CE   sing N N 360 
LYS CD  HD2  sing N N 361 
LYS CD  HD3  sing N N 362 
LYS CE  NZ   sing N N 363 
LYS CE  HE2  sing N N 364 
LYS CE  HE3  sing N N 365 
LYS NZ  HZ1  sing N N 366 
LYS NZ  HZ2  sing N N 367 
LYS NZ  HZ3  sing N N 368 
LYS OXT HXT  sing N N 369 
MAN C1  C2   sing N N 370 
MAN C1  O1   sing N N 371 
MAN C1  O5   sing N N 372 
MAN C1  H1   sing N N 373 
MAN C2  C3   sing N N 374 
MAN C2  O2   sing N N 375 
MAN C2  H2   sing N N 376 
MAN C3  C4   sing N N 377 
MAN C3  O3   sing N N 378 
MAN C3  H3   sing N N 379 
MAN C4  C5   sing N N 380 
MAN C4  O4   sing N N 381 
MAN C4  H4   sing N N 382 
MAN C5  C6   sing N N 383 
MAN C5  O5   sing N N 384 
MAN C5  H5   sing N N 385 
MAN C6  O6   sing N N 386 
MAN C6  H61  sing N N 387 
MAN C6  H62  sing N N 388 
MAN O1  HO1  sing N N 389 
MAN O2  HO2  sing N N 390 
MAN O3  HO3  sing N N 391 
MAN O4  HO4  sing N N 392 
MAN O6  HO6  sing N N 393 
MET N   CA   sing N N 394 
MET N   H    sing N N 395 
MET N   H2   sing N N 396 
MET CA  C    sing N N 397 
MET CA  CB   sing N N 398 
MET CA  HA   sing N N 399 
MET C   O    doub N N 400 
MET C   OXT  sing N N 401 
MET CB  CG   sing N N 402 
MET CB  HB2  sing N N 403 
MET CB  HB3  sing N N 404 
MET CG  SD   sing N N 405 
MET CG  HG2  sing N N 406 
MET CG  HG3  sing N N 407 
MET SD  CE   sing N N 408 
MET CE  HE1  sing N N 409 
MET CE  HE2  sing N N 410 
MET CE  HE3  sing N N 411 
MET OXT HXT  sing N N 412 
NAG C1  C2   sing N N 413 
NAG C1  O1   sing N N 414 
NAG C1  O5   sing N N 415 
NAG C1  H1   sing N N 416 
NAG C2  C3   sing N N 417 
NAG C2  N2   sing N N 418 
NAG C2  H2   sing N N 419 
NAG C3  C4   sing N N 420 
NAG C3  O3   sing N N 421 
NAG C3  H3   sing N N 422 
NAG C4  C5   sing N N 423 
NAG C4  O4   sing N N 424 
NAG C4  H4   sing N N 425 
NAG C5  C6   sing N N 426 
NAG C5  O5   sing N N 427 
NAG C5  H5   sing N N 428 
NAG C6  O6   sing N N 429 
NAG C6  H61  sing N N 430 
NAG C6  H62  sing N N 431 
NAG C7  C8   sing N N 432 
NAG C7  N2   sing N N 433 
NAG C7  O7   doub N N 434 
NAG C8  H81  sing N N 435 
NAG C8  H82  sing N N 436 
NAG C8  H83  sing N N 437 
NAG N2  HN2  sing N N 438 
NAG O1  HO1  sing N N 439 
NAG O3  HO3  sing N N 440 
NAG O4  HO4  sing N N 441 
NAG O6  HO6  sing N N 442 
PHE N   CA   sing N N 443 
PHE N   H    sing N N 444 
PHE N   H2   sing N N 445 
PHE CA  C    sing N N 446 
PHE CA  CB   sing N N 447 
PHE CA  HA   sing N N 448 
PHE C   O    doub N N 449 
PHE C   OXT  sing N N 450 
PHE CB  CG   sing N N 451 
PHE CB  HB2  sing N N 452 
PHE CB  HB3  sing N N 453 
PHE CG  CD1  doub Y N 454 
PHE CG  CD2  sing Y N 455 
PHE CD1 CE1  sing Y N 456 
PHE CD1 HD1  sing N N 457 
PHE CD2 CE2  doub Y N 458 
PHE CD2 HD2  sing N N 459 
PHE CE1 CZ   doub Y N 460 
PHE CE1 HE1  sing N N 461 
PHE CE2 CZ   sing Y N 462 
PHE CE2 HE2  sing N N 463 
PHE CZ  HZ   sing N N 464 
PHE OXT HXT  sing N N 465 
PRO N   CA   sing N N 466 
PRO N   CD   sing N N 467 
PRO N   H    sing N N 468 
PRO CA  C    sing N N 469 
PRO CA  CB   sing N N 470 
PRO CA  HA   sing N N 471 
PRO C   O    doub N N 472 
PRO C   OXT  sing N N 473 
PRO CB  CG   sing N N 474 
PRO CB  HB2  sing N N 475 
PRO CB  HB3  sing N N 476 
PRO CG  CD   sing N N 477 
PRO CG  HG2  sing N N 478 
PRO CG  HG3  sing N N 479 
PRO CD  HD2  sing N N 480 
PRO CD  HD3  sing N N 481 
PRO OXT HXT  sing N N 482 
SER N   CA   sing N N 483 
SER N   H    sing N N 484 
SER N   H2   sing N N 485 
SER CA  C    sing N N 486 
SER CA  CB   sing N N 487 
SER CA  HA   sing N N 488 
SER C   O    doub N N 489 
SER C   OXT  sing N N 490 
SER CB  OG   sing N N 491 
SER CB  HB2  sing N N 492 
SER CB  HB3  sing N N 493 
SER OG  HG   sing N N 494 
SER OXT HXT  sing N N 495 
SO4 S   O1   doub N N 496 
SO4 S   O2   doub N N 497 
SO4 S   O3   sing N N 498 
SO4 S   O4   sing N N 499 
THR N   CA   sing N N 500 
THR N   H    sing N N 501 
THR N   H2   sing N N 502 
THR CA  C    sing N N 503 
THR CA  CB   sing N N 504 
THR CA  HA   sing N N 505 
THR C   O    doub N N 506 
THR C   OXT  sing N N 507 
THR CB  OG1  sing N N 508 
THR CB  CG2  sing N N 509 
THR CB  HB   sing N N 510 
THR OG1 HG1  sing N N 511 
THR CG2 HG21 sing N N 512 
THR CG2 HG22 sing N N 513 
THR CG2 HG23 sing N N 514 
THR OXT HXT  sing N N 515 
TRP N   CA   sing N N 516 
TRP N   H    sing N N 517 
TRP N   H2   sing N N 518 
TRP CA  C    sing N N 519 
TRP CA  CB   sing N N 520 
TRP CA  HA   sing N N 521 
TRP C   O    doub N N 522 
TRP C   OXT  sing N N 523 
TRP CB  CG   sing N N 524 
TRP CB  HB2  sing N N 525 
TRP CB  HB3  sing N N 526 
TRP CG  CD1  doub Y N 527 
TRP CG  CD2  sing Y N 528 
TRP CD1 NE1  sing Y N 529 
TRP CD1 HD1  sing N N 530 
TRP CD2 CE2  doub Y N 531 
TRP CD2 CE3  sing Y N 532 
TRP NE1 CE2  sing Y N 533 
TRP NE1 HE1  sing N N 534 
TRP CE2 CZ2  sing Y N 535 
TRP CE3 CZ3  doub Y N 536 
TRP CE3 HE3  sing N N 537 
TRP CZ2 CH2  doub Y N 538 
TRP CZ2 HZ2  sing N N 539 
TRP CZ3 CH2  sing Y N 540 
TRP CZ3 HZ3  sing N N 541 
TRP CH2 HH2  sing N N 542 
TRP OXT HXT  sing N N 543 
TYR N   CA   sing N N 544 
TYR N   H    sing N N 545 
TYR N   H2   sing N N 546 
TYR CA  C    sing N N 547 
TYR CA  CB   sing N N 548 
TYR CA  HA   sing N N 549 
TYR C   O    doub N N 550 
TYR C   OXT  sing N N 551 
TYR CB  CG   sing N N 552 
TYR CB  HB2  sing N N 553 
TYR CB  HB3  sing N N 554 
TYR CG  CD1  doub Y N 555 
TYR CG  CD2  sing Y N 556 
TYR CD1 CE1  sing Y N 557 
TYR CD1 HD1  sing N N 558 
TYR CD2 CE2  doub Y N 559 
TYR CD2 HD2  sing N N 560 
TYR CE1 CZ   doub Y N 561 
TYR CE1 HE1  sing N N 562 
TYR CE2 CZ   sing Y N 563 
TYR CE2 HE2  sing N N 564 
TYR CZ  OH   sing N N 565 
TYR OH  HH   sing N N 566 
TYR OXT HXT  sing N N 567 
VAL N   CA   sing N N 568 
VAL N   H    sing N N 569 
VAL N   H2   sing N N 570 
VAL CA  C    sing N N 571 
VAL CA  CB   sing N N 572 
VAL CA  HA   sing N N 573 
VAL C   O    doub N N 574 
VAL C   OXT  sing N N 575 
VAL CB  CG1  sing N N 576 
VAL CB  CG2  sing N N 577 
VAL CB  HB   sing N N 578 
VAL CG1 HG11 sing N N 579 
VAL CG1 HG12 sing N N 580 
VAL CG1 HG13 sing N N 581 
VAL CG2 HG21 sing N N 582 
VAL CG2 HG22 sing N N 583 
VAL CG2 HG23 sing N N 584 
VAL OXT HXT  sing N N 585 
# 
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 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
5 MAN 4 n 
5 MAN 5 n 
5 MAN 6 n 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
6 MAN 4 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5OXU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HE6 
_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]   0.003665 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001452 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013362 
_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]   0.010187 
_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   ? 62.917  3.900   59.000 1.00 90.68  ? 14  GLN A N   1 
ATOM   2    C  CA  . GLN A  1  1   ? 61.747  3.008   59.234 1.00 97.51  ? 14  GLN A CA  1 
ATOM   3    C  C   . GLN A  1  1   ? 61.175  2.520   57.898 1.00 97.59  ? 14  GLN A C   1 
ATOM   4    O  O   . GLN A  1  1   ? 59.967  2.611   57.660 1.00 89.53  ? 14  GLN A O   1 
ATOM   5    C  CB  . GLN A  1  1   ? 60.721  3.773   60.073 1.00 102.53 ? 14  GLN A CB  1 
ATOM   6    C  CG  . GLN A  1  1   ? 59.535  2.935   60.536 1.00 109.78 ? 14  GLN A CG  1 
ATOM   7    C  CD  . GLN A  1  1   ? 58.596  3.701   61.440 1.00 119.48 ? 14  GLN A CD  1 
ATOM   8    O  OE1 . GLN A  1  1   ? 58.907  4.796   61.922 1.00 125.97 ? 14  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A  1  1   ? 57.431  3.120   61.683 1.00 121.72 ? 14  GLN A NE2 1 
ATOM   10   N  N   . GLY A  1  2   ? 62.060  2.004   57.031 1.00 82.87  ? 15  GLY A N   1 
ATOM   11   C  CA  . GLY A  1  2   ? 61.681  1.568   55.703 1.00 71.49  ? 15  GLY A CA  1 
ATOM   12   C  C   . GLY A  1  2   ? 61.545  0.052   55.630 1.00 61.78  ? 15  GLY A C   1 
ATOM   13   O  O   . GLY A  1  2   ? 61.552  -0.643  56.639 1.00 59.30  ? 15  GLY A O   1 
ATOM   14   N  N   . VAL A  1  3   ? 61.375  -0.448  54.411 1.00 55.05  ? 16  VAL A N   1 
ATOM   15   C  CA  . VAL A  1  3   ? 61.141  -1.856  54.170 1.00 54.73  ? 16  VAL A CA  1 
ATOM   16   C  C   . VAL A  1  3   ? 62.044  -2.264  53.014 1.00 52.10  ? 16  VAL A C   1 
ATOM   17   O  O   . VAL A  1  3   ? 62.389  -1.429  52.191 1.00 46.85  ? 16  VAL A O   1 
ATOM   18   C  CB  . VAL A  1  3   ? 59.643  -2.101  53.873 1.00 62.72  ? 16  VAL A CB  1 
ATOM   19   C  CG1 . VAL A  1  3   ? 59.355  -3.518  53.400 1.00 67.12  ? 16  VAL A CG1 1 
ATOM   20   C  CG2 . VAL A  1  3   ? 58.784  -1.789  55.093 1.00 64.18  ? 16  VAL A CG2 1 
ATOM   21   N  N   . ASP A  1  4   ? 62.413  -3.544  52.967 1.00 53.97  ? 17  ASP A N   1 
ATOM   22   C  CA  . ASP A  1  4   ? 63.123  -4.110  51.838 1.00 57.85  ? 17  ASP A CA  1 
ATOM   23   C  C   . ASP A  1  4   ? 62.110  -4.729  50.871 1.00 51.42  ? 17  ASP A C   1 
ATOM   24   O  O   . ASP A  1  4   ? 61.444  -5.688  51.232 1.00 57.90  ? 17  ASP A O   1 
ATOM   25   C  CB  . ASP A  1  4   ? 64.169  -5.094  52.339 1.00 66.35  ? 17  ASP A CB  1 
ATOM   26   C  CG  . ASP A  1  4   ? 65.252  -5.432  51.325 1.00 71.11  ? 17  ASP A CG  1 
ATOM   27   O  OD1 . ASP A  1  4   ? 64.896  -5.733  50.166 1.00 84.18  ? 17  ASP A OD1 1 
ATOM   28   O  OD2 . ASP A  1  4   ? 66.434  -5.394  51.696 1.00 79.90  ? 17  ASP A OD2 1 
ATOM   29   N  N   . PRO A  1  5   ? 61.955  -4.214  49.628 1.00 57.01  ? 18  PRO A N   1 
ATOM   30   C  CA  . PRO A  1  5   ? 60.928  -4.704  48.700 1.00 52.95  ? 18  PRO A CA  1 
ATOM   31   C  C   . PRO A  1  5   ? 61.196  -6.101  48.124 1.00 51.02  ? 18  PRO A C   1 
ATOM   32   O  O   . PRO A  1  5   ? 62.223  -6.313  47.475 1.00 50.81  ? 18  PRO A O   1 
ATOM   33   C  CB  . PRO A  1  5   ? 60.887  -3.647  47.580 1.00 56.83  ? 18  PRO A CB  1 
ATOM   34   C  CG  . PRO A  1  5   ? 61.935  -2.601  47.937 1.00 59.16  ? 18  PRO A CG  1 
ATOM   35   C  CD  . PRO A  1  5   ? 62.778  -3.140  49.051 1.00 58.19  ? 18  PRO A CD  1 
ATOM   36   N  N   . PRO A  1  6   ? 60.257  -7.063  48.287 1.00 44.91  ? 19  PRO A N   1 
ATOM   37   C  CA  . PRO A  1  6   ? 60.411  -8.410  47.744 1.00 46.59  ? 19  PRO A CA  1 
ATOM   38   C  C   . PRO A  1  6   ? 60.320  -8.371  46.223 1.00 46.94  ? 19  PRO A C   1 
ATOM   39   O  O   . PRO A  1  6   ? 59.684  -7.493  45.659 1.00 41.88  ? 19  PRO A O   1 
ATOM   40   C  CB  . PRO A  1  6   ? 59.253  -9.236  48.339 1.00 46.94  ? 19  PRO A CB  1 
ATOM   41   C  CG  . PRO A  1  6   ? 58.562  -8.313  49.316 1.00 49.61  ? 19  PRO A CG  1 
ATOM   42   C  CD  . PRO A  1  6   ? 58.978  -6.897  48.982 1.00 50.25  ? 19  PRO A CD  1 
ATOM   43   N  N   . PRO A  1  7   ? 60.921  -9.342  45.508 1.00 47.64  ? 20  PRO A N   1 
ATOM   44   C  CA  . PRO A  1  7   ? 60.709  -9.448  44.068 1.00 47.06  ? 20  PRO A CA  1 
ATOM   45   C  C   . PRO A  1  7   ? 59.235  -9.729  43.781 1.00 44.02  ? 20  PRO A C   1 
ATOM   46   O  O   . PRO A  1  7   ? 58.483  -10.128 44.664 1.00 40.09  ? 20  PRO A O   1 
ATOM   47   C  CB  . PRO A  1  7   ? 61.641  -10.586 43.630 1.00 47.05  ? 20  PRO A CB  1 
ATOM   48   C  CG  . PRO A  1  7   ? 61.910  -11.349 44.905 1.00 48.71  ? 20  PRO A CG  1 
ATOM   49   C  CD  . PRO A  1  7   ? 61.819  -10.373 46.046 1.00 48.83  ? 20  PRO A CD  1 
ATOM   50   N  N   . PRO A  1  8   ? 58.756  -9.453  42.551 1.00 42.46  ? 21  PRO A N   1 
ATOM   51   C  CA  . PRO A  1  8   ? 57.364  -9.732  42.199 1.00 43.58  ? 21  PRO A CA  1 
ATOM   52   C  C   . PRO A  1  8   ? 57.007  -11.212 42.339 1.00 40.93  ? 21  PRO A C   1 
ATOM   53   O  O   . PRO A  1  8   ? 57.781  -12.080 41.958 1.00 40.97  ? 21  PRO A O   1 
ATOM   54   C  CB  . PRO A  1  8   ? 57.262  -9.244  40.742 1.00 43.39  ? 21  PRO A CB  1 
ATOM   55   C  CG  . PRO A  1  8   ? 58.690  -9.170  40.254 1.00 43.00  ? 21  PRO A CG  1 
ATOM   56   C  CD  . PRO A  1  8   ? 59.525  -8.834  41.460 1.00 40.89  ? 21  PRO A CD  1 
ATOM   57   N  N   . PRO A  1  9   ? 55.813  -11.558 42.864 1.00 41.79  ? 22  PRO A N   1 
ATOM   58   C  CA  . PRO A  1  9   ? 55.314  -12.930 42.835 1.00 40.44  ? 22  PRO A CA  1 
ATOM   59   C  C   . PRO A  1  9   ? 55.222  -13.450 41.401 1.00 40.73  ? 22  PRO A C   1 
ATOM   60   O  O   . PRO A  1  9   ? 54.989  -12.685 40.469 1.00 35.41  ? 22  PRO A O   1 
ATOM   61   C  CB  . PRO A  1  9   ? 53.921  -12.862 43.501 1.00 40.71  ? 22  PRO A CB  1 
ATOM   62   C  CG  . PRO A  1  9   ? 53.938  -11.581 44.274 1.00 44.10  ? 22  PRO A CG  1 
ATOM   63   C  CD  . PRO A  1  9   ? 54.855  -10.642 43.491 1.00 46.62  ? 22  PRO A CD  1 
ATOM   64   N  N   . GLY A  1  10  ? 55.387  -14.766 41.257 1.00 39.21  ? 23  GLY A N   1 
ATOM   65   C  CA  . GLY A  1  10  ? 55.198  -15.437 39.986 1.00 39.80  ? 23  GLY A CA  1 
ATOM   66   C  C   . GLY A  1  10  ? 53.728  -15.792 39.751 1.00 44.74  ? 23  GLY A C   1 
ATOM   67   O  O   . GLY A  1  10  ? 52.852  -15.453 40.556 1.00 38.79  ? 23  GLY A O   1 
ATOM   68   N  N   . PRO A  1  11  ? 53.424  -16.513 38.648 1.00 47.23  ? 24  PRO A N   1 
ATOM   69   C  CA  . PRO A  1  11  ? 52.050  -16.902 38.324 1.00 46.50  ? 24  PRO A CA  1 
ATOM   70   C  C   . PRO A  1  11  ? 51.494  -17.810 39.421 1.00 43.35  ? 24  PRO A C   1 
ATOM   71   O  O   . PRO A  1  11  ? 52.244  -18.402 40.177 1.00 42.96  ? 24  PRO A O   1 
ATOM   72   C  CB  . PRO A  1  11  ? 52.147  -17.622 36.966 1.00 47.09  ? 24  PRO A CB  1 
ATOM   73   C  CG  . PRO A  1  11  ? 53.564  -17.356 36.472 1.00 48.67  ? 24  PRO A CG  1 
ATOM   74   C  CD  . PRO A  1  11  ? 54.407  -17.052 37.697 1.00 46.83  ? 24  PRO A CD  1 
ATOM   75   N  N   . PRO A  1  12  ? 50.162  -17.929 39.581 1.00 42.68  ? 25  PRO A N   1 
ATOM   76   C  CA  . PRO A  1  12  ? 49.592  -18.890 40.529 1.00 46.23  ? 25  PRO A CA  1 
ATOM   77   C  C   . PRO A  1  12  ? 49.866  -20.349 40.147 1.00 44.97  ? 25  PRO A C   1 
ATOM   78   O  O   . PRO A  1  12  ? 50.041  -20.664 38.980 1.00 40.55  ? 25  PRO A O   1 
ATOM   79   C  CB  . PRO A  1  12  ? 48.100  -18.531 40.504 1.00 46.48  ? 25  PRO A CB  1 
ATOM   80   C  CG  . PRO A  1  12  ? 47.879  -17.944 39.126 1.00 48.99  ? 25  PRO A CG  1 
ATOM   81   C  CD  . PRO A  1  12  ? 49.145  -17.173 38.846 1.00 45.57  ? 25  PRO A CD  1 
ATOM   82   N  N   . SER A  1  13  ? 49.926  -21.227 41.155 1.00 50.20  ? 26  SER A N   1 
ATOM   83   C  CA  A SER A  1  13  ? 50.082  -22.665 40.961 0.50 51.15  ? 26  SER A CA  1 
ATOM   84   C  CA  B SER A  1  13  ? 50.089  -22.659 40.951 0.50 50.83  ? 26  SER A CA  1 
ATOM   85   C  C   . SER A  1  13  ? 48.925  -23.226 40.141 1.00 48.95  ? 26  SER A C   1 
ATOM   86   O  O   . SER A  1  13  ? 49.149  -23.930 39.170 1.00 52.93  ? 26  SER A O   1 
ATOM   87   C  CB  A SER A  1  13  ? 50.163  -23.398 42.274 0.50 51.86  ? 26  SER A CB  1 
ATOM   88   C  CB  B SER A  1  13  ? 50.215  -23.375 42.261 0.50 51.16  ? 26  SER A CB  1 
ATOM   89   O  OG  A SER A  1  13  ? 51.123  -22.809 43.132 0.50 55.63  ? 26  SER A OG  1 
ATOM   90   O  OG  B SER A  1  13  ? 50.512  -24.742 42.039 0.50 54.24  ? 26  SER A OG  1 
ATOM   91   N  N   . PHE A  1  14  ? 47.690  -22.928 40.580 1.00 46.75  ? 27  PHE A N   1 
ATOM   92   C  CA  . PHE A  1  14  ? 46.470  -23.304 39.874 1.00 43.07  ? 27  PHE A CA  1 
ATOM   93   C  C   . PHE A  1  14  ? 46.023  -22.118 39.025 1.00 40.45  ? 27  PHE A C   1 
ATOM   94   O  O   . PHE A  1  14  ? 45.803  -21.035 39.558 1.00 40.71  ? 27  PHE A O   1 
ATOM   95   C  CB  . PHE A  1  14  ? 45.370  -23.734 40.857 1.00 40.75  ? 27  PHE A CB  1 
ATOM   96   C  CG  . PHE A  1  14  ? 44.034  -24.094 40.222 1.00 42.20  ? 27  PHE A CG  1 
ATOM   97   C  CD1 . PHE A  1  14  ? 43.891  -25.265 39.482 1.00 39.02  ? 27  PHE A CD1 1 
ATOM   98   C  CD2 . PHE A  1  14  ? 42.917  -23.280 40.400 1.00 42.82  ? 27  PHE A CD2 1 
ATOM   99   C  CE1 . PHE A  1  14  ? 42.673  -25.586 38.895 1.00 42.25  ? 27  PHE A CE1 1 
ATOM   100  C  CE2 . PHE A  1  14  ? 41.698  -23.612 39.820 1.00 45.48  ? 27  PHE A CE2 1 
ATOM   101  C  CZ  . PHE A  1  14  ? 41.580  -24.765 39.069 1.00 45.01  ? 27  PHE A CZ  1 
ATOM   102  N  N   . THR A  1  15  ? 45.877  -22.341 37.712 1.00 40.10  ? 28  THR A N   1 
ATOM   103  C  CA  . THR A  1  15  ? 45.505  -21.288 36.779 1.00 42.25  ? 28  THR A CA  1 
ATOM   104  C  C   . THR A  1  15  ? 44.143  -21.571 36.141 1.00 38.26  ? 28  THR A C   1 
ATOM   105  O  O   . THR A  1  15  ? 43.822  -20.941 35.141 1.00 39.51  ? 28  THR A O   1 
ATOM   106  C  CB  . THR A  1  15  ? 46.570  -21.122 35.688 1.00 46.04  ? 28  THR A CB  1 
ATOM   107  O  OG1 . THR A  1  15  ? 46.573  -22.272 34.845 1.00 45.07  ? 28  THR A OG1 1 
ATOM   108  C  CG2 . THR A  1  15  ? 47.965  -20.930 36.251 1.00 48.09  ? 28  THR A CG2 1 
ATOM   109  N  N   . GLY A  1  16  ? 43.367  -22.522 36.683 1.00 36.38  ? 29  GLY A N   1 
ATOM   110  C  CA  . GLY A  1  16  ? 42.029  -22.790 36.172 1.00 37.95  ? 29  GLY A CA  1 
ATOM   111  C  C   . GLY A  1  16  ? 40.970  -21.867 36.781 1.00 36.27  ? 29  GLY A C   1 
ATOM   112  O  O   . GLY A  1  16  ? 41.286  -20.988 37.572 1.00 39.77  ? 29  GLY A O   1 
ATOM   113  N  N   . THR A  1  17  ? 39.707  -22.075 36.403 1.00 38.96  ? 30  THR A N   1 
ATOM   114  C  CA  . THR A  1  17  ? 38.604  -21.337 36.994 1.00 40.24  ? 30  THR A CA  1 
ATOM   115  C  C   . THR A  1  17  ? 38.381  -21.839 38.412 1.00 36.90  ? 30  THR A C   1 
ATOM   116  O  O   . THR A  1  17  ? 38.788  -22.941 38.752 1.00 39.64  ? 30  THR A O   1 
ATOM   117  C  CB  . THR A  1  17  ? 37.344  -21.425 36.135 1.00 42.10  ? 30  THR A CB  1 
ATOM   118  O  OG1 . THR A  1  17  ? 36.417  -20.550 36.767 1.00 43.95  ? 30  THR A OG1 1 
ATOM   119  C  CG2 . THR A  1  17  ? 36.788  -22.828 36.069 1.00 42.37  ? 30  THR A CG2 1 
ATOM   120  N  N   . LYS A  1  18  ? 37.791  -20.977 39.238 1.00 38.43  ? 31  LYS A N   1 
ATOM   121  C  CA  . LYS A  1  18  ? 37.338  -21.336 40.570 1.00 37.32  ? 31  LYS A CA  1 
ATOM   122  C  C   . LYS A  1  18  ? 36.337  -20.282 41.031 1.00 38.01  ? 31  LYS A C   1 
ATOM   123  O  O   . LYS A  1  18  ? 36.265  -19.205 40.446 1.00 40.59  ? 31  LYS A O   1 
ATOM   124  C  CB  . LYS A  1  18  ? 38.525  -21.464 41.523 1.00 39.60  ? 31  LYS A CB  1 
ATOM   125  C  CG  . LYS A  1  18  ? 39.283  -20.183 41.776 1.00 46.72  ? 31  LYS A CG  1 
ATOM   126  C  CD  . LYS A  1  18  ? 40.439  -20.390 42.747 1.00 52.37  ? 31  LYS A CD  1 
ATOM   127  C  CE  . LYS A  1  18  ? 40.645  -19.237 43.667 1.00 66.24  ? 31  LYS A CE  1 
ATOM   128  N  NZ  . LYS A  1  18  ? 41.963  -19.314 44.312 1.00 74.15  ? 31  LYS A NZ  1 
ATOM   129  N  N   . LEU A  1  19  ? 35.565  -20.609 42.071 1.00 40.80  ? 32  LEU A N   1 
ATOM   130  C  CA  . LEU A  1  19  ? 34.709  -19.648 42.745 1.00 39.35  ? 32  LEU A CA  1 
ATOM   131  C  C   . LEU A  1  19  ? 35.611  -18.647 43.453 1.00 37.89  ? 32  LEU A C   1 
ATOM   132  O  O   . LEU A  1  19  ? 36.454  -19.057 44.249 1.00 41.03  ? 32  LEU A O   1 
ATOM   133  C  CB  . LEU A  1  19  ? 33.789  -20.349 43.747 1.00 39.31  ? 32  LEU A CB  1 
ATOM   134  C  CG  . LEU A  1  19  ? 32.874  -19.433 44.579 1.00 41.45  ? 32  LEU A CG  1 
ATOM   135  C  CD1 . LEU A  1  19  ? 31.836  -18.758 43.702 1.00 39.18  ? 32  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A  1  19  ? 32.202  -20.164 45.723 1.00 41.00  ? 32  LEU A CD2 1 
ATOM   137  N  N   . VAL A  1  20  ? 35.414  -17.348 43.179 1.00 38.90  ? 33  VAL A N   1 
ATOM   138  C  CA  . VAL A  1  20  ? 36.196  -16.319 43.855 1.00 39.52  ? 33  VAL A CA  1 
ATOM   139  C  C   . VAL A  1  20  ? 35.321  -15.544 44.838 1.00 36.73  ? 33  VAL A C   1 
ATOM   140  O  O   . VAL A  1  20  ? 35.842  -14.976 45.797 1.00 37.27  ? 33  VAL A O   1 
ATOM   141  C  CB  . VAL A  1  20  ? 36.949  -15.390 42.880 1.00 37.86  ? 33  VAL A CB  1 
ATOM   142  C  CG1 . VAL A  1  20  ? 37.893  -16.174 41.975 1.00 39.59  ? 33  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A  1  20  ? 36.015  -14.547 42.042 1.00 40.16  ? 33  VAL A CG2 1 
ATOM   144  N  N   . ASN A  1  21  ? 34.008  -15.503 44.591 1.00 38.07  ? 34  ASN A N   1 
ATOM   145  C  CA  . ASN A  1  21  ? 33.039  -14.927 45.512 1.00 38.73  ? 34  ASN A CA  1 
ATOM   146  C  C   . ASN A  1  21  ? 32.665  -15.970 46.561 1.00 38.26  ? 34  ASN A C   1 
ATOM   147  O  O   . ASN A  1  21  ? 31.614  -16.575 46.469 1.00 38.32  ? 34  ASN A O   1 
ATOM   148  C  CB  . ASN A  1  21  ? 31.840  -14.409 44.731 1.00 38.80  ? 34  ASN A CB  1 
ATOM   149  C  CG  . ASN A  1  21  ? 30.945  -13.500 45.541 1.00 41.25  ? 34  ASN A CG  1 
ATOM   150  O  OD1 . ASN A  1  21  ? 31.152  -13.300 46.743 1.00 38.45  ? 34  ASN A OD1 1 
ATOM   151  N  ND2 . ASN A  1  21  ? 29.937  -12.938 44.890 1.00 41.30  ? 34  ASN A ND2 1 
ATOM   152  N  N   . ASP A  1  22  ? 33.543  -16.194 47.542 1.00 40.58  ? 35  ASP A N   1 
ATOM   153  C  CA  . ASP A  1  22  ? 33.422  -17.332 48.446 1.00 42.26  ? 35  ASP A CA  1 
ATOM   154  C  C   . ASP A  1  22  ? 33.335  -16.808 49.873 1.00 38.43  ? 35  ASP A C   1 
ATOM   155  O  O   . ASP A  1  22  ? 33.358  -15.603 50.072 1.00 41.66  ? 35  ASP A O   1 
ATOM   156  C  CB  . ASP A  1  22  ? 34.558  -18.333 48.255 1.00 43.55  ? 35  ASP A CB  1 
ATOM   157  C  CG  . ASP A  1  22  ? 35.975  -17.783 48.370 1.00 41.81  ? 35  ASP A CG  1 
ATOM   158  O  OD1 . ASP A  1  22  ? 36.190  -16.856 49.171 1.00 47.74  ? 35  ASP A OD1 1 
ATOM   159  O  OD2 . ASP A  1  22  ? 36.868  -18.316 47.680 1.00 48.32  ? 35  ASP A OD2 1 
ATOM   160  N  N   . ALA A  1  23  ? 33.276  -17.719 50.847 1.00 39.32  ? 36  ALA A N   1 
ATOM   161  C  CA  . ALA A  1  23  ? 32.918  -17.378 52.217 1.00 43.26  ? 36  ALA A CA  1 
ATOM   162  C  C   . ALA A  1  23  ? 34.019  -16.570 52.899 1.00 43.65  ? 36  ALA A C   1 
ATOM   163  O  O   . ALA A  1  23  ? 33.735  -15.782 53.790 1.00 46.53  ? 36  ALA A O   1 
ATOM   164  C  CB  . ALA A  1  23  ? 32.606  -18.642 52.997 1.00 42.99  ? 36  ALA A CB  1 
ATOM   165  N  N   . ASP A  1  24  ? 35.269  -16.784 52.479 1.00 44.96  ? 37  ASP A N   1 
ATOM   166  C  CA  . ASP A  1  24  ? 36.417  -16.098 53.044 1.00 44.22  ? 37  ASP A CA  1 
ATOM   167  C  C   . ASP A  1  24  ? 36.608  -14.716 52.407 1.00 41.45  ? 37  ASP A C   1 
ATOM   168  O  O   . ASP A  1  24  ? 37.404  -13.916 52.897 1.00 39.44  ? 37  ASP A O   1 
ATOM   169  C  CB  . ASP A  1  24  ? 37.660  -16.960 52.894 1.00 47.75  ? 37  ASP A CB  1 
ATOM   170  C  CG  . ASP A  1  24  ? 38.780  -16.703 53.888 1.00 49.55  ? 37  ASP A CG  1 
ATOM   171  O  OD1 . ASP A  1  24  ? 38.488  -16.689 55.097 1.00 52.45  ? 37  ASP A OD1 1 
ATOM   172  O  OD2 . ASP A  1  24  ? 39.926  -16.558 53.440 1.00 57.60  ? 37  ASP A OD2 1 
ATOM   173  N  N   . HIS A  1  25  ? 35.877  -14.433 51.318 1.00 41.34  ? 38  HIS A N   1 
ATOM   174  C  CA  . HIS A  1  25  ? 36.001  -13.180 50.586 1.00 36.64  ? 38  HIS A CA  1 
ATOM   175  C  C   . HIS A  1  25  ? 34.627  -12.538 50.390 1.00 33.35  ? 38  HIS A C   1 
ATOM   176  O  O   . HIS A  1  25  ? 34.212  -12.292 49.256 1.00 34.24  ? 38  HIS A O   1 
ATOM   177  C  CB  . HIS A  1  25  ? 36.739  -13.427 49.264 1.00 38.95  ? 38  HIS A CB  1 
ATOM   178  C  CG  . HIS A  1  25  ? 38.134  -13.918 49.451 1.00 40.62  ? 38  HIS A CG  1 
ATOM   179  N  ND1 . HIS A  1  25  ? 38.518  -15.234 49.353 1.00 38.15  ? 38  HIS A ND1 1 
ATOM   180  C  CD2 . HIS A  1  25  ? 39.242  -13.242 49.728 1.00 44.90  ? 38  HIS A CD2 1 
ATOM   181  C  CE1 . HIS A  1  25  ? 39.821  -15.329 49.566 1.00 45.16  ? 38  HIS A CE1 1 
ATOM   182  N  NE2 . HIS A  1  25  ? 40.287  -14.126 49.796 1.00 44.92  ? 38  HIS A NE2 1 
ATOM   183  N  N   . PRO A  1  26  ? 33.868  -12.238 51.473 1.00 32.73  ? 39  PRO A N   1 
ATOM   184  C  CA  . PRO A  1  26  ? 32.563  -11.577 51.339 1.00 33.46  ? 39  PRO A CA  1 
ATOM   185  C  C   . PRO A  1  26  ? 32.684  -10.099 50.970 1.00 36.57  ? 39  PRO A C   1 
ATOM   186  O  O   . PRO A  1  26  ? 33.594  -9.422  51.447 1.00 38.35  ? 39  PRO A O   1 
ATOM   187  C  CB  . PRO A  1  26  ? 31.948  -11.755 52.740 1.00 32.92  ? 39  PRO A CB  1 
ATOM   188  C  CG  . PRO A  1  26  ? 33.152  -11.754 53.666 1.00 30.87  ? 39  PRO A CG  1 
ATOM   189  C  CD  . PRO A  1  26  ? 34.227  -12.495 52.880 1.00 30.68  ? 39  PRO A CD  1 
ATOM   190  N  N   . TRP A  1  27  ? 31.763  -9.603  50.132 1.00 33.91  ? 40  TRP A N   1 
ATOM   191  C  CA  . TRP A  1  27  ? 31.571  -8.170  49.976 1.00 32.30  ? 40  TRP A CA  1 
ATOM   192  C  C   . TRP A  1  27  ? 31.218  -7.572  51.334 1.00 31.55  ? 40  TRP A C   1 
ATOM   193  O  O   . TRP A  1  27  ? 30.394  -8.141  52.054 1.00 31.69  ? 40  TRP A O   1 
ATOM   194  C  CB  . TRP A  1  27  ? 30.486  -7.862  48.927 1.00 30.84  ? 40  TRP A CB  1 
ATOM   195  C  CG  . TRP A  1  27  ? 30.315  -6.394  48.639 1.00 34.41  ? 40  TRP A CG  1 
ATOM   196  C  CD1 . TRP A  1  27  ? 30.981  -5.670  47.692 1.00 34.78  ? 40  TRP A CD1 1 
ATOM   197  C  CD2 . TRP A  1  27  ? 29.455  -5.454  49.332 1.00 36.71  ? 40  TRP A CD2 1 
ATOM   198  N  NE1 . TRP A  1  27  ? 30.569  -4.363  47.721 1.00 36.13  ? 40  TRP A NE1 1 
ATOM   199  C  CE2 . TRP A  1  27  ? 29.653  -4.194  48.726 1.00 36.03  ? 40  TRP A CE2 1 
ATOM   200  C  CE3 . TRP A  1  27  ? 28.553  -5.548  50.403 1.00 36.42  ? 40  TRP A CE3 1 
ATOM   201  C  CZ2 . TRP A  1  27  ? 28.985  -3.048  49.158 1.00 37.53  ? 40  TRP A CZ2 1 
ATOM   202  C  CZ3 . TRP A  1  27  ? 27.892  -4.414  50.827 1.00 35.61  ? 40  TRP A CZ3 1 
ATOM   203  C  CH2 . TRP A  1  27  ? 28.120  -3.176  50.223 1.00 36.64  ? 40  TRP A CH2 1 
ATOM   204  N  N   . GLN A  1  28  ? 31.878  -6.454  51.682 1.00 31.21  ? 41  GLN A N   1 
ATOM   205  C  CA  . GLN A  1  28  ? 31.531  -5.677  52.860 1.00 33.17  ? 41  GLN A CA  1 
ATOM   206  C  C   . GLN A  1  28  ? 31.471  -4.206  52.469 1.00 34.03  ? 41  GLN A C   1 
ATOM   207  O  O   . GLN A  1  28  ? 32.179  -3.783  51.559 1.00 31.72  ? 41  GLN A O   1 
ATOM   208  C  CB  . GLN A  1  28  ? 32.520  -5.907  54.005 1.00 34.55  ? 41  GLN A CB  1 
ATOM   209  C  CG  . GLN A  1  28  ? 32.511  -7.334  54.536 1.00 36.49  ? 41  GLN A CG  1 
ATOM   210  C  CD  . GLN A  1  28  ? 33.510  -7.557  55.649 1.00 36.62  ? 41  GLN A CD  1 
ATOM   211  O  OE1 . GLN A  1  28  ? 34.276  -6.663  56.033 1.00 33.98  ? 41  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A  1  28  ? 33.497  -8.768  56.183 1.00 37.50  ? 41  GLN A NE2 1 
ATOM   213  N  N   . PRO A  1  29  ? 30.612  -3.389  53.126 1.00 33.95  ? 42  PRO A N   1 
ATOM   214  C  CA  . PRO A  1  29  ? 30.581  -1.952  52.857 1.00 34.59  ? 42  PRO A CA  1 
ATOM   215  C  C   . PRO A  1  29  ? 31.846  -1.233  53.332 1.00 36.01  ? 42  PRO A C   1 
ATOM   216  O  O   . PRO A  1  29  ? 32.574  -1.721  54.198 1.00 33.48  ? 42  PRO A O   1 
ATOM   217  C  CB  . PRO A  1  29  ? 29.316  -1.495  53.608 1.00 34.95  ? 42  PRO A CB  1 
ATOM   218  C  CG  . PRO A  1  29  ? 29.166  -2.483  54.734 1.00 32.74  ? 42  PRO A CG  1 
ATOM   219  C  CD  . PRO A  1  29  ? 29.642  -3.799  54.151 1.00 32.15  ? 42  PRO A CD  1 
ATOM   220  N  N   . LEU A  1  30  ? 32.083  -0.051  52.757 1.00 39.55  ? 43  LEU A N   1 
ATOM   221  C  CA  . LEU A  1  30  ? 33.191  0.809   53.146 1.00 40.75  ? 43  LEU A CA  1 
ATOM   222  C  C   . LEU A  1  30  ? 33.017  1.293   54.582 1.00 41.27  ? 43  LEU A C   1 
ATOM   223  O  O   . LEU A  1  30  ? 31.917  1.632   54.993 1.00 43.51  ? 43  LEU A O   1 
ATOM   224  C  CB  . LEU A  1  30  ? 33.265  2.000   52.193 1.00 39.71  ? 43  LEU A CB  1 
ATOM   225  C  CG  . LEU A  1  30  ? 33.568  1.686   50.725 1.00 41.97  ? 43  LEU A CG  1 
ATOM   226  C  CD1 . LEU A  1  30  ? 33.836  3.002   50.012 1.00 36.95  ? 43  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A  1  30  ? 34.760  0.727   50.539 1.00 42.20  ? 43  LEU A CD2 1 
ATOM   228  N  N   . ARG A  1  31  ? 34.122  1.288   55.334 1.00 43.08  ? 44  ARG A N   1 
ATOM   229  C  CA  . ARG A  1  31  ? 34.231  1.952   56.626 1.00 47.08  ? 44  ARG A CA  1 
ATOM   230  C  C   . ARG A  1  31  ? 34.995  3.264   56.445 1.00 47.70  ? 44  ARG A C   1 
ATOM   231  O  O   . ARG A  1  31  ? 35.624  3.472   55.421 1.00 42.55  ? 44  ARG A O   1 
ATOM   232  C  CB  . ARG A  1  31  ? 35.016  1.091   57.621 1.00 45.86  ? 44  ARG A CB  1 
ATOM   233  C  CG  . ARG A  1  31  ? 34.631  -0.377  57.727 1.00 45.04  ? 44  ARG A CG  1 
ATOM   234  C  CD  . ARG A  1  31  ? 35.785  -1.234  58.224 1.00 48.35  ? 44  ARG A CD  1 
ATOM   235  N  NE  . ARG A  1  31  ? 36.974  -1.092  57.369 1.00 56.95  ? 44  ARG A NE  1 
ATOM   236  C  CZ  . ARG A  1  31  ? 38.088  -1.818  57.415 1.00 60.23  ? 44  ARG A CZ  1 
ATOM   237  N  NH1 . ARG A  1  31  ? 38.177  -2.846  58.237 1.00 67.37  ? 44  ARG A NH1 1 
ATOM   238  N  NH2 . ARG A  1  31  ? 39.096  -1.551  56.599 1.00 61.02  ? 44  ARG A NH2 1 
ATOM   239  N  N   . GLU A  1  32  ? 34.968  4.133   57.455 1.00 50.50  ? 45  GLU A N   1 
ATOM   240  C  CA  . GLU A  1  32  ? 35.658  5.413   57.388 1.00 59.23  ? 45  GLU A CA  1 
ATOM   241  C  C   . GLU A  1  32  ? 37.159  5.166   57.261 1.00 53.41  ? 45  GLU A C   1 
ATOM   242  O  O   . GLU A  1  32  ? 37.722  4.367   58.005 1.00 50.14  ? 45  GLU A O   1 
ATOM   243  C  CB  . GLU A  1  32  ? 35.265  6.251   58.607 1.00 73.51  ? 45  GLU A CB  1 
ATOM   244  C  CG  . GLU A  1  32  ? 35.773  7.692   58.577 1.00 86.51  ? 45  GLU A CG  1 
ATOM   245  C  CD  . GLU A  1  32  ? 36.880  8.031   59.566 1.00 99.69  ? 45  GLU A CD  1 
ATOM   246  O  OE1 . GLU A  1  32  ? 37.602  9.021   59.317 1.00 107.67 ? 45  GLU A OE1 1 
ATOM   247  O  OE2 . GLU A  1  32  ? 37.006  7.345   60.606 1.00 102.64 ? 45  GLU A OE2 1 
ATOM   248  N  N   . GLY A  1  33  ? 37.789  5.837   56.288 1.00 46.58  ? 46  GLY A N   1 
ATOM   249  C  CA  . GLY A  1  33  ? 39.217  5.694   56.043 1.00 47.01  ? 46  GLY A CA  1 
ATOM   250  C  C   . GLY A  1  33  ? 39.538  4.765   54.874 1.00 45.64  ? 46  GLY A C   1 
ATOM   251  O  O   . GLY A  1  33  ? 40.661  4.778   54.377 1.00 48.10  ? 46  GLY A O   1 
ATOM   252  N  N   . ASP A  1  34  ? 38.556  3.953   54.449 1.00 43.88  ? 47  ASP A N   1 
ATOM   253  C  CA  . ASP A  1  34  ? 38.757  3.001   53.366 1.00 44.47  ? 47  ASP A CA  1 
ATOM   254  C  C   . ASP A  1  34  ? 38.853  3.764   52.056 1.00 36.47  ? 47  ASP A C   1 
ATOM   255  O  O   . ASP A  1  34  ? 38.058  4.654   51.818 1.00 39.38  ? 47  ASP A O   1 
ATOM   256  C  CB  . ASP A  1  34  ? 37.648  1.963   53.293 1.00 46.55  ? 47  ASP A CB  1 
ATOM   257  C  CG  . ASP A  1  34  ? 37.613  0.944   54.427 1.00 44.81  ? 47  ASP A CG  1 
ATOM   258  O  OD1 . ASP A  1  34  ? 38.580  0.913   55.230 1.00 45.32  ? 47  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A  1  34  ? 36.613  0.194   54.502 1.00 41.86  ? 47  ASP A OD2 1 
ATOM   260  N  N   . ILE A  1  35  ? 39.818  3.391   51.218 1.00 34.14  ? 48  ILE A N   1 
ATOM   261  C  CA  . ILE A  1  35  ? 40.086  4.097   49.981 1.00 35.68  ? 48  ILE A CA  1 
ATOM   262  C  C   . ILE A  1  35  ? 39.702  3.234   48.790 1.00 34.42  ? 48  ILE A C   1 
ATOM   263  O  O   . ILE A  1  35  ? 40.001  2.048   48.753 1.00 33.38  ? 48  ILE A O   1 
ATOM   264  C  CB  . ILE A  1  35  ? 41.566  4.510   49.951 1.00 41.38  ? 48  ILE A CB  1 
ATOM   265  C  CG1 . ILE A  1  35  ? 41.807  5.581   51.008 1.00 45.89  ? 48  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A  1  35  ? 41.998  4.961   48.560 1.00 38.68  ? 48  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A  1  35  ? 43.258  5.800   51.288 1.00 54.12  ? 48  ILE A CD1 1 
ATOM   268  N  N   . ARG A  1  36  ? 39.011  3.867   47.837 1.00 34.84  ? 49  ARG A N   1 
ATOM   269  C  CA  . ARG A  1  36  ? 38.670  3.289   46.551 1.00 33.48  ? 49  ARG A CA  1 
ATOM   270  C  C   . ARG A  1  36  ? 39.038  4.334   45.508 1.00 32.80  ? 49  ARG A C   1 
ATOM   271  O  O   . ARG A  1  36  ? 39.247  5.483   45.855 1.00 33.77  ? 49  ARG A O   1 
ATOM   272  C  CB  . ARG A  1  36  ? 37.188  2.887   46.521 1.00 33.15  ? 49  ARG A CB  1 
ATOM   273  C  CG  . ARG A  1  36  ? 36.773  1.835   47.544 1.00 33.17  ? 49  ARG A CG  1 
ATOM   274  C  CD  . ARG A  1  36  ? 37.400  0.452   47.245 1.00 32.91  ? 49  ARG A CD  1 
ATOM   275  N  NE  . ARG A  1  36  ? 37.013  -0.583  48.217 1.00 31.26  ? 49  ARG A NE  1 
ATOM   276  C  CZ  . ARG A  1  36  ? 37.561  -0.767  49.417 1.00 31.71  ? 49  ARG A CZ  1 
ATOM   277  N  NH1 . ARG A  1  36  ? 38.560  -0.012  49.824 1.00 34.12  ? 49  ARG A NH1 1 
ATOM   278  N  NH2 . ARG A  1  36  ? 37.124  -1.717  50.218 1.00 32.01  ? 49  ARG A NH2 1 
ATOM   279  N  N   . GLY A  1  37  ? 39.142  3.936   44.236 1.00 35.10  ? 50  GLY A N   1 
ATOM   280  C  CA  . GLY A  1  37  ? 39.725  4.796   43.222 1.00 31.43  ? 50  GLY A CA  1 
ATOM   281  C  C   . GLY A  1  37  ? 39.138  4.544   41.842 1.00 30.60  ? 50  GLY A C   1 
ATOM   282  O  O   . GLY A  1  37  ? 38.005  4.112   41.718 1.00 31.81  ? 50  GLY A O   1 
ATOM   283  N  N   . PRO A  1  38  ? 39.909  4.812   40.768 1.00 32.89  ? 51  PRO A N   1 
ATOM   284  C  CA  . PRO A  1  38  ? 39.397  4.693   39.404 1.00 31.83  ? 51  PRO A CA  1 
ATOM   285  C  C   . PRO A  1  38  ? 39.406  3.292   38.791 1.00 33.25  ? 51  PRO A C   1 
ATOM   286  O  O   . PRO A  1  38  ? 38.873  3.123   37.692 1.00 33.81  ? 51  PRO A O   1 
ATOM   287  C  CB  . PRO A  1  38  ? 40.366  5.630   38.681 1.00 31.76  ? 51  PRO A CB  1 
ATOM   288  C  CG  . PRO A  1  38  ? 41.687  5.387   39.369 1.00 34.83  ? 51  PRO A CG  1 
ATOM   289  C  CD  . PRO A  1  38  ? 41.334  5.205   40.825 1.00 33.65  ? 51  PRO A CD  1 
ATOM   290  N  N   . CYS A  1  39  ? 40.030  2.315   39.477 1.00 31.92  ? 52  CYS A N   1 
ATOM   291  C  CA  . CYS A  1  39  ? 40.098  0.944   38.984 1.00 34.89  ? 52  CYS A CA  1 
ATOM   292  C  C   . CYS A  1  39  ? 38.992  0.081   39.590 1.00 30.09  ? 52  CYS A C   1 
ATOM   293  O  O   . CYS A  1  39  ? 39.009  -0.222  40.782 1.00 30.05  ? 52  CYS A O   1 
ATOM   294  C  CB  . CYS A  1  39  ? 41.424  0.260   39.292 1.00 35.70  ? 52  CYS A CB  1 
ATOM   295  S  SG  . CYS A  1  39  ? 41.600  -1.371  38.515 1.00 34.55  ? 52  CYS A SG  1 
ATOM   296  N  N   . PRO A  1  40  ? 38.022  -0.374  38.774 1.00 30.76  ? 53  PRO A N   1 
ATOM   297  C  CA  . PRO A  1  40  ? 36.966  -1.258  39.269 1.00 32.65  ? 53  PRO A CA  1 
ATOM   298  C  C   . PRO A  1  40  ? 37.474  -2.629  39.713 1.00 33.00  ? 53  PRO A C   1 
ATOM   299  O  O   . PRO A  1  40  ? 36.896  -3.247  40.605 1.00 34.36  ? 53  PRO A O   1 
ATOM   300  C  CB  . PRO A  1  40  ? 35.964  -1.346  38.087 1.00 34.60  ? 53  PRO A CB  1 
ATOM   301  C  CG  . PRO A  1  40  ? 36.787  -0.981  36.862 1.00 34.80  ? 53  PRO A CG  1 
ATOM   302  C  CD  . PRO A  1  40  ? 37.878  -0.038  37.347 1.00 32.60  ? 53  PRO A CD  1 
ATOM   303  N  N   . GLY A  1  41  ? 38.569  -3.095  39.099 1.00 32.42  ? 54  GLY A N   1 
ATOM   304  C  CA  . GLY A  1  41  ? 39.162  -4.374  39.460 1.00 31.11  ? 54  GLY A CA  1 
ATOM   305  C  C   . GLY A  1  41  ? 39.712  -4.366  40.884 1.00 31.73  ? 54  GLY A C   1 
ATOM   306  O  O   . GLY A  1  41  ? 39.327  -5.192  41.712 1.00 30.85  ? 54  GLY A O   1 
ATOM   307  N  N   . LEU A  1  42  ? 40.591  -3.401  41.168 1.00 29.38  ? 55  LEU A N   1 
ATOM   308  C  CA  . LEU A  1  42  ? 41.178  -3.277  42.487 1.00 30.85  ? 55  LEU A CA  1 
ATOM   309  C  C   . LEU A  1  42  ? 40.113  -2.922  43.529 1.00 30.05  ? 55  LEU A C   1 
ATOM   310  O  O   . LEU A  1  42  ? 40.203  -3.378  44.666 1.00 30.18  ? 55  LEU A O   1 
ATOM   311  C  CB  . LEU A  1  42  ? 42.297  -2.239  42.424 1.00 31.52  ? 55  LEU A CB  1 
ATOM   312  C  CG  . LEU A  1  42  ? 43.468  -2.574  41.499 1.00 33.93  ? 55  LEU A CG  1 
ATOM   313  C  CD1 . LEU A  1  42  ? 44.445  -1.410  41.387 1.00 33.65  ? 55  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A  1  42  ? 44.197  -3.824  41.944 1.00 34.86  ? 55  LEU A CD2 1 
ATOM   315  N  N   . ASN A  1  43  ? 39.137  -2.087  43.152 1.00 31.67  ? 56  ASN A N   1 
ATOM   316  C  CA  . ASN A  1  43  ? 38.044  -1.715  44.041 1.00 33.16  ? 56  ASN A CA  1 
ATOM   317  C  C   . ASN A  1  43  ? 37.283  -2.956  44.510 1.00 32.64  ? 56  ASN A C   1 
ATOM   318  O  O   . ASN A  1  43  ? 37.033  -3.129  45.712 1.00 29.17  ? 56  ASN A O   1 
ATOM   319  C  CB  . ASN A  1  43  ? 37.076  -0.733  43.383 1.00 32.60  ? 56  ASN A CB  1 
ATOM   320  C  CG  . ASN A  1  43  ? 37.615  0.675   43.260 1.00 33.87  ? 56  ASN A CG  1 
ATOM   321  O  OD1 . ASN A  1  43  ? 38.608  1.041   43.903 1.00 35.14  ? 56  ASN A OD1 1 
ATOM   322  N  ND2 . ASN A  1  43  ? 36.946  1.498   42.467 1.00 31.59  ? 56  ASN A ND2 1 
ATOM   323  N  N   . THR A  1  44  ? 36.936  -3.826  43.553 1.00 32.45  ? 57  THR A N   1 
ATOM   324  C  CA  . THR A  1  44  ? 36.204  -5.051  43.858 1.00 34.00  ? 57  THR A CA  1 
ATOM   325  C  C   . THR A  1  44  ? 37.055  -5.973  44.736 1.00 33.21  ? 57  THR A C   1 
ATOM   326  O  O   . THR A  1  44  ? 36.542  -6.560  45.681 1.00 34.08  ? 57  THR A O   1 
ATOM   327  C  CB  . THR A  1  44  ? 35.758  -5.729  42.560 1.00 34.42  ? 57  THR A CB  1 
ATOM   328  O  OG1 . THR A  1  44  ? 34.984  -4.745  41.882 1.00 31.44  ? 57  THR A OG1 1 
ATOM   329  C  CG2 . THR A  1  44  ? 34.906  -6.967  42.785 1.00 35.20  ? 57  THR A CG2 1 
ATOM   330  N  N   . LEU A  1  45  ? 38.359  -6.079  44.447 1.00 33.23  ? 58  LEU A N   1 
ATOM   331  C  CA  . LEU A  1  45  ? 39.237  -6.955  45.212 1.00 33.25  ? 58  LEU A CA  1 
ATOM   332  C  C   . LEU A  1  45  ? 39.352  -6.508  46.673 1.00 31.82  ? 58  LEU A C   1 
ATOM   333  O  O   . LEU A  1  45  ? 39.418  -7.344  47.575 1.00 29.48  ? 58  LEU A O   1 
ATOM   334  C  CB  . LEU A  1  45  ? 40.606  -7.023  44.540 1.00 35.16  ? 58  LEU A CB  1 
ATOM   335  C  CG  . LEU A  1  45  ? 40.648  -7.759  43.200 1.00 34.15  ? 58  LEU A CG  1 
ATOM   336  C  CD1 . LEU A  1  45  ? 41.958  -7.480  42.470 1.00 32.64  ? 58  LEU A CD1 1 
ATOM   337  C  CD2 . LEU A  1  45  ? 40.467  -9.248  43.381 1.00 33.22  ? 58  LEU A CD2 1 
ATOM   338  N  N   . ALA A  1  46  ? 39.388  -5.194  46.900 1.00 30.53  ? 59  ALA A N   1 
ATOM   339  C  CA  . ALA A  1  46  ? 39.447  -4.635  48.243 1.00 32.14  ? 59  ALA A CA  1 
ATOM   340  C  C   . ALA A  1  46  ? 38.121  -4.840  48.971 1.00 28.28  ? 59  ALA A C   1 
ATOM   341  O  O   . ALA A  1  46  ? 38.105  -5.177  50.145 1.00 31.17  ? 59  ALA A O   1 
ATOM   342  C  CB  . ALA A  1  46  ? 39.809  -3.158  48.162 1.00 33.33  ? 59  ALA A CB  1 
ATOM   343  N  N   . SER A  1  47  ? 37.010  -4.672  48.258 1.00 28.83  ? 60  SER A N   1 
ATOM   344  C  CA  . SER A  1  47  ? 35.701  -4.764  48.883 1.00 31.18  ? 60  SER A CA  1 
ATOM   345  C  C   . SER A  1  47  ? 35.313  -6.221  49.154 1.00 30.91  ? 60  SER A C   1 
ATOM   346  O  O   . SER A  1  47  ? 34.358  -6.457  49.878 1.00 32.38  ? 60  SER A O   1 
ATOM   347  C  CB  . SER A  1  47  ? 34.651  -4.011  48.086 1.00 29.65  ? 60  SER A CB  1 
ATOM   348  O  OG  . SER A  1  47  ? 34.755  -2.614  48.329 1.00 28.70  ? 60  SER A OG  1 
ATOM   349  N  N   . HIS A  1  48  ? 36.083  -7.178  48.624 1.00 33.38  ? 61  HIS A N   1 
ATOM   350  C  CA  . HIS A  1  48  ? 35.919  -8.592  48.933 1.00 33.30  ? 61  HIS A CA  1 
ATOM   351  C  C   . HIS A  1  48  ? 37.061  -9.140  49.790 1.00 32.58  ? 61  HIS A C   1 
ATOM   352  O  O   . HIS A  1  48  ? 37.063  -10.316 50.119 1.00 31.88  ? 61  HIS A O   1 
ATOM   353  C  CB  . HIS A  1  48  ? 35.790  -9.411  47.642 1.00 32.13  ? 61  HIS A CB  1 
ATOM   354  C  CG  . HIS A  1  48  ? 34.429  -9.364  47.016 1.00 34.08  ? 61  HIS A CG  1 
ATOM   355  N  ND1 . HIS A  1  48  ? 33.456  -10.312 47.270 1.00 33.47  ? 61  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A  1  48  ? 33.880  -8.499  46.140 1.00 34.82  ? 61  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A  1  48  ? 32.372  -10.018 46.564 1.00 35.18  ? 61  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A  1  48  ? 32.604  -8.924  45.871 1.00 32.83  ? 61  HIS A NE2 1 
ATOM   359  N  N   . GLY A  1  49  ? 38.057  -8.321  50.132 1.00 32.47  ? 62  GLY A N   1 
ATOM   360  C  CA  . GLY A  1  49  ? 39.134  -8.772  51.008 1.00 31.60  ? 62  GLY A CA  1 
ATOM   361  C  C   . GLY A  1  49  ? 40.239  -9.578  50.308 1.00 31.57  ? 62  GLY A C   1 
ATOM   362  O  O   . GLY A  1  49  ? 41.073  -10.167 50.974 1.00 36.46  ? 62  GLY A O   1 
ATOM   363  N  N   . TYR A  1  50  ? 40.281  -9.602  48.974 1.00 33.27  ? 63  TYR A N   1 
ATOM   364  C  CA  . TYR A  1  50  ? 41.462  -10.068 48.257 1.00 34.31  ? 63  TYR A CA  1 
ATOM   365  C  C   . TYR A  1  50  ? 42.631  -9.112  48.499 1.00 36.21  ? 63  TYR A C   1 
ATOM   366  O  O   . TYR A  1  50  ? 43.768  -9.555  48.598 1.00 35.54  ? 63  TYR A O   1 
ATOM   367  C  CB  . TYR A  1  50  ? 41.207  -10.263 46.756 1.00 33.88  ? 63  TYR A CB  1 
ATOM   368  C  CG  . TYR A  1  50  ? 40.460  -11.561 46.482 1.00 37.31  ? 63  TYR A CG  1 
ATOM   369  C  CD1 . TYR A  1  50  ? 41.144  -12.776 46.428 1.00 37.97  ? 63  TYR A CD1 1 
ATOM   370  C  CD2 . TYR A  1  50  ? 39.071  -11.586 46.351 1.00 34.64  ? 63  TYR A CD2 1 
ATOM   371  C  CE1 . TYR A  1  50  ? 40.470  -13.974 46.241 1.00 38.47  ? 63  TYR A CE1 1 
ATOM   372  C  CE2 . TYR A  1  50  ? 38.393  -12.774 46.136 1.00 35.15  ? 63  TYR A CE2 1 
ATOM   373  C  CZ  . TYR A  1  50  ? 39.093  -13.965 46.084 1.00 38.74  ? 63  TYR A CZ  1 
ATOM   374  O  OH  . TYR A  1  50  ? 38.427  -15.125 45.887 1.00 39.25  ? 63  TYR A OH  1 
ATOM   375  N  N   . LEU A  1  51  ? 42.329  -7.805  48.554 1.00 39.20  ? 64  LEU A N   1 
ATOM   376  C  CA  . LEU A  1  51  ? 43.248  -6.776  49.005 1.00 38.00  ? 64  LEU A CA  1 
ATOM   377  C  C   . LEU A  1  51  ? 42.827  -6.348  50.401 1.00 37.36  ? 64  LEU A C   1 
ATOM   378  O  O   . LEU A  1  51  ? 41.692  -6.582  50.800 1.00 35.19  ? 64  LEU A O   1 
ATOM   379  C  CB  . LEU A  1  51  ? 43.233  -5.569  48.071 1.00 39.88  ? 64  LEU A CB  1 
ATOM   380  C  CG  . LEU A  1  51  ? 43.892  -5.765  46.707 1.00 42.74  ? 64  LEU A CG  1 
ATOM   381  C  CD1 . LEU A  1  51  ? 43.556  -4.589  45.825 1.00 41.48  ? 64  LEU A CD1 1 
ATOM   382  C  CD2 . LEU A  1  51  ? 45.397  -5.943  46.855 1.00 44.91  ? 64  LEU A CD2 1 
ATOM   383  N  N   . PRO A  1  52  ? 43.711  -5.678  51.168 1.00 35.12  ? 65  PRO A N   1 
ATOM   384  C  CA  . PRO A  1  52  ? 43.289  -5.008  52.395 1.00 34.09  ? 65  PRO A CA  1 
ATOM   385  C  C   . PRO A  1  52  ? 42.097  -4.087  52.130 1.00 34.83  ? 65  PRO A C   1 
ATOM   386  O  O   . PRO A  1  52  ? 42.047  -3.385  51.114 1.00 34.44  ? 65  PRO A O   1 
ATOM   387  C  CB  . PRO A  1  52  ? 44.563  -4.252  52.815 1.00 35.93  ? 65  PRO A CB  1 
ATOM   388  C  CG  . PRO A  1  52  ? 45.692  -5.098  52.239 1.00 35.03  ? 65  PRO A CG  1 
ATOM   389  C  CD  . PRO A  1  52  ? 45.152  -5.538  50.893 1.00 36.03  ? 65  PRO A CD  1 
ATOM   390  N  N   . ARG A  1  53  ? 41.111  -4.123  53.035 1.00 36.54  ? 66  ARG A N   1 
ATOM   391  C  CA  . ARG A  1  53  ? 39.818  -3.510  52.771 1.00 33.37  ? 66  ARG A CA  1 
ATOM   392  C  C   . ARG A  1  53  ? 39.906  -1.982  52.832 1.00 33.17  ? 66  ARG A C   1 
ATOM   393  O  O   . ARG A  1  53  ? 39.005  -1.290  52.364 1.00 30.78  ? 66  ARG A O   1 
ATOM   394  C  CB  . ARG A  1  53  ? 38.747  -4.051  53.725 1.00 34.86  ? 66  ARG A CB  1 
ATOM   395  C  CG  . ARG A  1  53  ? 38.450  -5.527  53.512 1.00 35.39  ? 66  ARG A CG  1 
ATOM   396  C  CD  . ARG A  1  53  ? 37.276  -6.003  54.347 1.00 37.80  ? 66  ARG A CD  1 
ATOM   397  N  NE  . ARG A  1  53  ? 36.961  -7.412  54.090 1.00 40.10  ? 66  ARG A NE  1 
ATOM   398  C  CZ  . ARG A  1  53  ? 36.115  -7.876  53.177 1.00 37.73  ? 66  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A  1  53  ? 35.473  -7.053  52.360 1.00 35.49  ? 66  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A  1  53  ? 35.936  -9.179  53.076 1.00 37.60  ? 66  ARG A NH2 1 
ATOM   401  N  N   . ASP A  1  54  ? 41.004  -1.459  53.382 1.00 33.64  ? 67  ASP A N   1 
ATOM   402  C  CA  . ASP A  1  54  ? 41.246  -0.027  53.434 1.00 33.60  ? 67  ASP A CA  1 
ATOM   403  C  C   . ASP A  1  54  ? 41.817  0.506   52.126 1.00 32.14  ? 67  ASP A C   1 
ATOM   404  O  O   . ASP A  1  54  ? 41.912  1.712   51.960 1.00 36.58  ? 67  ASP A O   1 
ATOM   405  C  CB  . ASP A  1  54  ? 42.100  0.347   54.629 1.00 37.60  ? 67  ASP A CB  1 
ATOM   406  C  CG  . ASP A  1  54  ? 43.510  -0.203  54.654 1.00 38.01  ? 67  ASP A CG  1 
ATOM   407  O  OD1 . ASP A  1  54  ? 43.925  -0.824  53.662 1.00 43.00  ? 67  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A  1  54  ? 44.158  -0.003  55.689 1.00 47.65  ? 67  ASP A OD2 1 
ATOM   409  N  N   . GLY A  1  55  ? 42.170  -0.371  51.183 1.00 35.13  ? 68  GLY A N   1 
ATOM   410  C  CA  . GLY A  1  55  ? 42.526  0.065   49.836 1.00 35.44  ? 68  GLY A CA  1 
ATOM   411  C  C   . GLY A  1  55  ? 43.976  0.533   49.726 1.00 34.55  ? 68  GLY A C   1 
ATOM   412  O  O   . GLY A  1  55  ? 44.323  1.248   48.788 1.00 31.47  ? 68  GLY A O   1 
ATOM   413  N  N   . VAL A  1  56  ? 44.808  0.107   50.684 1.00 34.16  ? 69  VAL A N   1 
ATOM   414  C  CA  . VAL A  1  56  ? 46.240  0.367   50.683 1.00 36.58  ? 69  VAL A CA  1 
ATOM   415  C  C   . VAL A  1  56  ? 46.953  -0.974  50.801 1.00 34.53  ? 69  VAL A C   1 
ATOM   416  O  O   . VAL A  1  56  ? 46.689  -1.709  51.752 1.00 34.34  ? 69  VAL A O   1 
ATOM   417  C  CB  . VAL A  1  56  ? 46.612  1.291   51.863 1.00 37.70  ? 69  VAL A CB  1 
ATOM   418  C  CG1 . VAL A  1  56  ? 48.116  1.514   51.967 1.00 38.81  ? 69  VAL A CG1 1 
ATOM   419  C  CG2 . VAL A  1  56  ? 45.875  2.619   51.774 1.00 38.05  ? 69  VAL A CG2 1 
ATOM   420  N  N   . ALA A  1  57  ? 47.871  -1.253  49.868 1.00 34.57  ? 70  ALA A N   1 
ATOM   421  C  CA  . ALA A  1  57  ? 48.504  -2.566  49.763 1.00 34.11  ? 70  ALA A CA  1 
ATOM   422  C  C   . ALA A  1  57  ? 49.938  -2.459  49.252 1.00 33.87  ? 70  ALA A C   1 
ATOM   423  O  O   . ALA A  1  57  ? 50.326  -1.444  48.695 1.00 37.12  ? 70  ALA A O   1 
ATOM   424  C  CB  . ALA A  1  57  ? 47.692  -3.398  48.810 1.00 33.52  ? 70  ALA A CB  1 
ATOM   425  N  N   . THR A  1  58  ? 50.709  -3.538  49.392 1.00 34.00  ? 71  THR A N   1 
ATOM   426  C  CA  . THR A  1  58  ? 52.032  -3.629  48.797 1.00 35.35  ? 71  THR A CA  1 
ATOM   427  C  C   . THR A  1  58  ? 51.870  -4.025  47.339 1.00 35.32  ? 71  THR A C   1 
ATOM   428  O  O   . THR A  1  58  ? 50.835  -4.563  46.973 1.00 38.46  ? 71  THR A O   1 
ATOM   429  C  CB  . THR A  1  58  ? 52.916  -4.634  49.538 1.00 36.30  ? 71  THR A CB  1 
ATOM   430  O  OG1 . THR A  1  58  ? 52.399  -5.929  49.264 1.00 41.68  ? 71  THR A OG1 1 
ATOM   431  C  CG2 . THR A  1  58  ? 52.969  -4.397  51.036 1.00 35.20  ? 71  THR A CG2 1 
ATOM   432  N  N   . PRO A  1  59  ? 52.865  -3.767  46.464 1.00 36.87  ? 72  PRO A N   1 
ATOM   433  C  CA  . PRO A  1  59  ? 52.847  -4.307  45.105 1.00 37.98  ? 72  PRO A CA  1 
ATOM   434  C  C   . PRO A  1  59  ? 52.637  -5.824  45.055 1.00 37.19  ? 72  PRO A C   1 
ATOM   435  O  O   . PRO A  1  59  ? 51.897  -6.312  44.209 1.00 35.37  ? 72  PRO A O   1 
ATOM   436  C  CB  . PRO A  1  59  ? 54.225  -3.881  44.538 1.00 37.23  ? 72  PRO A CB  1 
ATOM   437  C  CG  . PRO A  1  59  ? 54.536  -2.615  45.302 1.00 36.33  ? 72  PRO A CG  1 
ATOM   438  C  CD  . PRO A  1  59  ? 54.004  -2.866  46.695 1.00 37.53  ? 72  PRO A CD  1 
ATOM   439  N  N   . ALA A  1  60  ? 53.309  -6.559  45.944 1.00 34.35  ? 73  ALA A N   1 
ATOM   440  C  CA  . ALA A  1  60  ? 53.185  -8.010  45.989 1.00 36.99  ? 73  ALA A CA  1 
ATOM   441  C  C   . ALA A  1  60  ? 51.747  -8.429  46.291 1.00 33.86  ? 73  ALA A C   1 
ATOM   442  O  O   . ALA A  1  60  ? 51.244  -9.337  45.656 1.00 33.12  ? 73  ALA A O   1 
ATOM   443  C  CB  . ALA A  1  60  ? 54.149  -8.598  46.995 1.00 37.85  ? 73  ALA A CB  1 
ATOM   444  N  N   . GLN A  1  61  ? 51.072  -7.730  47.212 1.00 34.99  ? 74  GLN A N   1 
ATOM   445  C  CA  . GLN A  1  61  ? 49.680  -8.018  47.538 1.00 35.54  ? 74  GLN A CA  1 
ATOM   446  C  C   . GLN A  1  61  ? 48.753  -7.775  46.347 1.00 36.67  ? 74  GLN A C   1 
ATOM   447  O  O   . GLN A  1  61  ? 47.810  -8.544  46.136 1.00 37.72  ? 74  GLN A O   1 
ATOM   448  C  CB  . GLN A  1  61  ? 49.212  -7.206  48.732 1.00 34.65  ? 74  GLN A CB  1 
ATOM   449  C  CG  . GLN A  1  61  ? 49.799  -7.676  50.054 1.00 36.55  ? 74  GLN A CG  1 
ATOM   450  C  CD  . GLN A  1  61  ? 49.401  -6.781  51.205 1.00 40.17  ? 74  GLN A CD  1 
ATOM   451  O  OE1 . GLN A  1  61  ? 49.457  -5.554  51.110 1.00 44.32  ? 74  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A  1  61  ? 48.969  -7.378  52.302 1.00 42.62  ? 74  GLN A NE2 1 
ATOM   453  N  N   . ILE A  1  62  ? 49.045  -6.732  45.559 1.00 38.03  ? 75  ILE A N   1 
ATOM   454  C  CA  . ILE A  1  62  ? 48.228  -6.372  44.410 1.00 38.31  ? 75  ILE A CA  1 
ATOM   455  C  C   . ILE A  1  62  ? 48.348  -7.427  43.319 1.00 35.67  ? 75  ILE A C   1 
ATOM   456  O  O   . ILE A  1  62  ? 47.345  -7.788  42.704 1.00 33.23  ? 75  ILE A O   1 
ATOM   457  C  CB  . ILE A  1  62  ? 48.584  -4.962  43.907 1.00 38.86  ? 75  ILE A CB  1 
ATOM   458  C  CG1 . ILE A  1  62  ? 48.202  -3.917  44.962 1.00 41.09  ? 75  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A  1  62  ? 47.943  -4.660  42.548 1.00 37.37  ? 75  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A  1  62  ? 48.822  -2.547  44.740 1.00 42.24  ? 75  ILE A CD1 1 
ATOM   461  N  N   . ILE A  1  63  ? 49.570  -7.917  43.087 1.00 36.13  ? 76  ILE A N   1 
ATOM   462  C  CA  . ILE A  1  63  ? 49.792  -8.929  42.070 1.00 38.15  ? 76  ILE A CA  1 
ATOM   463  C  C   . ILE A  1  63  ? 49.076  -10.217 42.468 1.00 34.86  ? 76  ILE A C   1 
ATOM   464  O  O   . ILE A  1  63  ? 48.367  -10.780 41.644 1.00 35.84  ? 76  ILE A O   1 
ATOM   465  C  CB  . ILE A  1  63  ? 51.297  -9.116  41.800 1.00 38.68  ? 76  ILE A CB  1 
ATOM   466  C  CG1 . ILE A  1  63  ? 51.849  -7.897  41.055 1.00 38.80  ? 76  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A  1  63  ? 51.587  -10.402 41.026 1.00 37.25  ? 76  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A  1  63  ? 53.315  -7.608  41.334 1.00 39.87  ? 76  ILE A CD1 1 
ATOM   469  N  N   . THR A  1  64  ? 49.229  -10.661 43.719 1.00 37.11  ? 77  THR A N   1 
ATOM   470  C  CA  A THR A  1  64  ? 48.605  -11.899 44.158 0.50 37.22  ? 77  THR A CA  1 
ATOM   471  C  CA  B THR A  1  64  ? 48.605  -11.902 44.158 0.50 39.17  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A  1  64  ? 47.084  -11.775 44.019 1.00 35.07  ? 77  THR A C   1 
ATOM   473  O  O   . THR A  1  64  ? 46.451  -12.667 43.489 1.00 35.33  ? 77  THR A O   1 
ATOM   474  C  CB  A THR A  1  64  ? 49.050  -12.246 45.581 0.50 36.45  ? 77  THR A CB  1 
ATOM   475  C  CB  B THR A  1  64  ? 49.055  -12.278 45.574 0.50 42.24  ? 77  THR A CB  1 
ATOM   476  O  OG1 A THR A  1  64  ? 48.649  -11.144 46.385 0.50 46.76  ? 77  THR A OG1 1 
ATOM   477  O  OG1 B THR A  1  64  ? 48.362  -13.448 46.015 0.50 41.34  ? 77  THR A OG1 1 
ATOM   478  C  CG2 A THR A  1  64  ? 50.547  -12.445 45.716 0.50 31.25  ? 77  THR A CG2 1 
ATOM   479  C  CG2 B THR A  1  64  ? 48.656  -11.262 46.621 0.50 47.87  ? 77  THR A CG2 1 
ATOM   480  N  N   . ALA A  1  65  ? 46.509  -10.635 44.444 1.00 37.34  ? 78  ALA A N   1 
ATOM   481  C  CA  . ALA A  1  65  ? 45.062  -10.409 44.440 1.00 35.17  ? 78  ALA A CA  1 
ATOM   482  C  C   . ALA A  1  65  ? 44.476  -10.412 43.031 1.00 34.70  ? 78  ALA A C   1 
ATOM   483  O  O   . ALA A  1  65  ? 43.424  -11.018 42.806 1.00 36.44  ? 78  ALA A O   1 
ATOM   484  C  CB  . ALA A  1  65  ? 44.724  -9.118  45.145 1.00 35.92  ? 78  ALA A CB  1 
ATOM   485  N  N   . THR A  1  66  ? 45.140  -9.735  42.085 1.00 34.22  ? 79  THR A N   1 
ATOM   486  C  CA  . THR A  1  66  ? 44.660  -9.687  40.709 1.00 34.49  ? 79  THR A CA  1 
ATOM   487  C  C   . THR A  1  66  ? 44.695  -11.079 40.084 1.00 34.50  ? 79  THR A C   1 
ATOM   488  O  O   . THR A  1  66  ? 43.844  -11.385 39.251 1.00 35.84  ? 79  THR A O   1 
ATOM   489  C  CB  . THR A  1  66  ? 45.450  -8.688  39.857 1.00 38.62  ? 79  THR A CB  1 
ATOM   490  O  OG1 . THR A  1  66  ? 46.833  -9.045  39.843 1.00 38.72  ? 79  THR A OG1 1 
ATOM   491  C  CG2 . THR A  1  66  ? 45.251  -7.262  40.340 1.00 37.84  ? 79  THR A CG2 1 
ATOM   492  N  N   . GLN A  1  67  ? 45.681  -11.898 40.470 1.00 34.71  ? 80  GLN A N   1 
ATOM   493  C  CA  . GLN A  1  67  ? 45.803  -13.265 39.982 1.00 38.18  ? 80  GLN A CA  1 
ATOM   494  C  C   . GLN A  1  67  ? 44.747  -14.170 40.623 1.00 35.24  ? 80  GLN A C   1 
ATOM   495  O  O   . GLN A  1  67  ? 44.049  -14.888 39.924 1.00 37.68  ? 80  GLN A O   1 
ATOM   496  C  CB  . GLN A  1  67  ? 47.224  -13.776 40.242 1.00 37.63  ? 80  GLN A CB  1 
ATOM   497  C  CG  . GLN A  1  67  ? 48.285  -13.028 39.433 1.00 41.17  ? 80  GLN A CG  1 
ATOM   498  C  CD  . GLN A  1  67  ? 49.718  -13.497 39.621 1.00 39.53  ? 80  GLN A CD  1 
ATOM   499  O  OE1 . GLN A  1  67  ? 50.550  -13.292 38.737 1.00 41.09  ? 80  GLN A OE1 1 
ATOM   500  N  NE2 . GLN A  1  67  ? 50.040  -14.157 40.725 1.00 39.87  ? 80  GLN A NE2 1 
ATOM   501  N  N   . GLU A  1  68  ? 44.643  -14.137 41.951 1.00 36.35  ? 81  GLU A N   1 
ATOM   502  C  CA  . GLU A  1  68  ? 43.724  -14.984 42.694 1.00 40.59  ? 81  GLU A CA  1 
ATOM   503  C  C   . GLU A  1  68  ? 42.272  -14.667 42.322 1.00 40.07  ? 81  GLU A C   1 
ATOM   504  O  O   . GLU A  1  68  ? 41.492  -15.582 42.055 1.00 42.95  ? 81  GLU A O   1 
ATOM   505  C  CB  . GLU A  1  68  ? 43.934  -14.827 44.200 1.00 38.82  ? 81  GLU A CB  1 
ATOM   506  C  CG  . GLU A  1  68  ? 45.209  -15.480 44.714 1.00 48.82  ? 81  GLU A CG  1 
ATOM   507  C  CD  . GLU A  1  68  ? 45.399  -16.938 44.319 1.00 57.02  ? 81  GLU A CD  1 
ATOM   508  O  OE1 . GLU A  1  68  ? 46.476  -17.266 43.750 1.00 54.39  ? 81  GLU A OE1 1 
ATOM   509  O  OE2 . GLU A  1  68  ? 44.460  -17.734 44.575 1.00 63.58  ? 81  GLU A OE2 1 
ATOM   510  N  N   . GLY A  1  69  ? 41.936  -13.370 42.300 1.00 38.67  ? 82  GLY A N   1 
ATOM   511  C  CA  . GLY A  1  69  ? 40.566  -12.916 42.150 1.00 36.51  ? 82  GLY A CA  1 
ATOM   512  C  C   . GLY A  1  69  ? 40.065  -12.973 40.708 1.00 35.53  ? 82  GLY A C   1 
ATOM   513  O  O   . GLY A  1  69  ? 38.887  -13.248 40.504 1.00 34.25  ? 82  GLY A O   1 
ATOM   514  N  N   . PHE A  1  70  ? 40.935  -12.661 39.728 1.00 36.99  ? 83  PHE A N   1 
ATOM   515  C  CA  . PHE A  1  70  ? 40.505  -12.472 38.347 1.00 36.83  ? 83  PHE A CA  1 
ATOM   516  C  C   . PHE A  1  70  ? 41.310  -13.294 37.332 1.00 34.19  ? 83  PHE A C   1 
ATOM   517  O  O   . PHE A  1  70  ? 40.975  -13.281 36.154 1.00 34.50  ? 83  PHE A O   1 
ATOM   518  C  CB  . PHE A  1  70  ? 40.582  -10.981 37.992 1.00 37.38  ? 83  PHE A CB  1 
ATOM   519  C  CG  . PHE A  1  70  ? 39.455  -10.095 38.513 1.00 38.08  ? 83  PHE A CG  1 
ATOM   520  C  CD1 . PHE A  1  70  ? 38.176  -10.172 37.970 1.00 40.99  ? 83  PHE A CD1 1 
ATOM   521  C  CD2 . PHE A  1  70  ? 39.675  -9.161  39.518 1.00 36.37  ? 83  PHE A CD2 1 
ATOM   522  C  CE1 . PHE A  1  70  ? 37.151  -9.356  38.433 1.00 38.98  ? 83  PHE A CE1 1 
ATOM   523  C  CE2 . PHE A  1  70  ? 38.648  -8.350  39.967 1.00 36.57  ? 83  PHE A CE2 1 
ATOM   524  C  CZ  . PHE A  1  70  ? 37.394  -8.439  39.418 1.00 36.71  ? 83  PHE A CZ  1 
ATOM   525  N  N   . ASN A  1  71  ? 42.369  -13.995 37.764 1.00 35.33  ? 84  ASN A N   1 
ATOM   526  C  CA  . ASN A  1  71  ? 43.297  -14.668 36.858 1.00 34.67  ? 84  ASN A CA  1 
ATOM   527  C  C   . ASN A  1  71  ? 43.966  -13.667 35.908 1.00 32.89  ? 84  ASN A C   1 
ATOM   528  O  O   . ASN A  1  71  ? 44.215  -13.969 34.746 1.00 31.96  ? 84  ASN A O   1 
ATOM   529  C  CB  . ASN A  1  71  ? 42.613  -15.788 36.074 1.00 37.02  ? 84  ASN A CB  1 
ATOM   530  C  CG  . ASN A  1  71  ? 43.466  -17.029 35.942 1.00 39.10  ? 84  ASN A CG  1 
ATOM   531  O  OD1 . ASN A  1  71  ? 44.677  -17.007 36.198 1.00 41.89  ? 84  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A  1  71  ? 42.844  -18.138 35.575 1.00 42.09  ? 84  ASN A ND2 1 
ATOM   533  N  N   . PHE A  1  72  ? 44.256  -12.451 36.385 1.00 34.74  ? 85  PHE A N   1 
ATOM   534  C  CA  . PHE A  1  72  ? 45.047  -11.501 35.609 1.00 33.77  ? 85  PHE A CA  1 
ATOM   535  C  C   . PHE A  1  72  ? 46.425  -12.119 35.358 1.00 32.06  ? 85  PHE A C   1 
ATOM   536  O  O   . PHE A  1  72  ? 47.038  -12.658 36.270 1.00 29.52  ? 85  PHE A O   1 
ATOM   537  C  CB  . PHE A  1  72  ? 45.139  -10.175 36.375 1.00 33.21  ? 85  PHE A CB  1 
ATOM   538  C  CG  . PHE A  1  72  ? 45.511  -8.932  35.578 1.00 33.86  ? 85  PHE A CG  1 
ATOM   539  C  CD1 . PHE A  1  72  ? 44.933  -8.670  34.343 1.00 34.45  ? 85  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A  1  72  ? 46.413  -7.998  36.083 1.00 37.31  ? 85  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A  1  72  ? 45.261  -7.527  33.625 1.00 35.37  ? 85  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A  1  72  ? 46.727  -6.844  35.369 1.00 35.97  ? 85  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A  1  72  ? 46.174  -6.625  34.129 1.00 34.39  ? 85  PHE A CZ  1 
ATOM   544  N  N   . GLU A  1  73  ? 46.903  -12.066 34.115 1.00 34.79  ? 86  GLU A N   1 
ATOM   545  C  CA  . GLU A  1  73  ? 48.167  -12.703 33.765 1.00 38.81  ? 86  GLU A CA  1 
ATOM   546  C  C   . GLU A  1  73  ? 49.334  -12.024 34.493 1.00 37.70  ? 86  GLU A C   1 
ATOM   547  O  O   . GLU A  1  73  ? 49.358  -10.802 34.652 1.00 40.17  ? 86  GLU A O   1 
ATOM   548  C  CB  . GLU A  1  73  ? 48.257  -12.692 32.241 1.00 41.01  ? 86  GLU A CB  1 
ATOM   549  C  CG  . GLU A  1  73  ? 49.376  -13.560 31.681 1.00 44.29  ? 86  GLU A CG  1 
ATOM   550  C  CD  . GLU A  1  73  ? 50.740  -12.902 31.643 1.00 50.47  ? 86  GLU A CD  1 
ATOM   551  O  OE1 . GLU A  1  73  ? 51.761  -13.537 32.023 1.00 53.27  ? 86  GLU A OE1 1 
ATOM   552  O  OE2 . GLU A  1  73  ? 50.768  -11.719 31.244 1.00 52.51  ? 86  GLU A OE2 1 
ATOM   553  N  N   . ASN A  1  74  ? 50.303  -12.838 34.922 1.00 40.11  ? 87  ASN A N   1 
ATOM   554  C  CA  . ASN A  1  74  ? 51.407  -12.424 35.785 1.00 40.77  ? 87  ASN A CA  1 
ATOM   555  C  C   . ASN A  1  74  ? 52.163  -11.211 35.232 1.00 40.09  ? 87  ASN A C   1 
ATOM   556  O  O   . ASN A  1  74  ? 52.406  -10.254 35.971 1.00 41.67  ? 87  ASN A O   1 
ATOM   557  C  CB  . ASN A  1  74  ? 52.342  -13.600 36.045 1.00 38.14  ? 87  ASN A CB  1 
ATOM   558  C  CG  . ASN A  1  74  ? 53.506  -13.271 36.945 1.00 36.07  ? 87  ASN A CG  1 
ATOM   559  O  OD1 . ASN A  1  74  ? 54.645  -13.329 36.474 1.00 40.77  ? 87  ASN A OD1 1 
ATOM   560  N  ND2 . ASN A  1  74  ? 53.260  -12.941 38.208 1.00 33.32  ? 87  ASN A ND2 1 
ATOM   561  N  N   . ASN A  1  75  ? 52.567  -11.249 33.953 1.00 40.71  ? 88  ASN A N   1 
ATOM   562  C  CA  . ASN A  1  75  ? 53.372  -10.172 33.394 1.00 45.09  ? 88  ASN A CA  1 
ATOM   563  C  C   . ASN A  1  75  ? 52.561  -8.885  33.316 1.00 38.16  ? 88  ASN A C   1 
ATOM   564  O  O   . ASN A  1  75  ? 53.100  -7.813  33.584 1.00 40.74  ? 88  ASN A O   1 
ATOM   565  C  CB  . ASN A  1  75  ? 54.009  -10.532 32.051 1.00 53.46  ? 88  ASN A CB  1 
ATOM   566  C  CG  . ASN A  1  75  ? 55.200  -11.455 32.219 1.00 71.88  ? 88  ASN A CG  1 
ATOM   567  O  OD1 . ASN A  1  75  ? 55.969  -11.361 33.194 1.00 64.30  ? 88  ASN A OD1 1 
ATOM   568  N  ND2 . ASN A  1  75  ? 55.410  -12.326 31.242 1.00 85.82  ? 88  ASN A ND2 1 
ATOM   569  N  N   . ALA A  1  76  ? 51.286  -8.997  32.928 1.00 40.79  ? 89  ALA A N   1 
ATOM   570  C  CA  . ALA A  1  76  ? 50.391  -7.853  32.891 1.00 41.06  ? 89  ALA A CA  1 
ATOM   571  C  C   . ALA A  1  76  ? 50.252  -7.234  34.285 1.00 37.34  ? 89  ALA A C   1 
ATOM   572  O  O   . ALA A  1  76  ? 50.247  -6.013  34.422 1.00 41.07  ? 89  ALA A O   1 
ATOM   573  C  CB  . ALA A  1  76  ? 49.055  -8.264  32.309 1.00 40.81  ? 89  ALA A CB  1 
ATOM   574  N  N   . ALA A  1  77  ? 50.154  -8.082  35.313 1.00 33.72  ? 90  ALA A N   1 
ATOM   575  C  CA  . ALA A  1  77  ? 50.062  -7.617  36.689 1.00 34.52  ? 90  ALA A CA  1 
ATOM   576  C  C   . ALA A  1  77  ? 51.333  -6.860  37.097 1.00 33.88  ? 90  ALA A C   1 
ATOM   577  O  O   . ALA A  1  77  ? 51.252  -5.820  37.745 1.00 35.78  ? 90  ALA A O   1 
ATOM   578  C  CB  . ALA A  1  77  ? 49.765  -8.787  37.617 1.00 30.76  ? 90  ALA A CB  1 
ATOM   579  N  N   . ILE A  1  78  ? 52.499  -7.380  36.714 1.00 36.85  ? 91  ILE A N   1 
ATOM   580  C  CA  . ILE A  1  78  ? 53.777  -6.755  37.034 1.00 36.78  ? 91  ILE A CA  1 
ATOM   581  C  C   . ILE A  1  78  ? 53.876  -5.393  36.343 1.00 33.29  ? 91  ILE A C   1 
ATOM   582  O  O   . ILE A  1  78  ? 54.252  -4.409  36.967 1.00 32.69  ? 91  ILE A O   1 
ATOM   583  C  CB  . ILE A  1  78  ? 54.942  -7.708  36.686 1.00 37.40  ? 91  ILE A CB  1 
ATOM   584  C  CG1 . ILE A  1  78  ? 54.972  -8.878  37.677 1.00 37.74  ? 91  ILE A CG1 1 
ATOM   585  C  CG2 . ILE A  1  78  ? 56.304  -6.990  36.628 1.00 39.92  ? 91  ILE A CG2 1 
ATOM   586  C  CD1 . ILE A  1  78  ? 55.809  -10.063 37.237 1.00 36.69  ? 91  ILE A CD1 1 
ATOM   587  N  N   . VAL A  1  79  ? 53.474  -5.319  35.073 1.00 32.78  ? 92  VAL A N   1 
ATOM   588  C  CA  . VAL A  1  79  ? 53.636  -4.092  34.310 1.00 34.60  ? 92  VAL A CA  1 
ATOM   589  C  C   . VAL A  1  79  ? 52.763  -2.982  34.898 1.00 37.73  ? 92  VAL A C   1 
ATOM   590  O  O   . VAL A  1  79  ? 53.215  -1.845  35.045 1.00 38.94  ? 92  VAL A O   1 
ATOM   591  C  CB  . VAL A  1  79  ? 53.348  -4.345  32.819 1.00 36.59  ? 92  VAL A CB  1 
ATOM   592  C  CG1 . VAL A  1  79  ? 53.158  -3.049  32.046 1.00 36.18  ? 92  VAL A CG1 1 
ATOM   593  C  CG2 . VAL A  1  79  ? 54.468  -5.177  32.180 1.00 36.14  ? 92  VAL A CG2 1 
ATOM   594  N  N   . ALA A  1  80  ? 51.504  -3.320  35.216 1.00 35.81  ? 93  ALA A N   1 
ATOM   595  C  CA  . ALA A  1  80  ? 50.553  -2.353  35.735 1.00 34.12  ? 93  ALA A CA  1 
ATOM   596  C  C   . ALA A  1  80  ? 50.913  -1.984  37.174 1.00 34.03  ? 93  ALA A C   1 
ATOM   597  O  O   . ALA A  1  80  ? 50.851  -0.814  37.545 1.00 29.77  ? 93  ALA A O   1 
ATOM   598  C  CB  . ALA A  1  80  ? 49.145  -2.900  35.642 1.00 33.20  ? 93  ALA A CB  1 
ATOM   599  N  N   . THR A  1  81  ? 51.303  -2.969  37.990 1.00 34.96  ? 94  THR A N   1 
ATOM   600  C  CA  . THR A  1  81  ? 51.457  -2.696  39.410 1.00 36.44  ? 94  THR A CA  1 
ATOM   601  C  C   . THR A  1  81  ? 52.651  -1.775  39.670 1.00 36.45  ? 94  THR A C   1 
ATOM   602  O  O   . THR A  1  81  ? 52.522  -0.832  40.438 1.00 36.15  ? 94  THR A O   1 
ATOM   603  C  CB  . THR A  1  81  ? 51.560  -3.995  40.202 1.00 36.28  ? 94  THR A CB  1 
ATOM   604  O  OG1 . THR A  1  81  ? 50.301  -4.640  40.014 1.00 37.22  ? 94  THR A OG1 1 
ATOM   605  C  CG2 . THR A  1  81  ? 51.789  -3.765  41.688 1.00 36.43  ? 94  THR A CG2 1 
ATOM   606  N  N   . TYR A  1  82  ? 53.807  -2.046  39.054 1.00 37.31  ? 95  TYR A N   1 
ATOM   607  C  CA  . TYR A  1  82  ? 55.023  -1.295  39.363 1.00 36.91  ? 95  TYR A CA  1 
ATOM   608  C  C   . TYR A  1  82  ? 54.989  0.075   38.675 1.00 36.30  ? 95  TYR A C   1 
ATOM   609  O  O   . TYR A  1  82  ? 55.562  1.030   39.187 1.00 36.09  ? 95  TYR A O   1 
ATOM   610  C  CB  . TYR A  1  82  ? 56.279  -2.128  39.049 1.00 34.65  ? 95  TYR A CB  1 
ATOM   611  C  CG  . TYR A  1  82  ? 56.466  -3.256  40.050 1.00 35.01  ? 95  TYR A CG  1 
ATOM   612  C  CD1 . TYR A  1  82  ? 56.877  -2.996  41.356 1.00 37.42  ? 95  TYR A CD1 1 
ATOM   613  C  CD2 . TYR A  1  82  ? 56.193  -4.575  39.711 1.00 38.01  ? 95  TYR A CD2 1 
ATOM   614  C  CE1 . TYR A  1  82  ? 56.991  -4.009  42.294 1.00 37.89  ? 95  TYR A CE1 1 
ATOM   615  C  CE2 . TYR A  1  82  ? 56.301  -5.595  40.646 1.00 37.62  ? 95  TYR A CE2 1 
ATOM   616  C  CZ  . TYR A  1  82  ? 56.716  -5.315  41.933 1.00 35.97  ? 95  TYR A CZ  1 
ATOM   617  O  OH  . TYR A  1  82  ? 56.858  -6.306  42.858 1.00 39.18  ? 95  TYR A OH  1 
ATOM   618  N  N   . LEU A  1  83  ? 54.285  0.177   37.541 1.00 37.86  ? 96  LEU A N   1 
ATOM   619  C  CA  . LEU A  1  83  ? 53.966  1.470   36.943 1.00 41.07  ? 96  LEU A CA  1 
ATOM   620  C  C   . LEU A  1  83  ? 53.229  2.340   37.957 1.00 37.56  ? 96  LEU A C   1 
ATOM   621  O  O   . LEU A  1  83  ? 53.599  3.483   38.207 1.00 42.22  ? 96  LEU A O   1 
ATOM   622  C  CB  . LEU A  1  83  ? 53.128  1.251   35.686 1.00 41.36  ? 96  LEU A CB  1 
ATOM   623  C  CG  . LEU A  1  83  ? 52.565  2.500   35.011 1.00 46.65  ? 96  LEU A CG  1 
ATOM   624  C  CD1 . LEU A  1  83  ? 53.659  3.401   34.479 1.00 47.90  ? 96  LEU A CD1 1 
ATOM   625  C  CD2 . LEU A  1  83  ? 51.605  2.101   33.896 1.00 50.10  ? 96  LEU A CD2 1 
ATOM   626  N  N   . GLY A  1  84  ? 52.152  1.791   38.511 1.00 36.88  ? 97  GLY A N   1 
ATOM   627  C  CA  . GLY A  1  84  ? 51.345  2.503   39.485 1.00 35.92  ? 97  GLY A CA  1 
ATOM   628  C  C   . GLY A  1  84  ? 52.160  2.859   40.725 1.00 35.89  ? 97  GLY A C   1 
ATOM   629  O  O   . GLY A  1  84  ? 52.009  3.950   41.270 1.00 35.91  ? 97  GLY A O   1 
ATOM   630  N  N   . HIS A  1  85  ? 53.020  1.935   41.165 1.00 33.96  ? 98  HIS A N   1 
ATOM   631  C  CA  . HIS A  1  85  ? 53.796  2.136   42.379 1.00 37.47  ? 98  HIS A CA  1 
ATOM   632  C  C   . HIS A  1  85  ? 54.913  3.166   42.169 1.00 35.97  ? 98  HIS A C   1 
ATOM   633  O  O   . HIS A  1  85  ? 55.102  4.032   43.011 1.00 34.29  ? 98  HIS A O   1 
ATOM   634  C  CB  . HIS A  1  85  ? 54.356  0.808   42.880 1.00 36.97  ? 98  HIS A CB  1 
ATOM   635  C  CG  . HIS A  1  85  ? 54.985  0.888   44.222 1.00 36.75  ? 98  HIS A CG  1 
ATOM   636  N  ND1 . HIS A  1  85  ? 54.322  1.405   45.313 1.00 34.23  ? 98  HIS A ND1 1 
ATOM   637  C  CD2 . HIS A  1  85  ? 56.181  0.463   44.664 1.00 35.38  ? 98  HIS A CD2 1 
ATOM   638  C  CE1 . HIS A  1  85  ? 55.106  1.302   46.383 1.00 35.50  ? 98  HIS A CE1 1 
ATOM   639  N  NE2 . HIS A  1  85  ? 56.245  0.736   46.010 1.00 35.62  ? 98  HIS A NE2 1 
ATOM   640  N  N   . LEU A  1  86  ? 55.663  3.059   41.071 1.00 37.51  ? 99  LEU A N   1 
ATOM   641  C  CA  . LEU A  1  86  ? 56.765  3.979   40.804 1.00 37.39  ? 99  LEU A CA  1 
ATOM   642  C  C   . LEU A  1  86  ? 56.254  5.421   40.798 1.00 36.88  ? 99  LEU A C   1 
ATOM   643  O  O   . LEU A  1  86  ? 56.848  6.292   41.436 1.00 35.98  ? 99  LEU A O   1 
ATOM   644  C  CB  . LEU A  1  86  ? 57.461  3.609   39.494 1.00 36.69  ? 99  LEU A CB  1 
ATOM   645  C  CG  . LEU A  1  86  ? 58.416  2.412   39.566 1.00 38.62  ? 99  LEU A CG  1 
ATOM   646  C  CD1 . LEU A  1  86  ? 58.801  1.949   38.171 1.00 38.73  ? 99  LEU A CD1 1 
ATOM   647  C  CD2 . LEU A  1  86  ? 59.665  2.750   40.359 1.00 39.80  ? 99  LEU A CD2 1 
ATOM   648  N  N   . LEU A  1  87  ? 55.120  5.650   40.121 1.00 34.41  ? 100 LEU A N   1 
ATOM   649  C  CA  . LEU A  1  87  ? 54.572  6.984   39.935 1.00 33.33  ? 100 LEU A CA  1 
ATOM   650  C  C   . LEU A  1  87  ? 53.777  7.464   41.145 1.00 34.51  ? 100 LEU A C   1 
ATOM   651  O  O   . LEU A  1  87  ? 53.778  8.658   41.431 1.00 36.51  ? 100 LEU A O   1 
ATOM   652  C  CB  . LEU A  1  87  ? 53.705  7.004   38.675 1.00 36.04  ? 100 LEU A CB  1 
ATOM   653  C  CG  . LEU A  1  87  ? 54.448  6.795   37.349 1.00 35.40  ? 100 LEU A CG  1 
ATOM   654  C  CD1 . LEU A  1  87  ? 53.495  6.779   36.180 1.00 35.13  ? 100 LEU A CD1 1 
ATOM   655  C  CD2 . LEU A  1  87  ? 55.487  7.867   37.107 1.00 38.67  ? 100 LEU A CD2 1 
ATOM   656  N  N   . ASN A  1  88  ? 53.050  6.564   41.826 1.00 38.81  ? 101 ASN A N   1 
ATOM   657  C  CA  . ASN A  1  88  ? 52.001  6.994   42.742 1.00 35.05  ? 101 ASN A CA  1 
ATOM   658  C  C   . ASN A  1  88  ? 52.145  6.404   44.142 1.00 33.61  ? 101 ASN A C   1 
ATOM   659  O  O   . ASN A  1  88  ? 51.339  6.731   45.021 1.00 34.52  ? 101 ASN A O   1 
ATOM   660  C  CB  . ASN A  1  88  ? 50.610  6.640   42.227 1.00 34.98  ? 101 ASN A CB  1 
ATOM   661  C  CG  . ASN A  1  88  ? 50.257  7.322   40.926 1.00 38.40  ? 101 ASN A CG  1 
ATOM   662  O  OD1 . ASN A  1  88  ? 50.505  8.524   40.747 1.00 38.69  ? 101 ASN A OD1 1 
ATOM   663  N  ND2 . ASN A  1  88  ? 49.654  6.584   40.009 1.00 41.13  ? 101 ASN A ND2 1 
ATOM   664  N  N   . GLY A  1  89  ? 53.136  5.530   44.354 1.00 31.92  ? 102 GLY A N   1 
ATOM   665  C  CA  . GLY A  1  89  ? 53.250  4.823   45.623 1.00 36.67  ? 102 GLY A CA  1 
ATOM   666  C  C   . GLY A  1  89  ? 54.380  5.364   46.496 1.00 33.37  ? 102 GLY A C   1 
ATOM   667  O  O   . GLY A  1  89  ? 55.166  6.187   46.049 1.00 34.00  ? 102 GLY A O   1 
ATOM   668  N  N   . ASN A  1  90  ? 54.442  4.873   47.738 1.00 32.94  ? 103 ASN A N   1 
ATOM   669  C  CA  . ASN A  1  90  ? 55.522  5.174   48.661 1.00 33.68  ? 103 ASN A CA  1 
ATOM   670  C  C   . ASN A  1  90  ? 56.553  4.046   48.599 1.00 37.28  ? 103 ASN A C   1 
ATOM   671  O  O   . ASN A  1  90  ? 56.295  2.932   49.054 1.00 37.50  ? 103 ASN A O   1 
ATOM   672  C  CB  . ASN A  1  90  ? 54.970  5.360   50.068 1.00 33.19  ? 103 ASN A CB  1 
ATOM   673  C  CG  . ASN A  1  90  ? 56.006  5.897   51.030 1.00 32.91  ? 103 ASN A CG  1 
ATOM   674  O  OD1 . ASN A  1  90  ? 57.133  5.395   51.082 1.00 31.89  ? 103 ASN A OD1 1 
ATOM   675  N  ND2 . ASN A  1  90  ? 55.646  6.905   51.805 1.00 32.11  ? 103 ASN A ND2 1 
ATOM   676  N  N   . LEU A  1  91  ? 57.732  4.354   48.056 1.00 39.91  ? 104 LEU A N   1 
ATOM   677  C  CA  . LEU A  1  91  ? 58.741  3.354   47.753 1.00 40.04  ? 104 LEU A CA  1 
ATOM   678  C  C   . LEU A  1  91  ? 59.484  2.919   49.010 1.00 36.63  ? 104 LEU A C   1 
ATOM   679  O  O   . LEU A  1  91  ? 59.996  1.811   49.048 1.00 41.99  ? 104 LEU A O   1 
ATOM   680  C  CB  . LEU A  1  91  ? 59.663  3.945   46.693 1.00 45.85  ? 104 LEU A CB  1 
ATOM   681  C  CG  . LEU A  1  91  ? 58.957  4.262   45.369 1.00 51.49  ? 104 LEU A CG  1 
ATOM   682  C  CD1 . LEU A  1  91  ? 59.823  5.050   44.442 1.00 56.89  ? 104 LEU A CD1 1 
ATOM   683  C  CD2 . LEU A  1  91  ? 58.533  3.001   44.659 1.00 56.70  ? 104 LEU A CD2 1 
ATOM   684  N  N   . VAL A  1  92  ? 59.474  3.758   50.048 1.00 35.52  ? 105 VAL A N   1 
ATOM   685  C  CA  . VAL A  1  92  ? 60.160  3.467   51.296 1.00 39.43  ? 105 VAL A CA  1 
ATOM   686  C  C   . VAL A  1  92  ? 59.338  2.476   52.120 1.00 41.45  ? 105 VAL A C   1 
ATOM   687  O  O   . VAL A  1  92  ? 59.891  1.489   52.614 1.00 37.35  ? 105 VAL A O   1 
ATOM   688  C  CB  . VAL A  1  92  ? 60.473  4.777   52.054 1.00 39.56  ? 105 VAL A CB  1 
ATOM   689  C  CG1 . VAL A  1  92  ? 60.920  4.559   53.495 1.00 38.83  ? 105 VAL A CG1 1 
ATOM   690  C  CG2 . VAL A  1  92  ? 61.526  5.589   51.310 1.00 38.08  ? 105 VAL A CG2 1 
ATOM   691  N  N   . THR A  1  93  ? 58.020  2.724   52.240 1.00 41.68  ? 106 THR A N   1 
ATOM   692  C  CA  . THR A  1  93  ? 57.141  1.848   53.004 1.00 37.65  ? 106 THR A CA  1 
ATOM   693  C  C   . THR A  1  93  ? 56.597  0.703   52.149 1.00 36.88  ? 106 THR A C   1 
ATOM   694  O  O   . THR A  1  93  ? 56.054  -0.255  52.704 1.00 41.60  ? 106 THR A O   1 
ATOM   695  C  CB  . THR A  1  93  ? 56.002  2.642   53.640 1.00 38.23  ? 106 THR A CB  1 
ATOM   696  O  OG1 . THR A  1  93  ? 55.237  3.178   52.565 1.00 38.03  ? 106 THR A OG1 1 
ATOM   697  C  CG2 . THR A  1  93  ? 56.507  3.741   54.557 1.00 36.90  ? 106 THR A CG2 1 
ATOM   698  N  N   . ASP A  1  94  ? 56.722  0.801   50.817 1.00 35.39  ? 107 ASP A N   1 
ATOM   699  C  CA  . ASP A  1  94  ? 56.270  -0.233  49.898 1.00 36.79  ? 107 ASP A CA  1 
ATOM   700  C  C   . ASP A  1  94  ? 54.743  -0.328  49.913 1.00 37.33  ? 107 ASP A C   1 
ATOM   701  O  O   . ASP A  1  94  ? 54.204  -1.423  49.824 1.00 38.88  ? 107 ASP A O   1 
ATOM   702  C  CB  . ASP A  1  94  ? 56.925  -1.570  50.220 1.00 35.62  ? 107 ASP A CB  1 
ATOM   703  C  CG  . ASP A  1  94  ? 56.905  -2.604  49.102 1.00 38.31  ? 107 ASP A CG  1 
ATOM   704  O  OD1 . ASP A  1  94  ? 57.167  -2.216  47.943 1.00 34.90  ? 107 ASP A OD1 1 
ATOM   705  O  OD2 . ASP A  1  94  ? 56.661  -3.801  49.402 1.00 42.88  ? 107 ASP A OD2 1 
ATOM   706  N  N   . LEU A  1  95  ? 54.064  0.825   50.006 1.00 35.97  ? 108 LEU A N   1 
ATOM   707  C  CA  . LEU A  1  95  ? 52.612  0.886   50.070 1.00 38.01  ? 108 LEU A CA  1 
ATOM   708  C  C   . LEU A  1  95  ? 52.068  1.799   48.974 1.00 37.77  ? 108 LEU A C   1 
ATOM   709  O  O   . LEU A  1  95  ? 52.596  2.885   48.764 1.00 37.44  ? 108 LEU A O   1 
ATOM   710  C  CB  . LEU A  1  95  ? 52.154  1.369   51.439 1.00 36.13  ? 108 LEU A CB  1 
ATOM   711  C  CG  . LEU A  1  95  ? 52.480  0.466   52.628 1.00 38.85  ? 108 LEU A CG  1 
ATOM   712  C  CD1 . LEU A  1  95  ? 52.034  1.147   53.913 1.00 39.03  ? 108 LEU A CD1 1 
ATOM   713  C  CD2 . LEU A  1  95  ? 51.810  -0.886  52.510 1.00 38.86  ? 108 LEU A CD2 1 
ATOM   714  N  N   . LEU A  1  96  ? 50.998  1.328   48.310 1.00 34.06  ? 109 LEU A N   1 
ATOM   715  C  CA  . LEU A  1  96  ? 50.282  2.058   47.276 1.00 33.08  ? 109 LEU A CA  1 
ATOM   716  C  C   . LEU A  1  96  ? 48.797  2.139   47.631 1.00 34.40  ? 109 LEU A C   1 
ATOM   717  O  O   . LEU A  1  96  ? 48.187  1.132   47.964 1.00 37.13  ? 109 LEU A O   1 
ATOM   718  C  CB  . LEU A  1  96  ? 50.499  1.345   45.944 1.00 32.37  ? 109 LEU A CB  1 
ATOM   719  C  CG  . LEU A  1  96  ? 49.666  1.855   44.763 1.00 33.98  ? 109 LEU A CG  1 
ATOM   720  C  CD1 . LEU A  1  96  ? 49.902  3.332   44.499 1.00 35.79  ? 109 LEU A CD1 1 
ATOM   721  C  CD2 . LEU A  1  96  ? 49.950  1.066   43.509 1.00 35.17  ? 109 LEU A CD2 1 
ATOM   722  N  N   . SER A  1  97  ? 48.243  3.359   47.571 1.00 35.11  ? 110 SER A N   1 
ATOM   723  C  CA  . SER A  1  97  ? 46.819  3.618   47.665 1.00 34.90  ? 110 SER A CA  1 
ATOM   724  C  C   . SER A  1  97  ? 46.164  3.410   46.301 1.00 35.00  ? 110 SER A C   1 
ATOM   725  O  O   . SER A  1  97  ? 46.663  3.909   45.295 1.00 31.71  ? 110 SER A O   1 
ATOM   726  C  CB  . SER A  1  97  ? 46.573  5.031   48.159 1.00 37.74  ? 110 SER A CB  1 
ATOM   727  O  OG  . SER A  1  97  ? 45.232  5.447   47.943 1.00 36.94  ? 110 SER A OG  1 
ATOM   728  N  N   . ILE A  1  98  ? 45.029  2.697   46.274 1.00 33.97  ? 111 ILE A N   1 
ATOM   729  C  CA  . ILE A  1  98  ? 44.330  2.439   45.022 1.00 34.32  ? 111 ILE A CA  1 
ATOM   730  C  C   . ILE A  1  98  ? 43.442  3.627   44.672 1.00 36.06  ? 111 ILE A C   1 
ATOM   731  O  O   . ILE A  1  98  ? 42.793  3.611   43.631 1.00 37.70  ? 111 ILE A O   1 
ATOM   732  C  CB  . ILE A  1  98  ? 43.535  1.119   45.054 1.00 35.46  ? 111 ILE A CB  1 
ATOM   733  C  CG1 . ILE A  1  98  ? 42.422  1.110   46.107 1.00 34.06  ? 111 ILE A CG1 1 
ATOM   734  C  CG2 . ILE A  1  98  ? 44.490  -0.068  45.209 1.00 35.70  ? 111 ILE A CG2 1 
ATOM   735  C  CD1 . ILE A  1  98  ? 41.506  -0.098  46.015 1.00 34.58  ? 111 ILE A CD1 1 
ATOM   736  N  N   . GLY A  1  99  ? 43.418  4.640   45.550 1.00 38.39  ? 112 GLY A N   1 
ATOM   737  C  CA  . GLY A  1  99  ? 42.670  5.859   45.317 1.00 41.95  ? 112 GLY A CA  1 
ATOM   738  C  C   . GLY A  1  99  ? 43.508  7.110   45.556 1.00 39.14  ? 112 GLY A C   1 
ATOM   739  O  O   . GLY A  1  99  ? 44.512  7.299   44.890 1.00 37.16  ? 112 GLY A O   1 
ATOM   740  N  N   . GLY A  1  100 ? 43.053  7.958   46.483 1.00 40.46  ? 113 GLY A N   1 
ATOM   741  C  CA  . GLY A  1  100 ? 43.671  9.245   46.752 1.00 42.26  ? 113 GLY A CA  1 
ATOM   742  C  C   . GLY A  1  100 ? 44.684  9.170   47.890 1.00 40.77  ? 113 GLY A C   1 
ATOM   743  O  O   . GLY A  1  100 ? 44.996  8.093   48.382 1.00 41.95  ? 113 GLY A O   1 
ATOM   744  N  N   . ALA A  1  101 ? 45.176  10.340  48.311 1.00 43.55  ? 114 ALA A N   1 
ATOM   745  C  CA  . ALA A  1  101 ? 46.228  10.445  49.309 1.00 44.87  ? 114 ALA A CA  1 
ATOM   746  C  C   . ALA A  1  101 ? 45.710  10.029  50.679 1.00 37.95  ? 114 ALA A C   1 
ATOM   747  O  O   . ALA A  1  101 ? 44.552  10.268  51.015 1.00 39.56  ? 114 ALA A O   1 
ATOM   748  C  CB  . ALA A  1  101 ? 46.762  11.865  49.364 1.00 44.70  ? 114 ALA A CB  1 
ATOM   749  N  N   . THR A  1  102 ? 46.603  9.435   51.474 1.00 38.35  ? 115 THR A N   1 
ATOM   750  C  CA  . THR A  1  102 ? 46.225  8.930   52.779 1.00 38.77  ? 115 THR A CA  1 
ATOM   751  C  C   . THR A  1  102 ? 47.473  8.806   53.635 1.00 36.64  ? 115 THR A C   1 
ATOM   752  O  O   . THR A  1  102 ? 48.518  8.396   53.136 1.00 39.19  ? 115 THR A O   1 
ATOM   753  C  CB  . THR A  1  102 ? 45.516  7.582   52.608 1.00 38.41  ? 115 THR A CB  1 
ATOM   754  O  OG1 . THR A  1  102 ? 45.306  7.054   53.917 1.00 39.50  ? 115 THR A OG1 1 
ATOM   755  C  CG2 . THR A  1  102 ? 46.320  6.583   51.787 1.00 37.52  ? 115 THR A CG2 1 
ATOM   756  N  N   . PRO A  1  103 ? 47.390  9.115   54.951 1.00 43.47  ? 116 PRO A N   1 
ATOM   757  C  CA  . PRO A  1  103 ? 48.490  8.814   55.877 1.00 42.06  ? 116 PRO A CA  1 
ATOM   758  C  C   . PRO A  1  103 ? 48.841  7.328   56.001 1.00 40.66  ? 116 PRO A C   1 
ATOM   759  O  O   . PRO A  1  103 ? 49.945  6.983   56.430 1.00 43.23  ? 116 PRO A O   1 
ATOM   760  C  CB  . PRO A  1  103 ? 47.998  9.406   57.216 1.00 41.80  ? 116 PRO A CB  1 
ATOM   761  C  CG  . PRO A  1  103 ? 46.491  9.506   57.072 1.00 42.81  ? 116 PRO A CG  1 
ATOM   762  C  CD  . PRO A  1  103 ? 46.239  9.774   55.601 1.00 41.54  ? 116 PRO A CD  1 
ATOM   763  N  N   . LYS A  1  104 ? 47.902  6.454   55.610 1.00 38.41  ? 117 LYS A N   1 
ATOM   764  C  CA  . LYS A  1  104 ? 48.097  5.012   55.659 1.00 37.87  ? 117 LYS A CA  1 
ATOM   765  C  C   . LYS A  1  104 ? 49.288  4.555   54.813 1.00 37.32  ? 117 LYS A C   1 
ATOM   766  O  O   . LYS A  1  104 ? 49.815  3.491   55.077 1.00 38.06  ? 117 LYS A O   1 
ATOM   767  C  CB  . LYS A  1  104 ? 46.817  4.292   55.222 1.00 38.67  ? 117 LYS A CB  1 
ATOM   768  C  CG  . LYS A  1  104 ? 45.674  4.298   56.222 1.00 38.86  ? 117 LYS A CG  1 
ATOM   769  C  CD  . LYS A  1  104 ? 44.326  3.902   55.624 1.00 46.11  ? 117 LYS A CD  1 
ATOM   770  C  CE  . LYS A  1  104 ? 43.224  3.874   56.642 1.00 50.74  ? 117 LYS A CE  1 
ATOM   771  N  NZ  . LYS A  1  104 ? 43.282  2.680   57.485 1.00 56.17  ? 117 LYS A NZ  1 
ATOM   772  N  N   . THR A  1  105 ? 49.726  5.324   53.804 1.00 37.98  ? 118 THR A N   1 
ATOM   773  C  CA  . THR A  1  105 ? 50.911  4.944   53.039 1.00 38.12  ? 118 THR A CA  1 
ATOM   774  C  C   . THR A  1  105 ? 52.182  5.374   53.766 1.00 38.85  ? 118 THR A C   1 
ATOM   775  O  O   . THR A  1  105 ? 53.282  5.048   53.314 1.00 38.12  ? 118 THR A O   1 
ATOM   776  C  CB  . THR A  1  105 ? 50.903  5.500   51.613 1.00 39.47  ? 118 THR A CB  1 
ATOM   777  O  OG1 . THR A  1  105 ? 50.773  6.915   51.696 1.00 39.51  ? 118 THR A OG1 1 
ATOM   778  C  CG2 . THR A  1  105 ? 49.788  4.901   50.775 1.00 42.75  ? 118 THR A CG2 1 
ATOM   779  N  N   . GLY A  1  106 ? 52.025  6.128   54.862 1.00 39.95  ? 119 GLY A N   1 
ATOM   780  C  CA  . GLY A  1  106 ? 53.137  6.460   55.735 1.00 42.70  ? 119 GLY A CA  1 
ATOM   781  C  C   . GLY A  1  106 ? 53.725  7.845   55.445 1.00 43.58  ? 119 GLY A C   1 
ATOM   782  O  O   . GLY A  1  106 ? 53.195  8.607   54.633 1.00 38.95  ? 119 GLY A O   1 
ATOM   783  N  N   . PRO A  1  107 ? 54.837  8.212   56.126 1.00 46.62  ? 120 PRO A N   1 
ATOM   784  C  CA  . PRO A  1  107 ? 55.458  9.525   55.951 1.00 47.54  ? 120 PRO A CA  1 
ATOM   785  C  C   . PRO A  1  107 ? 55.679  9.873   54.477 1.00 48.98  ? 120 PRO A C   1 
ATOM   786  O  O   . PRO A  1  107 ? 56.201  9.076   53.705 1.00 50.62  ? 120 PRO A O   1 
ATOM   787  C  CB  . PRO A  1  107 ? 56.792  9.390   56.725 1.00 46.95  ? 120 PRO A CB  1 
ATOM   788  C  CG  . PRO A  1  107 ? 56.521  8.325   57.770 1.00 46.40  ? 120 PRO A CG  1 
ATOM   789  C  CD  . PRO A  1  107 ? 55.546  7.372   57.113 1.00 47.97  ? 120 PRO A CD  1 
ATOM   790  N  N   . PRO A  1  108 ? 55.290  11.082  54.030 1.00 50.47  ? 121 PRO A N   1 
ATOM   791  C  CA  . PRO A  1  108 ? 55.382  11.443  52.618 1.00 50.65  ? 121 PRO A CA  1 
ATOM   792  C  C   . PRO A  1  108 ? 56.806  11.436  52.069 1.00 50.99  ? 121 PRO A C   1 
ATOM   793  O  O   . PRO A  1  108 ? 57.770  11.687  52.792 1.00 47.29  ? 121 PRO A O   1 
ATOM   794  C  CB  . PRO A  1  108 ? 54.748  12.846  52.587 1.00 50.18  ? 121 PRO A CB  1 
ATOM   795  C  CG  . PRO A  1  108 ? 54.981  13.374  53.981 1.00 55.63  ? 121 PRO A CG  1 
ATOM   796  C  CD  . PRO A  1  108 ? 54.725  12.160  54.855 1.00 54.36  ? 121 PRO A CD  1 
ATOM   797  N  N   . PRO A  1  109 ? 56.985  11.139  50.761 1.00 48.08  ? 122 PRO A N   1 
ATOM   798  C  CA  . PRO A  1  109 ? 58.296  11.260  50.131 1.00 45.60  ? 122 PRO A CA  1 
ATOM   799  C  C   . PRO A  1  109 ? 58.661  12.728  49.921 1.00 44.41  ? 122 PRO A C   1 
ATOM   800  O  O   . PRO A  1  109 ? 57.811  13.611  49.998 1.00 41.21  ? 122 PRO A O   1 
ATOM   801  C  CB  . PRO A  1  109 ? 58.106  10.517  48.812 1.00 46.80  ? 122 PRO A CB  1 
ATOM   802  C  CG  . PRO A  1  109 ? 56.647  10.726  48.488 1.00 49.54  ? 122 PRO A CG  1 
ATOM   803  C  CD  . PRO A  1  109 ? 55.929  10.710  49.826 1.00 46.81  ? 122 PRO A CD  1 
ATOM   804  N  N   . PRO A  1  110 ? 59.934  13.041  49.610 1.00 47.62  ? 123 PRO A N   1 
ATOM   805  C  CA  . PRO A  1  110 ? 60.324  14.427  49.338 1.00 45.45  ? 123 PRO A CA  1 
ATOM   806  C  C   . PRO A  1  110 ? 59.738  14.907  48.013 1.00 47.07  ? 123 PRO A C   1 
ATOM   807  O  O   . PRO A  1  110 ? 59.768  14.190  47.006 1.00 41.75  ? 123 PRO A O   1 
ATOM   808  C  CB  . PRO A  1  110 ? 61.864  14.372  49.336 1.00 47.02  ? 123 PRO A CB  1 
ATOM   809  C  CG  . PRO A  1  110 ? 62.203  12.924  48.979 1.00 47.45  ? 123 PRO A CG  1 
ATOM   810  C  CD  . PRO A  1  110 ? 61.048  12.081  49.510 1.00 48.93  ? 123 PRO A CD  1 
ATOM   811  N  N   . PRO A  1  111 ? 59.136  16.117  47.962 1.00 45.64  ? 124 PRO A N   1 
ATOM   812  C  CA  . PRO A  1  111 ? 58.622  16.655  46.697 1.00 43.38  ? 124 PRO A CA  1 
ATOM   813  C  C   . PRO A  1  111 ? 59.749  16.766  45.677 1.00 42.87  ? 124 PRO A C   1 
ATOM   814  O  O   . PRO A  1  111 ? 60.898  16.958  46.063 1.00 47.57  ? 124 PRO A O   1 
ATOM   815  C  CB  . PRO A  1  111 ? 58.007  18.000  47.080 1.00 44.48  ? 124 PRO A CB  1 
ATOM   816  C  CG  . PRO A  1  111 ? 57.721  17.864  48.565 1.00 44.89  ? 124 PRO A CG  1 
ATOM   817  C  CD  . PRO A  1  111 ? 58.840  16.979  49.113 1.00 44.75  ? 124 PRO A CD  1 
ATOM   818  N  N   . PRO A  1  112 ? 59.506  16.633  44.353 1.00 40.35  ? 125 PRO A N   1 
ATOM   819  C  CA  . PRO A  1  112 ? 58.159  16.545  43.774 1.00 42.74  ? 125 PRO A CA  1 
ATOM   820  C  C   . PRO A  1  112 ? 57.351  15.240  43.830 1.00 44.14  ? 125 PRO A C   1 
ATOM   821  O  O   . PRO A  1  112 ? 56.221  15.209  43.356 1.00 47.22  ? 125 PRO A O   1 
ATOM   822  C  CB  . PRO A  1  112 ? 58.422  16.922  42.282 1.00 42.51  ? 125 PRO A CB  1 
ATOM   823  C  CG  . PRO A  1  112 ? 59.916  17.155  42.150 1.00 41.69  ? 125 PRO A CG  1 
ATOM   824  C  CD  . PRO A  1  112 ? 60.575  16.537  43.351 1.00 39.87  ? 125 PRO A CD  1 
ATOM   825  N  N   . ALA A  1  113 ? 57.922  14.159  44.379 1.00 43.77  ? 126 ALA A N   1 
ATOM   826  C  CA  . ALA A  1  113 ? 57.194  12.916  44.569 1.00 42.53  ? 126 ALA A CA  1 
ATOM   827  C  C   . ALA A  1  113 ? 56.059  13.158  45.561 1.00 42.35  ? 126 ALA A C   1 
ATOM   828  O  O   . ALA A  1  113 ? 56.125  14.086  46.353 1.00 43.40  ? 126 ALA A O   1 
ATOM   829  C  CB  . ALA A  1  113 ? 58.144  11.820  45.034 1.00 41.52  ? 126 ALA A CB  1 
ATOM   830  N  N   . HIS A  1  114 ? 55.011  12.323  45.520 1.00 43.32  ? 127 HIS A N   1 
ATOM   831  C  CA  . HIS A  1  114 ? 53.789  12.601  46.271 1.00 39.40  ? 127 HIS A CA  1 
ATOM   832  C  C   . HIS A  1  114 ? 53.188  11.369  46.944 1.00 37.89  ? 127 HIS A C   1 
ATOM   833  O  O   . HIS A  1  114 ? 52.551  11.518  47.983 1.00 41.91  ? 127 HIS A O   1 
ATOM   834  C  CB  . HIS A  1  114 ? 52.764  13.277  45.360 1.00 40.74  ? 127 HIS A CB  1 
ATOM   835  C  CG  . HIS A  1  114 ? 52.631  12.628  44.015 1.00 40.51  ? 127 HIS A CG  1 
ATOM   836  N  ND1 . HIS A  1  114 ? 51.849  11.516  43.831 1.00 38.77  ? 127 HIS A ND1 1 
ATOM   837  C  CD2 . HIS A  1  114 ? 53.165  12.900  42.820 1.00 40.29  ? 127 HIS A CD2 1 
ATOM   838  C  CE1 . HIS A  1  114 ? 51.910  11.155  42.560 1.00 42.98  ? 127 HIS A CE1 1 
ATOM   839  N  NE2 . HIS A  1  114 ? 52.698  11.989  41.931 1.00 38.53  ? 127 HIS A NE2 1 
ATOM   840  N  N   . ALA A  1  115 ? 53.380  10.170  46.368 1.00 38.98  ? 128 ALA A N   1 
ATOM   841  C  CA  . ALA A  1  115 ? 52.702  8.959   46.816 1.00 37.63  ? 128 ALA A CA  1 
ATOM   842  C  C   . ALA A  1  115 ? 51.207  9.223   47.011 1.00 35.46  ? 128 ALA A C   1 
ATOM   843  O  O   . ALA A  1  115 ? 50.621  8.866   48.026 1.00 36.54  ? 128 ALA A O   1 
ATOM   844  C  CB  . ALA A  1  115 ? 53.341  8.430   48.068 1.00 37.06  ? 128 ALA A CB  1 
ATOM   845  N  N   . GLY A  1  116 ? 50.584  9.794   45.980 1.00 36.64  ? 129 GLY A N   1 
ATOM   846  C  CA  . GLY A  1  116 ? 49.228  10.326  46.053 1.00 37.17  ? 129 GLY A CA  1 
ATOM   847  C  C   . GLY A  1  116 ? 48.160  9.333   45.614 1.00 35.41  ? 129 GLY A C   1 
ATOM   848  O  O   . GLY A  1  116 ? 46.990  9.660   45.712 1.00 41.65  ? 129 GLY A O   1 
ATOM   849  N  N   . GLY A  1  117 ? 48.568  8.147   45.140 1.00 40.95  ? 130 GLY A N   1 
ATOM   850  C  CA  . GLY A  1  117 ? 47.653  7.059   44.823 1.00 39.92  ? 130 GLY A CA  1 
ATOM   851  C  C   . GLY A  1  117 ? 47.247  7.054   43.350 1.00 39.38  ? 130 GLY A C   1 
ATOM   852  O  O   . GLY A  1  117 ? 47.656  7.933   42.591 1.00 32.45  ? 130 GLY A O   1 
ATOM   853  N  N   . LEU A  1  118 ? 46.420  6.064   42.970 1.00 36.58  ? 131 LEU A N   1 
ATOM   854  C  CA  . LEU A  1  118 ? 46.048  5.845   41.579 1.00 35.25  ? 131 LEU A CA  1 
ATOM   855  C  C   . LEU A  1  118 ? 45.162  6.975   41.048 1.00 34.34  ? 131 LEU A C   1 
ATOM   856  O  O   . LEU A  1  118 ? 45.010  7.098   39.829 1.00 34.43  ? 131 LEU A O   1 
ATOM   857  C  CB  . LEU A  1  118 ? 45.377  4.479   41.428 1.00 38.43  ? 131 LEU A CB  1 
ATOM   858  C  CG  . LEU A  1  118 ? 46.280  3.261   41.657 1.00 39.51  ? 131 LEU A CG  1 
ATOM   859  C  CD1 . LEU A  1  118 ? 45.507  1.975   41.393 1.00 39.46  ? 131 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A  1  118 ? 47.560  3.324   40.816 1.00 36.34  ? 131 LEU A CD2 1 
ATOM   861  N  N   . ASN A  1  119 ? 44.604  7.797   41.954 1.00 32.21  ? 132 ASN A N   1 
ATOM   862  C  CA  . ASN A  1  119 ? 43.790  8.939   41.577 1.00 33.43  ? 132 ASN A CA  1 
ATOM   863  C  C   . ASN A  1  119 ? 44.587  10.060  40.906 1.00 35.71  ? 132 ASN A C   1 
ATOM   864  O  O   . ASN A  1  119 ? 43.989  10.912  40.266 1.00 37.13  ? 132 ASN A O   1 
ATOM   865  C  CB  . ASN A  1  119 ? 43.123  9.611   42.770 1.00 35.57  ? 132 ASN A CB  1 
ATOM   866  C  CG  . ASN A  1  119 ? 41.871  8.930   43.266 1.00 36.18  ? 132 ASN A CG  1 
ATOM   867  O  OD1 . ASN A  1  119 ? 41.488  7.857   42.794 1.00 35.70  ? 132 ASN A OD1 1 
ATOM   868  N  ND2 . ASN A  1  119 ? 41.229  9.532   44.248 1.00 38.74  ? 132 ASN A ND2 1 
ATOM   869  N  N   . VAL A  1  120 ? 45.913  10.105  41.069 1.00 38.24  ? 133 VAL A N   1 
ATOM   870  C  CA  . VAL A  1  120 ? 46.696  11.198  40.508 1.00 39.01  ? 133 VAL A CA  1 
ATOM   871  C  C   . VAL A  1  120 ? 46.579  11.190  38.980 1.00 39.25  ? 133 VAL A C   1 
ATOM   872  O  O   . VAL A  1  120 ? 46.929  10.213  38.324 1.00 37.47  ? 133 VAL A O   1 
ATOM   873  C  CB  . VAL A  1  120 ? 48.163  11.158  40.983 1.00 37.42  ? 133 VAL A CB  1 
ATOM   874  C  CG1 . VAL A  1  120 ? 49.057  12.160  40.251 1.00 37.83  ? 133 VAL A CG1 1 
ATOM   875  C  CG2 . VAL A  1  120 ? 48.258  11.367  42.494 1.00 37.30  ? 133 VAL A CG2 1 
ATOM   876  N  N   . HIS A  1  121 ? 46.101  12.316  38.427 1.00 41.57  ? 134 HIS A N   1 
ATOM   877  C  CA  . HIS A  1  121 ? 45.891  12.477  36.993 1.00 43.57  ? 134 HIS A CA  1 
ATOM   878  C  C   . HIS A  1  121 ? 47.188  12.922  36.330 1.00 43.43  ? 134 HIS A C   1 
ATOM   879  O  O   . HIS A  1  121 ? 47.969  13.654  36.918 1.00 44.64  ? 134 HIS A O   1 
ATOM   880  C  CB  . HIS A  1  121 ? 44.794  13.518  36.728 1.00 43.69  ? 134 HIS A CB  1 
ATOM   881  C  CG  . HIS A  1  121 ? 44.592  13.859  35.287 1.00 47.06  ? 134 HIS A CG  1 
ATOM   882  N  ND1 . HIS A  1  121 ? 43.997  13.019  34.366 1.00 50.06  ? 134 HIS A ND1 1 
ATOM   883  C  CD2 . HIS A  1  121 ? 44.950  14.959  34.606 1.00 48.71  ? 134 HIS A CD2 1 
ATOM   884  C  CE1 . HIS A  1  121 ? 43.974  13.615  33.179 1.00 52.28  ? 134 HIS A CE1 1 
ATOM   885  N  NE2 . HIS A  1  121 ? 44.543  14.801  33.304 1.00 47.34  ? 134 HIS A NE2 1 
ATOM   886  N  N   . GLY A  1  122 ? 47.420  12.485  35.092 1.00 48.66  ? 135 GLY A N   1 
ATOM   887  C  CA  . GLY A  1  122 ? 48.431  13.126  34.270 1.00 50.98  ? 135 GLY A CA  1 
ATOM   888  C  C   . GLY A  1  122 ? 49.386  12.132  33.627 1.00 47.88  ? 135 GLY A C   1 
ATOM   889  O  O   . GLY A  1  122 ? 49.843  12.383  32.519 1.00 50.35  ? 135 GLY A O   1 
ATOM   890  N  N   . THR A  1  123 ? 49.763  11.071  34.349 1.00 45.96  ? 136 THR A N   1 
ATOM   891  C  CA  . THR A  1  123 ? 50.790  10.170  33.847 1.00 55.16  ? 136 THR A CA  1 
ATOM   892  C  C   . THR A  1  123 ? 50.278  8.725   33.753 1.00 54.59  ? 136 THR A C   1 
ATOM   893  O  O   . THR A  1  123 ? 50.604  8.036   32.789 1.00 53.83  ? 136 THR A O   1 
ATOM   894  C  CB  . THR A  1  123 ? 52.060  10.259  34.698 1.00 61.94  ? 136 THR A CB  1 
ATOM   895  O  OG1 . THR A  1  123 ? 52.277  11.622  35.059 1.00 55.79  ? 136 THR A OG1 1 
ATOM   896  C  CG2 . THR A  1  123 ? 53.275  9.735   33.950 1.00 58.27  ? 136 THR A CG2 1 
ATOM   897  N  N   . PHE A  1  124 ? 49.534  8.236   34.757 1.00 48.37  ? 137 PHE A N   1 
ATOM   898  C  CA  . PHE A  1  124 ? 48.838  6.957   34.653 1.00 48.99  ? 137 PHE A CA  1 
ATOM   899  C  C   . PHE A  1  124 ? 47.343  7.171   34.352 1.00 48.09  ? 137 PHE A C   1 
ATOM   900  O  O   . PHE A  1  124 ? 46.918  6.995   33.217 1.00 50.13  ? 137 PHE A O   1 
ATOM   901  C  CB  . PHE A  1  124 ? 49.070  6.133   35.922 1.00 48.95  ? 137 PHE A CB  1 
ATOM   902  C  CG  . PHE A  1  124 ? 48.766  4.639   35.821 1.00 47.66  ? 137 PHE A CG  1 
ATOM   903  C  CD1 . PHE A  1  124 ? 48.065  4.089   34.753 1.00 45.87  ? 137 PHE A CD1 1 
ATOM   904  C  CD2 . PHE A  1  124 ? 49.196  3.771   36.820 1.00 49.63  ? 137 PHE A CD2 1 
ATOM   905  C  CE1 . PHE A  1  124 ? 47.816  2.726   34.686 1.00 43.30  ? 137 PHE A CE1 1 
ATOM   906  C  CE2 . PHE A  1  124 ? 48.934  2.411   36.755 1.00 44.26  ? 137 PHE A CE2 1 
ATOM   907  C  CZ  . PHE A  1  124 ? 48.256  1.892   35.686 1.00 43.96  ? 137 PHE A CZ  1 
ATOM   908  N  N   . GLU A  1  125 ? 46.542  7.504   35.370 1.00 41.98  ? 138 GLU A N   1 
ATOM   909  C  CA  . GLU A  1  125 ? 45.138  7.825   35.178 1.00 43.17  ? 138 GLU A CA  1 
ATOM   910  C  C   . GLU A  1  125 ? 44.993  8.931   34.129 1.00 43.35  ? 138 GLU A C   1 
ATOM   911  O  O   . GLU A  1  125 ? 45.710  9.934   34.174 1.00 46.35  ? 138 GLU A O   1 
ATOM   912  C  CB  . GLU A  1  125 ? 44.523  8.275   36.504 1.00 42.30  ? 138 GLU A CB  1 
ATOM   913  C  CG  . GLU A  1  125 ? 43.012  8.458   36.464 1.00 45.22  ? 138 GLU A CG  1 
ATOM   914  C  CD  . GLU A  1  125 ? 42.477  9.615   35.634 1.00 48.00  ? 138 GLU A CD  1 
ATOM   915  O  OE1 . GLU A  1  125 ? 43.013  10.729  35.825 1.00 46.98  ? 138 GLU A OE1 1 
ATOM   916  O  OE2 . GLU A  1  125 ? 41.517  9.405   34.824 1.00 43.86  ? 138 GLU A OE2 1 
ATOM   917  N  N   . GLY A  1  126 ? 44.047  8.751   33.199 1.00 39.32  ? 139 GLY A N   1 
ATOM   918  C  CA  . GLY A  1  126 ? 43.759  9.749   32.179 1.00 37.28  ? 139 GLY A CA  1 
ATOM   919  C  C   . GLY A  1  126 ? 42.324  9.672   31.652 1.00 35.60  ? 139 GLY A C   1 
ATOM   920  O  O   . GLY A  1  126 ? 41.427  9.146   32.304 1.00 41.27  ? 139 GLY A O   1 
ATOM   921  N  N   . ASP A  1  127 ? 42.150  10.177  30.427 1.00 39.37  ? 140 ASP A N   1 
ATOM   922  C  CA  . ASP A  1  127 ? 40.879  10.661  29.901 1.00 39.41  ? 140 ASP A CA  1 
ATOM   923  C  C   . ASP A  1  127 ? 40.210  9.623   28.996 1.00 37.12  ? 140 ASP A C   1 
ATOM   924  O  O   . ASP A  1  127 ? 40.847  8.670   28.549 1.00 38.17  ? 140 ASP A O   1 
ATOM   925  C  CB  . ASP A  1  127 ? 41.080  11.947  29.113 1.00 41.54  ? 140 ASP A CB  1 
ATOM   926  C  CG  . ASP A  1  127 ? 41.666  13.145  29.859 1.00 45.35  ? 140 ASP A CG  1 
ATOM   927  O  OD1 . ASP A  1  127 ? 41.368  13.304  31.073 1.00 39.47  ? 140 ASP A OD1 1 
ATOM   928  O  OD2 . ASP A  1  127 ? 42.406  13.926  29.212 1.00 42.79  ? 140 ASP A OD2 1 
ATOM   929  N  N   . ALA A  1  128 ? 38.919  9.848   28.708 1.00 34.12  ? 141 ALA A N   1 
ATOM   930  C  CA  . ALA A  1  128 ? 38.127  9.008   27.813 1.00 35.11  ? 141 ALA A CA  1 
ATOM   931  C  C   . ALA A  1  128 ? 37.927  7.602   28.389 1.00 33.87  ? 141 ALA A C   1 
ATOM   932  O  O   . ALA A  1  128 ? 37.933  6.609   27.668 1.00 39.43  ? 141 ALA A O   1 
ATOM   933  C  CB  . ALA A  1  128 ? 38.742  8.981   26.422 1.00 35.18  ? 141 ALA A CB  1 
ATOM   934  N  N   . GLY A  1  129 ? 37.705  7.521   29.702 1.00 33.27  ? 142 GLY A N   1 
ATOM   935  C  CA  . GLY A  1  129 ? 37.336  6.265   30.339 1.00 35.42  ? 142 GLY A CA  1 
ATOM   936  C  C   . GLY A  1  129 ? 35.881  5.883   30.073 1.00 36.08  ? 142 GLY A C   1 
ATOM   937  O  O   . GLY A  1  129 ? 35.126  6.675   29.535 1.00 39.72  ? 142 GLY A O   1 
ATOM   938  N  N   . MET A  1  130 ? 35.498  4.672   30.479 1.00 37.79  ? 143 MET A N   1 
ATOM   939  C  CA  . MET A  1  130 ? 34.176  4.133   30.208 1.00 37.26  ? 143 MET A CA  1 
ATOM   940  C  C   . MET A  1  130 ? 33.157  4.573   31.268 1.00 37.54  ? 143 MET A C   1 
ATOM   941  O  O   . MET A  1  130 ? 32.035  4.939   30.894 1.00 35.48  ? 143 MET A O   1 
ATOM   942  C  CB  . MET A  1  130 ? 34.227  2.601   30.151 1.00 40.18  ? 143 MET A CB  1 
ATOM   943  C  CG  . MET A  1  130 ? 35.007  2.032   28.968 1.00 40.43  ? 143 MET A CG  1 
ATOM   944  S  SD  . MET A  1  130 ? 35.140  0.227   29.020 1.00 40.07  ? 143 MET A SD  1 
ATOM   945  C  CE  . MET A  1  130 ? 36.146  -0.086  30.472 1.00 37.65  ? 143 MET A CE  1 
ATOM   946  N  N   . THR A  1  131 ? 33.520  4.515   32.569 1.00 35.77  ? 144 THR A N   1 
ATOM   947  C  CA  . THR A  1  131 ? 32.575  4.831   33.638 1.00 36.04  ? 144 THR A CA  1 
ATOM   948  C  C   . THR A  1  131 ? 33.074  5.958   34.544 1.00 35.12  ? 144 THR A C   1 
ATOM   949  O  O   . THR A  1  131 ? 32.396  6.312   35.510 1.00 40.39  ? 144 THR A O   1 
ATOM   950  C  CB  . THR A  1  131 ? 32.237  3.574   34.437 1.00 34.84  ? 144 THR A CB  1 
ATOM   951  O  OG1 . THR A  1  131 ? 33.380  3.177   35.184 1.00 32.91  ? 144 THR A OG1 1 
ATOM   952  C  CG2 . THR A  1  131 ? 31.765  2.450   33.529 1.00 35.02  ? 144 THR A CG2 1 
ATOM   953  N  N   . ARG A  1  132 ? 34.241  6.529   34.221 1.00 35.12  ? 145 ARG A N   1 
ATOM   954  C  CA  . ARG A  1  132 ? 34.785  7.669   34.945 1.00 35.69  ? 145 ARG A CA  1 
ATOM   955  C  C   . ARG A  1  132 ? 34.952  8.854   34.001 1.00 34.97  ? 145 ARG A C   1 
ATOM   956  O  O   . ARG A  1  132 ? 35.326  8.663   32.847 1.00 37.97  ? 145 ARG A O   1 
ATOM   957  C  CB  . ARG A  1  132 ? 36.117  7.290   35.603 1.00 37.06  ? 145 ARG A CB  1 
ATOM   958  C  CG  . ARG A  1  132 ? 35.998  6.703   37.005 1.00 38.08  ? 145 ARG A CG  1 
ATOM   959  C  CD  . ARG A  1  132 ? 35.431  5.294   37.039 1.00 38.86  ? 145 ARG A CD  1 
ATOM   960  N  NE  . ARG A  1  132 ? 35.338  4.810   38.420 1.00 41.76  ? 145 ARG A NE  1 
ATOM   961  C  CZ  . ARG A  1  132 ? 34.605  3.790   38.875 1.00 41.66  ? 145 ARG A CZ  1 
ATOM   962  N  NH1 . ARG A  1  132 ? 34.604  3.549   40.182 1.00 41.97  ? 145 ARG A NH1 1 
ATOM   963  N  NH2 . ARG A  1  132 ? 33.889  3.036   38.047 1.00 36.71  ? 145 ARG A NH2 1 
ATOM   964  N  N   . ALA A  1  133 ? 34.676  10.065  34.511 1.00 37.98  ? 146 ALA A N   1 
ATOM   965  C  CA  . ALA A  1  133 ? 34.772  11.310  33.758 1.00 37.59  ? 146 ALA A CA  1 
ATOM   966  C  C   . ALA A  1  133 ? 36.207  11.842  33.800 1.00 37.62  ? 146 ALA A C   1 
ATOM   967  O  O   . ALA A  1  133 ? 36.927  11.601  34.759 1.00 32.49  ? 146 ALA A O   1 
ATOM   968  N  N   . ASP A  1  134 ? 36.600  12.580  32.755 1.00 38.52  ? 147 ASP A N   1 
ATOM   969  C  CA  . ASP A  1  134 ? 37.898  13.240  32.673 1.00 39.21  ? 147 ASP A CA  1 
ATOM   970  C  C   . ASP A  1  134 ? 38.100  14.171  33.864 1.00 40.73  ? 147 ASP A C   1 
ATOM   971  O  O   . ASP A  1  134 ? 37.140  14.776  34.333 1.00 37.81  ? 147 ASP A O   1 
ATOM   972  C  CB  . ASP A  1  134 ? 38.027  14.040  31.385 1.00 37.85  ? 147 ASP A CB  1 
ATOM   973  C  CG  . ASP A  1  134 ? 37.917  13.250  30.096 1.00 38.45  ? 147 ASP A CG  1 
ATOM   974  O  OD1 . ASP A  1  134 ? 37.618  12.040  30.169 1.00 38.15  ? 147 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A  1  134 ? 38.168  13.846  29.030 1.00 45.11  ? 147 ASP A OD2 1 
ATOM   976  N  N   . GLU A  1  135 ? 39.360  14.303  34.312 1.00 41.47  ? 148 GLU A N   1 
ATOM   977  C  CA  . GLU A  1  135 ? 39.705  15.111  35.473 1.00 46.58  ? 148 GLU A CA  1 
ATOM   978  C  C   . GLU A  1  135 ? 39.280  16.571  35.287 1.00 47.77  ? 148 GLU A C   1 
ATOM   979  O  O   . GLU A  1  135 ? 38.925  17.244  36.256 1.00 44.79  ? 148 GLU A O   1 
ATOM   980  C  CB  . GLU A  1  135 ? 41.203  14.992  35.755 1.00 53.13  ? 148 GLU A CB  1 
ATOM   981  C  CG  . GLU A  1  135 ? 41.653  15.721  37.022 1.00 56.39  ? 148 GLU A CG  1 
ATOM   982  C  CD  . GLU A  1  135 ? 42.075  17.166  36.828 1.00 66.92  ? 148 GLU A CD  1 
ATOM   983  O  OE1 . GLU A  1  135 ? 42.279  17.646  35.678 1.00 68.70  ? 148 GLU A OE1 1 
ATOM   984  O  OE2 . GLU A  1  135 ? 42.195  17.820  37.887 1.00 72.05  ? 148 GLU A OE2 1 
ATOM   985  N  N   . PHE A  1  136 ? 39.306  17.060  34.042 1.00 47.15  ? 149 PHE A N   1 
ATOM   986  C  CA  . PHE A  1  136 ? 38.925  18.426  33.734 1.00 45.38  ? 149 PHE A CA  1 
ATOM   987  C  C   . PHE A  1  136 ? 37.557  18.753  34.333 1.00 46.09  ? 149 PHE A C   1 
ATOM   988  O  O   . PHE A  1  136 ? 37.321  19.889  34.724 1.00 44.34  ? 149 PHE A O   1 
ATOM   989  C  CB  . PHE A  1  136 ? 38.893  18.684  32.225 1.00 51.25  ? 149 PHE A CB  1 
ATOM   990  C  CG  . PHE A  1  136 ? 38.461  20.102  31.872 1.00 58.62  ? 149 PHE A CG  1 
ATOM   991  C  CD1 . PHE A  1  136 ? 39.332  21.176  32.053 1.00 58.35  ? 149 PHE A CD1 1 
ATOM   992  C  CD2 . PHE A  1  136 ? 37.188  20.361  31.373 1.00 59.25  ? 149 PHE A CD2 1 
ATOM   993  C  CE1 . PHE A  1  136 ? 38.934  22.468  31.753 1.00 54.39  ? 149 PHE A CE1 1 
ATOM   994  C  CE2 . PHE A  1  136 ? 36.800  21.658  31.063 1.00 56.88  ? 149 PHE A CE2 1 
ATOM   995  C  CZ  . PHE A  1  136 ? 37.671  22.706  31.259 1.00 54.83  ? 149 PHE A CZ  1 
ATOM   996  N  N   . PHE A  1  137 ? 36.653  17.765  34.402 1.00 43.92  ? 150 PHE A N   1 
ATOM   997  C  CA  . PHE A  1  137 ? 35.290  18.009  34.845 1.00 42.39  ? 150 PHE A CA  1 
ATOM   998  C  C   . PHE A  1  137 ? 35.164  17.885  36.361 1.00 43.53  ? 150 PHE A C   1 
ATOM   999  O  O   . PHE A  1  137 ? 34.086  18.126  36.873 1.00 45.69  ? 150 PHE A O   1 
ATOM   1000 C  CB  . PHE A  1  137 ? 34.295  17.072  34.154 1.00 43.20  ? 150 PHE A CB  1 
ATOM   1001 C  CG  . PHE A  1  137 ? 34.352  17.125  32.633 1.00 44.43  ? 150 PHE A CG  1 
ATOM   1002 C  CD1 . PHE A  1  137 ? 34.203  18.330  31.958 1.00 50.80  ? 150 PHE A CD1 1 
ATOM   1003 C  CD2 . PHE A  1  137 ? 34.624  15.986  31.882 1.00 45.07  ? 150 PHE A CD2 1 
ATOM   1004 C  CE1 . PHE A  1  137 ? 34.280  18.381  30.575 1.00 49.18  ? 150 PHE A CE1 1 
ATOM   1005 C  CE2 . PHE A  1  137 ? 34.720  16.046  30.503 1.00 45.54  ? 150 PHE A CE2 1 
ATOM   1006 C  CZ  . PHE A  1  137 ? 34.530  17.240  29.853 1.00 47.77  ? 150 PHE A CZ  1 
ATOM   1007 N  N   . GLY A  1  138 ? 36.231  17.517  37.083 1.00 44.17  ? 151 GLY A N   1 
ATOM   1008 C  CA  . GLY A  1  138 ? 36.247  17.704  38.529 1.00 45.78  ? 151 GLY A CA  1 
ATOM   1009 C  C   . GLY A  1  138 ? 36.330  16.417  39.354 1.00 48.89  ? 151 GLY A C   1 
ATOM   1010 O  O   . GLY A  1  138 ? 36.564  16.505  40.553 1.00 54.12  ? 151 GLY A O   1 
ATOM   1011 N  N   . ASP A  1  139 ? 36.119  15.236  38.750 1.00 47.60  ? 152 ASP A N   1 
ATOM   1012 C  CA  . ASP A  1  139 ? 36.176  13.980  39.489 1.00 43.98  ? 152 ASP A CA  1 
ATOM   1013 C  C   . ASP A  1  139 ? 36.580  12.837  38.555 1.00 41.16  ? 152 ASP A C   1 
ATOM   1014 O  O   . ASP A  1  139 ? 35.784  12.409  37.722 1.00 41.68  ? 152 ASP A O   1 
ATOM   1015 C  CB  . ASP A  1  139 ? 34.851  13.698  40.181 1.00 46.86  ? 152 ASP A CB  1 
ATOM   1016 C  CG  . ASP A  1  139 ? 34.797  12.439  41.035 1.00 49.66  ? 152 ASP A CG  1 
ATOM   1017 O  OD1 . ASP A  1  139 ? 35.687  11.576  40.873 1.00 49.50  ? 152 ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A  1  139 ? 33.876  12.344  41.884 1.00 47.85  ? 152 ASP A OD2 1 
ATOM   1019 N  N   . ASN A  1  140 ? 37.803  12.319  38.718 1.00 39.58  ? 153 ASN A N   1 
ATOM   1020 C  CA  . ASN A  1  140 ? 38.367  11.354  37.779 1.00 40.11  ? 153 ASN A CA  1 
ATOM   1021 C  C   . ASN A  1  140 ? 38.261  9.918   38.308 1.00 40.00  ? 153 ASN A C   1 
ATOM   1022 O  O   . ASN A  1  140 ? 38.771  9.005   37.656 1.00 40.79  ? 153 ASN A O   1 
ATOM   1023 C  CB  . ASN A  1  140 ? 39.827  11.660  37.442 1.00 38.35  ? 153 ASN A CB  1 
ATOM   1024 C  CG  . ASN A  1  140 ? 40.749  11.541  38.640 1.00 38.26  ? 153 ASN A CG  1 
ATOM   1025 O  OD1 . ASN A  1  140 ? 40.304  11.442  39.791 1.00 39.20  ? 153 ASN A OD1 1 
ATOM   1026 N  ND2 . ASN A  1  140 ? 42.046  11.539  38.398 1.00 40.96  ? 153 ASN A ND2 1 
ATOM   1027 N  N   . HIS A  1  141 ? 37.617  9.728   39.471 1.00 38.90  ? 154 HIS A N   1 
ATOM   1028 C  CA  . HIS A  1  141 ? 37.690  8.463   40.188 1.00 44.68  ? 154 HIS A CA  1 
ATOM   1029 C  C   . HIS A  1  141 ? 36.310  7.855   40.453 1.00 42.48  ? 154 HIS A C   1 
ATOM   1030 O  O   . HIS A  1  141 ? 36.184  6.630   40.464 1.00 42.38  ? 154 HIS A O   1 
ATOM   1031 C  CB  . HIS A  1  141 ? 38.527  8.590   41.470 1.00 44.35  ? 154 HIS A CB  1 
ATOM   1032 C  CG  . HIS A  1  141 ? 38.051  9.657   42.390 1.00 48.81  ? 154 HIS A CG  1 
ATOM   1033 N  ND1 . HIS A  1  141 ? 38.538  10.949  42.338 1.00 51.17  ? 154 HIS A ND1 1 
ATOM   1034 C  CD2 . HIS A  1  141 ? 37.128  9.635   43.363 1.00 50.08  ? 154 HIS A CD2 1 
ATOM   1035 C  CE1 . HIS A  1  141 ? 37.916  11.678  43.254 1.00 54.03  ? 154 HIS A CE1 1 
ATOM   1036 N  NE2 . HIS A  1  141 ? 37.046  10.904  43.880 1.00 52.14  ? 154 HIS A NE2 1 
ATOM   1037 N  N   . SER A  1  142 ? 35.290  8.686   40.700 1.00 39.63  ? 155 SER A N   1 
ATOM   1038 C  CA  . SER A  1  142 ? 33.953  8.205   41.029 1.00 38.50  ? 155 SER A CA  1 
ATOM   1039 C  C   . SER A  1  142 ? 33.252  7.610   39.812 1.00 35.47  ? 155 SER A C   1 
ATOM   1040 O  O   . SER A  1  142 ? 33.400  8.099   38.697 1.00 37.75  ? 155 SER A O   1 
ATOM   1041 C  CB  . SER A  1  142 ? 33.094  9.305   41.612 1.00 40.18  ? 155 SER A CB  1 
ATOM   1042 O  OG  . SER A  1  142 ? 33.551  9.644   42.915 1.00 45.75  ? 155 SER A OG  1 
ATOM   1043 N  N   . PHE A  1  143 ? 32.459  6.560   40.054 1.00 36.31  ? 156 PHE A N   1 
ATOM   1044 C  CA  . PHE A  1  143 ? 31.513  6.052   39.071 1.00 36.48  ? 156 PHE A CA  1 
ATOM   1045 C  C   . PHE A  1  143 ? 30.538  7.152   38.643 1.00 36.49  ? 156 PHE A C   1 
ATOM   1046 O  O   . PHE A  1  143 ? 29.991  7.842   39.493 1.00 34.17  ? 156 PHE A O   1 
ATOM   1047 C  CB  . PHE A  1  143 ? 30.730  4.879   39.669 1.00 37.54  ? 156 PHE A CB  1 
ATOM   1048 C  CG  . PHE A  1  143 ? 29.617  4.363   38.765 1.00 36.11  ? 156 PHE A CG  1 
ATOM   1049 C  CD1 . PHE A  1  143 ? 29.894  3.452   37.745 1.00 33.95  ? 156 PHE A CD1 1 
ATOM   1050 C  CD2 . PHE A  1  143 ? 28.307  4.801   38.920 1.00 32.57  ? 156 PHE A CD2 1 
ATOM   1051 C  CE1 . PHE A  1  143 ? 28.884  2.967   36.931 1.00 33.28  ? 156 PHE A CE1 1 
ATOM   1052 C  CE2 . PHE A  1  143 ? 27.304  4.324   38.089 1.00 32.53  ? 156 PHE A CE2 1 
ATOM   1053 C  CZ  . PHE A  1  143 ? 27.589  3.401   37.106 1.00 29.59  ? 156 PHE A CZ  1 
ATOM   1054 N  N   . ASN A  1  144 ? 30.293  7.248   37.326 1.00 36.98  ? 157 ASN A N   1 
ATOM   1055 C  CA  . ASN A  1  144 ? 29.458  8.269   36.708 1.00 37.46  ? 157 ASN A CA  1 
ATOM   1056 C  C   . ASN A  1  144 ? 28.318  7.610   35.932 1.00 35.11  ? 157 ASN A C   1 
ATOM   1057 O  O   . ASN A  1  144 ? 28.560  6.945   34.924 1.00 36.94  ? 157 ASN A O   1 
ATOM   1058 C  CB  . ASN A  1  144 ? 30.317  9.126   35.786 1.00 41.96  ? 157 ASN A CB  1 
ATOM   1059 C  CG  . ASN A  1  144 ? 29.567  10.175  34.993 1.00 42.53  ? 157 ASN A CG  1 
ATOM   1060 O  OD1 . ASN A  1  144 ? 28.546  9.870   34.371 1.00 44.99  ? 157 ASN A OD1 1 
ATOM   1061 N  ND2 . ASN A  1  144 ? 30.060  11.412  34.999 1.00 51.00  ? 157 ASN A ND2 1 
ATOM   1062 N  N   . GLN A  1  145 ? 27.078  7.837   36.380 1.00 33.81  ? 158 GLN A N   1 
ATOM   1063 C  CA  . GLN A  1  145 ? 25.904  7.144   35.851 1.00 36.03  ? 158 GLN A CA  1 
ATOM   1064 C  C   . GLN A  1  145 ? 25.638  7.532   34.396 1.00 36.26  ? 158 GLN A C   1 
ATOM   1065 O  O   . GLN A  1  145 ? 25.207  6.693   33.609 1.00 39.32  ? 158 GLN A O   1 
ATOM   1066 C  CB  . GLN A  1  145 ? 24.679  7.410   36.731 1.00 33.66  ? 158 GLN A CB  1 
ATOM   1067 C  CG  . GLN A  1  145 ? 23.416  6.654   36.328 1.00 34.35  ? 158 GLN A CG  1 
ATOM   1068 C  CD  . GLN A  1  145 ? 23.493  5.147   36.496 1.00 36.14  ? 158 GLN A CD  1 
ATOM   1069 O  OE1 . GLN A  1  145 ? 23.874  4.614   37.539 1.00 33.01  ? 158 GLN A OE1 1 
ATOM   1070 N  NE2 . GLN A  1  145 ? 23.102  4.419   35.463 1.00 38.81  ? 158 GLN A NE2 1 
ATOM   1071 N  N   . THR A  1  146 ? 25.875  8.800   34.045 1.00 36.52  ? 159 THR A N   1 
ATOM   1072 C  CA  . THR A  1  146 ? 25.672  9.275   32.684 1.00 39.56  ? 159 THR A CA  1 
ATOM   1073 C  C   . THR A  1  146 ? 26.532  8.458   31.724 1.00 39.54  ? 159 THR A C   1 
ATOM   1074 O  O   . THR A  1  146 ? 26.044  8.055   30.677 1.00 44.22  ? 159 THR A O   1 
ATOM   1075 C  CB  . THR A  1  146 ? 25.994  10.767  32.572 1.00 40.26  ? 159 THR A CB  1 
ATOM   1076 O  OG1 . THR A  1  146 ? 25.137  11.441  33.486 1.00 41.08  ? 159 THR A OG1 1 
ATOM   1077 C  CG2 . THR A  1  146 ? 25.750  11.319  31.181 1.00 39.76  ? 159 THR A CG2 1 
ATOM   1078 N  N   . LEU A  1  147 ? 27.800  8.216   32.089 1.00 37.82  ? 160 LEU A N   1 
ATOM   1079 C  CA  . LEU A  1  147 ? 28.703  7.441   31.249 1.00 37.39  ? 160 LEU A CA  1 
ATOM   1080 C  C   . LEU A  1  147 ? 28.291  5.971   31.215 1.00 33.68  ? 160 LEU A C   1 
ATOM   1081 O  O   . LEU A  1  147 ? 28.381  5.336   30.170 1.00 33.72  ? 160 LEU A O   1 
ATOM   1082 C  CB  . LEU A  1  147 ? 30.152  7.623   31.699 1.00 37.99  ? 160 LEU A CB  1 
ATOM   1083 C  CG  . LEU A  1  147 ? 30.753  8.997   31.398 1.00 39.45  ? 160 LEU A CG  1 
ATOM   1084 C  CD1 . LEU A  1  147 ? 32.171  9.097   31.943 1.00 39.35  ? 160 LEU A CD1 1 
ATOM   1085 C  CD2 . LEU A  1  147 ? 30.739  9.287   29.896 1.00 37.14  ? 160 LEU A CD2 1 
ATOM   1086 N  N   . PHE A  1  148 ? 27.798  5.442   32.336 1.00 33.25  ? 161 PHE A N   1 
ATOM   1087 C  CA  . PHE A  1  148 ? 27.320  4.067   32.355 1.00 34.80  ? 161 PHE A CA  1 
ATOM   1088 C  C   . PHE A  1  148 ? 26.091  3.910   31.452 1.00 38.28  ? 161 PHE A C   1 
ATOM   1089 O  O   . PHE A  1  148 ? 25.894  2.852   30.856 1.00 38.33  ? 161 PHE A O   1 
ATOM   1090 C  CB  . PHE A  1  148 ? 27.039  3.576   33.774 1.00 35.66  ? 161 PHE A CB  1 
ATOM   1091 C  CG  . PHE A  1  148 ? 26.732  2.084   33.837 1.00 34.09  ? 161 PHE A CG  1 
ATOM   1092 C  CD1 . PHE A  1  148 ? 27.745  1.148   33.639 1.00 31.39  ? 161 PHE A CD1 1 
ATOM   1093 C  CD2 . PHE A  1  148 ? 25.436  1.625   34.084 1.00 30.10  ? 161 PHE A CD2 1 
ATOM   1094 C  CE1 . PHE A  1  148 ? 27.468  -0.211  33.664 1.00 32.83  ? 161 PHE A CE1 1 
ATOM   1095 C  CE2 . PHE A  1  148 ? 25.167  0.267   34.084 1.00 32.38  ? 161 PHE A CE2 1 
ATOM   1096 C  CZ  . PHE A  1  148 ? 26.182  -0.649  33.896 1.00 33.76  ? 161 PHE A CZ  1 
ATOM   1097 N  N   . ASP A  1  149 ? 25.268  4.959   31.343 1.00 39.07  ? 162 ASP A N   1 
ATOM   1098 C  CA  . ASP A  1  149 ? 24.102  4.933   30.470 1.00 39.81  ? 162 ASP A CA  1 
ATOM   1099 C  C   . ASP A  1  149 ? 24.542  4.806   29.008 1.00 36.89  ? 162 ASP A C   1 
ATOM   1100 O  O   . ASP A  1  149 ? 23.918  4.071   28.247 1.00 41.98  ? 162 ASP A O   1 
ATOM   1101 C  CB  . ASP A  1  149 ? 23.180  6.110   30.759 1.00 37.89  ? 162 ASP A CB  1 
ATOM   1102 C  CG  . ASP A  1  149 ? 22.432  6.054   32.086 1.00 41.59  ? 162 ASP A CG  1 
ATOM   1103 O  OD1 . ASP A  1  149 ? 22.234  4.940   32.611 1.00 39.55  ? 162 ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A  1  149 ? 22.057  7.132   32.596 1.00 46.35  ? 162 ASP A OD2 1 
ATOM   1105 N  N   . LYS A  1  150 ? 25.622  5.502   28.631 1.00 38.32  ? 163 LYS A N   1 
ATOM   1106 C  CA  . LYS A  1  150 ? 26.211  5.394   27.300 1.00 39.70  ? 163 LYS A CA  1 
ATOM   1107 C  C   . LYS A  1  150 ? 26.766  3.982   27.073 1.00 39.31  ? 163 LYS A C   1 
ATOM   1108 O  O   . LYS A  1  150 ? 26.642  3.428   25.990 1.00 39.24  ? 163 LYS A O   1 
ATOM   1109 C  CB  . LYS A  1  150 ? 27.300  6.458   27.110 1.00 40.81  ? 163 LYS A CB  1 
ATOM   1110 C  CG  . LYS A  1  150 ? 27.886  6.556   25.707 1.00 43.75  ? 163 LYS A CG  1 
ATOM   1111 C  CD  . LYS A  1  150 ? 29.096  7.475   25.599 1.00 49.10  ? 163 LYS A CD  1 
ATOM   1112 C  CE  . LYS A  1  150 ? 29.577  7.790   24.204 1.00 54.05  ? 163 LYS A CE  1 
ATOM   1113 N  NZ  . LYS A  1  150 ? 28.900  8.967   23.656 1.00 61.47  ? 163 LYS A NZ  1 
ATOM   1114 N  N   . PHE A  1  151 ? 27.384  3.407   28.109 1.00 40.85  ? 164 PHE A N   1 
ATOM   1115 C  CA  . PHE A  1  151 ? 27.832  2.025   28.100 1.00 38.32  ? 164 PHE A CA  1 
ATOM   1116 C  C   . PHE A  1  151 ? 26.669  1.103   27.750 1.00 37.20  ? 164 PHE A C   1 
ATOM   1117 O  O   . PHE A  1  151 ? 26.825  0.199   26.933 1.00 35.98  ? 164 PHE A O   1 
ATOM   1118 C  CB  . PHE A  1  151 ? 28.382  1.642   29.479 1.00 39.49  ? 164 PHE A CB  1 
ATOM   1119 C  CG  . PHE A  1  151 ? 29.159  0.336   29.560 1.00 39.11  ? 164 PHE A CG  1 
ATOM   1120 C  CD1 . PHE A  1  151 ? 30.534  0.357   29.405 1.00 39.38  ? 164 PHE A CD1 1 
ATOM   1121 C  CD2 . PHE A  1  151 ? 28.537  -0.885  29.833 1.00 38.23  ? 164 PHE A CD2 1 
ATOM   1122 C  CE1 . PHE A  1  151 ? 31.278  -0.799  29.491 1.00 40.63  ? 164 PHE A CE1 1 
ATOM   1123 C  CE2 . PHE A  1  151 ? 29.289  -2.058  29.881 1.00 40.12  ? 164 PHE A CE2 1 
ATOM   1124 C  CZ  . PHE A  1  151 ? 30.660  -2.009  29.698 1.00 38.82  ? 164 PHE A CZ  1 
ATOM   1125 N  N   . VAL A  1  152 ? 25.524  1.313   28.419 1.00 36.31  ? 165 VAL A N   1 
ATOM   1126 C  CA  . VAL A  1  152 ? 24.343  0.493   28.211 1.00 36.27  ? 165 VAL A CA  1 
ATOM   1127 C  C   . VAL A  1  152 ? 23.809  0.713   26.791 1.00 36.47  ? 165 VAL A C   1 
ATOM   1128 O  O   . VAL A  1  152 ? 23.453  -0.250  26.112 1.00 34.32  ? 165 VAL A O   1 
ATOM   1129 C  CB  . VAL A  1  152 ? 23.254  0.760   29.269 1.00 34.55  ? 165 VAL A CB  1 
ATOM   1130 C  CG1 . VAL A  1  152 ? 21.947  0.059   28.938 1.00 36.52  ? 165 VAL A CG1 1 
ATOM   1131 C  CG2 . VAL A  1  152 ? 23.693  0.366   30.667 1.00 34.75  ? 165 VAL A CG2 1 
ATOM   1132 N  N   . ASP A  1  153 ? 23.756  1.978   26.357 1.00 34.03  ? 166 ASP A N   1 
ATOM   1133 C  CA  . ASP A  1  153 ? 23.234  2.331   25.046 1.00 40.24  ? 166 ASP A CA  1 
ATOM   1134 C  C   . ASP A  1  153 ? 24.018  1.607   23.950 1.00 41.41  ? 166 ASP A C   1 
ATOM   1135 O  O   . ASP A  1  153 ? 23.421  0.977   23.073 1.00 43.35  ? 166 ASP A O   1 
ATOM   1136 C  CB  . ASP A  1  153 ? 23.208  3.841   24.840 1.00 44.53  ? 166 ASP A CB  1 
ATOM   1137 C  CG  . ASP A  1  153 ? 22.607  4.323   23.520 1.00 48.52  ? 166 ASP A CG  1 
ATOM   1138 O  OD1 . ASP A  1  153 ? 21.525  3.834   23.156 1.00 51.01  ? 166 ASP A OD1 1 
ATOM   1139 O  OD2 . ASP A  1  153 ? 23.210  5.205   22.869 1.00 52.67  ? 166 ASP A OD2 1 
ATOM   1140 N  N   . PHE A  1  154 ? 25.352  1.695   24.017 1.00 38.50  ? 167 PHE A N   1 
ATOM   1141 C  CA  . PHE A  1  154 ? 26.210  1.120   22.997 1.00 38.99  ? 167 PHE A CA  1 
ATOM   1142 C  C   . PHE A  1  154 ? 26.118  -0.401  23.026 1.00 35.98  ? 167 PHE A C   1 
ATOM   1143 O  O   . PHE A  1  154 ? 26.194  -1.050  21.986 1.00 36.28  ? 167 PHE A O   1 
ATOM   1144 C  CB  . PHE A  1  154 ? 27.651  1.609   23.169 1.00 41.35  ? 167 PHE A CB  1 
ATOM   1145 C  CG  . PHE A  1  154 ? 27.971  2.895   22.422 1.00 39.31  ? 167 PHE A CG  1 
ATOM   1146 C  CD1 . PHE A  1  154 ? 27.362  4.095   22.770 1.00 37.56  ? 167 PHE A CD1 1 
ATOM   1147 C  CD2 . PHE A  1  154 ? 28.892  2.900   21.387 1.00 40.56  ? 167 PHE A CD2 1 
ATOM   1148 C  CE1 . PHE A  1  154 ? 27.662  5.263   22.090 1.00 36.04  ? 167 PHE A CE1 1 
ATOM   1149 C  CE2 . PHE A  1  154 ? 29.185  4.073   20.708 1.00 40.82  ? 167 PHE A CE2 1 
ATOM   1150 C  CZ  . PHE A  1  154 ? 28.564  5.245   21.060 1.00 39.72  ? 167 PHE A CZ  1 
ATOM   1151 N  N   . SER A  1  155 ? 25.961  -0.972  24.218 1.00 36.29  ? 168 SER A N   1 
ATOM   1152 C  CA  . SER A  1  155 ? 25.734  -2.405  24.343 1.00 40.27  ? 168 SER A CA  1 
ATOM   1153 C  C   . SER A  1  155 ? 24.404  -2.798  23.682 1.00 39.34  ? 168 SER A C   1 
ATOM   1154 O  O   . SER A  1  155 ? 24.317  -3.851  23.047 1.00 41.89  ? 168 SER A O   1 
ATOM   1155 C  CB  . SER A  1  155 ? 25.791  -2.836  25.789 1.00 40.24  ? 168 SER A CB  1 
ATOM   1156 O  OG  . SER A  1  155 ? 27.039  -2.502  26.384 1.00 48.27  ? 168 SER A OG  1 
ATOM   1157 N  N   . ASN A  1  156 ? 23.369  -1.953  23.833 1.00 38.40  ? 169 ASN A N   1 
ATOM   1158 C  CA  . ASN A  1  156 ? 22.081  -2.195  23.198 1.00 37.48  ? 169 ASN A CA  1 
ATOM   1159 C  C   . ASN A  1  156 ? 22.226  -2.111  21.681 1.00 42.65  ? 169 ASN A C   1 
ATOM   1160 O  O   . ASN A  1  156 ? 21.666  -2.923  20.956 1.00 39.19  ? 169 ASN A O   1 
ATOM   1161 C  CB  . ASN A  1  156 ? 21.001  -1.233  23.679 1.00 36.59  ? 169 ASN A CB  1 
ATOM   1162 C  CG  . ASN A  1  156 ? 20.547  -1.512  25.095 1.00 38.01  ? 169 ASN A CG  1 
ATOM   1163 O  OD1 . ASN A  1  156 ? 20.716  -2.620  25.620 1.00 43.75  ? 169 ASN A OD1 1 
ATOM   1164 N  ND2 . ASN A  1  156 ? 19.965  -0.511  25.731 1.00 36.09  ? 169 ASN A ND2 1 
ATOM   1165 N  N   . ARG A  1  157 ? 23.020  -1.142  21.205 1.00 43.01  ? 170 ARG A N   1 
ATOM   1166 C  CA  . ARG A  1  157 ? 23.105  -0.858  19.783 1.00 39.01  ? 170 ARG A CA  1 
ATOM   1167 C  C   . ARG A  1  157 ? 24.002  -1.838  19.031 1.00 39.53  ? 170 ARG A C   1 
ATOM   1168 O  O   . ARG A  1  157 ? 23.777  -2.055  17.845 1.00 45.14  ? 170 ARG A O   1 
ATOM   1169 C  CB  . ARG A  1  157 ? 23.619  0.568   19.585 1.00 37.91  ? 170 ARG A CB  1 
ATOM   1170 C  CG  . ARG A  1  157 ? 22.533  1.583   19.879 1.00 41.23  ? 170 ARG A CG  1 
ATOM   1171 C  CD  . ARG A  1  157 ? 23.084  2.947   20.171 1.00 44.91  ? 170 ARG A CD  1 
ATOM   1172 N  NE  . ARG A  1  157 ? 23.966  3.463   19.127 1.00 46.59  ? 170 ARG A NE  1 
ATOM   1173 C  CZ  . ARG A  1  157 ? 24.568  4.633   19.200 1.00 48.00  ? 170 ARG A CZ  1 
ATOM   1174 N  NH1 . ARG A  1  157 ? 25.380  4.996   18.231 1.00 48.35  ? 170 ARG A NH1 1 
ATOM   1175 N  NH2 . ARG A  1  157 ? 24.382  5.428   20.242 1.00 50.42  ? 170 ARG A NH2 1 
ATOM   1176 N  N   . TYR A  1  158 ? 25.022  -2.410  19.691 1.00 41.51  ? 171 TYR A N   1 
ATOM   1177 C  CA  . TYR A  1  158 ? 26.039  -3.172  18.971 1.00 39.33  ? 171 TYR A CA  1 
ATOM   1178 C  C   . TYR A  1  158 ? 26.229  -4.581  19.527 1.00 38.52  ? 171 TYR A C   1 
ATOM   1179 O  O   . TYR A  1  158 ? 26.919  -5.392  18.896 1.00 36.37  ? 171 TYR A O   1 
ATOM   1180 C  CB  . TYR A  1  158 ? 27.384  -2.436  18.948 1.00 36.42  ? 171 TYR A CB  1 
ATOM   1181 C  CG  . TYR A  1  158 ? 27.319  -1.070  18.285 1.00 38.36  ? 171 TYR A CG  1 
ATOM   1182 C  CD1 . TYR A  1  158 ? 27.147  -0.930  16.908 1.00 40.88  ? 171 TYR A CD1 1 
ATOM   1183 C  CD2 . TYR A  1  158 ? 27.392  0.083   19.042 1.00 40.57  ? 171 TYR A CD2 1 
ATOM   1184 C  CE1 . TYR A  1  158 ? 27.057  0.320   16.312 1.00 41.75  ? 171 TYR A CE1 1 
ATOM   1185 C  CE2 . TYR A  1  158 ? 27.335  1.339   18.458 1.00 44.20  ? 171 TYR A CE2 1 
ATOM   1186 C  CZ  . TYR A  1  158 ? 27.163  1.458   17.089 1.00 48.45  ? 171 TYR A CZ  1 
ATOM   1187 O  OH  . TYR A  1  158 ? 27.068  2.696   16.515 1.00 52.96  ? 171 TYR A OH  1 
ATOM   1188 N  N   . GLY A  1  159 ? 25.635  -4.883  20.693 1.00 35.39  ? 172 GLY A N   1 
ATOM   1189 C  CA  . GLY A  1  159 ? 25.923  -6.144  21.360 1.00 34.37  ? 172 GLY A CA  1 
ATOM   1190 C  C   . GLY A  1  159 ? 24.673  -6.879  21.830 1.00 37.52  ? 172 GLY A C   1 
ATOM   1191 O  O   . GLY A  1  159 ? 24.763  -7.736  22.697 1.00 36.59  ? 172 GLY A O   1 
ATOM   1192 N  N   . GLY A  1  160 ? 23.514  -6.569  21.241 1.00 40.57  ? 173 GLY A N   1 
ATOM   1193 C  CA  . GLY A  1  160 ? 22.279  -7.246  21.584 1.00 40.38  ? 173 GLY A CA  1 
ATOM   1194 C  C   . GLY A  1  160 ? 21.903  -7.077  23.056 1.00 42.68  ? 173 GLY A C   1 
ATOM   1195 O  O   . GLY A  1  160 ? 21.166  -7.903  23.578 1.00 44.10  ? 173 GLY A O   1 
ATOM   1196 N  N   . GLY A  1  161 ? 22.392  -6.005  23.704 1.00 43.22  ? 174 GLY A N   1 
ATOM   1197 C  CA  . GLY A  1  161 ? 22.123  -5.737  25.111 1.00 43.87  ? 174 GLY A CA  1 
ATOM   1198 C  C   . GLY A  1  161 ? 23.283  -6.137  26.024 1.00 41.15  ? 174 GLY A C   1 
ATOM   1199 O  O   . GLY A  1  161 ? 23.210  -5.942  27.233 1.00 38.94  ? 174 GLY A O   1 
ATOM   1200 N  N   . PHE A  1  162 ? 24.352  -6.683  25.430 1.00 39.97  ? 175 PHE A N   1 
ATOM   1201 C  CA  . PHE A  1  162 ? 25.519  -7.173  26.155 1.00 39.43  ? 175 PHE A CA  1 
ATOM   1202 C  C   . PHE A  1  162 ? 26.782  -6.460  25.668 1.00 36.71  ? 175 PHE A C   1 
ATOM   1203 O  O   . PHE A  1  162 ? 26.848  -5.996  24.536 1.00 35.87  ? 175 PHE A O   1 
ATOM   1204 C  CB  . PHE A  1  162 ? 25.643  -8.687  25.954 1.00 42.34  ? 175 PHE A CB  1 
ATOM   1205 C  CG  . PHE A  1  162 ? 24.499  -9.503  26.541 1.00 45.60  ? 175 PHE A CG  1 
ATOM   1206 C  CD1 . PHE A  1  162 ? 24.567  -9.971  27.846 1.00 43.93  ? 175 PHE A CD1 1 
ATOM   1207 C  CD2 . PHE A  1  162 ? 23.361  -9.803  25.789 1.00 43.20  ? 175 PHE A CD2 1 
ATOM   1208 C  CE1 . PHE A  1  162 ? 23.521  -10.707 28.387 1.00 45.51  ? 175 PHE A CE1 1 
ATOM   1209 C  CE2 . PHE A  1  162 ? 22.326  -10.543 26.330 1.00 42.46  ? 175 PHE A CE2 1 
ATOM   1210 C  CZ  . PHE A  1  162 ? 22.401  -10.976 27.632 1.00 48.00  ? 175 PHE A CZ  1 
ATOM   1211 N  N   . TYR A  1  163 ? 27.794  -6.368  26.536 1.00 38.15  ? 176 TYR A N   1 
ATOM   1212 C  CA  . TYR A  1  163 ? 29.076  -5.799  26.147 1.00 36.32  ? 176 TYR A CA  1 
ATOM   1213 C  C   . TYR A  1  163 ? 29.972  -6.890  25.552 1.00 33.52  ? 176 TYR A C   1 
ATOM   1214 O  O   . TYR A  1  163 ? 30.272  -7.874  26.230 1.00 34.50  ? 176 TYR A O   1 
ATOM   1215 C  CB  . TYR A  1  163 ? 29.699  -5.109  27.363 1.00 37.03  ? 176 TYR A CB  1 
ATOM   1216 C  CG  . TYR A  1  163 ? 30.957  -4.314  27.054 1.00 36.61  ? 176 TYR A CG  1 
ATOM   1217 C  CD1 . TYR A  1  163 ? 30.879  -3.043  26.513 1.00 39.16  ? 176 TYR A CD1 1 
ATOM   1218 C  CD2 . TYR A  1  163 ? 32.221  -4.825  27.311 1.00 40.19  ? 176 TYR A CD2 1 
ATOM   1219 C  CE1 . TYR A  1  163 ? 32.020  -2.306  26.227 1.00 39.10  ? 176 TYR A CE1 1 
ATOM   1220 C  CE2 . TYR A  1  163 ? 33.369  -4.095  27.034 1.00 38.98  ? 176 TYR A CE2 1 
ATOM   1221 C  CZ  . TYR A  1  163 ? 33.273  -2.832  26.489 1.00 38.36  ? 176 TYR A CZ  1 
ATOM   1222 O  OH  . TYR A  1  163 ? 34.422  -2.134  26.225 1.00 34.80  ? 176 TYR A OH  1 
ATOM   1223 N  N   . ASN A  1  164 ? 30.365  -6.703  24.279 1.00 34.55  ? 177 ASN A N   1 
ATOM   1224 C  CA  . ASN A  1  164 ? 31.257  -7.597  23.549 1.00 37.03  ? 177 ASN A CA  1 
ATOM   1225 C  C   . ASN A  1  164 ? 32.284  -6.745  22.792 1.00 39.79  ? 177 ASN A C   1 
ATOM   1226 O  O   . ASN A  1  164 ? 32.296  -5.513  22.914 1.00 36.81  ? 177 ASN A O   1 
ATOM   1227 C  CB  . ASN A  1  164 ? 30.465  -8.606  22.704 1.00 41.02  ? 177 ASN A CB  1 
ATOM   1228 C  CG  . ASN A  1  164 ? 29.874  -8.074  21.405 1.00 44.38  ? 177 ASN A CG  1 
ATOM   1229 O  OD1 . ASN A  1  164 ? 30.066  -6.900  21.080 1.00 41.62  ? 177 ASN A OD1 1 
ATOM   1230 N  ND2 . ASN A  1  164 ? 29.153  -8.904  20.637 1.00 47.10  ? 177 ASN A ND2 1 
ATOM   1231 N  N   . LEU A  1  165 ? 33.142  -7.404  21.993 1.00 42.46  ? 178 LEU A N   1 
ATOM   1232 C  CA  . LEU A  1  165 ? 34.252  -6.734  21.319 1.00 40.46  ? 178 LEU A CA  1 
ATOM   1233 C  C   . LEU A  1  165 ? 33.772  -5.653  20.352 1.00 41.52  ? 178 LEU A C   1 
ATOM   1234 O  O   . LEU A  1  165 ? 34.432  -4.623  20.212 1.00 43.04  ? 178 LEU A O   1 
ATOM   1235 C  CB  . LEU A  1  165 ? 35.139  -7.722  20.572 1.00 44.43  ? 178 LEU A CB  1 
ATOM   1236 C  CG  . LEU A  1  165 ? 36.513  -8.016  21.172 1.00 52.48  ? 178 LEU A CG  1 
ATOM   1237 C  CD1 . LEU A  1  165 ? 37.261  -8.938  20.228 1.00 53.11  ? 178 LEU A CD1 1 
ATOM   1238 C  CD2 . LEU A  1  165 ? 37.342  -6.777  21.423 1.00 54.36  ? 178 LEU A CD2 1 
ATOM   1239 N  N   . THR A  1  166 ? 32.665  -5.910  19.646 1.00 37.77  ? 179 THR A N   1 
ATOM   1240 C  CA  . THR A  1  166 ? 32.095  -4.929  18.733 1.00 40.02  ? 179 THR A CA  1 
ATOM   1241 C  C   . THR A  1  166 ? 31.732  -3.670  19.514 1.00 38.94  ? 179 THR A C   1 
ATOM   1242 O  O   . THR A  1  166 ? 32.040  -2.567  19.075 1.00 42.14  ? 179 THR A O   1 
ATOM   1243 C  CB  . THR A  1  166 ? 30.876  -5.510  18.001 1.00 42.94  ? 179 THR A CB  1 
ATOM   1244 O  OG1 . THR A  1  166 ? 31.226  -6.769  17.432 1.00 39.40  ? 179 THR A OG1 1 
ATOM   1245 C  CG2 . THR A  1  166 ? 30.358  -4.601  16.901 1.00 40.41  ? 179 THR A CG2 1 
ATOM   1246 N  N   . VAL A  1  167 ? 31.094  -3.837  20.683 1.00 39.36  ? 180 VAL A N   1 
ATOM   1247 C  CA  . VAL A  1  167 ? 30.694  -2.705  21.514 1.00 38.94  ? 180 VAL A CA  1 
ATOM   1248 C  C   . VAL A  1  167 ? 31.950  -1.947  21.950 1.00 37.56  ? 180 VAL A C   1 
ATOM   1249 O  O   . VAL A  1  167 ? 31.988  -0.718  21.905 1.00 37.15  ? 180 VAL A O   1 
ATOM   1250 C  CB  . VAL A  1  167 ? 29.861  -3.096  22.752 1.00 37.73  ? 180 VAL A CB  1 
ATOM   1251 C  CG1 . VAL A  1  167 ? 29.374  -1.872  23.507 1.00 34.81  ? 180 VAL A CG1 1 
ATOM   1252 C  CG2 . VAL A  1  167 ? 28.687  -4.006  22.410 1.00 40.83  ? 180 VAL A CG2 1 
ATOM   1253 N  N   . ALA A  1  168 ? 32.969  -2.696  22.387 1.00 38.18  ? 181 ALA A N   1 
ATOM   1254 C  CA  . ALA A  1  168 ? 34.217  -2.109  22.858 1.00 39.12  ? 181 ALA A CA  1 
ATOM   1255 C  C   . ALA A  1  168 ? 34.817  -1.200  21.789 1.00 37.03  ? 181 ALA A C   1 
ATOM   1256 O  O   . ALA A  1  168 ? 35.201  -0.071  22.081 1.00 39.41  ? 181 ALA A O   1 
ATOM   1257 C  CB  . ALA A  1  168 ? 35.193  -3.197  23.251 1.00 40.78  ? 181 ALA A CB  1 
ATOM   1258 N  N   . GLY A  1  169 ? 34.871  -1.692  20.545 1.00 39.54  ? 182 GLY A N   1 
ATOM   1259 C  CA  . GLY A  1  169 ? 35.425  -0.929  19.437 1.00 37.46  ? 182 GLY A CA  1 
ATOM   1260 C  C   . GLY A  1  169 ? 34.700  0.399   19.242 1.00 38.37  ? 182 GLY A C   1 
ATOM   1261 O  O   . GLY A  1  169 ? 35.337  1.439   19.069 1.00 41.46  ? 182 GLY A O   1 
ATOM   1262 N  N   . GLU A  1  170 ? 33.361  0.353   19.274 1.00 40.41  ? 183 GLU A N   1 
ATOM   1263 C  CA  . GLU A  1  170 ? 32.541  1.528   19.021 1.00 40.02  ? 183 GLU A CA  1 
ATOM   1264 C  C   . GLU A  1  170 ? 32.602  2.486   20.208 1.00 38.48  ? 183 GLU A C   1 
ATOM   1265 O  O   . GLU A  1  170 ? 32.768  3.692   20.021 1.00 44.05  ? 183 GLU A O   1 
ATOM   1266 C  CB  . GLU A  1  170 ? 31.103  1.116   18.690 1.00 47.32  ? 183 GLU A CB  1 
ATOM   1267 C  CG  . GLU A  1  170 ? 30.938  0.300   17.405 1.00 49.51  ? 183 GLU A CG  1 
ATOM   1268 C  CD  . GLU A  1  170 ? 31.681  0.873   16.211 1.00 50.66  ? 183 GLU A CD  1 
ATOM   1269 O  OE1 . GLU A  1  170 ? 31.496  2.077   15.949 1.00 46.47  ? 183 GLU A OE1 1 
ATOM   1270 O  OE2 . GLU A  1  170 ? 32.478  0.137   15.585 1.00 56.23  ? 183 GLU A OE2 1 
ATOM   1271 N  N   . LEU A  1  171 ? 32.481  1.958   21.434 1.00 37.32  ? 184 LEU A N   1 
ATOM   1272 C  CA  . LEU A  1  171 ? 32.463  2.800   22.623 1.00 35.00  ? 184 LEU A CA  1 
ATOM   1273 C  C   . LEU A  1  171 ? 33.784  3.556   22.785 1.00 34.23  ? 184 LEU A C   1 
ATOM   1274 O  O   . LEU A  1  171 ? 33.781  4.745   23.087 1.00 32.58  ? 184 LEU A O   1 
ATOM   1275 C  CB  . LEU A  1  171 ? 32.121  1.972   23.861 1.00 35.51  ? 184 LEU A CB  1 
ATOM   1276 C  CG  . LEU A  1  171 ? 32.001  2.752   25.176 1.00 36.24  ? 184 LEU A CG  1 
ATOM   1277 C  CD1 . LEU A  1  171 ? 30.907  3.803   25.107 1.00 36.08  ? 184 LEU A CD1 1 
ATOM   1278 C  CD2 . LEU A  1  171 ? 31.755  1.810   26.339 1.00 38.61  ? 184 LEU A CD2 1 
ATOM   1279 N  N   . ARG A  1  172 ? 34.914  2.874   22.578 1.00 39.94  ? 185 ARG A N   1 
ATOM   1280 C  CA  . ARG A  1  172 ? 36.232  3.488   22.733 1.00 40.40  ? 185 ARG A CA  1 
ATOM   1281 C  C   . ARG A  1  172 ? 36.337  4.750   21.871 1.00 43.30  ? 185 ARG A C   1 
ATOM   1282 O  O   . ARG A  1  172 ? 36.756  5.800   22.359 1.00 42.56  ? 185 ARG A O   1 
ATOM   1283 C  CB  . ARG A  1  172 ? 37.300  2.420   22.448 1.00 39.83  ? 185 ARG A CB  1 
ATOM   1284 C  CG  . ARG A  1  172 ? 38.723  2.853   22.125 1.00 43.81  ? 185 ARG A CG  1 
ATOM   1285 C  CD  . ARG A  1  172 ? 39.372  3.767   23.152 1.00 51.49  ? 185 ARG A CD  1 
ATOM   1286 N  NE  . ARG A  1  172 ? 39.219  3.392   24.567 1.00 49.33  ? 185 ARG A NE  1 
ATOM   1287 C  CZ  . ARG A  1  172 ? 38.768  4.185   25.537 1.00 47.67  ? 185 ARG A CZ  1 
ATOM   1288 N  NH1 . ARG A  1  172 ? 38.414  5.435   25.272 1.00 47.65  ? 185 ARG A NH1 1 
ATOM   1289 N  NH2 . ARG A  1  172 ? 38.687  3.739   26.784 1.00 49.32  ? 185 ARG A NH2 1 
ATOM   1290 N  N   . TYR A  1  173 ? 35.936  4.654   20.594 1.00 46.48  ? 186 TYR A N   1 
ATOM   1291 C  CA  . TYR A  1  173 ? 36.060  5.763   19.657 1.00 43.37  ? 186 TYR A CA  1 
ATOM   1292 C  C   . TYR A  1  173 ? 35.123  6.895   20.077 1.00 43.78  ? 186 TYR A C   1 
ATOM   1293 O  O   . TYR A  1  173 ? 35.533  8.053   20.094 1.00 44.22  ? 186 TYR A O   1 
ATOM   1294 C  CB  . TYR A  1  173 ? 35.791  5.273   18.229 1.00 47.49  ? 186 TYR A CB  1 
ATOM   1295 C  CG  . TYR A  1  173 ? 35.886  6.349   17.152 1.00 49.27  ? 186 TYR A CG  1 
ATOM   1296 C  CD1 . TYR A  1  173 ? 37.109  6.925   16.826 1.00 51.24  ? 186 TYR A CD1 1 
ATOM   1297 C  CD2 . TYR A  1  173 ? 34.763  6.784   16.453 1.00 52.66  ? 186 TYR A CD2 1 
ATOM   1298 C  CE1 . TYR A  1  173 ? 37.215  7.907   15.857 1.00 48.54  ? 186 TYR A CE1 1 
ATOM   1299 C  CE2 . TYR A  1  173 ? 34.854  7.767   15.477 1.00 53.52  ? 186 TYR A CE2 1 
ATOM   1300 C  CZ  . TYR A  1  173 ? 36.086  8.323   15.174 1.00 52.32  ? 186 TYR A CZ  1 
ATOM   1301 O  OH  . TYR A  1  173 ? 36.191  9.293   14.221 1.00 52.38  ? 186 TYR A OH  1 
ATOM   1302 N  N   . SER A  1  174 ? 33.868  6.559   20.418 1.00 42.98  ? 187 SER A N   1 
ATOM   1303 C  CA  . SER A  1  174 ? 32.878  7.569   20.764 1.00 40.11  ? 187 SER A CA  1 
ATOM   1304 C  C   . SER A  1  174 ? 33.330  8.375   21.978 1.00 37.48  ? 187 SER A C   1 
ATOM   1305 O  O   . SER A  1  174 ? 33.187  9.596   21.982 1.00 37.91  ? 187 SER A O   1 
ATOM   1306 C  CB  . SER A  1  174 ? 31.522  6.960   20.991 1.00 40.01  ? 187 SER A CB  1 
ATOM   1307 O  OG  . SER A  1  174 ? 30.572  7.955   21.355 1.00 41.02  ? 187 SER A OG  1 
ATOM   1308 N  N   . ARG A  1  175 ? 33.918  7.695   22.975 1.00 39.00  ? 188 ARG A N   1 
ATOM   1309 C  CA  . ARG A  1  175 ? 34.379  8.352   24.199 1.00 41.05  ? 188 ARG A CA  1 
ATOM   1310 C  C   . ARG A  1  175 ? 35.522  9.318   23.889 1.00 40.06  ? 188 ARG A C   1 
ATOM   1311 O  O   . ARG A  1  175 ? 35.587  10.406  24.463 1.00 38.34  ? 188 ARG A O   1 
ATOM   1312 C  CB  . ARG A  1  175 ? 34.793  7.359   25.300 1.00 39.27  ? 188 ARG A CB  1 
ATOM   1313 C  CG  . ARG A  1  175 ? 33.640  6.543   25.877 1.00 40.46  ? 188 ARG A CG  1 
ATOM   1314 C  CD  . ARG A  1  175 ? 32.659  7.386   26.700 1.00 39.30  ? 188 ARG A CD  1 
ATOM   1315 N  NE  . ARG A  1  175 ? 33.330  7.967   27.863 1.00 39.63  ? 188 ARG A NE  1 
ATOM   1316 C  CZ  . ARG A  1  175 ? 33.657  9.240   28.071 1.00 41.94  ? 188 ARG A CZ  1 
ATOM   1317 N  NH1 . ARG A  1  175 ? 33.183  10.198  27.307 1.00 43.11  ? 188 ARG A NH1 1 
ATOM   1318 N  NH2 . ARG A  1  175 ? 34.441  9.564   29.087 1.00 41.71  ? 188 ARG A NH2 1 
ATOM   1319 N  N   . ILE A  1  176 ? 36.409  8.916   22.966 1.00 40.64  ? 189 ILE A N   1 
ATOM   1320 C  CA  . ILE A  1  176 ? 37.462  9.800   22.491 1.00 41.56  ? 189 ILE A CA  1 
ATOM   1321 C  C   . ILE A  1  176 ? 36.836  11.064  21.895 1.00 41.57  ? 189 ILE A C   1 
ATOM   1322 O  O   . ILE A  1  176 ? 37.233  12.175  22.253 1.00 42.09  ? 189 ILE A O   1 
ATOM   1323 C  CB  . ILE A  1  176 ? 38.381  9.067   21.496 1.00 43.61  ? 189 ILE A CB  1 
ATOM   1324 C  CG1 . ILE A  1  176 ? 39.237  8.010   22.193 1.00 42.03  ? 189 ILE A CG1 1 
ATOM   1325 C  CG2 . ILE A  1  176 ? 39.252  10.061  20.725 1.00 45.86  ? 189 ILE A CG2 1 
ATOM   1326 C  CD1 . ILE A  1  176 ? 39.954  7.067   21.244 1.00 42.70  ? 189 ILE A CD1 1 
ATOM   1327 N  N   . GLN A  1  177 ? 35.829  10.888  21.028 1.00 40.48  ? 190 GLN A N   1 
ATOM   1328 C  CA  . GLN A  1  177 ? 35.137  12.019  20.424 1.00 42.90  ? 190 GLN A CA  1 
ATOM   1329 C  C   . GLN A  1  177 ? 34.502  12.920  21.488 1.00 39.57  ? 190 GLN A C   1 
ATOM   1330 O  O   . GLN A  1  177 ? 34.661  14.139  21.435 1.00 42.71  ? 190 GLN A O   1 
ATOM   1331 C  CB  . GLN A  1  177 ? 34.152  11.530  19.361 1.00 48.34  ? 190 GLN A CB  1 
ATOM   1332 C  CG  . GLN A  1  177 ? 34.821  10.865  18.162 1.00 49.10  ? 190 GLN A CG  1 
ATOM   1333 C  CD  . GLN A  1  177 ? 35.705  11.807  17.369 1.00 56.53  ? 190 GLN A CD  1 
ATOM   1334 O  OE1 . GLN A  1  177 ? 35.550  13.033  17.396 1.00 61.62  ? 190 GLN A OE1 1 
ATOM   1335 N  NE2 . GLN A  1  177 ? 36.632  11.236  16.616 1.00 62.55  ? 190 GLN A NE2 1 
ATOM   1336 N  N   . ASP A  1  178 ? 33.825  12.330  22.482 1.00 40.30  ? 191 ASP A N   1 
ATOM   1337 C  CA  . ASP A  1  178 ? 33.235  13.100  23.572 1.00 40.91  ? 191 ASP A CA  1 
ATOM   1338 C  C   . ASP A  1  178 ? 34.263  14.055  24.177 1.00 43.43  ? 191 ASP A C   1 
ATOM   1339 O  O   . ASP A  1  178 ? 33.975  15.228  24.399 1.00 45.86  ? 191 ASP A O   1 
ATOM   1340 C  CB  . ASP A  1  178 ? 32.687  12.203  24.675 1.00 46.12  ? 191 ASP A CB  1 
ATOM   1341 C  CG  . ASP A  1  178 ? 31.509  11.315  24.302 1.00 48.07  ? 191 ASP A CG  1 
ATOM   1342 O  OD1 . ASP A  1  178 ? 30.919  11.538  23.227 1.00 51.65  ? 191 ASP A OD1 1 
ATOM   1343 O  OD2 . ASP A  1  178 ? 31.192  10.406  25.093 1.00 49.09  ? 191 ASP A OD2 1 
ATOM   1344 N  N   . SER A  1  179 ? 35.466  13.539  24.460 1.00 46.30  ? 192 SER A N   1 
ATOM   1345 C  CA  . SER A  1  179 ? 36.502  14.325  25.114 1.00 45.78  ? 192 SER A CA  1 
ATOM   1346 C  C   . SER A  1  179 ? 37.069  15.395  24.172 1.00 44.81  ? 192 SER A C   1 
ATOM   1347 O  O   . SER A  1  179 ? 37.371  16.501  24.619 1.00 42.35  ? 192 SER A O   1 
ATOM   1348 C  CB  . SER A  1  179 ? 37.598  13.432  25.679 1.00 46.57  ? 192 SER A CB  1 
ATOM   1349 O  OG  . SER A  1  179 ? 37.222  12.899  26.946 1.00 48.16  ? 192 SER A OG  1 
ATOM   1350 N  N   . ILE A  1  180 ? 37.243  15.068  22.883 1.00 44.85  ? 193 ILE A N   1 
ATOM   1351 C  CA  . ILE A  1  180 ? 37.717  16.052  21.918 1.00 49.34  ? 193 ILE A CA  1 
ATOM   1352 C  C   . ILE A  1  180 ? 36.772  17.254  21.929 1.00 48.50  ? 193 ILE A C   1 
ATOM   1353 O  O   . ILE A  1  180 ? 37.221  18.397  21.991 1.00 49.06  ? 193 ILE A O   1 
ATOM   1354 C  CB  . ILE A  1  180 ? 37.863  15.436  20.510 1.00 49.70  ? 193 ILE A CB  1 
ATOM   1355 C  CG1 . ILE A  1  180 ? 39.043  14.470  20.459 1.00 47.18  ? 193 ILE A CG1 1 
ATOM   1356 C  CG2 . ILE A  1  180 ? 37.988  16.520  19.434 1.00 47.44  ? 193 ILE A CG2 1 
ATOM   1357 C  CD1 . ILE A  1  180 ? 39.162  13.685  19.167 1.00 46.26  ? 193 ILE A CD1 1 
ATOM   1358 N  N   . ALA A  1  181 ? 35.464  16.968  21.905 1.00 47.36  ? 194 ALA A N   1 
ATOM   1359 C  CA  . ALA A  1  181 ? 34.421  17.980  21.782 1.00 46.50  ? 194 ALA A CA  1 
ATOM   1360 C  C   . ALA A  1  181 ? 34.228  18.790  23.061 1.00 45.25  ? 194 ALA A C   1 
ATOM   1361 O  O   . ALA A  1  181 ? 33.753  19.910  22.965 1.00 51.76  ? 194 ALA A O   1 
ATOM   1362 C  CB  . ALA A  1  181 ? 33.113  17.330  21.384 1.00 45.26  ? 194 ALA A CB  1 
ATOM   1363 N  N   . THR A  1  182 ? 34.560  18.238  24.240 1.00 43.07  ? 195 THR A N   1 
ATOM   1364 C  CA  . THR A  1  182 ? 34.118  18.833  25.498 1.00 45.36  ? 195 THR A CA  1 
ATOM   1365 C  C   . THR A  1  182 ? 35.267  19.196  26.437 1.00 43.19  ? 195 THR A C   1 
ATOM   1366 O  O   . THR A  1  182 ? 35.043  19.957  27.368 1.00 45.01  ? 195 THR A O   1 
ATOM   1367 C  CB  . THR A  1  182 ? 33.140  17.896  26.224 1.00 49.97  ? 195 THR A CB  1 
ATOM   1368 O  OG1 . THR A  1  182 ? 33.822  16.671  26.493 1.00 47.78  ? 195 THR A OG1 1 
ATOM   1369 C  CG2 . THR A  1  182 ? 31.872  17.633  25.428 1.00 45.04  ? 195 THR A CG2 1 
ATOM   1370 N  N   . ASN A  1  183 ? 36.457  18.613  26.266 1.00 44.51  ? 196 ASN A N   1 
ATOM   1371 C  CA  . ASN A  1  183 ? 37.546  18.797  27.217 1.00 47.04  ? 196 ASN A CA  1 
ATOM   1372 C  C   . ASN A  1  183 ? 38.708  19.497  26.516 1.00 47.40  ? 196 ASN A C   1 
ATOM   1373 O  O   . ASN A  1  183 ? 39.385  18.889  25.694 1.00 44.13  ? 196 ASN A O   1 
ATOM   1374 C  CB  . ASN A  1  183 ? 37.973  17.462  27.821 1.00 46.69  ? 196 ASN A CB  1 
ATOM   1375 C  CG  . ASN A  1  183 ? 39.078  17.583  28.848 1.00 45.01  ? 196 ASN A CG  1 
ATOM   1376 O  OD1 . ASN A  1  183 ? 39.567  18.687  29.124 1.00 40.63  ? 196 ASN A OD1 1 
ATOM   1377 N  ND2 . ASN A  1  183 ? 39.491  16.458  29.419 1.00 42.81  ? 196 ASN A ND2 1 
ATOM   1378 N  N   . PRO A  1  184 ? 38.968  20.792  26.804 1.00 50.38  ? 197 PRO A N   1 
ATOM   1379 C  CA  . PRO A  1  184 ? 40.041  21.528  26.129 1.00 50.24  ? 197 PRO A CA  1 
ATOM   1380 C  C   . PRO A  1  184 ? 41.442  21.105  26.564 1.00 51.68  ? 197 PRO A C   1 
ATOM   1381 O  O   . PRO A  1  184 ? 42.412  21.410  25.872 1.00 56.24  ? 197 PRO A O   1 
ATOM   1382 C  CB  . PRO A  1  184 ? 39.740  22.989  26.496 1.00 49.90  ? 197 PRO A CB  1 
ATOM   1383 C  CG  . PRO A  1  184 ? 39.091  22.887  27.863 1.00 47.84  ? 197 PRO A CG  1 
ATOM   1384 C  CD  . PRO A  1  184 ? 38.252  21.613  27.794 1.00 52.07  ? 197 PRO A CD  1 
ATOM   1385 N  N   . GLU A  1  185 ? 41.526  20.395  27.700 1.00 52.70  ? 198 GLU A N   1 
ATOM   1386 C  CA  . GLU A  1  185 ? 42.779  19.870  28.229 1.00 50.82  ? 198 GLU A CA  1 
ATOM   1387 C  C   . GLU A  1  185 ? 42.953  18.379  27.910 1.00 48.51  ? 198 GLU A C   1 
ATOM   1388 O  O   . GLU A  1  185 ? 43.857  17.746  28.452 1.00 47.24  ? 198 GLU A O   1 
ATOM   1389 C  CB  . GLU A  1  185 ? 42.817  20.059  29.747 1.00 52.93  ? 198 GLU A CB  1 
ATOM   1390 C  CG  . GLU A  1  185 ? 42.965  21.503  30.213 1.00 56.34  ? 198 GLU A CG  1 
ATOM   1391 C  CD  . GLU A  1  185 ? 42.917  21.648  31.731 1.00 63.61  ? 198 GLU A CD  1 
ATOM   1392 O  OE1 . GLU A  1  185 ? 42.797  20.620  32.432 1.00 60.20  ? 198 GLU A OE1 1 
ATOM   1393 O  OE2 . GLU A  1  185 ? 42.993  22.790  32.233 1.00 74.27  ? 198 GLU A OE2 1 
ATOM   1394 N  N   . PHE A  1  186 ? 42.118  17.823  27.015 1.00 46.96  ? 199 PHE A N   1 
ATOM   1395 C  CA  . PHE A  1  186 ? 42.137  16.404  26.683 1.00 45.22  ? 199 PHE A CA  1 
ATOM   1396 C  C   . PHE A  1  186 ? 43.505  15.955  26.173 1.00 48.98  ? 199 PHE A C   1 
ATOM   1397 O  O   . PHE A  1  186 ? 44.010  16.484  25.182 1.00 50.37  ? 199 PHE A O   1 
ATOM   1398 C  CB  . PHE A  1  186 ? 41.110  16.108  25.592 1.00 45.32  ? 199 PHE A CB  1 
ATOM   1399 C  CG  . PHE A  1  186 ? 41.053  14.670  25.090 1.00 46.29  ? 199 PHE A CG  1 
ATOM   1400 C  CD1 . PHE A  1  186 ? 41.030  13.598  25.977 1.00 47.16  ? 199 PHE A CD1 1 
ATOM   1401 C  CD2 . PHE A  1  186 ? 41.012  14.391  23.727 1.00 43.56  ? 199 PHE A CD2 1 
ATOM   1402 C  CE1 . PHE A  1  186 ? 40.965  12.293  25.513 1.00 42.34  ? 199 PHE A CE1 1 
ATOM   1403 C  CE2 . PHE A  1  186 ? 40.950  13.082  23.271 1.00 40.41  ? 199 PHE A CE2 1 
ATOM   1404 C  CZ  . PHE A  1  186 ? 40.932  12.038  24.164 1.00 40.90  ? 199 PHE A CZ  1 
ATOM   1405 N  N   . GLN A  1  187 ? 44.062  14.939  26.845 1.00 46.20  ? 200 GLN A N   1 
ATOM   1406 C  CA  . GLN A  1  187 ? 45.294  14.285  26.444 1.00 46.66  ? 200 GLN A CA  1 
ATOM   1407 C  C   . GLN A  1  187 ? 45.024  12.792  26.250 1.00 45.55  ? 200 GLN A C   1 
ATOM   1408 O  O   . GLN A  1  187 ? 44.326  12.179  27.052 1.00 48.51  ? 200 GLN A O   1 
ATOM   1409 C  CB  . GLN A  1  187 ? 46.355  14.503  27.523 1.00 49.13  ? 200 GLN A CB  1 
ATOM   1410 C  CG  . GLN A  1  187 ? 46.773  15.955  27.714 1.00 53.80  ? 200 GLN A CG  1 
ATOM   1411 C  CD  . GLN A  1  187 ? 47.455  16.529  26.492 1.00 58.70  ? 200 GLN A CD  1 
ATOM   1412 O  OE1 . GLN A  1  187 ? 48.543  16.084  26.126 1.00 65.72  ? 200 GLN A OE1 1 
ATOM   1413 N  NE2 . GLN A  1  187 ? 46.831  17.508  25.846 1.00 60.20  ? 200 GLN A NE2 1 
ATOM   1414 N  N   . PHE A  1  188 ? 45.605  12.211  25.195 1.00 40.51  ? 201 PHE A N   1 
ATOM   1415 C  CA  . PHE A  1  188 ? 45.466  10.795  24.903 1.00 41.19  ? 201 PHE A CA  1 
ATOM   1416 C  C   . PHE A  1  188 ? 46.778  10.277  24.314 1.00 42.89  ? 201 PHE A C   1 
ATOM   1417 O  O   . PHE A  1  188 ? 46.835  9.891   23.152 1.00 40.18  ? 201 PHE A O   1 
ATOM   1418 C  CB  . PHE A  1  188 ? 44.254  10.602  23.984 1.00 40.58  ? 201 PHE A CB  1 
ATOM   1419 C  CG  . PHE A  1  188 ? 43.662  9.201   23.999 1.00 39.71  ? 201 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A  1  188 ? 42.997  8.730   25.125 1.00 45.45  ? 201 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A  1  188 ? 43.711  8.381   22.881 1.00 38.77  ? 201 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A  1  188 ? 42.432  7.459   25.146 1.00 44.38  ? 201 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A  1  188 ? 43.148  7.111   22.908 1.00 42.87  ? 201 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A  1  188 ? 42.510  6.652   24.042 1.00 43.93  ? 201 PHE A CZ  1 
ATOM   1425 N  N   . LYS A  1  189 ? 47.827  10.255  25.145 1.00 51.24  ? 202 LYS A N   1 
ATOM   1426 C  CA  . LYS A  1  189 ? 49.167  9.912   24.689 1.00 50.20  ? 202 LYS A CA  1 
ATOM   1427 C  C   . LYS A  1  189 ? 49.910  9.101   25.754 1.00 44.24  ? 202 LYS A C   1 
ATOM   1428 O  O   . LYS A  1  189 ? 49.480  9.005   26.899 1.00 43.43  ? 202 LYS A O   1 
ATOM   1429 C  CB  . LYS A  1  189 ? 49.939  11.194  24.353 1.00 52.81  ? 202 LYS A CB  1 
ATOM   1430 C  CG  . LYS A  1  189 ? 50.030  12.207  25.483 1.00 55.91  ? 202 LYS A CG  1 
ATOM   1431 C  CD  . LYS A  1  189 ? 50.931  13.398  25.186 1.00 55.81  ? 202 LYS A CD  1 
ATOM   1432 C  CE  . LYS A  1  189 ? 50.470  14.176  24.003 1.00 62.41  ? 202 LYS A CE  1 
ATOM   1433 N  NZ  . LYS A  1  189 ? 51.064  15.519  23.990 1.00 64.20  ? 202 LYS A NZ  1 
ATOM   1434 N  N   . ASN A  1  190 ? 51.038  8.524   25.336 1.00 41.43  ? 203 ASN A N   1 
ATOM   1435 C  CA  . ASN A  1  190 ? 51.951  7.789   26.194 1.00 41.90  ? 203 ASN A CA  1 
ATOM   1436 C  C   . ASN A  1  190 ? 51.194  6.699   26.957 1.00 42.82  ? 203 ASN A C   1 
ATOM   1437 O  O   . ASN A  1  190 ? 50.571  5.841   26.347 1.00 48.55  ? 203 ASN A O   1 
ATOM   1438 C  CB  . ASN A  1  190 ? 52.782  8.764   27.019 1.00 42.52  ? 203 ASN A CB  1 
ATOM   1439 C  CG  . ASN A  1  190 ? 53.649  9.648   26.148 1.00 47.16  ? 203 ASN A CG  1 
ATOM   1440 O  OD1 . ASN A  1  190 ? 54.354  9.158   25.252 1.00 48.80  ? 203 ASN A OD1 1 
ATOM   1441 N  ND2 . ASN A  1  190 ? 53.592  10.949  26.380 1.00 45.47  ? 203 ASN A ND2 1 
ATOM   1442 N  N   . VAL A  1  191 ? 51.254  6.724   28.289 1.00 40.49  ? 204 VAL A N   1 
ATOM   1443 C  CA  . VAL A  1  191 ? 50.684  5.656   29.090 1.00 44.21  ? 204 VAL A CA  1 
ATOM   1444 C  C   . VAL A  1  191 ? 49.192  5.503   28.776 1.00 42.21  ? 204 VAL A C   1 
ATOM   1445 O  O   . VAL A  1  191 ? 48.704  4.391   28.595 1.00 39.64  ? 204 VAL A O   1 
ATOM   1446 C  CB  . VAL A  1  191 ? 50.906  5.896   30.596 1.00 45.56  ? 204 VAL A CB  1 
ATOM   1447 C  CG1 . VAL A  1  191 ? 50.190  4.854   31.450 1.00 45.89  ? 204 VAL A CG1 1 
ATOM   1448 C  CG2 . VAL A  1  191 ? 52.383  5.955   30.968 1.00 44.84  ? 204 VAL A CG2 1 
ATOM   1449 N  N   . ARG A  1  192 ? 48.466  6.621   28.736 1.00 40.56  ? 205 ARG A N   1 
ATOM   1450 C  CA  . ARG A  1  192 ? 47.022  6.574   28.611 1.00 41.74  ? 205 ARG A CA  1 
ATOM   1451 C  C   . ARG A  1  192 ? 46.623  5.939   27.281 1.00 41.67  ? 205 ARG A C   1 
ATOM   1452 O  O   . ARG A  1  192 ? 45.688  5.143   27.243 1.00 46.48  ? 205 ARG A O   1 
ATOM   1453 C  CB  . ARG A  1  192 ? 46.390  7.963   28.771 1.00 43.17  ? 205 ARG A CB  1 
ATOM   1454 C  CG  . ARG A  1  192 ? 44.870  7.944   28.702 1.00 43.04  ? 205 ARG A CG  1 
ATOM   1455 C  CD  . ARG A  1  192 ? 44.287  6.962   29.707 1.00 43.05  ? 205 ARG A CD  1 
ATOM   1456 N  NE  . ARG A  1  192 ? 42.834  6.832   29.582 1.00 43.38  ? 205 ARG A NE  1 
ATOM   1457 C  CZ  . ARG A  1  192 ? 42.099  5.844   30.069 1.00 42.90  ? 205 ARG A CZ  1 
ATOM   1458 N  NH1 . ARG A  1  192 ? 42.655  4.856   30.748 1.00 41.91  ? 205 ARG A NH1 1 
ATOM   1459 N  NH2 . ARG A  1  192 ? 40.792  5.856   29.861 1.00 45.56  ? 205 ARG A NH2 1 
ATOM   1460 N  N   . PHE A  1  193 ? 47.328  6.286   26.197 1.00 39.74  ? 206 PHE A N   1 
ATOM   1461 C  CA  . PHE A  1  193 ? 47.022  5.730   24.890 1.00 41.80  ? 206 PHE A CA  1 
ATOM   1462 C  C   . PHE A  1  193 ? 47.073  4.200   24.940 1.00 46.91  ? 206 PHE A C   1 
ATOM   1463 O  O   . PHE A  1  193 ? 46.198  3.535   24.390 1.00 47.51  ? 206 PHE A O   1 
ATOM   1464 C  CB  . PHE A  1  193 ? 47.960  6.260   23.804 1.00 45.01  ? 206 PHE A CB  1 
ATOM   1465 C  CG  . PHE A  1  193 ? 47.620  5.750   22.410 1.00 42.57  ? 206 PHE A CG  1 
ATOM   1466 C  CD1 . PHE A  1  193 ? 46.529  6.255   21.716 1.00 42.01  ? 206 PHE A CD1 1 
ATOM   1467 C  CD2 . PHE A  1  193 ? 48.402  4.783   21.794 1.00 44.07  ? 206 PHE A CD2 1 
ATOM   1468 C  CE1 . PHE A  1  193 ? 46.216  5.788   20.453 1.00 41.64  ? 206 PHE A CE1 1 
ATOM   1469 C  CE2 . PHE A  1  193 ? 48.092  4.325   20.523 1.00 45.43  ? 206 PHE A CE2 1 
ATOM   1470 C  CZ  . PHE A  1  193 ? 46.997  4.824   19.859 1.00 43.78  ? 206 PHE A CZ  1 
ATOM   1471 N  N   . ILE A  1  194 ? 48.080  3.638   25.621 1.00 42.80  ? 207 ILE A N   1 
ATOM   1472 C  CA  . ILE A  1  194 ? 48.269  2.195   25.625 1.00 42.86  ? 207 ILE A CA  1 
ATOM   1473 C  C   . ILE A  1  194 ? 47.263  1.527   26.572 1.00 41.91  ? 207 ILE A C   1 
ATOM   1474 O  O   . ILE A  1  194 ? 46.589  0.581   26.175 1.00 44.59  ? 207 ILE A O   1 
ATOM   1475 C  CB  . ILE A  1  194 ? 49.726  1.844   25.976 1.00 45.29  ? 207 ILE A CB  1 
ATOM   1476 C  CG1 . ILE A  1  194 ? 50.736  2.543   25.037 1.00 43.90  ? 207 ILE A CG1 1 
ATOM   1477 C  CG2 . ILE A  1  194 ? 49.931  0.329   25.998 1.00 45.76  ? 207 ILE A CG2 1 
ATOM   1478 C  CD1 . ILE A  1  194 ? 50.616  2.178   23.564 1.00 43.25  ? 207 ILE A CD1 1 
ATOM   1479 N  N   . THR A  1  195 ? 47.155  2.024   27.812 1.00 41.91  ? 208 THR A N   1 
ATOM   1480 C  CA  . THR A  1  195 ? 46.348  1.379   28.837 1.00 43.93  ? 208 THR A CA  1 
ATOM   1481 C  C   . THR A  1  195 ? 44.859  1.462   28.490 1.00 44.06  ? 208 THR A C   1 
ATOM   1482 O  O   . THR A  1  195 ? 44.091  0.593   28.894 1.00 47.13  ? 208 THR A O   1 
ATOM   1483 C  CB  . THR A  1  195 ? 46.629  1.958   30.222 1.00 41.15  ? 208 THR A CB  1 
ATOM   1484 O  OG1 . THR A  1  195 ? 46.359  3.355   30.180 1.00 47.62  ? 208 THR A OG1 1 
ATOM   1485 C  CG2 . THR A  1  195 ? 48.057  1.721   30.670 1.00 48.04  ? 208 THR A CG2 1 
ATOM   1486 N  N   . ALA A  1  196 ? 44.450  2.498   27.752 1.00 42.69  ? 209 ALA A N   1 
ATOM   1487 C  CA  . ALA A  1  196 ? 43.042  2.720   27.446 1.00 48.61  ? 209 ALA A CA  1 
ATOM   1488 C  C   . ALA A  1  196 ? 42.467  1.602   26.570 1.00 53.29  ? 209 ALA A C   1 
ATOM   1489 O  O   . ALA A  1  196 ? 41.301  1.261   26.713 1.00 60.09  ? 209 ALA A O   1 
ATOM   1490 C  CB  . ALA A  1  196 ? 42.846  4.064   26.781 1.00 47.97  ? 209 ALA A CB  1 
ATOM   1491 N  N   . TYR A  1  197 ? 43.260  1.043   25.646 1.00 46.36  ? 210 TYR A N   1 
ATOM   1492 C  CA  . TYR A  1  197 ? 42.746  -0.001  24.774 1.00 43.77  ? 210 TYR A CA  1 
ATOM   1493 C  C   . TYR A  1  197 ? 42.599  -1.302  25.570 1.00 42.39  ? 210 TYR A C   1 
ATOM   1494 O  O   . TYR A  1  197 ? 41.618  -2.023  25.397 1.00 43.59  ? 210 TYR A O   1 
ATOM   1495 C  CB  . TYR A  1  197 ? 43.571  -0.059  23.477 1.00 41.90  ? 210 TYR A CB  1 
ATOM   1496 C  CG  . TYR A  1  197 ? 43.215  1.099   22.553 1.00 38.90  ? 210 TYR A CG  1 
ATOM   1497 C  CD1 . TYR A  1  197 ? 42.158  1.006   21.651 1.00 41.32  ? 210 TYR A CD1 1 
ATOM   1498 C  CD2 . TYR A  1  197 ? 43.875  2.315   22.642 1.00 38.08  ? 210 TYR A CD2 1 
ATOM   1499 C  CE1 . TYR A  1  197 ? 41.803  2.068   20.835 1.00 39.98  ? 210 TYR A CE1 1 
ATOM   1500 C  CE2 . TYR A  1  197 ? 43.531  3.390   21.835 1.00 41.79  ? 210 TYR A CE2 1 
ATOM   1501 C  CZ  . TYR A  1  197 ? 42.486  3.268   20.934 1.00 41.71  ? 210 TYR A CZ  1 
ATOM   1502 O  OH  . TYR A  1  197 ? 42.148  4.326   20.146 1.00 40.30  ? 210 TYR A OH  1 
ATOM   1503 N  N   . GLY A  1  198 ? 43.555  -1.579  26.464 1.00 41.29  ? 211 GLY A N   1 
ATOM   1504 C  CA  . GLY A  1  198 ? 43.485  -2.751  27.329 1.00 40.43  ? 211 GLY A CA  1 
ATOM   1505 C  C   . GLY A  1  198 ? 42.273  -2.724  28.266 1.00 37.74  ? 211 GLY A C   1 
ATOM   1506 O  O   . GLY A  1  198 ? 41.602  -3.738  28.448 1.00 36.27  ? 211 GLY A O   1 
ATOM   1507 N  N   . GLU A  1  199 ? 41.970  -1.546  28.815 1.00 39.17  ? 212 GLU A N   1 
ATOM   1508 C  CA  A GLU A  1  199 ? 40.887  -1.412  29.775 0.50 38.62  ? 212 GLU A CA  1 
ATOM   1509 C  CA  B GLU A  1  199 ? 40.885  -1.383  29.774 0.50 40.79  ? 212 GLU A CA  1 
ATOM   1510 C  C   . GLU A  1  199 ? 39.549  -1.761  29.119 1.00 40.11  ? 212 GLU A C   1 
ATOM   1511 O  O   . GLU A  1  199 ? 38.671  -2.314  29.784 1.00 36.63  ? 212 GLU A O   1 
ATOM   1512 C  CB  A GLU A  1  199 ? 40.967  -0.034  30.431 0.50 36.73  ? 212 GLU A CB  1 
ATOM   1513 C  CB  B GLU A  1  199 ? 40.906  0.029   30.388 0.50 41.97  ? 212 GLU A CB  1 
ATOM   1514 C  CG  A GLU A  1  199 ? 42.041  0.003   31.515 0.50 35.29  ? 212 GLU A CG  1 
ATOM   1515 C  CG  B GLU A  1  199 ? 39.988  1.052   29.707 0.50 43.80  ? 212 GLU A CG  1 
ATOM   1516 C  CD  A GLU A  1  199 ? 42.595  1.367   31.844 0.50 32.35  ? 212 GLU A CD  1 
ATOM   1517 C  CD  B GLU A  1  199 ? 39.975  2.509   30.196 0.50 42.16  ? 212 GLU A CD  1 
ATOM   1518 O  OE1 A GLU A  1  199 ? 41.936  2.355   31.494 0.50 30.10  ? 212 GLU A OE1 1 
ATOM   1519 O  OE1 B GLU A  1  199 ? 40.636  2.910   31.179 0.50 39.48  ? 212 GLU A OE1 1 
ATOM   1520 O  OE2 A GLU A  1  199 ? 43.691  1.427   32.434 0.50 35.11  ? 212 GLU A OE2 1 
ATOM   1521 O  OE2 B GLU A  1  199 ? 39.278  3.299   29.540 0.50 42.45  ? 212 GLU A OE2 1 
ATOM   1522 N  N   . THR A  1  200 ? 39.406  -1.489  27.804 1.00 39.10  ? 213 THR A N   1 
ATOM   1523 C  CA  . THR A  1  200 ? 38.127  -1.689  27.137 1.00 37.19  ? 213 THR A CA  1 
ATOM   1524 C  C   . THR A  1  200 ? 37.832  -3.174  26.941 1.00 36.54  ? 213 THR A C   1 
ATOM   1525 O  O   . THR A  1  200 ? 36.669  -3.507  26.730 1.00 37.76  ? 213 THR A O   1 
ATOM   1526 C  CB  . THR A  1  200 ? 38.026  -0.954  25.798 1.00 41.98  ? 213 THR A CB  1 
ATOM   1527 O  OG1 . THR A  1  200 ? 38.837  -1.639  24.853 1.00 55.84  ? 213 THR A OG1 1 
ATOM   1528 C  CG2 . THR A  1  200 ? 38.475  0.490   25.859 1.00 41.73  ? 213 THR A CG2 1 
ATOM   1529 N  N   . VAL A  1  201 ? 38.848  -4.054  26.987 1.00 35.59  ? 214 VAL A N   1 
ATOM   1530 C  CA  . VAL A  1  201 ? 38.634  -5.489  26.804 1.00 33.46  ? 214 VAL A CA  1 
ATOM   1531 C  C   . VAL A  1  201 ? 38.648  -6.250  28.132 1.00 32.93  ? 214 VAL A C   1 
ATOM   1532 O  O   . VAL A  1  201 ? 38.152  -7.378  28.188 1.00 35.04  ? 214 VAL A O   1 
ATOM   1533 C  CB  . VAL A  1  201 ? 39.607  -6.144  25.807 1.00 35.28  ? 214 VAL A CB  1 
ATOM   1534 C  CG1 . VAL A  1  201 ? 39.451  -5.546  24.411 1.00 36.77  ? 214 VAL A CG1 1 
ATOM   1535 C  CG2 . VAL A  1  201 ? 41.058  -6.066  26.253 1.00 36.10  ? 214 VAL A CG2 1 
ATOM   1536 N  N   . PHE A  1  202 ? 39.203  -5.657  29.196 1.00 32.55  ? 215 PHE A N   1 
ATOM   1537 C  CA  . PHE A  1  202 ? 39.199  -6.305  30.500 1.00 34.86  ? 215 PHE A CA  1 
ATOM   1538 C  C   . PHE A  1  202 ? 37.787  -6.747  30.893 1.00 35.06  ? 215 PHE A C   1 
ATOM   1539 O  O   . PHE A  1  202 ? 37.632  -7.825  31.453 1.00 38.59  ? 215 PHE A O   1 
ATOM   1540 C  CB  . PHE A  1  202 ? 39.795  -5.426  31.605 1.00 34.78  ? 215 PHE A CB  1 
ATOM   1541 C  CG  . PHE A  1  202 ? 41.298  -5.188  31.547 1.00 35.43  ? 215 PHE A CG  1 
ATOM   1542 C  CD1 . PHE A  1  202 ? 42.126  -5.901  30.681 1.00 39.77  ? 215 PHE A CD1 1 
ATOM   1543 C  CD2 . PHE A  1  202 ? 41.885  -4.261  32.396 1.00 37.56  ? 215 PHE A CD2 1 
ATOM   1544 C  CE1 . PHE A  1  202 ? 43.497  -5.660  30.644 1.00 39.45  ? 215 PHE A CE1 1 
ATOM   1545 C  CE2 . PHE A  1  202 ? 43.252  -4.035  32.367 1.00 39.65  ? 215 PHE A CE2 1 
ATOM   1546 C  CZ  . PHE A  1  202 ? 44.054  -4.735  31.494 1.00 39.65  ? 215 PHE A CZ  1 
ATOM   1547 N  N   . PRO A  1  203 ? 36.709  -5.957  30.670 1.00 38.34  ? 216 PRO A N   1 
ATOM   1548 C  CA  . PRO A  1  203 ? 35.362  -6.411  31.031 1.00 40.40  ? 216 PRO A CA  1 
ATOM   1549 C  C   . PRO A  1  203 ? 34.965  -7.732  30.375 1.00 41.27  ? 216 PRO A C   1 
ATOM   1550 O  O   . PRO A  1  203 ? 34.232  -8.517  30.970 1.00 44.31  ? 216 PRO A O   1 
ATOM   1551 C  CB  . PRO A  1  203 ? 34.475  -5.241  30.578 1.00 39.70  ? 216 PRO A CB  1 
ATOM   1552 C  CG  . PRO A  1  203 ? 35.391  -4.053  30.645 1.00 38.38  ? 216 PRO A CG  1 
ATOM   1553 C  CD  . PRO A  1  203 ? 36.716  -4.580  30.148 1.00 37.42  ? 216 PRO A CD  1 
ATOM   1554 N  N   . ILE A  1  204 ? 35.456  -7.963  29.152 1.00 40.43  ? 217 ILE A N   1 
ATOM   1555 C  CA  . ILE A  1  204 ? 35.159  -9.167  28.395 1.00 38.74  ? 217 ILE A CA  1 
ATOM   1556 C  C   . ILE A  1  204 ? 36.005  -10.328 28.907 1.00 35.87  ? 217 ILE A C   1 
ATOM   1557 O  O   . ILE A  1  204 ? 35.485  -11.423 29.134 1.00 36.59  ? 217 ILE A O   1 
ATOM   1558 C  CB  . ILE A  1  204 ? 35.393  -8.925  26.884 1.00 43.53  ? 217 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A  1  204 ? 34.484  -7.832  26.345 1.00 43.51  ? 217 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A  1  204 ? 35.238  -10.217 26.077 1.00 42.20  ? 217 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A  1  204 ? 34.889  -7.305  24.985 1.00 43.94  ? 217 ILE A CD1 1 
ATOM   1562 N  N   . ASN A  1  205 ? 37.317  -10.094 29.051 1.00 35.42  ? 218 ASN A N   1 
ATOM   1563 C  CA  . ASN A  1  205 ? 38.261  -11.159 29.352 1.00 37.10  ? 218 ASN A CA  1 
ATOM   1564 C  C   . ASN A  1  205 ? 38.263  -11.513 30.834 1.00 35.32  ? 218 ASN A C   1 
ATOM   1565 O  O   . ASN A  1  205 ? 38.617  -12.637 31.162 1.00 37.10  ? 218 ASN A O   1 
ATOM   1566 C  CB  . ASN A  1  205 ? 39.682  -10.820 28.907 1.00 37.55  ? 218 ASN A CB  1 
ATOM   1567 C  CG  . ASN A  1  205 ? 39.759  -10.556 27.421 1.00 37.71  ? 218 ASN A CG  1 
ATOM   1568 O  OD1 . ASN A  1  205 ? 38.965  -11.110 26.654 1.00 41.07  ? 218 ASN A OD1 1 
ATOM   1569 N  ND2 . ASN A  1  205 ? 40.657  -9.677  26.999 1.00 37.47  ? 218 ASN A ND2 1 
ATOM   1570 N  N   . LEU A  1  206 ? 37.905  -10.566 31.715 1.00 34.11  ? 219 LEU A N   1 
ATOM   1571 C  CA  . LEU A  1  206 ? 38.048  -10.791 33.146 1.00 38.88  ? 219 LEU A CA  1 
ATOM   1572 C  C   . LEU A  1  206 ? 36.744  -10.659 33.943 1.00 35.94  ? 219 LEU A C   1 
ATOM   1573 O  O   . LEU A  1  206 ? 36.671  -11.221 35.034 1.00 33.63  ? 219 LEU A O   1 
ATOM   1574 C  CB  . LEU A  1  206 ? 39.130  -9.846  33.665 1.00 40.25  ? 219 LEU A CB  1 
ATOM   1575 C  CG  . LEU A  1  206 ? 40.513  -10.014 33.029 1.00 41.35  ? 219 LEU A CG  1 
ATOM   1576 C  CD1 . LEU A  1  206 ? 41.409  -8.830  33.383 1.00 42.20  ? 219 LEU A CD1 1 
ATOM   1577 C  CD2 . LEU A  1  206 ? 41.159  -11.320 33.453 1.00 40.96  ? 219 LEU A CD2 1 
ATOM   1578 N  N   . PHE A  1  207 ? 35.751  -9.905  33.453 1.00 34.60  ? 220 PHE A N   1 
ATOM   1579 C  CA  . PHE A  1  207 ? 34.535  -9.643  34.225 1.00 36.92  ? 220 PHE A CA  1 
ATOM   1580 C  C   . PHE A  1  207 ? 33.453  -10.660 33.870 1.00 36.34  ? 220 PHE A C   1 
ATOM   1581 O  O   . PHE A  1  207 ? 32.506  -10.842 34.630 1.00 39.74  ? 220 PHE A O   1 
ATOM   1582 C  CB  . PHE A  1  207 ? 33.970  -8.228  34.036 1.00 33.89  ? 220 PHE A CB  1 
ATOM   1583 C  CG  . PHE A  1  207 ? 34.796  -7.088  34.614 1.00 33.88  ? 220 PHE A CG  1 
ATOM   1584 C  CD1 . PHE A  1  207 ? 35.896  -7.329  35.431 1.00 35.66  ? 220 PHE A CD1 1 
ATOM   1585 C  CD2 . PHE A  1  207 ? 34.432  -5.766  34.379 1.00 34.16  ? 220 PHE A CD2 1 
ATOM   1586 C  CE1 . PHE A  1  207 ? 36.632  -6.279  35.961 1.00 34.75  ? 220 PHE A CE1 1 
ATOM   1587 C  CE2 . PHE A  1  207 ? 35.173  -4.722  34.912 1.00 34.88  ? 220 PHE A CE2 1 
ATOM   1588 C  CZ  . PHE A  1  207 ? 36.265  -4.982  35.712 1.00 34.56  ? 220 PHE A CZ  1 
ATOM   1589 N  N   . VAL A  1  208 ? 33.603  -11.308 32.711 1.00 37.60  ? 221 VAL A N   1 
ATOM   1590 C  CA  . VAL A  1  208 ? 32.717  -12.381 32.291 1.00 37.84  ? 221 VAL A CA  1 
ATOM   1591 C  C   . VAL A  1  208 ? 33.157  -13.681 32.957 1.00 36.96  ? 221 VAL A C   1 
ATOM   1592 O  O   . VAL A  1  208 ? 34.326  -14.045 32.913 1.00 43.45  ? 221 VAL A O   1 
ATOM   1593 C  CB  . VAL A  1  208 ? 32.681  -12.545 30.759 1.00 37.67  ? 221 VAL A CB  1 
ATOM   1594 C  CG1 . VAL A  1  208 ? 31.862  -13.765 30.343 1.00 37.79  ? 221 VAL A CG1 1 
ATOM   1595 C  CG2 . VAL A  1  208 ? 32.178  -11.285 30.072 1.00 38.18  ? 221 VAL A CG2 1 
ATOM   1596 N  N   . ASP A  1  209 ? 32.185  -14.374 33.556 1.00 39.72  ? 222 ASP A N   1 
ATOM   1597 C  CA  . ASP A  1  209 ? 32.397  -15.611 34.283 1.00 38.69  ? 222 ASP A CA  1 
ATOM   1598 C  C   . ASP A  1  209 ? 33.198  -16.596 33.421 1.00 40.75  ? 222 ASP A C   1 
ATOM   1599 O  O   . ASP A  1  209 ? 32.965  -16.737 32.220 1.00 39.58  ? 222 ASP A O   1 
ATOM   1600 C  CB  . ASP A  1  209 ? 31.059  -16.164 34.745 1.00 39.71  ? 222 ASP A CB  1 
ATOM   1601 C  CG  . ASP A  1  209 ? 31.153  -17.295 35.745 1.00 39.54  ? 222 ASP A CG  1 
ATOM   1602 O  OD1 . ASP A  1  209 ? 31.587  -18.386 35.327 1.00 41.98  ? 222 ASP A OD1 1 
ATOM   1603 O  OD2 . ASP A  1  209 ? 30.842  -17.056 36.939 1.00 38.66  ? 222 ASP A OD2 1 
ATOM   1604 N  N   . GLY A  1  210 ? 34.143  -17.292 34.064 1.00 40.60  ? 223 GLY A N   1 
ATOM   1605 C  CA  . GLY A  1  210 ? 35.101  -18.149 33.379 1.00 39.34  ? 223 GLY A CA  1 
ATOM   1606 C  C   . GLY A  1  210 ? 34.513  -19.469 32.872 1.00 40.27  ? 223 GLY A C   1 
ATOM   1607 O  O   . GLY A  1  210 ? 35.132  -20.125 32.036 1.00 44.48  ? 223 GLY A O   1 
ATOM   1608 N  N   . ARG A  1  211 ? 33.344  -19.868 33.386 1.00 37.85  ? 224 ARG A N   1 
ATOM   1609 C  CA  . ARG A  1  211 ? 32.622  -21.032 32.891 1.00 38.80  ? 224 ARG A CA  1 
ATOM   1610 C  C   . ARG A  1  211 ? 32.010  -20.750 31.517 1.00 41.58  ? 224 ARG A C   1 
ATOM   1611 O  O   . ARG A  1  211 ? 31.659  -21.684 30.804 1.00 46.97  ? 224 ARG A O   1 
ATOM   1612 C  CB  . ARG A  1  211 ? 31.538  -21.480 33.876 1.00 38.62  ? 224 ARG A CB  1 
ATOM   1613 C  CG  . ARG A  1  211 ? 32.121  -21.978 35.193 1.00 40.37  ? 224 ARG A CG  1 
ATOM   1614 C  CD  . ARG A  1  211 ? 31.088  -22.075 36.292 1.00 40.46  ? 224 ARG A CD  1 
ATOM   1615 N  NE  . ARG A  1  211 ? 30.503  -20.776 36.634 1.00 42.63  ? 224 ARG A NE  1 
ATOM   1616 C  CZ  . ARG A  1  211 ? 29.656  -20.567 37.641 1.00 46.22  ? 224 ARG A CZ  1 
ATOM   1617 N  NH1 . ARG A  1  211 ? 29.263  -21.583 38.393 1.00 42.86  ? 224 ARG A NH1 1 
ATOM   1618 N  NH2 . ARG A  1  211 ? 29.234  -19.339 37.908 1.00 43.90  ? 224 ARG A NH2 1 
ATOM   1619 N  N   . VAL A  1  212 ? 31.881  -19.473 31.141 1.00 44.02  ? 225 VAL A N   1 
ATOM   1620 C  CA  . VAL A  1  212 ? 31.406  -19.104 29.817 1.00 44.73  ? 225 VAL A CA  1 
ATOM   1621 C  C   . VAL A  1  212 ? 32.592  -19.172 28.851 1.00 53.93  ? 225 VAL A C   1 
ATOM   1622 O  O   . VAL A  1  212 ? 33.556  -18.434 29.017 1.00 55.61  ? 225 VAL A O   1 
ATOM   1623 C  CB  . VAL A  1  212 ? 30.753  -17.704 29.786 1.00 43.56  ? 225 VAL A CB  1 
ATOM   1624 C  CG1 . VAL A  1  212 ? 30.251  -17.344 28.388 1.00 39.63  ? 225 VAL A CG1 1 
ATOM   1625 C  CG2 . VAL A  1  212 ? 29.606  -17.572 30.776 1.00 43.02  ? 225 VAL A CG2 1 
ATOM   1626 N  N   . THR A  1  213 ? 32.515  -20.028 27.822 1.00 59.76  ? 226 THR A N   1 
ATOM   1627 C  CA  . THR A  1  213 ? 33.645  -20.212 26.914 1.00 64.90  ? 226 THR A CA  1 
ATOM   1628 C  C   . THR A  1  213 ? 33.319  -19.833 25.472 1.00 60.16  ? 226 THR A C   1 
ATOM   1629 O  O   . THR A  1  213 ? 34.249  -19.619 24.713 1.00 64.52  ? 226 THR A O   1 
ATOM   1630 C  CB  . THR A  1  213 ? 34.174  -21.646 26.976 1.00 66.80  ? 226 THR A CB  1 
ATOM   1631 O  OG1 . THR A  1  213 ? 33.148  -22.527 26.540 1.00 61.37  ? 226 THR A OG1 1 
ATOM   1632 C  CG2 . THR A  1  213 ? 34.594  -22.052 28.378 1.00 71.53  ? 226 THR A CG2 1 
ATOM   1633 N  N   . THR A  1  214 ? 32.042  -19.792 25.084 1.00 64.50  ? 227 THR A N   1 
ATOM   1634 C  CA  . THR A  1  214 ? 31.659  -19.342 23.755 1.00 71.21  ? 227 THR A CA  1 
ATOM   1635 C  C   . THR A  1  214 ? 30.897  -18.021 23.892 1.00 64.86  ? 227 THR A C   1 
ATOM   1636 O  O   . THR A  1  214 ? 30.169  -17.837 24.860 1.00 65.37  ? 227 THR A O   1 
ATOM   1637 C  CB  . THR A  1  214 ? 30.849  -20.454 23.069 1.00 78.53  ? 227 THR A CB  1 
ATOM   1638 O  OG1 . THR A  1  214 ? 30.757  -20.052 21.707 1.00 82.67  ? 227 THR A OG1 1 
ATOM   1639 C  CG2 . THR A  1  214 ? 29.451  -20.678 23.630 1.00 80.16  ? 227 THR A CG2 1 
ATOM   1640 N  N   . ASP A  1  215 ? 31.075  -17.099 22.933 1.00 62.56  ? 228 ASP A N   1 
ATOM   1641 C  CA  . ASP A  1  215 ? 30.286  -15.871 22.849 1.00 66.23  ? 228 ASP A CA  1 
ATOM   1642 C  C   . ASP A  1  215 ? 30.368  -15.102 24.170 1.00 56.67  ? 228 ASP A C   1 
ATOM   1643 O  O   . ASP A  1  215 ? 29.346  -14.772 24.773 1.00 48.41  ? 228 ASP A O   1 
ATOM   1644 C  CB  . ASP A  1  215 ? 28.835  -16.147 22.459 1.00 72.48  ? 228 ASP A CB  1 
ATOM   1645 C  CG  . ASP A  1  215 ? 27.955  -14.932 22.155 1.00 81.71  ? 228 ASP A CG  1 
ATOM   1646 O  OD1 . ASP A  1  215 ? 28.509  -13.872 21.770 1.00 83.58  ? 228 ASP A OD1 1 
ATOM   1647 O  OD2 . ASP A  1  215 ? 26.709  -15.037 22.332 1.00 73.02  ? 228 ASP A OD2 1 
ATOM   1648 N  N   . ARG A  1  216 ? 31.600  -14.827 24.615 1.00 51.03  ? 229 ARG A N   1 
ATOM   1649 C  CA  . ARG A  1  216 ? 31.821  -14.187 25.896 1.00 46.77  ? 229 ARG A CA  1 
ATOM   1650 C  C   . ARG A  1  216 ? 31.331  -12.742 25.799 1.00 43.71  ? 229 ARG A C   1 
ATOM   1651 O  O   . ARG A  1  216 ? 31.758  -11.999 24.930 1.00 46.36  ? 229 ARG A O   1 
ATOM   1652 C  CB  . ARG A  1  216 ? 33.286  -14.361 26.318 1.00 47.23  ? 229 ARG A CB  1 
ATOM   1653 C  CG  . ARG A  1  216 ? 33.622  -15.738 26.877 1.00 45.85  ? 229 ARG A CG  1 
ATOM   1654 C  CD  . ARG A  1  216 ? 35.103  -15.888 27.197 1.00 46.13  ? 229 ARG A CD  1 
ATOM   1655 N  NE  . ARG A  1  216 ? 35.584  -14.982 28.245 1.00 47.69  ? 229 ARG A NE  1 
ATOM   1656 C  CZ  . ARG A  1  216 ? 35.347  -15.087 29.547 1.00 43.23  ? 229 ARG A CZ  1 
ATOM   1657 N  NH1 . ARG A  1  216 ? 34.667  -16.112 30.022 1.00 40.56  ? 229 ARG A NH1 1 
ATOM   1658 N  NH2 . ARG A  1  216 ? 35.816  -14.159 30.374 1.00 49.54  ? 229 ARG A NH2 1 
ATOM   1659 N  N   . LYS A  1  217 ? 30.427  -12.363 26.709 1.00 39.14  ? 230 LYS A N   1 
ATOM   1660 C  CA  . LYS A  1  217 ? 29.777  -11.066 26.694 1.00 39.34  ? 230 LYS A CA  1 
ATOM   1661 C  C   . LYS A  1  217 ? 29.319  -10.751 28.118 1.00 37.87  ? 230 LYS A C   1 
ATOM   1662 O  O   . LYS A  1  217 ? 28.971  -11.662 28.872 1.00 36.98  ? 230 LYS A O   1 
ATOM   1663 C  CB  . LYS A  1  217 ? 28.618  -11.071 25.684 1.00 42.25  ? 230 LYS A CB  1 
ATOM   1664 C  CG  . LYS A  1  217 ? 27.470  -12.033 25.999 1.00 48.30  ? 230 LYS A CG  1 
ATOM   1665 C  CD  . LYS A  1  217 ? 26.423  -12.170 24.900 1.00 57.13  ? 230 LYS A CD  1 
ATOM   1666 C  CE  . LYS A  1  217 ? 25.302  -13.102 25.286 1.00 63.71  ? 230 LYS A CE  1 
ATOM   1667 N  NZ  . LYS A  1  217 ? 24.298  -13.246 24.228 1.00 67.42  ? 230 LYS A NZ  1 
ATOM   1668 N  N   . LEU A  1  218 ? 29.320  -9.461  28.474 1.00 37.11  ? 231 LEU A N   1 
ATOM   1669 C  CA  . LEU A  1  218 ? 29.006  -9.048  29.832 1.00 37.86  ? 231 LEU A CA  1 
ATOM   1670 C  C   . LEU A  1  218 ? 27.596  -8.457  29.891 1.00 36.54  ? 231 LEU A C   1 
ATOM   1671 O  O   . LEU A  1  218 ? 27.274  -7.537  29.145 1.00 38.59  ? 231 LEU A O   1 
ATOM   1672 C  CB  . LEU A  1  218 ? 30.052  -8.039  30.302 1.00 36.25  ? 231 LEU A CB  1 
ATOM   1673 C  CG  . LEU A  1  218 ? 29.996  -7.675  31.785 1.00 36.84  ? 231 LEU A CG  1 
ATOM   1674 C  CD1 . LEU A  1  218 ? 30.360  -8.859  32.667 1.00 37.06  ? 231 LEU A CD1 1 
ATOM   1675 C  CD2 . LEU A  1  218 ? 30.892  -6.486  32.060 1.00 36.08  ? 231 LEU A CD2 1 
ATOM   1676 N  N   . SER A  1  219 ? 26.772  -8.973  30.805 1.00 39.07  ? 232 SER A N   1 
ATOM   1677 C  CA  . SER A  1  219 ? 25.464  -8.400  31.090 1.00 38.31  ? 232 SER A CA  1 
ATOM   1678 C  C   . SER A  1  219 ? 25.626  -7.046  31.774 1.00 35.02  ? 232 SER A C   1 
ATOM   1679 O  O   . SER A  1  219 ? 26.626  -6.821  32.439 1.00 35.69  ? 232 SER A O   1 
ATOM   1680 C  CB  . SER A  1  219 ? 24.636  -9.338  31.925 1.00 37.61  ? 232 SER A CB  1 
ATOM   1681 O  OG  . SER A  1  219 ? 25.091  -9.373  33.268 1.00 38.39  ? 232 SER A OG  1 
ATOM   1682 N  N   . MET A  1  220 ? 24.634  -6.158  31.625 1.00 36.75  ? 233 MET A N   1 
ATOM   1683 C  CA  . MET A  1  220 ? 24.664  -4.847  32.265 1.00 37.41  ? 233 MET A CA  1 
ATOM   1684 C  C   . MET A  1  220 ? 24.557  -4.972  33.784 1.00 36.61  ? 233 MET A C   1 
ATOM   1685 O  O   . MET A  1  220 ? 25.099  -4.123  34.495 1.00 35.03  ? 233 MET A O   1 
ATOM   1686 C  CB  . MET A  1  220 ? 23.554  -3.940  31.731 1.00 36.58  ? 233 MET A CB  1 
ATOM   1687 C  CG  . MET A  1  220 ? 23.687  -3.626  30.253 1.00 40.09  ? 233 MET A CG  1 
ATOM   1688 S  SD  . MET A  1  220 ? 25.276  -2.932  29.740 1.00 39.16  ? 233 MET A SD  1 
ATOM   1689 C  CE  . MET A  1  220 ? 26.111  -4.418  29.153 1.00 37.56  ? 233 MET A CE  1 
ATOM   1690 N  N   . GLU A  1  221 ? 23.897  -6.039  34.270 1.00 34.74  ? 234 GLU A N   1 
ATOM   1691 C  CA  . GLU A  1  221 ? 23.752  -6.271  35.702 1.00 40.22  ? 234 GLU A CA  1 
ATOM   1692 C  C   . GLU A  1  221 ? 25.134  -6.536  36.318 1.00 40.97  ? 234 GLU A C   1 
ATOM   1693 O  O   . GLU A  1  221 ? 25.473  -5.980  37.355 1.00 38.32  ? 234 GLU A O   1 
ATOM   1694 C  CB  . GLU A  1  221 ? 22.773  -7.417  36.001 1.00 38.48  ? 234 GLU A CB  1 
ATOM   1695 C  CG  . GLU A  1  221 ? 21.333  -7.141  35.579 1.00 45.62  ? 234 GLU A CG  1 
ATOM   1696 C  CD  . GLU A  1  221 ? 20.951  -7.316  34.101 1.00 55.15  ? 234 GLU A CD  1 
ATOM   1697 O  OE1 . GLU A  1  221 ? 21.757  -7.741  33.219 1.00 53.07  ? 234 GLU A OE1 1 
ATOM   1698 O  OE2 . GLU A  1  221 ? 19.780  -6.967  33.829 1.00 63.76  ? 234 GLU A OE2 1 
ATOM   1699 N  N   . ASP A  1  222 ? 25.909  -7.412  35.665 1.00 40.70  ? 235 ASP A N   1 
ATOM   1700 C  CA  . ASP A  1  222 ? 27.245  -7.768  36.104 1.00 38.68  ? 235 ASP A CA  1 
ATOM   1701 C  C   . ASP A  1  222 ? 28.172  -6.553  35.979 1.00 36.95  ? 235 ASP A C   1 
ATOM   1702 O  O   . ASP A  1  222 ? 28.942  -6.268  36.887 1.00 35.31  ? 235 ASP A O   1 
ATOM   1703 C  CB  . ASP A  1  222 ? 27.758  -9.000  35.371 1.00 38.98  ? 235 ASP A CB  1 
ATOM   1704 C  CG  . ASP A  1  222 ? 27.116  -10.330 35.744 1.00 39.97  ? 235 ASP A CG  1 
ATOM   1705 O  OD1 . ASP A  1  222 ? 26.302  -10.344 36.693 1.00 43.24  ? 235 ASP A OD1 1 
ATOM   1706 O  OD2 . ASP A  1  222 ? 27.443  -11.350 35.090 1.00 42.87  ? 235 ASP A OD2 1 
ATOM   1707 N  N   . ALA A  1  223 ? 28.087  -5.822  34.866 1.00 35.48  ? 236 ALA A N   1 
ATOM   1708 C  CA  . ALA A  1  223 ? 28.830  -4.582  34.715 1.00 37.23  ? 236 ALA A CA  1 
ATOM   1709 C  C   . ALA A  1  223 ? 28.523  -3.602  35.855 1.00 35.84  ? 236 ALA A C   1 
ATOM   1710 O  O   . ALA A  1  223 ? 29.443  -3.015  36.413 1.00 32.12  ? 236 ALA A O   1 
ATOM   1711 C  CB  . ALA A  1  223 ? 28.535  -3.968  33.371 1.00 35.25  ? 236 ALA A CB  1 
ATOM   1712 N  N   . ALA A  1  224 ? 27.244  -3.411  36.201 1.00 34.44  ? 237 ALA A N   1 
ATOM   1713 C  CA  . ALA A  1  224 ? 26.885  -2.438  37.227 1.00 36.71  ? 237 ALA A CA  1 
ATOM   1714 C  C   . ALA A  1  224 ? 27.469  -2.886  38.564 1.00 34.42  ? 237 ALA A C   1 
ATOM   1715 O  O   . ALA A  1  224 ? 27.993  -2.088  39.328 1.00 31.77  ? 237 ALA A O   1 
ATOM   1716 C  CB  . ALA A  1  224 ? 25.376  -2.269  37.317 1.00 34.74  ? 237 ALA A CB  1 
ATOM   1717 N  N   . SER A  1  225 ? 27.379  -4.187  38.821 1.00 33.12  ? 238 SER A N   1 
ATOM   1718 C  CA  . SER A  1  225 ? 27.818  -4.755  40.078 1.00 35.22  ? 238 SER A CA  1 
ATOM   1719 C  C   . SER A  1  225 ? 29.301  -4.447  40.316 1.00 34.16  ? 238 SER A C   1 
ATOM   1720 O  O   . SER A  1  225 ? 29.678  -4.061  41.418 1.00 34.20  ? 238 SER A O   1 
ATOM   1721 C  CB  . SER A  1  225 ? 27.505  -6.244  40.117 1.00 35.17  ? 238 SER A CB  1 
ATOM   1722 O  OG  . SER A  1  225 ? 27.909  -6.820  41.352 1.00 36.25  ? 238 SER A OG  1 
ATOM   1723 N  N   . ILE A  1  226 ? 30.138  -4.593  39.288 1.00 32.77  ? 239 ILE A N   1 
ATOM   1724 C  CA  . ILE A  1  226 ? 31.576  -4.400  39.445 1.00 36.65  ? 239 ILE A CA  1 
ATOM   1725 C  C   . ILE A  1  226 ? 31.917  -2.908  39.367 1.00 33.55  ? 239 ILE A C   1 
ATOM   1726 O  O   . ILE A  1  226 ? 32.546  -2.370  40.272 1.00 33.39  ? 239 ILE A O   1 
ATOM   1727 C  CB  . ILE A  1  226 ? 32.345  -5.231  38.400 1.00 35.53  ? 239 ILE A CB  1 
ATOM   1728 C  CG1 . ILE A  1  226 ? 32.129  -6.724  38.636 1.00 35.86  ? 239 ILE A CG1 1 
ATOM   1729 C  CG2 . ILE A  1  226 ? 33.829  -4.868  38.390 1.00 32.77  ? 239 ILE A CG2 1 
ATOM   1730 C  CD1 . ILE A  1  226 ? 32.582  -7.600  37.486 1.00 40.99  ? 239 ILE A CD1 1 
ATOM   1731 N  N   . PHE A  1  227 ? 31.493  -2.257  38.281 1.00 32.64  ? 240 PHE A N   1 
ATOM   1732 C  CA  . PHE A  1  227 ? 31.848  -0.874  38.006 1.00 34.51  ? 240 PHE A CA  1 
ATOM   1733 C  C   . PHE A  1  227 ? 31.287  0.108   39.039 1.00 32.71  ? 240 PHE A C   1 
ATOM   1734 O  O   . PHE A  1  227 ? 31.924  1.124   39.306 1.00 32.31  ? 240 PHE A O   1 
ATOM   1735 C  CB  . PHE A  1  227 ? 31.332  -0.451  36.631 1.00 35.71  ? 240 PHE A CB  1 
ATOM   1736 C  CG  . PHE A  1  227 ? 32.162  -0.865  35.428 1.00 35.50  ? 240 PHE A CG  1 
ATOM   1737 C  CD1 . PHE A  1  227 ? 33.399  -0.287  35.185 1.00 40.31  ? 240 PHE A CD1 1 
ATOM   1738 C  CD2 . PHE A  1  227 ? 31.666  -1.756  34.491 1.00 41.25  ? 240 PHE A CD2 1 
ATOM   1739 C  CE1 . PHE A  1  227 ? 34.130  -0.621  34.058 1.00 40.86  ? 240 PHE A CE1 1 
ATOM   1740 C  CE2 . PHE A  1  227 ? 32.404  -2.092  33.364 1.00 43.42  ? 240 PHE A CE2 1 
ATOM   1741 C  CZ  . PHE A  1  227 ? 33.628  -1.516  33.145 1.00 39.26  ? 240 PHE A CZ  1 
ATOM   1742 N  N   . ARG A  1  228 ? 30.093  -0.157  39.582 1.00 32.53  ? 241 ARG A N   1 
ATOM   1743 C  CA  . ARG A  1  228 ? 29.459  0.766   40.520 1.00 32.89  ? 241 ARG A CA  1 
ATOM   1744 C  C   . ARG A  1  228 ? 29.552  0.262   41.964 1.00 31.84  ? 241 ARG A C   1 
ATOM   1745 O  O   . ARG A  1  228 ? 29.919  1.043   42.822 1.00 32.52  ? 241 ARG A O   1 
ATOM   1746 C  CB  . ARG A  1  228 ? 28.003  1.046   40.156 1.00 32.91  ? 241 ARG A CB  1 
ATOM   1747 C  CG  . ARG A  1  228 ? 27.288  2.035   41.068 1.00 38.09  ? 241 ARG A CG  1 
ATOM   1748 C  CD  . ARG A  1  228 ? 25.891  2.418   40.562 1.00 36.76  ? 241 ARG A CD  1 
ATOM   1749 N  NE  . ARG A  1  228 ? 24.964  1.284   40.566 1.00 38.27  ? 241 ARG A NE  1 
ATOM   1750 C  CZ  . ARG A  1  228 ? 24.145  0.922   39.587 1.00 39.42  ? 241 ARG A CZ  1 
ATOM   1751 N  NH1 . ARG A  1  228 ? 24.131  1.594   38.456 1.00 40.45  ? 241 ARG A NH1 1 
ATOM   1752 N  NH2 . ARG A  1  228 ? 23.348  -0.127  39.736 1.00 41.06  ? 241 ARG A NH2 1 
ATOM   1753 N  N   . ASP A  1  229 ? 29.224  -1.014  42.241 1.00 30.35  ? 242 ASP A N   1 
ATOM   1754 C  CA  . ASP A  1  229 ? 29.110  -1.474  43.616 1.00 30.48  ? 242 ASP A CA  1 
ATOM   1755 C  C   . ASP A  1  229 ? 30.380  -2.158  44.132 1.00 30.95  ? 242 ASP A C   1 
ATOM   1756 O  O   . ASP A  1  229 ? 30.447  -2.484  45.319 1.00 34.45  ? 242 ASP A O   1 
ATOM   1757 C  CB  . ASP A  1  229 ? 27.886  -2.356  43.812 1.00 33.58  ? 242 ASP A CB  1 
ATOM   1758 C  CG  . ASP A  1  229 ? 26.551  -1.696  43.506 1.00 34.56  ? 242 ASP A CG  1 
ATOM   1759 O  OD1 . ASP A  1  229 ? 26.415  -0.477  43.740 1.00 38.15  ? 242 ASP A OD1 1 
ATOM   1760 O  OD2 . ASP A  1  229 ? 25.654  -2.410  43.046 1.00 39.12  ? 242 ASP A OD2 1 
ATOM   1761 N  N   . MET A  1  230 ? 31.372  -2.388  43.261 1.00 31.20  ? 243 MET A N   1 
ATOM   1762 C  CA  . MET A  1  230 ? 32.628  -3.021  43.653 1.00 33.04  ? 243 MET A CA  1 
ATOM   1763 C  C   . MET A  1  230 ? 32.375  -4.439  44.171 1.00 30.13  ? 243 MET A C   1 
ATOM   1764 O  O   . MET A  1  230 ? 32.982  -4.853  45.157 1.00 33.27  ? 243 MET A O   1 
ATOM   1765 C  CB  . MET A  1  230 ? 33.353  -2.210  44.741 1.00 35.13  ? 243 MET A CB  1 
ATOM   1766 C  CG  . MET A  1  230 ? 33.491  -0.726  44.424 1.00 37.36  ? 243 MET A CG  1 
ATOM   1767 S  SD  . MET A  1  230 ? 34.094  0.236   45.825 1.00 39.95  ? 243 MET A SD  1 
ATOM   1768 C  CE  . MET A  1  230 ? 33.898  1.893   45.158 1.00 46.00  ? 243 MET A CE  1 
ATOM   1769 N  N   . ARG A  1  231 ? 31.451  -5.154  43.518 1.00 32.73  ? 244 ARG A N   1 
ATOM   1770 C  CA  . ARG A  1  231 ? 30.952  -6.442  43.977 1.00 33.87  ? 244 ARG A CA  1 
ATOM   1771 C  C   . ARG A  1  231 ? 31.052  -7.453  42.830 1.00 33.18  ? 244 ARG A C   1 
ATOM   1772 O  O   . ARG A  1  231 ? 30.612  -7.199  41.716 1.00 32.83  ? 244 ARG A O   1 
ATOM   1773 C  CB  . ARG A  1  231 ? 29.515  -6.302  44.489 1.00 36.08  ? 244 ARG A CB  1 
ATOM   1774 C  CG  . ARG A  1  231 ? 28.985  -7.490  45.279 1.00 41.54  ? 244 ARG A CG  1 
ATOM   1775 C  CD  . ARG A  1  231 ? 27.538  -7.359  45.711 1.00 45.35  ? 244 ARG A CD  1 
ATOM   1776 N  NE  . ARG A  1  231 ? 26.649  -7.383  44.547 1.00 61.33  ? 244 ARG A NE  1 
ATOM   1777 C  CZ  . ARG A  1  231 ? 26.322  -8.457  43.808 1.00 73.99  ? 244 ARG A CZ  1 
ATOM   1778 N  NH1 . ARG A  1  231 ? 26.572  -9.687  44.253 1.00 76.72  ? 244 ARG A NH1 1 
ATOM   1779 N  NH2 . ARG A  1  231 ? 25.712  -8.292  42.639 1.00 66.34  ? 244 ARG A NH2 1 
ATOM   1780 N  N   . PHE A  1  232 ? 31.653  -8.610  43.106 1.00 33.02  ? 245 PHE A N   1 
ATOM   1781 C  CA  . PHE A  1  232 ? 31.572  -9.739  42.199 1.00 33.98  ? 245 PHE A CA  1 
ATOM   1782 C  C   . PHE A  1  232 ? 30.116  -10.148 42.026 1.00 34.10  ? 245 PHE A C   1 
ATOM   1783 O  O   . PHE A  1  232 ? 29.346  -10.112 42.977 1.00 36.72  ? 245 PHE A O   1 
ATOM   1784 C  CB  . PHE A  1  232 ? 32.311  -10.966 42.726 1.00 34.38  ? 245 PHE A CB  1 
ATOM   1785 C  CG  . PHE A  1  232 ? 33.828  -10.851 42.728 1.00 34.92  ? 245 PHE A CG  1 
ATOM   1786 C  CD1 . PHE A  1  232 ? 34.531  -10.778 41.538 1.00 34.68  ? 245 PHE A CD1 1 
ATOM   1787 C  CD2 . PHE A  1  232 ? 34.545  -10.887 43.916 1.00 33.16  ? 245 PHE A CD2 1 
ATOM   1788 C  CE1 . PHE A  1  232 ? 35.914  -10.715 41.546 1.00 38.67  ? 245 PHE A CE1 1 
ATOM   1789 C  CE2 . PHE A  1  232 ? 35.929  -10.832 43.912 1.00 33.95  ? 245 PHE A CE2 1 
ATOM   1790 C  CZ  . PHE A  1  232 ? 36.615  -10.752 42.735 1.00 35.35  ? 245 PHE A CZ  1 
ATOM   1791 N  N   . PRO A  1  233 ? 29.698  -10.550 40.808 1.00 35.69  ? 246 PRO A N   1 
ATOM   1792 C  CA  . PRO A  1  233 ? 28.428  -11.261 40.627 1.00 36.61  ? 246 PRO A CA  1 
ATOM   1793 C  C   . PRO A  1  233 ? 28.316  -12.458 41.564 1.00 34.70  ? 246 PRO A C   1 
ATOM   1794 O  O   . PRO A  1  233 ? 29.329  -13.017 41.979 1.00 32.08  ? 246 PRO A O   1 
ATOM   1795 C  CB  . PRO A  1  233 ? 28.442  -11.678 39.147 1.00 32.62  ? 246 PRO A CB  1 
ATOM   1796 C  CG  . PRO A  1  233 ? 29.366  -10.675 38.484 1.00 34.31  ? 246 PRO A CG  1 
ATOM   1797 C  CD  . PRO A  1  233 ? 30.396  -10.293 39.538 1.00 35.27  ? 246 PRO A CD  1 
ATOM   1798 N  N   . ASP A  1  234 ? 27.077  -12.820 41.915 1.00 34.82  ? 247 ASP A N   1 
ATOM   1799 C  CA  . ASP A  1  234 ? 26.825  -14.017 42.704 1.00 38.51  ? 247 ASP A CA  1 
ATOM   1800 C  C   . ASP A  1  234 ? 27.497  -15.211 42.023 1.00 34.94  ? 247 ASP A C   1 
ATOM   1801 O  O   . ASP A  1  234 ? 27.440  -15.347 40.817 1.00 34.20  ? 247 ASP A O   1 
ATOM   1802 C  CB  . ASP A  1  234 ? 25.341  -14.294 42.902 1.00 40.69  ? 247 ASP A CB  1 
ATOM   1803 C  CG  . ASP A  1  234 ? 24.568  -13.317 43.780 1.00 43.48  ? 247 ASP A CG  1 
ATOM   1804 O  OD1 . ASP A  1  234 ? 25.154  -12.318 44.230 1.00 41.61  ? 247 ASP A OD1 1 
ATOM   1805 O  OD2 . ASP A  1  234 ? 23.363  -13.570 44.002 1.00 43.79  ? 247 ASP A OD2 1 
ATOM   1806 N  N   . ASP A  1  235 ? 28.167  -16.052 42.809 1.00 38.71  ? 248 ASP A N   1 
ATOM   1807 C  CA  . ASP A  1  235 ? 28.740  -17.297 42.322 1.00 41.73  ? 248 ASP A CA  1 
ATOM   1808 C  C   . ASP A  1  235 ? 29.809  -17.045 41.252 1.00 37.59  ? 248 ASP A C   1 
ATOM   1809 O  O   . ASP A  1  235 ? 30.024  -17.885 40.382 1.00 38.50  ? 248 ASP A O   1 
ATOM   1810 C  CB  . ASP A  1  235 ? 27.637  -18.237 41.847 1.00 40.11  ? 248 ASP A CB  1 
ATOM   1811 C  CG  . ASP A  1  235 ? 28.093  -19.670 41.617 1.00 42.12  ? 248 ASP A CG  1 
ATOM   1812 O  OD1 . ASP A  1  235 ? 28.712  -20.235 42.532 1.00 44.32  ? 248 ASP A OD1 1 
ATOM   1813 O  OD2 . ASP A  1  235 ? 27.865  -20.193 40.507 1.00 46.54  ? 248 ASP A OD2 1 
ATOM   1814 N  N   . PHE A  1  236 ? 30.511  -15.909 41.323 1.00 36.71  ? 249 PHE A N   1 
ATOM   1815 C  CA  . PHE A  1  236 ? 31.415  -15.523 40.252 1.00 36.47  ? 249 PHE A CA  1 
ATOM   1816 C  C   . PHE A  1  236 ? 32.626  -16.453 40.201 1.00 36.27  ? 249 PHE A C   1 
ATOM   1817 O  O   . PHE A  1  236 ? 33.300  -16.699 41.211 1.00 33.41  ? 249 PHE A O   1 
ATOM   1818 C  CB  . PHE A  1  236 ? 31.894  -14.079 40.382 1.00 37.11  ? 249 PHE A CB  1 
ATOM   1819 C  CG  . PHE A  1  236 ? 32.818  -13.656 39.251 1.00 34.15  ? 249 PHE A CG  1 
ATOM   1820 C  CD1 . PHE A  1  236 ? 32.314  -13.388 37.991 1.00 34.64  ? 249 PHE A CD1 1 
ATOM   1821 C  CD2 . PHE A  1  236 ? 34.182  -13.530 39.458 1.00 34.78  ? 249 PHE A CD2 1 
ATOM   1822 C  CE1 . PHE A  1  236 ? 33.158  -13.006 36.960 1.00 37.00  ? 249 PHE A CE1 1 
ATOM   1823 C  CE2 . PHE A  1  236 ? 35.020  -13.141 38.427 1.00 35.52  ? 249 PHE A CE2 1 
ATOM   1824 C  CZ  . PHE A  1  236 ? 34.507  -12.873 37.183 1.00 35.89  ? 249 PHE A CZ  1 
ATOM   1825 N  N   . HIS A  1  237 ? 32.881  -16.954 38.990 1.00 36.26  ? 250 HIS A N   1 
ATOM   1826 C  CA  . HIS A  1  237 ? 34.032  -17.795 38.713 1.00 38.02  ? 250 HIS A CA  1 
ATOM   1827 C  C   . HIS A  1  237 ? 34.956  -17.027 37.772 1.00 37.24  ? 250 HIS A C   1 
ATOM   1828 O  O   . HIS A  1  237 ? 34.539  -16.587 36.705 1.00 34.58  ? 250 HIS A O   1 
ATOM   1829 C  CB  . HIS A  1  237 ? 33.601  -19.138 38.106 1.00 37.72  ? 250 HIS A CB  1 
ATOM   1830 C  CG  . HIS A  1  237 ? 33.012  -20.115 39.069 1.00 42.94  ? 250 HIS A CG  1 
ATOM   1831 N  ND1 . HIS A  1  237 ? 31.922  -19.844 39.868 1.00 43.74  ? 250 HIS A ND1 1 
ATOM   1832 C  CD2 . HIS A  1  237 ? 33.355  -21.386 39.326 1.00 43.49  ? 250 HIS A CD2 1 
ATOM   1833 C  CE1 . HIS A  1  237 ? 31.643  -20.918 40.594 1.00 49.65  ? 250 HIS A CE1 1 
ATOM   1834 N  NE2 . HIS A  1  237 ? 32.506  -21.862 40.288 1.00 47.13  ? 250 HIS A NE2 1 
ATOM   1835 N  N   . ARG A  1  238 ? 36.227  -16.903 38.154 1.00 37.10  ? 251 ARG A N   1 
ATOM   1836 C  CA  . ARG A  1  238 ? 37.206  -16.186 37.348 1.00 38.95  ? 251 ARG A CA  1 
ATOM   1837 C  C   . ARG A  1  238 ? 37.488  -16.908 36.027 1.00 36.84  ? 251 ARG A C   1 
ATOM   1838 O  O   . ARG A  1  238 ? 37.169  -18.083 35.874 1.00 35.39  ? 251 ARG A O   1 
ATOM   1839 C  CB  . ARG A  1  238 ? 38.502  -16.028 38.145 1.00 36.49  ? 251 ARG A CB  1 
ATOM   1840 C  CG  . ARG A  1  238 ? 39.205  -17.357 38.372 1.00 38.35  ? 251 ARG A CG  1 
ATOM   1841 C  CD  . ARG A  1  238 ? 40.516  -17.182 39.116 1.00 40.13  ? 251 ARG A CD  1 
ATOM   1842 N  NE  . ARG A  1  238 ? 41.336  -18.377 38.927 1.00 42.35  ? 251 ARG A NE  1 
ATOM   1843 C  CZ  . ARG A  1  238 ? 42.437  -18.695 39.603 1.00 44.76  ? 251 ARG A CZ  1 
ATOM   1844 N  NH1 . ARG A  1  238 ? 42.964  -17.861 40.483 1.00 44.83  ? 251 ARG A NH1 1 
ATOM   1845 N  NH2 . ARG A  1  238 ? 43.016  -19.858 39.379 1.00 40.83  ? 251 ARG A NH2 1 
ATOM   1846 N  N   . SER A  1  239 ? 38.114  -16.178 35.096 1.00 36.07  ? 252 SER A N   1 
ATOM   1847 C  CA  . SER A  1  239 ? 38.625  -16.706 33.838 1.00 36.34  ? 252 SER A CA  1 
ATOM   1848 C  C   . SER A  1  239 ? 39.321  -18.046 34.046 1.00 37.44  ? 252 SER A C   1 
ATOM   1849 O  O   . SER A  1  239 ? 40.061  -18.206 35.015 1.00 37.54  ? 252 SER A O   1 
ATOM   1850 C  CB  . SER A  1  239 ? 39.589  -15.721 33.209 1.00 36.38  ? 252 SER A CB  1 
ATOM   1851 O  OG  . SER A  1  239 ? 40.148  -16.229 31.998 1.00 35.56  ? 252 SER A OG  1 
ATOM   1852 N  N   . ALA A  1  240 ? 39.087  -18.991 33.124 1.00 39.19  ? 253 ALA A N   1 
ATOM   1853 C  CA  . ALA A  1  240 ? 39.659  -20.330 33.224 1.00 44.05  ? 253 ALA A CA  1 
ATOM   1854 C  C   . ALA A  1  240 ? 41.124  -20.336 32.786 1.00 41.14  ? 253 ALA A C   1 
ATOM   1855 O  O   . ALA A  1  240 ? 41.808  -21.331 32.987 1.00 42.63  ? 253 ALA A O   1 
ATOM   1856 C  CB  . ALA A  1  240 ? 38.838  -21.318 32.416 1.00 42.69  ? 253 ALA A CB  1 
ATOM   1857 N  N   . VAL A  1  241 ? 41.587  -19.219 32.204 1.00 43.45  ? 254 VAL A N   1 
ATOM   1858 C  CA  . VAL A  1  241 ? 42.974  -19.025 31.794 1.00 45.90  ? 254 VAL A CA  1 
ATOM   1859 C  C   . VAL A  1  241 ? 43.467  -17.684 32.324 1.00 40.06  ? 254 VAL A C   1 
ATOM   1860 O  O   . VAL A  1  241 ? 42.682  -16.742 32.405 1.00 40.10  ? 254 VAL A O   1 
ATOM   1861 C  CB  . VAL A  1  241 ? 43.140  -19.056 30.256 1.00 46.86  ? 254 VAL A CB  1 
ATOM   1862 C  CG1 . VAL A  1  241 ? 42.830  -20.431 29.681 1.00 47.34  ? 254 VAL A CG1 1 
ATOM   1863 C  CG2 . VAL A  1  241 ? 42.270  -18.019 29.561 1.00 45.53  ? 254 VAL A CG2 1 
ATOM   1864 N  N   . PRO A  1  242 ? 44.780  -17.525 32.621 1.00 41.81  ? 255 PRO A N   1 
ATOM   1865 C  CA  . PRO A  1  242 ? 45.359  -16.193 32.848 1.00 39.71  ? 255 PRO A CA  1 
ATOM   1866 C  C   . PRO A  1  242 ? 45.083  -15.294 31.647 1.00 39.29  ? 255 PRO A C   1 
ATOM   1867 O  O   . PRO A  1  242 ? 45.252  -15.731 30.518 1.00 38.75  ? 255 PRO A O   1 
ATOM   1868 C  CB  . PRO A  1  242 ? 46.852  -16.487 33.031 1.00 38.33  ? 255 PRO A CB  1 
ATOM   1869 C  CG  . PRO A  1  242 ? 46.893  -17.931 33.510 1.00 38.69  ? 255 PRO A CG  1 
ATOM   1870 C  CD  . PRO A  1  242 ? 45.783  -18.599 32.727 1.00 40.06  ? 255 PRO A CD  1 
ATOM   1871 N  N   . ALA A  1  243 ? 44.642  -14.049 31.878 1.00 40.37  ? 256 ALA A N   1 
ATOM   1872 C  CA  . ALA A  1  243 ? 44.238  -13.187 30.777 1.00 39.10  ? 256 ALA A CA  1 
ATOM   1873 C  C   . ALA A  1  243 ? 44.520  -11.719 31.082 1.00 37.82  ? 256 ALA A C   1 
ATOM   1874 O  O   . ALA A  1  243 ? 44.698  -11.353 32.234 1.00 37.67  ? 256 ALA A O   1 
ATOM   1875 C  CB  . ALA A  1  243 ? 42.775  -13.413 30.483 1.00 41.17  ? 256 ALA A CB  1 
ATOM   1876 N  N   . SER A  1  244 ? 44.528  -10.898 30.022 1.00 40.56  ? 257 SER A N   1 
ATOM   1877 C  CA  . SER A  1  244 ? 44.938  -9.499  30.070 1.00 40.89  ? 257 SER A CA  1 
ATOM   1878 C  C   . SER A  1  244 ? 44.221  -8.769  28.936 1.00 41.47  ? 257 SER A C   1 
ATOM   1879 O  O   . SER A  1  244 ? 43.005  -8.647  28.987 1.00 42.24  ? 257 SER A O   1 
ATOM   1880 C  CB  . SER A  1  244 ? 46.457  -9.330  30.015 1.00 38.68  ? 257 SER A CB  1 
ATOM   1881 O  OG  . SER A  1  244 ? 47.025  -10.052 28.929 1.00 42.42  ? 257 SER A OG  1 
ATOM   1882 N  N   . ASN A  1  245 ? 44.939  -8.342  27.888 1.00 43.22  ? 258 ASN A N   1 
ATOM   1883 C  CA  . ASN A  1  245 ? 44.406  -7.380  26.933 1.00 41.35  ? 258 ASN A CA  1 
ATOM   1884 C  C   . ASN A  1  245 ? 44.069  -8.018  25.578 1.00 41.20  ? 258 ASN A C   1 
ATOM   1885 O  O   . ASN A  1  245 ? 44.140  -7.338  24.559 1.00 38.39  ? 258 ASN A O   1 
ATOM   1886 C  CB  . ASN A  1  245 ? 45.390  -6.224  26.751 1.00 47.27  ? 258 ASN A CB  1 
ATOM   1887 C  CG  . ASN A  1  245 ? 46.740  -6.661  26.221 1.00 46.71  ? 258 ASN A CG  1 
ATOM   1888 O  OD1 . ASN A  1  245 ? 47.037  -7.859  26.170 1.00 46.19  ? 258 ASN A OD1 1 
ATOM   1889 N  ND2 . ASN A  1  245 ? 47.574  -5.706  25.833 1.00 55.60  ? 258 ASN A ND2 1 
ATOM   1890 N  N   . GLU A  1  246 ? 43.691  -9.306  25.562 1.00 41.38  ? 259 GLU A N   1 
ATOM   1891 C  CA  . GLU A  1  246 ? 43.383  -9.994  24.319 1.00 39.34  ? 259 GLU A CA  1 
ATOM   1892 C  C   . GLU A  1  246 ? 42.216  -9.283  23.629 1.00 39.51  ? 259 GLU A C   1 
ATOM   1893 O  O   . GLU A  1  246 ? 41.202  -9.003  24.269 1.00 34.63  ? 259 GLU A O   1 
ATOM   1894 C  CB  . GLU A  1  246 ? 43.050  -11.472 24.537 1.00 41.88  ? 259 GLU A CB  1 
ATOM   1895 C  CG  . GLU A  1  246 ? 44.224  -12.307 25.050 1.00 44.92  ? 259 GLU A CG  1 
ATOM   1896 C  CD  . GLU A  1  246 ? 44.457  -12.293 26.554 1.00 48.81  ? 259 GLU A CD  1 
ATOM   1897 O  OE1 . GLU A  1  246 ? 43.762  -11.558 27.282 1.00 49.34  ? 259 GLU A OE1 1 
ATOM   1898 O  OE2 . GLU A  1  246 ? 45.340  -13.053 27.008 1.00 49.69  ? 259 GLU A OE2 1 
ATOM   1899 N  N   . GLY A  1  247 ? 42.408  -8.941  22.342 1.00 36.51  ? 260 GLY A N   1 
ATOM   1900 C  CA  . GLY A  1  247 ? 41.391  -8.298  21.531 1.00 37.73  ? 260 GLY A CA  1 
ATOM   1901 C  C   . GLY A  1  247 ? 41.590  -6.787  21.421 1.00 40.87  ? 260 GLY A C   1 
ATOM   1902 O  O   . GLY A  1  247 ? 40.863  -6.122  20.683 1.00 43.87  ? 260 GLY A O   1 
ATOM   1903 N  N   . ALA A  1  248 ? 42.564  -6.237  22.151 1.00 41.17  ? 261 ALA A N   1 
ATOM   1904 C  CA  . ALA A  1  248 ? 42.766  -4.791  22.182 1.00 41.74  ? 261 ALA A CA  1 
ATOM   1905 C  C   . ALA A  1  248 ? 43.189  -4.270  20.810 1.00 40.06  ? 261 ALA A C   1 
ATOM   1906 O  O   . ALA A  1  248 ? 42.871  -3.141  20.457 1.00 40.98  ? 261 ALA A O   1 
ATOM   1907 C  CB  . ALA A  1  248 ? 43.783  -4.425  23.242 1.00 41.82  ? 261 ALA A CB  1 
ATOM   1908 N  N   . ASP A  1  249 ? 43.902  -5.097  20.043 1.00 43.79  ? 262 ASP A N   1 
ATOM   1909 C  CA  . ASP A  1  249 ? 44.298  -4.773  18.678 1.00 47.97  ? 262 ASP A CA  1 
ATOM   1910 C  C   . ASP A  1  249 ? 43.067  -4.596  17.785 1.00 45.87  ? 262 ASP A C   1 
ATOM   1911 O  O   . ASP A  1  249 ? 43.037  -3.717  16.931 1.00 46.76  ? 262 ASP A O   1 
ATOM   1912 C  CB  . ASP A  1  249 ? 45.292  -5.792  18.131 1.00 53.37  ? 262 ASP A CB  1 
ATOM   1913 C  CG  . ASP A  1  249 ? 44.912  -7.275  18.223 1.00 70.75  ? 262 ASP A CG  1 
ATOM   1914 O  OD1 . ASP A  1  249 ? 43.897  -7.635  18.891 1.00 64.90  ? 262 ASP A OD1 1 
ATOM   1915 O  OD2 . ASP A  1  249 ? 45.646  -8.090  17.625 1.00 79.22  ? 262 ASP A OD2 1 
ATOM   1916 N  N   . GLN A  1  250 ? 42.032  -5.414  17.990 1.00 49.09  ? 263 GLN A N   1 
ATOM   1917 C  CA  . GLN A  1  250 ? 40.803  -5.303  17.210 1.00 47.71  ? 263 GLN A CA  1 
ATOM   1918 C  C   . GLN A  1  250 ? 40.053  -4.015  17.546 1.00 45.76  ? 263 GLN A C   1 
ATOM   1919 O  O   . GLN A  1  250 ? 39.438  -3.424  16.667 1.00 46.02  ? 263 GLN A O   1 
ATOM   1920 C  CB  . GLN A  1  250 ? 39.931  -6.544  17.388 1.00 51.61  ? 263 GLN A CB  1 
ATOM   1921 C  CG  . GLN A  1  250 ? 40.539  -7.788  16.742 1.00 57.79  ? 263 GLN A CG  1 
ATOM   1922 C  CD  . GLN A  1  250 ? 39.723  -9.041  16.957 1.00 67.41  ? 263 GLN A CD  1 
ATOM   1923 O  OE1 . GLN A  1  250 ? 38.609  -9.006  17.484 1.00 85.45  ? 263 GLN A OE1 1 
ATOM   1924 N  NE2 . GLN A  1  250 ? 40.267  -10.169 16.528 1.00 80.36  ? 263 GLN A NE2 1 
ATOM   1925 N  N   . VAL A  1  251 ? 40.125  -3.562  18.803 1.00 42.99  ? 264 VAL A N   1 
ATOM   1926 C  CA  . VAL A  1  251 ? 39.450  -2.340  19.209 1.00 41.97  ? 264 VAL A CA  1 
ATOM   1927 C  C   . VAL A  1  251 ? 40.064  -1.147  18.477 1.00 39.14  ? 264 VAL A C   1 
ATOM   1928 O  O   . VAL A  1  251 ? 39.345  -0.261  18.009 1.00 39.99  ? 264 VAL A O   1 
ATOM   1929 C  CB  . VAL A  1  251 ? 39.477  -2.173  20.742 1.00 39.89  ? 264 VAL A CB  1 
ATOM   1930 C  CG1 . VAL A  1  251 ? 39.018  -0.790  21.176 1.00 41.33  ? 264 VAL A CG1 1 
ATOM   1931 C  CG2 . VAL A  1  251 ? 38.628  -3.234  21.427 1.00 40.04  ? 264 VAL A CG2 1 
ATOM   1932 N  N   . LEU A  1  252 ? 41.397  -1.120  18.400 1.00 40.37  ? 265 LEU A N   1 
ATOM   1933 C  CA  . LEU A  1  252 ? 42.109  -0.080  17.673 1.00 44.52  ? 265 LEU A CA  1 
ATOM   1934 C  C   . LEU A  1  252 ? 41.800  -0.166  16.180 1.00 43.91  ? 265 LEU A C   1 
ATOM   1935 O  O   . LEU A  1  252 ? 41.632  0.860   15.533 1.00 50.65  ? 265 LEU A O   1 
ATOM   1936 C  CB  . LEU A  1  252 ? 43.609  -0.191  17.942 1.00 45.06  ? 265 LEU A CB  1 
ATOM   1937 C  CG  . LEU A  1  252 ? 44.485  0.894   17.306 1.00 45.33  ? 265 LEU A CG  1 
ATOM   1938 C  CD1 . LEU A  1  252 ? 44.155  2.292   17.828 1.00 45.15  ? 265 LEU A CD1 1 
ATOM   1939 C  CD2 . LEU A  1  252 ? 45.961  0.581   17.518 1.00 42.95  ? 265 LEU A CD2 1 
ATOM   1940 N  N   . ALA A  1  253 ? 41.725  -1.389  15.643 1.00 45.94  ? 266 ALA A N   1 
ATOM   1941 C  CA  . ALA A  1  253 ? 41.514  -1.600  14.216 1.00 49.81  ? 266 ALA A CA  1 
ATOM   1942 C  C   . ALA A  1  253 ? 40.149  -1.073  13.777 1.00 49.96  ? 266 ALA A C   1 
ATOM   1943 O  O   . ALA A  1  253 ? 40.022  -0.583  12.663 1.00 54.02  ? 266 ALA A O   1 
ATOM   1944 C  CB  . ALA A  1  253 ? 41.674  -3.069  13.869 1.00 48.63  ? 266 ALA A CB  1 
ATOM   1945 N  N   . ALA A  1  254 ? 39.137  -1.163  14.649 1.00 51.76  ? 267 ALA A N   1 
ATOM   1946 C  CA  . ALA A  1  254 ? 37.779  -0.732  14.331 1.00 48.12  ? 267 ALA A CA  1 
ATOM   1947 C  C   . ALA A  1  254 ? 37.724  0.770   14.055 1.00 46.01  ? 267 ALA A C   1 
ATOM   1948 O  O   . ALA A  1  254 ? 36.950  1.200   13.207 1.00 49.59  ? 267 ALA A O   1 
ATOM   1949 C  CB  . ALA A  1  254 ? 36.835  -1.113  15.461 1.00 48.21  ? 267 ALA A CB  1 
ATOM   1950 N  N   . HIS A  1  255 ? 38.506  1.564   14.798 1.00 44.22  ? 268 HIS A N   1 
ATOM   1951 C  CA  . HIS A  1  255 ? 38.619  2.995   14.556 1.00 48.67  ? 268 HIS A CA  1 
ATOM   1952 C  C   . HIS A  1  255 ? 40.070  3.427   14.763 1.00 49.78  ? 268 HIS A C   1 
ATOM   1953 O  O   . HIS A  1  255 ? 40.432  3.898   15.834 1.00 49.42  ? 268 HIS A O   1 
ATOM   1954 C  CB  . HIS A  1  255 ? 37.627  3.795   15.407 1.00 50.74  ? 268 HIS A CB  1 
ATOM   1955 C  CG  . HIS A  1  255 ? 36.191  3.553   15.058 1.00 57.53  ? 268 HIS A CG  1 
ATOM   1956 N  ND1 . HIS A  1  255 ? 35.608  4.054   13.914 1.00 59.47  ? 268 HIS A ND1 1 
ATOM   1957 C  CD2 . HIS A  1  255 ? 35.226  2.847   15.684 1.00 59.74  ? 268 HIS A CD2 1 
ATOM   1958 C  CE1 . HIS A  1  255 ? 34.336  3.670   13.869 1.00 61.08  ? 268 HIS A CE1 1 
ATOM   1959 N  NE2 . HIS A  1  255 ? 34.081  2.940   14.937 1.00 57.91  ? 268 HIS A NE2 1 
ATOM   1960 N  N   . PRO A  1  256 ? 40.948  3.255   13.746 1.00 54.58  ? 269 PRO A N   1 
ATOM   1961 C  CA  . PRO A  1  256 ? 42.361  3.637   13.861 1.00 49.74  ? 269 PRO A CA  1 
ATOM   1962 C  C   . PRO A  1  256 ? 42.514  5.054   14.398 1.00 47.96  ? 269 PRO A C   1 
ATOM   1963 O  O   . PRO A  1  256 ? 41.820  5.960   13.947 1.00 43.65  ? 269 PRO A O   1 
ATOM   1964 C  CB  . PRO A  1  256 ? 42.899  3.491   12.430 1.00 49.60  ? 269 PRO A CB  1 
ATOM   1965 C  CG  . PRO A  1  256 ? 42.014  2.414   11.831 1.00 51.88  ? 269 PRO A CG  1 
ATOM   1966 C  CD  . PRO A  1  256 ? 40.631  2.645   12.443 1.00 50.66  ? 269 PRO A CD  1 
ATOM   1967 N  N   . TRP A  1  257 ? 43.405  5.210   15.389 1.00 46.08  ? 270 TRP A N   1 
ATOM   1968 C  CA  . TRP A  1  257 ? 43.583  6.471   16.089 1.00 45.90  ? 270 TRP A CA  1 
ATOM   1969 C  C   . TRP A  1  257 ? 45.053  6.640   16.463 1.00 43.83  ? 270 TRP A C   1 
ATOM   1970 O  O   . TRP A  1  257 ? 45.770  5.657   16.628 1.00 41.52  ? 270 TRP A O   1 
ATOM   1971 C  CB  . TRP A  1  257 ? 42.664  6.514   17.319 1.00 43.21  ? 270 TRP A CB  1 
ATOM   1972 C  CG  . TRP A  1  257 ? 42.689  7.821   18.052 1.00 42.91  ? 270 TRP A CG  1 
ATOM   1973 C  CD1 . TRP A  1  257 ? 43.376  8.075   19.197 1.00 49.35  ? 270 TRP A CD1 1 
ATOM   1974 C  CD2 . TRP A  1  257 ? 42.033  9.054   17.689 1.00 43.25  ? 270 TRP A CD2 1 
ATOM   1975 N  NE1 . TRP A  1  257 ? 43.181  9.370   19.589 1.00 51.64  ? 270 TRP A NE1 1 
ATOM   1976 C  CE2 . TRP A  1  257 ? 42.371  9.992   18.680 1.00 46.02  ? 270 TRP A CE2 1 
ATOM   1977 C  CE3 . TRP A  1  257 ? 41.209  9.459   16.632 1.00 49.02  ? 270 TRP A CE3 1 
ATOM   1978 C  CZ2 . TRP A  1  257 ? 41.912  11.302  18.646 1.00 54.76  ? 270 TRP A CZ2 1 
ATOM   1979 C  CZ3 . TRP A  1  257 ? 40.762  10.764  16.595 1.00 47.44  ? 270 TRP A CZ3 1 
ATOM   1980 C  CH2 . TRP A  1  257 ? 41.121  11.672  17.585 1.00 49.55  ? 270 TRP A CH2 1 
ATOM   1981 N  N   . VAL A  1  258 ? 45.488  7.897   16.567 1.00 46.83  ? 271 VAL A N   1 
ATOM   1982 C  CA  . VAL A  1  258 ? 46.883  8.226   16.801 1.00 51.98  ? 271 VAL A CA  1 
ATOM   1983 C  C   . VAL A  1  258 ? 46.994  8.953   18.138 1.00 47.16  ? 271 VAL A C   1 
ATOM   1984 O  O   . VAL A  1  258 ? 46.117  9.747   18.469 1.00 48.53  ? 271 VAL A O   1 
ATOM   1985 C  CB  . VAL A  1  258 ? 47.428  9.088   15.647 1.00 53.77  ? 271 VAL A CB  1 
ATOM   1986 C  CG1 . VAL A  1  258 ? 48.867  9.502   15.900 1.00 62.76  ? 271 VAL A CG1 1 
ATOM   1987 C  CG2 . VAL A  1  258 ? 47.331  8.385   14.302 1.00 53.01  ? 271 VAL A CG2 1 
ATOM   1988 N  N   . PRO A  1  259 ? 48.053  8.715   18.950 1.00 42.17  ? 272 PRO A N   1 
ATOM   1989 C  CA  . PRO A  1  259 ? 48.229  9.457   20.199 1.00 44.18  ? 272 PRO A CA  1 
ATOM   1990 C  C   . PRO A  1  259 ? 48.350  10.954  19.946 1.00 45.32  ? 272 PRO A C   1 
ATOM   1991 O  O   . PRO A  1  259 ? 48.898  11.376  18.932 1.00 46.77  ? 272 PRO A O   1 
ATOM   1992 C  CB  . PRO A  1  259 ? 49.513  8.864   20.806 1.00 46.79  ? 272 PRO A CB  1 
ATOM   1993 C  CG  . PRO A  1  259 ? 50.223  8.234   19.618 1.00 45.34  ? 272 PRO A CG  1 
ATOM   1994 C  CD  . PRO A  1  259 ? 49.098  7.695   18.755 1.00 43.98  ? 272 PRO A CD  1 
ATOM   1995 N  N   . GLY A  1  260 ? 47.851  11.743  20.900 1.00 45.22  ? 273 GLY A N   1 
ATOM   1996 C  CA  . GLY A  1  260 ? 47.896  13.190  20.814 1.00 44.86  ? 273 GLY A CA  1 
ATOM   1997 C  C   . GLY A  1  260 ? 47.030  13.824  21.890 1.00 45.37  ? 273 GLY A C   1 
ATOM   1998 O  O   . GLY A  1  260 ? 46.897  13.257  22.966 1.00 46.56  ? 273 GLY A O   1 
ATOM   1999 N  N   . GLY A  1  261 ? 46.443  14.985  21.568 1.00 47.98  ? 274 GLY A N   1 
ATOM   2000 C  CA  . GLY A  1  261 ? 45.569  15.715  22.473 1.00 49.43  ? 274 GLY A CA  1 
ATOM   2001 C  C   . GLY A  1  261 ? 45.083  17.021  21.842 1.00 52.91  ? 274 GLY A C   1 
ATOM   2002 O  O   . GLY A  1  261 ? 45.597  17.445  20.810 1.00 53.10  ? 274 GLY A O   1 
ATOM   2003 N  N   . ASN A  1  262 ? 44.084  17.649  22.478 1.00 50.22  ? 275 ASN A N   1 
ATOM   2004 C  CA  . ASN A  1  262 ? 43.634  18.979  22.103 1.00 49.17  ? 275 ASN A CA  1 
ATOM   2005 C  C   . ASN A  1  262 ? 44.727  19.999  22.430 1.00 54.87  ? 275 ASN A C   1 
ATOM   2006 O  O   . ASN A  1  262 ? 45.234  20.008  23.549 1.00 57.58  ? 275 ASN A O   1 
ATOM   2007 C  CB  . ASN A  1  262 ? 42.349  19.359  22.831 1.00 46.50  ? 275 ASN A CB  1 
ATOM   2008 C  CG  . ASN A  1  262 ? 41.096  18.890  22.138 1.00 45.26  ? 275 ASN A CG  1 
ATOM   2009 O  OD1 . ASN A  1  262 ? 41.114  18.599  20.937 1.00 49.91  ? 275 ASN A OD1 1 
ATOM   2010 N  ND2 . ASN A  1  262 ? 39.999  18.823  22.883 1.00 44.59  ? 275 ASN A ND2 1 
ATOM   2011 N  N   . ALA A  1  263 ? 45.047  20.882  21.472 1.00 57.17  ? 276 ALA A N   1 
ATOM   2012 C  CA  . ALA A  1  263 ? 46.094  21.879  21.660 1.00 56.44  ? 276 ALA A CA  1 
ATOM   2013 C  C   . ALA A  1  263 ? 45.512  23.219  22.105 1.00 58.78  ? 276 ALA A C   1 
ATOM   2014 O  O   . ALA A  1  263 ? 44.379  23.552  21.763 1.00 56.44  ? 276 ALA A O   1 
ATOM   2015 C  CB  . ALA A  1  263 ? 46.876  22.032  20.379 1.00 57.37  ? 276 ALA A CB  1 
ATOM   2016 N  N   . ASP A  1  264 ? 46.314  23.965  22.887 1.00 65.06  ? 277 ASP A N   1 
ATOM   2017 C  CA  . ASP A  1  264 ? 46.086  25.366  23.217 1.00 68.84  ? 277 ASP A CA  1 
ATOM   2018 C  C   . ASP A  1  264 ? 44.756  25.580  23.925 1.00 69.55  ? 277 ASP A C   1 
ATOM   2019 O  O   . ASP A  1  264 ? 43.990  26.464  23.545 1.00 73.12  ? 277 ASP A O   1 
ATOM   2020 C  CB  . ASP A  1  264 ? 46.189  26.253  21.988 1.00 78.00  ? 277 ASP A CB  1 
ATOM   2021 C  CG  . ASP A  1  264 ? 47.548  26.203  21.292 1.00 84.58  ? 277 ASP A CG  1 
ATOM   2022 O  OD1 . ASP A  1  264 ? 48.570  26.297  22.035 1.00 87.78  ? 277 ASP A OD1 1 
ATOM   2023 O  OD2 . ASP A  1  264 ? 47.568  26.062  20.028 1.00 82.99  ? 277 ASP A OD2 1 
ATOM   2024 N  N   . ASN A  1  265 ? 44.518  24.791  24.979 1.00 71.87  ? 278 ASN A N   1 
ATOM   2025 C  CA  . ASN A  1  265 ? 43.340  24.935  25.818 1.00 69.61  ? 278 ASN A CA  1 
ATOM   2026 C  C   . ASN A  1  265 ? 42.098  25.163  24.952 1.00 61.04  ? 278 ASN A C   1 
ATOM   2027 O  O   . ASN A  1  265 ? 41.254  25.972  25.309 1.00 56.94  ? 278 ASN A O   1 
ATOM   2028 C  CB  . ASN A  1  265 ? 43.580  26.042  26.843 1.00 75.39  ? 278 ASN A CB  1 
ATOM   2029 C  CG  . ASN A  1  265 ? 42.593  26.031  27.986 1.00 87.11  ? 278 ASN A CG  1 
ATOM   2030 O  OD1 . ASN A  1  265 ? 42.235  24.957  28.485 1.00 91.72  ? 278 ASN A OD1 1 
ATOM   2031 N  ND2 . ASN A  1  265 ? 42.137  27.205  28.403 1.00 95.51  ? 278 ASN A ND2 1 
ATOM   2032 N  N   . GLN A  1  266 ? 41.974  24.429  23.837 1.00 61.09  ? 279 GLN A N   1 
ATOM   2033 C  CA  . GLN A  1  266 ? 40.854  24.582  22.918 1.00 65.96  ? 279 GLN A CA  1 
ATOM   2034 C  C   . GLN A  1  266 ? 40.242  23.220  22.593 1.00 65.72  ? 279 GLN A C   1 
ATOM   2035 O  O   . GLN A  1  266 ? 40.957  22.252  22.372 1.00 66.03  ? 279 GLN A O   1 
ATOM   2036 C  CB  . GLN A  1  266 ? 41.266  25.274  21.615 1.00 74.72  ? 279 GLN A CB  1 
ATOM   2037 C  CG  . GLN A  1  266 ? 41.236  26.798  21.716 1.00 83.27  ? 279 GLN A CG  1 
ATOM   2038 C  CD  . GLN A  1  266 ? 41.758  27.503  20.484 1.00 92.67  ? 279 GLN A CD  1 
ATOM   2039 O  OE1 . GLN A  1  266 ? 42.346  26.898  19.578 1.00 82.48  ? 279 GLN A OE1 1 
ATOM   2040 N  NE2 . GLN A  1  266 ? 41.556  28.811  20.455 1.00 99.79  ? 279 GLN A NE2 1 
ATOM   2041 N  N   . VAL A  1  267 ? 38.909  23.174  22.502 1.00 60.51  ? 280 VAL A N   1 
ATOM   2042 C  CA  . VAL A  1  267 ? 38.209  21.968  22.089 1.00 59.61  ? 280 VAL A CA  1 
ATOM   2043 C  C   . VAL A  1  267 ? 38.290  21.812  20.569 1.00 60.70  ? 280 VAL A C   1 
ATOM   2044 O  O   . VAL A  1  267 ? 38.707  22.727  19.861 1.00 64.40  ? 280 VAL A O   1 
ATOM   2045 C  CB  . VAL A  1  267 ? 36.745  21.955  22.570 1.00 63.34  ? 280 VAL A CB  1 
ATOM   2046 C  CG1 . VAL A  1  267 ? 36.664  21.857  24.089 1.00 61.01  ? 280 VAL A CG1 1 
ATOM   2047 C  CG2 . VAL A  1  267 ? 35.950  23.154  22.055 1.00 66.29  ? 280 VAL A CG2 1 
ATOM   2048 N  N   . ASN A  1  268 ? 37.909  20.619  20.094 1.00 57.20  ? 281 ASN A N   1 
ATOM   2049 C  CA  . ASN A  1  268 ? 37.920  20.260  18.684 1.00 60.48  ? 281 ASN A CA  1 
ATOM   2050 C  C   . ASN A  1  268 ? 39.207  20.713  18.003 1.00 58.07  ? 281 ASN A C   1 
ATOM   2051 O  O   . ASN A  1  268 ? 39.165  21.249  16.903 1.00 57.36  ? 281 ASN A O   1 
ATOM   2052 C  CB  . ASN A  1  268 ? 36.691  20.804  17.968 1.00 60.55  ? 281 ASN A CB  1 
ATOM   2053 C  CG  . ASN A  1  268 ? 35.437  20.131  18.462 1.00 58.69  ? 281 ASN A CG  1 
ATOM   2054 O  OD1 . ASN A  1  268 ? 35.221  18.941  18.206 1.00 68.52  ? 281 ASN A OD1 1 
ATOM   2055 N  ND2 . ASN A  1  268 ? 34.617  20.866  19.190 1.00 58.43  ? 281 ASN A ND2 1 
ATOM   2056 N  N   . ASN A  1  269 ? 40.344  20.451  18.654 1.00 58.78  ? 282 ASN A N   1 
ATOM   2057 C  CA  . ASN A  1  269 ? 41.638  20.866  18.145 1.00 55.22  ? 282 ASN A CA  1 
ATOM   2058 C  C   . ASN A  1  269 ? 42.665  19.772  18.426 1.00 52.72  ? 282 ASN A C   1 
ATOM   2059 O  O   . ASN A  1  269 ? 43.710  20.033  19.018 1.00 51.76  ? 282 ASN A O   1 
ATOM   2060 C  CB  . ASN A  1  269 ? 42.044  22.204  18.756 1.00 59.04  ? 282 ASN A CB  1 
ATOM   2061 C  CG  . ASN A  1  269 ? 43.171  22.853  17.992 1.00 57.51  ? 282 ASN A CG  1 
ATOM   2062 O  OD1 . ASN A  1  269 ? 43.357  22.583  16.798 1.00 55.90  ? 282 ASN A OD1 1 
ATOM   2063 N  ND2 . ASN A  1  269 ? 43.913  23.715  18.665 1.00 60.50  ? 282 ASN A ND2 1 
ATOM   2064 N  N   . TYR A  1  270 ? 42.357  18.544  17.996 1.00 50.58  ? 283 TYR A N   1 
ATOM   2065 C  CA  . TYR A  1  270 ? 43.191  17.394  18.307 1.00 51.03  ? 283 TYR A CA  1 
ATOM   2066 C  C   . TYR A  1  270 ? 44.405  17.369  17.380 1.00 52.25  ? 283 TYR A C   1 
ATOM   2067 O  O   . TYR A  1  270 ? 44.247  17.329  16.163 1.00 52.44  ? 283 TYR A O   1 
ATOM   2068 C  CB  . TYR A  1  270 ? 42.399  16.090  18.174 1.00 49.43  ? 283 TYR A CB  1 
ATOM   2069 C  CG  . TYR A  1  270 ? 43.106  14.852  18.718 1.00 51.31  ? 283 TYR A CG  1 
ATOM   2070 C  CD1 . TYR A  1  270 ? 43.002  14.507  20.061 1.00 52.51  ? 283 TYR A CD1 1 
ATOM   2071 C  CD2 . TYR A  1  270 ? 43.881  14.032  17.901 1.00 48.19  ? 283 TYR A CD2 1 
ATOM   2072 C  CE1 . TYR A  1  270 ? 43.638  13.385  20.573 1.00 51.53  ? 283 TYR A CE1 1 
ATOM   2073 C  CE2 . TYR A  1  270 ? 44.530  12.914  18.402 1.00 45.35  ? 283 TYR A CE2 1 
ATOM   2074 C  CZ  . TYR A  1  270 ? 44.406  12.588  19.743 1.00 47.51  ? 283 TYR A CZ  1 
ATOM   2075 O  OH  . TYR A  1  270 ? 45.001  11.475  20.261 1.00 47.24  ? 283 TYR A OH  1 
ATOM   2076 N  N   . VAL A  1  271 ? 45.603  17.334  17.981 1.00 53.55  ? 284 VAL A N   1 
ATOM   2077 C  CA  . VAL A  1  271 ? 46.870  17.301  17.266 1.00 56.38  ? 284 VAL A CA  1 
ATOM   2078 C  C   . VAL A  1  271 ? 47.604  16.004  17.607 1.00 55.22  ? 284 VAL A C   1 
ATOM   2079 O  O   . VAL A  1  271 ? 47.735  15.664  18.782 1.00 55.19  ? 284 VAL A O   1 
ATOM   2080 C  CB  . VAL A  1  271 ? 47.698  18.547  17.657 1.00 59.20  ? 284 VAL A CB  1 
ATOM   2081 C  CG1 . VAL A  1  271 ? 49.104  18.544  17.066 1.00 60.14  ? 284 VAL A CG1 1 
ATOM   2082 C  CG2 . VAL A  1  271 ? 46.979  19.836  17.281 1.00 55.34  ? 284 VAL A CG2 1 
ATOM   2083 N  N   . GLU A  1  272 ? 48.106  15.312  16.571 1.00 54.95  ? 285 GLU A N   1 
ATOM   2084 C  CA  A GLU A  1  272 ? 48.904  14.107  16.740 0.50 53.70  ? 285 GLU A CA  1 
ATOM   2085 C  CA  B GLU A  1  272 ? 48.907  14.107  16.736 0.50 53.17  ? 285 GLU A CA  1 
ATOM   2086 C  C   . GLU A  1  272 ? 50.193  14.439  17.493 1.00 52.62  ? 285 GLU A C   1 
ATOM   2087 O  O   . GLU A  1  272 ? 50.742  15.530  17.345 1.00 54.71  ? 285 GLU A O   1 
ATOM   2088 C  CB  A GLU A  1  272 ? 49.191  13.490  15.369 0.50 56.46  ? 285 GLU A CB  1 
ATOM   2089 C  CB  B GLU A  1  272 ? 49.236  13.490  15.373 0.50 55.29  ? 285 GLU A CB  1 
ATOM   2090 C  CG  A GLU A  1  272 ? 47.928  13.046  14.631 0.50 59.71  ? 285 GLU A CG  1 
ATOM   2091 C  CG  B GLU A  1  272 ? 50.251  12.348  15.449 0.50 56.81  ? 285 GLU A CG  1 
ATOM   2092 C  CD  A GLU A  1  272 ? 48.111  12.394  13.272 0.50 57.50  ? 285 GLU A CD  1 
ATOM   2093 C  CD  B GLU A  1  272 ? 50.589  11.662  14.137 0.50 58.33  ? 285 GLU A CD  1 
ATOM   2094 O  OE1 A GLU A  1  272 ? 49.249  12.067  12.893 0.50 61.10  ? 285 GLU A OE1 1 
ATOM   2095 O  OE1 B GLU A  1  272 ? 49.985  12.026  13.100 0.50 66.52  ? 285 GLU A OE1 1 
ATOM   2096 O  OE2 A GLU A  1  272 ? 47.087  12.214  12.590 0.50 58.23  ? 285 GLU A OE2 1 
ATOM   2097 O  OE2 B GLU A  1  272 ? 51.472  10.772  14.160 0.50 51.81  ? 285 GLU A OE2 1 
ATOM   2098 N  N   . ASP A  1  273 ? 50.671  13.483  18.309 1.00 52.20  ? 286 ASP A N   1 
ATOM   2099 C  CA  . ASP A  1  273 ? 51.985  13.562  18.932 1.00 55.15  ? 286 ASP A CA  1 
ATOM   2100 C  C   . ASP A  1  273 ? 52.858  12.461  18.339 1.00 57.78  ? 286 ASP A C   1 
ATOM   2101 O  O   . ASP A  1  273 ? 52.672  11.293  18.664 1.00 53.95  ? 286 ASP A O   1 
ATOM   2102 C  CB  . ASP A  1  273 ? 51.940  13.447  20.449 1.00 56.05  ? 286 ASP A CB  1 
ATOM   2103 C  CG  . ASP A  1  273 ? 53.289  13.515  21.159 1.00 56.38  ? 286 ASP A CG  1 
ATOM   2104 O  OD1 . ASP A  1  273 ? 54.323  13.612  20.464 1.00 54.00  ? 286 ASP A OD1 1 
ATOM   2105 O  OD2 . ASP A  1  273 ? 53.300  13.476  22.405 1.00 56.56  ? 286 ASP A OD2 1 
ATOM   2106 N  N   . PRO A  1  274 ? 53.828  12.790  17.454 1.00 63.05  ? 287 PRO A N   1 
ATOM   2107 C  CA  . PRO A  1  274 ? 54.641  11.759  16.800 1.00 60.73  ? 287 PRO A CA  1 
ATOM   2108 C  C   . PRO A  1  274 ? 55.720  11.129  17.685 1.00 58.55  ? 287 PRO A C   1 
ATOM   2109 O  O   . PRO A  1  274 ? 56.288  10.114  17.312 1.00 53.09  ? 287 PRO A O   1 
ATOM   2110 C  CB  . PRO A  1  274 ? 55.230  12.522  15.596 1.00 62.26  ? 287 PRO A CB  1 
ATOM   2111 C  CG  . PRO A  1  274 ? 55.350  13.957  16.084 1.00 64.83  ? 287 PRO A CG  1 
ATOM   2112 C  CD  . PRO A  1  274 ? 54.188  14.159  17.045 1.00 62.08  ? 287 PRO A CD  1 
ATOM   2113 N  N   . ASP A  1  275 ? 55.978  11.720  18.863 1.00 56.78  ? 288 ASP A N   1 
ATOM   2114 C  CA  . ASP A  1  275 ? 56.988  11.243  19.798 1.00 57.75  ? 288 ASP A CA  1 
ATOM   2115 C  C   . ASP A  1  275 ? 56.392  10.267  20.815 1.00 58.35  ? 288 ASP A C   1 
ATOM   2116 O  O   . ASP A  1  275 ? 57.130  9.564   21.504 1.00 54.70  ? 288 ASP A O   1 
ATOM   2117 C  CB  . ASP A  1  275 ? 57.648  12.404  20.531 1.00 63.27  ? 288 ASP A CB  1 
ATOM   2118 C  CG  . ASP A  1  275 ? 58.497  13.330  19.669 1.00 67.38  ? 288 ASP A CG  1 
ATOM   2119 O  OD1 . ASP A  1  275 ? 58.905  12.896  18.565 1.00 62.42  ? 288 ASP A OD1 1 
ATOM   2120 O  OD2 . ASP A  1  275 ? 58.721  14.483  20.099 1.00 68.05  ? 288 ASP A OD2 1 
ATOM   2121 N  N   . SER A  1  276 ? 55.056  10.232  20.918 1.00 55.70  ? 289 SER A N   1 
ATOM   2122 C  CA  . SER A  1  276 ? 54.373  9.375   21.874 1.00 49.15  ? 289 SER A CA  1 
ATOM   2123 C  C   . SER A  1  276 ? 54.626  7.906   21.560 1.00 44.88  ? 289 SER A C   1 
ATOM   2124 O  O   . SER A  1  276 ? 54.826  7.527   20.408 1.00 41.41  ? 289 SER A O   1 
ATOM   2125 C  CB  . SER A  1  276 ? 52.887  9.649   21.886 1.00 50.78  ? 289 SER A CB  1 
ATOM   2126 O  OG  . SER A  1  276 ? 52.189  8.656   22.627 1.00 45.59  ? 289 SER A OG  1 
ATOM   2127 N  N   . ALA A  1  277 ? 54.558  7.078   22.602 1.00 45.09  ? 290 ALA A N   1 
ATOM   2128 C  CA  . ALA A  1  277 ? 54.457  5.639   22.412 1.00 46.15  ? 290 ALA A CA  1 
ATOM   2129 C  C   . ALA A  1  277 ? 53.185  5.317   21.639 1.00 43.21  ? 290 ALA A C   1 
ATOM   2130 O  O   . ALA A  1  277 ? 52.211  6.049   21.733 1.00 42.38  ? 290 ALA A O   1 
ATOM   2131 C  CB  . ALA A  1  277 ? 54.463  4.927   23.746 1.00 46.83  ? 290 ALA A CB  1 
ATOM   2132 N  N   . ASP A  1  278 ? 53.230  4.220   20.876 1.00 45.69  ? 291 ASP A N   1 
ATOM   2133 C  CA  . ASP A  1  278 ? 52.063  3.613   20.258 1.00 47.98  ? 291 ASP A CA  1 
ATOM   2134 C  C   . ASP A  1  278 ? 52.305  2.106   20.269 1.00 49.35  ? 291 ASP A C   1 
ATOM   2135 O  O   . ASP A  1  278 ? 53.244  1.663   20.935 1.00 44.19  ? 291 ASP A O   1 
ATOM   2136 C  CB  . ASP A  1  278 ? 51.774  4.245   18.905 1.00 49.89  ? 291 ASP A CB  1 
ATOM   2137 C  CG  . ASP A  1  278 ? 52.779  3.952   17.798 1.00 51.65  ? 291 ASP A CG  1 
ATOM   2138 O  OD1 . ASP A  1  278 ? 53.522  2.950   17.908 1.00 49.07  ? 291 ASP A OD1 1 
ATOM   2139 O  OD2 . ASP A  1  278 ? 52.811  4.744   16.835 1.00 54.96  ? 291 ASP A OD2 1 
ATOM   2140 N  N   . PHE A  1  279 ? 51.496  1.325   19.533 1.00 44.36  ? 292 PHE A N   1 
ATOM   2141 C  CA  . PHE A  1  279 ? 51.523  -0.124  19.698 1.00 46.37  ? 292 PHE A CA  1 
ATOM   2142 C  C   . PHE A  1  279 ? 52.641  -0.769  18.884 1.00 46.17  ? 292 PHE A C   1 
ATOM   2143 O  O   . PHE A  1  279 ? 52.904  -1.950  19.085 1.00 45.74  ? 292 PHE A O   1 
ATOM   2144 C  CB  . PHE A  1  279 ? 50.171  -0.779  19.406 1.00 47.35  ? 292 PHE A CB  1 
ATOM   2145 C  CG  . PHE A  1  279 ? 49.159  -0.502  20.507 1.00 46.65  ? 292 PHE A CG  1 
ATOM   2146 C  CD1 . PHE A  1  279 ? 49.164  -1.246  21.683 1.00 50.75  ? 292 PHE A CD1 1 
ATOM   2147 C  CD2 . PHE A  1  279 ? 48.233  0.525   20.380 1.00 46.92  ? 292 PHE A CD2 1 
ATOM   2148 C  CE1 . PHE A  1  279 ? 48.247  -0.981  22.696 1.00 50.97  ? 292 PHE A CE1 1 
ATOM   2149 C  CE2 . PHE A  1  279 ? 47.326  0.793   21.398 1.00 51.45  ? 292 PHE A CE2 1 
ATOM   2150 C  CZ  . PHE A  1  279 ? 47.337  0.044   22.555 1.00 50.10  ? 292 PHE A CZ  1 
ATOM   2151 N  N   . THR A  1  280 ? 53.300  -0.017  17.995 1.00 49.66  ? 293 THR A N   1 
ATOM   2152 C  CA  . THR A  1  280 ? 54.475  -0.514  17.285 1.00 54.82  ? 293 THR A CA  1 
ATOM   2153 C  C   . THR A  1  280 ? 55.746  0.153   17.826 1.00 56.28  ? 293 THR A C   1 
ATOM   2154 O  O   . THR A  1  280 ? 56.833  -0.135  17.332 1.00 61.44  ? 293 THR A O   1 
ATOM   2155 C  CB  . THR A  1  280 ? 54.319  -0.268  15.778 1.00 54.83  ? 293 THR A CB  1 
ATOM   2156 O  OG1 . THR A  1  280 ? 54.226  1.143   15.572 1.00 50.87  ? 293 THR A OG1 1 
ATOM   2157 C  CG2 . THR A  1  280 ? 53.090  -0.943  15.194 1.00 52.39  ? 293 THR A CG2 1 
ATOM   2158 N  N   . HIS A  1  281 ? 55.600  1.042   18.824 1.00 55.40  ? 294 HIS A N   1 
ATOM   2159 C  CA  . HIS A  1  281 ? 56.712  1.763   19.436 1.00 52.54  ? 294 HIS A CA  1 
ATOM   2160 C  C   . HIS A  1  281 ? 56.535  1.777   20.958 1.00 49.69  ? 294 HIS A C   1 
ATOM   2161 O  O   . HIS A  1  281 ? 56.382  2.829   21.572 1.00 52.51  ? 294 HIS A O   1 
ATOM   2162 C  CB  . HIS A  1  281 ? 56.851  3.181   18.854 1.00 59.17  ? 294 HIS A CB  1 
ATOM   2163 C  CG  . HIS A  1  281 ? 57.108  3.251   17.379 1.00 74.23  ? 294 HIS A CG  1 
ATOM   2164 N  ND1 . HIS A  1  281 ? 58.348  3.029   16.816 1.00 79.20  ? 294 HIS A ND1 1 
ATOM   2165 C  CD2 . HIS A  1  281 ? 56.285  3.514   16.356 1.00 80.47  ? 294 HIS A CD2 1 
ATOM   2166 C  CE1 . HIS A  1  281 ? 58.266  3.158   15.499 1.00 84.12  ? 294 HIS A CE1 1 
ATOM   2167 N  NE2 . HIS A  1  281 ? 57.021  3.454   15.199 1.00 84.56  ? 294 HIS A NE2 1 
ATOM   2168 N  N   . LEU A  1  282 ? 56.558  0.589   21.569 1.00 48.09  ? 295 LEU A N   1 
ATOM   2169 C  CA  . LEU A  1  282 ? 56.179  0.389   22.959 1.00 47.14  ? 295 LEU A CA  1 
ATOM   2170 C  C   . LEU A  1  282 ? 57.301  0.759   23.924 1.00 50.55  ? 295 LEU A C   1 
ATOM   2171 O  O   . LEU A  1  282 ? 57.012  1.124   25.061 1.00 50.52  ? 295 LEU A O   1 
ATOM   2172 C  CB  . LEU A  1  282 ? 55.761  -1.066  23.169 1.00 50.26  ? 295 LEU A CB  1 
ATOM   2173 C  CG  . LEU A  1  282 ? 54.348  -1.470  22.728 1.00 50.56  ? 295 LEU A CG  1 
ATOM   2174 C  CD1 . LEU A  1  282 ? 54.166  -2.977  22.772 1.00 49.90  ? 295 LEU A CD1 1 
ATOM   2175 C  CD2 . LEU A  1  282 ? 53.267  -0.822  23.562 1.00 49.09  ? 295 LEU A CD2 1 
ATOM   2176 N  N   . CYS A  1  283 ? 58.565  0.609   23.512 1.00 51.01  ? 296 CYS A N   1 
ATOM   2177 C  CA  . CYS A  1  283 ? 59.689  0.887   24.396 1.00 51.65  ? 296 CYS A CA  1 
ATOM   2178 C  C   . CYS A  1  283 ? 59.753  2.379   24.727 1.00 49.06  ? 296 CYS A C   1 
ATOM   2179 O  O   . CYS A  1  283 ? 60.310  2.761   25.759 1.00 51.88  ? 296 CYS A O   1 
ATOM   2180 C  CB  . CYS A  1  283 ? 61.018  0.362   23.846 1.00 53.53  ? 296 CYS A CB  1 
ATOM   2181 S  SG  . CYS A  1  283 ? 61.173  -1.450  23.787 1.00 61.77  ? 296 CYS A SG  1 
ATOM   2182 N  N   . ARG A  1  284 ? 59.150  3.220   23.873 1.00 45.71  ? 297 ARG A N   1 
ATOM   2183 C  CA  . ARG A  1  284 ? 59.020  4.640   24.162 1.00 45.38  ? 297 ARG A CA  1 
ATOM   2184 C  C   . ARG A  1  284 ? 58.280  4.852   25.480 1.00 46.26  ? 297 ARG A C   1 
ATOM   2185 O  O   . ARG A  1  284 ? 58.582  5.789   26.214 1.00 47.76  ? 297 ARG A O   1 
ATOM   2186 C  CB  . ARG A  1  284 ? 58.261  5.380   23.061 1.00 47.32  ? 297 ARG A CB  1 
ATOM   2187 C  CG  . ARG A  1  284 ? 59.025  5.471   21.748 1.00 51.48  ? 297 ARG A CG  1 
ATOM   2188 C  CD  . ARG A  1  284 ? 58.273  6.344   20.765 1.00 53.12  ? 297 ARG A CD  1 
ATOM   2189 N  NE  . ARG A  1  284 ? 58.916  6.364   19.451 1.00 59.50  ? 297 ARG A NE  1 
ATOM   2190 C  CZ  . ARG A  1  284 ? 58.336  6.772   18.338 1.00 65.66  ? 297 ARG A CZ  1 
ATOM   2191 N  NH1 . ARG A  1  284 ? 57.115  7.278   18.381 1.00 59.11  ? 297 ARG A NH1 1 
ATOM   2192 N  NH2 . ARG A  1  284 ? 58.979  6.649   17.184 1.00 68.44  ? 297 ARG A NH2 1 
ATOM   2193 N  N   . LEU A  1  285 ? 57.309  3.977   25.769 1.00 44.59  ? 298 LEU A N   1 
ATOM   2194 C  CA  . LEU A  1  285 ? 56.548  4.073   27.001 1.00 46.83  ? 298 LEU A CA  1 
ATOM   2195 C  C   . LEU A  1  285 ? 57.478  3.807   28.181 1.00 44.12  ? 298 LEU A C   1 
ATOM   2196 O  O   . LEU A  1  285 ? 57.422  4.533   29.166 1.00 39.29  ? 298 LEU A O   1 
ATOM   2197 C  CB  . LEU A  1  285 ? 55.354  3.120   26.997 1.00 51.41  ? 298 LEU A CB  1 
ATOM   2198 C  CG  . LEU A  1  285 ? 54.391  3.259   28.184 1.00 57.45  ? 298 LEU A CG  1 
ATOM   2199 C  CD1 . LEU A  1  285 ? 52.992  2.863   27.779 1.00 64.12  ? 298 LEU A CD1 1 
ATOM   2200 C  CD2 . LEU A  1  285 ? 54.799  2.414   29.375 1.00 57.54  ? 298 LEU A CD2 1 
ATOM   2201 N  N   . TYR A  1  286 ? 58.318  2.767   28.059 1.00 45.50  ? 299 TYR A N   1 
ATOM   2202 C  CA  . TYR A  1  286 ? 59.279  2.403   29.094 1.00 46.08  ? 299 TYR A CA  1 
ATOM   2203 C  C   . TYR A  1  286 ? 60.117  3.634   29.435 1.00 44.00  ? 299 TYR A C   1 
ATOM   2204 O  O   . TYR A  1  286 ? 60.194  4.011   30.597 1.00 48.89  ? 299 TYR A O   1 
ATOM   2205 C  CB  . TYR A  1  286 ? 60.149  1.199   28.699 1.00 46.60  ? 299 TYR A CB  1 
ATOM   2206 C  CG  . TYR A  1  286 ? 61.285  0.888   29.668 1.00 42.29  ? 299 TYR A CG  1 
ATOM   2207 C  CD1 . TYR A  1  286 ? 61.032  0.571   31.000 1.00 41.77  ? 299 TYR A CD1 1 
ATOM   2208 C  CD2 . TYR A  1  286 ? 62.615  0.927   29.254 1.00 40.44  ? 299 TYR A CD2 1 
ATOM   2209 C  CE1 . TYR A  1  286 ? 62.063  0.300   31.885 1.00 40.61  ? 299 TYR A CE1 1 
ATOM   2210 C  CE2 . TYR A  1  286 ? 63.657  0.662   30.129 1.00 39.93  ? 299 TYR A CE2 1 
ATOM   2211 C  CZ  . TYR A  1  286 ? 63.380  0.348   31.450 1.00 42.72  ? 299 TYR A CZ  1 
ATOM   2212 O  OH  . TYR A  1  286 ? 64.397  0.087   32.326 1.00 40.96  ? 299 TYR A OH  1 
ATOM   2213 N  N   . GLU A  1  287 ? 60.658  4.310   28.419 1.00 45.88  ? 300 GLU A N   1 
ATOM   2214 C  CA  . GLU A  1  287 ? 61.571  5.429   28.624 1.00 49.87  ? 300 GLU A CA  1 
ATOM   2215 C  C   . GLU A  1  287 ? 60.853  6.662   29.178 1.00 47.98  ? 300 GLU A C   1 
ATOM   2216 O  O   . GLU A  1  287 ? 61.421  7.360   30.008 1.00 44.77  ? 300 GLU A O   1 
ATOM   2217 C  CB  . GLU A  1  287 ? 62.264  5.807   27.319 1.00 52.65  ? 300 GLU A CB  1 
ATOM   2218 C  CG  . GLU A  1  287 ? 63.074  4.652   26.731 1.00 58.14  ? 300 GLU A CG  1 
ATOM   2219 C  CD  . GLU A  1  287 ? 63.630  4.905   25.332 1.00 72.23  ? 300 GLU A CD  1 
ATOM   2220 O  OE1 . GLU A  1  287 ? 62.831  5.212   24.401 1.00 66.74  ? 300 GLU A OE1 1 
ATOM   2221 O  OE2 . GLU A  1  287 ? 64.872  4.771   25.150 1.00 77.75  ? 300 GLU A OE2 1 
ATOM   2222 N  N   . PHE A  1  288 ? 59.626  6.935   28.704 1.00 44.52  ? 301 PHE A N   1 
ATOM   2223 C  CA  . PHE A  1  288 ? 58.825  8.038   29.212 1.00 42.01  ? 301 PHE A CA  1 
ATOM   2224 C  C   . PHE A  1  288 ? 58.666  7.921   30.730 1.00 39.62  ? 301 PHE A C   1 
ATOM   2225 O  O   . PHE A  1  288 ? 58.804  8.924   31.427 1.00 38.11  ? 301 PHE A O   1 
ATOM   2226 C  CB  . PHE A  1  288 ? 57.473  8.088   28.489 1.00 45.16  ? 301 PHE A CB  1 
ATOM   2227 C  CG  . PHE A  1  288 ? 56.555  9.205   28.970 1.00 46.34  ? 301 PHE A CG  1 
ATOM   2228 C  CD1 . PHE A  1  288 ? 56.714  10.503  28.498 1.00 45.38  ? 301 PHE A CD1 1 
ATOM   2229 C  CD2 . PHE A  1  288 ? 55.556  8.955   29.914 1.00 44.44  ? 301 PHE A CD2 1 
ATOM   2230 C  CE1 . PHE A  1  288 ? 55.892  11.521  28.957 1.00 45.38  ? 301 PHE A CE1 1 
ATOM   2231 C  CE2 . PHE A  1  288 ? 54.757  9.977   30.374 1.00 43.99  ? 301 PHE A CE2 1 
ATOM   2232 C  CZ  . PHE A  1  288 ? 54.923  11.256  29.894 1.00 43.74  ? 301 PHE A CZ  1 
ATOM   2233 N  N   . VAL A  1  289 ? 58.405  6.707   31.241 1.00 39.86  ? 302 VAL A N   1 
ATOM   2234 C  CA  . VAL A  1  289 ? 58.115  6.519   32.659 1.00 43.08  ? 302 VAL A CA  1 
ATOM   2235 C  C   . VAL A  1  289 ? 59.401  6.605   33.469 1.00 37.93  ? 302 VAL A C   1 
ATOM   2236 O  O   . VAL A  1  289 ? 59.384  7.171   34.560 1.00 45.27  ? 302 VAL A O   1 
ATOM   2237 C  CB  . VAL A  1  289 ? 57.369  5.203   32.967 1.00 40.66  ? 302 VAL A CB  1 
ATOM   2238 C  CG1 . VAL A  1  289 ? 57.123  5.005   34.461 1.00 42.02  ? 302 VAL A CG1 1 
ATOM   2239 C  CG2 . VAL A  1  289 ? 56.056  5.128   32.209 1.00 41.26  ? 302 VAL A CG2 1 
ATOM   2240 N  N   . VAL A  1  290 ? 60.489  6.017   32.954 1.00 43.34  ? 303 VAL A N   1 
ATOM   2241 C  CA  . VAL A  1  290 ? 61.774  6.115   33.633 1.00 45.53  ? 303 VAL A CA  1 
ATOM   2242 C  C   . VAL A  1  290 ? 62.093  7.602   33.817 1.00 42.91  ? 303 VAL A C   1 
ATOM   2243 O  O   . VAL A  1  290 ? 62.465  8.033   34.900 1.00 47.65  ? 303 VAL A O   1 
ATOM   2244 C  CB  . VAL A  1  290 ? 62.886  5.342   32.899 1.00 42.88  ? 303 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A  1  290 ? 64.270  5.652   33.449 1.00 42.65  ? 303 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A  1  290 ? 62.628  3.841   32.935 1.00 41.49  ? 303 VAL A CG2 1 
ATOM   2247 N  N   . GLY A  1  291 ? 61.845  8.396   32.770 1.00 43.40  ? 304 GLY A N   1 
ATOM   2248 C  CA  . GLY A  1  291 ? 62.022  9.840   32.800 1.00 43.69  ? 304 GLY A CA  1 
ATOM   2249 C  C   . GLY A  1  291 ? 61.081  10.555  33.777 1.00 45.61  ? 304 GLY A C   1 
ATOM   2250 O  O   . GLY A  1  291 ? 61.498  11.488  34.469 1.00 47.42  ? 304 GLY A O   1 
ATOM   2251 N  N   . SER A  1  292 ? 59.809  10.142  33.831 1.00 41.76  ? 305 SER A N   1 
ATOM   2252 C  CA  . SER A  1  292 ? 58.863  10.740  34.762 1.00 44.13  ? 305 SER A CA  1 
ATOM   2253 C  C   . SER A  1  292 ? 59.308  10.469  36.196 1.00 38.28  ? 305 SER A C   1 
ATOM   2254 O  O   . SER A  1  292 ? 59.148  11.304  37.077 1.00 41.03  ? 305 SER A O   1 
ATOM   2255 C  CB  . SER A  1  292 ? 57.444  10.250  34.519 1.00 44.23  ? 305 SER A CB  1 
ATOM   2256 O  OG  . SER A  1  292 ? 57.085  10.362  33.152 1.00 44.71  ? 305 SER A OG  1 
ATOM   2257 N  N   . VAL A  1  293 ? 59.865  9.285   36.428 1.00 39.26  ? 306 VAL A N   1 
ATOM   2258 C  CA  . VAL A  1  293 ? 60.355  8.907   37.748 1.00 43.56  ? 306 VAL A CA  1 
ATOM   2259 C  C   . VAL A  1  293 ? 61.546  9.793   38.129 1.00 41.29  ? 306 VAL A C   1 
ATOM   2260 O  O   . VAL A  1  293 ? 61.664  10.186  39.289 1.00 38.06  ? 306 VAL A O   1 
ATOM   2261 C  CB  . VAL A  1  293 ? 60.702  7.399   37.791 1.00 45.48  ? 306 VAL A CB  1 
ATOM   2262 C  CG1 . VAL A  1  293 ? 61.525  7.006   39.021 1.00 45.08  ? 306 VAL A CG1 1 
ATOM   2263 C  CG2 . VAL A  1  293 ? 59.455  6.534   37.705 1.00 46.35  ? 306 VAL A CG2 1 
ATOM   2264 N  N   . GLN A  1  294 ? 62.413  10.102  37.154 1.00 40.32  ? 307 GLN A N   1 
ATOM   2265 C  CA  . GLN A  1  294 ? 63.548  10.990  37.364 1.00 40.99  ? 307 GLN A CA  1 
ATOM   2266 C  C   . GLN A  1  294 ? 63.093  12.394  37.761 1.00 41.26  ? 307 GLN A C   1 
ATOM   2267 O  O   . GLN A  1  294 ? 63.742  13.032  38.594 1.00 42.07  ? 307 GLN A O   1 
ATOM   2268 C  CB  . GLN A  1  294 ? 64.467  11.046  36.147 1.00 41.39  ? 307 GLN A CB  1 
ATOM   2269 C  CG  . GLN A  1  294 ? 65.216  9.738   35.899 1.00 45.01  ? 307 GLN A CG  1 
ATOM   2270 C  CD  . GLN A  1  294 ? 66.047  9.771   34.637 1.00 48.53  ? 307 GLN A CD  1 
ATOM   2271 O  OE1 . GLN A  1  294 ? 65.555  9.540   33.527 1.00 53.12  ? 307 GLN A OE1 1 
ATOM   2272 N  NE2 . GLN A  1  294 ? 67.328  10.079  34.794 1.00 45.89  ? 307 GLN A NE2 1 
ATOM   2273 N  N   . GLU A  1  295 ? 61.970  12.857  37.197 1.00 41.96  ? 308 GLU A N   1 
ATOM   2274 C  CA  . GLU A  1  295 ? 61.386  14.132  37.584 1.00 41.45  ? 308 GLU A CA  1 
ATOM   2275 C  C   . GLU A  1  295 ? 60.846  14.070  39.012 1.00 41.05  ? 308 GLU A C   1 
ATOM   2276 O  O   . GLU A  1  295 ? 60.992  15.037  39.740 1.00 44.62  ? 308 GLU A O   1 
ATOM   2277 C  CB  . GLU A  1  295 ? 60.264  14.593  36.658 1.00 46.11  ? 308 GLU A CB  1 
ATOM   2278 C  CG  . GLU A  1  295 ? 60.688  14.785  35.206 1.00 60.06  ? 308 GLU A CG  1 
ATOM   2279 C  CD  . GLU A  1  295 ? 59.531  15.055  34.245 1.00 69.30  ? 308 GLU A CD  1 
ATOM   2280 O  OE1 . GLU A  1  295 ? 58.397  15.298  34.713 1.00 68.90  ? 308 GLU A OE1 1 
ATOM   2281 O  OE2 . GLU A  1  295 ? 59.747  15.012  33.013 1.00 80.31  ? 308 GLU A OE2 1 
ATOM   2282 N  N   . LEU A  1  296 ? 60.228  12.949  39.413 1.00 37.73  ? 309 LEU A N   1 
ATOM   2283 C  CA  . LEU A  1  296 ? 59.676  12.809  40.752 1.00 40.26  ? 309 LEU A CA  1 
ATOM   2284 C  C   . LEU A  1  296 ? 60.808  12.668  41.772 1.00 38.80  ? 309 LEU A C   1 
ATOM   2285 O  O   . LEU A  1  296 ? 60.684  13.142  42.898 1.00 33.71  ? 309 LEU A O   1 
ATOM   2286 C  CB  . LEU A  1  296 ? 58.711  11.618  40.828 1.00 41.74  ? 309 LEU A CB  1 
ATOM   2287 C  CG  . LEU A  1  296 ? 57.402  11.753  40.031 1.00 42.84  ? 309 LEU A CG  1 
ATOM   2288 C  CD1 . LEU A  1  296 ? 56.634  10.452  40.068 1.00 44.92  ? 309 LEU A CD1 1 
ATOM   2289 C  CD2 . LEU A  1  296 ? 56.495  12.879  40.512 1.00 39.86  ? 309 LEU A CD2 1 
ATOM   2290 N  N   . TYR A  1  297 ? 61.893  11.992  41.365 1.00 39.04  ? 310 TYR A N   1 
ATOM   2291 C  CA  . TYR A  1  297 ? 62.994  11.634  42.248 1.00 39.05  ? 310 TYR A CA  1 
ATOM   2292 C  C   . TYR A  1  297 ? 64.318  12.116  41.641 1.00 38.18  ? 310 TYR A C   1 
ATOM   2293 O  O   . TYR A  1  297 ? 65.100  11.323  41.113 1.00 38.81  ? 310 TYR A O   1 
ATOM   2294 C  CB  . TYR A  1  297 ? 62.961  10.115  42.463 1.00 37.25  ? 310 TYR A CB  1 
ATOM   2295 C  CG  . TYR A  1  297 ? 61.736  9.624   43.216 1.00 36.87  ? 310 TYR A CG  1 
ATOM   2296 C  CD1 . TYR A  1  297 ? 61.633  9.772   44.596 1.00 36.37  ? 310 TYR A CD1 1 
ATOM   2297 C  CD2 . TYR A  1  297 ? 60.673  9.022   42.545 1.00 37.44  ? 310 TYR A CD2 1 
ATOM   2298 C  CE1 . TYR A  1  297 ? 60.518  9.324   45.287 1.00 38.37  ? 310 TYR A CE1 1 
ATOM   2299 C  CE2 . TYR A  1  297 ? 59.556  8.567   43.226 1.00 35.93  ? 310 TYR A CE2 1 
ATOM   2300 C  CZ  . TYR A  1  297 ? 59.480  8.714   44.599 1.00 37.15  ? 310 TYR A CZ  1 
ATOM   2301 O  OH  . TYR A  1  297 ? 58.369  8.286   45.261 1.00 37.12  ? 310 TYR A OH  1 
ATOM   2302 N  N   . PRO A  1  298 ? 64.598  13.438  41.669 1.00 39.74  ? 311 PRO A N   1 
ATOM   2303 C  CA  . PRO A  1  298 ? 65.795  13.988  41.024 1.00 38.02  ? 311 PRO A CA  1 
ATOM   2304 C  C   . PRO A  1  298 ? 67.136  13.621  41.670 1.00 39.18  ? 311 PRO A C   1 
ATOM   2305 O  O   . PRO A  1  298 ? 68.123  13.437  40.960 1.00 35.78  ? 311 PRO A O   1 
ATOM   2306 C  CB  . PRO A  1  298 ? 65.529  15.501  41.041 1.00 40.01  ? 311 PRO A CB  1 
ATOM   2307 C  CG  . PRO A  1  298 ? 64.637  15.714  42.247 1.00 42.15  ? 311 PRO A CG  1 
ATOM   2308 C  CD  . PRO A  1  298 ? 63.751  14.475  42.289 1.00 39.53  ? 311 PRO A CD  1 
ATOM   2309 N  N   . ASN A  1  299 ? 67.185  13.475  43.000 1.00 39.23  ? 312 ASN A N   1 
ATOM   2310 C  CA  . ASN A  1  299 ? 68.437  13.118  43.650 1.00 38.11  ? 312 ASN A CA  1 
ATOM   2311 C  C   . ASN A  1  299 ? 68.194  12.227  44.863 1.00 36.79  ? 312 ASN A C   1 
ATOM   2312 O  O   . ASN A  1  299 ? 68.523  12.613  45.972 1.00 35.91  ? 312 ASN A O   1 
ATOM   2313 C  CB  . ASN A  1  299 ? 69.255  14.357  44.006 1.00 40.36  ? 312 ASN A CB  1 
ATOM   2314 C  CG  . ASN A  1  299 ? 70.633  14.003  44.500 1.00 39.86  ? 312 ASN A CG  1 
ATOM   2315 O  OD1 . ASN A  1  299 ? 71.315  13.163  43.888 1.00 45.58  ? 312 ASN A OD1 1 
ATOM   2316 N  ND2 . ASN A  1  299 ? 71.018  14.587  45.624 1.00 35.04  ? 312 ASN A ND2 1 
ATOM   2317 N  N   . PRO A  1  300 ? 67.696  10.982  44.686 1.00 40.21  ? 313 PRO A N   1 
ATOM   2318 C  CA  . PRO A  1  300 ? 67.443  10.087  45.819 1.00 41.09  ? 313 PRO A CA  1 
ATOM   2319 C  C   . PRO A  1  300 ? 68.742  9.558   46.430 1.00 42.86  ? 313 PRO A C   1 
ATOM   2320 O  O   . PRO A  1  300 ? 69.704  9.260   45.711 1.00 40.37  ? 313 PRO A O   1 
ATOM   2321 C  CB  . PRO A  1  300 ? 66.607  8.961   45.187 1.00 40.41  ? 313 PRO A CB  1 
ATOM   2322 C  CG  . PRO A  1  300 ? 67.148  8.900   43.782 1.00 40.31  ? 313 PRO A CG  1 
ATOM   2323 C  CD  . PRO A  1  300 ? 67.397  10.359  43.390 1.00 41.49  ? 313 PRO A CD  1 
ATOM   2324 N  N   . THR A  1  301 ? 68.749  9.423   47.761 1.00 42.49  ? 314 THR A N   1 
ATOM   2325 C  CA  . THR A  1  301 ? 69.841  8.764   48.464 1.00 46.49  ? 314 THR A CA  1 
ATOM   2326 C  C   . THR A  1  301 ? 69.243  7.759   49.452 1.00 46.69  ? 314 THR A C   1 
ATOM   2327 O  O   . THR A  1  301 ? 68.063  7.825   49.785 1.00 50.75  ? 314 THR A O   1 
ATOM   2328 C  CB  . THR A  1  301 ? 70.766  9.768   49.163 1.00 44.43  ? 314 THR A CB  1 
ATOM   2329 O  OG1 . THR A  1  301 ? 69.984  10.480  50.113 1.00 49.62  ? 314 THR A OG1 1 
ATOM   2330 C  CG2 . THR A  1  301 ? 71.378  10.785  48.214 1.00 49.72  ? 314 THR A CG2 1 
ATOM   2331 N  N   . GLY A  1  302 ? 70.068  6.796   49.868 1.00 44.66  ? 315 GLY A N   1 
ATOM   2332 C  CA  . GLY A  1  302 ? 69.766  5.909   50.974 1.00 43.95  ? 315 GLY A CA  1 
ATOM   2333 C  C   . GLY A  1  302 ? 68.768  4.818   50.599 1.00 46.46  ? 315 GLY A C   1 
ATOM   2334 O  O   . GLY A  1  302 ? 68.829  4.270   49.508 1.00 48.50  ? 315 GLY A O   1 
ATOM   2335 N  N   . ILE A  1  303 ? 67.854  4.522   51.532 1.00 48.65  ? 316 ILE A N   1 
ATOM   2336 C  CA  . ILE A  1  303 ? 66.828  3.493   51.392 1.00 50.46  ? 316 ILE A CA  1 
ATOM   2337 C  C   . ILE A  1  303 ? 65.940  3.808   50.183 1.00 42.78  ? 316 ILE A C   1 
ATOM   2338 O  O   . ILE A  1  303 ? 65.535  2.910   49.433 1.00 41.97  ? 316 ILE A O   1 
ATOM   2339 C  CB  . ILE A  1  303 ? 66.027  3.399   52.712 1.00 56.23  ? 316 ILE A CB  1 
ATOM   2340 C  CG1 . ILE A  1  303 ? 66.946  3.118   53.910 1.00 71.35  ? 316 ILE A CG1 1 
ATOM   2341 C  CG2 . ILE A  1  303 ? 64.892  2.380   52.656 1.00 59.48  ? 316 ILE A CG2 1 
ATOM   2342 C  CD1 . ILE A  1  303 ? 67.762  1.837   53.809 1.00 77.85  ? 316 ILE A CD1 1 
ATOM   2343 N  N   . LEU A  1  304 ? 65.640  5.097   50.006 1.00 40.02  ? 317 LEU A N   1 
ATOM   2344 C  CA  . LEU A  1  304 ? 64.820  5.550   48.898 1.00 41.83  ? 317 LEU A CA  1 
ATOM   2345 C  C   . LEU A  1  304 ? 65.489  5.180   47.578 1.00 39.77  ? 317 LEU A C   1 
ATOM   2346 O  O   . LEU A  1  304 ? 64.825  4.655   46.687 1.00 40.42  ? 317 LEU A O   1 
ATOM   2347 C  CB  . LEU A  1  304 ? 64.556  7.051   49.014 1.00 42.43  ? 317 LEU A CB  1 
ATOM   2348 C  CG  . LEU A  1  304 ? 63.787  7.686   47.854 1.00 44.90  ? 317 LEU A CG  1 
ATOM   2349 C  CD1 . LEU A  1  304 ? 62.413  7.065   47.721 1.00 49.11  ? 317 LEU A CD1 1 
ATOM   2350 C  CD2 . LEU A  1  304 ? 63.655  9.187   48.028 1.00 44.73  ? 317 LEU A CD2 1 
ATOM   2351 N  N   . ARG A  1  305 ? 66.796  5.455   47.459 1.00 39.95  ? 318 ARG A N   1 
ATOM   2352 C  CA  A ARG A  1  305 ? 67.545  5.125   46.259 0.50 38.35  ? 318 ARG A CA  1 
ATOM   2353 C  CA  B ARG A  1  305 ? 67.549  5.125   46.261 0.50 40.71  ? 318 ARG A CA  1 
ATOM   2354 C  C   . ARG A  1  305 ? 67.499  3.615   46.032 1.00 39.16  ? 318 ARG A C   1 
ATOM   2355 O  O   . ARG A  1  305 ? 67.229  3.180   44.923 1.00 38.78  ? 318 ARG A O   1 
ATOM   2356 C  CB  A ARG A  1  305 ? 68.994  5.618   46.346 0.50 36.28  ? 318 ARG A CB  1 
ATOM   2357 C  CB  B ARG A  1  305 ? 69.001  5.613   46.344 0.50 42.14  ? 318 ARG A CB  1 
ATOM   2358 C  CG  A ARG A  1  305 ? 69.879  5.340   45.140 0.50 32.83  ? 318 ARG A CG  1 
ATOM   2359 C  CG  B ARG A  1  305 ? 69.873  5.349   45.122 0.50 41.86  ? 318 ARG A CG  1 
ATOM   2360 C  CD  A ARG A  1  305 ? 71.339  5.724   45.396 0.50 30.45  ? 318 ARG A CD  1 
ATOM   2361 C  CD  B ARG A  1  305 ? 71.323  5.812   45.323 0.50 42.71  ? 318 ARG A CD  1 
ATOM   2362 N  NE  A ARG A  1  305 ? 72.190  5.169   44.341 0.50 27.76  ? 318 ARG A NE  1 
ATOM   2363 N  NE  B ARG A  1  305 ? 72.160  5.636   44.130 0.50 43.86  ? 318 ARG A NE  1 
ATOM   2364 C  CZ  A ARG A  1  305 ? 72.711  3.964   44.367 0.50 23.66  ? 318 ARG A CZ  1 
ATOM   2365 C  CZ  B ARG A  1  305 ? 72.211  6.422   43.045 0.50 42.25  ? 318 ARG A CZ  1 
ATOM   2366 N  NH1 A ARG A  1  305 ? 72.636  3.269   45.481 0.50 22.56  ? 318 ARG A NH1 1 
ATOM   2367 N  NH1 B ARG A  1  305 ? 71.507  7.527   42.930 0.50 40.69  ? 318 ARG A NH1 1 
ATOM   2368 N  NH2 A ARG A  1  305 ? 73.323  3.493   43.300 0.50 21.41  ? 318 ARG A NH2 1 
ATOM   2369 N  NH2 B ARG A  1  305 ? 73.020  6.105   42.063 0.50 46.48  ? 318 ARG A NH2 1 
ATOM   2370 N  N   . ARG A  1  306 ? 67.759  2.830   47.086 1.00 41.10  ? 319 ARG A N   1 
ATOM   2371 C  CA  . ARG A  1  306 ? 67.776  1.378   46.990 1.00 46.56  ? 319 ARG A CA  1 
ATOM   2372 C  C   . ARG A  1  306 ? 66.435  0.862   46.460 1.00 43.36  ? 319 ARG A C   1 
ATOM   2373 O  O   . ARG A  1  306 ? 66.417  0.061   45.519 1.00 42.09  ? 319 ARG A O   1 
ATOM   2374 C  CB  . ARG A  1  306 ? 68.145  0.724   48.330 1.00 51.06  ? 319 ARG A CB  1 
ATOM   2375 C  CG  . ARG A  1  306 ? 68.204  -0.807  48.330 1.00 59.75  ? 319 ARG A CG  1 
ATOM   2376 C  CD  . ARG A  1  306 ? 68.219  -1.410  49.736 1.00 59.42  ? 319 ARG A CD  1 
ATOM   2377 N  NE  . ARG A  1  306 ? 66.923  -1.255  50.408 1.00 65.64  ? 319 ARG A NE  1 
ATOM   2378 C  CZ  . ARG A  1  306 ? 66.673  -1.491  51.696 1.00 69.94  ? 319 ARG A CZ  1 
ATOM   2379 N  NH1 . ARG A  1  306 ? 67.639  -1.923  52.500 1.00 65.62  ? 319 ARG A NH1 1 
ATOM   2380 N  NH2 . ARG A  1  306 ? 65.453  -1.279  52.171 1.00 67.92  ? 319 ARG A NH2 1 
ATOM   2381 N  N   . ASN A  1  307 ? 65.329  1.342   47.048 1.00 37.65  ? 320 ASN A N   1 
ATOM   2382 C  CA  . ASN A  1  307 ? 64.009  0.814   46.732 1.00 39.60  ? 320 ASN A CA  1 
ATOM   2383 C  C   . ASN A  1  307 ? 63.594  1.215   45.317 1.00 40.24  ? 320 ASN A C   1 
ATOM   2384 O  O   . ASN A  1  307 ? 62.975  0.422   44.604 1.00 43.90  ? 320 ASN A O   1 
ATOM   2385 C  CB  . ASN A  1  307 ? 62.998  1.198   47.805 1.00 40.81  ? 320 ASN A CB  1 
ATOM   2386 C  CG  . ASN A  1  307 ? 63.276  0.473   49.101 1.00 41.85  ? 320 ASN A CG  1 
ATOM   2387 O  OD1 . ASN A  1  307 ? 64.278  -0.238  49.216 1.00 44.47  ? 320 ASN A OD1 1 
ATOM   2388 N  ND2 . ASN A  1  307 ? 62.411  0.629   50.083 1.00 43.40  ? 320 ASN A ND2 1 
ATOM   2389 N  N   . LEU A  1  308 ? 63.982  2.430   44.910 1.00 41.52  ? 321 LEU A N   1 
ATOM   2390 C  CA  . LEU A  1  308 ? 63.807  2.874   43.539 1.00 42.08  ? 321 LEU A CA  1 
ATOM   2391 C  C   . LEU A  1  308 ? 64.514  1.938   42.562 1.00 43.34  ? 321 LEU A C   1 
ATOM   2392 O  O   . LEU A  1  308 ? 63.944  1.592   41.532 1.00 39.45  ? 321 LEU A O   1 
ATOM   2393 C  CB  . LEU A  1  308 ? 64.331  4.297   43.373 1.00 45.35  ? 321 LEU A CB  1 
ATOM   2394 C  CG  . LEU A  1  308 ? 63.317  5.424   43.563 1.00 49.07  ? 321 LEU A CG  1 
ATOM   2395 C  CD1 . LEU A  1  308 ? 64.050  6.737   43.680 1.00 50.42  ? 321 LEU A CD1 1 
ATOM   2396 C  CD2 . LEU A  1  308 ? 62.340  5.479   42.385 1.00 52.56  ? 321 LEU A CD2 1 
ATOM   2397 N  N   . ILE A  1  309 ? 65.779  1.593   42.845 1.00 42.90  ? 322 ILE A N   1 
ATOM   2398 C  CA  . ILE A  1  309 ? 66.555  0.750   41.949 1.00 44.11  ? 322 ILE A CA  1 
ATOM   2399 C  C   . ILE A  1  309 ? 65.850  -0.594  41.799 1.00 38.98  ? 322 ILE A C   1 
ATOM   2400 O  O   . ILE A  1  309 ? 65.679  -1.063  40.679 1.00 39.31  ? 322 ILE A O   1 
ATOM   2401 C  CB  . ILE A  1  309 ? 68.016  0.613   42.430 1.00 43.56  ? 322 ILE A CB  1 
ATOM   2402 C  CG1 . ILE A  1  309 ? 68.774  1.934   42.194 1.00 47.66  ? 322 ILE A CG1 1 
ATOM   2403 C  CG2 . ILE A  1  309 ? 68.729  -0.574  41.771 1.00 39.74  ? 322 ILE A CG2 1 
ATOM   2404 C  CD1 . ILE A  1  309 ? 70.139  1.992   42.867 1.00 49.74  ? 322 ILE A CD1 1 
ATOM   2405 N  N   . LYS A  1  310 ? 65.424  -1.180  42.927 1.00 37.91  ? 323 LYS A N   1 
ATOM   2406 C  CA  . LYS A  1  310 ? 64.757  -2.478  42.924 1.00 39.90  ? 323 LYS A CA  1 
ATOM   2407 C  C   . LYS A  1  310 ? 63.446  -2.435  42.136 1.00 37.48  ? 323 LYS A C   1 
ATOM   2408 O  O   . LYS A  1  310 ? 63.241  -3.261  41.250 1.00 40.65  ? 323 LYS A O   1 
ATOM   2409 C  CB  . LYS A  1  310 ? 64.557  -2.982  44.356 1.00 42.28  ? 323 LYS A CB  1 
ATOM   2410 C  CG  . LYS A  1  310 ? 65.838  -3.482  45.003 1.00 47.81  ? 323 LYS A CG  1 
ATOM   2411 C  CD  . LYS A  1  310 ? 65.683  -3.810  46.480 1.00 53.05  ? 323 LYS A CD  1 
ATOM   2412 C  CE  . LYS A  1  310 ? 66.884  -4.483  47.081 1.00 57.94  ? 323 LYS A CE  1 
ATOM   2413 N  NZ  . LYS A  1  310 ? 66.648  -4.661  48.516 1.00 67.08  ? 323 LYS A NZ  1 
ATOM   2414 N  N   . ASN A  1  311 ? 62.587  -1.453  42.445 1.00 38.18  ? 324 ASN A N   1 
ATOM   2415 C  CA  . ASN A  1  311 ? 61.274  -1.344  41.829 1.00 36.92  ? 324 ASN A CA  1 
ATOM   2416 C  C   . ASN A  1  311 ? 61.409  -1.088  40.328 1.00 40.02  ? 324 ASN A C   1 
ATOM   2417 O  O   . ASN A  1  311 ? 60.604  -1.577  39.553 1.00 43.88  ? 324 ASN A O   1 
ATOM   2418 C  CB  . ASN A  1  311 ? 60.417  -0.299  42.531 1.00 36.59  ? 324 ASN A CB  1 
ATOM   2419 C  CG  . ASN A  1  311 ? 59.743  -0.836  43.769 1.00 38.68  ? 324 ASN A CG  1 
ATOM   2420 O  OD1 . ASN A  1  311 ? 58.740  -1.539  43.656 1.00 41.91  ? 324 ASN A OD1 1 
ATOM   2421 N  ND2 . ASN A  1  311 ? 60.239  -0.508  44.954 1.00 40.05  ? 324 ASN A ND2 1 
ATOM   2422 N  N   . LEU A  1  312 ? 62.440  -0.345  39.913 1.00 42.34  ? 325 LEU A N   1 
ATOM   2423 C  CA  . LEU A  1  312 ? 62.681  -0.074  38.504 1.00 42.38  ? 325 LEU A CA  1 
ATOM   2424 C  C   . LEU A  1  312 ? 63.065  -1.363  37.795 1.00 41.14  ? 325 LEU A C   1 
ATOM   2425 O  O   . LEU A  1  312 ? 62.589  -1.607  36.697 1.00 43.39  ? 325 LEU A O   1 
ATOM   2426 C  CB  . LEU A  1  312 ? 63.759  0.989   38.300 1.00 44.71  ? 325 LEU A CB  1 
ATOM   2427 C  CG  . LEU A  1  312 ? 63.309  2.435   38.499 1.00 45.16  ? 325 LEU A CG  1 
ATOM   2428 C  CD1 . LEU A  1  312 ? 64.514  3.344   38.693 1.00 50.43  ? 325 LEU A CD1 1 
ATOM   2429 C  CD2 . LEU A  1  312 ? 62.488  2.906   37.326 1.00 41.89  ? 325 LEU A CD2 1 
ATOM   2430 N  N   . HIS A  1  313 ? 63.925  -2.169  38.421 1.00 42.20  ? 326 HIS A N   1 
ATOM   2431 C  CA  . HIS A  1  313 ? 64.313  -3.453  37.859 1.00 43.15  ? 326 HIS A CA  1 
ATOM   2432 C  C   . HIS A  1  313 ? 63.094  -4.381  37.788 1.00 38.26  ? 326 HIS A C   1 
ATOM   2433 O  O   . HIS A  1  313 ? 62.859  -5.018  36.771 1.00 35.93  ? 326 HIS A O   1 
ATOM   2434 C  CB  . HIS A  1  313 ? 65.500  -4.040  38.636 1.00 42.19  ? 326 HIS A CB  1 
ATOM   2435 C  CG  . HIS A  1  313 ? 65.957  -5.329  38.053 1.00 44.51  ? 326 HIS A CG  1 
ATOM   2436 N  ND1 . HIS A  1  313 ? 66.526  -5.392  36.800 1.00 41.59  ? 326 HIS A ND1 1 
ATOM   2437 C  CD2 . HIS A  1  313 ? 65.835  -6.594  38.486 1.00 45.68  ? 326 HIS A CD2 1 
ATOM   2438 C  CE1 . HIS A  1  313 ? 66.789  -6.660  36.519 1.00 45.50  ? 326 HIS A CE1 1 
ATOM   2439 N  NE2 . HIS A  1  313 ? 66.362  -7.405  37.517 1.00 46.52  ? 326 HIS A NE2 1 
ATOM   2440 N  N   . TYR A  1  314 ? 62.309  -4.432  38.863 1.00 38.27  ? 327 TYR A N   1 
ATOM   2441 C  CA  . TYR A  1  314 ? 61.096  -5.241  38.909 1.00 40.16  ? 327 TYR A CA  1 
ATOM   2442 C  C   . TYR A  1  314 ? 60.166  -4.891  37.746 1.00 42.40  ? 327 TYR A C   1 
ATOM   2443 O  O   . TYR A  1  314 ? 59.664  -5.792  37.075 1.00 41.82  ? 327 TYR A O   1 
ATOM   2444 C  CB  . TYR A  1  314 ? 60.335  -5.094  40.235 1.00 38.20  ? 327 TYR A CB  1 
ATOM   2445 C  CG  . TYR A  1  314 ? 61.099  -5.557  41.467 1.00 36.30  ? 327 TYR A CG  1 
ATOM   2446 C  CD1 . TYR A  1  314 ? 62.192  -6.412  41.374 1.00 36.81  ? 327 TYR A CD1 1 
ATOM   2447 C  CD2 . TYR A  1  314 ? 60.708  -5.144  42.736 1.00 37.54  ? 327 TYR A CD2 1 
ATOM   2448 C  CE1 . TYR A  1  314 ? 62.875  -6.841  42.504 1.00 35.36  ? 327 TYR A CE1 1 
ATOM   2449 C  CE2 . TYR A  1  314 ? 61.387  -5.549  43.871 1.00 40.16  ? 327 TYR A CE2 1 
ATOM   2450 C  CZ  . TYR A  1  314 ? 62.475  -6.398  43.755 1.00 39.49  ? 327 TYR A CZ  1 
ATOM   2451 O  OH  . TYR A  1  314 ? 63.078  -6.744  44.934 1.00 38.98  ? 327 TYR A OH  1 
ATOM   2452 N  N   . TRP A  1  315 ? 59.964  -3.590  37.492 1.00 41.46  ? 328 TRP A N   1 
ATOM   2453 C  CA  . TRP A  1  315 ? 59.107  -3.151  36.404 1.00 37.94  ? 328 TRP A CA  1 
ATOM   2454 C  C   . TRP A  1  315 ? 59.683  -3.590  35.060 1.00 40.15  ? 328 TRP A C   1 
ATOM   2455 O  O   . TRP A  1  315 ? 58.924  -4.062  34.214 1.00 39.50  ? 328 TRP A O   1 
ATOM   2456 C  CB  . TRP A  1  315 ? 58.866  -1.633  36.461 1.00 37.77  ? 328 TRP A CB  1 
ATOM   2457 C  CG  . TRP A  1  315 ? 57.802  -1.116  35.517 1.00 37.50  ? 328 TRP A CG  1 
ATOM   2458 C  CD1 . TRP A  1  315 ? 56.517  -1.566  35.336 1.00 36.84  ? 328 TRP A CD1 1 
ATOM   2459 C  CD2 . TRP A  1  315 ? 57.978  -0.037  34.567 1.00 39.12  ? 328 TRP A CD2 1 
ATOM   2460 N  NE1 . TRP A  1  315 ? 55.888  -0.835  34.355 1.00 39.44  ? 328 TRP A NE1 1 
ATOM   2461 C  CE2 . TRP A  1  315 ? 56.757  0.111   33.866 1.00 43.64  ? 328 TRP A CE2 1 
ATOM   2462 C  CE3 . TRP A  1  315 ? 59.037  0.809   34.250 1.00 38.51  ? 328 TRP A CE3 1 
ATOM   2463 C  CZ2 . TRP A  1  315 ? 56.587  1.070   32.870 1.00 42.82  ? 328 TRP A CZ2 1 
ATOM   2464 C  CZ3 . TRP A  1  315 ? 58.865  1.760   33.274 1.00 43.10  ? 328 TRP A CZ3 1 
ATOM   2465 C  CH2 . TRP A  1  315 ? 57.668  1.871   32.579 1.00 46.69  ? 328 TRP A CH2 1 
ATOM   2466 N  N   . TRP A  1  316 ? 61.011  -3.472  34.880 1.00 42.28  ? 329 TRP A N   1 
ATOM   2467 C  CA  . TRP A  1  316 ? 61.665  -3.855  33.632 1.00 42.54  ? 329 TRP A CA  1 
ATOM   2468 C  C   . TRP A  1  316 ? 61.440  -5.336  33.318 1.00 40.76  ? 329 TRP A C   1 
ATOM   2469 O  O   . TRP A  1  316 ? 61.221  -5.688  32.161 1.00 43.14  ? 329 TRP A O   1 
ATOM   2470 C  CB  . TRP A  1  316 ? 63.171  -3.523  33.645 1.00 44.49  ? 329 TRP A CB  1 
ATOM   2471 C  CG  . TRP A  1  316 ? 63.831  -3.921  32.356 1.00 42.43  ? 329 TRP A CG  1 
ATOM   2472 C  CD1 . TRP A  1  316 ? 63.792  -3.237  31.178 1.00 47.28  ? 329 TRP A CD1 1 
ATOM   2473 C  CD2 . TRP A  1  316 ? 64.534  -5.143  32.085 1.00 40.40  ? 329 TRP A CD2 1 
ATOM   2474 N  NE1 . TRP A  1  316 ? 64.450  -3.928  30.200 1.00 48.11  ? 329 TRP A NE1 1 
ATOM   2475 C  CE2 . TRP A  1  316 ? 64.910  -5.100  30.728 1.00 40.94  ? 329 TRP A CE2 1 
ATOM   2476 C  CE3 . TRP A  1  316 ? 64.881  -6.260  32.849 1.00 45.03  ? 329 TRP A CE3 1 
ATOM   2477 C  CZ2 . TRP A  1  316 ? 65.624  -6.125  30.122 1.00 45.62  ? 329 TRP A CZ2 1 
ATOM   2478 C  CZ3 . TRP A  1  316 ? 65.584  -7.284  32.240 1.00 43.67  ? 329 TRP A CZ3 1 
ATOM   2479 C  CH2 . TRP A  1  316 ? 65.932  -7.222  30.892 1.00 42.02  ? 329 TRP A CH2 1 
ATOM   2480 N  N   . THR A  1  317 ? 61.468  -6.197  34.347 1.00 44.24  ? 330 THR A N   1 
ATOM   2481 C  CA  . THR A  1  317 ? 61.308  -7.634  34.140 1.00 47.03  ? 330 THR A CA  1 
ATOM   2482 C  C   . THR A  1  317 ? 59.975  -7.911  33.442 1.00 46.61  ? 330 THR A C   1 
ATOM   2483 O  O   . THR A  1  317 ? 59.922  -8.760  32.564 1.00 49.67  ? 330 THR A O   1 
ATOM   2484 C  CB  . THR A  1  317 ? 61.401  -8.455  35.432 1.00 43.67  ? 330 THR A CB  1 
ATOM   2485 O  OG1 . THR A  1  317 ? 60.323  -8.101  36.292 1.00 45.84  ? 330 THR A OG1 1 
ATOM   2486 C  CG2 . THR A  1  317 ? 62.731  -8.297  36.146 1.00 46.44  ? 330 THR A CG2 1 
ATOM   2487 N  N   . GLY A  1  318 ? 58.907  -7.200  33.833 1.00 42.77  ? 331 GLY A N   1 
ATOM   2488 C  CA  . GLY A  1  318 ? 57.620  -7.332  33.177 1.00 41.12  ? 331 GLY A CA  1 
ATOM   2489 C  C   . GLY A  1  318 ? 57.599  -6.682  31.789 1.00 42.32  ? 331 GLY A C   1 
ATOM   2490 O  O   . GLY A  1  318 ? 57.093  -7.251  30.827 1.00 40.87  ? 331 GLY A O   1 
ATOM   2491 N  N   . VAL A  1  319 ? 58.122  -5.461  31.701 1.00 42.90  ? 332 VAL A N   1 
ATOM   2492 C  CA  . VAL A  1  319 ? 58.081  -4.688  30.471 1.00 43.16  ? 332 VAL A CA  1 
ATOM   2493 C  C   . VAL A  1  319 ? 58.855  -5.418  29.372 1.00 46.57  ? 332 VAL A C   1 
ATOM   2494 O  O   . VAL A  1  319 ? 58.426  -5.451  28.217 1.00 45.43  ? 332 VAL A O   1 
ATOM   2495 C  CB  . VAL A  1  319 ? 58.647  -3.281  30.746 1.00 46.40  ? 332 VAL A CB  1 
ATOM   2496 C  CG1 . VAL A  1  319 ? 58.901  -2.488  29.486 1.00 47.87  ? 332 VAL A CG1 1 
ATOM   2497 C  CG2 . VAL A  1  319 ? 57.726  -2.486  31.651 1.00 49.09  ? 332 VAL A CG2 1 
ATOM   2498 N  N   . ASN A  1  320 ? 59.992  -6.017  29.749 1.00 49.96  ? 333 ASN A N   1 
ATOM   2499 C  CA  . ASN A  1  320 ? 60.882  -6.662  28.789 1.00 51.08  ? 333 ASN A CA  1 
ATOM   2500 C  C   . ASN A  1  320 ? 60.116  -7.722  27.997 1.00 48.49  ? 333 ASN A C   1 
ATOM   2501 O  O   . ASN A  1  320 ? 60.231  -7.784  26.779 1.00 47.51  ? 333 ASN A O   1 
ATOM   2502 C  CB  . ASN A  1  320 ? 62.118  -7.224  29.486 1.00 49.54  ? 333 ASN A CB  1 
ATOM   2503 C  CG  . ASN A  1  320 ? 63.164  -7.709  28.513 1.00 51.88  ? 333 ASN A CG  1 
ATOM   2504 O  OD1 . ASN A  1  320 ? 63.578  -6.965  27.620 1.00 52.77  ? 333 ASN A OD1 1 
ATOM   2505 N  ND2 . ASN A  1  320 ? 63.631  -8.935  28.681 1.00 49.49  ? 333 ASN A ND2 1 
ATOM   2506 N  N   . VAL A  1  321 ? 59.321  -8.536  28.701 1.00 48.95  ? 334 VAL A N   1 
ATOM   2507 C  CA  . VAL A  1  321 ? 58.555  -9.607  28.091 1.00 51.40  ? 334 VAL A CA  1 
ATOM   2508 C  C   . VAL A  1  321 ? 57.359  -9.017  27.349 1.00 51.89  ? 334 VAL A C   1 
ATOM   2509 O  O   . VAL A  1  321 ? 57.081  -9.418  26.223 1.00 52.82  ? 334 VAL A O   1 
ATOM   2510 C  CB  . VAL A  1  321 ? 58.106  -10.652 29.132 1.00 56.14  ? 334 VAL A CB  1 
ATOM   2511 C  CG1 . VAL A  1  321 ? 57.262  -11.766 28.512 1.00 57.44  ? 334 VAL A CG1 1 
ATOM   2512 C  CG2 . VAL A  1  321 ? 59.297  -11.239 29.878 1.00 54.41  ? 334 VAL A CG2 1 
ATOM   2513 N  N   . ALA A  1  322 ? 56.676  -8.046  27.970 1.00 49.87  ? 335 ALA A N   1 
ATOM   2514 C  CA  . ALA A  1  322 ? 55.409  -7.539  27.461 1.00 47.32  ? 335 ALA A CA  1 
ATOM   2515 C  C   . ALA A  1  322 ? 55.599  -6.713  26.189 1.00 51.78  ? 335 ALA A C   1 
ATOM   2516 O  O   . ALA A  1  322 ? 54.717  -6.724  25.336 1.00 49.97  ? 335 ALA A O   1 
ATOM   2517 C  CB  . ALA A  1  322 ? 54.702  -6.725  28.522 1.00 44.96  ? 335 ALA A CB  1 
ATOM   2518 N  N   . PHE A  1  323 ? 56.723  -5.983  26.074 1.00 53.93  ? 336 PHE A N   1 
ATOM   2519 C  CA  . PHE A  1  323 ? 56.969  -5.129  24.921 1.00 51.91  ? 336 PHE A CA  1 
ATOM   2520 C  C   . PHE A  1  323 ? 57.901  -5.815  23.916 1.00 51.89  ? 336 PHE A C   1 
ATOM   2521 O  O   . PHE A  1  323 ? 58.209  -5.226  22.887 1.00 54.93  ? 336 PHE A O   1 
ATOM   2522 C  CB  . PHE A  1  323 ? 57.507  -3.779  25.412 1.00 54.33  ? 336 PHE A CB  1 
ATOM   2523 C  CG  . PHE A  1  323 ? 56.579  -2.975  26.317 1.00 54.27  ? 336 PHE A CG  1 
ATOM   2524 C  CD1 . PHE A  1  323 ? 55.281  -3.403  26.593 1.00 57.37  ? 336 PHE A CD1 1 
ATOM   2525 C  CD2 . PHE A  1  323 ? 56.987  -1.764  26.863 1.00 52.91  ? 336 PHE A CD2 1 
ATOM   2526 C  CE1 . PHE A  1  323 ? 54.437  -2.669  27.412 1.00 52.24  ? 336 PHE A CE1 1 
ATOM   2527 C  CE2 . PHE A  1  323 ? 56.129  -1.025  27.673 1.00 54.66  ? 336 PHE A CE2 1 
ATOM   2528 C  CZ  . PHE A  1  323 ? 54.859  -1.481  27.947 1.00 53.23  ? 336 PHE A CZ  1 
ATOM   2529 N  N   . GLY A  1  324 ? 58.344  -7.047  24.206 1.00 53.05  ? 337 GLY A N   1 
ATOM   2530 C  CA  . GLY A  1  324 ? 59.170  -7.825  23.293 1.00 54.24  ? 337 GLY A CA  1 
ATOM   2531 C  C   . GLY A  1  324 ? 60.619  -7.335  23.225 1.00 58.11  ? 337 GLY A C   1 
ATOM   2532 O  O   . GLY A  1  324 ? 61.222  -7.366  22.154 1.00 61.06  ? 337 GLY A O   1 
ATOM   2533 N  N   . GLY A  1  325 ? 61.180  -6.925  24.375 1.00 57.87  ? 338 GLY A N   1 
ATOM   2534 C  CA  . GLY A  1  325 ? 62.578  -6.523  24.478 1.00 50.33  ? 338 GLY A CA  1 
ATOM   2535 C  C   . GLY A  1  325 ? 62.738  -5.004  24.503 1.00 52.54  ? 338 GLY A C   1 
ATOM   2536 O  O   . GLY A  1  325 ? 62.479  -4.335  23.505 1.00 47.28  ? 338 GLY A O   1 
ATOM   2537 N  N   . CYS A  1  326 ? 63.137  -4.475  25.670 1.00 53.89  ? 339 CYS A N   1 
ATOM   2538 C  CA  . CYS A  1  326 ? 63.552  -3.087  25.823 1.00 53.43  ? 339 CYS A CA  1 
ATOM   2539 C  C   . CYS A  1  326 ? 64.861  -3.102  26.606 1.00 50.63  ? 339 CYS A C   1 
ATOM   2540 O  O   . CYS A  1  326 ? 64.993  -3.884  27.545 1.00 52.27  ? 339 CYS A O   1 
ATOM   2541 C  CB  . CYS A  1  326 ? 62.497  -2.245  26.547 1.00 57.35  ? 339 CYS A CB  1 
ATOM   2542 S  SG  . CYS A  1  326 ? 60.873  -2.199  25.731 1.00 70.59  ? 339 CYS A SG  1 
ATOM   2543 N  N   . ASP A  1  327 ? 65.830  -2.267  26.206 1.00 52.28  ? 340 ASP A N   1 
ATOM   2544 C  CA  . ASP A  1  327 ? 67.080  -2.161  26.939 1.00 51.85  ? 340 ASP A CA  1 
ATOM   2545 C  C   . ASP A  1  327 ? 66.810  -1.480  28.278 1.00 47.96  ? 340 ASP A C   1 
ATOM   2546 O  O   . ASP A  1  327 ? 66.227  -0.391  28.314 1.00 49.33  ? 340 ASP A O   1 
ATOM   2547 C  CB  . ASP A  1  327 ? 68.131  -1.397  26.154 1.00 54.94  ? 340 ASP A CB  1 
ATOM   2548 C  CG  . ASP A  1  327 ? 68.522  -1.989  24.810 1.00 59.43  ? 340 ASP A CG  1 
ATOM   2549 O  OD1 . ASP A  1  327 ? 68.423  -3.224  24.629 1.00 59.85  ? 340 ASP A OD1 1 
ATOM   2550 O  OD2 . ASP A  1  327 ? 68.903  -1.190  23.952 1.00 58.10  ? 340 ASP A OD2 1 
ATOM   2551 N  N   . GLU A  1  328 ? 67.235  -2.135  29.371 1.00 45.97  ? 341 GLU A N   1 
ATOM   2552 C  CA  . GLU A  1  328 ? 67.047  -1.615  30.718 1.00 47.97  ? 341 GLU A CA  1 
ATOM   2553 C  C   . GLU A  1  328 ? 67.872  -0.339  30.908 1.00 47.70  ? 341 GLU A C   1 
ATOM   2554 O  O   . GLU A  1  328 ? 69.014  -0.277  30.475 1.00 46.95  ? 341 GLU A O   1 
ATOM   2555 C  CB  . GLU A  1  328 ? 67.412  -2.682  31.749 1.00 45.33  ? 341 GLU A CB  1 
ATOM   2556 C  CG  . GLU A  1  328 ? 67.046  -2.308  33.185 1.00 48.29  ? 341 GLU A CG  1 
ATOM   2557 C  CD  . GLU A  1  328 ? 67.313  -3.349  34.261 1.00 46.95  ? 341 GLU A CD  1 
ATOM   2558 O  OE1 . GLU A  1  328 ? 67.840  -4.431  33.926 1.00 49.47  ? 341 GLU A OE1 1 
ATOM   2559 O  OE2 . GLU A  1  328 ? 66.987  -3.090  35.449 1.00 49.88  ? 341 GLU A OE2 1 
ATOM   2560 N  N   . LEU A  1  329 ? 67.257  0.674   31.536 1.00 48.29  ? 342 LEU A N   1 
ATOM   2561 C  CA  . LEU A  1  329 ? 67.914  1.922   31.889 1.00 47.23  ? 342 LEU A CA  1 
ATOM   2562 C  C   . LEU A  1  329 ? 68.235  1.891   33.382 1.00 45.35  ? 342 LEU A C   1 
ATOM   2563 O  O   . LEU A  1  329 ? 67.521  1.239   34.153 1.00 44.03  ? 342 LEU A O   1 
ATOM   2564 C  CB  . LEU A  1  329 ? 67.023  3.110   31.517 1.00 47.57  ? 342 LEU A CB  1 
ATOM   2565 C  CG  . LEU A  1  329 ? 66.705  3.290   30.026 1.00 47.47  ? 342 LEU A CG  1 
ATOM   2566 C  CD1 . LEU A  1  329 ? 65.596  4.308   29.843 1.00 47.15  ? 342 LEU A CD1 1 
ATOM   2567 C  CD2 . LEU A  1  329 ? 67.917  3.703   29.222 1.00 46.06  ? 342 LEU A CD2 1 
ATOM   2568 N  N   . PHE A  1  330 ? 69.319  2.590   33.763 1.00 47.34  ? 343 PHE A N   1 
ATOM   2569 C  CA  . PHE A  1  330 ? 69.820  2.627   35.132 1.00 46.76  ? 343 PHE A CA  1 
ATOM   2570 C  C   . PHE A  1  330 ? 70.034  4.072   35.574 1.00 48.03  ? 343 PHE A C   1 
ATOM   2571 O  O   . PHE A  1  330 ? 71.158  4.482   35.845 1.00 53.84  ? 343 PHE A O   1 
ATOM   2572 C  CB  . PHE A  1  330 ? 71.135  1.851   35.231 1.00 48.29  ? 343 PHE A CB  1 
ATOM   2573 C  CG  . PHE A  1  330 ? 70.989  0.401   34.795 1.00 50.29  ? 343 PHE A CG  1 
ATOM   2574 C  CD1 . PHE A  1  330 ? 70.418  -0.547  35.644 1.00 52.68  ? 343 PHE A CD1 1 
ATOM   2575 C  CD2 . PHE A  1  330 ? 71.389  -0.004  33.529 1.00 50.74  ? 343 PHE A CD2 1 
ATOM   2576 C  CE1 . PHE A  1  330 ? 70.250  -1.861  35.236 1.00 52.38  ? 343 PHE A CE1 1 
ATOM   2577 C  CE2 . PHE A  1  330 ? 71.241  -1.331  33.133 1.00 49.76  ? 343 PHE A CE2 1 
ATOM   2578 C  CZ  . PHE A  1  330 ? 70.660  -2.251  33.983 1.00 48.61  ? 343 PHE A CZ  1 
ATOM   2579 N  N   . PRO A  1  331 ? 68.961  4.881   35.723 1.00 47.42  ? 344 PRO A N   1 
ATOM   2580 C  CA  . PRO A  1  331 ? 69.115  6.292   36.080 1.00 44.35  ? 344 PRO A CA  1 
ATOM   2581 C  C   . PRO A  1  331 ? 69.763  6.564   37.437 1.00 42.33  ? 344 PRO A C   1 
ATOM   2582 O  O   . PRO A  1  331 ? 70.284  7.658   37.639 1.00 46.78  ? 344 PRO A O   1 
ATOM   2583 C  CB  . PRO A  1  331 ? 67.650  6.783   36.011 1.00 45.38  ? 344 PRO A CB  1 
ATOM   2584 C  CG  . PRO A  1  331 ? 66.855  5.549   36.389 1.00 44.83  ? 344 PRO A CG  1 
ATOM   2585 C  CD  . PRO A  1  331 ? 67.550  4.479   35.589 1.00 44.01  ? 344 PRO A CD  1 
ATOM   2586 N  N   . TYR A  1  332 ? 69.724  5.590   38.359 1.00 40.74  ? 345 TYR A N   1 
ATOM   2587 C  CA  . TYR A  1  332 ? 70.350  5.737   39.670 1.00 41.75  ? 345 TYR A CA  1 
ATOM   2588 C  C   . TYR A  1  332 ? 71.483  4.720   39.833 1.00 41.46  ? 345 TYR A C   1 
ATOM   2589 O  O   . TYR A  1  332 ? 71.883  4.389   40.953 1.00 40.14  ? 345 TYR A O   1 
ATOM   2590 C  CB  . TYR A  1  332 ? 69.321  5.615   40.799 1.00 41.07  ? 345 TYR A CB  1 
ATOM   2591 C  CG  . TYR A  1  332 ? 68.106  6.503   40.578 1.00 46.36  ? 345 TYR A CG  1 
ATOM   2592 C  CD1 . TYR A  1  332 ? 68.197  7.895   40.659 1.00 44.63  ? 345 TYR A CD1 1 
ATOM   2593 C  CD2 . TYR A  1  332 ? 66.870  5.948   40.265 1.00 47.97  ? 345 TYR A CD2 1 
ATOM   2594 C  CE1 . TYR A  1  332 ? 67.098  8.699   40.408 1.00 49.81  ? 345 TYR A CE1 1 
ATOM   2595 C  CE2 . TYR A  1  332 ? 65.758  6.745   40.038 1.00 50.73  ? 345 TYR A CE2 1 
ATOM   2596 C  CZ  . TYR A  1  332 ? 65.875  8.124   40.101 1.00 48.48  ? 345 TYR A CZ  1 
ATOM   2597 O  OH  . TYR A  1  332 ? 64.818  8.949   39.892 1.00 44.66  ? 345 TYR A OH  1 
ATOM   2598 N  N   . GLY A  1  333 ? 71.997  4.231   38.700 1.00 40.62  ? 346 GLY A N   1 
ATOM   2599 C  CA  . GLY A  1  333 ? 73.025  3.208   38.703 1.00 42.29  ? 346 GLY A CA  1 
ATOM   2600 C  C   . GLY A  1  333 ? 72.519  1.885   39.280 1.00 49.00  ? 346 GLY A C   1 
ATOM   2601 O  O   . GLY A  1  333 ? 71.358  1.514   39.096 1.00 51.84  ? 346 GLY A O   1 
ATOM   2602 N  N   . GLN A  1  334 ? 73.412  1.191   39.998 1.00 49.55  ? 347 GLN A N   1 
ATOM   2603 C  CA  . GLN A  1  334 ? 73.155  -0.138  40.528 1.00 56.65  ? 347 GLN A CA  1 
ATOM   2604 C  C   . GLN A  1  334 ? 73.387  -0.155  42.034 1.00 53.22  ? 347 GLN A C   1 
ATOM   2605 O  O   . GLN A  1  334 ? 73.879  0.824   42.591 1.00 50.42  ? 347 GLN A O   1 
ATOM   2606 C  CB  . GLN A  1  334 ? 74.086  -1.115  39.821 1.00 65.66  ? 347 GLN A CB  1 
ATOM   2607 C  CG  . GLN A  1  334 ? 73.727  -1.316  38.351 1.00 80.23  ? 347 GLN A CG  1 
ATOM   2608 C  CD  . GLN A  1  334 ? 74.689  -2.223  37.620 1.00 95.98  ? 347 GLN A CD  1 
ATOM   2609 O  OE1 . GLN A  1  334 ? 75.808  -2.484  38.079 1.00 118.55 ? 347 GLN A OE1 1 
ATOM   2610 N  NE2 . GLN A  1  334 ? 74.261  -2.704  36.463 1.00 93.61  ? 347 GLN A NE2 1 
ATOM   2611 N  N   . LEU A  1  335 ? 73.018  -1.272  42.675 1.00 50.86  ? 348 LEU A N   1 
ATOM   2612 C  CA  . LEU A  1  335 ? 73.096  -1.408  44.122 1.00 58.72  ? 348 LEU A CA  1 
ATOM   2613 C  C   . LEU A  1  335 ? 74.561  -1.511  44.593 1.00 61.57  ? 348 LEU A C   1 
ATOM   2614 O  O   . LEU A  1  335 ? 75.294  -2.300  43.962 1.00 69.13  ? 348 LEU A O   1 
ATOM   2615 C  CB  . LEU A  1  335 ? 72.291  -2.631  44.558 1.00 55.27  ? 348 LEU A CB  1 
ATOM   2616 C  CG  . LEU A  1  335 ? 70.769  -2.482  44.497 1.00 62.91  ? 348 LEU A CG  1 
ATOM   2617 C  CD1 . LEU A  1  335 ? 70.070  -3.763  44.922 1.00 61.33  ? 348 LEU A CD1 1 
ATOM   2618 C  CD2 . LEU A  1  335 ? 70.282  -1.309  45.352 1.00 61.54  ? 348 LEU A CD2 1 
ATOM   2619 N  N   . GLN B  1  1   ? -0.359  19.277  56.698 1.00 104.85 ? 14  GLN B N   1 
ATOM   2620 C  CA  . GLN B  1  1   ? 0.102   18.734  58.007 1.00 112.25 ? 14  GLN B CA  1 
ATOM   2621 C  C   . GLN B  1  1   ? -0.486  17.342  58.241 1.00 109.73 ? 14  GLN B C   1 
ATOM   2622 O  O   . GLN B  1  1   ? 0.231   16.343  58.179 1.00 103.30 ? 14  GLN B O   1 
ATOM   2623 C  CB  . GLN B  1  1   ? -0.288  19.685  59.139 1.00 114.24 ? 14  GLN B CB  1 
ATOM   2624 C  CG  . GLN B  1  1   ? 0.476   21.003  59.131 1.00 117.77 ? 14  GLN B CG  1 
ATOM   2625 C  CD  . GLN B  1  1   ? 0.019   21.939  60.227 1.00 125.02 ? 14  GLN B CD  1 
ATOM   2626 O  OE1 . GLN B  1  1   ? -1.115  21.848  60.713 1.00 127.83 ? 14  GLN B OE1 1 
ATOM   2627 N  NE2 . GLN B  1  1   ? 0.894   22.854  60.624 1.00 127.28 ? 14  GLN B NE2 1 
ATOM   2628 N  N   . GLY B  1  2   ? -1.801  17.292  58.501 1.00 101.13 ? 15  GLY B N   1 
ATOM   2629 C  CA  . GLY B  1  2   ? -2.521  16.038  58.630 1.00 85.27  ? 15  GLY B CA  1 
ATOM   2630 C  C   . GLY B  1  2   ? -2.876  15.480  57.257 1.00 74.84  ? 15  GLY B C   1 
ATOM   2631 O  O   . GLY B  1  2   ? -3.060  16.230  56.310 1.00 75.30  ? 15  GLY B O   1 
ATOM   2632 N  N   . VAL B  1  3   ? -2.995  14.158  57.180 1.00 68.70  ? 16  VAL B N   1 
ATOM   2633 C  CA  . VAL B  1  3   ? -3.306  13.468  55.945 1.00 65.97  ? 16  VAL B CA  1 
ATOM   2634 C  C   . VAL B  1  3   ? -4.581  12.680  56.202 1.00 58.51  ? 16  VAL B C   1 
ATOM   2635 O  O   . VAL B  1  3   ? -4.850  12.287  57.338 1.00 50.43  ? 16  VAL B O   1 
ATOM   2636 C  CB  . VAL B  1  3   ? -2.122  12.554  55.561 1.00 69.95  ? 16  VAL B CB  1 
ATOM   2637 C  CG1 . VAL B  1  3   ? -2.433  11.634  54.390 1.00 70.52  ? 16  VAL B CG1 1 
ATOM   2638 C  CG2 . VAL B  1  3   ? -0.851  13.353  55.289 1.00 74.10  ? 16  VAL B CG2 1 
ATOM   2639 N  N   . ASP B  1  4   ? -5.359  12.472  55.139 1.00 63.15  ? 17  ASP B N   1 
ATOM   2640 C  CA  . ASP B  1  4   ? -6.483  11.559  55.183 1.00 69.61  ? 17  ASP B CA  1 
ATOM   2641 C  C   . ASP B  1  4   ? -6.005  10.190  54.686 1.00 70.39  ? 17  ASP B C   1 
ATOM   2642 O  O   . ASP B  1  4   ? -5.631  10.051  53.527 1.00 75.48  ? 17  ASP B O   1 
ATOM   2643 C  CB  . ASP B  1  4   ? -7.648  12.157  54.419 1.00 75.30  ? 17  ASP B CB  1 
ATOM   2644 C  CG  . ASP B  1  4   ? -8.986  11.480  54.638 1.00 86.85  ? 17  ASP B CG  1 
ATOM   2645 O  OD1 . ASP B  1  4   ? -9.029  10.220  54.630 1.00 95.47  ? 17  ASP B OD1 1 
ATOM   2646 O  OD2 . ASP B  1  4   ? -9.977  12.223  54.792 1.00 97.84  ? 17  ASP B OD2 1 
ATOM   2647 N  N   . PRO B  1  5   ? -5.979  9.139   55.541 1.00 72.56  ? 18  PRO B N   1 
ATOM   2648 C  CA  . PRO B  1  5   ? -5.399  7.844   55.179 1.00 66.28  ? 18  PRO B CA  1 
ATOM   2649 C  C   . PRO B  1  5   ? -6.238  7.042   54.188 1.00 58.17  ? 18  PRO B C   1 
ATOM   2650 O  O   . PRO B  1  5   ? -7.403  6.745   54.455 1.00 58.29  ? 18  PRO B O   1 
ATOM   2651 C  CB  . PRO B  1  5   ? -5.275  7.091   56.525 1.00 69.35  ? 18  PRO B CB  1 
ATOM   2652 C  CG  . PRO B  1  5   ? -5.537  8.122   57.572 1.00 69.68  ? 18  PRO B CG  1 
ATOM   2653 C  CD  . PRO B  1  5   ? -6.464  9.142   56.927 1.00 72.19  ? 18  PRO B CD  1 
ATOM   2654 N  N   . PRO B  1  6   ? -5.648  6.611   53.048 1.00 56.57  ? 19  PRO B N   1 
ATOM   2655 C  CA  . PRO B  1  6   ? -6.349  5.795   52.057 1.00 53.18  ? 19  PRO B CA  1 
ATOM   2656 C  C   . PRO B  1  6   ? -6.624  4.408   52.618 1.00 51.76  ? 19  PRO B C   1 
ATOM   2657 O  O   . PRO B  1  6   ? -5.897  3.932   53.473 1.00 51.67  ? 19  PRO B O   1 
ATOM   2658 C  CB  . PRO B  1  6   ? -5.389  5.709   50.850 1.00 53.18  ? 19  PRO B CB  1 
ATOM   2659 C  CG  . PRO B  1  6   ? -4.301  6.704   51.160 1.00 56.66  ? 19  PRO B CG  1 
ATOM   2660 C  CD  . PRO B  1  6   ? -4.249  6.856   52.663 1.00 58.22  ? 19  PRO B CD  1 
ATOM   2661 N  N   . PRO B  1  7   ? -7.655  3.695   52.132 1.00 54.32  ? 20  PRO B N   1 
ATOM   2662 C  CA  . PRO B  1  7   ? -7.842  2.299   52.508 1.00 56.04  ? 20  PRO B CA  1 
ATOM   2663 C  C   . PRO B  1  7   ? -6.638  1.475   52.046 1.00 57.29  ? 20  PRO B C   1 
ATOM   2664 O  O   . PRO B  1  7   ? -5.847  1.910   51.212 1.00 53.55  ? 20  PRO B O   1 
ATOM   2665 C  CB  . PRO B  1  7   ? -9.164  1.909   51.803 1.00 55.12  ? 20  PRO B CB  1 
ATOM   2666 C  CG  . PRO B  1  7   ? -9.276  2.889   50.648 1.00 56.13  ? 20  PRO B CG  1 
ATOM   2667 C  CD  . PRO B  1  7   ? -8.670  4.180   51.185 1.00 57.56  ? 20  PRO B CD  1 
ATOM   2668 N  N   . PRO B  1  8   ? -6.435  0.268   52.606 1.00 57.07  ? 21  PRO B N   1 
ATOM   2669 C  CA  . PRO B  1  8   ? -5.343  -0.601  52.165 1.00 53.67  ? 21  PRO B CA  1 
ATOM   2670 C  C   . PRO B  1  8   ? -5.469  -0.977  50.688 1.00 48.72  ? 21  PRO B C   1 
ATOM   2671 O  O   . PRO B  1  8   ? -6.558  -1.249  50.197 1.00 49.79  ? 21  PRO B O   1 
ATOM   2672 C  CB  . PRO B  1  8   ? -5.452  -1.815  53.097 1.00 54.88  ? 21  PRO B CB  1 
ATOM   2673 C  CG  . PRO B  1  8   ? -6.868  -1.771  53.633 1.00 59.42  ? 21  PRO B CG  1 
ATOM   2674 C  CD  . PRO B  1  8   ? -7.221  -0.296  53.712 1.00 58.69  ? 21  PRO B CD  1 
ATOM   2675 N  N   . PRO B  1  9   ? -4.357  -1.024  49.924 1.00 44.98  ? 22  PRO B N   1 
ATOM   2676 C  CA  . PRO B  1  9   ? -4.363  -1.584  48.572 1.00 43.27  ? 22  PRO B CA  1 
ATOM   2677 C  C   . PRO B  1  9   ? -4.824  -3.036  48.590 1.00 41.21  ? 22  PRO B C   1 
ATOM   2678 O  O   . PRO B  1  9   ? -4.592  -3.749  49.566 1.00 40.96  ? 22  PRO B O   1 
ATOM   2679 C  CB  . PRO B  1  9   ? -2.897  -1.454  48.096 1.00 42.91  ? 22  PRO B CB  1 
ATOM   2680 C  CG  . PRO B  1  9   ? -2.312  -0.389  48.976 1.00 46.27  ? 22  PRO B CG  1 
ATOM   2681 C  CD  . PRO B  1  9   ? -3.031  -0.541  50.314 1.00 45.36  ? 22  PRO B CD  1 
ATOM   2682 N  N   . GLY B  1  10  ? -5.443  -3.467  47.486 1.00 37.95  ? 23  GLY B N   1 
ATOM   2683 C  CA  . GLY B  1  10  ? -5.795  -4.867  47.291 1.00 38.06  ? 23  GLY B CA  1 
ATOM   2684 C  C   . GLY B  1  10  ? -4.619  -5.679  46.742 1.00 39.20  ? 23  GLY B C   1 
ATOM   2685 O  O   . GLY B  1  10  ? -3.514  -5.159  46.572 1.00 37.67  ? 23  GLY B O   1 
ATOM   2686 N  N   . PRO B  1  11  ? -4.839  -6.972  46.410 1.00 40.55  ? 24  PRO B N   1 
ATOM   2687 C  CA  . PRO B  1  11  ? -3.787  -7.816  45.851 1.00 42.66  ? 24  PRO B CA  1 
ATOM   2688 C  C   . PRO B  1  11  ? -3.307  -7.243  44.514 1.00 44.57  ? 24  PRO B C   1 
ATOM   2689 O  O   . PRO B  1  11  ? -4.014  -6.483  43.872 1.00 44.04  ? 24  PRO B O   1 
ATOM   2690 C  CB  . PRO B  1  11  ? -4.446  -9.198  45.680 1.00 43.09  ? 24  PRO B CB  1 
ATOM   2691 C  CG  . PRO B  1  11  ? -5.753  -9.114  46.434 1.00 43.19  ? 24  PRO B CG  1 
ATOM   2692 C  CD  . PRO B  1  11  ? -6.134  -7.656  46.471 1.00 39.21  ? 24  PRO B CD  1 
ATOM   2693 N  N   . PRO B  1  12  ? -2.088  -7.570  44.044 1.00 50.03  ? 25  PRO B N   1 
ATOM   2694 C  CA  . PRO B  1  12  ? -1.666  -7.169  42.703 1.00 52.51  ? 25  PRO B CA  1 
ATOM   2695 C  C   . PRO B  1  12  ? -2.484  -7.840  41.596 1.00 51.06  ? 25  PRO B C   1 
ATOM   2696 O  O   . PRO B  1  12  ? -3.001  -8.940  41.786 1.00 49.31  ? 25  PRO B O   1 
ATOM   2697 C  CB  . PRO B  1  12  ? -0.183  -7.591  42.690 1.00 51.93  ? 25  PRO B CB  1 
ATOM   2698 C  CG  . PRO B  1  12  ? -0.088  -8.713  43.682 1.00 51.28  ? 25  PRO B CG  1 
ATOM   2699 C  CD  . PRO B  1  12  ? -1.076  -8.356  44.764 1.00 49.92  ? 25  PRO B CD  1 
ATOM   2700 N  N   . SER B  1  13  ? -2.588  -7.165  40.442 1.00 57.08  ? 26  SER B N   1 
ATOM   2701 C  CA  A SER B  1  13  ? -3.235  -7.717  39.257 0.50 54.58  ? 26  SER B CA  1 
ATOM   2702 C  CA  B SER B  1  13  ? -3.241  -7.720  39.263 0.50 54.72  ? 26  SER B CA  1 
ATOM   2703 C  C   . SER B  1  13  ? -2.528  -8.990  38.800 1.00 54.03  ? 26  SER B C   1 
ATOM   2704 O  O   . SER B  1  13  ? -3.182  -10.009 38.580 1.00 50.77  ? 26  SER B O   1 
ATOM   2705 C  CB  A SER B  1  13  ? -3.259  -6.723  38.129 0.50 56.02  ? 26  SER B CB  1 
ATOM   2706 C  CB  B SER B  1  13  ? -3.303  -6.711  38.153 0.50 56.19  ? 26  SER B CB  1 
ATOM   2707 O  OG  A SER B  1  13  ? -3.761  -5.466  38.549 0.50 54.72  ? 26  SER B OG  1 
ATOM   2708 O  OG  B SER B  1  13  ? -4.137  -7.178  37.098 0.50 55.04  ? 26  SER B OG  1 
ATOM   2709 N  N   . PHE B  1  14  ? -1.191  -8.898  38.627 1.00 49.80  ? 27  PHE B N   1 
ATOM   2710 C  CA  . PHE B  1  14  ? -0.363  -10.039 38.246 1.00 48.50  ? 27  PHE B CA  1 
ATOM   2711 C  C   . PHE B  1  14  ? 0.240   -10.621 39.525 1.00 44.73  ? 27  PHE B C   1 
ATOM   2712 O  O   . PHE B  1  14  ? 0.912   -9.907  40.257 1.00 47.12  ? 27  PHE B O   1 
ATOM   2713 C  CB  . PHE B  1  14  ? 0.714   -9.647  37.223 1.00 44.49  ? 27  PHE B CB  1 
ATOM   2714 C  CG  . PHE B  1  14  ? 1.668   -10.772 36.830 1.00 51.28  ? 27  PHE B CG  1 
ATOM   2715 C  CD1 . PHE B  1  14  ? 1.234   -11.837 36.034 1.00 47.46  ? 27  PHE B CD1 1 
ATOM   2716 C  CD2 . PHE B  1  14  ? 3.005   -10.754 37.233 1.00 47.92  ? 27  PHE B CD2 1 
ATOM   2717 C  CE1 . PHE B  1  14  ? 2.104   -12.854 35.683 1.00 48.63  ? 27  PHE B CE1 1 
ATOM   2718 C  CE2 . PHE B  1  14  ? 3.863   -11.780 36.878 1.00 46.56  ? 27  PHE B CE2 1 
ATOM   2719 C  CZ  . PHE B  1  14  ? 3.415   -12.821 36.103 1.00 46.14  ? 27  PHE B CZ  1 
ATOM   2720 N  N   . THR B  1  15  ? 0.003   -11.915 39.772 1.00 46.04  ? 28  THR B N   1 
ATOM   2721 C  CA  . THR B  1  15  ? 0.458   -12.579 40.987 1.00 46.15  ? 28  THR B CA  1 
ATOM   2722 C  C   . THR B  1  15  ? 1.436   -13.698 40.644 1.00 45.08  ? 28  THR B C   1 
ATOM   2723 O  O   . THR B  1  15  ? 1.675   -14.550 41.495 1.00 45.32  ? 28  THR B O   1 
ATOM   2724 C  CB  . THR B  1  15  ? -0.721  -13.148 41.791 1.00 44.25  ? 28  THR B CB  1 
ATOM   2725 O  OG1 . THR B  1  15  ? -1.332  -14.214 41.070 1.00 39.23  ? 28  THR B OG1 1 
ATOM   2726 C  CG2 . THR B  1  15  ? -1.797  -12.125 42.071 1.00 43.60  ? 28  THR B CG2 1 
ATOM   2727 N  N   . GLY B  1  16  ? 1.974   -13.723 39.411 1.00 42.88  ? 29  GLY B N   1 
ATOM   2728 C  CA  . GLY B  1  16  ? 2.976   -14.719 39.046 1.00 44.18  ? 29  GLY B CA  1 
ATOM   2729 C  C   . GLY B  1  16  ? 4.390   -14.277 39.424 1.00 43.05  ? 29  GLY B C   1 
ATOM   2730 O  O   . GLY B  1  16  ? 4.566   -13.214 40.019 1.00 37.66  ? 29  GLY B O   1 
ATOM   2731 N  N   . THR B  1  17  ? 5.385   -15.105 39.067 1.00 43.73  ? 30  THR B N   1 
ATOM   2732 C  CA  . THR B  1  17  ? 6.784   -14.764 39.259 1.00 44.65  ? 30  THR B CA  1 
ATOM   2733 C  C   . THR B  1  17  ? 7.134   -13.615 38.316 1.00 43.80  ? 30  THR B C   1 
ATOM   2734 O  O   . THR B  1  17  ? 6.490   -13.432 37.280 1.00 42.27  ? 30  THR B O   1 
ATOM   2735 C  CB  . THR B  1  17  ? 7.689   -15.977 39.008 1.00 46.57  ? 30  THR B CB  1 
ATOM   2736 O  OG1 . THR B  1  17  ? 8.911   -15.492 39.578 1.00 48.60  ? 30  THR B OG1 1 
ATOM   2737 C  CG2 . THR B  1  17  ? 7.743   -16.376 37.536 1.00 46.78  ? 30  THR B CG2 1 
ATOM   2738 N  N   . LYS B  1  18  ? 8.164   -12.853 38.690 1.00 44.06  ? 31  LYS B N   1 
ATOM   2739 C  CA  . LYS B  1  18  ? 8.807   -11.922 37.781 1.00 42.77  ? 31  LYS B CA  1 
ATOM   2740 C  C   . LYS B  1  18  ? 10.179  -11.593 38.355 1.00 41.24  ? 31  LYS B C   1 
ATOM   2741 O  O   . LYS B  1  18  ? 10.428  -11.865 39.529 1.00 40.32  ? 31  LYS B O   1 
ATOM   2742 C  CB  . LYS B  1  18  ? 7.935   -10.676 37.598 1.00 43.98  ? 31  LYS B CB  1 
ATOM   2743 C  CG  . LYS B  1  18  ? 7.727   -9.848  38.846 1.00 48.76  ? 31  LYS B CG  1 
ATOM   2744 C  CD  . LYS B  1  18  ? 6.869   -8.619  38.596 1.00 55.31  ? 31  LYS B CD  1 
ATOM   2745 C  CE  . LYS B  1  18  ? 7.346   -7.456  39.392 1.00 70.38  ? 31  LYS B CE  1 
ATOM   2746 N  NZ  . LYS B  1  18  ? 6.420   -6.321  39.387 1.00 82.25  ? 31  LYS B NZ  1 
ATOM   2747 N  N   . LEU B  1  19  ? 11.039  -11.005 37.517 1.00 41.14  ? 32  LEU B N   1 
ATOM   2748 C  CA  . LEU B  1  19  ? 12.300  -10.443 37.967 1.00 41.00  ? 32  LEU B CA  1 
ATOM   2749 C  C   . LEU B  1  19  ? 11.982  -9.225  38.827 1.00 39.89  ? 32  LEU B C   1 
ATOM   2750 O  O   . LEU B  1  19  ? 11.302  -8.321  38.354 1.00 38.25  ? 32  LEU B O   1 
ATOM   2751 C  CB  . LEU B  1  19  ? 13.174  -10.053 36.772 1.00 39.01  ? 32  LEU B CB  1 
ATOM   2752 C  CG  . LEU B  1  19  ? 14.503  -9.371  37.104 1.00 39.87  ? 32  LEU B CG  1 
ATOM   2753 C  CD1 . LEU B  1  19  ? 15.431  -10.333 37.805 1.00 40.05  ? 32  LEU B CD1 1 
ATOM   2754 C  CD2 . LEU B  1  19  ? 15.158  -8.805  35.866 1.00 40.24  ? 32  LEU B CD2 1 
ATOM   2755 N  N   . VAL B  1  20  ? 12.490  -9.199  40.069 1.00 40.48  ? 33  VAL B N   1 
ATOM   2756 C  CA  . VAL B  1  20  ? 12.264  -8.054  40.937 1.00 42.50  ? 33  VAL B CA  1 
ATOM   2757 C  C   . VAL B  1  20  ? 13.553  -7.257  41.118 1.00 39.36  ? 33  VAL B C   1 
ATOM   2758 O  O   . VAL B  1  20  ? 13.473  -6.062  41.386 1.00 36.95  ? 33  VAL B O   1 
ATOM   2759 C  CB  . VAL B  1  20  ? 11.629  -8.431  42.288 1.00 45.65  ? 33  VAL B CB  1 
ATOM   2760 C  CG1 . VAL B  1  20  ? 10.292  -9.134  42.093 1.00 44.50  ? 33  VAL B CG1 1 
ATOM   2761 C  CG2 . VAL B  1  20  ? 12.549  -9.268  43.157 1.00 48.01  ? 33  VAL B CG2 1 
ATOM   2762 N  N   . ASN B  1  21  ? 14.713  -7.914  40.953 1.00 38.40  ? 34  ASN B N   1 
ATOM   2763 C  CA  . ASN B  1  21  ? 15.999  -7.233  40.934 1.00 39.70  ? 34  ASN B CA  1 
ATOM   2764 C  C   . ASN B  1  21  ? 16.267  -6.737  39.512 1.00 38.12  ? 34  ASN B C   1 
ATOM   2765 O  O   . ASN B  1  21  ? 17.027  -7.352  38.771 1.00 41.07  ? 34  ASN B O   1 
ATOM   2766 C  CB  . ASN B  1  21  ? 17.084  -8.182  41.425 1.00 39.21  ? 34  ASN B CB  1 
ATOM   2767 C  CG  . ASN B  1  21  ? 18.400  -7.507  41.731 1.00 35.28  ? 34  ASN B CG  1 
ATOM   2768 O  OD1 . ASN B  1  21  ? 18.570  -6.308  41.509 1.00 32.87  ? 34  ASN B OD1 1 
ATOM   2769 N  ND2 . ASN B  1  21  ? 19.351  -8.285  42.223 1.00 37.09  ? 34  ASN B ND2 1 
ATOM   2770 N  N   . ASP B  1  22  ? 15.611  -5.640  39.131 1.00 39.56  ? 35  ASP B N   1 
ATOM   2771 C  CA  . ASP B  1  22  ? 15.573  -5.189  37.751 1.00 43.62  ? 35  ASP B CA  1 
ATOM   2772 C  C   . ASP B  1  22  ? 16.163  -3.785  37.688 1.00 40.74  ? 35  ASP B C   1 
ATOM   2773 O  O   . ASP B  1  22  ? 16.584  -3.258  38.719 1.00 39.90  ? 35  ASP B O   1 
ATOM   2774 C  CB  . ASP B  1  22  ? 14.160  -5.276  37.195 1.00 47.88  ? 35  ASP B CB  1 
ATOM   2775 C  CG  . ASP B  1  22  ? 13.074  -4.514  37.948 1.00 46.85  ? 35  ASP B CG  1 
ATOM   2776 O  OD1 . ASP B  1  22  ? 13.373  -3.469  38.566 1.00 52.84  ? 35  ASP B OD1 1 
ATOM   2777 O  OD2 . ASP B  1  22  ? 11.911  -4.923  37.831 1.00 61.50  ? 35  ASP B OD2 1 
ATOM   2778 N  N   . ALA B  1  23  ? 16.127  -3.176  36.495 1.00 38.71  ? 36  ALA B N   1 
ATOM   2779 C  CA  . ALA B  1  23  ? 16.918  -1.987  36.210 1.00 41.25  ? 36  ALA B CA  1 
ATOM   2780 C  C   . ALA B  1  23  ? 16.357  -0.780  36.948 1.00 36.53  ? 36  ALA B C   1 
ATOM   2781 O  O   . ALA B  1  23  ? 17.091  0.144   37.280 1.00 43.06  ? 36  ALA B O   1 
ATOM   2782 C  CB  . ALA B  1  23  ? 16.963  -1.748  34.709 1.00 42.49  ? 36  ALA B CB  1 
ATOM   2783 N  N   . ASP B  1  24  ? 15.042  -0.799  37.187 1.00 39.47  ? 37  ASP B N   1 
ATOM   2784 C  CA  . ASP B  1  24  ? 14.360  0.302   37.844 1.00 40.62  ? 37  ASP B CA  1 
ATOM   2785 C  C   . ASP B  1  24  ? 14.465  0.190   39.366 1.00 37.33  ? 37  ASP B C   1 
ATOM   2786 O  O   . ASP B  1  24  ? 14.114  1.126   40.071 1.00 44.06  ? 37  ASP B O   1 
ATOM   2787 C  CB  . ASP B  1  24  ? 12.926  0.372   37.356 1.00 44.01  ? 37  ASP B CB  1 
ATOM   2788 C  CG  . ASP B  1  24  ? 12.291  1.751   37.440 1.00 48.62  ? 37  ASP B CG  1 
ATOM   2789 O  OD1 . ASP B  1  24  ? 12.929  2.744   36.976 1.00 46.15  ? 37  ASP B OD1 1 
ATOM   2790 O  OD2 . ASP B  1  24  ? 11.162  1.807   37.967 1.00 56.24  ? 37  ASP B OD2 1 
ATOM   2791 N  N   . HIS B  1  25  ? 14.954  -0.948  39.865 1.00 34.83  ? 38  HIS B N   1 
ATOM   2792 C  CA  . HIS B  1  25  ? 15.069  -1.200  41.297 1.00 37.42  ? 38  HIS B CA  1 
ATOM   2793 C  C   . HIS B  1  25  ? 16.481  -1.672  41.649 1.00 38.26  ? 38  HIS B C   1 
ATOM   2794 O  O   . HIS B  1  25  ? 16.659  -2.776  42.183 1.00 39.36  ? 38  HIS B O   1 
ATOM   2795 C  CB  . HIS B  1  25  ? 13.999  -2.209  41.738 1.00 36.00  ? 38  HIS B CB  1 
ATOM   2796 C  CG  . HIS B  1  25  ? 12.613  -1.696  41.523 1.00 39.88  ? 38  HIS B CG  1 
ATOM   2797 N  ND1 . HIS B  1  25  ? 11.818  -2.022  40.440 1.00 42.80  ? 38  HIS B ND1 1 
ATOM   2798 C  CD2 . HIS B  1  25  ? 11.889  -0.870  42.285 1.00 37.47  ? 38  HIS B CD2 1 
ATOM   2799 C  CE1 . HIS B  1  25  ? 10.665  -1.386  40.559 1.00 44.14  ? 38  HIS B CE1 1 
ATOM   2800 N  NE2 . HIS B  1  25  ? 10.686  -0.692  41.674 1.00 38.03  ? 38  HIS B NE2 1 
ATOM   2801 N  N   . PRO B  1  26  ? 17.536  -0.868  41.359 1.00 35.16  ? 39  PRO B N   1 
ATOM   2802 C  CA  . PRO B  1  26  ? 18.906  -1.247  41.713 1.00 36.91  ? 39  PRO B CA  1 
ATOM   2803 C  C   . PRO B  1  26  ? 19.178  -1.125  43.213 1.00 38.44  ? 39  PRO B C   1 
ATOM   2804 O  O   . PRO B  1  26  ? 18.675  -0.207  43.861 1.00 36.96  ? 39  PRO B O   1 
ATOM   2805 C  CB  . PRO B  1  26  ? 19.731  -0.234  40.898 1.00 36.35  ? 39  PRO B CB  1 
ATOM   2806 C  CG  . PRO B  1  26  ? 18.864  1.003   40.867 1.00 35.22  ? 39  PRO B CG  1 
ATOM   2807 C  CD  . PRO B  1  26  ? 17.471  0.443   40.694 1.00 34.83  ? 39  PRO B CD  1 
ATOM   2808 N  N   . TRP B  1  27  ? 19.981  -2.047  43.760 1.00 39.43  ? 40  TRP B N   1 
ATOM   2809 C  CA  . TRP B  1  27  ? 20.569  -1.845  45.077 1.00 35.89  ? 40  TRP B CA  1 
ATOM   2810 C  C   . TRP B  1  27  ? 21.411  -0.566  45.051 1.00 36.47  ? 40  TRP B C   1 
ATOM   2811 O  O   . TRP B  1  27  ? 22.146  -0.334  44.087 1.00 37.03  ? 40  TRP B O   1 
ATOM   2812 C  CB  . TRP B  1  27  ? 21.397  -3.065  45.493 1.00 34.18  ? 40  TRP B CB  1 
ATOM   2813 C  CG  . TRP B  1  27  ? 21.971  -2.977  46.885 1.00 34.63  ? 40  TRP B CG  1 
ATOM   2814 C  CD1 . TRP B  1  27  ? 21.386  -3.428  48.028 1.00 34.94  ? 40  TRP B CD1 1 
ATOM   2815 C  CD2 . TRP B  1  27  ? 23.227  -2.381  47.283 1.00 34.92  ? 40  TRP B CD2 1 
ATOM   2816 N  NE1 . TRP B  1  27  ? 22.187  -3.171  49.107 1.00 35.79  ? 40  TRP B NE1 1 
ATOM   2817 C  CE2 . TRP B  1  27  ? 23.316  -2.524  48.685 1.00 33.86  ? 40  TRP B CE2 1 
ATOM   2818 C  CE3 . TRP B  1  27  ? 24.276  -1.739  46.600 1.00 36.53  ? 40  TRP B CE3 1 
ATOM   2819 C  CZ2 . TRP B  1  27  ? 24.400  -2.036  49.409 1.00 34.23  ? 40  TRP B CZ2 1 
ATOM   2820 C  CZ3 . TRP B  1  27  ? 25.348  -1.251  47.321 1.00 35.23  ? 40  TRP B CZ3 1 
ATOM   2821 C  CH2 . TRP B  1  27  ? 25.397  -1.390  48.708 1.00 36.02  ? 40  TRP B CH2 1 
ATOM   2822 N  N   . GLN B  1  28  ? 21.259  0.270   46.089 1.00 33.89  ? 41  GLN B N   1 
ATOM   2823 C  CA  . GLN B  1  28  ? 22.102  1.432   46.309 1.00 37.32  ? 41  GLN B CA  1 
ATOM   2824 C  C   . GLN B  1  28  ? 22.530  1.456   47.772 1.00 37.53  ? 41  GLN B C   1 
ATOM   2825 O  O   . GLN B  1  28  ? 21.798  0.984   48.635 1.00 39.02  ? 41  GLN B O   1 
ATOM   2826 C  CB  . GLN B  1  28  ? 21.399  2.728   45.914 1.00 40.07  ? 41  GLN B CB  1 
ATOM   2827 C  CG  . GLN B  1  28  ? 21.086  2.818   44.424 1.00 43.34  ? 41  GLN B CG  1 
ATOM   2828 C  CD  . GLN B  1  28  ? 20.356  4.088   44.046 1.00 43.13  ? 41  GLN B CD  1 
ATOM   2829 O  OE1 . GLN B  1  28  ? 20.039  4.927   44.891 1.00 42.27  ? 41  GLN B OE1 1 
ATOM   2830 N  NE2 . GLN B  1  28  ? 20.081  4.238   42.764 1.00 48.68  ? 41  GLN B NE2 1 
ATOM   2831 N  N   . PRO B  1  29  ? 23.732  1.984   48.098 1.00 39.01  ? 42  PRO B N   1 
ATOM   2832 C  CA  . PRO B  1  29  ? 24.163  2.109   49.490 1.00 37.14  ? 42  PRO B CA  1 
ATOM   2833 C  C   . PRO B  1  29  ? 23.345  3.144   50.265 1.00 38.98  ? 42  PRO B C   1 
ATOM   2834 O  O   . PRO B  1  29  ? 22.696  4.011   49.686 1.00 36.98  ? 42  PRO B O   1 
ATOM   2835 C  CB  . PRO B  1  29  ? 25.652  2.511   49.370 1.00 35.90  ? 42  PRO B CB  1 
ATOM   2836 C  CG  . PRO B  1  29  ? 25.748  3.209   48.038 1.00 37.08  ? 42  PRO B CG  1 
ATOM   2837 C  CD  . PRO B  1  29  ? 24.736  2.496   47.146 1.00 38.97  ? 42  PRO B CD  1 
ATOM   2838 N  N   . LEU B  1  30  ? 23.403  3.054   51.596 1.00 41.04  ? 43  LEU B N   1 
ATOM   2839 C  CA  . LEU B  1  30  ? 22.765  4.032   52.464 1.00 43.23  ? 43  LEU B CA  1 
ATOM   2840 C  C   . LEU B  1  30  ? 23.435  5.398   52.304 1.00 45.01  ? 43  LEU B C   1 
ATOM   2841 O  O   . LEU B  1  30  ? 24.653  5.484   52.198 1.00 43.22  ? 43  LEU B O   1 
ATOM   2842 C  CB  . LEU B  1  30  ? 22.842  3.541   53.908 1.00 44.63  ? 43  LEU B CB  1 
ATOM   2843 C  CG  . LEU B  1  30  ? 22.109  2.232   54.219 1.00 47.14  ? 43  LEU B CG  1 
ATOM   2844 C  CD1 . LEU B  1  30  ? 22.086  2.020   55.721 1.00 48.93  ? 43  LEU B CD1 1 
ATOM   2845 C  CD2 . LEU B  1  30  ? 20.698  2.110   53.656 1.00 47.73  ? 43  LEU B CD2 1 
ATOM   2846 N  N   . ARG B  1  31  ? 22.610  6.450   52.243 1.00 50.34  ? 44  ARG B N   1 
ATOM   2847 C  CA  . ARG B  1  31  ? 23.036  7.835   52.374 1.00 51.46  ? 44  ARG B CA  1 
ATOM   2848 C  C   . ARG B  1  31  ? 22.747  8.288   53.810 1.00 55.71  ? 44  ARG B C   1 
ATOM   2849 O  O   . ARG B  1  31  ? 22.008  7.621   54.541 1.00 53.91  ? 44  ARG B O   1 
ATOM   2850 C  CB  . ARG B  1  31  ? 22.233  8.758   51.446 1.00 50.95  ? 44  ARG B CB  1 
ATOM   2851 C  CG  . ARG B  1  31  ? 22.084  8.352   49.986 1.00 51.96  ? 44  ARG B CG  1 
ATOM   2852 C  CD  . ARG B  1  31  ? 20.848  8.983   49.324 1.00 58.75  ? 44  ARG B CD  1 
ATOM   2853 N  NE  . ARG B  1  31  ? 19.605  8.731   50.072 1.00 65.43  ? 44  ARG B NE  1 
ATOM   2854 C  CZ  . ARG B  1  31  ? 18.361  8.774   49.608 1.00 63.96  ? 44  ARG B CZ  1 
ATOM   2855 N  NH1 . ARG B  1  31  ? 18.115  9.086   48.348 1.00 67.96  ? 44  ARG B NH1 1 
ATOM   2856 N  NH2 . ARG B  1  31  ? 17.360  8.477   50.414 1.00 62.08  ? 44  ARG B NH2 1 
ATOM   2857 N  N   . GLU B  1  32  ? 23.281  9.455   54.189 1.00 60.04  ? 45  GLU B N   1 
ATOM   2858 C  CA  . GLU B  1  32  ? 23.026  10.031  55.501 1.00 69.13  ? 45  GLU B CA  1 
ATOM   2859 C  C   . GLU B  1  32  ? 21.525  10.292  55.653 1.00 60.36  ? 45  GLU B C   1 
ATOM   2860 O  O   . GLU B  1  32  ? 20.902  10.868  54.764 1.00 54.67  ? 45  GLU B O   1 
ATOM   2861 C  CB  . GLU B  1  32  ? 23.869  11.301  55.665 1.00 84.10  ? 45  GLU B CB  1 
ATOM   2862 C  CG  . GLU B  1  32  ? 23.827  11.936  57.056 1.00 101.47 ? 45  GLU B CG  1 
ATOM   2863 C  CD  . GLU B  1  32  ? 24.424  11.126  58.202 1.00 114.08 ? 45  GLU B CD  1 
ATOM   2864 O  OE1 . GLU B  1  32  ? 24.703  9.916   58.026 1.00 117.47 ? 45  GLU B OE1 1 
ATOM   2865 O  OE2 . GLU B  1  32  ? 24.602  11.722  59.294 1.00 116.76 ? 45  GLU B OE2 1 
ATOM   2866 N  N   . GLY B  1  33  ? 20.953  9.832   56.774 1.00 52.00  ? 46  GLY B N   1 
ATOM   2867 C  CA  . GLY B  1  33  ? 19.543  10.024  57.065 1.00 52.49  ? 46  GLY B CA  1 
ATOM   2868 C  C   . GLY B  1  33  ? 18.714  8.765   56.823 1.00 54.04  ? 46  GLY B C   1 
ATOM   2869 O  O   . GLY B  1  33  ? 17.598  8.678   57.335 1.00 57.13  ? 46  GLY B O   1 
ATOM   2870 N  N   . ASP B  1  34  ? 19.237  7.831   56.010 1.00 53.09  ? 47  ASP B N   1 
ATOM   2871 C  CA  . ASP B  1  34  ? 18.475  6.668   55.579 1.00 51.16  ? 47  ASP B CA  1 
ATOM   2872 C  C   . ASP B  1  34  ? 18.314  5.712   56.753 1.00 43.05  ? 47  ASP B C   1 
ATOM   2873 O  O   . ASP B  1  34  ? 19.272  5.453   57.453 1.00 47.31  ? 47  ASP B O   1 
ATOM   2874 C  CB  . ASP B  1  34  ? 19.134  5.962   54.403 1.00 52.88  ? 47  ASP B CB  1 
ATOM   2875 C  CG  . ASP B  1  34  ? 19.100  6.704   53.070 1.00 53.72  ? 47  ASP B CG  1 
ATOM   2876 O  OD1 . ASP B  1  34  ? 18.408  7.731   52.973 1.00 58.32  ? 47  ASP B OD1 1 
ATOM   2877 O  OD2 . ASP B  1  34  ? 19.773  6.249   52.131 1.00 54.17  ? 47  ASP B OD2 1 
ATOM   2878 N  N   . ILE B  1  35  ? 17.104  5.189   56.944 1.00 42.26  ? 48  ILE B N   1 
ATOM   2879 C  CA  . ILE B  1  35  ? 16.786  4.358   58.090 1.00 43.05  ? 48  ILE B CA  1 
ATOM   2880 C  C   . ILE B  1  35  ? 16.570  2.916   57.646 1.00 36.38  ? 48  ILE B C   1 
ATOM   2881 O  O   . ILE B  1  35  ? 15.901  2.663   56.657 1.00 38.44  ? 48  ILE B O   1 
ATOM   2882 C  CB  . ILE B  1  35  ? 15.560  4.937   58.817 1.00 46.89  ? 48  ILE B CB  1 
ATOM   2883 C  CG1 . ILE B  1  35  ? 15.934  6.266   59.458 1.00 49.39  ? 48  ILE B CG1 1 
ATOM   2884 C  CG2 . ILE B  1  35  ? 14.999  3.948   59.840 1.00 45.30  ? 48  ILE B CG2 1 
ATOM   2885 C  CD1 . ILE B  1  35  ? 14.748  7.089   59.878 1.00 57.87  ? 48  ILE B CD1 1 
ATOM   2886 N  N   . ARG B  1  36  ? 17.179  1.998   58.394 1.00 36.01  ? 49  ARG B N   1 
ATOM   2887 C  CA  . ARG B  1  36  ? 16.981  0.565   58.269 1.00 39.00  ? 49  ARG B CA  1 
ATOM   2888 C  C   . ARG B  1  36  ? 16.754  0.040   59.687 1.00 37.33  ? 49  ARG B C   1 
ATOM   2889 O  O   . ARG B  1  36  ? 17.047  0.742   60.644 1.00 38.41  ? 49  ARG B O   1 
ATOM   2890 C  CB  . ARG B  1  36  ? 18.200  -0.066  57.578 1.00 36.00  ? 49  ARG B CB  1 
ATOM   2891 C  CG  . ARG B  1  36  ? 18.466  0.427   56.161 1.00 35.92  ? 49  ARG B CG  1 
ATOM   2892 C  CD  . ARG B  1  36  ? 17.396  -0.017  55.168 1.00 36.94  ? 49  ARG B CD  1 
ATOM   2893 N  NE  . ARG B  1  36  ? 17.629  0.444   53.793 1.00 37.72  ? 49  ARG B NE  1 
ATOM   2894 C  CZ  . ARG B  1  36  ? 17.368  1.661   53.315 1.00 41.91  ? 49  ARG B CZ  1 
ATOM   2895 N  NH1 . ARG B  1  36  ? 16.804  2.581   54.078 1.00 43.01  ? 49  ARG B NH1 1 
ATOM   2896 N  NH2 . ARG B  1  36  ? 17.660  1.958   52.062 1.00 44.61  ? 49  ARG B NH2 1 
ATOM   2897 N  N   . GLY B  1  37  ? 16.245  -1.185  59.822 1.00 40.12  ? 50  GLY B N   1 
ATOM   2898 C  CA  . GLY B  1  37  ? 15.766  -1.658  61.106 1.00 36.86  ? 50  GLY B CA  1 
ATOM   2899 C  C   . GLY B  1  37  ? 15.832  -3.175  61.203 1.00 37.48  ? 50  GLY B C   1 
ATOM   2900 O  O   . GLY B  1  37  ? 16.701  -3.800  60.604 1.00 33.30  ? 50  GLY B O   1 
ATOM   2901 N  N   . PRO B  1  38  ? 14.931  -3.807  61.988 1.00 38.57  ? 51  PRO B N   1 
ATOM   2902 C  CA  . PRO B  1  38  ? 15.022  -5.240  62.271 1.00 36.19  ? 51  PRO B CA  1 
ATOM   2903 C  C   . PRO B  1  38  ? 14.457  -6.181  61.205 1.00 39.28  ? 51  PRO B C   1 
ATOM   2904 O  O   . PRO B  1  38  ? 14.605  -7.398  61.327 1.00 38.66  ? 51  PRO B O   1 
ATOM   2905 C  CB  . PRO B  1  38  ? 14.195  -5.295  63.557 1.00 36.04  ? 51  PRO B CB  1 
ATOM   2906 C  CG  . PRO B  1  38  ? 13.073  -4.312  63.327 1.00 37.23  ? 51  PRO B CG  1 
ATOM   2907 C  CD  . PRO B  1  38  ? 13.769  -3.166  62.622 1.00 38.61  ? 51  PRO B CD  1 
ATOM   2908 N  N   . CYS B  1  39  ? 13.761  -5.622  60.198 1.00 37.18  ? 52  CYS B N   1 
ATOM   2909 C  CA  . CYS B  1  39  ? 13.118  -6.417  59.167 1.00 37.31  ? 52  CYS B CA  1 
ATOM   2910 C  C   . CYS B  1  39  ? 13.991  -6.481  57.921 1.00 37.04  ? 52  CYS B C   1 
ATOM   2911 O  O   . CYS B  1  39  ? 14.160  -5.479  57.223 1.00 35.12  ? 52  CYS B O   1 
ATOM   2912 C  CB  . CYS B  1  39  ? 11.760  -5.861  58.761 1.00 38.71  ? 52  CYS B CB  1 
ATOM   2913 S  SG  . CYS B  1  39  ? 10.886  -6.960  57.626 1.00 37.63  ? 52  CYS B SG  1 
ATOM   2914 N  N   . PRO B  1  40  ? 14.537  -7.668  57.579 1.00 34.63  ? 53  PRO B N   1 
ATOM   2915 C  CA  . PRO B  1  40  ? 15.315  -7.821  56.350 1.00 34.26  ? 53  PRO B CA  1 
ATOM   2916 C  C   . PRO B  1  40  ? 14.492  -7.641  55.073 1.00 36.67  ? 53  PRO B C   1 
ATOM   2917 O  O   . PRO B  1  40  ? 15.022  -7.214  54.052 1.00 32.79  ? 53  PRO B O   1 
ATOM   2918 C  CB  . PRO B  1  40  ? 15.916  -9.232  56.496 1.00 36.17  ? 53  PRO B CB  1 
ATOM   2919 C  CG  . PRO B  1  40  ? 14.965  -9.970  57.427 1.00 36.47  ? 53  PRO B CG  1 
ATOM   2920 C  CD  . PRO B  1  40  ? 14.448  -8.902  58.367 1.00 35.04  ? 53  PRO B CD  1 
ATOM   2921 N  N   . GLY B  1  41  ? 13.186  -7.943  55.144 1.00 37.17  ? 54  GLY B N   1 
ATOM   2922 C  CA  . GLY B  1  41  ? 12.279  -7.753  54.019 1.00 35.85  ? 54  GLY B CA  1 
ATOM   2923 C  C   . GLY B  1  41  ? 12.159  -6.282  53.629 1.00 34.83  ? 54  GLY B C   1 
ATOM   2924 O  O   . GLY B  1  41  ? 12.448  -5.892  52.497 1.00 36.44  ? 54  GLY B O   1 
ATOM   2925 N  N   . LEU B  1  42  ? 11.749  -5.466  54.593 1.00 32.42  ? 55  LEU B N   1 
ATOM   2926 C  CA  . LEU B  1  42  ? 11.580  -4.043  54.365 1.00 34.59  ? 55  LEU B CA  1 
ATOM   2927 C  C   . LEU B  1  42  ? 12.923  -3.369  54.073 1.00 36.27  ? 55  LEU B C   1 
ATOM   2928 O  O   . LEU B  1  42  ? 12.972  -2.440  53.278 1.00 32.80  ? 55  LEU B O   1 
ATOM   2929 C  CB  . LEU B  1  42  ? 10.885  -3.441  55.586 1.00 33.34  ? 55  LEU B CB  1 
ATOM   2930 C  CG  . LEU B  1  42  ? 9.477   -3.979  55.874 1.00 35.30  ? 55  LEU B CG  1 
ATOM   2931 C  CD1 . LEU B  1  42  ? 8.937   -3.432  57.177 1.00 36.60  ? 55  LEU B CD1 1 
ATOM   2932 C  CD2 . LEU B  1  42  ? 8.510   -3.659  54.750 1.00 36.99  ? 55  LEU B CD2 1 
ATOM   2933 N  N   . ASN B  1  43  ? 14.001  -3.828  54.726 1.00 36.33  ? 56  ASN B N   1 
ATOM   2934 C  CA  . ASN B  1  43  ? 15.334  -3.292  54.504 1.00 35.52  ? 56  ASN B CA  1 
ATOM   2935 C  C   . ASN B  1  43  ? 15.737  -3.477  53.040 1.00 35.30  ? 56  ASN B C   1 
ATOM   2936 O  O   . ASN B  1  43  ? 16.192  -2.522  52.402 1.00 33.46  ? 56  ASN B O   1 
ATOM   2937 C  CB  . ASN B  1  43  ? 16.378  -3.938  55.413 1.00 33.33  ? 56  ASN B CB  1 
ATOM   2938 C  CG  . ASN B  1  43  ? 16.310  -3.473  56.851 1.00 35.89  ? 56  ASN B CG  1 
ATOM   2939 O  OD1 . ASN B  1  43  ? 15.684  -2.455  57.186 1.00 34.11  ? 56  ASN B OD1 1 
ATOM   2940 N  ND2 . ASN B  1  43  ? 16.989  -4.203  57.723 1.00 34.45  ? 56  ASN B ND2 1 
ATOM   2941 N  N   . THR B  1  44  ? 15.535  -4.688  52.516 1.00 31.46  ? 57  THR B N   1 
ATOM   2942 C  CA  . THR B  1  44  ? 15.876  -4.985  51.132 1.00 36.15  ? 57  THR B CA  1 
ATOM   2943 C  C   . THR B  1  44  ? 15.010  -4.157  50.176 1.00 36.48  ? 57  THR B C   1 
ATOM   2944 O  O   . THR B  1  44  ? 15.519  -3.636  49.183 1.00 35.71  ? 57  THR B O   1 
ATOM   2945 C  CB  . THR B  1  44  ? 15.741  -6.486  50.870 1.00 34.30  ? 57  THR B CB  1 
ATOM   2946 O  OG1 . THR B  1  44  ? 16.603  -7.115  51.805 1.00 33.67  ? 57  THR B OG1 1 
ATOM   2947 C  CG2 . THR B  1  44  ? 16.196  -6.894  49.484 1.00 33.71  ? 57  THR B CG2 1 
ATOM   2948 N  N   . LEU B  1  45  ? 13.714  -4.009  50.482 1.00 36.58  ? 58  LEU B N   1 
ATOM   2949 C  CA  . LEU B  1  45  ? 12.810  -3.261  49.620 1.00 36.70  ? 58  LEU B CA  1 
ATOM   2950 C  C   . LEU B  1  45  ? 13.200  -1.780  49.536 1.00 37.61  ? 58  LEU B C   1 
ATOM   2951 O  O   . LEU B  1  45  ? 13.091  -1.172  48.466 1.00 35.68  ? 58  LEU B O   1 
ATOM   2952 C  CB  . LEU B  1  45  ? 11.375  -3.433  50.097 1.00 37.24  ? 58  LEU B CB  1 
ATOM   2953 C  CG  . LEU B  1  45  ? 10.791  -4.838  49.918 1.00 37.46  ? 58  LEU B CG  1 
ATOM   2954 C  CD1 . LEU B  1  45  ? 9.519   -4.988  50.725 1.00 35.34  ? 58  LEU B CD1 1 
ATOM   2955 C  CD2 . LEU B  1  45  ? 10.535  -5.145  48.454 1.00 36.21  ? 58  LEU B CD2 1 
ATOM   2956 N  N   . ALA B  1  46  ? 13.655  -1.212  50.657 1.00 32.70  ? 59  ALA B N   1 
ATOM   2957 C  CA  . ALA B  1  46  ? 14.107  0.170   50.681 1.00 38.02  ? 59  ALA B CA  1 
ATOM   2958 C  C   . ALA B  1  46  ? 15.423  0.332   49.921 1.00 36.49  ? 59  ALA B C   1 
ATOM   2959 O  O   . ALA B  1  46  ? 15.608  1.301   49.185 1.00 34.31  ? 59  ALA B O   1 
ATOM   2960 C  CB  . ALA B  1  46  ? 14.235  0.636   52.115 1.00 38.83  ? 59  ALA B CB  1 
ATOM   2961 N  N   . SER B  1  47  ? 16.325  -0.643  50.080 1.00 35.20  ? 60  SER B N   1 
ATOM   2962 C  CA  . SER B  1  47  ? 17.646  -0.548  49.487 1.00 35.50  ? 60  SER B CA  1 
ATOM   2963 C  C   . SER B  1  47  ? 17.593  -0.828  47.984 1.00 38.17  ? 60  SER B C   1 
ATOM   2964 O  O   . SER B  1  47  ? 18.567  -0.566  47.300 1.00 35.40  ? 60  SER B O   1 
ATOM   2965 C  CB  . SER B  1  47  ? 18.635  -1.423  50.214 1.00 33.72  ? 60  SER B CB  1 
ATOM   2966 O  OG  . SER B  1  47  ? 19.048  -0.807  51.427 1.00 32.66  ? 60  SER B OG  1 
ATOM   2967 N  N   . HIS B  1  48  ? 16.444  -1.306  47.475 1.00 37.58  ? 61  HIS B N   1 
ATOM   2968 C  CA  . HIS B  1  48  ? 16.224  -1.459  46.046 1.00 36.69  ? 61  HIS B CA  1 
ATOM   2969 C  C   . HIS B  1  48  ? 15.194  -0.462  45.505 1.00 35.74  ? 61  HIS B C   1 
ATOM   2970 O  O   . HIS B  1  48  ? 14.879  -0.489  44.326 1.00 33.42  ? 61  HIS B O   1 
ATOM   2971 C  CB  . HIS B  1  48  ? 15.782  -2.886  45.708 1.00 37.51  ? 61  HIS B CB  1 
ATOM   2972 C  CG  . HIS B  1  48  ? 16.885  -3.892  45.691 1.00 35.89  ? 61  HIS B CG  1 
ATOM   2973 N  ND1 . HIS B  1  48  ? 17.519  -4.250  44.527 1.00 33.89  ? 61  HIS B ND1 1 
ATOM   2974 C  CD2 . HIS B  1  48  ? 17.463  -4.617  46.664 1.00 35.47  ? 61  HIS B CD2 1 
ATOM   2975 C  CE1 . HIS B  1  48  ? 18.439  -5.164  44.804 1.00 36.25  ? 61  HIS B CE1 1 
ATOM   2976 N  NE2 . HIS B  1  48  ? 18.417  -5.403  46.093 1.00 37.31  ? 61  HIS B NE2 1 
ATOM   2977 N  N   . GLY B  1  49  ? 14.646  0.412   46.351 1.00 38.06  ? 62  GLY B N   1 
ATOM   2978 C  CA  . GLY B  1  49  ? 13.725  1.445   45.892 1.00 36.24  ? 62  GLY B CA  1 
ATOM   2979 C  C   . GLY B  1  49  ? 12.288  0.969   45.656 1.00 35.28  ? 62  GLY B C   1 
ATOM   2980 O  O   . GLY B  1  49  ? 11.506  1.697   45.059 1.00 41.50  ? 62  GLY B O   1 
ATOM   2981 N  N   . TYR B  1  50  ? 11.919  -0.230  46.128 1.00 34.94  ? 63  TYR B N   1 
ATOM   2982 C  CA  . TYR B  1  50  ? 10.517  -0.614  46.207 1.00 35.08  ? 63  TYR B CA  1 
ATOM   2983 C  C   . TYR B  1  50  ? 9.807   0.260   47.241 1.00 33.44  ? 63  TYR B C   1 
ATOM   2984 O  O   . TYR B  1  50  ? 8.650   0.591   47.053 1.00 32.50  ? 63  TYR B O   1 
ATOM   2985 C  CB  . TYR B  1  50  ? 10.324  -2.107  46.490 1.00 35.66  ? 63  TYR B CB  1 
ATOM   2986 C  CG  . TYR B  1  50  ? 10.518  -2.942  45.234 1.00 36.52  ? 63  TYR B CG  1 
ATOM   2987 C  CD1 . TYR B  1  50  ? 9.502   -3.067  44.297 1.00 37.58  ? 63  TYR B CD1 1 
ATOM   2988 C  CD2 . TYR B  1  50  ? 11.742  -3.541  44.953 1.00 37.73  ? 63  TYR B CD2 1 
ATOM   2989 C  CE1 . TYR B  1  50  ? 9.679   -3.791  43.127 1.00 41.35  ? 63  TYR B CE1 1 
ATOM   2990 C  CE2 . TYR B  1  50  ? 11.926  -4.281  43.796 1.00 41.57  ? 63  TYR B CE2 1 
ATOM   2991 C  CZ  . TYR B  1  50  ? 10.890  -4.410  42.882 1.00 40.72  ? 63  TYR B CZ  1 
ATOM   2992 O  OH  . TYR B  1  50  ? 11.076  -5.133  41.740 1.00 41.07  ? 63  TYR B OH  1 
ATOM   2993 N  N   . LEU B  1  51  ? 10.502  0.576   48.338 1.00 36.53  ? 64  LEU B N   1 
ATOM   2994 C  CA  . LEU B  1  51  ? 10.096  1.581   49.305 1.00 38.23  ? 64  LEU B CA  1 
ATOM   2995 C  C   . LEU B  1  51  ? 10.969  2.813   49.104 1.00 41.76  ? 64  LEU B C   1 
ATOM   2996 O  O   . LEU B  1  51  ? 12.047  2.711   48.527 1.00 41.80  ? 64  LEU B O   1 
ATOM   2997 C  CB  . LEU B  1  51  ? 10.300  1.055   50.727 1.00 42.10  ? 64  LEU B CB  1 
ATOM   2998 C  CG  . LEU B  1  51  ? 9.318   -0.008  51.201 1.00 44.53  ? 64  LEU B CG  1 
ATOM   2999 C  CD1 . LEU B  1  51  ? 9.817   -0.589  52.488 1.00 45.65  ? 64  LEU B CD1 1 
ATOM   3000 C  CD2 . LEU B  1  51  ? 7.930   0.588   51.345 1.00 47.56  ? 64  LEU B CD2 1 
ATOM   3001 N  N   . PRO B  1  52  ? 10.580  3.989   49.645 1.00 37.63  ? 65  PRO B N   1 
ATOM   3002 C  CA  . PRO B  1  52  ? 11.493  5.125   49.736 1.00 38.33  ? 65  PRO B CA  1 
ATOM   3003 C  C   . PRO B  1  52  ? 12.818  4.720   50.378 1.00 40.61  ? 65  PRO B C   1 
ATOM   3004 O  O   . PRO B  1  52  ? 12.843  3.986   51.366 1.00 43.33  ? 65  PRO B O   1 
ATOM   3005 C  CB  . PRO B  1  52  ? 10.696  6.128   50.575 1.00 38.05  ? 65  PRO B CB  1 
ATOM   3006 C  CG  . PRO B  1  52  ? 9.249   5.791   50.263 1.00 37.69  ? 65  PRO B CG  1 
ATOM   3007 C  CD  . PRO B  1  52  ? 9.257   4.273   50.217 1.00 39.94  ? 65  PRO B CD  1 
ATOM   3008 N  N   . ARG B  1  53  ? 13.922  5.188   49.790 1.00 40.29  ? 66  ARG B N   1 
ATOM   3009 C  CA  . ARG B  1  53  ? 15.245  4.697   50.153 1.00 39.24  ? 66  ARG B CA  1 
ATOM   3010 C  C   . ARG B  1  53  ? 15.666  5.199   51.532 1.00 38.74  ? 66  ARG B C   1 
ATOM   3011 O  O   . ARG B  1  53  ? 16.606  4.663   52.115 1.00 41.05  ? 66  ARG B O   1 
ATOM   3012 C  CB  . ARG B  1  53  ? 16.279  5.049   49.077 1.00 38.65  ? 66  ARG B CB  1 
ATOM   3013 C  CG  . ARG B  1  53  ? 16.007  4.368   47.743 1.00 38.66  ? 66  ARG B CG  1 
ATOM   3014 C  CD  . ARG B  1  53  ? 17.143  4.532   46.767 1.00 40.38  ? 66  ARG B CD  1 
ATOM   3015 N  NE  . ARG B  1  53  ? 16.884  3.830   45.507 1.00 38.68  ? 66  ARG B NE  1 
ATOM   3016 C  CZ  . ARG B  1  53  ? 17.287  2.605   45.215 1.00 38.68  ? 66  ARG B CZ  1 
ATOM   3017 N  NH1 . ARG B  1  53  ? 17.951  1.878   46.098 1.00 39.62  ? 66  ARG B NH1 1 
ATOM   3018 N  NH2 . ARG B  1  53  ? 17.002  2.092   44.034 1.00 39.87  ? 66  ARG B NH2 1 
ATOM   3019 N  N   . ASP B  1  54  ? 14.963  6.209   52.056 1.00 40.83  ? 67  ASP B N   1 
ATOM   3020 C  CA  . ASP B  1  54  ? 15.229  6.734   53.387 1.00 42.73  ? 67  ASP B CA  1 
ATOM   3021 C  C   . ASP B  1  54  ? 14.559  5.896   54.476 1.00 40.34  ? 67  ASP B C   1 
ATOM   3022 O  O   . ASP B  1  54  ? 14.823  6.113   55.656 1.00 41.43  ? 67  ASP B O   1 
ATOM   3023 C  CB  . ASP B  1  54  ? 14.876  8.209   53.503 1.00 43.44  ? 67  ASP B CB  1 
ATOM   3024 C  CG  . ASP B  1  54  ? 13.415  8.566   53.353 1.00 43.04  ? 67  ASP B CG  1 
ATOM   3025 O  OD1 . ASP B  1  54  ? 12.594  7.637   53.198 1.00 48.16  ? 67  ASP B OD1 1 
ATOM   3026 O  OD2 . ASP B  1  54  ? 13.131  9.769   53.395 1.00 51.17  ? 67  ASP B OD2 1 
ATOM   3027 N  N   . GLY B  1  55  ? 13.718  4.931   54.099 1.00 38.76  ? 68  GLY B N   1 
ATOM   3028 C  CA  . GLY B  1  55  ? 13.204  3.963   55.062 1.00 42.22  ? 68  GLY B CA  1 
ATOM   3029 C  C   . GLY B  1  55  ? 12.010  4.493   55.862 1.00 44.27  ? 68  GLY B C   1 
ATOM   3030 O  O   . GLY B  1  55  ? 11.709  3.976   56.938 1.00 39.82  ? 68  GLY B O   1 
ATOM   3031 N  N   . VAL B  1  56  ? 11.344  5.517   55.311 1.00 44.79  ? 69  VAL B N   1 
ATOM   3032 C  CA  . VAL B  1  56  ? 10.123  6.084   55.858 1.00 43.60  ? 69  VAL B CA  1 
ATOM   3033 C  C   . VAL B  1  56  ? 9.064   6.050   54.766 1.00 41.22  ? 69  VAL B C   1 
ATOM   3034 O  O   . VAL B  1  56  ? 9.297   6.594   53.694 1.00 46.34  ? 69  VAL B O   1 
ATOM   3035 C  CB  . VAL B  1  56  ? 10.365  7.526   56.346 1.00 43.21  ? 69  VAL B CB  1 
ATOM   3036 C  CG1 . VAL B  1  56  ? 9.081   8.201   56.813 1.00 44.85  ? 69  VAL B CG1 1 
ATOM   3037 C  CG2 . VAL B  1  56  ? 11.424  7.552   57.439 1.00 42.34  ? 69  VAL B CG2 1 
ATOM   3038 N  N   . ALA B  1  57  ? 7.908   5.437   55.063 1.00 40.98  ? 70  ALA B N   1 
ATOM   3039 C  CA  . ALA B  1  57  ? 6.884   5.178   54.065 1.00 42.68  ? 70  ALA B CA  1 
ATOM   3040 C  C   . ALA B  1  57  ? 5.483   5.242   54.673 1.00 44.79  ? 70  ALA B C   1 
ATOM   3041 O  O   . ALA B  1  57  ? 5.331   5.148   55.888 1.00 41.00  ? 70  ALA B O   1 
ATOM   3042 C  CB  . ALA B  1  57  ? 7.129   3.816   53.472 1.00 46.89  ? 70  ALA B CB  1 
ATOM   3043 N  N   . THR B  1  58  ? 4.468   5.335   53.805 1.00 42.26  ? 71  THR B N   1 
ATOM   3044 C  CA  . THR B  1  58  ? 3.082   5.207   54.218 1.00 41.76  ? 71  THR B CA  1 
ATOM   3045 C  C   . THR B  1  58  ? 2.764   3.723   54.335 1.00 44.33  ? 71  THR B C   1 
ATOM   3046 O  O   . THR B  1  58  ? 3.446   2.894   53.739 1.00 43.70  ? 71  THR B O   1 
ATOM   3047 C  CB  . THR B  1  58  ? 2.123   5.888   53.236 1.00 39.94  ? 71  THR B CB  1 
ATOM   3048 O  OG1 . THR B  1  58  ? 2.141   5.116   52.040 1.00 44.96  ? 71  THR B OG1 1 
ATOM   3049 C  CG2 . THR B  1  58  ? 2.493   7.327   52.943 1.00 41.55  ? 71  THR B CG2 1 
ATOM   3050 N  N   . PRO B  1  59  ? 1.716   3.341   55.098 1.00 43.12  ? 72  PRO B N   1 
ATOM   3051 C  CA  . PRO B  1  59  ? 1.232   1.963   55.075 1.00 42.10  ? 72  PRO B CA  1 
ATOM   3052 C  C   . PRO B  1  59  ? 0.923   1.440   53.674 1.00 40.76  ? 72  PRO B C   1 
ATOM   3053 O  O   . PRO B  1  59  ? 1.232   0.288   53.374 1.00 39.55  ? 72  PRO B O   1 
ATOM   3054 C  CB  . PRO B  1  59  ? -0.030  2.044   55.975 1.00 43.40  ? 72  PRO B CB  1 
ATOM   3055 C  CG  . PRO B  1  59  ? 0.267   3.190   56.930 1.00 42.16  ? 72  PRO B CG  1 
ATOM   3056 C  CD  . PRO B  1  59  ? 0.982   4.190   56.048 1.00 41.05  ? 72  PRO B CD  1 
ATOM   3057 N  N   . ALA B  1  60  ? 0.289   2.276   52.833 1.00 37.45  ? 73  ALA B N   1 
ATOM   3058 C  CA  . ALA B  1  60  ? -0.062  1.874   51.479 1.00 41.40  ? 73  ALA B CA  1 
ATOM   3059 C  C   . ALA B  1  60  ? 1.192   1.542   50.670 1.00 35.66  ? 73  ALA B C   1 
ATOM   3060 O  O   . ALA B  1  60  ? 1.206   0.547   49.960 1.00 42.17  ? 73  ALA B O   1 
ATOM   3061 C  CB  . ALA B  1  60  ? -0.900  2.942   50.820 1.00 44.22  ? 73  ALA B CB  1 
ATOM   3062 N  N   . GLN B  1  61  ? 2.253   2.341   50.819 1.00 35.40  ? 74  GLN B N   1 
ATOM   3063 C  CA  . GLN B  1  61  ? 3.522   2.081   50.145 1.00 41.55  ? 74  GLN B CA  1 
ATOM   3064 C  C   . GLN B  1  61  ? 4.150   0.752   50.587 1.00 42.44  ? 74  GLN B C   1 
ATOM   3065 O  O   . GLN B  1  61  ? 4.724   0.039   49.764 1.00 41.04  ? 74  GLN B O   1 
ATOM   3066 C  CB  . GLN B  1  61  ? 4.517   3.217   50.371 1.00 41.50  ? 74  GLN B CB  1 
ATOM   3067 C  CG  . GLN B  1  61  ? 4.171   4.479   49.601 1.00 43.08  ? 74  GLN B CG  1 
ATOM   3068 C  CD  . GLN B  1  61  ? 5.083   5.637   49.931 1.00 44.36  ? 74  GLN B CD  1 
ATOM   3069 O  OE1 . GLN B  1  61  ? 5.383   5.918   51.092 1.00 40.20  ? 74  GLN B OE1 1 
ATOM   3070 N  NE2 . GLN B  1  61  ? 5.557   6.322   48.905 1.00 50.76  ? 74  GLN B NE2 1 
ATOM   3071 N  N   . ILE B  1  62  ? 4.017   0.419   51.879 1.00 40.50  ? 75  ILE B N   1 
ATOM   3072 C  CA  . ILE B  1  62  ? 4.601   -0.791  52.432 1.00 38.79  ? 75  ILE B CA  1 
ATOM   3073 C  C   . ILE B  1  62  ? 3.888   -2.024  51.895 1.00 38.03  ? 75  ILE B C   1 
ATOM   3074 O  O   . ILE B  1  62  ? 4.542   -3.010  51.556 1.00 41.31  ? 75  ILE B O   1 
ATOM   3075 C  CB  . ILE B  1  62  ? 4.618   -0.736  53.972 1.00 38.34  ? 75  ILE B CB  1 
ATOM   3076 C  CG1 . ILE B  1  62  ? 5.566   0.353   54.447 1.00 35.57  ? 75  ILE B CG1 1 
ATOM   3077 C  CG2 . ILE B  1  62  ? 4.987   -2.094  54.579 1.00 39.99  ? 75  ILE B CG2 1 
ATOM   3078 C  CD1 . ILE B  1  62  ? 5.429   0.711   55.912 1.00 36.53  ? 75  ILE B CD1 1 
ATOM   3079 N  N   . ILE B  1  63  ? 2.561   -1.963  51.808 1.00 38.21  ? 76  ILE B N   1 
ATOM   3080 C  CA  . ILE B  1  63  ? 1.778   -3.067  51.272 1.00 39.96  ? 76  ILE B CA  1 
ATOM   3081 C  C   . ILE B  1  63  ? 2.126   -3.291  49.803 1.00 36.81  ? 76  ILE B C   1 
ATOM   3082 O  O   . ILE B  1  63  ? 2.388   -4.429  49.423 1.00 36.22  ? 76  ILE B O   1 
ATOM   3083 C  CB  . ILE B  1  63  ? 0.272   -2.851  51.523 1.00 44.57  ? 76  ILE B CB  1 
ATOM   3084 C  CG1 . ILE B  1  63  ? -0.030  -3.006  53.014 1.00 47.06  ? 76  ILE B CG1 1 
ATOM   3085 C  CG2 . ILE B  1  63  ? -0.601  -3.793  50.699 1.00 43.32  ? 76  ILE B CG2 1 
ATOM   3086 C  CD1 . ILE B  1  63  ? -1.189  -2.163  53.510 1.00 51.76  ? 76  ILE B CD1 1 
ATOM   3087 N  N   . THR B  1  64  ? 2.176   -2.228  48.995 1.00 40.59  ? 77  THR B N   1 
ATOM   3088 C  CA  A THR B  1  64  ? 2.460   -2.379  47.576 0.50 42.61  ? 77  THR B CA  1 
ATOM   3089 C  CA  B THR B  1  64  ? 2.467   -2.370  47.571 0.50 41.33  ? 77  THR B CA  1 
ATOM   3090 C  C   . THR B  1  64  ? 3.858   -2.987  47.411 1.00 37.84  ? 77  THR B C   1 
ATOM   3091 O  O   . THR B  1  64  ? 4.019   -3.937  46.658 1.00 37.23  ? 77  THR B O   1 
ATOM   3092 C  CB  A THR B  1  64  ? 2.290   -1.045  46.847 0.50 45.99  ? 77  THR B CB  1 
ATOM   3093 C  CB  B THR B  1  64  ? 2.332   -1.055  46.793 0.50 44.33  ? 77  THR B CB  1 
ATOM   3094 O  OG1 A THR B  1  64  ? 3.200   -0.155  47.485 0.50 61.77  ? 77  THR B OG1 1 
ATOM   3095 O  OG1 B THR B  1  64  ? 2.727   -1.276  45.437 0.50 38.41  ? 77  THR B OG1 1 
ATOM   3096 C  CG2 A THR B  1  64  ? 0.882   -0.484  46.946 0.50 41.96  ? 77  THR B CG2 1 
ATOM   3097 C  CG2 B THR B  1  64  ? 3.275   0.034   47.265 0.50 50.51  ? 77  THR B CG2 1 
ATOM   3098 N  N   . ALA B  1  65  ? 4.848   -2.483  48.169 1.00 37.96  ? 78  ALA B N   1 
ATOM   3099 C  CA  . ALA B  1  65  ? 6.240   -2.920  48.065 1.00 35.97  ? 78  ALA B CA  1 
ATOM   3100 C  C   . ALA B  1  65  ? 6.425   -4.395  48.434 1.00 36.10  ? 78  ALA B C   1 
ATOM   3101 O  O   . ALA B  1  65  ? 7.128   -5.120  47.729 1.00 36.81  ? 78  ALA B O   1 
ATOM   3102 C  CB  . ALA B  1  65  ? 7.113   -2.041  48.917 1.00 35.32  ? 78  ALA B CB  1 
ATOM   3103 N  N   . THR B  1  66  ? 5.796   -4.840  49.529 1.00 36.85  ? 79  THR B N   1 
ATOM   3104 C  CA  . THR B  1  66  ? 5.901   -6.233  49.946 1.00 36.37  ? 79  THR B CA  1 
ATOM   3105 C  C   . THR B  1  66  ? 5.263   -7.161  48.919 1.00 34.00  ? 79  THR B C   1 
ATOM   3106 O  O   . THR B  1  66  ? 5.730   -8.287  48.754 1.00 34.51  ? 79  THR B O   1 
ATOM   3107 C  CB  . THR B  1  66  ? 5.293   -6.455  51.334 1.00 37.85  ? 79  THR B CB  1 
ATOM   3108 O  OG1 . THR B  1  66  ? 3.916   -6.090  51.330 1.00 36.04  ? 79  THR B OG1 1 
ATOM   3109 C  CG2 . THR B  1  66  ? 6.060   -5.702  52.408 1.00 38.15  ? 79  THR B CG2 1 
ATOM   3110 N  N   . GLN B  1  67  ? 4.187   -6.703  48.264 1.00 37.53  ? 80  GLN B N   1 
ATOM   3111 C  CA  . GLN B  1  67  ? 3.515   -7.469  47.218 1.00 37.28  ? 80  GLN B CA  1 
ATOM   3112 C  C   . GLN B  1  67  ? 4.345   -7.498  45.934 1.00 34.05  ? 80  GLN B C   1 
ATOM   3113 O  O   . GLN B  1  67  ? 4.578   -8.566  45.372 1.00 36.66  ? 80  GLN B O   1 
ATOM   3114 C  CB  . GLN B  1  67  ? 2.120   -6.895  46.964 1.00 40.26  ? 80  GLN B CB  1 
ATOM   3115 C  CG  . GLN B  1  67  ? 1.178   -7.058  48.155 1.00 43.12  ? 80  GLN B CG  1 
ATOM   3116 C  CD  . GLN B  1  67  ? -0.240  -6.527  47.975 1.00 44.66  ? 80  GLN B CD  1 
ATOM   3117 O  OE1 . GLN B  1  67  ? -1.162  -6.977  48.657 1.00 44.71  ? 80  GLN B OE1 1 
ATOM   3118 N  NE2 . GLN B  1  67  ? -0.470  -5.600  47.055 1.00 43.60  ? 80  GLN B NE2 1 
ATOM   3119 N  N   . GLU B  1  68  ? 4.794   -6.322  45.483 1.00 34.83  ? 81  GLU B N   1 
ATOM   3120 C  CA  . GLU B  1  68  ? 5.548   -6.199  44.244 1.00 40.40  ? 81  GLU B CA  1 
ATOM   3121 C  C   . GLU B  1  68  ? 6.881   -6.937  44.340 1.00 37.92  ? 81  GLU B C   1 
ATOM   3122 O  O   . GLU B  1  68  ? 7.226   -7.676  43.428 1.00 41.15  ? 81  GLU B O   1 
ATOM   3123 C  CB  . GLU B  1  68  ? 5.761   -4.727  43.899 1.00 45.60  ? 81  GLU B CB  1 
ATOM   3124 C  CG  . GLU B  1  68  ? 4.498   -4.028  43.401 1.00 54.89  ? 81  GLU B CG  1 
ATOM   3125 C  CD  . GLU B  1  68  ? 3.805   -4.719  42.240 1.00 63.55  ? 81  GLU B CD  1 
ATOM   3126 O  OE1 . GLU B  1  68  ? 2.586   -4.979  42.354 1.00 63.30  ? 81  GLU B OE1 1 
ATOM   3127 O  OE2 . GLU B  1  68  ? 4.495   -5.003  41.231 1.00 66.97  ? 81  GLU B OE2 1 
ATOM   3128 N  N   . GLY B  1  69  ? 7.598   -6.738  45.455 1.00 36.97  ? 82  GLY B N   1 
ATOM   3129 C  CA  . GLY B  1  69  ? 8.958   -7.220  45.624 1.00 33.19  ? 82  GLY B CA  1 
ATOM   3130 C  C   . GLY B  1  69  ? 9.036   -8.712  45.953 1.00 33.56  ? 82  GLY B C   1 
ATOM   3131 O  O   . GLY B  1  69  ? 9.967   -9.375  45.505 1.00 35.74  ? 82  GLY B O   1 
ATOM   3132 N  N   . PHE B  1  70  ? 8.094   -9.217  46.766 1.00 34.00  ? 83  PHE B N   1 
ATOM   3133 C  CA  . PHE B  1  70  ? 8.206   -10.544 47.353 1.00 34.18  ? 83  PHE B CA  1 
ATOM   3134 C  C   . PHE B  1  70  ? 6.945   -11.391 47.164 1.00 35.05  ? 83  PHE B C   1 
ATOM   3135 O  O   . PHE B  1  70  ? 6.949   -12.564 47.527 1.00 36.93  ? 83  PHE B O   1 
ATOM   3136 C  CB  . PHE B  1  70  ? 8.535   -10.420 48.851 1.00 35.30  ? 83  PHE B CB  1 
ATOM   3137 C  CG  . PHE B  1  70  ? 9.981   -10.096 49.215 1.00 34.98  ? 83  PHE B CG  1 
ATOM   3138 C  CD1 . PHE B  1  70  ? 10.997  -11.036 49.045 1.00 38.68  ? 83  PHE B CD1 1 
ATOM   3139 C  CD2 . PHE B  1  70  ? 10.323  -8.872  49.767 1.00 37.78  ? 83  PHE B CD2 1 
ATOM   3140 C  CE1 . PHE B  1  70  ? 12.311  -10.747 49.390 1.00 37.58  ? 83  PHE B CE1 1 
ATOM   3141 C  CE2 . PHE B  1  70  ? 11.642  -8.586  50.119 1.00 38.38  ? 83  PHE B CE2 1 
ATOM   3142 C  CZ  . PHE B  1  70  ? 12.629  -9.525  49.941 1.00 37.50  ? 83  PHE B CZ  1 
ATOM   3143 N  N   . ASN B  1  71  ? 5.867   -10.831 46.600 1.00 38.63  ? 84  ASN B N   1 
ATOM   3144 C  CA  . ASN B  1  71  ? 4.578   -11.516 46.499 1.00 37.90  ? 84  ASN B CA  1 
ATOM   3145 C  C   . ASN B  1  71  ? 4.027   -11.868 47.887 1.00 35.66  ? 84  ASN B C   1 
ATOM   3146 O  O   . ASN B  1  71  ? 3.412   -12.909 48.075 1.00 33.44  ? 84  ASN B O   1 
ATOM   3147 C  CB  . ASN B  1  71  ? 4.654   -12.749 45.601 1.00 40.51  ? 84  ASN B CB  1 
ATOM   3148 C  CG  . ASN B  1  71  ? 3.444   -12.902 44.699 1.00 40.75  ? 84  ASN B CG  1 
ATOM   3149 O  OD1 . ASN B  1  71  ? 2.400   -12.270 44.913 1.00 42.25  ? 84  ASN B OD1 1 
ATOM   3150 N  ND2 . ASN B  1  71  ? 3.564   -13.729 43.673 1.00 40.48  ? 84  ASN B ND2 1 
ATOM   3151 N  N   . PHE B  1  72  ? 4.250   -10.997 48.873 1.00 35.26  ? 85  PHE B N   1 
ATOM   3152 C  CA  . PHE B  1  72  ? 3.656   -11.173 50.190 1.00 35.16  ? 85  PHE B CA  1 
ATOM   3153 C  C   . PHE B  1  72  ? 2.138   -11.096 50.036 1.00 35.68  ? 85  PHE B C   1 
ATOM   3154 O  O   . PHE B  1  72  ? 1.626   -10.214 49.367 1.00 33.41  ? 85  PHE B O   1 
ATOM   3155 C  CB  . PHE B  1  72  ? 4.188   -10.098 51.141 1.00 37.27  ? 85  PHE B CB  1 
ATOM   3156 C  CG  . PHE B  1  72  ? 4.085   -10.367 52.638 1.00 36.01  ? 85  PHE B CG  1 
ATOM   3157 C  CD1 . PHE B  1  72  ? 4.369   -11.613 53.178 1.00 39.66  ? 85  PHE B CD1 1 
ATOM   3158 C  CD2 . PHE B  1  72  ? 3.722   -9.351  53.510 1.00 37.54  ? 85  PHE B CD2 1 
ATOM   3159 C  CE1 . PHE B  1  72  ? 4.282   -11.837 54.548 1.00 41.49  ? 85  PHE B CE1 1 
ATOM   3160 C  CE2 . PHE B  1  72  ? 3.642   -9.571  54.880 1.00 38.47  ? 85  PHE B CE2 1 
ATOM   3161 C  CZ  . PHE B  1  72  ? 3.904   -10.819 55.398 1.00 39.63  ? 85  PHE B CZ  1 
ATOM   3162 N  N   . GLU B  1  73  ? 1.413   -12.052 50.616 1.00 37.03  ? 86  GLU B N   1 
ATOM   3163 C  CA  . GLU B  1  73  ? -0.031  -12.117 50.448 1.00 40.26  ? 86  GLU B CA  1 
ATOM   3164 C  C   . GLU B  1  73  ? -0.697  -10.878 51.065 1.00 40.55  ? 86  GLU B C   1 
ATOM   3165 O  O   . GLU B  1  73  ? -0.286  -10.399 52.117 1.00 42.88  ? 86  GLU B O   1 
ATOM   3166 C  CB  . GLU B  1  73  ? -0.482  -13.457 51.022 1.00 41.44  ? 86  GLU B CB  1 
ATOM   3167 C  CG  . GLU B  1  73  ? -1.927  -13.810 50.691 1.00 48.19  ? 86  GLU B CG  1 
ATOM   3168 C  CD  . GLU B  1  73  ? -2.966  -13.191 51.612 1.00 54.58  ? 86  GLU B CD  1 
ATOM   3169 O  OE1 . GLU B  1  73  ? -3.998  -12.665 51.132 1.00 63.12  ? 86  GLU B OE1 1 
ATOM   3170 O  OE2 . GLU B  1  73  ? -2.719  -13.215 52.829 1.00 56.71  ? 86  GLU B OE2 1 
ATOM   3171 N  N   . ASN B  1  74  ? -1.733  -10.373 50.391 1.00 39.38  ? 87  ASN B N   1 
ATOM   3172 C  CA  . ASN B  1  74  ? -2.389  -9.104  50.699 1.00 39.68  ? 87  ASN B CA  1 
ATOM   3173 C  C   . ASN B  1  74  ? -2.828  -9.009  52.167 1.00 35.03  ? 87  ASN B C   1 
ATOM   3174 O  O   . ASN B  1  74  ? -2.556  -8.003  52.825 1.00 35.83  ? 87  ASN B O   1 
ATOM   3175 C  CB  . ASN B  1  74  ? -3.551  -8.876  49.729 1.00 38.42  ? 87  ASN B CB  1 
ATOM   3176 C  CG  . ASN B  1  74  ? -4.310  -7.595  49.976 1.00 37.37  ? 87  ASN B CG  1 
ATOM   3177 O  OD1 . ASN B  1  74  ? -5.489  -7.660  50.334 1.00 46.01  ? 87  ASN B OD1 1 
ATOM   3178 N  ND2 . ASN B  1  74  ? -3.684  -6.441  49.785 1.00 37.06  ? 87  ASN B ND2 1 
ATOM   3179 N  N   . ASN B  1  75  ? -3.508  -10.032 52.687 1.00 33.33  ? 88  ASN B N   1 
ATOM   3180 C  CA  . ASN B  1  75  ? -4.028  -9.966  54.047 1.00 40.19  ? 88  ASN B CA  1 
ATOM   3181 C  C   . ASN B  1  75  ? -2.883  -9.979  55.058 1.00 42.77  ? 88  ASN B C   1 
ATOM   3182 O  O   . ASN B  1  75  ? -2.944  -9.251  56.046 1.00 40.27  ? 88  ASN B O   1 
ATOM   3183 C  CB  . ASN B  1  75  ? -5.060  -11.052 54.350 1.00 46.85  ? 88  ASN B CB  1 
ATOM   3184 C  CG  . ASN B  1  75  ? -6.396  -10.779 53.694 1.00 52.46  ? 88  ASN B CG  1 
ATOM   3185 O  OD1 . ASN B  1  75  ? -6.821  -9.624  53.604 1.00 50.18  ? 88  ASN B OD1 1 
ATOM   3186 N  ND2 . ASN B  1  75  ? -7.090  -11.818 53.240 1.00 60.61  ? 88  ASN B ND2 1 
ATOM   3187 N  N   . ALA B  1  76  ? -1.852  -10.798 54.803 1.00 41.00  ? 89  ALA B N   1 
ATOM   3188 C  CA  . ALA B  1  76  ? -0.669  -10.830 55.653 1.00 40.41  ? 89  ALA B CA  1 
ATOM   3189 C  C   . ALA B  1  76  ? 0.020   -9.464  55.663 1.00 37.25  ? 89  ALA B C   1 
ATOM   3190 O  O   . ALA B  1  76  ? 0.469   -9.006  56.710 1.00 39.09  ? 89  ALA B O   1 
ATOM   3191 C  CB  . ALA B  1  76  ? 0.271   -11.922 55.195 1.00 40.35  ? 89  ALA B CB  1 
ATOM   3192 N  N   . ALA B  1  77  ? 0.073   -8.799  54.507 1.00 33.93  ? 90  ALA B N   1 
ATOM   3193 C  CA  . ALA B  1  77  ? 0.661   -7.470  54.406 1.00 35.60  ? 90  ALA B CA  1 
ATOM   3194 C  C   . ALA B  1  77  ? -0.135  -6.457  55.235 1.00 37.52  ? 90  ALA B C   1 
ATOM   3195 O  O   . ALA B  1  77  ? 0.451   -5.613  55.916 1.00 37.28  ? 90  ALA B O   1 
ATOM   3196 C  CB  . ALA B  1  77  ? 0.755   -7.061  52.939 1.00 33.48  ? 90  ALA B CB  1 
ATOM   3197 N  N   . ILE B  1  78  ? -1.470  -6.540  55.168 1.00 38.67  ? 91  ILE B N   1 
ATOM   3198 C  CA  . ILE B  1  78  ? -2.334  -5.633  55.909 1.00 41.54  ? 91  ILE B CA  1 
ATOM   3199 C  C   . ILE B  1  78  ? -2.143  -5.858  57.411 1.00 38.35  ? 91  ILE B C   1 
ATOM   3200 O  O   . ILE B  1  78  ? -2.021  -4.905  58.172 1.00 35.36  ? 91  ILE B O   1 
ATOM   3201 C  CB  . ILE B  1  78  ? -3.803  -5.788  55.452 1.00 41.65  ? 91  ILE B CB  1 
ATOM   3202 C  CG1 . ILE B  1  78  ? -4.001  -5.226  54.039 1.00 42.10  ? 91  ILE B CG1 1 
ATOM   3203 C  CG2 . ILE B  1  78  ? -4.783  -5.142  56.432 1.00 38.73  ? 91  ILE B CG2 1 
ATOM   3204 C  CD1 . ILE B  1  78  ? -5.272  -5.695  53.340 1.00 44.27  ? 91  ILE B CD1 1 
ATOM   3205 N  N   . VAL B  1  79  ? -2.073  -7.118  57.836 1.00 36.68  ? 92  VAL B N   1 
ATOM   3206 C  CA  . VAL B  1  79  ? -1.991  -7.436  59.253 1.00 38.61  ? 92  VAL B CA  1 
ATOM   3207 C  C   . VAL B  1  79  ? -0.685  -6.907  59.842 1.00 39.40  ? 92  VAL B C   1 
ATOM   3208 O  O   . VAL B  1  79  ? -0.687  -6.324  60.929 1.00 38.56  ? 92  VAL B O   1 
ATOM   3209 C  CB  . VAL B  1  79  ? -2.155  -8.950  59.488 1.00 41.32  ? 92  VAL B CB  1 
ATOM   3210 C  CG1 . VAL B  1  79  ? -1.737  -9.369  60.893 1.00 43.64  ? 92  VAL B CG1 1 
ATOM   3211 C  CG2 . VAL B  1  79  ? -3.580  -9.392  59.187 1.00 41.35  ? 92  VAL B CG2 1 
ATOM   3212 N  N   . ALA B  1  80  ? 0.428   -7.131  59.127 1.00 41.27  ? 93  ALA B N   1 
ATOM   3213 C  CA  . ALA B  1  80  ? 1.743   -6.715  59.597 1.00 38.73  ? 93  ALA B CA  1 
ATOM   3214 C  C   . ALA B  1  80  ? 1.870   -5.196  59.523 1.00 37.81  ? 93  ALA B C   1 
ATOM   3215 O  O   . ALA B  1  80  ? 2.408   -4.570  60.440 1.00 35.29  ? 93  ALA B O   1 
ATOM   3216 C  CB  . ALA B  1  80  ? 2.832   -7.404  58.797 1.00 39.07  ? 93  ALA B CB  1 
ATOM   3217 N  N   . THR B  1  81  ? 1.373   -4.589  58.440 1.00 36.13  ? 94  THR B N   1 
ATOM   3218 C  CA  . THR B  1  81  ? 1.670   -3.180  58.216 1.00 39.42  ? 94  THR B CA  1 
ATOM   3219 C  C   . THR B  1  81  ? 0.943   -2.306  59.238 1.00 40.51  ? 94  THR B C   1 
ATOM   3220 O  O   . THR B  1  81  ? 1.556   -1.399  59.797 1.00 42.63  ? 94  THR B O   1 
ATOM   3221 C  CB  . THR B  1  81  ? 1.328   -2.786  56.784 1.00 37.18  ? 94  THR B CB  1 
ATOM   3222 O  OG1 . THR B  1  81  ? 2.211   -3.545  55.970 1.00 36.76  ? 94  THR B OG1 1 
ATOM   3223 C  CG2 . THR B  1  81  ? 1.548   -1.311  56.542 1.00 36.63  ? 94  THR B CG2 1 
ATOM   3224 N  N   . TYR B  1  82  ? -0.358  -2.550  59.469 1.00 42.00  ? 95  TYR B N   1 
ATOM   3225 C  CA  . TYR B  1  82  ? -1.146  -1.658  60.313 1.00 45.42  ? 95  TYR B CA  1 
ATOM   3226 C  C   . TYR B  1  82  ? -0.839  -1.942  61.789 1.00 43.88  ? 95  TYR B C   1 
ATOM   3227 O  O   . TYR B  1  82  ? -0.932  -1.041  62.614 1.00 44.11  ? 95  TYR B O   1 
ATOM   3228 C  CB  . TYR B  1  82  ? -2.638  -1.701  59.950 1.00 47.15  ? 95  TYR B CB  1 
ATOM   3229 C  CG  . TYR B  1  82  ? -2.926  -1.049  58.603 1.00 45.39  ? 95  TYR B CG  1 
ATOM   3230 C  CD1 . TYR B  1  82  ? -2.898  0.334   58.457 1.00 47.78  ? 95  TYR B CD1 1 
ATOM   3231 C  CD2 . TYR B  1  82  ? -3.194  -1.807  57.473 1.00 43.16  ? 95  TYR B CD2 1 
ATOM   3232 C  CE1 . TYR B  1  82  ? -3.133  0.937   57.229 1.00 43.86  ? 95  TYR B CE1 1 
ATOM   3233 C  CE2 . TYR B  1  82  ? -3.428  -1.218  56.238 1.00 42.69  ? 95  TYR B CE2 1 
ATOM   3234 C  CZ  . TYR B  1  82  ? -3.399  0.159   56.116 1.00 43.72  ? 95  TYR B CZ  1 
ATOM   3235 O  OH  . TYR B  1  82  ? -3.627  0.778   54.921 1.00 51.14  ? 95  TYR B OH  1 
ATOM   3236 N  N   . LEU B  1  83  ? -0.441  -3.175  62.122 1.00 42.38  ? 96  LEU B N   1 
ATOM   3237 C  CA  . LEU B  1  83  ? 0.114   -3.473  63.440 1.00 40.76  ? 96  LEU B CA  1 
ATOM   3238 C  C   . LEU B  1  83  ? 1.316   -2.568  63.713 1.00 42.11  ? 96  LEU B C   1 
ATOM   3239 O  O   . LEU B  1  83  ? 1.395   -1.900  64.751 1.00 37.26  ? 96  LEU B O   1 
ATOM   3240 C  CB  . LEU B  1  83  ? 0.508   -4.947  63.502 1.00 41.76  ? 96  LEU B CB  1 
ATOM   3241 C  CG  . LEU B  1  83  ? 1.261   -5.401  64.755 1.00 44.02  ? 96  LEU B CG  1 
ATOM   3242 C  CD1 . LEU B  1  83  ? 0.391   -5.286  65.985 1.00 42.47  ? 96  LEU B CD1 1 
ATOM   3243 C  CD2 . LEU B  1  83  ? 1.759   -6.833  64.587 1.00 48.91  ? 96  LEU B CD2 1 
ATOM   3244 N  N   . GLY B  1  84  ? 2.267   -2.572  62.772 1.00 39.01  ? 97  GLY B N   1 
ATOM   3245 C  CA  . GLY B  1  84  ? 3.462   -1.766  62.903 1.00 36.66  ? 97  GLY B CA  1 
ATOM   3246 C  C   . GLY B  1  84  ? 3.121   -0.278  62.980 1.00 38.39  ? 97  GLY B C   1 
ATOM   3247 O  O   . GLY B  1  84  ? 3.729   0.459   63.753 1.00 39.42  ? 97  GLY B O   1 
ATOM   3248 N  N   . HIS B  1  85  ? 2.152   0.163   62.172 1.00 38.68  ? 98  HIS B N   1 
ATOM   3249 C  CA  . HIS B  1  85  ? 1.797   1.574   62.108 1.00 39.85  ? 98  HIS B CA  1 
ATOM   3250 C  C   . HIS B  1  85  ? 1.034   2.022   63.364 1.00 41.79  ? 98  HIS B C   1 
ATOM   3251 O  O   . HIS B  1  85  ? 1.331   3.081   63.911 1.00 40.19  ? 98  HIS B O   1 
ATOM   3252 C  CB  . HIS B  1  85  ? 0.974   1.850   60.852 1.00 39.93  ? 98  HIS B CB  1 
ATOM   3253 C  CG  . HIS B  1  85  ? 0.713   3.293   60.601 1.00 37.98  ? 98  HIS B CG  1 
ATOM   3254 N  ND1 . HIS B  1  85  ? 1.744   4.204   60.547 1.00 41.35  ? 98  HIS B ND1 1 
ATOM   3255 C  CD2 . HIS B  1  85  ? -0.414  3.964   60.341 1.00 38.39  ? 98  HIS B CD2 1 
ATOM   3256 C  CE1 . HIS B  1  85  ? 1.248   5.397   60.269 1.00 41.90  ? 98  HIS B CE1 1 
ATOM   3257 N  NE2 . HIS B  1  85  ? -0.061  5.277   60.152 1.00 43.30  ? 98  HIS B NE2 1 
ATOM   3258 N  N   . LEU B  1  86  ? 0.036   1.244   63.807 1.00 40.34  ? 99  LEU B N   1 
ATOM   3259 C  CA  . LEU B  1  86  ? -0.762  1.616   64.974 1.00 41.37  ? 99  LEU B CA  1 
ATOM   3260 C  C   . LEU B  1  86  ? 0.151   1.826   66.182 1.00 41.68  ? 99  LEU B C   1 
ATOM   3261 O  O   . LEU B  1  86  ? 0.033   2.835   66.880 1.00 43.21  ? 99  LEU B O   1 
ATOM   3262 C  CB  . LEU B  1  86  ? -1.836  0.564   65.242 1.00 40.89  ? 99  LEU B CB  1 
ATOM   3263 C  CG  . LEU B  1  86  ? -3.060  0.598   64.319 1.00 39.73  ? 99  LEU B CG  1 
ATOM   3264 C  CD1 . LEU B  1  86  ? -3.887  -0.664  64.430 1.00 40.79  ? 99  LEU B CD1 1 
ATOM   3265 C  CD2 . LEU B  1  86  ? -3.918  1.802   64.644 1.00 44.41  ? 99  LEU B CD2 1 
ATOM   3266 N  N   . LEU B  1  87  ? 1.105   0.907   66.378 1.00 43.08  ? 100 LEU B N   1 
ATOM   3267 C  CA  . LEU B  1  87  ? 1.972   0.921   67.551 1.00 42.14  ? 100 LEU B CA  1 
ATOM   3268 C  C   . LEU B  1  87  ? 3.156   1.878   67.386 1.00 44.29  ? 100 LEU B C   1 
ATOM   3269 O  O   . LEU B  1  87  ? 3.591   2.474   68.372 1.00 43.03  ? 100 LEU B O   1 
ATOM   3270 C  CB  . LEU B  1  87  ? 2.472   -0.490  67.855 1.00 41.92  ? 100 LEU B CB  1 
ATOM   3271 C  CG  . LEU B  1  87  ? 1.401   -1.513  68.243 1.00 44.93  ? 100 LEU B CG  1 
ATOM   3272 C  CD1 . LEU B  1  87  ? 2.015   -2.889  68.427 1.00 44.03  ? 100 LEU B CD1 1 
ATOM   3273 C  CD2 . LEU B  1  87  ? 0.641   -1.106  69.489 1.00 46.42  ? 100 LEU B CD2 1 
ATOM   3274 N  N   . ASN B  1  88  ? 3.707   2.000   66.167 1.00 45.26  ? 101 ASN B N   1 
ATOM   3275 C  CA  . ASN B  1  88  ? 5.026   2.601   66.014 1.00 47.64  ? 101 ASN B CA  1 
ATOM   3276 C  C   . ASN B  1  88  ? 5.057   3.762   65.023 1.00 48.20  ? 101 ASN B C   1 
ATOM   3277 O  O   . ASN B  1  88  ? 6.112   4.372   64.847 1.00 48.76  ? 101 ASN B O   1 
ATOM   3278 C  CB  . ASN B  1  88  ? 6.075   1.587   65.561 1.00 47.76  ? 101 ASN B CB  1 
ATOM   3279 C  CG  . ASN B  1  88  ? 6.298   0.469   66.553 1.00 49.40  ? 101 ASN B CG  1 
ATOM   3280 O  OD1 . ASN B  1  88  ? 6.389   0.709   67.763 1.00 55.23  ? 101 ASN B OD1 1 
ATOM   3281 N  ND2 . ASN B  1  88  ? 6.416   -0.755  66.068 1.00 48.60  ? 101 ASN B ND2 1 
ATOM   3282 N  N   . GLY B  1  89  ? 3.925   4.058   64.371 1.00 48.87  ? 102 GLY B N   1 
ATOM   3283 C  CA  . GLY B  1  89  ? 3.905   5.046   63.302 1.00 47.37  ? 102 GLY B CA  1 
ATOM   3284 C  C   . GLY B  1  89  ? 3.247   6.352   63.746 1.00 49.68  ? 102 GLY B C   1 
ATOM   3285 O  O   . GLY B  1  89  ? 2.689   6.438   64.840 1.00 46.06  ? 102 GLY B O   1 
ATOM   3286 N  N   . ASN B  1  90  ? 3.314   7.352   62.863 1.00 45.67  ? 103 ASN B N   1 
ATOM   3287 C  CA  . ASN B  1  90  ? 2.650   8.625   63.062 1.00 44.37  ? 103 ASN B CA  1 
ATOM   3288 C  C   . ASN B  1  90  ? 1.335   8.616   62.294 1.00 46.82  ? 103 ASN B C   1 
ATOM   3289 O  O   . ASN B  1  90  ? 1.331   8.643   61.062 1.00 45.63  ? 103 ASN B O   1 
ATOM   3290 C  CB  . ASN B  1  90  ? 3.552   9.769   62.623 1.00 44.54  ? 103 ASN B CB  1 
ATOM   3291 C  CG  . ASN B  1  90  ? 3.015   11.116  63.032 1.00 44.85  ? 103 ASN B CG  1 
ATOM   3292 O  OD1 . ASN B  1  90  ? 1.843   11.422  62.789 1.00 47.70  ? 103 ASN B OD1 1 
ATOM   3293 N  ND2 . ASN B  1  90  ? 3.862   11.935  63.637 1.00 46.58  ? 103 ASN B ND2 1 
ATOM   3294 N  N   . LEU B  1  91  ? 0.220   8.612   63.036 1.00 50.05  ? 104 LEU B N   1 
ATOM   3295 C  CA  . LEU B  1  91  ? -1.090  8.397   62.442 1.00 52.87  ? 104 LEU B CA  1 
ATOM   3296 C  C   . LEU B  1  91  ? -1.603  9.664   61.769 1.00 48.62  ? 104 LEU B C   1 
ATOM   3297 O  O   . LEU B  1  91  ? -2.418  9.567   60.858 1.00 53.40  ? 104 LEU B O   1 
ATOM   3298 C  CB  . LEU B  1  91  ? -2.025  7.887   63.530 1.00 56.70  ? 104 LEU B CB  1 
ATOM   3299 C  CG  . LEU B  1  91  ? -1.584  6.569   64.170 1.00 59.16  ? 104 LEU B CG  1 
ATOM   3300 C  CD1 . LEU B  1  91  ? -2.367  6.296   65.421 1.00 64.80  ? 104 LEU B CD1 1 
ATOM   3301 C  CD2 . LEU B  1  91  ? -1.751  5.432   63.183 1.00 62.17  ? 104 LEU B CD2 1 
ATOM   3302 N  N   . VAL B  1  92  ? -1.073  10.826  62.165 1.00 47.24  ? 105 VAL B N   1 
ATOM   3303 C  CA  . VAL B  1  92  ? -1.484  12.106  61.604 1.00 52.34  ? 105 VAL B CA  1 
ATOM   3304 C  C   . VAL B  1  92  ? -0.842  12.296  60.231 1.00 50.35  ? 105 VAL B C   1 
ATOM   3305 O  O   . VAL B  1  92  ? -1.541  12.651  59.285 1.00 50.10  ? 105 VAL B O   1 
ATOM   3306 C  CB  . VAL B  1  92  ? -1.141  13.258  62.576 1.00 52.38  ? 105 VAL B CB  1 
ATOM   3307 C  CG1 . VAL B  1  92  ? -1.285  14.641  61.954 1.00 50.95  ? 105 VAL B CG1 1 
ATOM   3308 C  CG2 . VAL B  1  92  ? -1.977  13.169  63.843 1.00 56.31  ? 105 VAL B CG2 1 
ATOM   3309 N  N   . THR B  1  93  ? 0.475   12.034  60.128 1.00 51.00  ? 106 THR B N   1 
ATOM   3310 C  CA  . THR B  1  93  ? 1.195   12.189  58.869 1.00 51.45  ? 106 THR B CA  1 
ATOM   3311 C  C   . THR B  1  93  ? 1.116   10.923  58.012 1.00 49.21  ? 106 THR B C   1 
ATOM   3312 O  O   . THR B  1  93  ? 1.428   10.994  56.829 1.00 51.45  ? 106 THR B O   1 
ATOM   3313 C  CB  . THR B  1  93  ? 2.647   12.570  59.127 1.00 54.43  ? 106 THR B CB  1 
ATOM   3314 O  OG1 . THR B  1  93  ? 3.240   11.488  59.837 1.00 56.59  ? 106 THR B OG1 1 
ATOM   3315 C  CG2 . THR B  1  93  ? 2.774   13.857  59.921 1.00 55.86  ? 106 THR B CG2 1 
ATOM   3316 N  N   . ASP B  1  94  ? 0.706   9.785   58.599 1.00 42.93  ? 107 ASP B N   1 
ATOM   3317 C  CA  . ASP B  1  94  ? 0.559   8.532   57.873 1.00 45.27  ? 107 ASP B CA  1 
ATOM   3318 C  C   . ASP B  1  94  ? 1.929   8.003   57.440 1.00 46.76  ? 107 ASP B C   1 
ATOM   3319 O  O   . ASP B  1  94  ? 2.055   7.456   56.352 1.00 47.92  ? 107 ASP B O   1 
ATOM   3320 C  CB  . ASP B  1  94  ? -0.381  8.693   56.689 1.00 45.12  ? 107 ASP B CB  1 
ATOM   3321 C  CG  . ASP B  1  94  ? -0.981  7.406   56.141 1.00 50.22  ? 107 ASP B CG  1 
ATOM   3322 O  OD1 . ASP B  1  94  ? -1.368  6.543   56.971 1.00 49.60  ? 107 ASP B OD1 1 
ATOM   3323 O  OD2 . ASP B  1  94  ? -1.081  7.292   54.893 1.00 51.58  ? 107 ASP B OD2 1 
ATOM   3324 N  N   . LEU B  1  95  ? 2.938   8.162   58.305 1.00 43.51  ? 108 LEU B N   1 
ATOM   3325 C  CA  . LEU B  1  95  ? 4.307   7.776   58.010 1.00 47.90  ? 108 LEU B CA  1 
ATOM   3326 C  C   . LEU B  1  95  ? 4.841   6.869   59.115 1.00 44.80  ? 108 LEU B C   1 
ATOM   3327 O  O   . LEU B  1  95  ? 4.644   7.148   60.289 1.00 41.00  ? 108 LEU B O   1 
ATOM   3328 C  CB  . LEU B  1  95  ? 5.201   9.005   57.854 1.00 47.57  ? 108 LEU B CB  1 
ATOM   3329 C  CG  . LEU B  1  95  ? 4.889   9.938   56.681 1.00 47.31  ? 108 LEU B CG  1 
ATOM   3330 C  CD1 . LEU B  1  95  ? 5.814   11.139  56.759 1.00 46.69  ? 108 LEU B CD1 1 
ATOM   3331 C  CD2 . LEU B  1  95  ? 5.022   9.262   55.339 1.00 48.46  ? 108 LEU B CD2 1 
ATOM   3332 N  N   . LEU B  1  96  ? 5.554   5.810   58.697 1.00 43.82  ? 109 LEU B N   1 
ATOM   3333 C  CA  . LEU B  1  96  ? 6.181   4.832   59.570 1.00 41.87  ? 109 LEU B CA  1 
ATOM   3334 C  C   . LEU B  1  96  ? 7.652   4.679   59.181 1.00 42.49  ? 109 LEU B C   1 
ATOM   3335 O  O   . LEU B  1  96  ? 7.976   4.512   58.007 1.00 42.99  ? 109 LEU B O   1 
ATOM   3336 C  CB  . LEU B  1  96  ? 5.423   3.507   59.435 1.00 39.55  ? 109 LEU B CB  1 
ATOM   3337 C  CG  . LEU B  1  96  ? 6.064   2.295   60.116 1.00 40.12  ? 109 LEU B CG  1 
ATOM   3338 C  CD1 . LEU B  1  96  ? 6.247   2.533   61.606 1.00 42.14  ? 109 LEU B CD1 1 
ATOM   3339 C  CD2 . LEU B  1  96  ? 5.246   1.036   59.883 1.00 40.45  ? 109 LEU B CD2 1 
ATOM   3340 N  N   . SER B  1  97  ? 8.531   4.739   60.187 1.00 43.76  ? 110 SER B N   1 
ATOM   3341 C  CA  . SER B  1  97  ? 9.944   4.426   60.056 1.00 40.99  ? 110 SER B CA  1 
ATOM   3342 C  C   . SER B  1  97  ? 10.145  2.920   60.200 1.00 44.88  ? 110 SER B C   1 
ATOM   3343 O  O   . SER B  1  97  ? 9.598   2.322   61.129 1.00 39.20  ? 110 SER B O   1 
ATOM   3344 C  CB  . SER B  1  97  ? 10.751  5.164   61.081 1.00 42.00  ? 110 SER B CB  1 
ATOM   3345 O  OG  . SER B  1  97  ? 12.062  4.627   61.223 1.00 38.58  ? 110 SER B OG  1 
ATOM   3346 N  N   . ILE B  1  98  ? 10.939  2.318   59.290 1.00 39.76  ? 111 ILE B N   1 
ATOM   3347 C  CA  . ILE B  1  98  ? 11.183  0.888   59.342 1.00 38.05  ? 111 ILE B CA  1 
ATOM   3348 C  C   . ILE B  1  98  ? 12.296  0.588   60.341 1.00 37.75  ? 111 ILE B C   1 
ATOM   3349 O  O   . ILE B  1  98  ? 12.636  -0.576  60.541 1.00 41.48  ? 111 ILE B O   1 
ATOM   3350 C  CB  . ILE B  1  98  ? 11.476  0.291   57.953 1.00 39.30  ? 111 ILE B CB  1 
ATOM   3351 C  CG1 . ILE B  1  98  ? 12.752  0.843   57.316 1.00 34.26  ? 111 ILE B CG1 1 
ATOM   3352 C  CG2 . ILE B  1  98  ? 10.255  0.441   57.041 1.00 40.52  ? 111 ILE B CG2 1 
ATOM   3353 C  CD1 . ILE B  1  98  ? 13.169  0.103   56.064 1.00 36.78  ? 111 ILE B CD1 1 
ATOM   3354 N  N   . GLY B  1  99  ? 12.855  1.636   60.956 1.00 40.50  ? 112 GLY B N   1 
ATOM   3355 C  CA  . GLY B  1  99  ? 13.882  1.488   61.978 1.00 44.57  ? 112 GLY B CA  1 
ATOM   3356 C  C   . GLY B  1  99  ? 13.571  2.320   63.220 1.00 48.44  ? 112 GLY B C   1 
ATOM   3357 O  O   . GLY B  1  99  ? 12.538  2.117   63.858 1.00 48.26  ? 112 GLY B O   1 
ATOM   3358 N  N   . GLY B  1  100 ? 14.483  3.244   63.555 1.00 49.78  ? 113 GLY B N   1 
ATOM   3359 C  CA  . GLY B  1  100 ? 14.375  4.049   64.763 1.00 51.27  ? 113 GLY B CA  1 
ATOM   3360 C  C   . GLY B  1  100 ? 13.675  5.390   64.525 1.00 48.44  ? 113 GLY B C   1 
ATOM   3361 O  O   . GLY B  1  100 ? 13.157  5.648   63.444 1.00 45.35  ? 113 GLY B O   1 
ATOM   3362 N  N   . ALA B  1  101 ? 13.693  6.254   65.546 1.00 52.75  ? 114 ALA B N   1 
ATOM   3363 C  CA  . ALA B  1  101 ? 12.958  7.511   65.530 1.00 53.90  ? 114 ALA B CA  1 
ATOM   3364 C  C   . ALA B  1  101 ? 13.634  8.505   64.594 1.00 54.51  ? 114 ALA B C   1 
ATOM   3365 O  O   . ALA B  1  101 ? 14.851  8.505   64.457 1.00 57.90  ? 114 ALA B O   1 
ATOM   3366 C  CB  . ALA B  1  101 ? 12.856  8.077   66.927 1.00 52.33  ? 114 ALA B CB  1 
ATOM   3367 N  N   . THR B  1  102 ? 12.829  9.374   63.984 1.00 52.94  ? 115 THR B N   1 
ATOM   3368 C  CA  . THR B  1  102 ? 13.324  10.294  62.981 1.00 51.41  ? 115 THR B CA  1 
ATOM   3369 C  C   . THR B  1  102 ? 12.338  11.444  62.834 1.00 51.43  ? 115 THR B C   1 
ATOM   3370 O  O   . THR B  1  102 ? 11.132  11.220  62.860 1.00 54.63  ? 115 THR B O   1 
ATOM   3371 C  CB  . THR B  1  102 ? 13.527  9.543   61.661 1.00 48.88  ? 115 THR B CB  1 
ATOM   3372 O  OG1 . THR B  1  102 ? 13.859  10.518  60.679 1.00 50.25  ? 115 THR B OG1 1 
ATOM   3373 C  CG2 . THR B  1  102 ? 12.294  8.794   61.185 1.00 48.98  ? 115 THR B CG2 1 
ATOM   3374 N  N   . PRO B  1  103 ? 12.817  12.692  62.635 1.00 53.68  ? 116 PRO B N   1 
ATOM   3375 C  CA  . PRO B  1  103 ? 11.938  13.803  62.258 1.00 56.44  ? 116 PRO B CA  1 
ATOM   3376 C  C   . PRO B  1  103 ? 11.203  13.622  60.928 1.00 59.25  ? 116 PRO B C   1 
ATOM   3377 O  O   . PRO B  1  103 ? 10.195  14.281  60.693 1.00 59.64  ? 116 PRO B O   1 
ATOM   3378 C  CB  . PRO B  1  103 ? 12.897  15.018  62.226 1.00 58.87  ? 116 PRO B CB  1 
ATOM   3379 C  CG  . PRO B  1  103 ? 14.280  14.426  62.031 1.00 55.13  ? 116 PRO B CG  1 
ATOM   3380 C  CD  . PRO B  1  103 ? 14.224  13.102  62.777 1.00 56.78  ? 116 PRO B CD  1 
ATOM   3381 N  N   . LYS B  1  104 ? 11.701  12.720  60.068 1.00 58.99  ? 117 LYS B N   1 
ATOM   3382 C  CA  . LYS B  1  104 ? 11.091  12.441  58.773 1.00 54.73  ? 117 LYS B CA  1 
ATOM   3383 C  C   . LYS B  1  104 ? 9.638   11.969  58.917 1.00 50.39  ? 117 LYS B C   1 
ATOM   3384 O  O   . LYS B  1  104 ? 8.865   12.131  57.983 1.00 49.85  ? 117 LYS B O   1 
ATOM   3385 C  CB  . LYS B  1  104 ? 11.930  11.422  57.988 1.00 56.66  ? 117 LYS B CB  1 
ATOM   3386 C  CG  . LYS B  1  104 ? 13.253  11.926  57.419 1.00 59.09  ? 117 LYS B CG  1 
ATOM   3387 C  CD  . LYS B  1  104 ? 14.236  10.832  57.010 1.00 62.47  ? 117 LYS B CD  1 
ATOM   3388 C  CE  . LYS B  1  104 ? 15.480  11.351  56.349 1.00 64.80  ? 117 LYS B CE  1 
ATOM   3389 N  NZ  . LYS B  1  104 ? 15.244  11.792  54.969 1.00 67.05  ? 117 LYS B NZ  1 
ATOM   3390 N  N   . THR B  1  105 ? 9.253   11.373  60.059 1.00 50.90  ? 118 THR B N   1 
ATOM   3391 C  CA  . THR B  1  105 ? 7.864   10.965  60.254 1.00 50.93  ? 118 THR B CA  1 
ATOM   3392 C  C   . THR B  1  105 ? 7.016   12.144  60.729 1.00 51.04  ? 118 THR B C   1 
ATOM   3393 O  O   . THR B  1  105 ? 5.802   12.013  60.860 1.00 53.96  ? 118 THR B O   1 
ATOM   3394 C  CB  . THR B  1  105 ? 7.721   9.791   61.221 1.00 49.20  ? 118 THR B CB  1 
ATOM   3395 O  OG1 . THR B  1  105 ? 8.310   10.156  62.464 1.00 46.99  ? 118 THR B OG1 1 
ATOM   3396 C  CG2 . THR B  1  105 ? 8.358   8.525   60.689 1.00 50.64  ? 118 THR B CG2 1 
ATOM   3397 N  N   . GLY B  1  106 ? 7.662   13.275  61.024 1.00 56.73  ? 119 GLY B N   1 
ATOM   3398 C  CA  . GLY B  1  106 ? 6.955   14.527  61.249 1.00 59.59  ? 119 GLY B CA  1 
ATOM   3399 C  C   . GLY B  1  106 ? 6.823   14.856  62.733 1.00 62.39  ? 119 GLY B C   1 
ATOM   3400 O  O   . GLY B  1  106 ? 7.374   14.161  63.585 1.00 65.00  ? 119 GLY B O   1 
ATOM   3401 N  N   . PRO B  1  107 ? 6.089   15.938  63.081 1.00 67.92  ? 120 PRO B N   1 
ATOM   3402 C  CA  . PRO B  1  107 ? 5.901   16.327  64.479 1.00 69.95  ? 120 PRO B CA  1 
ATOM   3403 C  C   . PRO B  1  107 ? 5.456   15.161  65.366 1.00 65.60  ? 120 PRO B C   1 
ATOM   3404 O  O   . PRO B  1  107 ? 4.516   14.435  65.047 1.00 60.79  ? 120 PRO B O   1 
ATOM   3405 C  CB  . PRO B  1  107 ? 4.829   17.435  64.391 1.00 72.71  ? 120 PRO B CB  1 
ATOM   3406 C  CG  . PRO B  1  107 ? 4.997   18.020  63.006 1.00 71.95  ? 120 PRO B CG  1 
ATOM   3407 C  CD  . PRO B  1  107 ? 5.406   16.843  62.142 1.00 73.59  ? 120 PRO B CD  1 
ATOM   3408 N  N   . PRO B  1  108 ? 6.121   14.933  66.516 1.00 61.73  ? 121 PRO B N   1 
ATOM   3409 C  CA  . PRO B  1  108 ? 5.805   13.779  67.359 1.00 65.27  ? 121 PRO B CA  1 
ATOM   3410 C  C   . PRO B  1  108 ? 4.392   13.799  67.940 1.00 66.96  ? 121 PRO B C   1 
ATOM   3411 O  O   . PRO B  1  108 ? 3.813   14.857  68.159 1.00 74.53  ? 121 PRO B O   1 
ATOM   3412 C  CB  . PRO B  1  108 ? 6.889   13.858  68.445 1.00 68.17  ? 121 PRO B CB  1 
ATOM   3413 C  CG  . PRO B  1  108 ? 7.223   15.334  68.505 1.00 71.25  ? 121 PRO B CG  1 
ATOM   3414 C  CD  . PRO B  1  108 ? 7.209   15.764  67.053 1.00 65.68  ? 121 PRO B CD  1 
ATOM   3415 N  N   . PRO B  1  109 ? 3.773   12.623  68.172 1.00 66.32  ? 122 PRO B N   1 
ATOM   3416 C  CA  . PRO B  1  109 ? 2.431   12.563  68.745 1.00 66.67  ? 122 PRO B CA  1 
ATOM   3417 C  C   . PRO B  1  109 ? 2.470   12.864  70.240 1.00 66.51  ? 122 PRO B C   1 
ATOM   3418 O  O   . PRO B  1  109 ? 3.532   12.871  70.856 1.00 65.19  ? 122 PRO B O   1 
ATOM   3419 C  CB  . PRO B  1  109 ? 2.005   11.111  68.460 1.00 69.74  ? 122 PRO B CB  1 
ATOM   3420 C  CG  . PRO B  1  109 ? 3.311   10.337  68.449 1.00 66.39  ? 122 PRO B CG  1 
ATOM   3421 C  CD  . PRO B  1  109 ? 4.323   11.292  67.863 1.00 65.74  ? 122 PRO B CD  1 
ATOM   3422 N  N   . PRO B  1  110 ? 1.309   13.093  70.887 1.00 68.34  ? 123 PRO B N   1 
ATOM   3423 C  CA  . PRO B  1  110 ? 1.286   13.338  72.328 1.00 63.97  ? 123 PRO B CA  1 
ATOM   3424 C  C   . PRO B  1  110 ? 1.638   12.075  73.119 1.00 59.14  ? 123 PRO B C   1 
ATOM   3425 O  O   . PRO B  1  110 ? 1.162   10.982  72.813 1.00 55.45  ? 123 PRO B O   1 
ATOM   3426 C  CB  . PRO B  1  110 ? -0.146  13.851  72.586 1.00 68.84  ? 123 PRO B CB  1 
ATOM   3427 C  CG  . PRO B  1  110 ? -0.970  13.269  71.461 1.00 73.04  ? 123 PRO B CG  1 
ATOM   3428 C  CD  . PRO B  1  110 ? -0.028  13.125  70.274 1.00 74.13  ? 123 PRO B CD  1 
ATOM   3429 N  N   . PRO B  1  111 ? 2.524   12.170  74.130 1.00 54.93  ? 124 PRO B N   1 
ATOM   3430 C  CA  . PRO B  1  111 ? 2.855   11.019  74.970 1.00 60.22  ? 124 PRO B CA  1 
ATOM   3431 C  C   . PRO B  1  111 ? 1.602   10.436  75.624 1.00 63.02  ? 124 PRO B C   1 
ATOM   3432 O  O   . PRO B  1  111 ? 0.641   11.158  75.867 1.00 59.12  ? 124 PRO B O   1 
ATOM   3433 C  CB  . PRO B  1  111 ? 3.834   11.598  76.017 1.00 58.79  ? 124 PRO B CB  1 
ATOM   3434 C  CG  . PRO B  1  111 ? 4.383   12.854  75.377 1.00 61.03  ? 124 PRO B CG  1 
ATOM   3435 C  CD  . PRO B  1  111 ? 3.276   13.378  74.490 1.00 59.34  ? 124 PRO B CD  1 
ATOM   3436 N  N   . PRO B  1  112 ? 1.553   9.121   75.942 1.00 60.93  ? 125 PRO B N   1 
ATOM   3437 C  CA  . PRO B  1  112 ? 2.684   8.198   75.744 1.00 52.92  ? 125 PRO B CA  1 
ATOM   3438 C  C   . PRO B  1  112 ? 2.967   7.602   74.359 1.00 53.24  ? 125 PRO B C   1 
ATOM   3439 O  O   . PRO B  1  112 ? 3.860   6.765   74.242 1.00 61.98  ? 125 PRO B O   1 
ATOM   3440 C  CB  . PRO B  1  112 ? 2.321   7.096   76.759 1.00 53.30  ? 125 PRO B CB  1 
ATOM   3441 C  CG  . PRO B  1  112 ? 0.814   7.049   76.713 1.00 57.08  ? 125 PRO B CG  1 
ATOM   3442 C  CD  . PRO B  1  112 ? 0.379   8.482   76.560 1.00 56.46  ? 125 PRO B CD  1 
ATOM   3443 N  N   . ALA B  1  113 ? 2.219   8.003   73.318 1.00 52.40  ? 126 ALA B N   1 
ATOM   3444 C  CA  . ALA B  1  113 ? 2.545   7.605   71.954 1.00 53.80  ? 126 ALA B CA  1 
ATOM   3445 C  C   . ALA B  1  113 ? 3.916   8.164   71.570 1.00 57.51  ? 126 ALA B C   1 
ATOM   3446 O  O   . ALA B  1  113 ? 4.352   9.160   72.152 1.00 53.71  ? 126 ALA B O   1 
ATOM   3447 C  CB  . ALA B  1  113 ? 1.462   8.050   71.004 1.00 53.68  ? 126 ALA B CB  1 
ATOM   3448 N  N   . HIS B  1  114 ? 4.585   7.531   70.591 1.00 60.31  ? 127 HIS B N   1 
ATOM   3449 C  CA  . HIS B  1  114 ? 5.979   7.854   70.310 1.00 54.81  ? 127 HIS B CA  1 
ATOM   3450 C  C   . HIS B  1  114 ? 6.303   7.936   68.820 1.00 51.79  ? 127 HIS B C   1 
ATOM   3451 O  O   . HIS B  1  114 ? 7.186   8.708   68.461 1.00 55.25  ? 127 HIS B O   1 
ATOM   3452 C  CB  . HIS B  1  114 ? 6.901   6.862   71.024 1.00 51.86  ? 127 HIS B CB  1 
ATOM   3453 C  CG  . HIS B  1  114 ? 6.499   5.433   70.873 1.00 51.69  ? 127 HIS B CG  1 
ATOM   3454 N  ND1 . HIS B  1  114 ? 6.758   4.699   69.734 1.00 56.37  ? 127 HIS B ND1 1 
ATOM   3455 C  CD2 . HIS B  1  114 ? 5.849   4.606   71.703 1.00 49.95  ? 127 HIS B CD2 1 
ATOM   3456 C  CE1 . HIS B  1  114 ? 6.295   3.462   69.886 1.00 53.33  ? 127 HIS B CE1 1 
ATOM   3457 N  NE2 . HIS B  1  114 ? 5.748   3.373   71.075 1.00 48.02  ? 127 HIS B NE2 1 
ATOM   3458 N  N   . ALA B  1  115 ? 5.615   7.159   67.967 1.00 53.10  ? 128 ALA B N   1 
ATOM   3459 C  CA  . ALA B  1  115 ? 5.981   7.027   66.560 1.00 56.22  ? 128 ALA B CA  1 
ATOM   3460 C  C   . ALA B  1  115 ? 7.488   6.767   66.414 1.00 49.73  ? 128 ALA B C   1 
ATOM   3461 O  O   . ALA B  1  115 ? 8.159   7.400   65.611 1.00 46.37  ? 128 ALA B O   1 
ATOM   3462 C  CB  . ALA B  1  115 ? 5.533   8.245   65.779 1.00 58.77  ? 128 ALA B CB  1 
ATOM   3463 N  N   . GLY B  1  116 ? 7.991   5.779   67.167 1.00 49.48  ? 129 GLY B N   1 
ATOM   3464 C  CA  . GLY B  1  116 ? 9.418   5.542   67.316 1.00 48.70  ? 129 GLY B CA  1 
ATOM   3465 C  C   . GLY B  1  116 ? 9.997   4.540   66.310 1.00 44.44  ? 129 GLY B C   1 
ATOM   3466 O  O   . GLY B  1  116 ? 11.202  4.329   66.309 1.00 44.91  ? 129 GLY B O   1 
ATOM   3467 N  N   . GLY B  1  117 ? 9.139   3.923   65.483 1.00 43.95  ? 130 GLY B N   1 
ATOM   3468 C  CA  . GLY B  1  117 ? 9.567   3.067   64.389 1.00 41.40  ? 130 GLY B CA  1 
ATOM   3469 C  C   . GLY B  1  117 ? 9.568   1.593   64.790 1.00 39.03  ? 130 GLY B C   1 
ATOM   3470 O  O   . GLY B  1  117 ? 9.289   1.275   65.941 1.00 38.39  ? 130 GLY B O   1 
ATOM   3471 N  N   . LEU B  1  118 ? 9.921   0.711   63.837 1.00 39.15  ? 131 LEU B N   1 
ATOM   3472 C  CA  . LEU B  1  118 ? 9.855   -0.732  64.033 1.00 40.00  ? 131 LEU B CA  1 
ATOM   3473 C  C   . LEU B  1  118 ? 10.885  -1.211  65.059 1.00 37.93  ? 131 LEU B C   1 
ATOM   3474 O  O   . LEU B  1  118 ? 10.774  -2.331  65.552 1.00 42.68  ? 131 LEU B O   1 
ATOM   3475 C  CB  . LEU B  1  118 ? 9.994   -1.461  62.695 1.00 38.05  ? 131 LEU B CB  1 
ATOM   3476 C  CG  . LEU B  1  118 ? 8.842   -1.263  61.706 1.00 40.64  ? 131 LEU B CG  1 
ATOM   3477 C  CD1 . LEU B  1  118 ? 9.065   -2.110  60.463 1.00 38.41  ? 131 LEU B CD1 1 
ATOM   3478 C  CD2 . LEU B  1  118 ? 7.499   -1.592  62.365 1.00 42.22  ? 131 LEU B CD2 1 
ATOM   3479 N  N   . ASN B  1  119 ? 11.870  -0.365  65.380 1.00 36.81  ? 132 ASN B N   1 
ATOM   3480 C  CA  . ASN B  1  119 ? 12.886  -0.670  66.377 1.00 40.06  ? 132 ASN B CA  1 
ATOM   3481 C  C   . ASN B  1  119 ? 12.334  -0.709  67.805 1.00 42.86  ? 132 ASN B C   1 
ATOM   3482 O  O   . ASN B  1  119 ? 13.004  -1.239  68.685 1.00 41.15  ? 132 ASN B O   1 
ATOM   3483 C  CB  . ASN B  1  119 ? 14.005  0.368   66.409 1.00 42.96  ? 132 ASN B CB  1 
ATOM   3484 C  CG  . ASN B  1  119 ? 15.058  0.191   65.342 1.00 46.39  ? 132 ASN B CG  1 
ATOM   3485 O  OD1 . ASN B  1  119 ? 14.946  -0.670  64.462 1.00 46.67  ? 132 ASN B OD1 1 
ATOM   3486 N  ND2 . ASN B  1  119 ? 16.086  1.025   65.394 1.00 46.67  ? 132 ASN B ND2 1 
ATOM   3487 N  N   . VAL B  1  120 ? 11.167  -0.104  68.071 1.00 42.59  ? 133 VAL B N   1 
ATOM   3488 C  CA  . VAL B  1  120 ? 10.649  -0.059  69.434 1.00 46.22  ? 133 VAL B CA  1 
ATOM   3489 C  C   . VAL B  1  120 ? 10.371  -1.482  69.928 1.00 47.87  ? 133 VAL B C   1 
ATOM   3490 O  O   . VAL B  1  120 ? 9.578   -2.211  69.337 1.00 46.91  ? 133 VAL B O   1 
ATOM   3491 C  CB  . VAL B  1  120 ? 9.403   0.842   69.568 1.00 46.29  ? 133 VAL B CB  1 
ATOM   3492 C  CG1 . VAL B  1  120 ? 8.743   0.740   70.945 1.00 44.15  ? 133 VAL B CG1 1 
ATOM   3493 C  CG2 . VAL B  1  120 ? 9.725   2.299   69.265 1.00 47.15  ? 133 VAL B CG2 1 
ATOM   3494 N  N   . HIS B  1  121 ? 11.030  -1.852  71.037 1.00 48.82  ? 134 HIS B N   1 
ATOM   3495 C  CA  . HIS B  1  121 ? 10.908  -3.171  71.636 1.00 48.40  ? 134 HIS B CA  1 
ATOM   3496 C  C   . HIS B  1  121 ? 9.681   -3.232  72.540 1.00 48.23  ? 134 HIS B C   1 
ATOM   3497 O  O   . HIS B  1  121 ? 9.344   -2.247  73.194 1.00 44.77  ? 134 HIS B O   1 
ATOM   3498 C  CB  . HIS B  1  121 ? 12.170  -3.479  72.456 1.00 49.16  ? 134 HIS B CB  1 
ATOM   3499 C  CG  . HIS B  1  121 ? 12.116  -4.765  73.216 1.00 50.13  ? 134 HIS B CG  1 
ATOM   3500 N  ND1 . HIS B  1  121 ? 12.236  -5.998  72.610 1.00 48.63  ? 134 HIS B ND1 1 
ATOM   3501 C  CD2 . HIS B  1  121 ? 11.926  -5.011  74.514 1.00 47.49  ? 134 HIS B CD2 1 
ATOM   3502 C  CE1 . HIS B  1  121 ? 12.154  -6.951  73.529 1.00 47.97  ? 134 HIS B CE1 1 
ATOM   3503 N  NE2 . HIS B  1  121 ? 11.952  -6.373  74.691 1.00 48.36  ? 134 HIS B NE2 1 
ATOM   3504 N  N   . GLY B  1  122 ? 9.025   -4.394  72.604 1.00 49.92  ? 135 GLY B N   1 
ATOM   3505 C  CA  . GLY B  1  122 ? 8.050   -4.604  73.659 1.00 56.33  ? 135 GLY B CA  1 
ATOM   3506 C  C   . GLY B  1  122 ? 6.684   -5.081  73.172 1.00 57.62  ? 135 GLY B C   1 
ATOM   3507 O  O   . GLY B  1  122 ? 6.079   -5.923  73.838 1.00 66.99  ? 135 GLY B O   1 
ATOM   3508 N  N   . THR B  1  123 ? 6.158   -4.510  72.081 1.00 58.03  ? 136 THR B N   1 
ATOM   3509 C  CA  . THR B  1  123 ? 4.833   -4.934  71.635 1.00 64.57  ? 136 THR B CA  1 
ATOM   3510 C  C   . THR B  1  123 ? 4.876   -5.559  70.237 1.00 60.88  ? 136 THR B C   1 
ATOM   3511 O  O   . THR B  1  123 ? 4.177   -6.547  70.029 1.00 63.74  ? 136 THR B O   1 
ATOM   3512 C  CB  . THR B  1  123 ? 3.809   -3.803  71.729 1.00 70.13  ? 136 THR B CB  1 
ATOM   3513 O  OG1 . THR B  1  123 ? 4.083   -3.069  72.916 1.00 64.39  ? 136 THR B OG1 1 
ATOM   3514 C  CG2 . THR B  1  123 ? 2.386   -4.331  71.824 1.00 68.52  ? 136 THR B CG2 1 
ATOM   3515 N  N   . PHE B  1  124 ? 5.686   -5.027  69.302 1.00 52.36  ? 137 PHE B N   1 
ATOM   3516 C  CA  . PHE B  1  124 ? 5.934   -5.727  68.041 1.00 52.48  ? 137 PHE B CA  1 
ATOM   3517 C  C   . PHE B  1  124 ? 7.289   -6.452  68.060 1.00 49.52  ? 137 PHE B C   1 
ATOM   3518 O  O   . PHE B  1  124 ? 7.335   -7.670  68.237 1.00 48.60  ? 137 PHE B O   1 
ATOM   3519 C  CB  . PHE B  1  124 ? 5.818   -4.758  66.865 1.00 51.75  ? 137 PHE B CB  1 
ATOM   3520 C  CG  . PHE B  1  124 ? 5.623   -5.379  65.488 1.00 49.02  ? 137 PHE B CG  1 
ATOM   3521 C  CD1 . PHE B  1  124 ? 5.837   -6.732  65.240 1.00 46.58  ? 137 PHE B CD1 1 
ATOM   3522 C  CD2 . PHE B  1  124 ? 5.201   -4.583  64.433 1.00 50.88  ? 137 PHE B CD2 1 
ATOM   3523 C  CE1 . PHE B  1  124 ? 5.633   -7.259  63.970 1.00 48.11  ? 137 PHE B CE1 1 
ATOM   3524 C  CE2 . PHE B  1  124 ? 4.977   -5.116  63.175 1.00 48.79  ? 137 PHE B CE2 1 
ATOM   3525 C  CZ  . PHE B  1  124 ? 5.185   -6.454  62.945 1.00 46.84  ? 137 PHE B CZ  1 
ATOM   3526 N  N   . GLU B  1  125 ? 8.385   -5.718  67.828 1.00 45.01  ? 138 GLU B N   1 
ATOM   3527 C  CA  . GLU B  1  125 ? 9.718   -6.300  67.851 1.00 43.48  ? 138 GLU B CA  1 
ATOM   3528 C  C   . GLU B  1  125 ? 9.961   -6.983  69.195 1.00 47.12  ? 138 GLU B C   1 
ATOM   3529 O  O   . GLU B  1  125 ? 9.634   -6.431  70.241 1.00 48.58  ? 138 GLU B O   1 
ATOM   3530 C  CB  . GLU B  1  125 ? 10.750  -5.201  67.602 1.00 43.69  ? 138 GLU B CB  1 
ATOM   3531 C  CG  . GLU B  1  125 ? 12.186  -5.705  67.475 1.00 43.74  ? 138 GLU B CG  1 
ATOM   3532 C  CD  . GLU B  1  125 ? 12.836  -6.232  68.756 1.00 47.32  ? 138 GLU B CD  1 
ATOM   3533 O  OE1 . GLU B  1  125 ? 12.725  -5.534  69.790 1.00 41.39  ? 138 GLU B OE1 1 
ATOM   3534 O  OE2 . GLU B  1  125 ? 13.466  -7.321  68.734 1.00 42.20  ? 138 GLU B OE2 1 
ATOM   3535 N  N   . GLY B  1  126 ? 10.549  -8.185  69.152 1.00 48.95  ? 139 GLY B N   1 
ATOM   3536 C  CA  . GLY B  1  126 ? 10.884  -8.933  70.351 1.00 46.63  ? 139 GLY B CA  1 
ATOM   3537 C  C   . GLY B  1  126 ? 12.043  -9.917  70.148 1.00 47.10  ? 139 GLY B C   1 
ATOM   3538 O  O   . GLY B  1  126 ? 12.850  -9.772  69.231 1.00 45.46  ? 139 GLY B O   1 
ATOM   3539 N  N   . ASP B  1  127 ? 12.058  -10.953 71.000 1.00 44.84  ? 140 ASP B N   1 
ATOM   3540 C  CA  . ASP B  1  127 ? 13.240  -11.727 71.346 1.00 47.50  ? 140 ASP B CA  1 
ATOM   3541 C  C   . ASP B  1  127 ? 13.296  -13.044 70.568 1.00 43.81  ? 140 ASP B C   1 
ATOM   3542 O  O   . ASP B  1  127 ? 12.297  -13.493 70.010 1.00 43.03  ? 140 ASP B O   1 
ATOM   3543 C  CB  . ASP B  1  127 ? 13.270  -12.038 72.842 1.00 44.99  ? 140 ASP B CB  1 
ATOM   3544 C  CG  . ASP B  1  127 ? 13.293  -10.852 73.801 1.00 43.53  ? 140 ASP B CG  1 
ATOM   3545 O  OD1 . ASP B  1  127 ? 13.912  -9.821  73.462 1.00 42.96  ? 140 ASP B OD1 1 
ATOM   3546 O  OD2 . ASP B  1  127 ? 12.709  -10.980 74.902 1.00 46.00  ? 140 ASP B OD2 1 
ATOM   3547 N  N   . ALA B  1  128 ? 14.477  -13.679 70.588 1.00 40.91  ? 141 ALA B N   1 
ATOM   3548 C  CA  . ALA B  1  128 ? 14.704  -14.987 69.981 1.00 42.95  ? 141 ALA B CA  1 
ATOM   3549 C  C   . ALA B  1  128 ? 14.581  -14.922 68.454 1.00 39.39  ? 141 ALA B C   1 
ATOM   3550 O  O   . ALA B  1  128 ? 14.099  -15.846 67.816 1.00 44.79  ? 141 ALA B O   1 
ATOM   3551 C  CB  . ALA B  1  128 ? 13.780  -16.032 70.594 1.00 43.59  ? 141 ALA B CB  1 
ATOM   3552 N  N   . GLY B  1  129 ? 15.072  -13.836 67.861 1.00 37.61  ? 142 GLY B N   1 
ATOM   3553 C  CA  . GLY B  1  129 ? 15.155  -13.714 66.415 1.00 37.37  ? 142 GLY B CA  1 
ATOM   3554 C  C   . GLY B  1  129 ? 16.320  -14.519 65.852 1.00 40.23  ? 142 GLY B C   1 
ATOM   3555 O  O   . GLY B  1  129 ? 17.137  -15.053 66.600 1.00 39.31  ? 142 GLY B O   1 
ATOM   3556 N  N   . MET B  1  130 ? 16.405  -14.567 64.516 1.00 41.72  ? 143 MET B N   1 
ATOM   3557 C  CA  . MET B  1  130 ? 17.361  -15.417 63.830 1.00 38.43  ? 143 MET B CA  1 
ATOM   3558 C  C   . MET B  1  130 ? 18.719  -14.724 63.673 1.00 40.20  ? 143 MET B C   1 
ATOM   3559 O  O   . MET B  1  130 ? 19.751  -15.360 63.895 1.00 39.00  ? 143 MET B O   1 
ATOM   3560 C  CB  . MET B  1  130 ? 16.808  -15.841 62.466 1.00 40.96  ? 143 MET B CB  1 
ATOM   3561 C  CG  . MET B  1  130 ? 15.618  -16.808 62.543 1.00 43.56  ? 143 MET B CG  1 
ATOM   3562 S  SD  . MET B  1  130 ? 14.902  -17.291 60.949 1.00 46.07  ? 143 MET B SD  1 
ATOM   3563 C  CE  . MET B  1  130 ? 14.260  -15.711 60.390 1.00 44.02  ? 143 MET B CE  1 
ATOM   3564 N  N   . THR B  1  131 ? 18.723  -13.449 63.250 1.00 38.25  ? 144 THR B N   1 
ATOM   3565 C  CA  . THR B  1  131 ? 19.951  -12.726 62.936 1.00 36.60  ? 144 THR B CA  1 
ATOM   3566 C  C   . THR B  1  131 ? 20.047  -11.424 63.729 1.00 37.92  ? 144 THR B C   1 
ATOM   3567 O  O   . THR B  1  131 ? 20.984  -10.655 63.519 1.00 37.58  ? 144 THR B O   1 
ATOM   3568 C  CB  . THR B  1  131 ? 20.038  -12.466 61.427 1.00 35.14  ? 144 THR B CB  1 
ATOM   3569 O  OG1 . THR B  1  131 ? 19.039  -11.532 61.039 1.00 33.38  ? 144 THR B OG1 1 
ATOM   3570 C  CG2 . THR B  1  131 ? 19.877  -13.741 60.623 1.00 35.47  ? 144 THR B CG2 1 
ATOM   3571 N  N   . ARG B  1  132 ? 19.078  -11.169 64.620 1.00 36.96  ? 145 ARG B N   1 
ATOM   3572 C  CA  . ARG B  1  132 ? 19.099  -10.014 65.505 1.00 36.25  ? 145 ARG B CA  1 
ATOM   3573 C  C   . ARG B  1  132 ? 19.074  -10.488 66.959 1.00 36.41  ? 145 ARG B C   1 
ATOM   3574 O  O   . ARG B  1  132 ? 18.389  -11.460 67.279 1.00 35.72  ? 145 ARG B O   1 
ATOM   3575 C  CB  . ARG B  1  132 ? 17.917  -9.088  65.213 1.00 36.06  ? 145 ARG B CB  1 
ATOM   3576 C  CG  . ARG B  1  132 ? 18.189  -8.027  64.159 1.00 37.77  ? 145 ARG B CG  1 
ATOM   3577 C  CD  . ARG B  1  132 ? 18.263  -8.584  62.731 1.00 39.19  ? 145 ARG B CD  1 
ATOM   3578 N  NE  . ARG B  1  132 ? 18.547  -7.497  61.788 1.00 42.84  ? 145 ARG B NE  1 
ATOM   3579 C  CZ  . ARG B  1  132 ? 19.014  -7.619  60.543 1.00 47.69  ? 145 ARG B CZ  1 
ATOM   3580 N  NH1 . ARG B  1  132 ? 19.261  -8.813  60.018 1.00 43.68  ? 145 ARG B NH1 1 
ATOM   3581 N  NH2 . ARG B  1  132 ? 19.286  -6.533  59.833 1.00 45.92  ? 145 ARG B NH2 1 
ATOM   3582 N  N   . ALA B  1  133 ? 19.832  -9.793  67.823 1.00 38.87  ? 146 ALA B N   1 
ATOM   3583 C  CA  . ALA B  1  133 ? 19.963  -10.138 69.234 1.00 38.67  ? 146 ALA B CA  1 
ATOM   3584 C  C   . ALA B  1  133 ? 18.848  -9.460  70.035 1.00 37.09  ? 146 ALA B C   1 
ATOM   3585 O  O   . ALA B  1  133 ? 18.357  -8.406  69.639 1.00 38.29  ? 146 ALA B O   1 
ATOM   3586 N  N   . ASP B  1  134 ? 18.468  -10.074 71.164 1.00 38.64  ? 147 ASP B N   1 
ATOM   3587 C  CA  . ASP B  1  134 ? 17.464  -9.543  72.082 1.00 40.50  ? 147 ASP B CA  1 
ATOM   3588 C  C   . ASP B  1  134 ? 17.857  -8.141  72.537 1.00 42.56  ? 147 ASP B C   1 
ATOM   3589 O  O   . ASP B  1  134 ? 19.046  -7.866  72.709 1.00 45.35  ? 147 ASP B O   1 
ATOM   3590 C  CB  . ASP B  1  134 ? 17.287  -10.443 73.296 1.00 38.51  ? 147 ASP B CB  1 
ATOM   3591 C  CG  . ASP B  1  134 ? 16.820  -11.864 73.001 1.00 43.40  ? 147 ASP B CG  1 
ATOM   3592 O  OD1 . ASP B  1  134 ? 16.718  -12.223 71.805 1.00 37.93  ? 147 ASP B OD1 1 
ATOM   3593 O  OD2 . ASP B  1  134 ? 16.514  -12.594 73.973 1.00 44.61  ? 147 ASP B OD2 1 
ATOM   3594 N  N   . GLU B  1  135 ? 16.849  -7.283  72.760 1.00 45.77  ? 148 GLU B N   1 
ATOM   3595 C  CA  . GLU B  1  135 ? 17.061  -5.899  73.160 1.00 52.31  ? 148 GLU B CA  1 
ATOM   3596 C  C   . GLU B  1  135 ? 17.864  -5.820  74.464 1.00 50.31  ? 148 GLU B C   1 
ATOM   3597 O  O   . GLU B  1  135 ? 18.633  -4.877  74.659 1.00 43.74  ? 148 GLU B O   1 
ATOM   3598 C  CB  . GLU B  1  135 ? 15.713  -5.176  73.261 1.00 56.20  ? 148 GLU B CB  1 
ATOM   3599 C  CG  . GLU B  1  135 ? 15.826  -3.694  73.616 1.00 60.68  ? 148 GLU B CG  1 
ATOM   3600 C  CD  . GLU B  1  135 ? 15.833  -3.366  75.101 1.00 66.62  ? 148 GLU B CD  1 
ATOM   3601 O  OE1 . GLU B  1  135 ? 15.510  -4.224  75.959 1.00 67.67  ? 148 GLU B OE1 1 
ATOM   3602 O  OE2 . GLU B  1  135 ? 16.170  -2.206  75.393 1.00 75.44  ? 148 GLU B OE2 1 
ATOM   3603 N  N   . PHE B  1  136 ? 17.685  -6.807  75.353 1.00 47.26  ? 149 PHE B N   1 
ATOM   3604 C  CA  . PHE B  1  136 ? 18.388  -6.827  76.628 1.00 53.61  ? 149 PHE B CA  1 
ATOM   3605 C  C   . PHE B  1  136 ? 19.896  -6.647  76.423 1.00 55.07  ? 149 PHE B C   1 
ATOM   3606 O  O   . PHE B  1  136 ? 20.552  -6.045  77.266 1.00 50.81  ? 149 PHE B O   1 
ATOM   3607 C  CB  . PHE B  1  136 ? 18.128  -8.119  77.406 1.00 54.73  ? 149 PHE B CB  1 
ATOM   3608 C  CG  . PHE B  1  136 ? 18.907  -8.207  78.713 1.00 60.84  ? 149 PHE B CG  1 
ATOM   3609 C  CD1 . PHE B  1  136 ? 18.509  -7.469  79.825 1.00 63.72  ? 149 PHE B CD1 1 
ATOM   3610 C  CD2 . PHE B  1  136 ? 20.037  -9.015  78.831 1.00 61.27  ? 149 PHE B CD2 1 
ATOM   3611 C  CE1 . PHE B  1  136 ? 19.211  -7.539  81.018 1.00 59.63  ? 149 PHE B CE1 1 
ATOM   3612 C  CE2 . PHE B  1  136 ? 20.731  -9.085  80.032 1.00 59.43  ? 149 PHE B CE2 1 
ATOM   3613 C  CZ  . PHE B  1  136 ? 20.316  -8.348  81.117 1.00 57.59  ? 149 PHE B CZ  1 
ATOM   3614 N  N   . PHE B  1  137 ? 20.436  -7.164  75.309 1.00 52.23  ? 150 PHE B N   1 
ATOM   3615 C  CA  . PHE B  1  137 ? 21.869  -7.149  75.083 1.00 46.60  ? 150 PHE B CA  1 
ATOM   3616 C  C   . PHE B  1  137 ? 22.318  -5.858  74.398 1.00 43.63  ? 150 PHE B C   1 
ATOM   3617 O  O   . PHE B  1  137 ? 23.505  -5.713  74.164 1.00 46.69  ? 150 PHE B O   1 
ATOM   3618 C  CB  . PHE B  1  137 ? 22.312  -8.358  74.258 1.00 44.87  ? 150 PHE B CB  1 
ATOM   3619 C  CG  . PHE B  1  137 ? 21.918  -9.697  74.858 1.00 48.12  ? 150 PHE B CG  1 
ATOM   3620 C  CD1 . PHE B  1  137 ? 22.299  -10.034 76.149 1.00 53.90  ? 150 PHE B CD1 1 
ATOM   3621 C  CD2 . PHE B  1  137 ? 21.137  -10.599 74.147 1.00 53.07  ? 150 PHE B CD2 1 
ATOM   3622 C  CE1 . PHE B  1  137 ? 21.933  -11.257 76.704 1.00 55.24  ? 150 PHE B CE1 1 
ATOM   3623 C  CE2 . PHE B  1  137 ? 20.755  -11.810 74.708 1.00 56.59  ? 150 PHE B CE2 1 
ATOM   3624 C  CZ  . PHE B  1  137 ? 21.151  -12.138 75.985 1.00 56.25  ? 150 PHE B CZ  1 
ATOM   3625 N  N   . GLY B  1  138 ? 21.402  -4.941  74.058 1.00 44.55  ? 151 GLY B N   1 
ATOM   3626 C  CA  . GLY B  1  138 ? 21.799  -3.581  73.716 1.00 47.77  ? 151 GLY B CA  1 
ATOM   3627 C  C   . GLY B  1  138 ? 21.505  -3.154  72.272 1.00 52.00  ? 151 GLY B C   1 
ATOM   3628 O  O   . GLY B  1  138 ? 21.601  -1.964  71.983 1.00 55.84  ? 151 GLY B O   1 
ATOM   3629 N  N   . ASP B  1  139 ? 21.165  -4.086  71.368 1.00 51.49  ? 152 ASP B N   1 
ATOM   3630 C  CA  . ASP B  1  139 ? 20.915  -3.736  69.969 1.00 48.58  ? 152 ASP B CA  1 
ATOM   3631 C  C   . ASP B  1  139 ? 19.977  -4.761  69.336 1.00 42.63  ? 152 ASP B C   1 
ATOM   3632 O  O   . ASP B  1  139 ? 20.374  -5.896  69.093 1.00 49.45  ? 152 ASP B O   1 
ATOM   3633 C  CB  . ASP B  1  139 ? 22.214  -3.631  69.182 1.00 49.88  ? 152 ASP B CB  1 
ATOM   3634 C  CG  . ASP B  1  139 ? 22.089  -3.245  67.716 1.00 52.41  ? 152 ASP B CG  1 
ATOM   3635 O  OD1 . ASP B  1  139 ? 20.973  -3.331  67.178 1.00 54.51  ? 152 ASP B OD1 1 
ATOM   3636 O  OD2 . ASP B  1  139 ? 23.104  -2.834  67.129 1.00 53.79  ? 152 ASP B OD2 1 
ATOM   3637 N  N   . ASN B  1  140 ? 18.733  -4.354  69.064 1.00 37.08  ? 153 ASN B N   1 
ATOM   3638 C  CA  . ASN B  1  140 ? 17.686  -5.276  68.642 1.00 39.18  ? 153 ASN B CA  1 
ATOM   3639 C  C   . ASN B  1  140 ? 17.452  -5.222  67.128 1.00 38.60  ? 153 ASN B C   1 
ATOM   3640 O  O   . ASN B  1  140 ? 16.515  -5.859  66.629 1.00 39.05  ? 153 ASN B O   1 
ATOM   3641 C  CB  . ASN B  1  140 ? 16.370  -4.987  69.356 1.00 38.02  ? 153 ASN B CB  1 
ATOM   3642 C  CG  . ASN B  1  140 ? 15.793  -3.624  69.040 1.00 39.51  ? 153 ASN B CG  1 
ATOM   3643 O  OD1 . ASN B  1  140 ? 16.455  -2.763  68.446 1.00 38.83  ? 153 ASN B OD1 1 
ATOM   3644 N  ND2 . ASN B  1  140 ? 14.560  -3.395  69.458 1.00 43.76  ? 153 ASN B ND2 1 
ATOM   3645 N  N   . HIS B  1  141 ? 18.277  -4.450  66.407 1.00 41.44  ? 154 HIS B N   1 
ATOM   3646 C  CA  . HIS B  1  141 ? 17.989  -4.113  65.017 1.00 47.83  ? 154 HIS B CA  1 
ATOM   3647 C  C   . HIS B  1  141 ? 19.126  -4.508  64.068 1.00 43.88  ? 154 HIS B C   1 
ATOM   3648 O  O   . HIS B  1  141 ? 18.854  -4.873  62.925 1.00 48.06  ? 154 HIS B O   1 
ATOM   3649 C  CB  . HIS B  1  141 ? 17.589  -2.637  64.867 1.00 47.19  ? 154 HIS B CB  1 
ATOM   3650 C  CG  . HIS B  1  141 ? 18.591  -1.687  65.407 1.00 53.05  ? 154 HIS B CG  1 
ATOM   3651 N  ND1 . HIS B  1  141 ? 18.545  -1.216  66.699 1.00 57.69  ? 154 HIS B ND1 1 
ATOM   3652 C  CD2 . HIS B  1  141 ? 19.674  -1.133  64.848 1.00 58.88  ? 154 HIS B CD2 1 
ATOM   3653 C  CE1 . HIS B  1  141 ? 19.570  -0.398  66.898 1.00 58.18  ? 154 HIS B CE1 1 
ATOM   3654 N  NE2 . HIS B  1  141 ? 20.274  -0.342  65.792 1.00 53.49  ? 154 HIS B NE2 1 
ATOM   3655 N  N   . SER B  1  142 ? 20.383  -4.416  64.522 1.00 41.25  ? 155 SER B N   1 
ATOM   3656 C  CA  . SER B  1  142 ? 21.539  -4.687  63.679 1.00 42.39  ? 155 SER B CA  1 
ATOM   3657 C  C   . SER B  1  142 ? 21.689  -6.175  63.380 1.00 40.60  ? 155 SER B C   1 
ATOM   3658 O  O   . SER B  1  142 ? 21.437  -7.012  64.232 1.00 44.24  ? 155 SER B O   1 
ATOM   3659 C  CB  . SER B  1  142 ? 22.808  -4.162  64.294 1.00 44.60  ? 155 SER B CB  1 
ATOM   3660 O  OG  . SER B  1  142 ? 22.841  -2.743  64.236 1.00 52.50  ? 155 SER B OG  1 
ATOM   3661 N  N   . PHE B  1  143 ? 22.153  -6.481  62.164 1.00 43.57  ? 156 PHE B N   1 
ATOM   3662 C  CA  . PHE B  1  143 ? 22.599  -7.821  61.811 1.00 41.27  ? 156 PHE B CA  1 
ATOM   3663 C  C   . PHE B  1  143 ? 23.732  -8.258  62.743 1.00 40.50  ? 156 PHE B C   1 
ATOM   3664 O  O   . PHE B  1  143 ? 24.660  -7.490  62.966 1.00 36.95  ? 156 PHE B O   1 
ATOM   3665 C  CB  . PHE B  1  143 ? 23.077  -7.860  60.355 1.00 38.43  ? 156 PHE B CB  1 
ATOM   3666 C  CG  . PHE B  1  143 ? 23.699  -9.193  59.959 1.00 37.78  ? 156 PHE B CG  1 
ATOM   3667 C  CD1 . PHE B  1  143 ? 22.906  -10.264 59.552 1.00 34.37  ? 156 PHE B CD1 1 
ATOM   3668 C  CD2 . PHE B  1  143 ? 25.078  -9.378  60.007 1.00 37.53  ? 156 PHE B CD2 1 
ATOM   3669 C  CE1 . PHE B  1  143 ? 23.468  -11.489 59.207 1.00 36.90  ? 156 PHE B CE1 1 
ATOM   3670 C  CE2 . PHE B  1  143 ? 25.636  -10.595 59.640 1.00 37.70  ? 156 PHE B CE2 1 
ATOM   3671 C  CZ  . PHE B  1  143 ? 24.829  -11.655 59.250 1.00 38.09  ? 156 PHE B CZ  1 
ATOM   3672 N  N   . ASN B  1  144 ? 23.657  -9.512  63.217 1.00 40.28  ? 157 ASN B N   1 
ATOM   3673 C  CA  . ASN B  1  144 ? 24.586  -10.098 64.167 1.00 41.59  ? 157 ASN B CA  1 
ATOM   3674 C  C   . ASN B  1  144 ? 25.203  -11.372 63.587 1.00 39.43  ? 157 ASN B C   1 
ATOM   3675 O  O   . ASN B  1  144 ? 24.519  -12.384 63.427 1.00 34.35  ? 157 ASN B O   1 
ATOM   3676 C  CB  . ASN B  1  144 ? 23.845  -10.400 65.463 1.00 45.25  ? 157 ASN B CB  1 
ATOM   3677 C  CG  . ASN B  1  144 ? 24.682  -11.072 66.523 1.00 45.83  ? 157 ASN B CG  1 
ATOM   3678 O  OD1 . ASN B  1  144 ? 25.378  -12.051 66.246 1.00 42.10  ? 157 ASN B OD1 1 
ATOM   3679 N  ND2 . ASN B  1  144 ? 24.584  -10.588 67.748 1.00 56.84  ? 157 ASN B ND2 1 
ATOM   3680 N  N   . GLN B  1  145 ? 26.520  -11.333 63.339 1.00 38.65  ? 158 GLN B N   1 
ATOM   3681 C  CA  . GLN B  1  145 ? 27.231  -12.400 62.643 1.00 38.66  ? 158 GLN B CA  1 
ATOM   3682 C  C   . GLN B  1  145 ? 27.260  -13.684 63.470 1.00 35.23  ? 158 GLN B C   1 
ATOM   3683 O  O   . GLN B  1  145 ? 27.202  -14.776 62.914 1.00 37.90  ? 158 GLN B O   1 
ATOM   3684 C  CB  . GLN B  1  145 ? 28.646  -11.940 62.279 1.00 39.93  ? 158 GLN B CB  1 
ATOM   3685 C  CG  . GLN B  1  145 ? 29.454  -12.935 61.451 1.00 37.44  ? 158 GLN B CG  1 
ATOM   3686 C  CD  . GLN B  1  145 ? 28.919  -13.171 60.050 1.00 39.16  ? 158 GLN B CD  1 
ATOM   3687 O  OE1 . GLN B  1  145 ? 28.687  -12.246 59.270 1.00 37.60  ? 158 GLN B OE1 1 
ATOM   3688 N  NE2 . GLN B  1  145 ? 28.772  -14.428 59.671 1.00 41.75  ? 158 GLN B NE2 1 
ATOM   3689 N  N   . THR B  1  146 ? 27.371  -13.558 64.796 1.00 36.56  ? 159 THR B N   1 
ATOM   3690 C  CA  . THR B  1  146 ? 27.405  -14.713 65.683 1.00 37.29  ? 159 THR B CA  1 
ATOM   3691 C  C   . THR B  1  146 ? 26.124  -15.522 65.505 1.00 35.83  ? 159 THR B C   1 
ATOM   3692 O  O   . THR B  1  146 ? 26.183  -16.744 65.400 1.00 41.94  ? 159 THR B O   1 
ATOM   3693 C  CB  . THR B  1  146 ? 27.577  -14.281 67.142 1.00 41.35  ? 159 THR B CB  1 
ATOM   3694 O  OG1 . THR B  1  146 ? 28.720  -13.435 67.230 1.00 40.73  ? 159 THR B OG1 1 
ATOM   3695 C  CG2 . THR B  1  146 ? 27.707  -15.467 68.080 1.00 37.11  ? 159 THR B CG2 1 
ATOM   3696 N  N   . LEU B  1  147 ? 24.972  -14.839 65.459 1.00 37.42  ? 160 LEU B N   1 
ATOM   3697 C  CA  . LEU B  1  147 ? 23.690  -15.508 65.275 1.00 36.87  ? 160 LEU B CA  1 
ATOM   3698 C  C   . LEU B  1  147 ? 23.568  -16.089 63.871 1.00 34.51  ? 160 LEU B C   1 
ATOM   3699 O  O   . LEU B  1  147 ? 23.019  -17.175 63.697 1.00 35.61  ? 160 LEU B O   1 
ATOM   3700 C  CB  . LEU B  1  147 ? 22.535  -14.568 65.607 1.00 38.72  ? 160 LEU B CB  1 
ATOM   3701 C  CG  . LEU B  1  147 ? 22.353  -14.222 67.088 1.00 40.12  ? 160 LEU B CG  1 
ATOM   3702 C  CD1 . LEU B  1  147 ? 21.217  -13.226 67.280 1.00 43.96  ? 160 LEU B CD1 1 
ATOM   3703 C  CD2 . LEU B  1  147 ? 22.080  -15.471 67.889 1.00 36.77  ? 160 LEU B CD2 1 
ATOM   3704 N  N   . PHE B  1  148 ? 24.108  -15.396 62.867 1.00 36.13  ? 161 PHE B N   1 
ATOM   3705 C  CA  . PHE B  1  148 ? 24.077  -15.906 61.506 1.00 35.35  ? 161 PHE B CA  1 
ATOM   3706 C  C   . PHE B  1  148 ? 24.921  -17.178 61.407 1.00 39.38  ? 161 PHE B C   1 
ATOM   3707 O  O   . PHE B  1  148 ? 24.595  -18.067 60.619 1.00 36.65  ? 161 PHE B O   1 
ATOM   3708 C  CB  . PHE B  1  148 ? 24.536  -14.843 60.502 1.00 36.87  ? 161 PHE B CB  1 
ATOM   3709 C  CG  . PHE B  1  148 ? 24.376  -15.277 59.052 1.00 37.18  ? 161 PHE B CG  1 
ATOM   3710 C  CD1 . PHE B  1  148 ? 23.114  -15.349 58.481 1.00 35.49  ? 161 PHE B CD1 1 
ATOM   3711 C  CD2 . PHE B  1  148 ? 25.475  -15.627 58.273 1.00 32.30  ? 161 PHE B CD2 1 
ATOM   3712 C  CE1 . PHE B  1  148 ? 22.958  -15.761 57.169 1.00 37.19  ? 161 PHE B CE1 1 
ATOM   3713 C  CE2 . PHE B  1  148 ? 25.314  -16.039 56.965 1.00 36.42  ? 161 PHE B CE2 1 
ATOM   3714 C  CZ  . PHE B  1  148 ? 24.057  -16.100 56.409 1.00 36.70  ? 161 PHE B CZ  1 
ATOM   3715 N  N   . ASP B  1  149 ? 26.006  -17.268 62.199 1.00 41.58  ? 162 ASP B N   1 
ATOM   3716 C  CA  . ASP B  1  149 ? 26.851  -18.456 62.207 1.00 41.73  ? 162 ASP B CA  1 
ATOM   3717 C  C   . ASP B  1  149 ? 26.057  -19.661 62.717 1.00 39.95  ? 162 ASP B C   1 
ATOM   3718 O  O   . ASP B  1  149 ? 26.205  -20.759 62.184 1.00 38.74  ? 162 ASP B O   1 
ATOM   3719 C  CB  . ASP B  1  149 ? 28.161  -18.182 62.931 1.00 43.70  ? 162 ASP B CB  1 
ATOM   3720 C  CG  . ASP B  1  149 ? 29.140  -17.269 62.189 1.00 48.10  ? 162 ASP B CG  1 
ATOM   3721 O  OD1 . ASP B  1  149 ? 29.038  -17.168 60.939 1.00 49.92  ? 162 ASP B OD1 1 
ATOM   3722 O  OD2 . ASP B  1  149 ? 29.988  -16.634 62.857 1.00 47.27  ? 162 ASP B OD2 1 
ATOM   3723 N  N   . LYS B  1  150 ? 25.210  -19.452 63.741 1.00 38.41  ? 163 LYS B N   1 
ATOM   3724 C  CA  . LYS B  1  150 ? 24.322  -20.489 64.252 1.00 37.41  ? 163 LYS B CA  1 
ATOM   3725 C  C   . LYS B  1  150 ? 23.298  -20.890 63.185 1.00 38.15  ? 163 LYS B C   1 
ATOM   3726 O  O   . LYS B  1  150 ? 22.977  -22.072 63.040 1.00 37.78  ? 163 LYS B O   1 
ATOM   3727 C  CB  . LYS B  1  150 ? 23.618  -20.013 65.529 1.00 38.38  ? 163 LYS B CB  1 
ATOM   3728 C  CG  . LYS B  1  150 ? 22.749  -21.052 66.237 1.00 40.54  ? 163 LYS B CG  1 
ATOM   3729 C  CD  . LYS B  1  150 ? 21.930  -20.475 67.387 1.00 49.37  ? 163 LYS B CD  1 
ATOM   3730 C  CE  . LYS B  1  150 ? 21.243  -21.490 68.271 1.00 51.41  ? 163 LYS B CE  1 
ATOM   3731 N  NZ  . LYS B  1  150 ? 22.099  -21.872 69.387 1.00 60.27  ? 163 LYS B NZ  1 
ATOM   3732 N  N   . PHE B  1  151 ? 22.783  -19.899 62.447 1.00 38.02  ? 164 PHE B N   1 
ATOM   3733 C  CA  . PHE B  1  151 ? 21.916  -20.142 61.303 1.00 39.04  ? 164 PHE B CA  1 
ATOM   3734 C  C   . PHE B  1  151 ? 22.593  -21.096 60.321 1.00 37.29  ? 164 PHE B C   1 
ATOM   3735 O  O   . PHE B  1  151 ? 21.964  -22.039 59.833 1.00 34.10  ? 164 PHE B O   1 
ATOM   3736 C  CB  . PHE B  1  151 ? 21.602  -18.817 60.606 1.00 40.14  ? 164 PHE B CB  1 
ATOM   3737 C  CG  . PHE B  1  151 ? 20.499  -18.843 59.562 1.00 38.96  ? 164 PHE B CG  1 
ATOM   3738 C  CD1 . PHE B  1  151 ? 20.762  -19.068 58.210 1.00 39.02  ? 164 PHE B CD1 1 
ATOM   3739 C  CD2 . PHE B  1  151 ? 19.191  -18.588 59.950 1.00 42.45  ? 164 PHE B CD2 1 
ATOM   3740 C  CE1 . PHE B  1  151 ? 19.716  -19.087 57.288 1.00 41.51  ? 164 PHE B CE1 1 
ATOM   3741 C  CE2 . PHE B  1  151 ? 18.163  -18.562 59.025 1.00 43.02  ? 164 PHE B CE2 1 
ATOM   3742 C  CZ  . PHE B  1  151 ? 18.421  -18.813 57.699 1.00 41.69  ? 164 PHE B CZ  1 
ATOM   3743 N  N   . VAL B  1  152 ? 23.864  -20.815 60.008 1.00 36.06  ? 165 VAL B N   1 
ATOM   3744 C  CA  . VAL B  1  152 ? 24.620  -21.623 59.064 1.00 37.89  ? 165 VAL B CA  1 
ATOM   3745 C  C   . VAL B  1  152 ? 24.842  -23.024 59.649 1.00 38.02  ? 165 VAL B C   1 
ATOM   3746 O  O   . VAL B  1  152 ? 24.690  -24.025 58.950 1.00 37.33  ? 165 VAL B O   1 
ATOM   3747 C  CB  . VAL B  1  152 ? 25.952  -20.957 58.664 1.00 37.85  ? 165 VAL B CB  1 
ATOM   3748 C  CG1 . VAL B  1  152 ? 26.825  -21.893 57.836 1.00 36.59  ? 165 VAL B CG1 1 
ATOM   3749 C  CG2 . VAL B  1  152 ? 25.744  -19.629 57.935 1.00 36.58  ? 165 VAL B CG2 1 
ATOM   3750 N  N   . ASP B  1  153 ? 25.215  -23.094 60.931 1.00 39.64  ? 166 ASP B N   1 
ATOM   3751 C  CA  . ASP B  1  153 ? 25.504  -24.361 61.593 1.00 40.25  ? 166 ASP B CA  1 
ATOM   3752 C  C   . ASP B  1  153 ? 24.283  -25.286 61.541 1.00 39.97  ? 166 ASP B C   1 
ATOM   3753 O  O   . ASP B  1  153 ? 24.399  -26.450 61.169 1.00 40.04  ? 166 ASP B O   1 
ATOM   3754 C  CB  . ASP B  1  153 ? 26.017  -24.127 63.008 1.00 42.42  ? 166 ASP B CB  1 
ATOM   3755 C  CG  . ASP B  1  153 ? 26.404  -25.374 63.798 1.00 44.83  ? 166 ASP B CG  1 
ATOM   3756 O  OD1 . ASP B  1  153 ? 27.128  -26.225 63.225 1.00 47.76  ? 166 ASP B OD1 1 
ATOM   3757 O  OD2 . ASP B  1  153 ? 25.984  -25.476 64.980 1.00 44.58  ? 166 ASP B OD2 1 
ATOM   3758 N  N   . PHE B  1  154 ? 23.111  -24.757 61.910 1.00 40.61  ? 167 PHE B N   1 
ATOM   3759 C  CA  . PHE B  1  154 ? 21.884  -25.538 61.943 1.00 39.96  ? 167 PHE B CA  1 
ATOM   3760 C  C   . PHE B  1  154 ? 21.482  -25.964 60.534 1.00 37.09  ? 167 PHE B C   1 
ATOM   3761 O  O   . PHE B  1  154 ? 20.943  -27.056 60.341 1.00 36.49  ? 167 PHE B O   1 
ATOM   3762 C  CB  . PHE B  1  154 ? 20.770  -24.756 62.648 1.00 41.24  ? 167 PHE B CB  1 
ATOM   3763 C  CG  . PHE B  1  154 ? 20.712  -24.977 64.154 1.00 42.85  ? 167 PHE B CG  1 
ATOM   3764 C  CD1 . PHE B  1  154 ? 21.755  -24.575 64.985 1.00 46.45  ? 167 PHE B CD1 1 
ATOM   3765 C  CD2 . PHE B  1  154 ? 19.610  -25.591 64.735 1.00 45.37  ? 167 PHE B CD2 1 
ATOM   3766 C  CE1 . PHE B  1  154 ? 21.691  -24.777 66.356 1.00 42.99  ? 167 PHE B CE1 1 
ATOM   3767 C  CE2 . PHE B  1  154 ? 19.547  -25.793 66.107 1.00 46.58  ? 167 PHE B CE2 1 
ATOM   3768 C  CZ  . PHE B  1  154 ? 20.595  -25.398 66.914 1.00 47.45  ? 167 PHE B CZ  1 
ATOM   3769 N  N   . SER B  1  155 ? 21.726  -25.099 59.550 1.00 37.04  ? 168 SER B N   1 
ATOM   3770 C  CA  . SER B  1  155 ? 21.496  -25.459 58.156 1.00 38.09  ? 168 SER B CA  1 
ATOM   3771 C  C   . SER B  1  155 ? 22.425  -26.600 57.735 1.00 40.84  ? 168 SER B C   1 
ATOM   3772 O  O   . SER B  1  155 ? 22.019  -27.481 56.981 1.00 42.63  ? 168 SER B O   1 
ATOM   3773 C  CB  . SER B  1  155 ? 21.656  -24.251 57.252 1.00 42.20  ? 168 SER B CB  1 
ATOM   3774 O  OG  . SER B  1  155 ? 20.774  -23.197 57.625 1.00 40.47  ? 168 SER B OG  1 
ATOM   3775 N  N   . ASN B  1  156 ? 23.680  -26.584 58.220 1.00 41.06  ? 169 ASN B N   1 
ATOM   3776 C  CA  . ASN B  1  156 ? 24.624  -27.656 57.937 1.00 38.94  ? 169 ASN B CA  1 
ATOM   3777 C  C   . ASN B  1  156 ? 24.156  -28.944 58.610 1.00 37.07  ? 169 ASN B C   1 
ATOM   3778 O  O   . ASN B  1  156 ? 24.233  -30.011 58.017 1.00 42.03  ? 169 ASN B O   1 
ATOM   3779 C  CB  . ASN B  1  156 ? 26.043  -27.319 58.387 1.00 39.95  ? 169 ASN B CB  1 
ATOM   3780 C  CG  . ASN B  1  156 ? 26.703  -26.263 57.537 1.00 39.28  ? 169 ASN B CG  1 
ATOM   3781 O  OD1 . ASN B  1  156 ? 26.332  -26.046 56.377 1.00 40.05  ? 169 ASN B OD1 1 
ATOM   3782 N  ND2 . ASN B  1  156 ? 27.698  -25.605 58.106 1.00 41.38  ? 169 ASN B ND2 1 
ATOM   3783 N  N   . ARG B  1  157 ? 23.640  -28.839 59.838 1.00 36.43  ? 170 ARG B N   1 
ATOM   3784 C  CA  . ARG B  1  157 ? 23.311  -30.011 60.630 1.00 41.61  ? 170 ARG B CA  1 
ATOM   3785 C  C   . ARG B  1  157 ? 21.992  -30.669 60.215 1.00 43.74  ? 170 ARG B C   1 
ATOM   3786 O  O   . ARG B  1  157 ? 21.840  -31.878 60.382 1.00 43.18  ? 170 ARG B O   1 
ATOM   3787 C  CB  . ARG B  1  157 ? 23.259  -29.621 62.108 1.00 41.36  ? 170 ARG B CB  1 
ATOM   3788 C  CG  . ARG B  1  157 ? 24.641  -29.475 62.717 1.00 42.90  ? 170 ARG B CG  1 
ATOM   3789 C  CD  . ARG B  1  157 ? 24.627  -28.597 63.952 1.00 46.05  ? 170 ARG B CD  1 
ATOM   3790 N  NE  . ARG B  1  157 ? 23.768  -29.152 64.998 1.00 53.24  ? 170 ARG B NE  1 
ATOM   3791 C  CZ  . ARG B  1  157 ? 23.598  -28.574 66.179 1.00 58.17  ? 170 ARG B CZ  1 
ATOM   3792 N  NH1 . ARG B  1  157 ? 22.705  -29.070 67.023 1.00 61.43  ? 170 ARG B NH1 1 
ATOM   3793 N  NH2 . ARG B  1  157 ? 24.281  -27.480 66.484 1.00 56.86  ? 170 ARG B NH2 1 
ATOM   3794 N  N   . TYR B  1  158 ? 21.035  -29.890 59.688 1.00 44.52  ? 171 TYR B N   1 
ATOM   3795 C  CA  . TYR B  1  158 ? 19.690  -30.410 59.469 1.00 40.74  ? 171 TYR B CA  1 
ATOM   3796 C  C   . TYR B  1  158 ? 19.207  -30.223 58.035 1.00 41.81  ? 171 TYR B C   1 
ATOM   3797 O  O   . TYR B  1  158 ? 18.185  -30.805 57.676 1.00 45.44  ? 171 TYR B O   1 
ATOM   3798 C  CB  . TYR B  1  158 ? 18.687  -29.775 60.437 1.00 40.62  ? 171 TYR B CB  1 
ATOM   3799 C  CG  . TYR B  1  158 ? 19.022  -30.020 61.906 1.00 41.10  ? 171 TYR B CG  1 
ATOM   3800 C  CD1 . TYR B  1  158 ? 18.883  -31.277 62.486 1.00 44.92  ? 171 TYR B CD1 1 
ATOM   3801 C  CD2 . TYR B  1  158 ? 19.516  -28.999 62.702 1.00 39.17  ? 171 TYR B CD2 1 
ATOM   3802 C  CE1 . TYR B  1  158 ? 19.204  -31.502 63.815 1.00 42.30  ? 171 TYR B CE1 1 
ATOM   3803 C  CE2 . TYR B  1  158 ? 19.823  -29.205 64.033 1.00 40.75  ? 171 TYR B CE2 1 
ATOM   3804 C  CZ  . TYR B  1  158 ? 19.661  -30.458 64.596 1.00 45.13  ? 171 TYR B CZ  1 
ATOM   3805 O  OH  . TYR B  1  158 ? 20.005  -30.661 65.910 1.00 49.04  ? 171 TYR B OH  1 
ATOM   3806 N  N   . GLY B  1  159 ? 19.927  -29.450 57.210 1.00 42.72  ? 172 GLY B N   1 
ATOM   3807 C  CA  . GLY B  1  159 ? 19.408  -29.098 55.893 1.00 39.38  ? 172 GLY B CA  1 
ATOM   3808 C  C   . GLY B  1  159 ? 20.421  -29.277 54.771 1.00 39.45  ? 172 GLY B C   1 
ATOM   3809 O  O   . GLY B  1  159 ? 20.254  -28.695 53.707 1.00 43.71  ? 172 GLY B O   1 
ATOM   3810 N  N   . GLY B  1  160 ? 21.459  -30.093 54.994 1.00 45.45  ? 173 GLY B N   1 
ATOM   3811 C  CA  . GLY B  1  160 ? 22.416  -30.376 53.935 1.00 43.29  ? 173 GLY B CA  1 
ATOM   3812 C  C   . GLY B  1  160 ? 23.169  -29.128 53.481 1.00 39.80  ? 173 GLY B C   1 
ATOM   3813 O  O   . GLY B  1  160 ? 23.674  -29.120 52.363 1.00 50.02  ? 173 GLY B O   1 
ATOM   3814 N  N   . GLY B  1  161 ? 23.236  -28.097 54.342 1.00 38.55  ? 174 GLY B N   1 
ATOM   3815 C  CA  . GLY B  1  161 ? 23.905  -26.841 54.029 1.00 39.84  ? 174 GLY B CA  1 
ATOM   3816 C  C   . GLY B  1  161 ? 22.933  -25.746 53.572 1.00 41.74  ? 174 GLY B C   1 
ATOM   3817 O  O   . GLY B  1  161 ? 23.358  -24.631 53.246 1.00 36.07  ? 174 GLY B O   1 
ATOM   3818 N  N   . PHE B  1  162 ? 21.630  -26.079 53.555 1.00 42.31  ? 175 PHE B N   1 
ATOM   3819 C  CA  . PHE B  1  162 ? 20.580  -25.177 53.109 1.00 40.43  ? 175 PHE B CA  1 
ATOM   3820 C  C   . PHE B  1  162 ? 19.554  -24.989 54.224 1.00 39.32  ? 175 PHE B C   1 
ATOM   3821 O  O   . PHE B  1  162 ? 19.370  -25.868 55.062 1.00 37.38  ? 175 PHE B O   1 
ATOM   3822 C  CB  . PHE B  1  162 ? 19.920  -25.736 51.846 1.00 39.49  ? 175 PHE B CB  1 
ATOM   3823 C  CG  . PHE B  1  162 ? 20.821  -25.806 50.623 1.00 39.81  ? 175 PHE B CG  1 
ATOM   3824 C  CD1 . PHE B  1  162 ? 20.914  -24.723 49.751 1.00 44.62  ? 175 PHE B CD1 1 
ATOM   3825 C  CD2 . PHE B  1  162 ? 21.572  -26.944 50.346 1.00 41.37  ? 175 PHE B CD2 1 
ATOM   3826 C  CE1 . PHE B  1  162 ? 21.724  -24.784 48.625 1.00 44.80  ? 175 PHE B CE1 1 
ATOM   3827 C  CE2 . PHE B  1  162 ? 22.389  -26.997 49.218 1.00 41.95  ? 175 PHE B CE2 1 
ATOM   3828 C  CZ  . PHE B  1  162 ? 22.463  -25.920 48.361 1.00 40.64  ? 175 PHE B CZ  1 
ATOM   3829 N  N   . TYR B  1  163 ? 18.881  -23.834 54.231 1.00 38.09  ? 176 TYR B N   1 
ATOM   3830 C  CA  . TYR B  1  163 ? 17.805  -23.589 55.177 1.00 38.25  ? 176 TYR B CA  1 
ATOM   3831 C  C   . TYR B  1  163 ? 16.484  -24.098 54.594 1.00 40.67  ? 176 TYR B C   1 
ATOM   3832 O  O   . TYR B  1  163 ? 16.063  -23.642 53.535 1.00 42.71  ? 176 TYR B O   1 
ATOM   3833 C  CB  . TYR B  1  163 ? 17.740  -22.096 55.502 1.00 37.58  ? 176 TYR B CB  1 
ATOM   3834 C  CG  . TYR B  1  163 ? 16.779  -21.738 56.625 1.00 36.53  ? 176 TYR B CG  1 
ATOM   3835 C  CD1 . TYR B  1  163 ? 17.134  -21.913 57.957 1.00 36.68  ? 176 TYR B CD1 1 
ATOM   3836 C  CD2 . TYR B  1  163 ? 15.519  -21.218 56.351 1.00 38.03  ? 176 TYR B CD2 1 
ATOM   3837 C  CE1 . TYR B  1  163 ? 16.260  -21.587 58.983 1.00 37.02  ? 176 TYR B CE1 1 
ATOM   3838 C  CE2 . TYR B  1  163 ? 14.636  -20.880 57.367 1.00 36.12  ? 176 TYR B CE2 1 
ATOM   3839 C  CZ  . TYR B  1  163 ? 15.008  -21.060 58.685 1.00 38.29  ? 176 TYR B CZ  1 
ATOM   3840 O  OH  . TYR B  1  163 ? 14.100  -20.720 59.649 1.00 37.23  ? 176 TYR B OH  1 
ATOM   3841 N  N   . ASN B  1  164 ? 15.858  -25.058 55.289 1.00 40.86  ? 177 ASN B N   1 
ATOM   3842 C  CA  . ASN B  1  164 ? 14.546  -25.599 54.942 1.00 41.77  ? 177 ASN B CA  1 
ATOM   3843 C  C   . ASN B  1  164 ? 13.713  -25.745 56.221 1.00 41.18  ? 177 ASN B C   1 
ATOM   3844 O  O   . ASN B  1  164 ? 14.134  -25.318 57.295 1.00 37.35  ? 177 ASN B O   1 
ATOM   3845 C  CB  . ASN B  1  164 ? 14.687  -26.884 54.115 1.00 44.47  ? 177 ASN B CB  1 
ATOM   3846 C  CG  . ASN B  1  164 ? 15.122  -28.115 54.886 1.00 43.93  ? 177 ASN B CG  1 
ATOM   3847 O  OD1 . ASN B  1  164 ? 15.239  -28.096 56.121 1.00 45.29  ? 177 ASN B OD1 1 
ATOM   3848 N  ND2 . ASN B  1  164 ? 15.376  -29.190 54.154 1.00 47.76  ? 177 ASN B ND2 1 
ATOM   3849 N  N   . LEU B  1  165 ? 12.534  -26.362 56.101 1.00 42.93  ? 178 LEU B N   1 
ATOM   3850 C  CA  . LEU B  1  165 ? 11.572  -26.447 57.194 1.00 47.36  ? 178 LEU B CA  1 
ATOM   3851 C  C   . LEU B  1  165 ? 12.118  -27.204 58.403 1.00 41.83  ? 178 LEU B C   1 
ATOM   3852 O  O   . LEU B  1  165 ? 11.813  -26.826 59.533 1.00 35.84  ? 178 LEU B O   1 
ATOM   3853 C  CB  . LEU B  1  165 ? 10.273  -27.101 56.725 1.00 50.38  ? 178 LEU B CB  1 
ATOM   3854 C  CG  . LEU B  1  165 ? 9.068   -26.179 56.548 1.00 56.48  ? 178 LEU B CG  1 
ATOM   3855 C  CD1 . LEU B  1  165 ? 7.870   -27.033 56.220 1.00 60.42  ? 178 LEU B CD1 1 
ATOM   3856 C  CD2 . LEU B  1  165 ? 8.758   -25.327 57.745 1.00 53.14  ? 178 LEU B CD2 1 
ATOM   3857 N  N   . THR B  1  166 ? 12.880  -28.282 58.158 1.00 39.57  ? 179 THR B N   1 
ATOM   3858 C  CA  . THR B  1  166 ? 13.508  -29.033 59.233 1.00 41.20  ? 179 THR B CA  1 
ATOM   3859 C  C   . THR B  1  166 ? 14.432  -28.109 60.031 1.00 40.15  ? 179 THR B C   1 
ATOM   3860 O  O   . THR B  1  166 ? 14.400  -28.107 61.266 1.00 45.54  ? 179 THR B O   1 
ATOM   3861 C  CB  . THR B  1  166 ? 14.269  -30.245 58.683 1.00 45.59  ? 179 THR B CB  1 
ATOM   3862 O  OG1 . THR B  1  166 ? 13.424  -30.984 57.806 1.00 39.99  ? 179 THR B OG1 1 
ATOM   3863 C  CG2 . THR B  1  166 ? 14.734  -31.186 59.782 1.00 44.60  ? 179 THR B CG2 1 
ATOM   3864 N  N   . VAL B  1  167 ? 15.239  -27.308 59.323 1.00 40.74  ? 180 VAL B N   1 
ATOM   3865 C  CA  . VAL B  1  167 ? 16.178  -26.393 59.964 1.00 38.90  ? 180 VAL B CA  1 
ATOM   3866 C  C   . VAL B  1  167 ? 15.390  -25.372 60.780 1.00 36.50  ? 180 VAL B C   1 
ATOM   3867 O  O   . VAL B  1  167 ? 15.745  -25.073 61.927 1.00 35.78  ? 180 VAL B O   1 
ATOM   3868 C  CB  . VAL B  1  167 ? 17.120  -25.676 58.976 1.00 40.20  ? 180 VAL B CB  1 
ATOM   3869 C  CG1 . VAL B  1  167 ? 18.153  -24.832 59.716 1.00 38.42  ? 180 VAL B CG1 1 
ATOM   3870 C  CG2 . VAL B  1  167 ? 17.803  -26.647 58.017 1.00 40.28  ? 180 VAL B CG2 1 
ATOM   3871 N  N   . ALA B  1  168 ? 14.324  -24.834 60.171 1.00 35.64  ? 181 ALA B N   1 
ATOM   3872 C  CA  . ALA B  1  168 ? 13.490  -23.823 60.813 1.00 35.03  ? 181 ALA B CA  1 
ATOM   3873 C  C   . ALA B  1  168 ? 12.978  -24.338 62.153 1.00 36.58  ? 181 ALA B C   1 
ATOM   3874 O  O   . ALA B  1  168 ? 13.066  -23.627 63.153 1.00 35.54  ? 181 ALA B O   1 
ATOM   3875 C  CB  . ALA B  1  168 ? 12.350  -23.428 59.899 1.00 37.63  ? 181 ALA B CB  1 
ATOM   3876 N  N   . GLY B  1  169 ? 12.460  -25.575 62.160 1.00 38.59  ? 182 GLY B N   1 
ATOM   3877 C  CA  . GLY B  1  169 ? 11.929  -26.177 63.372 1.00 40.86  ? 182 GLY B CA  1 
ATOM   3878 C  C   . GLY B  1  169 ? 12.972  -26.242 64.489 1.00 45.53  ? 182 GLY B C   1 
ATOM   3879 O  O   . GLY B  1  169 ? 12.685  -25.889 65.634 1.00 48.88  ? 182 GLY B O   1 
ATOM   3880 N  N   . GLU B  1  170 ? 14.186  -26.688 64.142 1.00 44.60  ? 183 GLU B N   1 
ATOM   3881 C  CA  . GLU B  1  170 ? 15.250  -26.860 65.125 1.00 43.30  ? 183 GLU B CA  1 
ATOM   3882 C  C   . GLU B  1  170 ? 15.791  -25.497 65.576 1.00 41.31  ? 183 GLU B C   1 
ATOM   3883 O  O   . GLU B  1  170 ? 15.981  -25.266 66.767 1.00 41.24  ? 183 GLU B O   1 
ATOM   3884 C  CB  . GLU B  1  170 ? 16.363  -27.753 64.567 1.00 45.97  ? 183 GLU B CB  1 
ATOM   3885 C  CG  . GLU B  1  170 ? 15.942  -29.185 64.246 1.00 47.09  ? 183 GLU B CG  1 
ATOM   3886 C  CD  . GLU B  1  170 ? 15.151  -29.864 65.347 1.00 52.03  ? 183 GLU B CD  1 
ATOM   3887 O  OE1 . GLU B  1  170 ? 15.627  -29.832 66.492 1.00 53.90  ? 183 GLU B OE1 1 
ATOM   3888 O  OE2 . GLU B  1  170 ? 14.039  -30.375 65.077 1.00 56.08  ? 183 GLU B OE2 1 
ATOM   3889 N  N   . LEU B  1  171 ? 16.029  -24.578 64.632 1.00 40.38  ? 184 LEU B N   1 
ATOM   3890 C  CA  . LEU B  1  171 ? 16.620  -23.289 64.973 1.00 39.82  ? 184 LEU B CA  1 
ATOM   3891 C  C   . LEU B  1  171 ? 15.693  -22.489 65.888 1.00 38.03  ? 184 LEU B C   1 
ATOM   3892 O  O   . LEU B  1  171 ? 16.142  -21.873 66.847 1.00 33.98  ? 184 LEU B O   1 
ATOM   3893 C  CB  . LEU B  1  171 ? 16.975  -22.512 63.704 1.00 41.84  ? 184 LEU B CB  1 
ATOM   3894 C  CG  . LEU B  1  171 ? 17.657  -21.155 63.917 1.00 42.58  ? 184 LEU B CG  1 
ATOM   3895 C  CD1 . LEU B  1  171 ? 18.980  -21.314 64.658 1.00 43.95  ? 184 LEU B CD1 1 
ATOM   3896 C  CD2 . LEU B  1  171 ? 17.886  -20.430 62.597 1.00 43.27  ? 184 LEU B CD2 1 
ATOM   3897 N  N   . ARG B  1  172 ? 14.390  -22.487 65.591 1.00 39.51  ? 185 ARG B N   1 
ATOM   3898 C  CA  . ARG B  1  172 ? 13.428  -21.722 66.373 1.00 41.92  ? 185 ARG B CA  1 
ATOM   3899 C  C   . ARG B  1  172 ? 13.517  -22.106 67.855 1.00 42.24  ? 185 ARG B C   1 
ATOM   3900 O  O   . ARG B  1  172 ? 13.587  -21.235 68.720 1.00 39.75  ? 185 ARG B O   1 
ATOM   3901 C  CB  . ARG B  1  172 ? 12.049  -21.900 65.715 1.00 40.55  ? 185 ARG B CB  1 
ATOM   3902 C  CG  . ARG B  1  172 ? 10.807  -21.567 66.524 1.00 41.53  ? 185 ARG B CG  1 
ATOM   3903 C  CD  . ARG B  1  172 ? 10.758  -20.179 67.135 1.00 43.57  ? 185 ARG B CD  1 
ATOM   3904 N  NE  . ARG B  1  172 ? 11.158  -19.075 66.253 1.00 43.95  ? 185 ARG B NE  1 
ATOM   3905 C  CZ  . ARG B  1  172 ? 12.062  -18.135 66.536 1.00 44.04  ? 185 ARG B CZ  1 
ATOM   3906 N  NH1 . ARG B  1  172 ? 12.682  -18.135 67.706 1.00 46.65  ? 185 ARG B NH1 1 
ATOM   3907 N  NH2 . ARG B  1  172 ? 12.328  -17.174 65.669 1.00 44.97  ? 185 ARG B NH2 1 
ATOM   3908 N  N   . TYR B  1  173 ? 13.525  -23.416 68.134 1.00 44.89  ? 186 TYR B N   1 
ATOM   3909 C  CA  . TYR B  1  173 ? 13.548  -23.921 69.498 1.00 48.64  ? 186 TYR B CA  1 
ATOM   3910 C  C   . TYR B  1  173 ? 14.868  -23.544 70.174 1.00 48.67  ? 186 TYR B C   1 
ATOM   3911 O  O   . TYR B  1  173 ? 14.864  -23.068 71.303 1.00 42.88  ? 186 TYR B O   1 
ATOM   3912 C  CB  . TYR B  1  173 ? 13.287  -25.435 69.494 1.00 50.76  ? 186 TYR B CB  1 
ATOM   3913 C  CG  . TYR B  1  173 ? 13.268  -26.078 70.874 1.00 56.18  ? 186 TYR B CG  1 
ATOM   3914 C  CD1 . TYR B  1  173 ? 12.245  -25.804 71.775 1.00 58.45  ? 186 TYR B CD1 1 
ATOM   3915 C  CD2 . TYR B  1  173 ? 14.257  -26.970 71.273 1.00 59.92  ? 186 TYR B CD2 1 
ATOM   3916 C  CE1 . TYR B  1  173 ? 12.215  -26.381 73.035 1.00 59.77  ? 186 TYR B CE1 1 
ATOM   3917 C  CE2 . TYR B  1  173 ? 14.239  -27.555 72.530 1.00 60.24  ? 186 TYR B CE2 1 
ATOM   3918 C  CZ  . TYR B  1  173 ? 13.213  -27.260 73.412 1.00 60.28  ? 186 TYR B CZ  1 
ATOM   3919 O  OH  . TYR B  1  173 ? 13.179  -27.827 74.653 1.00 61.68  ? 186 TYR B OH  1 
ATOM   3920 N  N   . SER B  1  174 ? 15.993  -23.759 69.479 1.00 49.63  ? 187 SER B N   1 
ATOM   3921 C  CA  . SER B  1  174 ? 17.309  -23.500 70.047 1.00 45.06  ? 187 SER B CA  1 
ATOM   3922 C  C   . SER B  1  174 ? 17.451  -22.030 70.433 1.00 43.21  ? 187 SER B C   1 
ATOM   3923 O  O   . SER B  1  174 ? 17.965  -21.742 71.513 1.00 43.65  ? 187 SER B O   1 
ATOM   3924 C  CB  . SER B  1  174 ? 18.406  -23.927 69.117 1.00 47.80  ? 187 SER B CB  1 
ATOM   3925 O  OG  . SER B  1  174 ? 19.678  -23.638 69.679 1.00 48.60  ? 187 SER B OG  1 
ATOM   3926 N  N   . ARG B  1  175 ? 16.955  -21.116 69.582 1.00 40.21  ? 188 ARG B N   1 
ATOM   3927 C  CA  . ARG B  1  175 ? 17.046  -19.681 69.849 1.00 43.48  ? 188 ARG B CA  1 
ATOM   3928 C  C   . ARG B  1  175 ? 16.220  -19.306 71.083 1.00 43.50  ? 188 ARG B C   1 
ATOM   3929 O  O   . ARG B  1  175 ? 16.635  -18.461 71.876 1.00 42.17  ? 188 ARG B O   1 
ATOM   3930 C  CB  . ARG B  1  175 ? 16.643  -18.830 68.638 1.00 43.66  ? 188 ARG B CB  1 
ATOM   3931 C  CG  . ARG B  1  175 ? 17.593  -18.915 67.445 1.00 42.92  ? 188 ARG B CG  1 
ATOM   3932 C  CD  . ARG B  1  175 ? 18.941  -18.258 67.697 1.00 41.96  ? 188 ARG B CD  1 
ATOM   3933 N  NE  . ARG B  1  175 ? 18.777  -16.824 67.955 1.00 40.43  ? 188 ARG B NE  1 
ATOM   3934 C  CZ  . ARG B  1  175 ? 18.950  -16.190 69.113 1.00 42.26  ? 188 ARG B CZ  1 
ATOM   3935 N  NH1 . ARG B  1  175 ? 19.514  -16.794 70.148 1.00 42.75  ? 188 ARG B NH1 1 
ATOM   3936 N  NH2 . ARG B  1  175 ? 18.577  -14.922 69.229 1.00 39.67  ? 188 ARG B NH2 1 
ATOM   3937 N  N   . ILE B  1  176 ? 15.058  -19.945 71.249 1.00 44.37  ? 189 ILE B N   1 
ATOM   3938 C  CA  . ILE B  1  176 ? 14.258  -19.773 72.451 1.00 44.33  ? 189 ILE B CA  1 
ATOM   3939 C  C   . ILE B  1  176 ? 15.077  -20.190 73.676 1.00 44.14  ? 189 ILE B C   1 
ATOM   3940 O  O   . ILE B  1  176 ? 15.144  -19.451 74.655 1.00 42.44  ? 189 ILE B O   1 
ATOM   3941 C  CB  . ILE B  1  176 ? 12.932  -20.546 72.346 1.00 44.51  ? 189 ILE B CB  1 
ATOM   3942 C  CG1 . ILE B  1  176 ? 11.994  -19.914 71.320 1.00 44.02  ? 189 ILE B CG1 1 
ATOM   3943 C  CG2 . ILE B  1  176 ? 12.260  -20.659 73.718 1.00 46.37  ? 189 ILE B CG2 1 
ATOM   3944 C  CD1 . ILE B  1  176 ? 10.806  -20.781 70.953 1.00 44.09  ? 189 ILE B CD1 1 
ATOM   3945 N  N   . GLN B  1  177 ? 15.726  -21.360 73.604 1.00 47.44  ? 190 GLN B N   1 
ATOM   3946 C  CA  . GLN B  1  177 ? 16.569  -21.836 74.694 1.00 50.22  ? 190 GLN B CA  1 
ATOM   3947 C  C   . GLN B  1  177 ? 17.697  -20.833 74.985 1.00 50.33  ? 190 GLN B C   1 
ATOM   3948 O  O   . GLN B  1  177 ? 17.930  -20.498 76.148 1.00 48.73  ? 190 GLN B O   1 
ATOM   3949 C  CB  . GLN B  1  177 ? 17.060  -23.254 74.404 1.00 53.47  ? 190 GLN B CB  1 
ATOM   3950 C  CG  . GLN B  1  177 ? 15.949  -24.298 74.364 1.00 59.34  ? 190 GLN B CG  1 
ATOM   3951 C  CD  . GLN B  1  177 ? 15.252  -24.478 75.696 1.00 72.66  ? 190 GLN B CD  1 
ATOM   3952 O  OE1 . GLN B  1  177 ? 15.784  -24.154 76.765 1.00 82.62  ? 190 GLN B OE1 1 
ATOM   3953 N  NE2 . GLN B  1  177 ? 14.042  -25.010 75.654 1.00 77.75  ? 190 GLN B NE2 1 
ATOM   3954 N  N   . ASP B  1  178 ? 18.369  -20.320 73.942 1.00 45.07  ? 191 ASP B N   1 
ATOM   3955 C  CA  . ASP B  1  178 ? 19.421  -19.328 74.123 1.00 45.24  ? 191 ASP B CA  1 
ATOM   3956 C  C   . ASP B  1  178 ? 18.933  -18.183 75.011 1.00 50.70  ? 191 ASP B C   1 
ATOM   3957 O  O   . ASP B  1  178 ? 19.633  -17.759 75.935 1.00 47.14  ? 191 ASP B O   1 
ATOM   3958 C  CB  . ASP B  1  178 ? 19.919  -18.775 72.797 1.00 45.96  ? 191 ASP B CB  1 
ATOM   3959 C  CG  . ASP B  1  178 ? 20.629  -19.759 71.873 1.00 48.10  ? 191 ASP B CG  1 
ATOM   3960 O  OD1 . ASP B  1  178 ? 20.973  -20.869 72.338 1.00 53.13  ? 191 ASP B OD1 1 
ATOM   3961 O  OD2 . ASP B  1  178 ? 20.840  -19.413 70.688 1.00 49.04  ? 191 ASP B OD2 1 
ATOM   3962 N  N   . SER B  1  179 ? 17.730  -17.675 74.716 1.00 49.97  ? 192 SER B N   1 
ATOM   3963 C  CA  . SER B  1  179 ? 17.187  -16.530 75.428 1.00 50.15  ? 192 SER B CA  1 
ATOM   3964 C  C   . SER B  1  179 ? 16.785  -16.899 76.861 1.00 45.25  ? 192 SER B C   1 
ATOM   3965 O  O   . SER B  1  179 ? 16.971  -16.097 77.773 1.00 41.29  ? 192 SER B O   1 
ATOM   3966 C  CB  . SER B  1  179 ? 16.033  -15.905 74.654 1.00 49.42  ? 192 SER B CB  1 
ATOM   3967 O  OG  . SER B  1  179 ? 16.505  -15.027 73.637 1.00 47.91  ? 192 SER B OG  1 
ATOM   3968 N  N   . ILE B  1  180 ? 16.212  -18.093 77.060 1.00 45.14  ? 193 ILE B N   1 
ATOM   3969 C  CA  . ILE B  1  180 ? 15.858  -18.542 78.399 1.00 51.69  ? 193 ILE B CA  1 
ATOM   3970 C  C   . ILE B  1  180 ? 17.110  -18.527 79.279 1.00 55.19  ? 193 ILE B C   1 
ATOM   3971 O  O   . ILE B  1  180 ? 17.079  -18.012 80.397 1.00 50.64  ? 193 ILE B O   1 
ATOM   3972 C  CB  . ILE B  1  180 ? 15.187  -19.928 78.368 1.00 52.97  ? 193 ILE B CB  1 
ATOM   3973 C  CG1 . ILE B  1  180 ? 13.781  -19.829 77.789 1.00 53.78  ? 193 ILE B CG1 1 
ATOM   3974 C  CG2 . ILE B  1  180 ? 15.176  -20.576 79.759 1.00 55.70  ? 193 ILE B CG2 1 
ATOM   3975 C  CD1 . ILE B  1  180 ? 13.112  -21.169 77.557 1.00 53.13  ? 193 ILE B CD1 1 
ATOM   3976 N  N   . ALA B  1  181 ? 18.211  -19.055 78.729 1.00 54.81  ? 194 ALA B N   1 
ATOM   3977 C  CA  . ALA B  1  181 ? 19.454  -19.263 79.458 1.00 53.97  ? 194 ALA B CA  1 
ATOM   3978 C  C   . ALA B  1  181 ? 20.201  -17.960 79.710 1.00 47.51  ? 194 ALA B C   1 
ATOM   3979 O  O   . ALA B  1  181 ? 20.970  -17.912 80.658 1.00 52.44  ? 194 ALA B O   1 
ATOM   3980 C  CB  . ALA B  1  181 ? 20.344  -20.235 78.702 1.00 53.22  ? 194 ALA B CB  1 
ATOM   3981 N  N   . THR B  1  182 ? 20.010  -16.930 78.872 1.00 46.85  ? 195 THR B N   1 
ATOM   3982 C  CA  . THR B  1  182 ? 20.916  -15.783 78.874 1.00 48.13  ? 195 THR B CA  1 
ATOM   3983 C  C   . THR B  1  182 ? 20.209  -14.454 79.131 1.00 45.88  ? 195 THR B C   1 
ATOM   3984 O  O   . THR B  1  182 ? 20.888  -13.479 79.434 1.00 48.26  ? 195 THR B O   1 
ATOM   3985 C  CB  . THR B  1  182 ? 21.689  -15.703 77.553 1.00 52.03  ? 195 THR B CB  1 
ATOM   3986 O  OG1 . THR B  1  182 ? 20.729  -15.553 76.503 1.00 50.34  ? 195 THR B OG1 1 
ATOM   3987 C  CG2 . THR B  1  182 ? 22.590  -16.908 77.328 1.00 48.90  ? 195 THR B CG2 1 
ATOM   3988 N  N   . ASN B  1  183 ? 18.885  -14.370 78.935 1.00 47.65  ? 196 ASN B N   1 
ATOM   3989 C  CA  . ASN B  1  183 ? 18.190  -13.090 78.983 1.00 49.35  ? 196 ASN B CA  1 
ATOM   3990 C  C   . ASN B  1  183 ? 17.178  -13.136 80.120 1.00 53.34  ? 196 ASN B C   1 
ATOM   3991 O  O   . ASN B  1  183 ? 16.157  -13.804 80.010 1.00 54.36  ? 196 ASN B O   1 
ATOM   3992 C  CB  . ASN B  1  183 ? 17.533  -12.758 77.645 1.00 53.08  ? 196 ASN B CB  1 
ATOM   3993 C  CG  . ASN B  1  183 ? 16.812  -11.425 77.635 1.00 56.03  ? 196 ASN B CG  1 
ATOM   3994 O  OD1 . ASN B  1  183 ? 16.779  -10.709 78.644 1.00 53.34  ? 196 ASN B OD1 1 
ATOM   3995 N  ND2 . ASN B  1  183 ? 16.218  -11.073 76.501 1.00 56.80  ? 196 ASN B ND2 1 
ATOM   3996 N  N   . PRO B  1  184 ? 17.429  -12.437 81.249 1.00 56.09  ? 197 PRO B N   1 
ATOM   3997 C  CA  . PRO B  1  184 ? 16.521  -12.489 82.395 1.00 59.47  ? 197 PRO B CA  1 
ATOM   3998 C  C   . PRO B  1  184 ? 15.214  -11.724 82.173 1.00 60.19  ? 197 PRO B C   1 
ATOM   3999 O  O   . PRO B  1  184 ? 14.263  -11.932 82.921 1.00 54.23  ? 197 PRO B O   1 
ATOM   4000 C  CB  . PRO B  1  184 ? 17.385  -11.886 83.515 1.00 53.96  ? 197 PRO B CB  1 
ATOM   4001 C  CG  . PRO B  1  184 ? 18.270  -10.897 82.802 1.00 56.50  ? 197 PRO B CG  1 
ATOM   4002 C  CD  . PRO B  1  184 ? 18.590  -11.561 81.478 1.00 53.73  ? 197 PRO B CD  1 
ATOM   4003 N  N   . GLU B  1  185 ? 15.186  -10.864 81.139 1.00 56.16  ? 198 GLU B N   1 
ATOM   4004 C  CA  . GLU B  1  185 ? 14.002  -10.106 80.752 1.00 54.35  ? 198 GLU B CA  1 
ATOM   4005 C  C   . GLU B  1  185 ? 13.289  -10.731 79.545 1.00 47.89  ? 198 GLU B C   1 
ATOM   4006 O  O   . GLU B  1  185 ? 12.415  -10.101 78.957 1.00 44.82  ? 198 GLU B O   1 
ATOM   4007 C  CB  . GLU B  1  185 ? 14.401  -8.670  80.401 1.00 57.65  ? 198 GLU B CB  1 
ATOM   4008 C  CG  . GLU B  1  185 ? 14.843  -7.816  81.586 1.00 61.05  ? 198 GLU B CG  1 
ATOM   4009 C  CD  . GLU B  1  185 ? 15.319  -6.422  81.193 1.00 63.23  ? 198 GLU B CD  1 
ATOM   4010 O  OE1 . GLU B  1  185 ? 15.308  -6.098  79.995 1.00 60.79  ? 198 GLU B OE1 1 
ATOM   4011 O  OE2 . GLU B  1  185 ? 15.727  -5.642  82.071 1.00 69.16  ? 198 GLU B OE2 1 
ATOM   4012 N  N   . PHE B  1  186 ? 13.644  -11.970 79.177 1.00 47.83  ? 199 PHE B N   1 
ATOM   4013 C  CA  . PHE B  1  186 ? 13.095  -12.645 78.004 1.00 48.44  ? 199 PHE B CA  1 
ATOM   4014 C  C   . PHE B  1  186 ? 11.570  -12.758 78.068 1.00 53.13  ? 199 PHE B C   1 
ATOM   4015 O  O   . PHE B  1  186 ? 11.026  -13.338 79.003 1.00 54.27  ? 199 PHE B O   1 
ATOM   4016 C  CB  . PHE B  1  186 ? 13.667  -14.060 77.898 1.00 46.12  ? 199 PHE B CB  1 
ATOM   4017 C  CG  . PHE B  1  186 ? 13.135  -14.921 76.759 1.00 47.01  ? 199 PHE B CG  1 
ATOM   4018 C  CD1 . PHE B  1  186 ? 13.028  -14.423 75.464 1.00 46.98  ? 199 PHE B CD1 1 
ATOM   4019 C  CD2 . PHE B  1  186 ? 12.752  -16.242 76.982 1.00 46.65  ? 199 PHE B CD2 1 
ATOM   4020 C  CE1 . PHE B  1  186 ? 12.556  -15.220 74.428 1.00 45.22  ? 199 PHE B CE1 1 
ATOM   4021 C  CE2 . PHE B  1  186 ? 12.273  -17.029 75.946 1.00 45.05  ? 199 PHE B CE2 1 
ATOM   4022 C  CZ  . PHE B  1  186 ? 12.178  -16.517 74.670 1.00 43.92  ? 199 PHE B CZ  1 
ATOM   4023 N  N   . GLN B  1  187 ? 10.904  -12.238 77.027 1.00 55.93  ? 200 GLN B N   1 
ATOM   4024 C  CA  . GLN B  1  187 ? 9.466   -12.368 76.840 1.00 51.24  ? 200 GLN B CA  1 
ATOM   4025 C  C   . GLN B  1  187 ? 9.191   -13.042 75.495 1.00 50.73  ? 200 GLN B C   1 
ATOM   4026 O  O   . GLN B  1  187 ? 9.836   -12.722 74.499 1.00 46.57  ? 200 GLN B O   1 
ATOM   4027 C  CB  . GLN B  1  187 ? 8.816   -10.988 76.884 1.00 51.21  ? 200 GLN B CB  1 
ATOM   4028 C  CG  . GLN B  1  187 ? 8.952   -10.269 78.224 1.00 57.60  ? 200 GLN B CG  1 
ATOM   4029 C  CD  . GLN B  1  187 ? 8.206   -10.979 79.335 1.00 59.75  ? 200 GLN B CD  1 
ATOM   4030 O  OE1 . GLN B  1  187 ? 6.976   -11.084 79.295 1.00 65.54  ? 200 GLN B OE1 1 
ATOM   4031 N  NE2 . GLN B  1  187 ? 8.937   -11.493 80.318 1.00 60.43  ? 200 GLN B NE2 1 
ATOM   4032 N  N   . PHE B  1  188 ? 8.250   -13.998 75.486 1.00 48.53  ? 201 PHE B N   1 
ATOM   4033 C  CA  . PHE B  1  188 ? 7.828   -14.675 74.271 1.00 43.29  ? 201 PHE B CA  1 
ATOM   4034 C  C   . PHE B  1  188 ? 6.318   -14.915 74.311 1.00 40.30  ? 201 PHE B C   1 
ATOM   4035 O  O   . PHE B  1  188 ? 5.859   -16.052 74.370 1.00 35.80  ? 201 PHE B O   1 
ATOM   4036 C  CB  . PHE B  1  188 ? 8.650   -15.957 74.143 1.00 41.25  ? 201 PHE B CB  1 
ATOM   4037 C  CG  . PHE B  1  188 ? 8.759   -16.518 72.734 1.00 38.51  ? 201 PHE B CG  1 
ATOM   4038 C  CD1 . PHE B  1  188 ? 9.484   -15.843 71.764 1.00 42.92  ? 201 PHE B CD1 1 
ATOM   4039 C  CD2 . PHE B  1  188 ? 8.191   -17.735 72.396 1.00 40.99  ? 201 PHE B CD2 1 
ATOM   4040 C  CE1 . PHE B  1  188 ? 9.593   -16.339 70.476 1.00 42.45  ? 201 PHE B CE1 1 
ATOM   4041 C  CE2 . PHE B  1  188 ? 8.308   -18.238 71.107 1.00 44.91  ? 201 PHE B CE2 1 
ATOM   4042 C  CZ  . PHE B  1  188 ? 9.009   -17.536 70.149 1.00 44.29  ? 201 PHE B CZ  1 
ATOM   4043 N  N   . LYS B  1  189 ? 5.547   -13.826 74.238 1.00 43.37  ? 202 LYS B N   1 
ATOM   4044 C  CA  . LYS B  1  189 ? 4.094   -13.895 74.368 1.00 49.15  ? 202 LYS B CA  1 
ATOM   4045 C  C   . LYS B  1  189 ? 3.416   -12.910 73.413 1.00 43.06  ? 202 LYS B C   1 
ATOM   4046 O  O   . LYS B  1  189 ? 4.065   -12.048 72.829 1.00 44.85  ? 202 LYS B O   1 
ATOM   4047 C  CB  . LYS B  1  189 ? 3.690   -13.603 75.818 1.00 47.54  ? 202 LYS B CB  1 
ATOM   4048 C  CG  . LYS B  1  189 ? 4.209   -12.264 76.355 1.00 53.27  ? 202 LYS B CG  1 
ATOM   4049 C  CD  . LYS B  1  189 ? 3.711   -11.889 77.747 1.00 53.10  ? 202 LYS B CD  1 
ATOM   4050 C  CE  . LYS B  1  189 ? 4.064   -12.921 78.763 1.00 53.05  ? 202 LYS B CE  1 
ATOM   4051 N  NZ  . LYS B  1  189 ? 3.592   -12.496 80.078 1.00 53.18  ? 202 LYS B NZ  1 
ATOM   4052 N  N   . ASN B  1  190 ? 2.099   -13.071 73.267 1.00 44.61  ? 203 ASN B N   1 
ATOM   4053 C  CA  . ASN B  1  190 ? 1.245   -12.179 72.500 1.00 43.58  ? 203 ASN B CA  1 
ATOM   4054 C  C   . ASN B  1  190 ? 1.798   -12.030 71.080 1.00 43.34  ? 203 ASN B C   1 
ATOM   4055 O  O   . ASN B  1  190 ? 1.949   -13.019 70.372 1.00 45.40  ? 203 ASN B O   1 
ATOM   4056 C  CB  . ASN B  1  190 ? 0.977   -10.897 73.288 1.00 44.30  ? 203 ASN B CB  1 
ATOM   4057 C  CG  . ASN B  1  190 ? 0.232   -11.194 74.578 1.00 47.43  ? 203 ASN B CG  1 
ATOM   4058 O  OD1 . ASN B  1  190 ? -0.794  -11.893 74.575 1.00 44.57  ? 203 ASN B OD1 1 
ATOM   4059 N  ND2 . ASN B  1  190 ? 0.729   -10.690 75.698 1.00 45.62  ? 203 ASN B ND2 1 
ATOM   4060 N  N   . VAL B  1  191 ? 2.095   -10.798 70.658 1.00 39.78  ? 204 VAL B N   1 
ATOM   4061 C  CA  . VAL B  1  191 ? 2.472   -10.541 69.282 1.00 42.82  ? 204 VAL B CA  1 
ATOM   4062 C  C   . VAL B  1  191 ? 3.712   -11.361 68.933 1.00 42.24  ? 204 VAL B C   1 
ATOM   4063 O  O   . VAL B  1  191 ? 3.765   -11.976 67.869 1.00 39.43  ? 204 VAL B O   1 
ATOM   4064 C  CB  . VAL B  1  191 ? 2.714   -9.039  69.029 1.00 44.30  ? 204 VAL B CB  1 
ATOM   4065 C  CG1 . VAL B  1  191 ? 3.272   -8.773  67.635 1.00 43.86  ? 204 VAL B CG1 1 
ATOM   4066 C  CG2 . VAL B  1  191 ? 1.455   -8.210  69.262 1.00 43.19  ? 204 VAL B CG2 1 
ATOM   4067 N  N   . ARG B  1  192 ? 4.715   -11.349 69.818 1.00 38.35  ? 205 ARG B N   1 
ATOM   4068 C  CA  . ARG B  1  192 ? 5.995   -11.950 69.496 1.00 40.20  ? 205 ARG B CA  1 
ATOM   4069 C  C   . ARG B  1  192 ? 5.838   -13.454 69.285 1.00 38.71  ? 205 ARG B C   1 
ATOM   4070 O  O   . ARG B  1  192 ? 6.438   -14.012 68.372 1.00 38.14  ? 205 ARG B O   1 
ATOM   4071 C  CB  . ARG B  1  192 ? 7.051   -11.636 70.562 1.00 43.87  ? 205 ARG B CB  1 
ATOM   4072 C  CG  . ARG B  1  192 ? 8.425   -12.188 70.207 1.00 46.45  ? 205 ARG B CG  1 
ATOM   4073 C  CD  . ARG B  1  192 ? 8.892   -11.734 68.837 1.00 45.04  ? 205 ARG B CD  1 
ATOM   4074 N  NE  . ARG B  1  192 ? 10.147  -12.373 68.437 1.00 45.77  ? 205 ARG B NE  1 
ATOM   4075 C  CZ  . ARG B  1  192 ? 10.628  -12.463 67.193 1.00 46.39  ? 205 ARG B CZ  1 
ATOM   4076 N  NH1 . ARG B  1  192 ? 9.977   -11.937 66.168 1.00 46.42  ? 205 ARG B NH1 1 
ATOM   4077 N  NH2 . ARG B  1  192 ? 11.765  -13.100 66.984 1.00 41.07  ? 205 ARG B NH2 1 
ATOM   4078 N  N   . PHE B  1  193 ? 5.030   -14.108 70.123 1.00 38.03  ? 206 PHE B N   1 
ATOM   4079 C  CA  . PHE B  1  193 ? 4.823   -15.541 70.009 1.00 38.75  ? 206 PHE B CA  1 
ATOM   4080 C  C   . PHE B  1  193 ? 4.305   -15.881 68.614 1.00 41.00  ? 206 PHE B C   1 
ATOM   4081 O  O   . PHE B  1  193 ? 4.755   -16.853 68.013 1.00 45.44  ? 206 PHE B O   1 
ATOM   4082 C  CB  . PHE B  1  193 ? 3.866   -16.070 71.082 1.00 41.62  ? 206 PHE B CB  1 
ATOM   4083 C  CG  . PHE B  1  193 ? 3.674   -17.580 71.029 1.00 43.55  ? 206 PHE B CG  1 
ATOM   4084 C  CD1 . PHE B  1  193 ? 4.665   -18.431 71.491 1.00 41.15  ? 206 PHE B CD1 1 
ATOM   4085 C  CD2 . PHE B  1  193 ? 2.509   -18.144 70.521 1.00 47.20  ? 206 PHE B CD2 1 
ATOM   4086 C  CE1 . PHE B  1  193 ? 4.496   -19.802 71.441 1.00 45.20  ? 206 PHE B CE1 1 
ATOM   4087 C  CE2 . PHE B  1  193 ? 2.349   -19.517 70.471 1.00 45.20  ? 206 PHE B CE2 1 
ATOM   4088 C  CZ  . PHE B  1  193 ? 3.341   -20.342 70.934 1.00 46.78  ? 206 PHE B CZ  1 
ATOM   4089 N  N   . ILE B  1  194 ? 3.372   -15.076 68.086 1.00 41.90  ? 207 ILE B N   1 
ATOM   4090 C  CA  . ILE B  1  194 ? 2.741   -15.393 66.813 1.00 40.47  ? 207 ILE B CA  1 
ATOM   4091 C  C   . ILE B  1  194 ? 3.679   -15.049 65.659 1.00 37.65  ? 207 ILE B C   1 
ATOM   4092 O  O   . ILE B  1  194 ? 3.906   -15.890 64.804 1.00 41.21  ? 207 ILE B O   1 
ATOM   4093 C  CB  . ILE B  1  194 ? 1.375   -14.690 66.685 1.00 43.47  ? 207 ILE B CB  1 
ATOM   4094 C  CG1 . ILE B  1  194 ? 0.445   -15.031 67.858 1.00 44.20  ? 207 ILE B CG1 1 
ATOM   4095 C  CG2 . ILE B  1  194 ? 0.719   -15.003 65.335 1.00 41.13  ? 207 ILE B CG2 1 
ATOM   4096 C  CD1 . ILE B  1  194 ? 0.102   -16.508 67.974 1.00 46.93  ? 207 ILE B CD1 1 
ATOM   4097 N  N   . THR B  1  195 ? 4.233   -13.829 65.654 1.00 38.76  ? 208 THR B N   1 
ATOM   4098 C  CA  . THR B  1  195 ? 5.020   -13.348 64.533 1.00 44.07  ? 208 THR B CA  1 
ATOM   4099 C  C   . THR B  1  195 ? 6.327   -14.130 64.409 1.00 47.13  ? 208 THR B C   1 
ATOM   4100 O  O   . THR B  1  195 ? 6.849   -14.256 63.313 1.00 51.93  ? 208 THR B O   1 
ATOM   4101 C  CB  . THR B  1  195 ? 5.284   -11.847 64.652 1.00 49.59  ? 208 THR B CB  1 
ATOM   4102 O  OG1 . THR B  1  195 ? 5.964   -11.607 65.878 1.00 54.92  ? 208 THR B OG1 1 
ATOM   4103 C  CG2 . THR B  1  195 ? 4.015   -11.018 64.580 1.00 49.20  ? 208 THR B CG2 1 
ATOM   4104 N  N   . ALA B  1  196 ? 6.850   -14.664 65.516 1.00 50.17  ? 209 ALA B N   1 
ATOM   4105 C  CA  . ALA B  1  196 ? 8.130   -15.358 65.508 1.00 52.51  ? 209 ALA B CA  1 
ATOM   4106 C  C   . ALA B  1  196 ? 8.082   -16.638 64.680 1.00 52.13  ? 209 ALA B C   1 
ATOM   4107 O  O   . ALA B  1  196 ? 9.077   -16.980 64.059 1.00 52.52  ? 209 ALA B O   1 
ATOM   4108 C  CB  . ALA B  1  196 ? 8.576   -15.664 66.919 1.00 55.22  ? 209 ALA B CB  1 
ATOM   4109 N  N   . TYR B  1  197 ? 6.956   -17.363 64.689 1.00 47.50  ? 210 TYR B N   1 
ATOM   4110 C  CA  . TYR B  1  197 ? 6.885   -18.604 63.935 1.00 45.54  ? 210 TYR B CA  1 
ATOM   4111 C  C   . TYR B  1  197 ? 6.770   -18.275 62.445 1.00 43.87  ? 210 TYR B C   1 
ATOM   4112 O  O   . TYR B  1  197 ? 7.371   -18.968 61.628 1.00 43.83  ? 210 TYR B O   1 
ATOM   4113 C  CB  . TYR B  1  197 ? 5.804   -19.527 64.511 1.00 44.53  ? 210 TYR B CB  1 
ATOM   4114 C  CG  . TYR B  1  197 ? 6.260   -20.179 65.807 1.00 42.07  ? 210 TYR B CG  1 
ATOM   4115 C  CD1 . TYR B  1  197 ? 6.958   -21.382 65.799 1.00 44.08  ? 210 TYR B CD1 1 
ATOM   4116 C  CD2 . TYR B  1  197 ? 6.080   -19.548 67.030 1.00 42.31  ? 210 TYR B CD2 1 
ATOM   4117 C  CE1 . TYR B  1  197 ? 7.434   -21.954 66.969 1.00 43.13  ? 210 TYR B CE1 1 
ATOM   4118 C  CE2 . TYR B  1  197 ? 6.548   -20.107 68.205 1.00 43.91  ? 210 TYR B CE2 1 
ATOM   4119 C  CZ  . TYR B  1  197 ? 7.224   -21.317 68.178 1.00 44.55  ? 210 TYR B CZ  1 
ATOM   4120 O  OH  . TYR B  1  197 ? 7.694   -21.872 69.335 1.00 44.77  ? 210 TYR B OH  1 
ATOM   4121 N  N   . GLY B  1  198 ? 6.033   -17.208 62.098 1.00 40.58  ? 211 GLY B N   1 
ATOM   4122 C  CA  . GLY B  1  198 ? 5.915   -16.766 60.716 1.00 40.14  ? 211 GLY B CA  1 
ATOM   4123 C  C   . GLY B  1  198 ? 7.268   -16.355 60.129 1.00 39.24  ? 211 GLY B C   1 
ATOM   4124 O  O   . GLY B  1  198 ? 7.594   -16.699 58.995 1.00 38.33  ? 211 GLY B O   1 
ATOM   4125 N  N   . GLU B  1  199 ? 8.062   -15.631 60.925 1.00 39.62  ? 212 GLU B N   1 
ATOM   4126 C  CA  A GLU B  1  199 ? 9.335   -15.104 60.467 0.50 37.90  ? 212 GLU B CA  1 
ATOM   4127 C  CA  B GLU B  1  199 ? 9.349   -15.095 60.499 0.50 40.74  ? 212 GLU B CA  1 
ATOM   4128 C  C   . GLU B  1  199 ? 10.280  -16.245 60.093 1.00 39.45  ? 212 GLU B C   1 
ATOM   4129 O  O   . GLU B  1  199 ? 11.073  -16.098 59.173 1.00 42.23  ? 212 GLU B O   1 
ATOM   4130 C  CB  A GLU B  1  199 ? 9.864   -14.099 61.489 0.50 36.35  ? 212 GLU B CB  1 
ATOM   4131 C  CB  B GLU B  1  199 ? 9.933   -14.154 61.571 0.50 43.36  ? 212 GLU B CB  1 
ATOM   4132 C  CG  A GLU B  1  199 ? 9.153   -12.752 61.368 0.50 33.99  ? 212 GLU B CG  1 
ATOM   4133 C  CG  B GLU B  1  199 ? 10.951  -14.789 62.531 0.50 45.25  ? 212 GLU B CG  1 
ATOM   4134 C  CD  A GLU B  1  199 ? 9.170   -11.889 62.611 0.50 32.65  ? 212 GLU B CD  1 
ATOM   4135 C  CD  B GLU B  1  199 ? 11.612  -13.969 63.648 0.50 43.03  ? 212 GLU B CD  1 
ATOM   4136 O  OE1 A GLU B  1  199 ? 10.022  -12.152 63.478 0.50 30.67  ? 212 GLU B OE1 1 
ATOM   4137 O  OE1 B GLU B  1  199 ? 11.496  -12.730 63.800 0.50 42.37  ? 212 GLU B OE1 1 
ATOM   4138 O  OE2 A GLU B  1  199 ? 8.323   -10.972 62.715 0.50 34.47  ? 212 GLU B OE2 1 
ATOM   4139 O  OE2 B GLU B  1  199 ? 12.295  -14.645 64.426 0.50 39.22  ? 212 GLU B OE2 1 
ATOM   4140 N  N   . THR B  1  200 ? 10.169  -17.405 60.764 1.00 38.51  ? 213 THR B N   1 
ATOM   4141 C  CA  . THR B  1  200 ? 11.095  -18.502 60.532 1.00 40.58  ? 213 THR B CA  1 
ATOM   4142 C  C   . THR B  1  200 ? 10.839  -19.174 59.187 1.00 36.11  ? 213 THR B C   1 
ATOM   4143 O  O   . THR B  1  200 ? 11.744  -19.854 58.709 1.00 36.12  ? 213 THR B O   1 
ATOM   4144 C  CB  . THR B  1  200 ? 11.078  -19.553 61.647 1.00 44.85  ? 213 THR B CB  1 
ATOM   4145 O  OG1 . THR B  1  200 ? 9.887   -20.320 61.529 1.00 53.91  ? 213 THR B OG1 1 
ATOM   4146 C  CG2 . THR B  1  200 ? 11.170  -18.945 63.026 1.00 45.38  ? 213 THR B CG2 1 
ATOM   4147 N  N   . VAL B  1  201 ? 9.630   -19.031 58.607 1.00 35.81  ? 214 VAL B N   1 
ATOM   4148 C  CA  . VAL B  1  201 ? 9.324   -19.654 57.322 1.00 34.28  ? 214 VAL B CA  1 
ATOM   4149 C  C   . VAL B  1  201 ? 9.391   -18.650 56.171 1.00 33.61  ? 214 VAL B C   1 
ATOM   4150 O  O   . VAL B  1  201 ? 9.477   -19.058 55.020 1.00 35.30  ? 214 VAL B O   1 
ATOM   4151 C  CB  . VAL B  1  201 ? 7.983   -20.411 57.296 1.00 38.25  ? 214 VAL B CB  1 
ATOM   4152 C  CG1 . VAL B  1  201 ? 7.998   -21.584 58.263 1.00 36.25  ? 214 VAL B CG1 1 
ATOM   4153 C  CG2 . VAL B  1  201 ? 6.778   -19.508 57.543 1.00 39.69  ? 214 VAL B CG2 1 
ATOM   4154 N  N   . PHE B  1  202 ? 9.361   -17.344 56.458 1.00 36.57  ? 215 PHE B N   1 
ATOM   4155 C  CA  . PHE B  1  202 ? 9.482   -16.336 55.416 1.00 36.55  ? 215 PHE B CA  1 
ATOM   4156 C  C   . PHE B  1  202 ? 10.727  -16.584 54.560 1.00 37.93  ? 215 PHE B C   1 
ATOM   4157 O  O   . PHE B  1  202 ? 10.661  -16.425 53.342 1.00 36.96  ? 215 PHE B O   1 
ATOM   4158 C  CB  . PHE B  1  202 ? 9.485   -14.905 55.960 1.00 37.04  ? 215 PHE B CB  1 
ATOM   4159 C  CG  . PHE B  1  202 ? 8.174   -14.387 56.539 1.00 41.17  ? 215 PHE B CG  1 
ATOM   4160 C  CD1 . PHE B  1  202 ? 6.975   -15.079 56.388 1.00 43.73  ? 215 PHE B CD1 1 
ATOM   4161 C  CD2 . PHE B  1  202 ? 8.135   -13.174 57.209 1.00 41.75  ? 215 PHE B CD2 1 
ATOM   4162 C  CE1 . PHE B  1  202 ? 5.788   -14.587 56.918 1.00 42.32  ? 215 PHE B CE1 1 
ATOM   4163 C  CE2 . PHE B  1  202 ? 6.949   -12.695 57.749 1.00 42.34  ? 215 PHE B CE2 1 
ATOM   4164 C  CZ  . PHE B  1  202 ? 5.775   -13.388 57.583 1.00 38.96  ? 215 PHE B CZ  1 
ATOM   4165 N  N   . PRO B  1  203 ? 11.898  -16.959 55.121 1.00 38.88  ? 216 PRO B N   1 
ATOM   4166 C  CA  . PRO B  1  203 ? 13.074  -17.235 54.294 1.00 41.03  ? 216 PRO B CA  1 
ATOM   4167 C  C   . PRO B  1  203 ? 12.847  -18.311 53.241 1.00 38.68  ? 216 PRO B C   1 
ATOM   4168 O  O   . PRO B  1  203 ? 13.419  -18.240 52.154 1.00 43.19  ? 216 PRO B O   1 
ATOM   4169 C  CB  . PRO B  1  203 ? 14.147  -17.631 55.318 1.00 40.55  ? 216 PRO B CB  1 
ATOM   4170 C  CG  . PRO B  1  203 ? 13.732  -16.913 56.577 1.00 39.27  ? 216 PRO B CG  1 
ATOM   4171 C  CD  . PRO B  1  203 ? 12.209  -17.029 56.553 1.00 41.07  ? 216 PRO B CD  1 
ATOM   4172 N  N   . ILE B  1  204 ? 12.004  -19.292 53.577 1.00 38.27  ? 217 ILE B N   1 
ATOM   4173 C  CA  . ILE B  1  204 ? 11.687  -20.399 52.684 1.00 41.26  ? 217 ILE B CA  1 
ATOM   4174 C  C   . ILE B  1  204 ? 10.677  -19.949 51.628 1.00 39.10  ? 217 ILE B C   1 
ATOM   4175 O  O   . ILE B  1  204 ? 10.858  -20.211 50.442 1.00 38.58  ? 217 ILE B O   1 
ATOM   4176 C  CB  . ILE B  1  204 ? 11.171  -21.607 53.489 1.00 41.22  ? 217 ILE B CB  1 
ATOM   4177 C  CG1 . ILE B  1  204 ? 12.218  -22.106 54.473 1.00 41.55  ? 217 ILE B CG1 1 
ATOM   4178 C  CG2 . ILE B  1  204 ? 10.695  -22.727 52.563 1.00 41.99  ? 217 ILE B CG2 1 
ATOM   4179 C  CD1 . ILE B  1  204 ? 11.665  -23.046 55.529 1.00 44.16  ? 217 ILE B CD1 1 
ATOM   4180 N  N   . ASN B  1  205 ? 9.593   -19.301 52.073 1.00 40.10  ? 218 ASN B N   1 
ATOM   4181 C  CA  . ASN B  1  205 ? 8.459   -19.013 51.205 1.00 36.36  ? 218 ASN B CA  1 
ATOM   4182 C  C   . ASN B  1  205 ? 8.700   -17.770 50.361 1.00 36.33  ? 218 ASN B C   1 
ATOM   4183 O  O   . ASN B  1  205 ? 8.102   -17.666 49.289 1.00 39.98  ? 218 ASN B O   1 
ATOM   4184 C  CB  . ASN B  1  205 ? 7.160   -18.854 51.981 1.00 35.20  ? 218 ASN B CB  1 
ATOM   4185 C  CG  . ASN B  1  205 ? 6.816   -20.098 52.762 1.00 34.22  ? 218 ASN B CG  1 
ATOM   4186 O  OD1 . ASN B  1  205 ? 7.160   -21.199 52.343 1.00 37.66  ? 218 ASN B OD1 1 
ATOM   4187 N  ND2 . ASN B  1  205 ? 6.173   -19.952 53.908 1.00 36.73  ? 218 ASN B ND2 1 
ATOM   4188 N  N   . LEU B  1  206 ? 9.550   -16.839 50.835 1.00 34.86  ? 219 LEU B N   1 
ATOM   4189 C  CA  . LEU B  1  206 ? 9.712   -15.567 50.145 1.00 34.71  ? 219 LEU B CA  1 
ATOM   4190 C  C   . LEU B  1  206 ? 11.147  -15.275 49.696 1.00 33.60  ? 219 LEU B C   1 
ATOM   4191 O  O   . LEU B  1  206 ? 11.309  -14.474 48.782 1.00 33.02  ? 219 LEU B O   1 
ATOM   4192 C  CB  . LEU B  1  206 ? 9.154   -14.472 51.048 1.00 35.33  ? 219 LEU B CB  1 
ATOM   4193 C  CG  . LEU B  1  206 ? 7.685   -14.644 51.457 1.00 38.10  ? 219 LEU B CG  1 
ATOM   4194 C  CD1 . LEU B  1  206 ? 7.294   -13.756 52.612 1.00 39.74  ? 219 LEU B CD1 1 
ATOM   4195 C  CD2 . LEU B  1  206 ? 6.754   -14.389 50.285 1.00 39.49  ? 219 LEU B CD2 1 
ATOM   4196 N  N   . PHE B  1  207 ? 12.176  -15.851 50.341 1.00 36.53  ? 220 PHE B N   1 
ATOM   4197 C  CA  . PHE B  1  207 ? 13.560  -15.494 50.031 1.00 37.10  ? 220 PHE B CA  1 
ATOM   4198 C  C   . PHE B  1  207 ? 14.132  -16.460 48.994 1.00 35.74  ? 220 PHE B C   1 
ATOM   4199 O  O   . PHE B  1  207 ? 15.130  -16.150 48.344 1.00 39.57  ? 220 PHE B O   1 
ATOM   4200 C  CB  . PHE B  1  207 ? 14.480  -15.475 51.258 1.00 37.80  ? 220 PHE B CB  1 
ATOM   4201 C  CG  . PHE B  1  207 ? 14.233  -14.373 52.275 1.00 40.82  ? 220 PHE B CG  1 
ATOM   4202 C  CD1 . PHE B  1  207 ? 13.354  -13.328 52.015 1.00 41.89  ? 220 PHE B CD1 1 
ATOM   4203 C  CD2 . PHE B  1  207 ? 14.939  -14.356 53.475 1.00 40.41  ? 220 PHE B CD2 1 
ATOM   4204 C  CE1 . PHE B  1  207 ? 13.168  -12.313 52.946 1.00 44.82  ? 220 PHE B CE1 1 
ATOM   4205 C  CE2 . PHE B  1  207 ? 14.739  -13.350 54.403 1.00 40.31  ? 220 PHE B CE2 1 
ATOM   4206 C  CZ  . PHE B  1  207 ? 13.857  -12.332 54.140 1.00 42.66  ? 220 PHE B CZ  1 
ATOM   4207 N  N   . VAL B  1  208 ? 13.506  -17.636 48.868 1.00 34.53  ? 221 VAL B N   1 
ATOM   4208 C  CA  . VAL B  1  208 ? 13.860  -18.605 47.847 1.00 38.56  ? 221 VAL B CA  1 
ATOM   4209 C  C   . VAL B  1  208 ? 13.209  -18.202 46.522 1.00 38.78  ? 221 VAL B C   1 
ATOM   4210 O  O   . VAL B  1  208 ? 12.010  -17.933 46.470 1.00 37.67  ? 221 VAL B O   1 
ATOM   4211 C  CB  . VAL B  1  208 ? 13.445  -20.035 48.241 1.00 37.29  ? 221 VAL B CB  1 
ATOM   4212 C  CG1 . VAL B  1  208 ? 13.686  -21.031 47.109 1.00 35.65  ? 221 VAL B CG1 1 
ATOM   4213 C  CG2 . VAL B  1  208 ? 14.148  -20.493 49.512 1.00 36.88  ? 221 VAL B CG2 1 
ATOM   4214 N  N   . ASP B  1  209 ? 14.024  -18.197 45.460 1.00 35.53  ? 222 ASP B N   1 
ATOM   4215 C  CA  . ASP B  1  209 ? 13.607  -17.782 44.132 1.00 36.75  ? 222 ASP B CA  1 
ATOM   4216 C  C   . ASP B  1  209 ? 12.328  -18.522 43.732 1.00 36.32  ? 222 ASP B C   1 
ATOM   4217 O  O   . ASP B  1  209 ? 12.189  -19.716 43.987 1.00 34.48  ? 222 ASP B O   1 
ATOM   4218 C  CB  . ASP B  1  209 ? 14.756  -17.966 43.151 1.00 34.38  ? 222 ASP B CB  1 
ATOM   4219 C  CG  . ASP B  1  209 ? 14.539  -17.325 41.797 1.00 34.04  ? 222 ASP B CG  1 
ATOM   4220 O  OD1 . ASP B  1  209 ? 13.693  -17.849 41.056 1.00 36.55  ? 222 ASP B OD1 1 
ATOM   4221 O  OD2 . ASP B  1  209 ? 15.182  -16.291 41.514 1.00 34.82  ? 222 ASP B OD2 1 
ATOM   4222 N  N   . GLY B  1  210 ? 11.405  -17.805 43.079 1.00 41.61  ? 223 GLY B N   1 
ATOM   4223 C  CA  . GLY B  1  210 ? 10.082  -18.325 42.757 1.00 43.39  ? 223 GLY B CA  1 
ATOM   4224 C  C   . GLY B  1  210 ? 10.068  -19.368 41.634 1.00 45.94  ? 223 GLY B C   1 
ATOM   4225 O  O   . GLY B  1  210 ? 9.094   -20.115 41.507 1.00 46.20  ? 223 GLY B O   1 
ATOM   4226 N  N   . ARG B  1  211 ? 11.130  -19.396 40.813 1.00 45.37  ? 224 ARG B N   1 
ATOM   4227 C  CA  . ARG B  1  211 ? 11.299  -20.408 39.778 1.00 43.96  ? 224 ARG B CA  1 
ATOM   4228 C  C   . ARG B  1  211 ? 11.631  -21.766 40.398 1.00 42.44  ? 224 ARG B C   1 
ATOM   4229 O  O   . ARG B  1  211 ? 11.553  -22.779 39.727 1.00 50.29  ? 224 ARG B O   1 
ATOM   4230 C  CB  . ARG B  1  211 ? 12.381  -20.001 38.775 1.00 42.25  ? 224 ARG B CB  1 
ATOM   4231 C  CG  . ARG B  1  211 ? 12.011  -18.775 37.958 1.00 43.06  ? 224 ARG B CG  1 
ATOM   4232 C  CD  . ARG B  1  211 ? 13.203  -18.161 37.249 1.00 46.86  ? 224 ARG B CD  1 
ATOM   4233 N  NE  . ARG B  1  211 ? 14.231  -17.680 38.179 1.00 48.02  ? 224 ARG B NE  1 
ATOM   4234 C  CZ  . ARG B  1  211 ? 15.322  -17.006 37.826 1.00 45.39  ? 224 ARG B CZ  1 
ATOM   4235 N  NH1 . ARG B  1  211 ? 15.553  -16.750 36.553 1.00 40.94  ? 224 ARG B NH1 1 
ATOM   4236 N  NH2 . ARG B  1  211 ? 16.163  -16.579 38.757 1.00 43.33  ? 224 ARG B NH2 1 
ATOM   4237 N  N   . VAL B  1  212 ? 12.041  -21.795 41.668 1.00 44.13  ? 225 VAL B N   1 
ATOM   4238 C  CA  . VAL B  1  212 ? 12.325  -23.046 42.357 1.00 47.37  ? 225 VAL B CA  1 
ATOM   4239 C  C   . VAL B  1  212 ? 10.999  -23.582 42.904 1.00 54.47  ? 225 VAL B C   1 
ATOM   4240 O  O   . VAL B  1  212 ? 10.354  -22.925 43.724 1.00 54.90  ? 225 VAL B O   1 
ATOM   4241 C  CB  . VAL B  1  212 ? 13.374  -22.878 43.478 1.00 46.39  ? 225 VAL B CB  1 
ATOM   4242 C  CG1 . VAL B  1  212 ? 13.618  -24.176 44.236 1.00 43.37  ? 225 VAL B CG1 1 
ATOM   4243 C  CG2 . VAL B  1  212 ? 14.694  -22.302 42.963 1.00 46.23  ? 225 VAL B CG2 1 
ATOM   4244 N  N   . THR B  1  213 ? 10.592  -24.781 42.460 1.00 55.94  ? 226 THR B N   1 
ATOM   4245 C  CA  . THR B  1  213 ? 9.268   -25.292 42.806 1.00 58.58  ? 226 THR B CA  1 
ATOM   4246 C  C   . THR B  1  213 ? 9.333   -26.623 43.552 1.00 58.80  ? 226 THR B C   1 
ATOM   4247 O  O   . THR B  1  213 ? 8.352   -26.987 44.187 1.00 55.53  ? 226 THR B O   1 
ATOM   4248 C  CB  . THR B  1  213 ? 8.381   -25.437 41.566 1.00 60.70  ? 226 THR B CB  1 
ATOM   4249 O  OG1 . THR B  1  213 ? 8.937   -26.409 40.690 1.00 58.26  ? 226 THR B OG1 1 
ATOM   4250 C  CG2 . THR B  1  213 ? 8.260   -24.158 40.758 1.00 57.16  ? 226 THR B CG2 1 
ATOM   4251 N  N   . THR B  1  214 ? 10.438  -27.373 43.442 1.00 65.99  ? 227 THR B N   1 
ATOM   4252 C  CA  . THR B  1  214 ? 10.614  -28.576 44.239 1.00 72.57  ? 227 THR B CA  1 
ATOM   4253 C  C   . THR B  1  214 ? 11.713  -28.318 45.276 1.00 72.22  ? 227 THR B C   1 
ATOM   4254 O  O   . THR B  1  214 ? 12.676  -27.614 44.987 1.00 77.89  ? 227 THR B O   1 
ATOM   4255 C  CB  . THR B  1  214 ? 10.904  -29.754 43.302 1.00 80.82  ? 227 THR B CB  1 
ATOM   4256 O  OG1 . THR B  1  214 ? 10.788  -30.910 44.126 1.00 92.40  ? 227 THR B OG1 1 
ATOM   4257 C  CG2 . THR B  1  214 ? 12.271  -29.713 42.633 1.00 84.91  ? 227 THR B CG2 1 
ATOM   4258 N  N   . ASP B  1  215 ? 11.533  -28.856 46.493 1.00 67.19  ? 228 ASP B N   1 
ATOM   4259 C  CA  . ASP B  1  215 ? 12.567  -28.868 47.524 1.00 68.61  ? 228 ASP B CA  1 
ATOM   4260 C  C   . ASP B  1  215 ? 13.078  -27.450 47.783 1.00 57.07  ? 228 ASP B C   1 
ATOM   4261 O  O   . ASP B  1  215 ? 14.271  -27.186 47.668 1.00 53.49  ? 228 ASP B O   1 
ATOM   4262 C  CB  . ASP B  1  215 ? 13.704  -29.816 47.146 1.00 80.50  ? 228 ASP B CB  1 
ATOM   4263 C  CG  . ASP B  1  215 ? 14.777  -30.076 48.201 1.00 95.66  ? 228 ASP B CG  1 
ATOM   4264 O  OD1 . ASP B  1  215 ? 14.478  -29.929 49.412 1.00 101.83 ? 228 ASP B OD1 1 
ATOM   4265 O  OD2 . ASP B  1  215 ? 15.925  -30.398 47.798 1.00 96.55  ? 228 ASP B OD2 1 
ATOM   4266 N  N   . ARG B  1  216 ? 12.164  -26.538 48.121 1.00 49.30  ? 229 ARG B N   1 
ATOM   4267 C  CA  . ARG B  1  216 ? 12.507  -25.139 48.308 1.00 41.56  ? 229 ARG B CA  1 
ATOM   4268 C  C   . ARG B  1  216 ? 13.393  -25.011 49.549 1.00 43.57  ? 229 ARG B C   1 
ATOM   4269 O  O   . ARG B  1  216 ? 13.030  -25.454 50.634 1.00 47.69  ? 229 ARG B O   1 
ATOM   4270 C  CB  . ARG B  1  216 ? 11.254  -24.255 48.339 1.00 37.85  ? 229 ARG B CB  1 
ATOM   4271 C  CG  . ARG B  1  216 ? 10.624  -24.020 46.970 1.00 38.99  ? 229 ARG B CG  1 
ATOM   4272 C  CD  . ARG B  1  216 ? 9.285   -23.293 47.029 1.00 37.60  ? 229 ARG B CD  1 
ATOM   4273 N  NE  . ARG B  1  216 ? 9.379   -21.934 47.577 1.00 35.94  ? 229 ARG B NE  1 
ATOM   4274 C  CZ  . ARG B  1  216 ? 9.882   -20.876 46.951 1.00 35.50  ? 229 ARG B CZ  1 
ATOM   4275 N  NH1 . ARG B  1  216 ? 10.273  -20.958 45.689 1.00 34.97  ? 229 ARG B NH1 1 
ATOM   4276 N  NH2 . ARG B  1  216 ? 9.980   -19.718 47.588 1.00 38.18  ? 229 ARG B NH2 1 
ATOM   4277 N  N   . LYS B  1  217 ? 14.572  -24.408 49.357 1.00 42.52  ? 230 LYS B N   1 
ATOM   4278 C  CA  . LYS B  1  217 ? 15.584  -24.282 50.391 1.00 41.55  ? 230 LYS B CA  1 
ATOM   4279 C  C   . LYS B  1  217 ? 16.463  -23.079 50.051 1.00 37.94  ? 230 LYS B C   1 
ATOM   4280 O  O   . LYS B  1  217 ? 16.689  -22.775 48.877 1.00 39.47  ? 230 LYS B O   1 
ATOM   4281 C  CB  . LYS B  1  217 ? 16.376  -25.592 50.482 1.00 44.86  ? 230 LYS B CB  1 
ATOM   4282 C  CG  . LYS B  1  217 ? 17.172  -25.979 49.237 1.00 46.99  ? 230 LYS B CG  1 
ATOM   4283 C  CD  . LYS B  1  217 ? 17.789  -27.373 49.275 1.00 54.13  ? 230 LYS B CD  1 
ATOM   4284 C  CE  . LYS B  1  217 ? 18.583  -27.667 48.024 1.00 61.56  ? 230 LYS B CE  1 
ATOM   4285 N  NZ  . LYS B  1  217 ? 19.189  -28.999 48.012 1.00 64.18  ? 230 LYS B NZ  1 
ATOM   4286 N  N   . LEU B  1  218 ? 16.954  -22.396 51.087 1.00 36.87  ? 231 LEU B N   1 
ATOM   4287 C  CA  . LEU B  1  218 ? 17.706  -21.162 50.904 1.00 40.06  ? 231 LEU B CA  1 
ATOM   4288 C  C   . LEU B  1  218 ? 19.202  -21.426 51.095 1.00 37.74  ? 231 LEU B C   1 
ATOM   4289 O  O   . LEU B  1  218 ? 19.613  -21.975 52.114 1.00 41.06  ? 231 LEU B O   1 
ATOM   4290 C  CB  . LEU B  1  218 ? 17.192  -20.110 51.889 1.00 36.70  ? 231 LEU B CB  1 
ATOM   4291 C  CG  . LEU B  1  218 ? 17.727  -18.693 51.678 1.00 38.87  ? 231 LEU B CG  1 
ATOM   4292 C  CD1 . LEU B  1  218 ? 17.219  -18.112 50.378 1.00 38.67  ? 231 LEU B CD1 1 
ATOM   4293 C  CD2 . LEU B  1  218 ? 17.380  -17.793 52.847 1.00 41.11  ? 231 LEU B CD2 1 
ATOM   4294 N  N   . SER B  1  219 ? 20.010  -21.014 50.116 1.00 37.32  ? 232 SER B N   1 
ATOM   4295 C  CA  . SER B  1  219 ? 21.461  -21.054 50.249 1.00 38.12  ? 232 SER B CA  1 
ATOM   4296 C  C   . SER B  1  219 ? 21.911  -20.010 51.272 1.00 36.10  ? 232 SER B C   1 
ATOM   4297 O  O   . SER B  1  219 ? 21.228  -19.002 51.473 1.00 40.24  ? 232 SER B O   1 
ATOM   4298 C  CB  . SER B  1  219 ? 22.124  -20.837 48.917 1.00 33.52  ? 232 SER B CB  1 
ATOM   4299 O  OG  . SER B  1  219 ? 21.991  -19.475 48.523 1.00 34.90  ? 232 SER B OG  1 
ATOM   4300 N  N   . MET B  1  220 ? 23.075  -20.236 51.899 1.00 35.84  ? 233 MET B N   1 
ATOM   4301 C  CA  . MET B  1  220 ? 23.615  -19.287 52.864 1.00 35.86  ? 233 MET B CA  1 
ATOM   4302 C  C   . MET B  1  220 ? 24.051  -17.987 52.183 1.00 32.84  ? 233 MET B C   1 
ATOM   4303 O  O   . MET B  1  220 ? 24.009  -16.924 52.805 1.00 34.57  ? 233 MET B O   1 
ATOM   4304 C  CB  . MET B  1  220 ? 24.775  -19.901 53.650 1.00 37.50  ? 233 MET B CB  1 
ATOM   4305 C  CG  . MET B  1  220 ? 24.387  -21.126 54.460 1.00 36.81  ? 233 MET B CG  1 
ATOM   4306 S  SD  . MET B  1  220 ? 23.030  -20.857 55.625 1.00 40.58  ? 233 MET B SD  1 
ATOM   4307 C  CE  . MET B  1  220 ? 21.664  -21.526 54.674 1.00 40.55  ? 233 MET B CE  1 
ATOM   4308 N  N   . GLU B  1  221 ? 24.429  -18.065 50.900 1.00 34.49  ? 234 GLU B N   1 
ATOM   4309 C  CA  . GLU B  1  221 ? 24.835  -16.891 50.135 1.00 37.99  ? 234 GLU B CA  1 
ATOM   4310 C  C   . GLU B  1  221 ? 23.641  -15.939 49.981 1.00 37.55  ? 234 GLU B C   1 
ATOM   4311 O  O   . GLU B  1  221 ? 23.768  -14.729 50.177 1.00 37.92  ? 234 GLU B O   1 
ATOM   4312 C  CB  . GLU B  1  221 ? 25.416  -17.284 48.771 1.00 37.81  ? 234 GLU B CB  1 
ATOM   4313 C  CG  . GLU B  1  221 ? 26.706  -18.097 48.842 1.00 41.17  ? 234 GLU B CG  1 
ATOM   4314 C  CD  . GLU B  1  221 ? 26.615  -19.610 49.061 1.00 49.52  ? 234 GLU B CD  1 
ATOM   4315 O  OE1 . GLU B  1  221 ? 25.540  -20.217 49.244 1.00 47.04  ? 234 GLU B OE1 1 
ATOM   4316 O  OE2 . GLU B  1  221 ? 27.691  -20.240 48.986 1.00 58.31  ? 234 GLU B OE2 1 
ATOM   4317 N  N   . ASP B  1  222 ? 22.483  -16.509 49.617 1.00 36.60  ? 235 ASP B N   1 
ATOM   4318 C  CA  . ASP B  1  222 ? 21.255  -15.752 49.437 1.00 37.84  ? 235 ASP B CA  1 
ATOM   4319 C  C   . ASP B  1  222 ? 20.781  -15.202 50.777 1.00 33.26  ? 235 ASP B C   1 
ATOM   4320 O  O   . ASP B  1  222 ? 20.414  -14.031 50.861 1.00 33.05  ? 235 ASP B O   1 
ATOM   4321 C  CB  . ASP B  1  222 ? 20.199  -16.561 48.696 1.00 39.14  ? 235 ASP B CB  1 
ATOM   4322 C  CG  . ASP B  1  222 ? 20.455  -16.783 47.207 1.00 41.99  ? 235 ASP B CG  1 
ATOM   4323 O  OD1 . ASP B  1  222 ? 21.427  -16.209 46.682 1.00 40.44  ? 235 ASP B OD1 1 
ATOM   4324 O  OD2 . ASP B  1  222 ? 19.674  -17.531 46.578 1.00 45.57  ? 235 ASP B OD2 1 
ATOM   4325 N  N   . ALA B  1  223 ? 20.830  -16.031 51.824 1.00 32.52  ? 236 ALA B N   1 
ATOM   4326 C  CA  . ALA B  1  223 ? 20.524  -15.563 53.172 1.00 35.46  ? 236 ALA B CA  1 
ATOM   4327 C  C   . ALA B  1  223 ? 21.410  -14.374 53.562 1.00 34.64  ? 236 ALA B C   1 
ATOM   4328 O  O   . ALA B  1  223 ? 20.910  -13.402 54.104 1.00 36.31  ? 236 ALA B O   1 
ATOM   4329 C  CB  . ALA B  1  223 ? 20.667  -16.698 54.155 1.00 35.14  ? 236 ALA B CB  1 
ATOM   4330 N  N   . ALA B  1  224 ? 22.725  -14.450 53.314 1.00 34.65  ? 237 ALA B N   1 
ATOM   4331 C  CA  . ALA B  1  224 ? 23.620  -13.384 53.743 1.00 39.11  ? 237 ALA B CA  1 
ATOM   4332 C  C   . ALA B  1  224 ? 23.266  -12.102 52.995 1.00 36.95  ? 237 ALA B C   1 
ATOM   4333 O  O   . ALA B  1  224 ? 23.229  -11.015 53.567 1.00 36.59  ? 237 ALA B O   1 
ATOM   4334 C  CB  . ALA B  1  224 ? 25.077  -13.764 53.526 1.00 38.15  ? 237 ALA B CB  1 
ATOM   4335 N  N   . SER B  1  225 ? 22.998  -12.259 51.699 1.00 34.74  ? 238 SER B N   1 
ATOM   4336 C  CA  . SER B  1  225 ? 22.719  -11.129 50.840 1.00 35.35  ? 238 SER B CA  1 
ATOM   4337 C  C   . SER B  1  225 ? 21.527  -10.324 51.377 1.00 33.80  ? 238 SER B C   1 
ATOM   4338 O  O   . SER B  1  225 ? 21.587  -9.098  51.423 1.00 33.44  ? 238 SER B O   1 
ATOM   4339 C  CB  . SER B  1  225 ? 22.524  -11.599 49.412 1.00 36.42  ? 238 SER B CB  1 
ATOM   4340 O  OG  . SER B  1  225 ? 22.283  -10.503 48.538 1.00 40.51  ? 238 SER B OG  1 
ATOM   4341 N  N   . ILE B  1  226 ? 20.456  -11.009 51.800 1.00 34.15  ? 239 ILE B N   1 
ATOM   4342 C  CA  . ILE B  1  226 ? 19.244  -10.337 52.244 1.00 36.60  ? 239 ILE B CA  1 
ATOM   4343 C  C   . ILE B  1  226 ? 19.396  -9.884  53.698 1.00 37.23  ? 239 ILE B C   1 
ATOM   4344 O  O   . ILE B  1  226 ? 19.206  -8.704  53.995 1.00 37.18  ? 239 ILE B O   1 
ATOM   4345 C  CB  . ILE B  1  226 ? 18.023  -11.252 52.046 1.00 37.51  ? 239 ILE B CB  1 
ATOM   4346 C  CG1 . ILE B  1  226 ? 17.770  -11.504 50.561 1.00 38.00  ? 239 ILE B CG1 1 
ATOM   4347 C  CG2 . ILE B  1  226 ? 16.781  -10.696 52.745 1.00 37.10  ? 239 ILE B CG2 1 
ATOM   4348 C  CD1 . ILE B  1  226 ? 16.794  -12.636 50.287 1.00 39.78  ? 239 ILE B CD1 1 
ATOM   4349 N  N   . PHE B  1  227 ? 19.734  -10.824 54.590 1.00 33.32  ? 240 PHE B N   1 
ATOM   4350 C  CA  . PHE B  1  227 ? 19.796  -10.558 56.020 1.00 37.02  ? 240 PHE B CA  1 
ATOM   4351 C  C   . PHE B  1  227 ? 20.873  -9.531  56.393 1.00 37.27  ? 240 PHE B C   1 
ATOM   4352 O  O   . PHE B  1  227 ? 20.682  -8.777  57.344 1.00 40.49  ? 240 PHE B O   1 
ATOM   4353 C  CB  . PHE B  1  227 ? 20.080  -11.832 56.808 1.00 36.87  ? 240 PHE B CB  1 
ATOM   4354 C  CG  . PHE B  1  227 ? 18.900  -12.760 57.044 1.00 39.64  ? 240 PHE B CG  1 
ATOM   4355 C  CD1 . PHE B  1  227 ? 17.885  -12.409 57.927 1.00 38.78  ? 240 PHE B CD1 1 
ATOM   4356 C  CD2 . PHE B  1  227 ? 18.851  -14.024 56.474 1.00 43.34  ? 240 PHE B CD2 1 
ATOM   4357 C  CE1 . PHE B  1  227 ? 16.833  -13.275 58.186 1.00 35.66  ? 240 PHE B CE1 1 
ATOM   4358 C  CE2 . PHE B  1  227 ? 17.789  -14.883 56.732 1.00 44.33  ? 240 PHE B CE2 1 
ATOM   4359 C  CZ  . PHE B  1  227 ? 16.780  -14.503 57.589 1.00 37.95  ? 240 PHE B CZ  1 
ATOM   4360 N  N   . ARG B  1  228 ? 22.005  -9.511  55.679 1.00 34.96  ? 241 ARG B N   1 
ATOM   4361 C  CA  . ARG B  1  228 ? 23.119  -8.646  56.039 1.00 35.16  ? 241 ARG B CA  1 
ATOM   4362 C  C   . ARG B  1  228 ? 23.236  -7.455  55.096 1.00 34.34  ? 241 ARG B C   1 
ATOM   4363 O  O   . ARG B  1  228 ? 23.375  -6.347  55.574 1.00 36.51  ? 241 ARG B O   1 
ATOM   4364 C  CB  . ARG B  1  228 ? 24.457  -9.401  56.096 1.00 38.41  ? 241 ARG B CB  1 
ATOM   4365 C  CG  . ARG B  1  228 ? 25.654  -8.552  56.522 1.00 37.23  ? 241 ARG B CG  1 
ATOM   4366 C  CD  . ARG B  1  228 ? 26.923  -9.374  56.716 1.00 36.26  ? 241 ARG B CD  1 
ATOM   4367 N  NE  . ARG B  1  228 ? 27.445  -9.932  55.461 1.00 36.22  ? 241 ARG B NE  1 
ATOM   4368 C  CZ  . ARG B  1  228 ? 27.831  -11.185 55.246 1.00 38.50  ? 241 ARG B CZ  1 
ATOM   4369 N  NH1 . ARG B  1  228 ? 27.849  -12.030 56.249 1.00 43.81  ? 241 ARG B NH1 1 
ATOM   4370 N  NH2 . ARG B  1  228 ? 28.225  -11.593 54.049 1.00 38.99  ? 241 ARG B NH2 1 
ATOM   4371 N  N   . ASP B  1  229 ? 23.189  -7.668  53.774 1.00 34.26  ? 242 ASP B N   1 
ATOM   4372 C  CA  . ASP B  1  229 ? 23.482  -6.595  52.835 1.00 35.87  ? 242 ASP B CA  1 
ATOM   4373 C  C   . ASP B  1  229 ? 22.220  -5.891  52.329 1.00 37.36  ? 242 ASP B C   1 
ATOM   4374 O  O   . ASP B  1  229 ? 22.349  -4.881  51.634 1.00 36.88  ? 242 ASP B O   1 
ATOM   4375 C  CB  . ASP B  1  229 ? 24.354  -7.080  51.687 1.00 38.20  ? 242 ASP B CB  1 
ATOM   4376 C  CG  . ASP B  1  229 ? 25.709  -7.642  52.095 1.00 40.10  ? 242 ASP B CG  1 
ATOM   4377 O  OD1 . ASP B  1  229 ? 26.299  -7.134  53.086 1.00 39.48  ? 242 ASP B OD1 1 
ATOM   4378 O  OD2 . ASP B  1  229 ? 26.179  -8.560  51.396 1.00 41.39  ? 242 ASP B OD2 1 
ATOM   4379 N  N   . MET B  1  230 ? 21.020  -6.413  52.669 1.00 37.25  ? 243 MET B N   1 
ATOM   4380 C  CA  . MET B  1  230 ? 19.755  -5.813  52.252 1.00 38.57  ? 243 MET B CA  1 
ATOM   4381 C  C   . MET B  1  230 ? 19.655  -5.799  50.722 1.00 36.14  ? 243 MET B C   1 
ATOM   4382 O  O   . MET B  1  230 ? 19.204  -4.815  50.137 1.00 31.38  ? 243 MET B O   1 
ATOM   4383 C  CB  . MET B  1  230 ? 19.618  -4.374  52.769 1.00 38.07  ? 243 MET B CB  1 
ATOM   4384 C  CG  . MET B  1  230 ? 19.940  -4.182  54.248 1.00 42.61  ? 243 MET B CG  1 
ATOM   4385 S  SD  . MET B  1  230 ? 20.003  -2.451  54.770 1.00 41.06  ? 243 MET B SD  1 
ATOM   4386 C  CE  . MET B  1  230 ? 20.556  -2.674  56.462 1.00 54.92  ? 243 MET B CE  1 
ATOM   4387 N  N   . ARG B  1  231 ? 20.109  -6.897  50.097 1.00 37.12  ? 244 ARG B N   1 
ATOM   4388 C  CA  . ARG B  1  231 ? 20.268  -6.996  48.651 1.00 35.87  ? 244 ARG B CA  1 
ATOM   4389 C  C   . ARG B  1  231 ? 19.566  -8.270  48.171 1.00 35.03  ? 244 ARG B C   1 
ATOM   4390 O  O   . ARG B  1  231 ? 19.777  -9.353  48.704 1.00 32.72  ? 244 ARG B O   1 
ATOM   4391 C  CB  . ARG B  1  231 ? 21.751  -6.978  48.265 1.00 35.66  ? 244 ARG B CB  1 
ATOM   4392 C  CG  . ARG B  1  231 ? 22.053  -6.771  46.786 1.00 41.96  ? 244 ARG B CG  1 
ATOM   4393 C  CD  . ARG B  1  231 ? 23.555  -6.831  46.451 1.00 44.95  ? 244 ARG B CD  1 
ATOM   4394 N  NE  . ARG B  1  231 ? 24.168  -8.130  46.748 1.00 56.09  ? 244 ARG B NE  1 
ATOM   4395 C  CZ  . ARG B  1  231 ? 24.002  -9.269  46.044 1.00 69.13  ? 244 ARG B CZ  1 
ATOM   4396 N  NH1 . ARG B  1  231 ? 23.385  -9.291  44.869 1.00 73.61  ? 244 ARG B NH1 1 
ATOM   4397 N  NH2 . ARG B  1  231 ? 24.464  -10.413 46.521 1.00 69.01  ? 244 ARG B NH2 1 
ATOM   4398 N  N   . PHE B  1  232 ? 18.711  -8.131  47.159 1.00 31.07  ? 245 PHE B N   1 
ATOM   4399 C  CA  . PHE B  1  232 ? 18.202  -9.278  46.440 1.00 34.19  ? 245 PHE B CA  1 
ATOM   4400 C  C   . PHE B  1  232 ? 19.357  -10.039 45.808 1.00 35.01  ? 245 PHE B C   1 
ATOM   4401 O  O   . PHE B  1  232 ? 20.304  -9.429  45.319 1.00 35.93  ? 245 PHE B O   1 
ATOM   4402 C  CB  . PHE B  1  232 ? 17.259  -8.887  45.301 1.00 33.33  ? 245 PHE B CB  1 
ATOM   4403 C  CG  . PHE B  1  232 ? 15.909  -8.354  45.751 1.00 35.90  ? 245 PHE B CG  1 
ATOM   4404 C  CD1 . PHE B  1  232 ? 15.001  -9.187  46.397 1.00 34.31  ? 245 PHE B CD1 1 
ATOM   4405 C  CD2 . PHE B  1  232 ? 15.524  -7.046  45.469 1.00 36.30  ? 245 PHE B CD2 1 
ATOM   4406 C  CE1 . PHE B  1  232 ? 13.753  -8.710  46.774 1.00 36.46  ? 245 PHE B CE1 1 
ATOM   4407 C  CE2 . PHE B  1  232 ? 14.271  -6.575  45.842 1.00 36.01  ? 245 PHE B CE2 1 
ATOM   4408 C  CZ  . PHE B  1  232 ? 13.388  -7.406  46.493 1.00 35.84  ? 245 PHE B CZ  1 
ATOM   4409 N  N   . PRO B  1  233 ? 19.307  -11.389 45.790 1.00 34.35  ? 246 PRO B N   1 
ATOM   4410 C  CA  . PRO B  1  233 ? 20.206  -12.170 44.942 1.00 33.21  ? 246 PRO B CA  1 
ATOM   4411 C  C   . PRO B  1  233 ? 20.149  -11.706 43.490 1.00 35.40  ? 246 PRO B C   1 
ATOM   4412 O  O   . PRO B  1  233 ? 19.144  -11.149 43.050 1.00 32.85  ? 246 PRO B O   1 
ATOM   4413 C  CB  . PRO B  1  233 ? 19.694  -13.608 45.106 1.00 36.60  ? 246 PRO B CB  1 
ATOM   4414 C  CG  . PRO B  1  233 ? 18.967  -13.629 46.452 1.00 35.29  ? 246 PRO B CG  1 
ATOM   4415 C  CD  . PRO B  1  233 ? 18.421  -12.217 46.632 1.00 32.45  ? 246 PRO B CD  1 
ATOM   4416 N  N   . ASP B  1  234 ? 21.253  -11.908 42.764 1.00 37.86  ? 247 ASP B N   1 
ATOM   4417 C  CA  . ASP B  1  234 ? 21.290  -11.629 41.332 1.00 39.18  ? 247 ASP B CA  1 
ATOM   4418 C  C   . ASP B  1  234 ? 20.118  -12.341 40.654 1.00 37.44  ? 247 ASP B C   1 
ATOM   4419 O  O   . ASP B  1  234 ? 19.825  -13.489 40.959 1.00 36.71  ? 247 ASP B O   1 
ATOM   4420 C  CB  . ASP B  1  234 ? 22.618  -12.048 40.712 1.00 38.61  ? 247 ASP B CB  1 
ATOM   4421 C  CG  . ASP B  1  234 ? 23.835  -11.205 41.088 1.00 43.26  ? 247 ASP B CG  1 
ATOM   4422 O  OD1 . ASP B  1  234 ? 23.673  -10.216 41.844 1.00 44.70  ? 247 ASP B OD1 1 
ATOM   4423 O  OD2 . ASP B  1  234 ? 24.940  -11.518 40.589 1.00 43.33  ? 247 ASP B OD2 1 
ATOM   4424 N  N   . ASP B  1  235 ? 19.439  -11.637 39.746 1.00 36.30  ? 248 ASP B N   1 
ATOM   4425 C  CA  . ASP B  1  235 ? 18.399  -12.222 38.922 1.00 41.16  ? 248 ASP B CA  1 
ATOM   4426 C  C   . ASP B  1  235 ? 17.225  -12.746 39.768 1.00 41.15  ? 248 ASP B C   1 
ATOM   4427 O  O   . ASP B  1  235 ? 16.547  -13.695 39.371 1.00 39.34  ? 248 ASP B O   1 
ATOM   4428 C  CB  . ASP B  1  235 ? 18.984  -13.292 38.007 1.00 40.99  ? 248 ASP B CB  1 
ATOM   4429 C  CG  . ASP B  1  235 ? 18.044  -13.731 36.890 1.00 43.74  ? 248 ASP B CG  1 
ATOM   4430 O  OD1 . ASP B  1  235 ? 17.514  -12.844 36.184 1.00 49.55  ? 248 ASP B OD1 1 
ATOM   4431 O  OD2 . ASP B  1  235 ? 17.811  -14.947 36.767 1.00 43.01  ? 248 ASP B OD2 1 
ATOM   4432 N  N   . PHE B  1  236 ? 16.959  -12.127 40.927 1.00 37.00  ? 249 PHE B N   1 
ATOM   4433 C  CA  . PHE B  1  236 ? 16.004  -12.699 41.858 1.00 36.15  ? 249 PHE B CA  1 
ATOM   4434 C  C   . PHE B  1  236 ? 14.582  -12.587 41.308 1.00 34.99  ? 249 PHE B C   1 
ATOM   4435 O  O   . PHE B  1  236 ? 14.121  -11.522 40.895 1.00 33.02  ? 249 PHE B O   1 
ATOM   4436 C  CB  . PHE B  1  236 ? 16.077  -12.045 43.236 1.00 38.97  ? 249 PHE B CB  1 
ATOM   4437 C  CG  . PHE B  1  236 ? 15.089  -12.635 44.226 1.00 36.18  ? 249 PHE B CG  1 
ATOM   4438 C  CD1 . PHE B  1  236 ? 15.320  -13.873 44.799 1.00 35.39  ? 249 PHE B CD1 1 
ATOM   4439 C  CD2 . PHE B  1  236 ? 13.946  -11.940 44.589 1.00 36.47  ? 249 PHE B CD2 1 
ATOM   4440 C  CE1 . PHE B  1  236 ? 14.414  -14.409 45.702 1.00 36.68  ? 249 PHE B CE1 1 
ATOM   4441 C  CE2 . PHE B  1  236 ? 13.045  -12.477 45.499 1.00 35.29  ? 249 PHE B CE2 1 
ATOM   4442 C  CZ  . PHE B  1  236 ? 13.284  -13.703 46.057 1.00 33.86  ? 249 PHE B CZ  1 
ATOM   4443 N  N   . HIS B  1  237 ? 13.889  -13.727 41.332 1.00 35.30  ? 250 HIS B N   1 
ATOM   4444 C  CA  . HIS B  1  237 ? 12.493  -13.807 40.930 1.00 38.10  ? 250 HIS B CA  1 
ATOM   4445 C  C   . HIS B  1  237 ? 11.668  -14.120 42.178 1.00 35.20  ? 250 HIS B C   1 
ATOM   4446 O  O   . HIS B  1  237 ? 11.925  -15.105 42.865 1.00 32.89  ? 250 HIS B O   1 
ATOM   4447 C  CB  . HIS B  1  237 ? 12.288  -14.860 39.834 1.00 39.64  ? 250 HIS B CB  1 
ATOM   4448 C  CG  . HIS B  1  237 ? 12.758  -14.459 38.466 1.00 45.70  ? 250 HIS B CG  1 
ATOM   4449 N  ND1 . HIS B  1  237 ? 14.045  -14.041 38.182 1.00 46.38  ? 250 HIS B ND1 1 
ATOM   4450 C  CD2 . HIS B  1  237 ? 12.094  -14.458 37.290 1.00 40.90  ? 250 HIS B CD2 1 
ATOM   4451 C  CE1 . HIS B  1  237 ? 14.138  -13.778 36.882 1.00 49.04  ? 250 HIS B CE1 1 
ATOM   4452 N  NE2 . HIS B  1  237 ? 12.957  -14.013 36.323 1.00 47.37  ? 250 HIS B NE2 1 
ATOM   4453 N  N   . ARG B  1  238 ? 10.661  -13.291 42.450 1.00 34.89  ? 251 ARG B N   1 
ATOM   4454 C  CA  . ARG B  1  238 ? 9.779   -13.508 43.584 1.00 38.77  ? 251 ARG B CA  1 
ATOM   4455 C  C   . ARG B  1  238 ? 8.953   -14.793 43.442 1.00 37.61  ? 251 ARG B C   1 
ATOM   4456 O  O   . ARG B  1  238 ? 8.839   -15.361 42.357 1.00 37.44  ? 251 ARG B O   1 
ATOM   4457 C  CB  . ARG B  1  238 ? 8.829   -12.322 43.736 1.00 39.54  ? 251 ARG B CB  1 
ATOM   4458 C  CG  . ARG B  1  238 ? 7.823   -12.221 42.602 1.00 43.78  ? 251 ARG B CG  1 
ATOM   4459 C  CD  . ARG B  1  238 ? 6.853   -11.069 42.797 1.00 43.93  ? 251 ARG B CD  1 
ATOM   4460 N  NE  . ARG B  1  238 ? 5.692   -11.280 41.928 1.00 45.15  ? 251 ARG B NE  1 
ATOM   4461 C  CZ  . ARG B  1  238 ? 4.759   -10.385 41.631 1.00 46.96  ? 251 ARG B CZ  1 
ATOM   4462 N  NH1 . ARG B  1  238 ? 4.776   -9.203  42.216 1.00 49.36  ? 251 ARG B NH1 1 
ATOM   4463 N  NH2 . ARG B  1  238 ? 3.836   -10.670 40.719 1.00 48.18  ? 251 ARG B NH2 1 
ATOM   4464 N  N   . SER B  1  239 ? 8.365   -15.216 44.576 1.00 37.90  ? 252 SER B N   1 
ATOM   4465 C  CA  . SER B  1  239 ? 7.430   -16.332 44.654 1.00 39.70  ? 252 SER B CA  1 
ATOM   4466 C  C   . SER B  1  239 ? 6.421   -16.278 43.507 1.00 40.70  ? 252 SER B C   1 
ATOM   4467 O  O   . SER B  1  239 ? 5.935   -15.200 43.173 1.00 38.56  ? 252 SER B O   1 
ATOM   4468 C  CB  . SER B  1  239 ? 6.712   -16.317 45.975 1.00 39.05  ? 252 SER B CB  1 
ATOM   4469 O  OG  . SER B  1  239 ? 5.786   -17.391 46.061 1.00 42.37  ? 252 SER B OG  1 
ATOM   4470 N  N   . ALA B  1  240 ? 6.116   -17.441 42.917 1.00 37.43  ? 253 ALA B N   1 
ATOM   4471 C  CA  . ALA B  1  240 ? 5.199   -17.511 41.782 1.00 41.96  ? 253 ALA B CA  1 
ATOM   4472 C  C   . ALA B  1  240 ? 3.744   -17.417 42.257 1.00 46.45  ? 253 ALA B C   1 
ATOM   4473 O  O   . ALA B  1  240 ? 2.850   -17.279 41.428 1.00 47.48  ? 253 ALA B O   1 
ATOM   4474 C  CB  . ALA B  1  240 ? 5.431   -18.780 40.987 1.00 40.99  ? 253 ALA B CB  1 
ATOM   4475 N  N   . VAL B  1  241 ? 3.531   -17.485 43.585 1.00 43.57  ? 254 VAL B N   1 
ATOM   4476 C  CA  . VAL B  1  241 ? 2.229   -17.336 44.216 1.00 44.01  ? 254 VAL B CA  1 
ATOM   4477 C  C   . VAL B  1  241 ? 2.343   -16.347 45.371 1.00 43.21  ? 254 VAL B C   1 
ATOM   4478 O  O   . VAL B  1  241 ? 3.376   -16.285 46.028 1.00 48.60  ? 254 VAL B O   1 
ATOM   4479 C  CB  . VAL B  1  241 ? 1.693   -18.678 44.757 1.00 48.19  ? 254 VAL B CB  1 
ATOM   4480 C  CG1 . VAL B  1  241 ? 1.316   -19.630 43.629 1.00 48.37  ? 254 VAL B CG1 1 
ATOM   4481 C  CG2 . VAL B  1  241 ? 2.673   -19.345 45.718 1.00 49.33  ? 254 VAL B CG2 1 
ATOM   4482 N  N   . PRO B  1  242 ? 1.265   -15.599 45.714 1.00 43.86  ? 255 PRO B N   1 
ATOM   4483 C  CA  . PRO B  1  242 ? 1.210   -14.856 46.979 1.00 42.01  ? 255 PRO B CA  1 
ATOM   4484 C  C   . PRO B  1  242 ? 1.452   -15.800 48.154 1.00 40.85  ? 255 PRO B C   1 
ATOM   4485 O  O   . PRO B  1  242 ? 0.923   -16.909 48.168 1.00 39.53  ? 255 PRO B O   1 
ATOM   4486 C  CB  . PRO B  1  242 ? -0.207  -14.277 46.989 1.00 42.53  ? 255 PRO B CB  1 
ATOM   4487 C  CG  . PRO B  1  242 ? -0.577  -14.200 45.527 1.00 39.33  ? 255 PRO B CG  1 
ATOM   4488 C  CD  . PRO B  1  242 ? 0.028   -15.444 44.931 1.00 40.24  ? 255 PRO B CD  1 
ATOM   4489 N  N   . ALA B  1  243 ? 2.284   -15.390 49.121 1.00 43.00  ? 256 ALA B N   1 
ATOM   4490 C  CA  . ALA B  1  243 ? 2.685   -16.290 50.196 1.00 39.42  ? 256 ALA B CA  1 
ATOM   4491 C  C   . ALA B  1  243 ? 2.961   -15.514 51.483 1.00 38.02  ? 256 ALA B C   1 
ATOM   4492 O  O   . ALA B  1  243 ? 3.195   -14.307 51.442 1.00 38.58  ? 256 ALA B O   1 
ATOM   4493 C  CB  . ALA B  1  243 ? 3.900   -17.078 49.751 1.00 41.98  ? 256 ALA B CB  1 
ATOM   4494 N  N   . SER B  1  244 ? 2.989   -16.239 52.606 1.00 37.98  ? 257 SER B N   1 
ATOM   4495 C  CA  . SER B  1  244 ? 3.125   -15.677 53.947 1.00 41.92  ? 257 SER B CA  1 
ATOM   4496 C  C   . SER B  1  244 ? 3.746   -16.742 54.852 1.00 43.99  ? 257 SER B C   1 
ATOM   4497 O  O   . SER B  1  244 ? 4.906   -17.076 54.658 1.00 41.01  ? 257 SER B O   1 
ATOM   4498 C  CB  . SER B  1  244 ? 1.802   -15.138 54.498 1.00 40.49  ? 257 SER B CB  1 
ATOM   4499 O  OG  . SER B  1  244 ? 0.820   -16.161 54.515 1.00 47.29  ? 257 SER B OG  1 
ATOM   4500 N  N   . ASN B  1  245 ? 2.963   -17.331 55.771 1.00 45.77  ? 258 ASN B N   1 
ATOM   4501 C  CA  . ASN B  1  245 ? 3.507   -18.149 56.844 1.00 41.43  ? 258 ASN B CA  1 
ATOM   4502 C  C   . ASN B  1  245 ? 3.213   -19.639 56.655 1.00 39.79  ? 258 ASN B C   1 
ATOM   4503 O  O   . ASN B  1  245 ? 3.101   -20.368 57.639 1.00 36.19  ? 258 ASN B O   1 
ATOM   4504 C  CB  . ASN B  1  245 ? 2.978   -17.697 58.201 1.00 44.64  ? 258 ASN B CB  1 
ATOM   4505 C  CG  . ASN B  1  245 ? 1.471   -17.765 58.310 1.00 46.21  ? 258 ASN B CG  1 
ATOM   4506 O  OD1 . ASN B  1  245 ? 0.777   -18.011 57.316 1.00 46.46  ? 258 ASN B OD1 1 
ATOM   4507 N  ND2 . ASN B  1  245 ? 0.951   -17.547 59.508 1.00 50.19  ? 258 ASN B ND2 1 
ATOM   4508 N  N   . GLU B  1  246 ? 3.139   -20.117 55.409 1.00 42.61  ? 259 GLU B N   1 
ATOM   4509 C  CA  . GLU B  1  246 ? 2.900   -21.533 55.153 1.00 43.99  ? 259 GLU B CA  1 
ATOM   4510 C  C   . GLU B  1  246 ? 4.036   -22.347 55.784 1.00 46.12  ? 259 GLU B C   1 
ATOM   4511 O  O   . GLU B  1  246 ? 5.210   -22.022 55.589 1.00 46.25  ? 259 GLU B O   1 
ATOM   4512 C  CB  . GLU B  1  246 ? 2.792   -21.833 53.656 1.00 46.80  ? 259 GLU B CB  1 
ATOM   4513 C  CG  . GLU B  1  246 ? 1.588   -21.193 52.967 1.00 49.06  ? 259 GLU B CG  1 
ATOM   4514 C  CD  . GLU B  1  246 ? 1.723   -19.728 52.572 1.00 54.24  ? 259 GLU B CD  1 
ATOM   4515 O  OE1 . GLU B  1  246 ? 2.814   -19.132 52.783 1.00 46.71  ? 259 GLU B OE1 1 
ATOM   4516 O  OE2 . GLU B  1  246 ? 0.712   -19.182 52.070 1.00 54.86  ? 259 GLU B OE2 1 
ATOM   4517 N  N   . GLY B  1  247 ? 3.674   -23.354 56.589 1.00 39.94  ? 260 GLY B N   1 
ATOM   4518 C  CA  . GLY B  1  247 ? 4.628   -24.239 57.232 1.00 40.92  ? 260 GLY B CA  1 
ATOM   4519 C  C   . GLY B  1  247 ? 4.885   -23.869 58.693 1.00 44.10  ? 260 GLY B C   1 
ATOM   4520 O  O   . GLY B  1  247 ? 5.573   -24.599 59.399 1.00 48.59  ? 260 GLY B O   1 
ATOM   4521 N  N   . ALA B  1  248 ? 4.358   -22.728 59.149 1.00 42.42  ? 261 ALA B N   1 
ATOM   4522 C  CA  . ALA B  1  248 ? 4.661   -22.239 60.485 1.00 42.67  ? 261 ALA B CA  1 
ATOM   4523 C  C   . ALA B  1  248 ? 4.112   -23.184 61.559 1.00 48.15  ? 261 ALA B C   1 
ATOM   4524 O  O   . ALA B  1  248 ? 4.705   -23.320 62.633 1.00 46.35  ? 261 ALA B O   1 
ATOM   4525 C  CB  . ALA B  1  248 ? 4.135   -20.841 60.655 1.00 41.31  ? 261 ALA B CB  1 
ATOM   4526 N  N   . ASP B  1  249 ? 2.991   -23.847 61.252 1.00 50.78  ? 262 ASP B N   1 
ATOM   4527 C  CA  A ASP B  1  249 ? 2.400   -24.852 62.123 0.50 52.35  ? 262 ASP B CA  1 
ATOM   4528 C  CA  B ASP B  1  249 ? 2.415   -24.837 62.150 0.50 54.02  ? 262 ASP B CA  1 
ATOM   4529 C  C   . ASP B  1  249 ? 3.356   -26.034 62.315 1.00 50.57  ? 262 ASP B C   1 
ATOM   4530 O  O   . ASP B  1  249 ? 3.451   -26.586 63.407 1.00 46.15  ? 262 ASP B O   1 
ATOM   4531 C  CB  A ASP B  1  249 ? 1.020   -25.275 61.629 0.50 52.31  ? 262 ASP B CB  1 
ATOM   4532 C  CB  B ASP B  1  249 ? 1.002   -25.216 61.729 0.50 56.49  ? 262 ASP B CB  1 
ATOM   4533 C  CG  A ASP B  1  249 ? 0.876   -25.685 60.164 0.50 54.45  ? 262 ASP B CG  1 
ATOM   4534 C  CG  B ASP B  1  249 ? -0.055  -24.174 62.063 0.50 60.80  ? 262 ASP B CG  1 
ATOM   4535 O  OD1 A ASP B  1  249 ? 1.849   -25.549 59.371 0.50 51.29  ? 262 ASP B OD1 1 
ATOM   4536 O  OD1 B ASP B  1  249 ? 0.283   -23.202 62.775 0.50 66.42  ? 262 ASP B OD1 1 
ATOM   4537 O  OD2 A ASP B  1  249 ? -0.245  -26.107 59.803 0.50 54.54  ? 262 ASP B OD2 1 
ATOM   4538 O  OD2 B ASP B  1  249 ? -1.206  -24.339 61.608 0.50 61.76  ? 262 ASP B OD2 1 
ATOM   4539 N  N   . GLN B  1  250 ? 4.066   -26.430 61.249 1.00 49.00  ? 263 GLN B N   1 
ATOM   4540 C  CA  . GLN B  1  250 ? 5.020   -27.531 61.343 1.00 50.25  ? 263 GLN B CA  1 
ATOM   4541 C  C   . GLN B  1  250 ? 6.219   -27.163 62.230 1.00 45.18  ? 263 GLN B C   1 
ATOM   4542 O  O   . GLN B  1  250 ? 6.752   -28.016 62.932 1.00 45.99  ? 263 GLN B O   1 
ATOM   4543 C  CB  . GLN B  1  250 ? 5.469   -27.983 59.956 1.00 53.04  ? 263 GLN B CB  1 
ATOM   4544 C  CG  . GLN B  1  250 ? 4.367   -28.625 59.116 1.00 57.64  ? 263 GLN B CG  1 
ATOM   4545 C  CD  . GLN B  1  250 ? 4.873   -29.187 57.803 1.00 65.97  ? 263 GLN B CD  1 
ATOM   4546 O  OE1 . GLN B  1  250 ? 6.080   -29.199 57.515 1.00 82.93  ? 263 GLN B OE1 1 
ATOM   4547 N  NE2 . GLN B  1  250 ? 3.957   -29.659 56.972 1.00 78.85  ? 263 GLN B NE2 1 
ATOM   4548 N  N   . VAL B  1  251 ? 6.631   -25.889 62.221 1.00 42.71  ? 264 VAL B N   1 
ATOM   4549 C  CA  . VAL B  1  251 ? 7.755   -25.438 63.023 1.00 40.71  ? 264 VAL B CA  1 
ATOM   4550 C  C   . VAL B  1  251 ? 7.401   -25.565 64.504 1.00 43.41  ? 264 VAL B C   1 
ATOM   4551 O  O   . VAL B  1  251 ? 8.227   -26.004 65.301 1.00 42.11  ? 264 VAL B O   1 
ATOM   4552 C  CB  . VAL B  1  251 ? 8.164   -24.002 62.637 1.00 43.23  ? 264 VAL B CB  1 
ATOM   4553 C  CG1 . VAL B  1  251 ? 9.124   -23.360 63.637 1.00 43.94  ? 264 VAL B CG1 1 
ATOM   4554 C  CG2 . VAL B  1  251 ? 8.754   -23.946 61.234 1.00 43.93  ? 264 VAL B CG2 1 
ATOM   4555 N  N   . LEU B  1  252 ? 6.179   -25.161 64.868 1.00 45.10  ? 265 LEU B N   1 
ATOM   4556 C  CA  . LEU B  1  252 ? 5.685   -25.299 66.230 1.00 45.64  ? 265 LEU B CA  1 
ATOM   4557 C  C   . LEU B  1  252 ? 5.544   -26.776 66.603 1.00 44.75  ? 265 LEU B C   1 
ATOM   4558 O  O   . LEU B  1  252 ? 5.863   -27.151 67.728 1.00 49.02  ? 265 LEU B O   1 
ATOM   4559 C  CB  . LEU B  1  252 ? 4.354   -24.566 66.386 1.00 47.01  ? 265 LEU B CB  1 
ATOM   4560 C  CG  . LEU B  1  252 ? 3.757   -24.555 67.798 1.00 48.53  ? 265 LEU B CG  1 
ATOM   4561 C  CD1 . LEU B  1  252 ? 4.651   -23.856 68.802 1.00 48.01  ? 265 LEU B CD1 1 
ATOM   4562 C  CD2 . LEU B  1  252 ? 2.384   -23.913 67.799 1.00 49.33  ? 265 LEU B CD2 1 
ATOM   4563 N  N   . ALA B  1  253 ? 5.076   -27.607 65.666 1.00 42.56  ? 266 ALA B N   1 
ATOM   4564 C  CA  . ALA B  1  253 ? 4.855   -29.022 65.933 1.00 47.96  ? 266 ALA B CA  1 
ATOM   4565 C  C   . ALA B  1  253 ? 6.171   -29.738 66.276 1.00 52.36  ? 266 ALA B C   1 
ATOM   4566 O  O   . ALA B  1  253 ? 6.168   -30.648 67.095 1.00 52.89  ? 266 ALA B O   1 
ATOM   4567 C  CB  . ALA B  1  253 ? 4.151   -29.680 64.756 1.00 44.92  ? 266 ALA B CB  1 
ATOM   4568 N  N   . ALA B  1  254 ? 7.283   -29.331 65.646 1.00 53.93  ? 267 ALA B N   1 
ATOM   4569 C  CA  . ALA B  1  254 ? 8.582   -29.955 65.859 1.00 54.90  ? 267 ALA B CA  1 
ATOM   4570 C  C   . ALA B  1  254 ? 9.049   -29.816 67.313 1.00 56.48  ? 267 ALA B C   1 
ATOM   4571 O  O   . ALA B  1  254 ? 9.684   -30.722 67.840 1.00 56.59  ? 267 ALA B O   1 
ATOM   4572 C  CB  . ALA B  1  254 ? 9.596   -29.362 64.905 1.00 50.86  ? 267 ALA B CB  1 
ATOM   4573 N  N   . HIS B  1  255 ? 8.766   -28.667 67.942 1.00 57.74  ? 268 HIS B N   1 
ATOM   4574 C  CA  . HIS B  1  255 ? 9.066   -28.452 69.352 1.00 55.18  ? 268 HIS B CA  1 
ATOM   4575 C  C   . HIS B  1  255 ? 7.930   -27.648 69.977 1.00 56.47  ? 268 HIS B C   1 
ATOM   4576 O  O   . HIS B  1  255 ? 8.013   -26.426 70.093 1.00 55.52  ? 268 HIS B O   1 
ATOM   4577 C  CB  . HIS B  1  255 ? 10.438  -27.794 69.565 1.00 53.84  ? 268 HIS B CB  1 
ATOM   4578 C  CG  . HIS B  1  255 ? 11.590  -28.648 69.152 1.00 56.44  ? 268 HIS B CG  1 
ATOM   4579 N  ND1 . HIS B  1  255 ? 11.995  -29.742 69.890 1.00 57.76  ? 268 HIS B ND1 1 
ATOM   4580 C  CD2 . HIS B  1  255 ? 12.397  -28.600 68.086 1.00 54.97  ? 268 HIS B CD2 1 
ATOM   4581 C  CE1 . HIS B  1  255 ? 13.020  -30.324 69.287 1.00 58.35  ? 268 HIS B CE1 1 
ATOM   4582 N  NE2 . HIS B  1  255 ? 13.286  -29.642 68.191 1.00 59.09  ? 268 HIS B NE2 1 
ATOM   4583 N  N   . PRO B  1  256 ? 6.828   -28.320 70.397 1.00 54.28  ? 269 PRO B N   1 
ATOM   4584 C  CA  . PRO B  1  256 ? 5.702   -27.634 71.033 1.00 50.95  ? 269 PRO B CA  1 
ATOM   4585 C  C   . PRO B  1  256 ? 6.176   -26.718 72.155 1.00 48.46  ? 269 PRO B C   1 
ATOM   4586 O  O   . PRO B  1  256 ? 7.011   -27.111 72.962 1.00 48.29  ? 269 PRO B O   1 
ATOM   4587 C  CB  . PRO B  1  256 ? 4.824   -28.786 71.542 1.00 51.48  ? 269 PRO B CB  1 
ATOM   4588 C  CG  . PRO B  1  256 ? 5.120   -29.912 70.563 1.00 51.74  ? 269 PRO B CG  1 
ATOM   4589 C  CD  . PRO B  1  256 ? 6.603   -29.770 70.246 1.00 49.09  ? 269 PRO B CD  1 
ATOM   4590 N  N   . TRP B  1  257 ? 5.648   -25.490 72.162 1.00 45.97  ? 270 TRP B N   1 
ATOM   4591 C  CA  . TRP B  1  257 ? 6.072   -24.446 73.074 1.00 46.07  ? 270 TRP B CA  1 
ATOM   4592 C  C   . TRP B  1  257 ? 4.868   -23.566 73.402 1.00 49.77  ? 270 TRP B C   1 
ATOM   4593 O  O   . TRP B  1  257 ? 3.948   -23.429 72.596 1.00 50.88  ? 270 TRP B O   1 
ATOM   4594 C  CB  . TRP B  1  257 ? 7.232   -23.642 72.466 1.00 45.28  ? 270 TRP B CB  1 
ATOM   4595 C  CG  . TRP B  1  257 ? 7.790   -22.594 73.385 1.00 46.10  ? 270 TRP B CG  1 
ATOM   4596 C  CD1 . TRP B  1  257 ? 7.514   -21.259 73.353 1.00 53.75  ? 270 TRP B CD1 1 
ATOM   4597 C  CD2 . TRP B  1  257 ? 8.682   -22.794 74.497 1.00 43.60  ? 270 TRP B CD2 1 
ATOM   4598 N  NE1 . TRP B  1  257 ? 8.188   -20.608 74.350 1.00 53.89  ? 270 TRP B NE1 1 
ATOM   4599 C  CE2 . TRP B  1  257 ? 8.904   -21.525 75.070 1.00 49.42  ? 270 TRP B CE2 1 
ATOM   4600 C  CE3 . TRP B  1  257 ? 9.305   -23.910 75.066 1.00 47.42  ? 270 TRP B CE3 1 
ATOM   4601 C  CZ2 . TRP B  1  257 ? 9.724   -21.346 76.177 1.00 52.37  ? 270 TRP B CZ2 1 
ATOM   4602 C  CZ3 . TRP B  1  257 ? 10.103  -23.731 76.176 1.00 48.84  ? 270 TRP B CZ3 1 
ATOM   4603 C  CH2 . TRP B  1  257 ? 10.308  -22.465 76.720 1.00 50.00  ? 270 TRP B CH2 1 
ATOM   4604 N  N   . VAL B  1  258 ? 4.882   -22.986 74.603 1.00 48.04  ? 271 VAL B N   1 
ATOM   4605 C  CA  . VAL B  1  258 ? 3.757   -22.221 75.104 1.00 53.13  ? 271 VAL B CA  1 
ATOM   4606 C  C   . VAL B  1  258 ? 4.211   -20.778 75.317 1.00 51.98  ? 271 VAL B C   1 
ATOM   4607 O  O   . VAL B  1  258 ? 5.344   -20.550 75.738 1.00 49.24  ? 271 VAL B O   1 
ATOM   4608 C  CB  . VAL B  1  258 ? 3.228   -22.849 76.411 1.00 56.50  ? 271 VAL B CB  1 
ATOM   4609 C  CG1 . VAL B  1  258 ? 2.109   -22.033 77.020 1.00 61.88  ? 271 VAL B CG1 1 
ATOM   4610 C  CG2 . VAL B  1  258 ? 2.744   -24.279 76.218 1.00 54.88  ? 271 VAL B CG2 1 
ATOM   4611 N  N   . PRO B  1  259 ? 3.363   -19.759 75.033 1.00 47.28  ? 272 PRO B N   1 
ATOM   4612 C  CA  . PRO B  1  259 ? 3.732   -18.373 75.312 1.00 49.40  ? 272 PRO B CA  1 
ATOM   4613 C  C   . PRO B  1  259 ? 4.028   -18.152 76.793 1.00 48.92  ? 272 PRO B C   1 
ATOM   4614 O  O   . PRO B  1  259 ? 3.409   -18.773 77.646 1.00 47.34  ? 272 PRO B O   1 
ATOM   4615 C  CB  . PRO B  1  259 ? 2.507   -17.571 74.832 1.00 48.63  ? 272 PRO B CB  1 
ATOM   4616 C  CG  . PRO B  1  259 ? 1.385   -18.578 74.834 1.00 47.98  ? 272 PRO B CG  1 
ATOM   4617 C  CD  . PRO B  1  259 ? 2.042   -19.867 74.392 1.00 46.38  ? 272 PRO B CD  1 
ATOM   4618 N  N   . GLY B  1  260 ? 4.968   -17.249 77.074 1.00 48.41  ? 273 GLY B N   1 
ATOM   4619 C  CA  . GLY B  1  260 ? 5.357   -16.916 78.431 1.00 50.62  ? 273 GLY B CA  1 
ATOM   4620 C  C   . GLY B  1  260 ? 6.611   -16.046 78.436 1.00 50.20  ? 273 GLY B C   1 
ATOM   4621 O  O   . GLY B  1  260 ? 6.826   -15.268 77.516 1.00 51.59  ? 273 GLY B O   1 
ATOM   4622 N  N   . GLY B  1  261 ? 7.432   -16.201 79.482 1.00 52.54  ? 274 GLY B N   1 
ATOM   4623 C  CA  . GLY B  1  261 ? 8.674   -15.460 79.633 1.00 50.87  ? 274 GLY B CA  1 
ATOM   4624 C  C   . GLY B  1  261 ? 9.395   -15.838 80.927 1.00 55.41  ? 274 GLY B C   1 
ATOM   4625 O  O   . GLY B  1  261 ? 8.811   -16.483 81.794 1.00 55.12  ? 274 GLY B O   1 
ATOM   4626 N  N   . ASN B  1  262 ? 10.667  -15.433 81.039 1.00 54.92  ? 275 ASN B N   1 
ATOM   4627 C  CA  . ASN B  1  262 ? 11.422  -15.559 82.277 1.00 56.15  ? 275 ASN B CA  1 
ATOM   4628 C  C   . ASN B  1  262 ? 10.831  -14.604 83.315 1.00 59.55  ? 275 ASN B C   1 
ATOM   4629 O  O   . ASN B  1  262 ? 10.650  -13.425 83.029 1.00 54.28  ? 275 ASN B O   1 
ATOM   4630 C  CB  . ASN B  1  262 ? 12.904  -15.244 82.082 1.00 50.33  ? 275 ASN B CB  1 
ATOM   4631 C  CG  . ASN B  1  262 ? 13.727  -16.431 81.633 1.00 49.60  ? 275 ASN B CG  1 
ATOM   4632 O  OD1 . ASN B  1  262 ? 13.319  -17.586 81.785 1.00 46.45  ? 275 ASN B OD1 1 
ATOM   4633 N  ND2 . ASN B  1  262 ? 14.899  -16.169 81.074 1.00 52.75  ? 275 ASN B ND2 1 
ATOM   4634 N  N   . ALA B  1  263 ? 10.574  -15.102 84.533 1.00 64.26  ? 276 ALA B N   1 
ATOM   4635 C  CA  . ALA B  1  263 ? 10.013  -14.280 85.598 1.00 65.66  ? 276 ALA B CA  1 
ATOM   4636 C  C   . ALA B  1  263 ? 11.110  -13.712 86.505 1.00 67.74  ? 276 ALA B C   1 
ATOM   4637 O  O   . ALA B  1  263 ? 12.151  -14.338 86.684 1.00 71.76  ? 276 ALA B O   1 
ATOM   4638 C  CB  . ALA B  1  263 ? 9.022   -15.102 86.389 1.00 63.69  ? 276 ALA B CB  1 
ATOM   4639 N  N   . ASP B  1  264 ? 10.856  -12.522 87.069 1.00 72.27  ? 277 ASP B N   1 
ATOM   4640 C  CA  . ASP B  1  264 ? 11.589  -12.031 88.230 1.00 79.94  ? 277 ASP B CA  1 
ATOM   4641 C  C   . ASP B  1  264 ? 13.044  -11.717 87.887 1.00 77.46  ? 277 ASP B C   1 
ATOM   4642 O  O   . ASP B  1  264 ? 13.929  -12.071 88.653 1.00 82.15  ? 277 ASP B O   1 
ATOM   4643 C  CB  . ASP B  1  264 ? 11.527  -13.037 89.379 1.00 81.21  ? 277 ASP B CB  1 
ATOM   4644 C  CG  . ASP B  1  264 ? 10.115  -13.345 89.869 1.00 80.97  ? 277 ASP B CG  1 
ATOM   4645 O  OD1 . ASP B  1  264 ? 9.345   -12.379 90.052 1.00 77.72  ? 277 ASP B OD1 1 
ATOM   4646 O  OD2 . ASP B  1  264 ? 9.799   -14.543 90.042 1.00 84.52  ? 277 ASP B OD2 1 
ATOM   4647 N  N   . ASN B  1  265 ? 13.287  -11.049 86.758 1.00 73.63  ? 278 ASN B N   1 
ATOM   4648 C  CA  . ASN B  1  265 ? 14.633  -10.702 86.326 1.00 73.67  ? 278 ASN B CA  1 
ATOM   4649 C  C   . ASN B  1  265 ? 15.599  -11.864 86.569 1.00 67.34  ? 278 ASN B C   1 
ATOM   4650 O  O   . ASN B  1  265 ? 16.732  -11.641 86.984 1.00 69.77  ? 278 ASN B O   1 
ATOM   4651 C  CB  . ASN B  1  265 ? 15.124  -9.411  86.978 1.00 78.75  ? 278 ASN B CB  1 
ATOM   4652 C  CG  . ASN B  1  265 ? 14.775  -8.185  86.168 1.00 95.88  ? 278 ASN B CG  1 
ATOM   4653 O  OD1 . ASN B  1  265 ? 14.942  -8.195  84.942 1.00 107.58 ? 278 ASN B OD1 1 
ATOM   4654 N  ND2 . ASN B  1  265 ? 14.306  -7.124  86.818 1.00 104.83 ? 278 ASN B ND2 1 
ATOM   4655 N  N   . GLN B  1  266 ? 15.169  -13.101 86.273 1.00 61.13  ? 279 GLN B N   1 
ATOM   4656 C  CA  . GLN B  1  266 ? 15.989  -14.284 86.501 1.00 64.49  ? 279 GLN B CA  1 
ATOM   4657 C  C   . GLN B  1  266 ? 16.024  -15.155 85.243 1.00 64.03  ? 279 GLN B C   1 
ATOM   4658 O  O   . GLN B  1  266 ? 15.006  -15.363 84.583 1.00 66.27  ? 279 GLN B O   1 
ATOM   4659 C  CB  . GLN B  1  266 ? 15.441  -15.154 87.632 1.00 71.10  ? 279 GLN B CB  1 
ATOM   4660 C  CG  . GLN B  1  266 ? 15.621  -14.609 89.045 1.00 80.42  ? 279 GLN B CG  1 
ATOM   4661 C  CD  . GLN B  1  266 ? 15.081  -15.551 90.100 1.00 85.02  ? 279 GLN B CD  1 
ATOM   4662 O  OE1 . GLN B  1  266 ? 14.169  -16.343 89.847 1.00 84.40  ? 279 GLN B OE1 1 
ATOM   4663 N  NE2 . GLN B  1  266 ? 15.661  -15.512 91.291 1.00 90.64  ? 279 GLN B NE2 1 
ATOM   4664 N  N   . VAL B  1  267 ? 17.203  -15.704 84.933 1.00 58.11  ? 280 VAL B N   1 
ATOM   4665 C  CA  . VAL B  1  267 ? 17.351  -16.632 83.823 1.00 53.22  ? 280 VAL B CA  1 
ATOM   4666 C  C   . VAL B  1  267 ? 16.846  -18.012 84.230 1.00 55.32  ? 280 VAL B C   1 
ATOM   4667 O  O   . VAL B  1  267 ? 16.580  -18.264 85.397 1.00 60.45  ? 280 VAL B O   1 
ATOM   4668 C  CB  . VAL B  1  267 ? 18.805  -16.694 83.319 1.00 57.66  ? 280 VAL B CB  1 
ATOM   4669 C  CG1 . VAL B  1  267 ? 19.224  -15.380 82.673 1.00 56.33  ? 280 VAL B CG1 1 
ATOM   4670 C  CG2 . VAL B  1  267 ? 19.788  -17.084 84.415 1.00 56.62  ? 280 VAL B CG2 1 
ATOM   4671 N  N   . ASN B  1  268 ? 16.699  -18.890 83.232 1.00 60.48  ? 281 ASN B N   1 
ATOM   4672 C  CA  . ASN B  1  268 ? 16.220  -20.255 83.403 1.00 59.23  ? 281 ASN B CA  1 
ATOM   4673 C  C   . ASN B  1  268 ? 15.010  -20.303 84.332 1.00 58.56  ? 281 ASN B C   1 
ATOM   4674 O  O   . ASN B  1  268 ? 14.933  -21.173 85.188 1.00 55.80  ? 281 ASN B O   1 
ATOM   4675 C  CB  . ASN B  1  268 ? 17.340  -21.166 83.884 1.00 60.77  ? 281 ASN B CB  1 
ATOM   4676 C  CG  . ASN B  1  268 ? 18.408  -21.321 82.828 1.00 63.11  ? 281 ASN B CG  1 
ATOM   4677 O  OD1 . ASN B  1  268 ? 18.176  -21.955 81.791 1.00 62.65  ? 281 ASN B OD1 1 
ATOM   4678 N  ND2 . ASN B  1  268 ? 19.574  -20.740 83.064 1.00 63.22  ? 281 ASN B ND2 1 
ATOM   4679 N  N   . ASN B  1  269 ? 14.058  -19.387 84.131 1.00 59.50  ? 282 ASN B N   1 
ATOM   4680 C  CA  . ASN B  1  269 ? 12.881  -19.285 84.973 1.00 58.14  ? 282 ASN B CA  1 
ATOM   4681 C  C   . ASN B  1  269 ? 11.661  -18.968 84.107 1.00 54.43  ? 282 ASN B C   1 
ATOM   4682 O  O   . ASN B  1  269 ? 10.938  -18.004 84.362 1.00 49.30  ? 282 ASN B O   1 
ATOM   4683 C  CB  . ASN B  1  269 ? 13.099  -18.241 86.065 1.00 60.88  ? 282 ASN B CB  1 
ATOM   4684 C  CG  . ASN B  1  269 ? 12.078  -18.343 87.171 1.00 57.30  ? 282 ASN B CG  1 
ATOM   4685 O  OD1 . ASN B  1  269 ? 11.512  -19.423 87.396 1.00 52.28  ? 282 ASN B OD1 1 
ATOM   4686 N  ND2 . ASN B  1  269 ? 11.837  -17.232 87.852 1.00 56.53  ? 282 ASN B ND2 1 
ATOM   4687 N  N   . TYR B  1  270 ? 11.439  -19.800 83.084 1.00 56.02  ? 283 TYR B N   1 
ATOM   4688 C  CA  . TYR B  1  270 ? 10.383  -19.560 82.112 1.00 59.08  ? 283 TYR B CA  1 
ATOM   4689 C  C   . TYR B  1  270 ? 9.038   -19.991 82.694 1.00 61.22  ? 283 TYR B C   1 
ATOM   4690 O  O   . TYR B  1  270 ? 8.875   -21.149 83.066 1.00 56.93  ? 283 TYR B O   1 
ATOM   4691 C  CB  . TYR B  1  270 ? 10.651  -20.322 80.809 1.00 58.82  ? 283 TYR B CB  1 
ATOM   4692 C  CG  . TYR B  1  270 ? 9.752   -19.924 79.645 1.00 57.12  ? 283 TYR B CG  1 
ATOM   4693 C  CD1 . TYR B  1  270 ? 10.069  -18.839 78.833 1.00 57.57  ? 283 TYR B CD1 1 
ATOM   4694 C  CD2 . TYR B  1  270 ? 8.588   -20.627 79.360 1.00 52.47  ? 283 TYR B CD2 1 
ATOM   4695 C  CE1 . TYR B  1  270 ? 9.261   -18.471 77.770 1.00 56.92  ? 283 TYR B CE1 1 
ATOM   4696 C  CE2 . TYR B  1  270 ? 7.773   -20.274 78.297 1.00 55.28  ? 283 TYR B CE2 1 
ATOM   4697 C  CZ  . TYR B  1  270 ? 8.109   -19.189 77.501 1.00 57.99  ? 283 TYR B CZ  1 
ATOM   4698 O  OH  . TYR B  1  270 ? 7.336   -18.830 76.434 1.00 50.27  ? 283 TYR B OH  1 
ATOM   4699 N  N   . VAL B  1  271 ? 8.077   -19.055 82.706 1.00 63.41  ? 284 VAL B N   1 
ATOM   4700 C  CA  . VAL B  1  271 ? 6.729   -19.290 83.197 1.00 60.30  ? 284 VAL B CA  1 
ATOM   4701 C  C   . VAL B  1  271 ? 5.736   -19.086 82.053 1.00 56.37  ? 284 VAL B C   1 
ATOM   4702 O  O   . VAL B  1  271 ? 5.772   -18.062 81.381 1.00 54.57  ? 284 VAL B O   1 
ATOM   4703 C  CB  . VAL B  1  271 ? 6.429   -18.330 84.366 1.00 67.39  ? 284 VAL B CB  1 
ATOM   4704 C  CG1 . VAL B  1  271 ? 5.010   -18.505 84.898 1.00 66.44  ? 284 VAL B CG1 1 
ATOM   4705 C  CG2 . VAL B  1  271 ? 7.449   -18.461 85.496 1.00 72.33  ? 284 VAL B CG2 1 
ATOM   4706 N  N   . GLU B  1  272 ? 4.846   -20.067 81.865 1.00 54.91  ? 285 GLU B N   1 
ATOM   4707 C  CA  A GLU B  1  272 ? 3.765   -19.994 80.894 0.50 53.50  ? 285 GLU B CA  1 
ATOM   4708 C  CA  B GLU B  1  272 ? 3.766   -19.993 80.893 0.50 55.49  ? 285 GLU B CA  1 
ATOM   4709 C  C   . GLU B  1  272 ? 2.830   -18.825 81.217 1.00 55.24  ? 285 GLU B C   1 
ATOM   4710 O  O   . GLU B  1  272 ? 2.616   -18.496 82.379 1.00 56.12  ? 285 GLU B O   1 
ATOM   4711 C  CB  A GLU B  1  272 ? 3.014   -21.329 80.885 0.50 51.59  ? 285 GLU B CB  1 
ATOM   4712 C  CB  B GLU B  1  272 ? 3.023   -21.331 80.906 0.50 56.33  ? 285 GLU B CB  1 
ATOM   4713 C  CG  A GLU B  1  272 ? 3.889   -22.506 80.454 0.50 51.86  ? 285 GLU B CG  1 
ATOM   4714 C  CG  B GLU B  1  272 ? 1.776   -21.362 80.025 0.50 60.14  ? 285 GLU B CG  1 
ATOM   4715 C  CD  A GLU B  1  272 ? 3.220   -23.867 80.395 0.50 53.57  ? 285 GLU B CD  1 
ATOM   4716 C  CD  B GLU B  1  272 ? 1.083   -22.716 79.943 0.50 62.48  ? 285 GLU B CD  1 
ATOM   4717 O  OE1 A GLU B  1  272 ? 1.979   -23.936 80.504 0.50 58.21  ? 285 GLU B OE1 1 
ATOM   4718 O  OE1 B GLU B  1  272 ? 1.581   -23.675 80.575 0.50 67.11  ? 285 GLU B OE1 1 
ATOM   4719 O  OE2 A GLU B  1  272 ? 3.958   -24.864 80.228 0.50 49.95  ? 285 GLU B OE2 1 
ATOM   4720 O  OE2 B GLU B  1  272 ? 0.044   -22.818 79.253 0.50 61.20  ? 285 GLU B OE2 1 
ATOM   4721 N  N   . ASP B  1  273 ? 2.281   -18.193 80.166 1.00 57.17  ? 286 ASP B N   1 
ATOM   4722 C  CA  . ASP B  1  273 ? 1.250   -17.167 80.296 1.00 55.17  ? 286 ASP B CA  1 
ATOM   4723 C  C   . ASP B  1  273 ? -0.035  -17.710 79.682 1.00 55.94  ? 286 ASP B C   1 
ATOM   4724 O  O   . ASP B  1  273 ? -0.146  -17.806 78.464 1.00 53.26  ? 286 ASP B O   1 
ATOM   4725 C  CB  . ASP B  1  273 ? 1.613   -15.845 79.636 1.00 52.88  ? 286 ASP B CB  1 
ATOM   4726 C  CG  . ASP B  1  273 ? 0.562   -14.741 79.720 1.00 51.72  ? 286 ASP B CG  1 
ATOM   4727 O  OD1 . ASP B  1  273 ? -0.529  -14.996 80.261 1.00 57.82  ? 286 ASP B OD1 1 
ATOM   4728 O  OD2 . ASP B  1  273 ? 0.839   -13.620 79.251 1.00 56.63  ? 286 ASP B OD2 1 
ATOM   4729 N  N   . PRO B  1  274 ? -1.038  -18.105 80.499 1.00 61.01  ? 287 PRO B N   1 
ATOM   4730 C  CA  . PRO B  1  274 ? -2.248  -18.730 79.956 1.00 61.22  ? 287 PRO B CA  1 
ATOM   4731 C  C   . PRO B  1  274 ? -3.232  -17.757 79.300 1.00 54.71  ? 287 PRO B C   1 
ATOM   4732 O  O   . PRO B  1  274 ? -4.139  -18.202 78.605 1.00 52.09  ? 287 PRO B O   1 
ATOM   4733 C  CB  . PRO B  1  274 ? -2.824  -19.432 81.206 1.00 62.92  ? 287 PRO B CB  1 
ATOM   4734 C  CG  . PRO B  1  274 ? -2.400  -18.548 82.367 1.00 61.12  ? 287 PRO B CG  1 
ATOM   4735 C  CD  . PRO B  1  274 ? -1.049  -17.977 81.969 1.00 60.03  ? 287 PRO B CD  1 
ATOM   4736 N  N   . ASP B  1  275 ? -3.025  -16.442 79.495 1.00 53.81  ? 288 ASP B N   1 
ATOM   4737 C  CA  . ASP B  1  275 ? -3.883  -15.403 78.937 1.00 57.53  ? 288 ASP B CA  1 
ATOM   4738 C  C   . ASP B  1  275 ? -3.407  -14.946 77.555 1.00 60.18  ? 288 ASP B C   1 
ATOM   4739 O  O   . ASP B  1  275 ? -4.154  -14.284 76.835 1.00 50.81  ? 288 ASP B O   1 
ATOM   4740 C  CB  . ASP B  1  275 ? -3.972  -14.217 79.883 1.00 56.52  ? 288 ASP B CB  1 
ATOM   4741 C  CG  . ASP B  1  275 ? -4.752  -14.477 81.167 1.00 64.60  ? 288 ASP B CG  1 
ATOM   4742 O  OD1 . ASP B  1  275 ? -5.503  -15.484 81.222 1.00 66.40  ? 288 ASP B OD1 1 
ATOM   4743 O  OD2 . ASP B  1  275 ? -4.592  -13.680 82.111 1.00 67.72  ? 288 ASP B OD2 1 
ATOM   4744 N  N   . SER B  1  276 ? -2.158  -15.286 77.204 1.00 59.79  ? 289 SER B N   1 
ATOM   4745 C  CA  . SER B  1  276 ? -1.565  -14.881 75.942 1.00 56.40  ? 289 SER B CA  1 
ATOM   4746 C  C   . SER B  1  276 ? -2.323  -15.482 74.764 1.00 50.47  ? 289 SER B C   1 
ATOM   4747 O  O   . SER B  1  276 ? -2.894  -16.563 74.859 1.00 49.22  ? 289 SER B O   1 
ATOM   4748 C  CB  . SER B  1  276 ? -0.106  -15.277 75.872 1.00 56.37  ? 289 SER B CB  1 
ATOM   4749 O  OG  . SER B  1  276 ? 0.408   -15.109 74.556 1.00 51.59  ? 289 SER B OG  1 
ATOM   4750 N  N   . ALA B  1  277 ? -2.271  -14.781 73.631 1.00 50.10  ? 290 ALA B N   1 
ATOM   4751 C  CA  . ALA B  1  277 ? -2.655  -15.367 72.357 1.00 47.43  ? 290 ALA B CA  1 
ATOM   4752 C  C   . ALA B  1  277 ? -1.770  -16.572 72.059 1.00 48.51  ? 290 ALA B C   1 
ATOM   4753 O  O   . ALA B  1  277 ? -0.618  -16.612 72.492 1.00 46.58  ? 290 ALA B O   1 
ATOM   4754 C  CB  . ALA B  1  277 ? -2.527  -14.338 71.258 1.00 48.48  ? 290 ALA B CB  1 
ATOM   4755 N  N   . ASP B  1  278 ? -2.336  -17.539 71.329 1.00 50.52  ? 291 ASP B N   1 
ATOM   4756 C  CA  . ASP B  1  278 ? -1.592  -18.633 70.726 1.00 48.83  ? 291 ASP B CA  1 
ATOM   4757 C  C   . ASP B  1  278 ? -2.266  -18.946 69.389 1.00 46.71  ? 291 ASP B C   1 
ATOM   4758 O  O   . ASP B  1  278 ? -3.087  -18.152 68.939 1.00 44.63  ? 291 ASP B O   1 
ATOM   4759 C  CB  . ASP B  1  278 ? -1.454  -19.788 71.705 1.00 52.14  ? 291 ASP B CB  1 
ATOM   4760 C  CG  . ASP B  1  278 ? -2.724  -20.565 72.013 1.00 53.49  ? 291 ASP B CG  1 
ATOM   4761 O  OD1 . ASP B  1  278 ? -3.705  -20.454 71.235 1.00 55.67  ? 291 ASP B OD1 1 
ATOM   4762 O  OD2 . ASP B  1  278 ? -2.709  -21.286 73.022 1.00 57.01  ? 291 ASP B OD2 1 
ATOM   4763 N  N   . PHE B  1  279 ? -1.946  -20.094 68.768 1.00 44.43  ? 292 PHE B N   1 
ATOM   4764 C  CA  . PHE B  1  279 ? -2.364  -20.341 67.396 1.00 49.73  ? 292 PHE B CA  1 
ATOM   4765 C  C   . PHE B  1  279 ? -3.793  -20.869 67.319 1.00 53.91  ? 292 PHE B C   1 
ATOM   4766 O  O   . PHE B  1  279 ? -4.336  -20.916 66.224 1.00 52.12  ? 292 PHE B O   1 
ATOM   4767 C  CB  . PHE B  1  279 ? -1.391  -21.255 66.645 1.00 46.36  ? 292 PHE B CB  1 
ATOM   4768 C  CG  . PHE B  1  279 ? -0.116  -20.514 66.278 1.00 50.96  ? 292 PHE B CG  1 
ATOM   4769 C  CD1 . PHE B  1  279 ? -0.074  -19.649 65.185 1.00 57.12  ? 292 PHE B CD1 1 
ATOM   4770 C  CD2 . PHE B  1  279 ? 1.016   -20.622 67.075 1.00 54.08  ? 292 PHE B CD2 1 
ATOM   4771 C  CE1 . PHE B  1  279 ? 1.078   -18.936 64.887 1.00 59.08  ? 292 PHE B CE1 1 
ATOM   4772 C  CE2 . PHE B  1  279 ? 2.164   -19.912 66.772 1.00 57.11  ? 292 PHE B CE2 1 
ATOM   4773 C  CZ  . PHE B  1  279 ? 2.190   -19.068 65.684 1.00 59.74  ? 292 PHE B CZ  1 
ATOM   4774 N  N   . THR B  1  280 ? -4.394  -21.247 68.457 1.00 56.13  ? 293 THR B N   1 
ATOM   4775 C  CA  . THR B  1  280 ? -5.801  -21.623 68.493 1.00 58.08  ? 293 THR B CA  1 
ATOM   4776 C  C   . THR B  1  280 ? -6.629  -20.525 69.163 1.00 58.89  ? 293 THR B C   1 
ATOM   4777 O  O   . THR B  1  280 ? -7.838  -20.683 69.294 1.00 64.08  ? 293 THR B O   1 
ATOM   4778 C  CB  . THR B  1  280 ? -5.980  -22.968 69.200 1.00 54.97  ? 293 THR B CB  1 
ATOM   4779 O  OG1 . THR B  1  280 ? -5.500  -22.810 70.528 1.00 60.67  ? 293 THR B OG1 1 
ATOM   4780 C  CG2 . THR B  1  280 ? -5.217  -24.094 68.529 1.00 53.98  ? 293 THR B CG2 1 
ATOM   4781 N  N   . HIS B  1  281 ? -5.975  -19.434 69.589 1.00 55.08  ? 294 HIS B N   1 
ATOM   4782 C  CA  . HIS B  1  281 ? -6.622  -18.313 70.262 1.00 54.91  ? 294 HIS B CA  1 
ATOM   4783 C  C   . HIS B  1  281 ? -6.075  -16.994 69.696 1.00 52.80  ? 294 HIS B C   1 
ATOM   4784 O  O   . HIS B  1  281 ? -5.462  -16.208 70.415 1.00 57.07  ? 294 HIS B O   1 
ATOM   4785 C  CB  . HIS B  1  281 ? -6.458  -18.416 71.791 1.00 59.16  ? 294 HIS B CB  1 
ATOM   4786 C  CG  . HIS B  1  281 ? -7.030  -19.652 72.423 1.00 65.47  ? 294 HIS B CG  1 
ATOM   4787 N  ND1 . HIS B  1  281 ? -8.374  -19.815 72.687 1.00 72.04  ? 294 HIS B ND1 1 
ATOM   4788 C  CD2 . HIS B  1  281 ? -6.433  -20.774 72.849 1.00 64.81  ? 294 HIS B CD2 1 
ATOM   4789 C  CE1 . HIS B  1  281 ? -8.569  -21.000 73.246 1.00 72.19  ? 294 HIS B CE1 1 
ATOM   4790 N  NE2 . HIS B  1  281 ? -7.405  -21.591 73.360 1.00 74.12  ? 294 HIS B NE2 1 
ATOM   4791 N  N   . LEU B  1  282 ? -6.309  -16.752 68.399 1.00 49.02  ? 295 LEU B N   1 
ATOM   4792 C  CA  . LEU B  1  282 ? -5.673  -15.672 67.657 1.00 48.01  ? 295 LEU B CA  1 
ATOM   4793 C  C   . LEU B  1  282 ? -6.341  -14.320 67.892 1.00 50.08  ? 295 LEU B C   1 
ATOM   4794 O  O   . LEU B  1  282 ? -5.675  -13.286 67.780 1.00 48.14  ? 295 LEU B O   1 
ATOM   4795 C  CB  . LEU B  1  282 ? -5.651  -15.975 66.161 1.00 52.76  ? 295 LEU B CB  1 
ATOM   4796 C  CG  . LEU B  1  282 ? -4.602  -16.981 65.669 1.00 56.14  ? 295 LEU B CG  1 
ATOM   4797 C  CD1 . LEU B  1  282 ? -4.882  -17.438 64.252 1.00 56.10  ? 295 LEU B CD1 1 
ATOM   4798 C  CD2 . LEU B  1  282 ? -3.207  -16.393 65.745 1.00 55.94  ? 295 LEU B CD2 1 
ATOM   4799 N  N   . CYS B  1  283 ? -7.649  -14.313 68.169 1.00 49.70  ? 296 CYS B N   1 
ATOM   4800 C  CA  . CYS B  1  283 ? -8.369  -13.062 68.366 1.00 49.66  ? 296 CYS B CA  1 
ATOM   4801 C  C   . CYS B  1  283 ? -7.897  -12.368 69.643 1.00 49.83  ? 296 CYS B C   1 
ATOM   4802 O  O   . CYS B  1  283 ? -8.045  -11.150 69.775 1.00 50.48  ? 296 CYS B O   1 
ATOM   4803 C  CB  . CYS B  1  283 ? -9.884  -13.264 68.335 1.00 59.15  ? 296 CYS B CB  1 
ATOM   4804 S  SG  . CYS B  1  283 ? -10.542 -13.809 66.728 1.00 73.05  ? 296 CYS B SG  1 
ATOM   4805 N  N   . ARG B  1  284 ? -7.301  -13.125 70.575 1.00 50.02  ? 297 ARG B N   1 
ATOM   4806 C  CA  . ARG B  1  284 ? -6.688  -12.529 71.754 1.00 51.34  ? 297 ARG B CA  1 
ATOM   4807 C  C   . ARG B  1  284 ? -5.615  -11.522 71.346 1.00 47.50  ? 297 ARG B C   1 
ATOM   4808 O  O   . ARG B  1  284 ? -5.409  -10.517 72.020 1.00 48.23  ? 297 ARG B O   1 
ATOM   4809 C  CB  . ARG B  1  284 ? -6.059  -13.594 72.651 1.00 53.74  ? 297 ARG B CB  1 
ATOM   4810 C  CG  . ARG B  1  284 ? -7.049  -14.504 73.354 1.00 58.76  ? 297 ARG B CG  1 
ATOM   4811 C  CD  . ARG B  1  284 ? -6.332  -15.416 74.328 1.00 63.66  ? 297 ARG B CD  1 
ATOM   4812 N  NE  . ARG B  1  284 ? -7.244  -16.396 74.931 1.00 69.30  ? 297 ARG B NE  1 
ATOM   4813 C  CZ  . ARG B  1  284 ? -6.856  -17.486 75.583 1.00 65.94  ? 297 ARG B CZ  1 
ATOM   4814 N  NH1 . ARG B  1  284 ? -5.570  -17.726 75.793 1.00 62.97  ? 297 ARG B NH1 1 
ATOM   4815 N  NH2 . ARG B  1  284 ? -7.766  -18.342 76.005 1.00 64.07  ? 297 ARG B NH2 1 
ATOM   4816 N  N   . LEU B  1  285 ? -4.911  -11.813 70.247 1.00 44.50  ? 298 LEU B N   1 
ATOM   4817 C  CA  . LEU B  1  285 ? -3.877  -10.919 69.760 1.00 46.39  ? 298 LEU B CA  1 
ATOM   4818 C  C   . LEU B  1  285 ? -4.519  -9.612  69.303 1.00 44.15  ? 298 LEU B C   1 
ATOM   4819 O  O   . LEU B  1  285 ? -4.011  -8.535  69.605 1.00 39.41  ? 298 LEU B O   1 
ATOM   4820 C  CB  . LEU B  1  285 ? -3.067  -11.570 68.639 1.00 51.23  ? 298 LEU B CB  1 
ATOM   4821 C  CG  . LEU B  1  285 ? -1.850  -10.778 68.147 1.00 51.02  ? 298 LEU B CG  1 
ATOM   4822 C  CD1 . LEU B  1  285 ? -0.794  -11.698 67.625 1.00 51.53  ? 298 LEU B CD1 1 
ATOM   4823 C  CD2 . LEU B  1  285 ? -2.187  -9.798  67.050 1.00 54.71  ? 298 LEU B CD2 1 
ATOM   4824 N  N   . TYR B  1  286 ? -5.633  -9.725  68.569 1.00 45.23  ? 299 TYR B N   1 
ATOM   4825 C  CA  . TYR B  1  286 ? -6.382  -8.571  68.092 1.00 48.27  ? 299 TYR B CA  1 
ATOM   4826 C  C   . TYR B  1  286 ? -6.709  -7.657  69.274 1.00 43.45  ? 299 TYR B C   1 
ATOM   4827 O  O   . TYR B  1  286 ? -6.387  -6.478  69.239 1.00 42.53  ? 299 TYR B O   1 
ATOM   4828 C  CB  . TYR B  1  286 ? -7.605  -9.011  67.268 1.00 47.71  ? 299 TYR B CB  1 
ATOM   4829 C  CG  . TYR B  1  286 ? -8.543  -7.874  66.894 1.00 44.11  ? 299 TYR B CG  1 
ATOM   4830 C  CD1 . TYR B  1  286 ? -8.099  -6.826  66.102 1.00 43.15  ? 299 TYR B CD1 1 
ATOM   4831 C  CD2 . TYR B  1  286 ? -9.857  -7.840  67.346 1.00 44.84  ? 299 TYR B CD2 1 
ATOM   4832 C  CE1 . TYR B  1  286 ? -8.934  -5.774  65.770 1.00 45.95  ? 299 TYR B CE1 1 
ATOM   4833 C  CE2 . TYR B  1  286 ? -10.706 -6.796  67.014 1.00 44.63  ? 299 TYR B CE2 1 
ATOM   4834 C  CZ  . TYR B  1  286 ? -10.244 -5.764  66.222 1.00 47.06  ? 299 TYR B CZ  1 
ATOM   4835 O  OH  . TYR B  1  286 ? -11.035 -4.714  65.883 1.00 43.31  ? 299 TYR B OH  1 
ATOM   4836 N  N   . GLU B  1  287 ? -7.254  -8.224  70.350 1.00 48.57  ? 300 GLU B N   1 
ATOM   4837 C  CA  . GLU B  1  287 ? -7.687  -7.458  71.513 1.00 49.96  ? 300 GLU B CA  1 
ATOM   4838 C  C   . GLU B  1  287 ? -6.518  -6.871  72.299 1.00 45.95  ? 300 GLU B C   1 
ATOM   4839 O  O   . GLU B  1  287 ? -6.637  -5.762  72.802 1.00 47.68  ? 300 GLU B O   1 
ATOM   4840 C  CB  . GLU B  1  287 ? -8.484  -8.345  72.469 1.00 54.13  ? 300 GLU B CB  1 
ATOM   4841 C  CG  . GLU B  1  287 ? -9.747  -8.911  71.833 1.00 65.32  ? 300 GLU B CG  1 
ATOM   4842 C  CD  . GLU B  1  287 ? -10.255 -10.216 72.435 1.00 81.18  ? 300 GLU B CD  1 
ATOM   4843 O  OE1 . GLU B  1  287 ? -9.582  -10.827 73.299 1.00 83.58  ? 300 GLU B OE1 1 
ATOM   4844 O  OE2 . GLU B  1  287 ? -11.358 -10.629 72.011 1.00 90.19  ? 300 GLU B OE2 1 
ATOM   4845 N  N   . PHE B  1  288 ? -5.410  -7.613  72.420 1.00 46.75  ? 301 PHE B N   1 
ATOM   4846 C  CA  . PHE B  1  288 ? -4.213  -7.117  73.081 1.00 45.50  ? 301 PHE B CA  1 
ATOM   4847 C  C   . PHE B  1  288 ? -3.746  -5.810  72.442 1.00 44.19  ? 301 PHE B C   1 
ATOM   4848 O  O   . PHE B  1  288 ? -3.431  -4.862  73.162 1.00 44.28  ? 301 PHE B O   1 
ATOM   4849 C  CB  . PHE B  1  288 ? -3.112  -8.184  73.050 1.00 51.05  ? 301 PHE B CB  1 
ATOM   4850 C  CG  . PHE B  1  288 ? -1.891  -7.780  73.857 1.00 56.17  ? 301 PHE B CG  1 
ATOM   4851 C  CD1 . PHE B  1  288 ? -1.888  -7.947  75.240 1.00 56.83  ? 301 PHE B CD1 1 
ATOM   4852 C  CD2 . PHE B  1  288 ? -0.762  -7.244  73.247 1.00 55.68  ? 301 PHE B CD2 1 
ATOM   4853 C  CE1 . PHE B  1  288 ? -0.791  -7.572  76.001 1.00 56.77  ? 301 PHE B CE1 1 
ATOM   4854 C  CE2 . PHE B  1  288 ? 0.330   -6.862  74.018 1.00 57.80  ? 301 PHE B CE2 1 
ATOM   4855 C  CZ  . PHE B  1  288 ? 0.308   -7.018  75.392 1.00 52.10  ? 301 PHE B CZ  1 
ATOM   4856 N  N   . VAL B  1  289 ? -3.751  -5.741  71.096 1.00 43.44  ? 302 VAL B N   1 
ATOM   4857 C  CA  . VAL B  1  289 ? -3.230  -4.580  70.387 1.00 45.88  ? 302 VAL B CA  1 
ATOM   4858 C  C   . VAL B  1  289 ? -4.216  -3.427  70.501 1.00 41.85  ? 302 VAL B C   1 
ATOM   4859 O  O   . VAL B  1  289 ? -3.786  -2.289  70.637 1.00 42.28  ? 302 VAL B O   1 
ATOM   4860 C  CB  . VAL B  1  289 ? -2.883  -4.870  68.909 1.00 46.93  ? 302 VAL B CB  1 
ATOM   4861 C  CG1 . VAL B  1  289 ? -2.408  -3.632  68.152 1.00 47.59  ? 302 VAL B CG1 1 
ATOM   4862 C  CG2 . VAL B  1  289 ? -1.844  -5.979  68.812 1.00 46.79  ? 302 VAL B CG2 1 
ATOM   4863 N  N   . VAL B  1  290 ? -5.517  -3.711  70.397 1.00 43.23  ? 303 VAL B N   1 
ATOM   4864 C  CA  . VAL B  1  290 ? -6.522  -2.670  70.581 1.00 48.97  ? 303 VAL B CA  1 
ATOM   4865 C  C   . VAL B  1  290 ? -6.291  -2.012  71.942 1.00 44.98  ? 303 VAL B C   1 
ATOM   4866 O  O   . VAL B  1  290 ? -6.251  -0.784  72.036 1.00 49.13  ? 303 VAL B O   1 
ATOM   4867 C  CB  . VAL B  1  290 ? -7.959  -3.205  70.407 1.00 49.53  ? 303 VAL B CB  1 
ATOM   4868 C  CG1 . VAL B  1  290 ? -9.016  -2.192  70.830 1.00 51.30  ? 303 VAL B CG1 1 
ATOM   4869 C  CG2 . VAL B  1  290 ? -8.208  -3.654  68.973 1.00 50.31  ? 303 VAL B CG2 1 
ATOM   4870 N  N   . GLY B  1  291 ? -6.045  -2.852  72.963 1.00 46.81  ? 304 GLY B N   1 
ATOM   4871 C  CA  . GLY B  1  291 ? -5.690  -2.410  74.307 1.00 45.22  ? 304 GLY B CA  1 
ATOM   4872 C  C   . GLY B  1  291 ? -4.417  -1.566  74.347 1.00 44.77  ? 304 GLY B C   1 
ATOM   4873 O  O   . GLY B  1  291 ? -4.426  -0.503  74.954 1.00 42.56  ? 304 GLY B O   1 
ATOM   4874 N  N   . SER B  1  292 ? -3.341  -2.043  73.694 1.00 41.75  ? 305 SER B N   1 
ATOM   4875 C  CA  . SER B  1  292 ? -2.074  -1.334  73.675 1.00 38.07  ? 305 SER B CA  1 
ATOM   4876 C  C   . SER B  1  292 ? -2.258  0.033   73.024 1.00 36.82  ? 305 SER B C   1 
ATOM   4877 O  O   . SER B  1  292 ? -1.667  1.009   73.463 1.00 39.66  ? 305 SER B O   1 
ATOM   4878 C  CB  . SER B  1  292 ? -1.005  -2.147  72.971 1.00 40.44  ? 305 SER B CB  1 
ATOM   4879 O  OG  . SER B  1  292 ? -0.950  -3.468  73.487 1.00 39.14  ? 305 SER B OG  1 
ATOM   4880 N  N   . VAL B  1  293 ? -3.086  0.090   71.973 1.00 37.96  ? 306 VAL B N   1 
ATOM   4881 C  CA  . VAL B  1  293 ? -3.334  1.332   71.255 1.00 44.28  ? 306 VAL B CA  1 
ATOM   4882 C  C   . VAL B  1  293 ? -4.033  2.339   72.179 1.00 44.38  ? 306 VAL B C   1 
ATOM   4883 O  O   . VAL B  1  293 ? -3.710  3.529   72.170 1.00 45.66  ? 306 VAL B O   1 
ATOM   4884 C  CB  . VAL B  1  293 ? -4.137  1.066   69.961 1.00 44.15  ? 306 VAL B CB  1 
ATOM   4885 C  CG1 . VAL B  1  293 ? -4.675  2.341   69.333 1.00 43.87  ? 306 VAL B CG1 1 
ATOM   4886 C  CG2 . VAL B  1  293 ? -3.329  0.302   68.923 1.00 49.33  ? 306 VAL B CG2 1 
ATOM   4887 N  N   . GLN B  1  294 ? -4.993  1.846   72.976 1.00 50.38  ? 307 GLN B N   1 
ATOM   4888 C  CA  . GLN B  1  294 ? -5.715  2.671   73.934 1.00 48.73  ? 307 GLN B CA  1 
ATOM   4889 C  C   . GLN B  1  294 ? -4.782  3.233   75.001 1.00 47.27  ? 307 GLN B C   1 
ATOM   4890 O  O   . GLN B  1  294 ? -4.975  4.359   75.431 1.00 54.59  ? 307 GLN B O   1 
ATOM   4891 C  CB  . GLN B  1  294 ? -6.846  1.883   74.588 1.00 48.29  ? 307 GLN B CB  1 
ATOM   4892 C  CG  . GLN B  1  294 ? -8.013  1.642   73.645 1.00 50.49  ? 307 GLN B CG  1 
ATOM   4893 C  CD  . GLN B  1  294 ? -9.095  0.820   74.286 1.00 53.78  ? 307 GLN B CD  1 
ATOM   4894 O  OE1 . GLN B  1  294 ? -9.205  -0.393  74.069 1.00 56.07  ? 307 GLN B OE1 1 
ATOM   4895 N  NE2 . GLN B  1  294 ? -9.864  1.499   75.118 1.00 54.89  ? 307 GLN B NE2 1 
ATOM   4896 N  N   . GLU B  1  295 ? -3.763  2.469   75.399 1.00 48.29  ? 308 GLU B N   1 
ATOM   4897 C  CA  . GLU B  1  295 ? -2.753  2.954   76.330 1.00 51.89  ? 308 GLU B CA  1 
ATOM   4898 C  C   . GLU B  1  295 ? -1.898  4.041   75.686 1.00 52.23  ? 308 GLU B C   1 
ATOM   4899 O  O   . GLU B  1  295 ? -1.564  5.002   76.363 1.00 55.31  ? 308 GLU B O   1 
ATOM   4900 C  CB  . GLU B  1  295 ? -1.852  1.840   76.859 1.00 59.41  ? 308 GLU B CB  1 
ATOM   4901 C  CG  . GLU B  1  295 ? -2.617  0.768   77.637 1.00 66.37  ? 308 GLU B CG  1 
ATOM   4902 C  CD  . GLU B  1  295 ? -1.823  -0.477  77.998 1.00 76.33  ? 308 GLU B CD  1 
ATOM   4903 O  OE1 . GLU B  1  295 ? -0.607  -0.527  77.717 1.00 83.46  ? 308 GLU B OE1 1 
ATOM   4904 O  OE2 . GLU B  1  295 ? -2.453  -1.418  78.525 1.00 81.05  ? 308 GLU B OE2 1 
ATOM   4905 N  N   . LEU B  1  296 ? -1.546  3.895   74.397 1.00 51.38  ? 309 LEU B N   1 
ATOM   4906 C  CA  . LEU B  1  296 ? -0.731  4.886   73.707 1.00 51.98  ? 309 LEU B CA  1 
ATOM   4907 C  C   . LEU B  1  296 ? -1.546  6.153   73.462 1.00 46.85  ? 309 LEU B C   1 
ATOM   4908 O  O   . LEU B  1  296 ? -1.003  7.260   73.511 1.00 46.18  ? 309 LEU B O   1 
ATOM   4909 C  CB  . LEU B  1  296 ? -0.182  4.327   72.390 1.00 57.70  ? 309 LEU B CB  1 
ATOM   4910 C  CG  . LEU B  1  296 ? 0.848   3.196   72.487 1.00 53.51  ? 309 LEU B CG  1 
ATOM   4911 C  CD1 . LEU B  1  296 ? 1.116   2.611   71.111 1.00 53.99  ? 309 LEU B CD1 1 
ATOM   4912 C  CD2 . LEU B  1  296 ? 2.148   3.689   73.108 1.00 52.27  ? 309 LEU B CD2 1 
ATOM   4913 N  N   . TYR B  1  297 ? -2.845  5.966   73.187 1.00 45.11  ? 310 TYR B N   1 
ATOM   4914 C  CA  . TYR B  1  297 ? -3.732  7.047   72.777 1.00 49.51  ? 310 TYR B CA  1 
ATOM   4915 C  C   . TYR B  1  297 ? -4.972  7.074   73.670 1.00 51.85  ? 310 TYR B C   1 
ATOM   4916 O  O   . TYR B  1  297 ? -6.047  6.669   73.238 1.00 47.95  ? 310 TYR B O   1 
ATOM   4917 C  CB  . TYR B  1  297 ? -4.093  6.815   71.310 1.00 48.60  ? 310 TYR B CB  1 
ATOM   4918 C  CG  . TYR B  1  297 ? -2.921  6.965   70.360 1.00 46.35  ? 310 TYR B CG  1 
ATOM   4919 C  CD1 . TYR B  1  297 ? -2.453  8.220   70.002 1.00 45.03  ? 310 TYR B CD1 1 
ATOM   4920 C  CD2 . TYR B  1  297 ? -2.292  5.850   69.821 1.00 48.10  ? 310 TYR B CD2 1 
ATOM   4921 C  CE1 . TYR B  1  297 ? -1.381  8.361   69.133 1.00 49.25  ? 310 TYR B CE1 1 
ATOM   4922 C  CE2 . TYR B  1  297 ? -1.227  5.976   68.945 1.00 48.43  ? 310 TYR B CE2 1 
ATOM   4923 C  CZ  . TYR B  1  297 ? -0.772  7.236   68.599 1.00 49.88  ? 310 TYR B CZ  1 
ATOM   4924 O  OH  . TYR B  1  297 ? 0.275   7.359   67.737 1.00 46.26  ? 310 TYR B OH  1 
ATOM   4925 N  N   . PRO B  1  298 ? -4.854  7.517   74.946 1.00 53.39  ? 311 PRO B N   1 
ATOM   4926 C  CA  . PRO B  1  298 ? -5.984  7.466   75.882 1.00 54.86  ? 311 PRO B CA  1 
ATOM   4927 C  C   . PRO B  1  298 ? -7.144  8.422   75.589 1.00 55.52  ? 311 PRO B C   1 
ATOM   4928 O  O   . PRO B  1  298 ? -8.302  8.054   75.765 1.00 53.93  ? 311 PRO B O   1 
ATOM   4929 C  CB  . PRO B  1  298 ? -5.319  7.736   77.238 1.00 57.19  ? 311 PRO B CB  1 
ATOM   4930 C  CG  . PRO B  1  298 ? -4.095  8.556   76.899 1.00 58.45  ? 311 PRO B CG  1 
ATOM   4931 C  CD  . PRO B  1  298 ? -3.623  8.054   75.547 1.00 53.56  ? 311 PRO B CD  1 
ATOM   4932 N  N   . ASN B  1  299 ? -6.845  9.617   75.069 1.00 57.40  ? 312 ASN B N   1 
ATOM   4933 C  CA  . ASN B  1  299 ? -7.870  10.599  74.765 1.00 64.62  ? 312 ASN B CA  1 
ATOM   4934 C  C   . ASN B  1  299 ? -7.482  11.373  73.505 1.00 63.29  ? 312 ASN B C   1 
ATOM   4935 O  O   . ASN B  1  299 ? -7.232  12.577  73.559 1.00 59.36  ? 312 ASN B O   1 
ATOM   4936 C  CB  . ASN B  1  299 ? -8.093  11.565  75.924 1.00 72.52  ? 312 ASN B CB  1 
ATOM   4937 C  CG  . ASN B  1  299 ? -8.853  10.964  77.081 1.00 89.93  ? 312 ASN B CG  1 
ATOM   4938 O  OD1 . ASN B  1  299 ? -9.746  10.126  76.898 1.00 102.20 ? 312 ASN B OD1 1 
ATOM   4939 N  ND2 . ASN B  1  299 ? -8.555  11.428  78.284 1.00 102.41 ? 312 ASN B ND2 1 
ATOM   4940 N  N   . PRO B  1  300 ? -7.484  10.732  72.311 1.00 57.99  ? 313 PRO B N   1 
ATOM   4941 C  CA  . PRO B  1  300 ? -7.209  11.448  71.066 1.00 57.52  ? 313 PRO B CA  1 
ATOM   4942 C  C   . PRO B  1  300 ? -8.361  12.376  70.674 1.00 59.38  ? 313 PRO B C   1 
ATOM   4943 O  O   . PRO B  1  300 ? -9.526  12.049  70.910 1.00 59.32  ? 313 PRO B O   1 
ATOM   4944 C  CB  . PRO B  1  300 ? -7.043  10.267  70.092 1.00 58.32  ? 313 PRO B CB  1 
ATOM   4945 C  CG  . PRO B  1  300 ? -8.009  9.210   70.600 1.00 56.18  ? 313 PRO B CG  1 
ATOM   4946 C  CD  . PRO B  1  300 ? -7.835  9.312   72.096 1.00 59.66  ? 313 PRO B CD  1 
ATOM   4947 N  N   . THR B  1  301 ? -8.036  13.514  70.049 1.00 62.51  ? 314 THR B N   1 
ATOM   4948 C  CA  . THR B  1  301 ? -9.043  14.361  69.419 1.00 71.45  ? 314 THR B CA  1 
ATOM   4949 C  C   . THR B  1  301 ? -8.596  14.720  67.999 1.00 69.34  ? 314 THR B C   1 
ATOM   4950 O  O   . THR B  1  301 ? -7.423  14.625  67.657 1.00 71.96  ? 314 THR B O   1 
ATOM   4951 C  CB  . THR B  1  301 ? -9.316  15.620  70.256 1.00 73.84  ? 314 THR B CB  1 
ATOM   4952 O  OG1 . THR B  1  301 ? -8.094  16.343  70.368 1.00 75.57  ? 314 THR B OG1 1 
ATOM   4953 C  CG2 . THR B  1  301 ? -9.855  15.308  71.643 1.00 73.66  ? 314 THR B CG2 1 
ATOM   4954 N  N   . GLY B  1  302 ? -9.562  15.120  67.170 1.00 69.81  ? 315 GLY B N   1 
ATOM   4955 C  CA  . GLY B  1  302 ? -9.277  15.734  65.882 1.00 68.92  ? 315 GLY B CA  1 
ATOM   4956 C  C   . GLY B  1  302 ? -8.923  14.695  64.820 1.00 65.89  ? 315 GLY B C   1 
ATOM   4957 O  O   . GLY B  1  302 ? -9.483  13.590  64.813 1.00 59.09  ? 315 GLY B O   1 
ATOM   4958 N  N   . ILE B  1  303 ? -7.991  15.069  63.923 1.00 65.39  ? 316 ILE B N   1 
ATOM   4959 C  CA  . ILE B  1  303 ? -7.587  14.180  62.837 1.00 63.85  ? 316 ILE B CA  1 
ATOM   4960 C  C   . ILE B  1  303 ? -6.892  12.957  63.421 1.00 56.27  ? 316 ILE B C   1 
ATOM   4961 O  O   . ILE B  1  303 ? -7.030  11.889  62.867 1.00 55.71  ? 316 ILE B O   1 
ATOM   4962 C  CB  . ILE B  1  303 ? -6.703  14.851  61.776 1.00 73.90  ? 316 ILE B CB  1 
ATOM   4963 C  CG1 . ILE B  1  303 ? -5.438  15.427  62.403 1.00 74.21  ? 316 ILE B CG1 1 
ATOM   4964 C  CG2 . ILE B  1  303 ? -7.509  15.872  60.960 1.00 87.28  ? 316 ILE B CG2 1 
ATOM   4965 C  CD1 . ILE B  1  303 ? -4.421  15.923  61.393 1.00 82.54  ? 316 ILE B CD1 1 
ATOM   4966 N  N   . LEU B  1  304 ? -6.193  13.095  64.552 1.00 52.85  ? 317 LEU B N   1 
ATOM   4967 C  CA  . LEU B  1  304 ? -5.610  11.949  65.234 1.00 54.68  ? 317 LEU B CA  1 
ATOM   4968 C  C   . LEU B  1  304 ? -6.680  10.912  65.578 1.00 58.05  ? 317 LEU B C   1 
ATOM   4969 O  O   . LEU B  1  304 ? -6.492  9.729   65.318 1.00 63.77  ? 317 LEU B O   1 
ATOM   4970 C  CB  . LEU B  1  304 ? -4.851  12.406  66.475 1.00 52.81  ? 317 LEU B CB  1 
ATOM   4971 C  CG  . LEU B  1  304 ? -4.242  11.292  67.329 1.00 58.44  ? 317 LEU B CG  1 
ATOM   4972 C  CD1 . LEU B  1  304 ? -3.220  10.507  66.542 1.00 60.17  ? 317 LEU B CD1 1 
ATOM   4973 C  CD2 . LEU B  1  304 ? -3.645  11.822  68.615 1.00 59.28  ? 317 LEU B CD2 1 
ATOM   4974 N  N   . ARG B  1  305 ? -7.800  11.359  66.155 1.00 60.53  ? 318 ARG B N   1 
ATOM   4975 C  CA  . ARG B  1  305 ? -8.902  10.467  66.490 1.00 57.97  ? 318 ARG B CA  1 
ATOM   4976 C  C   . ARG B  1  305 ? -9.439  9.813   65.219 1.00 51.98  ? 318 ARG B C   1 
ATOM   4977 O  O   . ARG B  1  305 ? -9.641  8.597   65.175 1.00 55.22  ? 318 ARG B O   1 
ATOM   4978 C  CB  . ARG B  1  305 ? -9.991  11.214  67.276 1.00 62.43  ? 318 ARG B CB  1 
ATOM   4979 C  CG  . ARG B  1  305 ? -11.087 10.272  67.772 1.00 63.95  ? 318 ARG B CG  1 
ATOM   4980 C  CD  . ARG B  1  305 ? -12.156 10.885  68.679 1.00 64.52  ? 318 ARG B CD  1 
ATOM   4981 N  NE  . ARG B  1  305 ? -11.781 10.779  70.096 1.00 64.58  ? 318 ARG B NE  1 
ATOM   4982 C  CZ  . ARG B  1  305 ? -12.301 9.928   70.980 1.00 62.40  ? 318 ARG B CZ  1 
ATOM   4983 N  NH1 . ARG B  1  305 ? -11.703 9.742   72.150 1.00 67.84  ? 318 ARG B NH1 1 
ATOM   4984 N  NH2 . ARG B  1  305 ? -13.365 9.203   70.682 1.00 56.61  ? 318 ARG B NH2 1 
ATOM   4985 N  N   . ARG B  1  306 ? -9.678  10.635  64.192 1.00 52.32  ? 319 ARG B N   1 
ATOM   4986 C  CA  . ARG B  1  306 ? -10.200 10.149  62.917 1.00 58.88  ? 319 ARG B CA  1 
ATOM   4987 C  C   . ARG B  1  306 ? -9.282  9.066   62.334 1.00 49.86  ? 319 ARG B C   1 
ATOM   4988 O  O   . ARG B  1  306 ? -9.752  8.003   61.949 1.00 48.37  ? 319 ARG B O   1 
ATOM   4989 C  CB  . ARG B  1  306 ? -10.407 11.301  61.921 1.00 71.34  ? 319 ARG B CB  1 
ATOM   4990 C  CG  . ARG B  1  306 ? -11.070 10.884  60.613 1.00 88.96  ? 319 ARG B CG  1 
ATOM   4991 C  CD  . ARG B  1  306 ? -11.330 12.034  59.650 1.00 103.11 ? 319 ARG B CD  1 
ATOM   4992 N  NE  . ARG B  1  306 ? -10.106 12.665  59.136 1.00 109.77 ? 319 ARG B NE  1 
ATOM   4993 C  CZ  . ARG B  1  306 ? -10.063 13.659  58.250 1.00 114.25 ? 319 ARG B CZ  1 
ATOM   4994 N  NH1 . ARG B  1  306 ? -11.182 14.193  57.778 1.00 108.13 ? 319 ARG B NH1 1 
ATOM   4995 N  NH2 . ARG B  1  306 ? -8.891  14.104  57.815 1.00 115.98 ? 319 ARG B NH2 1 
ATOM   4996 N  N   . ASN B  1  307 ? -7.974  9.334   62.301 1.00 49.46  ? 320 ASN B N   1 
ATOM   4997 C  CA  . ASN B  1  307 ? -7.000  8.461   61.654 1.00 54.66  ? 320 ASN B CA  1 
ATOM   4998 C  C   . ASN B  1  307 ? -6.853  7.166   62.448 1.00 52.29  ? 320 ASN B C   1 
ATOM   4999 O  O   . ASN B  1  307 ? -6.699  6.103   61.861 1.00 52.41  ? 320 ASN B O   1 
ATOM   5000 C  CB  . ASN B  1  307 ? -5.680  9.185   61.392 1.00 52.27  ? 320 ASN B CB  1 
ATOM   5001 C  CG  . ASN B  1  307 ? -5.839  10.247  60.325 1.00 51.38  ? 320 ASN B CG  1 
ATOM   5002 O  OD1 . ASN B  1  307 ? -6.954  10.465  59.837 1.00 53.35  ? 320 ASN B OD1 1 
ATOM   5003 N  ND2 . ASN B  1  307 ? -4.753  10.908  59.943 1.00 55.32  ? 320 ASN B ND2 1 
ATOM   5004 N  N   . LEU B  1  308 ? -6.940  7.252   63.774 1.00 50.08  ? 321 LEU B N   1 
ATOM   5005 C  CA  . LEU B  1  308 ? -6.989  6.074   64.625 1.00 50.53  ? 321 LEU B CA  1 
ATOM   5006 C  C   . LEU B  1  308 ? -8.171  5.176   64.269 1.00 49.82  ? 321 LEU B C   1 
ATOM   5007 O  O   . LEU B  1  308 ? -8.001  3.961   64.158 1.00 47.51  ? 321 LEU B O   1 
ATOM   5008 C  CB  . LEU B  1  308 ? -7.052  6.472   66.095 1.00 55.55  ? 321 LEU B CB  1 
ATOM   5009 C  CG  . LEU B  1  308 ? -5.705  6.619   66.802 1.00 60.18  ? 321 LEU B CG  1 
ATOM   5010 C  CD1 . LEU B  1  308 ? -5.877  7.349   68.108 1.00 63.09  ? 321 LEU B CD1 1 
ATOM   5011 C  CD2 . LEU B  1  308 ? -5.047  5.270   67.037 1.00 61.02  ? 321 LEU B CD2 1 
ATOM   5012 N  N   . ILE B  1  309 ? -9.361  5.770   64.121 1.00 49.45  ? 322 ILE B N   1 
ATOM   5013 C  CA  . ILE B  1  309 ? -10.552 5.000   63.796 1.00 49.66  ? 322 ILE B CA  1 
ATOM   5014 C  C   . ILE B  1  309 ? -10.339 4.266   62.471 1.00 44.13  ? 322 ILE B C   1 
ATOM   5015 O  O   . ILE B  1  309 ? -10.598 3.063   62.373 1.00 46.98  ? 322 ILE B O   1 
ATOM   5016 C  CB  . ILE B  1  309 ? -11.810 5.893   63.784 1.00 49.77  ? 322 ILE B CB  1 
ATOM   5017 C  CG1 . ILE B  1  309 ? -12.139 6.382   65.185 1.00 56.10  ? 322 ILE B CG1 1 
ATOM   5018 C  CG2 . ILE B  1  309 ? -12.994 5.167   63.144 1.00 48.99  ? 322 ILE B CG2 1 
ATOM   5019 C  CD1 . ILE B  1  309 ? -13.228 7.441   65.246 1.00 60.53  ? 322 ILE B CD1 1 
ATOM   5020 N  N   . LYS B  1  310 ? -9.845  5.000   61.467 1.00 46.69  ? 323 LYS B N   1 
ATOM   5021 C  CA  . LYS B  1  310 ? -9.635  4.448   60.131 1.00 52.45  ? 323 LYS B CA  1 
ATOM   5022 C  C   . LYS B  1  310 ? -8.604  3.314   60.151 1.00 45.64  ? 323 LYS B C   1 
ATOM   5023 O  O   . LYS B  1  310 ? -8.878  2.223   59.654 1.00 42.64  ? 323 LYS B O   1 
ATOM   5024 C  CB  . LYS B  1  310 ? -9.249  5.559   59.152 1.00 54.42  ? 323 LYS B CB  1 
ATOM   5025 C  CG  . LYS B  1  310 ? -10.399 6.460   58.746 1.00 63.45  ? 323 LYS B CG  1 
ATOM   5026 C  CD  . LYS B  1  310 ? -9.963  7.687   57.954 1.00 71.81  ? 323 LYS B CD  1 
ATOM   5027 C  CE  . LYS B  1  310 ? -11.101 8.438   57.336 1.00 75.92  ? 323 LYS B CE  1 
ATOM   5028 N  NZ  . LYS B  1  310 ? -10.592 9.654   56.702 1.00 79.94  ? 323 LYS B NZ  1 
ATOM   5029 N  N   . ASN B  1  311 ? -7.438  3.574   60.761 1.00 46.42  ? 324 ASN B N   1 
ATOM   5030 C  CA  . ASN B  1  311 ? -6.336  2.620   60.775 1.00 46.61  ? 324 ASN B CA  1 
ATOM   5031 C  C   . ASN B  1  311 ? -6.732  1.359   61.541 1.00 46.57  ? 324 ASN B C   1 
ATOM   5032 O  O   . ASN B  1  311 ? -6.323  0.264   61.158 1.00 42.33  ? 324 ASN B O   1 
ATOM   5033 C  CB  . ASN B  1  311 ? -5.054  3.250   61.302 1.00 46.56  ? 324 ASN B CB  1 
ATOM   5034 C  CG  . ASN B  1  311 ? -4.308  4.027   60.235 1.00 46.72  ? 324 ASN B CG  1 
ATOM   5035 O  OD1 . ASN B  1  311 ? -3.660  3.438   59.364 1.00 52.15  ? 324 ASN B OD1 1 
ATOM   5036 N  ND2 . ASN B  1  311 ? -4.363  5.348   60.276 1.00 44.50  ? 324 ASN B ND2 1 
ATOM   5037 N  N   . LEU B  1  312 ? -7.562  1.508   62.586 1.00 46.86  ? 325 LEU B N   1 
ATOM   5038 C  CA  . LEU B  1  312 ? -8.039  0.364   63.348 1.00 42.97  ? 325 LEU B CA  1 
ATOM   5039 C  C   . LEU B  1  312 ? -8.940  -0.503  62.484 1.00 41.76  ? 325 LEU B C   1 
ATOM   5040 O  O   . LEU B  1  312 ? -8.811  -1.729  62.507 1.00 46.36  ? 325 LEU B O   1 
ATOM   5041 C  CB  . LEU B  1  312 ? -8.750  0.797   64.627 1.00 47.32  ? 325 LEU B CB  1 
ATOM   5042 C  CG  . LEU B  1  312 ? -7.826  1.209   65.782 1.00 44.87  ? 325 LEU B CG  1 
ATOM   5043 C  CD1 . LEU B  1  312 ? -8.588  2.000   66.826 1.00 44.36  ? 325 LEU B CD1 1 
ATOM   5044 C  CD2 . LEU B  1  312 ? -7.166  0.023   66.429 1.00 41.10  ? 325 LEU B CD2 1 
ATOM   5045 N  N   . HIS B  1  313 ? -9.846  0.140   61.733 1.00 40.85  ? 326 HIS B N   1 
ATOM   5046 C  CA  . HIS B  1  313 ? -10.725 -0.574  60.818 1.00 41.32  ? 326 HIS B CA  1 
ATOM   5047 C  C   . HIS B  1  313 ? -9.892  -1.281  59.738 1.00 39.24  ? 326 HIS B C   1 
ATOM   5048 O  O   . HIS B  1  313 ? -10.119 -2.451  59.428 1.00 39.16  ? 326 HIS B O   1 
ATOM   5049 C  CB  . HIS B  1  313 ? -11.802 0.366   60.251 1.00 38.70  ? 326 HIS B CB  1 
ATOM   5050 C  CG  . HIS B  1  313 ? -12.730 -0.334  59.316 1.00 39.54  ? 326 HIS B CG  1 
ATOM   5051 N  ND1 . HIS B  1  313 ? -13.583 -1.314  59.771 1.00 46.69  ? 326 HIS B ND1 1 
ATOM   5052 C  CD2 . HIS B  1  313 ? -12.875 -0.283  57.985 1.00 37.97  ? 326 HIS B CD2 1 
ATOM   5053 C  CE1 . HIS B  1  313 ? -14.249 -1.809  58.738 1.00 51.74  ? 326 HIS B CE1 1 
ATOM   5054 N  NE2 . HIS B  1  313 ? -13.826 -1.191  57.643 1.00 45.72  ? 326 HIS B NE2 1 
ATOM   5055 N  N   . TYR B  1  314 ? -8.923  -0.560  59.170 1.00 36.03  ? 327 TYR B N   1 
ATOM   5056 C  CA  . TYR B  1  314 ? -8.065  -1.110  58.129 1.00 40.84  ? 327 TYR B CA  1 
ATOM   5057 C  C   . TYR B  1  314 ? -7.355  -2.371  58.615 1.00 39.38  ? 327 TYR B C   1 
ATOM   5058 O  O   . TYR B  1  314 ? -7.334  -3.362  57.888 1.00 37.41  ? 327 TYR B O   1 
ATOM   5059 C  CB  . TYR B  1  314 ? -7.030  -0.086  57.673 1.00 42.90  ? 327 TYR B CB  1 
ATOM   5060 C  CG  . TYR B  1  314 ? -7.590  1.160   57.004 1.00 44.24  ? 327 TYR B CG  1 
ATOM   5061 C  CD1 . TYR B  1  314 ? -8.891  1.207   56.504 1.00 45.51  ? 327 TYR B CD1 1 
ATOM   5062 C  CD2 . TYR B  1  314 ? -6.795  2.287   56.861 1.00 43.31  ? 327 TYR B CD2 1 
ATOM   5063 C  CE1 . TYR B  1  314 ? -9.382  2.345   55.885 1.00 43.94  ? 327 TYR B CE1 1 
ATOM   5064 C  CE2 . TYR B  1  314 ? -7.277  3.434   56.259 1.00 47.27  ? 327 TYR B CE2 1 
ATOM   5065 C  CZ  . TYR B  1  314 ? -8.572  3.465   55.773 1.00 48.25  ? 327 TYR B CZ  1 
ATOM   5066 O  OH  . TYR B  1  314 ? -8.929  4.639   55.177 1.00 46.10  ? 327 TYR B OH  1 
ATOM   5067 N  N   . TRP B  1  315 ? -6.833  -2.343  59.854 1.00 37.43  ? 328 TRP B N   1 
ATOM   5068 C  CA  . TRP B  1  315 ? -6.166  -3.500  60.424 1.00 36.50  ? 328 TRP B CA  1 
ATOM   5069 C  C   . TRP B  1  315 ? -7.143  -4.661  60.560 1.00 38.74  ? 328 TRP B C   1 
ATOM   5070 O  O   . TRP B  1  315 ? -6.780  -5.792  60.218 1.00 39.36  ? 328 TRP B O   1 
ATOM   5071 C  CB  . TRP B  1  315 ? -5.497  -3.143  61.758 1.00 38.14  ? 328 TRP B CB  1 
ATOM   5072 C  CG  . TRP B  1  315 ? -4.600  -4.211  62.343 1.00 45.23  ? 328 TRP B CG  1 
ATOM   5073 C  CD1 . TRP B  1  315 ? -3.577  -4.893  61.740 1.00 43.48  ? 328 TRP B CD1 1 
ATOM   5074 C  CD2 . TRP B  1  315 ? -4.663  -4.715  63.696 1.00 48.42  ? 328 TRP B CD2 1 
ATOM   5075 N  NE1 . TRP B  1  315 ? -3.019  -5.793  62.613 1.00 45.78  ? 328 TRP B NE1 1 
ATOM   5076 C  CE2 . TRP B  1  315 ? -3.656  -5.703  63.825 1.00 51.87  ? 328 TRP B CE2 1 
ATOM   5077 C  CE3 . TRP B  1  315 ? -5.455  -4.419  64.808 1.00 48.22  ? 328 TRP B CE3 1 
ATOM   5078 C  CZ2 . TRP B  1  315 ? -3.440  -6.399  65.015 1.00 50.38  ? 328 TRP B CZ2 1 
ATOM   5079 C  CZ3 . TRP B  1  315 ? -5.229  -5.095  65.985 1.00 51.78  ? 328 TRP B CZ3 1 
ATOM   5080 C  CH2 . TRP B  1  315 ? -4.246  -6.080  66.082 1.00 51.14  ? 328 TRP B CH2 1 
ATOM   5081 N  N   . TRP B  1  316 ? -8.375  -4.382  61.030 1.00 41.21  ? 329 TRP B N   1 
ATOM   5082 C  CA  . TRP B  1  316 ? -9.378  -5.420  61.233 1.00 37.10  ? 329 TRP B CA  1 
ATOM   5083 C  C   . TRP B  1  316 ? -9.706  -6.138  59.924 1.00 34.43  ? 329 TRP B C   1 
ATOM   5084 O  O   . TRP B  1  316 ? -9.915  -7.355  59.920 1.00 33.53  ? 329 TRP B O   1 
ATOM   5085 C  CB  . TRP B  1  316 ? -10.654 -4.846  61.875 1.00 41.53  ? 329 TRP B CB  1 
ATOM   5086 C  CG  . TRP B  1  316 ? -11.698 -5.909  62.070 1.00 40.61  ? 329 TRP B CG  1 
ATOM   5087 C  CD1 . TRP B  1  316 ? -11.736 -6.804  63.092 1.00 44.45  ? 329 TRP B CD1 1 
ATOM   5088 C  CD2 . TRP B  1  316 ? -12.787 -6.243  61.193 1.00 37.47  ? 329 TRP B CD2 1 
ATOM   5089 N  NE1 . TRP B  1  316 ? -12.790 -7.656  62.933 1.00 46.90  ? 329 TRP B NE1 1 
ATOM   5090 C  CE2 . TRP B  1  316 ? -13.452 -7.333  61.784 1.00 42.09  ? 329 TRP B CE2 1 
ATOM   5091 C  CE3 . TRP B  1  316 ? -13.266 -5.732  59.982 1.00 45.17  ? 329 TRP B CE3 1 
ATOM   5092 C  CZ2 . TRP B  1  316 ? -14.576 -7.918  61.214 1.00 50.93  ? 329 TRP B CZ2 1 
ATOM   5093 C  CZ3 . TRP B  1  316 ? -14.385 -6.315  59.416 1.00 47.00  ? 329 TRP B CZ3 1 
ATOM   5094 C  CH2 . TRP B  1  316 ? -15.025 -7.395  60.025 1.00 45.57  ? 329 TRP B CH2 1 
ATOM   5095 N  N   . THR B  1  317 ? -9.746  -5.400  58.805 1.00 36.83  ? 330 THR B N   1 
ATOM   5096 C  CA  . THR B  1  317 ? -10.087 -6.005  57.516 1.00 44.79  ? 330 THR B CA  1 
ATOM   5097 C  C   . THR B  1  317 ? -9.123  -7.146  57.191 1.00 43.03  ? 330 THR B C   1 
ATOM   5098 O  O   . THR B  1  317 ? -9.552  -8.178  56.694 1.00 42.35  ? 330 THR B O   1 
ATOM   5099 C  CB  . THR B  1  317 ? -10.126 -5.003  56.358 1.00 44.88  ? 330 THR B CB  1 
ATOM   5100 O  OG1 . THR B  1  317 ? -8.824  -4.458  56.182 1.00 48.42  ? 330 THR B OG1 1 
ATOM   5101 C  CG2 . THR B  1  317 ? -11.131 -3.882  56.567 1.00 43.99  ? 330 THR B CG2 1 
ATOM   5102 N  N   . GLY B  1  318 ? -7.831  -6.967  57.490 1.00 42.09  ? 331 GLY B N   1 
ATOM   5103 C  CA  . GLY B  1  318 ? -6.853  -8.033  57.321 1.00 42.22  ? 331 GLY B CA  1 
ATOM   5104 C  C   . GLY B  1  318 ? -6.980  -9.126  58.382 1.00 41.39  ? 331 GLY B C   1 
ATOM   5105 O  O   . GLY B  1  318 ? -6.942  -10.316 58.061 1.00 41.99  ? 331 GLY B O   1 
ATOM   5106 N  N   . VAL B  1  319 ? -7.104  -8.706  59.647 1.00 40.40  ? 332 VAL B N   1 
ATOM   5107 C  CA  . VAL B  1  319 ? -7.153  -9.626  60.776 1.00 41.33  ? 332 VAL B CA  1 
ATOM   5108 C  C   . VAL B  1  319 ? -8.340  -10.573 60.612 1.00 43.30  ? 332 VAL B C   1 
ATOM   5109 O  O   . VAL B  1  319 ? -8.235  -11.768 60.885 1.00 45.90  ? 332 VAL B O   1 
ATOM   5110 C  CB  . VAL B  1  319 ? -7.220  -8.818  62.091 1.00 43.84  ? 332 VAL B CB  1 
ATOM   5111 C  CG1 . VAL B  1  319 ? -7.585  -9.666  63.300 1.00 44.77  ? 332 VAL B CG1 1 
ATOM   5112 C  CG2 . VAL B  1  319 ? -5.917  -8.074  62.375 1.00 42.29  ? 332 VAL B CG2 1 
ATOM   5113 N  N   . ASN B  1  320 ? -9.474  -10.031 60.156 1.00 43.96  ? 333 ASN B N   1 
ATOM   5114 C  CA  . ASN B  1  320 ? -10.716 -10.785 60.101 1.00 44.98  ? 333 ASN B CA  1 
ATOM   5115 C  C   . ASN B  1  320 ? -10.528 -12.038 59.251 1.00 43.30  ? 333 ASN B C   1 
ATOM   5116 O  O   . ASN B  1  320 ? -10.936 -13.128 59.655 1.00 46.64  ? 333 ASN B O   1 
ATOM   5117 C  CB  . ASN B  1  320 ? -11.862 -9.903  59.619 1.00 46.07  ? 333 ASN B CB  1 
ATOM   5118 C  CG  . ASN B  1  320 ? -13.205 -10.578 59.768 1.00 47.10  ? 333 ASN B CG  1 
ATOM   5119 O  OD1 . ASN B  1  320 ? -13.552 -11.069 60.852 1.00 48.83  ? 333 ASN B OD1 1 
ATOM   5120 N  ND2 . ASN B  1  320 ? -13.982 -10.596 58.699 1.00 46.71  ? 333 ASN B ND2 1 
ATOM   5121 N  N   . VAL B  1  321 ? -9.878  -11.878 58.090 1.00 47.69  ? 334 VAL B N   1 
ATOM   5122 C  CA  . VAL B  1  321 ? -9.663  -12.991 57.174 1.00 50.52  ? 334 VAL B CA  1 
ATOM   5123 C  C   . VAL B  1  321 ? -8.553  -13.890 57.712 1.00 44.19  ? 334 VAL B C   1 
ATOM   5124 O  O   . VAL B  1  321 ? -8.681  -15.105 57.705 1.00 47.54  ? 334 VAL B O   1 
ATOM   5125 C  CB  . VAL B  1  321 ? -9.368  -12.521 55.735 1.00 53.26  ? 334 VAL B CB  1 
ATOM   5126 C  CG1 . VAL B  1  321 ? -9.161  -13.708 54.799 1.00 55.15  ? 334 VAL B CG1 1 
ATOM   5127 C  CG2 . VAL B  1  321 ? -10.490 -11.641 55.197 1.00 50.99  ? 334 VAL B CG2 1 
ATOM   5128 N  N   . ALA B  1  322 ? -7.488  -13.275 58.219 1.00 48.87  ? 335 ALA B N   1 
ATOM   5129 C  CA  . ALA B  1  322 ? -6.282  -13.991 58.609 1.00 50.96  ? 335 ALA B CA  1 
ATOM   5130 C  C   . ALA B  1  322 ? -6.464  -14.817 59.880 1.00 54.00  ? 335 ALA B C   1 
ATOM   5131 O  O   . ALA B  1  322 ? -5.837  -15.867 59.981 1.00 56.85  ? 335 ALA B O   1 
ATOM   5132 C  CB  . ALA B  1  322 ? -5.147  -13.012 58.782 1.00 51.35  ? 335 ALA B CB  1 
ATOM   5133 N  N   . PHE B  1  323 ? -7.291  -14.355 60.839 1.00 50.74  ? 336 PHE B N   1 
ATOM   5134 C  CA  . PHE B  1  323 ? -7.481  -15.077 62.092 1.00 51.01  ? 336 PHE B CA  1 
ATOM   5135 C  C   . PHE B  1  323 ? -8.757  -15.923 62.058 1.00 51.13  ? 336 PHE B C   1 
ATOM   5136 O  O   . PHE B  1  323 ? -9.110  -16.547 63.055 1.00 56.65  ? 336 PHE B O   1 
ATOM   5137 C  CB  . PHE B  1  323 ? -7.460  -14.079 63.251 1.00 48.06  ? 336 PHE B CB  1 
ATOM   5138 C  CG  . PHE B  1  323 ? -6.158  -13.319 63.454 1.00 46.75  ? 336 PHE B CG  1 
ATOM   5139 C  CD1 . PHE B  1  323 ? -5.033  -13.560 62.660 1.00 50.80  ? 336 PHE B CD1 1 
ATOM   5140 C  CD2 . PHE B  1  323 ? -6.042  -12.395 64.489 1.00 44.13  ? 336 PHE B CD2 1 
ATOM   5141 C  CE1 . PHE B  1  323 ? -3.854  -12.847 62.853 1.00 47.47  ? 336 PHE B CE1 1 
ATOM   5142 C  CE2 . PHE B  1  323 ? -4.857  -11.700 64.694 1.00 47.62  ? 336 PHE B CE2 1 
ATOM   5143 C  CZ  . PHE B  1  323 ? -3.765  -11.924 63.871 1.00 51.29  ? 336 PHE B CZ  1 
ATOM   5144 N  N   . GLY B  1  324 ? -9.430  -15.948 60.897 1.00 51.87  ? 337 GLY B N   1 
ATOM   5145 C  CA  . GLY B  1  324 ? -10.636 -16.733 60.696 1.00 52.18  ? 337 GLY B CA  1 
ATOM   5146 C  C   . GLY B  1  324 ? -11.864 -16.154 61.399 1.00 50.62  ? 337 GLY B C   1 
ATOM   5147 O  O   . GLY B  1  324 ? -12.705 -16.922 61.836 1.00 50.81  ? 337 GLY B O   1 
ATOM   5148 N  N   . GLY B  1  325 ? -11.977 -14.818 61.477 1.00 50.32  ? 338 GLY B N   1 
ATOM   5149 C  CA  . GLY B  1  325 ? -13.122 -14.143 62.076 1.00 48.58  ? 338 GLY B CA  1 
ATOM   5150 C  C   . GLY B  1  325 ? -12.843 -13.665 63.503 1.00 48.79  ? 338 GLY B C   1 
ATOM   5151 O  O   . GLY B  1  325 ? -12.652 -14.476 64.406 1.00 53.23  ? 338 GLY B O   1 
ATOM   5152 N  N   . CYS B  1  326 ? -12.794 -12.341 63.674 1.00 49.02  ? 339 CYS B N   1 
ATOM   5153 C  CA  . CYS B  1  326 ? -12.712 -11.693 64.975 1.00 56.55  ? 339 CYS B CA  1 
ATOM   5154 C  C   . CYS B  1  326 ? -13.735 -10.563 65.000 1.00 55.14  ? 339 CYS B C   1 
ATOM   5155 O  O   . CYS B  1  326 ? -13.898 -9.872  64.000 1.00 52.94  ? 339 CYS B O   1 
ATOM   5156 C  CB  . CYS B  1  326 ? -11.316 -11.127 65.243 1.00 59.19  ? 339 CYS B CB  1 
ATOM   5157 S  SG  . CYS B  1  326 ? -10.012 -12.385 65.298 1.00 71.14  ? 339 CYS B SG  1 
ATOM   5158 N  N   . ASP B  1  327 ? -14.439 -10.394 66.120 1.00 52.19  ? 340 ASP B N   1 
ATOM   5159 C  CA  . ASP B  1  327 ? -15.408 -9.316  66.237 1.00 51.47  ? 340 ASP B CA  1 
ATOM   5160 C  C   . ASP B  1  327 ? -14.663 -7.992  66.350 1.00 48.86  ? 340 ASP B C   1 
ATOM   5161 O  O   . ASP B  1  327 ? -13.804 -7.853  67.213 1.00 51.84  ? 340 ASP B O   1 
ATOM   5162 C  CB  . ASP B  1  327 ? -16.356 -9.546  67.405 1.00 53.94  ? 340 ASP B CB  1 
ATOM   5163 C  CG  . ASP B  1  327 ? -17.157 -10.837 67.323 1.00 57.12  ? 340 ASP B CG  1 
ATOM   5164 O  OD1 . ASP B  1  327 ? -17.586 -11.180 66.202 1.00 64.41  ? 340 ASP B OD1 1 
ATOM   5165 O  OD2 . ASP B  1  327 ? -17.355 -11.478 68.374 1.00 56.93  ? 340 ASP B OD2 1 
ATOM   5166 N  N   . GLU B  1  328 ? -14.999 -7.039  65.476 1.00 46.61  ? 341 GLU B N   1 
ATOM   5167 C  CA  . GLU B  1  328 ? -14.351 -5.735  65.436 1.00 46.21  ? 341 GLU B CA  1 
ATOM   5168 C  C   . GLU B  1  328 ? -14.682 -4.947  66.703 1.00 43.65  ? 341 GLU B C   1 
ATOM   5169 O  O   . GLU B  1  328 ? -15.826 -4.952  67.144 1.00 44.32  ? 341 GLU B O   1 
ATOM   5170 C  CB  . GLU B  1  328 ? -14.770 -4.968  64.177 1.00 45.78  ? 341 GLU B CB  1 
ATOM   5171 C  CG  . GLU B  1  328 ? -13.969 -3.688  63.938 1.00 48.88  ? 341 GLU B CG  1 
ATOM   5172 C  CD  . GLU B  1  328 ? -14.263 -2.916  62.650 1.00 47.30  ? 341 GLU B CD  1 
ATOM   5173 O  OE1 . GLU B  1  328 ? -15.152 -3.321  61.889 1.00 52.24  ? 341 GLU B OE1 1 
ATOM   5174 O  OE2 . GLU B  1  328 ? -13.588 -1.907  62.391 1.00 45.47  ? 341 GLU B OE2 1 
ATOM   5175 N  N   . LEU B  1  329 ? -13.655 -4.296  67.274 1.00 40.18  ? 342 LEU B N   1 
ATOM   5176 C  CA  . LEU B  1  329 ? -13.790 -3.421  68.427 1.00 45.05  ? 342 LEU B CA  1 
ATOM   5177 C  C   . LEU B  1  329 ? -13.691 -1.973  67.950 1.00 44.86  ? 342 LEU B C   1 
ATOM   5178 O  O   . LEU B  1  329 ? -13.026 -1.712  66.954 1.00 45.34  ? 342 LEU B O   1 
ATOM   5179 C  CB  . LEU B  1  329 ? -12.717 -3.754  69.470 1.00 48.31  ? 342 LEU B CB  1 
ATOM   5180 C  CG  . LEU B  1  329 ? -12.753 -5.165  70.075 1.00 51.21  ? 342 LEU B CG  1 
ATOM   5181 C  CD1 . LEU B  1  329 ? -11.501 -5.395  70.908 1.00 53.38  ? 342 LEU B CD1 1 
ATOM   5182 C  CD2 . LEU B  1  329 ? -14.016 -5.432  70.913 1.00 48.45  ? 342 LEU B CD2 1 
ATOM   5183 N  N   . PHE B  1  330 ? -14.371 -1.053  68.655 1.00 47.91  ? 343 PHE B N   1 
ATOM   5184 C  CA  . PHE B  1  330 ? -14.454 0.357   68.297 1.00 47.12  ? 343 PHE B CA  1 
ATOM   5185 C  C   . PHE B  1  330 ? -14.152 1.225   69.520 1.00 53.31  ? 343 PHE B C   1 
ATOM   5186 O  O   . PHE B  1  330 ? -15.020 1.937   70.029 1.00 54.77  ? 343 PHE B O   1 
ATOM   5187 C  CB  . PHE B  1  330 ? -15.858 0.691   67.794 1.00 48.49  ? 343 PHE B CB  1 
ATOM   5188 C  CG  . PHE B  1  330 ? -16.281 -0.154  66.609 1.00 44.26  ? 343 PHE B CG  1 
ATOM   5189 C  CD1 . PHE B  1  330 ? -15.839 0.164   65.333 1.00 46.90  ? 343 PHE B CD1 1 
ATOM   5190 C  CD2 . PHE B  1  330 ? -17.085 -1.272  66.775 1.00 47.59  ? 343 PHE B CD2 1 
ATOM   5191 C  CE1 . PHE B  1  330 ? -16.223 -0.605  64.242 1.00 44.14  ? 343 PHE B CE1 1 
ATOM   5192 C  CE2 . PHE B  1  330 ? -17.459 -2.042  65.687 1.00 49.34  ? 343 PHE B CE2 1 
ATOM   5193 C  CZ  . PHE B  1  330 ? -17.033 -1.708  64.424 1.00 45.28  ? 343 PHE B CZ  1 
ATOM   5194 N  N   . PRO B  1  331 ? -12.901 1.231   70.021 1.00 56.23  ? 344 PRO B N   1 
ATOM   5195 C  CA  . PRO B  1  331 ? -12.580 1.980   71.239 1.00 55.86  ? 344 PRO B CA  1 
ATOM   5196 C  C   . PRO B  1  331 ? -12.758 3.495   71.170 1.00 51.21  ? 344 PRO B C   1 
ATOM   5197 O  O   . PRO B  1  331 ? -12.872 4.127   72.215 1.00 56.25  ? 344 PRO B O   1 
ATOM   5198 C  CB  . PRO B  1  331 ? -11.114 1.560   71.469 1.00 54.15  ? 344 PRO B CB  1 
ATOM   5199 C  CG  . PRO B  1  331 ? -10.601 1.311   70.084 1.00 52.52  ? 344 PRO B CG  1 
ATOM   5200 C  CD  . PRO B  1  331 ? -11.738 0.538   69.438 1.00 52.48  ? 344 PRO B CD  1 
ATOM   5201 N  N   . TYR B  1  332 ? -12.779 4.071   69.960 1.00 47.95  ? 345 TYR B N   1 
ATOM   5202 C  CA  . TYR B  1  332 ? -13.012 5.505   69.795 1.00 47.78  ? 345 TYR B CA  1 
ATOM   5203 C  C   . TYR B  1  332 ? -14.318 5.730   69.025 1.00 47.07  ? 345 TYR B C   1 
ATOM   5204 O  O   . TYR B  1  332 ? -14.548 6.794   68.459 1.00 50.19  ? 345 TYR B O   1 
ATOM   5205 C  CB  . TYR B  1  332 ? -11.824 6.185   69.105 1.00 47.13  ? 345 TYR B CB  1 
ATOM   5206 C  CG  . TYR B  1  332 ? -10.480 5.831   69.723 1.00 50.55  ? 345 TYR B CG  1 
ATOM   5207 C  CD1 . TYR B  1  332 ? -10.101 6.370   70.947 1.00 49.15  ? 345 TYR B CD1 1 
ATOM   5208 C  CD2 . TYR B  1  332 ? -9.597  4.956   69.090 1.00 51.20  ? 345 TYR B CD2 1 
ATOM   5209 C  CE1 . TYR B  1  332 ? -8.877  6.065   71.522 1.00 53.01  ? 345 TYR B CE1 1 
ATOM   5210 C  CE2 . TYR B  1  332 ? -8.383  4.622   69.667 1.00 54.97  ? 345 TYR B CE2 1 
ATOM   5211 C  CZ  . TYR B  1  332 ? -8.020  5.182   70.882 1.00 55.06  ? 345 TYR B CZ  1 
ATOM   5212 O  OH  . TYR B  1  332 ? -6.829  4.854   71.453 1.00 55.00  ? 345 TYR B OH  1 
ATOM   5213 N  N   . GLY B  1  333 ? -15.192 4.726   69.037 1.00 46.46  ? 346 GLY B N   1 
ATOM   5214 C  CA  . GLY B  1  333 ? -16.444 4.796   68.305 1.00 52.25  ? 346 GLY B CA  1 
ATOM   5215 C  C   . GLY B  1  333 ? -16.216 4.801   66.792 1.00 57.82  ? 346 GLY B C   1 
ATOM   5216 O  O   . GLY B  1  333 ? -15.277 4.175   66.302 1.00 58.17  ? 346 GLY B O   1 
ATOM   5217 N  N   . GLN B  1  334 ? -17.096 5.498   66.065 1.00 65.35  ? 347 GLN B N   1 
ATOM   5218 C  CA  . GLN B  1  334 ? -17.099 5.475   64.610 1.00 63.01  ? 347 GLN B CA  1 
ATOM   5219 C  C   . GLN B  1  334 ? -17.135 6.887   64.040 1.00 64.50  ? 347 GLN B C   1 
ATOM   5220 O  O   . GLN B  1  334 ? -17.453 7.853   64.724 1.00 71.24  ? 347 GLN B O   1 
ATOM   5221 C  CB  . GLN B  1  334 ? -18.281 4.682   64.055 1.00 67.50  ? 347 GLN B CB  1 
ATOM   5222 C  CG  . GLN B  1  334 ? -18.127 3.184   64.255 1.00 73.69  ? 347 GLN B CG  1 
ATOM   5223 C  CD  . GLN B  1  334 ? -19.326 2.398   63.779 1.00 80.94  ? 347 GLN B CD  1 
ATOM   5224 O  OE1 . GLN B  1  334 ? -20.323 2.957   63.312 1.00 82.49  ? 347 GLN B OE1 1 
ATOM   5225 N  NE2 . GLN B  1  334 ? -19.253 1.085   63.925 1.00 90.79  ? 347 GLN B NE2 1 
ATOM   5226 N  N   . LEU B  1  335 ? -16.876 6.970   62.730 1.00 69.05  ? 348 LEU B N   1 
ATOM   5227 C  CA  . LEU B  1  335 ? -16.888 8.242   62.023 1.00 68.62  ? 348 LEU B CA  1 
ATOM   5228 C  C   . LEU B  1  335 ? -18.332 8.672   61.719 1.00 70.01  ? 348 LEU B C   1 
ATOM   5229 O  O   . LEU B  1  335 ? -19.145 7.784   61.384 1.00 70.25  ? 348 LEU B O   1 
ATOM   5230 C  CB  . LEU B  1  335 ? -16.001 8.129   60.782 1.00 65.72  ? 348 LEU B CB  1 
ATOM   5231 C  CG  . LEU B  1  335 ? -14.494 8.145   61.079 1.00 68.83  ? 348 LEU B CG  1 
ATOM   5232 C  CD1 . LEU B  1  335 ? -13.694 8.276   59.802 1.00 70.67  ? 348 LEU B CD1 1 
ATOM   5233 C  CD2 . LEU B  1  335 ? -14.034 9.244   62.045 1.00 68.53  ? 348 LEU B CD2 1 
ATOM   5234 N  N   . GLN C  1  1   ? 2.555   -17.511 24.452 1.00 121.28 ? 14  GLN C N   1 
ATOM   5235 C  CA  . GLN C  1  1   ? 2.789   -16.339 25.343 1.00 118.38 ? 14  GLN C CA  1 
ATOM   5236 C  C   . GLN C  1  1   ? 3.204   -15.132 24.500 1.00 110.96 ? 14  GLN C C   1 
ATOM   5237 O  O   . GLN C  1  1   ? 2.442   -14.169 24.369 1.00 104.46 ? 14  GLN C O   1 
ATOM   5238 C  CB  . GLN C  1  1   ? 3.789   -16.661 26.457 1.00 117.08 ? 14  GLN C CB  1 
ATOM   5239 C  CG  . GLN C  1  1   ? 5.187   -17.063 25.995 1.00 118.05 ? 14  GLN C CG  1 
ATOM   5240 C  CD  . GLN C  1  1   ? 6.139   -17.309 27.140 1.00 119.64 ? 14  GLN C CD  1 
ATOM   5241 O  OE1 . GLN C  1  1   ? 5.732   -17.494 28.292 1.00 112.60 ? 14  GLN C OE1 1 
ATOM   5242 N  NE2 . GLN C  1  1   ? 7.426   -17.306 26.830 1.00 120.35 ? 14  GLN C NE2 1 
ATOM   5243 N  N   . GLY C  1  2   ? 4.407   -15.210 23.912 1.00 91.66  ? 15  GLY C N   1 
ATOM   5244 C  CA  . GLY C  1  2   ? 4.910   -14.169 23.036 1.00 77.79  ? 15  GLY C CA  1 
ATOM   5245 C  C   . GLY C  1  2   ? 4.365   -14.366 21.628 1.00 62.81  ? 15  GLY C C   1 
ATOM   5246 O  O   . GLY C  1  2   ? 4.084   -15.484 21.225 1.00 67.69  ? 15  GLY C O   1 
ATOM   5247 N  N   . VAL C  1  3   ? 4.259   -13.267 20.888 1.00 60.64  ? 16  VAL C N   1 
ATOM   5248 C  CA  . VAL C  1  3   ? 3.743   -13.269 19.535 1.00 61.14  ? 16  VAL C CA  1 
ATOM   5249 C  C   . VAL C  1  3   ? 4.828   -12.675 18.647 1.00 59.93  ? 16  VAL C C   1 
ATOM   5250 O  O   . VAL C  1  3   ? 5.644   -11.880 19.111 1.00 53.27  ? 16  VAL C O   1 
ATOM   5251 C  CB  . VAL C  1  3   ? 2.434   -12.455 19.528 1.00 64.39  ? 16  VAL C CB  1 
ATOM   5252 C  CG1 . VAL C  1  3   ? 1.933   -12.099 18.133 1.00 68.06  ? 16  VAL C CG1 1 
ATOM   5253 C  CG2 . VAL C  1  3   ? 1.336   -13.169 20.311 1.00 65.80  ? 16  VAL C CG2 1 
ATOM   5254 N  N   . ASP C  1  4   ? 4.827   -13.085 17.380 1.00 62.46  ? 17  ASP C N   1 
ATOM   5255 C  CA  . ASP C  1  4   ? 5.662   -12.466 16.370 1.00 62.67  ? 17  ASP C CA  1 
ATOM   5256 C  C   . ASP C  1  4   ? 4.835   -11.386 15.674 1.00 60.75  ? 17  ASP C C   1 
ATOM   5257 O  O   . ASP C  1  4   ? 3.845   -11.709 15.024 1.00 71.16  ? 17  ASP C O   1 
ATOM   5258 C  CB  . ASP C  1  4   ? 6.196   -13.519 15.415 1.00 71.71  ? 17  ASP C CB  1 
ATOM   5259 C  CG  . ASP C  1  4   ? 7.388   -13.075 14.581 1.00 81.35  ? 17  ASP C CG  1 
ATOM   5260 O  OD1 . ASP C  1  4   ? 7.326   -11.968 14.017 1.00 91.21  ? 17  ASP C OD1 1 
ATOM   5261 O  OD2 . ASP C  1  4   ? 8.365   -13.845 14.494 1.00 87.41  ? 17  ASP C OD2 1 
ATOM   5262 N  N   . PRO C  1  5   ? 5.186   -10.080 15.792 1.00 60.27  ? 18  PRO C N   1 
ATOM   5263 C  CA  . PRO C  1  5   ? 4.380   -9.002  15.211 1.00 57.18  ? 18  PRO C CA  1 
ATOM   5264 C  C   . PRO C  1  5   ? 4.412   -8.945  13.683 1.00 50.16  ? 18  PRO C C   1 
ATOM   5265 O  O   . PRO C  1  5   ? 5.482   -8.804  13.095 1.00 51.62  ? 18  PRO C O   1 
ATOM   5266 C  CB  . PRO C  1  5   ? 4.988   -7.722  15.820 1.00 62.49  ? 18  PRO C CB  1 
ATOM   5267 C  CG  . PRO C  1  5   ? 5.889   -8.204  16.936 1.00 61.29  ? 18  PRO C CG  1 
ATOM   5268 C  CD  . PRO C  1  5   ? 6.373   -9.570  16.501 1.00 59.05  ? 18  PRO C CD  1 
ATOM   5269 N  N   . PRO C  1  6   ? 3.239   -8.983  13.003 1.00 49.19  ? 19  PRO C N   1 
ATOM   5270 C  CA  . PRO C  1  6   ? 3.172   -8.872  11.544 1.00 50.05  ? 19  PRO C CA  1 
ATOM   5271 C  C   . PRO C  1  6   ? 3.540   -7.454  11.129 1.00 45.95  ? 19  PRO C C   1 
ATOM   5272 O  O   . PRO C  1  6   ? 3.351   -6.515  11.900 1.00 47.58  ? 19  PRO C O   1 
ATOM   5273 C  CB  . PRO C  1  6   ? 1.707   -9.184  11.173 1.00 47.78  ? 19  PRO C CB  1 
ATOM   5274 C  CG  . PRO C  1  6   ? 1.056   -9.612  12.464 1.00 48.81  ? 19  PRO C CG  1 
ATOM   5275 C  CD  . PRO C  1  6   ? 1.904   -9.094  13.613 1.00 48.64  ? 19  PRO C CD  1 
ATOM   5276 N  N   . PRO C  1  7   ? 4.035   -7.236  9.899  1.00 46.92  ? 20  PRO C N   1 
ATOM   5277 C  CA  . PRO C  1  7   ? 4.245   -5.875  9.411  1.00 44.80  ? 20  PRO C CA  1 
ATOM   5278 C  C   . PRO C  1  7   ? 2.909   -5.137  9.362  1.00 43.85  ? 20  PRO C C   1 
ATOM   5279 O  O   . PRO C  1  7   ? 1.842   -5.755  9.395  1.00 35.22  ? 20  PRO C O   1 
ATOM   5280 C  CB  . PRO C  1  7   ? 4.909   -6.065  8.037  1.00 46.24  ? 20  PRO C CB  1 
ATOM   5281 C  CG  . PRO C  1  7   ? 4.522   -7.471  7.633  1.00 49.81  ? 20  PRO C CG  1 
ATOM   5282 C  CD  . PRO C  1  7   ? 4.412   -8.271  8.928  1.00 51.26  ? 20  PRO C CD  1 
ATOM   5283 N  N   . PRO C  1  8   ? 2.919   -3.788  9.324  1.00 43.43  ? 21  PRO C N   1 
ATOM   5284 C  CA  . PRO C  1  8   ? 1.685   -3.022  9.192  1.00 42.65  ? 21  PRO C CA  1 
ATOM   5285 C  C   . PRO C  1  8   ? 0.941   -3.370  7.896  1.00 41.16  ? 21  PRO C C   1 
ATOM   5286 O  O   . PRO C  1  8   ? 1.538   -3.548  6.841  1.00 40.81  ? 21  PRO C O   1 
ATOM   5287 C  CB  . PRO C  1  8   ? 2.177   -1.555  9.226  1.00 46.57  ? 21  PRO C CB  1 
ATOM   5288 C  CG  . PRO C  1  8   ? 3.636   -1.624  8.842  1.00 50.89  ? 21  PRO C CG  1 
ATOM   5289 C  CD  . PRO C  1  8   ? 4.110   -2.940  9.390  1.00 47.88  ? 21  PRO C CD  1 
ATOM   5290 N  N   . PRO C  1  9   ? -0.402  -3.455  7.927  1.00 38.55  ? 22  PRO C N   1 
ATOM   5291 C  CA  . PRO C  1  9   ? -1.197  -3.550  6.702  1.00 38.39  ? 22  PRO C CA  1 
ATOM   5292 C  C   . PRO C  1  9   ? -0.954  -2.348  5.798  1.00 35.98  ? 22  PRO C C   1 
ATOM   5293 O  O   . PRO C  1  9   ? -0.682  -1.247  6.287  1.00 34.26  ? 22  PRO C O   1 
ATOM   5294 C  CB  . PRO C  1  9   ? -2.661  -3.601  7.205  1.00 39.12  ? 22  PRO C CB  1 
ATOM   5295 C  CG  . PRO C  1  9   ? -2.529  -4.027  8.669  1.00 41.51  ? 22  PRO C CG  1 
ATOM   5296 C  CD  . PRO C  1  9   ? -1.224  -3.443  9.144  1.00 39.54  ? 22  PRO C CD  1 
ATOM   5297 N  N   . GLY C  1  10  ? -1.086  -2.568  4.478  1.00 37.51  ? 23  GLY C N   1 
ATOM   5298 C  CA  . GLY C  1  10  ? -1.015  -1.486  3.505  1.00 38.20  ? 23  GLY C CA  1 
ATOM   5299 C  C   . GLY C  1  10  ? -2.365  -0.783  3.351  1.00 37.76  ? 23  GLY C C   1 
ATOM   5300 O  O   . GLY C  1  10  ? -3.331  -1.119  4.045  1.00 36.34  ? 23  GLY C O   1 
ATOM   5301 N  N   . PRO C  1  11  ? -2.478  0.180   2.403  1.00 42.01  ? 24  PRO C N   1 
ATOM   5302 C  CA  . PRO C  1  11  ? -3.736  0.890   2.166  1.00 42.36  ? 24  PRO C CA  1 
ATOM   5303 C  C   . PRO C  1  11  ? -4.808  -0.108  1.741  1.00 39.40  ? 24  PRO C C   1 
ATOM   5304 O  O   . PRO C  1  11  ? -4.473  -1.183  1.238  1.00 35.55  ? 24  PRO C O   1 
ATOM   5305 C  CB  . PRO C  1  11  ? -3.414  1.918   1.060  1.00 43.05  ? 24  PRO C CB  1 
ATOM   5306 C  CG  . PRO C  1  11  ? -1.902  1.920   0.946  1.00 42.68  ? 24  PRO C CG  1 
ATOM   5307 C  CD  . PRO C  1  11  ? -1.419  0.577   1.456  1.00 42.48  ? 24  PRO C CD  1 
ATOM   5308 N  N   . PRO C  1  12  ? -6.114  0.206   1.910  1.00 38.59  ? 25  PRO C N   1 
ATOM   5309 C  CA  . PRO C  1  12  ? -7.167  -0.683  1.404  1.00 40.22  ? 25  PRO C CA  1 
ATOM   5310 C  C   . PRO C  1  12  ? -7.166  -0.768  -0.124 1.00 38.65  ? 25  PRO C C   1 
ATOM   5311 O  O   . PRO C  1  12  ? -6.753  0.178   -0.791 1.00 39.92  ? 25  PRO C O   1 
ATOM   5312 C  CB  . PRO C  1  12  ? -8.450  -0.054  1.972  1.00 41.51  ? 25  PRO C CB  1 
ATOM   5313 C  CG  . PRO C  1  12  ? -8.095  1.397   2.187  1.00 43.27  ? 25  PRO C CG  1 
ATOM   5314 C  CD  . PRO C  1  12  ? -6.622  1.418   2.568  1.00 39.46  ? 25  PRO C CD  1 
ATOM   5315 N  N   . SER C  1  13  ? -7.615  -1.909  -0.668 1.00 45.30  ? 26  SER C N   1 
ATOM   5316 C  CA  . SER C  1  13  ? -7.859  -2.069  -2.098 1.00 48.16  ? 26  SER C CA  1 
ATOM   5317 C  C   . SER C  1  13  ? -8.823  -1.013  -2.635 1.00 44.06  ? 26  SER C C   1 
ATOM   5318 O  O   . SER C  1  13  ? -8.505  -0.374  -3.634 1.00 53.03  ? 26  SER C O   1 
ATOM   5319 C  CB  . SER C  1  13  ? -8.394  -3.438  -2.397 1.00 51.13  ? 26  SER C CB  1 
ATOM   5320 O  OG  . SER C  1  13  ? -7.496  -4.416  -1.920 1.00 55.44  ? 26  SER C OG  1 
ATOM   5321 N  N   . PHE C  1  14  ? -9.998  -0.882  -1.993 1.00 42.75  ? 27  PHE C N   1 
ATOM   5322 C  CA  . PHE C  1  14  ? -11.012 0.091   -2.383 1.00 41.60  ? 27  PHE C CA  1 
ATOM   5323 C  C   . PHE C  1  14  ? -10.871 1.284   -1.451 1.00 42.97  ? 27  PHE C C   1 
ATOM   5324 O  O   . PHE C  1  14  ? -10.952 1.119   -0.234 1.00 43.21  ? 27  PHE C O   1 
ATOM   5325 C  CB  . PHE C  1  14  ? -12.432 -0.489  -2.355 1.00 39.32  ? 27  PHE C CB  1 
ATOM   5326 C  CG  . PHE C  1  14  ? -13.566 0.478   -2.645 1.00 44.53  ? 27  PHE C CG  1 
ATOM   5327 C  CD1 . PHE C  1  14  ? -13.796 0.932   -3.940 1.00 44.68  ? 27  PHE C CD1 1 
ATOM   5328 C  CD2 . PHE C  1  14  ? -14.441 0.877   -1.637 1.00 48.57  ? 27  PHE C CD2 1 
ATOM   5329 C  CE1 . PHE C  1  14  ? -14.850 1.798   -4.204 1.00 43.02  ? 27  PHE C CE1 1 
ATOM   5330 C  CE2 . PHE C  1  14  ? -15.490 1.739   -1.908 1.00 50.21  ? 27  PHE C CE2 1 
ATOM   5331 C  CZ  . PHE C  1  14  ? -15.681 2.207   -3.190 1.00 46.16  ? 27  PHE C CZ  1 
ATOM   5332 N  N   . THR C  1  15  ? -10.686 2.481   -2.031 1.00 43.52  ? 28  THR C N   1 
ATOM   5333 C  CA  . THR C  1  15  ? -10.501 3.698   -1.257 1.00 37.75  ? 28  THR C CA  1 
ATOM   5334 C  C   . THR C  1  15  ? -11.641 4.683   -1.496 1.00 40.88  ? 28  THR C C   1 
ATOM   5335 O  O   . THR C  1  15  ? -11.480 5.850   -1.170 1.00 41.30  ? 28  THR C O   1 
ATOM   5336 C  CB  . THR C  1  15  ? -9.155  4.343   -1.604 1.00 40.75  ? 28  THR C CB  1 
ATOM   5337 O  OG1 . THR C  1  15  ? -9.196  4.871   -2.931 1.00 43.34  ? 28  THR C OG1 1 
ATOM   5338 C  CG2 . THR C  1  15  ? -7.972  3.397   -1.440 1.00 39.78  ? 28  THR C CG2 1 
ATOM   5339 N  N   . GLY C  1  16  ? -12.770 4.246   -2.070 1.00 39.51  ? 29  GLY C N   1 
ATOM   5340 C  CA  . GLY C  1  16  ? -13.919 5.123   -2.239 1.00 41.01  ? 29  GLY C CA  1 
ATOM   5341 C  C   . GLY C  1  16  ? -14.827 5.141   -1.003 1.00 44.32  ? 29  GLY C C   1 
ATOM   5342 O  O   . GLY C  1  16  ? -14.530 4.505   0.006  1.00 41.59  ? 29  GLY C O   1 
ATOM   5343 N  N   . THR C  1  17  ? -15.939 5.883   -1.090 1.00 46.91  ? 30  THR C N   1 
ATOM   5344 C  CA  . THR C  1  17  ? -16.934 5.891   -0.031 1.00 48.50  ? 30  THR C CA  1 
ATOM   5345 C  C   . THR C  1  17  ? -17.677 4.558   -0.042 1.00 48.40  ? 30  THR C C   1 
ATOM   5346 O  O   . THR C  1  17  ? -17.670 3.841   -1.039 1.00 39.81  ? 30  THR C O   1 
ATOM   5347 C  CB  . THR C  1  17  ? -17.873 7.083   -0.188 1.00 50.11  ? 30  THR C CB  1 
ATOM   5348 O  OG1 . THR C  1  17  ? -18.621 7.044   1.017  1.00 52.15  ? 30  THR C OG1 1 
ATOM   5349 C  CG2 . THR C  1  17  ? -18.775 6.982   -1.407 1.00 47.41  ? 30  THR C CG2 1 
ATOM   5350 N  N   . LYS C  1  18  ? -18.253 4.223   1.113  1.00 47.27  ? 31  LYS C N   1 
ATOM   5351 C  CA  . LYS C  1  18  ? -19.166 3.102   1.252  1.00 48.28  ? 31  LYS C CA  1 
ATOM   5352 C  C   . LYS C  1  18  ? -19.930 3.282   2.563  1.00 47.59  ? 31  LYS C C   1 
ATOM   5353 O  O   . LYS C  1  18  ? -19.523 4.080   3.408  1.00 44.35  ? 31  LYS C O   1 
ATOM   5354 C  CB  . LYS C  1  18  ? -18.400 1.778   1.224  1.00 50.53  ? 31  LYS C CB  1 
ATOM   5355 C  CG  . LYS C  1  18  ? -17.424 1.575   2.374  1.00 57.85  ? 31  LYS C CG  1 
ATOM   5356 C  CD  . LYS C  1  18  ? -16.700 0.240   2.277  1.00 68.58  ? 31  LYS C CD  1 
ATOM   5357 C  CE  . LYS C  1  18  ? -16.510 -0.377  3.625  1.00 88.59  ? 31  LYS C CE  1 
ATOM   5358 N  NZ  . LYS C  1  18  ? -15.552 -1.484  3.611  1.00 97.72  ? 31  LYS C NZ  1 
ATOM   5359 N  N   . LEU C  1  19  ? -21.033 2.542   2.712  1.00 48.24  ? 32  LEU C N   1 
ATOM   5360 C  CA  . LEU C  1  19  ? -21.771 2.466   3.958  1.00 44.86  ? 32  LEU C CA  1 
ATOM   5361 C  C   . LEU C  1  19  ? -20.898 1.727   4.957  1.00 44.32  ? 32  LEU C C   1 
ATOM   5362 O  O   . LEU C  1  19  ? -20.478 0.612   4.673  1.00 49.83  ? 32  LEU C O   1 
ATOM   5363 C  CB  . LEU C  1  19  ? -23.105 1.744   3.761  1.00 44.97  ? 32  LEU C CB  1 
ATOM   5364 C  CG  . LEU C  1  19  ? -23.954 1.525   5.017  1.00 46.20  ? 32  LEU C CG  1 
ATOM   5365 C  CD1 . LEU C  1  19  ? -24.458 2.855   5.554  1.00 43.81  ? 32  LEU C CD1 1 
ATOM   5366 C  CD2 . LEU C  1  19  ? -25.107 0.572   4.770  1.00 47.40  ? 32  LEU C CD2 1 
ATOM   5367 N  N   . VAL C  1  20  ? -20.636 2.343   6.116  1.00 44.89  ? 33  VAL C N   1 
ATOM   5368 C  CA  . VAL C  1  20  ? -19.835 1.688   7.142  1.00 48.80  ? 33  VAL C CA  1 
ATOM   5369 C  C   . VAL C  1  20  ? -20.717 1.298   8.327  1.00 45.78  ? 33  VAL C C   1 
ATOM   5370 O  O   . VAL C  1  20  ? -20.377 0.366   9.041  1.00 49.11  ? 33  VAL C O   1 
ATOM   5371 C  CB  . VAL C  1  20  ? -18.610 2.513   7.587  1.00 47.58  ? 33  VAL C CB  1 
ATOM   5372 C  CG1 . VAL C  1  20  ? -17.686 2.810   6.417  1.00 49.51  ? 33  VAL C CG1 1 
ATOM   5373 C  CG2 . VAL C  1  20  ? -18.997 3.808   8.279  1.00 46.61  ? 33  VAL C CG2 1 
ATOM   5374 N  N   . ASN C  1  21  ? -21.839 2.001   8.513  1.00 48.73  ? 34  ASN C N   1 
ATOM   5375 C  CA  . ASN C  1  21  ? -22.848 1.641   9.499  1.00 48.24  ? 34  ASN C CA  1 
ATOM   5376 C  C   . ASN C  1  21  ? -23.787 0.607   8.886  1.00 48.84  ? 34  ASN C C   1 
ATOM   5377 O  O   . ASN C  1  21  ? -24.890 0.945   8.476  1.00 50.37  ? 34  ASN C O   1 
ATOM   5378 C  CB  . ASN C  1  21  ? -23.583 2.900   9.946  1.00 46.05  ? 34  ASN C CB  1 
ATOM   5379 C  CG  . ASN C  1  21  ? -24.397 2.704   11.196 1.00 46.08  ? 34  ASN C CG  1 
ATOM   5380 O  OD1 . ASN C  1  21  ? -24.533 1.588   11.711 1.00 50.31  ? 34  ASN C OD1 1 
ATOM   5381 N  ND2 . ASN C  1  21  ? -24.961 3.797   11.672 1.00 47.81  ? 34  ASN C ND2 1 
ATOM   5382 N  N   . ASP C  1  22  ? -23.334 -0.645  8.806  1.00 50.49  ? 35  ASP C N   1 
ATOM   5383 C  CA  . ASP C  1  22  ? -24.024 -1.669  8.036  1.00 56.56  ? 35  ASP C CA  1 
ATOM   5384 C  C   . ASP C  1  22  ? -24.397 -2.813  8.970  1.00 57.89  ? 35  ASP C C   1 
ATOM   5385 O  O   . ASP C  1  22  ? -24.120 -2.740  10.158 1.00 65.55  ? 35  ASP C O   1 
ATOM   5386 C  CB  . ASP C  1  22  ? -23.192 -2.124  6.843  1.00 61.82  ? 35  ASP C CB  1 
ATOM   5387 C  CG  . ASP C  1  22  ? -21.784 -2.624  7.146  1.00 67.14  ? 35  ASP C CG  1 
ATOM   5388 O  OD1 . ASP C  1  22  ? -21.568 -3.188  8.231  1.00 70.63  ? 35  ASP C OD1 1 
ATOM   5389 O  OD2 . ASP C  1  22  ? -20.911 -2.481  6.269  1.00 79.06  ? 35  ASP C OD2 1 
ATOM   5390 N  N   . ALA C  1  23  ? -24.979 -3.878  8.413  1.00 58.91  ? 36  ALA C N   1 
ATOM   5391 C  CA  . ALA C  1  23  ? -25.624 -4.918  9.198  1.00 64.09  ? 36  ALA C CA  1 
ATOM   5392 C  C   . ALA C  1  23  ? -24.596 -5.754  9.953  1.00 61.53  ? 36  ALA C C   1 
ATOM   5393 O  O   . ALA C  1  23  ? -24.907 -6.287  11.017 1.00 65.20  ? 36  ALA C O   1 
ATOM   5394 C  CB  . ALA C  1  23  ? -26.481 -5.783  8.297  1.00 61.95  ? 36  ALA C CB  1 
ATOM   5395 N  N   . ASP C  1  24  ? -23.386 -5.862  9.387  1.00 62.74  ? 37  ASP C N   1 
ATOM   5396 C  CA  . ASP C  1  24  ? -22.311 -6.641  9.982  1.00 62.35  ? 37  ASP C CA  1 
ATOM   5397 C  C   . ASP C  1  24  ? -21.595 -5.837  11.078 1.00 51.99  ? 37  ASP C C   1 
ATOM   5398 O  O   . ASP C  1  24  ? -20.821 -6.405  11.831 1.00 51.07  ? 37  ASP C O   1 
ATOM   5399 C  CB  . ASP C  1  24  ? -21.324 -7.115  8.922  1.00 66.08  ? 37  ASP C CB  1 
ATOM   5400 C  CG  . ASP C  1  24  ? -21.894 -7.940  7.786  1.00 68.38  ? 37  ASP C CG  1 
ATOM   5401 O  OD1 . ASP C  1  24  ? -22.465 -8.991  8.096  1.00 71.20  ? 37  ASP C OD1 1 
ATOM   5402 O  OD2 . ASP C  1  24  ? -21.738 -7.525  6.614  1.00 82.30  ? 37  ASP C OD2 1 
ATOM   5403 N  N   . HIS C  1  25  ? -21.856 -4.523  11.161 1.00 46.85  ? 38  HIS C N   1 
ATOM   5404 C  CA  . HIS C  1  25  ? -21.201 -3.640  12.110 1.00 44.31  ? 38  HIS C CA  1 
ATOM   5405 C  C   . HIS C  1  25  ? -22.237 -2.810  12.880 1.00 42.05  ? 38  HIS C C   1 
ATOM   5406 O  O   . HIS C  1  25  ? -22.196 -1.573  12.863 1.00 38.17  ? 38  HIS C O   1 
ATOM   5407 C  CB  . HIS C  1  25  ? -20.182 -2.761  11.373 1.00 46.30  ? 38  HIS C CB  1 
ATOM   5408 C  CG  . HIS C  1  25  ? -19.087 -3.547  10.735 1.00 47.18  ? 38  HIS C CG  1 
ATOM   5409 N  ND1 . HIS C  1  25  ? -19.048 -3.873  9.396  1.00 50.38  ? 38  HIS C ND1 1 
ATOM   5410 C  CD2 . HIS C  1  25  ? -17.977 -4.061  11.279 1.00 47.03  ? 38  HIS C CD2 1 
ATOM   5411 C  CE1 . HIS C  1  25  ? -17.954 -4.581  9.155  1.00 50.76  ? 38  HIS C CE1 1 
ATOM   5412 N  NE2 . HIS C  1  25  ? -17.284 -4.700  10.284 1.00 47.15  ? 38  HIS C NE2 1 
ATOM   5413 N  N   . PRO C  1  26  ? -23.178 -3.452  13.618 1.00 43.13  ? 39  PRO C N   1 
ATOM   5414 C  CA  . PRO C  1  26  ? -24.139 -2.714  14.447 1.00 43.74  ? 39  PRO C CA  1 
ATOM   5415 C  C   . PRO C  1  26  ? -23.519 -2.098  15.704 1.00 44.84  ? 39  PRO C C   1 
ATOM   5416 O  O   . PRO C  1  26  ? -22.656 -2.715  16.325 1.00 45.85  ? 39  PRO C O   1 
ATOM   5417 C  CB  . PRO C  1  26  ? -25.144 -3.827  14.810 1.00 43.77  ? 39  PRO C CB  1 
ATOM   5418 C  CG  . PRO C  1  26  ? -24.314 -5.086  14.884 1.00 43.17  ? 39  PRO C CG  1 
ATOM   5419 C  CD  . PRO C  1  26  ? -23.310 -4.915  13.749 1.00 43.62  ? 39  PRO C CD  1 
ATOM   5420 N  N   . TRP C  1  27  ? -23.963 -0.889  16.078 1.00 45.68  ? 40  TRP C N   1 
ATOM   5421 C  CA  . TRP C  1  27  ? -23.699 -0.355  17.406 1.00 48.72  ? 40  TRP C CA  1 
ATOM   5422 C  C   . TRP C  1  27  ? -24.293 -1.305  18.447 1.00 50.26  ? 40  TRP C C   1 
ATOM   5423 O  O   . TRP C  1  27  ? -25.407 -1.784  18.268 1.00 58.06  ? 40  TRP C O   1 
ATOM   5424 C  CB  . TRP C  1  27  ? -24.266 1.062   17.555 1.00 49.45  ? 40  TRP C CB  1 
ATOM   5425 C  CG  . TRP C  1  27  ? -23.954 1.717   18.875 1.00 58.79  ? 40  TRP C CG  1 
ATOM   5426 C  CD1 . TRP C  1  27  ? -22.888 2.511   19.155 1.00 59.36  ? 40  TRP C CD1 1 
ATOM   5427 C  CD2 . TRP C  1  27  ? -24.738 1.655   20.088 1.00 68.72  ? 40  TRP C CD2 1 
ATOM   5428 N  NE1 . TRP C  1  27  ? -22.944 2.951   20.452 1.00 63.62  ? 40  TRP C NE1 1 
ATOM   5429 C  CE2 . TRP C  1  27  ? -24.064 2.441   21.053 1.00 68.16  ? 40  TRP C CE2 1 
ATOM   5430 C  CE3 . TRP C  1  27  ? -25.927 1.012   20.460 1.00 68.23  ? 40  TRP C CE3 1 
ATOM   5431 C  CZ2 . TRP C  1  27  ? -24.541 2.603   22.354 1.00 59.63  ? 40  TRP C CZ2 1 
ATOM   5432 C  CZ3 . TRP C  1  27  ? -26.392 1.172   21.748 1.00 64.98  ? 40  TRP C CZ3 1 
ATOM   5433 C  CH2 . TRP C  1  27  ? -25.713 1.962   22.678 1.00 64.00  ? 40  TRP C CH2 1 
ATOM   5434 N  N   . GLN C  1  28  ? -23.521 -1.603  19.499 1.00 47.77  ? 41  GLN C N   1 
ATOM   5435 C  CA  . GLN C  1  28  ? -24.002 -2.329  20.667 1.00 46.50  ? 41  GLN C CA  1 
ATOM   5436 C  C   . GLN C  1  28  ? -23.545 -1.588  21.920 1.00 51.10  ? 41  GLN C C   1 
ATOM   5437 O  O   . GLN C  1  28  ? -22.501 -0.939  21.911 1.00 46.84  ? 41  GLN C O   1 
ATOM   5438 C  CB  . GLN C  1  28  ? -23.523 -3.777  20.670 1.00 45.40  ? 41  GLN C CB  1 
ATOM   5439 C  CG  . GLN C  1  28  ? -24.030 -4.589  19.484 1.00 46.83  ? 41  GLN C CG  1 
ATOM   5440 C  CD  . GLN C  1  28  ? -23.514 -6.010  19.463 1.00 51.31  ? 41  GLN C CD  1 
ATOM   5441 O  OE1 . GLN C  1  28  ? -22.701 -6.413  20.301 1.00 60.18  ? 41  GLN C OE1 1 
ATOM   5442 N  NE2 . GLN C  1  28  ? -23.968 -6.776  18.479 1.00 54.56  ? 41  GLN C NE2 1 
ATOM   5443 N  N   . PRO C  1  29  ? -24.330 -1.616  23.024 1.00 59.46  ? 42  PRO C N   1 
ATOM   5444 C  CA  . PRO C  1  29  ? -23.905 -0.980  24.275 1.00 53.46  ? 42  PRO C CA  1 
ATOM   5445 C  C   . PRO C  1  29  ? -22.723 -1.699  24.914 1.00 45.67  ? 42  PRO C C   1 
ATOM   5446 O  O   . PRO C  1  29  ? -22.469 -2.876  24.641 1.00 42.02  ? 42  PRO C O   1 
ATOM   5447 C  CB  . PRO C  1  29  ? -25.175 -1.023  25.148 1.00 55.59  ? 42  PRO C CB  1 
ATOM   5448 C  CG  . PRO C  1  29  ? -25.938 -2.219  24.622 1.00 60.55  ? 42  PRO C CG  1 
ATOM   5449 C  CD  . PRO C  1  29  ? -25.656 -2.252  23.125 1.00 56.03  ? 42  PRO C CD  1 
ATOM   5450 N  N   . LEU C  1  30  ? -22.008 -0.968  25.776 1.00 45.98  ? 43  LEU C N   1 
ATOM   5451 C  CA  . LEU C  1  30  ? -20.887 -1.527  26.517 1.00 47.33  ? 43  LEU C CA  1 
ATOM   5452 C  C   . LEU C  1  30  ? -21.383 -2.616  27.461 1.00 45.22  ? 43  LEU C C   1 
ATOM   5453 O  O   . LEU C  1  30  ? -22.425 -2.449  28.102 1.00 47.62  ? 43  LEU C O   1 
ATOM   5454 C  CB  . LEU C  1  30  ? -20.199 -0.393  27.276 1.00 46.82  ? 43  LEU C CB  1 
ATOM   5455 C  CG  . LEU C  1  30  ? -19.597 0.722   26.415 1.00 50.14  ? 43  LEU C CG  1 
ATOM   5456 C  CD1 . LEU C  1  30  ? -18.968 1.792   27.259 1.00 50.07  ? 43  LEU C CD1 1 
ATOM   5457 C  CD2 . LEU C  1  30  ? -18.591 0.131   25.435 1.00 50.65  ? 43  LEU C CD2 1 
ATOM   5458 N  N   . ARG C  1  31  ? -20.630 -3.722  27.508 1.00 45.23  ? 44  ARG C N   1 
ATOM   5459 C  CA  . ARG C  1  31  ? -20.772 -4.740  28.533 1.00 46.90  ? 44  ARG C CA  1 
ATOM   5460 C  C   . ARG C  1  31  ? -19.717 -4.481  29.607 1.00 53.18  ? 44  ARG C C   1 
ATOM   5461 O  O   . ARG C  1  31  ? -18.732 -3.792  29.348 1.00 52.59  ? 44  ARG C O   1 
ATOM   5462 C  CB  . ARG C  1  31  ? -20.551 -6.147  27.968 1.00 47.35  ? 44  ARG C CB  1 
ATOM   5463 C  CG  . ARG C  1  31  ? -21.320 -6.500  26.705 1.00 51.65  ? 44  ARG C CG  1 
ATOM   5464 C  CD  . ARG C  1  31  ? -20.636 -7.600  25.922 1.00 58.44  ? 44  ARG C CD  1 
ATOM   5465 N  NE  . ARG C  1  31  ? -19.314 -7.171  25.443 1.00 70.71  ? 44  ARG C NE  1 
ATOM   5466 C  CZ  . ARG C  1  31  ? -18.438 -7.909  24.744 1.00 70.90  ? 44  ARG C CZ  1 
ATOM   5467 N  NH1 . ARG C  1  31  ? -18.783 -9.106  24.297 1.00 72.15  ? 44  ARG C NH1 1 
ATOM   5468 N  NH2 . ARG C  1  31  ? -17.216 -7.447  24.492 1.00 64.58  ? 44  ARG C NH2 1 
ATOM   5469 N  N   . GLU C  1  32  ? -19.929 -5.048  30.803 1.00 52.76  ? 45  GLU C N   1 
ATOM   5470 C  CA  . GLU C  1  32  ? -18.930 -5.051  31.861 1.00 55.06  ? 45  GLU C CA  1 
ATOM   5471 C  C   . GLU C  1  32  ? -17.601 -5.604  31.346 1.00 50.30  ? 45  GLU C C   1 
ATOM   5472 O  O   . GLU C  1  32  ? -17.594 -6.697  30.794 1.00 45.59  ? 45  GLU C O   1 
ATOM   5473 C  CB  . GLU C  1  32  ? -19.396 -5.947  33.017 1.00 61.62  ? 45  GLU C CB  1 
ATOM   5474 C  CG  . GLU C  1  32  ? -19.795 -5.189  34.281 1.00 66.06  ? 45  GLU C CG  1 
ATOM   5475 C  CD  . GLU C  1  32  ? -18.665 -4.464  34.978 1.00 60.95  ? 45  GLU C CD  1 
ATOM   5476 O  OE1 . GLU C  1  32  ? -17.616 -5.111  35.108 1.00 64.23  ? 45  GLU C OE1 1 
ATOM   5477 O  OE2 . GLU C  1  32  ? -18.842 -3.301  35.419 1.00 65.13  ? 45  GLU C OE2 1 
ATOM   5478 N  N   . GLY C  1  33  ? -16.498 -4.858  31.543 1.00 49.15  ? 46  GLY C N   1 
ATOM   5479 C  CA  . GLY C  1  33  ? -15.181 -5.318  31.119 1.00 53.82  ? 46  GLY C CA  1 
ATOM   5480 C  C   . GLY C  1  33  ? -14.688 -4.650  29.833 1.00 54.00  ? 46  GLY C C   1 
ATOM   5481 O  O   . GLY C  1  33  ? -13.487 -4.637  29.559 1.00 70.40  ? 46  GLY C O   1 
ATOM   5482 N  N   . ASP C  1  34  ? -15.614 -4.085  29.054 1.00 51.07  ? 47  ASP C N   1 
ATOM   5483 C  CA  . ASP C  1  34  ? -15.285 -3.423  27.798 1.00 49.58  ? 47  ASP C CA  1 
ATOM   5484 C  C   . ASP C  1  34  ? -14.573 -2.112  28.102 1.00 48.50  ? 47  ASP C C   1 
ATOM   5485 O  O   . ASP C  1  34  ? -15.000 -1.379  28.982 1.00 46.70  ? 47  ASP C O   1 
ATOM   5486 C  CB  . ASP C  1  34  ? -16.530 -3.149  26.963 1.00 45.59  ? 47  ASP C CB  1 
ATOM   5487 C  CG  . ASP C  1  34  ? -17.217 -4.368  26.372 1.00 46.22  ? 47  ASP C CG  1 
ATOM   5488 O  OD1 . ASP C  1  34  ? -16.612 -5.468  26.421 1.00 46.27  ? 47  ASP C OD1 1 
ATOM   5489 O  OD2 . ASP C  1  34  ? -18.347 -4.215  25.866 1.00 48.26  ? 47  ASP C OD2 1 
ATOM   5490 N  N   . ILE C  1  35  ? -13.523 -1.811  27.334 1.00 47.82  ? 48  ILE C N   1 
ATOM   5491 C  CA  . ILE C  1  35  ? -12.703 -0.632  27.565 1.00 46.13  ? 48  ILE C CA  1 
ATOM   5492 C  C   . ILE C  1  35  ? -12.942 0.388   26.453 1.00 43.66  ? 48  ILE C C   1 
ATOM   5493 O  O   . ILE C  1  35  ? -12.965 0.033   25.280 1.00 43.03  ? 48  ILE C O   1 
ATOM   5494 C  CB  . ILE C  1  35  ? -11.228 -1.047  27.677 1.00 49.32  ? 48  ILE C CB  1 
ATOM   5495 C  CG1 . ILE C  1  35  ? -11.026 -1.915  28.937 1.00 47.46  ? 48  ILE C CG1 1 
ATOM   5496 C  CG2 . ILE C  1  35  ? -10.300 0.175   27.625 1.00 49.31  ? 48  ILE C CG2 1 
ATOM   5497 C  CD1 . ILE C  1  35  ? -9.678  -2.626  29.000 1.00 57.64  ? 48  ILE C CD1 1 
ATOM   5498 N  N   . ARG C  1  36  ? -13.135 1.651   26.858 1.00 41.22  ? 49  ARG C N   1 
ATOM   5499 C  CA  . ARG C  1  36  ? -13.181 2.802   25.973 1.00 40.30  ? 49  ARG C CA  1 
ATOM   5500 C  C   . ARG C  1  36  ? -12.240 3.848   26.569 1.00 40.80  ? 49  ARG C C   1 
ATOM   5501 O  O   . ARG C  1  36  ? -11.855 3.727   27.724 1.00 41.68  ? 49  ARG C O   1 
ATOM   5502 C  CB  . ARG C  1  36  ? -14.628 3.290   25.815 1.00 41.49  ? 49  ARG C CB  1 
ATOM   5503 C  CG  . ARG C  1  36  ? -15.579 2.275   25.193 1.00 41.79  ? 49  ARG C CG  1 
ATOM   5504 C  CD  . ARG C  1  36  ? -15.284 1.993   23.713 1.00 41.62  ? 49  ARG C CD  1 
ATOM   5505 N  NE  . ARG C  1  36  ? -16.189 1.018   23.090 1.00 38.15  ? 49  ARG C NE  1 
ATOM   5506 C  CZ  . ARG C  1  36  ? -16.096 -0.298  23.195 1.00 38.53  ? 49  ARG C CZ  1 
ATOM   5507 N  NH1 . ARG C  1  36  ? -15.111 -0.858  23.870 1.00 39.92  ? 49  ARG C NH1 1 
ATOM   5508 N  NH2 . ARG C  1  36  ? -16.994 -1.067  22.615 1.00 42.57  ? 49  ARG C NH2 1 
ATOM   5509 N  N   . GLY C  1  37  ? -11.860 4.864   25.789 1.00 38.78  ? 50  GLY C N   1 
ATOM   5510 C  CA  . GLY C  1  37  ? -10.793 5.759   26.203 1.00 38.94  ? 50  GLY C CA  1 
ATOM   5511 C  C   . GLY C  1  37  ? -10.964 7.152   25.612 1.00 38.80  ? 50  GLY C C   1 
ATOM   5512 O  O   . GLY C  1  37  ? -12.077 7.593   25.351 1.00 36.63  ? 50  GLY C O   1 
ATOM   5513 N  N   . PRO C  1  38  ? -9.857  7.888   25.395 1.00 38.90  ? 51  PRO C N   1 
ATOM   5514 C  CA  . PRO C  1  38  ? -9.934  9.280   24.949 1.00 38.42  ? 51  PRO C CA  1 
ATOM   5515 C  C   . PRO C  1  38  ? -10.132 9.522   23.453 1.00 38.78  ? 51  PRO C C   1 
ATOM   5516 O  O   . PRO C  1  38  ? -10.340 10.672  23.053 1.00 40.50  ? 51  PRO C O   1 
ATOM   5517 C  CB  . PRO C  1  38  ? -8.561  9.786   25.419 1.00 38.50  ? 51  PRO C CB  1 
ATOM   5518 C  CG  . PRO C  1  38  ? -7.653  8.614   25.172 1.00 40.52  ? 51  PRO C CG  1 
ATOM   5519 C  CD  . PRO C  1  38  ? -8.479  7.405   25.557 1.00 38.89  ? 51  PRO C CD  1 
ATOM   5520 N  N   . CYS C  1  39  ? -10.041 8.460   22.639 1.00 40.42  ? 52  CYS C N   1 
ATOM   5521 C  CA  . CYS C  1  39  ? -10.196 8.579   21.190 1.00 40.37  ? 52  CYS C CA  1 
ATOM   5522 C  C   . CYS C  1  39  ? -11.619 8.236   20.763 1.00 36.63  ? 52  CYS C C   1 
ATOM   5523 O  O   . CYS C  1  39  ? -12.040 7.080   20.827 1.00 40.34  ? 52  CYS C O   1 
ATOM   5524 C  CB  . CYS C  1  39  ? -9.259  7.651   20.421 1.00 39.96  ? 52  CYS C CB  1 
ATOM   5525 S  SG  . CYS C  1  39  ? -9.298  7.923   18.631 1.00 41.04  ? 52  CYS C SG  1 
ATOM   5526 N  N   . PRO C  1  40  ? -12.403 9.217   20.281 1.00 39.67  ? 53  PRO C N   1 
ATOM   5527 C  CA  . PRO C  1  40  ? -13.750 8.941   19.777 1.00 40.58  ? 53  PRO C CA  1 
ATOM   5528 C  C   . PRO C  1  40  ? -13.773 8.065   18.519 1.00 42.57  ? 53  PRO C C   1 
ATOM   5529 O  O   . PRO C  1  40  ? -14.731 7.324   18.302 1.00 42.97  ? 53  PRO C O   1 
ATOM   5530 C  CB  . PRO C  1  40  ? -14.337 10.345  19.550 1.00 41.65  ? 53  PRO C CB  1 
ATOM   5531 C  CG  . PRO C  1  40  ? -13.140 11.240  19.345 1.00 41.71  ? 53  PRO C CG  1 
ATOM   5532 C  CD  . PRO C  1  40  ? -12.024 10.633  20.180 1.00 42.80  ? 53  PRO C CD  1 
ATOM   5533 N  N   . GLY C  1  41  ? -12.701 8.128   17.709 1.00 40.17  ? 54  GLY C N   1 
ATOM   5534 C  CA  . GLY C  1  41  ? -12.583 7.290   16.525 1.00 39.90  ? 54  GLY C CA  1 
ATOM   5535 C  C   . GLY C  1  41  ? -12.523 5.804   16.869 1.00 39.78  ? 54  GLY C C   1 
ATOM   5536 O  O   . GLY C  1  41  ? -13.342 5.010   16.405 1.00 45.38  ? 54  GLY C O   1 
ATOM   5537 N  N   . LEU C  1  42  ? -11.560 5.443   17.713 1.00 39.08  ? 55  LEU C N   1 
ATOM   5538 C  CA  . LEU C  1  42  ? -11.387 4.059   18.121 1.00 40.66  ? 55  LEU C CA  1 
ATOM   5539 C  C   . LEU C  1  42  ? -12.574 3.584   18.962 1.00 38.77  ? 55  LEU C C   1 
ATOM   5540 O  O   . LEU C  1  42  ? -12.956 2.422   18.871 1.00 37.27  ? 55  LEU C O   1 
ATOM   5541 C  CB  . LEU C  1  42  ? -10.065 3.936   18.879 1.00 43.76  ? 55  LEU C CB  1 
ATOM   5542 C  CG  . LEU C  1  42  ? -8.803  4.282   18.080 1.00 45.87  ? 55  LEU C CG  1 
ATOM   5543 C  CD1 . LEU C  1  42  ? -7.601  4.238   19.000 1.00 47.29  ? 55  LEU C CD1 1 
ATOM   5544 C  CD2 . LEU C  1  42  ? -8.621  3.342   16.898 1.00 43.40  ? 55  LEU C CD2 1 
ATOM   5545 N  N   . ASN C  1  43  ? -13.138 4.474   19.786 1.00 39.00  ? 56  ASN C N   1 
ATOM   5546 C  CA  . ASN C  1  43  ? -14.309 4.149   20.596 1.00 41.67  ? 56  ASN C CA  1 
ATOM   5547 C  C   . ASN C  1  43  ? -15.474 3.728   19.696 1.00 41.13  ? 56  ASN C C   1 
ATOM   5548 O  O   . ASN C  1  43  ? -16.102 2.693   19.938 1.00 41.80  ? 56  ASN C O   1 
ATOM   5549 C  CB  . ASN C  1  43  ? -14.727 5.313   21.496 1.00 40.55  ? 56  ASN C CB  1 
ATOM   5550 C  CG  . ASN C  1  43  ? -13.799 5.551   22.670 1.00 39.74  ? 56  ASN C CG  1 
ATOM   5551 O  OD1 . ASN C  1  43  ? -12.986 4.688   23.047 1.00 34.56  ? 56  ASN C OD1 1 
ATOM   5552 N  ND2 . ASN C  1  43  ? -13.937 6.719   23.287 1.00 39.37  ? 56  ASN C ND2 1 
ATOM   5553 N  N   . THR C  1  44  ? -15.734 4.524   18.643 1.00 38.99  ? 57  THR C N   1 
ATOM   5554 C  CA  . THR C  1  44  ? -16.812 4.232   17.702 1.00 37.55  ? 57  THR C CA  1 
ATOM   5555 C  C   . THR C  1  44  ? -16.548 2.915   16.972 1.00 39.98  ? 57  THR C C   1 
ATOM   5556 O  O   . THR C  1  44  ? -17.469 2.111   16.801 1.00 39.92  ? 57  THR C O   1 
ATOM   5557 C  CB  . THR C  1  44  ? -17.010 5.401   16.741 1.00 42.32  ? 57  THR C CB  1 
ATOM   5558 O  OG1 . THR C  1  44  ? -17.260 6.523   17.584 1.00 38.94  ? 57  THR C OG1 1 
ATOM   5559 C  CG2 . THR C  1  44  ? -18.183 5.223   15.783 1.00 42.60  ? 57  THR C CG2 1 
ATOM   5560 N  N   . LEU C  1  45  ? -15.290 2.673   16.575 1.00 37.04  ? 58  LEU C N   1 
ATOM   5561 C  CA  . LEU C  1  45  ? -14.954 1.465   15.835 1.00 35.62  ? 58  LEU C CA  1 
ATOM   5562 C  C   . LEU C  1  45  ? -15.178 0.212   16.676 1.00 36.08  ? 58  LEU C C   1 
ATOM   5563 O  O   . LEU C  1  45  ? -15.617 -0.819  16.156 1.00 40.03  ? 58  LEU C O   1 
ATOM   5564 C  CB  . LEU C  1  45  ? -13.518 1.566   15.326 1.00 38.22  ? 58  LEU C CB  1 
ATOM   5565 C  CG  . LEU C  1  45  ? -13.288 2.603   14.223 1.00 41.38  ? 58  LEU C CG  1 
ATOM   5566 C  CD1 . LEU C  1  45  ? -11.815 2.876   14.027 1.00 39.70  ? 58  LEU C CD1 1 
ATOM   5567 C  CD2 . LEU C  1  45  ? -13.929 2.168   12.904 1.00 42.14  ? 58  LEU C CD2 1 
ATOM   5568 N  N   . ALA C  1  46  ? -14.848 0.291   17.971 1.00 38.95  ? 59  ALA C N   1 
ATOM   5569 C  CA  . ALA C  1  46  ? -15.056 -0.819  18.893 1.00 40.21  ? 59  ALA C CA  1 
ATOM   5570 C  C   . ALA C  1  46  ? -16.547 -1.054  19.145 1.00 37.02  ? 59  ALA C C   1 
ATOM   5571 O  O   . ALA C  1  46  ? -17.009 -2.192  19.179 1.00 34.73  ? 59  ALA C O   1 
ATOM   5572 C  CB  . ALA C  1  46  ? -14.318 -0.539  20.186 1.00 41.34  ? 59  ALA C CB  1 
ATOM   5573 N  N   . SER C  1  47  ? -17.305 0.035   19.281 1.00 35.95  ? 60  SER C N   1 
ATOM   5574 C  CA  . SER C  1  47  ? -18.719 -0.077  19.602 1.00 42.52  ? 60  SER C CA  1 
ATOM   5575 C  C   . SER C  1  47  ? -19.539 -0.510  18.383 1.00 44.71  ? 60  SER C C   1 
ATOM   5576 O  O   . SER C  1  47  ? -20.695 -0.882  18.547 1.00 42.04  ? 60  SER C O   1 
ATOM   5577 C  CB  . SER C  1  47  ? -19.235 1.202   20.231 1.00 40.38  ? 60  SER C CB  1 
ATOM   5578 O  OG  . SER C  1  47  ? -18.830 1.267   21.596 1.00 42.72  ? 60  SER C OG  1 
ATOM   5579 N  N   . HIS C  1  48  ? -18.923 -0.523  17.185 1.00 43.70  ? 61  HIS C N   1 
ATOM   5580 C  CA  . HIS C  1  48  ? -19.556 -1.064  15.985 1.00 42.23  ? 61  HIS C CA  1 
ATOM   5581 C  C   . HIS C  1  48  ? -18.924 -2.382  15.535 1.00 40.12  ? 61  HIS C C   1 
ATOM   5582 O  O   . HIS C  1  48  ? -19.334 -2.936  14.518 1.00 39.47  ? 61  HIS C O   1 
ATOM   5583 C  CB  . HIS C  1  48  ? -19.518 -0.052  14.838 1.00 40.18  ? 61  HIS C CB  1 
ATOM   5584 C  CG  . HIS C  1  48  ? -20.553 1.025   14.926 1.00 39.78  ? 61  HIS C CG  1 
ATOM   5585 N  ND1 . HIS C  1  48  ? -21.764 0.928   14.262 1.00 39.15  ? 61  HIS C ND1 1 
ATOM   5586 C  CD2 . HIS C  1  48  ? -20.555 2.216   15.549 1.00 36.51  ? 61  HIS C CD2 1 
ATOM   5587 C  CE1 . HIS C  1  48  ? -22.465 2.041   14.495 1.00 38.19  ? 61  HIS C CE1 1 
ATOM   5588 N  NE2 . HIS C  1  48  ? -21.748 2.838   15.268 1.00 34.89  ? 61  HIS C NE2 1 
ATOM   5589 N  N   . GLY C  1  49  ? -17.911 -2.874  16.255 1.00 38.97  ? 62  GLY C N   1 
ATOM   5590 C  CA  . GLY C  1  49  ? -17.310 -4.157  15.924 1.00 39.91  ? 62  GLY C CA  1 
ATOM   5591 C  C   . GLY C  1  49  ? -16.298 -4.108  14.769 1.00 36.56  ? 62  GLY C C   1 
ATOM   5592 O  O   . GLY C  1  49  ? -15.904 -5.154  14.282 1.00 37.91  ? 62  GLY C O   1 
ATOM   5593 N  N   . TYR C  1  50  ? -15.853 -2.920  14.339 1.00 36.63  ? 63  TYR C N   1 
ATOM   5594 C  CA  . TYR C  1  50  ? -14.684 -2.810  13.474 1.00 38.33  ? 63  TYR C CA  1 
ATOM   5595 C  C   . TYR C  1  50  ? -13.442 -3.241  14.253 1.00 39.63  ? 63  TYR C C   1 
ATOM   5596 O  O   . TYR C  1  50  ? -12.556 -3.851  13.680 1.00 39.91  ? 63  TYR C O   1 
ATOM   5597 C  CB  . TYR C  1  50  ? -14.527 -1.410  12.871 1.00 38.10  ? 63  TYR C CB  1 
ATOM   5598 C  CG  . TYR C  1  50  ? -15.464 -1.194  11.689 1.00 40.94  ? 63  TYR C CG  1 
ATOM   5599 C  CD1 . TYR C  1  50  ? -15.134 -1.664  10.415 1.00 42.20  ? 63  TYR C CD1 1 
ATOM   5600 C  CD2 . TYR C  1  50  ? -16.692 -0.565  11.850 1.00 39.74  ? 63  TYR C CD2 1 
ATOM   5601 C  CE1 . TYR C  1  50  ? -15.993 -1.503  9.339  1.00 40.72  ? 63  TYR C CE1 1 
ATOM   5602 C  CE2 . TYR C  1  50  ? -17.553 -0.386  10.778 1.00 41.94  ? 63  TYR C CE2 1 
ATOM   5603 C  CZ  . TYR C  1  50  ? -17.206 -0.858  9.523  1.00 43.89  ? 63  TYR C CZ  1 
ATOM   5604 O  OH  . TYR C  1  50  ? -18.068 -0.689  8.484  1.00 46.58  ? 63  TYR C OH  1 
ATOM   5605 N  N   . LEU C  1  51  ? -13.392 -2.895  15.546 1.00 42.50  ? 64  LEU C N   1 
ATOM   5606 C  CA  . LEU C  1  51  ? -12.408 -3.401  16.491 1.00 46.33  ? 64  LEU C CA  1 
ATOM   5607 C  C   . LEU C  1  51  ? -13.094 -4.394  17.418 1.00 47.32  ? 64  LEU C C   1 
ATOM   5608 O  O   . LEU C  1  51  ? -14.316 -4.400  17.512 1.00 48.11  ? 64  LEU C O   1 
ATOM   5609 C  CB  . LEU C  1  51  ? -11.809 -2.269  17.325 1.00 46.44  ? 64  LEU C CB  1 
ATOM   5610 C  CG  . LEU C  1  51  ? -10.851 -1.325  16.602 1.00 47.69  ? 64  LEU C CG  1 
ATOM   5611 C  CD1 . LEU C  1  51  ? -10.579 -0.131  17.482 1.00 50.52  ? 64  LEU C CD1 1 
ATOM   5612 C  CD2 . LEU C  1  51  ? -9.578  -2.057  16.241 1.00 49.29  ? 64  LEU C CD2 1 
ATOM   5613 N  N   . PRO C  1  52  ? -12.324 -5.229  18.156 1.00 48.11  ? 65  PRO C N   1 
ATOM   5614 C  CA  . PRO C  1  52  ? -12.882 -6.013  19.257 1.00 44.88  ? 65  PRO C CA  1 
ATOM   5615 C  C   . PRO C  1  52  ? -13.673 -5.133  20.216 1.00 48.14  ? 65  PRO C C   1 
ATOM   5616 O  O   . PRO C  1  52  ? -13.230 -4.039  20.574 1.00 42.59  ? 65  PRO C O   1 
ATOM   5617 C  CB  . PRO C  1  52  ? -11.653 -6.669  19.884 1.00 45.21  ? 65  PRO C CB  1 
ATOM   5618 C  CG  . PRO C  1  52  ? -10.679 -6.784  18.725 1.00 44.41  ? 65  PRO C CG  1 
ATOM   5619 C  CD  . PRO C  1  52  ? -10.883 -5.474  17.971 1.00 45.27  ? 65  PRO C CD  1 
ATOM   5620 N  N   . ARG C  1  53  ? -14.865 -5.607  20.607 1.00 46.74  ? 66  ARG C N   1 
ATOM   5621 C  CA  . ARG C  1  53  ? -15.814 -4.774  21.328 1.00 46.07  ? 66  ARG C CA  1 
ATOM   5622 C  C   . ARG C  1  53  ? -15.344 -4.524  22.767 1.00 45.10  ? 66  ARG C C   1 
ATOM   5623 O  O   . ARG C  1  53  ? -15.830 -3.592  23.417 1.00 38.91  ? 66  ARG C O   1 
ATOM   5624 C  CB  . ARG C  1  53  ? -17.217 -5.391  21.270 1.00 50.36  ? 66  ARG C CB  1 
ATOM   5625 C  CG  . ARG C  1  53  ? -17.818 -5.427  19.870 1.00 50.84  ? 66  ARG C CG  1 
ATOM   5626 C  CD  . ARG C  1  53  ? -19.291 -5.824  19.866 1.00 48.06  ? 66  ARG C CD  1 
ATOM   5627 N  NE  . ARG C  1  53  ? -19.861 -5.832  18.511 1.00 43.25  ? 66  ARG C NE  1 
ATOM   5628 C  CZ  . ARG C  1  53  ? -20.480 -4.819  17.924 1.00 40.37  ? 66  ARG C CZ  1 
ATOM   5629 N  NH1 . ARG C  1  53  ? -20.612 -3.651  18.540 1.00 42.52  ? 66  ARG C NH1 1 
ATOM   5630 N  NH2 . ARG C  1  53  ? -20.957 -4.960  16.699 1.00 44.35  ? 66  ARG C NH2 1 
ATOM   5631 N  N   . ASP C  1  54  ? -14.381 -5.326  23.244 1.00 43.16  ? 67  ASP C N   1 
ATOM   5632 C  CA  . ASP C  1  54  ? -13.808 -5.129  24.568 1.00 47.71  ? 67  ASP C CA  1 
ATOM   5633 C  C   . ASP C  1  54  ? -12.738 -4.034  24.575 1.00 44.65  ? 67  ASP C C   1 
ATOM   5634 O  O   . ASP C  1  54  ? -12.302 -3.643  25.646 1.00 44.78  ? 67  ASP C O   1 
ATOM   5635 C  CB  . ASP C  1  54  ? -13.294 -6.431  25.167 1.00 47.55  ? 67  ASP C CB  1 
ATOM   5636 C  CG  . ASP C  1  54  ? -12.118 -7.086  24.454 1.00 53.43  ? 67  ASP C CG  1 
ATOM   5637 O  OD1 . ASP C  1  54  ? -11.600 -6.496  23.452 1.00 57.77  ? 67  ASP C OD1 1 
ATOM   5638 O  OD2 . ASP C  1  54  ? -11.721 -8.178  24.927 1.00 54.36  ? 67  ASP C OD2 1 
ATOM   5639 N  N   . GLY C  1  55  ? -12.323 -3.523  23.411 1.00 42.63  ? 68  GLY C N   1 
ATOM   5640 C  CA  . GLY C  1  55  ? -11.459 -2.346  23.368 1.00 39.90  ? 68  GLY C CA  1 
ATOM   5641 C  C   . GLY C  1  55  ? -9.975  -2.677  23.571 1.00 37.95  ? 68  GLY C C   1 
ATOM   5642 O  O   . GLY C  1  55  ? -9.189  -1.793  23.924 1.00 40.01  ? 68  GLY C O   1 
ATOM   5643 N  N   . VAL C  1  56  ? -9.612  -3.942  23.312 1.00 35.57  ? 69  VAL C N   1 
ATOM   5644 C  CA  . VAL C  1  56  ? -8.231  -4.392  23.266 1.00 40.01  ? 69  VAL C CA  1 
ATOM   5645 C  C   . VAL C  1  56  ? -7.972  -5.039  21.911 1.00 39.83  ? 69  VAL C C   1 
ATOM   5646 O  O   . VAL C  1  56  ? -8.694  -5.964  21.547 1.00 40.46  ? 69  VAL C O   1 
ATOM   5647 C  CB  . VAL C  1  56  ? -7.957  -5.390  24.408 1.00 41.66  ? 69  VAL C CB  1 
ATOM   5648 C  CG1 . VAL C  1  56  ? -6.544  -5.959  24.360 1.00 45.13  ? 69  VAL C CG1 1 
ATOM   5649 C  CG2 . VAL C  1  56  ? -8.207  -4.761  25.769 1.00 42.42  ? 69  VAL C CG2 1 
ATOM   5650 N  N   . ALA C  1  57  ? -6.920  -4.591  21.205 1.00 41.86  ? 70  ALA C N   1 
ATOM   5651 C  CA  . ALA C  1  57  ? -6.666  -4.995  19.828 1.00 39.16  ? 70  ALA C CA  1 
ATOM   5652 C  C   . ALA C  1  57  ? -5.168  -5.050  19.526 1.00 39.85  ? 70  ALA C C   1 
ATOM   5653 O  O   . ALA C  1  57  ? -4.370  -4.451  20.243 1.00 38.82  ? 70  ALA C O   1 
ATOM   5654 C  CB  . ALA C  1  57  ? -7.351  -4.025  18.908 1.00 38.93  ? 70  ALA C CB  1 
ATOM   5655 N  N   . THR C  1  58  ? -4.814  -5.711  18.411 1.00 40.30  ? 71  THR C N   1 
ATOM   5656 C  CA  . THR C  1  58  ? -3.461  -5.662  17.887 1.00 37.36  ? 71  THR C CA  1 
ATOM   5657 C  C   . THR C  1  58  ? -3.299  -4.365  17.102 1.00 38.56  ? 71  THR C C   1 
ATOM   5658 O  O   . THR C  1  58  ? -4.284  -3.766  16.671 1.00 43.58  ? 71  THR C O   1 
ATOM   5659 C  CB  . THR C  1  58  ? -3.158  -6.869  17.008 1.00 37.67  ? 71  THR C CB  1 
ATOM   5660 O  OG1 . THR C  1  58  ? -3.913  -6.706  15.810 1.00 40.47  ? 71  THR C OG1 1 
ATOM   5661 C  CG2 . THR C  1  58  ? -3.459  -8.188  17.702 1.00 36.83  ? 71  THR C CG2 1 
ATOM   5662 N  N   . PRO C  1  59  ? -2.057  -3.873  16.911 1.00 42.14  ? 72  PRO C N   1 
ATOM   5663 C  CA  . PRO C  1  59  ? -1.818  -2.754  15.994 1.00 42.25  ? 72  PRO C CA  1 
ATOM   5664 C  C   . PRO C  1  59  ? -2.392  -2.963  14.594 1.00 34.59  ? 72  PRO C C   1 
ATOM   5665 O  O   . PRO C  1  59  ? -2.947  -2.032  14.013 1.00 35.35  ? 72  PRO C O   1 
ATOM   5666 C  CB  . PRO C  1  59  ? -0.276  -2.649  15.995 1.00 40.00  ? 72  PRO C CB  1 
ATOM   5667 C  CG  . PRO C  1  59  ? 0.119   -3.157  17.352 1.00 40.13  ? 72  PRO C CG  1 
ATOM   5668 C  CD  . PRO C  1  59  ? -0.832  -4.320  17.596 1.00 41.26  ? 72  PRO C CD  1 
ATOM   5669 N  N   . ALA C  1  60  ? -2.242  -4.178  14.058 1.00 35.48  ? 73  ALA C N   1 
ATOM   5670 C  CA  . ALA C  1  60  ? -2.722  -4.490  12.718 1.00 39.43  ? 73  ALA C CA  1 
ATOM   5671 C  C   . ALA C  1  60  ? -4.239  -4.339  12.655 1.00 38.32  ? 73  ALA C C   1 
ATOM   5672 O  O   . ALA C  1  60  ? -4.742  -3.772  11.688 1.00 38.57  ? 73  ALA C O   1 
ATOM   5673 C  CB  . ALA C  1  60  ? -2.283  -5.868  12.298 1.00 39.96  ? 73  ALA C CB  1 
ATOM   5674 N  N   . GLN C  1  61  ? -4.952  -4.779  13.704 1.00 37.99  ? 74  GLN C N   1 
ATOM   5675 C  CA  . GLN C  1  61  ? -6.403  -4.632  13.762 1.00 37.87  ? 74  GLN C CA  1 
ATOM   5676 C  C   . GLN C  1  61  ? -6.828  -3.163  13.783 1.00 38.47  ? 74  GLN C C   1 
ATOM   5677 O  O   . GLN C  1  61  ? -7.833  -2.797  13.170 1.00 42.86  ? 74  GLN C O   1 
ATOM   5678 C  CB  . GLN C  1  61  ? -6.977  -5.345  14.981 1.00 38.54  ? 74  GLN C CB  1 
ATOM   5679 C  CG  . GLN C  1  61  ? -6.988  -6.860  14.836 1.00 38.41  ? 74  GLN C CG  1 
ATOM   5680 C  CD  . GLN C  1  61  ? -7.465  -7.538  16.103 1.00 44.77  ? 74  GLN C CD  1 
ATOM   5681 O  OE1 . GLN C  1  61  ? -7.045  -7.213  17.222 1.00 47.73  ? 74  GLN C OE1 1 
ATOM   5682 N  NE2 . GLN C  1  61  ? -8.390  -8.468  15.933 1.00 50.67  ? 74  GLN C NE2 1 
ATOM   5683 N  N   . ILE C  1  62  ? -6.056  -2.320  14.478 1.00 38.02  ? 75  ILE C N   1 
ATOM   5684 C  CA  . ILE C  1  62  ? -6.380  -0.904  14.609 1.00 41.12  ? 75  ILE C CA  1 
ATOM   5685 C  C   . ILE C  1  62  ? -6.214  -0.185  13.268 1.00 39.71  ? 75  ILE C C   1 
ATOM   5686 O  O   . ILE C  1  62  ? -7.043  0.646   12.913 1.00 40.34  ? 75  ILE C O   1 
ATOM   5687 C  CB  . ILE C  1  62  ? -5.541  -0.271  15.735 1.00 40.70  ? 75  ILE C CB  1 
ATOM   5688 C  CG1 . ILE C  1  62  ? -5.961  -0.853  17.084 1.00 42.62  ? 75  ILE C CG1 1 
ATOM   5689 C  CG2 . ILE C  1  62  ? -5.638  1.254   15.723 1.00 37.27  ? 75  ILE C CG2 1 
ATOM   5690 C  CD1 . ILE C  1  62  ? -5.032  -0.528  18.239 1.00 45.71  ? 75  ILE C CD1 1 
ATOM   5691 N  N   . ILE C  1  63  ? -5.149  -0.516  12.529 1.00 38.59  ? 76  ILE C N   1 
ATOM   5692 C  CA  . ILE C  1  63  ? -4.916  0.085   11.227 1.00 39.57  ? 76  ILE C CA  1 
ATOM   5693 C  C   . ILE C  1  63  ? -6.030  -0.316  10.264 1.00 37.56  ? 76  ILE C C   1 
ATOM   5694 O  O   . ILE C  1  63  ? -6.567  0.558   9.598  1.00 35.04  ? 76  ILE C O   1 
ATOM   5695 C  CB  . ILE C  1  63  ? -3.508  -0.265  10.702 1.00 40.52  ? 76  ILE C CB  1 
ATOM   5696 C  CG1 . ILE C  1  63  ? -2.456  0.473   11.517 1.00 43.49  ? 76  ILE C CG1 1 
ATOM   5697 C  CG2 . ILE C  1  63  ? -3.351  0.040   9.207  1.00 39.23  ? 76  ILE C CG2 1 
ATOM   5698 C  CD1 . ILE C  1  63  ? -1.153  -0.273  11.642 1.00 43.34  ? 76  ILE C CD1 1 
ATOM   5699 N  N   . THR C  1  64  ? -6.382  -1.611  10.207 1.00 39.53  ? 77  THR C N   1 
ATOM   5700 C  CA  A THR C  1  64  ? -7.405  -2.070  9.284  0.50 43.01  ? 77  THR C CA  1 
ATOM   5701 C  CA  B THR C  1  64  ? -7.408  -2.075  9.285  0.50 44.49  ? 77  THR C CA  1 
ATOM   5702 C  C   . THR C  1  64  ? -8.727  -1.370  9.616  1.00 41.18  ? 77  THR C C   1 
ATOM   5703 O  O   . THR C  1  64  ? -9.391  -0.867  8.714  1.00 41.64  ? 77  THR C O   1 
ATOM   5704 C  CB  A THR C  1  64  ? -7.532  -3.596  9.310  0.50 44.79  ? 77  THR C CB  1 
ATOM   5705 C  CB  B THR C  1  64  ? -7.534  -3.603  9.290  0.50 50.47  ? 77  THR C CB  1 
ATOM   5706 O  OG1 A THR C  1  64  ? -7.832  -3.922  10.662 0.50 66.59  ? 77  THR C OG1 1 
ATOM   5707 O  OG1 B THR C  1  64  ? -8.554  -3.990  8.372  0.50 48.82  ? 77  THR C OG1 1 
ATOM   5708 C  CG2 A THR C  1  64  ? -6.264  -4.329  8.924  0.50 37.64  ? 77  THR C CG2 1 
ATOM   5709 C  CG2 B THR C  1  64  ? -8.067  -4.176  10.588 0.50 61.01  ? 77  THR C CG2 1 
ATOM   5710 N  N   . ALA C  1  65  ? -9.073  -1.282  10.916 1.00 37.33  ? 78  ALA C N   1 
ATOM   5711 C  CA  . ALA C  1  65  ? -10.339 -0.705  11.368 1.00 35.95  ? 78  ALA C CA  1 
ATOM   5712 C  C   . ALA C  1  65  ? -10.458 0.780   11.028 1.00 37.56  ? 78  ALA C C   1 
ATOM   5713 O  O   . ALA C  1  65  ? -11.511 1.228   10.561 1.00 36.40  ? 78  ALA C O   1 
ATOM   5714 C  CB  . ALA C  1  65  ? -10.526 -0.939  12.857 1.00 36.99  ? 78  ALA C CB  1 
ATOM   5715 N  N   . THR C  1  66  ? -9.389  1.550   11.265 1.00 38.80  ? 79  THR C N   1 
ATOM   5716 C  CA  . THR C  1  66  ? -9.403  2.976   10.951 1.00 37.93  ? 79  THR C CA  1 
ATOM   5717 C  C   . THR C  1  66  ? -9.532  3.201   9.443  1.00 34.13  ? 79  THR C C   1 
ATOM   5718 O  O   . THR C  1  66  ? -10.131 4.194   9.036  1.00 34.16  ? 79  THR C O   1 
ATOM   5719 C  CB  . THR C  1  66  ? -8.180  3.699   11.505 1.00 37.01  ? 79  THR C CB  1 
ATOM   5720 O  OG1 . THR C  1  66  ? -7.000  3.134   10.940 1.00 37.91  ? 79  THR C OG1 1 
ATOM   5721 C  CG2 . THR C  1  66  ? -8.139  3.625   13.018 1.00 38.58  ? 79  THR C CG2 1 
ATOM   5722 N  N   . GLN C  1  67  ? -8.958  2.301   8.636  1.00 33.21  ? 80  GLN C N   1 
ATOM   5723 C  CA  . GLN C  1  67  ? -9.053  2.393   7.180  1.00 40.11  ? 80  GLN C CA  1 
ATOM   5724 C  C   . GLN C  1  67  ? -10.456 2.005   6.695  1.00 41.11  ? 80  GLN C C   1 
ATOM   5725 O  O   . GLN C  1  67  ? -11.067 2.738   5.922  1.00 45.22  ? 80  GLN C O   1 
ATOM   5726 C  CB  . GLN C  1  67  ? -7.977  1.520   6.530  1.00 37.13  ? 80  GLN C CB  1 
ATOM   5727 C  CG  . GLN C  1  67  ? -6.569  2.042   6.783  1.00 41.48  ? 80  GLN C CG  1 
ATOM   5728 C  CD  . GLN C  1  67  ? -5.434  1.250   6.162  1.00 40.48  ? 80  GLN C CD  1 
ATOM   5729 O  OE1 . GLN C  1  67  ? -4.348  1.792   5.968  1.00 38.75  ? 80  GLN C OE1 1 
ATOM   5730 N  NE2 . GLN C  1  67  ? -5.640  -0.010  5.809  1.00 42.42  ? 80  GLN C NE2 1 
ATOM   5731 N  N   . GLU C  1  68  ? -10.952 0.850   7.157  1.00 39.18  ? 81  GLU C N   1 
ATOM   5732 C  CA  . GLU C  1  68  ? -12.237 0.331   6.737  1.00 42.71  ? 81  GLU C CA  1 
ATOM   5733 C  C   . GLU C  1  68  ? -13.362 1.263   7.177  1.00 43.07  ? 81  GLU C C   1 
ATOM   5734 O  O   . GLU C  1  68  ? -14.241 1.575   6.380  1.00 43.45  ? 81  GLU C O   1 
ATOM   5735 C  CB  . GLU C  1  68  ? -12.454 -1.080  7.286  1.00 47.25  ? 81  GLU C CB  1 
ATOM   5736 C  CG  . GLU C  1  68  ? -11.601 -2.142  6.593  1.00 53.12  ? 81  GLU C CG  1 
ATOM   5737 C  CD  . GLU C  1  68  ? -11.674 -2.160  5.069  1.00 63.01  ? 81  GLU C CD  1 
ATOM   5738 O  OE1 . GLU C  1  68  ? -10.582 -2.138  4.446  1.00 61.15  ? 81  GLU C OE1 1 
ATOM   5739 O  OE2 . GLU C  1  68  ? -12.801 -2.153  4.507  1.00 71.30  ? 81  GLU C OE2 1 
ATOM   5740 N  N   . GLY C  1  69  ? -13.322 1.696   8.448  1.00 41.64  ? 82  GLY C N   1 
ATOM   5741 C  CA  . GLY C  1  69  ? -14.404 2.448   9.061  1.00 38.61  ? 82  GLY C CA  1 
ATOM   5742 C  C   . GLY C  1  69  ? -14.446 3.915   8.649  1.00 34.88  ? 82  GLY C C   1 
ATOM   5743 O  O   . GLY C  1  69  ? -15.537 4.462   8.537  1.00 38.11  ? 82  GLY C O   1 
ATOM   5744 N  N   . PHE C  1  70  ? -13.276 4.548   8.482  1.00 33.80  ? 83  PHE C N   1 
ATOM   5745 C  CA  . PHE C  1  70  ? -13.188 5.997   8.324  1.00 36.85  ? 83  PHE C CA  1 
ATOM   5746 C  C   . PHE C  1  70  ? -12.350 6.439   7.116  1.00 35.95  ? 83  PHE C C   1 
ATOM   5747 O  O   . PHE C  1  70  ? -12.265 7.634   6.849  1.00 34.53  ? 83  PHE C O   1 
ATOM   5748 C  CB  . PHE C  1  70  ? -12.602 6.607   9.608  1.00 38.78  ? 83  PHE C CB  1 
ATOM   5749 C  CG  . PHE C  1  70  ? -13.550 6.751   10.792 1.00 40.43  ? 83  PHE C CG  1 
ATOM   5750 C  CD1 . PHE C  1  70  ? -14.570 7.700   10.779 1.00 42.66  ? 83  PHE C CD1 1 
ATOM   5751 C  CD2 . PHE C  1  70  ? -13.399 5.971   11.932 1.00 43.49  ? 83  PHE C CD2 1 
ATOM   5752 C  CE1 . PHE C  1  70  ? -15.429 7.830   11.861 1.00 45.58  ? 83  PHE C CE1 1 
ATOM   5753 C  CE2 . PHE C  1  70  ? -14.262 6.115   13.014 1.00 42.38  ? 83  PHE C CE2 1 
ATOM   5754 C  CZ  . PHE C  1  70  ? -15.262 7.047   12.976 1.00 44.74  ? 83  PHE C CZ  1 
ATOM   5755 N  N   . ASN C  1  71  ? -11.705 5.504   6.398  1.00 39.51  ? 84  ASN C N   1 
ATOM   5756 C  CA  . ASN C  1  71  ? -10.768 5.827   5.322  1.00 37.91  ? 84  ASN C CA  1 
ATOM   5757 C  C   . ASN C  1  71  ? -9.596  6.662   5.845  1.00 38.73  ? 84  ASN C C   1 
ATOM   5758 O  O   . ASN C  1  71  ? -9.098  7.571   5.169  1.00 37.56  ? 84  ASN C O   1 
ATOM   5759 C  CB  . ASN C  1  71  ? -11.466 6.522   4.159  1.00 37.50  ? 84  ASN C CB  1 
ATOM   5760 C  CG  . ASN C  1  71  ? -10.972 6.071   2.800  1.00 40.79  ? 84  ASN C CG  1 
ATOM   5761 O  OD1 . ASN C  1  71  ? -9.920  5.435   2.671  1.00 40.66  ? 84  ASN C OD1 1 
ATOM   5762 N  ND2 . ASN C  1  71  ? -11.732 6.375   1.765  1.00 44.12  ? 84  ASN C ND2 1 
ATOM   5763 N  N   . PHE C  1  72  ? -9.148  6.368   7.073  1.00 40.11  ? 85  PHE C N   1 
ATOM   5764 C  CA  . PHE C  1  72  ? -7.969  7.030   7.617  1.00 37.30  ? 85  PHE C CA  1 
ATOM   5765 C  C   . PHE C  1  72  ? -6.778  6.627   6.748  1.00 33.46  ? 85  PHE C C   1 
ATOM   5766 O  O   . PHE C  1  72  ? -6.635  5.459   6.416  1.00 32.21  ? 85  PHE C O   1 
ATOM   5767 C  CB  . PHE C  1  72  ? -7.793  6.617   9.082  1.00 36.59  ? 85  PHE C CB  1 
ATOM   5768 C  CG  . PHE C  1  72  ? -6.902  7.504   9.948  1.00 35.83  ? 85  PHE C CG  1 
ATOM   5769 C  CD1 . PHE C  1  72  ? -6.982  8.891   9.892  1.00 35.53  ? 85  PHE C CD1 1 
ATOM   5770 C  CD2 . PHE C  1  72  ? -6.011  6.940   10.855 1.00 38.62  ? 85  PHE C CD2 1 
ATOM   5771 C  CE1 . PHE C  1  72  ? -6.169  9.682   10.691 1.00 39.83  ? 85  PHE C CE1 1 
ATOM   5772 C  CE2 . PHE C  1  72  ? -5.216  7.737   11.673 1.00 37.35  ? 85  PHE C CE2 1 
ATOM   5773 C  CZ  . PHE C  1  72  ? -5.279  9.103   11.575 1.00 36.55  ? 85  PHE C CZ  1 
ATOM   5774 N  N   . GLU C  1  73  ? -5.953  7.591   6.340  1.00 34.92  ? 86  GLU C N   1 
ATOM   5775 C  CA  . GLU C  1  73  ? -4.866  7.303   5.413  1.00 36.48  ? 86  GLU C CA  1 
ATOM   5776 C  C   . GLU C  1  73  ? -3.841  6.380   6.084  1.00 36.45  ? 86  GLU C C   1 
ATOM   5777 O  O   . GLU C  1  73  ? -3.544  6.515   7.270  1.00 37.06  ? 86  GLU C O   1 
ATOM   5778 C  CB  . GLU C  1  73  ? -4.317  8.645   4.938  1.00 38.99  ? 86  GLU C CB  1 
ATOM   5779 C  CG  . GLU C  1  73  ? -3.336  8.534   3.774  1.00 46.42  ? 86  GLU C CG  1 
ATOM   5780 C  CD  . GLU C  1  73  ? -1.896  8.229   4.177  1.00 50.83  ? 86  GLU C CD  1 
ATOM   5781 O  OE1 . GLU C  1  73  ? -1.243  7.364   3.545  1.00 50.90  ? 86  GLU C OE1 1 
ATOM   5782 O  OE2 . GLU C  1  73  ? -1.439  8.846   5.158  1.00 50.01  ? 86  GLU C OE2 1 
ATOM   5783 N  N   . ASN C  1  74  ? -3.297  5.442   5.304  1.00 37.75  ? 87  ASN C N   1 
ATOM   5784 C  CA  . ASN C  1  74  ? -2.453  4.353   5.780  1.00 35.33  ? 87  ASN C CA  1 
ATOM   5785 C  C   . ASN C  1  74  ? -1.278  4.852   6.627  1.00 37.49  ? 87  ASN C C   1 
ATOM   5786 O  O   . ASN C  1  74  ? -1.039  4.324   7.710  1.00 32.97  ? 87  ASN C O   1 
ATOM   5787 C  CB  . ASN C  1  74  ? -1.980  3.520   4.594  1.00 37.21  ? 87  ASN C CB  1 
ATOM   5788 C  CG  . ASN C  1  74  ? -1.082  2.366   4.964  1.00 35.69  ? 87  ASN C CG  1 
ATOM   5789 O  OD1 . ASN C  1  74  ? 0.087   2.369   4.577  1.00 40.82  ? 87  ASN C OD1 1 
ATOM   5790 N  ND2 . ASN C  1  74  ? -1.594  1.380   5.683  1.00 34.82  ? 87  ASN C ND2 1 
ATOM   5791 N  N   . ASN C  1  75  ? -0.533  5.854   6.153  1.00 37.76  ? 88  ASN C N   1 
ATOM   5792 C  CA  . ASN C  1  75  ? 0.656   6.300   6.866  1.00 37.16  ? 88  ASN C CA  1 
ATOM   5793 C  C   . ASN C  1  75  ? 0.261   6.982   8.173  1.00 38.60  ? 88  ASN C C   1 
ATOM   5794 O  O   . ASN C  1  75  ? 0.931   6.791   9.180  1.00 37.31  ? 88  ASN C O   1 
ATOM   5795 C  CB  . ASN C  1  75  ? 1.581   7.169   6.016  1.00 38.34  ? 88  ASN C CB  1 
ATOM   5796 C  CG  . ASN C  1  75  ? 2.202   6.387   4.877  1.00 43.56  ? 88  ASN C CG  1 
ATOM   5797 O  OD1 . ASN C  1  75  ? 1.976   6.730   3.712  1.00 51.17  ? 88  ASN C OD1 1 
ATOM   5798 N  ND2 . ASN C  1  75  ? 2.900   5.299   5.167  1.00 39.43  ? 88  ASN C ND2 1 
ATOM   5799 N  N   . ALA C  1  76  ? -0.814  7.772   8.156  1.00 36.87  ? 89  ALA C N   1 
ATOM   5800 C  CA  . ALA C  1  76  ? -1.331  8.396   9.364  1.00 39.13  ? 89  ALA C CA  1 
ATOM   5801 C  C   . ALA C  1  76  ? -1.758  7.332   10.378 1.00 39.12  ? 89  ALA C C   1 
ATOM   5802 O  O   . ALA C  1  76  ? -1.511  7.480   11.574 1.00 41.52  ? 89  ALA C O   1 
ATOM   5803 C  CB  . ALA C  1  76  ? -2.478  9.320   9.017  1.00 42.62  ? 89  ALA C CB  1 
ATOM   5804 N  N   . ALA C  1  77  ? -2.374  6.248   9.901  1.00 35.18  ? 90  ALA C N   1 
ATOM   5805 C  CA  . ALA C  1  77  ? -2.774  5.147   10.764 1.00 37.88  ? 90  ALA C CA  1 
ATOM   5806 C  C   . ALA C  1  77  ? -1.555  4.483   11.406 1.00 39.39  ? 90  ALA C C   1 
ATOM   5807 O  O   . ALA C  1  77  ? -1.580  4.149   12.592 1.00 38.22  ? 90  ALA C O   1 
ATOM   5808 C  CB  . ALA C  1  77  ? -3.610  4.143   9.980  1.00 37.44  ? 90  ALA C CB  1 
ATOM   5809 N  N   . ILE C  1  78  ? -0.496  4.278   10.610 1.00 36.73  ? 91  ILE C N   1 
ATOM   5810 C  CA  . ILE C  1  78  ? 0.719   3.645   11.096 1.00 34.27  ? 91  ILE C CA  1 
ATOM   5811 C  C   . ILE C  1  78  ? 1.367   4.550   12.144 1.00 33.90  ? 91  ILE C C   1 
ATOM   5812 O  O   . ILE C  1  78  ? 1.792   4.077   13.182 1.00 35.13  ? 91  ILE C O   1 
ATOM   5813 C  CB  . ILE C  1  78  ? 1.652   3.298   9.919  1.00 37.99  ? 91  ILE C CB  1 
ATOM   5814 C  CG1 . ILE C  1  78  ? 1.094   2.145   9.078  1.00 38.40  ? 91  ILE C CG1 1 
ATOM   5815 C  CG2 . ILE C  1  78  ? 3.068   2.980   10.395 1.00 37.08  ? 91  ILE C CG2 1 
ATOM   5816 C  CD1 . ILE C  1  78  ? 1.739   2.018   7.709  1.00 36.20  ? 91  ILE C CD1 1 
ATOM   5817 N  N   . VAL C  1  79  ? 1.410   5.859   11.897 1.00 35.63  ? 92  VAL C N   1 
ATOM   5818 C  CA  . VAL C  1  79  ? 2.090   6.786   12.782 1.00 36.82  ? 92  VAL C CA  1 
ATOM   5819 C  C   . VAL C  1  79  ? 1.397   6.812   14.144 1.00 39.04  ? 92  VAL C C   1 
ATOM   5820 O  O   . VAL C  1  79  ? 2.072   6.771   15.176 1.00 33.11  ? 92  VAL C O   1 
ATOM   5821 C  CB  . VAL C  1  79  ? 2.208   8.198   12.169 1.00 38.78  ? 92  VAL C CB  1 
ATOM   5822 C  CG1 . VAL C  1  79  ? 2.658   9.230   13.188 1.00 39.63  ? 92  VAL C CG1 1 
ATOM   5823 C  CG2 . VAL C  1  79  ? 3.170   8.223   10.995 1.00 40.27  ? 92  VAL C CG2 1 
ATOM   5824 N  N   . ALA C  1  80  ? 0.058   6.902   14.136 1.00 35.05  ? 93  ALA C N   1 
ATOM   5825 C  CA  . ALA C  1  80  ? -0.718  6.970   15.361 1.00 33.27  ? 93  ALA C CA  1 
ATOM   5826 C  C   . ALA C  1  80  ? -0.697  5.625   16.085 1.00 34.49  ? 93  ALA C C   1 
ATOM   5827 O  O   . ALA C  1  80  ? -0.529  5.569   17.304 1.00 34.79  ? 93  ALA C O   1 
ATOM   5828 C  CB  . ALA C  1  80  ? -2.125  7.426   15.070 1.00 34.33  ? 93  ALA C CB  1 
ATOM   5829 N  N   . THR C  1  81  ? -0.824  4.525   15.344 1.00 35.15  ? 94  THR C N   1 
ATOM   5830 C  CA  . THR C  1  81  ? -1.025  3.244   15.997 1.00 34.82  ? 94  THR C CA  1 
ATOM   5831 C  C   . THR C  1  81  ? 0.242   2.799   16.727 1.00 39.22  ? 94  THR C C   1 
ATOM   5832 O  O   . THR C  1  81  ? 0.152   2.370   17.883 1.00 35.47  ? 94  THR C O   1 
ATOM   5833 C  CB  . THR C  1  81  ? -1.506  2.208   14.993 1.00 36.25  ? 94  THR C CB  1 
ATOM   5834 O  OG1 . THR C  1  81  ? -2.783  2.669   14.547 1.00 34.92  ? 94  THR C OG1 1 
ATOM   5835 C  CG2 . THR C  1  81  ? -1.626  0.826   15.604 1.00 36.07  ? 94  THR C CG2 1 
ATOM   5836 N  N   . TYR C  1  82  ? 1.410   2.873   16.061 1.00 37.05  ? 95  TYR C N   1 
ATOM   5837 C  CA  . TYR C  1  82  ? 2.633   2.327   16.639 1.00 37.12  ? 95  TYR C CA  1 
ATOM   5838 C  C   . TYR C  1  82  ? 3.184   3.280   17.700 1.00 34.78  ? 95  TYR C C   1 
ATOM   5839 O  O   . TYR C  1  82  ? 3.834   2.837   18.630 1.00 31.41  ? 95  TYR C O   1 
ATOM   5840 C  CB  . TYR C  1  82  ? 3.649   1.922   15.563 1.00 36.87  ? 95  TYR C CB  1 
ATOM   5841 C  CG  . TYR C  1  82  ? 3.199   0.702   14.773 1.00 36.05  ? 95  TYR C CG  1 
ATOM   5842 C  CD1 . TYR C  1  82  ? 3.256   -0.563  15.335 1.00 34.93  ? 95  TYR C CD1 1 
ATOM   5843 C  CD2 . TYR C  1  82  ? 2.667   0.814   13.494 1.00 37.73  ? 95  TYR C CD2 1 
ATOM   5844 C  CE1 . TYR C  1  82  ? 2.821   -1.685  14.649 1.00 35.51  ? 95  TYR C CE1 1 
ATOM   5845 C  CE2 . TYR C  1  82  ? 2.239   -0.297  12.787 1.00 35.60  ? 95  TYR C CE2 1 
ATOM   5846 C  CZ  . TYR C  1  82  ? 2.315   -1.553  13.364 1.00 39.17  ? 95  TYR C CZ  1 
ATOM   5847 O  OH  . TYR C  1  82  ? 1.914   -2.669  12.679 1.00 40.12  ? 95  TYR C OH  1 
ATOM   5848 N  N   . LEU C  1  83  ? 2.908   4.582   17.580 1.00 37.41  ? 96  LEU C N   1 
ATOM   5849 C  CA  . LEU C  1  83  ? 3.173   5.533   18.650 1.00 36.12  ? 96  LEU C CA  1 
ATOM   5850 C  C   . LEU C  1  83  ? 2.436   5.093   19.909 1.00 39.79  ? 96  LEU C C   1 
ATOM   5851 O  O   . LEU C  1  83  ? 3.014   4.991   20.982 1.00 39.64  ? 96  LEU C O   1 
ATOM   5852 C  CB  . LEU C  1  83  ? 2.712   6.926   18.224 1.00 36.87  ? 96  LEU C CB  1 
ATOM   5853 C  CG  . LEU C  1  83  ? 2.784   8.027   19.284 1.00 37.31  ? 96  LEU C CG  1 
ATOM   5854 C  CD1 . LEU C  1  83  ? 4.210   8.299   19.697 1.00 39.97  ? 96  LEU C CD1 1 
ATOM   5855 C  CD2 . LEU C  1  83  ? 2.128   9.289   18.749 1.00 40.48  ? 96  LEU C CD2 1 
ATOM   5856 N  N   . GLY C  1  84  ? 1.133   4.858   19.775 1.00 39.55  ? 97  GLY C N   1 
ATOM   5857 C  CA  . GLY C  1  84  ? 0.316   4.423   20.896 1.00 37.62  ? 97  GLY C CA  1 
ATOM   5858 C  C   . GLY C  1  84  ? 0.800   3.088   21.456 1.00 36.16  ? 97  GLY C C   1 
ATOM   5859 O  O   . GLY C  1  84  ? 0.834   2.913   22.665 1.00 35.20  ? 97  GLY C O   1 
ATOM   5860 N  N   . HIS C  1  85  ? 1.192   2.163   20.580 1.00 33.59  ? 98  HIS C N   1 
ATOM   5861 C  CA  . HIS C  1  85  ? 1.623   0.838   21.005 1.00 33.82  ? 98  HIS C CA  1 
ATOM   5862 C  C   . HIS C  1  85  ? 3.006   0.879   21.668 1.00 36.96  ? 98  HIS C C   1 
ATOM   5863 O  O   . HIS C  1  85  ? 3.199   0.255   22.708 1.00 34.84  ? 98  HIS C O   1 
ATOM   5864 C  CB  . HIS C  1  85  ? 1.652   -0.119  19.813 1.00 33.53  ? 98  HIS C CB  1 
ATOM   5865 C  CG  . HIS C  1  85  ? 1.841   -1.537  20.183 1.00 34.58  ? 98  HIS C CG  1 
ATOM   5866 N  ND1 . HIS C  1  85  ? 1.066   -2.167  21.129 1.00 36.78  ? 98  HIS C ND1 1 
ATOM   5867 C  CD2 . HIS C  1  85  ? 2.692   -2.465  19.712 1.00 35.28  ? 98  HIS C CD2 1 
ATOM   5868 C  CE1 . HIS C  1  85  ? 1.452   -3.440  21.217 1.00 37.58  ? 98  HIS C CE1 1 
ATOM   5869 N  NE2 . HIS C  1  85  ? 2.443   -3.647  20.368 1.00 34.88  ? 98  HIS C NE2 1 
ATOM   5870 N  N   . LEU C  1  86  ? 3.981   1.579   21.063 1.00 36.64  ? 99  LEU C N   1 
ATOM   5871 C  CA  . LEU C  1  86  ? 5.330   1.646   21.615 1.00 37.52  ? 99  LEU C CA  1 
ATOM   5872 C  C   . LEU C  1  86  ? 5.272   2.162   23.056 1.00 36.53  ? 99  LEU C C   1 
ATOM   5873 O  O   . LEU C  1  86  ? 5.891   1.600   23.948 1.00 33.90  ? 99  LEU C O   1 
ATOM   5874 C  CB  . LEU C  1  86  ? 6.232   2.518   20.738 1.00 36.45  ? 99  LEU C CB  1 
ATOM   5875 C  CG  . LEU C  1  86  ? 6.767   1.884   19.450 1.00 33.30  ? 99  LEU C CG  1 
ATOM   5876 C  CD1 . LEU C  1  86  ? 7.363   2.956   18.547 1.00 34.49  ? 99  LEU C CD1 1 
ATOM   5877 C  CD2 . LEU C  1  86  ? 7.785   0.815   19.766 1.00 33.07  ? 99  LEU C CD2 1 
ATOM   5878 N  N   . LEU C  1  87  ? 4.497   3.232   23.277 1.00 40.19  ? 100 LEU C N   1 
ATOM   5879 C  CA  . LEU C  1  87  ? 4.441   3.915   24.559 1.00 38.17  ? 100 LEU C CA  1 
ATOM   5880 C  C   . LEU C  1  87  ? 3.491   3.229   25.540 1.00 42.32  ? 100 LEU C C   1 
ATOM   5881 O  O   . LEU C  1  87  ? 3.762   3.241   26.739 1.00 40.26  ? 100 LEU C O   1 
ATOM   5882 C  CB  . LEU C  1  87  ? 4.026   5.366   24.331 1.00 39.40  ? 100 LEU C CB  1 
ATOM   5883 C  CG  . LEU C  1  87  ? 5.029   6.239   23.568 1.00 40.75  ? 100 LEU C CG  1 
ATOM   5884 C  CD1 . LEU C  1  87  ? 4.474   7.634   23.405 1.00 40.52  ? 100 LEU C CD1 1 
ATOM   5885 C  CD2 . LEU C  1  87  ? 6.396   6.310   24.230 1.00 42.98  ? 100 LEU C CD2 1 
ATOM   5886 N  N   . ASN C  1  88  ? 2.366   2.672   25.056 1.00 40.10  ? 101 ASN C N   1 
ATOM   5887 C  CA  . ASN C  1  88  ? 1.272   2.316   25.946 1.00 34.90  ? 101 ASN C CA  1 
ATOM   5888 C  C   . ASN C  1  88  ? 0.825   0.857   25.807 1.00 38.40  ? 101 ASN C C   1 
ATOM   5889 O  O   . ASN C  1  88  ? -0.083  0.432   26.525 1.00 32.86  ? 101 ASN C O   1 
ATOM   5890 C  CB  . ASN C  1  88  ? 0.043   3.184   25.725 1.00 35.45  ? 101 ASN C CB  1 
ATOM   5891 C  CG  . ASN C  1  88  ? 0.275   4.654   25.979 1.00 38.89  ? 101 ASN C CG  1 
ATOM   5892 O  OD1 . ASN C  1  88  ? 0.915   5.047   26.961 1.00 44.67  ? 101 ASN C OD1 1 
ATOM   5893 N  ND2 . ASN C  1  88  ? -0.263  5.504   25.119 1.00 40.95  ? 101 ASN C ND2 1 
ATOM   5894 N  N   . GLY C  1  89  ? 1.437   0.084   24.904 1.00 37.94  ? 102 GLY C N   1 
ATOM   5895 C  CA  . GLY C  1  89  ? 0.963   -1.263  24.617 1.00 35.48  ? 102 GLY C CA  1 
ATOM   5896 C  C   . GLY C  1  89  ? 1.906   -2.323  25.172 1.00 38.60  ? 102 GLY C C   1 
ATOM   5897 O  O   . GLY C  1  89  ? 2.994   -2.004  25.664 1.00 40.60  ? 102 GLY C O   1 
ATOM   5898 N  N   . ASN C  1  90  ? 1.476   -3.587  25.067 1.00 41.05  ? 103 ASN C N   1 
ATOM   5899 C  CA  . ASN C  1  90  ? 2.295   -4.726  25.438 1.00 39.90  ? 103 ASN C CA  1 
ATOM   5900 C  C   . ASN C  1  90  ? 2.943   -5.305  24.187 1.00 40.08  ? 103 ASN C C   1 
ATOM   5901 O  O   . ASN C  1  90  ? 2.256   -5.893  23.349 1.00 43.52  ? 103 ASN C O   1 
ATOM   5902 C  CB  . ASN C  1  90  ? 1.462   -5.757  26.183 1.00 40.45  ? 103 ASN C CB  1 
ATOM   5903 C  CG  . ASN C  1  90  ? 2.309   -6.853  26.793 1.00 40.64  ? 103 ASN C CG  1 
ATOM   5904 O  OD1 . ASN C  1  90  ? 3.166   -7.442  26.126 1.00 41.55  ? 103 ASN C OD1 1 
ATOM   5905 N  ND2 . ASN C  1  90  ? 2.070   -7.156  28.057 1.00 42.24  ? 103 ASN C ND2 1 
ATOM   5906 N  N   . LEU C  1  91  ? 4.272   -5.169  24.093 1.00 40.21  ? 104 LEU C N   1 
ATOM   5907 C  CA  . LEU C  1  91  ? 4.988   -5.490  22.867 1.00 41.75  ? 104 LEU C CA  1 
ATOM   5908 C  C   . LEU C  1  91  ? 5.172   -6.992  22.700 1.00 39.21  ? 104 LEU C C   1 
ATOM   5909 O  O   . LEU C  1  91  ? 5.310   -7.468  21.578 1.00 42.22  ? 104 LEU C O   1 
ATOM   5910 C  CB  . LEU C  1  91  ? 6.310   -4.730  22.866 1.00 45.07  ? 104 LEU C CB  1 
ATOM   5911 C  CG  . LEU C  1  91  ? 6.144   -3.211  22.926 1.00 50.13  ? 104 LEU C CG  1 
ATOM   5912 C  CD1 . LEU C  1  91  ? 7.448   -2.541  23.201 1.00 56.81  ? 104 LEU C CD1 1 
ATOM   5913 C  CD2 . LEU C  1  91  ? 5.556   -2.682  21.641 1.00 58.43  ? 104 LEU C CD2 1 
ATOM   5914 N  N   . VAL C  1  92  ? 5.116   -7.728  23.815 1.00 42.18  ? 105 VAL C N   1 
ATOM   5915 C  CA  . VAL C  1  92  ? 5.305   -9.171  23.812 1.00 44.18  ? 105 VAL C CA  1 
ATOM   5916 C  C   . VAL C  1  92  ? 4.029   -9.860  23.326 1.00 44.21  ? 105 VAL C C   1 
ATOM   5917 O  O   . VAL C  1  92  ? 4.103   -10.733 22.463 1.00 47.02  ? 105 VAL C O   1 
ATOM   5918 C  CB  . VAL C  1  92  ? 5.777   -9.665  25.195 1.00 44.58  ? 105 VAL C CB  1 
ATOM   5919 C  CG1 . VAL C  1  92  ? 5.765   -11.189 25.308 1.00 42.55  ? 105 VAL C CG1 1 
ATOM   5920 C  CG2 . VAL C  1  92  ? 7.183   -9.142  25.503 1.00 44.59  ? 105 VAL C CG2 1 
ATOM   5921 N  N   . THR C  1  93  ? 2.868   -9.429  23.838 1.00 44.90  ? 106 THR C N   1 
ATOM   5922 C  CA  . THR C  1  93  ? 1.584   -10.002 23.433 1.00 46.16  ? 106 THR C CA  1 
ATOM   5923 C  C   . THR C  1  93  ? 1.003   -9.310  22.197 1.00 44.58  ? 106 THR C C   1 
ATOM   5924 O  O   . THR C  1  93  ? 0.086   -9.857  21.596 1.00 50.72  ? 106 THR C O   1 
ATOM   5925 C  CB  . THR C  1  93  ? 0.587   -9.959  24.592 1.00 44.52  ? 106 THR C CB  1 
ATOM   5926 O  OG1 . THR C  1  93  ? 0.365   -8.584  24.890 1.00 38.80  ? 106 THR C OG1 1 
ATOM   5927 C  CG2 . THR C  1  93  ? 1.093   -10.705 25.814 1.00 46.34  ? 106 THR C CG2 1 
ATOM   5928 N  N   . ASP C  1  94  ? 1.515   -8.124  21.836 1.00 43.63  ? 107 ASP C N   1 
ATOM   5929 C  CA  . ASP C  1  94  ? 1.063   -7.399  20.654 1.00 42.49  ? 107 ASP C CA  1 
ATOM   5930 C  C   . ASP C  1  94  ? -0.361  -6.883  20.851 1.00 41.95  ? 107 ASP C C   1 
ATOM   5931 O  O   . ASP C  1  94  ? -1.149  -6.860  19.902 1.00 41.12  ? 107 ASP C O   1 
ATOM   5932 C  CB  . ASP C  1  94  ? 1.169   -8.242  19.387 1.00 42.66  ? 107 ASP C CB  1 
ATOM   5933 C  CG  . ASP C  1  94  ? 1.201   -7.471  18.074 1.00 43.67  ? 107 ASP C CG  1 
ATOM   5934 O  OD1 . ASP C  1  94  ? 1.885   -6.413  18.033 1.00 45.89  ? 107 ASP C OD1 1 
ATOM   5935 O  OD2 . ASP C  1  94  ? 0.558   -7.939  17.097 1.00 43.05  ? 107 ASP C OD2 1 
ATOM   5936 N  N   . LEU C  1  95  ? -0.675  -6.443  22.078 1.00 41.01  ? 108 LEU C N   1 
ATOM   5937 C  CA  . LEU C  1  95  ? -2.014  -5.976  22.424 1.00 39.56  ? 108 LEU C CA  1 
ATOM   5938 C  C   . LEU C  1  95  ? -1.933  -4.584  23.046 1.00 35.58  ? 108 LEU C C   1 
ATOM   5939 O  O   . LEU C  1  95  ? -1.071  -4.333  23.883 1.00 37.90  ? 108 LEU C O   1 
ATOM   5940 C  CB  . LEU C  1  95  ? -2.681  -6.954  23.392 1.00 41.84  ? 108 LEU C CB  1 
ATOM   5941 C  CG  . LEU C  1  95  ? -2.961  -8.364  22.860 1.00 42.26  ? 108 LEU C CG  1 
ATOM   5942 C  CD1 . LEU C  1  95  ? -3.515  -9.208  23.997 1.00 41.69  ? 108 LEU C CD1 1 
ATOM   5943 C  CD2 . LEU C  1  95  ? -3.926  -8.343  21.674 1.00 42.69  ? 108 LEU C CD2 1 
ATOM   5944 N  N   . LEU C  1  96  ? -2.863  -3.716  22.634 1.00 35.47  ? 109 LEU C N   1 
ATOM   5945 C  CA  . LEU C  1  96  ? -3.004  -2.352  23.112 1.00 36.21  ? 109 LEU C CA  1 
ATOM   5946 C  C   . LEU C  1  96  ? -4.453  -2.123  23.566 1.00 41.44  ? 109 LEU C C   1 
ATOM   5947 O  O   . LEU C  1  96  ? -5.400  -2.461  22.850 1.00 40.90  ? 109 LEU C O   1 
ATOM   5948 C  CB  . LEU C  1  96  ? -2.633  -1.399  21.973 1.00 34.33  ? 109 LEU C CB  1 
ATOM   5949 C  CG  . LEU C  1  96  ? -2.924  0.088   22.210 1.00 34.15  ? 109 LEU C CG  1 
ATOM   5950 C  CD1 . LEU C  1  96  ? -2.197  0.595   23.465 1.00 36.07  ? 109 LEU C CD1 1 
ATOM   5951 C  CD2 . LEU C  1  96  ? -2.542  0.921   20.997 1.00 34.13  ? 109 LEU C CD2 1 
ATOM   5952 N  N   . SER C  1  97  ? -4.608  -1.543  24.763 1.00 38.29  ? 110 SER C N   1 
ATOM   5953 C  CA  . SER C  1  97  ? -5.891  -1.087  25.274 1.00 39.03  ? 110 SER C CA  1 
ATOM   5954 C  C   . SER C  1  97  ? -6.163  0.323   24.768 1.00 36.91  ? 110 SER C C   1 
ATOM   5955 O  O   . SER C  1  97  ? -5.271  1.172   24.842 1.00 36.51  ? 110 SER C O   1 
ATOM   5956 C  CB  . SER C  1  97  ? -5.902  -1.118  26.788 1.00 40.64  ? 110 SER C CB  1 
ATOM   5957 O  OG  . SER C  1  97  ? -6.985  -0.358  27.323 1.00 39.01  ? 110 SER C OG  1 
ATOM   5958 N  N   . ILE C  1  98  ? -7.396  0.572   24.287 1.00 33.27  ? 111 ILE C N   1 
ATOM   5959 C  CA  . ILE C  1  98  ? -7.737  1.882   23.759 1.00 37.02  ? 111 ILE C CA  1 
ATOM   5960 C  C   . ILE C  1  98  ? -8.138  2.808   24.902 1.00 39.83  ? 111 ILE C C   1 
ATOM   5961 O  O   . ILE C  1  98  ? -8.439  3.977   24.659 1.00 43.83  ? 111 ILE C O   1 
ATOM   5962 C  CB  . ILE C  1  98  ? -8.818  1.818   22.661 1.00 39.99  ? 111 ILE C CB  1 
ATOM   5963 C  CG1 . ILE C  1  98  ? -10.176 1.291   23.167 1.00 42.80  ? 111 ILE C CG1 1 
ATOM   5964 C  CG2 . ILE C  1  98  ? -8.321  1.016   21.463 1.00 38.50  ? 111 ILE C CG2 1 
ATOM   5965 C  CD1 . ILE C  1  98  ? -11.302 1.448   22.148 1.00 40.46  ? 111 ILE C CD1 1 
ATOM   5966 N  N   . GLY C  1  99  ? -8.138  2.276   26.133 1.00 43.21  ? 112 GLY C N   1 
ATOM   5967 C  CA  . GLY C  1  99  ? -8.417  3.061   27.327 1.00 44.40  ? 112 GLY C CA  1 
ATOM   5968 C  C   . GLY C  1  99  ? -7.367  2.825   28.416 1.00 44.34  ? 112 GLY C C   1 
ATOM   5969 O  O   . GLY C  1  99  ? -6.182  3.102   28.209 1.00 39.37  ? 112 GLY C O   1 
ATOM   5970 N  N   . GLY C  1  100 ? -7.820  2.337   29.584 1.00 47.94  ? 113 GLY C N   1 
ATOM   5971 C  CA  . GLY C  1  100 ? -6.962  2.169   30.755 1.00 50.36  ? 113 GLY C CA  1 
ATOM   5972 C  C   . GLY C  1  100 ? -6.338  0.773   30.854 1.00 47.56  ? 113 GLY C C   1 
ATOM   5973 O  O   . GLY C  1  100 ? -6.504  -0.053  29.961 1.00 45.72  ? 113 GLY C O   1 
ATOM   5974 N  N   . ALA C  1  101 ? -5.659  0.514   31.981 1.00 45.66  ? 114 ALA C N   1 
ATOM   5975 C  CA  . ALA C  1  101 ? -4.894  -0.708  32.175 1.00 45.11  ? 114 ALA C CA  1 
ATOM   5976 C  C   . ALA C  1  101 ? -5.831  -1.881  32.409 1.00 44.86  ? 114 ALA C C   1 
ATOM   5977 O  O   . ALA C  1  101 ? -6.900  -1.723  32.981 1.00 49.46  ? 114 ALA C O   1 
ATOM   5978 C  CB  . ALA C  1  101 ? -3.925  -0.556  33.330 1.00 47.33  ? 114 ALA C CB  1 
ATOM   5979 N  N   . THR C  1  102 ? -5.395  -3.064  31.980 1.00 42.61  ? 115 THR C N   1 
ATOM   5980 C  CA  . THR C  1  102 ? -6.246  -4.231  31.984 1.00 47.67  ? 115 THR C CA  1 
ATOM   5981 C  C   . THR C  1  102 ? -5.360  -5.466  31.898 1.00 49.35  ? 115 THR C C   1 
ATOM   5982 O  O   . THR C  1  102 ? -4.386  -5.476  31.156 1.00 52.49  ? 115 THR C O   1 
ATOM   5983 C  CB  . THR C  1  102 ? -7.249  -4.152  30.825 1.00 51.81  ? 115 THR C CB  1 
ATOM   5984 O  OG1 . THR C  1  102 ? -7.940  -5.400  30.806 1.00 51.71  ? 115 THR C OG1 1 
ATOM   5985 C  CG2 . THR C  1  102 ? -6.600  -3.937  29.465 1.00 49.85  ? 115 THR C CG2 1 
ATOM   5986 N  N   . PRO C  1  103 ? -5.692  -6.553  32.630 1.00 56.95  ? 116 PRO C N   1 
ATOM   5987 C  CA  . PRO C  1  103 ? -5.035  -7.844  32.419 1.00 54.64  ? 116 PRO C CA  1 
ATOM   5988 C  C   . PRO C  1  103 ? -5.229  -8.445  31.028 1.00 49.19  ? 116 PRO C C   1 
ATOM   5989 O  O   . PRO C  1  103 ? -4.453  -9.318  30.648 1.00 54.87  ? 116 PRO C O   1 
ATOM   5990 C  CB  . PRO C  1  103 ? -5.652  -8.728  33.534 1.00 59.33  ? 116 PRO C CB  1 
ATOM   5991 C  CG  . PRO C  1  103 ? -6.983  -8.070  33.854 1.00 64.12  ? 116 PRO C CG  1 
ATOM   5992 C  CD  . PRO C  1  103 ? -6.705  -6.588  33.701 1.00 60.29  ? 116 PRO C CD  1 
ATOM   5993 N  N   . LYS C  1  104 ? -6.246  -7.979  30.279 1.00 51.98  ? 117 LYS C N   1 
ATOM   5994 C  CA  . LYS C  1  104 ? -6.511  -8.452  28.922 1.00 54.06  ? 117 LYS C CA  1 
ATOM   5995 C  C   . LYS C  1  104 ? -5.290  -8.265  28.007 1.00 50.51  ? 117 LYS C C   1 
ATOM   5996 O  O   . LYS C  1  104 ? -5.133  -9.025  27.049 1.00 55.96  ? 117 LYS C O   1 
ATOM   5997 C  CB  . LYS C  1  104 ? -7.749  -7.759  28.332 1.00 57.09  ? 117 LYS C CB  1 
ATOM   5998 C  CG  . LYS C  1  104 ? -9.123  -8.186  28.858 1.00 61.79  ? 117 LYS C CG  1 
ATOM   5999 C  CD  . LYS C  1  104 ? -10.250 -7.217  28.499 1.00 67.56  ? 117 LYS C CD  1 
ATOM   6000 C  CE  . LYS C  1  104 ? -11.611 -7.622  28.992 1.00 76.40  ? 117 LYS C CE  1 
ATOM   6001 N  NZ  . LYS C  1  104 ? -12.204 -8.687  28.178 1.00 84.37  ? 117 LYS C NZ  1 
ATOM   6002 N  N   . THR C  1  105 ? -4.417  -7.274  28.285 1.00 47.19  ? 118 THR C N   1 
ATOM   6003 C  CA  . THR C  1  105 ? -3.218  -7.091  27.469 1.00 49.11  ? 118 THR C CA  1 
ATOM   6004 C  C   . THR C  1  105 ? -2.105  -8.035  27.922 1.00 48.91  ? 118 THR C C   1 
ATOM   6005 O  O   . THR C  1  105 ? -1.063  -8.111  27.281 1.00 47.75  ? 118 THR C O   1 
ATOM   6006 C  CB  . THR C  1  105 ? -2.720  -5.647  27.466 1.00 43.18  ? 118 THR C CB  1 
ATOM   6007 O  OG1 . THR C  1  105 ? -2.430  -5.270  28.807 1.00 44.03  ? 118 THR C OG1 1 
ATOM   6008 C  CG2 . THR C  1  105 ? -3.712  -4.681  26.840 1.00 42.01  ? 118 THR C CG2 1 
ATOM   6009 N  N   . GLY C  1  106 ? -2.327  -8.752  29.025 1.00 50.45  ? 119 GLY C N   1 
ATOM   6010 C  CA  . GLY C  1  106 ? -1.471  -9.871  29.394 1.00 51.80  ? 119 GLY C CA  1 
ATOM   6011 C  C   . GLY C  1  106 ? -0.466  -9.503  30.484 1.00 50.32  ? 119 GLY C C   1 
ATOM   6012 O  O   . GLY C  1  106 ? -0.518  -8.412  31.048 1.00 44.78  ? 119 GLY C O   1 
ATOM   6013 N  N   . PRO C  1  107 ? 0.473   -10.416 30.816 1.00 52.52  ? 120 PRO C N   1 
ATOM   6014 C  CA  . PRO C  1  107 ? 1.460   -10.160 31.866 1.00 58.06  ? 120 PRO C CA  1 
ATOM   6015 C  C   . PRO C  1  107 ? 2.182   -8.818  31.695 1.00 61.71  ? 120 PRO C C   1 
ATOM   6016 O  O   . PRO C  1  107 ? 2.676   -8.486  30.622 1.00 63.81  ? 120 PRO C O   1 
ATOM   6017 C  CB  . PRO C  1  107 ? 2.415   -11.369 31.760 1.00 58.67  ? 120 PRO C CB  1 
ATOM   6018 C  CG  . PRO C  1  107 ? 1.580   -12.463 31.126 1.00 57.98  ? 120 PRO C CG  1 
ATOM   6019 C  CD  . PRO C  1  107 ? 0.629   -11.742 30.189 1.00 58.08  ? 120 PRO C CD  1 
ATOM   6020 N  N   . PRO C  1  108 ? 2.255   -7.985  32.750 1.00 63.67  ? 121 PRO C N   1 
ATOM   6021 C  CA  . PRO C  1  108 ? 2.810   -6.634  32.620 1.00 60.23  ? 121 PRO C CA  1 
ATOM   6022 C  C   . PRO C  1  108 ? 4.296   -6.604  32.270 1.00 54.79  ? 121 PRO C C   1 
ATOM   6023 O  O   . PRO C  1  108 ? 5.041   -7.511  32.616 1.00 47.27  ? 121 PRO C O   1 
ATOM   6024 C  CB  . PRO C  1  108 ? 2.523   -6.008  33.991 1.00 61.48  ? 121 PRO C CB  1 
ATOM   6025 C  CG  . PRO C  1  108 ? 2.454   -7.192  34.915 1.00 65.10  ? 121 PRO C CG  1 
ATOM   6026 C  CD  . PRO C  1  108 ? 1.779   -8.287  34.110 1.00 65.94  ? 121 PRO C CD  1 
ATOM   6027 N  N   . PRO C  1  109 ? 4.763   -5.584  31.518 1.00 50.99  ? 122 PRO C N   1 
ATOM   6028 C  CA  . PRO C  1  109 ? 6.168   -5.493  31.133 1.00 51.12  ? 122 PRO C CA  1 
ATOM   6029 C  C   . PRO C  1  109 ? 7.031   -5.056  32.312 1.00 49.23  ? 122 PRO C C   1 
ATOM   6030 O  O   . PRO C  1  109 ? 6.523   -4.572  33.314 1.00 45.74  ? 122 PRO C O   1 
ATOM   6031 C  CB  . PRO C  1  109 ? 6.159   -4.447  30.008 1.00 47.91  ? 122 PRO C CB  1 
ATOM   6032 C  CG  . PRO C  1  109 ? 5.000   -3.565  30.342 1.00 48.24  ? 122 PRO C CG  1 
ATOM   6033 C  CD  . PRO C  1  109 ? 3.965   -4.484  30.964 1.00 49.12  ? 122 PRO C CD  1 
ATOM   6034 N  N   . PRO C  1  110 ? 8.372   -5.161  32.209 1.00 48.88  ? 123 PRO C N   1 
ATOM   6035 C  CA  . PRO C  1  110 ? 9.251   -4.708  33.283 1.00 49.06  ? 123 PRO C CA  1 
ATOM   6036 C  C   . PRO C  1  110 ? 9.241   -3.184  33.411 1.00 50.32  ? 123 PRO C C   1 
ATOM   6037 O  O   . PRO C  1  110 ? 9.291   -2.462  32.419 1.00 51.60  ? 123 PRO C O   1 
ATOM   6038 C  CB  . PRO C  1  110 ? 10.623  -5.285  32.909 1.00 45.64  ? 123 PRO C CB  1 
ATOM   6039 C  CG  . PRO C  1  110 ? 10.559  -5.483  31.416 1.00 48.27  ? 123 PRO C CG  1 
ATOM   6040 C  CD  . PRO C  1  110 ? 9.108   -5.714  31.060 1.00 49.64  ? 123 PRO C CD  1 
ATOM   6041 N  N   . PRO C  1  111 ? 9.099   -2.637  34.638 1.00 49.51  ? 124 PRO C N   1 
ATOM   6042 C  CA  . PRO C  1  111 ? 9.086   -1.184  34.820 1.00 47.82  ? 124 PRO C CA  1 
ATOM   6043 C  C   . PRO C  1  111 ? 10.409  -0.596  34.337 1.00 50.27  ? 124 PRO C C   1 
ATOM   6044 O  O   . PRO C  1  111 ? 11.437  -1.272  34.362 1.00 49.26  ? 124 PRO C O   1 
ATOM   6045 C  CB  . PRO C  1  111 ? 8.874   -1.012  36.333 1.00 49.06  ? 124 PRO C CB  1 
ATOM   6046 C  CG  . PRO C  1  111 ? 8.217   -2.306  36.767 1.00 54.93  ? 124 PRO C CG  1 
ATOM   6047 C  CD  . PRO C  1  111 ? 8.836   -3.377  35.885 1.00 50.83  ? 124 PRO C CD  1 
ATOM   6048 N  N   . PRO C  1  112 ? 10.473  0.674   33.891 1.00 43.60  ? 125 PRO C N   1 
ATOM   6049 C  CA  . PRO C  1  112 ? 9.344   1.615   33.887 1.00 43.74  ? 125 PRO C CA  1 
ATOM   6050 C  C   . PRO C  1  112 ? 8.259   1.530   32.800 1.00 48.44  ? 125 PRO C C   1 
ATOM   6051 O  O   . PRO C  1  112 ? 7.350   2.365   32.790 1.00 42.83  ? 125 PRO C O   1 
ATOM   6052 C  CB  . PRO C  1  112 ? 10.026  3.003   33.802 1.00 42.20  ? 125 PRO C CB  1 
ATOM   6053 C  CG  . PRO C  1  112 ? 11.516  2.741   33.621 1.00 43.30  ? 125 PRO C CG  1 
ATOM   6054 C  CD  . PRO C  1  112 ? 11.706  1.259   33.364 1.00 43.94  ? 125 PRO C CD  1 
ATOM   6055 N  N   . ALA C  1  113 ? 8.332   0.552   31.886 1.00 46.39  ? 126 ALA C N   1 
ATOM   6056 C  CA  . ALA C  1  113 ? 7.245   0.322   30.943 1.00 46.81  ? 126 ALA C CA  1 
ATOM   6057 C  C   . ALA C  1  113 ? 5.991   -0.101  31.722 1.00 46.24  ? 126 ALA C C   1 
ATOM   6058 O  O   . ALA C  1  113 ? 6.108   -0.587  32.842 1.00 46.93  ? 126 ALA C O   1 
ATOM   6059 C  CB  . ALA C  1  113 ? 7.662   -0.726  29.929 1.00 45.40  ? 126 ALA C CB  1 
ATOM   6060 N  N   . HIS C  1  114 ? 4.797   0.083   31.139 1.00 46.70  ? 127 HIS C N   1 
ATOM   6061 C  CA  . HIS C  1  114 ? 3.550   -0.099  31.879 1.00 43.14  ? 127 HIS C CA  1 
ATOM   6062 C  C   . HIS C  1  114 ? 2.447   -0.799  31.078 1.00 45.13  ? 127 HIS C C   1 
ATOM   6063 O  O   . HIS C  1  114 ? 1.612   -1.475  31.677 1.00 47.50  ? 127 HIS C O   1 
ATOM   6064 C  CB  . HIS C  1  114 ? 3.050   1.246   32.412 1.00 43.98  ? 127 HIS C CB  1 
ATOM   6065 C  CG  . HIS C  1  114 ? 3.109   2.353   31.411 1.00 45.52  ? 127 HIS C CG  1 
ATOM   6066 N  ND1 . HIS C  1  114 ? 2.157   2.515   30.427 1.00 47.84  ? 127 HIS C ND1 1 
ATOM   6067 C  CD2 . HIS C  1  114 ? 3.995   3.346   31.242 1.00 43.69  ? 127 HIS C CD2 1 
ATOM   6068 C  CE1 . HIS C  1  114 ? 2.465   3.582   29.709 1.00 46.77  ? 127 HIS C CE1 1 
ATOM   6069 N  NE2 . HIS C  1  114 ? 3.577   4.104   30.187 1.00 46.36  ? 127 HIS C NE2 1 
ATOM   6070 N  N   . ALA C  1  115 ? 2.426   -0.642  29.744 1.00 45.41  ? 128 ALA C N   1 
ATOM   6071 C  CA  . ALA C  1  115 ? 1.323   -1.118  28.915 1.00 42.12  ? 128 ALA C CA  1 
ATOM   6072 C  C   . ALA C  1  115 ? -0.019  -0.682  29.506 1.00 37.40  ? 128 ALA C C   1 
ATOM   6073 O  O   . ALA C  1  115 ? -0.933  -1.476  29.592 1.00 36.80  ? 128 ALA C O   1 
ATOM   6074 C  CB  . ALA C  1  115 ? 1.400   -2.618  28.715 1.00 40.41  ? 128 ALA C CB  1 
ATOM   6075 N  N   . GLY C  1  116 ? -0.138  0.611   29.833 1.00 37.63  ? 129 GLY C N   1 
ATOM   6076 C  CA  . GLY C  1  116 ? -1.262  1.146   30.589 1.00 39.71  ? 129 GLY C CA  1 
ATOM   6077 C  C   . GLY C  1  116 ? -2.419  1.655   29.721 1.00 43.25  ? 129 GLY C C   1 
ATOM   6078 O  O   . GLY C  1  116 ? -3.440  2.077   30.263 1.00 43.60  ? 129 GLY C O   1 
ATOM   6079 N  N   . GLY C  1  117 ? -2.257  1.643   28.382 1.00 40.76  ? 130 GLY C N   1 
ATOM   6080 C  CA  . GLY C  1  117 ? -3.318  1.988   27.447 1.00 36.97  ? 130 GLY C CA  1 
ATOM   6081 C  C   . GLY C  1  117 ? -3.267  3.463   27.049 1.00 35.25  ? 130 GLY C C   1 
ATOM   6082 O  O   . GLY C  1  117 ? -2.426  4.206   27.547 1.00 33.55  ? 130 GLY C O   1 
ATOM   6083 N  N   . LEU C  1  118 ? -4.185  3.869   26.157 1.00 35.31  ? 131 LEU C N   1 
ATOM   6084 C  CA  . LEU C  1  118 ? -4.196  5.205   25.577 1.00 37.77  ? 131 LEU C CA  1 
ATOM   6085 C  C   . LEU C  1  118 ? -4.532  6.263   26.627 1.00 39.18  ? 131 LEU C C   1 
ATOM   6086 O  O   . LEU C  1  118 ? -4.319  7.447   26.385 1.00 38.97  ? 131 LEU C O   1 
ATOM   6087 C  CB  . LEU C  1  118 ? -5.155  5.245   24.382 1.00 39.91  ? 131 LEU C CB  1 
ATOM   6088 C  CG  . LEU C  1  118 ? -4.734  4.426   23.156 1.00 42.00  ? 131 LEU C CG  1 
ATOM   6089 C  CD1 . LEU C  1  118 ? -5.699  4.633   21.988 1.00 42.52  ? 131 LEU C CD1 1 
ATOM   6090 C  CD2 . LEU C  1  118 ? -3.308  4.756   22.729 1.00 39.92  ? 131 LEU C CD2 1 
ATOM   6091 N  N   . ASN C  1  119 ? -5.065  5.831   27.785 1.00 41.61  ? 132 ASN C N   1 
ATOM   6092 C  CA  . ASN C  1  119 ? -5.382  6.726   28.889 1.00 46.85  ? 132 ASN C CA  1 
ATOM   6093 C  C   . ASN C  1  119 ? -4.147  7.309   29.580 1.00 45.02  ? 132 ASN C C   1 
ATOM   6094 O  O   . ASN C  1  119 ? -4.282  8.287   30.304 1.00 46.37  ? 132 ASN C O   1 
ATOM   6095 C  CB  . ASN C  1  119 ? -6.177  6.035   29.991 1.00 49.53  ? 132 ASN C CB  1 
ATOM   6096 C  CG  . ASN C  1  119 ? -7.660  5.908   29.707 1.00 53.16  ? 132 ASN C CG  1 
ATOM   6097 O  OD1 . ASN C  1  119 ? -8.154  6.246   28.627 1.00 49.67  ? 132 ASN C OD1 1 
ATOM   6098 N  ND2 . ASN C  1  119 ? -8.400  5.387   30.671 1.00 53.76  ? 132 ASN C ND2 1 
ATOM   6099 N  N   . VAL C  1  120 ? -2.961  6.716   29.414 1.00 44.88  ? 133 VAL C N   1 
ATOM   6100 C  CA  . VAL C  1  120 ? -1.776  7.213   30.108 1.00 46.04  ? 133 VAL C CA  1 
ATOM   6101 C  C   . VAL C  1  120 ? -1.463  8.636   29.627 1.00 46.04  ? 133 VAL C C   1 
ATOM   6102 O  O   . VAL C  1  120 ? -1.248  8.871   28.441 1.00 44.23  ? 133 VAL C O   1 
ATOM   6103 C  CB  . VAL C  1  120 ? -0.566  6.273   29.934 1.00 45.05  ? 133 VAL C CB  1 
ATOM   6104 C  CG1 . VAL C  1  120 ? 0.738   6.883   30.452 1.00 44.98  ? 133 VAL C CG1 1 
ATOM   6105 C  CG2 . VAL C  1  120 ? -0.819  4.918   30.575 1.00 41.98  ? 133 VAL C CG2 1 
ATOM   6106 N  N   . HIS C  1  121 ? -1.419  9.577   30.577 1.00 47.03  ? 134 HIS C N   1 
ATOM   6107 C  CA  . HIS C  1  121 ? -1.148  10.980  30.298 1.00 45.96  ? 134 HIS C CA  1 
ATOM   6108 C  C   . HIS C  1  121 ? 0.353   11.241  30.211 1.00 46.08  ? 134 HIS C C   1 
ATOM   6109 O  O   . HIS C  1  121 ? 1.115   10.636  30.954 1.00 47.19  ? 134 HIS C O   1 
ATOM   6110 C  CB  . HIS C  1  121 ? -1.764  11.847  31.402 1.00 44.69  ? 134 HIS C CB  1 
ATOM   6111 C  CG  . HIS C  1  121 ? -1.469  13.306  31.281 1.00 44.93  ? 134 HIS C CG  1 
ATOM   6112 N  ND1 . HIS C  1  121 ? -2.039  14.123  30.329 1.00 50.55  ? 134 HIS C ND1 1 
ATOM   6113 C  CD2 . HIS C  1  121 ? -0.629  14.071  31.975 1.00 43.60  ? 134 HIS C CD2 1 
ATOM   6114 C  CE1 . HIS C  1  121 ? -1.563  15.348  30.480 1.00 54.50  ? 134 HIS C CE1 1 
ATOM   6115 N  NE2 . HIS C  1  121 ? -0.696  15.334  31.468 1.00 51.86  ? 134 HIS C NE2 1 
ATOM   6116 N  N   . GLY C  1  122 ? 0.777   12.143  29.314 1.00 49.67  ? 135 GLY C N   1 
ATOM   6117 C  CA  . GLY C  1  122 ? 2.102   12.726  29.439 1.00 56.66  ? 135 GLY C CA  1 
ATOM   6118 C  C   . GLY C  1  122 ? 3.000   12.605  28.208 1.00 57.85  ? 135 GLY C C   1 
ATOM   6119 O  O   . GLY C  1  122 ? 3.812   13.495  27.989 1.00 61.50  ? 135 GLY C O   1 
ATOM   6120 N  N   . THR C  1  123 ? 2.898   11.521  27.435 1.00 58.19  ? 136 THR C N   1 
ATOM   6121 C  CA  . THR C  1  123 ? 3.686   11.424  26.210 1.00 68.46  ? 136 THR C CA  1 
ATOM   6122 C  C   . THR C  1  123 ? 2.788   11.340  24.968 1.00 61.32  ? 136 THR C C   1 
ATOM   6123 O  O   . THR C  1  123 ? 3.155   11.915  23.952 1.00 67.13  ? 136 THR C O   1 
ATOM   6124 C  CB  . THR C  1  123 ? 4.680   10.263  26.287 1.00 75.55  ? 136 THR C CB  1 
ATOM   6125 O  OG1 . THR C  1  123 ? 5.205   10.215  27.611 1.00 73.91  ? 136 THR C OG1 1 
ATOM   6126 C  CG2 . THR C  1  123 ? 5.852   10.449  25.338 1.00 71.25  ? 136 THR C CG2 1 
ATOM   6127 N  N   . PHE C  1  124 ? 1.629   10.659  25.034 1.00 53.29  ? 137 PHE C N   1 
ATOM   6128 C  CA  . PHE C  1  124 ? 0.655   10.707  23.949 1.00 52.45  ? 137 PHE C CA  1 
ATOM   6129 C  C   . PHE C  1  124 ? -0.558  11.568  24.315 1.00 50.27  ? 137 PHE C C   1 
ATOM   6130 O  O   . PHE C  1  124 ? -0.646  12.715  23.873 1.00 47.86  ? 137 PHE C O   1 
ATOM   6131 C  CB  . PHE C  1  124 ? 0.245   9.291   23.538 1.00 52.38  ? 137 PHE C CB  1 
ATOM   6132 C  CG  . PHE C  1  124 ? -0.395  9.155   22.160 1.00 48.07  ? 137 PHE C CG  1 
ATOM   6133 C  CD1 . PHE C  1  124 ? -0.869  10.248  21.443 1.00 48.06  ? 137 PHE C CD1 1 
ATOM   6134 C  CD2 . PHE C  1  124 ? -0.521  7.903   21.586 1.00 47.52  ? 137 PHE C CD2 1 
ATOM   6135 C  CE1 . PHE C  1  124 ? -1.452  10.086  20.197 1.00 48.68  ? 137 PHE C CE1 1 
ATOM   6136 C  CE2 . PHE C  1  124 ? -1.099  7.750   20.343 1.00 45.32  ? 137 PHE C CE2 1 
ATOM   6137 C  CZ  . PHE C  1  124 ? -1.559  8.842   19.649 1.00 46.00  ? 137 PHE C CZ  1 
ATOM   6138 N  N   . GLU C  1  125 ? -1.518  11.006  25.071 1.00 51.15  ? 138 GLU C N   1 
ATOM   6139 C  CA  . GLU C  1  125 ? -2.684  11.748  25.534 1.00 49.19  ? 138 GLU C CA  1 
ATOM   6140 C  C   . GLU C  1  125 ? -2.226  13.009  26.264 1.00 49.91  ? 138 GLU C C   1 
ATOM   6141 O  O   . GLU C  1  125 ? -1.314  12.945  27.084 1.00 49.86  ? 138 GLU C O   1 
ATOM   6142 C  CB  . GLU C  1  125 ? -3.525  10.880  26.470 1.00 49.02  ? 138 GLU C CB  1 
ATOM   6143 C  CG  . GLU C  1  125 ? -4.859  11.507  26.885 1.00 52.74  ? 138 GLU C CG  1 
ATOM   6144 C  CD  . GLU C  1  125 ? -4.777  12.714  27.819 1.00 57.34  ? 138 GLU C CD  1 
ATOM   6145 O  OE1 . GLU C  1  125 ? -4.021  12.629  28.832 1.00 49.38  ? 138 GLU C OE1 1 
ATOM   6146 O  OE2 . GLU C  1  125 ? -5.475  13.736  27.534 1.00 55.73  ? 138 GLU C OE2 1 
ATOM   6147 N  N   . GLY C  1  126 ? -2.865  14.148  25.965 1.00 47.41  ? 139 GLY C N   1 
ATOM   6148 C  CA  . GLY C  1  126 ? -2.547  15.397  26.644 1.00 49.15  ? 139 GLY C CA  1 
ATOM   6149 C  C   . GLY C  1  126 ? -3.713  16.386  26.675 1.00 46.98  ? 139 GLY C C   1 
ATOM   6150 O  O   . GLY C  1  126 ? -4.877  16.004  26.522 1.00 45.26  ? 139 GLY C O   1 
ATOM   6151 N  N   . ASP C  1  127 ? -3.344  17.672  26.803 1.00 51.92  ? 140 ASP C N   1 
ATOM   6152 C  CA  . ASP C  1  127 ? -4.206  18.729  27.319 1.00 55.02  ? 140 ASP C CA  1 
ATOM   6153 C  C   . ASP C  1  127 ? -4.824  19.547  26.184 1.00 58.71  ? 140 ASP C C   1 
ATOM   6154 O  O   . ASP C  1  127 ? -4.352  19.512  25.044 1.00 61.10  ? 140 ASP C O   1 
ATOM   6155 C  CB  . ASP C  1  127 ? -3.426  19.680  28.224 1.00 52.97  ? 140 ASP C CB  1 
ATOM   6156 C  CG  . ASP C  1  127 ? -2.776  19.076  29.463 1.00 52.35  ? 140 ASP C CG  1 
ATOM   6157 O  OD1 . ASP C  1  127 ? -3.381  18.139  30.039 1.00 44.28  ? 140 ASP C OD1 1 
ATOM   6158 O  OD2 . ASP C  1  127 ? -1.661  19.551  29.849 1.00 52.55  ? 140 ASP C OD2 1 
ATOM   6159 N  N   . ALA C  1  128 ? -5.863  20.321  26.534 1.00 53.96  ? 141 ALA C N   1 
ATOM   6160 C  CA  . ALA C  1  128 ? -6.532  21.236  25.616 1.00 53.17  ? 141 ALA C CA  1 
ATOM   6161 C  C   . ALA C  1  128 ? -7.272  20.469  24.516 1.00 55.02  ? 141 ALA C C   1 
ATOM   6162 O  O   . ALA C  1  128 ? -7.336  20.910  23.371 1.00 58.93  ? 141 ALA C O   1 
ATOM   6163 C  CB  . ALA C  1  128 ? -5.553  22.262  25.060 1.00 49.34  ? 141 ALA C CB  1 
ATOM   6164 N  N   . GLY C  1  129 ? -7.884  19.341  24.889 1.00 53.41  ? 142 GLY C N   1 
ATOM   6165 C  CA  . GLY C  1  129 ? -8.755  18.607  23.990 1.00 54.59  ? 142 GLY C CA  1 
ATOM   6166 C  C   . GLY C  1  129 ? -10.112 19.292  23.823 1.00 58.71  ? 142 GLY C C   1 
ATOM   6167 O  O   . GLY C  1  129 ? -10.430 20.245  24.522 1.00 65.67  ? 142 GLY C O   1 
ATOM   6168 N  N   . MET C  1  130 ? -10.921 18.777  22.896 1.00 61.49  ? 143 MET C N   1 
ATOM   6169 C  CA  . MET C  1  130 ? -12.190 19.388  22.534 1.00 58.96  ? 143 MET C CA  1 
ATOM   6170 C  C   . MET C  1  130 ? -13.322 18.914  23.451 1.00 59.68  ? 143 MET C C   1 
ATOM   6171 O  O   . MET C  1  130 ? -14.132 19.741  23.867 1.00 59.94  ? 143 MET C O   1 
ATOM   6172 C  CB  . MET C  1  130 ? -12.531 19.074  21.073 1.00 62.22  ? 143 MET C CB  1 
ATOM   6173 C  CG  . MET C  1  130 ? -11.603 19.750  20.066 1.00 64.80  ? 143 MET C CG  1 
ATOM   6174 S  SD  . MET C  1  130 ? -11.951 19.271  18.362 1.00 64.60  ? 143 MET C SD  1 
ATOM   6175 C  CE  . MET C  1  130 ? -11.589 17.509  18.325 1.00 54.85  ? 143 MET C CE  1 
ATOM   6176 N  N   . THR C  1  131 ? -13.401 17.599  23.731 1.00 54.15  ? 144 THR C N   1 
ATOM   6177 C  CA  . THR C  1  131 ? -14.494 17.041  24.516 1.00 54.87  ? 144 THR C CA  1 
ATOM   6178 C  C   . THR C  1  131 ? -13.993 16.285  25.750 1.00 51.71  ? 144 THR C C   1 
ATOM   6179 O  O   . THR C  1  131 ? -14.806 15.704  26.474 1.00 49.73  ? 144 THR C O   1 
ATOM   6180 C  CB  . THR C  1  131 ? -15.366 16.148  23.632 1.00 57.12  ? 144 THR C CB  1 
ATOM   6181 O  OG1 . THR C  1  131 ? -14.645 14.971  23.280 1.00 51.01  ? 144 THR C OG1 1 
ATOM   6182 C  CG2 . THR C  1  131 ? -15.816 16.875  22.380 1.00 60.63  ? 144 THR C CG2 1 
ATOM   6183 N  N   . ARG C  1  132 ? -12.672 16.300  25.983 1.00 47.93  ? 145 ARG C N   1 
ATOM   6184 C  CA  . ARG C  1  132 ? -12.083 15.691  27.167 1.00 48.83  ? 145 ARG C CA  1 
ATOM   6185 C  C   . ARG C  1  132 ? -11.314 16.750  27.956 1.00 50.57  ? 145 ARG C C   1 
ATOM   6186 O  O   . ARG C  1  132 ? -10.679 17.619  27.361 1.00 48.00  ? 145 ARG C O   1 
ATOM   6187 C  CB  . ARG C  1  132 ? -11.164 14.527  26.789 1.00 48.21  ? 145 ARG C CB  1 
ATOM   6188 C  CG  . ARG C  1  132 ? -11.846 13.172  26.689 1.00 49.45  ? 145 ARG C CG  1 
ATOM   6189 C  CD  . ARG C  1  132 ? -12.740 13.032  25.461 1.00 50.51  ? 145 ARG C CD  1 
ATOM   6190 N  NE  . ARG C  1  132 ? -13.377 11.709  25.459 1.00 51.59  ? 145 ARG C NE  1 
ATOM   6191 C  CZ  . ARG C  1  132 ? -14.470 11.357  24.791 1.00 49.67  ? 145 ARG C CZ  1 
ATOM   6192 N  NH1 . ARG C  1  132 ? -15.092 12.220  24.007 1.00 47.43  ? 145 ARG C NH1 1 
ATOM   6193 N  NH2 . ARG C  1  132 ? -14.963 10.145  24.940 1.00 51.05  ? 145 ARG C NH2 1 
ATOM   6194 N  N   . ALA C  1  133 ? -11.378 16.656  29.296 1.00 54.28  ? 146 ALA C N   1 
ATOM   6195 C  CA  . ALA C  1  133 ? -10.714 17.593  30.191 1.00 52.73  ? 146 ALA C CA  1 
ATOM   6196 C  C   . ALA C  1  133 ? -9.271  17.155  30.442 1.00 50.24  ? 146 ALA C C   1 
ATOM   6197 O  O   . ALA C  1  133 ? -8.961  15.964  30.388 1.00 45.19  ? 146 ALA C O   1 
ATOM   6198 N  N   . ASP C  1  134 ? -8.414  18.143  30.747 1.00 51.28  ? 147 ASP C N   1 
ATOM   6199 C  CA  . ASP C  1  134 ? -7.026  17.918  31.115 1.00 53.84  ? 147 ASP C CA  1 
ATOM   6200 C  C   . ASP C  1  134 ? -6.946  16.968  32.309 1.00 58.41  ? 147 ASP C C   1 
ATOM   6201 O  O   . ASP C  1  134 ? -7.805  17.013  33.191 1.00 58.39  ? 147 ASP C O   1 
ATOM   6202 C  CB  . ASP C  1  134 ? -6.325  19.225  31.447 1.00 53.47  ? 147 ASP C CB  1 
ATOM   6203 C  CG  . ASP C  1  134 ? -6.255  20.252  30.327 1.00 53.75  ? 147 ASP C CG  1 
ATOM   6204 O  OD1 . ASP C  1  134 ? -6.891  20.026  29.277 1.00 55.70  ? 147 ASP C OD1 1 
ATOM   6205 O  OD2 . ASP C  1  134 ? -5.532  21.256  30.499 1.00 54.95  ? 147 ASP C OD2 1 
ATOM   6206 N  N   . GLU C  1  135 ? -5.885  16.143  32.339 1.00 55.93  ? 148 GLU C N   1 
ATOM   6207 C  CA  . GLU C  1  135 ? -5.699  15.137  33.374 1.00 59.23  ? 148 GLU C CA  1 
ATOM   6208 C  C   . GLU C  1  135 ? -5.635  15.785  34.761 1.00 59.30  ? 148 GLU C C   1 
ATOM   6209 O  O   . GLU C  1  135 ? -6.059  15.189  35.750 1.00 53.23  ? 148 GLU C O   1 
ATOM   6210 C  CB  . GLU C  1  135 ? -4.446  14.314  33.063 1.00 61.96  ? 148 GLU C CB  1 
ATOM   6211 C  CG  . GLU C  1  135 ? -4.210  13.169  34.046 1.00 66.60  ? 148 GLU C CG  1 
ATOM   6212 C  CD  . GLU C  1  135 ? -3.368  13.511  35.262 1.00 75.63  ? 148 GLU C CD  1 
ATOM   6213 O  OE1 . GLU C  1  135 ? -2.705  14.578  35.312 1.00 83.30  ? 148 GLU C OE1 1 
ATOM   6214 O  OE2 . GLU C  1  135 ? -3.391  12.665  36.176 1.00 85.18  ? 148 GLU C OE2 1 
ATOM   6215 N  N   . PHE C  1  136 ? -5.097  17.008  34.834 1.00 62.19  ? 149 PHE C N   1 
ATOM   6216 C  CA  . PHE C  1  136 ? -4.976  17.726  36.093 1.00 68.68  ? 149 PHE C CA  1 
ATOM   6217 C  C   . PHE C  1  136 ? -6.315  17.759  36.832 1.00 69.78  ? 149 PHE C C   1 
ATOM   6218 O  O   . PHE C  1  136 ? -6.332  17.738  38.056 1.00 72.63  ? 149 PHE C O   1 
ATOM   6219 C  CB  . PHE C  1  136 ? -4.470  19.155  35.878 1.00 71.08  ? 149 PHE C CB  1 
ATOM   6220 C  CG  . PHE C  1  136 ? -4.366  19.948  37.173 1.00 78.25  ? 149 PHE C CG  1 
ATOM   6221 C  CD1 . PHE C  1  136 ? -3.330  19.711  38.076 1.00 81.52  ? 149 PHE C CD1 1 
ATOM   6222 C  CD2 . PHE C  1  136 ? -5.305  20.927  37.488 1.00 81.93  ? 149 PHE C CD2 1 
ATOM   6223 C  CE1 . PHE C  1  136 ? -3.242  20.438  39.257 1.00 79.98  ? 149 PHE C CE1 1 
ATOM   6224 C  CE2 . PHE C  1  136 ? -5.208  21.654  38.667 1.00 76.90  ? 149 PHE C CE2 1 
ATOM   6225 C  CZ  . PHE C  1  136 ? -4.178  21.409  39.548 1.00 77.34  ? 149 PHE C CZ  1 
ATOM   6226 N  N   . PHE C  1  137 ? -7.433  17.818  36.093 1.00 66.78  ? 150 PHE C N   1 
ATOM   6227 C  CA  . PHE C  1  137 ? -8.745  17.966  36.703 1.00 60.42  ? 150 PHE C CA  1 
ATOM   6228 C  C   . PHE C  1  137 ? -9.371  16.613  37.043 1.00 58.34  ? 150 PHE C C   1 
ATOM   6229 O  O   . PHE C  1  137 ? -10.501 16.592  37.523 1.00 57.15  ? 150 PHE C O   1 
ATOM   6230 C  CB  . PHE C  1  137 ? -9.693  18.747  35.792 1.00 60.68  ? 150 PHE C CB  1 
ATOM   6231 C  CG  . PHE C  1  137 ? -9.176  20.111  35.369 1.00 67.24  ? 150 PHE C CG  1 
ATOM   6232 C  CD1 . PHE C  1  137 ? -8.765  21.046  36.311 1.00 69.38  ? 150 PHE C CD1 1 
ATOM   6233 C  CD2 . PHE C  1  137 ? -9.061  20.434  34.022 1.00 70.92  ? 150 PHE C CD2 1 
ATOM   6234 C  CE1 . PHE C  1  137 ? -8.268  22.277  35.914 1.00 75.97  ? 150 PHE C CE1 1 
ATOM   6235 C  CE2 . PHE C  1  137 ? -8.580  21.673  33.628 1.00 68.34  ? 150 PHE C CE2 1 
ATOM   6236 C  CZ  . PHE C  1  137 ? -8.172  22.588  34.573 1.00 77.13  ? 150 PHE C CZ  1 
ATOM   6237 N  N   . GLY C  1  138 ? -8.696  15.488  36.761 1.00 59.58  ? 151 GLY C N   1 
ATOM   6238 C  CA  . GLY C  1  138 ? -9.079  14.221  37.369 1.00 59.12  ? 151 GLY C CA  1 
ATOM   6239 C  C   . GLY C  1  138 ? -9.531  13.135  36.390 1.00 61.64  ? 151 GLY C C   1 
ATOM   6240 O  O   . GLY C  1  138 ? -9.535  11.966  36.766 1.00 61.09  ? 151 GLY C O   1 
ATOM   6241 N  N   . ASP C  1  139 ? -9.897  13.489  35.148 1.00 63.00  ? 152 ASP C N   1 
ATOM   6242 C  CA  . ASP C  1  139 ? -10.415 12.508  34.198 1.00 63.41  ? 152 ASP C CA  1 
ATOM   6243 C  C   . ASP C  1  139 ? -10.096 12.941  32.768 1.00 58.60  ? 152 ASP C C   1 
ATOM   6244 O  O   . ASP C  1  139 ? -10.689 13.893  32.267 1.00 55.39  ? 152 ASP C O   1 
ATOM   6245 C  CB  . ASP C  1  139 ? -11.906 12.285  34.396 1.00 65.28  ? 152 ASP C CB  1 
ATOM   6246 C  CG  . ASP C  1  139 ? -12.563 11.256  33.480 1.00 67.36  ? 152 ASP C CG  1 
ATOM   6247 O  OD1 . ASP C  1  139 ? -11.949 10.881  32.469 1.00 67.74  ? 152 ASP C OD1 1 
ATOM   6248 O  OD2 . ASP C  1  139 ? -13.674 10.808  33.801 1.00 67.77  ? 152 ASP C OD2 1 
ATOM   6249 N  N   . ASN C  1  140 ? -9.168  12.222  32.119 1.00 53.70  ? 153 ASN C N   1 
ATOM   6250 C  CA  . ASN C  1  140 ? -8.640  12.647  30.831 1.00 51.48  ? 153 ASN C CA  1 
ATOM   6251 C  C   . ASN C  1  140 ? -9.287  11.890  29.674 1.00 49.05  ? 153 ASN C C   1 
ATOM   6252 O  O   . ASN C  1  140 ? -8.889  12.095  28.533 1.00 55.02  ? 153 ASN C O   1 
ATOM   6253 C  CB  . ASN C  1  140 ? -7.122  12.489  30.768 1.00 48.38  ? 153 ASN C CB  1 
ATOM   6254 C  CG  . ASN C  1  140 ? -6.660  11.052  30.851 1.00 44.90  ? 153 ASN C CG  1 
ATOM   6255 O  OD1 . ASN C  1  140 ? -7.436  10.151  31.175 1.00 43.91  ? 153 ASN C OD1 1 
ATOM   6256 N  ND2 . ASN C  1  140 ? -5.387  10.819  30.566 1.00 48.51  ? 153 ASN C ND2 1 
ATOM   6257 N  N   . HIS C  1  141 ? -10.270 11.026  29.966 1.00 49.29  ? 154 HIS C N   1 
ATOM   6258 C  CA  . HIS C  1  141 ? -10.763 10.061  28.991 1.00 53.27  ? 154 HIS C CA  1 
ATOM   6259 C  C   . HIS C  1  141 ? -12.270 10.188  28.751 1.00 56.25  ? 154 HIS C C   1 
ATOM   6260 O  O   . HIS C  1  141 ? -12.713 9.959   27.631 1.00 56.76  ? 154 HIS C O   1 
ATOM   6261 C  CB  . HIS C  1  141 ? -10.337 8.636   29.368 1.00 54.74  ? 154 HIS C CB  1 
ATOM   6262 C  CG  . HIS C  1  141 ? -10.763 8.220   30.725 1.00 63.31  ? 154 HIS C CG  1 
ATOM   6263 N  ND1 . HIS C  1  141 ? -9.958  8.383   31.832 1.00 66.13  ? 154 HIS C ND1 1 
ATOM   6264 C  CD2 . HIS C  1  141 ? -11.905 7.666   31.161 1.00 68.62  ? 154 HIS C CD2 1 
ATOM   6265 C  CE1 . HIS C  1  141 ? -10.607 7.941   32.901 1.00 69.71  ? 154 HIS C CE1 1 
ATOM   6266 N  NE2 . HIS C  1  141 ? -11.794 7.508   32.517 1.00 63.57  ? 154 HIS C NE2 1 
ATOM   6267 N  N   . SER C  1  142 ? -13.049 10.530  29.786 1.00 54.63  ? 155 SER C N   1 
ATOM   6268 C  CA  . SER C  1  142 ? -14.500 10.599  29.683 1.00 52.03  ? 155 SER C CA  1 
ATOM   6269 C  C   . SER C  1  142 ? -14.949 11.816  28.882 1.00 53.44  ? 155 SER C C   1 
ATOM   6270 O  O   . SER C  1  142 ? -14.349 12.892  28.966 1.00 52.45  ? 155 SER C O   1 
ATOM   6271 C  CB  . SER C  1  142 ? -15.150 10.629  31.043 1.00 56.84  ? 155 SER C CB  1 
ATOM   6272 O  OG  . SER C  1  142 ? -15.045 9.365   31.686 1.00 62.03  ? 155 SER C OG  1 
ATOM   6273 N  N   . PHE C  1  143 ? -16.046 11.635  28.131 1.00 51.07  ? 156 PHE C N   1 
ATOM   6274 C  CA  . PHE C  1  143 ? -16.747 12.747  27.506 1.00 55.04  ? 156 PHE C CA  1 
ATOM   6275 C  C   . PHE C  1  143 ? -17.215 13.745  28.570 1.00 56.32  ? 156 PHE C C   1 
ATOM   6276 O  O   . PHE C  1  143 ? -17.779 13.345  29.580 1.00 53.09  ? 156 PHE C O   1 
ATOM   6277 C  CB  . PHE C  1  143 ? -17.952 12.230  26.716 1.00 57.75  ? 156 PHE C CB  1 
ATOM   6278 C  CG  . PHE C  1  143 ? -18.852 13.326  26.158 1.00 57.62  ? 156 PHE C CG  1 
ATOM   6279 C  CD1 . PHE C  1  143 ? -18.559 13.939  24.947 1.00 55.82  ? 156 PHE C CD1 1 
ATOM   6280 C  CD2 . PHE C  1  143 ? -19.982 13.751  26.859 1.00 61.01  ? 156 PHE C CD2 1 
ATOM   6281 C  CE1 . PHE C  1  143 ? -19.387 14.936  24.442 1.00 58.86  ? 156 PHE C CE1 1 
ATOM   6282 C  CE2 . PHE C  1  143 ? -20.803 14.752  26.355 1.00 63.31  ? 156 PHE C CE2 1 
ATOM   6283 C  CZ  . PHE C  1  143 ? -20.512 15.334  25.140 1.00 61.92  ? 156 PHE C CZ  1 
ATOM   6284 N  N   . ASN C  1  144 ? -17.028 15.041  28.287 1.00 59.33  ? 157 ASN C N   1 
ATOM   6285 C  CA  . ASN C  1  144 ? -17.298 16.138  29.204 1.00 60.90  ? 157 ASN C CA  1 
ATOM   6286 C  C   . ASN C  1  144 ? -18.292 17.107  28.561 1.00 63.17  ? 157 ASN C C   1 
ATOM   6287 O  O   . ASN C  1  144 ? -17.945 17.797  27.602 1.00 57.53  ? 157 ASN C O   1 
ATOM   6288 C  CB  . ASN C  1  144 ? -15.989 16.840  29.535 1.00 69.79  ? 157 ASN C CB  1 
ATOM   6289 C  CG  . ASN C  1  144 ? -16.122 18.069  30.405 1.00 74.13  ? 157 ASN C CG  1 
ATOM   6290 O  OD1 . ASN C  1  144 ? -16.984 18.922  30.162 1.00 66.84  ? 157 ASN C OD1 1 
ATOM   6291 N  ND2 . ASN C  1  144 ? -15.222 18.201  31.373 1.00 79.61  ? 157 ASN C ND2 1 
ATOM   6292 N  N   . GLN C  1  145 ? -19.498 17.197  29.142 1.00 67.98  ? 158 GLN C N   1 
ATOM   6293 C  CA  . GLN C  1  145 ? -20.602 17.964  28.575 1.00 69.12  ? 158 GLN C CA  1 
ATOM   6294 C  C   . GLN C  1  145 ? -20.297 19.466  28.546 1.00 63.45  ? 158 GLN C C   1 
ATOM   6295 O  O   . GLN C  1  145 ? -20.688 20.155  27.603 1.00 70.70  ? 158 GLN C O   1 
ATOM   6296 C  CB  . GLN C  1  145 ? -21.900 17.702  29.345 1.00 69.62  ? 158 GLN C CB  1 
ATOM   6297 C  CG  . GLN C  1  145 ? -23.147 18.356  28.747 1.00 69.18  ? 158 GLN C CG  1 
ATOM   6298 C  CD  . GLN C  1  145 ? -23.558 17.806  27.392 1.00 67.55  ? 158 GLN C CD  1 
ATOM   6299 O  OE1 . GLN C  1  145 ? -23.713 16.592  27.209 1.00 64.33  ? 158 GLN C OE1 1 
ATOM   6300 N  NE2 . GLN C  1  145 ? -23.764 18.691  26.424 1.00 67.18  ? 158 GLN C NE2 1 
ATOM   6301 N  N   . THR C  1  146 ? -19.606 19.970  29.576 1.00 60.52  ? 159 THR C N   1 
ATOM   6302 C  CA  . THR C  1  146 ? -19.256 21.382  29.649 1.00 61.66  ? 159 THR C CA  1 
ATOM   6303 C  C   . THR C  1  146 ? -18.429 21.763  28.426 1.00 64.64  ? 159 THR C C   1 
ATOM   6304 O  O   . THR C  1  146 ? -18.689 22.794  27.813 1.00 63.51  ? 159 THR C O   1 
ATOM   6305 C  CB  . THR C  1  146 ? -18.505 21.694  30.944 1.00 62.40  ? 159 THR C CB  1 
ATOM   6306 O  OG1 . THR C  1  146 ? -19.349 21.278  32.014 1.00 63.81  ? 159 THR C OG1 1 
ATOM   6307 C  CG2 . THR C  1  146 ? -18.163 23.168  31.084 1.00 61.45  ? 159 THR C CG2 1 
ATOM   6308 N  N   . LEU C  1  147 ? -17.440 20.924  28.078 1.00 67.76  ? 160 LEU C N   1 
ATOM   6309 C  CA  . LEU C  1  147 ? -16.577 21.191  26.935 1.00 62.50  ? 160 LEU C CA  1 
ATOM   6310 C  C   . LEU C  1  147 ? -17.347 21.029  25.627 1.00 58.95  ? 160 LEU C C   1 
ATOM   6311 O  O   . LEU C  1  147 ? -17.125 21.803  24.699 1.00 60.30  ? 160 LEU C O   1 
ATOM   6312 C  CB  . LEU C  1  147 ? -15.327 20.315  26.978 1.00 62.73  ? 160 LEU C CB  1 
ATOM   6313 C  CG  . LEU C  1  147 ? -14.316 20.684  28.069 1.00 62.94  ? 160 LEU C CG  1 
ATOM   6314 C  CD1 . LEU C  1  147 ? -13.160 19.694  28.066 1.00 64.38  ? 160 LEU C CD1 1 
ATOM   6315 C  CD2 . LEU C  1  147 ? -13.818 22.119  27.913 1.00 62.81  ? 160 LEU C CD2 1 
ATOM   6316 N  N   . PHE C  1  148 ? -18.277 20.069  25.566 1.00 54.13  ? 161 PHE C N   1 
ATOM   6317 C  CA  . PHE C  1  148 ? -19.093 19.906  24.372 1.00 60.89  ? 161 PHE C CA  1 
ATOM   6318 C  C   . PHE C  1  148 ? -19.985 21.132  24.167 1.00 66.86  ? 161 PHE C C   1 
ATOM   6319 O  O   . PHE C  1  148 ? -20.262 21.497  23.026 1.00 68.08  ? 161 PHE C O   1 
ATOM   6320 C  CB  . PHE C  1  148 ? -19.926 18.623  24.403 1.00 66.22  ? 161 PHE C CB  1 
ATOM   6321 C  CG  . PHE C  1  148 ? -20.637 18.337  23.083 1.00 72.48  ? 161 PHE C CG  1 
ATOM   6322 C  CD1 . PHE C  1  148 ? -19.918 17.931  21.956 1.00 73.07  ? 161 PHE C CD1 1 
ATOM   6323 C  CD2 . PHE C  1  148 ? -22.017 18.468  22.973 1.00 69.91  ? 161 PHE C CD2 1 
ATOM   6324 C  CE1 . PHE C  1  148 ? -20.564 17.662  20.755 1.00 74.26  ? 161 PHE C CE1 1 
ATOM   6325 C  CE2 . PHE C  1  148 ? -22.659 18.192  21.769 1.00 77.01  ? 161 PHE C CE2 1 
ATOM   6326 C  CZ  . PHE C  1  148 ? -21.933 17.798  20.658 1.00 76.07  ? 161 PHE C CZ  1 
ATOM   6327 N  N   . ASP C  1  149 ? -20.427 21.769  25.263 1.00 67.89  ? 162 ASP C N   1 
ATOM   6328 C  CA  . ASP C  1  149 ? -21.252 22.966  25.168 1.00 62.52  ? 162 ASP C CA  1 
ATOM   6329 C  C   . ASP C  1  149 ? -20.451 24.099  24.532 1.00 59.21  ? 162 ASP C C   1 
ATOM   6330 O  O   . ASP C  1  149 ? -21.003 24.841  23.726 1.00 60.46  ? 162 ASP C O   1 
ATOM   6331 C  CB  . ASP C  1  149 ? -21.873 23.321  26.514 1.00 68.75  ? 162 ASP C CB  1 
ATOM   6332 C  CG  . ASP C  1  149 ? -22.970 22.380  27.001 1.00 71.89  ? 162 ASP C CG  1 
ATOM   6333 O  OD1 . ASP C  1  149 ? -23.588 21.702  26.154 1.00 68.79  ? 162 ASP C OD1 1 
ATOM   6334 O  OD2 . ASP C  1  149 ? -23.185 22.307  28.231 1.00 72.76  ? 162 ASP C OD2 1 
ATOM   6335 N  N   . LYS C  1  150 ? -19.157 24.213  24.876 1.00 60.85  ? 163 LYS C N   1 
ATOM   6336 C  CA  . LYS C  1  150 ? -18.263 25.193  24.268 1.00 60.02  ? 163 LYS C CA  1 
ATOM   6337 C  C   . LYS C  1  150 ? -18.077 24.884  22.779 1.00 66.86  ? 163 LYS C C   1 
ATOM   6338 O  O   . LYS C  1  150 ? -18.043 25.797  21.955 1.00 60.40  ? 163 LYS C O   1 
ATOM   6339 C  CB  . LYS C  1  150 ? -16.908 25.218  24.987 1.00 57.01  ? 163 LYS C CB  1 
ATOM   6340 C  CG  . LYS C  1  150 ? -15.954 26.331  24.559 1.00 60.08  ? 163 LYS C CG  1 
ATOM   6341 C  CD  . LYS C  1  150 ? -14.553 26.198  25.154 1.00 66.76  ? 163 LYS C CD  1 
ATOM   6342 C  CE  . LYS C  1  150 ? -13.621 27.358  24.930 1.00 69.71  ? 163 LYS C CE  1 
ATOM   6343 N  NZ  . LYS C  1  150 ? -13.742 28.367  25.982 1.00 80.92  ? 163 LYS C NZ  1 
ATOM   6344 N  N   . PHE C  1  151 ? -17.956 23.591  22.448 1.00 66.03  ? 164 PHE C N   1 
ATOM   6345 C  CA  . PHE C  1  151 ? -17.910 23.128  21.069 1.00 67.72  ? 164 PHE C CA  1 
ATOM   6346 C  C   . PHE C  1  151 ? -19.130 23.635  20.307 1.00 66.68  ? 164 PHE C C   1 
ATOM   6347 O  O   . PHE C  1  151 ? -19.001 24.122  19.188 1.00 61.73  ? 164 PHE C O   1 
ATOM   6348 C  CB  . PHE C  1  151 ? -17.905 21.595  21.039 1.00 70.48  ? 164 PHE C CB  1 
ATOM   6349 C  CG  . PHE C  1  151 ? -17.536 20.956  19.709 1.00 73.68  ? 164 PHE C CG  1 
ATOM   6350 C  CD1 . PHE C  1  151 ? -18.510 20.603  18.778 1.00 71.43  ? 164 PHE C CD1 1 
ATOM   6351 C  CD2 . PHE C  1  151 ? -16.208 20.664  19.418 1.00 77.42  ? 164 PHE C CD2 1 
ATOM   6352 C  CE1 . PHE C  1  151 ? -18.156 20.007  17.577 1.00 72.89  ? 164 PHE C CE1 1 
ATOM   6353 C  CE2 . PHE C  1  151 ? -15.864 20.059  18.222 1.00 80.62  ? 164 PHE C CE2 1 
ATOM   6354 C  CZ  . PHE C  1  151 ? -16.840 19.734  17.304 1.00 75.37  ? 164 PHE C CZ  1 
ATOM   6355 N  N   . VAL C  1  152 ? -20.316 23.470  20.911 1.00 62.86  ? 165 VAL C N   1 
ATOM   6356 C  CA  . VAL C  1  152 ? -21.569 23.872  20.289 1.00 64.81  ? 165 VAL C CA  1 
ATOM   6357 C  C   . VAL C  1  152 ? -21.611 25.394  20.160 1.00 63.50  ? 165 VAL C C   1 
ATOM   6358 O  O   . VAL C  1  152 ? -22.015 25.910  19.117 1.00 60.60  ? 165 VAL C O   1 
ATOM   6359 C  CB  . VAL C  1  152 ? -22.794 23.340  21.059 1.00 66.45  ? 165 VAL C CB  1 
ATOM   6360 C  CG1 . VAL C  1  152 ? -24.104 23.942  20.567 1.00 70.06  ? 165 VAL C CG1 1 
ATOM   6361 C  CG2 . VAL C  1  152 ? -22.883 21.824  20.982 1.00 67.77  ? 165 VAL C CG2 1 
ATOM   6362 N  N   . ASP C  1  153 ? -21.192 26.098  21.220 1.00 67.51  ? 166 ASP C N   1 
ATOM   6363 C  CA  . ASP C  1  153 ? -21.241 27.549  21.245 1.00 73.80  ? 166 ASP C CA  1 
ATOM   6364 C  C   . ASP C  1  153 ? -20.387 28.120  20.118 1.00 74.87  ? 166 ASP C C   1 
ATOM   6365 O  O   . ASP C  1  153 ? -20.855 28.970  19.366 1.00 76.85  ? 166 ASP C O   1 
ATOM   6366 C  CB  . ASP C  1  153 ? -20.852 28.109  22.606 1.00 80.72  ? 166 ASP C CB  1 
ATOM   6367 C  CG  . ASP C  1  153 ? -21.046 29.613  22.761 1.00 85.12  ? 166 ASP C CG  1 
ATOM   6368 O  OD1 . ASP C  1  153 ? -22.114 30.119  22.350 1.00 88.85  ? 166 ASP C OD1 1 
ATOM   6369 O  OD2 . ASP C  1  153 ? -20.149 30.267  23.323 1.00 84.23  ? 166 ASP C OD2 1 
ATOM   6370 N  N   . PHE C  1  154 ? -19.144 27.634  19.997 1.00 75.36  ? 167 PHE C N   1 
ATOM   6371 C  CA  . PHE C  1  154 ? -18.209 28.121  18.990 1.00 72.57  ? 167 PHE C CA  1 
ATOM   6372 C  C   . PHE C  1  154 ? -18.716 27.774  17.590 1.00 68.60  ? 167 PHE C C   1 
ATOM   6373 O  O   . PHE C  1  154 ? -18.514 28.547  16.665 1.00 63.36  ? 167 PHE C O   1 
ATOM   6374 C  CB  . PHE C  1  154 ? -16.799 27.573  19.234 1.00 68.88  ? 167 PHE C CB  1 
ATOM   6375 C  CG  . PHE C  1  154 ? -15.926 28.440  20.130 1.00 66.94  ? 167 PHE C CG  1 
ATOM   6376 C  CD1 . PHE C  1  154 ? -16.252 28.629  21.469 1.00 69.30  ? 167 PHE C CD1 1 
ATOM   6377 C  CD2 . PHE C  1  154 ? -14.760 29.033  19.640 1.00 64.59  ? 167 PHE C CD2 1 
ATOM   6378 C  CE1 . PHE C  1  154 ? -15.450 29.419  22.287 1.00 68.94  ? 167 PHE C CE1 1 
ATOM   6379 C  CE2 . PHE C  1  154 ? -13.957 29.813  20.461 1.00 62.24  ? 167 PHE C CE2 1 
ATOM   6380 C  CZ  . PHE C  1  154 ? -14.304 30.008  21.781 1.00 67.14  ? 167 PHE C CZ  1 
ATOM   6381 N  N   . SER C  1  155 ? -19.361 26.617  17.436 1.00 65.66  ? 168 SER C N   1 
ATOM   6382 C  CA  . SER C  1  155 ? -19.979 26.260  16.170 1.00 70.61  ? 168 SER C CA  1 
ATOM   6383 C  C   . SER C  1  155 ? -21.123 27.224  15.838 1.00 76.28  ? 168 SER C C   1 
ATOM   6384 O  O   . SER C  1  155 ? -21.307 27.585  14.674 1.00 74.98  ? 168 SER C O   1 
ATOM   6385 C  CB  . SER C  1  155 ? -20.457 24.825  16.172 1.00 72.26  ? 168 SER C CB  1 
ATOM   6386 O  OG  . SER C  1  155 ? -19.400 23.918  16.449 1.00 71.21  ? 168 SER C OG  1 
ATOM   6387 N  N   . ASN C  1  156 ? -21.901 27.630  16.857 1.00 75.06  ? 169 ASN C N   1 
ATOM   6388 C  CA  . ASN C  1  156 ? -22.966 28.608  16.668 1.00 69.59  ? 169 ASN C CA  1 
ATOM   6389 C  C   . ASN C  1  156 ? -22.364 29.958  16.281 1.00 64.26  ? 169 ASN C C   1 
ATOM   6390 O  O   . ASN C  1  156 ? -22.877 30.636  15.403 1.00 61.75  ? 169 ASN C O   1 
ATOM   6391 C  CB  . ASN C  1  156 ? -23.847 28.752  17.907 1.00 65.74  ? 169 ASN C CB  1 
ATOM   6392 C  CG  . ASN C  1  156 ? -24.770 27.571  18.108 1.00 66.25  ? 169 ASN C CG  1 
ATOM   6393 O  OD1 . ASN C  1  156 ? -25.120 26.874  17.150 1.00 66.50  ? 169 ASN C OD1 1 
ATOM   6394 N  ND2 . ASN C  1  156 ? -25.217 27.346  19.333 1.00 67.08  ? 169 ASN C ND2 1 
ATOM   6395 N  N   . ARG C  1  157 ? -21.253 30.328  16.919 1.00 68.98  ? 170 ARG C N   1 
ATOM   6396 C  CA  . ARG C  1  157 ? -20.690 31.663  16.786 1.00 73.53  ? 170 ARG C CA  1 
ATOM   6397 C  C   . ARG C  1  157 ? -19.898 31.825  15.486 1.00 73.76  ? 170 ARG C C   1 
ATOM   6398 O  O   . ARG C  1  157 ? -19.801 32.937  14.985 1.00 78.61  ? 170 ARG C O   1 
ATOM   6399 C  CB  . ARG C  1  157 ? -19.798 31.962  17.997 1.00 78.72  ? 170 ARG C CB  1 
ATOM   6400 C  CG  . ARG C  1  157 ? -19.754 33.431  18.396 1.00 82.47  ? 170 ARG C CG  1 
ATOM   6401 C  CD  . ARG C  1  157 ? -18.613 33.699  19.346 1.00 86.27  ? 170 ARG C CD  1 
ATOM   6402 N  NE  . ARG C  1  157 ? -18.739 32.933  20.591 1.00 91.10  ? 170 ARG C NE  1 
ATOM   6403 C  CZ  . ARG C  1  157 ? -17.821 32.864  21.555 1.00 90.50  ? 170 ARG C CZ  1 
ATOM   6404 N  NH1 . ARG C  1  157 ? -16.662 33.498  21.434 1.00 82.31  ? 170 ARG C NH1 1 
ATOM   6405 N  NH2 . ARG C  1  157 ? -18.073 32.137  22.636 1.00 85.59  ? 170 ARG C NH2 1 
ATOM   6406 N  N   . TYR C  1  158 ? -19.292 30.749  14.960 1.00 72.95  ? 171 TYR C N   1 
ATOM   6407 C  CA  . TYR C  1  158 ? -18.355 30.882  13.851 1.00 68.13  ? 171 TYR C CA  1 
ATOM   6408 C  C   . TYR C  1  158 ? -18.710 29.986  12.666 1.00 64.04  ? 171 TYR C C   1 
ATOM   6409 O  O   . TYR C  1  158 ? -18.092 30.139  11.613 1.00 62.98  ? 171 TYR C O   1 
ATOM   6410 C  CB  . TYR C  1  158 ? -16.936 30.553  14.317 1.00 67.50  ? 171 TYR C CB  1 
ATOM   6411 C  CG  . TYR C  1  158 ? -16.382 31.509  15.359 1.00 66.33  ? 171 TYR C CG  1 
ATOM   6412 C  CD1 . TYR C  1  158 ? -15.862 32.736  14.971 1.00 67.75  ? 171 TYR C CD1 1 
ATOM   6413 C  CD2 . TYR C  1  158 ? -16.304 31.165  16.707 1.00 68.97  ? 171 TYR C CD2 1 
ATOM   6414 C  CE1 . TYR C  1  158 ? -15.315 33.617  15.895 1.00 68.00  ? 171 TYR C CE1 1 
ATOM   6415 C  CE2 . TYR C  1  158 ? -15.777 32.039  17.646 1.00 67.83  ? 171 TYR C CE2 1 
ATOM   6416 C  CZ  . TYR C  1  158 ? -15.288 33.274  17.239 1.00 69.01  ? 171 TYR C CZ  1 
ATOM   6417 O  OH  . TYR C  1  158 ? -14.734 34.137  18.141 1.00 69.43  ? 171 TYR C OH  1 
ATOM   6418 N  N   . GLY C  1  159 ? -19.678 29.070  12.811 1.00 64.18  ? 172 GLY C N   1 
ATOM   6419 C  CA  . GLY C  1  159 ? -19.932 28.095  11.758 1.00 65.43  ? 172 GLY C CA  1 
ATOM   6420 C  C   . GLY C  1  159 ? -21.412 27.916  11.417 1.00 67.10  ? 172 GLY C C   1 
ATOM   6421 O  O   . GLY C  1  159 ? -21.791 26.894  10.853 1.00 61.11  ? 172 GLY C O   1 
ATOM   6422 N  N   . GLY C  1  160 ? -22.247 28.906  11.749 1.00 70.23  ? 173 GLY C N   1 
ATOM   6423 C  CA  . GLY C  1  160 ? -23.665 28.849  11.428 1.00 63.35  ? 173 GLY C CA  1 
ATOM   6424 C  C   . GLY C  1  160 ? -24.379 27.657  12.069 1.00 62.31  ? 173 GLY C C   1 
ATOM   6425 O  O   . GLY C  1  160 ? -25.417 27.224  11.563 1.00 63.23  ? 173 GLY C O   1 
ATOM   6426 N  N   . GLY C  1  161 ? -23.827 27.145  13.183 1.00 57.69  ? 174 GLY C N   1 
ATOM   6427 C  CA  . GLY C  1  161 ? -24.402 26.009  13.893 1.00 60.98  ? 174 GLY C CA  1 
ATOM   6428 C  C   . GLY C  1  161 ? -23.738 24.676  13.532 1.00 61.23  ? 174 GLY C C   1 
ATOM   6429 O  O   . GLY C  1  161 ? -24.159 23.618  14.014 1.00 55.29  ? 174 GLY C O   1 
ATOM   6430 N  N   . PHE C  1  162 ? -22.700 24.748  12.688 1.00 65.32  ? 175 PHE C N   1 
ATOM   6431 C  CA  . PHE C  1  162 ? -21.963 23.582  12.223 1.00 67.41  ? 175 PHE C CA  1 
ATOM   6432 C  C   . PHE C  1  162 ? -20.481 23.752  12.559 1.00 65.85  ? 175 PHE C C   1 
ATOM   6433 O  O   . PHE C  1  162 ? -19.973 24.874  12.643 1.00 61.19  ? 175 PHE C O   1 
ATOM   6434 C  CB  . PHE C  1  162 ? -22.156 23.399  10.713 1.00 64.60  ? 175 PHE C CB  1 
ATOM   6435 C  CG  . PHE C  1  162 ? -23.578 23.069  10.283 1.00 61.91  ? 175 PHE C CG  1 
ATOM   6436 C  CD1 . PHE C  1  162 ? -24.000 21.743  10.207 1.00 61.76  ? 175 PHE C CD1 1 
ATOM   6437 C  CD2 . PHE C  1  162 ? -24.486 24.074  9.957  1.00 60.69  ? 175 PHE C CD2 1 
ATOM   6438 C  CE1 . PHE C  1  162 ? -25.289 21.426  9.802  1.00 60.82  ? 175 PHE C CE1 1 
ATOM   6439 C  CE2 . PHE C  1  162 ? -25.776 23.751  9.549  1.00 62.11  ? 175 PHE C CE2 1 
ATOM   6440 C  CZ  . PHE C  1  162 ? -26.175 22.426  9.473  1.00 61.37  ? 175 PHE C CZ  1 
ATOM   6441 N  N   . TYR C  1  163 ? -19.781 22.625  12.737 1.00 61.82  ? 176 TYR C N   1 
ATOM   6442 C  CA  . TYR C  1  163 ? -18.341 22.655  12.942 1.00 58.25  ? 176 TYR C CA  1 
ATOM   6443 C  C   . TYR C  1  163 ? -17.641 22.627  11.581 1.00 57.64  ? 176 TYR C C   1 
ATOM   6444 O  O   . TYR C  1  163 ? -17.810 21.673  10.815 1.00 55.93  ? 176 TYR C O   1 
ATOM   6445 C  CB  . TYR C  1  163 ? -17.942 21.480  13.842 1.00 59.09  ? 176 TYR C CB  1 
ATOM   6446 C  CG  . TYR C  1  163 ? -16.479 21.494  14.267 1.00 59.66  ? 176 TYR C CG  1 
ATOM   6447 C  CD1 . TYR C  1  163 ? -16.044 22.305  15.308 1.00 60.02  ? 176 TYR C CD1 1 
ATOM   6448 C  CD2 . TYR C  1  163 ? -15.534 20.693  13.631 1.00 57.14  ? 176 TYR C CD2 1 
ATOM   6449 C  CE1 . TYR C  1  163 ? -14.710 22.321  15.697 1.00 63.61  ? 176 TYR C CE1 1 
ATOM   6450 C  CE2 . TYR C  1  163 ? -14.202 20.702  14.008 1.00 54.44  ? 176 TYR C CE2 1 
ATOM   6451 C  CZ  . TYR C  1  163 ? -13.787 21.513  15.048 1.00 56.65  ? 176 TYR C CZ  1 
ATOM   6452 O  OH  . TYR C  1  163 ? -12.467 21.500  15.404 1.00 56.67  ? 176 TYR C OH  1 
ATOM   6453 N  N   . ASN C  1  164 ? -16.861 23.683  11.302 1.00 55.54  ? 177 ASN C N   1 
ATOM   6454 C  CA  . ASN C  1  164 ? -16.073 23.809  10.082 1.00 57.62  ? 177 ASN C CA  1 
ATOM   6455 C  C   . ASN C  1  164 ? -14.689 24.347  10.452 1.00 55.53  ? 177 ASN C C   1 
ATOM   6456 O  O   . ASN C  1  164 ? -14.382 24.511  11.632 1.00 62.08  ? 177 ASN C O   1 
ATOM   6457 C  CB  . ASN C  1  164 ? -16.819 24.600  9.004  1.00 61.23  ? 177 ASN C CB  1 
ATOM   6458 C  CG  . ASN C  1  164 ? -16.867 26.102  9.212  1.00 68.25  ? 177 ASN C CG  1 
ATOM   6459 O  OD1 . ASN C  1  164 ? -16.280 26.644  10.164 1.00 69.60  ? 177 ASN C OD1 1 
ATOM   6460 N  ND2 . ASN C  1  164 ? -17.565 26.784  8.308  1.00 78.18  ? 177 ASN C ND2 1 
ATOM   6461 N  N   . LEU C  1  165 ? -13.859 24.624  9.437  1.00 57.94  ? 178 LEU C N   1 
ATOM   6462 C  CA  . LEU C  1  165 ? -12.463 24.990  9.640  1.00 61.20  ? 178 LEU C CA  1 
ATOM   6463 C  C   . LEU C  1  165 ? -12.327 26.273  10.451 1.00 60.47  ? 178 LEU C C   1 
ATOM   6464 O  O   . LEU C  1  165 ? -11.396 26.392  11.247 1.00 63.41  ? 178 LEU C O   1 
ATOM   6465 C  CB  . LEU C  1  165 ? -11.720 25.135  8.314  1.00 65.35  ? 178 LEU C CB  1 
ATOM   6466 C  CG  . LEU C  1  165 ? -10.723 24.026  7.972  1.00 76.57  ? 178 LEU C CG  1 
ATOM   6467 C  CD1 . LEU C  1  165 ? -10.057 24.379  6.649  1.00 78.99  ? 178 LEU C CD1 1 
ATOM   6468 C  CD2 . LEU C  1  165 ? -9.663  23.791  9.051  1.00 73.55  ? 178 LEU C CD2 1 
ATOM   6469 N  N   . THR C  1  166 ? -13.208 27.249  10.195 1.00 65.72  ? 179 THR C N   1 
ATOM   6470 C  CA  . THR C  1  166 ? -13.200 28.499  10.945 1.00 68.49  ? 179 THR C CA  1 
ATOM   6471 C  C   . THR C  1  166 ? -13.406 28.199  12.431 1.00 60.20  ? 179 THR C C   1 
ATOM   6472 O  O   . THR C  1  166 ? -12.680 28.724  13.266 1.00 59.00  ? 179 THR C O   1 
ATOM   6473 C  CB  . THR C  1  166 ? -14.261 29.465  10.408 1.00 74.71  ? 179 THR C CB  1 
ATOM   6474 O  OG1 . THR C  1  166 ? -14.074 29.581  8.999  1.00 74.83  ? 179 THR C OG1 1 
ATOM   6475 C  CG2 . THR C  1  166 ? -14.148 30.853  11.019 1.00 77.35  ? 179 THR C CG2 1 
ATOM   6476 N  N   . VAL C  1  167 ? -14.381 27.336  12.750 1.00 53.86  ? 180 VAL C N   1 
ATOM   6477 C  CA  . VAL C  1  167 ? -14.674 26.975  14.132 1.00 57.37  ? 180 VAL C CA  1 
ATOM   6478 C  C   . VAL C  1  167 ? -13.444 26.301  14.743 1.00 63.70  ? 180 VAL C C   1 
ATOM   6479 O  O   . VAL C  1  167 ? -13.055 26.609  15.869 1.00 57.25  ? 180 VAL C O   1 
ATOM   6480 C  CB  . VAL C  1  167 ? -15.908 26.066  14.295 1.00 57.18  ? 180 VAL C CB  1 
ATOM   6481 C  CG1 . VAL C  1  167 ? -16.249 25.834  15.767 1.00 59.38  ? 180 VAL C CG1 1 
ATOM   6482 C  CG2 . VAL C  1  167 ? -17.136 26.597  13.564 1.00 60.06  ? 180 VAL C CG2 1 
ATOM   6483 N  N   . ALA C  1  168 ? -12.845 25.372  13.987 1.00 70.26  ? 181 ALA C N   1 
ATOM   6484 C  CA  . ALA C  1  168 ? -11.679 24.629  14.443 1.00 69.78  ? 181 ALA C CA  1 
ATOM   6485 C  C   . ALA C  1  168 ? -10.566 25.586  14.860 1.00 66.42  ? 181 ALA C C   1 
ATOM   6486 O  O   . ALA C  1  168 ? -9.992  25.435  15.934 1.00 61.78  ? 181 ALA C O   1 
ATOM   6487 C  CB  . ALA C  1  168 ? -11.204 23.672  13.367 1.00 71.74  ? 181 ALA C CB  1 
ATOM   6488 N  N   . GLY C  1  169 ? -10.281 26.575  14.007 1.00 66.08  ? 182 GLY C N   1 
ATOM   6489 C  CA  . GLY C  1  169 ? -9.234  27.548  14.280 1.00 68.70  ? 182 GLY C CA  1 
ATOM   6490 C  C   . GLY C  1  169 ? -9.475  28.291  15.594 1.00 76.07  ? 182 GLY C C   1 
ATOM   6491 O  O   . GLY C  1  169 ? -8.555  28.456  16.392 1.00 75.03  ? 182 GLY C O   1 
ATOM   6492 N  N   . GLU C  1  170 ? -10.725 28.726  15.810 1.00 73.56  ? 183 GLU C N   1 
ATOM   6493 C  CA  . GLU C  1  170 ? -11.076 29.528  16.974 1.00 69.22  ? 183 GLU C CA  1 
ATOM   6494 C  C   . GLU C  1  170 ? -11.102 28.650  18.223 1.00 64.76  ? 183 GLU C C   1 
ATOM   6495 O  O   . GLU C  1  170 ? -10.557 29.033  19.254 1.00 63.14  ? 183 GLU C O   1 
ATOM   6496 C  CB  . GLU C  1  170 ? -12.406 30.265  16.758 1.00 69.01  ? 183 GLU C CB  1 
ATOM   6497 C  CG  . GLU C  1  170 ? -12.387 31.279  15.614 1.00 66.52  ? 183 GLU C CG  1 
ATOM   6498 C  CD  . GLU C  1  170 ? -11.181 32.206  15.620 1.00 69.03  ? 183 GLU C CD  1 
ATOM   6499 O  OE1 . GLU C  1  170 ? -10.949 32.800  16.687 1.00 67.37  ? 183 GLU C OE1 1 
ATOM   6500 O  OE2 . GLU C  1  170 ? -10.458 32.315  14.602 1.00 70.78  ? 183 GLU C OE2 1 
ATOM   6501 N  N   . LEU C  1  171 ? -11.724 27.468  18.131 1.00 63.48  ? 184 LEU C N   1 
ATOM   6502 C  CA  . LEU C  1  171 ? -11.864 26.591  19.285 1.00 65.07  ? 184 LEU C CA  1 
ATOM   6503 C  C   . LEU C  1  171 ? -10.492 26.136  19.795 1.00 64.50  ? 184 LEU C C   1 
ATOM   6504 O  O   . LEU C  1  171 ? -10.257 26.127  20.996 1.00 64.97  ? 184 LEU C O   1 
ATOM   6505 C  CB  . LEU C  1  171 ? -12.760 25.396  18.955 1.00 64.43  ? 184 LEU C CB  1 
ATOM   6506 C  CG  . LEU C  1  171 ? -13.057 24.443  20.119 1.00 64.63  ? 184 LEU C CG  1 
ATOM   6507 C  CD1 . LEU C  1  171 ? -13.756 25.162  21.265 1.00 67.17  ? 184 LEU C CD1 1 
ATOM   6508 C  CD2 . LEU C  1  171 ? -13.886 23.253  19.673 1.00 65.06  ? 184 LEU C CD2 1 
ATOM   6509 N  N   . ARG C  1  172 ? -9.585  25.763  18.885 1.00 62.53  ? 185 ARG C N   1 
ATOM   6510 C  CA  . ARG C  1  172 ? -8.261  25.284  19.260 1.00 65.47  ? 185 ARG C CA  1 
ATOM   6511 C  C   . ARG C  1  172 ? -7.556  26.310  20.156 1.00 65.19  ? 185 ARG C C   1 
ATOM   6512 O  O   . ARG C  1  172 ? -7.032  25.951  21.212 1.00 60.02  ? 185 ARG C O   1 
ATOM   6513 C  CB  . ARG C  1  172 ? -7.502  24.900  17.980 1.00 61.74  ? 185 ARG C CB  1 
ATOM   6514 C  CG  . ARG C  1  172 ? -5.985  24.766  18.030 1.00 59.16  ? 185 ARG C CG  1 
ATOM   6515 C  CD  . ARG C  1  172 ? -5.440  23.820  19.082 1.00 58.43  ? 185 ARG C CD  1 
ATOM   6516 N  NE  . ARG C  1  172 ? -6.121  22.524  19.195 1.00 56.98  ? 185 ARG C NE  1 
ATOM   6517 C  CZ  . ARG C  1  172 ? -6.593  21.983  20.318 1.00 61.09  ? 185 ARG C CZ  1 
ATOM   6518 N  NH1 . ARG C  1  172 ? -6.485  22.624  21.469 1.00 61.08  ? 185 ARG C NH1 1 
ATOM   6519 N  NH2 . ARG C  1  172 ? -7.156  20.784  20.300 1.00 63.60  ? 185 ARG C NH2 1 
ATOM   6520 N  N   . TYR C  1  173 ? -7.563  27.583  19.738 1.00 64.54  ? 186 TYR C N   1 
ATOM   6521 C  CA  . TYR C  1  173 ? -6.876  28.641  20.465 1.00 66.01  ? 186 TYR C CA  1 
ATOM   6522 C  C   . TYR C  1  173 ? -7.536  28.856  21.828 1.00 68.47  ? 186 TYR C C   1 
ATOM   6523 O  O   . TYR C  1  173 ? -6.843  28.945  22.841 1.00 68.69  ? 186 TYR C O   1 
ATOM   6524 C  CB  . TYR C  1  173 ? -6.839  29.921  19.624 1.00 70.33  ? 186 TYR C CB  1 
ATOM   6525 C  CG  . TYR C  1  173 ? -6.104  31.088  20.275 1.00 78.26  ? 186 TYR C CG  1 
ATOM   6526 C  CD1 . TYR C  1  173 ? -4.727  31.047  20.465 1.00 79.67  ? 186 TYR C CD1 1 
ATOM   6527 C  CD2 . TYR C  1  173 ? -6.780  32.236  20.680 1.00 82.30  ? 186 TYR C CD2 1 
ATOM   6528 C  CE1 . TYR C  1  173 ? -4.046  32.101  21.051 1.00 85.71  ? 186 TYR C CE1 1 
ATOM   6529 C  CE2 . TYR C  1  173 ? -6.111  33.297  21.269 1.00 86.20  ? 186 TYR C CE2 1 
ATOM   6530 C  CZ  . TYR C  1  173 ? -4.740  33.227  21.455 1.00 87.63  ? 186 TYR C CZ  1 
ATOM   6531 O  OH  . TYR C  1  173 ? -4.052  34.250  22.037 1.00 90.67  ? 186 TYR C OH  1 
ATOM   6532 N  N   . SER C  1  174 ? -8.873  28.933  21.849 1.00 65.43  ? 187 SER C N   1 
ATOM   6533 C  CA  . SER C  1  174 ? -9.604  29.206  23.076 1.00 65.97  ? 187 SER C CA  1 
ATOM   6534 C  C   . SER C  1  174 ? -9.325  28.125  24.116 1.00 64.11  ? 187 SER C C   1 
ATOM   6535 O  O   . SER C  1  174 ? -9.119  28.447  25.282 1.00 66.76  ? 187 SER C O   1 
ATOM   6536 C  CB  . SER C  1  174 ? -11.090 29.346  22.818 1.00 71.83  ? 187 SER C CB  1 
ATOM   6537 O  OG  . SER C  1  174 ? -11.795 29.581  24.029 1.00 76.70  ? 187 SER C OG  1 
ATOM   6538 N  N   . ARG C  1  175 ? -9.290  26.851  23.687 1.00 63.43  ? 188 ARG C N   1 
ATOM   6539 C  CA  . ARG C  1  175 ? -9.060  25.732  24.593 1.00 60.46  ? 188 ARG C CA  1 
ATOM   6540 C  C   . ARG C  1  175 ? -7.649  25.801  25.179 1.00 59.21  ? 188 ARG C C   1 
ATOM   6541 O  O   . ARG C  1  175 ? -7.452  25.488  26.351 1.00 59.23  ? 188 ARG C O   1 
ATOM   6542 C  CB  . ARG C  1  175 ? -9.308  24.375  23.923 1.00 63.99  ? 188 ARG C CB  1 
ATOM   6543 C  CG  . ARG C  1  175 ? -10.761 24.086  23.567 1.00 59.34  ? 188 ARG C CG  1 
ATOM   6544 C  CD  . ARG C  1  175 ? -11.662 23.874  24.762 1.00 58.82  ? 188 ARG C CD  1 
ATOM   6545 N  NE  . ARG C  1  175 ? -11.228 22.706  25.532 1.00 61.29  ? 188 ARG C NE  1 
ATOM   6546 C  CZ  . ARG C  1  175 ? -10.649 22.697  26.731 1.00 64.87  ? 188 ARG C CZ  1 
ATOM   6547 N  NH1 . ARG C  1  175 ? -10.592 23.782  27.481 1.00 68.67  ? 188 ARG C NH1 1 
ATOM   6548 N  NH2 . ARG C  1  175 ? -10.139 21.567  27.189 1.00 67.24  ? 188 ARG C NH2 1 
ATOM   6549 N  N   . ILE C  1  176 ? -6.674  26.227  24.368 1.00 63.64  ? 189 ILE C N   1 
ATOM   6550 C  CA  . ILE C  1  176 ? -5.321  26.463  24.853 1.00 61.10  ? 189 ILE C CA  1 
ATOM   6551 C  C   . ILE C  1  176 ? -5.362  27.509  25.963 1.00 63.41  ? 189 ILE C C   1 
ATOM   6552 O  O   . ILE C  1  176 ? -4.784  27.299  27.027 1.00 60.84  ? 189 ILE C O   1 
ATOM   6553 C  CB  . ILE C  1  176 ? -4.378  26.861  23.703 1.00 57.73  ? 189 ILE C CB  1 
ATOM   6554 C  CG1 . ILE C  1  176 ? -4.111  25.686  22.762 1.00 61.00  ? 189 ILE C CG1 1 
ATOM   6555 C  CG2 . ILE C  1  176 ? -3.070  27.442  24.243 1.00 60.14  ? 189 ILE C CG2 1 
ATOM   6556 C  CD1 . ILE C  1  176 ? -3.412  26.071  21.470 1.00 63.07  ? 189 ILE C CD1 1 
ATOM   6557 N  N   . GLN C  1  177 ? -6.067  28.623  25.719 1.00 69.34  ? 190 GLN C N   1 
ATOM   6558 C  CA  . GLN C  1  177 ? -6.198  29.679  26.714 1.00 70.86  ? 190 GLN C CA  1 
ATOM   6559 C  C   . GLN C  1  177 ? -6.851  29.139  27.991 1.00 66.68  ? 190 GLN C C   1 
ATOM   6560 O  O   . GLN C  1  177 ? -6.354  29.403  29.086 1.00 65.05  ? 190 GLN C O   1 
ATOM   6561 C  CB  . GLN C  1  177 ? -6.911  30.894  26.117 1.00 74.15  ? 190 GLN C CB  1 
ATOM   6562 C  CG  . GLN C  1  177 ? -6.131  31.578  24.996 1.00 78.81  ? 190 GLN C CG  1 
ATOM   6563 C  CD  . GLN C  1  177 ? -4.807  32.163  25.442 1.00 86.25  ? 190 GLN C CD  1 
ATOM   6564 O  OE1 . GLN C  1  177 ? -4.609  32.481  26.619 1.00 93.56  ? 190 GLN C OE1 1 
ATOM   6565 N  NE2 . GLN C  1  177 ? -3.891  32.333  24.499 1.00 89.81  ? 190 GLN C NE2 1 
ATOM   6566 N  N   . ASP C  1  178 ? -7.931  28.353  27.863 1.00 60.37  ? 191 ASP C N   1 
ATOM   6567 C  CA  . ASP C  1  178 ? -8.584  27.751  29.022 1.00 62.90  ? 191 ASP C CA  1 
ATOM   6568 C  C   . ASP C  1  178 ? -7.558  27.051  29.914 1.00 68.19  ? 191 ASP C C   1 
ATOM   6569 O  O   . ASP C  1  178 ? -7.567  27.219  31.128 1.00 67.14  ? 191 ASP C O   1 
ATOM   6570 C  CB  . ASP C  1  178 ? -9.675  26.770  28.623 1.00 61.71  ? 191 ASP C CB  1 
ATOM   6571 C  CG  . ASP C  1  178 ? -10.884 27.353  27.899 1.00 68.58  ? 191 ASP C CG  1 
ATOM   6572 O  OD1 . ASP C  1  178 ? -11.027 28.596  27.879 1.00 74.87  ? 191 ASP C OD1 1 
ATOM   6573 O  OD2 . ASP C  1  178 ? -11.688 26.560  27.362 1.00 66.69  ? 191 ASP C OD2 1 
ATOM   6574 N  N   . SER C  1  179 ? -6.675  26.257  29.300 1.00 72.24  ? 192 SER C N   1 
ATOM   6575 C  CA  . SER C  1  179 ? -5.702  25.466  30.036 1.00 68.28  ? 192 SER C CA  1 
ATOM   6576 C  C   . SER C  1  179 ? -4.611  26.350  30.647 1.00 66.57  ? 192 SER C C   1 
ATOM   6577 O  O   . SER C  1  179 ? -4.165  26.088  31.760 1.00 65.12  ? 192 SER C O   1 
ATOM   6578 C  CB  . SER C  1  179 ? -5.115  24.369  29.161 1.00 69.83  ? 192 SER C CB  1 
ATOM   6579 O  OG  . SER C  1  179 ? -5.980  23.240  29.104 1.00 66.17  ? 192 SER C OG  1 
ATOM   6580 N  N   . ILE C  1  180 ? -4.160  27.379  29.920 1.00 69.66  ? 193 ILE C N   1 
ATOM   6581 C  CA  . ILE C  1  180 ? -3.173  28.307  30.459 1.00 73.46  ? 193 ILE C CA  1 
ATOM   6582 C  C   . ILE C  1  180 ? -3.711  28.910  31.759 1.00 81.10  ? 193 ILE C C   1 
ATOM   6583 O  O   . ILE C  1  180 ? -3.002  28.956  32.763 1.00 72.44  ? 193 ILE C O   1 
ATOM   6584 C  CB  . ILE C  1  180 ? -2.796  29.388  29.426 1.00 70.20  ? 193 ILE C CB  1 
ATOM   6585 C  CG1 . ILE C  1  180 ? -1.950  28.791  28.307 1.00 69.89  ? 193 ILE C CG1 1 
ATOM   6586 C  CG2 . ILE C  1  180 ? -2.082  30.570  30.082 1.00 71.23  ? 193 ILE C CG2 1 
ATOM   6587 C  CD1 . ILE C  1  180 ? -1.674  29.736  27.156 1.00 65.94  ? 193 ILE C CD1 1 
ATOM   6588 N  N   . ALA C  1  181 ? -4.984  29.327  31.726 1.00 87.96  ? 194 ALA C N   1 
ATOM   6589 C  CA  . ALA C  1  181 ? -5.621  30.059  32.810 1.00 82.23  ? 194 ALA C CA  1 
ATOM   6590 C  C   . ALA C  1  181 ? -5.946  29.164  34.002 1.00 79.65  ? 194 ALA C C   1 
ATOM   6591 O  O   . ALA C  1  181 ? -6.038  29.675  35.113 1.00 83.40  ? 194 ALA C O   1 
ATOM   6592 C  CB  . ALA C  1  181 ? -6.882  30.737  32.313 1.00 79.71  ? 194 ALA C CB  1 
ATOM   6593 N  N   . THR C  1  182 ? -6.148  27.855  33.784 1.00 77.40  ? 195 THR C N   1 
ATOM   6594 C  CA  . THR C  1  182 ? -6.767  27.014  34.803 1.00 75.11  ? 195 THR C CA  1 
ATOM   6595 C  C   . THR C  1  182 ? -5.894  25.831  35.220 1.00 71.96  ? 195 THR C C   1 
ATOM   6596 O  O   . THR C  1  182 ? -6.164  25.242  36.260 1.00 70.34  ? 195 THR C O   1 
ATOM   6597 C  CB  . THR C  1  182 ? -8.132  26.510  34.331 1.00 81.52  ? 195 THR C CB  1 
ATOM   6598 O  OG1 . THR C  1  182 ? -7.917  25.743  33.149 1.00 83.71  ? 195 THR C OG1 1 
ATOM   6599 C  CG2 . THR C  1  182 ? -9.123  27.631  34.068 1.00 81.97  ? 195 THR C CG2 1 
ATOM   6600 N  N   . ASN C  1  183 ? -4.907  25.434  34.405 1.00 73.99  ? 196 ASN C N   1 
ATOM   6601 C  CA  . ASN C  1  183 ? -4.154  24.214  34.664 1.00 67.76  ? 196 ASN C CA  1 
ATOM   6602 C  C   . ASN C  1  183 ? -2.691  24.582  34.887 1.00 64.97  ? 196 ASN C C   1 
ATOM   6603 O  O   . ASN C  1  183 ? -1.989  24.937  33.942 1.00 61.08  ? 196 ASN C O   1 
ATOM   6604 C  CB  . ASN C  1  183 ? -4.322  23.205  33.533 1.00 69.51  ? 196 ASN C CB  1 
ATOM   6605 C  CG  . ASN C  1  183 ? -3.588  21.902  33.767 1.00 71.00  ? 196 ASN C CG  1 
ATOM   6606 O  OD1 . ASN C  1  183 ? -2.922  21.721  34.794 1.00 68.10  ? 196 ASN C OD1 1 
ATOM   6607 N  ND2 . ASN C  1  183 ? -3.703  20.975  32.827 1.00 68.44  ? 196 ASN C ND2 1 
ATOM   6608 N  N   . PRO C  1  184 ? -2.185  24.515  36.140 1.00 62.94  ? 197 PRO C N   1 
ATOM   6609 C  CA  . PRO C  1  184 ? -0.801  24.894  36.421 1.00 66.42  ? 197 PRO C CA  1 
ATOM   6610 C  C   . PRO C  1  184 ? 0.229   23.889  35.906 1.00 70.37  ? 197 PRO C C   1 
ATOM   6611 O  O   . PRO C  1  184 ? 1.405   24.226  35.792 1.00 72.76  ? 197 PRO C O   1 
ATOM   6612 C  CB  . PRO C  1  184 ? -0.800  25.004  37.948 1.00 67.20  ? 197 PRO C CB  1 
ATOM   6613 C  CG  . PRO C  1  184 ? -1.819  23.984  38.393 1.00 65.83  ? 197 PRO C CG  1 
ATOM   6614 C  CD  . PRO C  1  184 ? -2.909  24.057  37.339 1.00 66.75  ? 197 PRO C CD  1 
ATOM   6615 N  N   . GLU C  1  185 ? -0.235  22.669  35.584 1.00 76.48  ? 198 GLU C N   1 
ATOM   6616 C  CA  . GLU C  1  185 ? 0.598   21.606  35.035 1.00 79.18  ? 198 GLU C CA  1 
ATOM   6617 C  C   . GLU C  1  185 ? 0.455   21.493  33.510 1.00 73.71  ? 198 GLU C C   1 
ATOM   6618 O  O   . GLU C  1  185 ? 0.986   20.555  32.927 1.00 63.76  ? 198 GLU C O   1 
ATOM   6619 C  CB  . GLU C  1  185 ? 0.232   20.267  35.680 1.00 77.78  ? 198 GLU C CB  1 
ATOM   6620 C  CG  . GLU C  1  185 ? 0.637   20.151  37.146 1.00 80.99  ? 198 GLU C CG  1 
ATOM   6621 C  CD  . GLU C  1  185 ? 0.198   18.865  37.821 1.00 87.41  ? 198 GLU C CD  1 
ATOM   6622 O  OE1 . GLU C  1  185 ? -0.413  18.009  37.150 1.00 79.03  ? 198 GLU C OE1 1 
ATOM   6623 O  OE2 . GLU C  1  185 ? 0.463   18.726  39.032 1.00 97.81  ? 198 GLU C OE2 1 
ATOM   6624 N  N   . PHE C  1  186 ? -0.198  22.473  32.868 1.00 69.37  ? 199 PHE C N   1 
ATOM   6625 C  CA  . PHE C  1  186 ? -0.451  22.463  31.435 1.00 65.34  ? 199 PHE C CA  1 
ATOM   6626 C  C   . PHE C  1  186 ? 0.834   22.333  30.618 1.00 63.02  ? 199 PHE C C   1 
ATOM   6627 O  O   . PHE C  1  186 ? 1.735   23.169  30.716 1.00 62.78  ? 199 PHE C O   1 
ATOM   6628 C  CB  . PHE C  1  186 ? -1.137  23.766  31.019 1.00 66.83  ? 199 PHE C CB  1 
ATOM   6629 C  CG  . PHE C  1  186 ? -1.438  23.919  29.533 1.00 64.37  ? 199 PHE C CG  1 
ATOM   6630 C  CD1 . PHE C  1  186 ? -2.023  22.886  28.807 1.00 64.72  ? 199 PHE C CD1 1 
ATOM   6631 C  CD2 . PHE C  1  186 ? -1.144  25.104  28.867 1.00 62.78  ? 199 PHE C CD2 1 
ATOM   6632 C  CE1 . PHE C  1  186 ? -2.303  23.037  27.458 1.00 61.74  ? 199 PHE C CE1 1 
ATOM   6633 C  CE2 . PHE C  1  186 ? -1.415  25.243  27.517 1.00 65.78  ? 199 PHE C CE2 1 
ATOM   6634 C  CZ  . PHE C  1  186 ? -1.997  24.209  26.816 1.00 63.91  ? 199 PHE C CZ  1 
ATOM   6635 N  N   . GLN C  1  187 ? 0.863   21.293  29.770 1.00 63.55  ? 200 GLN C N   1 
ATOM   6636 C  CA  . GLN C  1  187 ? 1.924   21.068  28.800 1.00 61.03  ? 200 GLN C CA  1 
ATOM   6637 C  C   . GLN C  1  187 ? 1.324   21.013  27.396 1.00 58.08  ? 200 GLN C C   1 
ATOM   6638 O  O   . GLN C  1  187 ? 0.273   20.397  27.197 1.00 57.27  ? 200 GLN C O   1 
ATOM   6639 C  CB  . GLN C  1  187 ? 2.639   19.759  29.135 1.00 60.61  ? 200 GLN C CB  1 
ATOM   6640 C  CG  . GLN C  1  187 ? 3.382   19.776  30.467 1.00 69.46  ? 200 GLN C CG  1 
ATOM   6641 C  CD  . GLN C  1  187 ? 4.528   20.765  30.482 1.00 79.99  ? 200 GLN C CD  1 
ATOM   6642 O  OE1 . GLN C  1  187 ? 5.504   20.619  29.734 1.00 82.85  ? 200 GLN C OE1 1 
ATOM   6643 N  NE2 . GLN C  1  187 ? 4.413   21.785  31.325 1.00 86.86  ? 200 GLN C NE2 1 
ATOM   6644 N  N   . PHE C  1  188 ? 2.002   21.660  26.436 1.00 55.93  ? 201 PHE C N   1 
ATOM   6645 C  CA  . PHE C  1  188 ? 1.583   21.638  25.041 1.00 54.23  ? 201 PHE C CA  1 
ATOM   6646 C  C   . PHE C  1  188 ? 2.813   21.587  24.132 1.00 52.31  ? 201 PHE C C   1 
ATOM   6647 O  O   . PHE C  1  188 ? 3.095   22.537  23.405 1.00 48.65  ? 201 PHE C O   1 
ATOM   6648 C  CB  . PHE C  1  188 ? 0.687   22.853  24.795 1.00 52.55  ? 201 PHE C CB  1 
ATOM   6649 C  CG  . PHE C  1  188 ? -0.263  22.725  23.611 1.00 50.88  ? 201 PHE C CG  1 
ATOM   6650 C  CD1 . PHE C  1  188 ? -1.335  21.844  23.650 1.00 51.60  ? 201 PHE C CD1 1 
ATOM   6651 C  CD2 . PHE C  1  188 ? -0.117  23.521  22.482 1.00 52.30  ? 201 PHE C CD2 1 
ATOM   6652 C  CE1 . PHE C  1  188 ? -2.218  21.748  22.583 1.00 53.37  ? 201 PHE C CE1 1 
ATOM   6653 C  CE2 . PHE C  1  188 ? -0.999  23.420  21.416 1.00 51.73  ? 201 PHE C CE2 1 
ATOM   6654 C  CZ  . PHE C  1  188 ? -2.044  22.530  21.465 1.00 49.94  ? 201 PHE C CZ  1 
ATOM   6655 N  N   . LYS C  1  189 ? 3.535   20.457  24.166 1.00 51.31  ? 202 LYS C N   1 
ATOM   6656 C  CA  . LYS C  1  189 ? 4.788   20.312  23.439 1.00 49.93  ? 202 LYS C CA  1 
ATOM   6657 C  C   . LYS C  1  189 ? 4.929   18.900  22.866 1.00 49.82  ? 202 LYS C C   1 
ATOM   6658 O  O   . LYS C  1  189 ? 4.170   18.000  23.215 1.00 53.75  ? 202 LYS C O   1 
ATOM   6659 C  CB  . LYS C  1  189 ? 5.961   20.629  24.373 1.00 57.47  ? 202 LYS C CB  1 
ATOM   6660 C  CG  . LYS C  1  189 ? 6.014   19.796  25.645 1.00 62.90  ? 202 LYS C CG  1 
ATOM   6661 C  CD  . LYS C  1  189 ? 7.259   20.007  26.499 1.00 65.62  ? 202 LYS C CD  1 
ATOM   6662 C  CE  . LYS C  1  189 ? 7.401   21.418  26.938 1.00 72.90  ? 202 LYS C CE  1 
ATOM   6663 N  NZ  . LYS C  1  189 ? 8.302   21.553  28.083 1.00 73.93  ? 202 LYS C NZ  1 
ATOM   6664 N  N   . ASN C  1  190 ? 5.917   18.731  21.981 1.00 53.16  ? 203 ASN C N   1 
ATOM   6665 C  CA  . ASN C  1  190 ? 6.286   17.448  21.400 1.00 51.57  ? 203 ASN C CA  1 
ATOM   6666 C  C   . ASN C  1  190 ? 5.055   16.760  20.800 1.00 49.09  ? 203 ASN C C   1 
ATOM   6667 O  O   . ASN C  1  190 ? 4.412   17.323  19.919 1.00 45.58  ? 203 ASN C O   1 
ATOM   6668 C  CB  . ASN C  1  190 ? 7.084   16.628  22.408 1.00 54.13  ? 203 ASN C CB  1 
ATOM   6669 C  CG  . ASN C  1  190 ? 8.375   17.307  22.801 1.00 52.00  ? 203 ASN C CG  1 
ATOM   6670 O  OD1 . ASN C  1  190 ? 9.143   17.743  21.934 1.00 56.07  ? 203 ASN C OD1 1 
ATOM   6671 N  ND2 . ASN C  1  190 ? 8.624   17.408  24.096 1.00 48.19  ? 203 ASN C ND2 1 
ATOM   6672 N  N   . VAL C  1  191 ? 4.725   15.546  21.262 1.00 45.07  ? 204 VAL C N   1 
ATOM   6673 C  CA  . VAL C  1  191 ? 3.661   14.778  20.636 1.00 47.75  ? 204 VAL C CA  1 
ATOM   6674 C  C   . VAL C  1  191 ? 2.346   15.564  20.679 1.00 49.14  ? 204 VAL C C   1 
ATOM   6675 O  O   . VAL C  1  191 ? 1.630   15.641  19.683 1.00 51.24  ? 204 VAL C O   1 
ATOM   6676 C  CB  . VAL C  1  191 ? 3.497   13.394  21.290 1.00 48.21  ? 204 VAL C CB  1 
ATOM   6677 C  CG1 . VAL C  1  191 ? 2.274   12.650  20.756 1.00 51.55  ? 204 VAL C CG1 1 
ATOM   6678 C  CG2 . VAL C  1  191 ? 4.743   12.535  21.133 1.00 45.13  ? 204 VAL C CG2 1 
ATOM   6679 N  N   . ARG C  1  192 ? 2.017   16.132  21.840 1.00 48.27  ? 205 ARG C N   1 
ATOM   6680 C  CA  . ARG C  1  192 ? 0.720   16.759  22.019 1.00 51.54  ? 205 ARG C CA  1 
ATOM   6681 C  C   . ARG C  1  192 ? 0.566   17.952  21.075 1.00 52.52  ? 205 ARG C C   1 
ATOM   6682 O  O   . ARG C  1  192 ? -0.502  18.145  20.501 1.00 49.10  ? 205 ARG C O   1 
ATOM   6683 C  CB  . ARG C  1  192 ? 0.483   17.176  23.475 1.00 53.28  ? 205 ARG C CB  1 
ATOM   6684 C  CG  . ARG C  1  192 ? -0.912  17.735  23.711 1.00 52.28  ? 205 ARG C CG  1 
ATOM   6685 C  CD  . ARG C  1  192 ? -2.013  16.810  23.214 1.00 51.07  ? 205 ARG C CD  1 
ATOM   6686 N  NE  . ARG C  1  192 ? -3.342  17.423  23.301 1.00 53.41  ? 205 ARG C NE  1 
ATOM   6687 C  CZ  . ARG C  1  192 ? -4.441  17.043  22.651 1.00 57.16  ? 205 ARG C CZ  1 
ATOM   6688 N  NH1 . ARG C  1  192 ? -4.414  15.996  21.848 1.00 63.88  ? 205 ARG C NH1 1 
ATOM   6689 N  NH2 . ARG C  1  192 ? -5.568  17.718  22.817 1.00 53.65  ? 205 ARG C NH2 1 
ATOM   6690 N  N   . PHE C  1  193 ? 1.632   18.747  20.908 1.00 50.97  ? 206 PHE C N   1 
ATOM   6691 C  CA  . PHE C  1  193 ? 1.580   19.909  20.037 1.00 53.54  ? 206 PHE C CA  1 
ATOM   6692 C  C   . PHE C  1  193 ? 1.184   19.487  18.622 1.00 55.34  ? 206 PHE C C   1 
ATOM   6693 O  O   . PHE C  1  193 ? 0.366   20.149  17.994 1.00 59.16  ? 206 PHE C O   1 
ATOM   6694 C  CB  . PHE C  1  193 ? 2.905   20.674  20.015 1.00 53.80  ? 206 PHE C CB  1 
ATOM   6695 C  CG  . PHE C  1  193 ? 2.873   21.936  19.171 1.00 54.48  ? 206 PHE C CG  1 
ATOM   6696 C  CD1 . PHE C  1  193 ? 2.222   23.074  19.632 1.00 55.88  ? 206 PHE C CD1 1 
ATOM   6697 C  CD2 . PHE C  1  193 ? 3.492   21.980  17.929 1.00 52.85  ? 206 PHE C CD2 1 
ATOM   6698 C  CE1 . PHE C  1  193 ? 2.184   24.222  18.863 1.00 59.39  ? 206 PHE C CE1 1 
ATOM   6699 C  CE2 . PHE C  1  193 ? 3.457   23.135  17.166 1.00 56.69  ? 206 PHE C CE2 1 
ATOM   6700 C  CZ  . PHE C  1  193 ? 2.802   24.252  17.632 1.00 59.29  ? 206 PHE C CZ  1 
ATOM   6701 N  N   . ILE C  1  194 ? 1.742   18.374  18.133 1.00 57.42  ? 207 ILE C N   1 
ATOM   6702 C  CA  . ILE C  1  194 ? 1.517   17.947  16.760 1.00 54.77  ? 207 ILE C CA  1 
ATOM   6703 C  C   . ILE C  1  194 ? 0.132   17.310  16.627 1.00 54.38  ? 207 ILE C C   1 
ATOM   6704 O  O   . ILE C  1  194 ? -0.629  17.703  15.742 1.00 55.16  ? 207 ILE C O   1 
ATOM   6705 C  CB  . ILE C  1  194 ? 2.644   17.013  16.276 1.00 52.59  ? 207 ILE C CB  1 
ATOM   6706 C  CG1 . ILE C  1  194 ? 4.032   17.668  16.419 1.00 55.24  ? 207 ILE C CG1 1 
ATOM   6707 C  CG2 . ILE C  1  194 ? 2.395   16.546  14.841 1.00 50.39  ? 207 ILE C CG2 1 
ATOM   6708 C  CD1 . ILE C  1  194 ? 4.234   18.956  15.629 1.00 54.29  ? 207 ILE C CD1 1 
ATOM   6709 N  N   . THR C  1  195 ? -0.192  16.350  17.504 1.00 50.73  ? 208 THR C N   1 
ATOM   6710 C  CA  . THR C  1  195 ? -1.419  15.578  17.377 1.00 51.33  ? 208 THR C CA  1 
ATOM   6711 C  C   . THR C  1  195 ? -2.647  16.454  17.624 1.00 52.38  ? 208 THR C C   1 
ATOM   6712 O  O   . THR C  1  195 ? -3.705  16.175  17.079 1.00 57.10  ? 208 THR C O   1 
ATOM   6713 C  CB  . THR C  1  195 ? -1.413  14.363  18.306 1.00 50.24  ? 208 THR C CB  1 
ATOM   6714 O  OG1 . THR C  1  195 ? -1.253  14.828  19.644 1.00 57.95  ? 208 THR C OG1 1 
ATOM   6715 C  CG2 . THR C  1  195 ? -0.316  13.374  17.963 1.00 51.02  ? 208 THR C CG2 1 
ATOM   6716 N  N   . ALA C  1  196 ? -2.508  17.519  18.419 1.00 57.37  ? 209 ALA C N   1 
ATOM   6717 C  CA  . ALA C  1  196 ? -3.640  18.361  18.786 1.00 60.10  ? 209 ALA C CA  1 
ATOM   6718 C  C   . ALA C  1  196 ? -4.213  19.105  17.582 1.00 56.51  ? 209 ALA C C   1 
ATOM   6719 O  O   . ALA C  1  196 ? -5.421  19.310  17.522 1.00 58.60  ? 209 ALA C O   1 
ATOM   6720 C  CB  . ALA C  1  196 ? -3.247  19.341  19.867 1.00 61.99  ? 209 ALA C CB  1 
ATOM   6721 N  N   . TYR C  1  197 ? -3.363  19.531  16.639 1.00 52.87  ? 210 TYR C N   1 
ATOM   6722 C  CA  . TYR C  1  197 ? -3.861  20.277  15.494 1.00 51.85  ? 210 TYR C CA  1 
ATOM   6723 C  C   . TYR C  1  197 ? -4.576  19.315  14.545 1.00 50.76  ? 210 TYR C C   1 
ATOM   6724 O  O   . TYR C  1  197 ? -5.612  19.670  13.983 1.00 52.11  ? 210 TYR C O   1 
ATOM   6725 C  CB  . TYR C  1  197 ? -2.745  21.129  14.880 1.00 53.09  ? 210 TYR C CB  1 
ATOM   6726 C  CG  . TYR C  1  197 ? -2.486  22.368  15.725 1.00 59.15  ? 210 TYR C CG  1 
ATOM   6727 C  CD1 . TYR C  1  197 ? -3.204  23.548  15.531 1.00 62.77  ? 210 TYR C CD1 1 
ATOM   6728 C  CD2 . TYR C  1  197 ? -1.562  22.335  16.759 1.00 58.91  ? 210 TYR C CD2 1 
ATOM   6729 C  CE1 . TYR C  1  197 ? -2.998  24.658  16.335 1.00 61.59  ? 210 TYR C CE1 1 
ATOM   6730 C  CE2 . TYR C  1  197 ? -1.344  23.442  17.564 1.00 60.85  ? 210 TYR C CE2 1 
ATOM   6731 C  CZ  . TYR C  1  197 ? -2.071  24.601  17.359 1.00 60.01  ? 210 TYR C CZ  1 
ATOM   6732 O  OH  . TYR C  1  197 ? -1.849  25.686  18.154 1.00 58.75  ? 210 TYR C OH  1 
ATOM   6733 N  N   . GLY C  1  198 ? -4.044  18.095  14.398 1.00 46.49  ? 211 GLY C N   1 
ATOM   6734 C  CA  . GLY C  1  198 ? -4.671  17.087  13.561 1.00 44.61  ? 211 GLY C CA  1 
ATOM   6735 C  C   . GLY C  1  198 ? -6.049  16.692  14.081 1.00 44.91  ? 211 GLY C C   1 
ATOM   6736 O  O   . GLY C  1  198 ? -6.986  16.536  13.305 1.00 47.00  ? 211 GLY C O   1 
ATOM   6737 N  N   . GLU C  1  199 ? -6.172  16.545  15.404 1.00 48.31  ? 212 GLU C N   1 
ATOM   6738 C  CA  . GLU C  1  199 ? -7.418  16.109  16.017 1.00 51.80  ? 212 GLU C CA  1 
ATOM   6739 C  C   . GLU C  1  199 ? -8.539  17.110  15.734 1.00 47.49  ? 212 GLU C C   1 
ATOM   6740 O  O   . GLU C  1  199 ? -9.685  16.698  15.575 1.00 47.12  ? 212 GLU C O   1 
ATOM   6741 C  CB  . GLU C  1  199 ? -7.180  15.791  17.493 1.00 54.93  ? 212 GLU C CB  1 
ATOM   6742 C  CG  . GLU C  1  199 ? -6.521  14.423  17.665 1.00 57.39  ? 212 GLU C CG  1 
ATOM   6743 C  CD  . GLU C  1  199 ? -5.752  14.219  18.956 1.00 58.84  ? 212 GLU C CD  1 
ATOM   6744 O  OE1 . GLU C  1  199 ? -6.016  15.015  19.884 1.00 58.28  ? 212 GLU C OE1 1 
ATOM   6745 O  OE2 . GLU C  1  199 ? -4.894  13.295  19.014 1.00 56.82  ? 212 GLU C OE2 1 
ATOM   6746 N  N   . THR C  1  200 ? -8.210  18.403  15.610 1.00 46.97  ? 213 THR C N   1 
ATOM   6747 C  CA  . THR C  1  200 ? -9.233  19.426  15.437 1.00 51.08  ? 213 THR C CA  1 
ATOM   6748 C  C   . THR C  1  200 ? -9.842  19.369  14.038 1.00 52.99  ? 213 THR C C   1 
ATOM   6749 O  O   . THR C  1  200 ? -10.937 19.900  13.870 1.00 54.05  ? 213 THR C O   1 
ATOM   6750 C  CB  . THR C  1  200 ? -8.727  20.841  15.728 1.00 55.77  ? 213 THR C CB  1 
ATOM   6751 O  OG1 . THR C  1  200 ? -7.892  21.254  14.653 1.00 64.08  ? 213 THR C OG1 1 
ATOM   6752 C  CG2 . THR C  1  200 ? -7.963  20.943  17.031 1.00 57.06  ? 213 THR C CG2 1 
ATOM   6753 N  N   . VAL C  1  201 ? -9.148  18.764  13.047 1.00 50.64  ? 214 VAL C N   1 
ATOM   6754 C  CA  . VAL C  1  201 ? -9.676  18.684  11.687 1.00 45.63  ? 214 VAL C CA  1 
ATOM   6755 C  C   . VAL C  1  201 ? -10.256 17.304  11.382 1.00 45.67  ? 214 VAL C C   1 
ATOM   6756 O  O   . VAL C  1  201 ? -11.029 17.176  10.437 1.00 50.10  ? 214 VAL C O   1 
ATOM   6757 C  CB  . VAL C  1  201 ? -8.673  19.095  10.595 1.00 47.89  ? 214 VAL C CB  1 
ATOM   6758 C  CG1 . VAL C  1  201 ? -8.294  20.567  10.742 1.00 50.64  ? 214 VAL C CG1 1 
ATOM   6759 C  CG2 . VAL C  1  201 ? -7.431  18.201  10.538 1.00 49.15  ? 214 VAL C CG2 1 
ATOM   6760 N  N   . PHE C  1  202 ? -9.911  16.276  12.168 1.00 42.50  ? 215 PHE C N   1 
ATOM   6761 C  CA  . PHE C  1  202 ? -10.473 14.952  11.949 1.00 42.58  ? 215 PHE C CA  1 
ATOM   6762 C  C   . PHE C  1  202 ? -12.004 14.997  11.915 1.00 45.46  ? 215 PHE C C   1 
ATOM   6763 O  O   . PHE C  1  202 ? -12.604 14.305  11.106 1.00 47.43  ? 215 PHE C O   1 
ATOM   6764 C  CB  . PHE C  1  202 ? -9.999  13.943  12.997 1.00 44.22  ? 215 PHE C CB  1 
ATOM   6765 C  CG  . PHE C  1  202 ? -8.537  13.514  12.932 1.00 44.67  ? 215 PHE C CG  1 
ATOM   6766 C  CD1 . PHE C  1  202 ? -7.711  13.845  11.852 1.00 45.13  ? 215 PHE C CD1 1 
ATOM   6767 C  CD2 . PHE C  1  202 ? -8.001  12.734  13.949 1.00 44.54  ? 215 PHE C CD2 1 
ATOM   6768 C  CE1 . PHE C  1  202 ? -6.382  13.443  11.826 1.00 42.10  ? 215 PHE C CE1 1 
ATOM   6769 C  CE2 . PHE C  1  202 ? -6.673  12.335  13.910 1.00 49.02  ? 215 PHE C CE2 1 
ATOM   6770 C  CZ  . PHE C  1  202 ? -5.870  12.685  12.849 1.00 43.29  ? 215 PHE C CZ  1 
ATOM   6771 N  N   . PRO C  1  203 ? -12.710 15.762  12.781 1.00 50.89  ? 216 PRO C N   1 
ATOM   6772 C  CA  . PRO C  1  203 ? -14.171 15.843  12.703 1.00 52.24  ? 216 PRO C CA  1 
ATOM   6773 C  C   . PRO C  1  203 ? -14.698 16.280  11.337 1.00 50.69  ? 216 PRO C C   1 
ATOM   6774 O  O   . PRO C  1  203 ? -15.759 15.829  10.910 1.00 49.12  ? 216 PRO C O   1 
ATOM   6775 C  CB  . PRO C  1  203 ? -14.537 16.837  13.816 1.00 49.87  ? 216 PRO C CB  1 
ATOM   6776 C  CG  . PRO C  1  203 ? -13.406 16.706  14.795 1.00 49.99  ? 216 PRO C CG  1 
ATOM   6777 C  CD  . PRO C  1  203 ? -12.176 16.530  13.916 1.00 51.52  ? 216 PRO C CD  1 
ATOM   6778 N  N   . ILE C  1  204 ? -13.940 17.155  10.668 1.00 48.39  ? 217 ILE C N   1 
ATOM   6779 C  CA  . ILE C  1  204 ? -14.304 17.661  9.354  1.00 50.70  ? 217 ILE C CA  1 
ATOM   6780 C  C   . ILE C  1  204 ? -13.987 16.620  8.278  1.00 46.06  ? 217 ILE C C   1 
ATOM   6781 O  O   . ILE C  1  204 ? -14.819 16.345  7.422  1.00 44.91  ? 217 ILE C O   1 
ATOM   6782 C  CB  . ILE C  1  204 ? -13.587 18.998  9.082  1.00 54.25  ? 217 ILE C CB  1 
ATOM   6783 C  CG1 . ILE C  1  204 ? -13.996 20.059  10.101 1.00 53.84  ? 217 ILE C CG1 1 
ATOM   6784 C  CG2 . ILE C  1  204 ? -13.814 19.473  7.645  1.00 52.00  ? 217 ILE C CG2 1 
ATOM   6785 C  CD1 . ILE C  1  204 ? -13.116 21.294  10.089 1.00 56.92  ? 217 ILE C CD1 1 
ATOM   6786 N  N   . ASN C  1  205 ? -12.767 16.071  8.308  1.00 46.08  ? 218 ASN C N   1 
ATOM   6787 C  CA  . ASN C  1  205 ? -12.271 15.233  7.225  1.00 43.27  ? 218 ASN C CA  1 
ATOM   6788 C  C   . ASN C  1  205 ? -12.792 13.806  7.332  1.00 44.40  ? 218 ASN C C   1 
ATOM   6789 O  O   . ASN C  1  205 ? -12.867 13.134  6.310  1.00 47.77  ? 218 ASN C O   1 
ATOM   6790 C  CB  . ASN C  1  205 ? -10.747 15.191  7.165  1.00 41.26  ? 218 ASN C CB  1 
ATOM   6791 C  CG  . ASN C  1  205 ? -10.156 16.558  6.960  1.00 41.60  ? 218 ASN C CG  1 
ATOM   6792 O  OD1 . ASN C  1  205 ? -10.809 17.420  6.358  1.00 45.84  ? 218 ASN C OD1 1 
ATOM   6793 N  ND2 . ASN C  1  205 ? -8.959  16.785  7.486  1.00 41.57  ? 218 ASN C ND2 1 
ATOM   6794 N  N   . LEU C  1  206 ? -13.137 13.340  8.542  1.00 44.77  ? 219 LEU C N   1 
ATOM   6795 C  CA  . LEU C  1  206 ? -13.490 11.940  8.734  1.00 42.48  ? 219 LEU C CA  1 
ATOM   6796 C  C   . LEU C  1  206 ? -14.877 11.727  9.344  1.00 40.26  ? 219 LEU C C   1 
ATOM   6797 O  O   . LEU C  1  206 ? -15.424 10.644  9.160  1.00 40.27  ? 219 LEU C O   1 
ATOM   6798 C  CB  . LEU C  1  206 ? -12.396 11.298  9.587  1.00 45.11  ? 219 LEU C CB  1 
ATOM   6799 C  CG  . LEU C  1  206 ? -10.975 11.383  9.014  1.00 47.11  ? 219 LEU C CG  1 
ATOM   6800 C  CD1 . LEU C  1  206 ? -9.947  11.017  10.062 1.00 45.22  ? 219 LEU C CD1 1 
ATOM   6801 C  CD2 . LEU C  1  206 ? -10.807 10.492  7.783  1.00 48.37  ? 219 LEU C CD2 1 
ATOM   6802 N  N   . PHE C  1  207 ? -15.431 12.700  10.095 1.00 45.35  ? 220 PHE C N   1 
ATOM   6803 C  CA  . PHE C  1  207 ? -16.706 12.497  10.781 1.00 45.03  ? 220 PHE C CA  1 
ATOM   6804 C  C   . PHE C  1  207 ? -17.866 12.974  9.907  1.00 42.32  ? 220 PHE C C   1 
ATOM   6805 O  O   . PHE C  1  207 ? -19.007 12.586  10.128 1.00 50.32  ? 220 PHE C O   1 
ATOM   6806 C  CB  . PHE C  1  207 ? -16.783 13.195  12.142 1.00 48.30  ? 220 PHE C CB  1 
ATOM   6807 C  CG  . PHE C  1  207 ? -15.892 12.640  13.244 1.00 50.77  ? 220 PHE C CG  1 
ATOM   6808 C  CD1 . PHE C  1  207 ? -15.187 11.451  13.078 1.00 47.61  ? 220 PHE C CD1 1 
ATOM   6809 C  CD2 . PHE C  1  207 ? -15.812 13.286  14.475 1.00 51.92  ? 220 PHE C CD2 1 
ATOM   6810 C  CE1 . PHE C  1  207 ? -14.399 10.953  14.103 1.00 47.47  ? 220 PHE C CE1 1 
ATOM   6811 C  CE2 . PHE C  1  207 ? -15.017 12.781  15.491 1.00 47.19  ? 220 PHE C CE2 1 
ATOM   6812 C  CZ  . PHE C  1  207 ? -14.314 11.622  15.302 1.00 44.38  ? 220 PHE C CZ  1 
ATOM   6813 N  N   . VAL C  1  208 ? -17.563 13.825  8.924  1.00 41.72  ? 221 VAL C N   1 
ATOM   6814 C  CA  . VAL C  1  208 ? -18.536 14.289  7.953  1.00 45.30  ? 221 VAL C CA  1 
ATOM   6815 C  C   . VAL C  1  208 ? -18.684 13.235  6.860  1.00 46.84  ? 221 VAL C C   1 
ATOM   6816 O  O   . VAL C  1  208 ? -17.695 12.768  6.299  1.00 47.34  ? 221 VAL C O   1 
ATOM   6817 C  CB  . VAL C  1  208 ? -18.148 15.649  7.349  1.00 46.25  ? 221 VAL C CB  1 
ATOM   6818 C  CG1 . VAL C  1  208 ? -19.090 16.063  6.227  1.00 49.80  ? 221 VAL C CG1 1 
ATOM   6819 C  CG2 . VAL C  1  208 ? -18.094 16.733  8.414  1.00 45.53  ? 221 VAL C CG2 1 
ATOM   6820 N  N   . ASP C  1  209 ? -19.940 12.904  6.553  1.00 45.51  ? 222 ASP C N   1 
ATOM   6821 C  CA  . ASP C  1  209 ? -20.289 11.878  5.587  1.00 50.98  ? 222 ASP C CA  1 
ATOM   6822 C  C   . ASP C  1  209 ? -19.548 12.131  4.269  1.00 50.55  ? 222 ASP C C   1 
ATOM   6823 O  O   . ASP C  1  209 ? -19.429 13.271  3.828  1.00 44.35  ? 222 ASP C O   1 
ATOM   6824 C  CB  . ASP C  1  209 ? -21.803 11.802  5.440  1.00 45.67  ? 222 ASP C CB  1 
ATOM   6825 C  CG  . ASP C  1  209 ? -22.295 10.608  4.649  1.00 46.50  ? 222 ASP C CG  1 
ATOM   6826 O  OD1 . ASP C  1  209 ? -22.058 10.589  3.420  1.00 56.36  ? 222 ASP C OD1 1 
ATOM   6827 O  OD2 . ASP C  1  209 ? -22.861 9.693   5.263  1.00 47.16  ? 222 ASP C OD2 1 
ATOM   6828 N  N   . GLY C  1  210 ? -19.062 11.048  3.647  1.00 47.26  ? 223 GLY C N   1 
ATOM   6829 C  CA  . GLY C  1  210 ? -18.184 11.132  2.486  1.00 52.85  ? 223 GLY C CA  1 
ATOM   6830 C  C   . GLY C  1  210 ? -18.901 11.534  1.192  1.00 54.94  ? 223 GLY C C   1 
ATOM   6831 O  O   . GLY C  1  210 ? -18.234 11.983  0.256  1.00 50.11  ? 223 GLY C O   1 
ATOM   6832 N  N   . ARG C  1  211 ? -20.238 11.369  1.152  1.00 52.78  ? 224 ARG C N   1 
ATOM   6833 C  CA  . ARG C  1  211 ? -21.064 11.825  0.042  1.00 48.82  ? 224 ARG C CA  1 
ATOM   6834 C  C   . ARG C  1  211 ? -21.144 13.352  0.016  1.00 53.17  ? 224 ARG C C   1 
ATOM   6835 O  O   . ARG C  1  211 ? -21.510 13.922  -1.012 1.00 62.69  ? 224 ARG C O   1 
ATOM   6836 C  CB  . ARG C  1  211 ? -22.477 11.229  0.112  1.00 45.68  ? 224 ARG C CB  1 
ATOM   6837 C  CG  . ARG C  1  211 ? -22.503 9.723   -0.103 1.00 43.90  ? 224 ARG C CG  1 
ATOM   6838 C  CD  . ARG C  1  211 ? -23.788 9.079   0.336  1.00 51.36  ? 224 ARG C CD  1 
ATOM   6839 N  NE  . ARG C  1  211 ? -24.079 9.261   1.764  1.00 56.11  ? 224 ARG C NE  1 
ATOM   6840 C  CZ  . ARG C  1  211 ? -25.094 8.701   2.407  1.00 59.41  ? 224 ARG C CZ  1 
ATOM   6841 N  NH1 . ARG C  1  211 ? -25.956 7.939   1.748  1.00 60.58  ? 224 ARG C NH1 1 
ATOM   6842 N  NH2 . ARG C  1  211 ? -25.231 8.895   3.709  1.00 59.36  ? 224 ARG C NH2 1 
ATOM   6843 N  N   . VAL C  1  212 ? -20.822 14.015  1.136  1.00 51.51  ? 225 VAL C N   1 
ATOM   6844 C  CA  . VAL C  1  212 ? -20.833 15.471  1.203  1.00 58.63  ? 225 VAL C CA  1 
ATOM   6845 C  C   . VAL C  1  212 ? -19.498 15.966  0.652  1.00 60.68  ? 225 VAL C C   1 
ATOM   6846 O  O   . VAL C  1  212 ? -18.449 15.645  1.205  1.00 70.63  ? 225 VAL C O   1 
ATOM   6847 C  CB  . VAL C  1  212 ? -21.079 16.005  2.635  1.00 55.44  ? 225 VAL C CB  1 
ATOM   6848 C  CG1 . VAL C  1  212 ? -21.032 17.528  2.698  1.00 50.94  ? 225 VAL C CG1 1 
ATOM   6849 C  CG2 . VAL C  1  212 ? -22.381 15.478  3.235  1.00 57.57  ? 225 VAL C CG2 1 
ATOM   6850 N  N   . THR C  1  213 ? -19.519 16.748  -0.436 1.00 69.06  ? 226 THR C N   1 
ATOM   6851 C  CA  . THR C  1  213 ? -18.279 17.073  -1.139 1.00 66.49  ? 226 THR C CA  1 
ATOM   6852 C  C   . THR C  1  213 ? -18.022 18.575  -1.204 1.00 68.03  ? 226 THR C C   1 
ATOM   6853 O  O   . THR C  1  213 ? -16.888 18.967  -1.447 1.00 65.88  ? 226 THR C O   1 
ATOM   6854 C  CB  . THR C  1  213 ? -18.253 16.481  -2.549 1.00 69.65  ? 226 THR C CB  1 
ATOM   6855 O  OG1 . THR C  1  213 ? -19.305 17.064  -3.311 1.00 70.47  ? 226 THR C OG1 1 
ATOM   6856 C  CG2 . THR C  1  213 ? -18.436 14.976  -2.561 1.00 75.27  ? 226 THR C CG2 1 
ATOM   6857 N  N   . THR C  1  214 ? -19.057 19.411  -1.043 1.00 77.26  ? 227 THR C N   1 
ATOM   6858 C  CA  . THR C  1  214 ? -18.851 20.848  -0.949 1.00 80.38  ? 227 THR C CA  1 
ATOM   6859 C  C   . THR C  1  214 ? -19.207 21.289  0.474  1.00 78.36  ? 227 THR C C   1 
ATOM   6860 O  O   . THR C  1  214 ? -20.121 20.726  1.079  1.00 73.93  ? 227 THR C O   1 
ATOM   6861 C  CB  . THR C  1  214 ? -19.663 21.555  -2.043 1.00 80.46  ? 227 THR C CB  1 
ATOM   6862 O  OG1 . THR C  1  214 ? -19.200 22.899  -2.030 1.00 81.46  ? 227 THR C OG1 1 
ATOM   6863 C  CG2 . THR C  1  214 ? -21.168 21.530  -1.829 1.00 85.55  ? 227 THR C CG2 1 
ATOM   6864 N  N   . ASP C  1  215 ? -18.462 22.275  1.008  1.00 76.22  ? 228 ASP C N   1 
ATOM   6865 C  CA  . ASP C  1  215 ? -18.800 22.933  2.265  1.00 84.50  ? 228 ASP C CA  1 
ATOM   6866 C  C   . ASP C  1  215 ? -18.935 21.892  3.377  1.00 75.98  ? 228 ASP C C   1 
ATOM   6867 O  O   . ASP C  1  215 ? -19.963 21.817  4.049  1.00 70.12  ? 228 ASP C O   1 
ATOM   6868 C  CB  . ASP C  1  215 ? -20.066 23.779  2.141  1.00 94.17  ? 228 ASP C CB  1 
ATOM   6869 C  CG  . ASP C  1  215 ? -20.413 24.675  3.328  1.00 99.56  ? 228 ASP C CG  1 
ATOM   6870 O  OD1 . ASP C  1  215 ? -19.489 25.044  4.083  1.00 107.43 ? 228 ASP C OD1 1 
ATOM   6871 O  OD2 . ASP C  1  215 ? -21.612 24.983  3.504  1.00 99.35  ? 228 ASP C OD2 1 
ATOM   6872 N  N   . ARG C  1  216 ? -17.886 21.086  3.557  1.00 68.63  ? 229 ARG C N   1 
ATOM   6873 C  CA  . ARG C  1  216 ? -17.912 19.997  4.518  1.00 65.23  ? 229 ARG C CA  1 
ATOM   6874 C  C   . ARG C  1  216 ? -17.946 20.583  5.930  1.00 57.58  ? 229 ARG C C   1 
ATOM   6875 O  O   . ARG C  1  216 ? -17.102 21.396  6.288  1.00 54.78  ? 229 ARG C O   1 
ATOM   6876 C  CB  . ARG C  1  216 ? -16.745 19.033  4.258  1.00 63.28  ? 229 ARG C CB  1 
ATOM   6877 C  CG  . ARG C  1  216 ? -16.982 18.096  3.082  1.00 61.98  ? 229 ARG C CG  1 
ATOM   6878 C  CD  . ARG C  1  216 ? -15.754 17.252  2.746  1.00 60.15  ? 229 ARG C CD  1 
ATOM   6879 N  NE  . ARG C  1  216 ? -15.366 16.321  3.812  1.00 52.74  ? 229 ARG C NE  1 
ATOM   6880 C  CZ  . ARG C  1  216 ? -16.015 15.203  4.133  1.00 55.88  ? 229 ARG C CZ  1 
ATOM   6881 N  NH1 . ARG C  1  216 ? -17.057 14.787  3.424  1.00 50.05  ? 229 ARG C NH1 1 
ATOM   6882 N  NH2 . ARG C  1  216 ? -15.606 14.488  5.167  1.00 56.65  ? 229 ARG C NH2 1 
ATOM   6883 N  N   . LYS C  1  217 ? -18.954 20.174  6.708  1.00 57.46  ? 230 LYS C N   1 
ATOM   6884 C  CA  . LYS C  1  217 ? -19.196 20.706  8.039  1.00 61.60  ? 230 LYS C CA  1 
ATOM   6885 C  C   . LYS C  1  217 ? -19.977 19.665  8.842  1.00 57.74  ? 230 LYS C C   1 
ATOM   6886 O  O   . LYS C  1  217 ? -20.780 18.914  8.277  1.00 57.52  ? 230 LYS C O   1 
ATOM   6887 C  CB  . LYS C  1  217 ? -19.943 22.044  7.922  1.00 69.93  ? 230 LYS C CB  1 
ATOM   6888 C  CG  . LYS C  1  217 ? -21.327 21.987  7.282  1.00 75.41  ? 230 LYS C CG  1 
ATOM   6889 C  CD  . LYS C  1  217 ? -21.959 23.349  6.996  1.00 83.48  ? 230 LYS C CD  1 
ATOM   6890 C  CE  . LYS C  1  217 ? -23.330 23.220  6.387  1.00 87.32  ? 230 LYS C CE  1 
ATOM   6891 N  NZ  . LYS C  1  217 ? -23.948 24.521  6.117  1.00 92.62  ? 230 LYS C NZ  1 
ATOM   6892 N  N   . LEU C  1  218 ? -19.741 19.625  10.160 1.00 52.17  ? 231 LEU C N   1 
ATOM   6893 C  CA  . LEU C  1  218 ? -20.331 18.593  11.003 1.00 56.39  ? 231 LEU C CA  1 
ATOM   6894 C  C   . LEU C  1  218 ? -21.487 19.165  11.824 1.00 55.42  ? 231 LEU C C   1 
ATOM   6895 O  O   . LEU C  1  218 ? -21.322 20.171  12.506 1.00 59.89  ? 231 LEU C O   1 
ATOM   6896 C  CB  . LEU C  1  218 ? -19.244 18.007  11.903 1.00 53.40  ? 231 LEU C CB  1 
ATOM   6897 C  CG  . LEU C  1  218 ? -19.642 16.754  12.686 1.00 53.79  ? 231 LEU C CG  1 
ATOM   6898 C  CD1 . LEU C  1  218 ? -19.869 15.576  11.766 1.00 55.06  ? 231 LEU C CD1 1 
ATOM   6899 C  CD2 . LEU C  1  218 ? -18.598 16.421  13.737 1.00 54.11  ? 231 LEU C CD2 1 
ATOM   6900 N  N   . SER C  1  219 ? -22.653 18.509  11.760 1.00 55.81  ? 232 SER C N   1 
ATOM   6901 C  CA  . SER C  1  219 ? -23.792 18.873  12.591 1.00 59.24  ? 232 SER C CA  1 
ATOM   6902 C  C   . SER C  1  219 ? -23.496 18.496  14.044 1.00 67.68  ? 232 SER C C   1 
ATOM   6903 O  O   . SER C  1  219 ? -22.708 17.583  14.287 1.00 63.19  ? 232 SER C O   1 
ATOM   6904 C  CB  . SER C  1  219 ? -25.057 18.210  12.113 1.00 58.01  ? 232 SER C CB  1 
ATOM   6905 O  OG  . SER C  1  219 ? -25.057 16.821  12.414 1.00 63.54  ? 232 SER C OG  1 
ATOM   6906 N  N   . MET C  1  220 ? -24.142 19.185  15.000 1.00 65.11  ? 233 MET C N   1 
ATOM   6907 C  CA  . MET C  1  220 ? -23.949 18.894  16.415 1.00 60.74  ? 233 MET C CA  1 
ATOM   6908 C  C   . MET C  1  220 ? -24.514 17.519  16.777 1.00 58.06  ? 233 MET C C   1 
ATOM   6909 O  O   . MET C  1  220 ? -24.006 16.874  17.691 1.00 61.79  ? 233 MET C O   1 
ATOM   6910 C  CB  . MET C  1  220 ? -24.586 19.972  17.299 1.00 59.22  ? 233 MET C CB  1 
ATOM   6911 C  CG  . MET C  1  220 ? -24.000 21.361  17.122 1.00 58.28  ? 233 MET C CG  1 
ATOM   6912 S  SD  . MET C  1  220 ? -22.210 21.473  17.306 1.00 63.11  ? 233 MET C SD  1 
ATOM   6913 C  CE  . MET C  1  220 ? -21.603 21.308  15.623 1.00 64.06  ? 233 MET C CE  1 
ATOM   6914 N  N   . GLU C  1  221 ? -25.540 17.063  16.049 1.00 58.52  ? 234 GLU C N   1 
ATOM   6915 C  CA  . GLU C  1  221 ? -26.152 15.765  16.299 1.00 63.19  ? 234 GLU C CA  1 
ATOM   6916 C  C   . GLU C  1  221 ? -25.147 14.658  15.977 1.00 60.35  ? 234 GLU C C   1 
ATOM   6917 O  O   . GLU C  1  221 ? -24.988 13.720  16.752 1.00 61.48  ? 234 GLU C O   1 
ATOM   6918 C  CB  . GLU C  1  221 ? -27.456 15.596  15.512 1.00 70.07  ? 234 GLU C CB  1 
ATOM   6919 C  CG  . GLU C  1  221 ? -28.566 16.573  15.909 1.00 80.65  ? 234 GLU C CG  1 
ATOM   6920 C  CD  . GLU C  1  221 ? -28.516 18.006  15.365 1.00 84.98  ? 234 GLU C CD  1 
ATOM   6921 O  OE1 . GLU C  1  221 ? -27.664 18.369  14.504 1.00 77.91  ? 234 GLU C OE1 1 
ATOM   6922 O  OE2 . GLU C  1  221 ? -29.351 18.796  15.862 1.00 83.89  ? 234 GLU C OE2 1 
ATOM   6923 N  N   . ASP C  1  222 ? -24.473 14.786  14.828 1.00 55.16  ? 235 ASP C N   1 
ATOM   6924 C  CA  . ASP C  1  222 ? -23.463 13.833  14.393 1.00 52.33  ? 235 ASP C CA  1 
ATOM   6925 C  C   . ASP C  1  222 ? -22.256 13.892  15.337 1.00 47.17  ? 235 ASP C C   1 
ATOM   6926 O  O   . ASP C  1  222 ? -21.739 12.862  15.735 1.00 46.47  ? 235 ASP C O   1 
ATOM   6927 C  CB  . ASP C  1  222 ? -23.110 14.044  12.926 1.00 55.02  ? 235 ASP C CB  1 
ATOM   6928 C  CG  . ASP C  1  222 ? -24.175 13.635  11.912 1.00 58.12  ? 235 ASP C CG  1 
ATOM   6929 O  OD1 . ASP C  1  222 ? -25.186 13.030  12.328 1.00 60.07  ? 235 ASP C OD1 1 
ATOM   6930 O  OD2 . ASP C  1  222 ? -23.982 13.925  10.707 1.00 57.33  ? 235 ASP C OD2 1 
ATOM   6931 N  N   . ALA C  1  223 ? -21.819 15.097  15.710 1.00 47.63  ? 236 ALA C N   1 
ATOM   6932 C  CA  . ALA C  1  223 ? -20.762 15.261  16.703 1.00 50.90  ? 236 ALA C CA  1 
ATOM   6933 C  C   . ALA C  1  223 ? -21.113 14.558  18.015 1.00 57.14  ? 236 ALA C C   1 
ATOM   6934 O  O   . ALA C  1  223 ? -20.269 13.861  18.573 1.00 63.33  ? 236 ALA C O   1 
ATOM   6935 C  CB  . ALA C  1  223 ? -20.476 16.729  16.936 1.00 46.31  ? 236 ALA C CB  1 
ATOM   6936 N  N   . ALA C  1  224 ? -22.345 14.734  18.516 1.00 58.02  ? 237 ALA C N   1 
ATOM   6937 C  CA  . ALA C  1  224 ? -22.719 14.150  19.800 1.00 55.97  ? 237 ALA C CA  1 
ATOM   6938 C  C   . ALA C  1  224 ? -22.687 12.633  19.683 1.00 52.81  ? 237 ALA C C   1 
ATOM   6939 O  O   . ALA C  1  224 ? -22.209 11.934  20.572 1.00 57.52  ? 237 ALA C O   1 
ATOM   6940 C  CB  . ALA C  1  224 ? -24.089 14.637  20.241 1.00 56.11  ? 237 ALA C CB  1 
ATOM   6941 N  N   . SER C  1  225 ? -23.199 12.142  18.553 1.00 51.55  ? 238 SER C N   1 
ATOM   6942 C  CA  . SER C  1  225 ? -23.306 10.715  18.307 1.00 49.71  ? 238 SER C CA  1 
ATOM   6943 C  C   . SER C  1  225 ? -21.931 10.051  18.414 1.00 49.56  ? 238 SER C C   1 
ATOM   6944 O  O   . SER C  1  225 ? -21.812 9.003   19.024 1.00 49.86  ? 238 SER C O   1 
ATOM   6945 C  CB  . SER C  1  225 ? -23.965 10.472  16.963 1.00 45.53  ? 238 SER C CB  1 
ATOM   6946 O  OG  . SER C  1  225 ? -24.132 9.088   16.700 1.00 46.80  ? 238 SER C OG  1 
ATOM   6947 N  N   . ILE C  1  226 ? -20.888 10.663  17.839 1.00 48.49  ? 239 ILE C N   1 
ATOM   6948 C  CA  . ILE C  1  226 ? -19.565 10.051  17.807 1.00 51.75  ? 239 ILE C CA  1 
ATOM   6949 C  C   . ILE C  1  226 ? -18.833 10.328  19.121 1.00 45.10  ? 239 ILE C C   1 
ATOM   6950 O  O   . ILE C  1  226 ? -18.367 9.400   19.773 1.00 46.02  ? 239 ILE C O   1 
ATOM   6951 C  CB  . ILE C  1  226 ? -18.767 10.538  16.580 1.00 51.53  ? 239 ILE C CB  1 
ATOM   6952 C  CG1 . ILE C  1  226 ? -19.423 10.057  15.291 1.00 54.72  ? 239 ILE C CG1 1 
ATOM   6953 C  CG2 . ILE C  1  226 ? -17.305 10.097  16.666 1.00 53.64  ? 239 ILE C CG2 1 
ATOM   6954 C  CD1 . ILE C  1  226 ? -18.903 10.726  14.039 1.00 58.57  ? 239 ILE C CD1 1 
ATOM   6955 N  N   . PHE C  1  227 ? -18.733 11.609  19.486 1.00 43.29  ? 240 PHE C N   1 
ATOM   6956 C  CA  . PHE C  1  227 ? -17.952 12.036  20.635 1.00 51.08  ? 240 PHE C CA  1 
ATOM   6957 C  C   . PHE C  1  227 ? -18.505 11.510  21.961 1.00 52.21  ? 240 PHE C C   1 
ATOM   6958 O  O   . PHE C  1  227 ? -17.728 11.261  22.878 1.00 56.87  ? 240 PHE C O   1 
ATOM   6959 C  CB  . PHE C  1  227 ? -17.901 13.558  20.724 1.00 53.67  ? 240 PHE C CB  1 
ATOM   6960 C  CG  . PHE C  1  227 ? -16.895 14.247  19.816 1.00 56.66  ? 240 PHE C CG  1 
ATOM   6961 C  CD1 . PHE C  1  227 ? -15.530 14.144  20.064 1.00 53.07  ? 240 PHE C CD1 1 
ATOM   6962 C  CD2 . PHE C  1  227 ? -17.317 15.081  18.782 1.00 62.33  ? 240 PHE C CD2 1 
ATOM   6963 C  CE1 . PHE C  1  227 ? -14.612 14.819  19.276 1.00 52.88  ? 240 PHE C CE1 1 
ATOM   6964 C  CE2 . PHE C  1  227 ? -16.389 15.750  17.998 1.00 58.81  ? 240 PHE C CE2 1 
ATOM   6965 C  CZ  . PHE C  1  227 ? -15.042 15.623  18.253 1.00 53.99  ? 240 PHE C CZ  1 
ATOM   6966 N  N   . ARG C  1  228 ? -19.833 11.366  22.085 1.00 53.89  ? 241 ARG C N   1 
ATOM   6967 C  CA  . ARG C  1  228 ? -20.432 10.933  23.342 1.00 53.71  ? 241 ARG C CA  1 
ATOM   6968 C  C   . ARG C  1  228 ? -20.895 9.479   23.266 1.00 48.94  ? 241 ARG C C   1 
ATOM   6969 O  O   . ARG C  1  228 ? -20.583 8.711   24.163 1.00 51.35  ? 241 ARG C O   1 
ATOM   6970 C  CB  . ARG C  1  228 ? -21.593 11.840  23.776 1.00 61.92  ? 241 ARG C CB  1 
ATOM   6971 C  CG  . ARG C  1  228 ? -22.253 11.452  25.096 1.00 68.27  ? 241 ARG C CG  1 
ATOM   6972 C  CD  . ARG C  1  228 ? -23.570 12.180  25.302 1.00 67.16  ? 241 ARG C CD  1 
ATOM   6973 N  NE  . ARG C  1  228 ? -24.592 11.685  24.370 1.00 70.75  ? 241 ARG C NE  1 
ATOM   6974 C  CZ  . ARG C  1  228 ? -25.647 12.380  23.959 1.00 82.02  ? 241 ARG C CZ  1 
ATOM   6975 N  NH1 . ARG C  1  228 ? -25.775 13.665  24.260 1.00 89.49  ? 241 ARG C NH1 1 
ATOM   6976 N  NH2 . ARG C  1  228 ? -26.578 11.802  23.216 1.00 79.79  ? 241 ARG C NH2 1 
ATOM   6977 N  N   . ASP C  1  229 ? -21.626 9.088   22.212 1.00 49.17  ? 242 ASP C N   1 
ATOM   6978 C  CA  . ASP C  1  229 ? -22.280 7.786   22.200 1.00 47.07  ? 242 ASP C CA  1 
ATOM   6979 C  C   . ASP C  1  229 ? -21.476 6.724   21.465 1.00 43.72  ? 242 ASP C C   1 
ATOM   6980 O  O   . ASP C  1  229 ? -21.865 5.567   21.508 1.00 43.63  ? 242 ASP C O   1 
ATOM   6981 C  CB  . ASP C  1  229 ? -23.710 7.881   21.688 1.00 52.19  ? 242 ASP C CB  1 
ATOM   6982 C  CG  . ASP C  1  229 ? -24.630 8.721   22.562 1.00 57.02  ? 242 ASP C CG  1 
ATOM   6983 O  OD1 . ASP C  1  229 ? -24.474 8.636   23.812 1.00 52.84  ? 242 ASP C OD1 1 
ATOM   6984 O  OD2 . ASP C  1  229 ? -25.475 9.459   21.990 1.00 64.98  ? 242 ASP C OD2 1 
ATOM   6985 N  N   . MET C  1  230 ? -20.362 7.105   20.820 1.00 44.59  ? 243 MET C N   1 
ATOM   6986 C  CA  . MET C  1  230 ? -19.484 6.164   20.138 1.00 43.36  ? 243 MET C CA  1 
ATOM   6987 C  C   . MET C  1  230 ? -20.244 5.468   19.008 1.00 41.64  ? 243 MET C C   1 
ATOM   6988 O  O   . MET C  1  230 ? -20.091 4.260   18.813 1.00 39.55  ? 243 MET C O   1 
ATOM   6989 C  CB  . MET C  1  230 ? -18.951 5.098   21.106 1.00 45.00  ? 243 MET C CB  1 
ATOM   6990 C  CG  . MET C  1  230 ? -18.355 5.648   22.392 1.00 47.45  ? 243 MET C CG  1 
ATOM   6991 S  SD  . MET C  1  230 ? -18.008 4.346   23.593 1.00 48.78  ? 243 MET C SD  1 
ATOM   6992 C  CE  . MET C  1  230 ? -17.573 5.396   24.989 1.00 53.14  ? 243 MET C CE  1 
ATOM   6993 N  N   . ARG C  1  231 ? -21.080 6.234   18.295 1.00 46.73  ? 244 ARG C N   1 
ATOM   6994 C  CA  . ARG C  1  231 ? -22.019 5.704   17.314 1.00 50.33  ? 244 ARG C CA  1 
ATOM   6995 C  C   . ARG C  1  231 ? -21.860 6.482   16.008 1.00 45.80  ? 244 ARG C C   1 
ATOM   6996 O  O   . ARG C  1  231 ? -21.860 7.716   15.989 1.00 39.19  ? 244 ARG C O   1 
ATOM   6997 C  CB  . ARG C  1  231 ? -23.456 5.797   17.846 1.00 54.52  ? 244 ARG C CB  1 
ATOM   6998 C  CG  . ARG C  1  231 ? -24.505 5.000   17.088 1.00 62.27  ? 244 ARG C CG  1 
ATOM   6999 C  CD  . ARG C  1  231 ? -25.857 5.026   17.812 1.00 67.79  ? 244 ARG C CD  1 
ATOM   7000 N  NE  . ARG C  1  231 ? -26.697 3.876   17.456 1.00 74.45  ? 244 ARG C NE  1 
ATOM   7001 C  CZ  . ARG C  1  231 ? -27.739 3.402   18.141 1.00 81.09  ? 244 ARG C CZ  1 
ATOM   7002 N  NH1 . ARG C  1  231 ? -28.008 3.846   19.360 1.00 82.78  ? 244 ARG C NH1 1 
ATOM   7003 N  NH2 . ARG C  1  231 ? -28.475 2.430   17.623 1.00 76.25  ? 244 ARG C NH2 1 
ATOM   7004 N  N   . PHE C  1  232 ? -21.711 5.745   14.908 1.00 44.63  ? 245 PHE C N   1 
ATOM   7005 C  CA  . PHE C  1  232 ? -21.816 6.346   13.589 1.00 45.75  ? 245 PHE C CA  1 
ATOM   7006 C  C   . PHE C  1  232 ? -23.206 6.942   13.405 1.00 46.51  ? 245 PHE C C   1 
ATOM   7007 O  O   . PHE C  1  232 ? -24.194 6.363   13.857 1.00 48.71  ? 245 PHE C O   1 
ATOM   7008 C  CB  . PHE C  1  232 ? -21.623 5.325   12.468 1.00 44.29  ? 245 PHE C CB  1 
ATOM   7009 C  CG  . PHE C  1  232 ? -20.206 4.799   12.312 1.00 44.49  ? 245 PHE C CG  1 
ATOM   7010 C  CD1 . PHE C  1  232 ? -19.177 5.643   11.906 1.00 42.99  ? 245 PHE C CD1 1 
ATOM   7011 C  CD2 . PHE C  1  232 ? -19.925 3.450   12.508 1.00 46.70  ? 245 PHE C CD2 1 
ATOM   7012 C  CE1 . PHE C  1  232 ? -17.894 5.153   11.730 1.00 43.75  ? 245 PHE C CE1 1 
ATOM   7013 C  CE2 . PHE C  1  232 ? -18.643 2.959   12.321 1.00 47.86  ? 245 PHE C CE2 1 
ATOM   7014 C  CZ  . PHE C  1  232 ? -17.633 3.809   11.931 1.00 45.09  ? 245 PHE C CZ  1 
ATOM   7015 N  N   . PRO C  1  233 ? -23.321 8.108   12.735 1.00 48.72  ? 246 PRO C N   1 
ATOM   7016 C  CA  . PRO C  1  233 ? -24.607 8.578   12.212 1.00 48.85  ? 246 PRO C CA  1 
ATOM   7017 C  C   . PRO C  1  233 ? -25.323 7.502   11.410 1.00 50.80  ? 246 PRO C C   1 
ATOM   7018 O  O   . PRO C  1  233 ? -24.674 6.621   10.845 1.00 44.10  ? 246 PRO C O   1 
ATOM   7019 C  CB  . PRO C  1  233 ? -24.220 9.786   11.328 1.00 51.96  ? 246 PRO C CB  1 
ATOM   7020 C  CG  . PRO C  1  233 ? -22.925 10.301  11.951 1.00 51.36  ? 246 PRO C CG  1 
ATOM   7021 C  CD  . PRO C  1  233 ? -22.217 9.052   12.479 1.00 49.80  ? 246 PRO C CD  1 
ATOM   7022 N  N   . ASP C  1  234 ? -26.663 7.562   11.386 1.00 52.86  ? 247 ASP C N   1 
ATOM   7023 C  CA  . ASP C  1  234 ? -27.460 6.659   10.569 1.00 53.92  ? 247 ASP C CA  1 
ATOM   7024 C  C   . ASP C  1  234 ? -26.966 6.746   9.127  1.00 49.79  ? 247 ASP C C   1 
ATOM   7025 O  O   . ASP C  1  234 ? -26.701 7.839   8.627  1.00 43.24  ? 247 ASP C O   1 
ATOM   7026 C  CB  . ASP C  1  234 ? -28.951 6.974   10.649 1.00 62.90  ? 247 ASP C CB  1 
ATOM   7027 C  CG  . ASP C  1  234 ? -29.621 6.725   11.996 1.00 74.53  ? 247 ASP C CG  1 
ATOM   7028 O  OD1 . ASP C  1  234 ? -29.014 6.017   12.822 1.00 82.14  ? 247 ASP C OD1 1 
ATOM   7029 O  OD2 . ASP C  1  234 ? -30.731 7.262   12.216 1.00 92.64  ? 247 ASP C OD2 1 
ATOM   7030 N  N   . ASP C  1  235 ? -26.815 5.586   8.475  1.00 45.56  ? 248 ASP C N   1 
ATOM   7031 C  CA  . ASP C  1  235 ? -26.476 5.527   7.061  1.00 55.56  ? 248 ASP C CA  1 
ATOM   7032 C  C   . ASP C  1  235 ? -25.110 6.175   6.777  1.00 54.21  ? 248 ASP C C   1 
ATOM   7033 O  O   . ASP C  1  235 ? -24.873 6.707   5.694  1.00 52.90  ? 248 ASP C O   1 
ATOM   7034 C  CB  . ASP C  1  235 ? -27.599 6.127   6.224  1.00 54.95  ? 248 ASP C CB  1 
ATOM   7035 C  CG  . ASP C  1  235 ? -27.476 5.881   4.724  1.00 54.77  ? 248 ASP C CG  1 
ATOM   7036 O  OD1 . ASP C  1  235 ? -27.349 4.708   4.338  1.00 50.50  ? 248 ASP C OD1 1 
ATOM   7037 O  OD2 . ASP C  1  235 ? -27.484 6.865   3.952  1.00 50.38  ? 248 ASP C OD2 1 
ATOM   7038 N  N   . PHE C  1  236 ? -24.185 6.121   7.735  1.00 50.74  ? 249 PHE C N   1 
ATOM   7039 C  CA  . PHE C  1  236 ? -22.934 6.853   7.610  1.00 48.01  ? 249 PHE C CA  1 
ATOM   7040 C  C   . PHE C  1  236 ? -22.054 6.246   6.512  1.00 45.29  ? 249 PHE C C   1 
ATOM   7041 O  O   . PHE C  1  236 ? -21.796 5.039   6.464  1.00 37.16  ? 249 PHE C O   1 
ATOM   7042 C  CB  . PHE C  1  236 ? -22.145 6.883   8.918  1.00 45.88  ? 249 PHE C CB  1 
ATOM   7043 C  CG  . PHE C  1  236 ? -20.858 7.674   8.810  1.00 41.22  ? 249 PHE C CG  1 
ATOM   7044 C  CD1 . PHE C  1  236 ? -20.876 9.056   8.765  1.00 39.64  ? 249 PHE C CD1 1 
ATOM   7045 C  CD2 . PHE C  1  236 ? -19.631 7.029   8.757  1.00 43.40  ? 249 PHE C CD2 1 
ATOM   7046 C  CE1 . PHE C  1  236 ? -19.693 9.770   8.678  1.00 39.36  ? 249 PHE C CE1 1 
ATOM   7047 C  CE2 . PHE C  1  236 ? -18.453 7.749   8.662  1.00 37.10  ? 249 PHE C CE2 1 
ATOM   7048 C  CZ  . PHE C  1  236 ? -18.485 9.117   8.617  1.00 35.98  ? 249 PHE C CZ  1 
ATOM   7049 N  N   . HIS C  1  237 ? -21.594 7.129   5.630  1.00 40.28  ? 250 HIS C N   1 
ATOM   7050 C  CA  . HIS C  1  237 ? -20.678 6.774   4.564  1.00 44.89  ? 250 HIS C CA  1 
ATOM   7051 C  C   . HIS C  1  237 ? -19.344 7.462   4.837  1.00 41.68  ? 250 HIS C C   1 
ATOM   7052 O  O   . HIS C  1  237 ? -19.292 8.678   5.001  1.00 36.94  ? 250 HIS C O   1 
ATOM   7053 C  CB  . HIS C  1  237 ? -21.243 7.179   3.191  1.00 47.67  ? 250 HIS C CB  1 
ATOM   7054 C  CG  . HIS C  1  237 ? -22.335 6.297   2.669  1.00 53.63  ? 250 HIS C CG  1 
ATOM   7055 N  ND1 . HIS C  1  237 ? -23.500 6.032   3.353  1.00 58.16  ? 250 HIS C ND1 1 
ATOM   7056 C  CD2 . HIS C  1  237 ? -22.439 5.656   1.502  1.00 53.31  ? 250 HIS C CD2 1 
ATOM   7057 C  CE1 . HIS C  1  237 ? -24.259 5.236   2.620  1.00 61.09  ? 250 HIS C CE1 1 
ATOM   7058 N  NE2 . HIS C  1  237 ? -23.627 4.981   1.496  1.00 55.33  ? 250 HIS C NE2 1 
ATOM   7059 N  N   . ARG C  1  238 ? -18.261 6.683   4.858  1.00 44.35  ? 251 ARG C N   1 
ATOM   7060 C  CA  . ARG C  1  238 ? -16.937 7.229   5.141  1.00 43.91  ? 251 ARG C CA  1 
ATOM   7061 C  C   . ARG C  1  238 ? -16.456 8.155   4.024  1.00 41.72  ? 251 ARG C C   1 
ATOM   7062 O  O   . ARG C  1  238 ? -17.006 8.158   2.925  1.00 44.81  ? 251 ARG C O   1 
ATOM   7063 C  CB  . ARG C  1  238 ? -15.928 6.092   5.309  1.00 45.11  ? 251 ARG C CB  1 
ATOM   7064 C  CG  . ARG C  1  238 ? -15.711 5.317   4.017  1.00 48.81  ? 251 ARG C CG  1 
ATOM   7065 C  CD  . ARG C  1  238 ? -14.682 4.221   4.175  1.00 45.75  ? 251 ARG C CD  1 
ATOM   7066 N  NE  . ARG C  1  238 ? -14.197 3.834   2.848  1.00 49.64  ? 251 ARG C NE  1 
ATOM   7067 C  CZ  . ARG C  1  238 ? -13.478 2.762   2.552  1.00 46.76  ? 251 ARG C CZ  1 
ATOM   7068 N  NH1 . ARG C  1  238 ? -13.048 1.967   3.508  1.00 45.99  ? 251 ARG C NH1 1 
ATOM   7069 N  NH2 . ARG C  1  238 ? -13.185 2.502   1.287  1.00 47.02  ? 251 ARG C NH2 1 
ATOM   7070 N  N   . SER C  1  239 ? -15.397 8.914   4.324  1.00 40.23  ? 252 SER C N   1 
ATOM   7071 C  CA  . SER C  1  239 ? -14.691 9.766   3.379  1.00 41.74  ? 252 SER C CA  1 
ATOM   7072 C  C   . SER C  1  239 ? -14.483 9.047   2.054  1.00 39.66  ? 252 SER C C   1 
ATOM   7073 O  O   . SER C  1  239 ? -14.143 7.868   2.049  1.00 38.36  ? 252 SER C O   1 
ATOM   7074 C  CB  . SER C  1  239 ? -13.355 10.186  3.939  1.00 43.99  ? 252 SER C CB  1 
ATOM   7075 O  OG  . SER C  1  239 ? -12.627 10.992  3.023  1.00 46.50  ? 252 SER C OG  1 
ATOM   7076 N  N   . ALA C  1  240 ? -14.674 9.773   0.945  1.00 41.20  ? 253 ALA C N   1 
ATOM   7077 C  CA  . ALA C  1  240 ? -14.579 9.177   -0.385 1.00 44.66  ? 253 ALA C CA  1 
ATOM   7078 C  C   . ALA C  1  240 ? -13.112 9.052   -0.804 1.00 43.46  ? 253 ALA C C   1 
ATOM   7079 O  O   . ALA C  1  240 ? -12.826 8.424   -1.822 1.00 40.78  ? 253 ALA C O   1 
ATOM   7080 C  CB  . ALA C  1  240 ? -15.368 9.989   -1.393 1.00 39.83  ? 253 ALA C CB  1 
ATOM   7081 N  N   . VAL C  1  241 ? -12.202 9.650   -0.012 1.00 43.96  ? 254 VAL C N   1 
ATOM   7082 C  CA  . VAL C  1  241 ? -10.758 9.565   -0.220 1.00 42.63  ? 254 VAL C CA  1 
ATOM   7083 C  C   . VAL C  1  241 ? -10.091 9.208   1.105  1.00 44.99  ? 254 VAL C C   1 
ATOM   7084 O  O   . VAL C  1  241 ? -10.571 9.617   2.162  1.00 43.59  ? 254 VAL C O   1 
ATOM   7085 C  CB  . VAL C  1  241 ? -10.163 10.889  -0.742 1.00 44.38  ? 254 VAL C CB  1 
ATOM   7086 C  CG1 . VAL C  1  241 ? -10.600 11.171  -2.170 1.00 49.77  ? 254 VAL C CG1 1 
ATOM   7087 C  CG2 . VAL C  1  241 ? -10.517 12.068  0.169  1.00 48.22  ? 254 VAL C CG2 1 
ATOM   7088 N  N   . PRO C  1  242 ? -8.924  8.519   1.102  1.00 47.01  ? 255 PRO C N   1 
ATOM   7089 C  CA  . PRO C  1  242 ? -8.094  8.403   2.304  1.00 44.42  ? 255 PRO C CA  1 
ATOM   7090 C  C   . PRO C  1  242 ? -7.746  9.793   2.824  1.00 42.75  ? 255 PRO C C   1 
ATOM   7091 O  O   . PRO C  1  242 ? -7.421  10.677  2.033  1.00 43.13  ? 255 PRO C O   1 
ATOM   7092 C  CB  . PRO C  1  242 ? -6.846  7.629   1.842  1.00 44.35  ? 255 PRO C CB  1 
ATOM   7093 C  CG  . PRO C  1  242 ? -7.313  6.904   0.603  1.00 44.36  ? 255 PRO C CG  1 
ATOM   7094 C  CD  . PRO C  1  242 ? -8.320  7.839   -0.054 1.00 44.75  ? 255 PRO C CD  1 
ATOM   7095 N  N   . ALA C  1  243 ? -7.850  10.003  4.144  1.00 45.98  ? 256 ALA C N   1 
ATOM   7096 C  CA  . ALA C  1  243 ? -7.673  11.343  4.685  1.00 44.38  ? 256 ALA C CA  1 
ATOM   7097 C  C   . ALA C  1  243 ? -7.103  11.290  6.097  1.00 41.00  ? 256 ALA C C   1 
ATOM   7098 O  O   . ALA C  1  243 ? -7.209  10.272  6.766  1.00 40.30  ? 256 ALA C O   1 
ATOM   7099 C  CB  . ALA C  1  243 ? -8.990  12.091  4.651  1.00 50.11  ? 256 ALA C CB  1 
ATOM   7100 N  N   . SER C  1  244 ? -6.510  12.414  6.518  1.00 45.01  ? 257 SER C N   1 
ATOM   7101 C  CA  . SER C  1  244 ? -5.779  12.541  7.773  1.00 45.79  ? 257 SER C CA  1 
ATOM   7102 C  C   . SER C  1  244 ? -5.947  13.985  8.275  1.00 47.18  ? 257 SER C C   1 
ATOM   7103 O  O   . SER C  1  244 ? -7.068  14.376  8.604  1.00 38.77  ? 257 SER C O   1 
ATOM   7104 C  CB  . SER C  1  244 ? -4.330  12.117  7.613  1.00 43.55  ? 257 SER C CB  1 
ATOM   7105 O  OG  . SER C  1  244 ? -3.696  12.785  6.532  1.00 53.03  ? 257 SER C OG  1 
ATOM   7106 N  N   . ASN C  1  245 ? -4.883  14.807  8.246  1.00 49.82  ? 258 ASN C N   1 
ATOM   7107 C  CA  . ASN C  1  245 ? -4.910  16.097  8.927  1.00 46.74  ? 258 ASN C CA  1 
ATOM   7108 C  C   . ASN C  1  245 ? -4.934  17.274  7.952  1.00 44.78  ? 258 ASN C C   1 
ATOM   7109 O  O   . ASN C  1  245 ? -4.363  18.327  8.233  1.00 48.80  ? 258 ASN C O   1 
ATOM   7110 C  CB  . ASN C  1  245 ? -3.756  16.254  9.915  1.00 50.54  ? 258 ASN C CB  1 
ATOM   7111 C  CG  . ASN C  1  245 ? -2.393  16.083  9.295  1.00 51.13  ? 258 ASN C CG  1 
ATOM   7112 O  OD1 . ASN C  1  245 ? -2.276  15.700  8.126  1.00 54.25  ? 258 ASN C OD1 1 
ATOM   7113 N  ND2 . ASN C  1  245 ? -1.354  16.333  10.075 1.00 53.43  ? 258 ASN C ND2 1 
ATOM   7114 N  N   . GLU C  1  246 ? -5.649  17.128  6.833  1.00 46.79  ? 259 GLU C N   1 
ATOM   7115 C  CA  . GLU C  1  246 ? -5.775  18.206  5.864  1.00 51.39  ? 259 GLU C CA  1 
ATOM   7116 C  C   . GLU C  1  246 ? -6.455  19.398  6.536  1.00 52.87  ? 259 GLU C C   1 
ATOM   7117 O  O   . GLU C  1  246 ? -7.497  19.237  7.173  1.00 48.80  ? 259 GLU C O   1 
ATOM   7118 C  CB  . GLU C  1  246 ? -6.561  17.783  4.620  1.00 53.43  ? 259 GLU C CB  1 
ATOM   7119 C  CG  . GLU C  1  246 ? -5.851  16.729  3.772  1.00 53.57  ? 259 GLU C CG  1 
ATOM   7120 C  CD  . GLU C  1  246 ? -6.039  15.292  4.203  1.00 54.36  ? 259 GLU C CD  1 
ATOM   7121 O  OE1 . GLU C  1  246 ? -6.685  15.034  5.251  1.00 55.61  ? 259 GLU C OE1 1 
ATOM   7122 O  OE2 . GLU C  1  246 ? -5.533  14.425  3.460  1.00 52.97  ? 259 GLU C OE2 1 
ATOM   7123 N  N   . GLY C  1  247 ? -5.829  20.577  6.404  1.00 49.31  ? 260 GLY C N   1 
ATOM   7124 C  CA  . GLY C  1  247 ? -6.362  21.823  6.932  1.00 53.23  ? 260 GLY C CA  1 
ATOM   7125 C  C   . GLY C  1  247 ? -5.764  22.198  8.290  1.00 57.03  ? 260 GLY C C   1 
ATOM   7126 O  O   . GLY C  1  247 ? -6.042  23.280  8.812  1.00 60.58  ? 260 GLY C O   1 
ATOM   7127 N  N   . ALA C  1  248 ? -4.942  21.312  8.866  1.00 53.83  ? 261 ALA C N   1 
ATOM   7128 C  CA  . ALA C  1  248 ? -4.385  21.544  10.189 1.00 58.01  ? 261 ALA C CA  1 
ATOM   7129 C  C   . ALA C  1  248 ? -3.453  22.756  10.179 1.00 60.50  ? 261 ALA C C   1 
ATOM   7130 O  O   . ALA C  1  248 ? -3.341  23.453  11.185 1.00 59.02  ? 261 ALA C O   1 
ATOM   7131 C  CB  . ALA C  1  248 ? -3.670  20.307  10.683 1.00 55.94  ? 261 ALA C CB  1 
ATOM   7132 N  N   . ASP C  1  249 ? -2.794  22.998  9.038  1.00 60.95  ? 262 ASP C N   1 
ATOM   7133 C  CA  . ASP C  1  249 ? -1.942  24.162  8.847  1.00 64.58  ? 262 ASP C CA  1 
ATOM   7134 C  C   . ASP C  1  249 ? -2.754  25.457  8.965  1.00 63.37  ? 262 ASP C C   1 
ATOM   7135 O  O   . ASP C  1  249 ? -2.276  26.439  9.527  1.00 62.76  ? 262 ASP C O   1 
ATOM   7136 C  CB  . ASP C  1  249 ? -1.157  24.063  7.543  1.00 70.88  ? 262 ASP C CB  1 
ATOM   7137 C  CG  . ASP C  1  249 ? -1.937  23.822  6.249  1.00 84.25  ? 262 ASP C CG  1 
ATOM   7138 O  OD1 . ASP C  1  249 ? -3.145  23.486  6.309  1.00 81.46  ? 262 ASP C OD1 1 
ATOM   7139 O  OD2 . ASP C  1  249 ? -1.333  23.989  5.169  1.00 98.08  ? 262 ASP C OD2 1 
ATOM   7140 N  N   . GLN C  1  250 ? -3.988  25.462  8.446  1.00 65.02  ? 263 GLN C N   1 
ATOM   7141 C  CA  . GLN C  1  250 ? -4.841  26.638  8.517  1.00 64.68  ? 263 GLN C CA  1 
ATOM   7142 C  C   . GLN C  1  250 ? -5.267  26.911  9.960  1.00 63.74  ? 263 GLN C C   1 
ATOM   7143 O  O   . GLN C  1  250 ? -5.407  28.066  10.345 1.00 68.94  ? 263 GLN C O   1 
ATOM   7144 C  CB  . GLN C  1  250 ? -6.042  26.507  7.580  1.00 65.22  ? 263 GLN C CB  1 
ATOM   7145 C  CG  . GLN C  1  250 ? -5.675  26.563  6.100  1.00 67.13  ? 263 GLN C CG  1 
ATOM   7146 C  CD  . GLN C  1  250 ? -6.877  26.512  5.181  1.00 70.91  ? 263 GLN C CD  1 
ATOM   7147 O  OE1 . GLN C  1  250 ? -8.034  26.464  5.613  1.00 85.49  ? 263 GLN C OE1 1 
ATOM   7148 N  NE2 . GLN C  1  250 ? -6.612  26.540  3.885  1.00 73.40  ? 263 GLN C NE2 1 
ATOM   7149 N  N   . VAL C  1  251 ? -5.466  25.858  10.762 1.00 63.99  ? 264 VAL C N   1 
ATOM   7150 C  CA  . VAL C  1  251 ? -5.880  26.020  12.147 1.00 61.90  ? 264 VAL C CA  1 
ATOM   7151 C  C   . VAL C  1  251 ? -4.773  26.726  12.931 1.00 63.85  ? 264 VAL C C   1 
ATOM   7152 O  O   . VAL C  1  251 ? -5.053  27.616  13.733 1.00 68.39  ? 264 VAL C O   1 
ATOM   7153 C  CB  . VAL C  1  251 ? -6.265  24.660  12.767 1.00 62.23  ? 264 VAL C CB  1 
ATOM   7154 C  CG1 . VAL C  1  251 ? -6.422  24.719  14.281 1.00 61.67  ? 264 VAL C CG1 1 
ATOM   7155 C  CG2 . VAL C  1  251 ? -7.537  24.097  12.142 1.00 61.43  ? 264 VAL C CG2 1 
ATOM   7156 N  N   . LEU C  1  252 ? -3.520  26.318  12.696 1.00 63.41  ? 265 LEU C N   1 
ATOM   7157 C  CA  . LEU C  1  252 ? -2.368  26.949  13.317 1.00 65.08  ? 265 LEU C CA  1 
ATOM   7158 C  C   . LEU C  1  252 ? -2.222  28.392  12.828 1.00 70.09  ? 265 LEU C C   1 
ATOM   7159 O  O   . LEU C  1  252 ? -1.899  29.274  13.616 1.00 67.40  ? 265 LEU C O   1 
ATOM   7160 C  CB  . LEU C  1  252 ? -1.109  26.135  13.022 1.00 59.36  ? 265 LEU C CB  1 
ATOM   7161 C  CG  . LEU C  1  252 ? 0.191   26.628  13.660 1.00 62.37  ? 265 LEU C CG  1 
ATOM   7162 C  CD1 . LEU C  1  252 ? 0.103   26.608  15.184 1.00 64.08  ? 265 LEU C CD1 1 
ATOM   7163 C  CD2 . LEU C  1  252 ? 1.369   25.790  13.181 1.00 58.59  ? 265 LEU C CD2 1 
ATOM   7164 N  N   . ALA C  1  253 ? -2.455  28.627  11.530 1.00 71.32  ? 266 ALA C N   1 
ATOM   7165 C  CA  . ALA C  1  253 ? -2.276  29.944  10.939 1.00 68.48  ? 266 ALA C CA  1 
ATOM   7166 C  C   . ALA C  1  253 ? -3.252  30.961  11.540 1.00 70.47  ? 266 ALA C C   1 
ATOM   7167 O  O   . ALA C  1  253 ? -2.903  32.128  11.680 1.00 73.15  ? 266 ALA C O   1 
ATOM   7168 C  CB  . ALA C  1  253 ? -2.426  29.855  9.436  1.00 71.81  ? 266 ALA C CB  1 
ATOM   7169 N  N   . ALA C  1  254 ? -4.468  30.523  11.896 1.00 67.66  ? 267 ALA C N   1 
ATOM   7170 C  CA  . ALA C  1  254 ? -5.495  31.399  12.445 1.00 66.73  ? 267 ALA C CA  1 
ATOM   7171 C  C   . ALA C  1  254 ? -5.057  32.006  13.779 1.00 73.29  ? 267 ALA C C   1 
ATOM   7172 O  O   . ALA C  1  254 ? -5.395  33.152  14.065 1.00 79.66  ? 267 ALA C O   1 
ATOM   7173 C  CB  . ALA C  1  254 ? -6.793  30.639  12.600 1.00 65.01  ? 267 ALA C CB  1 
ATOM   7174 N  N   . HIS C  1  255 ? -4.343  31.232  14.608 1.00 74.25  ? 268 HIS C N   1 
ATOM   7175 C  CA  . HIS C  1  255 ? -3.779  31.739  15.850 1.00 72.92  ? 268 HIS C CA  1 
ATOM   7176 C  C   . HIS C  1  255 ? -2.402  31.119  16.070 1.00 70.65  ? 268 HIS C C   1 
ATOM   7177 O  O   . HIS C  1  255 ? -2.267  30.133  16.790 1.00 66.78  ? 268 HIS C O   1 
ATOM   7178 C  CB  . HIS C  1  255 ? -4.726  31.489  17.029 1.00 75.79  ? 268 HIS C CB  1 
ATOM   7179 C  CG  . HIS C  1  255 ? -5.999  32.270  16.967 1.00 82.10  ? 268 HIS C CG  1 
ATOM   7180 N  ND1 . HIS C  1  255 ? -6.059  33.629  17.190 1.00 83.23  ? 268 HIS C ND1 1 
ATOM   7181 C  CD2 . HIS C  1  255 ? -7.250  31.885  16.682 1.00 84.16  ? 268 HIS C CD2 1 
ATOM   7182 C  CE1 . HIS C  1  255 ? -7.311  34.037  17.058 1.00 82.37  ? 268 HIS C CE1 1 
ATOM   7183 N  NE2 . HIS C  1  255 ? -8.054  32.993  16.754 1.00 81.81  ? 268 HIS C NE2 1 
ATOM   7184 N  N   . PRO C  1  256 ? -1.340  31.672  15.437 1.00 73.66  ? 269 PRO C N   1 
ATOM   7185 C  CA  . PRO C  1  256 ? 0.016   31.138  15.577 1.00 72.85  ? 269 PRO C CA  1 
ATOM   7186 C  C   . PRO C  1  256 ? 0.381   30.913  17.039 1.00 77.14  ? 269 PRO C C   1 
ATOM   7187 O  O   . PRO C  1  256 ? 0.134   31.779  17.874 1.00 81.85  ? 269 PRO C O   1 
ATOM   7188 C  CB  . PRO C  1  256 ? 0.899   32.193  14.901 1.00 70.26  ? 269 PRO C CB  1 
ATOM   7189 C  CG  . PRO C  1  256 ? -0.017  32.816  13.874 1.00 73.77  ? 269 PRO C CG  1 
ATOM   7190 C  CD  . PRO C  1  256 ? -1.399  32.824  14.526 1.00 74.74  ? 269 PRO C CD  1 
ATOM   7191 N  N   . TRP C  1  257 ? 0.943   29.731  17.320 1.00 74.89  ? 270 TRP C N   1 
ATOM   7192 C  CA  . TRP C  1  257 ? 1.259   29.309  18.672 1.00 72.57  ? 270 TRP C CA  1 
ATOM   7193 C  C   . TRP C  1  257 ? 2.534   28.469  18.654 1.00 70.45  ? 270 TRP C C   1 
ATOM   7194 O  O   . TRP C  1  257 ? 2.839   27.814  17.657 1.00 77.99  ? 270 TRP C O   1 
ATOM   7195 C  CB  . TRP C  1  257 ? 0.069   28.541  19.258 1.00 75.78  ? 270 TRP C CB  1 
ATOM   7196 C  CG  . TRP C  1  257 ? 0.255   28.133  20.693 1.00 81.40  ? 270 TRP C CG  1 
ATOM   7197 C  CD1 . TRP C  1  257 ? 0.620   26.903  21.148 1.00 83.79  ? 270 TRP C CD1 1 
ATOM   7198 C  CD2 . TRP C  1  257 ? 0.108   28.972  21.856 1.00 84.60  ? 270 TRP C CD2 1 
ATOM   7199 N  NE1 . TRP C  1  257 ? 0.687   26.906  22.513 1.00 85.81  ? 270 TRP C NE1 1 
ATOM   7200 C  CE2 . TRP C  1  257 ? 0.382   28.157  22.973 1.00 84.48  ? 270 TRP C CE2 1 
ATOM   7201 C  CE3 . TRP C  1  257 ? -0.234  30.316  22.064 1.00 82.96  ? 270 TRP C CE3 1 
ATOM   7202 C  CZ2 . TRP C  1  257 ? 0.330   28.649  24.271 1.00 92.79  ? 270 TRP C CZ2 1 
ATOM   7203 C  CZ3 . TRP C  1  257 ? -0.275  30.801  23.351 1.00 82.80  ? 270 TRP C CZ3 1 
ATOM   7204 C  CH2 . TRP C  1  257 ? 0.011   29.978  24.436 1.00 90.04  ? 270 TRP C CH2 1 
ATOM   7205 N  N   . VAL C  1  258 ? 3.275   28.506  19.765 1.00 67.38  ? 271 VAL C N   1 
ATOM   7206 C  CA  . VAL C  1  258 ? 4.567   27.848  19.860 1.00 68.72  ? 271 VAL C CA  1 
ATOM   7207 C  C   . VAL C  1  258 ? 4.484   26.778  20.947 1.00 67.32  ? 271 VAL C C   1 
ATOM   7208 O  O   . VAL C  1  258 ? 3.823   26.989  21.967 1.00 69.34  ? 271 VAL C O   1 
ATOM   7209 C  CB  . VAL C  1  258 ? 5.670   28.882  20.157 1.00 70.67  ? 271 VAL C CB  1 
ATOM   7210 C  CG1 . VAL C  1  258 ? 7.023   28.229  20.395 1.00 76.33  ? 271 VAL C CG1 1 
ATOM   7211 C  CG2 . VAL C  1  258 ? 5.800   29.917  19.046 1.00 68.26  ? 271 VAL C CG2 1 
ATOM   7212 N  N   . PRO C  1  259 ? 5.128   25.599  20.773 1.00 63.41  ? 272 PRO C N   1 
ATOM   7213 C  CA  . PRO C  1  259 ? 5.135   24.579  21.820 1.00 64.54  ? 272 PRO C CA  1 
ATOM   7214 C  C   . PRO C  1  259 ? 5.748   25.101  23.119 1.00 67.63  ? 272 PRO C C   1 
ATOM   7215 O  O   . PRO C  1  259 ? 6.667   25.915  23.086 1.00 67.69  ? 272 PRO C O   1 
ATOM   7216 C  CB  . PRO C  1  259 ? 5.964   23.432  21.203 1.00 59.40  ? 272 PRO C CB  1 
ATOM   7217 C  CG  . PRO C  1  259 ? 6.787   24.101  20.123 1.00 58.90  ? 272 PRO C CG  1 
ATOM   7218 C  CD  . PRO C  1  259 ? 5.848   25.155  19.566 1.00 61.32  ? 272 PRO C CD  1 
ATOM   7219 N  N   . GLY C  1  260 ? 5.227   24.614  24.250 1.00 61.10  ? 273 GLY C N   1 
ATOM   7220 C  CA  . GLY C  1  260 ? 5.706   24.995  25.564 1.00 61.24  ? 273 GLY C CA  1 
ATOM   7221 C  C   . GLY C  1  260 ? 4.774   24.472  26.657 1.00 65.58  ? 273 GLY C C   1 
ATOM   7222 O  O   . GLY C  1  260 ? 4.163   23.414  26.494 1.00 67.45  ? 273 GLY C O   1 
ATOM   7223 N  N   . GLY C  1  261 ? 4.663   25.235  27.755 1.00 68.16  ? 274 GLY C N   1 
ATOM   7224 C  CA  . GLY C  1  261 ? 3.789   24.895  28.869 1.00 72.25  ? 274 GLY C CA  1 
ATOM   7225 C  C   . GLY C  1  261 ? 3.886   25.928  29.990 1.00 69.31  ? 274 GLY C C   1 
ATOM   7226 O  O   . GLY C  1  261 ? 4.783   26.774  29.975 1.00 63.96  ? 274 GLY C O   1 
ATOM   7227 N  N   . ASN C  1  262 ? 2.945   25.858  30.942 1.00 67.89  ? 275 ASN C N   1 
ATOM   7228 C  CA  . ASN C  1  262 ? 3.001   26.659  32.160 1.00 65.83  ? 275 ASN C CA  1 
ATOM   7229 C  C   . ASN C  1  262 ? 4.175   26.191  33.020 1.00 65.61  ? 275 ASN C C   1 
ATOM   7230 O  O   . ASN C  1  262 ? 4.297   25.000  33.281 1.00 67.89  ? 275 ASN C O   1 
ATOM   7231 C  CB  . ASN C  1  262 ? 1.709   26.557  32.969 1.00 64.74  ? 275 ASN C CB  1 
ATOM   7232 C  CG  . ASN C  1  262 ? 0.634   27.525  32.533 1.00 60.93  ? 275 ASN C CG  1 
ATOM   7233 O  OD1 . ASN C  1  262 ? 0.926   28.542  31.893 1.00 63.76  ? 275 ASN C OD1 1 
ATOM   7234 N  ND2 . ASN C  1  262 ? -0.608  27.243  32.903 1.00 61.12  ? 275 ASN C ND2 1 
ATOM   7235 N  N   . ALA C  1  263 ? 5.014   27.125  33.486 1.00 65.70  ? 276 ALA C N   1 
ATOM   7236 C  CA  . ALA C  1  263 ? 6.179   26.783  34.292 1.00 70.29  ? 276 ALA C CA  1 
ATOM   7237 C  C   . ALA C  1  263 ? 5.877   26.898  35.789 1.00 76.69  ? 276 ALA C C   1 
ATOM   7238 O  O   . ALA C  1  263 ? 5.039   27.702  36.201 1.00 73.12  ? 276 ALA C O   1 
ATOM   7239 C  CB  . ALA C  1  263 ? 7.335   27.676  33.904 1.00 71.70  ? 276 ALA C CB  1 
ATOM   7240 N  N   . ASP C  1  264 ? 6.571   26.063  36.580 1.00 77.69  ? 277 ASP C N   1 
ATOM   7241 C  CA  . ASP C  1  264 ? 6.643   26.163  38.032 1.00 82.01  ? 277 ASP C CA  1 
ATOM   7242 C  C   . ASP C  1  264 ? 5.269   26.051  38.684 1.00 82.63  ? 277 ASP C C   1 
ATOM   7243 O  O   . ASP C  1  264 ? 4.914   26.866  39.532 1.00 84.48  ? 277 ASP C O   1 
ATOM   7244 C  CB  . ASP C  1  264 ? 7.366   27.428  38.461 1.00 88.26  ? 277 ASP C CB  1 
ATOM   7245 C  CG  . ASP C  1  264 ? 8.807   27.522  37.964 1.00 92.51  ? 277 ASP C CG  1 
ATOM   7246 O  OD1 . ASP C  1  264 ? 9.527   26.488  38.103 1.00 92.00  ? 277 ASP C OD1 1 
ATOM   7247 O  OD2 . ASP C  1  264 ? 9.193   28.615  37.441 1.00 96.78  ? 277 ASP C OD2 1 
ATOM   7248 N  N   . ASN C  1  265 ? 4.530   25.007  38.306 1.00 76.51  ? 278 ASN C N   1 
ATOM   7249 C  CA  . ASN C  1  265 ? 3.229   24.715  38.883 1.00 78.49  ? 278 ASN C CA  1 
ATOM   7250 C  C   . ASN C  1  265 ? 2.416   25.998  39.073 1.00 77.87  ? 278 ASN C C   1 
ATOM   7251 O  O   . ASN C  1  265 ? 1.747   26.149  40.089 1.00 73.09  ? 278 ASN C O   1 
ATOM   7252 C  CB  . ASN C  1  265 ? 3.388   23.926  40.176 1.00 77.49  ? 278 ASN C CB  1 
ATOM   7253 C  CG  . ASN C  1  265 ? 2.214   23.023  40.473 1.00 88.64  ? 278 ASN C CG  1 
ATOM   7254 O  OD1 . ASN C  1  265 ? 1.418   22.670  39.594 1.00 105.48 ? 278 ASN C OD1 1 
ATOM   7255 N  ND2 . ASN C  1  265 ? 2.124   22.579  41.714 1.00 94.32  ? 278 ASN C ND2 1 
ATOM   7256 N  N   . GLN C  1  266 ? 2.440   26.895  38.073 1.00 82.26  ? 279 GLN C N   1 
ATOM   7257 C  CA  . GLN C  1  266 ? 1.734   28.170  38.145 1.00 84.68  ? 279 GLN C CA  1 
ATOM   7258 C  C   . GLN C  1  266 ? 0.903   28.394  36.884 1.00 79.00  ? 279 GLN C C   1 
ATOM   7259 O  O   . GLN C  1  266 ? 1.360   28.116  35.782 1.00 76.28  ? 279 GLN C O   1 
ATOM   7260 C  CB  . GLN C  1  266 ? 2.706   29.345  38.274 1.00 91.63  ? 279 GLN C CB  1 
ATOM   7261 C  CG  . GLN C  1  266 ? 3.266   29.562  39.676 1.00 96.99  ? 279 GLN C CG  1 
ATOM   7262 C  CD  . GLN C  1  266 ? 4.605   30.273  39.678 1.00 100.17 ? 279 GLN C CD  1 
ATOM   7263 O  OE1 . GLN C  1  266 ? 4.977   30.962  38.718 1.00 99.96  ? 279 GLN C OE1 1 
ATOM   7264 N  NE2 . GLN C  1  266 ? 5.343   30.107  40.766 1.00 106.32 ? 279 GLN C NE2 1 
ATOM   7265 N  N   . VAL C  1  267 ? -0.300  28.952  37.055 1.00 73.46  ? 280 VAL C N   1 
ATOM   7266 C  CA  . VAL C  1  267 ? -1.153  29.311  35.935 1.00 72.22  ? 280 VAL C CA  1 
ATOM   7267 C  C   . VAL C  1  267 ? -0.661  30.616  35.309 1.00 77.47  ? 280 VAL C C   1 
ATOM   7268 O  O   . VAL C  1  267 ? 0.185   31.306  35.867 1.00 81.86  ? 280 VAL C O   1 
ATOM   7269 C  CB  . VAL C  1  267 ? -2.631  29.412  36.354 1.00 75.00  ? 280 VAL C CB  1 
ATOM   7270 C  CG1 . VAL C  1  267 ? -3.194  28.049  36.741 1.00 73.76  ? 280 VAL C CG1 1 
ATOM   7271 C  CG2 . VAL C  1  267 ? -2.859  30.434  37.466 1.00 77.99  ? 280 VAL C CG2 1 
ATOM   7272 N  N   . ASN C  1  268 ? -1.195  30.917  34.118 1.00 78.40  ? 281 ASN C N   1 
ATOM   7273 C  CA  . ASN C  1  268 ? -0.858  32.102  33.344 1.00 79.99  ? 281 ASN C CA  1 
ATOM   7274 C  C   . ASN C  1  268 ? 0.647   32.350  33.331 1.00 81.16  ? 281 ASN C C   1 
ATOM   7275 O  O   . ASN C  1  268 ? 1.083   33.483  33.495 1.00 82.00  ? 281 ASN C O   1 
ATOM   7276 C  CB  . ASN C  1  268 ? -1.622  33.318  33.850 1.00 84.19  ? 281 ASN C CB  1 
ATOM   7277 C  CG  . ASN C  1  268 ? -3.106  33.170  33.616 1.00 85.55  ? 281 ASN C CG  1 
ATOM   7278 O  OD1 . ASN C  1  268 ? -3.565  33.219  32.469 1.00 89.31  ? 281 ASN C OD1 1 
ATOM   7279 N  ND2 . ASN C  1  268 ? -3.872  32.975  34.679 1.00 81.09  ? 281 ASN C ND2 1 
ATOM   7280 N  N   . ASN C  1  269 ? 1.428   31.288  33.096 1.00 83.41  ? 282 ASN C N   1 
ATOM   7281 C  CA  . ASN C  1  269 ? 2.878   31.372  33.091 1.00 79.54  ? 282 ASN C CA  1 
ATOM   7282 C  C   . ASN C  1  269 ? 3.430   30.496  31.964 1.00 72.75  ? 282 ASN C C   1 
ATOM   7283 O  O   . ASN C  1  269 ? 4.285   29.644  32.195 1.00 70.85  ? 282 ASN C O   1 
ATOM   7284 C  CB  . ASN C  1  269 ? 3.439   30.991  34.456 1.00 75.58  ? 282 ASN C CB  1 
ATOM   7285 C  CG  . ASN C  1  269 ? 4.887   31.389  34.615 1.00 75.81  ? 282 ASN C CG  1 
ATOM   7286 O  OD1 . ASN C  1  269 ? 5.358   32.322  33.954 1.00 80.26  ? 282 ASN C OD1 1 
ATOM   7287 N  ND2 . ASN C  1  269 ? 5.604   30.700  35.489 1.00 76.73  ? 282 ASN C ND2 1 
ATOM   7288 N  N   . TYR C  1  270 ? 2.941   30.721  30.741 1.00 70.16  ? 283 TYR C N   1 
ATOM   7289 C  CA  . TYR C  1  270 ? 3.301   29.893  29.601 1.00 66.90  ? 283 TYR C CA  1 
ATOM   7290 C  C   . TYR C  1  270 ? 4.681   30.286  29.077 1.00 68.44  ? 283 TYR C C   1 
ATOM   7291 O  O   . TYR C  1  270 ? 4.888   31.436  28.706 1.00 67.84  ? 283 TYR C O   1 
ATOM   7292 C  CB  . TYR C  1  270 ? 2.257   30.024  28.487 1.00 67.33  ? 283 TYR C CB  1 
ATOM   7293 C  CG  . TYR C  1  270 ? 2.393   28.992  27.374 1.00 73.85  ? 283 TYR C CG  1 
ATOM   7294 C  CD1 . TYR C  1  270 ? 1.807   27.731  27.486 1.00 84.86  ? 283 TYR C CD1 1 
ATOM   7295 C  CD2 . TYR C  1  270 ? 3.114   29.267  26.218 1.00 73.88  ? 283 TYR C CD2 1 
ATOM   7296 C  CE1 . TYR C  1  270 ? 1.934   26.781  26.485 1.00 78.51  ? 283 TYR C CE1 1 
ATOM   7297 C  CE2 . TYR C  1  270 ? 3.251   28.324  25.209 1.00 76.07  ? 283 TYR C CE2 1 
ATOM   7298 C  CZ  . TYR C  1  270 ? 2.660   27.079  25.343 1.00 76.43  ? 283 TYR C CZ  1 
ATOM   7299 O  OH  . TYR C  1  270 ? 2.759   26.152  24.346 1.00 66.35  ? 283 TYR C OH  1 
ATOM   7300 N  N   . VAL C  1  271 ? 5.591   29.304  29.003 1.00 70.73  ? 284 VAL C N   1 
ATOM   7301 C  CA  . VAL C  1  271 ? 6.949   29.492  28.508 1.00 73.81  ? 284 VAL C CA  1 
ATOM   7302 C  C   . VAL C  1  271 ? 7.166   28.621  27.265 1.00 75.53  ? 284 VAL C C   1 
ATOM   7303 O  O   . VAL C  1  271 ? 6.877   27.426  27.295 1.00 81.03  ? 284 VAL C O   1 
ATOM   7304 C  CB  . VAL C  1  271 ? 7.951   29.124  29.624 1.00 76.08  ? 284 VAL C CB  1 
ATOM   7305 C  CG1 . VAL C  1  271 ? 9.401   29.233  29.163 1.00 77.85  ? 284 VAL C CG1 1 
ATOM   7306 C  CG2 . VAL C  1  271 ? 7.733   29.950  30.886 1.00 79.94  ? 284 VAL C CG2 1 
ATOM   7307 N  N   . GLU C  1  272 ? 7.702   29.230  26.193 1.00 70.60  ? 285 GLU C N   1 
ATOM   7308 C  CA  A GLU C  1  272 ? 8.040   28.529  24.965 0.50 66.58  ? 285 GLU C CA  1 
ATOM   7309 C  CA  B GLU C  1  272 ? 8.059   28.541  24.958 0.50 69.35  ? 285 GLU C CA  1 
ATOM   7310 C  C   . GLU C  1  272 ? 9.122   27.484  25.242 1.00 69.34  ? 285 GLU C C   1 
ATOM   7311 O  O   . GLU C  1  272 ? 9.978   27.685  26.098 1.00 67.04  ? 285 GLU C O   1 
ATOM   7312 C  CB  A GLU C  1  272 ? 8.503   29.542  23.915 0.50 67.37  ? 285 GLU C CB  1 
ATOM   7313 C  CB  B GLU C  1  272 ? 8.615   29.528  23.927 0.50 74.20  ? 285 GLU C CB  1 
ATOM   7314 C  CG  A GLU C  1  272 ? 7.426   30.546  23.503 0.50 66.04  ? 285 GLU C CG  1 
ATOM   7315 C  CG  B GLU C  1  272 ? 9.272   28.873  22.710 0.50 76.89  ? 285 GLU C CG  1 
ATOM   7316 C  CD  A GLU C  1  272 ? 7.836   31.543  22.427 0.50 65.93  ? 285 GLU C CD  1 
ATOM   7317 C  CD  B GLU C  1  272 ? 9.844   29.836  21.681 0.50 80.27  ? 285 GLU C CD  1 
ATOM   7318 O  OE1 A GLU C  1  272 ? 8.939   31.378  21.866 0.50 68.11  ? 285 GLU C OE1 1 
ATOM   7319 O  OE1 B GLU C  1  272 ? 9.684   31.064  21.852 0.50 84.00  ? 285 GLU C OE1 1 
ATOM   7320 O  OE2 A GLU C  1  272 ? 7.045   32.464  22.125 0.50 62.81  ? 285 GLU C OE2 1 
ATOM   7321 O  OE2 B GLU C  1  272 ? 10.465  29.355  20.710 0.50 82.25  ? 285 GLU C OE2 1 
ATOM   7322 N  N   . ASP C  1  273 ? 9.060   26.356  24.512 1.00 77.78  ? 286 ASP C N   1 
ATOM   7323 C  CA  . ASP C  1  273 ? 10.106  25.337  24.534 1.00 71.39  ? 286 ASP C CA  1 
ATOM   7324 C  C   . ASP C  1  273 ? 10.755  25.301  23.155 1.00 69.15  ? 286 ASP C C   1 
ATOM   7325 O  O   . ASP C  1  273 ? 10.160  24.802  22.207 1.00 68.57  ? 286 ASP C O   1 
ATOM   7326 C  CB  . ASP C  1  273 ? 9.591   23.951  24.907 1.00 68.83  ? 286 ASP C CB  1 
ATOM   7327 C  CG  . ASP C  1  273 ? 10.636  22.839  24.930 1.00 71.01  ? 286 ASP C CG  1 
ATOM   7328 O  OD1 . ASP C  1  273 ? 11.808  23.120  24.607 1.00 73.95  ? 286 ASP C OD1 1 
ATOM   7329 O  OD2 . ASP C  1  273 ? 10.282  21.692  25.282 1.00 70.59  ? 286 ASP C OD2 1 
ATOM   7330 N  N   . PRO C  1  274 ? 11.987  25.831  22.992 1.00 75.72  ? 287 PRO C N   1 
ATOM   7331 C  CA  . PRO C  1  274 ? 12.621  25.885  21.674 1.00 75.84  ? 287 PRO C CA  1 
ATOM   7332 C  C   . PRO C  1  274 ? 13.190  24.553  21.169 1.00 73.14  ? 287 PRO C C   1 
ATOM   7333 O  O   . PRO C  1  274 ? 13.524  24.450  19.991 1.00 66.91  ? 287 PRO C O   1 
ATOM   7334 C  CB  . PRO C  1  274 ? 13.704  26.961  21.892 1.00 79.11  ? 287 PRO C CB  1 
ATOM   7335 C  CG  . PRO C  1  274 ? 14.093  26.818  23.350 1.00 77.20  ? 287 PRO C CG  1 
ATOM   7336 C  CD  . PRO C  1  274 ? 12.823  26.401  24.063 1.00 77.68  ? 287 PRO C CD  1 
ATOM   7337 N  N   . ASP C  1  275 ? 13.265  23.539  22.049 1.00 69.02  ? 288 ASP C N   1 
ATOM   7338 C  CA  . ASP C  1  275 ? 13.763  22.213  21.696 1.00 71.21  ? 288 ASP C CA  1 
ATOM   7339 C  C   . ASP C  1  275 ? 12.643  21.280  21.219 1.00 69.57  ? 288 ASP C C   1 
ATOM   7340 O  O   . ASP C  1  275 ? 12.911  20.211  20.671 1.00 69.05  ? 288 ASP C O   1 
ATOM   7341 C  CB  . ASP C  1  275 ? 14.500  21.594  22.873 1.00 72.28  ? 288 ASP C CB  1 
ATOM   7342 C  CG  . ASP C  1  275 ? 15.844  22.229  23.200 1.00 69.52  ? 288 ASP C CG  1 
ATOM   7343 O  OD1 . ASP C  1  275 ? 16.390  22.932  22.331 1.00 63.23  ? 288 ASP C OD1 1 
ATOM   7344 O  OD2 . ASP C  1  275 ? 16.327  22.019  24.326 1.00 73.33  ? 288 ASP C OD2 1 
ATOM   7345 N  N   . SER C  1  276 ? 11.387  21.669  21.451 1.00 65.58  ? 289 SER C N   1 
ATOM   7346 C  CA  . SER C  1  276 ? 10.244  20.846  21.090 1.00 62.71  ? 289 SER C CA  1 
ATOM   7347 C  C   . SER C  1  276 ? 10.145  20.694  19.576 1.00 60.83  ? 289 SER C C   1 
ATOM   7348 O  O   . SER C  1  276 ? 10.555  21.569  18.825 1.00 64.83  ? 289 SER C O   1 
ATOM   7349 C  CB  . SER C  1  276 ? 8.959   21.422  21.639 1.00 62.82  ? 289 SER C CB  1 
ATOM   7350 O  OG  . SER C  1  276 ? 7.825   20.783  21.069 1.00 60.83  ? 289 SER C OG  1 
ATOM   7351 N  N   . ALA C  1  277 ? 9.567   19.575  19.136 1.00 58.55  ? 290 ALA C N   1 
ATOM   7352 C  CA  . ALA C  1  277 ? 9.117   19.436  17.763 1.00 53.23  ? 290 ALA C CA  1 
ATOM   7353 C  C   . ALA C  1  277 ? 8.078   20.509  17.464 1.00 50.95  ? 290 ALA C C   1 
ATOM   7354 O  O   . ALA C  1  277 ? 7.360   20.949  18.362 1.00 53.71  ? 290 ALA C O   1 
ATOM   7355 C  CB  . ALA C  1  277 ? 8.528   18.057  17.543 1.00 49.19  ? 290 ALA C CB  1 
ATOM   7356 N  N   . ASP C  1  278 ? 8.017   20.911  16.192 1.00 48.65  ? 291 ASP C N   1 
ATOM   7357 C  CA  . ASP C  1  278 ? 6.953   21.749  15.660 1.00 51.99  ? 291 ASP C CA  1 
ATOM   7358 C  C   . ASP C  1  278 ? 6.734   21.294  14.216 1.00 53.56  ? 291 ASP C C   1 
ATOM   7359 O  O   . ASP C  1  278 ? 7.255   20.249  13.835 1.00 54.26  ? 291 ASP C O   1 
ATOM   7360 C  CB  . ASP C  1  278 ? 7.267   23.226  15.863 1.00 56.23  ? 291 ASP C CB  1 
ATOM   7361 C  CG  . ASP C  1  278 ? 8.429   23.788  15.051 1.00 60.58  ? 291 ASP C CG  1 
ATOM   7362 O  OD1 . ASP C  1  278 ? 8.791   23.176  14.023 1.00 61.23  ? 291 ASP C OD1 1 
ATOM   7363 O  OD2 . ASP C  1  278 ? 8.983   24.829  15.470 1.00 69.33  ? 291 ASP C OD2 1 
ATOM   7364 N  N   . PHE C  1  279 ? 5.993   22.067  13.412 1.00 51.97  ? 292 PHE C N   1 
ATOM   7365 C  CA  . PHE C  1  279 ? 5.550   21.585  12.113 1.00 55.32  ? 292 PHE C CA  1 
ATOM   7366 C  C   . PHE C  1  279 ? 6.629   21.757  11.047 1.00 56.31  ? 292 PHE C C   1 
ATOM   7367 O  O   . PHE C  1  279 ? 6.471   21.202  9.966  1.00 62.21  ? 292 PHE C O   1 
ATOM   7368 C  CB  . PHE C  1  279 ? 4.225   22.219  11.676 1.00 56.60  ? 292 PHE C CB  1 
ATOM   7369 C  CG  . PHE C  1  279 ? 3.049   21.648  12.454 1.00 58.91  ? 292 PHE C CG  1 
ATOM   7370 C  CD1 . PHE C  1  279 ? 2.493   20.413  12.117 1.00 59.57  ? 292 PHE C CD1 1 
ATOM   7371 C  CD2 . PHE C  1  279 ? 2.540   22.326  13.557 1.00 62.49  ? 292 PHE C CD2 1 
ATOM   7372 C  CE1 . PHE C  1  279 ? 1.448   19.876  12.864 1.00 62.19  ? 292 PHE C CE1 1 
ATOM   7373 C  CE2 . PHE C  1  279 ? 1.490   21.794  14.296 1.00 61.06  ? 292 PHE C CE2 1 
ATOM   7374 C  CZ  . PHE C  1  279 ? 0.948   20.569  13.954 1.00 62.35  ? 292 PHE C CZ  1 
ATOM   7375 N  N   . THR C  1  280 ? 7.708   22.497  11.339 1.00 61.55  ? 293 THR C N   1 
ATOM   7376 C  CA  . THR C  1  280 ? 8.843   22.593  10.427 1.00 61.97  ? 293 THR C CA  1 
ATOM   7377 C  C   . THR C  1  280 ? 10.025  21.783  10.966 1.00 61.40  ? 293 THR C C   1 
ATOM   7378 O  O   . THR C  1  280 ? 11.072  21.748  10.330 1.00 64.74  ? 293 THR C O   1 
ATOM   7379 C  CB  . THR C  1  280 ? 9.220   24.060  10.202 1.00 63.63  ? 293 THR C CB  1 
ATOM   7380 O  OG1 . THR C  1  280 ? 9.592   24.601  11.468 1.00 72.71  ? 293 THR C OG1 1 
ATOM   7381 C  CG2 . THR C  1  280 ? 8.081   24.878  9.613  1.00 58.80  ? 293 THR C CG2 1 
ATOM   7382 N  N   . HIS C  1  281 ? 9.850   21.147  12.140 1.00 64.00  ? 294 HIS C N   1 
ATOM   7383 C  CA  . HIS C  1  281 ? 10.879  20.348  12.791 1.00 61.41  ? 294 HIS C CA  1 
ATOM   7384 C  C   . HIS C  1  281 ? 10.262  19.035  13.298 1.00 58.44  ? 294 HIS C C   1 
ATOM   7385 O  O   . HIS C  1  281 ? 10.258  18.761  14.495 1.00 63.15  ? 294 HIS C O   1 
ATOM   7386 C  CB  . HIS C  1  281 ? 11.590  21.152  13.888 1.00 67.42  ? 294 HIS C CB  1 
ATOM   7387 C  CG  . HIS C  1  281 ? 12.291  22.397  13.429 1.00 76.48  ? 294 HIS C CG  1 
ATOM   7388 N  ND1 . HIS C  1  281 ? 13.521  22.397  12.802 1.00 86.45  ? 294 HIS C ND1 1 
ATOM   7389 C  CD2 . HIS C  1  281 ? 11.926  23.685  13.511 1.00 75.78  ? 294 HIS C CD2 1 
ATOM   7390 C  CE1 . HIS C  1  281 ? 13.876  23.644  12.526 1.00 85.70  ? 294 HIS C CE1 1 
ATOM   7391 N  NE2 . HIS C  1  281 ? 12.917  24.439  12.945 1.00 85.02  ? 294 HIS C NE2 1 
ATOM   7392 N  N   . LEU C  1  282 ? 9.749   18.216  12.371 1.00 52.25  ? 295 LEU C N   1 
ATOM   7393 C  CA  . LEU C  1  282 ? 8.942   17.042  12.678 1.00 53.76  ? 295 LEU C CA  1 
ATOM   7394 C  C   . LEU C  1  282 ? 9.793   15.840  13.077 1.00 50.43  ? 295 LEU C C   1 
ATOM   7395 O  O   . LEU C  1  282 ? 9.308   14.979  13.809 1.00 48.16  ? 295 LEU C O   1 
ATOM   7396 C  CB  . LEU C  1  282 ? 8.053   16.636  11.497 1.00 53.11  ? 295 LEU C CB  1 
ATOM   7397 C  CG  . LEU C  1  282 ? 6.804   17.483  11.250 1.00 53.94  ? 295 LEU C CG  1 
ATOM   7398 C  CD1 . LEU C  1  282 ? 6.208   17.170  9.884  1.00 55.21  ? 295 LEU C CD1 1 
ATOM   7399 C  CD2 . LEU C  1  282 ? 5.766   17.281  12.324 1.00 53.34  ? 295 LEU C CD2 1 
ATOM   7400 N  N   . CYS C  1  283 ? 11.014  15.731  12.545 1.00 45.10  ? 296 CYS C N   1 
ATOM   7401 C  CA  . CYS C  1  283 ? 11.849  14.577  12.846 1.00 46.80  ? 296 CYS C CA  1 
ATOM   7402 C  C   . CYS C  1  283 ? 12.281  14.599  14.311 1.00 45.09  ? 296 CYS C C   1 
ATOM   7403 O  O   . CYS C  1  283 ? 12.625  13.551  14.843 1.00 48.95  ? 296 CYS C O   1 
ATOM   7404 C  CB  . CYS C  1  283 ? 13.035  14.405  11.901 1.00 52.15  ? 296 CYS C CB  1 
ATOM   7405 S  SG  . CYS C  1  283 ? 12.579  14.012  10.186 1.00 58.97  ? 296 CYS C SG  1 
ATOM   7406 N  N   . ARG C  1  284 ? 12.209  15.759  14.978 1.00 46.87  ? 297 ARG C N   1 
ATOM   7407 C  CA  . ARG C  1  284 ? 12.426  15.820  16.419 1.00 50.71  ? 297 ARG C CA  1 
ATOM   7408 C  C   . ARG C  1  284 ? 11.449  14.908  17.150 1.00 46.08  ? 297 ARG C C   1 
ATOM   7409 O  O   . ARG C  1  284 ? 11.821  14.309  18.158 1.00 50.44  ? 297 ARG C O   1 
ATOM   7410 C  CB  . ARG C  1  284 ? 12.247  17.223  17.007 1.00 58.72  ? 297 ARG C CB  1 
ATOM   7411 C  CG  . ARG C  1  284 ? 13.333  18.183  16.559 1.00 64.37  ? 297 ARG C CG  1 
ATOM   7412 C  CD  . ARG C  1  284 ? 13.200  19.538  17.224 1.00 69.66  ? 297 ARG C CD  1 
ATOM   7413 N  NE  . ARG C  1  284 ? 14.151  20.479  16.620 1.00 75.50  ? 297 ARG C NE  1 
ATOM   7414 C  CZ  . ARG C  1  284 ? 14.138  21.795  16.787 1.00 73.77  ? 297 ARG C CZ  1 
ATOM   7415 N  NH1 . ARG C  1  284 ? 13.263  22.357  17.602 1.00 70.58  ? 297 ARG C NH1 1 
ATOM   7416 N  NH2 . ARG C  1  284 ? 15.013  22.549  16.150 1.00 73.98  ? 297 ARG C NH2 1 
ATOM   7417 N  N   . LEU C  1  285 ? 10.213  14.820  16.632 1.00 47.28  ? 298 LEU C N   1 
ATOM   7418 C  CA  . LEU C  1  285 ? 9.185   13.975  17.220 1.00 46.13  ? 298 LEU C CA  1 
ATOM   7419 C  C   . LEU C  1  285 ? 9.636   12.528  17.128 1.00 43.33  ? 298 LEU C C   1 
ATOM   7420 O  O   . LEU C  1  285 ? 9.519   11.823  18.126 1.00 45.39  ? 298 LEU C O   1 
ATOM   7421 C  CB  . LEU C  1  285 ? 7.824   14.181  16.552 1.00 48.91  ? 298 LEU C CB  1 
ATOM   7422 C  CG  . LEU C  1  285 ? 6.633   13.429  17.160 1.00 50.62  ? 298 LEU C CG  1 
ATOM   7423 C  CD1 . LEU C  1  285 ? 5.358   14.182  16.828 1.00 51.45  ? 298 LEU C CD1 1 
ATOM   7424 C  CD2 . LEU C  1  285 ? 6.481   11.973  16.693 1.00 57.48  ? 298 LEU C CD2 1 
ATOM   7425 N  N   . TYR C  1  286 ? 10.158  12.121  15.950 1.00 43.37  ? 299 TYR C N   1 
ATOM   7426 C  CA  . TYR C  1  286 ? 10.691  10.778  15.770 1.00 42.00  ? 299 TYR C CA  1 
ATOM   7427 C  C   . TYR C  1  286 ? 11.708  10.506  16.882 1.00 41.27  ? 299 TYR C C   1 
ATOM   7428 O  O   . TYR C  1  286 ? 11.589  9.507   17.590 1.00 44.72  ? 299 TYR C O   1 
ATOM   7429 C  CB  . TYR C  1  286 ? 11.248  10.557  14.357 1.00 35.80  ? 299 TYR C CB  1 
ATOM   7430 C  CG  . TYR C  1  286 ? 11.889  9.189   14.174 1.00 36.03  ? 299 TYR C CG  1 
ATOM   7431 C  CD1 . TYR C  1  286 ? 11.149  8.029   14.358 1.00 35.38  ? 299 TYR C CD1 1 
ATOM   7432 C  CD2 . TYR C  1  286 ? 13.224  9.052   13.839 1.00 33.74  ? 299 TYR C CD2 1 
ATOM   7433 C  CE1 . TYR C  1  286 ? 11.710  6.776   14.203 1.00 36.25  ? 299 TYR C CE1 1 
ATOM   7434 C  CE2 . TYR C  1  286 ? 13.789  7.804   13.661 1.00 35.70  ? 299 TYR C CE2 1 
ATOM   7435 C  CZ  . TYR C  1  286 ? 13.035  6.666   13.847 1.00 33.71  ? 299 TYR C CZ  1 
ATOM   7436 O  OH  . TYR C  1  286 ? 13.578  5.437   13.681 1.00 36.87  ? 299 TYR C OH  1 
ATOM   7437 N  N   . GLU C  1  287 ? 12.644  11.443  17.083 1.00 43.45  ? 300 GLU C N   1 
ATOM   7438 C  CA  . GLU C  1  287 ? 13.730  11.254  18.036 1.00 53.40  ? 300 GLU C CA  1 
ATOM   7439 C  C   . GLU C  1  287 ? 13.260  11.332  19.491 1.00 45.42  ? 300 GLU C C   1 
ATOM   7440 O  O   . GLU C  1  287 ? 13.776  10.565  20.298 1.00 47.38  ? 300 GLU C O   1 
ATOM   7441 C  CB  . GLU C  1  287 ? 14.857  12.253  17.780 1.00 59.17  ? 300 GLU C CB  1 
ATOM   7442 C  CG  . GLU C  1  287 ? 15.397  12.195  16.354 1.00 70.66  ? 300 GLU C CG  1 
ATOM   7443 C  CD  . GLU C  1  287 ? 16.052  13.466  15.830 1.00 87.41  ? 300 GLU C CD  1 
ATOM   7444 O  OE1 . GLU C  1  287 ? 16.255  14.416  16.622 1.00 84.06  ? 300 GLU C OE1 1 
ATOM   7445 O  OE2 . GLU C  1  287 ? 16.329  13.514  14.605 1.00 101.13 ? 300 GLU C OE2 1 
ATOM   7446 N  N   . PHE C  1  288 ? 12.316  12.237  19.821 1.00 43.03  ? 301 PHE C N   1 
ATOM   7447 C  CA  . PHE C  1  288 ? 11.762  12.320  21.172 1.00 47.33  ? 301 PHE C CA  1 
ATOM   7448 C  C   . PHE C  1  288 ? 11.211  10.952  21.590 1.00 46.43  ? 301 PHE C C   1 
ATOM   7449 O  O   . PHE C  1  288 ? 11.453  10.522  22.711 1.00 53.67  ? 301 PHE C O   1 
ATOM   7450 C  CB  . PHE C  1  288 ? 10.716  13.441  21.281 1.00 51.79  ? 301 PHE C CB  1 
ATOM   7451 C  CG  . PHE C  1  288 ? 10.043  13.565  22.642 1.00 55.51  ? 301 PHE C CG  1 
ATOM   7452 C  CD1 . PHE C  1  288 ? 10.664  14.227  23.700 1.00 55.83  ? 301 PHE C CD1 1 
ATOM   7453 C  CD2 . PHE C  1  288 ? 8.800   12.988  22.870 1.00 56.54  ? 301 PHE C CD2 1 
ATOM   7454 C  CE1 . PHE C  1  288 ? 10.043  14.325  24.941 1.00 52.96  ? 301 PHE C CE1 1 
ATOM   7455 C  CE2 . PHE C  1  288 ? 8.191   13.089  24.111 1.00 61.03  ? 301 PHE C CE2 1 
ATOM   7456 C  CZ  . PHE C  1  288 ? 8.810   13.763  25.139 1.00 57.07  ? 301 PHE C CZ  1 
ATOM   7457 N  N   . VAL C  1  289 ? 10.505  10.257  20.680 1.00 46.39  ? 302 VAL C N   1 
ATOM   7458 C  CA  . VAL C  1  289 ? 9.848   8.995   20.994 1.00 44.85  ? 302 VAL C CA  1 
ATOM   7459 C  C   . VAL C  1  289 ? 10.859  7.862   21.073 1.00 43.44  ? 302 VAL C C   1 
ATOM   7460 O  O   . VAL C  1  289 ? 10.682  7.017   21.940 1.00 50.69  ? 302 VAL C O   1 
ATOM   7461 C  CB  . VAL C  1  289 ? 8.711   8.636   20.012 1.00 45.91  ? 302 VAL C CB  1 
ATOM   7462 C  CG1 . VAL C  1  289 ? 8.061   7.285   20.301 1.00 46.97  ? 302 VAL C CG1 1 
ATOM   7463 C  CG2 . VAL C  1  289 ? 7.648   9.713   20.010 1.00 42.32  ? 302 VAL C CG2 1 
ATOM   7464 N  N   . VAL C  1  290 ? 11.864  7.821   20.183 1.00 43.49  ? 303 VAL C N   1 
ATOM   7465 C  CA  . VAL C  1  290 ? 12.908  6.813   20.292 1.00 45.36  ? 303 VAL C CA  1 
ATOM   7466 C  C   . VAL C  1  290 ? 13.493  6.910   21.700 1.00 40.73  ? 303 VAL C C   1 
ATOM   7467 O  O   . VAL C  1  290 ? 13.626  5.885   22.370 1.00 46.98  ? 303 VAL C O   1 
ATOM   7468 C  CB  . VAL C  1  290 ? 13.978  6.899   19.184 1.00 47.91  ? 303 VAL C CB  1 
ATOM   7469 C  CG1 . VAL C  1  290 ? 15.245  6.093   19.490 1.00 51.86  ? 303 VAL C CG1 1 
ATOM   7470 C  CG2 . VAL C  1  290 ? 13.392  6.462   17.851 1.00 49.12  ? 303 VAL C CG2 1 
ATOM   7471 N  N   . GLY C  1  291 ? 13.753  8.153   22.144 1.00 39.59  ? 304 GLY C N   1 
ATOM   7472 C  CA  . GLY C  1  291 ? 14.259  8.436   23.478 1.00 48.87  ? 304 GLY C CA  1 
ATOM   7473 C  C   . GLY C  1  291 ? 13.306  7.982   24.583 1.00 44.16  ? 304 GLY C C   1 
ATOM   7474 O  O   . GLY C  1  291 ? 13.760  7.351   25.531 1.00 49.19  ? 304 GLY C O   1 
ATOM   7475 N  N   . SER C  1  292 ? 12.004  8.280   24.438 1.00 40.84  ? 305 SER C N   1 
ATOM   7476 C  CA  . SER C  1  292 ? 11.010  7.893   25.431 1.00 39.97  ? 305 SER C CA  1 
ATOM   7477 C  C   . SER C  1  292 ? 10.958  6.373   25.556 1.00 36.06  ? 305 SER C C   1 
ATOM   7478 O  O   . SER C  1  292 ? 10.818  5.830   26.646 1.00 42.69  ? 305 SER C O   1 
ATOM   7479 C  CB  . SER C  1  292 ? 9.651   8.472   25.107 1.00 40.82  ? 305 SER C CB  1 
ATOM   7480 O  OG  . SER C  1  292 ? 9.730   9.877   24.905 1.00 45.08  ? 305 SER C OG  1 
ATOM   7481 N  N   . VAL C  1  293 ? 11.084  5.685   24.422 1.00 35.56  ? 306 VAL C N   1 
ATOM   7482 C  CA  . VAL C  1  293 ? 11.028  4.235   24.397 1.00 37.16  ? 306 VAL C CA  1 
ATOM   7483 C  C   . VAL C  1  293 ? 12.247  3.663   25.129 1.00 37.41  ? 306 VAL C C   1 
ATOM   7484 O  O   . VAL C  1  293 ? 12.117  2.678   25.858 1.00 39.83  ? 306 VAL C O   1 
ATOM   7485 C  CB  . VAL C  1  293 ? 10.900  3.708   22.952 1.00 33.47  ? 306 VAL C CB  1 
ATOM   7486 C  CG1 . VAL C  1  293 ? 11.127  2.203   22.859 1.00 32.88  ? 306 VAL C CG1 1 
ATOM   7487 C  CG2 . VAL C  1  293 ? 9.553   4.062   22.341 1.00 37.47  ? 306 VAL C CG2 1 
ATOM   7488 N  N   . GLN C  1  294 ? 13.416  4.290   24.934 1.00 38.30  ? 307 GLN C N   1 
ATOM   7489 C  CA  . GLN C  1  294 ? 14.648  3.887   25.600 1.00 43.49  ? 307 GLN C CA  1 
ATOM   7490 C  C   . GLN C  1  294 ? 14.532  4.032   27.114 1.00 40.85  ? 307 GLN C C   1 
ATOM   7491 O  O   . GLN C  1  294 ? 15.064  3.187   27.832 1.00 41.53  ? 307 GLN C O   1 
ATOM   7492 C  CB  . GLN C  1  294 ? 15.849  4.665   25.077 1.00 43.98  ? 307 GLN C CB  1 
ATOM   7493 C  CG  . GLN C  1  294 ? 16.304  4.215   23.689 1.00 45.23  ? 307 GLN C CG  1 
ATOM   7494 C  CD  . GLN C  1  294 ? 17.403  5.088   23.111 1.00 43.84  ? 307 GLN C CD  1 
ATOM   7495 O  OE1 . GLN C  1  294 ? 17.176  6.231   22.702 1.00 48.45  ? 307 GLN C OE1 1 
ATOM   7496 N  NE2 . GLN C  1  294 ? 18.618  4.573   23.063 1.00 43.31  ? 307 GLN C NE2 1 
ATOM   7497 N  N   . GLU C  1  295 ? 13.813  5.067   27.579 1.00 41.46  ? 308 GLU C N   1 
ATOM   7498 C  CA  . GLU C  1  295 ? 13.547  5.243   29.001 1.00 43.09  ? 308 GLU C CA  1 
ATOM   7499 C  C   . GLU C  1  295 ? 12.629  4.144   29.521 1.00 40.07  ? 308 GLU C C   1 
ATOM   7500 O  O   . GLU C  1  295 ? 12.875  3.654   30.612 1.00 45.77  ? 308 GLU C O   1 
ATOM   7501 C  CB  . GLU C  1  295 ? 12.909  6.589   29.341 1.00 48.22  ? 308 GLU C CB  1 
ATOM   7502 C  CG  . GLU C  1  295 ? 13.768  7.798   28.975 1.00 55.52  ? 308 GLU C CG  1 
ATOM   7503 C  CD  . GLU C  1  295 ? 13.056  9.136   29.132 1.00 70.53  ? 308 GLU C CD  1 
ATOM   7504 O  OE1 . GLU C  1  295 ? 11.970  9.172   29.759 1.00 77.62  ? 308 GLU C OE1 1 
ATOM   7505 O  OE2 . GLU C  1  295 ? 13.570  10.157  28.615 1.00 86.06  ? 308 GLU C OE2 1 
ATOM   7506 N  N   . LEU C  1  296 ? 11.604  3.755   28.746 1.00 37.70  ? 309 LEU C N   1 
ATOM   7507 C  CA  . LEU C  1  296 ? 10.663  2.729   29.170 1.00 37.56  ? 309 LEU C CA  1 
ATOM   7508 C  C   . LEU C  1  296 ? 11.352  1.362   29.147 1.00 38.03  ? 309 LEU C C   1 
ATOM   7509 O  O   . LEU C  1  296 ? 11.053  0.510   29.991 1.00 38.48  ? 309 LEU C O   1 
ATOM   7510 C  CB  . LEU C  1  296 ? 9.410   2.716   28.289 1.00 39.25  ? 309 LEU C CB  1 
ATOM   7511 C  CG  . LEU C  1  296 ? 8.497   3.947   28.342 1.00 40.97  ? 309 LEU C CG  1 
ATOM   7512 C  CD1 . LEU C  1  296 ? 7.380   3.794   27.316 1.00 41.41  ? 309 LEU C CD1 1 
ATOM   7513 C  CD2 . LEU C  1  296 ? 7.898   4.235   29.704 1.00 37.94  ? 309 LEU C CD2 1 
ATOM   7514 N  N   . TYR C  1  297 ? 12.251  1.164   28.167 1.00 38.47  ? 310 TYR C N   1 
ATOM   7515 C  CA  . TYR C  1  297 ? 12.866  -0.130  27.898 1.00 40.72  ? 310 TYR C CA  1 
ATOM   7516 C  C   . TYR C  1  297 ? 14.389  0.009   27.859 1.00 42.59  ? 310 TYR C C   1 
ATOM   7517 O  O   . TYR C  1  297 ? 14.994  0.003   26.784 1.00 38.95  ? 310 TYR C O   1 
ATOM   7518 C  CB  . TYR C  1  297 ? 12.303  -0.652  26.574 1.00 38.47  ? 310 TYR C CB  1 
ATOM   7519 C  CG  . TYR C  1  297 ? 10.824  -0.993  26.632 1.00 37.01  ? 310 TYR C CG  1 
ATOM   7520 C  CD1 . TYR C  1  297 ? 10.375  -2.166  27.240 1.00 38.23  ? 310 TYR C CD1 1 
ATOM   7521 C  CD2 . TYR C  1  297 ? 9.882   -0.144  26.070 1.00 35.21  ? 310 TYR C CD2 1 
ATOM   7522 C  CE1 . TYR C  1  297 ? 9.027   -2.484  27.285 1.00 40.70  ? 310 TYR C CE1 1 
ATOM   7523 C  CE2 . TYR C  1  297 ? 8.533   -0.465  26.085 1.00 38.49  ? 310 TYR C CE2 1 
ATOM   7524 C  CZ  . TYR C  1  297 ? 8.103   -1.629  26.702 1.00 38.53  ? 310 TYR C CZ  1 
ATOM   7525 O  OH  . TYR C  1  297 ? 6.770   -1.907  26.738 1.00 36.25  ? 310 TYR C OH  1 
ATOM   7526 N  N   . PRO C  1  298 ? 15.046  0.193   29.029 1.00 44.38  ? 311 PRO C N   1 
ATOM   7527 C  CA  . PRO C  1  298 ? 16.479  0.501   29.072 1.00 40.43  ? 311 PRO C CA  1 
ATOM   7528 C  C   . PRO C  1  298 ? 17.428  -0.606  28.618 1.00 38.01  ? 311 PRO C C   1 
ATOM   7529 O  O   . PRO C  1  298 ? 18.433  -0.300  27.981 1.00 34.35  ? 311 PRO C O   1 
ATOM   7530 C  CB  . PRO C  1  298 ? 16.701  0.920   30.532 1.00 41.10  ? 311 PRO C CB  1 
ATOM   7531 C  CG  . PRO C  1  298 ? 15.628  0.199   31.290 1.00 44.73  ? 311 PRO C CG  1 
ATOM   7532 C  CD  . PRO C  1  298 ? 14.423  0.188   30.360 1.00 43.93  ? 311 PRO C CD  1 
ATOM   7533 N  N   . ASN C  1  299 ? 17.113  -1.879  28.886 1.00 41.77  ? 312 ASN C N   1 
ATOM   7534 C  CA  . ASN C  1  299 ? 18.044  -2.940  28.504 1.00 39.47  ? 312 ASN C CA  1 
ATOM   7535 C  C   . ASN C  1  299 ? 17.317  -4.229  28.134 1.00 39.82  ? 312 ASN C C   1 
ATOM   7536 O  O   . ASN C  1  299 ? 17.551  -5.258  28.762 1.00 35.78  ? 312 ASN C O   1 
ATOM   7537 C  CB  . ASN C  1  299 ? 19.062  -3.170  29.626 1.00 43.09  ? 312 ASN C CB  1 
ATOM   7538 C  CG  . ASN C  1  299 ? 20.185  -4.111  29.249 1.00 40.43  ? 312 ASN C CG  1 
ATOM   7539 O  OD1 . ASN C  1  299 ? 20.553  -4.983  30.038 1.00 40.00  ? 312 ASN C OD1 1 
ATOM   7540 N  ND2 . ASN C  1  299 ? 20.754  -3.970  28.063 1.00 38.51  ? 312 ASN C ND2 1 
ATOM   7541 N  N   . PRO C  1  300 ? 16.454  -4.231  27.087 1.00 41.77  ? 313 PRO C N   1 
ATOM   7542 C  CA  . PRO C  1  300 ? 15.647  -5.403  26.747 1.00 41.18  ? 313 PRO C CA  1 
ATOM   7543 C  C   . PRO C  1  300 ? 16.483  -6.530  26.145 1.00 42.97  ? 313 PRO C C   1 
ATOM   7544 O  O   . PRO C  1  300 ? 17.439  -6.276  25.423 1.00 46.76  ? 313 PRO C O   1 
ATOM   7545 C  CB  . PRO C  1  300 ? 14.633  -4.809  25.729 1.00 40.49  ? 313 PRO C CB  1 
ATOM   7546 C  CG  . PRO C  1  300 ? 15.437  -3.740  25.032 1.00 40.80  ? 313 PRO C CG  1 
ATOM   7547 C  CD  . PRO C  1  300 ? 16.215  -3.106  26.176 1.00 39.25  ? 313 PRO C CD  1 
ATOM   7548 N  N   . THR C  1  301 ? 16.081  -7.776  26.422 1.00 46.17  ? 314 THR C N   1 
ATOM   7549 C  CA  . THR C  1  301 ? 16.628  -8.954  25.754 1.00 48.83  ? 314 THR C CA  1 
ATOM   7550 C  C   . THR C  1  301 ? 15.469  -9.842  25.299 1.00 45.46  ? 314 THR C C   1 
ATOM   7551 O  O   . THR C  1  301 ? 14.329  -9.663  25.728 1.00 54.68  ? 314 THR C O   1 
ATOM   7552 C  CB  . THR C  1  301 ? 17.590  -9.712  26.675 1.00 54.21  ? 314 THR C CB  1 
ATOM   7553 O  OG1 . THR C  1  301 ? 16.868  -10.098 27.845 1.00 52.24  ? 314 THR C OG1 1 
ATOM   7554 C  CG2 . THR C  1  301 ? 18.820  -8.888  27.026 1.00 58.15  ? 314 THR C CG2 1 
ATOM   7555 N  N   . GLY C  1  302 ? 15.768  -10.782 24.397 1.00 47.14  ? 315 GLY C N   1 
ATOM   7556 C  CA  . GLY C  1  302 ? 14.841  -11.839 24.023 1.00 50.03  ? 315 GLY C CA  1 
ATOM   7557 C  C   . GLY C  1  302 ? 13.728  -11.347 23.096 1.00 49.28  ? 315 GLY C C   1 
ATOM   7558 O  O   . GLY C  1  302 ? 13.963  -10.496 22.241 1.00 48.79  ? 315 GLY C O   1 
ATOM   7559 N  N   . ILE C  1  303 ? 12.527  -11.898 23.311 1.00 49.94  ? 316 ILE C N   1 
ATOM   7560 C  CA  . ILE C  1  303 ? 11.342  -11.614 22.510 1.00 54.42  ? 316 ILE C CA  1 
ATOM   7561 C  C   . ILE C  1  303 ? 11.012  -10.124 22.607 1.00 47.09  ? 316 ILE C C   1 
ATOM   7562 O  O   . ILE C  1  303 ? 10.614  -9.495  21.624 1.00 49.15  ? 316 ILE C O   1 
ATOM   7563 C  CB  . ILE C  1  303 ? 10.131  -12.457 22.967 1.00 63.14  ? 316 ILE C CB  1 
ATOM   7564 C  CG1 . ILE C  1  303 ? 10.477  -13.907 23.318 1.00 76.60  ? 316 ILE C CG1 1 
ATOM   7565 C  CG2 . ILE C  1  303 ? 9.024   -12.410 21.915 1.00 62.28  ? 316 ILE C CG2 1 
ATOM   7566 C  CD1 . ILE C  1  303 ? 9.440   -14.569 24.205 1.00 87.59  ? 316 ILE C CD1 1 
ATOM   7567 N  N   . LEU C  1  304 ? 11.178  -9.572  23.814 1.00 42.59  ? 317 LEU C N   1 
ATOM   7568 C  CA  . LEU C  1  304 ? 10.907  -8.167  24.050 1.00 43.20  ? 317 LEU C CA  1 
ATOM   7569 C  C   . LEU C  1  304 ? 11.790  -7.300  23.151 1.00 42.91  ? 317 LEU C C   1 
ATOM   7570 O  O   . LEU C  1  304 ? 11.297  -6.366  22.519 1.00 44.80  ? 317 LEU C O   1 
ATOM   7571 C  CB  . LEU C  1  304 ? 11.097  -7.833  25.525 1.00 41.31  ? 317 LEU C CB  1 
ATOM   7572 C  CG  . LEU C  1  304 ? 10.863  -6.363  25.895 1.00 42.04  ? 317 LEU C CG  1 
ATOM   7573 C  CD1 . LEU C  1  304 ? 9.469   -5.871  25.526 1.00 41.75  ? 317 LEU C CD1 1 
ATOM   7574 C  CD2 . LEU C  1  304 ? 11.086  -6.144  27.382 1.00 43.37  ? 317 LEU C CD2 1 
ATOM   7575 N  N   . ARG C  1  305 ? 13.091  -7.621  23.099 1.00 42.97  ? 318 ARG C N   1 
ATOM   7576 C  CA  A ARG C  1  305 ? 14.031  -6.894  22.261 0.50 38.68  ? 318 ARG C CA  1 
ATOM   7577 C  CA  B ARG C  1  305 ? 14.038  -6.909  22.259 0.50 40.98  ? 318 ARG C CA  1 
ATOM   7578 C  C   . ARG C  1  305 ? 13.607  -7.010  20.799 1.00 38.40  ? 318 ARG C C   1 
ATOM   7579 O  O   . ARG C  1  305 ? 13.562  -6.011  20.098 1.00 39.95  ? 318 ARG C O   1 
ATOM   7580 C  CB  A ARG C  1  305 ? 15.467  -7.404  22.428 0.50 35.94  ? 318 ARG C CB  1 
ATOM   7581 C  CB  B ARG C  1  305 ? 15.433  -7.504  22.463 0.50 41.43  ? 318 ARG C CB  1 
ATOM   7582 C  CG  A ARG C  1  305 ? 16.527  -6.639  21.645 0.50 34.87  ? 318 ARG C CG  1 
ATOM   7583 C  CG  B ARG C  1  305 ? 16.526  -6.764  21.706 0.50 44.24  ? 318 ARG C CG  1 
ATOM   7584 C  CD  A ARG C  1  305 ? 17.886  -7.323  21.718 0.50 33.18  ? 318 ARG C CD  1 
ATOM   7585 C  CD  B ARG C  1  305 ? 17.887  -7.426  21.845 0.50 46.02  ? 318 ARG C CD  1 
ATOM   7586 N  NE  A ARG C  1  305 ? 18.774  -6.786  20.683 0.50 30.93  ? 318 ARG C NE  1 
ATOM   7587 N  NE  B ARG C  1  305 ? 18.943  -6.494  21.432 0.50 47.59  ? 318 ARG C NE  1 
ATOM   7588 C  CZ  A ARG C  1  305 ? 18.901  -7.347  19.493 0.50 26.41  ? 318 ARG C CZ  1 
ATOM   7589 C  CZ  B ARG C  1  305 ? 19.350  -5.435  22.133 0.50 45.27  ? 318 ARG C CZ  1 
ATOM   7590 N  NH1 A ARG C  1  305 ? 18.317  -8.504  19.279 0.50 24.14  ? 318 ARG C NH1 1 
ATOM   7591 N  NH1 B ARG C  1  305 ? 18.975  -5.231  23.399 0.50 52.51  ? 318 ARG C NH1 1 
ATOM   7592 N  NH2 A ARG C  1  305 ? 19.583  -6.741  18.547 0.50 24.23  ? 318 ARG C NH2 1 
ATOM   7593 N  NH2 B ARG C  1  305 ? 20.158  -4.583  21.561 0.50 35.26  ? 318 ARG C NH2 1 
ATOM   7594 N  N   . ARG C  1  306 ? 13.292  -8.231  20.355 1.00 40.21  ? 319 ARG C N   1 
ATOM   7595 C  CA  . ARG C  1  306 ? 12.926  -8.484  18.969 1.00 44.81  ? 319 ARG C CA  1 
ATOM   7596 C  C   . ARG C  1  306 ? 11.698  -7.656  18.593 1.00 40.66  ? 319 ARG C C   1 
ATOM   7597 O  O   . ARG C  1  306 ? 11.724  -6.985  17.562 1.00 37.02  ? 319 ARG C O   1 
ATOM   7598 C  CB  . ARG C  1  306 ? 12.713  -9.984  18.737 1.00 50.98  ? 319 ARG C CB  1 
ATOM   7599 C  CG  . ARG C  1  306 ? 12.291  -10.409 17.339 1.00 59.30  ? 319 ARG C CG  1 
ATOM   7600 C  CD  . ARG C  1  306 ? 11.724  -11.837 17.310 1.00 63.71  ? 319 ARG C CD  1 
ATOM   7601 N  NE  . ARG C  1  306 ? 10.375  -11.897 17.895 1.00 73.19  ? 319 ARG C NE  1 
ATOM   7602 C  CZ  . ARG C  1  306 ? 9.662   -13.003 18.117 1.00 74.60  ? 319 ARG C CZ  1 
ATOM   7603 N  NH1 . ARG C  1  306 ? 10.149  -14.187 17.797 1.00 73.41  ? 319 ARG C NH1 1 
ATOM   7604 N  NH2 . ARG C  1  306 ? 8.475   -12.927 18.691 1.00 75.05  ? 319 ARG C NH2 1 
ATOM   7605 N  N   . ASN C  1  307 ? 10.665  -7.667  19.455 1.00 35.64  ? 320 ASN C N   1 
ATOM   7606 C  CA  . ASN C  1  307 ? 9.395   -7.026  19.149 1.00 36.97  ? 320 ASN C CA  1 
ATOM   7607 C  C   . ASN C  1  307 ? 9.549   -5.505  19.159 1.00 35.52  ? 320 ASN C C   1 
ATOM   7608 O  O   . ASN C  1  307 ? 8.953   -4.809  18.341 1.00 38.31  ? 320 ASN C O   1 
ATOM   7609 C  CB  . ASN C  1  307 ? 8.275   -7.545  20.049 1.00 37.27  ? 320 ASN C CB  1 
ATOM   7610 C  CG  . ASN C  1  307 ? 7.936   -8.983  19.738 1.00 36.09  ? 320 ASN C CG  1 
ATOM   7611 O  OD1 . ASN C  1  307 ? 8.616   -9.616  18.920 1.00 38.40  ? 320 ASN C OD1 1 
ATOM   7612 N  ND2 . ASN C  1  307 ? 6.873   -9.501  20.335 1.00 36.79  ? 320 ASN C ND2 1 
ATOM   7613 N  N   . LEU C  1  308 ? 10.396  -5.001  20.050 1.00 35.84  ? 321 LEU C N   1 
ATOM   7614 C  CA  . LEU C  1  308 ? 10.768  -3.594  20.055 1.00 39.91  ? 321 LEU C CA  1 
ATOM   7615 C  C   . LEU C  1  308 ? 11.409  -3.182  18.736 1.00 38.28  ? 321 LEU C C   1 
ATOM   7616 O  O   . LEU C  1  308 ? 11.061  -2.134  18.197 1.00 39.83  ? 321 LEU C O   1 
ATOM   7617 C  CB  . LEU C  1  308 ? 11.704  -3.285  21.221 1.00 42.77  ? 321 LEU C CB  1 
ATOM   7618 C  CG  . LEU C  1  308 ? 11.021  -2.843  22.518 1.00 44.81  ? 321 LEU C CG  1 
ATOM   7619 C  CD1 . LEU C  1  308 ? 12.026  -2.888  23.651 1.00 44.40  ? 321 LEU C CD1 1 
ATOM   7620 C  CD2 . LEU C  1  308 ? 10.424  -1.450  22.393 1.00 46.05  ? 321 LEU C CD2 1 
ATOM   7621 N  N   . ILE C  1  309 ? 12.368  -3.976  18.248 1.00 37.99  ? 322 ILE C N   1 
ATOM   7622 C  CA  . ILE C  1  309 ? 13.067  -3.643  17.013 1.00 40.57  ? 322 ILE C CA  1 
ATOM   7623 C  C   . ILE C  1  309 ? 12.049  -3.562  15.876 1.00 39.78  ? 322 ILE C C   1 
ATOM   7624 O  O   . ILE C  1  309 ? 12.057  -2.599  15.107 1.00 40.00  ? 322 ILE C O   1 
ATOM   7625 C  CB  . ILE C  1  309 ? 14.197  -4.649  16.726 1.00 39.87  ? 322 ILE C CB  1 
ATOM   7626 C  CG1 . ILE C  1  309 ? 15.342  -4.476  17.724 1.00 36.10  ? 322 ILE C CG1 1 
ATOM   7627 C  CG2 . ILE C  1  309 ? 14.690  -4.549  15.277 1.00 41.03  ? 322 ILE C CG2 1 
ATOM   7628 C  CD1 . ILE C  1  309 ? 16.364  -5.590  17.707 1.00 34.46  ? 322 ILE C CD1 1 
ATOM   7629 N  N   . LYS C  1  310 ? 11.160  -4.562  15.805 1.00 38.25  ? 323 LYS C N   1 
ATOM   7630 C  CA  . LYS C  1  310 ? 10.169  -4.641  14.740 1.00 40.12  ? 323 LYS C CA  1 
ATOM   7631 C  C   . LYS C  1  310 ? 9.203   -3.456  14.802 1.00 38.10  ? 323 LYS C C   1 
ATOM   7632 O  O   . LYS C  1  310 ? 9.021   -2.772  13.796 1.00 35.72  ? 323 LYS C O   1 
ATOM   7633 C  CB  . LYS C  1  310 ? 9.465   -5.994  14.790 1.00 38.60  ? 323 LYS C CB  1 
ATOM   7634 C  CG  . LYS C  1  310 ? 10.313  -7.138  14.247 1.00 41.28  ? 323 LYS C CG  1 
ATOM   7635 C  CD  . LYS C  1  310 ? 9.694   -8.511  14.477 1.00 46.28  ? 323 LYS C CD  1 
ATOM   7636 C  CE  . LYS C  1  310 ? 10.416  -9.641  13.808 1.00 49.61  ? 323 LYS C CE  1 
ATOM   7637 N  NZ  . LYS C  1  310 ? 9.755   -10.899 14.164 1.00 58.66  ? 323 LYS C NZ  1 
ATOM   7638 N  N   . ASN C  1  311 ? 8.629   -3.200  15.984 1.00 33.09  ? 324 ASN C N   1 
ATOM   7639 C  CA  . ASN C  1  311 ? 7.634   -2.149  16.154 1.00 34.32  ? 324 ASN C CA  1 
ATOM   7640 C  C   . ASN C  1  311 ? 8.241   -0.778  15.875 1.00 36.55  ? 324 ASN C C   1 
ATOM   7641 O  O   . ASN C  1  311 ? 7.556   0.084   15.327 1.00 37.29  ? 324 ASN C O   1 
ATOM   7642 C  CB  . ASN C  1  311 ? 6.965   -2.201  17.527 1.00 33.58  ? 324 ASN C CB  1 
ATOM   7643 C  CG  . ASN C  1  311 ? 5.846   -3.210  17.571 1.00 33.39  ? 324 ASN C CG  1 
ATOM   7644 O  OD1 . ASN C  1  311 ? 4.749   -2.935  17.078 1.00 39.80  ? 324 ASN C OD1 1 
ATOM   7645 N  ND2 . ASN C  1  311 ? 6.078   -4.369  18.161 1.00 36.46  ? 324 ASN C ND2 1 
ATOM   7646 N  N   . LEU C  1  312 ? 9.526   -0.592  16.222 1.00 38.45  ? 325 LEU C N   1 
ATOM   7647 C  CA  . LEU C  1  312 ? 10.215  0.660   15.937 1.00 38.29  ? 325 LEU C CA  1 
ATOM   7648 C  C   . LEU C  1  312 ? 10.355  0.864   14.429 1.00 33.83  ? 325 LEU C C   1 
ATOM   7649 O  O   . LEU C  1  312 ? 10.120  1.967   13.950 1.00 34.09  ? 325 LEU C O   1 
ATOM   7650 C  CB  . LEU C  1  312 ? 11.568  0.708   16.636 1.00 37.79  ? 325 LEU C CB  1 
ATOM   7651 C  CG  . LEU C  1  312 ? 11.528  1.038   18.130 1.00 37.21  ? 325 LEU C CG  1 
ATOM   7652 C  CD1 . LEU C  1  312 ? 12.823  0.656   18.803 1.00 38.67  ? 325 LEU C CD1 1 
ATOM   7653 C  CD2 . LEU C  1  312 ? 11.262  2.513   18.360 1.00 38.70  ? 325 LEU C CD2 1 
ATOM   7654 N  N   . HIS C  1  313 ? 10.730  -0.198  13.704 1.00 35.99  ? 326 HIS C N   1 
ATOM   7655 C  CA  . HIS C  1  313 ? 10.851  -0.151  12.251 1.00 34.63  ? 326 HIS C CA  1 
ATOM   7656 C  C   . HIS C  1  313 ? 9.485   0.138   11.631 1.00 34.94  ? 326 HIS C C   1 
ATOM   7657 O  O   . HIS C  1  313 ? 9.349   0.984   10.744 1.00 35.79  ? 326 HIS C O   1 
ATOM   7658 C  CB  . HIS C  1  313 ? 11.501  -1.428  11.697 1.00 36.31  ? 326 HIS C CB  1 
ATOM   7659 C  CG  . HIS C  1  313 ? 11.666  -1.364  10.210 1.00 41.50  ? 326 HIS C CG  1 
ATOM   7660 N  ND1 . HIS C  1  313 ? 12.499  -0.445  9.612  1.00 41.07  ? 326 HIS C ND1 1 
ATOM   7661 C  CD2 . HIS C  1  313 ? 11.043  -2.005  9.215  1.00 39.81  ? 326 HIS C CD2 1 
ATOM   7662 C  CE1 . HIS C  1  313 ? 12.387  -0.559  8.304  1.00 46.73  ? 326 HIS C CE1 1 
ATOM   7663 N  NE2 . HIS C  1  313 ? 11.515  -1.505  8.045  1.00 45.45  ? 326 HIS C NE2 1 
ATOM   7664 N  N   . TYR C  1  314 ? 8.454   -0.562  12.122 1.00 38.34  ? 327 TYR C N   1 
ATOM   7665 C  CA  . TYR C  1  314 ? 7.102   -0.385  11.621 1.00 35.46  ? 327 TYR C CA  1 
ATOM   7666 C  C   . TYR C  1  314 ? 6.660   1.068   11.760 1.00 34.67  ? 327 TYR C C   1 
ATOM   7667 O  O   . TYR C  1  314 ? 6.112   1.620   10.818 1.00 32.78  ? 327 TYR C O   1 
ATOM   7668 C  CB  . TYR C  1  314 ? 6.129   -1.303  12.352 1.00 36.02  ? 327 TYR C CB  1 
ATOM   7669 C  CG  . TYR C  1  314 ? 6.357   -2.793  12.164 1.00 34.31  ? 327 TYR C CG  1 
ATOM   7670 C  CD1 . TYR C  1  314 ? 7.154   -3.291  11.141 1.00 37.39  ? 327 TYR C CD1 1 
ATOM   7671 C  CD2 . TYR C  1  314 ? 5.764   -3.703  13.030 1.00 37.05  ? 327 TYR C CD2 1 
ATOM   7672 C  CE1 . TYR C  1  314 ? 7.366   -4.652  10.988 1.00 37.66  ? 327 TYR C CE1 1 
ATOM   7673 C  CE2 . TYR C  1  314 ? 5.954   -5.067  12.879 1.00 35.78  ? 327 TYR C CE2 1 
ATOM   7674 C  CZ  . TYR C  1  314 ? 6.753   -5.539  11.857 1.00 36.47  ? 327 TYR C CZ  1 
ATOM   7675 O  OH  . TYR C  1  314 ? 6.878   -6.889  11.801 1.00 37.98  ? 327 TYR C OH  1 
ATOM   7676 N  N   . TRP C  1  315 ? 6.935   1.688   12.910 1.00 35.22  ? 328 TRP C N   1 
ATOM   7677 C  CA  . TRP C  1  315 ? 6.586   3.083   13.131 1.00 36.75  ? 328 TRP C CA  1 
ATOM   7678 C  C   . TRP C  1  315 ? 7.333   3.983   12.145 1.00 35.42  ? 328 TRP C C   1 
ATOM   7679 O  O   . TRP C  1  315 ? 6.730   4.899   11.596 1.00 38.25  ? 328 TRP C O   1 
ATOM   7680 C  CB  . TRP C  1  315 ? 6.833   3.488   14.599 1.00 35.93  ? 328 TRP C CB  1 
ATOM   7681 C  CG  . TRP C  1  315 ? 6.292   4.842   14.983 1.00 37.89  ? 328 TRP C CG  1 
ATOM   7682 C  CD1 . TRP C  1  315 ? 5.031   5.325   14.800 1.00 37.15  ? 328 TRP C CD1 1 
ATOM   7683 C  CD2 . TRP C  1  315 ? 7.030   5.929   15.590 1.00 42.06  ? 328 TRP C CD2 1 
ATOM   7684 N  NE1 . TRP C  1  315 ? 4.925   6.618   15.255 1.00 37.80  ? 328 TRP C NE1 1 
ATOM   7685 C  CE2 . TRP C  1  315 ? 6.139   7.021   15.736 1.00 40.58  ? 328 TRP C CE2 1 
ATOM   7686 C  CE3 . TRP C  1  315 ? 8.352   6.080   16.007 1.00 41.52  ? 328 TRP C CE3 1 
ATOM   7687 C  CZ2 . TRP C  1  315 ? 6.529   8.231   16.302 1.00 40.13  ? 328 TRP C CZ2 1 
ATOM   7688 C  CZ3 . TRP C  1  315 ? 8.746   7.288   16.534 1.00 41.32  ? 328 TRP C CZ3 1 
ATOM   7689 C  CH2 . TRP C  1  315 ? 7.849   8.342   16.685 1.00 41.47  ? 328 TRP C CH2 1 
ATOM   7690 N  N   . TRP C  1  316 ? 8.632   3.710   11.917 1.00 39.60  ? 329 TRP C N   1 
ATOM   7691 C  CA  . TRP C  1  316 ? 9.453   4.507   11.015 1.00 36.97  ? 329 TRP C CA  1 
ATOM   7692 C  C   . TRP C  1  316 ? 8.867   4.505   9.594  1.00 33.83  ? 329 TRP C C   1 
ATOM   7693 O  O   . TRP C  1  316 ? 8.897   5.524   8.908  1.00 36.85  ? 329 TRP C O   1 
ATOM   7694 C  CB  . TRP C  1  316 ? 10.925  4.043   11.024 1.00 37.32  ? 329 TRP C CB  1 
ATOM   7695 C  CG  . TRP C  1  316 ? 11.760  4.793   10.016 1.00 37.04  ? 329 TRP C CG  1 
ATOM   7696 C  CD1 . TRP C  1  316 ? 12.286  6.045   10.137 1.00 37.44  ? 329 TRP C CD1 1 
ATOM   7697 C  CD2 . TRP C  1  316 ? 12.018  4.379   8.660  1.00 38.30  ? 329 TRP C CD2 1 
ATOM   7698 N  NE1 . TRP C  1  316 ? 12.898  6.417   8.969  1.00 41.43  ? 329 TRP C NE1 1 
ATOM   7699 C  CE2 . TRP C  1  316 ? 12.716  5.431   8.032  1.00 40.94  ? 329 TRP C CE2 1 
ATOM   7700 C  CE3 . TRP C  1  316 ? 11.707  3.230   7.920  1.00 38.40  ? 329 TRP C CE3 1 
ATOM   7701 C  CZ2 . TRP C  1  316 ? 13.109  5.356   6.698  1.00 41.11  ? 329 TRP C CZ2 1 
ATOM   7702 C  CZ3 . TRP C  1  316 ? 12.074  3.169   6.600  1.00 38.48  ? 329 TRP C CZ3 1 
ATOM   7703 C  CH2 . TRP C  1  316 ? 12.747  4.232   5.993  1.00 39.22  ? 329 TRP C CH2 1 
ATOM   7704 N  N   . THR C  1  317 ? 8.334   3.365   9.139  1.00 36.97  ? 330 THR C N   1 
ATOM   7705 C  CA  . THR C  1  317 ? 7.788   3.263   7.781  1.00 34.81  ? 330 THR C CA  1 
ATOM   7706 C  C   . THR C  1  317 ? 6.694   4.305   7.572  1.00 36.52  ? 330 THR C C   1 
ATOM   7707 O  O   . THR C  1  317 ? 6.624   4.907   6.504  1.00 40.41  ? 330 THR C O   1 
ATOM   7708 C  CB  . THR C  1  317 ? 7.252   1.870   7.446  1.00 32.28  ? 330 THR C CB  1 
ATOM   7709 O  OG1 . THR C  1  317 ? 6.161   1.590   8.316  1.00 36.11  ? 330 THR C OG1 1 
ATOM   7710 C  CG2 . THR C  1  317 ? 8.297   0.774   7.558  1.00 30.14  ? 330 THR C CG2 1 
ATOM   7711 N  N   . GLY C  1  318 ? 5.854   4.530   8.596  1.00 37.88  ? 331 GLY C N   1 
ATOM   7712 C  CA  . GLY C  1  318 ? 4.838   5.576   8.535  1.00 36.54  ? 331 GLY C CA  1 
ATOM   7713 C  C   . GLY C  1  318 ? 5.432   6.976   8.668  1.00 33.33  ? 331 GLY C C   1 
ATOM   7714 O  O   . GLY C  1  318 ? 5.068   7.880   7.918  1.00 36.79  ? 331 GLY C O   1 
ATOM   7715 N  N   . VAL C  1  319 ? 6.339   7.142   9.638  1.00 33.26  ? 332 VAL C N   1 
ATOM   7716 C  CA  . VAL C  1  319 ? 6.972   8.422   9.920  1.00 35.53  ? 332 VAL C CA  1 
ATOM   7717 C  C   . VAL C  1  319 ? 7.689   8.937   8.671  1.00 35.15  ? 332 VAL C C   1 
ATOM   7718 O  O   . VAL C  1  319 ? 7.608   10.118  8.363  1.00 37.24  ? 332 VAL C O   1 
ATOM   7719 C  CB  . VAL C  1  319 ? 7.930   8.251   11.124 1.00 34.38  ? 332 VAL C CB  1 
ATOM   7720 C  CG1 . VAL C  1  319 ? 8.958   9.383   11.265 1.00 33.70  ? 332 VAL C CG1 1 
ATOM   7721 C  CG2 . VAL C  1  319 ? 7.161   8.045   12.423 1.00 34.54  ? 332 VAL C CG2 1 
ATOM   7722 N  N   . ASN C  1  320 ? 8.387   8.041   7.965  1.00 38.21  ? 333 ASN C N   1 
ATOM   7723 C  CA  . ASN C  1  320 ? 9.228   8.434   6.846  1.00 41.55  ? 333 ASN C CA  1 
ATOM   7724 C  C   . ASN C  1  320 ? 8.404   9.204   5.810  1.00 38.69  ? 333 ASN C C   1 
ATOM   7725 O  O   . ASN C  1  320 ? 8.823   10.263  5.338  1.00 41.70  ? 333 ASN C O   1 
ATOM   7726 C  CB  . ASN C  1  320 ? 9.955   7.236   6.241  1.00 41.46  ? 333 ASN C CB  1 
ATOM   7727 C  CG  . ASN C  1  320 ? 11.014  7.664   5.247  1.00 41.96  ? 333 ASN C CG  1 
ATOM   7728 O  OD1 . ASN C  1  320 ? 11.878  8.483   5.594  1.00 48.99  ? 333 ASN C OD1 1 
ATOM   7729 N  ND2 . ASN C  1  320 ? 10.941  7.159   4.016  1.00 39.08  ? 333 ASN C ND2 1 
ATOM   7730 N  N   . VAL C  1  321 ? 7.224   8.663   5.487  1.00 39.87  ? 334 VAL C N   1 
ATOM   7731 C  CA  . VAL C  1  321 ? 6.363   9.254   4.474  1.00 42.50  ? 334 VAL C CA  1 
ATOM   7732 C  C   . VAL C  1  321 ? 5.704   10.510  5.047  1.00 43.32  ? 334 VAL C C   1 
ATOM   7733 O  O   . VAL C  1  321 ? 5.627   11.543  4.391  1.00 48.32  ? 334 VAL C O   1 
ATOM   7734 C  CB  . VAL C  1  321 ? 5.309   8.254   3.952  1.00 40.99  ? 334 VAL C CB  1 
ATOM   7735 C  CG1 . VAL C  1  321 ? 4.424   8.876   2.889  1.00 37.94  ? 334 VAL C CG1 1 
ATOM   7736 C  CG2 . VAL C  1  321 ? 5.944   6.974   3.418  1.00 41.32  ? 334 VAL C CG2 1 
ATOM   7737 N  N   . ALA C  1  322 ? 5.259   10.418  6.302  1.00 46.40  ? 335 ALA C N   1 
ATOM   7738 C  CA  . ALA C  1  322 ? 4.427   11.447  6.899  1.00 43.11  ? 335 ALA C CA  1 
ATOM   7739 C  C   . ALA C  1  322 ? 5.222   12.683  7.303  1.00 41.39  ? 335 ALA C C   1 
ATOM   7740 O  O   . ALA C  1  322 ? 4.628   13.749  7.323  1.00 39.58  ? 335 ALA C O   1 
ATOM   7741 C  CB  . ALA C  1  322 ? 3.697   10.858  8.067  1.00 43.52  ? 335 ALA C CB  1 
ATOM   7742 N  N   . PHE C  1  323 ? 6.513   12.546  7.651  1.00 42.14  ? 336 PHE C N   1 
ATOM   7743 C  CA  . PHE C  1  323 ? 7.339   13.678  8.052  1.00 47.88  ? 336 PHE C CA  1 
ATOM   7744 C  C   . PHE C  1  323 ? 8.251   14.133  6.911  1.00 48.32  ? 336 PHE C C   1 
ATOM   7745 O  O   . PHE C  1  323 ? 9.023   15.069  7.106  1.00 56.23  ? 336 PHE C O   1 
ATOM   7746 C  CB  . PHE C  1  323 ? 8.124   13.329  9.329  1.00 49.25  ? 336 PHE C CB  1 
ATOM   7747 C  CG  . PHE C  1  323 ? 7.280   13.011  10.560 1.00 45.95  ? 336 PHE C CG  1 
ATOM   7748 C  CD1 . PHE C  1  323 ? 5.894   13.137  10.537 1.00 50.60  ? 336 PHE C CD1 1 
ATOM   7749 C  CD2 . PHE C  1  323 ? 7.875   12.658  11.764 1.00 48.27  ? 336 PHE C CD2 1 
ATOM   7750 C  CE1 . PHE C  1  323 ? 5.121   12.859  11.652 1.00 49.09  ? 336 PHE C CE1 1 
ATOM   7751 C  CE2 . PHE C  1  323 ? 7.103   12.382  12.885 1.00 49.83  ? 336 PHE C CE2 1 
ATOM   7752 C  CZ  . PHE C  1  323 ? 5.725   12.487  12.828 1.00 49.83  ? 336 PHE C CZ  1 
ATOM   7753 N  N   . GLY C  1  324 ? 8.173   13.470  5.745  1.00 50.16  ? 337 GLY C N   1 
ATOM   7754 C  CA  . GLY C  1  324 ? 8.948   13.861  4.575  1.00 46.29  ? 337 GLY C CA  1 
ATOM   7755 C  C   . GLY C  1  324 ? 10.425  13.487  4.665  1.00 44.57  ? 337 GLY C C   1 
ATOM   7756 O  O   . GLY C  1  324 ? 11.259  14.240  4.177  1.00 57.89  ? 337 GLY C O   1 
ATOM   7757 N  N   . GLY C  1  325 ? 10.729  12.319  5.252  1.00 43.81  ? 338 GLY C N   1 
ATOM   7758 C  CA  . GLY C  1  325 ? 12.090  11.811  5.367  1.00 45.98  ? 338 GLY C CA  1 
ATOM   7759 C  C   . GLY C  1  325 ? 12.679  12.058  6.753  1.00 42.56  ? 338 GLY C C   1 
ATOM   7760 O  O   . GLY C  1  325 ? 12.910  13.209  7.118  1.00 50.37  ? 338 GLY C O   1 
ATOM   7761 N  N   . CYS C  1  326 ? 12.902  10.971  7.503  1.00 40.37  ? 339 CYS C N   1 
ATOM   7762 C  CA  . CYS C  1  326 ? 13.680  10.990  8.730  1.00 43.84  ? 339 CYS C CA  1 
ATOM   7763 C  C   . CYS C  1  326 ? 14.655  9.820   8.649  1.00 41.95  ? 339 CYS C C   1 
ATOM   7764 O  O   . CYS C  1  326 ? 14.271  8.743   8.198  1.00 40.52  ? 339 CYS C O   1 
ATOM   7765 C  CB  . CYS C  1  326 ? 12.788  10.869  9.973  1.00 48.86  ? 339 CYS C CB  1 
ATOM   7766 S  SG  . CYS C  1  326 ? 11.564  12.197  10.165 1.00 58.89  ? 339 CYS C SG  1 
ATOM   7767 N  N   . ASP C  1  327 ? 15.894  10.008  9.112  1.00 43.39  ? 340 ASP C N   1 
ATOM   7768 C  CA  . ASP C  1  327 ? 16.820  8.896   9.224  1.00 45.46  ? 340 ASP C CA  1 
ATOM   7769 C  C   . ASP C  1  327 ? 16.363  7.996   10.365 1.00 47.75  ? 340 ASP C C   1 
ATOM   7770 O  O   . ASP C  1  327 ? 16.182  8.459   11.488 1.00 46.16  ? 340 ASP C O   1 
ATOM   7771 C  CB  . ASP C  1  327 ? 18.260  9.364   9.387  1.00 53.01  ? 340 ASP C CB  1 
ATOM   7772 C  CG  . ASP C  1  327 ? 18.765  10.253  8.260  1.00 54.34  ? 340 ASP C CG  1 
ATOM   7773 O  OD1 . ASP C  1  327 ? 18.438  9.939   7.108  1.00 50.95  ? 340 ASP C OD1 1 
ATOM   7774 O  OD2 . ASP C  1  327 ? 19.454  11.258  8.549  1.00 62.92  ? 340 ASP C OD2 1 
ATOM   7775 N  N   . GLU C  1  328 ? 16.230  6.700   10.057 1.00 45.77  ? 341 GLU C N   1 
ATOM   7776 C  CA  . GLU C  1  328 ? 15.856  5.698   11.039 1.00 43.20  ? 341 GLU C CA  1 
ATOM   7777 C  C   . GLU C  1  328 ? 16.970  5.536   12.080 1.00 42.07  ? 341 GLU C C   1 
ATOM   7778 O  O   . GLU C  1  328 ? 18.146  5.505   11.726 1.00 44.79  ? 341 GLU C O   1 
ATOM   7779 C  CB  . GLU C  1  328 ? 15.555  4.389   10.308 1.00 39.64  ? 341 GLU C CB  1 
ATOM   7780 C  CG  . GLU C  1  328 ? 14.929  3.325   11.210 1.00 40.49  ? 341 GLU C CG  1 
ATOM   7781 C  CD  . GLU C  1  328 ? 14.556  2.010   10.543 1.00 39.76  ? 341 GLU C CD  1 
ATOM   7782 O  OE1 . GLU C  1  328 ? 14.802  1.868   9.328  1.00 38.60  ? 341 GLU C OE1 1 
ATOM   7783 O  OE2 . GLU C  1  328 ? 14.004  1.119   11.225 1.00 39.11  ? 341 GLU C OE2 1 
ATOM   7784 N  N   . LEU C  1  329 ? 16.569  5.436   13.356 1.00 41.27  ? 342 LEU C N   1 
ATOM   7785 C  CA  . LEU C  1  329 ? 17.450  5.159   14.481 1.00 44.11  ? 342 LEU C CA  1 
ATOM   7786 C  C   . LEU C  1  329 ? 17.300  3.691   14.875 1.00 40.68  ? 342 LEU C C   1 
ATOM   7787 O  O   . LEU C  1  329 ? 16.222  3.118   14.680 1.00 41.59  ? 342 LEU C O   1 
ATOM   7788 C  CB  . LEU C  1  329 ? 17.092  6.106   15.628 1.00 47.51  ? 342 LEU C CB  1 
ATOM   7789 C  CG  . LEU C  1  329 ? 17.360  7.598   15.393 1.00 49.81  ? 342 LEU C CG  1 
ATOM   7790 C  CD1 . LEU C  1  329 ? 16.720  8.411   16.503 1.00 53.80  ? 342 LEU C CD1 1 
ATOM   7791 C  CD2 . LEU C  1  329 ? 18.841  7.904   15.322 1.00 45.64  ? 342 LEU C CD2 1 
ATOM   7792 N  N   . PHE C  1  330 ? 18.388  3.101   15.404 1.00 37.98  ? 343 PHE C N   1 
ATOM   7793 C  CA  . PHE C  1  330 ? 18.432  1.698   15.803 1.00 40.10  ? 343 PHE C CA  1 
ATOM   7794 C  C   . PHE C  1  330 ? 18.935  1.565   17.239 1.00 41.08  ? 343 PHE C C   1 
ATOM   7795 O  O   . PHE C  1  330 ? 20.002  1.013   17.477 1.00 40.51  ? 343 PHE C O   1 
ATOM   7796 C  CB  . PHE C  1  330 ? 19.335  0.905   14.853 1.00 43.07  ? 343 PHE C CB  1 
ATOM   7797 C  CG  . PHE C  1  330 ? 18.889  1.014   13.401 1.00 45.31  ? 343 PHE C CG  1 
ATOM   7798 C  CD1 . PHE C  1  330 ? 17.822  0.252   12.929 1.00 44.61  ? 343 PHE C CD1 1 
ATOM   7799 C  CD2 . PHE C  1  330 ? 19.497  1.912   12.527 1.00 43.20  ? 343 PHE C CD2 1 
ATOM   7800 C  CE1 . PHE C  1  330 ? 17.376  0.385   11.623 1.00 45.23  ? 343 PHE C CE1 1 
ATOM   7801 C  CE2 . PHE C  1  330 ? 19.068  2.031   11.217 1.00 46.12  ? 343 PHE C CE2 1 
ATOM   7802 C  CZ  . PHE C  1  330 ? 18.004  1.265   10.761 1.00 47.44  ? 343 PHE C CZ  1 
ATOM   7803 N  N   . PRO C  1  331 ? 18.161  2.007   18.252 1.00 45.32  ? 344 PRO C N   1 
ATOM   7804 C  CA  . PRO C  1  331 ? 18.633  1.967   19.641 1.00 44.13  ? 344 PRO C CA  1 
ATOM   7805 C  C   . PRO C  1  331 ? 18.925  0.575   20.204 1.00 38.00  ? 344 PRO C C   1 
ATOM   7806 O  O   . PRO C  1  331 ? 19.694  0.460   21.153 1.00 40.34  ? 344 PRO C O   1 
ATOM   7807 C  CB  . PRO C  1  331 ? 17.493  2.690   20.380 1.00 44.03  ? 344 PRO C CB  1 
ATOM   7808 C  CG  . PRO C  1  331 ? 16.281  2.349   19.548 1.00 47.26  ? 344 PRO C CG  1 
ATOM   7809 C  CD  . PRO C  1  331 ? 16.792  2.536   18.124 1.00 43.77  ? 344 PRO C CD  1 
ATOM   7810 N  N   . TYR C  1  332 ? 18.324  -0.474  19.614 1.00 34.11  ? 345 TYR C N   1 
ATOM   7811 C  CA  . TYR C  1  332 ? 18.563  -1.847  20.035 1.00 34.57  ? 345 TYR C CA  1 
ATOM   7812 C  C   . TYR C  1  332 ? 19.226  -2.638  18.906 1.00 36.85  ? 345 TYR C C   1 
ATOM   7813 O  O   . TYR C  1  332 ? 19.229  -3.878  18.904 1.00 34.93  ? 345 TYR C O   1 
ATOM   7814 C  CB  . TYR C  1  332 ? 17.271  -2.514  20.516 1.00 36.99  ? 345 TYR C CB  1 
ATOM   7815 C  CG  . TYR C  1  332 ? 16.500  -1.680  21.526 1.00 39.47  ? 345 TYR C CG  1 
ATOM   7816 C  CD1 . TYR C  1  332 ? 16.978  -1.489  22.822 1.00 41.27  ? 345 TYR C CD1 1 
ATOM   7817 C  CD2 . TYR C  1  332 ? 15.310  -1.054  21.168 1.00 39.33  ? 345 TYR C CD2 1 
ATOM   7818 C  CE1 . TYR C  1  332 ? 16.276  -0.715  23.737 1.00 49.02  ? 345 TYR C CE1 1 
ATOM   7819 C  CE2 . TYR C  1  332 ? 14.610  -0.270  22.072 1.00 44.15  ? 345 TYR C CE2 1 
ATOM   7820 C  CZ  . TYR C  1  332 ? 15.089  -0.104  23.361 1.00 45.01  ? 345 TYR C CZ  1 
ATOM   7821 O  OH  . TYR C  1  332 ? 14.428  0.660   24.271 1.00 47.01  ? 345 TYR C OH  1 
ATOM   7822 N  N   . GLY C  1  333 ? 19.837  -1.908  17.968 1.00 35.53  ? 346 GLY C N   1 
ATOM   7823 C  CA  . GLY C  1  333 ? 20.508  -2.528  16.841 1.00 42.06  ? 346 GLY C CA  1 
ATOM   7824 C  C   . GLY C  1  333 ? 19.522  -3.222  15.897 1.00 45.25  ? 346 GLY C C   1 
ATOM   7825 O  O   . GLY C  1  333 ? 18.400  -2.767  15.714 1.00 42.20  ? 346 GLY C O   1 
ATOM   7826 N  N   . GLN C  1  334 ? 19.950  -4.362  15.339 1.00 46.82  ? 347 GLN C N   1 
ATOM   7827 C  CA  . GLN C  1  334 ? 19.203  -5.070  14.315 1.00 51.18  ? 347 GLN C CA  1 
ATOM   7828 C  C   . GLN C  1  334 ? 18.925  -6.502  14.768 1.00 52.23  ? 347 GLN C C   1 
ATOM   7829 O  O   . GLN C  1  334 ? 19.484  -6.963  15.768 1.00 49.17  ? 347 GLN C O   1 
ATOM   7830 C  CB  . GLN C  1  334 ? 20.028  -5.099  13.029 1.00 56.93  ? 347 GLN C CB  1 
ATOM   7831 C  CG  . GLN C  1  334 ? 20.551  -3.750  12.545 1.00 60.46  ? 347 GLN C CG  1 
ATOM   7832 C  CD  . GLN C  1  334 ? 19.612  -3.044  11.599 1.00 64.65  ? 347 GLN C CD  1 
ATOM   7833 O  OE1 . GLN C  1  334 ? 18.567  -3.571  11.205 1.00 71.21  ? 347 GLN C OE1 1 
ATOM   7834 N  NE2 . GLN C  1  334 ? 19.989  -1.832  11.225 1.00 73.18  ? 347 GLN C NE2 1 
ATOM   7835 N  N   . LEU C  1  335 ? 18.053  -7.196  14.026 1.00 50.10  ? 348 LEU C N   1 
ATOM   7836 C  CA  . LEU C  1  335 ? 17.637  -8.545  14.387 1.00 56.01  ? 348 LEU C CA  1 
ATOM   7837 C  C   . LEU C  1  335 ? 18.772  -9.562  14.146 1.00 58.20  ? 348 LEU C C   1 
ATOM   7838 O  O   . LEU C  1  335 ? 19.353  -9.492  13.045 1.00 66.14  ? 348 LEU C O   1 
ATOM   7839 C  CB  . LEU C  1  335 ? 16.400  -8.940  13.586 1.00 53.57  ? 348 LEU C CB  1 
ATOM   7840 C  CG  . LEU C  1  335 ? 15.111  -8.192  13.920 1.00 55.41  ? 348 LEU C CG  1 
ATOM   7841 C  CD1 . LEU C  1  335 ? 14.017  -8.519  12.928 1.00 54.68  ? 348 LEU C CD1 1 
ATOM   7842 C  CD2 . LEU C  1  335 ? 14.704  -8.536  15.335 1.00 57.59  ? 348 LEU C CD2 1 
HETATM 7843 C  C1  . NAG D  2  .   ? 29.601  12.563  34.233 1.00 57.91  ? 1   NAG G C1  1 
HETATM 7844 C  C2  . NAG D  2  .   ? 29.720  13.940  34.859 1.00 66.72  ? 1   NAG G C2  1 
HETATM 7845 C  C3  . NAG D  2  .   ? 29.176  14.987  33.889 1.00 69.50  ? 1   NAG G C3  1 
HETATM 7846 C  C4  . NAG D  2  .   ? 29.849  14.912  32.523 1.00 74.15  ? 1   NAG G C4  1 
HETATM 7847 C  C5  . NAG D  2  .   ? 29.770  13.478  31.993 1.00 71.36  ? 1   NAG G C5  1 
HETATM 7848 C  C6  . NAG D  2  .   ? 30.556  13.246  30.707 1.00 64.11  ? 1   NAG G C6  1 
HETATM 7849 C  C7  . NAG D  2  .   ? 27.837  13.489  36.400 1.00 92.21  ? 1   NAG G C7  1 
HETATM 7850 C  C8  . NAG D  2  .   ? 26.655  14.332  36.032 1.00 91.32  ? 1   NAG G C8  1 
HETATM 7851 N  N2  . NAG D  2  .   ? 29.045  14.018  36.141 1.00 82.60  ? 1   NAG G N2  1 
HETATM 7852 O  O3  . NAG D  2  .   ? 29.318  16.279  34.455 1.00 66.13  ? 1   NAG G O3  1 
HETATM 7853 O  O4  . NAG D  2  .   ? 29.145  15.814  31.643 1.00 80.56  ? 1   NAG G O4  1 
HETATM 7854 O  O5  . NAG D  2  .   ? 30.309  12.580  32.990 1.00 65.61  ? 1   NAG G O5  1 
HETATM 7855 O  O6  . NAG D  2  .   ? 31.943  13.664  30.821 1.00 55.07  ? 1   NAG G O6  1 
HETATM 7856 O  O7  . NAG D  2  .   ? 27.681  12.388  36.931 1.00 89.29  ? 1   NAG G O7  1 
HETATM 7857 C  C1  . NAG D  2  .   ? 29.802  16.730  30.820 1.00 84.21  ? 2   NAG G C1  1 
HETATM 7858 C  C2  . NAG D  2  .   ? 28.989  16.931  29.547 1.00 91.02  ? 2   NAG G C2  1 
HETATM 7859 C  C3  . NAG D  2  .   ? 29.634  18.000  28.665 1.00 100.25 ? 2   NAG G C3  1 
HETATM 7860 C  C4  . NAG D  2  .   ? 29.945  19.277  29.442 1.00 98.37  ? 2   NAG G C4  1 
HETATM 7861 C  C5  . NAG D  2  .   ? 30.718  18.928  30.711 1.00 91.24  ? 2   NAG G C5  1 
HETATM 7862 C  C6  . NAG D  2  .   ? 31.000  20.121  31.603 1.00 91.83  ? 2   NAG G C6  1 
HETATM 7863 C  C7  . NAG D  2  .   ? 27.667  14.980  28.802 1.00 90.20  ? 2   NAG G C7  1 
HETATM 7864 C  C8  . NAG D  2  .   ? 27.629  13.791  27.886 1.00 88.30  ? 2   NAG G C8  1 
HETATM 7865 N  N2  . NAG D  2  .   ? 28.797  15.703  28.796 1.00 93.38  ? 2   NAG G N2  1 
HETATM 7866 O  O3  . NAG D  2  .   ? 28.747  18.262  27.584 1.00 106.74 ? 2   NAG G O3  1 
HETATM 7867 O  O4  . NAG D  2  .   ? 30.757  20.158  28.645 1.00 104.83 ? 2   NAG G O4  1 
HETATM 7868 O  O5  . NAG D  2  .   ? 29.946  17.985  31.479 1.00 85.11  ? 2   NAG G O5  1 
HETATM 7869 O  O6  . NAG D  2  .   ? 29.810  20.809  31.963 1.00 89.04  ? 2   NAG G O6  1 
HETATM 7870 O  O7  . NAG D  2  .   ? 26.718  15.263  29.527 1.00 78.91  ? 2   NAG G O7  1 
HETATM 7871 C  C1  . BMA D  2  .   ? 30.264  21.067  27.706 1.00 108.37 ? 3   BMA G C1  1 
HETATM 7872 C  C2  . BMA D  2  .   ? 31.435  22.014  27.453 1.00 108.45 ? 3   BMA G C2  1 
HETATM 7873 C  C3  . BMA D  2  .   ? 31.178  22.907  26.253 1.00 116.15 ? 3   BMA G C3  1 
HETATM 7874 C  C4  . BMA D  2  .   ? 30.875  22.058  25.036 1.00 120.75 ? 3   BMA G C4  1 
HETATM 7875 C  C5  . BMA D  2  .   ? 29.635  21.204  25.306 1.00 117.75 ? 3   BMA G C5  1 
HETATM 7876 C  C6  . BMA D  2  .   ? 29.341  20.236  24.171 1.00 117.51 ? 3   BMA G C6  1 
HETATM 7877 O  O2  . BMA D  2  .   ? 32.644  21.269  27.309 1.00 97.41  ? 3   BMA G O2  1 
HETATM 7878 O  O3  . BMA D  2  .   ? 32.314  23.740  25.992 1.00 111.70 ? 3   BMA G O3  1 
HETATM 7879 O  O4  . BMA D  2  .   ? 30.663  22.901  23.905 1.00 114.74 ? 3   BMA G O4  1 
HETATM 7880 O  O5  . BMA D  2  .   ? 29.830  20.400  26.514 1.00 112.02 ? 3   BMA G O5  1 
HETATM 7881 O  O6  . BMA D  2  .   ? 28.032  19.652  24.315 1.00 123.00 ? 3   BMA G O6  1 
HETATM 7882 C  C1  . MAN D  2  .   ? 32.402  24.933  26.709 1.00 104.47 ? 4   MAN G C1  1 
HETATM 7883 C  C2  . MAN D  2  .   ? 33.076  25.932  25.775 1.00 104.36 ? 4   MAN G C2  1 
HETATM 7884 C  C3  . MAN D  2  .   ? 34.513  25.494  25.490 1.00 102.87 ? 4   MAN G C3  1 
HETATM 7885 C  C4  . MAN D  2  .   ? 35.269  25.346  26.804 1.00 97.68  ? 4   MAN G C4  1 
HETATM 7886 C  C5  . MAN D  2  .   ? 34.533  24.347  27.713 1.00 97.01  ? 4   MAN G C5  1 
HETATM 7887 C  C6  . MAN D  2  .   ? 35.159  24.208  29.084 1.00 95.50  ? 4   MAN G C6  1 
HETATM 7888 O  O2  . MAN D  2  .   ? 32.997  27.245  26.333 1.00 95.25  ? 4   MAN G O2  1 
HETATM 7889 O  O3  . MAN D  2  .   ? 35.166  26.424  24.625 1.00 104.38 ? 4   MAN G O3  1 
HETATM 7890 O  O4  . MAN D  2  .   ? 36.595  24.894  26.557 1.00 86.36  ? 4   MAN G O4  1 
HETATM 7891 O  O5  . MAN D  2  .   ? 33.156  24.781  27.915 1.00 96.82  ? 4   MAN G O5  1 
HETATM 7892 O  O6  . MAN D  2  .   ? 35.177  25.450  29.801 1.00 86.50  ? 4   MAN G O6  1 
HETATM 7893 C  C1  . MAN D  2  .   ? 27.557  18.867  23.250 1.00 122.86 ? 5   MAN G C1  1 
HETATM 7894 C  C2  . MAN D  2  .   ? 26.040  18.877  23.385 1.00 115.01 ? 5   MAN G C2  1 
HETATM 7895 C  C3  . MAN D  2  .   ? 25.622  18.145  24.654 1.00 111.22 ? 5   MAN G C3  1 
HETATM 7896 C  C4  . MAN D  2  .   ? 26.182  16.731  24.668 1.00 110.06 ? 5   MAN G C4  1 
HETATM 7897 C  C5  . MAN D  2  .   ? 27.708  16.734  24.464 1.00 115.77 ? 5   MAN G C5  1 
HETATM 7898 C  C6  . MAN D  2  .   ? 28.262  15.321  24.301 1.00 109.02 ? 5   MAN G C6  1 
HETATM 7899 O  O2  . MAN D  2  .   ? 25.446  18.329  22.212 1.00 119.97 ? 5   MAN G O2  1 
HETATM 7900 O  O3  . MAN D  2  .   ? 24.199  18.113  24.772 1.00 100.35 ? 5   MAN G O3  1 
HETATM 7901 O  O4  . MAN D  2  .   ? 25.864  16.125  25.920 1.00 108.12 ? 5   MAN G O4  1 
HETATM 7902 O  O5  . MAN D  2  .   ? 28.047  17.518  23.271 1.00 123.25 ? 5   MAN G O5  1 
HETATM 7903 O  O6  . MAN D  2  .   ? 29.546  15.240  23.671 1.00 95.59  ? 5   MAN G O6  1 
HETATM 7904 C  C1  . NAG E  3  .   ? 28.491  -8.658  19.308 1.00 59.33  ? 1   NAG I C1  1 
HETATM 7905 C  C2  . NAG E  3  .   ? 29.069  -9.579  18.229 1.00 56.19  ? 1   NAG I C2  1 
HETATM 7906 C  C3  . NAG E  3  .   ? 28.353  -9.521  16.876 1.00 55.77  ? 1   NAG I C3  1 
HETATM 7907 C  C4  . NAG E  3  .   ? 26.853  -9.676  17.067 1.00 55.43  ? 1   NAG I C4  1 
HETATM 7908 C  C5  . NAG E  3  .   ? 26.389  -8.598  18.048 1.00 56.37  ? 1   NAG I C5  1 
HETATM 7909 C  C6  . NAG E  3  .   ? 24.923  -8.712  18.396 1.00 50.02  ? 1   NAG I C6  1 
HETATM 7910 C  C7  . NAG E  3  .   ? 31.393  -10.123 18.524 1.00 56.97  ? 1   NAG I C7  1 
HETATM 7911 C  C8  . NAG E  3  .   ? 32.826  -9.738  18.323 1.00 57.55  ? 1   NAG I C8  1 
HETATM 7912 N  N2  . NAG E  3  .   ? 30.474  -9.271  18.075 1.00 55.79  ? 1   NAG I N2  1 
HETATM 7913 O  O3  . NAG E  3  .   ? 28.902  -10.567 16.073 1.00 52.85  ? 1   NAG I O3  1 
HETATM 7914 O  O4  . NAG E  3  .   ? 26.170  -9.559  15.802 1.00 61.67  ? 1   NAG I O4  1 
HETATM 7915 O  O5  . NAG E  3  .   ? 27.064  -8.729  19.324 1.00 54.28  ? 1   NAG I O5  1 
HETATM 7916 O  O6  . NAG E  3  .   ? 24.682  -9.951  19.086 1.00 41.20  ? 1   NAG I O6  1 
HETATM 7917 O  O7  . NAG E  3  .   ? 31.076  -11.176 19.066 1.00 49.66  ? 1   NAG I O7  1 
HETATM 7918 C  C1  . NAG E  3  .   ? 25.901  -10.710 15.061 1.00 69.07  ? 2   NAG I C1  1 
HETATM 7919 C  C2  . NAG E  3  .   ? 24.566  -10.489 14.363 1.00 65.16  ? 2   NAG I C2  1 
HETATM 7920 C  C3  . NAG E  3  .   ? 24.303  -11.575 13.322 1.00 70.28  ? 2   NAG I C3  1 
HETATM 7921 C  C4  . NAG E  3  .   ? 25.484  -11.655 12.361 1.00 76.22  ? 2   NAG I C4  1 
HETATM 7922 C  C5  . NAG E  3  .   ? 26.761  -11.925 13.154 1.00 78.50  ? 2   NAG I C5  1 
HETATM 7923 C  C6  . NAG E  3  .   ? 28.012  -11.919 12.312 1.00 75.79  ? 2   NAG I C6  1 
HETATM 7924 C  C7  . NAG E  3  .   ? 22.936  -9.236  15.703 1.00 53.03  ? 2   NAG I C7  1 
HETATM 7925 C  C8  . NAG E  3  .   ? 21.739  -9.344  16.600 1.00 51.34  ? 2   NAG I C8  1 
HETATM 7926 N  N2  . NAG E  3  .   ? 23.548  -10.385 15.385 1.00 56.24  ? 2   NAG I N2  1 
HETATM 7927 O  O3  . NAG E  3  .   ? 23.096  -11.263 12.641 1.00 70.69  ? 2   NAG I O3  1 
HETATM 7928 O  O4  . NAG E  3  .   ? 25.288  -12.697 11.394 1.00 89.43  ? 2   NAG I O4  1 
HETATM 7929 O  O5  . NAG E  3  .   ? 26.969  -10.886 14.131 1.00 71.56  ? 2   NAG I O5  1 
HETATM 7930 O  O6  . NAG E  3  .   ? 29.155  -12.056 13.145 1.00 74.62  ? 2   NAG I O6  1 
HETATM 7931 O  O7  . NAG E  3  .   ? 23.331  -8.150  15.289 1.00 44.46  ? 2   NAG I O7  1 
HETATM 7932 C  C1  . BMA E  3  .   ? 25.610  -12.317 10.093 1.00 89.05  ? 3   BMA I C1  1 
HETATM 7933 C  C2  . BMA E  3  .   ? 25.765  -13.567 9.243  1.00 88.18  ? 3   BMA I C2  1 
HETATM 7934 C  C3  . BMA E  3  .   ? 26.063  -13.151 7.821  1.00 87.61  ? 3   BMA I C3  1 
HETATM 7935 C  C4  . BMA E  3  .   ? 25.013  -12.181 7.297  1.00 88.50  ? 3   BMA I C4  1 
HETATM 7936 C  C5  . BMA E  3  .   ? 24.915  -10.972 8.229  1.00 88.40  ? 3   BMA I C5  1 
HETATM 7937 C  C6  . BMA E  3  .   ? 23.831  -9.975  7.850  1.00 90.43  ? 3   BMA I C6  1 
HETATM 7938 O  O2  . BMA E  3  .   ? 24.617  -14.402 9.360  1.00 86.86  ? 3   BMA I O2  1 
HETATM 7939 O  O3  . BMA E  3  .   ? 26.148  -14.326 7.012  1.00 82.86  ? 3   BMA I O3  1 
HETATM 7940 O  O4  . BMA E  3  .   ? 25.368  -11.744 5.988  1.00 91.59  ? 3   BMA I O4  1 
HETATM 7941 O  O5  . BMA E  3  .   ? 24.608  -11.459 9.547  1.00 90.19  ? 3   BMA I O5  1 
HETATM 7942 O  O6  . BMA E  3  .   ? 22.509  -10.570 7.815  1.00 89.23  ? 3   BMA I O6  1 
HETATM 7943 C  C1  . MAN E  3  .   ? 21.601  -9.990  6.909  1.00 98.82  ? 4   MAN I C1  1 
HETATM 7944 C  C2  . MAN E  3  .   ? 20.216  -10.559 7.222  1.00 95.83  ? 4   MAN I C2  1 
HETATM 7945 C  C3  . MAN E  3  .   ? 20.148  -12.048 6.879  1.00 93.66  ? 4   MAN I C3  1 
HETATM 7946 C  C4  . MAN E  3  .   ? 20.607  -12.302 5.448  1.00 98.69  ? 4   MAN I C4  1 
HETATM 7947 C  C5  . MAN E  3  .   ? 22.007  -11.710 5.251  1.00 111.25 ? 4   MAN I C5  1 
HETATM 7948 C  C6  . MAN E  3  .   ? 22.542  -11.866 3.843  1.00 112.52 ? 4   MAN I C6  1 
HETATM 7949 O  O2  . MAN E  3  .   ? 19.203  -9.796  6.564  1.00 91.99  ? 4   MAN I O2  1 
HETATM 7950 O  O3  . MAN E  3  .   ? 18.818  -12.552 7.091  1.00 90.80  ? 4   MAN I O3  1 
HETATM 7951 O  O4  . MAN E  3  .   ? 20.649  -13.704 5.197  1.00 91.13  ? 4   MAN I O4  1 
HETATM 7952 O  O5  . MAN E  3  .   ? 21.974  -10.283 5.558  1.00 105.33 ? 4   MAN I O5  1 
HETATM 7953 O  O6  . MAN E  3  .   ? 21.676  -11.220 2.891  1.00 120.88 ? 4   MAN I O6  1 
HETATM 7954 C  C1  . MAN E  3  .   ? 18.800  -13.688 7.900  1.00 90.20  ? 5   MAN I C1  1 
HETATM 7955 C  C2  . MAN E  3  .   ? 17.441  -14.367 7.833  1.00 87.76  ? 5   MAN I C2  1 
HETATM 7956 C  C3  . MAN E  3  .   ? 16.359  -13.483 8.426  1.00 90.19  ? 5   MAN I C3  1 
HETATM 7957 C  C4  . MAN E  3  .   ? 16.728  -13.029 9.835  1.00 89.84  ? 5   MAN I C4  1 
HETATM 7958 C  C5  . MAN E  3  .   ? 18.140  -12.419 9.863  1.00 89.35  ? 5   MAN I C5  1 
HETATM 7959 C  C6  . MAN E  3  .   ? 18.641  -12.134 11.270 1.00 84.51  ? 5   MAN I C6  1 
HETATM 7960 O  O2  . MAN E  3  .   ? 17.505  -15.615 8.519  1.00 82.28  ? 5   MAN I O2  1 
HETATM 7961 O  O3  . MAN E  3  .   ? 15.129  -14.202 8.458  1.00 94.57  ? 5   MAN I O3  1 
HETATM 7962 O  O4  . MAN E  3  .   ? 15.789  -12.055 10.281 1.00 79.76  ? 5   MAN I O4  1 
HETATM 7963 O  O5  . MAN E  3  .   ? 19.085  -13.344 9.257  1.00 87.71  ? 5   MAN I O5  1 
HETATM 7964 O  O6  . MAN E  3  .   ? 19.913  -11.459 11.268 1.00 73.32  ? 5   MAN I O6  1 
HETATM 7965 C  C1  . MAN E  3  .   ? 21.103  -12.045 1.908  1.00 126.09 ? 6   MAN I C1  1 
HETATM 7966 C  C2  . MAN E  3  .   ? 21.486  -11.459 0.556  1.00 117.36 ? 6   MAN I C2  1 
HETATM 7967 C  C3  . MAN E  3  .   ? 20.844  -10.086 0.361  1.00 112.13 ? 6   MAN I C3  1 
HETATM 7968 C  C4  . MAN E  3  .   ? 19.335  -10.140 0.597  1.00 111.10 ? 6   MAN I C4  1 
HETATM 7969 C  C5  . MAN E  3  .   ? 19.001  -10.805 1.946  1.00 117.72 ? 6   MAN I C5  1 
HETATM 7970 C  C6  . MAN E  3  .   ? 17.510  -11.051 2.130  1.00 107.48 ? 6   MAN I C6  1 
HETATM 7971 O  O2  . MAN E  3  .   ? 21.149  -12.389 -0.469 1.00 108.23 ? 6   MAN I O2  1 
HETATM 7972 O  O3  . MAN E  3  .   ? 21.137  -9.599  -0.949 1.00 109.01 ? 6   MAN I O3  1 
HETATM 7973 O  O4  . MAN E  3  .   ? 18.801  -8.814  0.592  1.00 96.99  ? 6   MAN I O4  1 
HETATM 7974 O  O5  . MAN E  3  .   ? 19.677  -12.096 2.036  1.00 129.25 ? 6   MAN I O5  1 
HETATM 7975 O  O6  . MAN E  3  .   ? 17.169  -11.390 3.477  1.00 91.06  ? 6   MAN I O6  1 
HETATM 7976 C  C1  . MAN E  3  .   ? 27.460  -14.751 6.780  1.00 82.77  ? 7   MAN I C1  1 
HETATM 7977 C  C2  . MAN E  3  .   ? 27.536  -15.431 5.412  1.00 77.58  ? 7   MAN I C2  1 
HETATM 7978 C  C3  . MAN E  3  .   ? 26.739  -16.749 5.405  1.00 78.16  ? 7   MAN I C3  1 
HETATM 7979 C  C4  . MAN E  3  .   ? 27.161  -17.656 6.559  1.00 76.03  ? 7   MAN I C4  1 
HETATM 7980 C  C5  . MAN E  3  .   ? 27.097  -16.896 7.904  1.00 78.99  ? 7   MAN I C5  1 
HETATM 7981 C  C6  . MAN E  3  .   ? 27.660  -17.711 9.051  1.00 74.26  ? 7   MAN I C6  1 
HETATM 7982 O  O2  . MAN E  3  .   ? 28.900  -15.628 5.039  1.00 64.84  ? 7   MAN I O2  1 
HETATM 7983 O  O3  . MAN E  3  .   ? 26.908  -17.432 4.160  1.00 80.13  ? 7   MAN I O3  1 
HETATM 7984 O  O4  . MAN E  3  .   ? 26.277  -18.791 6.613  1.00 72.54  ? 7   MAN I O4  1 
HETATM 7985 O  O5  . MAN E  3  .   ? 27.878  -15.653 7.813  1.00 81.06  ? 7   MAN I O5  1 
HETATM 7986 O  O6  . MAN E  3  .   ? 27.868  -16.922 10.221 1.00 74.09  ? 7   MAN I O6  1 
HETATM 7987 C  C1  . NAG F  4  .   ? 25.260  -11.186 68.859 1.00 67.35  ? 1   NAG b C1  1 
HETATM 7988 C  C2  . NAG F  4  .   ? 25.745  -10.037 69.715 1.00 75.04  ? 1   NAG b C2  1 
HETATM 7989 C  C3  . NAG F  4  .   ? 26.522  -10.587 70.901 1.00 85.80  ? 1   NAG b C3  1 
HETATM 7990 C  C4  . NAG F  4  .   ? 25.665  -11.571 71.691 1.00 85.67  ? 1   NAG b C4  1 
HETATM 7991 C  C5  . NAG F  4  .   ? 25.133  -12.663 70.760 1.00 85.41  ? 1   NAG b C5  1 
HETATM 7992 C  C6  . NAG F  4  .   ? 24.192  -13.660 71.438 1.00 81.30  ? 1   NAG b C6  1 
HETATM 7993 C  C7  . NAG F  4  .   ? 27.636  -9.194  68.295 1.00 85.53  ? 1   NAG b C7  1 
HETATM 7994 C  C8  . NAG F  4  .   ? 28.410  -7.929  68.079 1.00 85.60  ? 1   NAG b C8  1 
HETATM 7995 N  N2  . NAG F  4  .   ? 26.474  -9.043  68.952 1.00 82.81  ? 1   NAG b N2  1 
HETATM 7996 O  O3  . NAG F  4  .   ? 26.959  -9.507  71.711 1.00 91.87  ? 1   NAG b O3  1 
HETATM 7997 O  O4  . NAG F  4  .   ? 26.481  -12.199 72.687 1.00 97.99  ? 1   NAG b O4  1 
HETATM 7998 O  O5  . NAG F  4  .   ? 24.439  -12.063 69.642 1.00 77.12  ? 1   NAG b O5  1 
HETATM 7999 O  O6  . NAG F  4  .   ? 22.869  -13.169 71.710 1.00 62.09  ? 1   NAG b O6  1 
HETATM 8000 O  O7  . NAG F  4  .   ? 28.031  -10.273 67.854 1.00 76.80  ? 1   NAG b O7  1 
HETATM 8001 C  C1  . NAG F  4  .   ? 27.364  -11.482 73.496 1.00 102.87 ? 2   NAG b C1  1 
HETATM 8002 C  C2  . NAG F  4  .   ? 27.540  -12.326 74.751 1.00 97.96  ? 2   NAG b C2  1 
HETATM 8003 C  C3  . NAG F  4  .   ? 28.543  -11.663 75.699 1.00 103.60 ? 2   NAG b C3  1 
HETATM 8004 C  C4  . NAG F  4  .   ? 29.842  -11.325 74.973 1.00 105.31 ? 2   NAG b C4  1 
HETATM 8005 C  C5  . NAG F  4  .   ? 29.557  -10.517 73.708 1.00 102.36 ? 2   NAG b C5  1 
HETATM 8006 C  C6  . NAG F  4  .   ? 30.806  -10.272 72.883 1.00 106.58 ? 2   NAG b C6  1 
HETATM 8007 C  C7  . NAG F  4  .   ? 25.580  -13.735 75.167 1.00 78.29  ? 2   NAG b C7  1 
HETATM 8008 C  C8  . NAG F  4  .   ? 24.300  -13.881 75.927 1.00 83.93  ? 2   NAG b C8  1 
HETATM 8009 N  N2  . NAG F  4  .   ? 26.236  -12.583 75.337 1.00 81.86  ? 2   NAG b N2  1 
HETATM 8010 O  O3  . NAG F  4  .   ? 28.818  -12.511 76.807 1.00 104.30 ? 2   NAG b O3  1 
HETATM 8011 O  O4  . NAG F  4  .   ? 30.685  -10.557 75.832 1.00 97.58  ? 2   NAG b O4  1 
HETATM 8012 O  O5  . NAG F  4  .   ? 28.629  -11.243 72.874 1.00 96.51  ? 2   NAG b O5  1 
HETATM 8013 O  O6  . NAG F  4  .   ? 30.510  -9.782  71.566 1.00 105.67 ? 2   NAG b O6  1 
HETATM 8014 O  O7  . NAG F  4  .   ? 26.004  -14.629 74.440 1.00 71.04  ? 2   NAG b O7  1 
HETATM 8015 C  C1  . NAG G  5  .   ? 15.783  -30.471 54.678 1.00 50.57  ? 1   NAG c C1  1 
HETATM 8016 C  C2  . NAG G  5  .   ? 14.668  -31.484 54.438 1.00 53.96  ? 1   NAG c C2  1 
HETATM 8017 C  C3  . NAG G  5  .   ? 15.094  -32.841 54.973 1.00 54.51  ? 1   NAG c C3  1 
HETATM 8018 C  C4  . NAG G  5  .   ? 16.413  -33.267 54.345 1.00 51.63  ? 1   NAG c C4  1 
HETATM 8019 C  C5  . NAG G  5  .   ? 17.481  -32.218 54.620 1.00 50.19  ? 1   NAG c C5  1 
HETATM 8020 C  C6  . NAG G  5  .   ? 18.771  -32.523 53.889 1.00 46.67  ? 1   NAG c C6  1 
HETATM 8021 C  C7  . NAG G  5  .   ? 12.316  -30.785 54.255 1.00 55.96  ? 1   NAG c C7  1 
HETATM 8022 C  C8  . NAG G  5  .   ? 11.040  -30.482 54.986 1.00 53.09  ? 1   NAG c C8  1 
HETATM 8023 N  N2  . NAG G  5  .   ? 13.381  -31.112 55.004 1.00 54.59  ? 1   NAG c N2  1 
HETATM 8024 O  O3  . NAG G  5  .   ? 14.046  -33.744 54.657 1.00 54.47  ? 1   NAG c O3  1 
HETATM 8025 O  O4  . NAG G  5  .   ? 16.826  -34.523 54.872 1.00 51.97  ? 1   NAG c O4  1 
HETATM 8026 O  O5  . NAG G  5  .   ? 17.025  -30.934 54.145 1.00 50.17  ? 1   NAG c O5  1 
HETATM 8027 O  O6  . NAG G  5  .   ? 18.570  -32.422 52.475 1.00 46.28  ? 1   NAG c O6  1 
HETATM 8028 O  O7  . NAG G  5  .   ? 12.373  -30.744 53.028 1.00 50.50  ? 1   NAG c O7  1 
HETATM 8029 C  C1  . NAG G  5  .   ? 16.493  -35.565 54.012 1.00 63.83  ? 2   NAG c C1  1 
HETATM 8030 C  C2  . NAG G  5  .   ? 17.526  -36.654 54.290 1.00 65.80  ? 2   NAG c C2  1 
HETATM 8031 C  C3  . NAG G  5  .   ? 17.058  -37.972 53.694 1.00 70.27  ? 2   NAG c C3  1 
HETATM 8032 C  C4  . NAG G  5  .   ? 15.645  -38.278 54.160 1.00 71.92  ? 2   NAG c C4  1 
HETATM 8033 C  C5  . NAG G  5  .   ? 14.703  -37.161 53.724 1.00 71.95  ? 2   NAG c C5  1 
HETATM 8034 C  C6  . NAG G  5  .   ? 13.289  -37.370 54.211 1.00 75.80  ? 2   NAG c C6  1 
HETATM 8035 C  C7  . NAG G  5  .   ? 19.832  -36.007 54.591 1.00 55.27  ? 2   NAG c C7  1 
HETATM 8036 C  C8  . NAG G  5  .   ? 21.094  -35.535 53.935 1.00 50.68  ? 2   NAG c C8  1 
HETATM 8037 N  N2  . NAG G  5  .   ? 18.830  -36.311 53.771 1.00 63.51  ? 2   NAG c N2  1 
HETATM 8038 O  O3  . NAG G  5  .   ? 17.944  -39.020 54.061 1.00 65.51  ? 2   NAG c O3  1 
HETATM 8039 O  O4  . NAG G  5  .   ? 15.262  -39.513 53.551 1.00 82.56  ? 2   NAG c O4  1 
HETATM 8040 O  O5  . NAG G  5  .   ? 15.140  -35.907 54.286 1.00 73.63  ? 2   NAG c O5  1 
HETATM 8041 O  O6  . NAG G  5  .   ? 13.279  -37.592 55.621 1.00 79.68  ? 2   NAG c O6  1 
HETATM 8042 O  O7  . NAG G  5  .   ? 19.704  -36.086 55.807 1.00 54.57  ? 2   NAG c O7  1 
HETATM 8043 C  C1  . BMA G  5  .   ? 14.851  -40.613 54.305 1.00 88.03  ? 3   BMA c C1  1 
HETATM 8044 C  C2  . BMA G  5  .   ? 14.218  -41.582 53.312 1.00 88.38  ? 3   BMA c C2  1 
HETATM 8045 C  C3  . BMA G  5  .   ? 13.673  -42.771 54.077 1.00 96.36  ? 3   BMA c C3  1 
HETATM 8046 C  C4  . BMA G  5  .   ? 14.784  -43.446 54.896 1.00 96.54  ? 3   BMA c C4  1 
HETATM 8047 C  C5  . BMA G  5  .   ? 15.510  -42.420 55.809 1.00 89.76  ? 3   BMA c C5  1 
HETATM 8048 C  C6  . BMA G  5  .   ? 16.765  -42.957 56.508 1.00 86.67  ? 3   BMA c C6  1 
HETATM 8049 O  O2  . BMA G  5  .   ? 15.137  -41.936 52.279 1.00 78.58  ? 3   BMA c O2  1 
HETATM 8050 O  O3  . BMA G  5  .   ? 12.962  -43.644 53.166 1.00 108.17 ? 3   BMA c O3  1 
HETATM 8051 O  O4  . BMA G  5  .   ? 14.212  -44.447 55.737 1.00 90.69  ? 3   BMA c O4  1 
HETATM 8052 O  O5  . BMA G  5  .   ? 15.906  -41.257 55.027 1.00 89.28  ? 3   BMA c O5  1 
HETATM 8053 O  O6  . BMA G  5  .   ? 17.638  -43.788 55.669 1.00 88.94  ? 3   BMA c O6  1 
HETATM 8054 C  C1  . MAN G  5  .   ? 18.638  -44.547 56.315 1.00 95.58  ? 4   MAN c C1  1 
HETATM 8055 C  C2  . MAN G  5  .   ? 19.833  -44.658 55.366 1.00 92.52  ? 4   MAN c C2  1 
HETATM 8056 C  C3  . MAN G  5  .   ? 19.563  -45.571 54.169 1.00 98.34  ? 4   MAN c C3  1 
HETATM 8057 C  C4  . MAN G  5  .   ? 18.962  -46.905 54.600 1.00 107.02 ? 4   MAN c C4  1 
HETATM 8058 C  C5  . MAN G  5  .   ? 17.764  -46.668 55.516 1.00 112.18 ? 4   MAN c C5  1 
HETATM 8059 C  C6  . MAN G  5  .   ? 17.153  -47.954 56.040 1.00 112.33 ? 4   MAN c C6  1 
HETATM 8060 O  O2  . MAN G  5  .   ? 20.978  -45.126 56.073 1.00 88.48  ? 4   MAN c O2  1 
HETATM 8061 O  O3  . MAN G  5  .   ? 20.778  -45.801 53.439 1.00 94.76  ? 4   MAN c O3  1 
HETATM 8062 O  O4  . MAN G  5  .   ? 18.525  -47.639 53.454 1.00 104.10 ? 4   MAN c O4  1 
HETATM 8063 O  O5  . MAN G  5  .   ? 18.182  -45.861 56.660 1.00 104.65 ? 4   MAN c O5  1 
HETATM 8064 O  O6  . MAN G  5  .   ? 15.753  -47.809 56.282 1.00 108.88 ? 4   MAN c O6  1 
HETATM 8065 C  C1  . MAN G  5  .   ? 20.671  -45.542 52.074 1.00 98.28  ? 5   MAN c C1  1 
HETATM 8066 C  C2  . MAN G  5  .   ? 21.863  -46.115 51.314 1.00 102.57 ? 5   MAN c C2  1 
HETATM 8067 C  C3  . MAN G  5  .   ? 23.157  -45.463 51.809 1.00 105.42 ? 5   MAN c C3  1 
HETATM 8068 C  C4  . MAN G  5  .   ? 23.052  -43.942 51.665 1.00 105.70 ? 5   MAN c C4  1 
HETATM 8069 C  C5  . MAN G  5  .   ? 21.800  -43.444 52.419 1.00 100.33 ? 5   MAN c C5  1 
HETATM 8070 C  C6  . MAN G  5  .   ? 21.528  -41.964 52.270 1.00 95.20  ? 5   MAN c C6  1 
HETATM 8071 O  O2  . MAN G  5  .   ? 21.658  -45.943 49.910 1.00 99.64  ? 5   MAN c O2  1 
HETATM 8072 O  O3  . MAN G  5  .   ? 24.293  -45.986 51.114 1.00 96.29  ? 5   MAN c O3  1 
HETATM 8073 O  O4  . MAN G  5  .   ? 24.221  -43.309 52.190 1.00 96.83  ? 5   MAN c O4  1 
HETATM 8074 O  O5  . MAN G  5  .   ? 20.624  -44.126 51.912 1.00 99.77  ? 5   MAN c O5  1 
HETATM 8075 O  O6  . MAN G  5  .   ? 20.659  -41.506 53.313 1.00 83.95  ? 5   MAN c O6  1 
HETATM 8076 C  C1  . MAN G  5  .   ? 13.552  -44.594 52.328 1.00 119.80 ? 6   MAN c C1  1 
HETATM 8077 C  C2  . MAN G  5  .   ? 13.483  -44.172 50.857 1.00 113.91 ? 6   MAN c C2  1 
HETATM 8078 C  C3  . MAN G  5  .   ? 12.042  -44.122 50.357 1.00 108.52 ? 6   MAN c C3  1 
HETATM 8079 C  C4  . MAN G  5  .   ? 11.300  -45.417 50.682 1.00 120.14 ? 6   MAN c C4  1 
HETATM 8080 C  C5  . MAN G  5  .   ? 11.420  -45.732 52.180 1.00 123.83 ? 6   MAN c C5  1 
HETATM 8081 C  C6  . MAN G  5  .   ? 10.784  -47.047 52.586 1.00 121.37 ? 6   MAN c C6  1 
HETATM 8082 O  O2  . MAN G  5  .   ? 14.292  -45.027 50.047 1.00 99.91  ? 6   MAN c O2  1 
HETATM 8083 O  O3  . MAN G  5  .   ? 12.029  -43.861 48.953 1.00 94.85  ? 6   MAN c O3  1 
HETATM 8084 O  O4  . MAN G  5  .   ? 9.920   -45.274 50.341 1.00 122.12 ? 6   MAN c O4  1 
HETATM 8085 O  O5  . MAN G  5  .   ? 12.829  -45.811 52.533 1.00 128.49 ? 6   MAN c O5  1 
HETATM 8086 O  O6  . MAN G  5  .   ? 10.589  -47.102 54.007 1.00 113.66 ? 6   MAN c O6  1 
HETATM 8087 C  C1  . NAG H  6  .   ? -15.116 19.342  32.259 1.00 76.58  ? 1   NAG s C1  1 
HETATM 8088 C  C2  . NAG H  6  .   ? -15.115 18.999  33.744 1.00 76.57  ? 1   NAG s C2  1 
HETATM 8089 C  C3  . NAG H  6  .   ? -14.993 20.278  34.576 1.00 82.45  ? 1   NAG s C3  1 
HETATM 8090 C  C4  . NAG H  6  .   ? -13.918 21.243  34.075 1.00 81.84  ? 1   NAG s C4  1 
HETATM 8091 C  C5  . NAG H  6  .   ? -14.050 21.463  32.568 1.00 83.81  ? 1   NAG s C5  1 
HETATM 8092 C  C6  . NAG H  6  .   ? -12.974 22.353  31.955 1.00 77.38  ? 1   NAG s C6  1 
HETATM 8093 C  C7  . NAG H  6  .   ? -17.560 18.461  33.903 1.00 85.70  ? 1   NAG s C7  1 
HETATM 8094 C  C8  . NAG H  6  .   ? -18.437 17.302  33.528 1.00 78.50  ? 1   NAG s C8  1 
HETATM 8095 N  N2  . NAG H  6  .   ? -16.259 18.190  34.152 1.00 79.43  ? 1   NAG s N2  1 
HETATM 8096 O  O3  . NAG H  6  .   ? -14.714 19.879  35.912 1.00 89.34  ? 1   NAG s O3  1 
HETATM 8097 O  O4  . NAG H  6  .   ? -14.102 22.505  34.745 1.00 75.59  ? 1   NAG s O4  1 
HETATM 8098 O  O5  . NAG H  6  .   ? -13.993 20.169  31.933 1.00 82.22  ? 1   NAG s O5  1 
HETATM 8099 O  O6  . NAG H  6  .   ? -11.655 21.897  32.208 1.00 77.10  ? 1   NAG s O6  1 
HETATM 8100 O  O7  . NAG H  6  .   ? -18.028 19.595  33.994 1.00 85.89  ? 1   NAG s O7  1 
HETATM 8101 C  C1  . NAG H  6  .   ? -12.993 23.185  35.251 1.00 76.58  ? 2   NAG s C1  1 
HETATM 8102 C  C2  . NAG H  6  .   ? -13.201 24.698  35.191 1.00 73.94  ? 2   NAG s C2  1 
HETATM 8103 C  C3  . NAG H  6  .   ? -11.951 25.383  35.740 1.00 77.00  ? 2   NAG s C3  1 
HETATM 8104 C  C4  . NAG H  6  .   ? -11.648 24.887  37.154 1.00 73.75  ? 2   NAG s C4  1 
HETATM 8105 C  C5  . NAG H  6  .   ? -11.515 23.367  37.117 1.00 70.13  ? 2   NAG s C5  1 
HETATM 8106 C  C6  . NAG H  6  .   ? -11.259 22.756  38.479 1.00 69.52  ? 2   NAG s C6  1 
HETATM 8107 C  C7  . NAG H  6  .   ? -14.816 25.536  33.535 1.00 78.78  ? 2   NAG s C7  1 
HETATM 8108 C  C8  . NAG H  6  .   ? -15.004 26.240  32.222 1.00 74.92  ? 2   NAG s C8  1 
HETATM 8109 N  N2  . NAG H  6  .   ? -13.550 25.276  33.904 1.00 71.05  ? 2   NAG s N2  1 
HETATM 8110 O  O3  . NAG H  6  .   ? -12.155 26.792  35.699 1.00 76.56  ? 2   NAG s O3  1 
HETATM 8111 O  O4  . NAG H  6  .   ? -10.414 25.441  37.651 1.00 79.38  ? 2   NAG s O4  1 
HETATM 8112 O  O5  . NAG H  6  .   ? -12.747 22.806  36.609 1.00 70.29  ? 2   NAG s O5  1 
HETATM 8113 O  O6  . NAG H  6  .   ? -12.369 22.987  39.347 1.00 71.82  ? 2   NAG s O6  1 
HETATM 8114 O  O7  . NAG H  6  .   ? -15.778 25.205  34.227 1.00 68.81  ? 2   NAG s O7  1 
HETATM 8115 C  C1  . BMA H  6  .   ? -10.377 26.706  38.247 1.00 86.18  ? 3   BMA s C1  1 
HETATM 8116 C  C2  . BMA H  6  .   ? -8.988  26.874  38.874 1.00 83.80  ? 3   BMA s C2  1 
HETATM 8117 C  C3  . BMA H  6  .   ? -8.774  28.296  39.415 1.00 84.12  ? 3   BMA s C3  1 
HETATM 8118 C  C4  . BMA H  6  .   ? -9.064  29.307  38.307 1.00 83.17  ? 3   BMA s C4  1 
HETATM 8119 C  C5  . BMA H  6  .   ? -10.491 29.122  37.774 1.00 85.52  ? 3   BMA s C5  1 
HETATM 8120 C  C6  . BMA H  6  .   ? -10.797 30.086  36.629 1.00 87.17  ? 3   BMA s C6  1 
HETATM 8121 O  O2  . BMA H  6  .   ? -7.962  26.539  37.933 1.00 73.32  ? 3   BMA s O2  1 
HETATM 8122 O  O3  . BMA H  6  .   ? -7.423  28.477  39.912 1.00 74.76  ? 3   BMA s O3  1 
HETATM 8123 O  O4  . BMA H  6  .   ? -8.933  30.631  38.813 1.00 85.40  ? 3   BMA s O4  1 
HETATM 8124 O  O5  . BMA H  6  .   ? -10.650 27.740  37.289 1.00 77.31  ? 3   BMA s O5  1 
HETATM 8125 O  O6  . BMA H  6  .   ? -12.144 29.966  36.124 1.00 81.28  ? 3   BMA s O6  1 
HETATM 8126 C  C1  . MAN H  6  .   ? -7.149  27.984  41.190 1.00 78.05  ? 4   MAN s C1  1 
HETATM 8127 C  C2  . MAN H  6  .   ? -6.031  28.860  41.749 1.00 78.49  ? 4   MAN s C2  1 
HETATM 8128 C  C3  . MAN H  6  .   ? -4.719  28.649  40.978 1.00 75.74  ? 4   MAN s C3  1 
HETATM 8129 C  C4  . MAN H  6  .   ? -4.339  27.164  41.032 1.00 75.55  ? 4   MAN s C4  1 
HETATM 8130 C  C5  . MAN H  6  .   ? -5.491  26.313  40.482 1.00 75.71  ? 4   MAN s C5  1 
HETATM 8131 C  C6  . MAN H  6  .   ? -5.221  24.829  40.647 1.00 75.25  ? 4   MAN s C6  1 
HETATM 8132 O  O2  . MAN H  6  .   ? -5.870  28.585  43.144 1.00 76.75  ? 4   MAN s O2  1 
HETATM 8133 O  O3  . MAN H  6  .   ? -3.677  29.468  41.536 1.00 71.82  ? 4   MAN s O3  1 
HETATM 8134 O  O4  . MAN H  6  .   ? -3.139  26.884  40.282 1.00 72.02  ? 4   MAN s O4  1 
HETATM 8135 O  O5  . MAN H  6  .   ? -6.747  26.607  41.197 1.00 79.87  ? 4   MAN s O5  1 
HETATM 8136 O  O6  . MAN H  6  .   ? -4.853  24.502  41.998 1.00 62.13  ? 4   MAN s O6  1 
HETATM 8137 C  C1  . NAG I  4  .   ? -17.752 28.218  8.284  1.00 84.73  ? 1   NAG t C1  1 
HETATM 8138 C  C2  . NAG I  4  .   ? -17.095 28.859  7.066  1.00 83.55  ? 1   NAG t C2  1 
HETATM 8139 C  C3  . NAG I  4  .   ? -17.291 30.373  7.092  1.00 86.12  ? 1   NAG t C3  1 
HETATM 8140 C  C4  . NAG I  4  .   ? -18.754 30.757  7.295  1.00 87.62  ? 1   NAG t C4  1 
HETATM 8141 C  C5  . NAG I  4  .   ? -19.324 30.017  8.507  1.00 90.31  ? 1   NAG t C5  1 
HETATM 8142 C  C6  . NAG I  4  .   ? -20.813 30.225  8.685  1.00 90.31  ? 1   NAG t C6  1 
HETATM 8143 C  C7  . NAG I  4  .   ? -15.148 27.718  6.067  1.00 82.19  ? 1   NAG t C7  1 
HETATM 8144 C  C8  . NAG I  4  .   ? -13.651 27.627  6.043  1.00 82.10  ? 1   NAG t C8  1 
HETATM 8145 N  N2  . NAG I  4  .   ? -15.679 28.563  6.958  1.00 79.59  ? 1   NAG t N2  1 
HETATM 8146 O  O3  . NAG I  4  .   ? -16.795 30.881  5.859  1.00 79.03  ? 1   NAG t O3  1 
HETATM 8147 O  O4  . NAG I  4  .   ? -18.835 32.192  7.465  1.00 84.77  ? 1   NAG t O4  1 
HETATM 8148 O  O5  . NAG I  4  .   ? -19.128 28.594  8.352  1.00 83.99  ? 1   NAG t O5  1 
HETATM 8149 O  O6  . NAG I  4  .   ? -21.553 29.498  7.706  1.00 89.34  ? 1   NAG t O6  1 
HETATM 8150 O  O7  . NAG I  4  .   ? -15.843 27.034  5.325  1.00 78.09  ? 1   NAG t O7  1 
HETATM 8151 C  C1  . NAG I  4  .   ? -19.138 32.955  6.327  1.00 90.88  ? 2   NAG t C1  1 
HETATM 8152 C  C2  . NAG I  4  .   ? -19.899 34.244  6.653  1.00 80.33  ? 2   NAG t C2  1 
HETATM 8153 C  C3  . NAG I  4  .   ? -20.179 35.022  5.362  1.00 77.71  ? 2   NAG t C3  1 
HETATM 8154 C  C4  . NAG I  4  .   ? -18.884 35.253  4.583  1.00 87.29  ? 2   NAG t C4  1 
HETATM 8155 C  C5  . NAG I  4  .   ? -18.234 33.897  4.314  1.00 92.08  ? 2   NAG t C5  1 
HETATM 8156 C  C6  . NAG I  4  .   ? -16.942 34.001  3.515  1.00 91.53  ? 2   NAG t C6  1 
HETATM 8157 C  C7  . NAG I  4  .   ? -21.239 34.173  8.702  1.00 75.79  ? 2   NAG t C7  1 
HETATM 8158 C  C8  . NAG I  4  .   ? -22.566 33.832  9.321  1.00 66.40  ? 2   NAG t C8  1 
HETATM 8159 N  N2  . NAG I  4  .   ? -21.132 33.994  7.380  1.00 78.81  ? 2   NAG t N2  1 
HETATM 8160 O  O3  . NAG I  4  .   ? -20.826 36.255  5.645  1.00 72.02  ? 2   NAG t O3  1 
HETATM 8161 O  O4  . NAG I  4  .   ? -19.127 35.915  3.339  1.00 80.15  ? 2   NAG t O4  1 
HETATM 8162 O  O5  . NAG I  4  .   ? -17.948 33.292  5.600  1.00 91.02  ? 2   NAG t O5  1 
HETATM 8163 O  O6  . NAG I  4  .   ? -16.263 32.735  3.384  1.00 89.23  ? 2   NAG t O6  1 
HETATM 8164 O  O7  . NAG I  4  .   ? -20.294 34.598  9.366  1.00 72.44  ? 2   NAG t O7  1 
HETATM 8165 C  C1  . GOL J  7  .   ? 27.705  7.571   17.749 1.00 72.78  ? 401 GOL A C1  1 
HETATM 8166 O  O1  . GOL J  7  .   ? 29.010  6.993   17.712 1.00 75.64  ? 401 GOL A O1  1 
HETATM 8167 C  C2  . GOL J  7  .   ? 27.395  8.130   19.119 1.00 63.34  ? 401 GOL A C2  1 
HETATM 8168 O  O2  . GOL J  7  .   ? 28.255  9.227   19.402 1.00 66.77  ? 401 GOL A O2  1 
HETATM 8169 C  C3  . GOL J  7  .   ? 25.977  8.593   19.309 1.00 58.96  ? 401 GOL A C3  1 
HETATM 8170 O  O3  . GOL J  7  .   ? 25.706  8.724   20.700 1.00 63.70  ? 401 GOL A O3  1 
HETATM 8171 C  C1  . GOL K  7  .   ? 21.811  -1.348  36.269 1.00 65.60  ? 402 GOL A C1  1 
HETATM 8172 O  O1  . GOL K  7  .   ? 21.675  -1.133  37.672 1.00 55.93  ? 402 GOL A O1  1 
HETATM 8173 C  C2  . GOL K  7  .   ? 21.453  -0.097  35.494 1.00 70.57  ? 402 GOL A C2  1 
HETATM 8174 O  O2  . GOL K  7  .   ? 22.300  0.982   35.909 1.00 55.55  ? 402 GOL A O2  1 
HETATM 8175 C  C3  . GOL K  7  .   ? 21.505  -0.282  33.987 1.00 73.50  ? 402 GOL A C3  1 
HETATM 8176 O  O3  . GOL K  7  .   ? 20.721  -1.387  33.531 1.00 71.89  ? 402 GOL A O3  1 
HETATM 8177 C  C1  . GOL L  7  .   ? 45.108  -12.488 48.675 1.00 47.32  ? 403 GOL A C1  1 
HETATM 8178 O  O1  . GOL L  7  .   ? 44.637  -11.962 47.437 1.00 40.87  ? 403 GOL A O1  1 
HETATM 8179 C  C2  . GOL L  7  .   ? 44.174  -13.515 49.315 1.00 53.90  ? 403 GOL A C2  1 
HETATM 8180 O  O2  . GOL L  7  .   ? 42.917  -12.948 49.710 1.00 43.95  ? 403 GOL A O2  1 
HETATM 8181 C  C3  . GOL L  7  .   ? 43.893  -14.735 48.459 1.00 51.79  ? 403 GOL A C3  1 
HETATM 8182 O  O3  . GOL L  7  .   ? 43.016  -15.619 49.165 1.00 52.90  ? 403 GOL A O3  1 
HETATM 8183 N  N1  . EPE M  8  .   ? 60.426  1.833   19.267 0.70 52.15  ? 404 EPE A N1  1 
HETATM 8184 C  C2  . EPE M  8  .   ? 60.867  0.830   18.274 0.70 58.02  ? 404 EPE A C2  1 
HETATM 8185 C  C3  . EPE M  8  .   ? 60.079  -0.458  18.375 0.70 57.52  ? 404 EPE A C3  1 
HETATM 8186 N  N4  . EPE M  8  .   ? 60.170  -1.041  19.729 0.70 55.64  ? 404 EPE A N4  1 
HETATM 8187 C  C5  . EPE M  8  .   ? 59.713  -0.029  20.682 0.70 48.96  ? 404 EPE A C5  1 
HETATM 8188 C  C6  . EPE M  8  .   ? 60.529  1.235   20.597 0.70 47.29  ? 404 EPE A C6  1 
HETATM 8189 C  C7  . EPE M  8  .   ? 59.353  -2.264  19.851 0.70 57.23  ? 404 EPE A C7  1 
HETATM 8190 C  C8  . EPE M  8  .   ? 57.855  -2.024  20.004 0.70 58.14  ? 404 EPE A C8  1 
HETATM 8191 O  O8  . EPE M  8  .   ? 57.079  -3.193  20.184 0.70 55.86  ? 404 EPE A O8  1 
HETATM 8192 C  C9  . EPE M  8  .   ? 61.227  3.083   19.190 0.70 54.07  ? 404 EPE A C9  1 
HETATM 8193 C  C10 . EPE M  8  .   ? 61.464  3.624   17.783 0.70 52.43  ? 404 EPE A C10 1 
HETATM 8194 S  S   . EPE M  8  .   ? 62.162  5.249   17.866 0.70 55.61  ? 404 EPE A S   1 
HETATM 8195 O  O1S . EPE M  8  .   ? 63.586  5.070   17.975 0.70 59.95  ? 404 EPE A O1S 1 
HETATM 8196 O  O2S . EPE M  8  .   ? 61.495  5.908   18.958 0.70 47.52  ? 404 EPE A O2S 1 
HETATM 8197 O  O3S . EPE M  8  .   ? 61.856  5.872   16.451 0.70 45.42  ? 404 EPE A O3S 1 
HETATM 8198 N  N1  . EPE N  8  .   ? 34.523  -24.830 39.903 1.00 73.64  ? 405 EPE A N1  1 
HETATM 8199 C  C2  . EPE N  8  .   ? 34.954  -23.999 41.054 1.00 71.30  ? 405 EPE A C2  1 
HETATM 8200 C  C3  . EPE N  8  .   ? 34.668  -24.664 42.384 1.00 67.04  ? 405 EPE A C3  1 
HETATM 8201 N  N4  . EPE N  8  .   ? 33.412  -25.451 42.339 1.00 66.37  ? 405 EPE A N4  1 
HETATM 8202 C  C5  . EPE N  8  .   ? 33.523  -26.558 41.355 1.00 75.65  ? 405 EPE A C5  1 
HETATM 8203 C  C6  . EPE N  8  .   ? 34.560  -26.261 40.290 1.00 80.66  ? 405 EPE A C6  1 
HETATM 8204 C  C7  . EPE N  8  .   ? 32.233  -24.605 42.115 1.00 56.12  ? 405 EPE A C7  1 
HETATM 8205 C  C8  . EPE N  8  .   ? 31.727  -23.953 43.394 1.00 60.75  ? 405 EPE A C8  1 
HETATM 8206 O  O8  . EPE N  8  .   ? 30.471  -23.310 43.177 1.00 59.57  ? 405 EPE A O8  1 
HETATM 8207 C  C9  . EPE N  8  .   ? 35.327  -24.563 38.690 1.00 67.28  ? 405 EPE A C9  1 
HETATM 8208 C  C10 . EPE N  8  .   ? 34.475  -24.142 37.485 1.00 69.58  ? 405 EPE A C10 1 
HETATM 8209 S  S   . EPE N  8  .   ? 33.855  -25.502 36.527 1.00 74.57  ? 405 EPE A S   1 
HETATM 8210 O  O1S . EPE N  8  .   ? 32.493  -25.655 37.002 1.00 63.70  ? 405 EPE A O1S 1 
HETATM 8211 O  O2S . EPE N  8  .   ? 34.861  -26.541 36.649 1.00 69.20  ? 405 EPE A O2S 1 
HETATM 8212 O  O3S . EPE N  8  .   ? 33.823  -25.129 34.948 1.00 50.88  ? 405 EPE A O3S 1 
HETATM 8213 N  N1  . EPE O  8  .   ? 27.340  -21.871 30.634 1.00 68.84  ? 406 EPE A N1  1 
HETATM 8214 C  C2  . EPE O  8  .   ? 27.620  -22.543 31.927 1.00 70.07  ? 406 EPE A C2  1 
HETATM 8215 C  C3  . EPE O  8  .   ? 28.167  -21.568 32.951 1.00 71.11  ? 406 EPE A C3  1 
HETATM 8216 N  N4  . EPE O  8  .   ? 27.157  -20.540 33.339 1.00 64.08  ? 406 EPE A N4  1 
HETATM 8217 C  C5  . EPE O  8  .   ? 26.379  -20.153 32.133 1.00 65.88  ? 406 EPE A C5  1 
HETATM 8218 C  C6  . EPE O  8  .   ? 27.162  -20.410 30.863 1.00 67.30  ? 406 EPE A C6  1 
HETATM 8219 C  C7  . EPE O  8  .   ? 27.816  -19.385 33.972 1.00 65.63  ? 406 EPE A C7  1 
HETATM 8220 C  C8  . EPE O  8  .   ? 26.982  -18.126 34.098 1.00 65.72  ? 406 EPE A C8  1 
HETATM 8221 O  O8  . EPE O  8  .   ? 27.767  -17.093 34.657 1.00 63.22  ? 406 EPE A O8  1 
HETATM 8222 C  C9  . EPE O  8  .   ? 28.405  -22.143 29.634 1.00 67.69  ? 406 EPE A C9  1 
HETATM 8223 C  C10 . EPE O  8  .   ? 28.212  -21.399 28.309 1.00 63.89  ? 406 EPE A C10 1 
HETATM 8224 S  S   . EPE O  8  .   ? 29.544  -21.699 27.163 1.00 71.37  ? 406 EPE A S   1 
HETATM 8225 O  O1S . EPE O  8  .   ? 29.880  -20.387 26.638 1.00 64.92  ? 406 EPE A O1S 1 
HETATM 8226 O  O2S . EPE O  8  .   ? 29.087  -22.711 26.234 1.00 68.53  ? 406 EPE A O2S 1 
HETATM 8227 O  O3S . EPE O  8  .   ? 30.695  -22.360 28.076 1.00 63.43  ? 406 EPE A O3S 1 
HETATM 8228 C  C1  . GOL P  7  .   ? 40.604  13.964  45.293 1.00 64.54  ? 407 GOL A C1  1 
HETATM 8229 O  O1  . GOL P  7  .   ? 39.537  13.183  45.837 1.00 66.96  ? 407 GOL A O1  1 
HETATM 8230 C  C2  . GOL P  7  .   ? 41.951  13.283  45.475 1.00 60.63  ? 407 GOL A C2  1 
HETATM 8231 O  O2  . GOL P  7  .   ? 41.907  11.980  44.899 1.00 55.09  ? 407 GOL A O2  1 
HETATM 8232 C  C3  . GOL P  7  .   ? 42.410  13.142  46.914 1.00 59.45  ? 407 GOL A C3  1 
HETATM 8233 O  O3  . GOL P  7  .   ? 43.823  12.915  46.986 1.00 51.29  ? 407 GOL A O3  1 
HETATM 8234 N  N1  . EPE Q  8  .   ? 41.351  -7.219  55.807 1.00 65.24  ? 408 EPE A N1  1 
HETATM 8235 C  C2  . EPE Q  8  .   ? 41.366  -8.352  54.838 1.00 67.05  ? 408 EPE A C2  1 
HETATM 8236 C  C3  . EPE Q  8  .   ? 40.007  -9.003  54.691 1.00 64.52  ? 408 EPE A C3  1 
HETATM 8237 N  N4  . EPE Q  8  .   ? 39.498  -9.480  55.994 1.00 63.73  ? 408 EPE A N4  1 
HETATM 8238 C  C5  . EPE Q  8  .   ? 39.379  -8.315  56.890 1.00 66.38  ? 408 EPE A C5  1 
HETATM 8239 C  C6  . EPE Q  8  .   ? 40.720  -7.652  57.087 1.00 63.80  ? 408 EPE A C6  1 
HETATM 8240 C  C7  . EPE Q  8  .   ? 38.189  -10.137 55.884 1.00 61.89  ? 408 EPE A C7  1 
HETATM 8241 C  C8  . EPE Q  8  .   ? 38.078  -11.225 54.843 1.00 61.10  ? 408 EPE A C8  1 
HETATM 8242 O  O8  . EPE Q  8  .   ? 36.893  -11.947 55.122 1.00 62.44  ? 408 EPE A O8  1 
HETATM 8243 C  C9  . EPE Q  8  .   ? 42.760  -6.783  56.070 1.00 70.28  ? 408 EPE A C9  1 
HETATM 8244 C  C10 . EPE Q  8  .   ? 43.090  -5.328  55.800 1.00 62.77  ? 408 EPE A C10 1 
HETATM 8245 S  S   . EPE Q  8  .   ? 41.971  -4.243  56.626 1.00 63.57  ? 408 EPE A S   1 
HETATM 8246 O  O1S . EPE Q  8  .   ? 42.352  -4.246  58.022 1.00 71.21  ? 408 EPE A O1S 1 
HETATM 8247 O  O2S . EPE Q  8  .   ? 40.659  -4.744  56.294 1.00 67.83  ? 408 EPE A O2S 1 
HETATM 8248 O  O3S . EPE Q  8  .   ? 42.307  -2.801  55.987 1.00 47.99  ? 408 EPE A O3S 1 
HETATM 8249 C  CHA . HEM R  9  .   ? 41.197  1.421   35.115 1.00 30.24  ? 409 HEM A CHA 1 
HETATM 8250 C  CHB . HEM R  9  .   ? 45.259  0.667   37.652 1.00 31.59  ? 409 HEM A CHB 1 
HETATM 8251 C  CHC . HEM R  9  .   ? 44.361  -4.163  37.583 1.00 33.20  ? 409 HEM A CHC 1 
HETATM 8252 C  CHD . HEM R  9  .   ? 40.201  -3.304  35.216 1.00 33.36  ? 409 HEM A CHD 1 
HETATM 8253 C  C1A . HEM R  9  .   ? 42.355  1.594   35.858 1.00 31.51  ? 409 HEM A C1A 1 
HETATM 8254 C  C2A . HEM R  9  .   ? 42.881  2.856   36.172 1.00 32.32  ? 409 HEM A C2A 1 
HETATM 8255 C  C3A . HEM R  9  .   ? 44.024  2.641   36.882 1.00 34.96  ? 409 HEM A C3A 1 
HETATM 8256 C  C4A . HEM R  9  .   ? 44.225  1.260   36.991 1.00 32.16  ? 409 HEM A C4A 1 
HETATM 8257 C  CMA . HEM R  9  .   ? 44.942  3.692   37.447 1.00 36.52  ? 409 HEM A CMA 1 
HETATM 8258 C  CAA . HEM R  9  .   ? 42.294  4.180   35.795 1.00 33.51  ? 409 HEM A CAA 1 
HETATM 8259 C  CBA . HEM R  9  .   ? 42.757  4.603   34.375 1.00 35.14  ? 409 HEM A CBA 1 
HETATM 8260 C  CGA . HEM R  9  .   ? 41.662  5.517   33.856 1.00 44.00  ? 409 HEM A CGA 1 
HETATM 8261 O  O1A . HEM R  9  .   ? 41.838  6.774   34.004 1.00 40.13  ? 409 HEM A O1A 1 
HETATM 8262 O  O2A . HEM R  9  .   ? 40.529  5.033   33.353 1.00 45.52  ? 409 HEM A O2A 1 
HETATM 8263 C  C1B . HEM R  9  .   ? 45.333  -0.733  37.796 1.00 35.21  ? 409 HEM A C1B 1 
HETATM 8264 C  C2B . HEM R  9  .   ? 46.449  -1.355  38.409 1.00 34.60  ? 409 HEM A C2B 1 
HETATM 8265 C  C3B . HEM R  9  .   ? 46.210  -2.691  38.446 1.00 34.51  ? 409 HEM A C3B 1 
HETATM 8266 C  C4B . HEM R  9  .   ? 44.930  -2.908  37.755 1.00 35.00  ? 409 HEM A C4B 1 
HETATM 8267 C  CMB . HEM R  9  .   ? 47.656  -0.679  39.035 1.00 34.59  ? 409 HEM A CMB 1 
HETATM 8268 C  CAB . HEM R  9  .   ? 47.201  -3.655  38.934 1.00 38.53  ? 409 HEM A CAB 1 
HETATM 8269 C  CBB . HEM R  9  .   ? 47.318  -4.858  38.384 1.00 42.19  ? 409 HEM A CBB 1 
HETATM 8270 C  C1C . HEM R  9  .   ? 43.140  -4.357  36.961 1.00 34.60  ? 409 HEM A C1C 1 
HETATM 8271 C  C2C . HEM R  9  .   ? 42.461  -5.589  36.855 1.00 36.04  ? 409 HEM A C2C 1 
HETATM 8272 C  C3C . HEM R  9  .   ? 41.289  -5.325  36.137 1.00 34.51  ? 409 HEM A C3C 1 
HETATM 8273 C  C4C . HEM R  9  .   ? 41.231  -3.928  35.900 1.00 34.41  ? 409 HEM A C4C 1 
HETATM 8274 C  CMC . HEM R  9  .   ? 42.968  -6.936  37.352 1.00 34.04  ? 409 HEM A CMC 1 
HETATM 8275 C  CAC . HEM R  9  .   ? 40.172  -6.215  35.803 1.00 36.54  ? 409 HEM A CAC 1 
HETATM 8276 C  CBC . HEM R  9  .   ? 39.924  -7.298  36.541 1.00 39.62  ? 409 HEM A CBC 1 
HETATM 8277 C  C1D . HEM R  9  .   ? 40.184  -1.936  34.986 1.00 31.55  ? 409 HEM A C1D 1 
HETATM 8278 C  C2D . HEM R  9  .   ? 39.163  -1.314  34.148 1.00 32.48  ? 409 HEM A C2D 1 
HETATM 8279 C  C3D . HEM R  9  .   ? 39.431  0.025   34.125 1.00 31.87  ? 409 HEM A C3D 1 
HETATM 8280 C  C4D . HEM R  9  .   ? 40.641  0.180   34.919 1.00 29.77  ? 409 HEM A C4D 1 
HETATM 8281 C  CMD . HEM R  9  .   ? 37.998  -2.001  33.439 1.00 34.35  ? 409 HEM A CMD 1 
HETATM 8282 C  CAD . HEM R  9  .   ? 38.647  1.099   33.367 1.00 32.20  ? 409 HEM A CAD 1 
HETATM 8283 C  CBD . HEM R  9  .   ? 37.534  1.775   34.202 1.00 33.73  ? 409 HEM A CBD 1 
HETATM 8284 C  CGD . HEM R  9  .   ? 36.633  2.660   33.340 1.00 34.67  ? 409 HEM A CGD 1 
HETATM 8285 O  O1D . HEM R  9  .   ? 35.434  2.939   33.676 1.00 34.12  ? 409 HEM A O1D 1 
HETATM 8286 O  O2D . HEM R  9  .   ? 37.048  3.079   32.229 1.00 36.96  ? 409 HEM A O2D 1 
HETATM 8287 N  NA  . HEM R  9  .   ? 43.187  0.615   36.384 1.00 31.09  ? 409 HEM A NA  1 
HETATM 8288 N  NB  . HEM R  9  .   ? 44.448  -1.683  37.431 1.00 33.62  ? 409 HEM A NB  1 
HETATM 8289 N  NC  . HEM R  9  .   ? 42.385  -3.371  36.405 1.00 32.05  ? 409 HEM A NC  1 
HETATM 8290 N  ND  . HEM R  9  .   ? 41.053  -1.007  35.447 1.00 31.56  ? 409 HEM A ND  1 
HETATM 8291 FE FE  . HEM R  9  .   ? 42.632  -1.302  36.514 1.00 31.65  ? 409 HEM A FE  1 
HETATM 8292 MG MG  . MG  S  10 .   ? 40.232  7.995   33.586 1.00 44.08  ? 410 MG  A MG  1 
HETATM 8293 S  S   . SO4 T  11 .   ? 49.399  18.269  23.001 1.00 90.02  ? 411 SO4 A S   1 
HETATM 8294 O  O1  . SO4 T  11 .   ? 50.015  17.500  21.899 1.00 66.04  ? 411 SO4 A O1  1 
HETATM 8295 O  O2  . SO4 T  11 .   ? 48.994  19.601  22.549 1.00 78.77  ? 411 SO4 A O2  1 
HETATM 8296 O  O3  . SO4 T  11 .   ? 48.222  17.558  23.464 1.00 80.36  ? 411 SO4 A O3  1 
HETATM 8297 O  O4  . SO4 T  11 .   ? 50.347  18.408  24.110 1.00 73.79  ? 411 SO4 A O4  1 
HETATM 8298 S  S   . SO4 U  11 .   ? 27.286  -13.106 31.849 1.00 89.62  ? 412 SO4 A S   1 
HETATM 8299 O  O1  . SO4 U  11 .   ? 28.370  -14.049 32.109 1.00 71.22  ? 412 SO4 A O1  1 
HETATM 8300 O  O2  . SO4 U  11 .   ? 26.909  -13.151 30.418 1.00 63.40  ? 412 SO4 A O2  1 
HETATM 8301 O  O3  . SO4 U  11 .   ? 26.109  -13.494 32.637 1.00 69.61  ? 412 SO4 A O3  1 
HETATM 8302 O  O4  . SO4 U  11 .   ? 27.753  -11.748 32.245 1.00 43.66  ? 412 SO4 A O4  1 
HETATM 8303 S  S   . SO4 V  11 .   ? 29.487  1.046   50.303 1.00 74.48  ? 413 SO4 A S   1 
HETATM 8304 O  O1  . SO4 V  11 .   ? 30.377  0.233   49.437 1.00 57.50  ? 413 SO4 A O1  1 
HETATM 8305 O  O2  . SO4 V  11 .   ? 29.261  2.363   49.684 1.00 72.09  ? 413 SO4 A O2  1 
HETATM 8306 O  O3  . SO4 V  11 .   ? 28.212  0.381   50.490 1.00 68.12  ? 413 SO4 A O3  1 
HETATM 8307 O  O4  . SO4 V  11 .   ? 30.085  1.210   51.615 1.00 66.13  ? 413 SO4 A O4  1 
HETATM 8308 S  S   . SO4 W  11 .   ? 32.938  3.189   60.182 1.00 82.99  ? 414 SO4 A S   1 
HETATM 8309 O  O1  . SO4 W  11 .   ? 34.391  3.138   60.172 1.00 73.01  ? 414 SO4 A O1  1 
HETATM 8310 O  O2  . SO4 W  11 .   ? 32.438  3.903   59.007 1.00 61.74  ? 414 SO4 A O2  1 
HETATM 8311 O  O3  . SO4 W  11 .   ? 32.409  1.818   60.178 1.00 72.86  ? 414 SO4 A O3  1 
HETATM 8312 O  O4  . SO4 W  11 .   ? 32.515  3.885   61.402 1.00 75.95  ? 414 SO4 A O4  1 
HETATM 8313 C  C1  . GOL X  7  .   ? 24.626  -25.561 69.411 1.00 75.64  ? 401 GOL B C1  1 
HETATM 8314 O  O1  . GOL X  7  .   ? 24.242  -24.194 69.259 1.00 68.50  ? 401 GOL B O1  1 
HETATM 8315 C  C2  . GOL X  7  .   ? 23.660  -26.337 70.285 1.00 71.77  ? 401 GOL B C2  1 
HETATM 8316 O  O2  . GOL X  7  .   ? 22.509  -25.541 70.540 1.00 74.70  ? 401 GOL B O2  1 
HETATM 8317 C  C3  . GOL X  7  .   ? 23.210  -27.654 69.692 1.00 71.56  ? 401 GOL B C3  1 
HETATM 8318 O  O3  . GOL X  7  .   ? 21.907  -28.017 70.145 1.00 70.74  ? 401 GOL B O3  1 
HETATM 8319 C  C1  . GOL Y  7  .   ? 29.159  -14.580 55.493 1.00 55.68  ? 402 GOL B C1  1 
HETATM 8320 O  O1  . GOL Y  7  .   ? 28.696  -15.311 56.624 1.00 43.32  ? 402 GOL B O1  1 
HETATM 8321 C  C2  . GOL Y  7  .   ? 28.430  -14.955 54.221 1.00 53.52  ? 402 GOL B C2  1 
HETATM 8322 O  O2  . GOL Y  7  .   ? 28.969  -14.186 53.140 1.00 47.34  ? 402 GOL B O2  1 
HETATM 8323 C  C3  . GOL Y  7  .   ? 28.519  -16.441 53.919 1.00 58.35  ? 402 GOL B C3  1 
HETATM 8324 O  O3  . GOL Y  7  .   ? 27.799  -16.821 52.741 1.00 54.45  ? 402 GOL B O3  1 
HETATM 8325 C  C1  . GOL Z  7  .   ? 11.058  -11.281 34.151 1.00 51.17  ? 403 GOL B C1  1 
HETATM 8326 O  O1  . GOL Z  7  .   ? 9.781   -10.764 34.533 1.00 42.80  ? 403 GOL B O1  1 
HETATM 8327 C  C2  . GOL Z  7  .   ? 10.988  -12.692 33.592 1.00 56.53  ? 403 GOL B C2  1 
HETATM 8328 O  O2  . GOL Z  7  .   ? 12.316  -13.238 33.547 1.00 51.00  ? 403 GOL B O2  1 
HETATM 8329 C  C3  . GOL Z  7  .   ? 10.044  -13.608 34.362 1.00 60.08  ? 403 GOL B C3  1 
HETATM 8330 O  O3  . GOL Z  7  .   ? 10.199  -14.986 33.994 1.00 65.15  ? 403 GOL B O3  1 
HETATM 8331 N  N1  . EPE AA 8  .   ? -10.490 -16.031 70.518 1.00 59.85  ? 404 EPE B N1  1 
HETATM 8332 C  C2  . EPE AA 8  .   ? -10.044 -17.434 70.511 1.00 59.27  ? 404 EPE B C2  1 
HETATM 8333 C  C3  . EPE AA 8  .   ? -9.694  -17.885 69.120 1.00 59.61  ? 404 EPE B C3  1 
HETATM 8334 N  N4  . EPE AA 8  .   ? -10.886 -17.921 68.280 1.00 65.18  ? 404 EPE B N4  1 
HETATM 8335 C  C5  . EPE AA 8  .   ? -11.488 -16.565 68.268 1.00 67.88  ? 404 EPE B C5  1 
HETATM 8336 C  C6  . EPE AA 8  .   ? -11.702 -15.974 69.656 1.00 70.22  ? 404 EPE B C6  1 
HETATM 8337 C  C7  . EPE AA 8  .   ? -10.510 -18.396 66.933 1.00 68.09  ? 404 EPE B C7  1 
HETATM 8338 C  C8  . EPE AA 8  .   ? -9.195  -17.823 66.361 1.00 66.45  ? 404 EPE B C8  1 
HETATM 8339 O  O8  . EPE AA 8  .   ? -8.097  -18.743 66.320 1.00 55.28  ? 404 EPE B O8  1 
HETATM 8340 C  C9  . EPE AA 8  .   ? -10.803 -15.629 71.936 1.00 64.28  ? 404 EPE B C9  1 
HETATM 8341 C  C10 . EPE AA 8  .   ? -10.228 -16.632 72.971 1.00 59.23  ? 404 EPE B C10 1 
HETATM 8342 S  S   . EPE AA 8  .   ? -10.719 -16.426 74.668 1.00 67.31  ? 404 EPE B S   1 
HETATM 8343 O  O1S . EPE AA 8  .   ? -10.129 -15.164 75.070 1.00 60.35  ? 404 EPE B O1S 1 
HETATM 8344 O  O2S . EPE AA 8  .   ? -10.396 -17.639 75.388 1.00 59.45  ? 404 EPE B O2S 1 
HETATM 8345 O  O3S . EPE AA 8  .   ? -12.322 -16.463 74.629 1.00 54.08  ? 404 EPE B O3S 1 
HETATM 8346 N  N1  . EPE BA 8  .   ? 8.102   2.336   43.588 1.00 57.60  ? 405 EPE B N1  1 
HETATM 8347 C  C2  . EPE BA 8  .   ? 8.873   1.664   42.544 1.00 56.91  ? 405 EPE B C2  1 
HETATM 8348 C  C3  . EPE BA 8  .   ? 7.968   0.743   41.767 1.00 62.10  ? 405 EPE B C3  1 
HETATM 8349 N  N4  . EPE BA 8  .   ? 7.494   -0.356  42.622 1.00 57.78  ? 405 EPE B N4  1 
HETATM 8350 C  C5  . EPE BA 8  .   ? 6.746   0.237   43.763 1.00 63.32  ? 405 EPE B C5  1 
HETATM 8351 C  C6  . EPE BA 8  .   ? 7.581   1.274   44.494 1.00 67.98  ? 405 EPE B C6  1 
HETATM 8352 C  C7  . EPE BA 8  .   ? 6.653   -1.267  41.821 1.00 58.59  ? 405 EPE B C7  1 
HETATM 8353 C  C8  . EPE BA 8  .   ? 7.251   -1.685  40.463 1.00 57.38  ? 405 EPE B C8  1 
HETATM 8354 O  O8  . EPE BA 8  .   ? 6.820   -2.966  40.003 1.00 60.41  ? 405 EPE B O8  1 
HETATM 8355 C  C9  . EPE BA 8  .   ? 8.950   3.347   44.265 1.00 52.64  ? 405 EPE B C9  1 
HETATM 8356 C  C10 . EPE BA 8  .   ? 8.478   3.808   45.642 1.00 56.12  ? 405 EPE B C10 1 
HETATM 8357 S  S   . EPE BA 8  .   ? 9.233   5.380   45.997 1.00 72.90  ? 405 EPE B S   1 
HETATM 8358 O  O1S . EPE BA 8  .   ? 10.678  5.193   45.985 1.00 62.45  ? 405 EPE B O1S 1 
HETATM 8359 O  O2S . EPE BA 8  .   ? 8.583   5.950   47.162 1.00 61.62  ? 405 EPE B O2S 1 
HETATM 8360 O  O3S . EPE BA 8  .   ? 8.645   6.062   44.646 1.00 57.95  ? 405 EPE B O3S 1 
HETATM 8361 C  C1  . GOL CA 7  .   ? 25.035  -1.729  53.008 1.00 56.19  ? 406 GOL B C1  1 
HETATM 8362 O  O1  . GOL CA 7  .   ? 23.689  -2.132  52.750 1.00 48.35  ? 406 GOL B O1  1 
HETATM 8363 C  C2  . GOL CA 7  .   ? 25.264  -0.315  52.516 1.00 49.53  ? 406 GOL B C2  1 
HETATM 8364 O  O2  . GOL CA 7  .   ? 24.048  0.397   52.697 1.00 49.85  ? 406 GOL B O2  1 
HETATM 8365 C  C3  . GOL CA 7  .   ? 26.347  0.458   53.219 1.00 49.54  ? 406 GOL B C3  1 
HETATM 8366 O  O3  . GOL CA 7  .   ? 26.045  1.849   53.167 1.00 55.08  ? 406 GOL B O3  1 
HETATM 8367 N  N1  . EPE DA 8  .   ? 15.229  7.128   44.130 1.00 63.96  ? 407 EPE B N1  1 
HETATM 8368 C  C2  . EPE DA 8  .   ? 16.482  6.909   43.380 1.00 63.36  ? 407 EPE B C2  1 
HETATM 8369 C  C3  . EPE DA 8  .   ? 16.208  6.186   42.084 1.00 61.91  ? 407 EPE B C3  1 
HETATM 8370 N  N4  . EPE DA 8  .   ? 15.657  4.844   42.353 1.00 57.64  ? 407 EPE B N4  1 
HETATM 8371 C  C5  . EPE DA 8  .   ? 14.392  5.015   43.095 1.00 56.10  ? 407 EPE B C5  1 
HETATM 8372 C  C6  . EPE DA 8  .   ? 14.573  5.818   44.363 1.00 58.76  ? 407 EPE B C6  1 
HETATM 8373 C  C7  . EPE DA 8  .   ? 15.416  4.083   41.114 1.00 59.04  ? 407 EPE B C7  1 
HETATM 8374 C  C8  . EPE DA 8  .   ? 16.507  4.147   40.049 1.00 63.99  ? 407 EPE B C8  1 
HETATM 8375 O  O8  . EPE DA 8  .   ? 16.028  3.657   38.800 1.00 54.53  ? 407 EPE B O8  1 
HETATM 8376 C  C9  . EPE DA 8  .   ? 15.509  7.835   45.434 1.00 63.74  ? 407 EPE B C9  1 
HETATM 8377 C  C10 . EPE DA 8  .   ? 14.296  8.565   46.009 1.00 64.05  ? 407 EPE B C10 1 
HETATM 8378 S  S   . EPE DA 8  .   ? 13.878  7.994   47.643 1.00 67.13  ? 407 EPE B S   1 
HETATM 8379 O  O1S . EPE DA 8  .   ? 12.739  8.768   48.089 1.00 62.31  ? 407 EPE B O1S 1 
HETATM 8380 O  O2S . EPE DA 8  .   ? 15.091  8.075   48.425 1.00 59.05  ? 407 EPE B O2S 1 
HETATM 8381 O  O3S . EPE DA 8  .   ? 13.411  6.536   47.194 1.00 57.12  ? 407 EPE B O3S 1 
HETATM 8382 C  C1  . GOL EA 7  .   ? 14.112  5.319   68.883 1.00 65.35  ? 408 GOL B C1  1 
HETATM 8383 O  O1  . GOL EA 7  .   ? 12.914  4.529   68.759 1.00 61.68  ? 408 GOL B O1  1 
HETATM 8384 C  C2  . GOL EA 7  .   ? 15.258  4.821   68.018 1.00 55.77  ? 408 GOL B C2  1 
HETATM 8385 O  O2  . GOL EA 7  .   ? 16.200  5.876   67.831 1.00 58.75  ? 408 GOL B O2  1 
HETATM 8386 C  C3  . GOL EA 7  .   ? 15.981  3.605   68.568 1.00 57.76  ? 408 GOL B C3  1 
HETATM 8387 O  O3  . GOL EA 7  .   ? 17.115  3.253   67.768 1.00 55.46  ? 408 GOL B O3  1 
HETATM 8388 C  CHA . HEM FA 9  .   ? 11.285  -9.419  61.304 1.00 30.71  ? 409 HEM B CHA 1 
HETATM 8389 C  CHB . HEM FA 9  .   ? 7.920   -6.003  60.564 1.00 34.54  ? 409 HEM B CHB 1 
HETATM 8390 C  CHC . HEM FA 9  .   ? 7.247   -7.668  56.025 1.00 32.56  ? 409 HEM B CHC 1 
HETATM 8391 C  CHD . HEM FA 9  .   ? 10.697  -10.965 56.779 1.00 32.52  ? 409 HEM B CHD 1 
HETATM 8392 C  C1A . HEM FA 9  .   ? 10.453  -8.342  61.430 1.00 31.04  ? 409 HEM B C1A 1 
HETATM 8393 C  C2A . HEM FA 9  .   ? 10.418  -7.519  62.568 1.00 32.20  ? 409 HEM B C2A 1 
HETATM 8394 C  C3A . HEM FA 9  .   ? 9.471   -6.562  62.373 1.00 33.86  ? 409 HEM B C3A 1 
HETATM 8395 C  C4A . HEM FA 9  .   ? 8.897   -6.787  61.114 1.00 34.81  ? 409 HEM B C4A 1 
HETATM 8396 C  CMA . HEM FA 9  .   ? 9.113   -5.438  63.320 1.00 34.85  ? 409 HEM B CMA 1 
HETATM 8397 C  CAA . HEM FA 9  .   ? 11.276  -7.630  63.793 1.00 38.14  ? 409 HEM B CAA 1 
HETATM 8398 C  CBA . HEM FA 9  .   ? 10.738  -8.736  64.713 1.00 39.82  ? 409 HEM B CBA 1 
HETATM 8399 C  CGA . HEM FA 9  .   ? 11.943  -9.353  65.370 1.00 46.01  ? 409 HEM B CGA 1 
HETATM 8400 O  O1A . HEM FA 9  .   ? 12.163  -8.983  66.550 1.00 39.18  ? 409 HEM B O1A 1 
HETATM 8401 O  O2A . HEM FA 9  .   ? 12.733  -10.174 64.726 1.00 48.53  ? 409 HEM B O2A 1 
HETATM 8402 C  C1B . HEM FA 9  .   ? 7.444   -6.219  59.261 1.00 33.08  ? 409 HEM B C1B 1 
HETATM 8403 C  C2B . HEM FA 9  .   ? 6.397   -5.428  58.723 1.00 33.94  ? 409 HEM B C2B 1 
HETATM 8404 C  C3B . HEM FA 9  .   ? 6.176   -5.850  57.461 1.00 33.71  ? 409 HEM B C3B 1 
HETATM 8405 C  C4B . HEM FA 9  .   ? 7.131   -6.977  57.234 1.00 34.29  ? 409 HEM B C4B 1 
HETATM 8406 C  CMB . HEM FA 9  .   ? 5.646   -4.279  59.385 1.00 36.96  ? 409 HEM B CMB 1 
HETATM 8407 C  CAB . HEM FA 9  .   ? 5.106   -5.304  56.611 1.00 35.00  ? 409 HEM B CAB 1 
HETATM 8408 C  CBB . HEM FA 9  .   ? 4.593   -6.000  55.583 1.00 39.19  ? 409 HEM B CBB 1 
HETATM 8409 C  C1C . HEM FA 9  .   ? 8.150   -8.676  55.799 1.00 32.83  ? 409 HEM B C1C 1 
HETATM 8410 C  C2C . HEM FA 9  .   ? 8.328   -9.370  54.583 1.00 32.65  ? 409 HEM B C2C 1 
HETATM 8411 C  C3C . HEM FA 9  .   ? 9.319   -10.333 54.819 1.00 33.03  ? 409 HEM B C3C 1 
HETATM 8412 C  C4C . HEM FA 9  .   ? 9.727   -10.189 56.191 1.00 35.56  ? 409 HEM B C4C 1 
HETATM 8413 C  CMC . HEM FA 9  .   ? 7.552   -9.121  53.300 1.00 35.83  ? 409 HEM B CMC 1 
HETATM 8414 C  CAC . HEM FA 9  .   ? 9.975   -11.291 53.919 1.00 38.91  ? 409 HEM B CAC 1 
HETATM 8415 C  CBC . HEM FA 9  .   ? 10.019  -11.107 52.608 1.00 45.67  ? 409 HEM B CBC 1 
HETATM 8416 C  C1D . HEM FA 9  .   ? 11.089  -10.784 58.084 1.00 31.51  ? 409 HEM B C1D 1 
HETATM 8417 C  C2D . HEM FA 9  .   ? 12.033  -11.701 58.730 1.00 32.87  ? 409 HEM B C2D 1 
HETATM 8418 C  C3D . HEM FA 9  .   ? 12.217  -11.252 59.980 1.00 32.13  ? 409 HEM B C3D 1 
HETATM 8419 C  C4D . HEM FA 9  .   ? 11.333  -10.114 60.116 1.00 31.39  ? 409 HEM B C4D 1 
HETATM 8420 C  CMD . HEM FA 9  .   ? 12.728  -12.892 58.104 1.00 34.56  ? 409 HEM B CMD 1 
HETATM 8421 C  CAD . HEM FA 9  .   ? 13.094  -11.893 61.022 1.00 31.67  ? 409 HEM B CAD 1 
HETATM 8422 C  CBD . HEM FA 9  .   ? 14.489  -11.291 61.138 1.00 33.67  ? 409 HEM B CBD 1 
HETATM 8423 C  CGD . HEM FA 9  .   ? 15.331  -12.162 62.054 1.00 37.80  ? 409 HEM B CGD 1 
HETATM 8424 O  O1D . HEM FA 9  .   ? 16.556  -12.243 61.824 1.00 40.28  ? 409 HEM B O1D 1 
HETATM 8425 O  O2D . HEM FA 9  .   ? 14.853  -12.832 63.035 1.00 42.60  ? 409 HEM B O2D 1 
HETATM 8426 N  NA  . HEM FA 9  .   ? 9.513   -7.877  60.516 1.00 32.74  ? 409 HEM B NA  1 
HETATM 8427 N  NB  . HEM FA 9  .   ? 7.863   -7.098  58.363 1.00 31.62  ? 409 HEM B NB  1 
HETATM 8428 N  NC  . HEM FA 9  .   ? 8.998   -9.165  56.756 1.00 30.44  ? 409 HEM B NC  1 
HETATM 8429 N  ND  . HEM FA 9  .   ? 10.696  -9.838  58.934 1.00 33.74  ? 409 HEM B ND  1 
HETATM 8430 FE FE  . HEM FA 9  .   ? 9.411   -8.444  58.617 1.00 32.16  ? 409 HEM B FE  1 
HETATM 8431 MG MG  . MG  GA 10 .   ? 13.788  -9.218  67.697 1.00 43.91  ? 410 MG  B MG  1 
HETATM 8432 S  S   . SO4 HA 11 .   ? 18.488  -21.716 46.189 1.00 85.78  ? 411 SO4 B S   1 
HETATM 8433 O  O1  . SO4 HA 11 .   ? 19.102  -21.266 44.944 1.00 70.95  ? 411 SO4 B O1  1 
HETATM 8434 O  O2  . SO4 HA 11 .   ? 17.074  -22.040 45.935 1.00 68.01  ? 411 SO4 B O2  1 
HETATM 8435 O  O3  . SO4 HA 11 .   ? 19.199  -22.931 46.636 1.00 57.63  ? 411 SO4 B O3  1 
HETATM 8436 O  O4  . SO4 HA 11 .   ? 18.583  -20.634 47.223 1.00 55.01  ? 411 SO4 B O4  1 
HETATM 8437 S  S   . SO4 IA 11 .   ? -17.762 -10.937 58.860 1.00 83.95  ? 412 SO4 B S   1 
HETATM 8438 O  O1  . SO4 IA 11 .   ? -16.949 -10.025 58.052 1.00 71.63  ? 412 SO4 B O1  1 
HETATM 8439 O  O2  . SO4 IA 11 .   ? -18.642 -11.706 57.982 1.00 62.81  ? 412 SO4 B O2  1 
HETATM 8440 O  O3  . SO4 IA 11 .   ? -16.894 -11.867 59.578 1.00 72.00  ? 412 SO4 B O3  1 
HETATM 8441 O  O4  . SO4 IA 11 .   ? -18.565 -10.153 59.814 1.00 67.42  ? 412 SO4 B O4  1 
HETATM 8442 C  C1  . GOL JA 7  .   ? -15.240 32.626  24.279 1.00 85.54  ? 401 GOL C C1  1 
HETATM 8443 O  O1  . GOL JA 7  .   ? -14.736 33.646  23.418 1.00 82.16  ? 401 GOL C O1  1 
HETATM 8444 C  C2  . GOL JA 7  .   ? -14.233 32.277  25.354 1.00 86.94  ? 401 GOL C C2  1 
HETATM 8445 O  O2  . GOL JA 7  .   ? -13.684 33.491  25.865 1.00 83.03  ? 401 GOL C O2  1 
HETATM 8446 C  C3  . GOL JA 7  .   ? -14.787 31.445  26.499 1.00 84.32  ? 401 GOL C C3  1 
HETATM 8447 O  O3  . GOL JA 7  .   ? -15.890 30.622  26.119 1.00 79.27  ? 401 GOL C O3  1 
HETATM 8448 C  C1  . GOL KA 7  .   ? -26.110 3.867   14.235 1.00 53.65  ? 402 GOL C C1  1 
HETATM 8449 O  O1  . GOL KA 7  .   ? -26.970 4.970   13.958 1.00 51.87  ? 402 GOL C O1  1 
HETATM 8450 C  C2  . GOL KA 7  .   ? -26.820 2.527   14.221 1.00 55.21  ? 402 GOL C C2  1 
HETATM 8451 O  O2  . GOL KA 7  .   ? -27.436 2.284   12.960 1.00 67.91  ? 402 GOL C O2  1 
HETATM 8452 C  C3  . GOL KA 7  .   ? -25.867 1.398   14.534 1.00 54.16  ? 402 GOL C C3  1 
HETATM 8453 O  O3  . GOL KA 7  .   ? -26.398 0.112   14.243 1.00 51.67  ? 402 GOL C O3  1 
HETATM 8454 N  N1  . EPE LA 8  .   ? 14.486  17.943  11.750 0.70 53.42  ? 403 EPE C N1  1 
HETATM 8455 C  C2  . EPE LA 8  .   ? 13.069  17.624  11.764 0.70 53.34  ? 403 EPE C C2  1 
HETATM 8456 C  C3  . EPE LA 8  .   ? 12.287  18.663  11.008 0.70 55.09  ? 403 EPE C C3  1 
HETATM 8457 N  N4  . EPE LA 8  .   ? 12.535  18.624  9.567  0.70 53.08  ? 403 EPE C N4  1 
HETATM 8458 C  C5  . EPE LA 8  .   ? 13.829  17.966  9.355  0.70 55.42  ? 403 EPE C C5  1 
HETATM 8459 C  C6  . EPE LA 8  .   ? 14.825  18.439  10.399 0.70 55.96  ? 403 EPE C C6  1 
HETATM 8460 C  C7  . EPE LA 8  .   ? 11.387  18.057  8.838  0.70 52.57  ? 403 EPE C C7  1 
HETATM 8461 C  C8  . EPE LA 8  .   ? 10.079  18.838  9.036  0.70 52.03  ? 403 EPE C C8  1 
HETATM 8462 O  O8  . EPE LA 8  .   ? 9.051   18.488  8.136  0.70 52.51  ? 403 EPE C O8  1 
HETATM 8463 C  C9  . EPE LA 8  .   ? 14.827  18.893  12.831 0.70 57.15  ? 403 EPE C C9  1 
HETATM 8464 C  C10 . EPE LA 8  .   ? 16.314  19.237  12.885 0.70 57.32  ? 403 EPE C C10 1 
HETATM 8465 S  S   . EPE LA 8  .   ? 16.813  20.013  14.405 0.70 65.08  ? 403 EPE C S   1 
HETATM 8466 O  O1S . EPE LA 8  .   ? 18.246  20.145  14.343 0.70 52.37  ? 403 EPE C O1S 1 
HETATM 8467 O  O2S . EPE LA 8  .   ? 16.226  19.263  15.488 0.70 58.06  ? 403 EPE C O2S 1 
HETATM 8468 O  O3S . EPE LA 8  .   ? 16.162  21.443  14.278 0.70 58.60  ? 403 EPE C O3S 1 
HETATM 8469 N  N1  . EPE MA 8  .   ? -24.920 3.481   -0.895 1.00 62.71  ? 404 EPE C N1  1 
HETATM 8470 C  C2  . EPE MA 8  .   ? -25.300 2.091   -0.553 1.00 67.64  ? 404 EPE C C2  1 
HETATM 8471 C  C3  . EPE MA 8  .   ? -24.153 1.365   0.113  1.00 68.80  ? 404 EPE C C3  1 
HETATM 8472 N  N4  . EPE MA 8  .   ? -22.924 1.377   -0.725 1.00 66.95  ? 404 EPE C N4  1 
HETATM 8473 C  C5  . EPE MA 8  .   ? -22.579 2.766   -1.126 1.00 69.63  ? 404 EPE C C5  1 
HETATM 8474 C  C6  . EPE MA 8  .   ? -23.754 3.442   -1.805 1.00 69.11  ? 404 EPE C C6  1 
HETATM 8475 C  C7  . EPE MA 8  .   ? -21.800 0.740   -0.020 1.00 63.41  ? 404 EPE C C7  1 
HETATM 8476 C  C8  . EPE MA 8  .   ? -21.965 -0.748  0.246  1.00 66.75  ? 404 EPE C C8  1 
HETATM 8477 O  O8  . EPE MA 8  .   ? -22.336 -1.442  -0.933 1.00 69.76  ? 404 EPE C O8  1 
HETATM 8478 C  C9  . EPE MA 8  .   ? -26.063 4.265   -1.446 1.00 63.54  ? 404 EPE C C9  1 
HETATM 8479 C  C10 . EPE MA 8  .   ? -25.713 5.720   -1.798 1.00 65.13  ? 404 EPE C C10 1 
HETATM 8480 S  S   . EPE MA 8  .   ? -27.096 6.828   -1.567 1.00 71.56  ? 404 EPE C S   1 
HETATM 8481 O  O1S . EPE MA 8  .   ? -28.058 6.496   -2.601 1.00 65.74  ? 404 EPE C O1S 1 
HETATM 8482 O  O2S . EPE MA 8  .   ? -26.534 8.171   -1.515 1.00 57.74  ? 404 EPE C O2S 1 
HETATM 8483 O  O3S . EPE MA 8  .   ? -27.746 6.303   -0.164 1.00 59.79  ? 404 EPE C O3S 1 
HETATM 8484 N  N1  . EPE NA 8  .   ? -11.959 -4.643  -2.144 1.00 65.07  ? 405 EPE C N1  1 
HETATM 8485 C  C2  . EPE NA 8  .   ? -12.393 -5.847  -2.882 1.00 68.73  ? 405 EPE C C2  1 
HETATM 8486 C  C3  . EPE NA 8  .   ? -11.591 -6.005  -4.158 1.00 66.06  ? 405 EPE C C3  1 
HETATM 8487 N  N4  . EPE NA 8  .   ? -11.790 -4.857  -5.069 1.00 62.61  ? 405 EPE C N4  1 
HETATM 8488 C  C5  . EPE NA 8  .   ? -11.434 -3.631  -4.350 1.00 61.58  ? 405 EPE C C5  1 
HETATM 8489 C  C6  . EPE NA 8  .   ? -12.171 -3.493  -3.040 1.00 64.69  ? 405 EPE C C6  1 
HETATM 8490 C  C7  . EPE NA 8  .   ? -11.015 -4.967  -6.331 1.00 69.10  ? 405 EPE C C7  1 
HETATM 8491 C  C8  . EPE NA 8  .   ? -9.482  -4.749  -6.227 1.00 69.28  ? 405 EPE C C8  1 
HETATM 8492 O  O8  . EPE NA 8  .   ? -8.871  -4.376  -7.462 1.00 62.47  ? 405 EPE C O8  1 
HETATM 8493 C  C9  . EPE NA 8  .   ? -12.666 -4.440  -0.830 1.00 58.49  ? 405 EPE C C9  1 
HETATM 8494 C  C10 . EPE NA 8  .   ? -14.204 -4.366  -0.932 1.00 58.20  ? 405 EPE C C10 1 
HETATM 8495 S  S   . EPE NA 8  .   ? -14.888 -2.837  -0.294 1.00 77.33  ? 405 EPE C S   1 
HETATM 8496 O  O1S . EPE NA 8  .   ? -14.196 -1.782  -1.002 1.00 67.67  ? 405 EPE C O1S 1 
HETATM 8497 O  O2S . EPE NA 8  .   ? -14.804 -2.907  1.154  1.00 60.46  ? 405 EPE C O2S 1 
HETATM 8498 O  O3S . EPE NA 8  .   ? -16.428 -2.828  -0.807 1.00 59.19  ? 405 EPE C O3S 1 
HETATM 8499 N  N1  . EPE OA 8  .   ? -24.649 15.836  -1.635 1.00 73.59  ? 406 EPE C N1  1 
HETATM 8500 C  C2  . EPE OA 8  .   ? -25.606 16.569  -0.759 1.00 78.51  ? 406 EPE C C2  1 
HETATM 8501 C  C3  . EPE OA 8  .   ? -25.781 15.886  0.582  1.00 79.38  ? 406 EPE C C3  1 
HETATM 8502 N  N4  . EPE OA 8  .   ? -26.264 14.493  0.410  1.00 74.03  ? 406 EPE C N4  1 
HETATM 8503 C  C5  . EPE OA 8  .   ? -25.278 13.769  -0.427 1.00 69.62  ? 406 EPE C C5  1 
HETATM 8504 C  C6  . EPE OA 8  .   ? -25.111 14.432  -1.779 1.00 71.11  ? 406 EPE C C6  1 
HETATM 8505 C  C7  . EPE OA 8  .   ? -26.538 13.820  1.699  1.00 68.67  ? 406 EPE C C7  1 
HETATM 8506 C  C8  . EPE OA 8  .   ? -25.341 13.678  2.640  1.00 67.28  ? 406 EPE C C8  1 
HETATM 8507 O  O8  . EPE OA 8  .   ? -25.668 13.008  3.847  1.00 60.37  ? 406 EPE C O8  1 
HETATM 8508 C  C9  . EPE OA 8  .   ? -24.519 16.489  -2.976 1.00 69.87  ? 406 EPE C C9  1 
HETATM 8509 C  C10 . EPE OA 8  .   ? -24.074 17.958  -2.934 1.00 65.53  ? 406 EPE C C10 1 
HETATM 8510 S  S   . EPE OA 8  .   ? -22.436 18.085  -2.249 1.00 71.89  ? 406 EPE C S   1 
HETATM 8511 O  O1S . EPE OA 8  .   ? -22.571 18.251  -0.813 1.00 60.71  ? 406 EPE C O1S 1 
HETATM 8512 O  O2S . EPE OA 8  .   ? -21.726 19.067  -3.048 1.00 61.84  ? 406 EPE C O2S 1 
HETATM 8513 O  O3S . EPE OA 8  .   ? -21.924 16.602  -2.630 1.00 65.02  ? 406 EPE C O3S 1 
HETATM 8514 N  N1  . EPE PA 8  .   ? -16.437 -8.753  18.905 1.00 63.72  ? 407 EPE C N1  1 
HETATM 8515 C  C2  . EPE PA 8  .   ? -14.999 -8.534  19.027 1.00 61.15  ? 407 EPE C C2  1 
HETATM 8516 C  C3  . EPE PA 8  .   ? -14.496 -7.844  17.778 1.00 69.99  ? 407 EPE C C3  1 
HETATM 8517 N  N4  . EPE PA 8  .   ? -14.699 -8.662  16.571 1.00 66.38  ? 407 EPE C N4  1 
HETATM 8518 C  C5  . EPE PA 8  .   ? -16.149 -8.902  16.445 1.00 69.69  ? 407 EPE C C5  1 
HETATM 8519 C  C6  . EPE PA 8  .   ? -16.656 -9.592  17.693 1.00 69.31  ? 407 EPE C C6  1 
HETATM 8520 C  C7  . EPE PA 8  .   ? -14.150 -7.962  15.398 1.00 66.88  ? 407 EPE C C7  1 
HETATM 8521 C  C8  . EPE PA 8  .   ? -12.641 -7.828  15.392 1.00 64.25  ? 407 EPE C C8  1 
HETATM 8522 O  O8  . EPE PA 8  .   ? -12.195 -7.167  14.216 1.00 66.63  ? 407 EPE C O8  1 
HETATM 8523 C  C9  . EPE PA 8  .   ? -16.972 -9.410  20.116 1.00 71.80  ? 407 EPE C C9  1 
HETATM 8524 C  C10 . EPE PA 8  .   ? -16.422 -10.826 20.273 1.00 70.05  ? 407 EPE C C10 1 
HETATM 8525 S  S   . EPE PA 8  .   ? -17.137 -11.635 21.677 1.00 80.60  ? 407 EPE C S   1 
HETATM 8526 O  O1S . EPE PA 8  .   ? -16.509 -12.944 21.718 1.00 71.68  ? 407 EPE C O1S 1 
HETATM 8527 O  O2S . EPE PA 8  .   ? -18.574 -11.535 21.504 1.00 68.17  ? 407 EPE C O2S 1 
HETATM 8528 O  O3S . EPE PA 8  .   ? -16.645 -10.652 22.878 1.00 58.36  ? 407 EPE C O3S 1 
HETATM 8529 C  CHA . HEM QA 9  .   ? -7.898  11.710  20.332 1.00 37.79  ? 408 HEM C CHA 1 
HETATM 8530 C  CHB . HEM QA 9  .   ? -5.168  7.809   19.661 1.00 36.43  ? 408 HEM C CHB 1 
HETATM 8531 C  CHC . HEM QA 9  .   ? -7.231  7.179   15.306 1.00 35.22  ? 408 HEM C CHC 1 
HETATM 8532 C  CHD . HEM QA 9  .   ? -10.037 11.034  16.103 1.00 36.12  ? 408 HEM C CHD 1 
HETATM 8533 C  C1A . HEM QA 9  .   ? -7.025  10.669  20.502 1.00 38.91  ? 408 HEM C C1A 1 
HETATM 8534 C  C2A . HEM QA 9  .   ? -6.278  10.507  21.692 1.00 41.23  ? 408 HEM C C2A 1 
HETATM 8535 C  C3A . HEM QA 9  .   ? -5.486  9.415   21.498 1.00 38.13  ? 408 HEM C C3A 1 
HETATM 8536 C  C4A . HEM QA 9  .   ? -5.764  8.902   20.210 1.00 36.05  ? 408 HEM C C4A 1 
HETATM 8537 C  CMA . HEM QA 9  .   ? -4.545  8.830   22.518 1.00 39.56  ? 408 HEM C CMA 1 
HETATM 8538 C  CAA . HEM QA 9  .   ? -6.352  11.360  22.946 1.00 41.76  ? 408 HEM C CAA 1 
HETATM 8539 C  CBA . HEM QA 9  .   ? -5.386  12.536  22.809 1.00 48.75  ? 408 HEM C CBA 1 
HETATM 8540 C  CGA . HEM QA 9  .   ? -5.936  13.713  23.601 1.00 53.92  ? 408 HEM C CGA 1 
HETATM 8541 O  O1A . HEM QA 9  .   ? -5.415  13.940  24.726 1.00 48.69  ? 408 HEM C O1A 1 
HETATM 8542 O  O2A . HEM QA 9  .   ? -6.917  14.448  23.152 1.00 51.49  ? 408 HEM C O2A 1 
HETATM 8543 C  C1B . HEM QA 9  .   ? -5.505  7.351   18.384 1.00 36.18  ? 408 HEM C C1B 1 
HETATM 8544 C  C2B . HEM QA 9  .   ? -4.840  6.230   17.828 1.00 33.97  ? 408 HEM C C2B 1 
HETATM 8545 C  C3B . HEM QA 9  .   ? -5.413  6.018   16.622 1.00 36.06  ? 408 HEM C C3B 1 
HETATM 8546 C  C4B . HEM QA 9  .   ? -6.432  7.069   16.437 1.00 34.25  ? 408 HEM C C4B 1 
HETATM 8547 C  CMB . HEM QA 9  .   ? -3.738  5.370   18.422 1.00 33.64  ? 408 HEM C CMB 1 
HETATM 8548 C  CAB . HEM QA 9  .   ? -4.915  4.988   15.712 1.00 39.86  ? 408 HEM C CAB 1 
HETATM 8549 C  CBB . HEM QA 9  .   ? -5.027  5.152   14.408 1.00 46.02  ? 408 HEM C CBB 1 
HETATM 8550 C  C1C . HEM QA 9  .   ? -8.206  8.150   15.147 1.00 35.21  ? 408 HEM C C1C 1 
HETATM 8551 C  C2C . HEM QA 9  .   ? -9.128  8.219   14.073 1.00 38.09  ? 408 HEM C C2C 1 
HETATM 8552 C  C3C . HEM QA 9  .   ? -9.925  9.346   14.326 1.00 36.77  ? 408 HEM C C3C 1 
HETATM 8553 C  C4C . HEM QA 9  .   ? -9.483  9.917   15.553 1.00 35.76  ? 408 HEM C C4C 1 
HETATM 8554 C  CMC . HEM QA 9  .   ? -9.176  7.293   12.861 1.00 36.39  ? 408 HEM C CMC 1 
HETATM 8555 C  CAC . HEM QA 9  .   ? -11.046 9.888   13.568 1.00 40.30  ? 408 HEM C CAC 1 
HETATM 8556 C  CBC . HEM QA 9  .   ? -11.690 9.118   12.695 1.00 48.31  ? 408 HEM C CBC 1 
HETATM 8557 C  C1D . HEM QA 9  .   ? -9.639  11.518  17.328 1.00 37.38  ? 408 HEM C C1D 1 
HETATM 8558 C  C2D . HEM QA 9  .   ? -10.188 12.767  17.870 1.00 38.81  ? 408 HEM C C2D 1 
HETATM 8559 C  C3D . HEM QA 9  .   ? -9.588  12.962  19.063 1.00 40.01  ? 408 HEM C C3D 1 
HETATM 8560 C  C4D . HEM QA 9  .   ? -8.663  11.835  19.210 1.00 36.29  ? 408 HEM C C4D 1 
HETATM 8561 C  CMD . HEM QA 9  .   ? -11.207 13.677  17.238 1.00 41.41  ? 408 HEM C CMD 1 
HETATM 8562 C  CAD . HEM QA 9  .   ? -9.791  14.138  20.002 1.00 40.78  ? 408 HEM C CAD 1 
HETATM 8563 C  CBD . HEM QA 9  .   ? -10.953 13.936  20.992 1.00 44.45  ? 408 HEM C CBD 1 
HETATM 8564 C  CGD . HEM QA 9  .   ? -11.225 15.285  21.646 1.00 45.31  ? 408 HEM C CGD 1 
HETATM 8565 O  O1D . HEM QA 9  .   ? -10.337 16.166  21.706 1.00 40.72  ? 408 HEM C O1D 1 
HETATM 8566 O  O2D . HEM QA 9  .   ? -12.353 15.528  22.115 1.00 44.36  ? 408 HEM C O2D 1 
HETATM 8567 N  NA  . HEM QA 9  .   ? -6.699  9.674   19.607 1.00 33.46  ? 408 HEM C NA  1 
HETATM 8568 N  NB  . HEM QA 9  .   ? -6.451  7.806   17.560 1.00 32.00  ? 408 HEM C NB  1 
HETATM 8569 N  NC  . HEM QA 9  .   ? -8.451  9.168   16.024 1.00 32.43  ? 408 HEM C NC  1 
HETATM 8570 N  ND  . HEM QA 9  .   ? -8.733  10.996  18.159 1.00 36.25  ? 408 HEM C ND  1 
HETATM 8571 FE FE  . HEM QA 9  .   ? -7.700  9.436   17.929 1.00 35.65  ? 408 HEM C FE  1 
HETATM 8572 MG MG  . MG  RA 10 .   ? -6.835  15.410  25.888 1.00 59.06  ? 409 MG  C MG  1 
HETATM 8573 S  S   . SO4 SA 11 .   ? -23.564 16.792  8.473  1.00 97.07  ? 410 SO4 C S   1 
HETATM 8574 O  O1  . SO4 SA 11 .   ? -22.732 16.807  7.268  1.00 78.25  ? 410 SO4 C O1  1 
HETATM 8575 O  O2  . SO4 SA 11 .   ? -24.736 15.961  8.216  1.00 70.65  ? 410 SO4 C O2  1 
HETATM 8576 O  O3  . SO4 SA 11 .   ? -22.812 16.267  9.650  1.00 59.99  ? 410 SO4 C O3  1 
HETATM 8577 O  O4  . SO4 SA 11 .   ? -24.015 18.162  8.735  1.00 85.68  ? 410 SO4 C O4  1 
HETATM 8578 S  S   . SO4 TA 11 .   ? -6.342  4.169   34.022 1.00 78.58  ? 411 SO4 C S   1 
HETATM 8579 O  O1  . SO4 TA 11 .   ? -5.217  4.435   33.120 1.00 74.53  ? 411 SO4 C O1  1 
HETATM 8580 O  O2  . SO4 TA 11 .   ? -7.509  4.981   33.631 1.00 55.01  ? 411 SO4 C O2  1 
HETATM 8581 O  O3  . SO4 TA 11 .   ? -6.665  2.733   33.994 1.00 59.78  ? 411 SO4 C O3  1 
HETATM 8582 O  O4  . SO4 TA 11 .   ? -5.928  4.534   35.376 1.00 73.79  ? 411 SO4 C O4  1 
HETATM 8583 O  O   . HOH UA 12 .   ? 70.451  9.511   43.391 1.00 38.48  ? 501 HOH A O   1 
HETATM 8584 O  O   . HOH UA 12 .   ? 35.535  14.492  36.151 1.00 50.33  ? 502 HOH A O   1 
HETATM 8585 O  O   . HOH UA 12 .   ? 55.753  14.579  49.073 1.00 46.70  ? 503 HOH A O   1 
HETATM 8586 O  O   . HOH UA 12 .   ? 56.570  -5.116  51.504 1.00 51.59  ? 504 HOH A O   1 
HETATM 8587 O  O   . HOH UA 12 .   ? 39.072  -17.786 46.664 1.00 43.32  ? 505 HOH A O   1 
HETATM 8588 O  O   . HOH UA 12 .   ? 64.080  0.108   34.811 1.00 37.28  ? 506 HOH A O   1 
HETATM 8589 O  O   . HOH UA 12 .   ? 46.571  -1.773  54.267 1.00 45.02  ? 507 HOH A O   1 
HETATM 8590 O  O   . HOH UA 12 .   ? 52.501  -15.770 32.940 1.00 47.76  ? 508 HOH A O   1 
HETATM 8591 O  O   . HOH UA 12 .   ? 47.082  -12.685 28.815 1.00 42.98  ? 509 HOH A O   1 
HETATM 8592 O  O   . HOH UA 12 .   ? 23.333  -1.821  42.202 1.00 31.54  ? 510 HOH A O   1 
HETATM 8593 O  O   . HOH UA 12 .   ? 58.534  -12.773 39.615 1.00 49.87  ? 511 HOH A O   1 
HETATM 8594 O  O   . HOH UA 12 .   ? 75.242  5.616   40.889 1.00 42.27  ? 512 HOH A O   1 
HETATM 8595 O  O   . HOH UA 12 .   ? 28.491  -9.824  51.735 1.00 31.75  ? 513 HOH A O   1 
HETATM 8596 O  O   . HOH UA 12 .   ? 24.446  1.134   43.431 1.00 32.88  ? 514 HOH A O   1 
HETATM 8597 O  O   . HOH UA 12 .   ? 46.942  -9.941  48.102 1.00 46.58  ? 515 HOH A O   1 
HETATM 8598 O  O   . HOH UA 12 .   ? 58.058  -3.116  45.712 1.00 37.09  ? 516 HOH A O   1 
HETATM 8599 O  O   . HOH UA 12 .   ? 25.533  -5.103  44.106 1.00 47.36  ? 517 HOH A O   1 
HETATM 8600 O  O   . HOH UA 12 .   ? 39.733  7.698   35.570 1.00 32.02  ? 518 HOH A O   1 
HETATM 8601 O  O   . HOH UA 12 .   ? 19.776  1.948   23.387 1.00 35.35  ? 519 HOH A O   1 
HETATM 8602 O  O   . HOH UA 12 .   ? 53.097  8.266   52.071 1.00 34.56  ? 520 HOH A O   1 
HETATM 8603 O  O   . HOH UA 12 .   ? 58.321  7.215   47.621 1.00 35.45  ? 521 HOH A O   1 
HETATM 8604 O  O   . HOH UA 12 .   ? 27.381  -15.921 26.018 1.00 55.82  ? 522 HOH A O   1 
HETATM 8605 O  O   . HOH UA 12 .   ? 44.007  15.450  30.572 1.00 48.31  ? 523 HOH A O   1 
HETATM 8606 O  O   . HOH UA 12 .   ? 73.277  14.301  46.875 1.00 30.20  ? 524 HOH A O   1 
HETATM 8607 O  O   . HOH UA 12 .   ? 47.233  7.628   38.309 1.00 33.74  ? 525 HOH A O   1 
HETATM 8608 O  O   . HOH UA 12 .   ? 32.551  -1.929  49.553 1.00 34.14  ? 526 HOH A O   1 
HETATM 8609 O  O   . HOH UA 12 .   ? 47.013  24.740  17.842 1.00 54.90  ? 527 HOH A O   1 
HETATM 8610 O  O   . HOH UA 12 .   ? 45.298  4.750   32.120 1.00 44.28  ? 528 HOH A O   1 
HETATM 8611 O  O   . HOH UA 12 .   ? 37.346  9.722   31.364 1.00 34.78  ? 529 HOH A O   1 
HETATM 8612 O  O   . HOH UA 12 .   ? 41.130  12.207  33.446 1.00 36.89  ? 530 HOH A O   1 
HETATM 8613 O  O   . HOH UA 12 .   ? 34.037  10.327  37.450 1.00 32.70  ? 531 HOH A O   1 
HETATM 8614 O  O   . HOH UA 12 .   ? 22.762  -4.694  19.341 1.00 45.13  ? 532 HOH A O   1 
HETATM 8615 O  O   . HOH UA 12 .   ? 62.419  17.216  39.333 1.00 42.81  ? 533 HOH A O   1 
HETATM 8616 O  O   . HOH UA 12 .   ? 49.307  10.097  36.757 1.00 47.61  ? 534 HOH A O   1 
HETATM 8617 O  O   . HOH UA 12 .   ? 39.961  4.043   18.426 1.00 40.60  ? 535 HOH A O   1 
HETATM 8618 O  O   . HOH UA 12 .   ? 58.770  -0.202  47.346 1.00 35.40  ? 536 HOH A O   1 
HETATM 8619 O  O   . HOH UA 12 .   ? 57.619  -5.838  45.345 1.00 32.19  ? 537 HOH A O   1 
HETATM 8620 O  O   . HOH UA 12 .   ? 69.036  2.517   38.299 1.00 40.28  ? 538 HOH A O   1 
HETATM 8621 O  O   . HOH UA 12 .   ? 61.791  13.253  45.306 1.00 43.24  ? 539 HOH A O   1 
HETATM 8622 O  O   . HOH UA 12 .   ? 41.050  15.840  31.799 1.00 38.69  ? 540 HOH A O   1 
HETATM 8623 O  O   . HOH UA 12 .   ? 23.987  -5.376  39.488 1.00 44.60  ? 541 HOH A O   1 
HETATM 8624 O  O   . HOH UA 12 .   ? 37.136  5.577   12.342 1.00 51.40  ? 542 HOH A O   1 
HETATM 8625 O  O   . HOH UA 12 .   ? 35.375  -2.152  54.197 1.00 35.82  ? 543 HOH A O   1 
HETATM 8626 O  O   . HOH UA 12 .   ? 37.482  -13.332 26.699 1.00 38.02  ? 544 HOH A O   1 
HETATM 8627 O  O   . HOH UA 12 .   ? 45.970  12.277  45.526 1.00 55.01  ? 545 HOH A O   1 
HETATM 8628 O  O   . HOH UA 12 .   ? 66.282  -0.571  36.006 1.00 42.83  ? 546 HOH A O   1 
HETATM 8629 O  O   . HOH UA 12 .   ? 38.052  1.925   18.853 1.00 40.83  ? 547 HOH A O   1 
HETATM 8630 O  O   . HOH UA 12 .   ? 38.291  -13.241 35.730 1.00 36.92  ? 548 HOH A O   1 
HETATM 8631 O  O   . HOH UA 12 .   ? 52.293  -16.319 43.048 1.00 59.04  ? 549 HOH A O   1 
HETATM 8632 O  O   . HOH UA 12 .   ? 56.216  7.350   43.838 1.00 34.88  ? 550 HOH A O   1 
HETATM 8633 O  O   . HOH UA 12 .   ? 23.081  5.318   40.027 1.00 46.65  ? 551 HOH A O   1 
HETATM 8634 O  O   . HOH UA 12 .   ? 48.969  8.194   50.133 1.00 39.08  ? 552 HOH A O   1 
HETATM 8635 O  O   . HOH UA 12 .   ? 39.291  -15.052 29.704 1.00 45.30  ? 553 HOH A O   1 
HETATM 8636 O  O   . HOH UA 12 .   ? 35.005  -4.034  56.151 1.00 45.28  ? 554 HOH A O   1 
HETATM 8637 O  O   . HOH UA 12 .   ? 51.079  9.799   38.400 1.00 42.43  ? 555 HOH A O   1 
HETATM 8638 O  O   . HOH UA 12 .   ? 44.598  11.490  29.682 1.00 44.48  ? 556 HOH A O   1 
HETATM 8639 O  O   . HOH UA 12 .   ? 23.075  -13.958 46.698 1.00 40.31  ? 557 HOH A O   1 
HETATM 8640 O  O   . HOH UA 12 .   ? 55.178  -14.399 34.009 1.00 48.87  ? 558 HOH A O   1 
HETATM 8641 O  O   . HOH UA 12 .   ? 39.887  2.084   57.335 1.00 45.42  ? 559 HOH A O   1 
HETATM 8642 O  O   . HOH UA 12 .   ? 40.930  2.157   42.237 1.00 32.70  ? 560 HOH A O   1 
HETATM 8643 O  O   . HOH UA 12 .   ? 20.403  -10.333 22.539 1.00 49.51  ? 561 HOH A O   1 
HETATM 8644 O  O   . HOH UA 12 .   ? 38.981  8.224   45.896 1.00 45.13  ? 562 HOH A O   1 
HETATM 8645 O  O   . HOH UA 12 .   ? 46.748  -2.179  26.215 1.00 50.65  ? 563 HOH A O   1 
HETATM 8646 O  O   . HOH UA 12 .   ? 55.503  -0.824  55.357 1.00 46.14  ? 564 HOH A O   1 
HETATM 8647 O  O   . HOH UA 12 .   ? 51.492  -21.805 36.914 1.00 45.98  ? 565 HOH A O   1 
HETATM 8648 O  O   . HOH UA 12 .   ? 38.773  5.089   35.511 1.00 32.97  ? 566 HOH A O   1 
HETATM 8649 O  O   . HOH UA 12 .   ? 38.915  9.970   33.688 1.00 34.94  ? 567 HOH A O   1 
HETATM 8650 O  O   . HOH UA 12 .   ? 42.074  10.575  49.773 1.00 50.67  ? 568 HOH A O   1 
HETATM 8651 O  O   . HOH UA 12 .   ? 48.221  4.320   16.631 1.00 44.24  ? 569 HOH A O   1 
HETATM 8652 O  O   . HOH UA 12 .   ? 32.689  14.740  28.165 1.00 45.89  ? 570 HOH A O   1 
HETATM 8653 O  O   . HOH UA 12 .   ? 49.468  -4.608  32.128 1.00 49.30  ? 571 HOH A O   1 
HETATM 8654 O  O   . HOH UA 12 .   ? 47.123  -15.445 36.617 1.00 27.98  ? 572 HOH A O   1 
HETATM 8655 O  O   . HOH UA 12 .   ? 30.103  -12.287 34.845 1.00 39.00  ? 573 HOH A O   1 
HETATM 8656 O  O   . HOH UA 12 .   ? 50.073  5.785   47.350 1.00 34.77  ? 574 HOH A O   1 
HETATM 8657 O  O   . HOH UA 12 .   ? 42.750  17.631  32.893 1.00 51.02  ? 575 HOH A O   1 
HETATM 8658 O  O   . HOH UA 12 .   ? 34.544  12.774  27.865 1.00 41.25  ? 576 HOH A O   1 
HETATM 8659 O  O   . HOH UA 12 .   ? 62.238  -5.178  55.286 1.00 46.29  ? 577 HOH A O   1 
HETATM 8660 O  O   . HOH UA 12 .   ? 55.825  -5.810  47.573 1.00 37.26  ? 578 HOH A O   1 
HETATM 8661 O  O   . HOH UA 12 .   ? 29.026  -15.015 37.738 1.00 46.13  ? 579 HOH A O   1 
HETATM 8662 O  O   . HOH UA 12 .   ? 40.607  8.420   47.883 1.00 41.69  ? 580 HOH A O   1 
HETATM 8663 O  O   . HOH UA 12 .   ? 54.872  9.684   43.862 1.00 34.82  ? 581 HOH A O   1 
HETATM 8664 O  O   . HOH UA 12 .   ? 30.629  5.179   28.408 1.00 38.01  ? 582 HOH A O   1 
HETATM 8665 O  O   . HOH UA 12 .   ? 33.766  -2.367  16.779 1.00 41.35  ? 583 HOH A O   1 
HETATM 8666 O  O   . HOH UA 12 .   ? 44.872  -19.267 42.165 1.00 42.31  ? 584 HOH A O   1 
HETATM 8667 O  O   . HOH UA 12 .   ? 67.276  0.071   38.559 1.00 42.71  ? 585 HOH A O   1 
HETATM 8668 O  O   . HOH UA 12 .   ? 23.847  -11.728 34.400 1.00 47.48  ? 586 HOH A O   1 
HETATM 8669 O  O   . HOH UA 12 .   ? 20.795  5.969   21.332 1.00 46.91  ? 587 HOH A O   1 
HETATM 8670 O  O   . HOH UA 12 .   ? 49.291  -3.935  53.518 1.00 42.39  ? 588 HOH A O   1 
HETATM 8671 O  O   . HOH UA 12 .   ? 49.266  9.294   29.803 1.00 37.38  ? 589 HOH A O   1 
HETATM 8672 O  O   . HOH UA 12 .   ? 29.810  -11.421 48.899 1.00 42.05  ? 590 HOH A O   1 
HETATM 8673 O  O   . HOH UA 12 .   ? 46.299  -25.037 36.608 1.00 49.92  ? 591 HOH A O   1 
HETATM 8674 O  O   . HOH UA 12 .   ? 47.728  11.170  27.975 1.00 41.89  ? 592 HOH A O   1 
HETATM 8675 O  O   . HOH UA 12 .   ? 44.490  -22.717 32.755 1.00 46.62  ? 593 HOH A O   1 
HETATM 8676 O  O   . HOH UA 12 .   ? 59.046  7.531   50.205 1.00 41.33  ? 594 HOH A O   1 
HETATM 8677 O  O   . HOH UA 12 .   ? 29.292  7.418   42.380 1.00 49.99  ? 595 HOH A O   1 
HETATM 8678 O  O   . HOH UA 12 .   ? 48.909  -15.448 43.190 1.00 46.06  ? 596 HOH A O   1 
HETATM 8679 O  O   . HOH UA 12 .   ? 32.630  2.112   42.069 1.00 40.31  ? 597 HOH A O   1 
HETATM 8680 O  O   . HOH UA 12 .   ? 34.494  12.535  30.578 1.00 33.86  ? 598 HOH A O   1 
HETATM 8681 O  O   . HOH UA 12 .   ? 31.856  11.878  37.400 1.00 37.15  ? 599 HOH A O   1 
HETATM 8682 O  O   . HOH UA 12 .   ? 26.985  9.420   38.969 1.00 44.79  ? 600 HOH A O   1 
HETATM 8683 O  O   . HOH UA 12 .   ? 48.620  -10.410 25.699 1.00 55.49  ? 601 HOH A O   1 
HETATM 8684 O  O   . HOH UA 12 .   ? 66.569  10.592  49.527 1.00 46.41  ? 602 HOH A O   1 
HETATM 8685 O  O   . HOH UA 12 .   ? 51.965  17.395  26.481 1.00 51.30  ? 603 HOH A O   1 
HETATM 8686 O  O   . HOH UA 12 .   ? 34.417  -0.118  41.118 1.00 34.33  ? 604 HOH A O   1 
HETATM 8687 O  O   . HOH UA 12 .   ? 49.550  -15.742 35.505 1.00 34.88  ? 605 HOH A O   1 
HETATM 8688 O  O   . HOH UA 12 .   ? 35.191  -3.914  52.174 1.00 36.27  ? 606 HOH A O   1 
HETATM 8689 O  O   . HOH UA 12 .   ? 24.299  -3.600  15.234 1.00 57.94  ? 607 HOH A O   1 
HETATM 8690 O  O   . HOH UA 12 .   ? 35.457  4.948   43.285 1.00 55.38  ? 608 HOH A O   1 
HETATM 8691 O  O   . HOH UA 12 .   ? 30.968  -10.561 56.421 1.00 43.02  ? 609 HOH A O   1 
HETATM 8692 O  O   . HOH UA 12 .   ? 47.735  16.207  13.568 1.00 49.93  ? 610 HOH A O   1 
HETATM 8693 O  O   . HOH UA 12 .   ? 55.059  -2.932  54.058 1.00 52.67  ? 611 HOH A O   1 
HETATM 8694 O  O   . HOH UA 12 .   ? 20.920  -9.139  30.505 1.00 49.86  ? 612 HOH A O   1 
HETATM 8695 O  O   . HOH UA 12 .   ? 45.351  14.782  40.281 1.00 49.09  ? 613 HOH A O   1 
HETATM 8696 O  O   . HOH UA 12 .   ? 51.647  9.453   30.136 1.00 46.82  ? 614 HOH A O   1 
HETATM 8697 O  O   . HOH UA 12 .   ? 50.023  -20.136 44.471 1.00 43.84  ? 615 HOH A O   1 
HETATM 8698 O  O   . HOH UA 12 .   ? 27.530  -15.563 45.898 1.00 48.70  ? 616 HOH A O   1 
HETATM 8699 O  O   . HOH UA 12 .   ? 63.819  13.497  33.415 1.00 54.89  ? 617 HOH A O   1 
HETATM 8700 O  O   . HOH UA 12 .   ? 55.981  -16.865 43.675 1.00 52.51  ? 618 HOH A O   1 
HETATM 8701 O  O   . HOH UA 12 .   ? 51.935  10.605  51.058 1.00 51.65  ? 619 HOH A O   1 
HETATM 8702 O  O   . HOH UA 12 .   ? 40.741  -13.376 53.601 1.00 58.24  ? 620 HOH A O   1 
HETATM 8703 O  O   . HOH UA 12 .   ? 55.628  13.662  24.750 1.00 54.19  ? 621 HOH A O   1 
HETATM 8704 O  O   . HOH UA 12 .   ? 31.889  5.617   43.214 1.00 47.73  ? 622 HOH A O   1 
HETATM 8705 O  O   . HOH UA 12 .   ? 45.096  -1.291  34.109 1.00 48.82  ? 623 HOH A O   1 
HETATM 8706 O  O   . HOH UA 12 .   ? 20.140  2.268   32.315 1.00 64.73  ? 624 HOH A O   1 
HETATM 8707 O  O   . HOH UA 12 .   ? 55.518  -7.170  49.959 1.00 52.05  ? 625 HOH A O   1 
HETATM 8708 O  O   . HOH UA 12 .   ? 49.422  -10.773 52.808 1.00 52.39  ? 626 HOH A O   1 
HETATM 8709 O  O   . HOH UA 12 .   ? 59.679  12.140  30.453 1.00 61.82  ? 627 HOH A O   1 
HETATM 8710 O  O   . HOH UA 12 .   ? 49.966  11.570  52.779 1.00 48.08  ? 628 HOH A O   1 
HETATM 8711 O  O   . HOH UA 12 .   ? 37.068  6.541   49.023 1.00 48.05  ? 629 HOH A O   1 
HETATM 8712 O  O   . HOH UA 12 .   ? 34.179  -15.582 22.234 1.00 53.16  ? 630 HOH A O   1 
HETATM 8713 O  O   . HOH UA 12 .   ? 23.485  7.474   26.490 1.00 44.03  ? 631 HOH A O   1 
HETATM 8714 O  O   . HOH UA 12 .   ? 35.689  7.101   44.473 1.00 47.55  ? 632 HOH A O   1 
HETATM 8715 O  O   . HOH UA 12 .   ? 68.156  6.414   54.681 1.00 46.67  ? 633 HOH A O   1 
HETATM 8716 O  O   . HOH UA 12 .   ? 20.250  3.437   28.390 1.00 55.93  ? 634 HOH A O   1 
HETATM 8717 O  O   . HOH UA 12 .   ? 25.448  -17.202 45.245 1.00 47.05  ? 635 HOH A O   1 
HETATM 8718 O  O   . HOH UA 12 .   ? 48.369  -21.121 31.554 1.00 54.49  ? 636 HOH A O   1 
HETATM 8719 O  O   . HOH UA 12 .   ? 41.071  -14.561 26.783 1.00 58.11  ? 637 HOH A O   1 
HETATM 8720 O  O   . HOH UA 12 .   ? 24.819  3.686   43.859 1.00 42.19  ? 638 HOH A O   1 
HETATM 8721 O  O   . HOH UA 12 .   ? 35.072  -6.290  15.871 1.00 56.73  ? 639 HOH A O   1 
HETATM 8722 O  O   . HOH UA 12 .   ? 47.588  -4.831  55.388 1.00 65.82  ? 640 HOH A O   1 
HETATM 8723 O  O   . HOH UA 12 .   ? 46.391  -1.901  32.691 1.00 59.19  ? 641 HOH A O   1 
HETATM 8724 O  O   . HOH UA 12 .   ? 31.065  -7.807  13.174 1.00 53.76  ? 642 HOH A O   1 
HETATM 8725 O  O   . HOH UA 12 .   ? 50.636  -17.520 33.704 1.00 40.05  ? 643 HOH A O   1 
HETATM 8726 O  O   . HOH UA 12 .   ? 38.006  -18.868 27.953 1.00 53.82  ? 644 HOH A O   1 
HETATM 8727 O  O   . HOH UA 12 .   ? 57.722  -16.864 36.927 1.00 51.39  ? 645 HOH A O   1 
HETATM 8728 O  O   . HOH UA 12 .   ? 48.746  14.201  46.092 1.00 51.99  ? 646 HOH A O   1 
HETATM 8729 O  O   . HOH UA 12 .   ? 51.398  -20.248 34.492 1.00 46.48  ? 647 HOH A O   1 
HETATM 8730 O  O   . HOH UA 12 .   ? 39.575  -12.706 21.672 1.00 57.85  ? 648 HOH A O   1 
HETATM 8731 O  O   . HOH VA 12 .   ? 22.098  -8.195  43.355 1.00 35.65  ? 501 HOH B O   1 
HETATM 8732 O  O   . HOH VA 12 .   ? -2.937  4.729   57.100 1.00 39.83  ? 502 HOH B O   1 
HETATM 8733 O  O   . HOH VA 12 .   ? 28.286  -27.145 61.232 1.00 41.83  ? 503 HOH B O   1 
HETATM 8734 O  O   . HOH VA 12 .   ? 9.910   -10.622 73.159 1.00 41.32  ? 504 HOH B O   1 
HETATM 8735 O  O   . HOH VA 12 .   ? 14.725  -7.919  66.611 1.00 50.21  ? 505 HOH B O   1 
HETATM 8736 O  O   . HOH VA 12 .   ? 16.717  -11.547 69.224 1.00 40.54  ? 506 HOH B O   1 
HETATM 8737 O  O   . HOH VA 12 .   ? 11.677  -9.066  76.265 1.00 41.30  ? 507 HOH B O   1 
HETATM 8738 O  O   . HOH VA 12 .   ? 14.382  -8.010  71.703 1.00 38.63  ? 508 HOH B O   1 
HETATM 8739 O  O   . HOH VA 12 .   ? -0.206  -16.755 52.236 1.00 43.78  ? 509 HOH B O   1 
HETATM 8740 O  O   . HOH VA 12 .   ? 28.652  -7.506  54.085 1.00 33.39  ? 510 HOH B O   1 
HETATM 8741 O  O   . HOH VA 12 .   ? 20.395  6.101   47.182 1.00 47.69  ? 511 HOH B O   1 
HETATM 8742 O  O   . HOH VA 12 .   ? -2.266  7.277   59.637 1.00 40.96  ? 512 HOH B O   1 
HETATM 8743 O  O   . HOH VA 12 .   ? 20.192  4.706   49.776 1.00 39.94  ? 513 HOH B O   1 
HETATM 8744 O  O   . HOH VA 12 .   ? 7.855   -22.449 50.166 1.00 40.17  ? 514 HOH B O   1 
HETATM 8745 O  O   . HOH VA 12 .   ? 28.550  -18.864 54.176 1.00 46.77  ? 515 HOH B O   1 
HETATM 8746 O  O   . HOH VA 12 .   ? 27.389  -18.804 66.470 1.00 42.10  ? 516 HOH B O   1 
HETATM 8747 O  O   . HOH VA 12 .   ? 9.848   -4.518  39.390 1.00 45.17  ? 517 HOH B O   1 
HETATM 8748 O  O   . HOH VA 12 .   ? 26.025  -7.999  48.592 1.00 50.03  ? 518 HOH B O   1 
HETATM 8749 O  O   . HOH VA 12 .   ? -10.063 -2.441  64.987 1.00 40.22  ? 519 HOH B O   1 
HETATM 8750 O  O   . HOH VA 12 .   ? 0.461   9.144   65.806 1.00 48.90  ? 520 HOH B O   1 
HETATM 8751 O  O   . HOH VA 12 .   ? 11.633  6.047   70.497 1.00 53.35  ? 521 HOH B O   1 
HETATM 8752 O  O   . HOH VA 12 .   ? -5.228  -12.224 48.833 1.00 45.46  ? 522 HOH B O   1 
HETATM 8753 O  O   . HOH VA 12 .   ? -1.217  9.886   73.196 1.00 47.45  ? 523 HOH B O   1 
HETATM 8754 O  O   . HOH VA 12 .   ? -12.150 -0.769  64.305 1.00 40.02  ? 524 HOH B O   1 
HETATM 8755 O  O   . HOH VA 12 .   ? 8.425   -2.763  67.005 1.00 38.53  ? 525 HOH B O   1 
HETATM 8756 O  O   . HOH VA 12 .   ? -12.119 1.927   64.237 1.00 42.69  ? 526 HOH B O   1 
HETATM 8757 O  O   . HOH VA 12 .   ? 9.327   -14.020 47.045 1.00 30.47  ? 527 HOH B O   1 
HETATM 8758 O  O   . HOH VA 12 .   ? 1.581   5.019   66.938 1.00 40.93  ? 528 HOH B O   1 
HETATM 8759 O  O   . HOH VA 12 .   ? 19.562  -17.355 43.908 1.00 38.90  ? 529 HOH B O   1 
HETATM 8760 O  O   . HOH VA 12 .   ? 18.879  -4.474  39.469 1.00 51.92  ? 530 HOH B O   1 
HETATM 8761 O  O   . HOH VA 12 .   ? 25.649  -9.272  39.250 1.00 36.69  ? 531 HOH B O   1 
HETATM 8762 O  O   . HOH VA 12 .   ? 10.800  -6.915  36.084 1.00 44.67  ? 532 HOH B O   1 
HETATM 8763 O  O   . HOH VA 12 .   ? 16.823  -17.075 46.423 1.00 40.58  ? 533 HOH B O   1 
HETATM 8764 O  O   . HOH VA 12 .   ? 6.895   11.278  64.513 1.00 45.38  ? 534 HOH B O   1 
HETATM 8765 O  O   . HOH VA 12 .   ? 8.823   -29.156 73.077 1.00 49.51  ? 535 HOH B O   1 
HETATM 8766 O  O   . HOH VA 12 .   ? 20.426  -17.921 64.578 1.00 37.73  ? 536 HOH B O   1 
HETATM 8767 O  O   . HOH VA 12 .   ? 21.712  -0.072  51.344 1.00 38.71  ? 537 HOH B O   1 
HETATM 8768 O  O   . HOH VA 12 .   ? 19.356  -9.115  38.670 1.00 45.31  ? 538 HOH B O   1 
HETATM 8769 O  O   . HOH VA 12 .   ? 10.291  -25.072 66.853 1.00 39.40  ? 539 HOH B O   1 
HETATM 8770 O  O   . HOH VA 12 .   ? 6.612   -2.540  70.045 1.00 56.41  ? 540 HOH B O   1 
HETATM 8771 O  O   . HOH VA 12 .   ? 6.269   -19.518 47.746 1.00 42.81  ? 541 HOH B O   1 
HETATM 8772 O  O   . HOH VA 12 .   ? -16.049 1.779   72.584 1.00 39.48  ? 542 HOH B O   1 
HETATM 8773 O  O   . HOH VA 12 .   ? 15.890  -13.260 33.988 1.00 46.23  ? 543 HOH B O   1 
HETATM 8774 O  O   . HOH VA 12 .   ? 18.276  0.989   63.108 1.00 40.84  ? 544 HOH B O   1 
HETATM 8775 O  O   . HOH VA 12 .   ? 17.782  -15.994 42.416 1.00 48.06  ? 545 HOH B O   1 
HETATM 8776 O  O   . HOH VA 12 .   ? 15.323  -8.256  75.327 1.00 45.54  ? 546 HOH B O   1 
HETATM 8777 O  O   . HOH VA 12 .   ? 14.934  -8.822  63.684 1.00 34.09  ? 547 HOH B O   1 
HETATM 8778 O  O   . HOH VA 12 .   ? 1.225   -10.700 58.781 1.00 43.53  ? 548 HOH B O   1 
HETATM 8779 O  O   . HOH VA 12 .   ? 7.526   5.750   62.871 1.00 37.35  ? 549 HOH B O   1 
HETATM 8780 O  O   . HOH VA 12 .   ? 0.787   -10.534 46.719 1.00 40.47  ? 550 HOH B O   1 
HETATM 8781 O  O   . HOH VA 12 .   ? 9.371   -24.209 69.050 1.00 45.61  ? 551 HOH B O   1 
HETATM 8782 O  O   . HOH VA 12 .   ? 12.621  -29.923 62.694 1.00 46.32  ? 552 HOH B O   1 
HETATM 8783 O  O   . HOH VA 12 .   ? 30.186  -9.965  58.588 1.00 43.14  ? 553 HOH B O   1 
HETATM 8784 O  O   . HOH VA 12 .   ? 19.121  -14.914 72.591 1.00 38.37  ? 554 HOH B O   1 
HETATM 8785 O  O   . HOH VA 12 .   ? 5.173   -9.525  72.214 1.00 38.03  ? 555 HOH B O   1 
HETATM 8786 O  O   . HOH VA 12 .   ? 3.337   5.219   69.002 1.00 44.70  ? 556 HOH B O   1 
HETATM 8787 O  O   . HOH VA 12 .   ? 13.438  -2.969  59.244 1.00 33.99  ? 557 HOH B O   1 
HETATM 8788 O  O   . HOH VA 12 .   ? 25.188  -23.032 48.960 1.00 42.05  ? 558 HOH B O   1 
HETATM 8789 O  O   . HOH VA 12 .   ? 19.168  2.313   48.649 1.00 33.43  ? 559 HOH B O   1 
HETATM 8790 O  O   . HOH VA 12 .   ? 29.632  -18.933 58.767 1.00 51.20  ? 560 HOH B O   1 
HETATM 8791 O  O   . HOH VA 12 .   ? 20.665  -4.441  42.067 1.00 42.33  ? 561 HOH B O   1 
HETATM 8792 O  O   . HOH VA 12 .   ? 2.515   -0.717  73.402 1.00 51.38  ? 562 HOH B O   1 
HETATM 8793 O  O   . HOH VA 12 .   ? 23.576  -30.805 50.043 1.00 52.00  ? 563 HOH B O   1 
HETATM 8794 O  O   . HOH VA 12 .   ? -1.325  4.756   53.561 1.00 42.94  ? 564 HOH B O   1 
HETATM 8795 O  O   . HOH VA 12 .   ? 21.026  -5.922  57.420 1.00 36.29  ? 565 HOH B O   1 
HETATM 8796 O  O   . HOH VA 12 .   ? 21.766  3.177   40.674 1.00 43.99  ? 566 HOH B O   1 
HETATM 8797 O  O   . HOH VA 12 .   ? 28.299  -27.393 65.591 1.00 42.91  ? 567 HOH B O   1 
HETATM 8798 O  O   . HOH VA 12 .   ? 26.011  -13.015 49.560 1.00 48.67  ? 568 HOH B O   1 
HETATM 8799 O  O   . HOH VA 12 .   ? -12.496 -9.522  69.178 1.00 55.22  ? 569 HOH B O   1 
HETATM 8800 O  O   . HOH VA 12 .   ? 6.567   -11.005 73.842 1.00 39.92  ? 570 HOH B O   1 
HETATM 8801 O  O   . HOH VA 12 .   ? 10.808  -30.758 72.342 1.00 50.99  ? 571 HOH B O   1 
HETATM 8802 O  O   . HOH VA 12 .   ? -0.167  -16.878 41.166 1.00 45.00  ? 572 HOH B O   1 
HETATM 8803 O  O   . HOH VA 12 .   ? -1.937  -11.103 47.582 1.00 36.72  ? 573 HOH B O   1 
HETATM 8804 O  O   . HOH VA 12 .   ? 5.878   1.659   47.632 1.00 45.88  ? 574 HOH B O   1 
HETATM 8805 O  O   . HOH VA 12 .   ? 8.028   10.795  66.603 1.00 47.48  ? 575 HOH B O   1 
HETATM 8806 O  O   . HOH VA 12 .   ? -7.704  -5.784  50.651 1.00 46.40  ? 576 HOH B O   1 
HETATM 8807 O  O   . HOH VA 12 .   ? 0.507   -4.144  44.719 1.00 46.43  ? 577 HOH B O   1 
HETATM 8808 O  O   . HOH VA 12 .   ? -0.301  -22.333 69.709 1.00 46.76  ? 578 HOH B O   1 
HETATM 8809 O  O   . HOH VA 12 .   ? -7.090  -10.054 49.717 1.00 47.89  ? 579 HOH B O   1 
HETATM 8810 O  O   . HOH VA 12 .   ? 19.827  -12.690 71.318 1.00 39.12  ? 580 HOH B O   1 
HETATM 8811 O  O   . HOH VA 12 .   ? 11.351  -26.708 53.413 1.00 45.45  ? 581 HOH B O   1 
HETATM 8812 O  O   . HOH VA 12 .   ? 21.782  -15.421 73.716 1.00 53.46  ? 582 HOH B O   1 
HETATM 8813 O  O   . HOH VA 12 .   ? 6.387   8.669   51.663 1.00 47.73  ? 583 HOH B O   1 
HETATM 8814 O  O   . HOH VA 12 .   ? -13.476 -12.142 68.343 1.00 51.73  ? 584 HOH B O   1 
HETATM 8815 O  O   . HOH VA 12 .   ? 19.532  -2.840  60.427 1.00 48.34  ? 585 HOH B O   1 
HETATM 8816 O  O   . HOH VA 12 .   ? 21.454  -29.109 46.050 1.00 54.20  ? 586 HOH B O   1 
HETATM 8817 O  O   . HOH VA 12 .   ? -0.867  -11.248 78.540 1.00 51.54  ? 587 HOH B O   1 
HETATM 8818 O  O   . HOH VA 12 .   ? 23.921  -7.629  67.840 1.00 41.79  ? 588 HOH B O   1 
HETATM 8819 O  O   . HOH VA 12 .   ? 22.935  5.983   47.368 1.00 43.74  ? 589 HOH B O   1 
HETATM 8820 O  O   . HOH VA 12 .   ? -1.781  -14.519 38.065 1.00 50.59  ? 590 HOH B O   1 
HETATM 8821 O  O   . HOH VA 12 .   ? -6.176  -1.883  44.972 1.00 46.12  ? 591 HOH B O   1 
HETATM 8822 O  O   . HOH VA 12 .   ? 18.642  -6.674  56.361 1.00 33.08  ? 592 HOH B O   1 
HETATM 8823 O  O   . HOH VA 12 .   ? 5.703   -11.027 61.072 1.00 59.10  ? 593 HOH B O   1 
HETATM 8824 O  O   . HOH VA 12 .   ? -5.194  14.444  52.753 1.00 55.12  ? 594 HOH B O   1 
HETATM 8825 O  O   . HOH VA 12 .   ? -9.718  -3.412  74.556 1.00 51.11  ? 595 HOH B O   1 
HETATM 8826 O  O   . HOH VA 12 .   ? 17.457  3.630   62.731 1.00 51.31  ? 596 HOH B O   1 
HETATM 8827 O  O   . HOH VA 12 .   ? 7.097   -20.312 43.900 1.00 46.37  ? 597 HOH B O   1 
HETATM 8828 O  O   . HOH VA 12 .   ? 12.203  -26.939 40.827 1.00 48.45  ? 598 HOH B O   1 
HETATM 8829 O  O   . HOH VA 12 .   ? 6.947   -9.655  60.045 1.00 47.54  ? 599 HOH B O   1 
HETATM 8830 O  O   . HOH VA 12 .   ? 2.885   -8.283  72.428 1.00 41.11  ? 600 HOH B O   1 
HETATM 8831 O  O   . HOH VA 12 .   ? -10.047 5.445   75.280 1.00 62.48  ? 601 HOH B O   1 
HETATM 8832 O  O   . HOH VA 12 .   ? -3.841  -5.225  76.403 1.00 58.77  ? 602 HOH B O   1 
HETATM 8833 O  O   . HOH VA 12 .   ? -13.163 11.696  56.933 1.00 59.16  ? 603 HOH B O   1 
HETATM 8834 O  O   . HOH VA 12 .   ? 0.274   -5.989  39.152 1.00 49.14  ? 604 HOH B O   1 
HETATM 8835 O  O   . HOH VA 12 .   ? 19.352  3.431   60.439 1.00 45.88  ? 605 HOH B O   1 
HETATM 8836 O  O   . HOH VA 12 .   ? 7.892   -11.168 86.455 1.00 50.79  ? 606 HOH B O   1 
HETATM 8837 O  O   . HOH VA 12 .   ? -6.904  -18.880 60.901 1.00 54.52  ? 607 HOH B O   1 
HETATM 8838 O  O   . HOH VA 12 .   ? -1.854  -3.445  40.400 1.00 55.18  ? 608 HOH B O   1 
HETATM 8839 O  O   . HOH VA 12 .   ? -5.829  -9.927  75.294 1.00 53.53  ? 609 HOH B O   1 
HETATM 8840 O  O   . HOH VA 12 .   ? 14.371  -18.189 33.654 1.00 50.15  ? 610 HOH B O   1 
HETATM 8841 O  O   . HOH VA 12 .   ? 9.263   -28.150 49.050 1.00 52.24  ? 611 HOH B O   1 
HETATM 8842 O  O   . HOH VA 12 .   ? 23.896  -17.890 70.143 1.00 57.86  ? 612 HOH B O   1 
HETATM 8843 O  O   . HOH VA 12 .   ? -5.519  -15.173 53.394 1.00 52.92  ? 613 HOH B O   1 
HETATM 8844 O  O   . HOH VA 12 .   ? 21.599  -9.016  39.042 1.00 45.91  ? 614 HOH B O   1 
HETATM 8845 O  O   . HOH VA 12 .   ? 1.151   2.601   46.981 1.00 52.31  ? 615 HOH B O   1 
HETATM 8846 O  O   . HOH VA 12 .   ? 3.652   3.071   46.233 1.00 50.18  ? 616 HOH B O   1 
HETATM 8847 O  O   . HOH VA 12 .   ? 23.411  -3.919  60.091 1.00 41.25  ? 617 HOH B O   1 
HETATM 8848 O  O   . HOH VA 12 .   ? 4.182   -17.424 36.685 1.00 50.93  ? 618 HOH B O   1 
HETATM 8849 O  O   . HOH VA 12 .   ? 27.158  -21.412 66.046 1.00 41.64  ? 619 HOH B O   1 
HETATM 8850 O  O   . HOH VA 12 .   ? -10.031 -11.618 51.165 1.00 53.79  ? 620 HOH B O   1 
HETATM 8851 O  O   . HOH VA 12 .   ? -15.502 9.977   67.043 1.00 49.96  ? 621 HOH B O   1 
HETATM 8852 O  O   . HOH VA 12 .   ? -6.883  18.394  64.838 1.00 46.70  ? 622 HOH B O   1 
HETATM 8853 O  O   . HOH VA 12 .   ? -16.144 3.725   61.275 1.00 56.11  ? 623 HOH B O   1 
HETATM 8854 O  O   . HOH VA 12 .   ? 20.817  -0.900  61.752 1.00 53.88  ? 624 HOH B O   1 
HETATM 8855 O  O   . HOH VA 12 .   ? -1.593  -2.651  44.635 1.00 56.40  ? 625 HOH B O   1 
HETATM 8856 O  O   . HOH VA 12 .   ? -13.943 -14.807 67.864 1.00 59.83  ? 626 HOH B O   1 
HETATM 8857 O  O   . HOH VA 12 .   ? -6.749  -6.369  76.470 1.00 63.72  ? 627 HOH B O   1 
HETATM 8858 O  O   . HOH VA 12 .   ? 6.987   15.235  57.138 1.00 52.91  ? 628 HOH B O   1 
HETATM 8859 O  O   . HOH VA 12 .   ? 0.242   15.187  67.143 1.00 54.53  ? 629 HOH B O   1 
HETATM 8860 O  O   . HOH VA 12 .   ? 8.790   -30.731 59.584 1.00 55.22  ? 630 HOH B O   1 
HETATM 8861 O  O   . HOH VA 12 .   ? 24.252  -7.409  70.880 1.00 46.76  ? 631 HOH B O   1 
HETATM 8862 O  O   . HOH VA 12 .   ? 7.747   9.460   49.573 1.00 55.53  ? 632 HOH B O   1 
HETATM 8863 O  O   . HOH VA 12 .   ? 26.152  -4.984  47.968 1.00 47.26  ? 633 HOH B O   1 
HETATM 8864 O  O   . HOH VA 12 .   ? 17.153  -19.942 40.505 1.00 58.53  ? 634 HOH B O   1 
HETATM 8865 O  O   . HOH VA 12 .   ? -11.239 -21.690 74.614 1.00 57.22  ? 635 HOH B O   1 
HETATM 8866 O  O   . HOH VA 12 .   ? 29.030  -6.390  56.531 1.00 45.47  ? 636 HOH B O   1 
HETATM 8867 O  O   . HOH VA 12 .   ? 14.430  -5.198  33.393 1.00 52.47  ? 637 HOH B O   1 
HETATM 8868 O  O   . HOH VA 12 .   ? 6.322   0.448   74.334 1.00 48.84  ? 638 HOH B O   1 
HETATM 8869 O  O   . HOH VA 12 .   ? 18.046  2.733   33.951 1.00 59.00  ? 639 HOH B O   1 
HETATM 8870 O  O   . HOH VA 12 .   ? 4.754   -25.965 53.252 1.00 53.60  ? 640 HOH B O   1 
HETATM 8871 O  O   . HOH VA 12 .   ? 21.926  2.732   59.668 1.00 55.56  ? 641 HOH B O   1 
HETATM 8872 O  O   . HOH VA 12 .   ? 6.017   -22.377 44.489 1.00 55.76  ? 642 HOH B O   1 
HETATM 8873 O  O   . HOH VA 12 .   ? 4.109   -21.445 48.969 1.00 58.06  ? 643 HOH B O   1 
HETATM 8874 O  O   . HOH VA 12 .   ? -3.897  -12.692 46.526 1.00 45.43  ? 644 HOH B O   1 
HETATM 8875 O  O   . HOH VA 12 .   ? 9.493   3.897   73.780 1.00 55.58  ? 645 HOH B O   1 
HETATM 8876 O  O   . HOH VA 12 .   ? 8.636   -25.960 53.154 1.00 51.78  ? 646 HOH B O   1 
HETATM 8877 O  O   . HOH VA 12 .   ? 18.676  -35.875 50.109 1.00 51.31  ? 647 HOH B O   1 
HETATM 8878 O  O   . HOH WA 12 .   ? 12.314  3.567   14.517 1.00 35.39  ? 501 HOH C O   1 
HETATM 8879 O  O   . HOH WA 12 .   ? -8.358  18.241  27.698 1.00 44.69  ? 502 HOH C O   1 
HETATM 8880 O  O   . HOH WA 12 .   ? -25.478 -1.045  11.343 1.00 48.45  ? 503 HOH C O   1 
HETATM 8881 O  O   . HOH WA 12 .   ? -10.693 30.113  12.755 1.00 55.06  ? 504 HOH C O   1 
HETATM 8882 O  O   . HOH WA 12 .   ? 11.263  -1.879  30.690 1.00 44.02  ? 505 HOH C O   1 
HETATM 8883 O  O   . HOH WA 12 .   ? 5.152   -0.195  25.826 1.00 34.06  ? 506 HOH C O   1 
HETATM 8884 O  O   . HOH WA 12 .   ? -0.369  -10.250 16.603 1.00 49.33  ? 507 HOH C O   1 
HETATM 8885 O  O   . HOH WA 12 .   ? -7.785  13.520  26.493 1.00 48.29  ? 508 HOH C O   1 
HETATM 8886 O  O   . HOH WA 12 .   ? 1.803   -5.057  13.594 1.00 38.18  ? 509 HOH C O   1 
HETATM 8887 O  O   . HOH WA 12 .   ? -1.436  5.809   1.515  1.00 41.43  ? 510 HOH C O   1 
HETATM 8888 O  O   . HOH WA 12 .   ? 2.996   -5.027  16.159 1.00 36.74  ? 511 HOH C O   1 
HETATM 8889 O  O   . HOH WA 12 .   ? -9.428  12.863  24.111 1.00 43.70  ? 512 HOH C O   1 
HETATM 8890 O  O   . HOH WA 12 .   ? 1.654   9.241   27.254 1.00 46.02  ? 513 HOH C O   1 
HETATM 8891 O  O   . HOH WA 12 .   ? -4.908  -3.238  4.121  1.00 54.36  ? 514 HOH C O   1 
HETATM 8892 O  O   . HOH WA 12 .   ? 10.488  -1.755  5.609  1.00 40.61  ? 515 HOH C O   1 
HETATM 8893 O  O   . HOH WA 12 .   ? -25.788 21.517  13.813 1.00 53.57  ? 516 HOH C O   1 
HETATM 8894 O  O   . HOH WA 12 .   ? -1.717  8.027   25.952 1.00 37.49  ? 517 HOH C O   1 
HETATM 8895 O  O   . HOH WA 12 .   ? -14.648 8.844   7.067  1.00 33.14  ? 518 HOH C O   1 
HETATM 8896 O  O   . HOH WA 12 .   ? -20.181 -3.980  23.756 1.00 41.54  ? 519 HOH C O   1 
HETATM 8897 O  O   . HOH WA 12 .   ? -21.091 1.160   23.056 1.00 37.84  ? 520 HOH C O   1 
HETATM 8898 O  O   . HOH WA 12 .   ? 4.044   -6.025  19.613 1.00 35.02  ? 521 HOH C O   1 
HETATM 8899 O  O   . HOH WA 12 .   ? -0.105  -6.423  14.955 1.00 38.38  ? 522 HOH C O   1 
HETATM 8900 O  O   . HOH WA 12 .   ? 14.818  4.282   32.397 1.00 39.85  ? 523 HOH C O   1 
HETATM 8901 O  O   . HOH WA 12 .   ? -7.260  15.742  27.953 1.00 48.32  ? 524 HOH C O   1 
HETATM 8902 O  O   . HOH WA 12 .   ? -10.001 -8.420  22.384 1.00 46.45  ? 525 HOH C O   1 
HETATM 8903 O  O   . HOH WA 12 .   ? 22.290  -7.040  29.636 1.00 40.06  ? 526 HOH C O   1 
HETATM 8904 O  O   . HOH WA 12 .   ? 13.913  1.399   13.936 1.00 33.31  ? 527 HOH C O   1 
HETATM 8905 O  O   . HOH WA 12 .   ? -0.348  17.765  27.566 1.00 53.43  ? 528 HOH C O   1 
HETATM 8906 O  O   . HOH WA 12 .   ? -12.698 17.139  4.397  1.00 44.60  ? 529 HOH C O   1 
HETATM 8907 O  O   . HOH WA 12 .   ? 7.028   16.322  26.047 1.00 47.10  ? 530 HOH C O   1 
HETATM 8908 O  O   . HOH WA 12 .   ? 0.610   3.667   2.186  1.00 45.57  ? 531 HOH C O   1 
HETATM 8909 O  O   . HOH WA 12 .   ? -0.025  -5.848  30.062 1.00 42.59  ? 532 HOH C O   1 
HETATM 8910 O  O   . HOH WA 12 .   ? 16.748  -0.873  16.888 1.00 32.72  ? 533 HOH C O   1 
HETATM 8911 O  O   . HOH WA 12 .   ? -3.160  18.006  32.834 1.00 47.91  ? 534 HOH C O   1 
HETATM 8912 O  O   . HOH WA 12 .   ? -7.619  13.579  1.780  1.00 50.81  ? 535 HOH C O   1 
HETATM 8913 O  O   . HOH WA 12 .   ? -26.992 8.541   19.802 1.00 52.56  ? 536 HOH C O   1 
HETATM 8914 O  O   . HOH WA 12 .   ? -10.187 5.607   23.160 1.00 43.06  ? 537 HOH C O   1 
HETATM 8915 O  O   . HOH WA 12 .   ? 2.712   7.170   27.444 1.00 42.09  ? 538 HOH C O   1 
HETATM 8916 O  O   . HOH WA 12 .   ? -7.509  4.548   3.888  1.00 33.31  ? 539 HOH C O   1 
HETATM 8917 O  O   . HOH WA 12 .   ? -1.547  10.159  12.497 1.00 56.01  ? 540 HOH C O   1 
HETATM 8918 O  O   . HOH WA 12 .   ? -4.706  15.656  29.692 1.00 50.10  ? 541 HOH C O   1 
HETATM 8919 O  O   . HOH WA 12 .   ? 5.722   -4.552  26.533 1.00 36.53  ? 542 HOH C O   1 
HETATM 8920 O  O   . HOH WA 12 .   ? 4.437   0.994   28.365 1.00 38.11  ? 543 HOH C O   1 
HETATM 8921 O  O   . HOH WA 12 .   ? 22.483  -5.442  16.099 1.00 44.69  ? 544 HOH C O   1 
HETATM 8922 O  O   . HOH WA 12 .   ? -12.411 13.801  3.525  1.00 42.81  ? 545 HOH C O   1 
HETATM 8923 O  O   . HOH WA 12 .   ? -11.918 -3.909  10.889 1.00 41.29  ? 546 HOH C O   1 
HETATM 8924 O  O   . HOH WA 12 .   ? 19.513  5.812   9.204  1.00 48.29  ? 547 HOH C O   1 
HETATM 8925 O  O   . HOH WA 12 .   ? -17.705 9.257   28.153 1.00 48.43  ? 548 HOH C O   1 
HETATM 8926 O  O   . HOH WA 12 .   ? -2.356  -1.349  26.796 1.00 37.20  ? 549 HOH C O   1 
HETATM 8927 O  O   . HOH WA 12 .   ? 11.970  -10.975 26.819 1.00 44.59  ? 550 HOH C O   1 
HETATM 8928 O  O   . HOH WA 12 .   ? -4.826  4.687   2.921  1.00 34.06  ? 551 HOH C O   1 
HETATM 8929 O  O   . HOH WA 12 .   ? 16.308  12.838  9.776  1.00 50.04  ? 552 HOH C O   1 
HETATM 8930 O  O   . HOH WA 12 .   ? -7.639  -2.151  5.595  1.00 50.62  ? 553 HOH C O   1 
HETATM 8931 O  O   . HOH WA 12 .   ? 14.540  -1.024  14.993 1.00 37.97  ? 554 HOH C O   1 
HETATM 8932 O  O   . HOH WA 12 .   ? -19.968 -2.956  21.332 1.00 48.77  ? 555 HOH C O   1 
HETATM 8933 O  O   . HOH WA 12 .   ? 14.123  -7.995  28.666 1.00 48.52  ? 556 HOH C O   1 
HETATM 8934 O  O   . HOH WA 12 .   ? 15.905  11.481  12.445 1.00 59.46  ? 557 HOH C O   1 
HETATM 8935 O  O   . HOH WA 12 .   ? 16.486  -10.610 20.592 1.00 46.57  ? 558 HOH C O   1 
HETATM 8936 O  O   . HOH WA 12 .   ? 20.983  4.558   15.993 1.00 49.37  ? 559 HOH C O   1 
HETATM 8937 O  O   . HOH WA 12 .   ? -19.127 -8.580  17.454 1.00 63.07  ? 560 HOH C O   1 
HETATM 8938 O  O   . HOH WA 12 .   ? 2.678   18.120  25.946 1.00 42.31  ? 561 HOH C O   1 
HETATM 8939 O  O   . HOH WA 12 .   ? -14.481 -6.009  10.362 1.00 54.64  ? 562 HOH C O   1 
HETATM 8940 O  O   . HOH WA 12 .   ? 5.867   -6.804  27.499 1.00 43.34  ? 563 HOH C O   1 
HETATM 8941 O  O   . HOH WA 12 .   ? 3.031   -15.468 16.546 1.00 48.85  ? 564 HOH C O   1 
HETATM 8942 O  O   . HOH WA 12 .   ? 16.788  9.821   20.538 1.00 56.88  ? 565 HOH C O   1 
HETATM 8943 O  O   . HOH WA 12 .   ? 11.777  19.192  24.153 1.00 51.82  ? 566 HOH C O   1 
HETATM 8944 O  O   . HOH WA 12 .   ? -16.294 8.244   21.874 1.00 49.52  ? 567 HOH C O   1 
HETATM 8945 O  O   . HOH WA 12 .   ? -15.348 13.171  0.866  1.00 49.42  ? 568 HOH C O   1 
HETATM 8946 O  O   . HOH WA 12 .   ? 21.050  -12.054 13.893 1.00 47.59  ? 569 HOH C O   1 
HETATM 8947 O  O   . HOH WA 12 .   ? -11.004 2.602   30.592 1.00 51.99  ? 570 HOH C O   1 
HETATM 8948 O  O   . HOH WA 12 .   ? 16.972  5.805   7.043  1.00 42.99  ? 571 HOH C O   1 
HETATM 8949 O  O   . HOH WA 12 .   ? -5.014  10.642  16.950 1.00 60.67  ? 572 HOH C O   1 
HETATM 8950 O  O   . HOH WA 12 .   ? 5.349   14.427  24.249 1.00 45.13  ? 573 HOH C O   1 
HETATM 8951 O  O   . HOH WA 12 .   ? -1.892  -8.789  14.333 1.00 44.65  ? 574 HOH C O   1 
HETATM 8952 O  O   . HOH WA 12 .   ? -9.111  -9.795  13.044 1.00 51.09  ? 575 HOH C O   1 
HETATM 8953 O  O   . HOH WA 12 .   ? -7.973  -4.679  1.306  1.00 44.41  ? 576 HOH C O   1 
HETATM 8954 O  O   . HOH WA 12 .   ? 13.115  11.789  25.234 1.00 53.33  ? 577 HOH C O   1 
HETATM 8955 O  O   . HOH WA 12 .   ? -27.246 10.795  13.605 1.00 61.38  ? 578 HOH C O   1 
HETATM 8956 O  O   . HOH WA 12 .   ? 15.290  -3.397  11.691 1.00 66.14  ? 579 HOH C O   1 
HETATM 8957 O  O   . HOH WA 12 .   ? -0.352  -4.118  32.233 1.00 49.81  ? 580 HOH C O   1 
HETATM 8958 O  O   . HOH WA 12 .   ? -16.571 6.480   -4.324 1.00 40.54  ? 581 HOH C O   1 
HETATM 8959 O  O   . HOH WA 12 .   ? -0.589  12.481  7.818  1.00 50.60  ? 582 HOH C O   1 
HETATM 8960 O  O   . HOH WA 12 .   ? -1.764  -5.582  3.083  1.00 43.46  ? 583 HOH C O   1 
HETATM 8961 O  O   . HOH WA 12 .   ? -25.767 17.052  24.019 1.00 55.16  ? 584 HOH C O   1 
HETATM 8962 O  O   . HOH WA 12 .   ? 16.224  14.011  7.302  1.00 56.94  ? 585 HOH C O   1 
HETATM 8963 O  O   . HOH WA 12 .   ? -7.555  -9.679  19.547 1.00 64.96  ? 586 HOH C O   1 
HETATM 8964 O  O   . HOH WA 12 .   ? -18.822 -5.276  5.989  1.00 56.34  ? 587 HOH C O   1 
HETATM 8965 O  O   . HOH WA 12 .   ? 12.664  -14.540 25.692 1.00 48.97  ? 588 HOH C O   1 
HETATM 8966 O  O   . HOH WA 12 .   ? -14.673 -5.615  8.033  1.00 51.90  ? 589 HOH C O   1 
HETATM 8967 O  O   . HOH WA 12 .   ? -25.945 -4.140  4.916  1.00 56.74  ? 590 HOH C O   1 
HETATM 8968 O  O   . HOH WA 12 .   ? -17.824 -0.153  31.043 1.00 54.65  ? 591 HOH C O   1 
HETATM 8969 O  O   . HOH WA 12 .   ? -15.791 24.380  -0.620 1.00 60.99  ? 592 HOH C O   1 
HETATM 8970 O  O   . HOH WA 12 .   ? -9.264  29.607  7.958  1.00 55.99  ? 593 HOH C O   1 
HETATM 8971 O  O   . HOH WA 12 .   ? -3.340  11.270  15.753 1.00 62.33  ? 594 HOH C O   1 
HETATM 8972 O  O   . HOH WA 12 .   ? -3.635  5.697   0.479  1.00 42.83  ? 595 HOH C O   1 
HETATM 8973 O  O   . HOH WA 12 .   ? -7.998  -10.727 24.330 1.00 54.44  ? 596 HOH C O   1 
HETATM 8974 O  O   . HOH WA 12 .   ? -2.700  -12.744 26.615 1.00 55.88  ? 597 HOH C O   1 
HETATM 8975 O  O   . HOH WA 12 .   ? 13.998  14.974  0.692  1.00 62.98  ? 598 HOH C O   1 
HETATM 8976 O  O   . HOH WA 12 .   ? 13.336  -5.025  11.398 1.00 54.34  ? 599 HOH C O   1 
HETATM 8977 O  O   . HOH WA 12 .   ? -32.588 -2.566  10.235 1.00 56.32  ? 600 HOH C O   1 
# 
