data_9HEB
# 
_entry.id   9HEB 
# 
_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   9HEB         pdb_00009heb 10.2210/pdb9heb/pdb 
WWPDB D_1292136448 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Source and taxonomy' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' entity_src_gen        
2 2 'Structure model' pdbx_database_related 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_entity_src_gen.gene_src_common_name' 
2 2 'Structure model' '_entity_src_gen.host_org_common_name' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HEB 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9HE6 unspecified 
PDB . 9HE7 unspecified 
PDB . 9HE9 unspecified 
PDB . 9HEA unspecified 
PDB . 9HEC unspecified 
PDB . 9HED unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xjulia@iqfr.csic.es 
_pdbx_contact_author.name_first         Julia 
_pdbx_contact_author.name_last          Sanz-Aparicio 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6849-8621 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fernandez-Garcia, A.' 1 0000-0003-2052-6483 
'Sanz-Aparicio, J.'    2 0000-0002-6849-8621 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Characterization of Recombinant Unspecific Peroxygenase from Candolleomyces aberdarensis through Crystallographic and Substrate Selectivity Studies
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202402015 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Menes-Rubio, A.'      1 ? 
primary 'Fernandez-Garcia, A.' 2 ? 
primary 'Monterrey, D.T.'      3 ? 
primary 'de Santos, P.G.'      4 ? 
primary 'Sanchez-Moreno, I.'   5 ? 
primary 'Sanz-Aparicio, J.'    6 ? 
primary 'Alcalde, M.'          7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Heme-thiolate peroxidase' 36630.445 3   1.11.2.1 ? ? ? 
2  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   2   ?        ? ? ? 
3  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1235.105  1   ?        ? ? ? 
4  branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1   ?        ? ? ? 
5  branched    man 
;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1   ?        ? ? ? 
6  branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   1   
?        ? ? ? 
7  non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
8  non-polymer syn GLYCEROL 92.094    5   ?        ? ? ? 
9  non-polymer syn TETRADECANE 198.388   2   ?        ? ? ? 
10 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   5   ?        ? ? ? 
11 non-polymer syn 'SULFATE ION' 96.063    5   ?        ? ? ? 
12 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
13 non-polymer syn 'ACETATE ION' 59.044    1   ?        ? ? ? 
14 water       nat water 18.015    317 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
7  'PROTOPORPHYRIN IX CONTAINING FE'                     HEM 
8  GLYCEROL                                              GOL 
9  TETRADECANE                                           C14 
10 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
11 'SULFATE ION'                                         SO4 
12 'MAGNESIUM ION'                                       MG  
13 'ACETATE ION'                                         ACT 
14 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   GLY n 
1 3   VAL n 
1 4   ASP n 
1 5   PRO n 
1 6   PRO n 
1 7   PRO n 
1 8   PRO n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  PRO n 
1 13  SER n 
1 14  PHE n 
1 15  THR n 
1 16  GLY n 
1 17  THR n 
1 18  LYS n 
1 19  LEU n 
1 20  VAL n 
1 21  ASN n 
1 22  ASP n 
1 23  ALA n 
1 24  ASP n 
1 25  HIS n 
1 26  PRO n 
1 27  TRP n 
1 28  GLN n 
1 29  PRO n 
1 30  LEU n 
1 31  ARG n 
1 32  GLU n 
1 33  GLY n 
1 34  ASP n 
1 35  ILE n 
1 36  ARG n 
1 37  GLY n 
1 38  PRO n 
1 39  CYS n 
1 40  PRO n 
1 41  GLY n 
1 42  LEU n 
1 43  ASN n 
1 44  THR n 
1 45  LEU n 
1 46  ALA n 
1 47  SER n 
1 48  HIS n 
1 49  GLY n 
1 50  TYR n 
1 51  LEU n 
1 52  PRO n 
1 53  ARG n 
1 54  ASP n 
1 55  GLY n 
1 56  VAL n 
1 57  ALA n 
1 58  THR n 
1 59  PRO n 
1 60  ALA n 
1 61  GLN n 
1 62  ILE n 
1 63  ILE n 
1 64  THR n 
1 65  ALA n 
1 66  THR n 
1 67  GLN n 
1 68  GLU n 
1 69  GLY n 
1 70  PHE n 
1 71  ASN n 
1 72  PHE n 
1 73  GLU n 
1 74  ASN n 
1 75  ASN n 
1 76  ALA n 
1 77  ALA n 
1 78  ILE n 
1 79  VAL n 
1 80  ALA n 
1 81  THR n 
1 82  TYR n 
1 83  LEU n 
1 84  GLY n 
1 85  HIS n 
1 86  LEU n 
1 87  LEU n 
1 88  ASN n 
1 89  GLY n 
1 90  ASN n 
1 91  LEU n 
1 92  VAL n 
1 93  THR n 
1 94  ASP n 
1 95  LEU n 
1 96  LEU n 
1 97  SER n 
1 98  ILE n 
1 99  GLY n 
1 100 GLY n 
1 101 ALA n 
1 102 THR n 
1 103 PRO n 
1 104 LYS n 
1 105 THR n 
1 106 GLY n 
1 107 PRO n 
1 108 PRO n 
1 109 PRO n 
1 110 PRO n 
1 111 PRO n 
1 112 PRO n 
1 113 ALA n 
1 114 HIS n 
1 115 ALA n 
1 116 GLY n 
1 117 GLY n 
1 118 LEU n 
1 119 ASN n 
1 120 VAL n 
1 121 HIS n 
1 122 GLY n 
1 123 THR n 
1 124 PHE n 
1 125 GLU n 
1 126 GLY n 
1 127 ASP n 
1 128 ALA n 
1 129 GLY n 
1 130 MET n 
1 131 THR n 
1 132 ARG n 
1 133 ALA n 
1 134 ASP n 
1 135 GLU n 
1 136 PHE n 
1 137 PHE n 
1 138 GLY n 
1 139 ASP n 
1 140 ASN n 
1 141 HIS n 
1 142 SER n 
1 143 PHE n 
1 144 ASN n 
1 145 GLN n 
1 146 THR n 
1 147 LEU n 
1 148 PHE n 
1 149 ASP n 
1 150 LYS n 
1 151 PHE n 
1 152 VAL n 
1 153 ASP n 
1 154 PHE n 
1 155 SER n 
1 156 ASN n 
1 157 ARG n 
1 158 TYR n 
1 159 GLY n 
1 160 GLY n 
1 161 GLY n 
1 162 PHE n 
1 163 TYR n 
1 164 ASN n 
1 165 LEU n 
1 166 THR n 
1 167 VAL n 
1 168 ALA n 
1 169 GLY n 
1 170 GLU n 
1 171 LEU n 
1 172 ARG n 
1 173 TYR n 
1 174 SER n 
1 175 ARG n 
1 176 ILE n 
1 177 GLN n 
1 178 ASP n 
1 179 SER n 
1 180 ILE n 
1 181 ALA n 
1 182 THR n 
1 183 ASN n 
1 184 PRO n 
1 185 GLU n 
1 186 PHE n 
1 187 GLN n 
1 188 PHE n 
1 189 LYS n 
1 190 ASN n 
1 191 VAL n 
1 192 ARG n 
1 193 PHE n 
1 194 ILE n 
1 195 THR n 
1 196 ALA n 
1 197 TYR n 
1 198 GLY n 
1 199 GLU n 
1 200 THR n 
1 201 VAL n 
1 202 PHE n 
1 203 PRO n 
1 204 ILE n 
1 205 ASN n 
1 206 LEU n 
1 207 PHE n 
1 208 VAL n 
1 209 ASP n 
1 210 GLY n 
1 211 ARG n 
1 212 VAL n 
1 213 THR n 
1 214 THR n 
1 215 ASP n 
1 216 ARG n 
1 217 LYS n 
1 218 LEU n 
1 219 SER n 
1 220 MET n 
1 221 GLU n 
1 222 ASP n 
1 223 ALA n 
1 224 ALA n 
1 225 SER n 
1 226 ILE n 
1 227 PHE n 
1 228 ARG n 
1 229 ASP n 
1 230 MET n 
1 231 ARG n 
1 232 PHE n 
1 233 PRO n 
1 234 ASP n 
1 235 ASP n 
1 236 PHE n 
1 237 HIS n 
1 238 ARG n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 PRO n 
1 243 ALA n 
1 244 SER n 
1 245 ASN n 
1 246 GLU n 
1 247 GLY n 
1 248 ALA n 
1 249 ASP n 
1 250 GLN n 
1 251 VAL n 
1 252 LEU n 
1 253 ALA n 
1 254 ALA n 
1 255 HIS n 
1 256 PRO n 
1 257 TRP n 
1 258 VAL n 
1 259 PRO n 
1 260 GLY n 
1 261 GLY n 
1 262 ASN n 
1 263 ALA n 
1 264 ASP n 
1 265 ASN n 
1 266 GLN n 
1 267 VAL n 
1 268 ASN n 
1 269 ASN n 
1 270 TYR n 
1 271 VAL n 
1 272 GLU n 
1 273 ASP n 
1 274 PRO n 
1 275 ASP n 
1 276 SER n 
1 277 ALA n 
1 278 ASP n 
1 279 PHE n 
1 280 THR n 
1 281 HIS n 
1 282 LEU n 
1 283 CYS n 
1 284 ARG n 
1 285 LEU n 
1 286 TYR n 
1 287 GLU n 
1 288 PHE n 
1 289 VAL n 
1 290 VAL n 
1 291 GLY n 
1 292 SER n 
1 293 VAL n 
1 294 GLN n 
1 295 GLU n 
1 296 LEU n 
1 297 TYR n 
1 298 PRO n 
1 299 ASN n 
1 300 PRO n 
1 301 THR n 
1 302 GLY n 
1 303 ILE n 
1 304 LEU n 
1 305 ARG n 
1 306 ARG n 
1 307 ASN n 
1 308 LEU n 
1 309 ILE n 
1 310 LYS n 
1 311 ASN n 
1 312 LEU n 
1 313 HIS n 
1 314 TYR n 
1 315 TRP n 
1 316 TRP n 
1 317 THR n 
1 318 GLY n 
1 319 VAL n 
1 320 ASN n 
1 321 VAL n 
1 322 ALA n 
1 323 PHE n 
1 324 GLY n 
1 325 GLY n 
1 326 CYS n 
1 327 ASP n 
1 328 GLU n 
1 329 LEU n 
1 330 PHE n 
1 331 PRO n 
1 332 TYR n 
1 333 GLY n 
1 334 GLN n 
1 335 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   335 
_entity_src_gen.gene_src_common_name               'basidiomycete fungi' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EST38_g8238 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Candolleomyces aberdarensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2316362 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               yeast 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella phaffii CBS 7435' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     981350 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
6 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1  2 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
2  2 'WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1' WURCS PDB2Glycan 
1.1.0 
3  2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}' LINUCS PDB-CARE   ? 
4  3 'DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
5  3 'WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1' 
WURCS                       PDB2Glycan 1.1.0 
6  3 
;[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}
;
LINUCS                      PDB-CARE   ?     
7  4 'DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
8  4 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1' WURCS 
PDB2Glycan 1.1.0 
9  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
10 5 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1' WURCS PDB2Glycan 1.1.0 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   
?     
13 6 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}' LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3  2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4  2 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
5  3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
7  3 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
8  3 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
9  3 6 MAN C1 O1 4 MAN O6 HO6 sing ? 
10 3 7 MAN C1 O1 3 BMA O3 HO3 sing ? 
11 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
12 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
13 4 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
14 4 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
15 4 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
16 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
17 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
18 5 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
19 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
20 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer                   . 'ACETATE ION'                                         ? 'C2 H3 O2 -1'      59.044  
ALA 'L-peptide linking'           y ALANINE                                               ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking'           y ARGININE                                              ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking'           y ASPARAGINE                                            ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                                       ? 'C4 H7 N O4'       133.103 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                                  'beta-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
C14 non-polymer                   . TETRADECANE                                           ? 'C14 H30'          198.388 
CYS 'L-peptide linking'           y CYSTEINE                                              ? 'C3 H7 N O2 S'     121.158 
EPE non-polymer                   . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'   238.305 
GLN 'L-peptide linking'           y GLUTAMINE                                             ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'             y GLYCINE                                               ? 'C2 H5 N O2'       75.067  
GOL non-polymer                   . GLYCEROL                                              'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'         92.094  
HEM non-polymer                   . 'PROTOPORPHYRIN IX CONTAINING FE'                     HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking'           y HISTIDINE                                             ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer                   . WATER                                                 ? 'H2 O'             18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                                            ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking'           y LEUCINE                                               ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking'           y LYSINE                                                ? 'C6 H15 N2 O2 1'   147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                                 'alpha-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
MET 'L-peptide linking'           y METHIONINE                                            ? 'C5 H11 N O2 S'    149.211 
MG  non-polymer                   . 'MAGNESIUM ION'                                       ? 'Mg 2'             24.305  
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose              
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                                         ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking'           y PROLINE                                               ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking'           y SERINE                                                ? 'C3 H7 N O3'       105.093 
SO4 non-polymer                   . 'SULFATE ION'                                         ? 'O4 S -2'          96.063  
THR 'L-peptide linking'           y THREONINE                                             ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking'           y TYROSINE                                              ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking'           y VALINE                                                ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   14  14  GLN GLN A . n 
A 1 2   GLY 2   15  15  GLY GLY A . n 
A 1 3   VAL 3   16  16  VAL VAL A . n 
A 1 4   ASP 4   17  17  ASP ASP A . n 
A 1 5   PRO 5   18  18  PRO PRO A . n 
A 1 6   PRO 6   19  19  PRO PRO A . n 
A 1 7   PRO 7   20  20  PRO PRO A . n 
A 1 8   PRO 8   21  21  PRO PRO A . n 
A 1 9   PRO 9   22  22  PRO PRO A . n 
A 1 10  GLY 10  23  23  GLY GLY A . n 
A 1 11  PRO 11  24  24  PRO PRO A . n 
A 1 12  PRO 12  25  25  PRO PRO A . n 
A 1 13  SER 13  26  26  SER SER A . n 
A 1 14  PHE 14  27  27  PHE PHE A . n 
A 1 15  THR 15  28  28  THR THR A . n 
A 1 16  GLY 16  29  29  GLY GLY A . n 
A 1 17  THR 17  30  30  THR THR A . n 
A 1 18  LYS 18  31  31  LYS LYS A . n 
A 1 19  LEU 19  32  32  LEU LEU A . n 
A 1 20  VAL 20  33  33  VAL VAL A . n 
A 1 21  ASN 21  34  34  ASN ASN A . n 
A 1 22  ASP 22  35  35  ASP ASP A . n 
A 1 23  ALA 23  36  36  ALA ALA A . n 
A 1 24  ASP 24  37  37  ASP ASP A . n 
A 1 25  HIS 25  38  38  HIS HIS A . n 
A 1 26  PRO 26  39  39  PRO PRO A . n 
A 1 27  TRP 27  40  40  TRP TRP A . n 
A 1 28  GLN 28  41  41  GLN GLN A . n 
A 1 29  PRO 29  42  42  PRO PRO A . n 
A 1 30  LEU 30  43  43  LEU LEU A . n 
A 1 31  ARG 31  44  44  ARG ARG A . n 
A 1 32  GLU 32  45  45  GLU GLU A . n 
A 1 33  GLY 33  46  46  GLY GLY A . n 
A 1 34  ASP 34  47  47  ASP ASP A . n 
A 1 35  ILE 35  48  48  ILE ILE A . n 
A 1 36  ARG 36  49  49  ARG ARG A . n 
A 1 37  GLY 37  50  50  GLY GLY A . n 
A 1 38  PRO 38  51  51  PRO PRO A . n 
A 1 39  CYS 39  52  52  CYS CYS A . n 
A 1 40  PRO 40  53  53  PRO PRO A . n 
A 1 41  GLY 41  54  54  GLY GLY A . n 
A 1 42  LEU 42  55  55  LEU LEU A . n 
A 1 43  ASN 43  56  56  ASN ASN A . n 
A 1 44  THR 44  57  57  THR THR A . n 
A 1 45  LEU 45  58  58  LEU LEU A . n 
A 1 46  ALA 46  59  59  ALA ALA A . n 
A 1 47  SER 47  60  60  SER SER A . n 
A 1 48  HIS 48  61  61  HIS HIS A . n 
A 1 49  GLY 49  62  62  GLY GLY A . n 
A 1 50  TYR 50  63  63  TYR TYR A . n 
A 1 51  LEU 51  64  64  LEU LEU A . n 
A 1 52  PRO 52  65  65  PRO PRO A . n 
A 1 53  ARG 53  66  66  ARG ARG A . n 
A 1 54  ASP 54  67  67  ASP ASP A . n 
A 1 55  GLY 55  68  68  GLY GLY A . n 
A 1 56  VAL 56  69  69  VAL VAL A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  THR 58  71  71  THR THR A . n 
A 1 59  PRO 59  72  72  PRO PRO A . n 
A 1 60  ALA 60  73  73  ALA ALA A . n 
A 1 61  GLN 61  74  74  GLN GLN A . n 
A 1 62  ILE 62  75  75  ILE ILE A . n 
A 1 63  ILE 63  76  76  ILE ILE A . n 
A 1 64  THR 64  77  77  THR THR A . n 
A 1 65  ALA 65  78  78  ALA ALA A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  GLN 67  80  80  GLN GLN A . n 
A 1 68  GLU 68  81  81  GLU GLU A . n 
A 1 69  GLY 69  82  82  GLY GLY A . n 
A 1 70  PHE 70  83  83  PHE PHE A . n 
A 1 71  ASN 71  84  84  ASN ASN A . n 
A 1 72  PHE 72  85  85  PHE PHE A . n 
A 1 73  GLU 73  86  86  GLU GLU A . n 
A 1 74  ASN 74  87  87  ASN ASN A . n 
A 1 75  ASN 75  88  88  ASN ASN A . n 
A 1 76  ALA 76  89  89  ALA ALA A . n 
A 1 77  ALA 77  90  90  ALA ALA A . n 
A 1 78  ILE 78  91  91  ILE ILE A . n 
A 1 79  VAL 79  92  92  VAL VAL A . n 
A 1 80  ALA 80  93  93  ALA ALA A . n 
A 1 81  THR 81  94  94  THR THR A . n 
A 1 82  TYR 82  95  95  TYR TYR A . n 
A 1 83  LEU 83  96  96  LEU LEU A . n 
A 1 84  GLY 84  97  97  GLY GLY A . n 
A 1 85  HIS 85  98  98  HIS HIS A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  LEU 87  100 100 LEU LEU A . n 
A 1 88  ASN 88  101 101 ASN ASN A . n 
A 1 89  GLY 89  102 102 GLY GLY A . n 
A 1 90  ASN 90  103 103 ASN ASN A . n 
A 1 91  LEU 91  104 104 LEU LEU A . n 
A 1 92  VAL 92  105 105 VAL VAL A . n 
A 1 93  THR 93  106 106 THR THR A . n 
A 1 94  ASP 94  107 107 ASP ASP A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LEU 96  109 109 LEU LEU A . n 
A 1 97  SER 97  110 110 SER SER A . n 
A 1 98  ILE 98  111 111 ILE ILE A . n 
A 1 99  GLY 99  112 112 GLY GLY A . n 
A 1 100 GLY 100 113 113 GLY GLY A . n 
A 1 101 ALA 101 114 114 ALA ALA A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 PRO 103 116 116 PRO PRO A . n 
A 1 104 LYS 104 117 117 LYS LYS A . n 
A 1 105 THR 105 118 118 THR THR A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 PRO 107 120 120 PRO PRO A . n 
A 1 108 PRO 108 121 121 PRO PRO A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PRO 110 123 123 PRO PRO A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 PRO 112 125 125 PRO PRO A . n 
A 1 113 ALA 113 126 126 ALA ALA A . n 
A 1 114 HIS 114 127 127 HIS HIS A . n 
A 1 115 ALA 115 128 128 ALA ALA A . n 
A 1 116 GLY 116 129 129 GLY GLY A . n 
A 1 117 GLY 117 130 130 GLY GLY A . n 
A 1 118 LEU 118 131 131 LEU LEU A . n 
A 1 119 ASN 119 132 132 ASN ASN A . n 
A 1 120 VAL 120 133 133 VAL VAL A . n 
A 1 121 HIS 121 134 134 HIS HIS A . n 
A 1 122 GLY 122 135 135 GLY GLY A . n 
A 1 123 THR 123 136 136 THR THR A . n 
A 1 124 PHE 124 137 137 PHE PHE A . n 
A 1 125 GLU 125 138 138 GLU GLU A . n 
A 1 126 GLY 126 139 139 GLY GLY A . n 
A 1 127 ASP 127 140 140 ASP ASP A . n 
A 1 128 ALA 128 141 141 ALA ALA A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 MET 130 143 143 MET MET A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 ARG 132 145 145 ARG ARG A . n 
A 1 133 ALA 133 146 146 ALA ALA A . n 
A 1 134 ASP 134 147 147 ASP ASP A . n 
A 1 135 GLU 135 148 148 GLU GLU A . n 
A 1 136 PHE 136 149 149 PHE PHE A . n 
A 1 137 PHE 137 150 150 PHE PHE A . n 
A 1 138 GLY 138 151 151 GLY GLY A . n 
A 1 139 ASP 139 152 152 ASP ASP A . n 
A 1 140 ASN 140 153 153 ASN ASN A . n 
A 1 141 HIS 141 154 154 HIS HIS A . n 
A 1 142 SER 142 155 155 SER SER A . n 
A 1 143 PHE 143 156 156 PHE PHE A . n 
A 1 144 ASN 144 157 157 ASN ASN A . n 
A 1 145 GLN 145 158 158 GLN GLN A . n 
A 1 146 THR 146 159 159 THR THR A . n 
A 1 147 LEU 147 160 160 LEU LEU A . n 
A 1 148 PHE 148 161 161 PHE PHE A . n 
A 1 149 ASP 149 162 162 ASP ASP A . n 
A 1 150 LYS 150 163 163 LYS LYS A . n 
A 1 151 PHE 151 164 164 PHE PHE A . n 
A 1 152 VAL 152 165 165 VAL VAL A . n 
A 1 153 ASP 153 166 166 ASP ASP A . n 
A 1 154 PHE 154 167 167 PHE PHE A . n 
A 1 155 SER 155 168 168 SER SER A . n 
A 1 156 ASN 156 169 169 ASN ASN A . n 
A 1 157 ARG 157 170 170 ARG ARG A . n 
A 1 158 TYR 158 171 171 TYR TYR A . n 
A 1 159 GLY 159 172 172 GLY GLY A . n 
A 1 160 GLY 160 173 173 GLY GLY A . n 
A 1 161 GLY 161 174 174 GLY GLY A . n 
A 1 162 PHE 162 175 175 PHE PHE A . n 
A 1 163 TYR 163 176 176 TYR TYR A . n 
A 1 164 ASN 164 177 177 ASN ASN A . n 
A 1 165 LEU 165 178 178 LEU LEU A . n 
A 1 166 THR 166 179 179 THR THR A . n 
A 1 167 VAL 167 180 180 VAL VAL A . n 
A 1 168 ALA 168 181 181 ALA ALA A . n 
A 1 169 GLY 169 182 182 GLY GLY A . n 
A 1 170 GLU 170 183 183 GLU GLU A . n 
A 1 171 LEU 171 184 184 LEU LEU A . n 
A 1 172 ARG 172 185 185 ARG ARG A . n 
A 1 173 TYR 173 186 186 TYR TYR A . n 
A 1 174 SER 174 187 187 SER SER A . n 
A 1 175 ARG 175 188 188 ARG ARG A . n 
A 1 176 ILE 176 189 189 ILE ILE A . n 
A 1 177 GLN 177 190 190 GLN GLN A . n 
A 1 178 ASP 178 191 191 ASP ASP A . n 
A 1 179 SER 179 192 192 SER SER A . n 
A 1 180 ILE 180 193 193 ILE ILE A . n 
A 1 181 ALA 181 194 194 ALA ALA A . n 
A 1 182 THR 182 195 195 THR THR A . n 
A 1 183 ASN 183 196 196 ASN ASN A . n 
A 1 184 PRO 184 197 197 PRO PRO A . n 
A 1 185 GLU 185 198 198 GLU GLU A . n 
A 1 186 PHE 186 199 199 PHE PHE A . n 
A 1 187 GLN 187 200 200 GLN GLN A . n 
A 1 188 PHE 188 201 201 PHE PHE A . n 
A 1 189 LYS 189 202 202 LYS LYS A . n 
A 1 190 ASN 190 203 203 ASN ASN A . n 
A 1 191 VAL 191 204 204 VAL VAL A . n 
A 1 192 ARG 192 205 205 ARG ARG A . n 
A 1 193 PHE 193 206 206 PHE PHE A . n 
A 1 194 ILE 194 207 207 ILE ILE A . n 
A 1 195 THR 195 208 208 THR THR A . n 
A 1 196 ALA 196 209 209 ALA ALA A . n 
A 1 197 TYR 197 210 210 TYR TYR A . n 
A 1 198 GLY 198 211 211 GLY GLY A . n 
A 1 199 GLU 199 212 212 GLU GLU A . n 
A 1 200 THR 200 213 213 THR THR A . n 
A 1 201 VAL 201 214 214 VAL VAL A . n 
A 1 202 PHE 202 215 215 PHE PHE A . n 
A 1 203 PRO 203 216 216 PRO PRO A . n 
A 1 204 ILE 204 217 217 ILE ILE A . n 
A 1 205 ASN 205 218 218 ASN ASN A . n 
A 1 206 LEU 206 219 219 LEU LEU A . n 
A 1 207 PHE 207 220 220 PHE PHE A . n 
A 1 208 VAL 208 221 221 VAL VAL A . n 
A 1 209 ASP 209 222 222 ASP ASP A . n 
A 1 210 GLY 210 223 223 GLY GLY A . n 
A 1 211 ARG 211 224 224 ARG ARG A . n 
A 1 212 VAL 212 225 225 VAL VAL A . n 
A 1 213 THR 213 226 226 THR THR A . n 
A 1 214 THR 214 227 227 THR THR A . n 
A 1 215 ASP 215 228 228 ASP ASP A . n 
A 1 216 ARG 216 229 229 ARG ARG A . n 
A 1 217 LYS 217 230 230 LYS LYS A . n 
A 1 218 LEU 218 231 231 LEU LEU A . n 
A 1 219 SER 219 232 232 SER SER A . n 
A 1 220 MET 220 233 233 MET MET A . n 
A 1 221 GLU 221 234 234 GLU GLU A . n 
A 1 222 ASP 222 235 235 ASP ASP A . n 
A 1 223 ALA 223 236 236 ALA ALA A . n 
A 1 224 ALA 224 237 237 ALA ALA A . n 
A 1 225 SER 225 238 238 SER SER A . n 
A 1 226 ILE 226 239 239 ILE ILE A . n 
A 1 227 PHE 227 240 240 PHE PHE A . n 
A 1 228 ARG 228 241 241 ARG ARG A . n 
A 1 229 ASP 229 242 242 ASP ASP A . n 
A 1 230 MET 230 243 243 MET MET A . n 
A 1 231 ARG 231 244 244 ARG ARG A . n 
A 1 232 PHE 232 245 245 PHE PHE A . n 
A 1 233 PRO 233 246 246 PRO PRO A . n 
A 1 234 ASP 234 247 247 ASP ASP A . n 
A 1 235 ASP 235 248 248 ASP ASP A . n 
A 1 236 PHE 236 249 249 PHE PHE A . n 
A 1 237 HIS 237 250 250 HIS HIS A . n 
A 1 238 ARG 238 251 251 ARG ARG A . n 
A 1 239 SER 239 252 252 SER SER A . n 
A 1 240 ALA 240 253 253 ALA ALA A . n 
A 1 241 VAL 241 254 254 VAL VAL A . n 
A 1 242 PRO 242 255 255 PRO PRO A . n 
A 1 243 ALA 243 256 256 ALA ALA A . n 
A 1 244 SER 244 257 257 SER SER A . n 
A 1 245 ASN 245 258 258 ASN ASN A . n 
A 1 246 GLU 246 259 259 GLU GLU A . n 
A 1 247 GLY 247 260 260 GLY GLY A . n 
A 1 248 ALA 248 261 261 ALA ALA A . n 
A 1 249 ASP 249 262 262 ASP ASP A . n 
A 1 250 GLN 250 263 263 GLN GLN A . n 
A 1 251 VAL 251 264 264 VAL VAL A . n 
A 1 252 LEU 252 265 265 LEU LEU A . n 
A 1 253 ALA 253 266 266 ALA ALA A . n 
A 1 254 ALA 254 267 267 ALA ALA A . n 
A 1 255 HIS 255 268 268 HIS HIS A . n 
A 1 256 PRO 256 269 269 PRO PRO A . n 
A 1 257 TRP 257 270 270 TRP TRP A . n 
A 1 258 VAL 258 271 271 VAL VAL A . n 
A 1 259 PRO 259 272 272 PRO PRO A . n 
A 1 260 GLY 260 273 273 GLY GLY A . n 
A 1 261 GLY 261 274 274 GLY GLY A . n 
A 1 262 ASN 262 275 275 ASN ASN A . n 
A 1 263 ALA 263 276 276 ALA ALA A . n 
A 1 264 ASP 264 277 277 ASP ASP A . n 
A 1 265 ASN 265 278 278 ASN ASN A . n 
A 1 266 GLN 266 279 279 GLN GLN A . n 
A 1 267 VAL 267 280 280 VAL VAL A . n 
A 1 268 ASN 268 281 281 ASN ASN A . n 
A 1 269 ASN 269 282 282 ASN ASN A . n 
A 1 270 TYR 270 283 283 TYR TYR A . n 
A 1 271 VAL 271 284 284 VAL VAL A . n 
A 1 272 GLU 272 285 285 GLU GLU A . n 
A 1 273 ASP 273 286 286 ASP ASP A . n 
A 1 274 PRO 274 287 287 PRO PRO A . n 
A 1 275 ASP 275 288 288 ASP ASP A . n 
A 1 276 SER 276 289 289 SER SER A . n 
A 1 277 ALA 277 290 290 ALA ALA A . n 
A 1 278 ASP 278 291 291 ASP ASP A . n 
A 1 279 PHE 279 292 292 PHE PHE A . n 
A 1 280 THR 280 293 293 THR THR A . n 
A 1 281 HIS 281 294 294 HIS HIS A . n 
A 1 282 LEU 282 295 295 LEU LEU A . n 
A 1 283 CYS 283 296 296 CYS CYS A . n 
A 1 284 ARG 284 297 297 ARG ARG A . n 
A 1 285 LEU 285 298 298 LEU LEU A . n 
A 1 286 TYR 286 299 299 TYR TYR A . n 
A 1 287 GLU 287 300 300 GLU GLU A . n 
A 1 288 PHE 288 301 301 PHE PHE A . n 
A 1 289 VAL 289 302 302 VAL VAL A . n 
A 1 290 VAL 290 303 303 VAL VAL A . n 
A 1 291 GLY 291 304 304 GLY GLY A . n 
A 1 292 SER 292 305 305 SER SER A . n 
A 1 293 VAL 293 306 306 VAL VAL A . n 
A 1 294 GLN 294 307 307 GLN GLN A . n 
A 1 295 GLU 295 308 308 GLU GLU A . n 
A 1 296 LEU 296 309 309 LEU LEU A . n 
A 1 297 TYR 297 310 310 TYR TYR A . n 
A 1 298 PRO 298 311 311 PRO PRO A . n 
A 1 299 ASN 299 312 312 ASN ASN A . n 
A 1 300 PRO 300 313 313 PRO PRO A . n 
A 1 301 THR 301 314 314 THR THR A . n 
A 1 302 GLY 302 315 315 GLY GLY A . n 
A 1 303 ILE 303 316 316 ILE ILE A . n 
A 1 304 LEU 304 317 317 LEU LEU A . n 
A 1 305 ARG 305 318 318 ARG ARG A . n 
A 1 306 ARG 306 319 319 ARG ARG A . n 
A 1 307 ASN 307 320 320 ASN ASN A . n 
A 1 308 LEU 308 321 321 LEU LEU A . n 
A 1 309 ILE 309 322 322 ILE ILE A . n 
A 1 310 LYS 310 323 323 LYS LYS A . n 
A 1 311 ASN 311 324 324 ASN ASN A . n 
A 1 312 LEU 312 325 325 LEU LEU A . n 
A 1 313 HIS 313 326 326 HIS HIS A . n 
A 1 314 TYR 314 327 327 TYR TYR A . n 
A 1 315 TRP 315 328 328 TRP TRP A . n 
A 1 316 TRP 316 329 329 TRP TRP A . n 
A 1 317 THR 317 330 330 THR THR A . n 
A 1 318 GLY 318 331 331 GLY GLY A . n 
A 1 319 VAL 319 332 332 VAL VAL A . n 
A 1 320 ASN 320 333 333 ASN ASN A . n 
A 1 321 VAL 321 334 334 VAL VAL A . n 
A 1 322 ALA 322 335 335 ALA ALA A . n 
A 1 323 PHE 323 336 336 PHE PHE A . n 
A 1 324 GLY 324 337 337 GLY GLY A . n 
A 1 325 GLY 325 338 338 GLY GLY A . n 
A 1 326 CYS 326 339 339 CYS CYS A . n 
A 1 327 ASP 327 340 340 ASP ASP A . n 
A 1 328 GLU 328 341 341 GLU GLU A . n 
A 1 329 LEU 329 342 342 LEU LEU A . n 
A 1 330 PHE 330 343 343 PHE PHE A . n 
A 1 331 PRO 331 344 344 PRO PRO A . n 
A 1 332 TYR 332 345 345 TYR TYR A . n 
A 1 333 GLY 333 346 346 GLY GLY A . n 
A 1 334 GLN 334 347 347 GLN GLN A . n 
A 1 335 LEU 335 348 348 LEU LEU A . n 
B 1 1   GLN 1   14  14  GLN GLN B . n 
B 1 2   GLY 2   15  15  GLY GLY B . n 
B 1 3   VAL 3   16  16  VAL VAL B . n 
B 1 4   ASP 4   17  17  ASP ASP B . n 
B 1 5   PRO 5   18  18  PRO PRO B . n 
B 1 6   PRO 6   19  19  PRO PRO B . n 
B 1 7   PRO 7   20  20  PRO PRO B . n 
B 1 8   PRO 8   21  21  PRO PRO B . n 
B 1 9   PRO 9   22  22  PRO PRO B . n 
B 1 10  GLY 10  23  23  GLY GLY B . n 
B 1 11  PRO 11  24  24  PRO PRO B . n 
B 1 12  PRO 12  25  25  PRO PRO B . n 
B 1 13  SER 13  26  26  SER SER B . n 
B 1 14  PHE 14  27  27  PHE PHE B . n 
B 1 15  THR 15  28  28  THR THR B . n 
B 1 16  GLY 16  29  29  GLY GLY B . n 
B 1 17  THR 17  30  30  THR THR B . n 
B 1 18  LYS 18  31  31  LYS LYS B . n 
B 1 19  LEU 19  32  32  LEU LEU B . n 
B 1 20  VAL 20  33  33  VAL VAL B . n 
B 1 21  ASN 21  34  34  ASN ASN B . n 
B 1 22  ASP 22  35  35  ASP ASP B . n 
B 1 23  ALA 23  36  36  ALA ALA B . n 
B 1 24  ASP 24  37  37  ASP ASP B . n 
B 1 25  HIS 25  38  38  HIS HIS B . n 
B 1 26  PRO 26  39  39  PRO PRO B . n 
B 1 27  TRP 27  40  40  TRP TRP B . n 
B 1 28  GLN 28  41  41  GLN GLN B . n 
B 1 29  PRO 29  42  42  PRO PRO B . n 
B 1 30  LEU 30  43  43  LEU LEU B . n 
B 1 31  ARG 31  44  44  ARG ARG B . n 
B 1 32  GLU 32  45  45  GLU GLU B . n 
B 1 33  GLY 33  46  46  GLY GLY B . n 
B 1 34  ASP 34  47  47  ASP ASP B . n 
B 1 35  ILE 35  48  48  ILE ILE B . n 
B 1 36  ARG 36  49  49  ARG ARG B . n 
B 1 37  GLY 37  50  50  GLY GLY B . n 
B 1 38  PRO 38  51  51  PRO PRO B . n 
B 1 39  CYS 39  52  52  CYS CYS B . n 
B 1 40  PRO 40  53  53  PRO PRO B . n 
B 1 41  GLY 41  54  54  GLY GLY B . n 
B 1 42  LEU 42  55  55  LEU LEU B . n 
B 1 43  ASN 43  56  56  ASN ASN B . n 
B 1 44  THR 44  57  57  THR THR B . n 
B 1 45  LEU 45  58  58  LEU LEU B . n 
B 1 46  ALA 46  59  59  ALA ALA B . n 
B 1 47  SER 47  60  60  SER SER B . n 
B 1 48  HIS 48  61  61  HIS HIS B . n 
B 1 49  GLY 49  62  62  GLY GLY B . n 
B 1 50  TYR 50  63  63  TYR TYR B . n 
B 1 51  LEU 51  64  64  LEU LEU B . n 
B 1 52  PRO 52  65  65  PRO PRO B . n 
B 1 53  ARG 53  66  66  ARG ARG B . n 
B 1 54  ASP 54  67  67  ASP ASP B . n 
B 1 55  GLY 55  68  68  GLY GLY B . n 
B 1 56  VAL 56  69  69  VAL VAL B . n 
B 1 57  ALA 57  70  70  ALA ALA B . n 
B 1 58  THR 58  71  71  THR THR B . n 
B 1 59  PRO 59  72  72  PRO PRO B . n 
B 1 60  ALA 60  73  73  ALA ALA B . n 
B 1 61  GLN 61  74  74  GLN GLN B . n 
B 1 62  ILE 62  75  75  ILE ILE B . n 
B 1 63  ILE 63  76  76  ILE ILE B . n 
B 1 64  THR 64  77  77  THR THR B . n 
B 1 65  ALA 65  78  78  ALA ALA B . n 
B 1 66  THR 66  79  79  THR THR B . n 
B 1 67  GLN 67  80  80  GLN GLN B . n 
B 1 68  GLU 68  81  81  GLU GLU B . n 
B 1 69  GLY 69  82  82  GLY GLY B . n 
B 1 70  PHE 70  83  83  PHE PHE B . n 
B 1 71  ASN 71  84  84  ASN ASN B . n 
B 1 72  PHE 72  85  85  PHE PHE B . n 
B 1 73  GLU 73  86  86  GLU GLU B . n 
B 1 74  ASN 74  87  87  ASN ASN B . n 
B 1 75  ASN 75  88  88  ASN ASN B . n 
B 1 76  ALA 76  89  89  ALA ALA B . n 
B 1 77  ALA 77  90  90  ALA ALA B . n 
B 1 78  ILE 78  91  91  ILE ILE B . n 
B 1 79  VAL 79  92  92  VAL VAL B . n 
B 1 80  ALA 80  93  93  ALA ALA B . n 
B 1 81  THR 81  94  94  THR THR B . n 
B 1 82  TYR 82  95  95  TYR TYR B . n 
B 1 83  LEU 83  96  96  LEU LEU B . n 
B 1 84  GLY 84  97  97  GLY GLY B . n 
B 1 85  HIS 85  98  98  HIS HIS B . n 
B 1 86  LEU 86  99  99  LEU LEU B . n 
B 1 87  LEU 87  100 100 LEU LEU B . n 
B 1 88  ASN 88  101 101 ASN ASN B . n 
B 1 89  GLY 89  102 102 GLY GLY B . n 
B 1 90  ASN 90  103 103 ASN ASN B . n 
B 1 91  LEU 91  104 104 LEU LEU B . n 
B 1 92  VAL 92  105 105 VAL VAL B . n 
B 1 93  THR 93  106 106 THR THR B . n 
B 1 94  ASP 94  107 107 ASP ASP B . n 
B 1 95  LEU 95  108 108 LEU LEU B . n 
B 1 96  LEU 96  109 109 LEU LEU B . n 
B 1 97  SER 97  110 110 SER SER B . n 
B 1 98  ILE 98  111 111 ILE ILE B . n 
B 1 99  GLY 99  112 112 GLY GLY B . n 
B 1 100 GLY 100 113 113 GLY GLY B . n 
B 1 101 ALA 101 114 114 ALA ALA B . n 
B 1 102 THR 102 115 115 THR THR B . n 
B 1 103 PRO 103 116 116 PRO PRO B . n 
B 1 104 LYS 104 117 117 LYS LYS B . n 
B 1 105 THR 105 118 118 THR THR B . n 
B 1 106 GLY 106 119 119 GLY GLY B . n 
B 1 107 PRO 107 120 120 PRO PRO B . n 
B 1 108 PRO 108 121 121 PRO PRO B . n 
B 1 109 PRO 109 122 122 PRO PRO B . n 
B 1 110 PRO 110 123 123 PRO PRO B . n 
B 1 111 PRO 111 124 124 PRO PRO B . n 
B 1 112 PRO 112 125 125 PRO PRO B . n 
B 1 113 ALA 113 126 126 ALA ALA B . n 
B 1 114 HIS 114 127 127 HIS HIS B . n 
B 1 115 ALA 115 128 128 ALA ALA B . n 
B 1 116 GLY 116 129 129 GLY GLY B . n 
B 1 117 GLY 117 130 130 GLY GLY B . n 
B 1 118 LEU 118 131 131 LEU LEU B . n 
B 1 119 ASN 119 132 132 ASN ASN B . n 
B 1 120 VAL 120 133 133 VAL VAL B . n 
B 1 121 HIS 121 134 134 HIS HIS B . n 
B 1 122 GLY 122 135 135 GLY GLY B . n 
B 1 123 THR 123 136 136 THR THR B . n 
B 1 124 PHE 124 137 137 PHE PHE B . n 
B 1 125 GLU 125 138 138 GLU GLU B . n 
B 1 126 GLY 126 139 139 GLY GLY B . n 
B 1 127 ASP 127 140 140 ASP ASP B . n 
B 1 128 ALA 128 141 141 ALA ALA B . n 
B 1 129 GLY 129 142 142 GLY GLY B . n 
B 1 130 MET 130 143 143 MET MET B . n 
B 1 131 THR 131 144 144 THR THR B . n 
B 1 132 ARG 132 145 145 ARG ARG B . n 
B 1 133 ALA 133 146 146 ALA ALA B . n 
B 1 134 ASP 134 147 147 ASP ASP B . n 
B 1 135 GLU 135 148 148 GLU GLU B . n 
B 1 136 PHE 136 149 149 PHE PHE B . n 
B 1 137 PHE 137 150 150 PHE PHE B . n 
B 1 138 GLY 138 151 151 GLY GLY B . n 
B 1 139 ASP 139 152 152 ASP ASP B . n 
B 1 140 ASN 140 153 153 ASN ASN B . n 
B 1 141 HIS 141 154 154 HIS HIS B . n 
B 1 142 SER 142 155 155 SER SER B . n 
B 1 143 PHE 143 156 156 PHE PHE B . n 
B 1 144 ASN 144 157 157 ASN ASN B . n 
B 1 145 GLN 145 158 158 GLN GLN B . n 
B 1 146 THR 146 159 159 THR THR B . n 
B 1 147 LEU 147 160 160 LEU LEU B . n 
B 1 148 PHE 148 161 161 PHE PHE B . n 
B 1 149 ASP 149 162 162 ASP ASP B . n 
B 1 150 LYS 150 163 163 LYS LYS B . n 
B 1 151 PHE 151 164 164 PHE PHE B . n 
B 1 152 VAL 152 165 165 VAL VAL B . n 
B 1 153 ASP 153 166 166 ASP ASP B . n 
B 1 154 PHE 154 167 167 PHE PHE B . n 
B 1 155 SER 155 168 168 SER SER B . n 
B 1 156 ASN 156 169 169 ASN ASN B . n 
B 1 157 ARG 157 170 170 ARG ARG B . n 
B 1 158 TYR 158 171 171 TYR TYR B . n 
B 1 159 GLY 159 172 172 GLY GLY B . n 
B 1 160 GLY 160 173 173 GLY GLY B . n 
B 1 161 GLY 161 174 174 GLY GLY B . n 
B 1 162 PHE 162 175 175 PHE PHE B . n 
B 1 163 TYR 163 176 176 TYR TYR B . n 
B 1 164 ASN 164 177 177 ASN ASN B . n 
B 1 165 LEU 165 178 178 LEU LEU B . n 
B 1 166 THR 166 179 179 THR THR B . n 
B 1 167 VAL 167 180 180 VAL VAL B . n 
B 1 168 ALA 168 181 181 ALA ALA B . n 
B 1 169 GLY 169 182 182 GLY GLY B . n 
B 1 170 GLU 170 183 183 GLU GLU B . n 
B 1 171 LEU 171 184 184 LEU LEU B . n 
B 1 172 ARG 172 185 185 ARG ARG B . n 
B 1 173 TYR 173 186 186 TYR TYR B . n 
B 1 174 SER 174 187 187 SER SER B . n 
B 1 175 ARG 175 188 188 ARG ARG B . n 
B 1 176 ILE 176 189 189 ILE ILE B . n 
B 1 177 GLN 177 190 190 GLN GLN B . n 
B 1 178 ASP 178 191 191 ASP ASP B . n 
B 1 179 SER 179 192 192 SER SER B . n 
B 1 180 ILE 180 193 193 ILE ILE B . n 
B 1 181 ALA 181 194 194 ALA ALA B . n 
B 1 182 THR 182 195 195 THR THR B . n 
B 1 183 ASN 183 196 196 ASN ASN B . n 
B 1 184 PRO 184 197 197 PRO PRO B . n 
B 1 185 GLU 185 198 198 GLU GLU B . n 
B 1 186 PHE 186 199 199 PHE PHE B . n 
B 1 187 GLN 187 200 200 GLN GLN B . n 
B 1 188 PHE 188 201 201 PHE PHE B . n 
B 1 189 LYS 189 202 202 LYS LYS B . n 
B 1 190 ASN 190 203 203 ASN ASN B . n 
B 1 191 VAL 191 204 204 VAL VAL B . n 
B 1 192 ARG 192 205 205 ARG ARG B . n 
B 1 193 PHE 193 206 206 PHE PHE B . n 
B 1 194 ILE 194 207 207 ILE ILE B . n 
B 1 195 THR 195 208 208 THR THR B . n 
B 1 196 ALA 196 209 209 ALA ALA B . n 
B 1 197 TYR 197 210 210 TYR TYR B . n 
B 1 198 GLY 198 211 211 GLY GLY B . n 
B 1 199 GLU 199 212 212 GLU GLU B . n 
B 1 200 THR 200 213 213 THR THR B . n 
B 1 201 VAL 201 214 214 VAL VAL B . n 
B 1 202 PHE 202 215 215 PHE PHE B . n 
B 1 203 PRO 203 216 216 PRO PRO B . n 
B 1 204 ILE 204 217 217 ILE ILE B . n 
B 1 205 ASN 205 218 218 ASN ASN B . n 
B 1 206 LEU 206 219 219 LEU LEU B . n 
B 1 207 PHE 207 220 220 PHE PHE B . n 
B 1 208 VAL 208 221 221 VAL VAL B . n 
B 1 209 ASP 209 222 222 ASP ASP B . n 
B 1 210 GLY 210 223 223 GLY GLY B . n 
B 1 211 ARG 211 224 224 ARG ARG B . n 
B 1 212 VAL 212 225 225 VAL VAL B . n 
B 1 213 THR 213 226 226 THR THR B . n 
B 1 214 THR 214 227 227 THR THR B . n 
B 1 215 ASP 215 228 228 ASP ASP B . n 
B 1 216 ARG 216 229 229 ARG ARG B . n 
B 1 217 LYS 217 230 230 LYS LYS B . n 
B 1 218 LEU 218 231 231 LEU LEU B . n 
B 1 219 SER 219 232 232 SER SER B . n 
B 1 220 MET 220 233 233 MET MET B . n 
B 1 221 GLU 221 234 234 GLU GLU B . n 
B 1 222 ASP 222 235 235 ASP ASP B . n 
B 1 223 ALA 223 236 236 ALA ALA B . n 
B 1 224 ALA 224 237 237 ALA ALA B . n 
B 1 225 SER 225 238 238 SER SER B . n 
B 1 226 ILE 226 239 239 ILE ILE B . n 
B 1 227 PHE 227 240 240 PHE PHE B . n 
B 1 228 ARG 228 241 241 ARG ARG B . n 
B 1 229 ASP 229 242 242 ASP ASP B . n 
B 1 230 MET 230 243 243 MET MET B . n 
B 1 231 ARG 231 244 244 ARG ARG B . n 
B 1 232 PHE 232 245 245 PHE PHE B . n 
B 1 233 PRO 233 246 246 PRO PRO B . n 
B 1 234 ASP 234 247 247 ASP ASP B . n 
B 1 235 ASP 235 248 248 ASP ASP B . n 
B 1 236 PHE 236 249 249 PHE PHE B . n 
B 1 237 HIS 237 250 250 HIS HIS B . n 
B 1 238 ARG 238 251 251 ARG ARG B . n 
B 1 239 SER 239 252 252 SER SER B . n 
B 1 240 ALA 240 253 253 ALA ALA B . n 
B 1 241 VAL 241 254 254 VAL VAL B . n 
B 1 242 PRO 242 255 255 PRO PRO B . n 
B 1 243 ALA 243 256 256 ALA ALA B . n 
B 1 244 SER 244 257 257 SER SER B . n 
B 1 245 ASN 245 258 258 ASN ASN B . n 
B 1 246 GLU 246 259 259 GLU GLU B . n 
B 1 247 GLY 247 260 260 GLY GLY B . n 
B 1 248 ALA 248 261 261 ALA ALA B . n 
B 1 249 ASP 249 262 262 ASP ASP B . n 
B 1 250 GLN 250 263 263 GLN GLN B . n 
B 1 251 VAL 251 264 264 VAL VAL B . n 
B 1 252 LEU 252 265 265 LEU LEU B . n 
B 1 253 ALA 253 266 266 ALA ALA B . n 
B 1 254 ALA 254 267 267 ALA ALA B . n 
B 1 255 HIS 255 268 268 HIS HIS B . n 
B 1 256 PRO 256 269 269 PRO PRO B . n 
B 1 257 TRP 257 270 270 TRP TRP B . n 
B 1 258 VAL 258 271 271 VAL VAL B . n 
B 1 259 PRO 259 272 272 PRO PRO B . n 
B 1 260 GLY 260 273 273 GLY GLY B . n 
B 1 261 GLY 261 274 274 GLY GLY B . n 
B 1 262 ASN 262 275 275 ASN ASN B . n 
B 1 263 ALA 263 276 276 ALA ALA B . n 
B 1 264 ASP 264 277 277 ASP ASP B . n 
B 1 265 ASN 265 278 278 ASN ASN B . n 
B 1 266 GLN 266 279 279 GLN GLN B . n 
B 1 267 VAL 267 280 280 VAL VAL B . n 
B 1 268 ASN 268 281 281 ASN ASN B . n 
B 1 269 ASN 269 282 282 ASN ASN B . n 
B 1 270 TYR 270 283 283 TYR TYR B . n 
B 1 271 VAL 271 284 284 VAL VAL B . n 
B 1 272 GLU 272 285 285 GLU GLU B . n 
B 1 273 ASP 273 286 286 ASP ASP B . n 
B 1 274 PRO 274 287 287 PRO PRO B . n 
B 1 275 ASP 275 288 288 ASP ASP B . n 
B 1 276 SER 276 289 289 SER SER B . n 
B 1 277 ALA 277 290 290 ALA ALA B . n 
B 1 278 ASP 278 291 291 ASP ASP B . n 
B 1 279 PHE 279 292 292 PHE PHE B . n 
B 1 280 THR 280 293 293 THR THR B . n 
B 1 281 HIS 281 294 294 HIS HIS B . n 
B 1 282 LEU 282 295 295 LEU LEU B . n 
B 1 283 CYS 283 296 296 CYS CYS B . n 
B 1 284 ARG 284 297 297 ARG ARG B . n 
B 1 285 LEU 285 298 298 LEU LEU B . n 
B 1 286 TYR 286 299 299 TYR TYR B . n 
B 1 287 GLU 287 300 300 GLU GLU B . n 
B 1 288 PHE 288 301 301 PHE PHE B . n 
B 1 289 VAL 289 302 302 VAL VAL B . n 
B 1 290 VAL 290 303 303 VAL VAL B . n 
B 1 291 GLY 291 304 304 GLY GLY B . n 
B 1 292 SER 292 305 305 SER SER B . n 
B 1 293 VAL 293 306 306 VAL VAL B . n 
B 1 294 GLN 294 307 307 GLN GLN B . n 
B 1 295 GLU 295 308 308 GLU GLU B . n 
B 1 296 LEU 296 309 309 LEU LEU B . n 
B 1 297 TYR 297 310 310 TYR TYR B . n 
B 1 298 PRO 298 311 311 PRO PRO B . n 
B 1 299 ASN 299 312 312 ASN ASN B . n 
B 1 300 PRO 300 313 313 PRO PRO B . n 
B 1 301 THR 301 314 314 THR THR B . n 
B 1 302 GLY 302 315 315 GLY GLY B . n 
B 1 303 ILE 303 316 316 ILE ILE B . n 
B 1 304 LEU 304 317 317 LEU LEU B . n 
B 1 305 ARG 305 318 318 ARG ARG B . n 
B 1 306 ARG 306 319 319 ARG ARG B . n 
B 1 307 ASN 307 320 320 ASN ASN B . n 
B 1 308 LEU 308 321 321 LEU LEU B . n 
B 1 309 ILE 309 322 322 ILE ILE B . n 
B 1 310 LYS 310 323 323 LYS LYS B . n 
B 1 311 ASN 311 324 324 ASN ASN B . n 
B 1 312 LEU 312 325 325 LEU LEU B . n 
B 1 313 HIS 313 326 326 HIS HIS B . n 
B 1 314 TYR 314 327 327 TYR TYR B . n 
B 1 315 TRP 315 328 328 TRP TRP B . n 
B 1 316 TRP 316 329 329 TRP TRP B . n 
B 1 317 THR 317 330 330 THR THR B . n 
B 1 318 GLY 318 331 331 GLY GLY B . n 
B 1 319 VAL 319 332 332 VAL VAL B . n 
B 1 320 ASN 320 333 333 ASN ASN B . n 
B 1 321 VAL 321 334 334 VAL VAL B . n 
B 1 322 ALA 322 335 335 ALA ALA B . n 
B 1 323 PHE 323 336 336 PHE PHE B . n 
B 1 324 GLY 324 337 337 GLY GLY B . n 
B 1 325 GLY 325 338 338 GLY GLY B . n 
B 1 326 CYS 326 339 339 CYS CYS B . n 
B 1 327 ASP 327 340 340 ASP ASP B . n 
B 1 328 GLU 328 341 341 GLU GLU B . n 
B 1 329 LEU 329 342 342 LEU LEU B . n 
B 1 330 PHE 330 343 343 PHE PHE B . n 
B 1 331 PRO 331 344 344 PRO PRO B . n 
B 1 332 TYR 332 345 345 TYR TYR B . n 
B 1 333 GLY 333 346 346 GLY GLY B . n 
B 1 334 GLN 334 347 347 GLN GLN B . n 
B 1 335 LEU 335 348 348 LEU LEU B . n 
C 1 1   GLN 1   14  14  GLN GLN C . n 
C 1 2   GLY 2   15  15  GLY GLY C . n 
C 1 3   VAL 3   16  16  VAL VAL C . n 
C 1 4   ASP 4   17  17  ASP ASP C . n 
C 1 5   PRO 5   18  18  PRO PRO C . n 
C 1 6   PRO 6   19  19  PRO PRO C . n 
C 1 7   PRO 7   20  20  PRO PRO C . n 
C 1 8   PRO 8   21  21  PRO PRO C . n 
C 1 9   PRO 9   22  22  PRO PRO C . n 
C 1 10  GLY 10  23  23  GLY GLY C . n 
C 1 11  PRO 11  24  24  PRO PRO C . n 
C 1 12  PRO 12  25  25  PRO PRO C . n 
C 1 13  SER 13  26  26  SER SER C . n 
C 1 14  PHE 14  27  27  PHE PHE C . n 
C 1 15  THR 15  28  28  THR THR C . n 
C 1 16  GLY 16  29  29  GLY GLY C . n 
C 1 17  THR 17  30  30  THR THR C . n 
C 1 18  LYS 18  31  31  LYS LYS C . n 
C 1 19  LEU 19  32  32  LEU LEU C . n 
C 1 20  VAL 20  33  33  VAL VAL C . n 
C 1 21  ASN 21  34  34  ASN ASN C . n 
C 1 22  ASP 22  35  35  ASP ASP C . n 
C 1 23  ALA 23  36  36  ALA ALA C . n 
C 1 24  ASP 24  37  37  ASP ASP C . n 
C 1 25  HIS 25  38  38  HIS HIS C . n 
C 1 26  PRO 26  39  39  PRO PRO C . n 
C 1 27  TRP 27  40  40  TRP TRP C . n 
C 1 28  GLN 28  41  41  GLN GLN C . n 
C 1 29  PRO 29  42  42  PRO PRO C . n 
C 1 30  LEU 30  43  43  LEU LEU C . n 
C 1 31  ARG 31  44  44  ARG ARG C . n 
C 1 32  GLU 32  45  45  GLU GLU C . n 
C 1 33  GLY 33  46  46  GLY GLY C . n 
C 1 34  ASP 34  47  47  ASP ASP C . n 
C 1 35  ILE 35  48  48  ILE ILE C . n 
C 1 36  ARG 36  49  49  ARG ARG C . n 
C 1 37  GLY 37  50  50  GLY GLY C . n 
C 1 38  PRO 38  51  51  PRO PRO C . n 
C 1 39  CYS 39  52  52  CYS CYS C . n 
C 1 40  PRO 40  53  53  PRO PRO C . n 
C 1 41  GLY 41  54  54  GLY GLY C . n 
C 1 42  LEU 42  55  55  LEU LEU C . n 
C 1 43  ASN 43  56  56  ASN ASN C . n 
C 1 44  THR 44  57  57  THR THR C . n 
C 1 45  LEU 45  58  58  LEU LEU C . n 
C 1 46  ALA 46  59  59  ALA ALA C . n 
C 1 47  SER 47  60  60  SER SER C . n 
C 1 48  HIS 48  61  61  HIS HIS C . n 
C 1 49  GLY 49  62  62  GLY GLY C . n 
C 1 50  TYR 50  63  63  TYR TYR C . n 
C 1 51  LEU 51  64  64  LEU LEU C . n 
C 1 52  PRO 52  65  65  PRO PRO C . n 
C 1 53  ARG 53  66  66  ARG ARG C . n 
C 1 54  ASP 54  67  67  ASP ASP C . n 
C 1 55  GLY 55  68  68  GLY GLY C . n 
C 1 56  VAL 56  69  69  VAL VAL C . n 
C 1 57  ALA 57  70  70  ALA ALA C . n 
C 1 58  THR 58  71  71  THR THR C . n 
C 1 59  PRO 59  72  72  PRO PRO C . n 
C 1 60  ALA 60  73  73  ALA ALA C . n 
C 1 61  GLN 61  74  74  GLN GLN C . n 
C 1 62  ILE 62  75  75  ILE ILE C . n 
C 1 63  ILE 63  76  76  ILE ILE C . n 
C 1 64  THR 64  77  77  THR THR C . n 
C 1 65  ALA 65  78  78  ALA ALA C . n 
C 1 66  THR 66  79  79  THR THR C . n 
C 1 67  GLN 67  80  80  GLN GLN C . n 
C 1 68  GLU 68  81  81  GLU GLU C . n 
C 1 69  GLY 69  82  82  GLY GLY C . n 
C 1 70  PHE 70  83  83  PHE PHE C . n 
C 1 71  ASN 71  84  84  ASN ASN C . n 
C 1 72  PHE 72  85  85  PHE PHE C . n 
C 1 73  GLU 73  86  86  GLU GLU C . n 
C 1 74  ASN 74  87  87  ASN ASN C . n 
C 1 75  ASN 75  88  88  ASN ASN C . n 
C 1 76  ALA 76  89  89  ALA ALA C . n 
C 1 77  ALA 77  90  90  ALA ALA C . n 
C 1 78  ILE 78  91  91  ILE ILE C . n 
C 1 79  VAL 79  92  92  VAL VAL C . n 
C 1 80  ALA 80  93  93  ALA ALA C . n 
C 1 81  THR 81  94  94  THR THR C . n 
C 1 82  TYR 82  95  95  TYR TYR C . n 
C 1 83  LEU 83  96  96  LEU LEU C . n 
C 1 84  GLY 84  97  97  GLY GLY C . n 
C 1 85  HIS 85  98  98  HIS HIS C . n 
C 1 86  LEU 86  99  99  LEU LEU C . n 
C 1 87  LEU 87  100 100 LEU LEU C . n 
C 1 88  ASN 88  101 101 ASN ASN C . n 
C 1 89  GLY 89  102 102 GLY GLY C . n 
C 1 90  ASN 90  103 103 ASN ASN C . n 
C 1 91  LEU 91  104 104 LEU LEU C . n 
C 1 92  VAL 92  105 105 VAL VAL C . n 
C 1 93  THR 93  106 106 THR THR C . n 
C 1 94  ASP 94  107 107 ASP ASP C . n 
C 1 95  LEU 95  108 108 LEU LEU C . n 
C 1 96  LEU 96  109 109 LEU LEU C . n 
C 1 97  SER 97  110 110 SER SER C . n 
C 1 98  ILE 98  111 111 ILE ILE C . n 
C 1 99  GLY 99  112 112 GLY GLY C . n 
C 1 100 GLY 100 113 113 GLY GLY C . n 
C 1 101 ALA 101 114 114 ALA ALA C . n 
C 1 102 THR 102 115 115 THR THR C . n 
C 1 103 PRO 103 116 116 PRO PRO C . n 
C 1 104 LYS 104 117 117 LYS LYS C . n 
C 1 105 THR 105 118 118 THR THR C . n 
C 1 106 GLY 106 119 119 GLY GLY C . n 
C 1 107 PRO 107 120 120 PRO PRO C . n 
C 1 108 PRO 108 121 121 PRO PRO C . n 
C 1 109 PRO 109 122 122 PRO PRO C . n 
C 1 110 PRO 110 123 123 PRO PRO C . n 
C 1 111 PRO 111 124 124 PRO PRO C . n 
C 1 112 PRO 112 125 125 PRO PRO C . n 
C 1 113 ALA 113 126 126 ALA ALA C . n 
C 1 114 HIS 114 127 127 HIS HIS C . n 
C 1 115 ALA 115 128 128 ALA ALA C . n 
C 1 116 GLY 116 129 129 GLY GLY C . n 
C 1 117 GLY 117 130 130 GLY GLY C . n 
C 1 118 LEU 118 131 131 LEU LEU C . n 
C 1 119 ASN 119 132 132 ASN ASN C . n 
C 1 120 VAL 120 133 133 VAL VAL C . n 
C 1 121 HIS 121 134 134 HIS HIS C . n 
C 1 122 GLY 122 135 135 GLY GLY C . n 
C 1 123 THR 123 136 136 THR THR C . n 
C 1 124 PHE 124 137 137 PHE PHE C . n 
C 1 125 GLU 125 138 138 GLU GLU C . n 
C 1 126 GLY 126 139 139 GLY GLY C . n 
C 1 127 ASP 127 140 140 ASP ASP C . n 
C 1 128 ALA 128 141 141 ALA ALA C . n 
C 1 129 GLY 129 142 142 GLY GLY C . n 
C 1 130 MET 130 143 143 MET MET C . n 
C 1 131 THR 131 144 144 THR THR C . n 
C 1 132 ARG 132 145 145 ARG ARG C . n 
C 1 133 ALA 133 146 146 ALA ALA C . n 
C 1 134 ASP 134 147 147 ASP ASP C . n 
C 1 135 GLU 135 148 148 GLU GLU C . n 
C 1 136 PHE 136 149 149 PHE PHE C . n 
C 1 137 PHE 137 150 150 PHE PHE C . n 
C 1 138 GLY 138 151 151 GLY GLY C . n 
C 1 139 ASP 139 152 152 ASP ASP C . n 
C 1 140 ASN 140 153 153 ASN ASN C . n 
C 1 141 HIS 141 154 154 HIS HIS C . n 
C 1 142 SER 142 155 155 SER SER C . n 
C 1 143 PHE 143 156 156 PHE PHE C . n 
C 1 144 ASN 144 157 157 ASN ASN C . n 
C 1 145 GLN 145 158 158 GLN GLN C . n 
C 1 146 THR 146 159 159 THR THR C . n 
C 1 147 LEU 147 160 160 LEU LEU C . n 
C 1 148 PHE 148 161 161 PHE PHE C . n 
C 1 149 ASP 149 162 162 ASP ASP C . n 
C 1 150 LYS 150 163 163 LYS LYS C . n 
C 1 151 PHE 151 164 164 PHE PHE C . n 
C 1 152 VAL 152 165 165 VAL VAL C . n 
C 1 153 ASP 153 166 166 ASP ASP C . n 
C 1 154 PHE 154 167 167 PHE PHE C . n 
C 1 155 SER 155 168 168 SER SER C . n 
C 1 156 ASN 156 169 169 ASN ASN C . n 
C 1 157 ARG 157 170 170 ARG ARG C . n 
C 1 158 TYR 158 171 171 TYR TYR C . n 
C 1 159 GLY 159 172 172 GLY GLY C . n 
C 1 160 GLY 160 173 173 GLY GLY C . n 
C 1 161 GLY 161 174 174 GLY GLY C . n 
C 1 162 PHE 162 175 175 PHE PHE C . n 
C 1 163 TYR 163 176 176 TYR TYR C . n 
C 1 164 ASN 164 177 177 ASN ASN C . n 
C 1 165 LEU 165 178 178 LEU LEU C . n 
C 1 166 THR 166 179 179 THR THR C . n 
C 1 167 VAL 167 180 180 VAL VAL C . n 
C 1 168 ALA 168 181 181 ALA ALA C . n 
C 1 169 GLY 169 182 182 GLY GLY C . n 
C 1 170 GLU 170 183 183 GLU GLU C . n 
C 1 171 LEU 171 184 184 LEU LEU C . n 
C 1 172 ARG 172 185 185 ARG ARG C . n 
C 1 173 TYR 173 186 186 TYR TYR C . n 
C 1 174 SER 174 187 187 SER SER C . n 
C 1 175 ARG 175 188 188 ARG ARG C . n 
C 1 176 ILE 176 189 189 ILE ILE C . n 
C 1 177 GLN 177 190 190 GLN GLN C . n 
C 1 178 ASP 178 191 191 ASP ASP C . n 
C 1 179 SER 179 192 192 SER SER C . n 
C 1 180 ILE 180 193 193 ILE ILE C . n 
C 1 181 ALA 181 194 194 ALA ALA C . n 
C 1 182 THR 182 195 195 THR THR C . n 
C 1 183 ASN 183 196 196 ASN ASN C . n 
C 1 184 PRO 184 197 197 PRO PRO C . n 
C 1 185 GLU 185 198 198 GLU GLU C . n 
C 1 186 PHE 186 199 199 PHE PHE C . n 
C 1 187 GLN 187 200 200 GLN GLN C . n 
C 1 188 PHE 188 201 201 PHE PHE C . n 
C 1 189 LYS 189 202 202 LYS LYS C . n 
C 1 190 ASN 190 203 203 ASN ASN C . n 
C 1 191 VAL 191 204 204 VAL VAL C . n 
C 1 192 ARG 192 205 205 ARG ARG C . n 
C 1 193 PHE 193 206 206 PHE PHE C . n 
C 1 194 ILE 194 207 207 ILE ILE C . n 
C 1 195 THR 195 208 208 THR THR C . n 
C 1 196 ALA 196 209 209 ALA ALA C . n 
C 1 197 TYR 197 210 210 TYR TYR C . n 
C 1 198 GLY 198 211 211 GLY GLY C . n 
C 1 199 GLU 199 212 212 GLU GLU C . n 
C 1 200 THR 200 213 213 THR THR C . n 
C 1 201 VAL 201 214 214 VAL VAL C . n 
C 1 202 PHE 202 215 215 PHE PHE C . n 
C 1 203 PRO 203 216 216 PRO PRO C . n 
C 1 204 ILE 204 217 217 ILE ILE C . n 
C 1 205 ASN 205 218 218 ASN ASN C . n 
C 1 206 LEU 206 219 219 LEU LEU C . n 
C 1 207 PHE 207 220 220 PHE PHE C . n 
C 1 208 VAL 208 221 221 VAL VAL C . n 
C 1 209 ASP 209 222 222 ASP ASP C . n 
C 1 210 GLY 210 223 223 GLY GLY C . n 
C 1 211 ARG 211 224 224 ARG ARG C . n 
C 1 212 VAL 212 225 225 VAL VAL C . n 
C 1 213 THR 213 226 226 THR THR C . n 
C 1 214 THR 214 227 227 THR THR C . n 
C 1 215 ASP 215 228 228 ASP ASP C . n 
C 1 216 ARG 216 229 229 ARG ARG C . n 
C 1 217 LYS 217 230 230 LYS LYS C . n 
C 1 218 LEU 218 231 231 LEU LEU C . n 
C 1 219 SER 219 232 232 SER SER C . n 
C 1 220 MET 220 233 233 MET MET C . n 
C 1 221 GLU 221 234 234 GLU GLU C . n 
C 1 222 ASP 222 235 235 ASP ASP C . n 
C 1 223 ALA 223 236 236 ALA ALA C . n 
C 1 224 ALA 224 237 237 ALA ALA C . n 
C 1 225 SER 225 238 238 SER SER C . n 
C 1 226 ILE 226 239 239 ILE ILE C . n 
C 1 227 PHE 227 240 240 PHE PHE C . n 
C 1 228 ARG 228 241 241 ARG ARG C . n 
C 1 229 ASP 229 242 242 ASP ASP C . n 
C 1 230 MET 230 243 243 MET MET C . n 
C 1 231 ARG 231 244 244 ARG ARG C . n 
C 1 232 PHE 232 245 245 PHE PHE C . n 
C 1 233 PRO 233 246 246 PRO PRO C . n 
C 1 234 ASP 234 247 247 ASP ASP C . n 
C 1 235 ASP 235 248 248 ASP ASP C . n 
C 1 236 PHE 236 249 249 PHE PHE C . n 
C 1 237 HIS 237 250 250 HIS HIS C . n 
C 1 238 ARG 238 251 251 ARG ARG C . n 
C 1 239 SER 239 252 252 SER SER C . n 
C 1 240 ALA 240 253 253 ALA ALA C . n 
C 1 241 VAL 241 254 254 VAL VAL C . n 
C 1 242 PRO 242 255 255 PRO PRO C . n 
C 1 243 ALA 243 256 256 ALA ALA C . n 
C 1 244 SER 244 257 257 SER SER C . n 
C 1 245 ASN 245 258 258 ASN ASN C . n 
C 1 246 GLU 246 259 259 GLU GLU C . n 
C 1 247 GLY 247 260 260 GLY GLY C . n 
C 1 248 ALA 248 261 261 ALA ALA C . n 
C 1 249 ASP 249 262 262 ASP ASP C . n 
C 1 250 GLN 250 263 263 GLN GLN C . n 
C 1 251 VAL 251 264 264 VAL VAL C . n 
C 1 252 LEU 252 265 265 LEU LEU C . n 
C 1 253 ALA 253 266 266 ALA ALA C . n 
C 1 254 ALA 254 267 267 ALA ALA C . n 
C 1 255 HIS 255 268 268 HIS HIS C . n 
C 1 256 PRO 256 269 269 PRO PRO C . n 
C 1 257 TRP 257 270 270 TRP TRP C . n 
C 1 258 VAL 258 271 271 VAL VAL C . n 
C 1 259 PRO 259 272 272 PRO PRO C . n 
C 1 260 GLY 260 273 273 GLY GLY C . n 
C 1 261 GLY 261 274 274 GLY GLY C . n 
C 1 262 ASN 262 275 275 ASN ASN C . n 
C 1 263 ALA 263 276 276 ALA ALA C . n 
C 1 264 ASP 264 277 277 ASP ASP C . n 
C 1 265 ASN 265 278 278 ASN ASN C . n 
C 1 266 GLN 266 279 279 GLN GLN C . n 
C 1 267 VAL 267 280 280 VAL VAL C . n 
C 1 268 ASN 268 281 281 ASN ASN C . n 
C 1 269 ASN 269 282 282 ASN ASN C . n 
C 1 270 TYR 270 283 283 TYR TYR C . n 
C 1 271 VAL 271 284 284 VAL VAL C . n 
C 1 272 GLU 272 285 285 GLU GLU C . n 
C 1 273 ASP 273 286 286 ASP ASP C . n 
C 1 274 PRO 274 287 287 PRO PRO C . n 
C 1 275 ASP 275 288 288 ASP ASP C . n 
C 1 276 SER 276 289 289 SER SER C . n 
C 1 277 ALA 277 290 290 ALA ALA C . n 
C 1 278 ASP 278 291 291 ASP ASP C . n 
C 1 279 PHE 279 292 292 PHE PHE C . n 
C 1 280 THR 280 293 293 THR THR C . n 
C 1 281 HIS 281 294 294 HIS HIS C . n 
C 1 282 LEU 282 295 295 LEU LEU C . n 
C 1 283 CYS 283 296 296 CYS CYS C . n 
C 1 284 ARG 284 297 297 ARG ARG C . n 
C 1 285 LEU 285 298 298 LEU LEU C . n 
C 1 286 TYR 286 299 299 TYR TYR C . n 
C 1 287 GLU 287 300 300 GLU GLU C . n 
C 1 288 PHE 288 301 301 PHE PHE C . n 
C 1 289 VAL 289 302 302 VAL VAL C . n 
C 1 290 VAL 290 303 303 VAL VAL C . n 
C 1 291 GLY 291 304 304 GLY GLY C . n 
C 1 292 SER 292 305 305 SER SER C . n 
C 1 293 VAL 293 306 306 VAL VAL C . n 
C 1 294 GLN 294 307 307 GLN GLN C . n 
C 1 295 GLU 295 308 308 GLU GLU C . n 
C 1 296 LEU 296 309 309 LEU LEU C . n 
C 1 297 TYR 297 310 310 TYR TYR C . n 
C 1 298 PRO 298 311 311 PRO PRO C . n 
C 1 299 ASN 299 312 312 ASN ASN C . n 
C 1 300 PRO 300 313 313 PRO PRO C . n 
C 1 301 THR 301 314 314 THR THR C . n 
C 1 302 GLY 302 315 315 GLY GLY C . n 
C 1 303 ILE 303 316 316 ILE ILE C . n 
C 1 304 LEU 304 317 317 LEU LEU C . n 
C 1 305 ARG 305 318 318 ARG ARG C . n 
C 1 306 ARG 306 319 319 ARG ARG C . n 
C 1 307 ASN 307 320 320 ASN ASN C . n 
C 1 308 LEU 308 321 321 LEU LEU C . n 
C 1 309 ILE 309 322 322 ILE ILE C . n 
C 1 310 LYS 310 323 323 LYS LYS C . n 
C 1 311 ASN 311 324 324 ASN ASN C . n 
C 1 312 LEU 312 325 325 LEU LEU C . n 
C 1 313 HIS 313 326 326 HIS HIS C . n 
C 1 314 TYR 314 327 327 TYR TYR C . n 
C 1 315 TRP 315 328 328 TRP TRP C . n 
C 1 316 TRP 316 329 329 TRP TRP C . n 
C 1 317 THR 317 330 330 THR THR C . n 
C 1 318 GLY 318 331 331 GLY GLY C . n 
C 1 319 VAL 319 332 332 VAL VAL C . n 
C 1 320 ASN 320 333 333 ASN ASN C . n 
C 1 321 VAL 321 334 334 VAL VAL C . n 
C 1 322 ALA 322 335 335 ALA ALA C . n 
C 1 323 PHE 323 336 336 PHE PHE C . n 
C 1 324 GLY 324 337 337 GLY GLY C . n 
C 1 325 GLY 325 338 338 GLY GLY C . n 
C 1 326 CYS 326 339 339 CYS CYS C . n 
C 1 327 ASP 327 340 340 ASP ASP C . n 
C 1 328 GLU 328 341 341 GLU GLU C . n 
C 1 329 LEU 329 342 342 LEU LEU C . n 
C 1 330 PHE 330 343 343 PHE PHE C . n 
C 1 331 PRO 331 344 344 PRO PRO C . n 
C 1 332 TYR 332 345 345 TYR TYR C . n 
C 1 333 GLY 333 346 346 GLY GLY C . n 
C 1 334 GLN 334 347 347 GLN GLN C . n 
C 1 335 LEU 335 348 348 LEU LEU C . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
D 2 NAG 1 H NAG 1 A NAG 402 n 
D 2 NAG 2 H NAG 2 A NAG 430 n 
D 2 BMA 3 H BMA 3 A BMA 431 n 
D 2 MAN 4 H MAN 4 A MAN 433 n 
D 2 MAN 5 H MAN 5 A MAN 432 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 2 NAG 1 Z NAG 1 B NAG 402 n 
F 2 NAG 2 Z NAG 2 B NAG 415 n 
F 2 BMA 3 Z BMA 3 B BMA 421 n 
F 2 MAN 4 Z MAN 4 B MAN 423 n 
F 2 MAN 5 Z MAN 5 B MAN 422 n 
G 4 NAG 1 a NAG 1 B NAG 404 n 
G 4 NAG 2 a NAG 2 B NAG 405 n 
G 4 BMA 3 a BMA 3 B BMA 406 n 
G 4 MAN 4 a MAN 4 B MAN 408 n 
G 4 MAN 5 a MAN 5 B MAN 409 n 
G 4 MAN 6 a MAN 6 B MAN 407 n 
H 5 NAG 1 q NAG 1 C NAG 402 n 
H 5 NAG 2 q NAG 2 C NAG 403 n 
H 5 BMA 3 q BMA 3 C BMA 407 n 
H 5 MAN 4 q MAN 4 C MAN 411 n 
I 6 NAG 1 s NAG 1 C NAG 404 n 
I 6 NAG 2 s NAG 2 C NAG 405 n 
I 6 BMA 3 s BMA 3 C BMA 406 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 C14 ? ? C14 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
J  7  HEM 1   401 401 HEM HEM A . 
K  8  GOL 1   402 422 GOL GOL A . 
L  8  GOL 1   403 423 GOL GOL A . 
M  9  C14 1   404 424 C14 C14 A . 
N  10 EPE 1   405 428 EPE EPE A . 
O  8  GOL 1   406 429 GOL GOL A . 
P  11 SO4 1   407 1   SO4 SO4 A . 
Q  11 SO4 1   408 3   SO4 SO4 A . 
R  12 MG  1   409 1   MG  MG  A . 
S  7  HEM 1   401 401 HEM HEM B . 
T  10 EPE 1   402 413 EPE EPE B . 
U  10 EPE 1   403 414 EPE EPE B . 
V  10 EPE 1   404 416 EPE EPE B . 
W  8  GOL 1   405 419 GOL GOL B . 
X  9  C14 1   406 420 C14 C14 B . 
Y  11 SO4 1   407 2   SO4 SO4 B . 
Z  11 SO4 1   408 4   SO4 SO4 B . 
AA 12 MG  1   409 2   MG  MG  B . 
BA 7  HEM 1   401 401 HEM HEM C . 
CA 8  GOL 1   402 412 GOL GOL C . 
DA 13 ACT 1   403 413 ACT ACT C . 
EA 10 EPE 1   404 414 EPE EPE C . 
FA 11 SO4 1   405 5   SO4 SO4 C . 
GA 12 MG  1   406 3   MG  MG  C . 
HA 14 HOH 1   501 244 HOH HOH A . 
HA 14 HOH 2   502 281 HOH HOH A . 
HA 14 HOH 3   503 182 HOH HOH A . 
HA 14 HOH 4   504 87  HOH HOH A . 
HA 14 HOH 5   505 106 HOH HOH A . 
HA 14 HOH 6   506 86  HOH HOH A . 
HA 14 HOH 7   507 107 HOH HOH A . 
HA 14 HOH 8   508 13  HOH HOH A . 
HA 14 HOH 9   509 280 HOH HOH A . 
HA 14 HOH 10  510 44  HOH HOH A . 
HA 14 HOH 11  511 145 HOH HOH A . 
HA 14 HOH 12  512 66  HOH HOH A . 
HA 14 HOH 13  513 144 HOH HOH A . 
HA 14 HOH 14  514 113 HOH HOH A . 
HA 14 HOH 15  515 79  HOH HOH A . 
HA 14 HOH 16  516 31  HOH HOH A . 
HA 14 HOH 17  517 116 HOH HOH A . 
HA 14 HOH 18  518 90  HOH HOH A . 
HA 14 HOH 19  519 143 HOH HOH A . 
HA 14 HOH 20  520 56  HOH HOH A . 
HA 14 HOH 21  521 117 HOH HOH A . 
HA 14 HOH 22  522 26  HOH HOH A . 
HA 14 HOH 23  523 53  HOH HOH A . 
HA 14 HOH 24  524 286 HOH HOH A . 
HA 14 HOH 25  525 102 HOH HOH A . 
HA 14 HOH 26  526 166 HOH HOH A . 
HA 14 HOH 27  527 262 HOH HOH A . 
HA 14 HOH 28  528 273 HOH HOH A . 
HA 14 HOH 29  529 147 HOH HOH A . 
HA 14 HOH 30  530 23  HOH HOH A . 
HA 14 HOH 31  531 249 HOH HOH A . 
HA 14 HOH 32  532 19  HOH HOH A . 
HA 14 HOH 33  533 111 HOH HOH A . 
HA 14 HOH 34  534 57  HOH HOH A . 
HA 14 HOH 35  535 261 HOH HOH A . 
HA 14 HOH 36  536 267 HOH HOH A . 
HA 14 HOH 37  537 22  HOH HOH A . 
HA 14 HOH 38  538 133 HOH HOH A . 
HA 14 HOH 39  539 68  HOH HOH A . 
HA 14 HOH 40  540 279 HOH HOH A . 
HA 14 HOH 41  541 10  HOH HOH A . 
HA 14 HOH 42  542 260 HOH HOH A . 
HA 14 HOH 43  543 152 HOH HOH A . 
HA 14 HOH 44  544 118 HOH HOH A . 
HA 14 HOH 45  545 28  HOH HOH A . 
HA 14 HOH 46  546 142 HOH HOH A . 
HA 14 HOH 47  547 64  HOH HOH A . 
HA 14 HOH 48  548 8   HOH HOH A . 
HA 14 HOH 49  549 3   HOH HOH A . 
HA 14 HOH 50  550 20  HOH HOH A . 
HA 14 HOH 51  551 63  HOH HOH A . 
HA 14 HOH 52  552 24  HOH HOH A . 
HA 14 HOH 53  553 84  HOH HOH A . 
HA 14 HOH 54  554 18  HOH HOH A . 
HA 14 HOH 55  555 153 HOH HOH A . 
HA 14 HOH 56  556 59  HOH HOH A . 
HA 14 HOH 57  557 114 HOH HOH A . 
HA 14 HOH 58  558 169 HOH HOH A . 
HA 14 HOH 59  559 9   HOH HOH A . 
HA 14 HOH 60  560 35  HOH HOH A . 
HA 14 HOH 61  561 170 HOH HOH A . 
HA 14 HOH 62  562 270 HOH HOH A . 
HA 14 HOH 63  563 209 HOH HOH A . 
HA 14 HOH 64  564 61  HOH HOH A . 
HA 14 HOH 65  565 7   HOH HOH A . 
HA 14 HOH 66  566 110 HOH HOH A . 
HA 14 HOH 67  567 21  HOH HOH A . 
HA 14 HOH 68  568 256 HOH HOH A . 
HA 14 HOH 69  569 98  HOH HOH A . 
HA 14 HOH 70  570 284 HOH HOH A . 
HA 14 HOH 71  571 47  HOH HOH A . 
HA 14 HOH 72  572 272 HOH HOH A . 
HA 14 HOH 73  573 129 HOH HOH A . 
HA 14 HOH 74  574 46  HOH HOH A . 
HA 14 HOH 75  575 264 HOH HOH A . 
HA 14 HOH 76  576 36  HOH HOH A . 
HA 14 HOH 77  577 75  HOH HOH A . 
HA 14 HOH 78  578 282 HOH HOH A . 
HA 14 HOH 79  579 89  HOH HOH A . 
HA 14 HOH 80  580 4   HOH HOH A . 
HA 14 HOH 81  581 55  HOH HOH A . 
HA 14 HOH 82  582 12  HOH HOH A . 
HA 14 HOH 83  583 67  HOH HOH A . 
HA 14 HOH 84  584 274 HOH HOH A . 
HA 14 HOH 85  585 277 HOH HOH A . 
HA 14 HOH 86  586 255 HOH HOH A . 
HA 14 HOH 87  587 95  HOH HOH A . 
HA 14 HOH 88  588 1   HOH HOH A . 
HA 14 HOH 89  589 70  HOH HOH A . 
HA 14 HOH 90  590 156 HOH HOH A . 
HA 14 HOH 91  591 77  HOH HOH A . 
HA 14 HOH 92  592 155 HOH HOH A . 
HA 14 HOH 93  593 100 HOH HOH A . 
HA 14 HOH 94  594 88  HOH HOH A . 
HA 14 HOH 95  595 130 HOH HOH A . 
HA 14 HOH 96  596 257 HOH HOH A . 
HA 14 HOH 97  597 128 HOH HOH A . 
HA 14 HOH 98  598 177 HOH HOH A . 
HA 14 HOH 99  599 141 HOH HOH A . 
HA 14 HOH 100 600 250 HOH HOH A . 
HA 14 HOH 101 601 269 HOH HOH A . 
HA 14 HOH 102 602 109 HOH HOH A . 
HA 14 HOH 103 603 258 HOH HOH A . 
HA 14 HOH 104 604 131 HOH HOH A . 
HA 14 HOH 105 605 276 HOH HOH A . 
HA 14 HOH 106 606 76  HOH HOH A . 
HA 14 HOH 107 607 132 HOH HOH A . 
HA 14 HOH 108 608 149 HOH HOH A . 
HA 14 HOH 109 609 172 HOH HOH A . 
HA 14 HOH 110 610 148 HOH HOH A . 
HA 14 HOH 111 611 275 HOH HOH A . 
HA 14 HOH 112 612 78  HOH HOH A . 
HA 14 HOH 113 613 243 HOH HOH A . 
HA 14 HOH 114 614 259 HOH HOH A . 
HA 14 HOH 115 615 150 HOH HOH A . 
HA 14 HOH 116 616 85  HOH HOH A . 
HA 14 HOH 117 617 119 HOH HOH A . 
HA 14 HOH 118 618 292 HOH HOH A . 
HA 14 HOH 119 619 232 HOH HOH A . 
HA 14 HOH 120 620 268 HOH HOH A . 
HA 14 HOH 121 621 291 HOH HOH A . 
HA 14 HOH 122 622 246 HOH HOH A . 
HA 14 HOH 123 623 271 HOH HOH A . 
HA 14 HOH 124 624 115 HOH HOH A . 
HA 14 HOH 125 625 265 HOH HOH A . 
HA 14 HOH 126 626 290 HOH HOH A . 
HA 14 HOH 127 627 289 HOH HOH A . 
HA 14 HOH 128 628 171 HOH HOH A . 
HA 14 HOH 129 629 112 HOH HOH A . 
HA 14 HOH 130 630 318 HOH HOH A . 
HA 14 HOH 131 631 164 HOH HOH A . 
HA 14 HOH 132 632 134 HOH HOH A . 
HA 14 HOH 133 633 266 HOH HOH A . 
HA 14 HOH 134 634 285 HOH HOH A . 
HA 14 HOH 135 635 151 HOH HOH A . 
HA 14 HOH 136 636 146 HOH HOH A . 
HA 14 HOH 137 637 94  HOH HOH A . 
HA 14 HOH 138 638 231 HOH HOH A . 
HA 14 HOH 139 639 200 HOH HOH A . 
HA 14 HOH 140 640 253 HOH HOH A . 
HA 14 HOH 141 641 165 HOH HOH A . 
HA 14 HOH 142 642 254 HOH HOH A . 
IA 14 HOH 1   501 248 HOH HOH B . 
IA 14 HOH 2   502 181 HOH HOH B . 
IA 14 HOH 3   503 93  HOH HOH B . 
IA 14 HOH 4   504 204 HOH HOH B . 
IA 14 HOH 5   505 138 HOH HOH B . 
IA 14 HOH 6   506 82  HOH HOH B . 
IA 14 HOH 7   507 183 HOH HOH B . 
IA 14 HOH 8   508 54  HOH HOH B . 
IA 14 HOH 9   509 105 HOH HOH B . 
IA 14 HOH 10  510 186 HOH HOH B . 
IA 14 HOH 11  511 41  HOH HOH B . 
IA 14 HOH 12  512 210 HOH HOH B . 
IA 14 HOH 13  513 193 HOH HOH B . 
IA 14 HOH 14  514 202 HOH HOH B . 
IA 14 HOH 15  515 99  HOH HOH B . 
IA 14 HOH 16  516 65  HOH HOH B . 
IA 14 HOH 17  517 11  HOH HOH B . 
IA 14 HOH 18  518 194 HOH HOH B . 
IA 14 HOH 19  519 203 HOH HOH B . 
IA 14 HOH 20  520 180 HOH HOH B . 
IA 14 HOH 21  521 212 HOH HOH B . 
IA 14 HOH 22  522 198 HOH HOH B . 
IA 14 HOH 23  523 27  HOH HOH B . 
IA 14 HOH 24  524 300 HOH HOH B . 
IA 14 HOH 25  525 62  HOH HOH B . 
IA 14 HOH 26  526 81  HOH HOH B . 
IA 14 HOH 27  527 96  HOH HOH B . 
IA 14 HOH 28  528 167 HOH HOH B . 
IA 14 HOH 29  529 296 HOH HOH B . 
IA 14 HOH 30  530 60  HOH HOH B . 
IA 14 HOH 31  531 188 HOH HOH B . 
IA 14 HOH 32  532 299 HOH HOH B . 
IA 14 HOH 33  533 69  HOH HOH B . 
IA 14 HOH 34  534 206 HOH HOH B . 
IA 14 HOH 35  535 191 HOH HOH B . 
IA 14 HOH 36  536 40  HOH HOH B . 
IA 14 HOH 37  537 33  HOH HOH B . 
IA 14 HOH 38  538 211 HOH HOH B . 
IA 14 HOH 39  539 184 HOH HOH B . 
IA 14 HOH 40  540 190 HOH HOH B . 
IA 14 HOH 41  541 304 HOH HOH B . 
IA 14 HOH 42  542 120 HOH HOH B . 
IA 14 HOH 43  543 207 HOH HOH B . 
IA 14 HOH 44  544 195 HOH HOH B . 
IA 14 HOH 45  545 187 HOH HOH B . 
IA 14 HOH 46  546 25  HOH HOH B . 
IA 14 HOH 47  547 45  HOH HOH B . 
IA 14 HOH 48  548 49  HOH HOH B . 
IA 14 HOH 49  549 17  HOH HOH B . 
IA 14 HOH 50  550 185 HOH HOH B . 
IA 14 HOH 51  551 2   HOH HOH B . 
IA 14 HOH 52  552 196 HOH HOH B . 
IA 14 HOH 53  553 197 HOH HOH B . 
IA 14 HOH 54  554 163 HOH HOH B . 
IA 14 HOH 55  555 159 HOH HOH B . 
IA 14 HOH 56  556 92  HOH HOH B . 
IA 14 HOH 57  557 192 HOH HOH B . 
IA 14 HOH 58  558 302 HOH HOH B . 
IA 14 HOH 59  559 214 HOH HOH B . 
IA 14 HOH 60  560 189 HOH HOH B . 
IA 14 HOH 61  561 178 HOH HOH B . 
IA 14 HOH 62  562 199 HOH HOH B . 
IA 14 HOH 63  563 104 HOH HOH B . 
IA 14 HOH 64  564 157 HOH HOH B . 
IA 14 HOH 65  565 5   HOH HOH B . 
IA 14 HOH 66  566 278 HOH HOH B . 
IA 14 HOH 67  567 48  HOH HOH B . 
IA 14 HOH 68  568 301 HOH HOH B . 
IA 14 HOH 69  569 160 HOH HOH B . 
IA 14 HOH 70  570 205 HOH HOH B . 
IA 14 HOH 71  571 101 HOH HOH B . 
IA 14 HOH 72  572 213 HOH HOH B . 
IA 14 HOH 73  573 52  HOH HOH B . 
IA 14 HOH 74  574 247 HOH HOH B . 
IA 14 HOH 75  575 307 HOH HOH B . 
IA 14 HOH 76  576 122 HOH HOH B . 
IA 14 HOH 77  577 303 HOH HOH B . 
IA 14 HOH 78  578 295 HOH HOH B . 
IA 14 HOH 79  579 263 HOH HOH B . 
IA 14 HOH 80  580 108 HOH HOH B . 
IA 14 HOH 81  581 306 HOH HOH B . 
IA 14 HOH 82  582 161 HOH HOH B . 
IA 14 HOH 83  583 313 HOH HOH B . 
IA 14 HOH 84  584 74  HOH HOH B . 
IA 14 HOH 85  585 83  HOH HOH B . 
IA 14 HOH 86  586 175 HOH HOH B . 
IA 14 HOH 87  587 305 HOH HOH B . 
IA 14 HOH 88  588 121 HOH HOH B . 
IA 14 HOH 89  589 251 HOH HOH B . 
IA 14 HOH 90  590 174 HOH HOH B . 
IA 14 HOH 91  591 139 HOH HOH B . 
IA 14 HOH 92  592 42  HOH HOH B . 
IA 14 HOH 93  593 91  HOH HOH B . 
IA 14 HOH 94  594 293 HOH HOH B . 
IA 14 HOH 95  595 162 HOH HOH B . 
IA 14 HOH 96  596 158 HOH HOH B . 
IA 14 HOH 97  597 298 HOH HOH B . 
IA 14 HOH 98  598 173 HOH HOH B . 
IA 14 HOH 99  599 288 HOH HOH B . 
IA 14 HOH 100 600 103 HOH HOH B . 
IA 14 HOH 101 601 314 HOH HOH B . 
IA 14 HOH 102 602 97  HOH HOH B . 
IA 14 HOH 103 603 294 HOH HOH B . 
JA 14 HOH 1   501 235 HOH HOH C . 
JA 14 HOH 2   502 14  HOH HOH C . 
JA 14 HOH 3   503 136 HOH HOH C . 
JA 14 HOH 4   504 50  HOH HOH C . 
JA 14 HOH 5   505 34  HOH HOH C . 
JA 14 HOH 6   506 126 HOH HOH C . 
JA 14 HOH 7   507 15  HOH HOH C . 
JA 14 HOH 8   508 225 HOH HOH C . 
JA 14 HOH 9   509 238 HOH HOH C . 
JA 14 HOH 10  510 80  HOH HOH C . 
JA 14 HOH 11  511 32  HOH HOH C . 
JA 14 HOH 12  512 58  HOH HOH C . 
JA 14 HOH 13  513 71  HOH HOH C . 
JA 14 HOH 14  514 240 HOH HOH C . 
JA 14 HOH 15  515 127 HOH HOH C . 
JA 14 HOH 16  516 43  HOH HOH C . 
JA 14 HOH 17  517 30  HOH HOH C . 
JA 14 HOH 18  518 39  HOH HOH C . 
JA 14 HOH 19  519 16  HOH HOH C . 
JA 14 HOH 20  520 208 HOH HOH C . 
JA 14 HOH 21  521 242 HOH HOH C . 
JA 14 HOH 22  522 73  HOH HOH C . 
JA 14 HOH 23  523 137 HOH HOH C . 
JA 14 HOH 24  524 237 HOH HOH C . 
JA 14 HOH 25  525 6   HOH HOH C . 
JA 14 HOH 26  526 236 HOH HOH C . 
JA 14 HOH 27  527 72  HOH HOH C . 
JA 14 HOH 28  528 310 HOH HOH C . 
JA 14 HOH 29  529 215 HOH HOH C . 
JA 14 HOH 30  530 29  HOH HOH C . 
JA 14 HOH 31  531 228 HOH HOH C . 
JA 14 HOH 32  532 216 HOH HOH C . 
JA 14 HOH 33  533 179 HOH HOH C . 
JA 14 HOH 34  534 227 HOH HOH C . 
JA 14 HOH 35  535 37  HOH HOH C . 
JA 14 HOH 36  536 51  HOH HOH C . 
JA 14 HOH 37  537 38  HOH HOH C . 
JA 14 HOH 38  538 218 HOH HOH C . 
JA 14 HOH 39  539 245 HOH HOH C . 
JA 14 HOH 40  540 252 HOH HOH C . 
JA 14 HOH 41  541 223 HOH HOH C . 
JA 14 HOH 42  542 230 HOH HOH C . 
JA 14 HOH 43  543 311 HOH HOH C . 
JA 14 HOH 44  544 123 HOH HOH C . 
JA 14 HOH 45  545 316 HOH HOH C . 
JA 14 HOH 46  546 219 HOH HOH C . 
JA 14 HOH 47  547 220 HOH HOH C . 
JA 14 HOH 48  548 168 HOH HOH C . 
JA 14 HOH 49  549 135 HOH HOH C . 
JA 14 HOH 50  550 297 HOH HOH C . 
JA 14 HOH 51  551 241 HOH HOH C . 
JA 14 HOH 52  552 124 HOH HOH C . 
JA 14 HOH 53  553 222 HOH HOH C . 
JA 14 HOH 54  554 176 HOH HOH C . 
JA 14 HOH 55  555 140 HOH HOH C . 
JA 14 HOH 56  556 233 HOH HOH C . 
JA 14 HOH 57  557 317 HOH HOH C . 
JA 14 HOH 58  558 224 HOH HOH C . 
JA 14 HOH 59  559 221 HOH HOH C . 
JA 14 HOH 60  560 229 HOH HOH C . 
JA 14 HOH 61  561 234 HOH HOH C . 
JA 14 HOH 62  562 283 HOH HOH C . 
JA 14 HOH 63  563 309 HOH HOH C . 
JA 14 HOH 64  564 226 HOH HOH C . 
JA 14 HOH 65  565 239 HOH HOH C . 
JA 14 HOH 66  566 217 HOH HOH C . 
JA 14 HOH 67  567 308 HOH HOH C . 
JA 14 HOH 68  568 154 HOH HOH C . 
JA 14 HOH 69  569 315 HOH HOH C . 
JA 14 HOH 70  570 201 HOH HOH C . 
JA 14 HOH 71  571 125 HOH HOH C . 
JA 14 HOH 72  572 312 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                   111.75 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HEB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     272.422 
_cell.length_a_esd                 ? 
_cell.length_b                     75.256 
_cell.length_b_esd                 ? 
_cell.length_c                     106.362 
_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                         9HEB 
_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                   9HEB 
_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             4.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.73 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.85M ammonium sulphate, 100 mM HEPES pH 7.5; additive: 30% v/v ethylene glycol

Soaking: 35 mM tetradecane 3 hours, cryoprotected with 20% glycerol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'KB MIRRORS' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    M 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HEB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               48.69 
_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                                     64697 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.90 
_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                                0.169 
_reflns.pdbx_Rpim_I_all                                0.073 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.152 
_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                                    2.55 
_reflns_shell.d_res_low                                     2.61 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4538 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.3 
_reflns_shell.pdbx_chi_squared                              0.61 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.827 
_reflns_shell.pdbx_Rpim_I_all                               0.357 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.869 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.744 
_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]                            -3.86 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            5.52 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.26 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.344 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_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                                 9HEB 
_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                            2.55 
_refine.ls_d_res_low                             48.69 
_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                     61532 
_refine.ls_number_reflns_R_free                  3165 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.60 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19018 
_refine.ls_R_factor_R_free                       0.22490 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18837 
_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                       0.286 
_refine.pdbx_overall_ESU_R_Free                  0.222 
_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                             9.919 
_refine.overall_SU_ML                            0.199 
_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                       2.55 
_refine_hist.d_res_low                        48.69 
_refine_hist.number_atoms_solvent             317 
_refine_hist.number_atoms_total               8750 
_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        8405 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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  8833  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7782  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.455  1.844  12175 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.529  1.741  18025 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.498  5.000  1040  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.840  5.000  50    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.348 10.000 1124  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.200  1342  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  10344 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2088  ? 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' ? 3.203  4.393  4056  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.201  4.392  4055  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.922  7.899  5073  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.923  7.900  5074  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.330  5.165  4777  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.242  5.154  4755  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.583  9.313  7054  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.855  42.87  9543  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.849  42.89  9521  ? 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                       2.550 
_refine_ls_shell.d_res_low                        2.616 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             202 
_refine_ls_shell.number_reflns_R_work             4539 
_refine_ls_shell.percent_reflns_obs               98.14 
_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                  0.286 
_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                  0.334 
# 
_struct.entry_id                     9HEB 
_struct.title                        
'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II) in complex with tetradecane' 
_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        9HEB 
_struct_keywords.text            'Peroxygenase, peroxidase, complex, tetradecane, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 1  ? 
D  N N 2  ? 
E  N N 3  ? 
F  N N 2  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 6  ? 
J  N N 7  ? 
K  N N 8  ? 
L  N N 8  ? 
M  N N 9  ? 
N  N N 10 ? 
O  N N 8  ? 
P  N N 11 ? 
Q  N N 11 ? 
R  N N 12 ? 
S  N N 7  ? 
T  N N 10 ? 
U  N N 10 ? 
V  N N 10 ? 
W  N N 8  ? 
X  N N 9  ? 
Y  N N 11 ? 
Z  N N 11 ? 
AA N N 12 ? 
BA N N 7  ? 
CA N N 8  ? 
DA N N 13 ? 
EA N N 10 ? 
FA N N 11 ? 
GA N N 12 ? 
HA N N 14 ? 
IA N N 14 ? 
JA N N 14 ? 
# 
_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 9HEB A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HEB B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HEB 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,HA  
2 1 B,F,G,S,T,U,V,W,X,Y,Z,AA,IA 
3 1 C,H,I,BA,CA,DA,EA,FA,GA,JA  
# 
_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 ? GLU A 199 ? ASN A 203 GLU A 212 1 ? 10 
HELX_P HELX_P9  AA9 VAL A 201 ? PHE A 207 ? VAL A 214 PHE A 220 1 ? 7  
HELX_P HELX_P10 AB1 SER A 219 ? ARG A 228 ? SER A 232 ARG A 241 1 ? 10 
HELX_P HELX_P11 AB2 GLY A 247 ? HIS A 255 ? GLY A 260 HIS A 268 1 ? 9  
HELX_P HELX_P12 AB3 LEU A 282 ? TYR A 297 ? LEU A 295 TYR A 310 1 ? 16 
HELX_P HELX_P13 AB4 GLY A 302 ? PHE A 323 ? GLY A 315 PHE A 336 1 ? 22 
HELX_P HELX_P14 AB5 CYS B 39  ? HIS B 48  ? CYS B 52  HIS B 61  1 ? 10 
HELX_P HELX_P15 AB6 THR B 58  ? ASN B 71  ? THR B 71  ASN B 84  1 ? 14 
HELX_P HELX_P16 AB7 GLU B 73  ? GLY B 89  ? GLU B 86  GLY B 102 1 ? 17 
HELX_P HELX_P17 AB8 THR B 102 ? GLY B 106 ? THR B 115 GLY B 119 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 134 ? GLY B 138 ? ASP B 147 GLY B 151 5 ? 5  
HELX_P HELX_P19 AC1 ASN B 144 ? GLY B 159 ? ASN B 157 GLY B 172 1 ? 16 
HELX_P HELX_P20 AC2 ASN B 164 ? ASN B 183 ? ASN B 177 ASN B 196 1 ? 20 
HELX_P HELX_P21 AC3 ASN B 190 ? GLU B 199 ? ASN B 203 GLU B 212 1 ? 10 
HELX_P HELX_P22 AC4 VAL B 201 ? PHE B 207 ? VAL B 214 PHE B 220 1 ? 7  
HELX_P HELX_P23 AC5 SER B 219 ? ARG B 228 ? SER B 232 ARG B 241 1 ? 10 
HELX_P HELX_P24 AC6 GLY B 247 ? HIS B 255 ? GLY B 260 HIS B 268 1 ? 9  
HELX_P HELX_P25 AC7 LEU B 282 ? TYR B 297 ? LEU B 295 TYR B 310 1 ? 16 
HELX_P HELX_P26 AC8 GLY B 302 ? PHE B 323 ? GLY B 315 PHE B 336 1 ? 22 
HELX_P HELX_P27 AC9 CYS C 39  ? HIS C 48  ? CYS C 52  HIS C 61  1 ? 10 
HELX_P HELX_P28 AD1 THR C 58  ? ASN C 71  ? THR C 71  ASN C 84  1 ? 14 
HELX_P HELX_P29 AD2 GLU C 73  ? GLY C 89  ? GLU C 86  GLY C 102 1 ? 17 
HELX_P HELX_P30 AD3 THR C 102 ? GLY C 106 ? THR C 115 GLY C 119 5 ? 5  
HELX_P HELX_P31 AD4 ASP C 134 ? GLY C 138 ? ASP C 147 GLY C 151 5 ? 5  
HELX_P HELX_P32 AD5 ASN C 144 ? GLY C 159 ? ASN C 157 GLY C 172 1 ? 16 
HELX_P HELX_P33 AD6 ASN C 164 ? ASN C 183 ? ASN C 177 ASN C 196 1 ? 20 
HELX_P HELX_P34 AD7 ASN C 190 ? GLU C 199 ? ASN C 203 GLU C 212 1 ? 10 
HELX_P HELX_P35 AD8 VAL C 201 ? PHE C 207 ? VAL C 214 PHE C 220 1 ? 7  
HELX_P HELX_P36 AD9 SER C 219 ? ARG C 228 ? SER C 232 ARG C 241 1 ? 10 
HELX_P HELX_P37 AE1 GLY C 247 ? HIS C 255 ? GLY C 260 HIS C 268 1 ? 9  
HELX_P HELX_P38 AE2 LEU C 282 ? TYR C 297 ? LEU C 295 TYR C 310 1 ? 16 
HELX_P HELX_P39 AE3 GLY C 302 ? PHE C 323 ? GLY C 315 PHE C 336 1 ? 22 
# 
_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 ? ? ? ? ? ? ? 2.108 ? ? 
disulf2  disulf ?    ? B  CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
disulf3  disulf ?    ? C  CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
covale1  covale one  ? A  ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 H NAG 1   1_555 ? ? ? ? ? ? ? 1.449 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 I NAG 1   1_555 ? ? ? ? ? ? ? 1.434 ? 
N-Glycosylation 
covale3  covale one  ? B  ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 Z NAG 1   1_555 ? ? ? ? ? ? ? 1.514 ? 
N-Glycosylation 
covale4  covale one  ? B  ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 a NAG 1   1_555 ? ? ? ? ? ? ? 1.539 ? 
N-Glycosylation 
covale5  covale one  ? C  ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 q NAG 1   1_555 ? ? ? ? ? ? ? 1.445 ? 
N-Glycosylation 
covale6  covale one  ? C  ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 s NAG 1   1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale7  covale both ? D  NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale8  covale both ? D  NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale9  covale both ? D  BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? H BMA 3   H MAN 4   1_555 ? ? ? ? ? ? ? 1.400 ? ? 
covale10 covale both ? D  BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? H BMA 3   H MAN 5   1_555 ? ? ? ? ? ? ? 1.408 ? ? 
covale11 covale both ? E  NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
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 ? ? ? ? ? ? ? 1.407 ? ? 
covale14 covale both ? E  BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 7   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
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 ? ? ? ? ? ? ? 1.410 ? ? 
covale17 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? Z NAG 1   Z NAG 2   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale18 covale both ? F  NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? Z NAG 2   Z BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale19 covale both ? F  BMA .   O3  ? ? ? 1_555 F  MAN .   C1 ? ? Z BMA 3   Z MAN 4   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale20 covale both ? F  BMA .   O6  ? ? ? 1_555 F  MAN .   C1 ? ? Z BMA 3   Z MAN 5   1_555 ? ? ? ? ? ? ? 1.414 ? ? 
covale21 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? a NAG 1   a NAG 2   1_555 ? ? ? ? ? ? ? 1.390 ? ? 
covale22 covale both ? G  NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? a NAG 2   a BMA 3   1_555 ? ? ? ? ? ? ? 1.390 ? ? 
covale23 covale both ? G  BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? a BMA 3   a MAN 4   1_555 ? ? ? ? ? ? ? 1.404 ? ? 
covale24 covale both ? G  BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? a BMA 3   a MAN 6   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale25 covale both ? G  MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? a MAN 4   a MAN 5   1_555 ? ? ? ? ? ? ? 1.391 ? ? 
covale26 covale both ? H  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? q NAG 1   q NAG 2   1_555 ? ? ? ? ? ? ? 1.376 ? ? 
covale27 covale both ? H  NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? q NAG 2   q BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale28 covale both ? H  BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? q BMA 3   q MAN 4   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale29 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? s NAG 1   s NAG 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale30 covale both ? I  NAG .   O4  ? ? ? 1_555 I  BMA .   C1 ? ? s NAG 2   s BMA 3   1_555 ? ? ? ? ? ? ? 1.400 ? ? 
metalc1  metalc ?    ? A  CYS 39  SG  ? ? ? 1_555 J  HEM .   FE ? ? A CYS 52  A HEM 401 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc2  metalc ?    ? A  GLU 125 OE2 ? ? ? 1_555 R  MG  .   MG ? ? A GLU 138 A MG  409 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc3  metalc ?    ? A  GLY 126 O   ? ? ? 1_555 R  MG  .   MG ? ? A GLY 139 A MG  409 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc4  metalc ?    ? J  HEM .   O1A ? ? ? 1_555 R  MG  .   MG ? ? A HEM 401 A MG  409 1_555 ? ? ? ? ? ? ? 2.674 ? ? 
metalc5  metalc ?    ? R  MG  .   MG  ? ? ? 1_555 HA HOH .   O  ? ? A MG  409 A HOH 503 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc6  metalc ?    ? B  CYS 39  SG  ? ? ? 1_555 S  HEM .   FE ? ? B CYS 52  B HEM 401 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc7  metalc ?    ? B  GLU 125 OE2 ? ? ? 1_555 AA MG  .   MG ? ? B GLU 138 B MG  409 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc8  metalc ?    ? B  GLY 126 O   ? ? ? 1_555 AA MG  .   MG ? ? B GLY 139 B MG  409 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc9  metalc ?    ? S  HEM .   O1A ? ? ? 1_555 AA MG  .   MG ? ? B HEM 401 B MG  409 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc10 metalc ?    ? AA MG  .   MG  ? ? ? 1_555 IA HOH .   O  ? ? B MG  409 B HOH 502 1_555 ? ? ? ? ? ? ? 1.844 ? ? 
metalc11 metalc ?    ? C  CYS 39  SG  ? ? ? 1_555 BA HEM .   FE ? ? C CYS 52  C HEM 401 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
metalc12 metalc ?    ? C  GLU 125 OE2 ? ? ? 1_555 GA MG  .   MG ? ? C GLU 138 C MG  406 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc13 metalc ?    ? C  GLY 126 O   ? ? ? 1_555 GA MG  .   MG ? ? C GLY 139 C MG  406 1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc14 metalc ?    ? BA HEM .   O2A ? ? ? 1_555 GA MG  .   MG ? ? C HEM 401 C MG  406 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NA  ? J  HEM .   ? A HEM 401 ? 1_555 98.8  ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NB  ? J  HEM .   ? A HEM 401 ? 1_555 90.2  ? 
3  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NB  ? J  HEM .   ? A HEM 401 ? 1_555 88.4  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 88.1  ? 
5  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 171.3 ? 
6  NB  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 NC  ? J  HEM .   ? A HEM 401 ? 1_555 86.4  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 95.9  ? 
8  NA  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 93.6  ? 
9  NB  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 173.2 ? 
10 NC  ? J  HEM .   ? A HEM 401 ? 1_555 FE ? J  HEM . ? A HEM 401 ? 1_555 ND  ? J  HEM .   ? A HEM 401 ? 1_555 90.8  ? 
11 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 66.9  ? 
12 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O1A ? J  HEM .   ? A HEM 401 ? 1_555 69.3  ? 
13 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O1A ? J  HEM .   ? A HEM 401 ? 1_555 73.7  ? 
14 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O   ? HA HOH .   ? A HOH 503 ? 1_555 65.5  ? 
15 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O   ? HA HOH .   ? A HOH 503 ? 1_555 122.7 ? 
16 O1A ? J  HEM .   ? A HEM 401 ? 1_555 MG ? R  MG  . ? A MG  409 ? 1_555 O   ? HA HOH .   ? A HOH 503 ? 1_555 61.1  ? 
17 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NA  ? S  HEM .   ? B HEM 401 ? 1_555 99.1  ? 
18 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NB  ? S  HEM .   ? B HEM 401 ? 1_555 88.7  ? 
19 NA  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NB  ? S  HEM .   ? B HEM 401 ? 1_555 87.6  ? 
20 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NC  ? S  HEM .   ? B HEM 401 ? 1_555 84.5  ? 
21 NA  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NC  ? S  HEM .   ? B HEM 401 ? 1_555 174.4 ? 
22 NB  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 NC  ? S  HEM .   ? B HEM 401 ? 1_555 88.2  ? 
23 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 ND  ? S  HEM .   ? B HEM 401 ? 1_555 94.7  ? 
24 NA  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 ND  ? S  HEM .   ? B HEM 401 ? 1_555 92.1  ? 
25 NB  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 ND  ? S  HEM .   ? B HEM 401 ? 1_555 176.6 ? 
26 NC  ? S  HEM .   ? B HEM 401 ? 1_555 FE ? S  HEM . ? B HEM 401 ? 1_555 ND  ? S  HEM .   ? B HEM 401 ? 1_555 91.9  ? 
27 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 69.7  ? 
28 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O1A ? S  HEM .   ? B HEM 401 ? 1_555 78.6  ? 
29 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O1A ? S  HEM .   ? B HEM 401 ? 1_555 81.7  ? 
30 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O   ? IA HOH .   ? B HOH 502 ? 1_555 66.0  ? 
31 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O   ? IA HOH .   ? B HOH 502 ? 1_555 126.0 ? 
32 O1A ? S  HEM .   ? B HEM 401 ? 1_555 MG ? AA MG  . ? B MG  409 ? 1_555 O   ? IA HOH .   ? B HOH 502 ? 1_555 60.9  ? 
33 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NA  ? BA HEM .   ? C HEM 401 ? 1_555 97.8  ? 
34 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NB  ? BA HEM .   ? C HEM 401 ? 1_555 89.1  ? 
35 NA  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NB  ? BA HEM .   ? C HEM 401 ? 1_555 87.5  ? 
36 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NC  ? BA HEM .   ? C HEM 401 ? 1_555 86.6  ? 
37 NA  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NC  ? BA HEM .   ? C HEM 401 ? 1_555 173.3 ? 
38 NB  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 NC  ? BA HEM .   ? C HEM 401 ? 1_555 87.5  ? 
39 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 ND  ? BA HEM .   ? C HEM 401 ? 1_555 93.1  ? 
40 NA  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 ND  ? BA HEM .   ? C HEM 401 ? 1_555 94.5  ? 
41 NB  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 ND  ? BA HEM .   ? C HEM 401 ? 1_555 176.8 ? 
42 NC  ? BA HEM .   ? C HEM 401 ? 1_555 FE ? BA HEM . ? C HEM 401 ? 1_555 ND  ? BA HEM .   ? C HEM 401 ? 1_555 90.3  ? 
43 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? GA MG  . ? C MG  406 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 68.3  ? 
44 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? GA MG  . ? C MG  406 ? 1_555 O2A ? BA HEM .   ? C HEM 401 ? 1_555 90.2  ? 
45 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? GA MG  . ? C MG  406 ? 1_555 O2A ? BA HEM .   ? C HEM 401 ? 1_555 90.6  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG D .   ? ASN A 144 ? NAG H 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG I 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG Z 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG a 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG q 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG s 1   ? 1_555 ASN C 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 283 ? CYS A 326 ? CYS A 296 ? 1_555 CYS A 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 283 ? CYS B 326 ? CYS B 296 ? 1_555 CYS B 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS C 283 ? CYS C 326 ? CYS C 296 ? 1_555 CYS C 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 111 A . ? PRO 124 A PRO 112 A ? PRO 125 A 1 5.44 
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 3.11 
# 
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                   9HEB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 B ASP 262 ? ? O B HOH 501 ? ? 2.03 
2 1 OD1 A ASP 262 ? ? O A HOH 501 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH2 A ARG 145 ? ? 123.82 120.30 3.52  0.50 N 
2 1 NE C ARG 318 ? B CZ C ARG 318 ? B NH2 C ARG 318 ? B 117.23 120.30 -3.07 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 127 ? ? -131.47 -40.45  
2  1 PHE A 137 ? ? -108.36 -78.88  
3  1 ASP A 152 ? ? -160.13 112.54  
4  1 ASN A 203 ? ? 60.88   -124.21 
5  1 SER A 257 ? ? -158.76 -98.11  
6  1 ASN A 281 ? ? 39.30   47.35   
7  1 ASN A 282 ? ? -142.22 52.04   
8  1 ASN A 312 ? ? -157.96 61.95   
9  1 ASP B 107 ? ? 70.61   37.95   
10 1 HIS B 127 ? ? -131.25 -42.59  
11 1 PHE B 137 ? ? -106.58 -77.86  
12 1 ASN B 203 ? ? 62.05   -124.84 
13 1 PRO B 246 ? ? -49.41  153.62  
14 1 SER B 257 ? ? -159.34 -98.16  
15 1 ASN B 281 ? ? 39.31   46.01   
16 1 ASN B 282 ? ? -140.77 52.23   
17 1 ASN B 312 ? ? -156.92 63.15   
18 1 ASP C 107 ? ? 71.38   37.58   
19 1 HIS C 127 ? ? -132.88 -40.77  
20 1 PHE C 137 ? ? -108.40 -79.20  
21 1 ASN C 203 ? ? 61.04   -124.37 
22 1 PRO C 246 ? ? -48.47  154.35  
23 1 SER C 257 ? ? -157.56 -97.85  
24 1 ASN C 281 ? ? 39.29   45.85   
25 1 ASN C 282 ? ? -140.60 52.22   
26 1 ASN C 312 ? ? -158.80 61.60   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 603 ? 6.25 . 
2 1 O ? C HOH 571 ? 5.86 . 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
BMA C1   C  N R 81  
BMA C2   C  N S 82  
BMA C3   C  N S 83  
BMA C4   C  N S 84  
BMA C5   C  N R 85  
BMA C6   C  N N 86  
BMA O1   O  N N 87  
BMA O2   O  N N 88  
BMA O3   O  N N 89  
BMA O4   O  N N 90  
BMA O5   O  N N 91  
BMA O6   O  N N 92  
BMA H1   H  N N 93  
BMA H2   H  N N 94  
BMA H3   H  N N 95  
BMA H4   H  N N 96  
BMA H5   H  N N 97  
BMA H61  H  N N 98  
BMA H62  H  N N 99  
BMA HO1  H  N N 100 
BMA HO2  H  N N 101 
BMA HO3  H  N N 102 
BMA HO4  H  N N 103 
BMA HO6  H  N N 104 
C14 C01  C  N N 105 
C14 C02  C  N N 106 
C14 C03  C  N N 107 
C14 C04  C  N N 108 
C14 C05  C  N N 109 
C14 C06  C  N N 110 
C14 C07  C  N N 111 
C14 C08  C  N N 112 
C14 C09  C  N N 113 
C14 C10  C  N N 114 
C14 C11  C  N N 115 
C14 C12  C  N N 116 
C14 C13  C  N N 117 
C14 C14  C  N N 118 
C14 H011 H  N N 119 
C14 H012 H  N N 120 
C14 H013 H  N N 121 
C14 H021 H  N N 122 
C14 H022 H  N N 123 
C14 H031 H  N N 124 
C14 H032 H  N N 125 
C14 H041 H  N N 126 
C14 H042 H  N N 127 
C14 H051 H  N N 128 
C14 H052 H  N N 129 
C14 H061 H  N N 130 
C14 H062 H  N N 131 
C14 H071 H  N N 132 
C14 H072 H  N N 133 
C14 H081 H  N N 134 
C14 H082 H  N N 135 
C14 H091 H  N N 136 
C14 H092 H  N N 137 
C14 H101 H  N N 138 
C14 H102 H  N N 139 
C14 H111 H  N N 140 
C14 H112 H  N N 141 
C14 H121 H  N N 142 
C14 H122 H  N N 143 
C14 H131 H  N N 144 
C14 H132 H  N N 145 
C14 H141 H  N N 146 
C14 H142 H  N N 147 
C14 H143 H  N N 148 
CYS N    N  N N 149 
CYS CA   C  N R 150 
CYS C    C  N N 151 
CYS O    O  N N 152 
CYS CB   C  N N 153 
CYS SG   S  N N 154 
CYS OXT  O  N N 155 
CYS H    H  N N 156 
CYS H2   H  N N 157 
CYS HA   H  N N 158 
CYS HB2  H  N N 159 
CYS HB3  H  N N 160 
CYS HG   H  N N 161 
CYS HXT  H  N N 162 
EPE N1   N  N N 163 
EPE C2   C  N N 164 
EPE C3   C  N N 165 
EPE N4   N  N N 166 
EPE C5   C  N N 167 
EPE C6   C  N N 168 
EPE C7   C  N N 169 
EPE C8   C  N N 170 
EPE O8   O  N N 171 
EPE C9   C  N N 172 
EPE C10  C  N N 173 
EPE S    S  N N 174 
EPE O1S  O  N N 175 
EPE O2S  O  N N 176 
EPE O3S  O  N N 177 
EPE H21  H  N N 178 
EPE H22  H  N N 179 
EPE H31  H  N N 180 
EPE H32  H  N N 181 
EPE H51  H  N N 182 
EPE H52  H  N N 183 
EPE H61  H  N N 184 
EPE H62  H  N N 185 
EPE H71  H  N N 186 
EPE H72  H  N N 187 
EPE H81  H  N N 188 
EPE H82  H  N N 189 
EPE HO8  H  N N 190 
EPE H91  H  N N 191 
EPE H92  H  N N 192 
EPE H101 H  N N 193 
EPE H102 H  N N 194 
EPE HOS3 H  N N 195 
GLN N    N  N N 196 
GLN CA   C  N S 197 
GLN C    C  N N 198 
GLN O    O  N N 199 
GLN CB   C  N N 200 
GLN CG   C  N N 201 
GLN CD   C  N N 202 
GLN OE1  O  N N 203 
GLN NE2  N  N N 204 
GLN OXT  O  N N 205 
GLN H    H  N N 206 
GLN H2   H  N N 207 
GLN HA   H  N N 208 
GLN HB2  H  N N 209 
GLN HB3  H  N N 210 
GLN HG2  H  N N 211 
GLN HG3  H  N N 212 
GLN HE21 H  N N 213 
GLN HE22 H  N N 214 
GLN HXT  H  N N 215 
GLU N    N  N N 216 
GLU CA   C  N S 217 
GLU C    C  N N 218 
GLU O    O  N N 219 
GLU CB   C  N N 220 
GLU CG   C  N N 221 
GLU CD   C  N N 222 
GLU OE1  O  N N 223 
GLU OE2  O  N N 224 
GLU OXT  O  N N 225 
GLU H    H  N N 226 
GLU H2   H  N N 227 
GLU HA   H  N N 228 
GLU HB2  H  N N 229 
GLU HB3  H  N N 230 
GLU HG2  H  N N 231 
GLU HG3  H  N N 232 
GLU HE2  H  N N 233 
GLU HXT  H  N N 234 
GLY N    N  N N 235 
GLY CA   C  N N 236 
GLY C    C  N N 237 
GLY O    O  N N 238 
GLY OXT  O  N N 239 
GLY H    H  N N 240 
GLY H2   H  N N 241 
GLY HA2  H  N N 242 
GLY HA3  H  N N 243 
GLY HXT  H  N N 244 
GOL C1   C  N N 245 
GOL O1   O  N N 246 
GOL C2   C  N N 247 
GOL O2   O  N N 248 
GOL C3   C  N N 249 
GOL O3   O  N N 250 
GOL H11  H  N N 251 
GOL H12  H  N N 252 
GOL HO1  H  N N 253 
GOL H2   H  N N 254 
GOL HO2  H  N N 255 
GOL H31  H  N N 256 
GOL H32  H  N N 257 
GOL HO3  H  N N 258 
HEM CHA  C  N N 259 
HEM CHB  C  N N 260 
HEM CHC  C  N N 261 
HEM CHD  C  N N 262 
HEM C1A  C  Y N 263 
HEM C2A  C  Y N 264 
HEM C3A  C  Y N 265 
HEM C4A  C  Y N 266 
HEM CMA  C  N N 267 
HEM CAA  C  N N 268 
HEM CBA  C  N N 269 
HEM CGA  C  N N 270 
HEM O1A  O  N N 271 
HEM O2A  O  N N 272 
HEM C1B  C  N N 273 
HEM C2B  C  N N 274 
HEM C3B  C  N N 275 
HEM C4B  C  N N 276 
HEM CMB  C  N N 277 
HEM CAB  C  N N 278 
HEM CBB  C  N N 279 
HEM C1C  C  Y N 280 
HEM C2C  C  Y N 281 
HEM C3C  C  Y N 282 
HEM C4C  C  Y N 283 
HEM CMC  C  N N 284 
HEM CAC  C  N N 285 
HEM CBC  C  N N 286 
HEM C1D  C  N N 287 
HEM C2D  C  N N 288 
HEM C3D  C  N N 289 
HEM C4D  C  N N 290 
HEM CMD  C  N N 291 
HEM CAD  C  N N 292 
HEM CBD  C  N N 293 
HEM CGD  C  N N 294 
HEM O1D  O  N N 295 
HEM O2D  O  N N 296 
HEM NA   N  Y N 297 
HEM NB   N  N N 298 
HEM NC   N  Y N 299 
HEM ND   N  N N 300 
HEM FE   FE N N 301 
HEM HHB  H  N N 302 
HEM HHC  H  N N 303 
HEM HHD  H  N N 304 
HEM HMA  H  N N 305 
HEM HMAA H  N N 306 
HEM HMAB H  N N 307 
HEM HAA  H  N N 308 
HEM HAAA H  N N 309 
HEM HBA  H  N N 310 
HEM HBAA H  N N 311 
HEM HMB  H  N N 312 
HEM HMBA H  N N 313 
HEM HMBB H  N N 314 
HEM HAB  H  N N 315 
HEM HBB  H  N N 316 
HEM HBBA H  N N 317 
HEM HMC  H  N N 318 
HEM HMCA H  N N 319 
HEM HMCB H  N N 320 
HEM HAC  H  N N 321 
HEM HBC  H  N N 322 
HEM HBCA H  N N 323 
HEM HMD  H  N N 324 
HEM HMDA H  N N 325 
HEM HMDB H  N N 326 
HEM HAD  H  N N 327 
HEM HADA H  N N 328 
HEM HBD  H  N N 329 
HEM HBDA H  N N 330 
HEM H2A  H  N N 331 
HEM H2D  H  N N 332 
HEM HHA  H  N N 333 
HIS N    N  N N 334 
HIS CA   C  N S 335 
HIS C    C  N N 336 
HIS O    O  N N 337 
HIS CB   C  N N 338 
HIS CG   C  Y N 339 
HIS ND1  N  Y N 340 
HIS CD2  C  Y N 341 
HIS CE1  C  Y N 342 
HIS NE2  N  Y N 343 
HIS OXT  O  N N 344 
HIS H    H  N N 345 
HIS H2   H  N N 346 
HIS HA   H  N N 347 
HIS HB2  H  N N 348 
HIS HB3  H  N N 349 
HIS HD1  H  N N 350 
HIS HD2  H  N N 351 
HIS HE1  H  N N 352 
HIS HE2  H  N N 353 
HIS HXT  H  N N 354 
HOH O    O  N N 355 
HOH H1   H  N N 356 
HOH H2   H  N N 357 
ILE N    N  N N 358 
ILE CA   C  N S 359 
ILE C    C  N N 360 
ILE O    O  N N 361 
ILE CB   C  N S 362 
ILE CG1  C  N N 363 
ILE CG2  C  N N 364 
ILE CD1  C  N N 365 
ILE OXT  O  N N 366 
ILE H    H  N N 367 
ILE H2   H  N N 368 
ILE HA   H  N N 369 
ILE HB   H  N N 370 
ILE HG12 H  N N 371 
ILE HG13 H  N N 372 
ILE HG21 H  N N 373 
ILE HG22 H  N N 374 
ILE HG23 H  N N 375 
ILE HD11 H  N N 376 
ILE HD12 H  N N 377 
ILE HD13 H  N N 378 
ILE HXT  H  N N 379 
LEU N    N  N N 380 
LEU CA   C  N S 381 
LEU C    C  N N 382 
LEU O    O  N N 383 
LEU CB   C  N N 384 
LEU CG   C  N N 385 
LEU CD1  C  N N 386 
LEU CD2  C  N N 387 
LEU OXT  O  N N 388 
LEU H    H  N N 389 
LEU H2   H  N N 390 
LEU HA   H  N N 391 
LEU HB2  H  N N 392 
LEU HB3  H  N N 393 
LEU HG   H  N N 394 
LEU HD11 H  N N 395 
LEU HD12 H  N N 396 
LEU HD13 H  N N 397 
LEU HD21 H  N N 398 
LEU HD22 H  N N 399 
LEU HD23 H  N N 400 
LEU HXT  H  N N 401 
LYS N    N  N N 402 
LYS CA   C  N S 403 
LYS C    C  N N 404 
LYS O    O  N N 405 
LYS CB   C  N N 406 
LYS CG   C  N N 407 
LYS CD   C  N N 408 
LYS CE   C  N N 409 
LYS NZ   N  N N 410 
LYS OXT  O  N N 411 
LYS H    H  N N 412 
LYS H2   H  N N 413 
LYS HA   H  N N 414 
LYS HB2  H  N N 415 
LYS HB3  H  N N 416 
LYS HG2  H  N N 417 
LYS HG3  H  N N 418 
LYS HD2  H  N N 419 
LYS HD3  H  N N 420 
LYS HE2  H  N N 421 
LYS HE3  H  N N 422 
LYS HZ1  H  N N 423 
LYS HZ2  H  N N 424 
LYS HZ3  H  N N 425 
LYS HXT  H  N N 426 
MAN C1   C  N S 427 
MAN C2   C  N S 428 
MAN C3   C  N S 429 
MAN C4   C  N S 430 
MAN C5   C  N R 431 
MAN C6   C  N N 432 
MAN O1   O  N N 433 
MAN O2   O  N N 434 
MAN O3   O  N N 435 
MAN O4   O  N N 436 
MAN O5   O  N N 437 
MAN O6   O  N N 438 
MAN H1   H  N N 439 
MAN H2   H  N N 440 
MAN H3   H  N N 441 
MAN H4   H  N N 442 
MAN H5   H  N N 443 
MAN H61  H  N N 444 
MAN H62  H  N N 445 
MAN HO1  H  N N 446 
MAN HO2  H  N N 447 
MAN HO3  H  N N 448 
MAN HO4  H  N N 449 
MAN HO6  H  N N 450 
MET N    N  N N 451 
MET CA   C  N S 452 
MET C    C  N N 453 
MET O    O  N N 454 
MET CB   C  N N 455 
MET CG   C  N N 456 
MET SD   S  N N 457 
MET CE   C  N N 458 
MET OXT  O  N N 459 
MET H    H  N N 460 
MET H2   H  N N 461 
MET HA   H  N N 462 
MET HB2  H  N N 463 
MET HB3  H  N N 464 
MET HG2  H  N N 465 
MET HG3  H  N N 466 
MET HE1  H  N N 467 
MET HE2  H  N N 468 
MET HE3  H  N N 469 
MET HXT  H  N N 470 
MG  MG   MG N N 471 
NAG C1   C  N R 472 
NAG C2   C  N R 473 
NAG C3   C  N R 474 
NAG C4   C  N S 475 
NAG C5   C  N R 476 
NAG C6   C  N N 477 
NAG C7   C  N N 478 
NAG C8   C  N N 479 
NAG N2   N  N N 480 
NAG O1   O  N N 481 
NAG O3   O  N N 482 
NAG O4   O  N N 483 
NAG O5   O  N N 484 
NAG O6   O  N N 485 
NAG O7   O  N N 486 
NAG H1   H  N N 487 
NAG H2   H  N N 488 
NAG H3   H  N N 489 
NAG H4   H  N N 490 
NAG H5   H  N N 491 
NAG H61  H  N N 492 
NAG H62  H  N N 493 
NAG H81  H  N N 494 
NAG H82  H  N N 495 
NAG H83  H  N N 496 
NAG HN2  H  N N 497 
NAG HO1  H  N N 498 
NAG HO3  H  N N 499 
NAG HO4  H  N N 500 
NAG HO6  H  N N 501 
PHE N    N  N N 502 
PHE CA   C  N S 503 
PHE C    C  N N 504 
PHE O    O  N N 505 
PHE CB   C  N N 506 
PHE CG   C  Y N 507 
PHE CD1  C  Y N 508 
PHE CD2  C  Y N 509 
PHE CE1  C  Y N 510 
PHE CE2  C  Y N 511 
PHE CZ   C  Y N 512 
PHE OXT  O  N N 513 
PHE H    H  N N 514 
PHE H2   H  N N 515 
PHE HA   H  N N 516 
PHE HB2  H  N N 517 
PHE HB3  H  N N 518 
PHE HD1  H  N N 519 
PHE HD2  H  N N 520 
PHE HE1  H  N N 521 
PHE HE2  H  N N 522 
PHE HZ   H  N N 523 
PHE HXT  H  N N 524 
PRO N    N  N N 525 
PRO CA   C  N S 526 
PRO C    C  N N 527 
PRO O    O  N N 528 
PRO CB   C  N N 529 
PRO CG   C  N N 530 
PRO CD   C  N N 531 
PRO OXT  O  N N 532 
PRO H    H  N N 533 
PRO HA   H  N N 534 
PRO HB2  H  N N 535 
PRO HB3  H  N N 536 
PRO HG2  H  N N 537 
PRO HG3  H  N N 538 
PRO HD2  H  N N 539 
PRO HD3  H  N N 540 
PRO HXT  H  N N 541 
SER N    N  N N 542 
SER CA   C  N S 543 
SER C    C  N N 544 
SER O    O  N N 545 
SER CB   C  N N 546 
SER OG   O  N N 547 
SER OXT  O  N N 548 
SER H    H  N N 549 
SER H2   H  N N 550 
SER HA   H  N N 551 
SER HB2  H  N N 552 
SER HB3  H  N N 553 
SER HG   H  N N 554 
SER HXT  H  N N 555 
SO4 S    S  N N 556 
SO4 O1   O  N N 557 
SO4 O2   O  N N 558 
SO4 O3   O  N N 559 
SO4 O4   O  N N 560 
THR N    N  N N 561 
THR CA   C  N S 562 
THR C    C  N N 563 
THR O    O  N N 564 
THR CB   C  N R 565 
THR OG1  O  N N 566 
THR CG2  C  N N 567 
THR OXT  O  N N 568 
THR H    H  N N 569 
THR H2   H  N N 570 
THR HA   H  N N 571 
THR HB   H  N N 572 
THR HG1  H  N N 573 
THR HG21 H  N N 574 
THR HG22 H  N N 575 
THR HG23 H  N N 576 
THR HXT  H  N N 577 
TRP N    N  N N 578 
TRP CA   C  N S 579 
TRP C    C  N N 580 
TRP O    O  N N 581 
TRP CB   C  N N 582 
TRP CG   C  Y N 583 
TRP CD1  C  Y N 584 
TRP CD2  C  Y N 585 
TRP NE1  N  Y N 586 
TRP CE2  C  Y N 587 
TRP CE3  C  Y N 588 
TRP CZ2  C  Y N 589 
TRP CZ3  C  Y N 590 
TRP CH2  C  Y N 591 
TRP OXT  O  N N 592 
TRP H    H  N N 593 
TRP H2   H  N N 594 
TRP HA   H  N N 595 
TRP HB2  H  N N 596 
TRP HB3  H  N N 597 
TRP HD1  H  N N 598 
TRP HE1  H  N N 599 
TRP HE3  H  N N 600 
TRP HZ2  H  N N 601 
TRP HZ3  H  N N 602 
TRP HH2  H  N N 603 
TRP HXT  H  N N 604 
TYR N    N  N N 605 
TYR CA   C  N S 606 
TYR C    C  N N 607 
TYR O    O  N N 608 
TYR CB   C  N N 609 
TYR CG   C  Y N 610 
TYR CD1  C  Y N 611 
TYR CD2  C  Y N 612 
TYR CE1  C  Y N 613 
TYR CE2  C  Y N 614 
TYR CZ   C  Y N 615 
TYR OH   O  N N 616 
TYR OXT  O  N N 617 
TYR H    H  N N 618 
TYR H2   H  N N 619 
TYR HA   H  N N 620 
TYR HB2  H  N N 621 
TYR HB3  H  N N 622 
TYR HD1  H  N N 623 
TYR HD2  H  N N 624 
TYR HE1  H  N N 625 
TYR HE2  H  N N 626 
TYR HH   H  N N 627 
TYR HXT  H  N N 628 
VAL N    N  N N 629 
VAL CA   C  N S 630 
VAL C    C  N N 631 
VAL O    O  N N 632 
VAL CB   C  N N 633 
VAL CG1  C  N N 634 
VAL CG2  C  N N 635 
VAL OXT  O  N N 636 
VAL H    H  N N 637 
VAL H2   H  N N 638 
VAL HA   H  N N 639 
VAL HB   H  N N 640 
VAL HG11 H  N N 641 
VAL HG12 H  N N 642 
VAL HG13 H  N N 643 
VAL HG21 H  N N 644 
VAL HG22 H  N N 645 
VAL HG23 H  N N 646 
VAL HXT  H  N N 647 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
BMA C1  C2   sing N N 76  
BMA C1  O1   sing N N 77  
BMA C1  O5   sing N N 78  
BMA C1  H1   sing N N 79  
BMA C2  C3   sing N N 80  
BMA C2  O2   sing N N 81  
BMA C2  H2   sing N N 82  
BMA C3  C4   sing N N 83  
BMA C3  O3   sing N N 84  
BMA C3  H3   sing N N 85  
BMA C4  C5   sing N N 86  
BMA C4  O4   sing N N 87  
BMA C4  H4   sing N N 88  
BMA C5  C6   sing N N 89  
BMA C5  O5   sing N N 90  
BMA C5  H5   sing N N 91  
BMA C6  O6   sing N N 92  
BMA C6  H61  sing N N 93  
BMA C6  H62  sing N N 94  
BMA O1  HO1  sing N N 95  
BMA O2  HO2  sing N N 96  
BMA O3  HO3  sing N N 97  
BMA O4  HO4  sing N N 98  
BMA O6  HO6  sing N N 99  
C14 C01 C02  sing N N 100 
C14 C01 H011 sing N N 101 
C14 C01 H012 sing N N 102 
C14 C01 H013 sing N N 103 
C14 C02 C03  sing N N 104 
C14 C02 H021 sing N N 105 
C14 C02 H022 sing N N 106 
C14 C03 C04  sing N N 107 
C14 C03 H031 sing N N 108 
C14 C03 H032 sing N N 109 
C14 C04 C05  sing N N 110 
C14 C04 H041 sing N N 111 
C14 C04 H042 sing N N 112 
C14 C05 C06  sing N N 113 
C14 C05 H051 sing N N 114 
C14 C05 H052 sing N N 115 
C14 C06 C07  sing N N 116 
C14 C06 H061 sing N N 117 
C14 C06 H062 sing N N 118 
C14 C07 C08  sing N N 119 
C14 C07 H071 sing N N 120 
C14 C07 H072 sing N N 121 
C14 C08 C09  sing N N 122 
C14 C08 H081 sing N N 123 
C14 C08 H082 sing N N 124 
C14 C09 C10  sing N N 125 
C14 C09 H091 sing N N 126 
C14 C09 H092 sing N N 127 
C14 C10 C11  sing N N 128 
C14 C10 H101 sing N N 129 
C14 C10 H102 sing N N 130 
C14 C11 C12  sing N N 131 
C14 C11 H111 sing N N 132 
C14 C11 H112 sing N N 133 
C14 C12 C13  sing N N 134 
C14 C12 H121 sing N N 135 
C14 C12 H122 sing N N 136 
C14 C13 C14  sing N N 137 
C14 C13 H131 sing N N 138 
C14 C13 H132 sing N N 139 
C14 C14 H141 sing N N 140 
C14 C14 H142 sing N N 141 
C14 C14 H143 sing N N 142 
CYS N   CA   sing N N 143 
CYS N   H    sing N N 144 
CYS N   H2   sing N N 145 
CYS CA  C    sing N N 146 
CYS CA  CB   sing N N 147 
CYS CA  HA   sing N N 148 
CYS C   O    doub N N 149 
CYS C   OXT  sing N N 150 
CYS CB  SG   sing N N 151 
CYS CB  HB2  sing N N 152 
CYS CB  HB3  sing N N 153 
CYS SG  HG   sing N N 154 
CYS OXT HXT  sing N N 155 
EPE N1  C2   sing N N 156 
EPE N1  C6   sing N N 157 
EPE N1  C9   sing N N 158 
EPE C2  C3   sing N N 159 
EPE C2  H21  sing N N 160 
EPE C2  H22  sing N N 161 
EPE C3  N4   sing N N 162 
EPE C3  H31  sing N N 163 
EPE C3  H32  sing N N 164 
EPE N4  C5   sing N N 165 
EPE N4  C7   sing N N 166 
EPE C5  C6   sing N N 167 
EPE C5  H51  sing N N 168 
EPE C5  H52  sing N N 169 
EPE C6  H61  sing N N 170 
EPE C6  H62  sing N N 171 
EPE C7  C8   sing N N 172 
EPE C7  H71  sing N N 173 
EPE C7  H72  sing N N 174 
EPE C8  O8   sing N N 175 
EPE C8  H81  sing N N 176 
EPE C8  H82  sing N N 177 
EPE O8  HO8  sing N N 178 
EPE C9  C10  sing N N 179 
EPE C9  H91  sing N N 180 
EPE C9  H92  sing N N 181 
EPE C10 S    sing N N 182 
EPE C10 H101 sing N N 183 
EPE C10 H102 sing N N 184 
EPE S   O1S  doub N N 185 
EPE S   O2S  doub N N 186 
EPE S   O3S  sing N N 187 
EPE O3S HOS3 sing N N 188 
GLN N   CA   sing N N 189 
GLN N   H    sing N N 190 
GLN N   H2   sing N N 191 
GLN CA  C    sing N N 192 
GLN CA  CB   sing N N 193 
GLN CA  HA   sing N N 194 
GLN C   O    doub N N 195 
GLN C   OXT  sing N N 196 
GLN CB  CG   sing N N 197 
GLN CB  HB2  sing N N 198 
GLN CB  HB3  sing N N 199 
GLN CG  CD   sing N N 200 
GLN CG  HG2  sing N N 201 
GLN CG  HG3  sing N N 202 
GLN CD  OE1  doub N N 203 
GLN CD  NE2  sing N N 204 
GLN NE2 HE21 sing N N 205 
GLN NE2 HE22 sing N N 206 
GLN OXT HXT  sing N N 207 
GLU N   CA   sing N N 208 
GLU N   H    sing N N 209 
GLU N   H2   sing N N 210 
GLU CA  C    sing N N 211 
GLU CA  CB   sing N N 212 
GLU CA  HA   sing N N 213 
GLU C   O    doub N N 214 
GLU C   OXT  sing N N 215 
GLU CB  CG   sing N N 216 
GLU CB  HB2  sing N N 217 
GLU CB  HB3  sing N N 218 
GLU CG  CD   sing N N 219 
GLU CG  HG2  sing N N 220 
GLU CG  HG3  sing N N 221 
GLU CD  OE1  doub N N 222 
GLU CD  OE2  sing N N 223 
GLU OE2 HE2  sing N N 224 
GLU OXT HXT  sing N N 225 
GLY N   CA   sing N N 226 
GLY N   H    sing N N 227 
GLY N   H2   sing N N 228 
GLY CA  C    sing N N 229 
GLY CA  HA2  sing N N 230 
GLY CA  HA3  sing N N 231 
GLY C   O    doub N N 232 
GLY C   OXT  sing N N 233 
GLY OXT HXT  sing N N 234 
GOL C1  O1   sing N N 235 
GOL C1  C2   sing N N 236 
GOL C1  H11  sing N N 237 
GOL C1  H12  sing N N 238 
GOL O1  HO1  sing N N 239 
GOL C2  O2   sing N N 240 
GOL C2  C3   sing N N 241 
GOL C2  H2   sing N N 242 
GOL O2  HO2  sing N N 243 
GOL C3  O3   sing N N 244 
GOL C3  H31  sing N N 245 
GOL C3  H32  sing N N 246 
GOL O3  HO3  sing N N 247 
HEM CHA C1A  sing N N 248 
HEM CHA C4D  doub N N 249 
HEM CHA HHA  sing N N 250 
HEM CHB C4A  sing N N 251 
HEM CHB C1B  doub N N 252 
HEM CHB HHB  sing N N 253 
HEM CHC C4B  sing N N 254 
HEM CHC C1C  doub N N 255 
HEM CHC HHC  sing N N 256 
HEM CHD C4C  doub N N 257 
HEM CHD C1D  sing N N 258 
HEM CHD HHD  sing N N 259 
HEM C1A C2A  doub Y N 260 
HEM C1A NA   sing Y N 261 
HEM C2A C3A  sing Y N 262 
HEM C2A CAA  sing N N 263 
HEM C3A C4A  doub Y N 264 
HEM C3A CMA  sing N N 265 
HEM C4A NA   sing Y N 266 
HEM CMA HMA  sing N N 267 
HEM CMA HMAA sing N N 268 
HEM CMA HMAB sing N N 269 
HEM CAA CBA  sing N N 270 
HEM CAA HAA  sing N N 271 
HEM CAA HAAA sing N N 272 
HEM CBA CGA  sing N N 273 
HEM CBA HBA  sing N N 274 
HEM CBA HBAA sing N N 275 
HEM CGA O1A  doub N N 276 
HEM CGA O2A  sing N N 277 
HEM C1B C2B  sing N N 278 
HEM C1B NB   sing N N 279 
HEM C2B C3B  doub N N 280 
HEM C2B CMB  sing N N 281 
HEM C3B C4B  sing N N 282 
HEM C3B CAB  sing N N 283 
HEM C4B NB   doub N N 284 
HEM CMB HMB  sing N N 285 
HEM CMB HMBA sing N N 286 
HEM CMB HMBB sing N N 287 
HEM CAB CBB  doub N N 288 
HEM CAB HAB  sing N N 289 
HEM CBB HBB  sing N N 290 
HEM CBB HBBA sing N N 291 
HEM C1C C2C  sing Y N 292 
HEM C1C NC   sing Y N 293 
HEM C2C C3C  doub Y N 294 
HEM C2C CMC  sing N N 295 
HEM C3C C4C  sing Y N 296 
HEM C3C CAC  sing N N 297 
HEM C4C NC   sing Y N 298 
HEM CMC HMC  sing N N 299 
HEM CMC HMCA sing N N 300 
HEM CMC HMCB sing N N 301 
HEM CAC CBC  doub N N 302 
HEM CAC HAC  sing N N 303 
HEM CBC HBC  sing N N 304 
HEM CBC HBCA sing N N 305 
HEM C1D C2D  sing N N 306 
HEM C1D ND   doub N N 307 
HEM C2D C3D  doub N N 308 
HEM C2D CMD  sing N N 309 
HEM C3D C4D  sing N N 310 
HEM C3D CAD  sing N N 311 
HEM C4D ND   sing N N 312 
HEM CMD HMD  sing N N 313 
HEM CMD HMDA sing N N 314 
HEM CMD HMDB sing N N 315 
HEM CAD CBD  sing N N 316 
HEM CAD HAD  sing N N 317 
HEM CAD HADA sing N N 318 
HEM CBD CGD  sing N N 319 
HEM CBD HBD  sing N N 320 
HEM CBD HBDA sing N N 321 
HEM CGD O1D  doub N N 322 
HEM CGD O2D  sing N N 323 
HEM O2A H2A  sing N N 324 
HEM O2D H2D  sing N N 325 
HEM FE  NA   sing N N 326 
HEM FE  NB   sing N N 327 
HEM FE  NC   sing N N 328 
HEM FE  ND   sing N N 329 
HIS N   CA   sing N N 330 
HIS N   H    sing N N 331 
HIS N   H2   sing N N 332 
HIS CA  C    sing N N 333 
HIS CA  CB   sing N N 334 
HIS CA  HA   sing N N 335 
HIS C   O    doub N N 336 
HIS C   OXT  sing N N 337 
HIS CB  CG   sing N N 338 
HIS CB  HB2  sing N N 339 
HIS CB  HB3  sing N N 340 
HIS CG  ND1  sing Y N 341 
HIS CG  CD2  doub Y N 342 
HIS ND1 CE1  doub Y N 343 
HIS ND1 HD1  sing N N 344 
HIS CD2 NE2  sing Y N 345 
HIS CD2 HD2  sing N N 346 
HIS CE1 NE2  sing Y N 347 
HIS CE1 HE1  sing N N 348 
HIS NE2 HE2  sing N N 349 
HIS OXT HXT  sing N N 350 
HOH O   H1   sing N N 351 
HOH O   H2   sing N N 352 
ILE N   CA   sing N N 353 
ILE N   H    sing N N 354 
ILE N   H2   sing N N 355 
ILE CA  C    sing N N 356 
ILE CA  CB   sing N N 357 
ILE CA  HA   sing N N 358 
ILE C   O    doub N N 359 
ILE C   OXT  sing N N 360 
ILE CB  CG1  sing N N 361 
ILE CB  CG2  sing N N 362 
ILE CB  HB   sing N N 363 
ILE CG1 CD1  sing N N 364 
ILE CG1 HG12 sing N N 365 
ILE CG1 HG13 sing N N 366 
ILE CG2 HG21 sing N N 367 
ILE CG2 HG22 sing N N 368 
ILE CG2 HG23 sing N N 369 
ILE CD1 HD11 sing N N 370 
ILE CD1 HD12 sing N N 371 
ILE CD1 HD13 sing N N 372 
ILE OXT HXT  sing N N 373 
LEU N   CA   sing N N 374 
LEU N   H    sing N N 375 
LEU N   H2   sing N N 376 
LEU CA  C    sing N N 377 
LEU CA  CB   sing N N 378 
LEU CA  HA   sing N N 379 
LEU C   O    doub N N 380 
LEU C   OXT  sing N N 381 
LEU CB  CG   sing N N 382 
LEU CB  HB2  sing N N 383 
LEU CB  HB3  sing N N 384 
LEU CG  CD1  sing N N 385 
LEU CG  CD2  sing N N 386 
LEU CG  HG   sing N N 387 
LEU CD1 HD11 sing N N 388 
LEU CD1 HD12 sing N N 389 
LEU CD1 HD13 sing N N 390 
LEU CD2 HD21 sing N N 391 
LEU CD2 HD22 sing N N 392 
LEU CD2 HD23 sing N N 393 
LEU OXT HXT  sing N N 394 
LYS N   CA   sing N N 395 
LYS N   H    sing N N 396 
LYS N   H2   sing N N 397 
LYS CA  C    sing N N 398 
LYS CA  CB   sing N N 399 
LYS CA  HA   sing N N 400 
LYS C   O    doub N N 401 
LYS C   OXT  sing N N 402 
LYS CB  CG   sing N N 403 
LYS CB  HB2  sing N N 404 
LYS CB  HB3  sing N N 405 
LYS CG  CD   sing N N 406 
LYS CG  HG2  sing N N 407 
LYS CG  HG3  sing N N 408 
LYS CD  CE   sing N N 409 
LYS CD  HD2  sing N N 410 
LYS CD  HD3  sing N N 411 
LYS CE  NZ   sing N N 412 
LYS CE  HE2  sing N N 413 
LYS CE  HE3  sing N N 414 
LYS NZ  HZ1  sing N N 415 
LYS NZ  HZ2  sing N N 416 
LYS NZ  HZ3  sing N N 417 
LYS OXT HXT  sing N N 418 
MAN C1  C2   sing N N 419 
MAN C1  O1   sing N N 420 
MAN C1  O5   sing N N 421 
MAN C1  H1   sing N N 422 
MAN C2  C3   sing N N 423 
MAN C2  O2   sing N N 424 
MAN C2  H2   sing N N 425 
MAN C3  C4   sing N N 426 
MAN C3  O3   sing N N 427 
MAN C3  H3   sing N N 428 
MAN C4  C5   sing N N 429 
MAN C4  O4   sing N N 430 
MAN C4  H4   sing N N 431 
MAN C5  C6   sing N N 432 
MAN C5  O5   sing N N 433 
MAN C5  H5   sing N N 434 
MAN C6  O6   sing N N 435 
MAN C6  H61  sing N N 436 
MAN C6  H62  sing N N 437 
MAN O1  HO1  sing N N 438 
MAN O2  HO2  sing N N 439 
MAN O3  HO3  sing N N 440 
MAN O4  HO4  sing N N 441 
MAN O6  HO6  sing N N 442 
MET N   CA   sing N N 443 
MET N   H    sing N N 444 
MET N   H2   sing N N 445 
MET CA  C    sing N N 446 
MET CA  CB   sing N N 447 
MET CA  HA   sing N N 448 
MET C   O    doub N N 449 
MET C   OXT  sing N N 450 
MET CB  CG   sing N N 451 
MET CB  HB2  sing N N 452 
MET CB  HB3  sing N N 453 
MET CG  SD   sing N N 454 
MET CG  HG2  sing N N 455 
MET CG  HG3  sing N N 456 
MET SD  CE   sing N N 457 
MET CE  HE1  sing N N 458 
MET CE  HE2  sing N N 459 
MET CE  HE3  sing N N 460 
MET OXT HXT  sing N N 461 
NAG C1  C2   sing N N 462 
NAG C1  O1   sing N N 463 
NAG C1  O5   sing N N 464 
NAG C1  H1   sing N N 465 
NAG C2  C3   sing N N 466 
NAG C2  N2   sing N N 467 
NAG C2  H2   sing N N 468 
NAG C3  C4   sing N N 469 
NAG C3  O3   sing N N 470 
NAG C3  H3   sing N N 471 
NAG C4  C5   sing N N 472 
NAG C4  O4   sing N N 473 
NAG C4  H4   sing N N 474 
NAG C5  C6   sing N N 475 
NAG C5  O5   sing N N 476 
NAG C5  H5   sing N N 477 
NAG C6  O6   sing N N 478 
NAG C6  H61  sing N N 479 
NAG C6  H62  sing N N 480 
NAG C7  C8   sing N N 481 
NAG C7  N2   sing N N 482 
NAG C7  O7   doub N N 483 
NAG C8  H81  sing N N 484 
NAG C8  H82  sing N N 485 
NAG C8  H83  sing N N 486 
NAG N2  HN2  sing N N 487 
NAG O1  HO1  sing N N 488 
NAG O3  HO3  sing N N 489 
NAG O4  HO4  sing N N 490 
NAG O6  HO6  sing N N 491 
PHE N   CA   sing N N 492 
PHE N   H    sing N N 493 
PHE N   H2   sing N N 494 
PHE CA  C    sing N N 495 
PHE CA  CB   sing N N 496 
PHE CA  HA   sing N N 497 
PHE C   O    doub N N 498 
PHE C   OXT  sing N N 499 
PHE CB  CG   sing N N 500 
PHE CB  HB2  sing N N 501 
PHE CB  HB3  sing N N 502 
PHE CG  CD1  doub Y N 503 
PHE CG  CD2  sing Y N 504 
PHE CD1 CE1  sing Y N 505 
PHE CD1 HD1  sing N N 506 
PHE CD2 CE2  doub Y N 507 
PHE CD2 HD2  sing N N 508 
PHE CE1 CZ   doub Y N 509 
PHE CE1 HE1  sing N N 510 
PHE CE2 CZ   sing Y N 511 
PHE CE2 HE2  sing N N 512 
PHE CZ  HZ   sing N N 513 
PHE OXT HXT  sing N N 514 
PRO N   CA   sing N N 515 
PRO N   CD   sing N N 516 
PRO N   H    sing N N 517 
PRO CA  C    sing N N 518 
PRO CA  CB   sing N N 519 
PRO CA  HA   sing N N 520 
PRO C   O    doub N N 521 
PRO C   OXT  sing N N 522 
PRO CB  CG   sing N N 523 
PRO CB  HB2  sing N N 524 
PRO CB  HB3  sing N N 525 
PRO CG  CD   sing N N 526 
PRO CG  HG2  sing N N 527 
PRO CG  HG3  sing N N 528 
PRO CD  HD2  sing N N 529 
PRO CD  HD3  sing N N 530 
PRO OXT HXT  sing N N 531 
SER N   CA   sing N N 532 
SER N   H    sing N N 533 
SER N   H2   sing N N 534 
SER CA  C    sing N N 535 
SER CA  CB   sing N N 536 
SER CA  HA   sing N N 537 
SER C   O    doub N N 538 
SER C   OXT  sing N N 539 
SER CB  OG   sing N N 540 
SER CB  HB2  sing N N 541 
SER CB  HB3  sing N N 542 
SER OG  HG   sing N N 543 
SER OXT HXT  sing N N 544 
SO4 S   O1   doub N N 545 
SO4 S   O2   doub N N 546 
SO4 S   O3   sing N N 547 
SO4 S   O4   sing N N 548 
THR N   CA   sing N N 549 
THR N   H    sing N N 550 
THR N   H2   sing N N 551 
THR CA  C    sing N N 552 
THR CA  CB   sing N N 553 
THR CA  HA   sing N N 554 
THR C   O    doub N N 555 
THR C   OXT  sing N N 556 
THR CB  OG1  sing N N 557 
THR CB  CG2  sing N N 558 
THR CB  HB   sing N N 559 
THR OG1 HG1  sing N N 560 
THR CG2 HG21 sing N N 561 
THR CG2 HG22 sing N N 562 
THR CG2 HG23 sing N N 563 
THR OXT HXT  sing N N 564 
TRP N   CA   sing N N 565 
TRP N   H    sing N N 566 
TRP N   H2   sing N N 567 
TRP CA  C    sing N N 568 
TRP CA  CB   sing N N 569 
TRP CA  HA   sing N N 570 
TRP C   O    doub N N 571 
TRP C   OXT  sing N N 572 
TRP CB  CG   sing N N 573 
TRP CB  HB2  sing N N 574 
TRP CB  HB3  sing N N 575 
TRP CG  CD1  doub Y N 576 
TRP CG  CD2  sing Y N 577 
TRP CD1 NE1  sing Y N 578 
TRP CD1 HD1  sing N N 579 
TRP CD2 CE2  doub Y N 580 
TRP CD2 CE3  sing Y N 581 
TRP NE1 CE2  sing Y N 582 
TRP NE1 HE1  sing N N 583 
TRP CE2 CZ2  sing Y N 584 
TRP CE3 CZ3  doub Y N 585 
TRP CE3 HE3  sing N N 586 
TRP CZ2 CH2  doub Y N 587 
TRP CZ2 HZ2  sing N N 588 
TRP CZ3 CH2  sing Y N 589 
TRP CZ3 HZ3  sing N N 590 
TRP CH2 HH2  sing N N 591 
TRP OXT HXT  sing N N 592 
TYR N   CA   sing N N 593 
TYR N   H    sing N N 594 
TYR N   H2   sing N N 595 
TYR CA  C    sing N N 596 
TYR CA  CB   sing N N 597 
TYR CA  HA   sing N N 598 
TYR C   O    doub N N 599 
TYR C   OXT  sing N N 600 
TYR CB  CG   sing N N 601 
TYR CB  HB2  sing N N 602 
TYR CB  HB3  sing N N 603 
TYR CG  CD1  doub Y N 604 
TYR CG  CD2  sing Y N 605 
TYR CD1 CE1  sing Y N 606 
TYR CD1 HD1  sing N N 607 
TYR CD2 CE2  doub Y N 608 
TYR CD2 HD2  sing N N 609 
TYR CE1 CZ   doub Y N 610 
TYR CE1 HE1  sing N N 611 
TYR CE2 CZ   sing Y N 612 
TYR CE2 HE2  sing N N 613 
TYR CZ  OH   sing N N 614 
TYR OH  HH   sing N N 615 
TYR OXT HXT  sing N N 616 
VAL N   CA   sing N N 617 
VAL N   H    sing N N 618 
VAL N   H2   sing N N 619 
VAL CA  C    sing N N 620 
VAL CA  CB   sing N N 621 
VAL CA  HA   sing N N 622 
VAL C   O    doub N N 623 
VAL C   OXT  sing N N 624 
VAL CB  CG1  sing N N 625 
VAL CB  CG2  sing N N 626 
VAL CB  HB   sing N N 627 
VAL CG1 HG11 sing N N 628 
VAL CG1 HG12 sing N N 629 
VAL CG1 HG13 sing N N 630 
VAL CG2 HG21 sing N N 631 
VAL CG2 HG22 sing N N 632 
VAL CG2 HG23 sing N N 633 
VAL OXT HXT  sing N N 634 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Spanish Ministry of Science, Innovation, and Universities' Spain 'Synergy CAM Project Y2018/BIO-4738-EVOQUIMERA-CM' 1 
'Spanish Ministry of Science, Innovation, and Universities' Spain PID2022-136367OB-C33                               2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 MAN 4 n 
2 MAN 5 n 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
3 MAN 4 n 
3 MAN 5 n 
3 MAN 6 n 
3 MAN 7 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
4 MAN 4 n 
4 MAN 5 n 
4 MAN 6 n 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
5 MAN 4 n 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5OXU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HEB 
_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]   0.003671 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001465 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013288 
_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]   0.010123 
_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   ? 63.624  4.018   59.598 1.00 103.16 ? 14  GLN A N   1 
ATOM   2    C  CA  . GLN A  1  1   ? 62.270  3.502   59.257 1.00 112.92 ? 14  GLN A CA  1 
ATOM   3    C  C   . GLN A  1  1   ? 62.259  3.110   57.775 1.00 115.33 ? 14  GLN A C   1 
ATOM   4    O  O   . GLN A  1  1   ? 63.040  3.657   56.988 1.00 109.82 ? 14  GLN A O   1 
ATOM   5    C  CB  . GLN A  1  1   ? 61.232  4.550   59.681 1.00 117.99 ? 14  GLN A CB  1 
ATOM   6    C  CG  . GLN A  1  1   ? 59.770  4.164   59.450 1.00 125.14 ? 14  GLN A CG  1 
ATOM   7    C  CD  . GLN A  1  1   ? 59.352  2.846   60.072 1.00 119.13 ? 14  GLN A CD  1 
ATOM   8    O  OE1 . GLN A  1  1   ? 58.788  1.970   59.399 1.00 111.56 ? 14  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A  1  1   ? 59.597  2.706   61.369 1.00 109.10 ? 14  GLN A NE2 1 
ATOM   10   N  N   . GLY A  1  2   ? 61.413  2.118   57.429 1.00 100.76 ? 15  GLY A N   1 
ATOM   11   C  CA  . GLY A  1  2   ? 61.198  1.695   56.052 1.00 76.40  ? 15  GLY A CA  1 
ATOM   12   C  C   . GLY A  1  2   ? 61.141  0.173   55.902 1.00 60.53  ? 15  GLY A C   1 
ATOM   13   O  O   . GLY A  1  2   ? 61.296  -0.574  56.856 1.00 62.01  ? 15  GLY A O   1 
ATOM   14   N  N   . VAL A  1  3   ? 60.948  -0.277  54.666 1.00 50.51  ? 16  VAL A N   1 
ATOM   15   C  CA  . VAL A  1  3   ? 60.637  -1.663  54.360 1.00 49.72  ? 16  VAL A CA  1 
ATOM   16   C  C   . VAL A  1  3   ? 61.570  -2.116  53.248 1.00 47.76  ? 16  VAL A C   1 
ATOM   17   O  O   . VAL A  1  3   ? 61.952  -1.302  52.414 1.00 46.25  ? 16  VAL A O   1 
ATOM   18   C  CB  . VAL A  1  3   ? 59.151  -1.763  53.943 1.00 54.08  ? 16  VAL A CB  1 
ATOM   19   C  CG1 . VAL A  1  3   ? 58.740  -3.124  53.376 1.00 54.03  ? 16  VAL A CG1 1 
ATOM   20   C  CG2 . VAL A  1  3   ? 58.239  -1.381  55.099 1.00 54.16  ? 16  VAL A CG2 1 
ATOM   21   N  N   . ASP A  1  4   ? 61.916  -3.408  53.242 1.00 48.46  ? 17  ASP A N   1 
ATOM   22   C  CA  . ASP A  1  4   ? 62.709  -3.982  52.167 1.00 55.41  ? 17  ASP A CA  1 
ATOM   23   C  C   . ASP A  1  4   ? 61.779  -4.719  51.197 1.00 53.18  ? 17  ASP A C   1 
ATOM   24   O  O   . ASP A  1  4   ? 61.256  -5.769  51.552 1.00 54.84  ? 17  ASP A O   1 
ATOM   25   C  CB  . ASP A  1  4   ? 63.797  -4.883  52.727 1.00 60.73  ? 17  ASP A CB  1 
ATOM   26   C  CG  . ASP A  1  4   ? 64.986  -5.087  51.799 1.00 70.55  ? 17  ASP A CG  1 
ATOM   27   O  OD1 . ASP A  1  4   ? 64.775  -5.156  50.570 1.00 72.42  ? 17  ASP A OD1 1 
ATOM   28   O  OD2 . ASP A  1  4   ? 66.113  -5.177  52.316 1.00 85.24  ? 17  ASP A OD2 1 
ATOM   29   N  N   . PRO A  1  5   ? 61.521  -4.213  49.962 1.00 55.83  ? 18  PRO A N   1 
ATOM   30   C  CA  . PRO A  1  5   ? 60.413  -4.713  49.136 1.00 51.53  ? 18  PRO A CA  1 
ATOM   31   C  C   . PRO A  1  5   ? 60.714  -6.024  48.418 1.00 47.55  ? 18  PRO A C   1 
ATOM   32   O  O   . PRO A  1  5   ? 61.682  -6.109  47.665 1.00 41.95  ? 18  PRO A O   1 
ATOM   33   C  CB  . PRO A  1  5   ? 60.130  -3.592  48.122 1.00 51.67  ? 18  PRO A CB  1 
ATOM   34   C  CG  . PRO A  1  5   ? 61.272  -2.612  48.260 1.00 55.57  ? 18  PRO A CG  1 
ATOM   35   C  CD  . PRO A  1  5   ? 62.269  -3.145  49.282 1.00 57.72  ? 18  PRO A CD  1 
ATOM   36   N  N   . PRO A  1  6   ? 59.863  -7.064  48.587 1.00 46.75  ? 19  PRO A N   1 
ATOM   37   C  CA  . PRO A  1  6   ? 60.113  -8.374  47.993 1.00 44.52  ? 19  PRO A CA  1 
ATOM   38   C  C   . PRO A  1  6   ? 59.922  -8.298  46.485 1.00 46.69  ? 19  PRO A C   1 
ATOM   39   O  O   . PRO A  1  6   ? 59.255  -7.400  45.978 1.00 45.86  ? 19  PRO A O   1 
ATOM   40   C  CB  . PRO A  1  6   ? 59.106  -9.316  48.639 1.00 44.45  ? 19  PRO A CB  1 
ATOM   41   C  CG  . PRO A  1  6   ? 58.024  -8.419  49.213 1.00 48.00  ? 19  PRO A CG  1 
ATOM   42   C  CD  . PRO A  1  6   ? 58.582  -7.008  49.303 1.00 48.92  ? 19  PRO A CD  1 
ATOM   43   N  N   . PRO A  1  7   ? 60.498  -9.242  45.715 1.00 46.88  ? 20  PRO A N   1 
ATOM   44   C  CA  . PRO A  1  7   ? 60.209  -9.317  44.286 1.00 46.61  ? 20  PRO A CA  1 
ATOM   45   C  C   . PRO A  1  7   ? 58.752  -9.728  44.073 1.00 43.25  ? 20  PRO A C   1 
ATOM   46   O  O   . PRO A  1  7   ? 58.106  -10.264 44.966 1.00 39.39  ? 20  PRO A O   1 
ATOM   47   C  CB  . PRO A  1  7   ? 61.222  -10.335 43.750 1.00 46.03  ? 20  PRO A CB  1 
ATOM   48   C  CG  . PRO A  1  7   ? 61.591  -11.160 44.960 1.00 47.54  ? 20  PRO A CG  1 
ATOM   49   C  CD  . PRO A  1  7   ? 61.457  -10.258 46.168 1.00 46.82  ? 20  PRO A CD  1 
ATOM   50   N  N   . PRO A  1  8   ? 58.162  -9.439  42.894 1.00 41.53  ? 21  PRO A N   1 
ATOM   51   C  CA  . PRO A  1  8   ? 56.756  -9.767  42.666 1.00 39.63  ? 21  PRO A CA  1 
ATOM   52   C  C   . PRO A  1  8   ? 56.504  -11.268 42.692 1.00 36.09  ? 21  PRO A C   1 
ATOM   53   O  O   . PRO A  1  8   ? 57.334  -12.055 42.261 1.00 34.03  ? 21  PRO A O   1 
ATOM   54   C  CB  . PRO A  1  8   ? 56.468  -9.176  41.295 1.00 39.69  ? 21  PRO A CB  1 
ATOM   55   C  CG  . PRO A  1  8   ? 57.835  -9.110  40.637 1.00 40.60  ? 21  PRO A CG  1 
ATOM   56   C  CD  . PRO A  1  8   ? 58.807  -8.773  41.747 1.00 37.98  ? 21  PRO A CD  1 
ATOM   57   N  N   . PRO A  1  9   ? 55.330  -11.704 43.183 1.00 34.94  ? 22  PRO A N   1 
ATOM   58   C  CA  . PRO A  1  9   ? 54.923  -13.100 43.079 1.00 33.55  ? 22  PRO A CA  1 
ATOM   59   C  C   . PRO A  1  9   ? 54.934  -13.554 41.626 1.00 34.64  ? 22  PRO A C   1 
ATOM   60   O  O   . PRO A  1  9   ? 54.776  -12.742 40.723 1.00 33.70  ? 22  PRO A O   1 
ATOM   61   C  CB  . PRO A  1  9   ? 53.495  -13.105 43.657 1.00 33.72  ? 22  PRO A CB  1 
ATOM   62   C  CG  . PRO A  1  9   ? 53.400  -11.862 44.506 1.00 32.77  ? 22  PRO A CG  1 
ATOM   63   C  CD  . PRO A  1  9   ? 54.327  -10.865 43.859 1.00 35.60  ? 22  PRO A CD  1 
ATOM   64   N  N   . GLY A  1  10  ? 55.091  -14.862 41.422 1.00 37.71  ? 23  GLY A N   1 
ATOM   65   C  CA  . GLY A  1  10  ? 54.912  -15.484 40.121 1.00 37.31  ? 23  GLY A CA  1 
ATOM   66   C  C   . GLY A  1  10  ? 53.443  -15.853 39.891 1.00 42.10  ? 23  GLY A C   1 
ATOM   67   O  O   . GLY A  1  10  ? 52.557  -15.483 40.677 1.00 39.08  ? 23  GLY A O   1 
ATOM   68   N  N   . PRO A  1  11  ? 53.141  -16.583 38.790 1.00 41.44  ? 24  PRO A N   1 
ATOM   69   C  CA  . PRO A  1  11  ? 51.776  -17.033 38.514 1.00 39.84  ? 24  PRO A CA  1 
ATOM   70   C  C   . PRO A  1  11  ? 51.257  -17.912 39.645 1.00 37.48  ? 24  PRO A C   1 
ATOM   71   O  O   . PRO A  1  11  ? 52.037  -18.504 40.371 1.00 36.29  ? 24  PRO A O   1 
ATOM   72   C  CB  . PRO A  1  11  ? 51.889  -17.797 37.191 1.00 39.96  ? 24  PRO A CB  1 
ATOM   73   C  CG  . PRO A  1  11  ? 53.176  -17.280 36.574 1.00 41.51  ? 24  PRO A CG  1 
ATOM   74   C  CD  . PRO A  1  11  ? 54.092  -16.991 37.746 1.00 39.12  ? 24  PRO A CD  1 
ATOM   75   N  N   . PRO A  1  12  ? 49.926  -18.013 39.836 1.00 40.93  ? 25  PRO A N   1 
ATOM   76   C  CA  . PRO A  1  12  ? 49.373  -18.929 40.832 1.00 44.12  ? 25  PRO A CA  1 
ATOM   77   C  C   . PRO A  1  12  ? 49.567  -20.391 40.420 1.00 43.99  ? 25  PRO A C   1 
ATOM   78   O  O   . PRO A  1  12  ? 49.648  -20.701 39.240 1.00 43.16  ? 25  PRO A O   1 
ATOM   79   C  CB  . PRO A  1  12  ? 47.900  -18.498 40.914 1.00 44.79  ? 25  PRO A CB  1 
ATOM   80   C  CG  . PRO A  1  12  ? 47.604  -17.931 39.540 1.00 43.65  ? 25  PRO A CG  1 
ATOM   81   C  CD  . PRO A  1  12  ? 48.891  -17.283 39.084 1.00 42.14  ? 25  PRO A CD  1 
ATOM   82   N  N   . SER A  1  13  ? 49.667  -21.277 41.419 1.00 46.55  ? 26  SER A N   1 
ATOM   83   C  CA  A SER A  1  13  ? 49.871  -22.699 41.189 0.50 44.11  ? 26  SER A CA  1 
ATOM   84   C  CA  B SER A  1  13  ? 49.869  -22.700 41.192 0.50 45.00  ? 26  SER A CA  1 
ATOM   85   C  C   . SER A  1  13  ? 48.713  -23.264 40.378 1.00 42.49  ? 26  SER A C   1 
ATOM   86   O  O   . SER A  1  13  ? 48.934  -23.994 39.422 1.00 45.24  ? 26  SER A O   1 
ATOM   87   C  CB  A SER A  1  13  ? 50.008  -23.444 42.488 0.50 44.69  ? 26  SER A CB  1 
ATOM   88   C  CB  B SER A  1  13  ? 50.007  -23.443 42.497 0.50 46.69  ? 26  SER A CB  1 
ATOM   89   O  OG  A SER A  1  13  ? 50.970  -22.826 43.327 0.50 43.17  ? 26  SER A OG  1 
ATOM   90   O  OG  B SER A  1  13  ? 49.966  -24.852 42.300 0.50 47.49  ? 26  SER A OG  1 
ATOM   91   N  N   . PHE A  1  14  ? 47.487  -22.924 40.796 1.00 39.71  ? 27  PHE A N   1 
ATOM   92   C  CA  . PHE A  1  14  ? 46.265  -23.351 40.129 1.00 35.47  ? 27  PHE A CA  1 
ATOM   93   C  C   . PHE A  1  14  ? 45.742  -22.202 39.272 1.00 35.43  ? 27  PHE A C   1 
ATOM   94   O  O   . PHE A  1  14  ? 45.559  -21.100 39.778 1.00 38.10  ? 27  PHE A O   1 
ATOM   95   C  CB  . PHE A  1  14  ? 45.246  -23.792 41.185 1.00 33.61  ? 27  PHE A CB  1 
ATOM   96   C  CG  . PHE A  1  14  ? 43.905  -24.180 40.591 1.00 31.01  ? 27  PHE A CG  1 
ATOM   97   C  CD1 . PHE A  1  14  ? 43.791  -25.330 39.831 1.00 31.56  ? 27  PHE A CD1 1 
ATOM   98   C  CD2 . PHE A  1  14  ? 42.774  -23.392 40.770 1.00 33.19  ? 27  PHE A CD2 1 
ATOM   99   C  CE1 . PHE A  1  14  ? 42.588  -25.671 39.238 1.00 34.19  ? 27  PHE A CE1 1 
ATOM   100  C  CE2 . PHE A  1  14  ? 41.561  -23.745 40.188 1.00 33.53  ? 27  PHE A CE2 1 
ATOM   101  C  CZ  . PHE A  1  14  ? 41.476  -24.882 39.421 1.00 34.44  ? 27  PHE A CZ  1 
ATOM   102  N  N   . THR A  1  15  ? 45.504  -22.463 37.977 1.00 36.54  ? 28  THR A N   1 
ATOM   103  C  CA  . THR A  1  15  ? 45.136  -21.412 37.037 1.00 36.89  ? 28  THR A CA  1 
ATOM   104  C  C   . THR A  1  15  ? 43.776  -21.686 36.399 1.00 36.43  ? 28  THR A C   1 
ATOM   105  O  O   . THR A  1  15  ? 43.472  -21.062 35.392 1.00 38.13  ? 28  THR A O   1 
ATOM   106  C  CB  . THR A  1  15  ? 46.200  -21.246 35.944 1.00 39.41  ? 28  THR A CB  1 
ATOM   107  O  OG1 . THR A  1  15  ? 46.220  -22.436 35.158 1.00 37.15  ? 28  THR A OG1 1 
ATOM   108  C  CG2 . THR A  1  15  ? 47.579  -20.932 36.493 1.00 39.01  ? 28  THR A CG2 1 
ATOM   109  N  N   . GLY A  1  16  ? 42.975  -22.605 36.961 1.00 38.71  ? 29  GLY A N   1 
ATOM   110  C  CA  . GLY A  1  16  ? 41.646  -22.898 36.435 1.00 38.46  ? 29  GLY A CA  1 
ATOM   111  C  C   . GLY A  1  16  ? 40.584  -21.962 37.011 1.00 36.72  ? 29  GLY A C   1 
ATOM   112  O  O   . GLY A  1  16  ? 40.925  -21.078 37.787 1.00 36.02  ? 29  GLY A O   1 
ATOM   113  N  N   . THR A  1  17  ? 39.306  -22.163 36.632 1.00 39.60  ? 30  THR A N   1 
ATOM   114  C  CA  . THR A  1  17  ? 38.193  -21.431 37.236 1.00 40.53  ? 30  THR A CA  1 
ATOM   115  C  C   . THR A  1  17  ? 38.043  -21.905 38.665 1.00 37.24  ? 30  THR A C   1 
ATOM   116  O  O   . THR A  1  17  ? 38.440  -23.008 39.006 1.00 37.01  ? 30  THR A O   1 
ATOM   117  C  CB  . THR A  1  17  ? 36.815  -21.617 36.600 1.00 40.19  ? 30  THR A CB  1 
ATOM   118  O  OG1 . THR A  1  17  ? 36.582  -23.007 36.708 1.00 46.16  ? 30  THR A OG1 1 
ATOM   119  C  CG2 . THR A  1  17  ? 36.795  -21.324 35.124 1.00 47.64  ? 30  THR A CG2 1 
ATOM   120  N  N   . LYS A  1  18  ? 37.368  -21.071 39.444 1.00 37.34  ? 31  LYS A N   1 
ATOM   121  C  CA  . LYS A  1  18  ? 36.959  -21.416 40.786 1.00 36.71  ? 31  LYS A CA  1 
ATOM   122  C  C   . LYS A  1  18  ? 35.990  -20.345 41.263 1.00 34.54  ? 31  LYS A C   1 
ATOM   123  O  O   . LYS A  1  18  ? 35.918  -19.265 40.685 1.00 35.04  ? 31  LYS A O   1 
ATOM   124  C  CB  . LYS A  1  18  ? 38.152  -21.551 41.737 1.00 41.62  ? 31  LYS A CB  1 
ATOM   125  C  CG  . LYS A  1  18  ? 38.960  -20.300 41.969 1.00 48.85  ? 31  LYS A CG  1 
ATOM   126  C  CD  . LYS A  1  18  ? 40.067  -20.505 42.992 1.00 56.78  ? 31  LYS A CD  1 
ATOM   127  C  CE  . LYS A  1  18  ? 40.358  -19.249 43.731 1.00 65.01  ? 31  LYS A CE  1 
ATOM   128  N  NZ  . LYS A  1  18  ? 41.456  -19.465 44.675 1.00 71.79  ? 31  LYS A NZ  1 
ATOM   129  N  N   . LEU A  1  19  ? 35.225  -20.685 42.299 1.00 32.91  ? 32  LEU A N   1 
ATOM   130  C  CA  . LEU A  1  19  ? 34.365  -19.729 42.957 1.00 31.68  ? 32  LEU A CA  1 
ATOM   131  C  C   . LEU A  1  19  ? 35.249  -18.725 43.684 1.00 33.00  ? 32  LEU A C   1 
ATOM   132  O  O   . LEU A  1  19  ? 36.089  -19.134 44.480 1.00 33.33  ? 32  LEU A O   1 
ATOM   133  C  CB  . LEU A  1  19  ? 33.450  -20.458 43.936 1.00 31.83  ? 32  LEU A CB  1 
ATOM   134  C  CG  . LEU A  1  19  ? 32.539  -19.559 44.781 1.00 31.66  ? 32  LEU A CG  1 
ATOM   135  C  CD1 . LEU A  1  19  ? 31.466  -18.928 43.939 1.00 32.41  ? 32  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A  1  19  ? 31.895  -20.308 45.909 1.00 32.17  ? 32  LEU A CD2 1 
ATOM   137  N  N   . VAL A  1  20  ? 35.054  -17.428 43.397 1.00 32.80  ? 33  VAL A N   1 
ATOM   138  C  CA  . VAL A  1  20  ? 35.840  -16.388 44.043 1.00 33.74  ? 33  VAL A CA  1 
ATOM   139  C  C   . VAL A  1  20  ? 34.959  -15.583 44.989 1.00 30.32  ? 33  VAL A C   1 
ATOM   140  O  O   . VAL A  1  20  ? 35.467  -14.995 45.934 1.00 34.03  ? 33  VAL A O   1 
ATOM   141  C  CB  . VAL A  1  20  ? 36.609  -15.474 43.061 1.00 34.84  ? 33  VAL A CB  1 
ATOM   142  C  CG1 . VAL A  1  20  ? 37.629  -16.251 42.238 1.00 34.28  ? 33  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A  1  20  ? 35.687  -14.711 42.142 1.00 37.59  ? 33  VAL A CG2 1 
ATOM   144  N  N   . ASN A  1  21  ? 33.653  -15.545 44.721 1.00 32.02  ? 34  ASN A N   1 
ATOM   145  C  CA  . ASN A  1  21  ? 32.668  -14.952 45.619 1.00 30.86  ? 34  ASN A CA  1 
ATOM   146  C  C   . ASN A  1  21  ? 32.233  -15.989 46.641 1.00 31.18  ? 34  ASN A C   1 
ATOM   147  O  O   . ASN A  1  21  ? 31.148  -16.528 46.540 1.00 33.65  ? 34  ASN A O   1 
ATOM   148  C  CB  . ASN A  1  21  ? 31.467  -14.447 44.834 1.00 30.74  ? 34  ASN A CB  1 
ATOM   149  C  CG  . ASN A  1  21  ? 30.528  -13.590 45.646 1.00 30.97  ? 34  ASN A CG  1 
ATOM   150  O  OD1 . ASN A  1  21  ? 30.700  -13.434 46.862 1.00 31.61  ? 34  ASN A OD1 1 
ATOM   151  N  ND2 . ASN A  1  21  ? 29.535  -13.015 44.979 1.00 30.08  ? 34  ASN A ND2 1 
ATOM   152  N  N   . ASP A  1  22  ? 33.095  -16.279 47.611 1.00 35.06  ? 35  ASP A N   1 
ATOM   153  C  CA  . ASP A  1  22  ? 32.920  -17.413 48.505 1.00 36.97  ? 35  ASP A CA  1 
ATOM   154  C  C   . ASP A  1  22  ? 32.746  -16.910 49.938 1.00 35.39  ? 35  ASP A C   1 
ATOM   155  O  O   . ASP A  1  22  ? 32.603  -15.710 50.173 1.00 34.28  ? 35  ASP A O   1 
ATOM   156  C  CB  . ASP A  1  22  ? 34.058  -18.407 48.313 1.00 44.42  ? 35  ASP A CB  1 
ATOM   157  C  CG  . ASP A  1  22  ? 35.476  -17.917 48.619 1.00 48.14  ? 35  ASP A CG  1 
ATOM   158  O  OD1 . ASP A  1  22  ? 35.641  -16.785 49.117 1.00 47.45  ? 35  ASP A OD1 1 
ATOM   159  O  OD2 . ASP A  1  22  ? 36.431  -18.652 48.286 1.00 53.68  ? 35  ASP A OD2 1 
ATOM   160  N  N   . ALA A  1  23  ? 32.737  -17.843 50.894 1.00 37.51  ? 36  ALA A N   1 
ATOM   161  C  CA  . ALA A  1  23  ? 32.361  -17.526 52.265 1.00 38.69  ? 36  ALA A CA  1 
ATOM   162  C  C   . ALA A  1  23  ? 33.418  -16.651 52.931 1.00 38.00  ? 36  ALA A C   1 
ATOM   163  O  O   . ALA A  1  23  ? 33.085  -15.813 53.754 1.00 39.75  ? 36  ALA A O   1 
ATOM   164  C  CB  . ALA A  1  23  ? 32.156  -18.801 53.051 1.00 41.13  ? 36  ALA A CB  1 
ATOM   165  N  N   . ASP A  1  24  ? 34.685  -16.857 52.568 1.00 37.08  ? 37  ASP A N   1 
ATOM   166  C  CA  . ASP A  1  24  ? 35.798  -16.151 53.177 1.00 37.09  ? 37  ASP A CA  1 
ATOM   167  C  C   . ASP A  1  24  ? 36.012  -14.774 52.547 1.00 36.38  ? 37  ASP A C   1 
ATOM   168  O  O   . ASP A  1  24  ? 36.821  -14.001 53.055 1.00 34.03  ? 37  ASP A O   1 
ATOM   169  C  CB  . ASP A  1  24  ? 37.087  -16.951 53.036 1.00 45.24  ? 37  ASP A CB  1 
ATOM   170  C  CG  . ASP A  1  24  ? 38.171  -16.697 54.084 1.00 52.15  ? 37  ASP A CG  1 
ATOM   171  O  OD1 . ASP A  1  24  ? 37.817  -16.667 55.281 1.00 57.77  ? 37  ASP A OD1 1 
ATOM   172  O  OD2 . ASP A  1  24  ? 39.368  -16.573 53.704 1.00 53.58  ? 37  ASP A OD2 1 
ATOM   173  N  N   . HIS A  1  25  ? 35.320  -14.467 51.433 1.00 35.17  ? 38  HIS A N   1 
ATOM   174  C  CA  . HIS A  1  25  ? 35.513  -13.204 50.738 1.00 31.64  ? 38  HIS A CA  1 
ATOM   175  C  C   . HIS A  1  25  ? 34.169  -12.522 50.535 1.00 30.04  ? 38  HIS A C   1 
ATOM   176  O  O   . HIS A  1  25  ? 33.784  -12.199 49.415 1.00 32.76  ? 38  HIS A O   1 
ATOM   177  C  CB  . HIS A  1  25  ? 36.284  -13.429 49.431 1.00 34.52  ? 38  HIS A CB  1 
ATOM   178  C  CG  . HIS A  1  25  ? 37.654  -13.963 49.657 1.00 34.97  ? 38  HIS A CG  1 
ATOM   179  N  ND1 . HIS A  1  25  ? 37.976  -15.291 49.516 1.00 36.68  ? 38  HIS A ND1 1 
ATOM   180  C  CD2 . HIS A  1  25  ? 38.772  -13.352 50.034 1.00 36.46  ? 38  HIS A CD2 1 
ATOM   181  C  CE1 . HIS A  1  25  ? 39.261  -15.461 49.799 1.00 39.64  ? 38  HIS A CE1 1 
ATOM   182  N  NE2 . HIS A  1  25  ? 39.768  -14.292 50.113 1.00 37.14  ? 38  HIS A NE2 1 
ATOM   183  N  N   . PRO A  1  26  ? 33.419  -12.252 51.620 1.00 29.85  ? 39  PRO A N   1 
ATOM   184  C  CA  . PRO A  1  26  ? 32.098  -11.637 51.486 1.00 30.20  ? 39  PRO A CA  1 
ATOM   185  C  C   . PRO A  1  26  ? 32.203  -10.159 51.131 1.00 29.53  ? 39  PRO A C   1 
ATOM   186  O  O   . PRO A  1  26  ? 33.120  -9.484  51.576 1.00 32.27  ? 39  PRO A O   1 
ATOM   187  C  CB  . PRO A  1  26  ? 31.517  -11.865 52.907 1.00 30.22  ? 39  PRO A CB  1 
ATOM   188  C  CG  . PRO A  1  26  ? 32.748  -11.754 53.814 1.00 27.76  ? 39  PRO A CG  1 
ATOM   189  C  CD  . PRO A  1  26  ? 33.799  -12.504 53.027 1.00 27.35  ? 39  PRO A CD  1 
ATOM   190  N  N   . TRP A  1  27  ? 31.253  -9.661  50.341 1.00 31.43  ? 40  TRP A N   1 
ATOM   191  C  CA  . TRP A  1  27  ? 31.095  -8.228  50.170 1.00 29.63  ? 40  TRP A CA  1 
ATOM   192  C  C   . TRP A  1  27  ? 30.733  -7.591  51.513 1.00 29.06  ? 40  TRP A C   1 
ATOM   193  O  O   . TRP A  1  27  ? 29.950  -8.139  52.277 1.00 30.12  ? 40  TRP A O   1 
ATOM   194  C  CB  . TRP A  1  27  ? 30.041  -7.926  49.100 1.00 28.64  ? 40  TRP A CB  1 
ATOM   195  C  CG  . TRP A  1  27  ? 29.856  -6.461  48.814 1.00 28.67  ? 40  TRP A CG  1 
ATOM   196  C  CD1 . TRP A  1  27  ? 30.477  -5.744  47.841 1.00 30.09  ? 40  TRP A CD1 1 
ATOM   197  C  CD2 . TRP A  1  27  ? 29.014  -5.526  49.521 1.00 28.33  ? 40  TRP A CD2 1 
ATOM   198  N  NE1 . TRP A  1  27  ? 30.070  -4.437  47.875 1.00 30.53  ? 40  TRP A NE1 1 
ATOM   199  C  CE2 . TRP A  1  27  ? 29.178  -4.270  48.903 1.00 29.44  ? 40  TRP A CE2 1 
ATOM   200  C  CE3 . TRP A  1  27  ? 28.146  -5.623  50.608 1.00 29.15  ? 40  TRP A CE3 1 
ATOM   201  C  CZ2 . TRP A  1  27  ? 28.517  -3.125  49.348 1.00 28.39  ? 40  TRP A CZ2 1 
ATOM   202  C  CZ3 . TRP A  1  27  ? 27.494  -4.488  51.049 1.00 27.86  ? 40  TRP A CZ3 1 
ATOM   203  C  CH2 . TRP A  1  27  ? 27.686  -3.257  50.436 1.00 26.91  ? 40  TRP A CH2 1 
ATOM   204  N  N   . GLN A  1  28  ? 31.331  -6.433  51.796 1.00 28.29  ? 41  GLN A N   1 
ATOM   205  C  CA  . GLN A  1  28  ? 30.989  -5.646  52.960 1.00 27.42  ? 41  GLN A CA  1 
ATOM   206  C  C   . GLN A  1  28  ? 31.004  -4.165  52.601 1.00 28.31  ? 41  GLN A C   1 
ATOM   207  O  O   . GLN A  1  28  ? 31.754  -3.730  51.729 1.00 28.86  ? 41  GLN A O   1 
ATOM   208  C  CB  . GLN A  1  28  ? 31.989  -5.866  54.087 1.00 27.84  ? 41  GLN A CB  1 
ATOM   209  C  CG  . GLN A  1  28  ? 32.003  -7.286  54.630 1.00 28.06  ? 41  GLN A CG  1 
ATOM   210  C  CD  . GLN A  1  28  ? 33.014  -7.483  55.734 1.00 30.06  ? 41  GLN A CD  1 
ATOM   211  O  OE1 . GLN A  1  28  ? 33.761  -6.572  56.113 1.00 29.43  ? 41  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A  1  28  ? 33.049  -8.699  56.252 1.00 31.47  ? 41  GLN A NE2 1 
ATOM   213  N  N   . PRO A  1  29  ? 30.180  -3.338  53.279 1.00 30.11  ? 42  PRO A N   1 
ATOM   214  C  CA  . PRO A  1  29  ? 30.144  -1.911  52.996 1.00 29.83  ? 42  PRO A CA  1 
ATOM   215  C  C   . PRO A  1  29  ? 31.385  -1.180  53.501 1.00 32.48  ? 42  PRO A C   1 
ATOM   216  O  O   . PRO A  1  29  ? 32.126  -1.687  54.344 1.00 32.67  ? 42  PRO A O   1 
ATOM   217  C  CB  . PRO A  1  29  ? 28.854  -1.452  53.688 1.00 29.54  ? 42  PRO A CB  1 
ATOM   218  C  CG  . PRO A  1  29  ? 28.641  -2.439  54.818 1.00 29.33  ? 42  PRO A CG  1 
ATOM   219  C  CD  . PRO A  1  29  ? 29.255  -3.735  54.355 1.00 29.21  ? 42  PRO A CD  1 
ATOM   220  N  N   . LEU A  1  30  ? 31.598  0.020   52.953 1.00 34.37  ? 43  LEU A N   1 
ATOM   221  C  CA  . LEU A  1  30  ? 32.734  0.843   53.326 1.00 33.53  ? 43  LEU A CA  1 
ATOM   222  C  C   . LEU A  1  30  ? 32.605  1.295   54.771 1.00 33.87  ? 43  LEU A C   1 
ATOM   223  O  O   . LEU A  1  30  ? 31.521  1.648   55.215 1.00 34.52  ? 43  LEU A O   1 
ATOM   224  C  CB  . LEU A  1  30  ? 32.767  2.045   52.394 1.00 33.34  ? 43  LEU A CB  1 
ATOM   225  C  CG  . LEU A  1  30  ? 33.064  1.751   50.925 1.00 35.15  ? 43  LEU A CG  1 
ATOM   226  C  CD1 . LEU A  1  30  ? 33.168  3.088   50.213 1.00 33.85  ? 43  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A  1  30  ? 34.331  0.927   50.707 1.00 36.58  ? 43  LEU A CD2 1 
ATOM   228  N  N   . ARG A  1  31  ? 33.718  1.255   55.503 1.00 37.49  ? 44  ARG A N   1 
ATOM   229  C  CA  . ARG A  1  31  ? 33.823  1.904   56.802 1.00 38.04  ? 44  ARG A CA  1 
ATOM   230  C  C   . ARG A  1  31  ? 34.521  3.254   56.652 1.00 36.71  ? 44  ARG A C   1 
ATOM   231  O  O   . ARG A  1  31  ? 35.130  3.534   55.638 1.00 40.05  ? 44  ARG A O   1 
ATOM   232  C  CB  . ARG A  1  31  ? 34.643  1.060   57.774 1.00 39.97  ? 44  ARG A CB  1 
ATOM   233  C  CG  . ARG A  1  31  ? 34.178  -0.367  58.031 1.00 42.44  ? 44  ARG A CG  1 
ATOM   234  C  CD  . ARG A  1  31  ? 35.317  -1.179  58.644 1.00 55.52  ? 44  ARG A CD  1 
ATOM   235  N  NE  . ARG A  1  31  ? 36.584  -1.053  57.899 1.00 65.33  ? 44  ARG A NE  1 
ATOM   236  C  CZ  . ARG A  1  31  ? 37.468  -2.011  57.601 1.00 71.06  ? 44  ARG A CZ  1 
ATOM   237  N  NH1 . ARG A  1  31  ? 37.301  -3.256  58.014 1.00 81.99  ? 44  ARG A NH1 1 
ATOM   238  N  NH2 . ARG A  1  31  ? 38.524  -1.713  56.863 1.00 65.69  ? 44  ARG A NH2 1 
ATOM   239  N  N   . GLU A  1  32  ? 34.414  4.093   57.676 1.00 43.12  ? 45  GLU A N   1 
ATOM   240  C  CA  . GLU A  1  32  ? 35.186  5.319   57.793 1.00 50.35  ? 45  GLU A CA  1 
ATOM   241  C  C   . GLU A  1  32  ? 36.663  5.053   57.488 1.00 43.30  ? 45  GLU A C   1 
ATOM   242  O  O   . GLU A  1  32  ? 37.297  4.205   58.111 1.00 35.81  ? 45  GLU A O   1 
ATOM   243  C  CB  . GLU A  1  32  ? 35.004  5.845   59.218 1.00 65.50  ? 45  GLU A CB  1 
ATOM   244  C  CG  . GLU A  1  32  ? 35.668  7.194   59.477 1.00 79.03  ? 45  GLU A CG  1 
ATOM   245  C  CD  . GLU A  1  32  ? 35.427  7.768   60.867 1.00 97.58  ? 45  GLU A CD  1 
ATOM   246  O  OE1 . GLU A  1  32  ? 34.654  7.202   61.676 1.00 105.33 ? 45  GLU A OE1 1 
ATOM   247  O  OE2 . GLU A  1  32  ? 36.043  8.816   61.134 1.00 103.28 ? 45  GLU A OE2 1 
ATOM   248  N  N   . GLY A  1  33  ? 37.199  5.795   56.515 1.00 40.56  ? 46  GLY A N   1 
ATOM   249  C  CA  . GLY A  1  33  ? 38.615  5.760   56.194 1.00 38.86  ? 46  GLY A CA  1 
ATOM   250  C  C   . GLY A  1  33  ? 38.944  4.831   55.023 1.00 41.97  ? 46  GLY A C   1 
ATOM   251  O  O   . GLY A  1  33  ? 40.053  4.878   54.493 1.00 45.41  ? 46  GLY A O   1 
ATOM   252  N  N   . ASP A  1  34  ? 37.994  3.973   54.631 1.00 44.16  ? 47  ASP A N   1 
ATOM   253  C  CA  . ASP A  1  34  ? 38.209  3.031   53.545 1.00 42.17  ? 47  ASP A CA  1 
ATOM   254  C  C   . ASP A  1  34  ? 38.312  3.789   52.230 1.00 37.05  ? 47  ASP A C   1 
ATOM   255  O  O   . ASP A  1  34  ? 37.584  4.750   52.026 1.00 40.32  ? 47  ASP A O   1 
ATOM   256  C  CB  . ASP A  1  34  ? 37.118  1.974   53.486 1.00 45.42  ? 47  ASP A CB  1 
ATOM   257  C  CG  . ASP A  1  34  ? 37.143  0.914   54.583 1.00 48.78  ? 47  ASP A CG  1 
ATOM   258  O  OD1 . ASP A  1  34  ? 38.043  0.986   55.454 1.00 57.11  ? 47  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A  1  34  ? 36.263  0.019   54.553 1.00 46.33  ? 47  ASP A OD2 1 
ATOM   260  N  N   . ILE A  1  35  ? 39.208  3.341   51.347 1.00 32.39  ? 48  ILE A N   1 
ATOM   261  C  CA  . ILE A  1  35  ? 39.504  4.081   50.139 1.00 32.94  ? 48  ILE A CA  1 
ATOM   262  C  C   . ILE A  1  35  ? 39.175  3.244   48.916 1.00 30.44  ? 48  ILE A C   1 
ATOM   263  O  O   . ILE A  1  35  ? 39.442  2.048   48.892 1.00 28.88  ? 48  ILE A O   1 
ATOM   264  C  CB  . ILE A  1  35  ? 40.958  4.578   50.168 1.00 35.23  ? 48  ILE A CB  1 
ATOM   265  C  CG1 . ILE A  1  35  ? 41.005  5.832   51.014 1.00 37.03  ? 48  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A  1  35  ? 41.511  4.847   48.767 1.00 34.23  ? 48  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A  1  35  ? 42.354  6.083   51.591 1.00 41.04  ? 48  ILE A CD1 1 
ATOM   268  N  N   . ARG A  1  36  ? 38.573  3.918   47.927 1.00 29.15  ? 49  ARG A N   1 
ATOM   269  C  CA  . ARG A  1  36  ? 38.218  3.327   46.653 1.00 26.69  ? 49  ARG A CA  1 
ATOM   270  C  C   . ARG A  1  36  ? 38.522  4.370   45.587 1.00 27.63  ? 49  ARG A C   1 
ATOM   271  O  O   . ARG A  1  36  ? 38.620  5.549   45.909 1.00 27.61  ? 49  ARG A O   1 
ATOM   272  C  CB  . ARG A  1  36  ? 36.752  2.900   46.674 1.00 25.91  ? 49  ARG A CB  1 
ATOM   273  C  CG  . ARG A  1  36  ? 36.375  1.828   47.691 1.00 26.61  ? 49  ARG A CG  1 
ATOM   274  C  CD  . ARG A  1  36  ? 36.919  0.461   47.321 1.00 27.50  ? 49  ARG A CD  1 
ATOM   275  N  NE  . ARG A  1  36  ? 36.484  -0.562  48.283 1.00 29.04  ? 49  ARG A NE  1 
ATOM   276  C  CZ  . ARG A  1  36  ? 37.008  -0.769  49.492 1.00 29.57  ? 49  ARG A CZ  1 
ATOM   277  N  NH1 . ARG A  1  36  ? 37.997  -0.021  49.937 1.00 30.94  ? 49  ARG A NH1 1 
ATOM   278  N  NH2 . ARG A  1  36  ? 36.559  -1.744  50.261 1.00 30.22  ? 49  ARG A NH2 1 
ATOM   279  N  N   . GLY A  1  37  ? 38.701  3.936   44.327 1.00 28.98  ? 50  GLY A N   1 
ATOM   280  C  CA  . GLY A  1  37  ? 39.170  4.843   43.296 1.00 27.69  ? 50  GLY A CA  1 
ATOM   281  C  C   . GLY A  1  37  ? 38.660  4.492   41.906 1.00 28.30  ? 50  GLY A C   1 
ATOM   282  O  O   . GLY A  1  37  ? 37.570  3.972   41.733 1.00 29.05  ? 50  GLY A O   1 
ATOM   283  N  N   . PRO A  1  38  ? 39.449  4.769   40.857 1.00 30.02  ? 51  PRO A N   1 
ATOM   284  C  CA  . PRO A  1  38  ? 38.966  4.648   39.493 1.00 28.72  ? 51  PRO A CA  1 
ATOM   285  C  C   . PRO A  1  38  ? 38.966  3.248   38.903 1.00 29.49  ? 51  PRO A C   1 
ATOM   286  O  O   . PRO A  1  38  ? 38.469  3.106   37.787 1.00 33.18  ? 51  PRO A O   1 
ATOM   287  C  CB  . PRO A  1  38  ? 39.956  5.554   38.773 1.00 29.86  ? 51  PRO A CB  1 
ATOM   288  C  CG  . PRO A  1  38  ? 41.247  5.293   39.476 1.00 31.63  ? 51  PRO A CG  1 
ATOM   289  C  CD  . PRO A  1  38  ? 40.852  5.192   40.925 1.00 31.83  ? 51  PRO A CD  1 
ATOM   290  N  N   . CYS A  1  39  ? 39.537  2.260   39.617 1.00 28.22  ? 52  CYS A N   1 
ATOM   291  C  CA  . CYS A  1  39  ? 39.630  0.893   39.104 1.00 27.47  ? 52  CYS A CA  1 
ATOM   292  C  C   . CYS A  1  39  ? 38.548  -0.004  39.704 1.00 27.17  ? 52  CYS A C   1 
ATOM   293  O  O   . CYS A  1  39  ? 38.571  -0.318  40.895 1.00 26.08  ? 52  CYS A O   1 
ATOM   294  C  CB  . CYS A  1  39  ? 40.977  0.222   39.368 1.00 26.75  ? 52  CYS A CB  1 
ATOM   295  S  SG  . CYS A  1  39  ? 41.096  -1.430  38.621 1.00 27.11  ? 52  CYS A SG  1 
ATOM   296  N  N   . PRO A  1  40  ? 37.593  -0.479  38.883 1.00 28.86  ? 53  PRO A N   1 
ATOM   297  C  CA  . PRO A  1  40  ? 36.519  -1.349  39.366 1.00 31.06  ? 53  PRO A CA  1 
ATOM   298  C  C   . PRO A  1  40  ? 37.021  -2.723  39.795 1.00 31.32  ? 53  PRO A C   1 
ATOM   299  O  O   . PRO A  1  40  ? 36.432  -3.361  40.666 1.00 33.20  ? 53  PRO A O   1 
ATOM   300  C  CB  . PRO A  1  40  ? 35.538  -1.421  38.184 1.00 32.93  ? 53  PRO A CB  1 
ATOM   301  C  CG  . PRO A  1  40  ? 36.402  -1.140  36.947 1.00 33.88  ? 53  PRO A CG  1 
ATOM   302  C  CD  . PRO A  1  40  ? 37.497  -0.202  37.442 1.00 33.48  ? 53  PRO A CD  1 
ATOM   303  N  N   . GLY A  1  41  ? 38.129  -3.157  39.187 1.00 32.52  ? 54  GLY A N   1 
ATOM   304  C  CA  . GLY A  1  41  ? 38.768  -4.411  39.548 1.00 28.27  ? 54  GLY A CA  1 
ATOM   305  C  C   . GLY A  1  41  ? 39.285  -4.371  40.975 1.00 26.78  ? 54  GLY A C   1 
ATOM   306  O  O   . GLY A  1  41  ? 38.888  -5.183  41.805 1.00 27.65  ? 54  GLY A O   1 
ATOM   307  N  N   . LEU A  1  42  ? 40.163  -3.407  41.255 1.00 27.85  ? 55  LEU A N   1 
ATOM   308  C  CA  . LEU A  1  42  ? 40.764  -3.288  42.573 1.00 29.16  ? 55  LEU A CA  1 
ATOM   309  C  C   . LEU A  1  42  ? 39.678  -2.944  43.594 1.00 28.28  ? 55  LEU A C   1 
ATOM   310  O  O   . LEU A  1  42  ? 39.734  -3.398  44.731 1.00 25.69  ? 55  LEU A O   1 
ATOM   311  C  CB  . LEU A  1  42  ? 41.874  -2.239  42.554 1.00 29.34  ? 55  LEU A CB  1 
ATOM   312  C  CG  . LEU A  1  42  ? 43.081  -2.549  41.667 1.00 30.99  ? 55  LEU A CG  1 
ATOM   313  C  CD1 . LEU A  1  42  ? 44.058  -1.392  41.617 1.00 30.53  ? 55  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A  1  42  ? 43.797  -3.807  42.134 1.00 33.29  ? 55  LEU A CD2 1 
ATOM   315  N  N   . ASN A  1  43  ? 38.688  -2.140  43.187 1.00 27.67  ? 56  ASN A N   1 
ATOM   316  C  CA  . ASN A  1  43  ? 37.607  -1.769  44.081 1.00 27.63  ? 56  ASN A CA  1 
ATOM   317  C  C   . ASN A  1  43  ? 36.865  -3.018  44.546 1.00 26.15  ? 56  ASN A C   1 
ATOM   318  O  O   . ASN A  1  43  ? 36.614  -3.190  45.742 1.00 25.37  ? 56  ASN A O   1 
ATOM   319  C  CB  . ASN A  1  43  ? 36.668  -0.754  43.445 1.00 28.30  ? 56  ASN A CB  1 
ATOM   320  C  CG  . ASN A  1  43  ? 37.244  0.646   43.378 1.00 29.54  ? 56  ASN A CG  1 
ATOM   321  O  OD1 . ASN A  1  43  ? 38.173  1.001   44.116 1.00 31.35  ? 56  ASN A OD1 1 
ATOM   322  N  ND2 . ASN A  1  43  ? 36.680  1.472   42.514 1.00 28.04  ? 56  ASN A ND2 1 
ATOM   323  N  N   . THR A  1  44  ? 36.538  -3.904  43.604 1.00 26.18  ? 57  THR A N   1 
ATOM   324  C  CA  . THR A  1  44  ? 35.798  -5.109  43.938 1.00 27.01  ? 57  THR A CA  1 
ATOM   325  C  C   . THR A  1  44  ? 36.641  -6.017  44.835 1.00 26.64  ? 57  THR A C   1 
ATOM   326  O  O   . THR A  1  44  ? 36.113  -6.602  45.783 1.00 23.54  ? 57  THR A O   1 
ATOM   327  C  CB  . THR A  1  44  ? 35.349  -5.812  42.663 1.00 28.04  ? 57  THR A CB  1 
ATOM   328  O  OG1 . THR A  1  44  ? 34.483  -4.896  42.001 1.00 30.05  ? 57  THR A OG1 1 
ATOM   329  C  CG2 . THR A  1  44  ? 34.597  -7.095  42.946 1.00 27.53  ? 57  THR A CG2 1 
ATOM   330  N  N   . LEU A  1  45  ? 37.947  -6.128  44.550 1.00 25.36  ? 58  LEU A N   1 
ATOM   331  C  CA  . LEU A  1  45  ? 38.805  -6.988  45.348 1.00 24.99  ? 58  LEU A CA  1 
ATOM   332  C  C   . LEU A  1  45  ? 38.901  -6.471  46.785 1.00 25.24  ? 58  LEU A C   1 
ATOM   333  O  O   . LEU A  1  45  ? 39.006  -7.256  47.719 1.00 23.57  ? 58  LEU A O   1 
ATOM   334  C  CB  . LEU A  1  45  ? 40.183  -7.079  44.699 1.00 25.87  ? 58  LEU A CB  1 
ATOM   335  C  CG  . LEU A  1  45  ? 40.228  -7.805  43.356 1.00 25.77  ? 58  LEU A CG  1 
ATOM   336  C  CD1 . LEU A  1  45  ? 41.533  -7.558  42.629 1.00 25.94  ? 58  LEU A CD1 1 
ATOM   337  C  CD2 . LEU A  1  45  ? 40.033  -9.282  43.567 1.00 25.21  ? 58  LEU A CD2 1 
ATOM   338  N  N   . ALA A  1  46  ? 38.896  -5.149  46.972 1.00 26.55  ? 59  ALA A N   1 
ATOM   339  C  CA  . ALA A  1  46  ? 38.969  -4.581  48.310 1.00 27.16  ? 59  ALA A CA  1 
ATOM   340  C  C   . ALA A  1  46  ? 37.662  -4.821  49.058 1.00 27.21  ? 59  ALA A C   1 
ATOM   341  O  O   . ALA A  1  46  ? 37.680  -5.198  50.228 1.00 29.90  ? 59  ALA A O   1 
ATOM   342  C  CB  . ALA A  1  46  ? 39.282  -3.104  48.244 1.00 28.42  ? 59  ALA A CB  1 
ATOM   343  N  N   . SER A  1  47  ? 36.531  -4.617  48.375 1.00 27.08  ? 60  SER A N   1 
ATOM   344  C  CA  . SER A  1  47  ? 35.240  -4.719  49.033 1.00 29.36  ? 60  SER A CA  1 
ATOM   345  C  C   . SER A  1  47  ? 34.837  -6.176  49.295 1.00 29.19  ? 60  SER A C   1 
ATOM   346  O  O   . SER A  1  47  ? 33.871  -6.413  50.009 1.00 31.29  ? 60  SER A O   1 
ATOM   347  C  CB  . SER A  1  47  ? 34.188  -3.944  48.279 1.00 29.86  ? 60  SER A CB  1 
ATOM   348  O  OG  . SER A  1  47  ? 34.309  -2.549  48.545 1.00 31.16  ? 60  SER A OG  1 
ATOM   349  N  N   . HIS A  1  48  ? 35.601  -7.143  48.774 1.00 27.58  ? 61  HIS A N   1 
ATOM   350  C  CA  . HIS A  1  48  ? 35.429  -8.547  49.108 1.00 26.55  ? 61  HIS A CA  1 
ATOM   351  C  C   . HIS A  1  48  ? 36.577  -9.115  49.944 1.00 26.42  ? 61  HIS A C   1 
ATOM   352  O  O   . HIS A  1  48  ? 36.606  -10.315 50.199 1.00 25.63  ? 61  HIS A O   1 
ATOM   353  C  CB  . HIS A  1  48  ? 35.315  -9.388  47.835 1.00 26.84  ? 61  HIS A CB  1 
ATOM   354  C  CG  . HIS A  1  48  ? 33.951  -9.382  47.223 1.00 28.55  ? 61  HIS A CG  1 
ATOM   355  N  ND1 . HIS A  1  48  ? 32.995  -10.328 47.515 1.00 26.23  ? 61  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A  1  48  ? 33.400  -8.568  46.312 1.00 27.73  ? 61  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A  1  48  ? 31.918  -10.082 46.794 1.00 27.28  ? 61  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A  1  48  ? 32.137  -9.012  46.062 1.00 26.01  ? 61  HIS A NE2 1 
ATOM   359  N  N   . GLY A  1  49  ? 37.545  -8.288  50.339 1.00 26.99  ? 62  GLY A N   1 
ATOM   360  C  CA  . GLY A  1  49  ? 38.625  -8.745  51.207 1.00 26.16  ? 62  GLY A CA  1 
ATOM   361  C  C   . GLY A  1  49  ? 39.752  -9.530  50.518 1.00 26.54  ? 62  GLY A C   1 
ATOM   362  O  O   . GLY A  1  49  ? 40.569  -10.123 51.202 1.00 27.89  ? 62  GLY A O   1 
ATOM   363  N  N   . TYR A  1  50  ? 39.847  -9.534  49.184 1.00 29.84  ? 63  TYR A N   1 
ATOM   364  C  CA  . TYR A  1  50  ? 41.033  -10.045 48.496 1.00 29.80  ? 63  TYR A CA  1 
ATOM   365  C  C   . TYR A  1  50  ? 42.228  -9.110  48.688 1.00 30.52  ? 63  TYR A C   1 
ATOM   366  O  O   . TYR A  1  50  ? 43.361  -9.572  48.773 1.00 31.43  ? 63  TYR A O   1 
ATOM   367  C  CB  . TYR A  1  50  ? 40.786  -10.255 46.998 1.00 31.63  ? 63  TYR A CB  1 
ATOM   368  C  CG  . TYR A  1  50  ? 40.042  -11.552 46.721 1.00 32.29  ? 63  TYR A CG  1 
ATOM   369  C  CD1 . TYR A  1  50  ? 40.725  -12.763 46.659 1.00 31.57  ? 63  TYR A CD1 1 
ATOM   370  C  CD2 . TYR A  1  50  ? 38.659  -11.569 46.554 1.00 31.59  ? 63  TYR A CD2 1 
ATOM   371  C  CE1 . TYR A  1  50  ? 40.057  -13.954 46.435 1.00 32.24  ? 63  TYR A CE1 1 
ATOM   372  C  CE2 . TYR A  1  50  ? 37.984  -12.754 46.318 1.00 30.94  ? 63  TYR A CE2 1 
ATOM   373  C  CZ  . TYR A  1  50  ? 38.683  -13.945 46.268 1.00 31.90  ? 63  TYR A CZ  1 
ATOM   374  O  OH  . TYR A  1  50  ? 38.031  -15.117 46.064 1.00 32.12  ? 63  TYR A OH  1 
ATOM   375  N  N   . LEU A  1  51  ? 41.969  -7.795  48.703 1.00 33.66  ? 64  LEU A N   1 
ATOM   376  C  CA  . LEU A  1  51  ? 42.903  -6.799  49.215 1.00 35.13  ? 64  LEU A CA  1 
ATOM   377  C  C   . LEU A  1  51  ? 42.467  -6.387  50.614 1.00 33.95  ? 64  LEU A C   1 
ATOM   378  O  O   . LEU A  1  51  ? 41.326  -6.616  50.980 1.00 32.22  ? 64  LEU A O   1 
ATOM   379  C  CB  . LEU A  1  51  ? 42.905  -5.555  48.329 1.00 35.94  ? 64  LEU A CB  1 
ATOM   380  C  CG  . LEU A  1  51  ? 43.448  -5.736  46.913 1.00 36.79  ? 64  LEU A CG  1 
ATOM   381  C  CD1 . LEU A  1  51  ? 43.070  -4.530  46.087 1.00 35.75  ? 64  LEU A CD1 1 
ATOM   382  C  CD2 . LEU A  1  51  ? 44.954  -5.943  46.964 1.00 37.13  ? 64  LEU A CD2 1 
ATOM   383  N  N   . PRO A  1  52  ? 43.322  -5.695  51.405 1.00 34.53  ? 65  PRO A N   1 
ATOM   384  C  CA  . PRO A  1  52  ? 42.859  -5.029  52.622 1.00 31.37  ? 65  PRO A CA  1 
ATOM   385  C  C   . PRO A  1  52  ? 41.666  -4.128  52.309 1.00 32.87  ? 65  PRO A C   1 
ATOM   386  O  O   . PRO A  1  52  ? 41.661  -3.435  51.287 1.00 32.41  ? 65  PRO A O   1 
ATOM   387  C  CB  . PRO A  1  52  ? 44.079  -4.228  53.061 1.00 32.50  ? 65  PRO A CB  1 
ATOM   388  C  CG  . PRO A  1  52  ? 45.259  -4.955  52.461 1.00 31.47  ? 65  PRO A CG  1 
ATOM   389  C  CD  . PRO A  1  52  ? 44.764  -5.512  51.159 1.00 33.03  ? 65  PRO A CD  1 
ATOM   390  N  N   . ARG A  1  53  ? 40.668  -4.131  53.203 1.00 31.90  ? 66  ARG A N   1 
ATOM   391  C  CA  . ARG A  1  53  ? 39.375  -3.522  52.923 1.00 30.98  ? 66  ARG A CA  1 
ATOM   392  C  C   . ARG A  1  53  ? 39.448  -1.995  52.935 1.00 29.38  ? 66  ARG A C   1 
ATOM   393  O  O   . ARG A  1  53  ? 38.545  -1.329  52.437 1.00 28.17  ? 66  ARG A O   1 
ATOM   394  C  CB  . ARG A  1  53  ? 38.315  -4.036  53.899 1.00 33.25  ? 66  ARG A CB  1 
ATOM   395  C  CG  . ARG A  1  53  ? 38.051  -5.521  53.709 1.00 34.28  ? 66  ARG A CG  1 
ATOM   396  C  CD  . ARG A  1  53  ? 36.843  -6.024  54.488 1.00 35.12  ? 66  ARG A CD  1 
ATOM   397  N  NE  . ARG A  1  53  ? 36.611  -7.444  54.213 1.00 35.59  ? 66  ARG A NE  1 
ATOM   398  C  CZ  . ARG A  1  53  ? 35.715  -7.926  53.353 1.00 38.24  ? 66  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A  1  53  ? 35.055  -7.129  52.528 1.00 37.27  ? 66  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A  1  53  ? 35.512  -9.223  53.284 1.00 39.42  ? 66  ARG A NH2 1 
ATOM   401  N  N   . ASP A  1  54  ? 40.531  -1.453  53.494 1.00 31.56  ? 67  ASP A N   1 
ATOM   402  C  CA  . ASP A  1  54  ? 40.752  -0.020  53.561 1.00 32.37  ? 67  ASP A CA  1 
ATOM   403  C  C   . ASP A  1  54  ? 41.326  0.509   52.252 1.00 30.99  ? 67  ASP A C   1 
ATOM   404  O  O   . ASP A  1  54  ? 41.405  1.716   52.070 1.00 31.22  ? 67  ASP A O   1 
ATOM   405  C  CB  . ASP A  1  54  ? 41.605  0.341   54.761 1.00 37.78  ? 67  ASP A CB  1 
ATOM   406  C  CG  . ASP A  1  54  ? 43.032  -0.191  54.782 1.00 45.50  ? 67  ASP A CG  1 
ATOM   407  O  OD1 . ASP A  1  54  ? 43.474  -0.782  53.774 1.00 48.74  ? 67  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A  1  54  ? 43.697  -0.005  55.825 1.00 51.10  ? 67  ASP A OD2 1 
ATOM   409  N  N   . GLY A  1  55  ? 41.711  -0.384  51.336 1.00 32.37  ? 68  GLY A N   1 
ATOM   410  C  CA  . GLY A  1  55  ? 42.037  0.018   49.974 1.00 32.86  ? 68  GLY A CA  1 
ATOM   411  C  C   . GLY A  1  55  ? 43.469  0.524   49.849 1.00 33.80  ? 68  GLY A C   1 
ATOM   412  O  O   . GLY A  1  55  ? 43.788  1.243   48.910 1.00 35.83  ? 68  GLY A O   1 
ATOM   413  N  N   . VAL A  1  56  ? 44.318  0.122   50.799 1.00 34.00  ? 69  VAL A N   1 
ATOM   414  C  CA  . VAL A  1  56  ? 45.737  0.440   50.794 1.00 35.49  ? 69  VAL A CA  1 
ATOM   415  C  C   . VAL A  1  56  ? 46.494  -0.874  50.895 1.00 30.34  ? 69  VAL A C   1 
ATOM   416  O  O   . VAL A  1  56  ? 46.231  -1.650  51.805 1.00 32.74  ? 69  VAL A O   1 
ATOM   417  C  CB  . VAL A  1  56  ? 46.103  1.355   51.981 1.00 41.70  ? 69  VAL A CB  1 
ATOM   418  C  CG1 . VAL A  1  56  ? 47.603  1.578   52.093 1.00 42.29  ? 69  VAL A CG1 1 
ATOM   419  C  CG2 . VAL A  1  56  ? 45.356  2.681   51.941 1.00 42.25  ? 69  VAL A CG2 1 
ATOM   420  N  N   . ALA A  1  57  ? 47.437  -1.109  49.981 1.00 28.02  ? 70  ALA A N   1 
ATOM   421  C  CA  . ALA A  1  57  ? 48.078  -2.409  49.892 1.00 28.56  ? 70  ALA A CA  1 
ATOM   422  C  C   . ALA A  1  57  ? 49.503  -2.313  49.346 1.00 29.70  ? 70  ALA A C   1 
ATOM   423  O  O   . ALA A  1  57  ? 49.864  -1.312  48.736 1.00 31.83  ? 70  ALA A O   1 
ATOM   424  C  CB  . ALA A  1  57  ? 47.229  -3.276  49.018 1.00 28.62  ? 70  ALA A CB  1 
ATOM   425  N  N   . THR A  1  58  ? 50.290  -3.374  49.565 1.00 27.69  ? 71  THR A N   1 
ATOM   426  C  CA  . THR A  1  58  ? 51.616  -3.510  48.980 1.00 29.20  ? 71  THR A CA  1 
ATOM   427  C  C   . THR A  1  58  ? 51.486  -3.955  47.530 1.00 30.07  ? 71  THR A C   1 
ATOM   428  O  O   . THR A  1  58  ? 50.508  -4.597  47.172 1.00 32.47  ? 71  THR A O   1 
ATOM   429  C  CB  . THR A  1  58  ? 52.480  -4.521  49.733 1.00 30.11  ? 71  THR A CB  1 
ATOM   430  O  OG1 . THR A  1  58  ? 51.902  -5.796  49.489 1.00 31.16  ? 71  THR A OG1 1 
ATOM   431  C  CG2 . THR A  1  58  ? 52.543  -4.282  51.229 1.00 31.62  ? 71  THR A CG2 1 
ATOM   432  N  N   . PRO A  1  59  ? 52.472  -3.660  46.659 1.00 31.19  ? 72  PRO A N   1 
ATOM   433  C  CA  . PRO A  1  59  ? 52.515  -4.241  45.318 1.00 31.43  ? 72  PRO A CA  1 
ATOM   434  C  C   . PRO A  1  59  ? 52.265  -5.745  45.295 1.00 31.94  ? 72  PRO A C   1 
ATOM   435  O  O   . PRO A  1  59  ? 51.499  -6.226  44.457 1.00 33.44  ? 72  PRO A O   1 
ATOM   436  C  CB  . PRO A  1  59  ? 53.926  -3.867  44.831 1.00 31.04  ? 72  PRO A CB  1 
ATOM   437  C  CG  . PRO A  1  59  ? 54.154  -2.505  45.483 1.00 31.98  ? 72  PRO A CG  1 
ATOM   438  C  CD  . PRO A  1  59  ? 53.551  -2.684  46.881 1.00 31.68  ? 72  PRO A CD  1 
ATOM   439  N  N   . ALA A  1  60  ? 52.910  -6.485  46.206 1.00 32.35  ? 73  ALA A N   1 
ATOM   440  C  CA  . ALA A  1  60  ? 52.788  -7.941  46.208 1.00 33.58  ? 73  ALA A CA  1 
ATOM   441  C  C   . ALA A  1  60  ? 51.356  -8.396  46.501 1.00 33.90  ? 73  ALA A C   1 
ATOM   442  O  O   . ALA A  1  60  ? 50.885  -9.346  45.889 1.00 31.85  ? 73  ALA A O   1 
ATOM   443  C  CB  . ALA A  1  60  ? 53.748  -8.543  47.189 1.00 33.45  ? 73  ALA A CB  1 
ATOM   444  N  N   . GLN A  1  61  ? 50.667  -7.702  47.420 1.00 33.24  ? 74  GLN A N   1 
ATOM   445  C  CA  . GLN A  1  61  ? 49.288  -8.022  47.761 1.00 30.47  ? 74  GLN A CA  1 
ATOM   446  C  C   . GLN A  1  61  ? 48.354  -7.809  46.574 1.00 31.21  ? 74  GLN A C   1 
ATOM   447  O  O   . GLN A  1  61  ? 47.437  -8.602  46.354 1.00 29.90  ? 74  GLN A O   1 
ATOM   448  C  CB  . GLN A  1  61  ? 48.796  -7.163  48.914 1.00 28.17  ? 74  GLN A CB  1 
ATOM   449  C  CG  . GLN A  1  61  ? 49.428  -7.533  50.243 1.00 30.47  ? 74  GLN A CG  1 
ATOM   450  C  CD  . GLN A  1  61  ? 48.960  -6.636  51.362 1.00 33.93  ? 74  GLN A CD  1 
ATOM   451  O  OE1 . GLN A  1  61  ? 48.894  -5.406  51.241 1.00 37.92  ? 74  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A  1  61  ? 48.612  -7.265  52.468 1.00 35.55  ? 74  GLN A NE2 1 
ATOM   453  N  N   . ILE A  1  62  ? 48.594  -6.717  45.842 1.00 30.56  ? 75  ILE A N   1 
ATOM   454  C  CA  . ILE A  1  62  ? 47.803  -6.353  44.675 1.00 31.90  ? 75  ILE A CA  1 
ATOM   455  C  C   . ILE A  1  62  ? 47.956  -7.419  43.596 1.00 30.05  ? 75  ILE A C   1 
ATOM   456  O  O   . ILE A  1  62  ? 46.976  -7.818  42.973 1.00 29.77  ? 75  ILE A O   1 
ATOM   457  C  CB  . ILE A  1  62  ? 48.193  -4.945  44.175 1.00 33.98  ? 75  ILE A CB  1 
ATOM   458  C  CG1 . ILE A  1  62  ? 47.756  -3.886  45.206 1.00 36.66  ? 75  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A  1  62  ? 47.620  -4.649  42.788 1.00 33.16  ? 75  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A  1  62  ? 48.147  -2.457  44.864 1.00 37.75  ? 75  ILE A CD1 1 
ATOM   461  N  N   . ILE A  1  63  ? 49.184  -7.887  43.389 1.00 30.03  ? 76  ILE A N   1 
ATOM   462  C  CA  . ILE A  1  63  ? 49.427  -8.864  42.345 1.00 32.65  ? 76  ILE A CA  1 
ATOM   463  C  C   . ILE A  1  63  ? 48.728  -10.165 42.722 1.00 31.72  ? 76  ILE A C   1 
ATOM   464  O  O   . ILE A  1  63  ? 48.009  -10.728 41.896 1.00 32.11  ? 76  ILE A O   1 
ATOM   465  C  CB  . ILE A  1  63  ? 50.929  -9.036  42.057 1.00 32.42  ? 76  ILE A CB  1 
ATOM   466  C  CG1 . ILE A  1  63  ? 51.476  -7.790  41.375 1.00 35.10  ? 76  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A  1  63  ? 51.197  -10.277 41.209 1.00 33.20  ? 76  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A  1  63  ? 52.991  -7.646  41.414 1.00 38.31  ? 76  ILE A CD1 1 
ATOM   469  N  N   . THR A  1  64  ? 48.908  -10.645 43.958 1.00 31.46  ? 77  THR A N   1 
ATOM   470  C  CA  A THR A  1  64  ? 48.308  -11.916 44.327 0.50 32.27  ? 77  THR A CA  1 
ATOM   471  C  CA  B THR A  1  64  ? 48.305  -11.915 44.337 0.50 32.34  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A  1  64  ? 46.782  -11.782 44.253 1.00 31.63  ? 77  THR A C   1 
ATOM   473  O  O   . THR A  1  64  ? 46.113  -12.704 43.805 1.00 32.28  ? 77  THR A O   1 
ATOM   474  C  CB  A THR A  1  64  ? 48.804  -12.417 45.688 0.50 31.78  ? 77  THR A CB  1 
ATOM   475  C  CB  B THR A  1  64  ? 48.795  -12.411 45.705 0.50 32.61  ? 77  THR A CB  1 
ATOM   476  O  OG1 A THR A  1  64  ? 48.271  -11.509 46.645 0.50 37.86  ? 77  THR A OG1 1 
ATOM   477  O  OG1 B THR A  1  64  ? 48.008  -13.533 46.098 0.50 29.50  ? 77  THR A OG1 1 
ATOM   478  C  CG2 A THR A  1  64  ? 50.318  -12.534 45.773 0.50 29.10  ? 77  THR A CG2 1 
ATOM   479  C  CG2 B THR A  1  64  ? 48.608  -11.407 46.822 0.50 35.90  ? 77  THR A CG2 1 
ATOM   480  N  N   . ALA A  1  65  ? 46.232  -10.615 44.635 1.00 29.91  ? 78  ALA A N   1 
ATOM   481  C  CA  . ALA A  1  65  ? 44.787  -10.402 44.641 1.00 28.91  ? 78  ALA A CA  1 
ATOM   482  C  C   . ALA A  1  65  ? 44.184  -10.404 43.243 1.00 26.39  ? 78  ALA A C   1 
ATOM   483  O  O   . ALA A  1  65  ? 43.107  -10.959 43.057 1.00 28.74  ? 78  ALA A O   1 
ATOM   484  C  CB  . ALA A  1  65  ? 44.421  -9.119  45.349 1.00 30.61  ? 78  ALA A CB  1 
ATOM   485  N  N   . THR A  1  66  ? 44.825  -9.751  42.272 1.00 26.32  ? 79  THR A N   1 
ATOM   486  C  CA  . THR A  1  66  ? 44.297  -9.726  40.912 1.00 26.91  ? 79  THR A CA  1 
ATOM   487  C  C   . THR A  1  66  ? 44.342  -11.130 40.314 1.00 27.75  ? 79  THR A C   1 
ATOM   488  O  O   . THR A  1  66  ? 43.510  -11.470 39.482 1.00 28.89  ? 79  THR A O   1 
ATOM   489  C  CB  . THR A  1  66  ? 45.051  -8.728  40.028 1.00 30.36  ? 79  THR A CB  1 
ATOM   490  O  OG1 . THR A  1  66  ? 46.404  -9.163  39.917 1.00 32.37  ? 79  THR A OG1 1 
ATOM   491  C  CG2 . THR A  1  66  ? 45.001  -7.306  40.569 1.00 31.19  ? 79  THR A CG2 1 
ATOM   492  N  N   . GLN A  1  67  ? 45.317  -11.943 40.728 1.00 30.60  ? 80  GLN A N   1 
ATOM   493  C  CA  . GLN A  1  67  ? 45.451  -13.308 40.240 1.00 31.18  ? 80  GLN A CA  1 
ATOM   494  C  C   . GLN A  1  67  ? 44.398  -14.204 40.895 1.00 29.45  ? 80  GLN A C   1 
ATOM   495  O  O   . GLN A  1  67  ? 43.684  -14.905 40.203 1.00 29.96  ? 80  GLN A O   1 
ATOM   496  C  CB  . GLN A  1  67  ? 46.893  -13.794 40.440 1.00 33.72  ? 80  GLN A CB  1 
ATOM   497  C  CG  . GLN A  1  67  ? 47.919  -13.068 39.565 1.00 34.88  ? 80  GLN A CG  1 
ATOM   498  C  CD  . GLN A  1  67  ? 49.362  -13.527 39.705 1.00 35.87  ? 80  GLN A CD  1 
ATOM   499  O  OE1 . GLN A  1  67  ? 50.200  -13.256 38.845 1.00 38.10  ? 80  GLN A OE1 1 
ATOM   500  N  NE2 . GLN A  1  67  ? 49.704  -14.233 40.770 1.00 36.39  ? 80  GLN A NE2 1 
ATOM   501  N  N   . GLU A  1  68  ? 44.289  -14.191 42.223 1.00 31.84  ? 81  GLU A N   1 
ATOM   502  C  CA  . GLU A  1  68  ? 43.345  -15.043 42.936 1.00 35.29  ? 81  GLU A CA  1 
ATOM   503  C  C   . GLU A  1  68  ? 41.909  -14.705 42.548 1.00 35.21  ? 81  GLU A C   1 
ATOM   504  O  O   . GLU A  1  68  ? 41.096  -15.590 42.305 1.00 33.41  ? 81  GLU A O   1 
ATOM   505  C  CB  . GLU A  1  68  ? 43.459  -14.897 44.454 1.00 39.50  ? 81  GLU A CB  1 
ATOM   506  C  CG  . GLU A  1  68  ? 44.751  -15.475 45.026 1.00 46.08  ? 81  GLU A CG  1 
ATOM   507  C  CD  . GLU A  1  68  ? 44.956  -16.954 44.753 1.00 55.09  ? 81  GLU A CD  1 
ATOM   508  O  OE1 . GLU A  1  68  ? 45.999  -17.368 44.172 1.00 54.29  ? 81  GLU A OE1 1 
ATOM   509  O  OE2 . GLU A  1  68  ? 44.017  -17.690 45.122 1.00 66.10  ? 81  GLU A OE2 1 
ATOM   510  N  N   . GLY A  1  69  ? 41.602  -13.409 42.499 1.00 35.38  ? 82  GLY A N   1 
ATOM   511  C  CA  . GLY A  1  69  ? 40.234  -12.959 42.337 1.00 31.61  ? 82  GLY A CA  1 
ATOM   512  C  C   . GLY A  1  69  ? 39.758  -13.044 40.890 1.00 31.47  ? 82  GLY A C   1 
ATOM   513  O  O   . GLY A  1  69  ? 38.578  -13.283 40.661 1.00 30.43  ? 82  GLY A O   1 
ATOM   514  N  N   . PHE A  1  70  ? 40.648  -12.793 39.917 1.00 32.39  ? 83  PHE A N   1 
ATOM   515  C  CA  . PHE A  1  70  ? 40.198  -12.582 38.550 1.00 31.02  ? 83  PHE A CA  1 
ATOM   516  C  C   . PHE A  1  70  ? 40.990  -13.391 37.528 1.00 32.09  ? 83  PHE A C   1 
ATOM   517  O  O   . PHE A  1  70  ? 40.629  -13.397 36.353 1.00 34.10  ? 83  PHE A O   1 
ATOM   518  C  CB  . PHE A  1  70  ? 40.282  -11.101 38.173 1.00 30.24  ? 83  PHE A CB  1 
ATOM   519  C  CG  . PHE A  1  70  ? 39.157  -10.237 38.718 1.00 29.37  ? 83  PHE A CG  1 
ATOM   520  C  CD1 . PHE A  1  70  ? 37.871  -10.350 38.208 1.00 30.20  ? 83  PHE A CD1 1 
ATOM   521  C  CD2 . PHE A  1  70  ? 39.385  -9.290  39.702 1.00 29.85  ? 83  PHE A CD2 1 
ATOM   522  C  CE1 . PHE A  1  70  ? 36.839  -9.571  38.686 1.00 29.43  ? 83  PHE A CE1 1 
ATOM   523  C  CE2 . PHE A  1  70  ? 38.345  -8.502  40.166 1.00 30.42  ? 83  PHE A CE2 1 
ATOM   524  C  CZ  . PHE A  1  70  ? 37.080  -8.641  39.650 1.00 30.49  ? 83  PHE A CZ  1 
ATOM   525  N  N   . ASN A  1  71  ? 42.060  -14.059 37.971 1.00 32.75  ? 84  ASN A N   1 
ATOM   526  C  CA  . ASN A  1  71  ? 43.008  -14.723 37.086 1.00 30.31  ? 84  ASN A CA  1 
ATOM   527  C  C   . ASN A  1  71  ? 43.635  -13.722 36.112 1.00 28.51  ? 84  ASN A C   1 
ATOM   528  O  O   . ASN A  1  71  ? 43.858  -14.043 34.955 1.00 28.84  ? 84  ASN A O   1 
ATOM   529  C  CB  . ASN A  1  71  ? 42.340  -15.900 36.384 1.00 33.39  ? 84  ASN A CB  1 
ATOM   530  C  CG  . ASN A  1  71  ? 43.240  -17.104 36.220 1.00 35.44  ? 84  ASN A CG  1 
ATOM   531  O  OD1 . ASN A  1  71  ? 44.467  -17.020 36.383 1.00 38.07  ? 84  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A  1  71  ? 42.641  -18.240 35.888 1.00 33.80  ? 84  ASN A ND2 1 
ATOM   533  N  N   . PHE A  1  72  ? 43.918  -12.498 36.569 1.00 28.06  ? 85  PHE A N   1 
ATOM   534  C  CA  . PHE A  1  72  ? 44.700  -11.557 35.785 1.00 29.60  ? 85  PHE A CA  1 
ATOM   535  C  C   . PHE A  1  72  ? 46.084  -12.168 35.544 1.00 31.59  ? 85  PHE A C   1 
ATOM   536  O  O   . PHE A  1  72  ? 46.701  -12.707 36.461 1.00 29.89  ? 85  PHE A O   1 
ATOM   537  C  CB  . PHE A  1  72  ? 44.769  -10.238 36.563 1.00 30.62  ? 85  PHE A CB  1 
ATOM   538  C  CG  . PHE A  1  72  ? 45.168  -8.990  35.792 1.00 32.47  ? 85  PHE A CG  1 
ATOM   539  C  CD1 . PHE A  1  72  ? 44.673  -8.750  34.518 1.00 34.36  ? 85  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A  1  72  ? 46.032  -8.051  36.341 1.00 33.07  ? 85  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A  1  72  ? 45.023  -7.604  33.823 1.00 34.93  ? 85  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A  1  72  ? 46.364  -6.901  35.641 1.00 33.12  ? 85  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A  1  72  ? 45.871  -6.686  34.382 1.00 34.43  ? 85  PHE A CZ  1 
ATOM   544  N  N   . GLU A  1  73  ? 46.574  -12.088 34.306 1.00 32.74  ? 86  GLU A N   1 
ATOM   545  C  CA  . GLU A  1  73  ? 47.828  -12.732 33.944 1.00 34.81  ? 86  GLU A CA  1 
ATOM   546  C  C   . GLU A  1  73  ? 48.990  -12.052 34.668 1.00 32.22  ? 86  GLU A C   1 
ATOM   547  O  O   . GLU A  1  73  ? 48.991  -10.834 34.833 1.00 33.24  ? 86  GLU A O   1 
ATOM   548  C  CB  . GLU A  1  73  ? 47.928  -12.694 32.421 1.00 38.63  ? 86  GLU A CB  1 
ATOM   549  C  CG  . GLU A  1  73  ? 49.061  -13.532 31.841 1.00 41.64  ? 86  GLU A CG  1 
ATOM   550  C  CD  . GLU A  1  73  ? 50.395  -12.822 31.783 1.00 46.95  ? 86  GLU A CD  1 
ATOM   551  O  OE1 . GLU A  1  73  ? 51.414  -13.393 32.259 1.00 47.38  ? 86  GLU A OE1 1 
ATOM   552  O  OE2 . GLU A  1  73  ? 50.404  -11.674 31.264 1.00 52.56  ? 86  GLU A OE2 1 
ATOM   553  N  N   . ASN A  1  74  ? 49.977  -12.860 35.088 1.00 32.20  ? 87  ASN A N   1 
ATOM   554  C  CA  . ASN A  1  74  ? 51.054  -12.454 35.984 1.00 31.37  ? 87  ASN A CA  1 
ATOM   555  C  C   . ASN A  1  74  ? 51.819  -11.239 35.466 1.00 33.51  ? 87  ASN A C   1 
ATOM   556  O  O   . ASN A  1  74  ? 52.039  -10.276 36.203 1.00 36.62  ? 87  ASN A O   1 
ATOM   557  C  CB  . ASN A  1  74  ? 52.016  -13.613 36.204 1.00 33.62  ? 87  ASN A CB  1 
ATOM   558  C  CG  . ASN A  1  74  ? 53.175  -13.302 37.122 1.00 32.82  ? 87  ASN A CG  1 
ATOM   559  O  OD1 . ASN A  1  74  ? 54.338  -13.390 36.704 1.00 35.42  ? 87  ASN A OD1 1 
ATOM   560  N  ND2 . ASN A  1  74  ? 52.886  -12.992 38.377 1.00 32.07  ? 87  ASN A ND2 1 
ATOM   561  N  N   . ASN A  1  75  ? 52.254  -11.288 34.205 1.00 34.55  ? 88  ASN A N   1 
ATOM   562  C  CA  A ASN A  1  75  ? 53.074  -10.219 33.657 0.50 35.87  ? 88  ASN A CA  1 
ATOM   563  C  CA  B ASN A  1  75  ? 53.067  -10.222 33.643 0.50 37.46  ? 88  ASN A CA  1 
ATOM   564  C  C   . ASN A  1  75  ? 52.270  -8.922  33.564 1.00 35.19  ? 88  ASN A C   1 
ATOM   565  O  O   . ASN A  1  75  ? 52.805  -7.840  33.821 1.00 40.57  ? 88  ASN A O   1 
ATOM   566  C  CB  A ASN A  1  75  ? 53.741  -10.627 32.347 0.50 35.33  ? 88  ASN A CB  1 
ATOM   567  C  CB  B ASN A  1  75  ? 53.577  -10.594 32.257 0.50 39.10  ? 88  ASN A CB  1 
ATOM   568  C  CG  A ASN A  1  75  ? 54.990  -11.448 32.604 0.50 35.22  ? 88  ASN A CG  1 
ATOM   569  C  CG  B ASN A  1  75  ? 54.939  -10.039 31.981 0.50 42.27  ? 88  ASN A CG  1 
ATOM   570  O  OD1 A ASN A  1  75  ? 55.109  -12.597 32.160 0.50 34.86  ? 88  ASN A OD1 1 
ATOM   571  O  OD1 B ASN A  1  75  ? 55.935  -10.533 32.523 0.50 47.28  ? 88  ASN A OD1 1 
ATOM   572  N  ND2 A ASN A  1  75  ? 55.940  -10.879 33.343 0.50 33.83  ? 88  ASN A ND2 1 
ATOM   573  N  ND2 B ASN A  1  75  ? 54.997  -9.079  31.078 0.50 42.92  ? 88  ASN A ND2 1 
ATOM   574  N  N   . ALA A  1  76  ? 50.995  -9.043  33.189 1.00 33.63  ? 89  ALA A N   1 
ATOM   575  C  CA  . ALA A  1  76  ? 50.104  -7.905  33.073 1.00 36.40  ? 89  ALA A CA  1 
ATOM   576  C  C   . ALA A  1  76  ? 49.916  -7.227  34.429 1.00 34.20  ? 89  ALA A C   1 
ATOM   577  O  O   . ALA A  1  76  ? 49.810  -6.007  34.507 1.00 37.76  ? 89  ALA A O   1 
ATOM   578  C  CB  . ALA A  1  76  ? 48.782  -8.377  32.514 1.00 39.91  ? 89  ALA A CB  1 
ATOM   579  N  N   . ALA A  1  77  ? 49.851  -8.042  35.480 1.00 30.69  ? 90  ALA A N   1 
ATOM   580  C  CA  . ALA A  1  77  ? 49.679  -7.558  36.837 1.00 30.74  ? 90  ALA A CA  1 
ATOM   581  C  C   . ALA A  1  77  ? 50.929  -6.801  37.289 1.00 32.36  ? 90  ALA A C   1 
ATOM   582  O  O   . ALA A  1  77  ? 50.830  -5.794  37.992 1.00 31.04  ? 90  ALA A O   1 
ATOM   583  C  CB  . ALA A  1  77  ? 49.375  -8.730  37.751 1.00 29.20  ? 90  ALA A CB  1 
ATOM   584  N  N   . ILE A  1  78  ? 52.100  -7.314  36.893 1.00 34.17  ? 91  ILE A N   1 
ATOM   585  C  CA  . ILE A  1  78  ? 53.373  -6.698  37.235 1.00 34.12  ? 91  ILE A CA  1 
ATOM   586  C  C   . ILE A  1  78  ? 53.480  -5.330  36.553 1.00 31.70  ? 91  ILE A C   1 
ATOM   587  O  O   . ILE A  1  78  ? 53.818  -4.334  37.195 1.00 30.09  ? 91  ILE A O   1 
ATOM   588  C  CB  . ILE A  1  78  ? 54.535  -7.664  36.912 1.00 34.63  ? 91  ILE A CB  1 
ATOM   589  C  CG1 . ILE A  1  78  ? 54.585  -8.778  37.952 1.00 32.96  ? 91  ILE A CG1 1 
ATOM   590  C  CG2 . ILE A  1  78  ? 55.888  -6.948  36.823 1.00 38.22  ? 91  ILE A CG2 1 
ATOM   591  C  CD1 . ILE A  1  78  ? 55.378  -10.004 37.539 1.00 31.80  ? 91  ILE A CD1 1 
ATOM   592  N  N   . VAL A  1  79  ? 53.123  -5.273  35.269 1.00 31.65  ? 92  VAL A N   1 
ATOM   593  C  CA  . VAL A  1  79  ? 53.261  -4.047  34.501 1.00 31.52  ? 92  VAL A CA  1 
ATOM   594  C  C   . VAL A  1  79  ? 52.367  -2.972  35.099 1.00 30.70  ? 92  VAL A C   1 
ATOM   595  O  O   . VAL A  1  79  ? 52.801  -1.833  35.257 1.00 42.80  ? 92  VAL A O   1 
ATOM   596  C  CB  . VAL A  1  79  ? 52.969  -4.262  33.004 1.00 31.78  ? 92  VAL A CB  1 
ATOM   597  C  CG1 . VAL A  1  79  ? 52.768  -2.947  32.262 1.00 32.67  ? 92  VAL A CG1 1 
ATOM   598  C  CG2 . VAL A  1  79  ? 54.080  -5.068  32.334 1.00 30.34  ? 92  VAL A CG2 1 
ATOM   599  N  N   . ALA A  1  80  ? 51.132  -3.328  35.442 1.00 30.75  ? 93  ALA A N   1 
ATOM   600  C  CA  . ALA A  1  80  ? 50.189  -2.346  35.966 1.00 30.45  ? 93  ALA A CA  1 
ATOM   601  C  C   . ALA A  1  80  ? 50.539  -1.940  37.396 1.00 28.56  ? 93  ALA A C   1 
ATOM   602  O  O   . ALA A  1  80  ? 50.444  -0.762  37.736 1.00 25.74  ? 93  ALA A O   1 
ATOM   603  C  CB  . ALA A  1  80  ? 48.769  -2.869  35.899 1.00 32.27  ? 93  ALA A CB  1 
ATOM   604  N  N   . THR A  1  81  ? 50.934  -2.907  38.229 1.00 27.15  ? 94  THR A N   1 
ATOM   605  C  CA  . THR A  1  81  ? 51.066  -2.627  39.649 1.00 29.00  ? 94  THR A CA  1 
ATOM   606  C  C   . THR A  1  81  ? 52.254  -1.702  39.910 1.00 31.55  ? 94  THR A C   1 
ATOM   607  O  O   . THR A  1  81  ? 52.123  -0.735  40.655 1.00 32.96  ? 94  THR A O   1 
ATOM   608  C  CB  . THR A  1  81  ? 51.181  -3.926  40.440 1.00 29.26  ? 94  THR A CB  1 
ATOM   609  O  OG1 . THR A  1  81  ? 49.951  -4.621  40.231 1.00 30.21  ? 94  THR A OG1 1 
ATOM   610  C  CG2 . THR A  1  81  ? 51.367  -3.687  41.925 1.00 28.74  ? 94  THR A CG2 1 
ATOM   611  N  N   . TYR A  1  82  ? 53.415  -1.980  39.305 1.00 34.94  ? 95  TYR A N   1 
ATOM   612  C  CA  . TYR A  1  82  ? 54.621  -1.204  39.590 1.00 33.67  ? 95  TYR A CA  1 
ATOM   613  C  C   . TYR A  1  82  ? 54.558  0.149   38.876 1.00 33.89  ? 95  TYR A C   1 
ATOM   614  O  O   . TYR A  1  82  ? 55.094  1.142   39.360 1.00 36.42  ? 95  TYR A O   1 
ATOM   615  C  CB  . TYR A  1  82  ? 55.890  -2.020  39.301 1.00 33.72  ? 95  TYR A CB  1 
ATOM   616  C  CG  . TYR A  1  82  ? 56.085  -3.154  40.301 1.00 34.16  ? 95  TYR A CG  1 
ATOM   617  C  CD1 . TYR A  1  82  ? 56.530  -2.899  41.596 1.00 31.91  ? 95  TYR A CD1 1 
ATOM   618  C  CD2 . TYR A  1  82  ? 55.755  -4.467  39.984 1.00 33.93  ? 95  TYR A CD2 1 
ATOM   619  C  CE1 . TYR A  1  82  ? 56.647  -3.907  42.537 1.00 30.15  ? 95  TYR A CE1 1 
ATOM   620  C  CE2 . TYR A  1  82  ? 55.876  -5.483  40.921 1.00 34.27  ? 95  TYR A CE2 1 
ATOM   621  C  CZ  . TYR A  1  82  ? 56.332  -5.204  42.193 1.00 31.34  ? 95  TYR A CZ  1 
ATOM   622  O  OH  . TYR A  1  82  ? 56.464  -6.212  43.095 1.00 37.54  ? 95  TYR A OH  1 
ATOM   623  N  N   . LEU A  1  83  ? 53.866  0.208   37.739 1.00 34.26  ? 96  LEU A N   1 
ATOM   624  C  CA  . LEU A  1  83  ? 53.564  1.495   37.145 1.00 35.38  ? 96  LEU A CA  1 
ATOM   625  C  C   . LEU A  1  83  ? 52.833  2.369   38.163 1.00 34.02  ? 96  LEU A C   1 
ATOM   626  O  O   . LEU A  1  83  ? 53.215  3.502   38.436 1.00 38.78  ? 96  LEU A O   1 
ATOM   627  C  CB  . LEU A  1  83  ? 52.737  1.303   35.881 1.00 35.75  ? 96  LEU A CB  1 
ATOM   628  C  CG  . LEU A  1  83  ? 52.263  2.597   35.220 1.00 38.86  ? 96  LEU A CG  1 
ATOM   629  C  CD1 . LEU A  1  83  ? 53.465  3.386   34.730 1.00 37.44  ? 96  LEU A CD1 1 
ATOM   630  C  CD2 . LEU A  1  83  ? 51.262  2.277   34.102 1.00 43.03  ? 96  LEU A CD2 1 
ATOM   631  N  N   . GLY A  1  84  ? 51.750  1.841   38.717 1.00 33.42  ? 97  GLY A N   1 
ATOM   632  C  CA  . GLY A  1  84  ? 50.952  2.594   39.668 1.00 33.89  ? 97  GLY A CA  1 
ATOM   633  C  C   . GLY A  1  84  ? 51.752  2.958   40.915 1.00 33.38  ? 97  GLY A C   1 
ATOM   634  O  O   . GLY A  1  84  ? 51.603  4.064   41.445 1.00 32.65  ? 97  GLY A O   1 
ATOM   635  N  N   . HIS A  1  85  ? 52.594  2.023   41.370 1.00 33.56  ? 98  HIS A N   1 
ATOM   636  C  CA  . HIS A  1  85  ? 53.359  2.205   42.592 1.00 36.75  ? 98  HIS A CA  1 
ATOM   637  C  C   . HIS A  1  85  ? 54.478  3.228   42.407 1.00 34.99  ? 98  HIS A C   1 
ATOM   638  O  O   . HIS A  1  85  ? 54.658  4.083   43.264 1.00 38.01  ? 98  HIS A O   1 
ATOM   639  C  CB  . HIS A  1  85  ? 53.942  0.870   43.058 1.00 37.65  ? 98  HIS A CB  1 
ATOM   640  C  CG  . HIS A  1  85  ? 54.589  0.920   44.394 1.00 38.14  ? 98  HIS A CG  1 
ATOM   641  N  ND1 . HIS A  1  85  ? 53.975  1.467   45.502 1.00 41.31  ? 98  HIS A ND1 1 
ATOM   642  C  CD2 . HIS A  1  85  ? 55.758  0.427   44.813 1.00 36.79  ? 98  HIS A CD2 1 
ATOM   643  C  CE1 . HIS A  1  85  ? 54.776  1.326   46.554 1.00 40.05  ? 98  HIS A CE1 1 
ATOM   644  N  NE2 . HIS A  1  85  ? 55.870  0.700   46.157 1.00 38.11  ? 98  HIS A NE2 1 
ATOM   645  N  N   . LEU A  1  86  ? 55.228  3.140   41.303 1.00 32.94  ? 99  LEU A N   1 
ATOM   646  C  CA  . LEU A  1  86  ? 56.323  4.069   41.055 1.00 36.52  ? 99  LEU A CA  1 
ATOM   647  C  C   . LEU A  1  86  ? 55.817  5.512   41.043 1.00 37.29  ? 99  LEU A C   1 
ATOM   648  O  O   . LEU A  1  86  ? 56.425  6.386   41.664 1.00 36.34  ? 99  LEU A O   1 
ATOM   649  C  CB  . LEU A  1  86  ? 57.021  3.726   39.742 1.00 38.23  ? 99  LEU A CB  1 
ATOM   650  C  CG  . LEU A  1  86  ? 57.950  2.507   39.784 1.00 40.74  ? 99  LEU A CG  1 
ATOM   651  C  CD1 . LEU A  1  86  ? 58.277  2.007   38.393 1.00 41.60  ? 99  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A  1  86  ? 59.224  2.820   40.539 1.00 40.65  ? 99  LEU A CD2 1 
ATOM   653  N  N   . LEU A  1  87  ? 54.697  5.742   40.341 1.00 33.09  ? 100 LEU A N   1 
ATOM   654  C  CA  . LEU A  1  87  ? 54.147  7.069   40.131 1.00 31.03  ? 100 LEU A CA  1 
ATOM   655  C  C   . LEU A  1  87  ? 53.333  7.550   41.329 1.00 32.92  ? 100 LEU A C   1 
ATOM   656  O  O   . LEU A  1  87  ? 53.358  8.742   41.630 1.00 35.77  ? 100 LEU A O   1 
ATOM   657  C  CB  . LEU A  1  87  ? 53.289  7.042   38.874 1.00 32.23  ? 100 LEU A CB  1 
ATOM   658  C  CG  . LEU A  1  87  ? 54.040  6.787   37.564 1.00 33.85  ? 100 LEU A CG  1 
ATOM   659  C  CD1 . LEU A  1  87  ? 53.101  6.796   36.391 1.00 36.71  ? 100 LEU A CD1 1 
ATOM   660  C  CD2 . LEU A  1  87  ? 55.117  7.815   37.320 1.00 34.77  ? 100 LEU A CD2 1 
ATOM   661  N  N   . ASN A  1  88  ? 52.602  6.648   42.002 1.00 34.08  ? 101 ASN A N   1 
ATOM   662  C  CA  . ASN A  1  88  ? 51.574  7.081   42.939 1.00 34.86  ? 101 ASN A CA  1 
ATOM   663  C  C   . ASN A  1  88  ? 51.682  6.465   44.332 1.00 34.49  ? 101 ASN A C   1 
ATOM   664  O  O   . ASN A  1  88  ? 50.862  6.785   45.195 1.00 36.86  ? 101 ASN A O   1 
ATOM   665  C  CB  . ASN A  1  88  ? 50.177  6.746   42.445 1.00 35.25  ? 101 ASN A CB  1 
ATOM   666  C  CG  . ASN A  1  88  ? 49.886  7.325   41.087 1.00 37.10  ? 101 ASN A CG  1 
ATOM   667  O  OD1 . ASN A  1  88  ? 50.111  8.515   40.846 1.00 37.21  ? 101 ASN A OD1 1 
ATOM   668  N  ND2 . ASN A  1  88  ? 49.351  6.509   40.198 1.00 40.83  ? 101 ASN A ND2 1 
ATOM   669  N  N   . GLY A  1  89  ? 52.661  5.581   44.544 1.00 33.71  ? 102 GLY A N   1 
ATOM   670  C  CA  . GLY A  1  89  ? 52.784  4.872   45.808 1.00 34.32  ? 102 GLY A CA  1 
ATOM   671  C  C   . GLY A  1  89  ? 53.899  5.445   46.681 1.00 33.22  ? 102 GLY A C   1 
ATOM   672  O  O   . GLY A  1  89  ? 54.637  6.331   46.260 1.00 32.52  ? 102 GLY A O   1 
ATOM   673  N  N   . ASN A  1  90  ? 54.009  4.922   47.904 1.00 33.24  ? 103 ASN A N   1 
ATOM   674  C  CA  . ASN A  1  90  ? 55.072  5.310   48.809 1.00 33.21  ? 103 ASN A CA  1 
ATOM   675  C  C   . ASN A  1  90  ? 56.131  4.217   48.776 1.00 33.34  ? 103 ASN A C   1 
ATOM   676  O  O   . ASN A  1  90  ? 55.888  3.121   49.255 1.00 32.41  ? 103 ASN A O   1 
ATOM   677  C  CB  . ASN A  1  90  ? 54.515  5.548   50.204 1.00 34.79  ? 103 ASN A CB  1 
ATOM   678  C  CG  . ASN A  1  90  ? 55.565  6.023   51.180 1.00 34.87  ? 103 ASN A CG  1 
ATOM   679  O  OD1 . ASN A  1  90  ? 56.667  5.468   51.240 1.00 35.18  ? 103 ASN A OD1 1 
ATOM   680  N  ND2 . ASN A  1  90  ? 55.236  7.050   51.945 1.00 35.23  ? 103 ASN A ND2 1 
ATOM   681  N  N   . LEU A  1  91  ? 57.304  4.517   48.216 1.00 36.64  ? 104 LEU A N   1 
ATOM   682  C  CA  . LEU A  1  91  ? 58.300  3.488   47.945 1.00 37.50  ? 104 LEU A CA  1 
ATOM   683  C  C   . LEU A  1  91  ? 59.011  3.037   49.215 1.00 33.01  ? 104 LEU A C   1 
ATOM   684  O  O   . LEU A  1  91  ? 59.512  1.920   49.281 1.00 32.20  ? 104 LEU A O   1 
ATOM   685  C  CB  . LEU A  1  91  ? 59.253  4.044   46.898 1.00 40.20  ? 104 LEU A CB  1 
ATOM   686  C  CG  . LEU A  1  91  ? 58.574  4.357   45.562 1.00 44.24  ? 104 LEU A CG  1 
ATOM   687  C  CD1 . LEU A  1  91  ? 59.493  5.119   44.661 1.00 50.29  ? 104 LEU A CD1 1 
ATOM   688  C  CD2 . LEU A  1  91  ? 58.139  3.094   44.876 1.00 45.04  ? 104 LEU A CD2 1 
ATOM   689  N  N   . VAL A  1  92  ? 58.987  3.885   50.241 1.00 32.28  ? 105 VAL A N   1 
ATOM   690  C  CA  . VAL A  1  92  ? 59.685  3.605   51.477 1.00 33.02  ? 105 VAL A CA  1 
ATOM   691  C  C   . VAL A  1  92  ? 58.881  2.632   52.335 1.00 34.02  ? 105 VAL A C   1 
ATOM   692  O  O   . VAL A  1  92  ? 59.452  1.701   52.905 1.00 34.53  ? 105 VAL A O   1 
ATOM   693  C  CB  . VAL A  1  92  ? 59.976  4.923   52.212 1.00 33.54  ? 105 VAL A CB  1 
ATOM   694  C  CG1 . VAL A  1  92  ? 60.443  4.674   53.645 1.00 35.04  ? 105 VAL A CG1 1 
ATOM   695  C  CG2 . VAL A  1  92  ? 60.982  5.767   51.435 1.00 32.97  ? 105 VAL A CG2 1 
ATOM   696  N  N   . THR A  1  93  ? 57.567  2.871   52.455 1.00 35.86  ? 106 THR A N   1 
ATOM   697  C  CA  . THR A  1  93  ? 56.694  1.996   53.233 1.00 35.53  ? 106 THR A CA  1 
ATOM   698  C  C   . THR A  1  93  ? 56.144  0.858   52.370 1.00 33.72  ? 106 THR A C   1 
ATOM   699  O  O   . THR A  1  93  ? 55.583  -0.087  52.903 1.00 38.47  ? 106 THR A O   1 
ATOM   700  C  CB  . THR A  1  93  ? 55.536  2.771   53.863 1.00 36.06  ? 106 THR A CB  1 
ATOM   701  O  OG1 . THR A  1  93  ? 54.727  3.279   52.806 1.00 36.66  ? 106 THR A OG1 1 
ATOM   702  C  CG2 . THR A  1  93  ? 56.002  3.893   54.768 1.00 33.58  ? 106 THR A CG2 1 
ATOM   703  N  N   . ASP A  1  94  ? 56.238  0.984   51.045 1.00 33.08  ? 107 ASP A N   1 
ATOM   704  C  CA  . ASP A  1  94  ? 55.806  -0.040  50.108 1.00 31.43  ? 107 ASP A CA  1 
ATOM   705  C  C   . ASP A  1  94  ? 54.284  -0.165  50.094 1.00 32.17  ? 107 ASP A C   1 
ATOM   706  O  O   . ASP A  1  94  ? 53.766  -1.264  49.960 1.00 31.82  ? 107 ASP A O   1 
ATOM   707  C  CB  . ASP A  1  94  ? 56.471  -1.368  50.400 1.00 31.70  ? 107 ASP A CB  1 
ATOM   708  C  CG  . ASP A  1  94  ? 56.469  -2.377  49.254 1.00 33.82  ? 107 ASP A CG  1 
ATOM   709  O  OD1 . ASP A  1  94  ? 56.780  -1.966  48.093 1.00 34.47  ? 107 ASP A OD1 1 
ATOM   710  O  OD2 . ASP A  1  94  ? 56.205  -3.581  49.537 1.00 34.34  ? 107 ASP A OD2 1 
ATOM   711  N  N   . LEU A  1  95  ? 53.581  0.972   50.193 1.00 32.67  ? 108 LEU A N   1 
ATOM   712  C  CA  . LEU A  1  95  ? 52.132  0.988   50.224 1.00 31.05  ? 108 LEU A CA  1 
ATOM   713  C  C   . LEU A  1  95  ? 51.594  1.883   49.111 1.00 29.60  ? 108 LEU A C   1 
ATOM   714  O  O   . LEU A  1  95  ? 52.111  2.967   48.899 1.00 27.20  ? 108 LEU A O   1 
ATOM   715  C  CB  . LEU A  1  95  ? 51.671  1.457   51.598 1.00 30.30  ? 108 LEU A CB  1 
ATOM   716  C  CG  . LEU A  1  95  ? 51.979  0.536   52.782 1.00 30.45  ? 108 LEU A CG  1 
ATOM   717  C  CD1 . LEU A  1  95  ? 51.601  1.221   54.085 1.00 29.09  ? 108 LEU A CD1 1 
ATOM   718  C  CD2 . LEU A  1  95  ? 51.238  -0.774  52.710 1.00 32.41  ? 108 LEU A CD2 1 
ATOM   719  N  N   . LEU A  1  96  ? 50.531  1.413   48.444 1.00 29.14  ? 109 LEU A N   1 
ATOM   720  C  CA  . LEU A  1  96  ? 49.842  2.161   47.408 1.00 30.00  ? 109 LEU A CA  1 
ATOM   721  C  C   . LEU A  1  96  ? 48.349  2.271   47.736 1.00 30.37  ? 109 LEU A C   1 
ATOM   722  O  O   . LEU A  1  96  ? 47.712  1.275   48.032 1.00 30.39  ? 109 LEU A O   1 
ATOM   723  C  CB  . LEU A  1  96  ? 50.089  1.411   46.104 1.00 29.65  ? 109 LEU A CB  1 
ATOM   724  C  CG  . LEU A  1  96  ? 49.221  1.836   44.920 1.00 31.74  ? 109 LEU A CG  1 
ATOM   725  C  CD1 . LEU A  1  96  ? 49.484  3.302   44.605 1.00 34.05  ? 109 LEU A CD1 1 
ATOM   726  C  CD2 . LEU A  1  96  ? 49.495  0.947   43.710 1.00 32.32  ? 109 LEU A CD2 1 
ATOM   727  N  N   . SER A  1  97  ? 47.812  3.494   47.689 1.00 31.04  ? 110 SER A N   1 
ATOM   728  C  CA  . SER A  1  97  ? 46.379  3.749   47.764 1.00 32.01  ? 110 SER A CA  1 
ATOM   729  C  C   . SER A  1  97  ? 45.725  3.499   46.414 1.00 29.02  ? 110 SER A C   1 
ATOM   730  O  O   . SER A  1  97  ? 46.180  4.039   45.416 1.00 28.75  ? 110 SER A O   1 
ATOM   731  C  CB  . SER A  1  97  ? 46.097  5.171   48.179 1.00 33.63  ? 110 SER A CB  1 
ATOM   732  O  OG  . SER A  1  97  ? 44.729  5.513   47.988 1.00 33.61  ? 110 SER A OG  1 
ATOM   733  N  N   . ILE A  1  98  ? 44.622  2.750   46.394 1.00 28.35  ? 111 ILE A N   1 
ATOM   734  C  CA  . ILE A  1  98  ? 43.930  2.491   45.140 1.00 29.21  ? 111 ILE A CA  1 
ATOM   735  C  C   . ILE A  1  98  ? 43.005  3.658   44.799 1.00 29.63  ? 111 ILE A C   1 
ATOM   736  O  O   . ILE A  1  98  ? 42.310  3.606   43.796 1.00 29.70  ? 111 ILE A O   1 
ATOM   737  C  CB  . ILE A  1  98  ? 43.174  1.151   45.163 1.00 29.41  ? 111 ILE A CB  1 
ATOM   738  C  CG1 . ILE A  1  98  ? 41.979  1.172   46.121 1.00 31.68  ? 111 ILE A CG1 1 
ATOM   739  C  CG2 . ILE A  1  98  ? 44.129  0.006   45.475 1.00 29.41  ? 111 ILE A CG2 1 
ATOM   740  C  CD1 . ILE A  1  98  ? 41.132  -0.082  46.101 1.00 31.55  ? 111 ILE A CD1 1 
ATOM   741  N  N   . GLY A  1  99  ? 43.003  4.702   45.636 1.00 33.51  ? 112 GLY A N   1 
ATOM   742  C  CA  . GLY A  1  99  ? 42.196  5.894   45.409 1.00 35.65  ? 112 GLY A CA  1 
ATOM   743  C  C   . GLY A  1  99  ? 43.000  7.174   45.615 1.00 34.34  ? 112 GLY A C   1 
ATOM   744  O  O   . GLY A  1  99  ? 43.964  7.419   44.908 1.00 37.02  ? 112 GLY A O   1 
ATOM   745  N  N   . GLY A  1  100 ? 42.573  7.993   46.572 1.00 35.48  ? 113 GLY A N   1 
ATOM   746  C  CA  . GLY A  1  100 ? 43.193  9.282   46.822 1.00 36.93  ? 113 GLY A CA  1 
ATOM   747  C  C   . GLY A  1  100 ? 44.165  9.218   47.995 1.00 35.38  ? 113 GLY A C   1 
ATOM   748  O  O   . GLY A  1  100 ? 44.535  8.139   48.444 1.00 31.57  ? 113 GLY A O   1 
ATOM   749  N  N   . ALA A  1  101 ? 44.559  10.405  48.465 1.00 38.94  ? 114 ALA A N   1 
ATOM   750  C  CA  . ALA A  1  101 ? 45.550  10.553  49.521 1.00 40.50  ? 114 ALA A CA  1 
ATOM   751  C  C   . ALA A  1  101 ? 45.016  10.018  50.845 1.00 36.72  ? 114 ALA A C   1 
ATOM   752  O  O   . ALA A  1  101 ? 43.831  10.108  51.122 1.00 34.19  ? 114 ALA A O   1 
ATOM   753  C  CB  . ALA A  1  101 ? 45.929  12.011  49.668 1.00 41.29  ? 114 ALA A CB  1 
ATOM   754  N  N   . THR A  1  102 ? 45.913  9.471   51.664 1.00 38.36  ? 115 THR A N   1 
ATOM   755  C  CA  . THR A  1  102 ? 45.519  8.953   52.958 1.00 39.73  ? 115 THR A CA  1 
ATOM   756  C  C   . THR A  1  102 ? 46.746  8.874   53.851 1.00 40.77  ? 115 THR A C   1 
ATOM   757  O  O   . THR A  1  102 ? 47.820  8.496   53.386 1.00 39.59  ? 115 THR A O   1 
ATOM   758  C  CB  . THR A  1  102 ? 44.872  7.580   52.791 1.00 38.89  ? 115 THR A CB  1 
ATOM   759  O  OG1 . THR A  1  102 ? 44.505  7.066   54.073 1.00 39.84  ? 115 THR A OG1 1 
ATOM   760  C  CG2 . THR A  1  102 ? 45.807  6.531   52.222 1.00 40.87  ? 115 THR A CG2 1 
ATOM   761  N  N   . PRO A  1  103 ? 46.612  9.146   55.167 1.00 45.40  ? 116 PRO A N   1 
ATOM   762  C  CA  . PRO A  1  103 ? 47.718  8.891   56.105 1.00 44.92  ? 116 PRO A CA  1 
ATOM   763  C  C   . PRO A  1  103 ? 48.165  7.427   56.180 1.00 38.72  ? 116 PRO A C   1 
ATOM   764  O  O   . PRO A  1  103 ? 49.259  7.137   56.653 1.00 37.39  ? 116 PRO A O   1 
ATOM   765  C  CB  . PRO A  1  103 ? 47.169  9.403   57.469 1.00 46.26  ? 116 PRO A CB  1 
ATOM   766  C  CG  . PRO A  1  103 ? 45.648  9.456   57.291 1.00 46.38  ? 116 PRO A CG  1 
ATOM   767  C  CD  . PRO A  1  103 ? 45.405  9.702   55.809 1.00 43.91  ? 116 PRO A CD  1 
ATOM   768  N  N   . LYS A  1  104 ? 47.315  6.504   55.711 1.00 34.46  ? 117 LYS A N   1 
ATOM   769  C  CA  . LYS A  1  104 ? 47.578  5.081   55.804 1.00 34.05  ? 117 LYS A CA  1 
ATOM   770  C  C   . LYS A  1  104 ? 48.789  4.635   54.985 1.00 34.21  ? 117 LYS A C   1 
ATOM   771  O  O   . LYS A  1  104 ? 49.314  3.561   55.257 1.00 33.87  ? 117 LYS A O   1 
ATOM   772  C  CB  . LYS A  1  104 ? 46.342  4.326   55.318 1.00 36.00  ? 117 LYS A CB  1 
ATOM   773  C  CG  . LYS A  1  104 ? 45.148  4.388   56.242 1.00 38.87  ? 117 LYS A CG  1 
ATOM   774  C  CD  . LYS A  1  104 ? 43.852  3.976   55.552 1.00 44.70  ? 117 LYS A CD  1 
ATOM   775  C  CE  . LYS A  1  104 ? 42.686  3.961   56.484 1.00 44.77  ? 117 LYS A CE  1 
ATOM   776  N  NZ  . LYS A  1  104 ? 42.849  2.871   57.445 1.00 48.02  ? 117 LYS A NZ  1 
ATOM   777  N  N   . THR A  1  105 ? 49.224  5.421   53.986 1.00 35.61  ? 118 THR A N   1 
ATOM   778  C  CA  . THR A  1  105 ? 50.407  5.060   53.209 1.00 37.44  ? 118 THR A CA  1 
ATOM   779  C  C   . THR A  1  105 ? 51.679  5.472   53.948 1.00 38.39  ? 118 THR A C   1 
ATOM   780  O  O   . THR A  1  105 ? 52.775  5.109   53.522 1.00 38.10  ? 118 THR A O   1 
ATOM   781  C  CB  . THR A  1  105 ? 50.387  5.667   51.804 1.00 38.52  ? 118 THR A CB  1 
ATOM   782  O  OG1 . THR A  1  105 ? 50.133  7.065   51.865 1.00 37.00  ? 118 THR A OG1 1 
ATOM   783  C  CG2 . THR A  1  105 ? 49.340  5.049   50.897 1.00 39.39  ? 118 THR A CG2 1 
ATOM   784  N  N   . GLY A  1  106 ? 51.524  6.259   55.021 1.00 36.48  ? 119 GLY A N   1 
ATOM   785  C  CA  . GLY A  1  106 ? 52.617  6.589   55.917 1.00 37.76  ? 119 GLY A CA  1 
ATOM   786  C  C   . GLY A  1  106 ? 53.185  7.987   55.672 1.00 38.47  ? 119 GLY A C   1 
ATOM   787  O  O   . GLY A  1  106 ? 52.652  8.747   54.869 1.00 37.73  ? 119 GLY A O   1 
ATOM   788  N  N   . PRO A  1  107 ? 54.289  8.348   56.367 1.00 40.35  ? 120 PRO A N   1 
ATOM   789  C  CA  . PRO A  1  107 ? 54.934  9.659   56.219 1.00 44.72  ? 120 PRO A CA  1 
ATOM   790  C  C   . PRO A  1  107 ? 55.206  10.034  54.760 1.00 45.82  ? 120 PRO A C   1 
ATOM   791  O  O   . PRO A  1  107 ? 55.850  9.284   54.036 1.00 43.86  ? 120 PRO A O   1 
ATOM   792  C  CB  . PRO A  1  107 ? 56.251  9.490   56.999 1.00 43.31  ? 120 PRO A CB  1 
ATOM   793  C  CG  . PRO A  1  107 ? 55.953  8.410   58.013 1.00 41.81  ? 120 PRO A CG  1 
ATOM   794  C  CD  . PRO A  1  107 ? 54.983  7.475   57.328 1.00 40.78  ? 120 PRO A CD  1 
ATOM   795  N  N   . PRO A  1  108 ? 54.740  11.203  54.276 1.00 46.20  ? 121 PRO A N   1 
ATOM   796  C  CA  . PRO A  1  108 ? 54.772  11.497  52.846 1.00 45.96  ? 121 PRO A CA  1 
ATOM   797  C  C   . PRO A  1  108 ? 56.206  11.555  52.326 1.00 45.21  ? 121 PRO A C   1 
ATOM   798  O  O   . PRO A  1  108 ? 57.125  11.854  53.080 1.00 42.48  ? 121 PRO A O   1 
ATOM   799  C  CB  . PRO A  1  108 ? 54.007  12.828  52.712 1.00 44.76  ? 121 PRO A CB  1 
ATOM   800  C  CG  . PRO A  1  108 ? 54.029  13.440  54.093 1.00 49.42  ? 121 PRO A CG  1 
ATOM   801  C  CD  . PRO A  1  108 ? 54.156  12.287  55.073 1.00 48.62  ? 121 PRO A CD  1 
ATOM   802  N  N   . PRO A  1  109 ? 56.444  11.234  51.032 1.00 46.88  ? 122 PRO A N   1 
ATOM   803  C  CA  . PRO A  1  109 ? 57.776  11.375  50.440 1.00 47.25  ? 122 PRO A CA  1 
ATOM   804  C  C   . PRO A  1  109 ? 58.127  12.831  50.136 1.00 46.66  ? 122 PRO A C   1 
ATOM   805  O  O   . PRO A  1  109 ? 57.256  13.694  50.191 1.00 45.89  ? 122 PRO A O   1 
ATOM   806  C  CB  . PRO A  1  109 ? 57.639  10.529  49.166 1.00 46.54  ? 122 PRO A CB  1 
ATOM   807  C  CG  . PRO A  1  109 ? 56.213  10.723  48.750 1.00 44.41  ? 122 PRO A CG  1 
ATOM   808  C  CD  . PRO A  1  109 ? 55.442  10.755  50.059 1.00 44.15  ? 122 PRO A CD  1 
ATOM   809  N  N   . PRO A  1  110 ? 59.399  13.145  49.793 1.00 45.66  ? 123 PRO A N   1 
ATOM   810  C  CA  . PRO A  1  110 ? 59.797  14.519  49.463 1.00 45.35  ? 123 PRO A CA  1 
ATOM   811  C  C   . PRO A  1  110 ? 59.222  14.984  48.132 1.00 45.43  ? 123 PRO A C   1 
ATOM   812  O  O   . PRO A  1  110 ? 59.298  14.255  47.151 1.00 44.57  ? 123 PRO A O   1 
ATOM   813  C  CB  . PRO A  1  110 ? 61.327  14.449  49.402 1.00 46.18  ? 123 PRO A CB  1 
ATOM   814  C  CG  . PRO A  1  110 ? 61.616  12.994  49.055 1.00 44.73  ? 123 PRO A CG  1 
ATOM   815  C  CD  . PRO A  1  110 ? 60.519  12.188  49.719 1.00 46.13  ? 123 PRO A CD  1 
ATOM   816  N  N   . PRO A  1  111 ? 58.618  16.191  48.051 1.00 46.99  ? 124 PRO A N   1 
ATOM   817  C  CA  . PRO A  1  111 ? 58.042  16.669  46.788 1.00 44.97  ? 124 PRO A CA  1 
ATOM   818  C  C   . PRO A  1  111 ? 59.112  16.798  45.707 1.00 42.19  ? 124 PRO A C   1 
ATOM   819  O  O   . PRO A  1  111 ? 60.281  16.964  46.038 1.00 47.76  ? 124 PRO A O   1 
ATOM   820  C  CB  . PRO A  1  111 ? 57.371  18.009  47.148 1.00 44.61  ? 124 PRO A CB  1 
ATOM   821  C  CG  . PRO A  1  111 ? 57.234  17.980  48.659 1.00 44.97  ? 124 PRO A CG  1 
ATOM   822  C  CD  . PRO A  1  111 ? 58.381  17.106  49.181 1.00 46.15  ? 124 PRO A CD  1 
ATOM   823  N  N   . PRO A  1  112 ? 58.793  16.743  44.392 1.00 44.21  ? 125 PRO A N   1 
ATOM   824  C  CA  . PRO A  1  112 ? 57.418  16.674  43.871 1.00 43.83  ? 125 PRO A CA  1 
ATOM   825  C  C   . PRO A  1  112 ? 56.658  15.353  43.941 1.00 40.54  ? 125 PRO A C   1 
ATOM   826  O  O   . PRO A  1  112 ? 55.522  15.281  43.485 1.00 39.68  ? 125 PRO A O   1 
ATOM   827  C  CB  . PRO A  1  112 ? 57.560  17.062  42.371 1.00 45.00  ? 125 PRO A CB  1 
ATOM   828  C  CG  . PRO A  1  112 ? 59.036  17.325  42.142 1.00 46.64  ? 125 PRO A CG  1 
ATOM   829  C  CD  . PRO A  1  112 ? 59.799  16.750  43.323 1.00 43.93  ? 125 PRO A CD  1 
ATOM   830  N  N   . ALA A  1  113 ? 57.273  14.308  44.496 1.00 38.78  ? 126 ALA A N   1 
ATOM   831  C  CA  . ALA A  1  113 ? 56.580  13.048  44.686 1.00 38.77  ? 126 ALA A CA  1 
ATOM   832  C  C   . ALA A  1  113 ? 55.493  13.235  45.739 1.00 36.94  ? 126 ALA A C   1 
ATOM   833  O  O   . ALA A  1  113 ? 55.641  14.062  46.633 1.00 34.04  ? 126 ALA A O   1 
ATOM   834  C  CB  . ALA A  1  113 ? 57.568  11.977  45.082 1.00 38.92  ? 126 ALA A CB  1 
ATOM   835  N  N   . HIS A  1  114 ? 54.419  12.439  45.639 1.00 37.14  ? 127 HIS A N   1 
ATOM   836  C  CA  . HIS A  1  114 ? 53.193  12.700  46.381 1.00 35.16  ? 127 HIS A CA  1 
ATOM   837  C  C   . HIS A  1  114 ? 52.689  11.447  47.092 1.00 36.86  ? 127 HIS A C   1 
ATOM   838  O  O   . HIS A  1  114 ? 52.213  11.534  48.214 1.00 40.15  ? 127 HIS A O   1 
ATOM   839  C  CB  . HIS A  1  114 ? 52.148  13.315  45.447 1.00 35.36  ? 127 HIS A CB  1 
ATOM   840  C  CG  . HIS A  1  114 ? 52.068  12.634  44.124 1.00 37.68  ? 127 HIS A CG  1 
ATOM   841  N  ND1 . HIS A  1  114 ? 51.413  11.435  43.964 1.00 37.36  ? 127 HIS A ND1 1 
ATOM   842  C  CD2 . HIS A  1  114 ? 52.579  12.937  42.923 1.00 36.35  ? 127 HIS A CD2 1 
ATOM   843  C  CE1 . HIS A  1  114 ? 51.521  11.048  42.704 1.00 40.16  ? 127 HIS A CE1 1 
ATOM   844  N  NE2 . HIS A  1  114 ? 52.226  11.944  42.054 1.00 37.59  ? 127 HIS A NE2 1 
ATOM   845  N  N   . ALA A  1  115 ? 52.769  10.288  46.431 1.00 41.12  ? 128 ALA A N   1 
ATOM   846  C  CA  . ALA A  1  115 ? 52.164  9.059   46.933 1.00 41.35  ? 128 ALA A CA  1 
ATOM   847  C  C   . ALA A  1  115 ? 50.666  9.249   47.169 1.00 38.96  ? 128 ALA A C   1 
ATOM   848  O  O   . ALA A  1  115 ? 50.124  8.769   48.154 1.00 39.26  ? 128 ALA A O   1 
ATOM   849  C  CB  . ALA A  1  115 ? 52.849  8.596   48.195 1.00 40.85  ? 128 ALA A CB  1 
ATOM   850  N  N   . GLY A  1  116 ? 50.000  9.912   46.223 1.00 34.81  ? 129 GLY A N   1 
ATOM   851  C  CA  . GLY A  1  116 ? 48.624  10.342  46.374 1.00 36.20  ? 129 GLY A CA  1 
ATOM   852  C  C   . GLY A  1  116 ? 47.628  9.373   45.745 1.00 32.93  ? 129 GLY A C   1 
ATOM   853  O  O   . GLY A  1  116 ? 46.448  9.689   45.707 1.00 31.28  ? 129 GLY A O   1 
ATOM   854  N  N   . GLY A  1  117 ? 48.111  8.211   45.285 1.00 31.80  ? 130 GLY A N   1 
ATOM   855  C  CA  . GLY A  1  117 ? 47.259  7.091   44.920 1.00 31.19  ? 130 GLY A CA  1 
ATOM   856  C  C   . GLY A  1  117 ? 46.828  7.164   43.462 1.00 32.53  ? 130 GLY A C   1 
ATOM   857  O  O   . GLY A  1  117 ? 47.182  8.111   42.766 1.00 30.63  ? 130 GLY A O   1 
ATOM   858  N  N   . LEU A  1  118 ? 46.021  6.176   43.038 1.00 35.32  ? 131 LEU A N   1 
ATOM   859  C  CA  . LEU A  1  118 ? 45.659  5.989   41.640 1.00 33.25  ? 131 LEU A CA  1 
ATOM   860  C  C   . LEU A  1  118 ? 44.743  7.098   41.128 1.00 31.38  ? 131 LEU A C   1 
ATOM   861  O  O   . LEU A  1  118 ? 44.571  7.202   39.917 1.00 29.69  ? 131 LEU A O   1 
ATOM   862  C  CB  . LEU A  1  118 ? 45.006  4.624   41.465 1.00 34.71  ? 131 LEU A CB  1 
ATOM   863  C  CG  . LEU A  1  118 ? 45.874  3.405   41.791 1.00 35.53  ? 131 LEU A CG  1 
ATOM   864  C  CD1 . LEU A  1  118 ? 45.074  2.111   41.587 1.00 37.54  ? 131 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A  1  118 ? 47.155  3.376   40.977 1.00 35.10  ? 131 LEU A CD2 1 
ATOM   866  N  N   . ASN A  1  119 ? 44.182  7.922   42.025 1.00 29.17  ? 132 ASN A N   1 
ATOM   867  C  CA  . ASN A  1  119 ? 43.359  9.047   41.610 1.00 29.92  ? 132 ASN A CA  1 
ATOM   868  C  C   . ASN A  1  119 ? 44.153  10.123  40.882 1.00 31.18  ? 132 ASN A C   1 
ATOM   869  O  O   . ASN A  1  119 ? 43.566  10.904  40.156 1.00 32.34  ? 132 ASN A O   1 
ATOM   870  C  CB  . ASN A  1  119 ? 42.712  9.770   42.776 1.00 30.48  ? 132 ASN A CB  1 
ATOM   871  C  CG  . ASN A  1  119 ? 41.528  9.026   43.335 1.00 33.05  ? 132 ASN A CG  1 
ATOM   872  O  OD1 . ASN A  1  119 ? 41.171  7.948   42.860 1.00 31.08  ? 132 ASN A OD1 1 
ATOM   873  N  ND2 . ASN A  1  119 ? 40.913  9.591   44.357 1.00 36.53  ? 132 ASN A ND2 1 
ATOM   874  N  N   . VAL A  1  120 ? 45.470  10.181  41.085 1.00 35.14  ? 133 VAL A N   1 
ATOM   875  C  CA  . VAL A  1  120 ? 46.286  11.249  40.528 1.00 35.04  ? 133 VAL A CA  1 
ATOM   876  C  C   . VAL A  1  120 ? 46.216  11.229  39.001 1.00 35.25  ? 133 VAL A C   1 
ATOM   877  O  O   . VAL A  1  120 ? 46.557  10.233  38.366 1.00 32.72  ? 133 VAL A O   1 
ATOM   878  C  CB  . VAL A  1  120 ? 47.736  11.159  41.040 1.00 33.85  ? 133 VAL A CB  1 
ATOM   879  C  CG1 . VAL A  1  120 ? 48.671  12.109  40.291 1.00 32.69  ? 133 VAL A CG1 1 
ATOM   880  C  CG2 . VAL A  1  120 ? 47.799  11.393  42.551 1.00 32.23  ? 133 VAL A CG2 1 
ATOM   881  N  N   . HIS A  1  121 ? 45.802  12.375  38.439 1.00 39.62  ? 134 HIS A N   1 
ATOM   882  C  CA  . HIS A  1  121 ? 45.585  12.540  37.008 1.00 44.82  ? 134 HIS A CA  1 
ATOM   883  C  C   . HIS A  1  121 ? 46.896  12.894  36.314 1.00 41.61  ? 134 HIS A C   1 
ATOM   884  O  O   . HIS A  1  121 ? 47.731  13.554  36.915 1.00 42.91  ? 134 HIS A O   1 
ATOM   885  C  CB  . HIS A  1  121 ? 44.588  13.682  36.769 1.00 48.70  ? 134 HIS A CB  1 
ATOM   886  C  CG  . HIS A  1  121 ? 44.350  14.016  35.332 1.00 55.21  ? 134 HIS A CG  1 
ATOM   887  N  ND1 . HIS A  1  121 ? 43.691  13.161  34.472 1.00 59.22  ? 134 HIS A ND1 1 
ATOM   888  C  CD2 . HIS A  1  121 ? 44.695  15.087  34.597 1.00 52.66  ? 134 HIS A CD2 1 
ATOM   889  C  CE1 . HIS A  1  121 ? 43.633  13.711  33.265 1.00 53.82  ? 134 HIS A CE1 1 
ATOM   890  N  NE2 . HIS A  1  121 ? 44.224  14.887  33.324 1.00 50.13  ? 134 HIS A NE2 1 
ATOM   891  N  N   . GLY A  1  122 ? 47.065  12.482  35.051 1.00 38.73  ? 135 GLY A N   1 
ATOM   892  C  CA  . GLY A  1  122 ? 48.061  13.128  34.210 1.00 43.23  ? 135 GLY A CA  1 
ATOM   893  C  C   . GLY A  1  122 ? 49.120  12.202  33.617 1.00 44.90  ? 135 GLY A C   1 
ATOM   894  O  O   . GLY A  1  122 ? 49.510  12.433  32.481 1.00 44.62  ? 135 GLY A O   1 
ATOM   895  N  N   . THR A  1  123 ? 49.616  11.211  34.376 1.00 45.78  ? 136 THR A N   1 
ATOM   896  C  CA  A THR A  1  123 ? 50.673  10.331  33.899 0.50 43.77  ? 136 THR A CA  1 
ATOM   897  C  CA  B THR A  1  123 ? 50.670  10.330  33.889 0.50 47.79  ? 136 THR A CA  1 
ATOM   898  C  C   . THR A  1  123 ? 50.164  8.888   33.786 1.00 44.96  ? 136 THR A C   1 
ATOM   899  O  O   . THR A  1  123 ? 50.569  8.174   32.873 1.00 41.54  ? 136 THR A O   1 
ATOM   900  C  CB  A THR A  1  123 ? 51.898  10.443  34.815 0.50 43.25  ? 136 THR A CB  1 
ATOM   901  C  CB  B THR A  1  123 ? 51.924  10.437  34.764 0.50 53.07  ? 136 THR A CB  1 
ATOM   902  O  OG1 A THR A  1  123 ? 52.100  11.818  35.152 0.50 40.61  ? 136 THR A OG1 1 
ATOM   903  O  OG1 B THR A  1  123 ? 51.548  9.984   36.060 0.50 57.46  ? 136 THR A OG1 1 
ATOM   904  C  CG2 A THR A  1  123 ? 53.148  9.865   34.170 0.50 40.00  ? 136 THR A CG2 1 
ATOM   905  C  CG2 B THR A  1  123 ? 52.484  11.850  34.827 0.50 53.00  ? 136 THR A CG2 1 
ATOM   906  N  N   . PHE A  1  124 ? 49.307  8.441   34.730 1.00 44.10  ? 137 PHE A N   1 
ATOM   907  C  CA  . PHE A  1  124 ? 48.655  7.131   34.649 1.00 42.75  ? 137 PHE A CA  1 
ATOM   908  C  C   . PHE A  1  124 ? 47.162  7.312   34.330 1.00 42.64  ? 137 PHE A C   1 
ATOM   909  O  O   . PHE A  1  124 ? 46.761  7.093   33.188 1.00 47.87  ? 137 PHE A O   1 
ATOM   910  C  CB  . PHE A  1  124 ? 48.871  6.273   35.905 1.00 42.10  ? 137 PHE A CB  1 
ATOM   911  C  CG  . PHE A  1  124 ? 48.503  4.790   35.826 1.00 41.68  ? 137 PHE A CG  1 
ATOM   912  C  CD1 . PHE A  1  124 ? 47.813  4.246   34.744 1.00 39.42  ? 137 PHE A CD1 1 
ATOM   913  C  CD2 . PHE A  1  124 ? 48.843  3.921   36.867 1.00 42.43  ? 137 PHE A CD2 1 
ATOM   914  C  CE1 . PHE A  1  124 ? 47.503  2.893   34.696 1.00 36.01  ? 137 PHE A CE1 1 
ATOM   915  C  CE2 . PHE A  1  124 ? 48.518  2.566   36.813 1.00 37.48  ? 137 PHE A CE2 1 
ATOM   916  C  CZ  . PHE A  1  124 ? 47.854  2.061   35.728 1.00 36.82  ? 137 PHE A CZ  1 
ATOM   917  N  N   . GLU A  1  125 ? 46.330  7.662   35.330 1.00 39.71  ? 138 GLU A N   1 
ATOM   918  C  CA  . GLU A  1  125 ? 44.906  7.905   35.115 1.00 40.78  ? 138 GLU A CA  1 
ATOM   919  C  C   . GLU A  1  125 ? 44.736  8.983   34.042 1.00 38.69  ? 138 GLU A C   1 
ATOM   920  O  O   . GLU A  1  125 ? 45.492  9.944   33.999 1.00 42.51  ? 138 GLU A O   1 
ATOM   921  C  CB  . GLU A  1  125 ? 44.201  8.367   36.395 1.00 42.79  ? 138 GLU A CB  1 
ATOM   922  C  CG  . GLU A  1  125 ? 42.674  8.410   36.342 1.00 44.81  ? 138 GLU A CG  1 
ATOM   923  C  CD  . GLU A  1  125 ? 41.959  9.458   35.488 1.00 46.02  ? 138 GLU A CD  1 
ATOM   924  O  OE1 . GLU A  1  125 ? 42.405  10.632  35.575 1.00 37.85  ? 138 GLU A OE1 1 
ATOM   925  O  OE2 . GLU A  1  125 ? 40.962  9.103   34.762 1.00 40.78  ? 138 GLU A OE2 1 
ATOM   926  N  N   . GLY A  1  126 ? 43.739  8.809   33.174 1.00 38.75  ? 139 GLY A N   1 
ATOM   927  C  CA  . GLY A  1  126 ? 43.393  9.787   32.156 1.00 40.78  ? 139 GLY A CA  1 
ATOM   928  C  C   . GLY A  1  126 ? 41.952  9.652   31.649 1.00 43.55  ? 139 GLY A C   1 
ATOM   929  O  O   . GLY A  1  126 ? 41.076  9.061   32.308 1.00 52.23  ? 139 GLY A O   1 
ATOM   930  N  N   . ASP A  1  127 ? 41.766  10.164  30.421 1.00 41.90  ? 140 ASP A N   1 
ATOM   931  C  CA  . ASP A  1  127 ? 40.493  10.660  29.922 1.00 38.71  ? 140 ASP A CA  1 
ATOM   932  C  C   . ASP A  1  127 ? 39.816  9.591   29.058 1.00 35.94  ? 140 ASP A C   1 
ATOM   933  O  O   . ASP A  1  127 ? 40.440  8.602   28.676 1.00 36.12  ? 140 ASP A O   1 
ATOM   934  C  CB  . ASP A  1  127 ? 40.726  11.968  29.175 1.00 41.92  ? 140 ASP A CB  1 
ATOM   935  C  CG  . ASP A  1  127 ? 41.257  13.151  29.984 1.00 47.89  ? 140 ASP A CG  1 
ATOM   936  O  OD1 . ASP A  1  127 ? 41.017  13.206  31.209 1.00 50.66  ? 140 ASP A OD1 1 
ATOM   937  O  OD2 . ASP A  1  127 ? 41.935  14.019  29.388 1.00 51.92  ? 140 ASP A OD2 1 
ATOM   938  N  N   . ALA A  1  128 ? 38.528  9.808   28.753 1.00 33.30  ? 141 ALA A N   1 
ATOM   939  C  CA  . ALA A  1  128 ? 37.749  8.939   27.881 1.00 34.92  ? 141 ALA A CA  1 
ATOM   940  C  C   . ALA A  1  128 ? 37.488  7.571   28.521 1.00 36.01  ? 141 ALA A C   1 
ATOM   941  O  O   . ALA A  1  128 ? 37.403  6.561   27.828 1.00 38.42  ? 141 ALA A O   1 
ATOM   942  C  CB  . ALA A  1  128 ? 38.428  8.806   26.526 1.00 36.64  ? 141 ALA A CB  1 
ATOM   943  N  N   . GLY A  1  129 ? 37.316  7.542   29.847 1.00 35.65  ? 142 GLY A N   1 
ATOM   944  C  CA  . GLY A  1  129 ? 36.947  6.323   30.550 1.00 34.78  ? 142 GLY A CA  1 
ATOM   945  C  C   . GLY A  1  129 ? 35.533  5.893   30.191 1.00 36.02  ? 142 GLY A C   1 
ATOM   946  O  O   . GLY A  1  129 ? 34.809  6.670   29.588 1.00 40.29  ? 142 GLY A O   1 
ATOM   947  N  N   . MET A  1  130 ? 35.161  4.660   30.556 1.00 36.41  ? 143 MET A N   1 
ATOM   948  C  CA  . MET A  1  130 ? 33.859  4.087   30.244 1.00 35.60  ? 143 MET A CA  1 
ATOM   949  C  C   . MET A  1  130 ? 32.810  4.486   31.295 1.00 36.85  ? 143 MET A C   1 
ATOM   950  O  O   . MET A  1  130 ? 31.711  4.891   30.907 1.00 40.98  ? 143 MET A O   1 
ATOM   951  C  CB  . MET A  1  130 ? 33.923  2.553   30.211 1.00 37.30  ? 143 MET A CB  1 
ATOM   952  C  CG  . MET A  1  130 ? 34.594  1.912   29.005 1.00 37.75  ? 143 MET A CG  1 
ATOM   953  S  SD  . MET A  1  130 ? 34.676  0.102   29.164 1.00 40.38  ? 143 MET A SD  1 
ATOM   954  C  CE  . MET A  1  130 ? 35.744  -0.093  30.596 1.00 39.30  ? 143 MET A CE  1 
ATOM   955  N  N   . THR A  1  131 ? 33.127  4.356   32.603 1.00 34.99  ? 144 THR A N   1 
ATOM   956  C  CA  . THR A  1  131 ? 32.192  4.732   33.663 1.00 33.52  ? 144 THR A CA  1 
ATOM   957  C  C   . THR A  1  131 ? 32.721  5.840   34.574 1.00 32.56  ? 144 THR A C   1 
ATOM   958  O  O   . THR A  1  131 ? 32.081  6.104   35.588 1.00 34.61  ? 144 THR A O   1 
ATOM   959  C  CB  . THR A  1  131 ? 31.793  3.529   34.518 1.00 31.45  ? 144 THR A CB  1 
ATOM   960  O  OG1 . THR A  1  131 ? 32.897  3.184   35.344 1.00 29.52  ? 144 THR A OG1 1 
ATOM   961  C  CG2 . THR A  1  131 ? 31.388  2.327   33.691 1.00 31.49  ? 144 THR A CG2 1 
ATOM   962  N  N   . ARG A  1  132 ? 33.854  6.481   34.230 1.00 33.87  ? 145 ARG A N   1 
ATOM   963  C  CA  . ARG A  1  132 ? 34.367  7.630   34.971 1.00 33.47  ? 145 ARG A CA  1 
ATOM   964  C  C   . ARG A  1  132 ? 34.540  8.844   34.063 1.00 33.11  ? 145 ARG A C   1 
ATOM   965  O  O   . ARG A  1  132 ? 34.937  8.684   32.918 1.00 37.35  ? 145 ARG A O   1 
ATOM   966  C  CB  . ARG A  1  132 ? 35.686  7.292   35.670 1.00 37.59  ? 145 ARG A CB  1 
ATOM   967  C  CG  . ARG A  1  132 ? 35.520  6.691   37.064 1.00 40.28  ? 145 ARG A CG  1 
ATOM   968  C  CD  . ARG A  1  132 ? 35.210  5.199   37.067 1.00 42.07  ? 145 ARG A CD  1 
ATOM   969  N  NE  . ARG A  1  132 ? 35.068  4.719   38.446 1.00 45.22  ? 145 ARG A NE  1 
ATOM   970  C  CZ  . ARG A  1  132 ? 34.247  3.770   38.917 1.00 43.08  ? 145 ARG A CZ  1 
ATOM   971  N  NH1 . ARG A  1  132 ? 34.127  3.639   40.218 1.00 44.55  ? 145 ARG A NH1 1 
ATOM   972  N  NH2 . ARG A  1  132 ? 33.542  2.962   38.149 1.00 40.63  ? 145 ARG A NH2 1 
ATOM   973  N  N   . ALA A  1  133 ? 34.240  10.043  34.602 1.00 34.91  ? 146 ALA A N   1 
ATOM   974  C  CA  . ALA A  1  133 ? 34.272  11.306  33.876 1.00 31.64  ? 146 ALA A CA  1 
ATOM   975  C  C   . ALA A  1  133 ? 35.716  11.819  33.833 1.00 36.27  ? 146 ALA A C   1 
ATOM   976  O  O   . ALA A  1  133 ? 36.529  11.511  34.702 1.00 33.37  ? 146 ALA A O   1 
ATOM   977  N  N   . ASP A  1  134 ? 36.053  12.586  32.789 1.00 37.99  ? 147 ASP A N   1 
ATOM   978  C  CA  . ASP A  1  134 ? 37.351  13.233  32.698 1.00 36.55  ? 147 ASP A CA  1 
ATOM   979  C  C   . ASP A  1  134 ? 37.588  14.129  33.912 1.00 35.94  ? 147 ASP A C   1 
ATOM   980  O  O   . ASP A  1  134 ? 36.647  14.650  34.496 1.00 37.39  ? 147 ASP A O   1 
ATOM   981  C  CB  . ASP A  1  134 ? 37.488  14.014  31.403 1.00 37.49  ? 147 ASP A CB  1 
ATOM   982  C  CG  . ASP A  1  134 ? 37.470  13.187  30.131 1.00 39.63  ? 147 ASP A CG  1 
ATOM   983  O  OD1 . ASP A  1  134 ? 37.232  11.968  30.218 1.00 43.06  ? 147 ASP A OD1 1 
ATOM   984  O  OD2 . ASP A  1  134 ? 37.709  13.776  29.064 1.00 44.70  ? 147 ASP A OD2 1 
ATOM   985  N  N   . GLU A  1  135 ? 38.866  14.326  34.261 1.00 37.18  ? 148 GLU A N   1 
ATOM   986  C  CA  . GLU A  1  135 ? 39.256  15.051  35.459 1.00 43.19  ? 148 GLU A CA  1 
ATOM   987  C  C   . GLU A  1  135 ? 38.909  16.533  35.334 1.00 45.48  ? 148 GLU A C   1 
ATOM   988  O  O   . GLU A  1  135 ? 38.663  17.195  36.344 1.00 47.36  ? 148 GLU A O   1 
ATOM   989  C  CB  . GLU A  1  135 ? 40.750  14.872  35.728 1.00 48.45  ? 148 GLU A CB  1 
ATOM   990  C  CG  . GLU A  1  135 ? 41.234  15.483  37.042 1.00 53.80  ? 148 GLU A CG  1 
ATOM   991  C  CD  . GLU A  1  135 ? 41.800  16.901  36.979 1.00 62.76  ? 148 GLU A CD  1 
ATOM   992  O  OE1 . GLU A  1  135 ? 41.971  17.493  35.890 1.00 67.21  ? 148 GLU A OE1 1 
ATOM   993  O  OE2 . GLU A  1  135 ? 42.091  17.434  38.066 1.00 68.13  ? 148 GLU A OE2 1 
ATOM   994  N  N   . PHE A  1  136 ? 38.906  17.048  34.100 1.00 45.12  ? 149 PHE A N   1 
ATOM   995  C  CA  . PHE A  1  136 ? 38.567  18.438  33.851 1.00 46.60  ? 149 PHE A CA  1 
ATOM   996  C  C   . PHE A  1  136 ? 37.199  18.793  34.433 1.00 44.33  ? 149 PHE A C   1 
ATOM   997  O  O   . PHE A  1  136 ? 37.004  19.929  34.849 1.00 44.32  ? 149 PHE A O   1 
ATOM   998  C  CB  . PHE A  1  136 ? 38.573  18.723  32.350 1.00 53.82  ? 149 PHE A CB  1 
ATOM   999  C  CG  . PHE A  1  136 ? 38.122  20.137  32.018 1.00 58.90  ? 149 PHE A CG  1 
ATOM   1000 C  CD1 . PHE A  1  136 ? 38.948  21.222  32.308 1.00 60.30  ? 149 PHE A CD1 1 
ATOM   1001 C  CD2 . PHE A  1  136 ? 36.884  20.372  31.429 1.00 56.65  ? 149 PHE A CD2 1 
ATOM   1002 C  CE1 . PHE A  1  136 ? 38.546  22.510  32.012 1.00 56.61  ? 149 PHE A CE1 1 
ATOM   1003 C  CE2 . PHE A  1  136 ? 36.484  21.665  31.138 1.00 57.29  ? 149 PHE A CE2 1 
ATOM   1004 C  CZ  . PHE A  1  136 ? 37.315  22.729  31.430 1.00 57.59  ? 149 PHE A CZ  1 
ATOM   1005 N  N   . PHE A  1  137 ? 36.261  17.839  34.457 1.00 40.37  ? 150 PHE A N   1 
ATOM   1006 C  CA  . PHE A  1  137 ? 34.906  18.103  34.920 1.00 43.56  ? 150 PHE A CA  1 
ATOM   1007 C  C   . PHE A  1  137 ? 34.779  17.958  36.440 1.00 44.58  ? 150 PHE A C   1 
ATOM   1008 O  O   . PHE A  1  137 ? 33.701  18.157  36.979 1.00 45.40  ? 150 PHE A O   1 
ATOM   1009 C  CB  . PHE A  1  137 ? 33.922  17.160  34.225 1.00 44.47  ? 150 PHE A CB  1 
ATOM   1010 C  CG  . PHE A  1  137 ? 33.991  17.165  32.705 1.00 45.91  ? 150 PHE A CG  1 
ATOM   1011 C  CD1 . PHE A  1  137 ? 33.880  18.351  31.981 1.00 51.55  ? 150 PHE A CD1 1 
ATOM   1012 C  CD2 . PHE A  1  137 ? 34.205  15.983  32.002 1.00 45.71  ? 150 PHE A CD2 1 
ATOM   1013 C  CE1 . PHE A  1  137 ? 33.953  18.344  30.595 1.00 50.39  ? 150 PHE A CE1 1 
ATOM   1014 C  CE2 . PHE A  1  137 ? 34.284  15.981  30.618 1.00 48.08  ? 150 PHE A CE2 1 
ATOM   1015 C  CZ  . PHE A  1  137 ? 34.152  17.159  29.919 1.00 50.29  ? 150 PHE A CZ  1 
ATOM   1016 N  N   . GLY A  1  138 ? 35.857  17.591  37.137 1.00 45.59  ? 151 GLY A N   1 
ATOM   1017 C  CA  . GLY A  1  138 ? 35.927  17.770  38.577 1.00 46.11  ? 151 GLY A CA  1 
ATOM   1018 C  C   . GLY A  1  138 ? 35.951  16.468  39.383 1.00 49.57  ? 151 GLY A C   1 
ATOM   1019 O  O   . GLY A  1  138 ? 36.052  16.531  40.600 1.00 53.48  ? 151 GLY A O   1 
ATOM   1020 N  N   . ASP A  1  139 ? 35.835  15.300  38.736 1.00 53.23  ? 152 ASP A N   1 
ATOM   1021 C  CA  . ASP A  1  139 ? 35.834  14.032  39.454 1.00 48.02  ? 152 ASP A CA  1 
ATOM   1022 C  C   . ASP A  1  139 ? 36.182  12.877  38.511 1.00 43.47  ? 152 ASP A C   1 
ATOM   1023 O  O   . ASP A  1  139 ? 35.385  12.496  37.665 1.00 38.17  ? 152 ASP A O   1 
ATOM   1024 C  CB  . ASP A  1  139 ? 34.506  13.784  40.154 1.00 48.24  ? 152 ASP A CB  1 
ATOM   1025 C  CG  . ASP A  1  139 ? 34.432  12.503  40.978 1.00 57.01  ? 152 ASP A CG  1 
ATOM   1026 O  OD1 . ASP A  1  139 ? 35.318  11.639  40.795 1.00 66.03  ? 152 ASP A OD1 1 
ATOM   1027 O  OD2 . ASP A  1  139 ? 33.513  12.389  41.827 1.00 53.12  ? 152 ASP A OD2 1 
ATOM   1028 N  N   . ASN A  1  140 ? 37.352  12.270  38.735 1.00 42.59  ? 153 ASN A N   1 
ATOM   1029 C  CA  . ASN A  1  140 ? 37.900  11.260  37.839 1.00 41.26  ? 153 ASN A CA  1 
ATOM   1030 C  C   . ASN A  1  140 ? 37.795  9.850   38.437 1.00 41.97  ? 153 ASN A C   1 
ATOM   1031 O  O   . ASN A  1  140 ? 38.247  8.890   37.803 1.00 39.81  ? 153 ASN A O   1 
ATOM   1032 C  CB  . ASN A  1  140 ? 39.354  11.563  37.475 1.00 40.31  ? 153 ASN A CB  1 
ATOM   1033 C  CG  . ASN A  1  140 ? 40.281  11.500  38.674 1.00 40.54  ? 153 ASN A CG  1 
ATOM   1034 O  OD1 . ASN A  1  140 ? 39.837  11.555  39.828 1.00 42.46  ? 153 ASN A OD1 1 
ATOM   1035 N  ND2 . ASN A  1  140 ? 41.575  11.378  38.431 1.00 37.51  ? 153 ASN A ND2 1 
ATOM   1036 N  N   . HIS A  1  141 ? 37.216  9.720   39.644 1.00 39.99  ? 154 HIS A N   1 
ATOM   1037 C  CA  . HIS A  1  141 ? 37.232  8.449   40.361 1.00 39.67  ? 154 HIS A CA  1 
ATOM   1038 C  C   . HIS A  1  141 ? 35.830  7.856   40.561 1.00 38.32  ? 154 HIS A C   1 
ATOM   1039 O  O   . HIS A  1  141 ? 35.667  6.634   40.533 1.00 37.90  ? 154 HIS A O   1 
ATOM   1040 C  CB  . HIS A  1  141 ? 38.026  8.571   41.664 1.00 38.16  ? 154 HIS A CB  1 
ATOM   1041 C  CG  . HIS A  1  141 ? 37.544  9.638   42.572 1.00 40.51  ? 154 HIS A CG  1 
ATOM   1042 N  ND1 . HIS A  1  141 ? 37.981  10.943  42.477 1.00 44.12  ? 154 HIS A ND1 1 
ATOM   1043 C  CD2 . HIS A  1  141 ? 36.665  9.598   43.583 1.00 44.53  ? 154 HIS A CD2 1 
ATOM   1044 C  CE1 . HIS A  1  141 ? 37.366  11.677  43.392 1.00 47.82  ? 154 HIS A CE1 1 
ATOM   1045 N  NE2 . HIS A  1  141 ? 36.560  10.877  44.076 1.00 47.86  ? 154 HIS A NE2 1 
ATOM   1046 N  N   . SER A  1  142 ? 34.814  8.706   40.773 1.00 36.10  ? 155 SER A N   1 
ATOM   1047 C  CA  . SER A  1  142 ? 33.470  8.236   41.068 1.00 35.90  ? 155 SER A CA  1 
ATOM   1048 C  C   . SER A  1  142 ? 32.823  7.581   39.851 1.00 36.32  ? 155 SER A C   1 
ATOM   1049 O  O   . SER A  1  142 ? 33.018  8.010   38.716 1.00 33.13  ? 155 SER A O   1 
ATOM   1050 C  CB  . SER A  1  142 ? 32.612  9.354   41.549 1.00 38.13  ? 155 SER A CB  1 
ATOM   1051 O  OG  . SER A  1  142 ? 32.999  9.725   42.859 1.00 40.70  ? 155 SER A OG  1 
ATOM   1052 N  N   . PHE A  1  143 ? 31.998  6.564   40.122 1.00 36.84  ? 156 PHE A N   1 
ATOM   1053 C  CA  . PHE A  1  143 ? 31.061  6.046   39.139 1.00 36.51  ? 156 PHE A CA  1 
ATOM   1054 C  C   . PHE A  1  143 ? 30.128  7.160   38.657 1.00 35.32  ? 156 PHE A C   1 
ATOM   1055 O  O   . PHE A  1  143 ? 29.636  7.945   39.460 1.00 34.65  ? 156 PHE A O   1 
ATOM   1056 C  CB  . PHE A  1  143 ? 30.238  4.926   39.768 1.00 34.20  ? 156 PHE A CB  1 
ATOM   1057 C  CG  . PHE A  1  143 ? 29.174  4.366   38.840 1.00 34.07  ? 156 PHE A CG  1 
ATOM   1058 C  CD1 . PHE A  1  143 ? 29.499  3.401   37.892 1.00 35.23  ? 156 PHE A CD1 1 
ATOM   1059 C  CD2 . PHE A  1  143 ? 27.860  4.800   38.917 1.00 31.25  ? 156 PHE A CD2 1 
ATOM   1060 C  CE1 . PHE A  1  143 ? 28.530  2.870   37.051 1.00 33.51  ? 156 PHE A CE1 1 
ATOM   1061 C  CE2 . PHE A  1  143 ? 26.899  4.273   38.065 1.00 32.57  ? 156 PHE A CE2 1 
ATOM   1062 C  CZ  . PHE A  1  143 ? 27.228  3.298   37.147 1.00 31.61  ? 156 PHE A CZ  1 
ATOM   1063 N  N   . ASN A  1  144 ? 29.885  7.205   37.343 1.00 34.84  ? 157 ASN A N   1 
ATOM   1064 C  CA  . ASN A  1  144 ? 29.059  8.227   36.716 1.00 33.98  ? 157 ASN A CA  1 
ATOM   1065 C  C   . ASN A  1  144 ? 27.895  7.564   35.978 1.00 32.40  ? 157 ASN A C   1 
ATOM   1066 O  O   . ASN A  1  144 ? 28.112  6.837   35.010 1.00 30.94  ? 157 ASN A O   1 
ATOM   1067 C  CB  . ASN A  1  144 ? 29.933  9.067   35.799 1.00 36.96  ? 157 ASN A CB  1 
ATOM   1068 C  CG  . ASN A  1  144 ? 29.187  10.108  34.995 1.00 41.79  ? 157 ASN A CG  1 
ATOM   1069 O  OD1 . ASN A  1  144 ? 28.242  9.765   34.273 1.00 43.40  ? 157 ASN A OD1 1 
ATOM   1070 N  ND2 . ASN A  1  144 ? 29.611  11.368  35.088 1.00 44.37  ? 157 ASN A ND2 1 
ATOM   1071 N  N   . GLN A  1  145 ? 26.660  7.825   36.431 1.00 31.49  ? 158 GLN A N   1 
ATOM   1072 C  CA  . GLN A  1  145 ? 25.489  7.122   35.921 1.00 30.97  ? 158 GLN A CA  1 
ATOM   1073 C  C   . GLN A  1  145 ? 25.199  7.492   34.461 1.00 32.81  ? 158 GLN A C   1 
ATOM   1074 O  O   . GLN A  1  145 ? 24.752  6.647   33.686 1.00 32.84  ? 158 GLN A O   1 
ATOM   1075 C  CB  . GLN A  1  145 ? 24.290  7.381   36.827 1.00 27.93  ? 158 GLN A CB  1 
ATOM   1076 C  CG  . GLN A  1  145 ? 23.033  6.607   36.457 1.00 27.37  ? 158 GLN A CG  1 
ATOM   1077 C  CD  . GLN A  1  145 ? 23.194  5.107   36.564 1.00 28.98  ? 158 GLN A CD  1 
ATOM   1078 O  OE1 . GLN A  1  145 ? 23.586  4.553   37.594 1.00 29.85  ? 158 GLN A OE1 1 
ATOM   1079 N  NE2 . GLN A  1  145 ? 22.883  4.418   35.483 1.00 32.13  ? 158 GLN A NE2 1 
ATOM   1080 N  N   . THR A  1  146 ? 25.446  8.751   34.080 1.00 33.35  ? 159 THR A N   1 
ATOM   1081 C  CA  . THR A  1  146 ? 25.234  9.180   32.703 1.00 35.61  ? 159 THR A CA  1 
ATOM   1082 C  C   . THR A  1  146 ? 26.134  8.385   31.760 1.00 36.39  ? 159 THR A C   1 
ATOM   1083 O  O   . THR A  1  146 ? 25.724  8.066   30.655 1.00 36.63  ? 159 THR A O   1 
ATOM   1084 C  CB  . THR A  1  146 ? 25.525  10.672  32.534 1.00 38.15  ? 159 THR A CB  1 
ATOM   1085 O  OG1 . THR A  1  146 ? 24.689  11.381  33.436 1.00 42.15  ? 159 THR A OG1 1 
ATOM   1086 C  CG2 . THR A  1  146 ? 25.328  11.154  31.107 1.00 37.92  ? 159 THR A CG2 1 
ATOM   1087 N  N   . LEU A  1  147 ? 27.380  8.134   32.175 1.00 35.86  ? 160 LEU A N   1 
ATOM   1088 C  CA  . LEU A  1  147 ? 28.312  7.404   31.339 1.00 35.42  ? 160 LEU A CA  1 
ATOM   1089 C  C   . LEU A  1  147 ? 27.942  5.926   31.289 1.00 32.88  ? 160 LEU A C   1 
ATOM   1090 O  O   . LEU A  1  147 ? 28.095  5.294   30.251 1.00 31.65  ? 160 LEU A O   1 
ATOM   1091 C  CB  . LEU A  1  147 ? 29.736  7.627   31.843 1.00 37.02  ? 160 LEU A CB  1 
ATOM   1092 C  CG  . LEU A  1  147 ? 30.378  8.962   31.457 1.00 36.68  ? 160 LEU A CG  1 
ATOM   1093 C  CD1 . LEU A  1  147 ? 31.789  9.062   32.002 1.00 36.31  ? 160 LEU A CD1 1 
ATOM   1094 C  CD2 . LEU A  1  147 ? 30.388  9.175   29.957 1.00 39.59  ? 160 LEU A CD2 1 
ATOM   1095 N  N   . PHE A  1  148 ? 27.443  5.386   32.404 1.00 34.80  ? 161 PHE A N   1 
ATOM   1096 C  CA  . PHE A  1  148 ? 26.978  4.005   32.436 1.00 35.99  ? 161 PHE A CA  1 
ATOM   1097 C  C   . PHE A  1  148 ? 25.745  3.832   31.546 1.00 35.74  ? 161 PHE A C   1 
ATOM   1098 O  O   . PHE A  1  148 ? 25.530  2.759   30.991 1.00 29.67  ? 161 PHE A O   1 
ATOM   1099 C  CB  . PHE A  1  148 ? 26.647  3.520   33.851 1.00 33.82  ? 161 PHE A CB  1 
ATOM   1100 C  CG  . PHE A  1  148 ? 26.315  2.036   33.901 1.00 32.27  ? 161 PHE A CG  1 
ATOM   1101 C  CD1 . PHE A  1  148 ? 27.309  1.082   33.693 1.00 32.22  ? 161 PHE A CD1 1 
ATOM   1102 C  CD2 . PHE A  1  148 ? 25.012  1.597   34.119 1.00 29.55  ? 161 PHE A CD2 1 
ATOM   1103 C  CE1 . PHE A  1  148 ? 27.012  -0.277  33.698 1.00 32.70  ? 161 PHE A CE1 1 
ATOM   1104 C  CE2 . PHE A  1  148 ? 24.718  0.241   34.141 1.00 30.41  ? 161 PHE A CE2 1 
ATOM   1105 C  CZ  . PHE A  1  148 ? 25.722  -0.696  33.929 1.00 32.30  ? 161 PHE A CZ  1 
ATOM   1106 N  N   . ASP A  1  149 ? 24.928  4.883   31.430 1.00 38.79  ? 162 ASP A N   1 
ATOM   1107 C  CA  . ASP A  1  149 ? 23.754  4.860   30.572 1.00 38.28  ? 162 ASP A CA  1 
ATOM   1108 C  C   . ASP A  1  149 ? 24.190  4.710   29.120 1.00 39.14  ? 162 ASP A C   1 
ATOM   1109 O  O   . ASP A  1  149 ? 23.548  3.991   28.363 1.00 41.68  ? 162 ASP A O   1 
ATOM   1110 C  CB  . ASP A  1  149 ? 22.880  6.075   30.829 1.00 38.26  ? 162 ASP A CB  1 
ATOM   1111 C  CG  . ASP A  1  149 ? 22.122  6.055   32.147 1.00 41.09  ? 162 ASP A CG  1 
ATOM   1112 O  OD1 . ASP A  1  149 ? 21.845  4.924   32.635 1.00 40.08  ? 162 ASP A OD1 1 
ATOM   1113 O  OD2 . ASP A  1  149 ? 21.834  7.166   32.677 1.00 43.20  ? 162 ASP A OD2 1 
ATOM   1114 N  N   . LYS A  1  150 ? 25.301  5.365   28.756 1.00 37.63  ? 163 LYS A N   1 
ATOM   1115 C  CA  . LYS A  1  150 ? 25.862  5.259   27.415 1.00 37.97  ? 163 LYS A CA  1 
ATOM   1116 C  C   . LYS A  1  150 ? 26.431  3.859   27.170 1.00 34.67  ? 163 LYS A C   1 
ATOM   1117 O  O   . LYS A  1  150 ? 26.323  3.335   26.074 1.00 36.07  ? 163 LYS A O   1 
ATOM   1118 C  CB  . LYS A  1  150 ? 26.886  6.373   27.201 1.00 36.45  ? 163 LYS A CB  1 
ATOM   1119 C  CG  . LYS A  1  150 ? 27.504  6.424   25.829 1.00 37.21  ? 163 LYS A CG  1 
ATOM   1120 C  CD  . LYS A  1  150 ? 28.520  7.551   25.722 1.00 42.19  ? 163 LYS A CD  1 
ATOM   1121 C  CE  . LYS A  1  150 ? 29.337  7.513   24.458 1.00 46.80  ? 163 LYS A CE  1 
ATOM   1122 N  NZ  . LYS A  1  150 ? 29.045  8.650   23.587 1.00 45.27  ? 163 LYS A NZ  1 
ATOM   1123 N  N   . PHE A  1  151 ? 27.026  3.249   28.193 1.00 34.22  ? 164 PHE A N   1 
ATOM   1124 C  CA  . PHE A  1  151 ? 27.480  1.867   28.132 1.00 33.30  ? 164 PHE A CA  1 
ATOM   1125 C  C   . PHE A  1  151 ? 26.298  0.956   27.808 1.00 33.71  ? 164 PHE A C   1 
ATOM   1126 O  O   . PHE A  1  151 ? 26.412  0.066   26.967 1.00 34.87  ? 164 PHE A O   1 
ATOM   1127 C  CB  . PHE A  1  151 ? 28.165  1.542   29.470 1.00 33.61  ? 164 PHE A CB  1 
ATOM   1128 C  CG  . PHE A  1  151 ? 28.760  0.153   29.622 1.00 32.06  ? 164 PHE A CG  1 
ATOM   1129 C  CD1 . PHE A  1  151 ? 27.996  -0.904  30.099 1.00 33.12  ? 164 PHE A CD1 1 
ATOM   1130 C  CD2 . PHE A  1  151 ? 30.097  -0.081  29.327 1.00 34.56  ? 164 PHE A CD2 1 
ATOM   1131 C  CE1 . PHE A  1  151 ? 28.539  -2.179  30.216 1.00 34.57  ? 164 PHE A CE1 1 
ATOM   1132 C  CE2 . PHE A  1  151 ? 30.640  -1.354  29.456 1.00 35.80  ? 164 PHE A CE2 1 
ATOM   1133 C  CZ  . PHE A  1  151 ? 29.865  -2.397  29.912 1.00 34.21  ? 164 PHE A CZ  1 
ATOM   1134 N  N   . VAL A  1  152 ? 25.159  1.185   28.470 1.00 34.52  ? 165 VAL A N   1 
ATOM   1135 C  CA  . VAL A  1  152 ? 23.971  0.366   28.269 1.00 34.88  ? 165 VAL A CA  1 
ATOM   1136 C  C   . VAL A  1  152 ? 23.426  0.604   26.861 1.00 33.06  ? 165 VAL A C   1 
ATOM   1137 O  O   . VAL A  1  152 ? 23.077  -0.339  26.160 1.00 29.02  ? 165 VAL A O   1 
ATOM   1138 C  CB  . VAL A  1  152 ? 22.892  0.631   29.336 1.00 36.20  ? 165 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A  1  152 ? 21.630  -0.171  29.081 1.00 37.87  ? 165 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A  1  152 ? 23.388  0.320   30.737 1.00 36.43  ? 165 VAL A CG2 1 
ATOM   1141 N  N   . ASP A  1  153 ? 23.386  1.872   26.447 1.00 33.72  ? 166 ASP A N   1 
ATOM   1142 C  CA  . ASP A  1  153 ? 22.892  2.237   25.130 1.00 35.73  ? 166 ASP A CA  1 
ATOM   1143 C  C   . ASP A  1  153 ? 23.691  1.508   24.048 1.00 35.63  ? 166 ASP A C   1 
ATOM   1144 O  O   . ASP A  1  153 ? 23.096  0.876   23.171 1.00 30.64  ? 166 ASP A O   1 
ATOM   1145 C  CB  . ASP A  1  153 ? 22.836  3.750   24.962 1.00 40.17  ? 166 ASP A CB  1 
ATOM   1146 C  CG  . ASP A  1  153 ? 22.322  4.254   23.617 1.00 44.03  ? 166 ASP A CG  1 
ATOM   1147 O  OD1 . ASP A  1  153 ? 21.260  3.776   23.178 1.00 51.44  ? 166 ASP A OD1 1 
ATOM   1148 O  OD2 . ASP A  1  153 ? 22.991  5.116   23.007 1.00 42.20  ? 166 ASP A OD2 1 
ATOM   1149 N  N   . PHE A  1  154 ? 25.032  1.582   24.117 1.00 35.16  ? 167 PHE A N   1 
ATOM   1150 C  CA  . PHE A  1  154 ? 25.885  0.995   23.092 1.00 33.41  ? 167 PHE A CA  1 
ATOM   1151 C  C   . PHE A  1  154 ? 25.766  -0.524  23.124 1.00 31.01  ? 167 PHE A C   1 
ATOM   1152 O  O   . PHE A  1  154 ? 25.799  -1.159  22.082 1.00 29.66  ? 167 PHE A O   1 
ATOM   1153 C  CB  . PHE A  1  154 ? 27.334  1.468   23.224 1.00 35.31  ? 167 PHE A CB  1 
ATOM   1154 C  CG  . PHE A  1  154 ? 27.638  2.759   22.475 1.00 35.34  ? 167 PHE A CG  1 
ATOM   1155 C  CD1 . PHE A  1  154 ? 27.010  3.949   22.822 1.00 33.93  ? 167 PHE A CD1 1 
ATOM   1156 C  CD2 . PHE A  1  154 ? 28.530  2.773   21.412 1.00 36.56  ? 167 PHE A CD2 1 
ATOM   1157 C  CE1 . PHE A  1  154 ? 27.277  5.117   22.137 1.00 33.64  ? 167 PHE A CE1 1 
ATOM   1158 C  CE2 . PHE A  1  154 ? 28.804  3.948   20.737 1.00 35.62  ? 167 PHE A CE2 1 
ATOM   1159 C  CZ  . PHE A  1  154 ? 28.173  5.112   21.094 1.00 36.92  ? 167 PHE A CZ  1 
ATOM   1160 N  N   . SER A  1  155 ? 25.590  -1.104  24.311 1.00 31.67  ? 168 SER A N   1 
ATOM   1161 C  CA  . SER A  1  155 ? 25.363  -2.539  24.420 1.00 34.33  ? 168 SER A CA  1 
ATOM   1162 C  C   . SER A  1  155 ? 24.054  -2.941  23.731 1.00 37.30  ? 168 SER A C   1 
ATOM   1163 O  O   . SER A  1  155 ? 23.961  -4.013  23.133 1.00 35.99  ? 168 SER A O   1 
ATOM   1164 C  CB  . SER A  1  155 ? 25.370  -2.983  25.868 1.00 35.34  ? 168 SER A CB  1 
ATOM   1165 O  OG  . SER A  1  155 ? 26.607  -2.674  26.504 1.00 31.85  ? 168 SER A OG  1 
ATOM   1166 N  N   . ASN A  1  156 ? 23.032  -2.077  23.837 1.00 38.02  ? 169 ASN A N   1 
ATOM   1167 C  CA  . ASN A  1  156 ? 21.751  -2.304  23.200 1.00 36.22  ? 169 ASN A CA  1 
ATOM   1168 C  C   . ASN A  1  156 ? 21.899  -2.199  21.687 1.00 36.59  ? 169 ASN A C   1 
ATOM   1169 O  O   . ASN A  1  156 ? 21.348  -3.020  20.966 1.00 35.50  ? 169 ASN A O   1 
ATOM   1170 C  CB  . ASN A  1  156 ? 20.687  -1.343  23.722 1.00 38.41  ? 169 ASN A CB  1 
ATOM   1171 C  CG  . ASN A  1  156 ? 20.159  -1.731  25.083 1.00 39.02  ? 169 ASN A CG  1 
ATOM   1172 O  OD1 . ASN A  1  156 ? 20.150  -2.909  25.450 1.00 40.30  ? 169 ASN A OD1 1 
ATOM   1173 N  ND2 . ASN A  1  156 ? 19.648  -0.757  25.813 1.00 38.05  ? 169 ASN A ND2 1 
ATOM   1174 N  N   . ARG A  1  157 ? 22.672  -1.215  21.216 1.00 38.41  ? 170 ARG A N   1 
ATOM   1175 C  CA  . ARG A  1  157 ? 22.756  -0.919  19.795 1.00 35.71  ? 170 ARG A CA  1 
ATOM   1176 C  C   . ARG A  1  157 ? 23.651  -1.906  19.054 1.00 36.42  ? 170 ARG A C   1 
ATOM   1177 O  O   . ARG A  1  157 ? 23.425  -2.127  17.873 1.00 43.02  ? 170 ARG A O   1 
ATOM   1178 C  CB  . ARG A  1  157 ? 23.245  0.514   19.560 1.00 34.62  ? 170 ARG A CB  1 
ATOM   1179 C  CG  . ARG A  1  157 ? 22.464  1.517   20.394 1.00 36.90  ? 170 ARG A CG  1 
ATOM   1180 C  CD  . ARG A  1  157 ? 22.457  2.953   19.919 1.00 38.51  ? 170 ARG A CD  1 
ATOM   1181 N  NE  . ARG A  1  157 ? 23.641  3.376   19.166 1.00 42.32  ? 170 ARG A NE  1 
ATOM   1182 C  CZ  . ARG A  1  157 ? 24.279  4.525   19.321 1.00 45.15  ? 170 ARG A CZ  1 
ATOM   1183 N  NH1 . ARG A  1  157 ? 25.117  4.921   18.383 1.00 44.36  ? 170 ARG A NH1 1 
ATOM   1184 N  NH2 . ARG A  1  157 ? 24.033  5.310   20.359 1.00 44.43  ? 170 ARG A NH2 1 
ATOM   1185 N  N   . TYR A  1  158 ? 24.672  -2.484  19.706 1.00 38.38  ? 171 TYR A N   1 
ATOM   1186 C  CA  . TYR A  1  158 ? 25.671  -3.270  18.984 1.00 37.64  ? 171 TYR A CA  1 
ATOM   1187 C  C   . TYR A  1  158 ? 25.878  -4.676  19.550 1.00 37.58  ? 171 TYR A C   1 
ATOM   1188 O  O   . TYR A  1  158 ? 26.488  -5.509  18.870 1.00 36.05  ? 171 TYR A O   1 
ATOM   1189 C  CB  . TYR A  1  158 ? 27.015  -2.537  18.958 1.00 37.00  ? 171 TYR A CB  1 
ATOM   1190 C  CG  . TYR A  1  158 ? 26.915  -1.176  18.289 1.00 38.06  ? 171 TYR A CG  1 
ATOM   1191 C  CD1 . TYR A  1  158 ? 26.849  -1.067  16.904 1.00 38.27  ? 171 TYR A CD1 1 
ATOM   1192 C  CD2 . TYR A  1  158 ? 26.866  -0.004  19.039 1.00 40.33  ? 171 TYR A CD2 1 
ATOM   1193 C  CE1 . TYR A  1  158 ? 26.732  0.168   16.285 1.00 38.65  ? 171 TYR A CE1 1 
ATOM   1194 C  CE2 . TYR A  1  158 ? 26.765  1.243   18.433 1.00 41.43  ? 171 TYR A CE2 1 
ATOM   1195 C  CZ  . TYR A  1  158 ? 26.695  1.321   17.051 1.00 42.42  ? 171 TYR A CZ  1 
ATOM   1196 O  OH  . TYR A  1  158 ? 26.587  2.528   16.431 1.00 48.76  ? 171 TYR A OH  1 
ATOM   1197 N  N   . GLY A  1  159 ? 25.375  -4.959  20.766 1.00 35.74  ? 172 GLY A N   1 
ATOM   1198 C  CA  . GLY A  1  159 ? 25.682  -6.217  21.436 1.00 34.15  ? 172 GLY A CA  1 
ATOM   1199 C  C   . GLY A  1  159 ? 24.441  -6.993  21.875 1.00 35.75  ? 172 GLY A C   1 
ATOM   1200 O  O   . GLY A  1  159 ? 24.537  -7.898  22.704 1.00 33.99  ? 172 GLY A O   1 
ATOM   1201 N  N   . GLY A  1  160 ? 23.280  -6.656  21.305 1.00 37.35  ? 173 GLY A N   1 
ATOM   1202 C  CA  . GLY A  1  160 ? 22.049  -7.361  21.623 1.00 40.96  ? 173 GLY A CA  1 
ATOM   1203 C  C   . GLY A  1  160 ? 21.658  -7.208  23.094 1.00 42.24  ? 173 GLY A C   1 
ATOM   1204 O  O   . GLY A  1  160 ? 20.957  -8.060  23.632 1.00 40.10  ? 173 GLY A O   1 
ATOM   1205 N  N   . GLY A  1  161 ? 22.113  -6.118  23.733 1.00 41.49  ? 174 GLY A N   1 
ATOM   1206 C  CA  . GLY A  1  161 ? 21.815  -5.849  25.130 1.00 41.75  ? 174 GLY A CA  1 
ATOM   1207 C  C   . GLY A  1  161 ? 22.927  -6.308  26.073 1.00 42.24  ? 174 GLY A C   1 
ATOM   1208 O  O   . GLY A  1  161 ? 22.802  -6.160  27.288 1.00 39.81  ? 174 GLY A O   1 
ATOM   1209 N  N   . PHE A  1  162 ? 24.019  -6.840  25.501 1.00 43.27  ? 175 PHE A N   1 
ATOM   1210 C  CA  . PHE A  1  162 ? 25.184  -7.292  26.258 1.00 38.74  ? 175 PHE A CA  1 
ATOM   1211 C  C   . PHE A  1  162 ? 26.440  -6.563  25.782 1.00 34.61  ? 175 PHE A C   1 
ATOM   1212 O  O   . PHE A  1  162 ? 26.461  -5.998  24.699 1.00 34.04  ? 175 PHE A O   1 
ATOM   1213 C  CB  . PHE A  1  162 ? 25.348  -8.803  26.096 1.00 39.08  ? 175 PHE A CB  1 
ATOM   1214 C  CG  . PHE A  1  162 ? 24.178  -9.627  26.617 1.00 42.75  ? 175 PHE A CG  1 
ATOM   1215 C  CD1 . PHE A  1  162 ? 23.099  -9.941  25.797 1.00 40.70  ? 175 PHE A CD1 1 
ATOM   1216 C  CD2 . PHE A  1  162 ? 24.168  -10.087 27.932 1.00 43.74  ? 175 PHE A CD2 1 
ATOM   1217 C  CE1 . PHE A  1  162 ? 22.042  -10.696 26.280 1.00 43.48  ? 175 PHE A CE1 1 
ATOM   1218 C  CE2 . PHE A  1  162 ? 23.105  -10.838 28.413 1.00 43.59  ? 175 PHE A CE2 1 
ATOM   1219 C  CZ  . PHE A  1  162 ? 22.043  -11.142 27.585 1.00 45.79  ? 175 PHE A CZ  1 
ATOM   1220 N  N   . TYR A  1  163 ? 27.484  -6.564  26.610 1.00 34.30  ? 176 TYR A N   1 
ATOM   1221 C  CA  . TYR A  1  163 ? 28.759  -5.963  26.252 1.00 34.70  ? 176 TYR A CA  1 
ATOM   1222 C  C   . TYR A  1  163 ? 29.673  -7.039  25.674 1.00 33.60  ? 176 TYR A C   1 
ATOM   1223 O  O   . TYR A  1  163 ? 29.931  -8.047  26.330 1.00 35.62  ? 176 TYR A O   1 
ATOM   1224 C  CB  . TYR A  1  163 ? 29.382  -5.295  27.479 1.00 33.83  ? 176 TYR A CB  1 
ATOM   1225 C  CG  . TYR A  1  163 ? 30.617  -4.470  27.159 1.00 35.38  ? 176 TYR A CG  1 
ATOM   1226 C  CD1 . TYR A  1  163 ? 30.525  -3.198  26.616 1.00 34.53  ? 176 TYR A CD1 1 
ATOM   1227 C  CD2 . TYR A  1  163 ? 31.885  -4.963  27.419 1.00 37.67  ? 176 TYR A CD2 1 
ATOM   1228 C  CE1 . TYR A  1  163 ? 31.655  -2.450  26.325 1.00 34.16  ? 176 TYR A CE1 1 
ATOM   1229 C  CE2 . TYR A  1  163 ? 33.021  -4.225  27.133 1.00 35.79  ? 176 TYR A CE2 1 
ATOM   1230 C  CZ  . TYR A  1  163 ? 32.907  -2.967  26.583 1.00 32.98  ? 176 TYR A CZ  1 
ATOM   1231 O  OH  . TYR A  1  163 ? 34.035  -2.261  26.318 1.00 30.31  ? 176 TYR A OH  1 
ATOM   1232 N  N   . ASN A  1  164 ? 30.135  -6.812  24.437 1.00 33.74  ? 177 ASN A N   1 
ATOM   1233 C  CA  . ASN A  1  164 ? 31.017  -7.736  23.740 1.00 35.50  ? 177 ASN A CA  1 
ATOM   1234 C  C   . ASN A  1  164 ? 32.010  -6.925  22.910 1.00 35.67  ? 177 ASN A C   1 
ATOM   1235 O  O   . ASN A  1  164 ? 32.002  -5.698  22.956 1.00 36.28  ? 177 ASN A O   1 
ATOM   1236 C  CB  . ASN A  1  164 ? 30.213  -8.787  22.980 1.00 38.08  ? 177 ASN A CB  1 
ATOM   1237 C  CG  . ASN A  1  164 ? 29.611  -8.305  21.677 1.00 40.90  ? 177 ASN A CG  1 
ATOM   1238 O  OD1 . ASN A  1  164 ? 29.795  -7.141  21.270 1.00 36.13  ? 177 ASN A OD1 1 
ATOM   1239 N  ND2 . ASN A  1  164 ? 28.924  -9.224  21.009 1.00 42.32  ? 177 ASN A ND2 1 
ATOM   1240 N  N   . LEU A  1  165 ? 32.866  -7.607  22.137 1.00 38.08  ? 178 LEU A N   1 
ATOM   1241 C  CA  . LEU A  1  165 ? 33.989  -6.943  21.493 1.00 37.11  ? 178 LEU A CA  1 
ATOM   1242 C  C   . LEU A  1  165 ? 33.522  -5.884  20.489 1.00 35.72  ? 178 LEU A C   1 
ATOM   1243 O  O   . LEU A  1  165 ? 34.173  -4.850  20.366 1.00 36.38  ? 178 LEU A O   1 
ATOM   1244 C  CB  . LEU A  1  165 ? 34.867  -8.025  20.876 1.00 42.23  ? 178 LEU A CB  1 
ATOM   1245 C  CG  . LEU A  1  165 ? 36.156  -7.548  20.218 1.00 51.45  ? 178 LEU A CG  1 
ATOM   1246 C  CD1 . LEU A  1  165 ? 37.063  -6.922  21.226 1.00 51.40  ? 178 LEU A CD1 1 
ATOM   1247 C  CD2 . LEU A  1  165 ? 36.856  -8.661  19.478 1.00 55.64  ? 178 LEU A CD2 1 
ATOM   1248 N  N   . THR A  1  166 ? 32.399  -6.117  19.798 1.00 33.98  ? 179 THR A N   1 
ATOM   1249 C  CA  . THR A  1  166 ? 31.868  -5.147  18.854 1.00 34.25  ? 179 THR A CA  1 
ATOM   1250 C  C   . THR A  1  166 ? 31.520  -3.859  19.589 1.00 35.06  ? 179 THR A C   1 
ATOM   1251 O  O   . THR A  1  166 ? 31.871  -2.775  19.126 1.00 38.80  ? 179 THR A O   1 
ATOM   1252 C  CB  . THR A  1  166 ? 30.631  -5.706  18.142 1.00 37.79  ? 179 THR A CB  1 
ATOM   1253 O  OG1 . THR A  1  166 ? 30.871  -7.079  17.830 1.00 35.38  ? 179 THR A OG1 1 
ATOM   1254 C  CG2 . THR A  1  166 ? 30.291  -4.917  16.890 1.00 36.13  ? 179 THR A CG2 1 
ATOM   1255 N  N   . VAL A  1  167 ? 30.830  -3.995  20.731 1.00 34.62  ? 180 VAL A N   1 
ATOM   1256 C  CA  . VAL A  1  167 ? 30.407  -2.858  21.543 1.00 34.75  ? 180 VAL A CA  1 
ATOM   1257 C  C   . VAL A  1  167 ? 31.636  -2.064  21.981 1.00 38.33  ? 180 VAL A C   1 
ATOM   1258 O  O   . VAL A  1  167 ? 31.614  -0.832  22.001 1.00 39.84  ? 180 VAL A O   1 
ATOM   1259 C  CB  . VAL A  1  167 ? 29.602  -3.281  22.788 1.00 32.93  ? 180 VAL A CB  1 
ATOM   1260 C  CG1 . VAL A  1  167 ? 29.023  -2.083  23.528 1.00 31.04  ? 180 VAL A CG1 1 
ATOM   1261 C  CG2 . VAL A  1  167 ? 28.486  -4.260  22.446 1.00 34.07  ? 180 VAL A CG2 1 
ATOM   1262 N  N   . ALA A  1  168 ? 32.696  -2.784  22.370 1.00 36.94  ? 181 ALA A N   1 
ATOM   1263 C  CA  . ALA A  1  168 ? 33.897  -2.146  22.874 1.00 37.33  ? 181 ALA A CA  1 
ATOM   1264 C  C   . ALA A  1  168 ? 34.519  -1.244  21.799 1.00 38.69  ? 181 ALA A C   1 
ATOM   1265 O  O   . ALA A  1  168 ? 34.875  -0.095  22.075 1.00 36.23  ? 181 ALA A O   1 
ATOM   1266 C  CB  . ALA A  1  168 ? 34.852  -3.198  23.359 1.00 37.39  ? 181 ALA A CB  1 
ATOM   1267 N  N   . GLY A  1  169 ? 34.622  -1.754  20.563 1.00 37.49  ? 182 GLY A N   1 
ATOM   1268 C  CA  . GLY A  1  169 ? 35.155  -0.975  19.452 1.00 34.89  ? 182 GLY A CA  1 
ATOM   1269 C  C   . GLY A  1  169 ? 34.409  0.348   19.271 1.00 33.72  ? 182 GLY A C   1 
ATOM   1270 O  O   . GLY A  1  169 ? 35.021  1.415   19.148 1.00 35.80  ? 182 GLY A O   1 
ATOM   1271 N  N   . GLU A  1  170 ? 33.076  0.255   19.280 1.00 34.65  ? 183 GLU A N   1 
ATOM   1272 C  CA  . GLU A  1  170 ? 32.206  1.399   19.075 1.00 34.86  ? 183 GLU A CA  1 
ATOM   1273 C  C   . GLU A  1  170 ? 32.266  2.360   20.260 1.00 35.12  ? 183 GLU A C   1 
ATOM   1274 O  O   . GLU A  1  170 ? 32.341  3.570   20.059 1.00 34.66  ? 183 GLU A O   1 
ATOM   1275 C  CB  . GLU A  1  170 ? 30.765  0.939   18.840 1.00 38.11  ? 183 GLU A CB  1 
ATOM   1276 C  CG  . GLU A  1  170 ? 30.544  0.213   17.514 1.00 42.54  ? 183 GLU A CG  1 
ATOM   1277 C  CD  . GLU A  1  170 ? 31.067  0.969   16.303 1.00 46.38  ? 183 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A  1  170 ? 30.692  2.156   16.129 1.00 48.96  ? 183 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A  1  170 ? 31.876  0.362   15.562 1.00 51.06  ? 183 GLU A OE2 1 
ATOM   1280 N  N   . LEU A  1  171 ? 32.218  1.830   21.490 1.00 34.20  ? 184 LEU A N   1 
ATOM   1281 C  CA  . LEU A  1  171 ? 32.121  2.689   22.659 1.00 33.63  ? 184 LEU A CA  1 
ATOM   1282 C  C   . LEU A  1  171 ? 33.417  3.476   22.851 1.00 35.58  ? 184 LEU A C   1 
ATOM   1283 O  O   . LEU A  1  171 ? 33.378  4.658   23.196 1.00 32.92  ? 184 LEU A O   1 
ATOM   1284 C  CB  . LEU A  1  171 ? 31.778  1.875   23.900 1.00 33.65  ? 184 LEU A CB  1 
ATOM   1285 C  CG  . LEU A  1  171 ? 31.655  2.672   25.205 1.00 35.75  ? 184 LEU A CG  1 
ATOM   1286 C  CD1 . LEU A  1  171 ? 30.577  3.736   25.153 1.00 36.26  ? 184 LEU A CD1 1 
ATOM   1287 C  CD2 . LEU A  1  171 ? 31.384  1.715   26.357 1.00 36.10  ? 184 LEU A CD2 1 
ATOM   1288 N  N   . ARG A  1  172 ? 34.563  2.817   22.631 1.00 38.63  ? 185 ARG A N   1 
ATOM   1289 C  CA  . ARG A  1  172 ? 35.862  3.450   22.828 1.00 40.28  ? 185 ARG A CA  1 
ATOM   1290 C  C   . ARG A  1  172 ? 35.972  4.697   21.948 1.00 40.61  ? 185 ARG A C   1 
ATOM   1291 O  O   . ARG A  1  172 ? 36.344  5.771   22.429 1.00 40.08  ? 185 ARG A O   1 
ATOM   1292 C  CB  . ARG A  1  172 ? 36.961  2.400   22.598 1.00 40.32  ? 185 ARG A CB  1 
ATOM   1293 C  CG  . ARG A  1  172 ? 38.384  2.866   22.317 1.00 40.68  ? 185 ARG A CG  1 
ATOM   1294 C  CD  . ARG A  1  172 ? 38.955  3.868   23.302 1.00 42.91  ? 185 ARG A CD  1 
ATOM   1295 N  NE  . ARG A  1  172 ? 38.859  3.435   24.702 1.00 43.24  ? 185 ARG A NE  1 
ATOM   1296 C  CZ  . ARG A  1  172 ? 38.420  4.174   25.708 1.00 43.07  ? 185 ARG A CZ  1 
ATOM   1297 N  NH1 . ARG A  1  172 ? 37.993  5.408   25.501 1.00 46.27  ? 185 ARG A NH1 1 
ATOM   1298 N  NH2 . ARG A  1  172 ? 38.409  3.672   26.923 1.00 42.77  ? 185 ARG A NH2 1 
ATOM   1299 N  N   . TYR A  1  173 ? 35.636  4.541   20.660 1.00 41.44  ? 186 TYR A N   1 
ATOM   1300 C  CA  . TYR A  1  173 ? 35.708  5.633   19.699 1.00 44.34  ? 186 TYR A CA  1 
ATOM   1301 C  C   . TYR A  1  173 ? 34.786  6.769   20.138 1.00 41.69  ? 186 TYR A C   1 
ATOM   1302 O  O   . TYR A  1  173 ? 35.189  7.930   20.164 1.00 44.71  ? 186 TYR A O   1 
ATOM   1303 C  CB  . TYR A  1  173 ? 35.359  5.121   18.297 1.00 47.71  ? 186 TYR A CB  1 
ATOM   1304 C  CG  . TYR A  1  173 ? 35.456  6.190   17.215 1.00 48.95  ? 186 TYR A CG  1 
ATOM   1305 C  CD1 . TYR A  1  173 ? 36.688  6.719   16.853 1.00 48.07  ? 186 TYR A CD1 1 
ATOM   1306 C  CD2 . TYR A  1  173 ? 34.329  6.660   16.548 1.00 51.55  ? 186 TYR A CD2 1 
ATOM   1307 C  CE1 . TYR A  1  173 ? 36.799  7.693   15.879 1.00 47.52  ? 186 TYR A CE1 1 
ATOM   1308 C  CE2 . TYR A  1  173 ? 34.425  7.638   15.571 1.00 51.52  ? 186 TYR A CE2 1 
ATOM   1309 C  CZ  . TYR A  1  173 ? 35.664  8.156   15.239 1.00 51.38  ? 186 TYR A CZ  1 
ATOM   1310 O  OH  . TYR A  1  173 ? 35.790  9.123   14.284 1.00 50.87  ? 186 TYR A OH  1 
ATOM   1311 N  N   . SER A  1  174 ? 33.552  6.419   20.510 1.00 38.02  ? 187 SER A N   1 
ATOM   1312 C  CA  . SER A  1  174 ? 32.550  7.416   20.822 1.00 36.96  ? 187 SER A CA  1 
ATOM   1313 C  C   . SER A  1  174 ? 32.960  8.226   22.052 1.00 36.27  ? 187 SER A C   1 
ATOM   1314 O  O   . SER A  1  174 ? 32.774  9.443   22.069 1.00 37.95  ? 187 SER A O   1 
ATOM   1315 C  CB  . SER A  1  174 ? 31.205  6.779   20.965 1.00 38.27  ? 187 SER A CB  1 
ATOM   1316 O  OG  . SER A  1  174 ? 30.212  7.751   21.252 1.00 40.92  ? 187 SER A OG  1 
ATOM   1317 N  N   . ARG A  1  175 ? 33.563  7.571   23.053 1.00 34.86  ? 188 ARG A N   1 
ATOM   1318 C  CA  . ARG A  1  175 ? 34.027  8.274   24.248 1.00 33.61  ? 188 ARG A CA  1 
ATOM   1319 C  C   . ARG A  1  175 ? 35.174  9.225   23.916 1.00 33.38  ? 188 ARG A C   1 
ATOM   1320 O  O   . ARG A  1  175 ? 35.291  10.288  24.526 1.00 31.09  ? 188 ARG A O   1 
ATOM   1321 C  CB  . ARG A  1  175 ? 34.457  7.325   25.372 1.00 32.84  ? 188 ARG A CB  1 
ATOM   1322 C  CG  . ARG A  1  175 ? 33.305  6.539   25.976 1.00 34.08  ? 188 ARG A CG  1 
ATOM   1323 C  CD  . ARG A  1  175 ? 32.341  7.406   26.765 1.00 33.23  ? 188 ARG A CD  1 
ATOM   1324 N  NE  . ARG A  1  175 ? 33.053  7.939   27.924 1.00 31.79  ? 188 ARG A NE  1 
ATOM   1325 C  CZ  . ARG A  1  175 ? 33.352  9.202   28.186 1.00 33.86  ? 188 ARG A CZ  1 
ATOM   1326 N  NH1 . ARG A  1  175 ? 32.884  10.172  27.433 1.00 35.30  ? 188 ARG A NH1 1 
ATOM   1327 N  NH2 . ARG A  1  175 ? 34.110  9.506   29.234 1.00 31.09  ? 188 ARG A NH2 1 
ATOM   1328 N  N   . ILE A  1  176 ? 36.024  8.838   22.953 1.00 33.39  ? 189 ILE A N   1 
ATOM   1329 C  CA  . ILE A  1  176 ? 37.075  9.729   22.505 1.00 33.62  ? 189 ILE A CA  1 
ATOM   1330 C  C   . ILE A  1  176 ? 36.444  10.995  21.920 1.00 34.57  ? 189 ILE A C   1 
ATOM   1331 O  O   . ILE A  1  176 ? 36.821  12.101  22.308 1.00 35.13  ? 189 ILE A O   1 
ATOM   1332 C  CB  . ILE A  1  176 ? 38.010  9.004   21.526 1.00 36.10  ? 189 ILE A CB  1 
ATOM   1333 C  CG1 . ILE A  1  176 ? 38.862  7.981   22.267 1.00 36.75  ? 189 ILE A CG1 1 
ATOM   1334 C  CG2 . ILE A  1  176 ? 38.873  9.996   20.744 1.00 39.31  ? 189 ILE A CG2 1 
ATOM   1335 C  CD1 . ILE A  1  176 ? 39.602  7.021   21.360 1.00 36.59  ? 189 ILE A CD1 1 
ATOM   1336 N  N   . GLN A  1  177 ? 35.453  10.819  21.032 1.00 35.06  ? 190 GLN A N   1 
ATOM   1337 C  CA  . GLN A  1  177 ? 34.723  11.932  20.444 1.00 39.31  ? 190 GLN A CA  1 
ATOM   1338 C  C   . GLN A  1  177 ? 34.078  12.824  21.510 1.00 37.99  ? 190 GLN A C   1 
ATOM   1339 O  O   . GLN A  1  177 ? 34.178  14.042  21.415 1.00 36.80  ? 190 GLN A O   1 
ATOM   1340 C  CB  . GLN A  1  177 ? 33.686  11.443  19.429 1.00 44.05  ? 190 GLN A CB  1 
ATOM   1341 C  CG  . GLN A  1  177 ? 34.280  10.714  18.228 1.00 48.71  ? 190 GLN A CG  1 
ATOM   1342 C  CD  . GLN A  1  177 ? 35.346  11.521  17.517 1.00 57.75  ? 190 GLN A CD  1 
ATOM   1343 O  OE1 . GLN A  1  177 ? 35.348  12.760  17.524 1.00 62.28  ? 190 GLN A OE1 1 
ATOM   1344 N  NE2 . GLN A  1  177 ? 36.264  10.814  16.873 1.00 61.93  ? 190 GLN A NE2 1 
ATOM   1345 N  N   . ASP A  1  178 ? 33.429  12.234  22.523 1.00 39.02  ? 191 ASP A N   1 
ATOM   1346 C  CA  . ASP A  1  178 ? 32.842  13.003  23.617 1.00 41.35  ? 191 ASP A CA  1 
ATOM   1347 C  C   . ASP A  1  178 ? 33.862  13.944  24.248 1.00 41.29  ? 191 ASP A C   1 
ATOM   1348 O  O   . ASP A  1  178 ? 33.549  15.096  24.545 1.00 40.49  ? 191 ASP A O   1 
ATOM   1349 C  CB  . ASP A  1  178 ? 32.311  12.113  24.730 1.00 44.65  ? 191 ASP A CB  1 
ATOM   1350 C  CG  . ASP A  1  178 ? 31.064  11.300  24.412 1.00 50.02  ? 191 ASP A CG  1 
ATOM   1351 O  OD1 . ASP A  1  178 ? 30.423  11.593  23.384 1.00 54.72  ? 191 ASP A OD1 1 
ATOM   1352 O  OD2 . ASP A  1  178 ? 30.742  10.381  25.201 1.00 49.42  ? 191 ASP A OD2 1 
ATOM   1353 N  N   . SER A  1  179 ? 35.080  13.438  24.473 1.00 43.98  ? 192 SER A N   1 
ATOM   1354 C  CA  . SER A  1  179 ? 36.096  14.209  25.171 1.00 46.79  ? 192 SER A CA  1 
ATOM   1355 C  C   . SER A  1  179 ? 36.682  15.297  24.263 1.00 42.61  ? 192 SER A C   1 
ATOM   1356 O  O   . SER A  1  179 ? 36.979  16.393  24.741 1.00 39.14  ? 192 SER A O   1 
ATOM   1357 C  CB  . SER A  1  179 ? 37.155  13.295  25.764 1.00 50.86  ? 192 SER A CB  1 
ATOM   1358 O  OG  . SER A  1  179 ? 36.676  12.668  26.952 1.00 48.14  ? 192 SER A OG  1 
ATOM   1359 N  N   . ILE A  1  180 ? 36.837  15.001  22.962 1.00 42.18  ? 193 ILE A N   1 
ATOM   1360 C  CA  . ILE A  1  180 ? 37.315  15.988  21.998 1.00 46.07  ? 193 ILE A CA  1 
ATOM   1361 C  C   . ILE A  1  180 ? 36.381  17.197  22.010 1.00 46.49  ? 193 ILE A C   1 
ATOM   1362 O  O   . ILE A  1  180 ? 36.834  18.344  22.019 1.00 48.52  ? 193 ILE A O   1 
ATOM   1363 C  CB  . ILE A  1  180 ? 37.451  15.387  20.582 1.00 44.49  ? 193 ILE A CB  1 
ATOM   1364 C  CG1 . ILE A  1  180 ? 38.609  14.392  20.503 1.00 44.27  ? 193 ILE A CG1 1 
ATOM   1365 C  CG2 . ILE A  1  180 ? 37.605  16.497  19.542 1.00 43.02  ? 193 ILE A CG2 1 
ATOM   1366 C  CD1 . ILE A  1  180 ? 38.756  13.700  19.162 1.00 43.29  ? 193 ILE A CD1 1 
ATOM   1367 N  N   . ALA A  1  181 ? 35.076  16.915  22.033 1.00 48.93  ? 194 ALA A N   1 
ATOM   1368 C  CA  . ALA A  1  181 ? 34.047  17.931  21.861 1.00 48.25  ? 194 ALA A CA  1 
ATOM   1369 C  C   . ALA A  1  181 ? 33.795  18.734  23.135 1.00 44.38  ? 194 ALA A C   1 
ATOM   1370 O  O   . ALA A  1  181 ? 33.232  19.820  23.039 1.00 48.61  ? 194 ALA A O   1 
ATOM   1371 C  CB  . ALA A  1  181 ? 32.759  17.282  21.402 1.00 48.21  ? 194 ALA A CB  1 
ATOM   1372 N  N   . THR A  1  182 ? 34.159  18.216  24.314 1.00 37.30  ? 195 THR A N   1 
ATOM   1373 C  CA  . THR A  1  182 ? 33.679  18.847  25.536 1.00 40.06  ? 195 THR A CA  1 
ATOM   1374 C  C   . THR A  1  182 ? 34.804  19.170  26.520 1.00 39.80  ? 195 THR A C   1 
ATOM   1375 O  O   . THR A  1  182 ? 34.568  19.893  27.479 1.00 38.34  ? 195 THR A O   1 
ATOM   1376 C  CB  . THR A  1  182 ? 32.606  17.973  26.196 1.00 43.72  ? 195 THR A CB  1 
ATOM   1377 O  OG1 . THR A  1  182 ? 33.212  16.762  26.646 1.00 47.59  ? 195 THR A OG1 1 
ATOM   1378 C  CG2 . THR A  1  182 ? 31.445  17.637  25.276 1.00 41.05  ? 195 THR A CG2 1 
ATOM   1379 N  N   . ASN A  1  183 ? 36.011  18.635  26.314 1.00 42.38  ? 196 ASN A N   1 
ATOM   1380 C  CA  . ASN A  1  183 ? 37.091  18.790  27.277 1.00 42.15  ? 196 ASN A CA  1 
ATOM   1381 C  C   . ASN A  1  183 ? 38.269  19.474  26.591 1.00 43.79  ? 196 ASN A C   1 
ATOM   1382 O  O   . ASN A  1  183 ? 38.982  18.864  25.799 1.00 42.19  ? 196 ASN A O   1 
ATOM   1383 C  CB  . ASN A  1  183 ? 37.512  17.451  27.876 1.00 43.17  ? 196 ASN A CB  1 
ATOM   1384 C  CG  . ASN A  1  183 ? 38.647  17.559  28.874 1.00 43.16  ? 196 ASN A CG  1 
ATOM   1385 O  OD1 . ASN A  1  183 ? 39.123  18.663  29.168 1.00 39.28  ? 196 ASN A OD1 1 
ATOM   1386 N  ND2 . ASN A  1  183 ? 39.091  16.428  29.409 1.00 42.25  ? 196 ASN A ND2 1 
ATOM   1387 N  N   . PRO A  1  184 ? 38.522  20.764  26.878 1.00 44.43  ? 197 PRO A N   1 
ATOM   1388 C  CA  . PRO A  1  184 ? 39.635  21.474  26.250 1.00 46.78  ? 197 PRO A CA  1 
ATOM   1389 C  C   . PRO A  1  184 ? 41.026  20.987  26.657 1.00 49.28  ? 197 PRO A C   1 
ATOM   1390 O  O   . PRO A  1  184 ? 41.987  21.232  25.928 1.00 58.69  ? 197 PRO A O   1 
ATOM   1391 C  CB  . PRO A  1  184 ? 39.385  22.924  26.680 1.00 46.60  ? 197 PRO A CB  1 
ATOM   1392 C  CG  . PRO A  1  184 ? 38.684  22.791  28.002 1.00 45.32  ? 197 PRO A CG  1 
ATOM   1393 C  CD  . PRO A  1  184 ? 37.769  21.594  27.825 1.00 45.80  ? 197 PRO A CD  1 
ATOM   1394 N  N   . GLU A  1  185 ? 41.125  20.291  27.802 1.00 49.31  ? 198 GLU A N   1 
ATOM   1395 C  CA  . GLU A  1  185 ? 42.395  19.779  28.306 1.00 48.23  ? 198 GLU A CA  1 
ATOM   1396 C  C   . GLU A  1  185 ? 42.591  18.307  27.931 1.00 44.99  ? 198 GLU A C   1 
ATOM   1397 O  O   . GLU A  1  185 ? 43.507  17.666  28.432 1.00 44.29  ? 198 GLU A O   1 
ATOM   1398 C  CB  . GLU A  1  185 ? 42.484  19.953  29.823 1.00 49.92  ? 198 GLU A CB  1 
ATOM   1399 C  CG  . GLU A  1  185 ? 42.742  21.387  30.285 1.00 52.21  ? 198 GLU A CG  1 
ATOM   1400 C  CD  . GLU A  1  185 ? 42.606  21.580  31.789 1.00 55.90  ? 198 GLU A CD  1 
ATOM   1401 O  OE1 . GLU A  1  185 ? 42.407  20.562  32.490 1.00 56.65  ? 198 GLU A OE1 1 
ATOM   1402 O  OE2 . GLU A  1  185 ? 42.678  22.736  32.268 1.00 59.69  ? 198 GLU A OE2 1 
ATOM   1403 N  N   . PHE A  1  186 ? 41.758  17.785  27.020 1.00 41.45  ? 199 PHE A N   1 
ATOM   1404 C  CA  . PHE A  1  186 ? 41.761  16.369  26.690 1.00 39.51  ? 199 PHE A CA  1 
ATOM   1405 C  C   . PHE A  1  186 ? 43.126  15.935  26.167 1.00 38.96  ? 199 PHE A C   1 
ATOM   1406 O  O   . PHE A  1  186 ? 43.590  16.449  25.157 1.00 39.55  ? 199 PHE A O   1 
ATOM   1407 C  CB  . PHE A  1  186 ? 40.699  16.058  25.636 1.00 39.82  ? 199 PHE A CB  1 
ATOM   1408 C  CG  . PHE A  1  186 ? 40.656  14.618  25.140 1.00 38.56  ? 199 PHE A CG  1 
ATOM   1409 C  CD1 . PHE A  1  186 ? 40.634  13.550  26.027 1.00 40.63  ? 199 PHE A CD1 1 
ATOM   1410 C  CD2 . PHE A  1  186 ? 40.625  14.335  23.782 1.00 40.11  ? 199 PHE A CD2 1 
ATOM   1411 C  CE1 . PHE A  1  186 ? 40.579  12.238  25.568 1.00 39.08  ? 199 PHE A CE1 1 
ATOM   1412 C  CE2 . PHE A  1  186 ? 40.574  13.024  23.331 1.00 40.47  ? 199 PHE A CE2 1 
ATOM   1413 C  CZ  . PHE A  1  186 ? 40.561  11.977  24.224 1.00 38.53  ? 199 PHE A CZ  1 
ATOM   1414 N  N   . GLN A  1  187 ? 43.722  14.965  26.872 1.00 41.17  ? 200 GLN A N   1 
ATOM   1415 C  CA  . GLN A  1  187 ? 44.960  14.306  26.491 1.00 41.96  ? 200 GLN A CA  1 
ATOM   1416 C  C   . GLN A  1  187 ? 44.682  12.827  26.234 1.00 42.46  ? 200 GLN A C   1 
ATOM   1417 O  O   . GLN A  1  187 ? 43.919  12.210  26.972 1.00 47.37  ? 200 GLN A O   1 
ATOM   1418 C  CB  . GLN A  1  187 ? 45.971  14.467  27.628 1.00 42.73  ? 200 GLN A CB  1 
ATOM   1419 C  CG  . GLN A  1  187 ? 46.488  15.891  27.813 1.00 45.57  ? 200 GLN A CG  1 
ATOM   1420 C  CD  . GLN A  1  187 ? 47.354  16.343  26.655 1.00 50.72  ? 200 GLN A CD  1 
ATOM   1421 O  OE1 . GLN A  1  187 ? 48.518  15.942  26.554 1.00 54.44  ? 200 GLN A OE1 1 
ATOM   1422 N  NE2 . GLN A  1  187 ? 46.801  17.156  25.759 1.00 50.23  ? 200 GLN A NE2 1 
ATOM   1423 N  N   . PHE A  1  188 ? 45.307  12.258  25.198 1.00 38.86  ? 201 PHE A N   1 
ATOM   1424 C  CA  . PHE A  1  188 ? 45.148  10.843  24.900 1.00 39.44  ? 201 PHE A CA  1 
ATOM   1425 C  C   . PHE A  1  188 ? 46.451  10.303  24.320 1.00 41.95  ? 201 PHE A C   1 
ATOM   1426 O  O   . PHE A  1  188 ? 46.500  9.886   23.167 1.00 39.61  ? 201 PHE A O   1 
ATOM   1427 C  CB  . PHE A  1  188 ? 43.953  10.668  23.958 1.00 38.55  ? 201 PHE A CB  1 
ATOM   1428 C  CG  . PHE A  1  188 ? 43.346  9.275   23.971 1.00 35.73  ? 201 PHE A CG  1 
ATOM   1429 C  CD1 . PHE A  1  188 ? 42.676  8.816   25.093 1.00 39.89  ? 201 PHE A CD1 1 
ATOM   1430 C  CD2 . PHE A  1  188 ? 43.391  8.457   22.855 1.00 34.25  ? 201 PHE A CD2 1 
ATOM   1431 C  CE1 . PHE A  1  188 ? 42.115  7.548   25.116 1.00 38.87  ? 201 PHE A CE1 1 
ATOM   1432 C  CE2 . PHE A  1  188 ? 42.829  7.189   22.882 1.00 35.01  ? 201 PHE A CE2 1 
ATOM   1433 C  CZ  . PHE A  1  188 ? 42.183  6.742   24.006 1.00 36.60  ? 201 PHE A CZ  1 
ATOM   1434 N  N   . LYS A  1  189 ? 47.507  10.321  25.138 1.00 45.90  ? 202 LYS A N   1 
ATOM   1435 C  CA  . LYS A  1  189 ? 48.826  9.919   24.685 1.00 46.38  ? 202 LYS A CA  1 
ATOM   1436 C  C   . LYS A  1  189 ? 49.551  9.098   25.756 1.00 47.90  ? 202 LYS A C   1 
ATOM   1437 O  O   . LYS A  1  189 ? 49.135  9.037   26.908 1.00 52.43  ? 202 LYS A O   1 
ATOM   1438 C  CB  . LYS A  1  189 ? 49.613  11.175  24.304 1.00 47.55  ? 202 LYS A CB  1 
ATOM   1439 C  CG  . LYS A  1  189 ? 49.802  12.210  25.408 1.00 52.40  ? 202 LYS A CG  1 
ATOM   1440 C  CD  . LYS A  1  189 ? 50.490  13.502  24.961 1.00 56.81  ? 202 LYS A CD  1 
ATOM   1441 C  CE  . LYS A  1  189 ? 49.740  14.195  23.860 1.00 69.04  ? 202 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A  1  189 ? 50.272  15.499  23.450 1.00 70.20  ? 202 LYS A NZ  1 
ATOM   1443 N  N   . ASN A  1  190 ? 50.640  8.445   25.332 1.00 44.99  ? 203 ASN A N   1 
ATOM   1444 C  CA  . ASN A  1  190 ? 51.563  7.773   26.229 1.00 42.89  ? 203 ASN A CA  1 
ATOM   1445 C  C   . ASN A  1  190 ? 50.835  6.673   26.998 1.00 40.76  ? 203 ASN A C   1 
ATOM   1446 O  O   . ASN A  1  190 ? 50.247  5.790   26.399 1.00 42.36  ? 203 ASN A O   1 
ATOM   1447 C  CB  . ASN A  1  190 ? 52.292  8.782   27.112 1.00 42.44  ? 203 ASN A CB  1 
ATOM   1448 C  CG  . ASN A  1  190 ? 53.109  9.753   26.293 1.00 43.45  ? 203 ASN A CG  1 
ATOM   1449 O  OD1 . ASN A  1  190 ? 53.781  9.350   25.332 1.00 45.42  ? 203 ASN A OD1 1 
ATOM   1450 N  ND2 . ASN A  1  190 ? 53.058  11.027  26.649 1.00 42.30  ? 203 ASN A ND2 1 
ATOM   1451 N  N   . VAL A  1  191 ? 50.886  6.716   28.328 1.00 42.10  ? 204 VAL A N   1 
ATOM   1452 C  CA  . VAL A  1  191 ? 50.329  5.636   29.120 1.00 40.93  ? 204 VAL A CA  1 
ATOM   1453 C  C   . VAL A  1  191 ? 48.836  5.509   28.805 1.00 39.24  ? 204 VAL A C   1 
ATOM   1454 O  O   . VAL A  1  191 ? 48.330  4.416   28.588 1.00 36.86  ? 204 VAL A O   1 
ATOM   1455 C  CB  . VAL A  1  191 ? 50.556  5.862   30.625 1.00 40.33  ? 204 VAL A CB  1 
ATOM   1456 C  CG1 . VAL A  1  191 ? 49.916  4.754   31.451 1.00 39.98  ? 204 VAL A CG1 1 
ATOM   1457 C  CG2 . VAL A  1  191 ? 52.029  6.010   30.981 1.00 42.38  ? 204 VAL A CG2 1 
ATOM   1458 N  N   . ARG A  1  192 ? 48.123  6.635   28.776 1.00 36.09  ? 205 ARG A N   1 
ATOM   1459 C  CA  . ARG A  1  192 ? 46.684  6.590   28.634 1.00 34.75  ? 205 ARG A CA  1 
ATOM   1460 C  C   . ARG A  1  192 ? 46.290  5.946   27.309 1.00 35.31  ? 205 ARG A C   1 
ATOM   1461 O  O   . ARG A  1  192 ? 45.315  5.205   27.245 1.00 37.39  ? 205 ARG A O   1 
ATOM   1462 C  CB  . ARG A  1  192 ? 46.052  7.979   28.729 1.00 37.34  ? 205 ARG A CB  1 
ATOM   1463 C  CG  . ARG A  1  192 ? 44.530  7.934   28.650 1.00 39.49  ? 205 ARG A CG  1 
ATOM   1464 C  CD  . ARG A  1  192 ? 43.934  6.940   29.634 1.00 38.88  ? 205 ARG A CD  1 
ATOM   1465 N  NE  . ARG A  1  192 ? 42.480  6.808   29.514 1.00 38.78  ? 205 ARG A NE  1 
ATOM   1466 C  CZ  . ARG A  1  192 ? 41.783  5.757   29.915 1.00 36.54  ? 205 ARG A CZ  1 
ATOM   1467 N  NH1 . ARG A  1  192 ? 42.391  4.720   30.476 1.00 36.39  ? 205 ARG A NH1 1 
ATOM   1468 N  NH2 . ARG A  1  192 ? 40.473  5.744   29.722 1.00 35.46  ? 205 ARG A NH2 1 
ATOM   1469 N  N   . PHE A  1  193 ? 47.036  6.239   26.244 1.00 35.17  ? 206 PHE A N   1 
ATOM   1470 C  CA  . PHE A  1  193 ? 46.675  5.730   24.937 1.00 34.32  ? 206 PHE A CA  1 
ATOM   1471 C  C   . PHE A  1  193 ? 46.731  4.206   24.952 1.00 37.94  ? 206 PHE A C   1 
ATOM   1472 O  O   . PHE A  1  193 ? 45.873  3.566   24.351 1.00 40.38  ? 206 PHE A O   1 
ATOM   1473 C  CB  . PHE A  1  193 ? 47.573  6.322   23.853 1.00 34.61  ? 206 PHE A CB  1 
ATOM   1474 C  CG  . PHE A  1  193 ? 47.215  5.793   22.478 1.00 33.76  ? 206 PHE A CG  1 
ATOM   1475 C  CD1 . PHE A  1  193 ? 46.166  6.341   21.759 1.00 34.77  ? 206 PHE A CD1 1 
ATOM   1476 C  CD2 . PHE A  1  193 ? 47.908  4.731   21.927 1.00 33.95  ? 206 PHE A CD2 1 
ATOM   1477 C  CE1 . PHE A  1  193 ? 45.828  5.839   20.515 1.00 35.15  ? 206 PHE A CE1 1 
ATOM   1478 C  CE2 . PHE A  1  193 ? 47.571  4.234   20.683 1.00 34.38  ? 206 PHE A CE2 1 
ATOM   1479 C  CZ  . PHE A  1  193 ? 46.529  4.786   19.981 1.00 35.08  ? 206 PHE A CZ  1 
ATOM   1480 N  N   . ILE A  1  194 ? 47.715  3.632   25.655 1.00 34.87  ? 207 ILE A N   1 
ATOM   1481 C  CA  . ILE A  1  194 ? 47.838  2.184   25.725 1.00 35.11  ? 207 ILE A CA  1 
ATOM   1482 C  C   . ILE A  1  194 ? 46.778  1.606   26.669 1.00 36.63  ? 207 ILE A C   1 
ATOM   1483 O  O   . ILE A  1  194 ? 46.087  0.657   26.309 1.00 37.85  ? 207 ILE A O   1 
ATOM   1484 C  CB  . ILE A  1  194 ? 49.257  1.759   26.147 1.00 36.07  ? 207 ILE A CB  1 
ATOM   1485 C  CG1 . ILE A  1  194 ? 50.352  2.412   25.310 1.00 36.75  ? 207 ILE A CG1 1 
ATOM   1486 C  CG2 . ILE A  1  194 ? 49.367  0.238   26.108 1.00 37.07  ? 207 ILE A CG2 1 
ATOM   1487 C  CD1 . ILE A  1  194 ? 50.237  2.225   23.801 1.00 36.57  ? 207 ILE A CD1 1 
ATOM   1488 N  N   . THR A  1  195 ? 46.622  2.186   27.867 1.00 37.03  ? 208 THR A N   1 
ATOM   1489 C  CA  . THR A  1  195 ? 45.735  1.603   28.864 1.00 36.59  ? 208 THR A CA  1 
ATOM   1490 C  C   . THR A  1  195 ? 44.275  1.690   28.416 1.00 35.48  ? 208 THR A C   1 
ATOM   1491 O  O   . THR A  1  195 ? 43.500  0.795   28.730 1.00 36.81  ? 208 THR A O   1 
ATOM   1492 C  CB  . THR A  1  195 ? 45.971  2.191   30.257 1.00 36.51  ? 208 THR A CB  1 
ATOM   1493 O  OG1 . THR A  1  195 ? 45.634  3.572   30.336 1.00 36.89  ? 208 THR A OG1 1 
ATOM   1494 C  CG2 . THR A  1  195 ? 47.413  2.007   30.694 1.00 39.19  ? 208 THR A CG2 1 
ATOM   1495 N  N   . ALA A  1  196 ? 43.913  2.720   27.644 1.00 39.14  ? 209 ALA A N   1 
ATOM   1496 C  CA  . ALA A  1  196 ? 42.522  2.944   27.252 1.00 38.21  ? 209 ALA A CA  1 
ATOM   1497 C  C   . ALA A  1  196 ? 41.968  1.826   26.368 1.00 37.94  ? 209 ALA A C   1 
ATOM   1498 O  O   . ALA A  1  196 ? 40.762  1.642   26.308 1.00 41.19  ? 209 ALA A O   1 
ATOM   1499 C  CB  . ALA A  1  196 ? 42.381  4.271   26.544 1.00 36.35  ? 209 ALA A CB  1 
ATOM   1500 N  N   . TYR A  1  197 ? 42.823  1.109   25.634 1.00 37.69  ? 210 TYR A N   1 
ATOM   1501 C  CA  . TYR A  1  197 ? 42.327  0.056   24.764 1.00 35.25  ? 210 TYR A CA  1 
ATOM   1502 C  C   . TYR A  1  197 ? 42.173  -1.235  25.564 1.00 36.86  ? 210 TYR A C   1 
ATOM   1503 O  O   . TYR A  1  197 ? 41.184  -1.949  25.401 1.00 42.90  ? 210 TYR A O   1 
ATOM   1504 C  CB  . TYR A  1  197 ? 43.196  -0.026  23.503 1.00 34.90  ? 210 TYR A CB  1 
ATOM   1505 C  CG  . TYR A  1  197 ? 42.827  1.099   22.545 1.00 33.49  ? 210 TYR A CG  1 
ATOM   1506 C  CD1 . TYR A  1  197 ? 41.765  0.954   21.660 1.00 34.07  ? 210 TYR A CD1 1 
ATOM   1507 C  CD2 . TYR A  1  197 ? 43.460  2.335   22.602 1.00 32.09  ? 210 TYR A CD2 1 
ATOM   1508 C  CE1 . TYR A  1  197 ? 41.380  1.983   20.820 1.00 34.41  ? 210 TYR A CE1 1 
ATOM   1509 C  CE2 . TYR A  1  197 ? 43.090  3.378   21.767 1.00 33.95  ? 210 TYR A CE2 1 
ATOM   1510 C  CZ  . TYR A  1  197 ? 42.039  3.204   20.882 1.00 35.81  ? 210 TYR A CZ  1 
ATOM   1511 O  OH  . TYR A  1  197 ? 41.654  4.235   20.073 1.00 38.08  ? 210 TYR A OH  1 
ATOM   1512 N  N   . GLY A  1  198 ? 43.139  -1.512  26.448 1.00 36.64  ? 211 GLY A N   1 
ATOM   1513 C  CA  . GLY A  1  198 ? 43.090  -2.699  27.296 1.00 36.36  ? 211 GLY A CA  1 
ATOM   1514 C  C   . GLY A  1  198 ? 41.888  -2.700  28.246 1.00 34.97  ? 211 GLY A C   1 
ATOM   1515 O  O   . GLY A  1  198 ? 41.256  -3.740  28.441 1.00 30.93  ? 211 GLY A O   1 
ATOM   1516 N  N   . GLU A  1  199 ? 41.562  -1.523  28.806 1.00 35.18  ? 212 GLU A N   1 
ATOM   1517 C  CA  . GLU A  1  199 ? 40.500  -1.420  29.789 1.00 38.98  ? 212 GLU A CA  1 
ATOM   1518 C  C   . GLU A  1  199 ? 39.159  -1.823  29.163 1.00 37.16  ? 212 GLU A C   1 
ATOM   1519 O  O   . GLU A  1  199 ? 38.270  -2.318  29.867 1.00 34.35  ? 212 GLU A O   1 
ATOM   1520 C  CB  . GLU A  1  199 ? 40.518  -0.038  30.451 1.00 40.41  ? 212 GLU A CB  1 
ATOM   1521 C  CG  . GLU A  1  199 ? 39.700  1.028   29.719 1.00 46.25  ? 212 GLU A CG  1 
ATOM   1522 C  CD  . GLU A  1  199 ? 39.735  2.467   30.267 1.00 49.61  ? 212 GLU A CD  1 
ATOM   1523 O  OE1 . GLU A  1  199 ? 40.430  2.754   31.296 1.00 53.62  ? 212 GLU A OE1 1 
ATOM   1524 O  OE2 . GLU A  1  199 ? 39.029  3.314   29.648 1.00 38.36  ? 212 GLU A OE2 1 
ATOM   1525 N  N   . THR A  1  200 ? 39.010  -1.644  27.839 1.00 35.16  ? 213 THR A N   1 
ATOM   1526 C  CA  . THR A  1  200 ? 37.708  -1.857  27.224 1.00 32.59  ? 213 THR A CA  1 
ATOM   1527 C  C   . THR A  1  200 ? 37.461  -3.346  27.000 1.00 30.06  ? 213 THR A C   1 
ATOM   1528 O  O   . THR A  1  200 ? 36.318  -3.707  26.749 1.00 29.62  ? 213 THR A O   1 
ATOM   1529 C  CB  . THR A  1  200 ? 37.548  -1.082  25.915 1.00 34.36  ? 213 THR A CB  1 
ATOM   1530 O  OG1 . THR A  1  200 ? 38.349  -1.732  24.939 1.00 36.92  ? 213 THR A OG1 1 
ATOM   1531 C  CG2 . THR A  1  200 ? 37.938  0.383   26.027 1.00 35.73  ? 213 THR A CG2 1 
ATOM   1532 N  N   . VAL A  1  201 ? 38.495  -4.201  27.072 1.00 28.51  ? 214 VAL A N   1 
ATOM   1533 C  CA  . VAL A  1  201 ? 38.273  -5.632  26.907 1.00 29.44  ? 214 VAL A CA  1 
ATOM   1534 C  C   . VAL A  1  201 ? 38.332  -6.379  28.241 1.00 31.09  ? 214 VAL A C   1 
ATOM   1535 O  O   . VAL A  1  201 ? 37.941  -7.548  28.295 1.00 30.97  ? 214 VAL A O   1 
ATOM   1536 C  CB  . VAL A  1  201 ? 39.220  -6.281  25.884 1.00 30.89  ? 214 VAL A CB  1 
ATOM   1537 C  CG1 . VAL A  1  201 ? 39.036  -5.652  24.508 1.00 34.17  ? 214 VAL A CG1 1 
ATOM   1538 C  CG2 . VAL A  1  201 ? 40.679  -6.216  26.307 1.00 32.09  ? 214 VAL A CG2 1 
ATOM   1539 N  N   . PHE A  1  202 ? 38.786  -5.724  29.319 1.00 33.76  ? 215 PHE A N   1 
ATOM   1540 C  CA  . PHE A  1  202 ? 38.861  -6.396  30.612 1.00 35.94  ? 215 PHE A CA  1 
ATOM   1541 C  C   . PHE A  1  202 ? 37.481  -6.918  31.022 1.00 35.71  ? 215 PHE A C   1 
ATOM   1542 O  O   . PHE A  1  202 ? 37.355  -8.032  31.533 1.00 36.26  ? 215 PHE A O   1 
ATOM   1543 C  CB  . PHE A  1  202 ? 39.449  -5.531  31.730 1.00 35.51  ? 215 PHE A CB  1 
ATOM   1544 C  CG  . PHE A  1  202 ? 40.945  -5.271  31.641 1.00 40.23  ? 215 PHE A CG  1 
ATOM   1545 C  CD1 . PHE A  1  202 ? 41.755  -5.944  30.728 1.00 41.87  ? 215 PHE A CD1 1 
ATOM   1546 C  CD2 . PHE A  1  202 ? 41.541  -4.342  32.480 1.00 40.84  ? 215 PHE A CD2 1 
ATOM   1547 C  CE1 . PHE A  1  202 ? 43.111  -5.691  30.666 1.00 42.88  ? 215 PHE A CE1 1 
ATOM   1548 C  CE2 . PHE A  1  202 ? 42.896  -4.097  32.413 1.00 41.47  ? 215 PHE A CE2 1 
ATOM   1549 C  CZ  . PHE A  1  202 ? 43.681  -4.779  31.524 1.00 44.54  ? 215 PHE A CZ  1 
ATOM   1550 N  N   . PRO A  1  203 ? 36.386  -6.149  30.840 1.00 33.64  ? 216 PRO A N   1 
ATOM   1551 C  CA  . PRO A  1  203 ? 35.060  -6.652  31.202 1.00 34.40  ? 216 PRO A CA  1 
ATOM   1552 C  C   . PRO A  1  203 ? 34.682  -7.967  30.515 1.00 36.06  ? 216 PRO A C   1 
ATOM   1553 O  O   . PRO A  1  203 ? 33.983  -8.787  31.090 1.00 39.40  ? 216 PRO A O   1 
ATOM   1554 C  CB  . PRO A  1  203 ? 34.158  -5.488  30.783 1.00 33.39  ? 216 PRO A CB  1 
ATOM   1555 C  CG  . PRO A  1  203 ? 35.047  -4.277  30.879 1.00 33.24  ? 216 PRO A CG  1 
ATOM   1556 C  CD  . PRO A  1  203 ? 36.364  -4.765  30.335 1.00 32.78  ? 216 PRO A CD  1 
ATOM   1557 N  N   . ILE A  1  204 ? 35.145  -8.166  29.280 1.00 34.93  ? 217 ILE A N   1 
ATOM   1558 C  CA  . ILE A  1  204 ? 34.844  -9.367  28.523 1.00 32.41  ? 217 ILE A CA  1 
ATOM   1559 C  C   . ILE A  1  204 ? 35.693  -10.526 29.044 1.00 33.89  ? 217 ILE A C   1 
ATOM   1560 O  O   . ILE A  1  204 ? 35.187  -11.628 29.270 1.00 35.51  ? 217 ILE A O   1 
ATOM   1561 C  CB  . ILE A  1  204 ? 35.104  -9.122  27.025 1.00 32.73  ? 217 ILE A CB  1 
ATOM   1562 C  CG1 . ILE A  1  204 ? 34.260  -7.978  26.487 1.00 33.44  ? 217 ILE A CG1 1 
ATOM   1563 C  CG2 . ILE A  1  204 ? 34.895  -10.396 26.212 1.00 31.87  ? 217 ILE A CG2 1 
ATOM   1564 C  CD1 . ILE A  1  204 ? 34.718  -7.457  25.140 1.00 32.77  ? 217 ILE A CD1 1 
ATOM   1565 N  N   . ASN A  1  205 ? 37.000  -10.288 29.207 1.00 34.15  ? 218 ASN A N   1 
ATOM   1566 C  CA  . ASN A  1  205 ? 37.930  -11.365 29.497 1.00 32.88  ? 218 ASN A CA  1 
ATOM   1567 C  C   . ASN A  1  205 ? 37.938  -11.710 30.978 1.00 31.76  ? 218 ASN A C   1 
ATOM   1568 O  O   . ASN A  1  205 ? 38.257  -12.846 31.311 1.00 39.99  ? 218 ASN A O   1 
ATOM   1569 C  CB  . ASN A  1  205 ? 39.342  -11.041 29.024 1.00 35.04  ? 218 ASN A CB  1 
ATOM   1570 C  CG  . ASN A  1  205 ? 39.400  -10.698 27.554 1.00 34.10  ? 218 ASN A CG  1 
ATOM   1571 O  OD1 . ASN A  1  205 ? 38.593  -11.193 26.756 1.00 36.93  ? 218 ASN A OD1 1 
ATOM   1572 N  ND2 . ASN A  1  205 ? 40.314  -9.817  27.183 1.00 33.70  ? 218 ASN A ND2 1 
ATOM   1573 N  N   . LEU A  1  206 ? 37.584  -10.754 31.852 1.00 30.25  ? 219 LEU A N   1 
ATOM   1574 C  CA  . LEU A  1  206 ? 37.745  -10.950 33.288 1.00 31.00  ? 219 LEU A CA  1 
ATOM   1575 C  C   . LEU A  1  206 ? 36.450  -10.847 34.094 1.00 30.62  ? 219 LEU A C   1 
ATOM   1576 O  O   . LEU A  1  206 ? 36.394  -11.447 35.169 1.00 32.71  ? 219 LEU A O   1 
ATOM   1577 C  CB  . LEU A  1  206 ? 38.789  -9.965  33.796 1.00 30.63  ? 219 LEU A CB  1 
ATOM   1578 C  CG  . LEU A  1  206 ? 40.182  -10.155 33.190 1.00 31.49  ? 219 LEU A CG  1 
ATOM   1579 C  CD1 . LEU A  1  206 ? 41.049  -8.947  33.519 1.00 32.91  ? 219 LEU A CD1 1 
ATOM   1580 C  CD2 . LEU A  1  206 ? 40.827  -11.462 33.634 1.00 30.49  ? 219 LEU A CD2 1 
ATOM   1581 N  N   . PHE A  1  207 ? 35.451  -10.089 33.616 1.00 28.17  ? 220 PHE A N   1 
ATOM   1582 C  CA  . PHE A  1  207 ? 34.220  -9.885  34.373 1.00 29.05  ? 220 PHE A CA  1 
ATOM   1583 C  C   . PHE A  1  207 ? 33.142  -10.880 33.948 1.00 29.74  ? 220 PHE A C   1 
ATOM   1584 O  O   . PHE A  1  207 ? 32.137  -11.042 34.635 1.00 29.20  ? 220 PHE A O   1 
ATOM   1585 C  CB  . PHE A  1  207 ? 33.615  -8.488  34.225 1.00 27.57  ? 220 PHE A CB  1 
ATOM   1586 C  CG  . PHE A  1  207 ? 34.406  -7.335  34.808 1.00 27.66  ? 220 PHE A CG  1 
ATOM   1587 C  CD1 . PHE A  1  207 ? 35.442  -7.548  35.708 1.00 29.06  ? 220 PHE A CD1 1 
ATOM   1588 C  CD2 . PHE A  1  207 ? 34.092  -6.029  34.459 1.00 28.75  ? 220 PHE A CD2 1 
ATOM   1589 C  CE1 . PHE A  1  207 ? 36.145  -6.475  36.239 1.00 29.33  ? 220 PHE A CE1 1 
ATOM   1590 C  CE2 . PHE A  1  207 ? 34.806  -4.966  34.987 1.00 29.78  ? 220 PHE A CE2 1 
ATOM   1591 C  CZ  . PHE A  1  207 ? 35.828  -5.191  35.876 1.00 29.80  ? 220 PHE A CZ  1 
ATOM   1592 N  N   . VAL A  1  208 ? 33.328  -11.513 32.790 1.00 32.63  ? 221 VAL A N   1 
ATOM   1593 C  CA  . VAL A  1  208 ? 32.445  -12.585 32.373 1.00 34.16  ? 221 VAL A CA  1 
ATOM   1594 C  C   . VAL A  1  208 ? 32.852  -13.866 33.089 1.00 35.76  ? 221 VAL A C   1 
ATOM   1595 O  O   . VAL A  1  208 ? 34.026  -14.209 33.143 1.00 44.87  ? 221 VAL A O   1 
ATOM   1596 C  CB  . VAL A  1  208 ? 32.420  -12.771 30.847 1.00 31.13  ? 221 VAL A CB  1 
ATOM   1597 C  CG1 . VAL A  1  208 ? 31.583  -13.974 30.422 1.00 28.87  ? 221 VAL A CG1 1 
ATOM   1598 C  CG2 . VAL A  1  208 ? 31.916  -11.502 30.182 1.00 32.76  ? 221 VAL A CG2 1 
ATOM   1599 N  N   . ASP A  1  209 ? 31.848  -14.554 33.633 1.00 40.02  ? 222 ASP A N   1 
ATOM   1600 C  CA  . ASP A  1  209 ? 32.032  -15.786 34.377 1.00 39.37  ? 222 ASP A CA  1 
ATOM   1601 C  C   . ASP A  1  209 ? 32.855  -16.776 33.551 1.00 42.13  ? 222 ASP A C   1 
ATOM   1602 O  O   . ASP A  1  209 ? 32.675  -16.906 32.340 1.00 39.03  ? 222 ASP A O   1 
ATOM   1603 C  CB  . ASP A  1  209 ? 30.687  -16.350 34.791 1.00 38.36  ? 222 ASP A CB  1 
ATOM   1604 C  CG  . ASP A  1  209 ? 30.748  -17.452 35.831 1.00 40.75  ? 222 ASP A CG  1 
ATOM   1605 O  OD1 . ASP A  1  209 ? 31.111  -18.586 35.448 1.00 43.33  ? 222 ASP A OD1 1 
ATOM   1606 O  OD2 . ASP A  1  209 ? 30.455  -17.155 37.021 1.00 39.62  ? 222 ASP A OD2 1 
ATOM   1607 N  N   . GLY A  1  210 ? 33.755  -17.487 34.238 1.00 41.38  ? 223 GLY A N   1 
ATOM   1608 C  CA  . GLY A  1  210 ? 34.735  -18.343 33.592 1.00 41.66  ? 223 GLY A CA  1 
ATOM   1609 C  C   . GLY A  1  210 ? 34.139  -19.646 33.061 1.00 41.15  ? 223 GLY A C   1 
ATOM   1610 O  O   . GLY A  1  210 ? 34.768  -20.331 32.260 1.00 42.43  ? 223 GLY A O   1 
ATOM   1611 N  N   . ARG A  1  211 ? 32.934  -19.999 33.517 1.00 39.59  ? 224 ARG A N   1 
ATOM   1612 C  CA  . ARG A  1  211 ? 32.249  -21.178 33.017 1.00 40.03  ? 224 ARG A CA  1 
ATOM   1613 C  C   . ARG A  1  211 ? 31.641  -20.912 31.639 1.00 43.06  ? 224 ARG A C   1 
ATOM   1614 O  O   . ARG A  1  211 ? 31.273  -21.859 30.964 1.00 43.85  ? 224 ARG A O   1 
ATOM   1615 C  CB  . ARG A  1  211 ? 31.184  -21.643 34.009 1.00 40.30  ? 224 ARG A CB  1 
ATOM   1616 C  CG  . ARG A  1  211 ? 31.799  -22.159 35.302 1.00 42.33  ? 224 ARG A CG  1 
ATOM   1617 C  CD  . ARG A  1  211 ? 30.801  -22.251 36.436 1.00 41.76  ? 224 ARG A CD  1 
ATOM   1618 N  NE  . ARG A  1  211 ? 30.264  -20.932 36.794 1.00 42.06  ? 224 ARG A NE  1 
ATOM   1619 C  CZ  . ARG A  1  211 ? 29.436  -20.699 37.799 1.00 44.01  ? 224 ARG A CZ  1 
ATOM   1620 N  NH1 . ARG A  1  211 ? 29.014  -21.703 38.545 1.00 43.62  ? 224 ARG A NH1 1 
ATOM   1621 N  NH2 . ARG A  1  211 ? 29.048  -19.463 38.069 1.00 44.52  ? 224 ARG A NH2 1 
ATOM   1622 N  N   . VAL A  1  212 ? 31.539  -19.643 31.218 1.00 44.28  ? 225 VAL A N   1 
ATOM   1623 C  CA  . VAL A  1  212 ? 31.087  -19.323 29.871 1.00 44.30  ? 225 VAL A CA  1 
ATOM   1624 C  C   . VAL A  1  212 ? 32.277  -19.455 28.920 1.00 48.79  ? 225 VAL A C   1 
ATOM   1625 O  O   . VAL A  1  212 ? 33.185  -18.624 28.963 1.00 46.89  ? 225 VAL A O   1 
ATOM   1626 C  CB  . VAL A  1  212 ? 30.483  -17.904 29.810 1.00 40.57  ? 225 VAL A CB  1 
ATOM   1627 C  CG1 . VAL A  1  212 ? 30.028  -17.513 28.406 1.00 38.66  ? 225 VAL A CG1 1 
ATOM   1628 C  CG2 . VAL A  1  212 ? 29.327  -17.753 30.774 1.00 39.02  ? 225 VAL A CG2 1 
ATOM   1629 N  N   . THR A  1  213 ? 32.253  -20.472 28.044 1.00 58.32  ? 226 THR A N   1 
ATOM   1630 C  CA  . THR A  1  213 ? 33.396  -20.733 27.175 1.00 67.89  ? 226 THR A CA  1 
ATOM   1631 C  C   . THR A  1  213 ? 33.193  -20.115 25.790 1.00 65.37  ? 226 THR A C   1 
ATOM   1632 O  O   . THR A  1  213 ? 34.164  -19.913 25.080 1.00 57.21  ? 226 THR A O   1 
ATOM   1633 C  CB  . THR A  1  213 ? 33.667  -22.236 27.083 1.00 64.37  ? 226 THR A CB  1 
ATOM   1634 O  OG1 . THR A  1  213 ? 32.509  -22.778 26.465 1.00 64.61  ? 226 THR A OG1 1 
ATOM   1635 C  CG2 . THR A  1  213 ? 33.854  -22.898 28.438 1.00 62.80  ? 226 THR A CG2 1 
ATOM   1636 N  N   . THR A  1  214 ? 31.951  -19.776 25.431 1.00 70.67  ? 227 THR A N   1 
ATOM   1637 C  CA  . THR A  1  214 ? 31.638  -19.416 24.059 1.00 73.15  ? 227 THR A CA  1 
ATOM   1638 C  C   . THR A  1  214 ? 30.690  -18.211 24.033 1.00 69.67  ? 227 THR A C   1 
ATOM   1639 O  O   . THR A  1  214 ? 29.757  -18.138 24.828 1.00 71.89  ? 227 THR A O   1 
ATOM   1640 C  CB  . THR A  1  214 ? 31.056  -20.671 23.398 1.00 75.67  ? 227 THR A CB  1 
ATOM   1641 O  OG1 . THR A  1  214 ? 30.885  -20.303 22.037 1.00 84.36  ? 227 THR A OG1 1 
ATOM   1642 C  CG2 . THR A  1  214 ? 29.750  -21.150 24.014 1.00 71.91  ? 227 THR A CG2 1 
ATOM   1643 N  N   . ASP A  1  215 ? 30.925  -17.260 23.120 1.00 69.19  ? 228 ASP A N   1 
ATOM   1644 C  CA  . ASP A  1  215 ? 30.067  -16.087 22.973 1.00 71.85  ? 228 ASP A CA  1 
ATOM   1645 C  C   . ASP A  1  215 ? 30.094  -15.316 24.291 1.00 59.60  ? 228 ASP A C   1 
ATOM   1646 O  O   . ASP A  1  215 ? 29.059  -15.033 24.894 1.00 54.78  ? 228 ASP A O   1 
ATOM   1647 C  CB  . ASP A  1  215 ? 28.665  -16.454 22.489 1.00 82.17  ? 228 ASP A CB  1 
ATOM   1648 C  CG  . ASP A  1  215 ? 27.732  -15.295 22.116 1.00 93.98  ? 228 ASP A CG  1 
ATOM   1649 O  OD1 . ASP A  1  215 ? 28.201  -14.319 21.479 1.00 99.59  ? 228 ASP A OD1 1 
ATOM   1650 O  OD2 . ASP A  1  215 ? 26.515  -15.372 22.433 1.00 89.64  ? 228 ASP A OD2 1 
ATOM   1651 N  N   . ARG A  1  216 ? 31.307  -14.970 24.724 1.00 52.37  ? 229 ARG A N   1 
ATOM   1652 C  CA  . ARG A  1  216 ? 31.508  -14.316 26.002 1.00 46.23  ? 229 ARG A CA  1 
ATOM   1653 C  C   . ARG A  1  216 ? 30.997  -12.883 25.902 1.00 40.74  ? 229 ARG A C   1 
ATOM   1654 O  O   . ARG A  1  216 ? 31.399  -12.137 25.021 1.00 40.49  ? 229 ARG A O   1 
ATOM   1655 C  CB  . ARG A  1  216 ? 32.982  -14.434 26.408 1.00 47.31  ? 229 ARG A CB  1 
ATOM   1656 C  CG  . ARG A  1  216 ? 33.365  -15.827 26.901 1.00 47.90  ? 229 ARG A CG  1 
ATOM   1657 C  CD  . ARG A  1  216 ? 34.863  -15.995 27.183 1.00 49.21  ? 229 ARG A CD  1 
ATOM   1658 N  NE  . ARG A  1  216 ? 35.332  -15.152 28.290 1.00 50.48  ? 229 ARG A NE  1 
ATOM   1659 C  CZ  . ARG A  1  216 ? 35.053  -15.321 29.584 1.00 52.21  ? 229 ARG A CZ  1 
ATOM   1660 N  NH1 . ARG A  1  216 ? 34.392  -16.394 29.994 1.00 49.20  ? 229 ARG A NH1 1 
ATOM   1661 N  NH2 . ARG A  1  216 ? 35.469  -14.416 30.466 1.00 55.46  ? 229 ARG A NH2 1 
ATOM   1662 N  N   . LYS A  1  217 ? 30.112  -12.512 26.826 1.00 35.94  ? 230 LYS A N   1 
ATOM   1663 C  CA  . LYS A  1  217 ? 29.470  -11.208 26.805 1.00 36.65  ? 230 LYS A CA  1 
ATOM   1664 C  C   . LYS A  1  217 ? 28.965  -10.918 28.215 1.00 34.92  ? 230 LYS A C   1 
ATOM   1665 O  O   . LYS A  1  217 ? 28.587  -11.846 28.947 1.00 32.68  ? 230 LYS A O   1 
ATOM   1666 C  CB  . LYS A  1  217 ? 28.314  -11.224 25.798 1.00 38.86  ? 230 LYS A CB  1 
ATOM   1667 C  CG  . LYS A  1  217 ? 27.204  -12.215 26.164 1.00 41.01  ? 230 LYS A CG  1 
ATOM   1668 C  CD  . LYS A  1  217 ? 26.105  -12.402 25.127 1.00 42.67  ? 230 LYS A CD  1 
ATOM   1669 C  CE  . LYS A  1  217 ? 25.071  -13.362 25.630 1.00 46.13  ? 230 LYS A CE  1 
ATOM   1670 N  NZ  . LYS A  1  217 ? 23.883  -13.416 24.780 1.00 47.42  ? 230 LYS A NZ  1 
ATOM   1671 N  N   . LEU A  1  218 ? 28.972  -9.634  28.587 1.00 31.80  ? 231 LEU A N   1 
ATOM   1672 C  CA  . LEU A  1  218 ? 28.692  -9.242  29.956 1.00 31.34  ? 231 LEU A CA  1 
ATOM   1673 C  C   . LEU A  1  218 ? 27.293  -8.639  30.034 1.00 33.42  ? 231 LEU A C   1 
ATOM   1674 O  O   . LEU A  1  218 ? 26.968  -7.744  29.256 1.00 34.18  ? 231 LEU A O   1 
ATOM   1675 C  CB  . LEU A  1  218 ? 29.756  -8.240  30.395 1.00 30.07  ? 231 LEU A CB  1 
ATOM   1676 C  CG  . LEU A  1  218 ? 29.686  -7.800  31.861 1.00 28.71  ? 231 LEU A CG  1 
ATOM   1677 C  CD1 . LEU A  1  218 ? 30.051  -8.936  32.806 1.00 30.10  ? 231 LEU A CD1 1 
ATOM   1678 C  CD2 . LEU A  1  218 ? 30.588  -6.607  32.083 1.00 28.41  ? 231 LEU A CD2 1 
ATOM   1679 N  N   . SER A  1  219 ? 26.485  -9.112  30.991 1.00 34.26  ? 232 SER A N   1 
ATOM   1680 C  CA  . SER A  1  219 ? 25.152  -8.559  31.203 1.00 34.77  ? 232 SER A CA  1 
ATOM   1681 C  C   . SER A  1  219 ? 25.256  -7.199  31.884 1.00 33.91  ? 232 SER A C   1 
ATOM   1682 O  O   . SER A  1  219 ? 26.242  -6.920  32.549 1.00 34.61  ? 232 SER A O   1 
ATOM   1683 C  CB  . SER A  1  219 ? 24.297  -9.500  32.014 1.00 34.98  ? 232 SER A CB  1 
ATOM   1684 O  OG  . SER A  1  219 ? 24.726  -9.511  33.366 1.00 36.48  ? 232 SER A OG  1 
ATOM   1685 N  N   . MET A  1  220 ? 24.229  -6.357  31.754 1.00 37.32  ? 233 MET A N   1 
ATOM   1686 C  CA  . MET A  1  220 ? 24.272  -5.054  32.398 1.00 37.07  ? 233 MET A CA  1 
ATOM   1687 C  C   . MET A  1  220 ? 24.100  -5.182  33.915 1.00 38.11  ? 233 MET A C   1 
ATOM   1688 O  O   . MET A  1  220 ? 24.561  -4.318  34.654 1.00 39.85  ? 233 MET A O   1 
ATOM   1689 C  CB  . MET A  1  220 ? 23.217  -4.111  31.825 1.00 36.81  ? 233 MET A CB  1 
ATOM   1690 C  CG  . MET A  1  220 ? 23.379  -3.835  30.338 1.00 41.23  ? 233 MET A CG  1 
ATOM   1691 S  SD  . MET A  1  220 ? 24.953  -3.102  29.844 1.00 41.10  ? 233 MET A SD  1 
ATOM   1692 C  CE  . MET A  1  220 ? 25.813  -4.570  29.266 1.00 40.20  ? 233 MET A CE  1 
ATOM   1693 N  N   . GLU A  1  221 ? 23.460  -6.257  34.388 1.00 38.06  ? 234 GLU A N   1 
ATOM   1694 C  CA  . GLU A  1  221 ? 23.288  -6.476  35.821 1.00 41.06  ? 234 GLU A CA  1 
ATOM   1695 C  C   . GLU A  1  221 ? 24.654  -6.703  36.468 1.00 43.08  ? 234 GLU A C   1 
ATOM   1696 O  O   . GLU A  1  221 ? 24.940  -6.131  37.513 1.00 39.17  ? 234 GLU A O   1 
ATOM   1697 C  CB  . GLU A  1  221 ? 22.366  -7.655  36.143 1.00 41.17  ? 234 GLU A CB  1 
ATOM   1698 C  CG  . GLU A  1  221 ? 20.920  -7.441  35.695 1.00 46.06  ? 234 GLU A CG  1 
ATOM   1699 C  CD  . GLU A  1  221 ? 20.556  -7.633  34.214 1.00 49.95  ? 234 GLU A CD  1 
ATOM   1700 O  OE1 . GLU A  1  221 ? 21.404  -7.851  33.281 1.00 43.85  ? 234 GLU A OE1 1 
ATOM   1701 O  OE2 . GLU A  1  221 ? 19.312  -7.562  34.014 1.00 50.93  ? 234 GLU A OE2 1 
ATOM   1702 N  N   . ASP A  1  222 ? 25.487  -7.525  35.813 1.00 42.45  ? 235 ASP A N   1 
ATOM   1703 C  CA  . ASP A  1  222 ? 26.819  -7.851  36.291 1.00 39.10  ? 235 ASP A CA  1 
ATOM   1704 C  C   . ASP A  1  222 ? 27.742  -6.640  36.137 1.00 38.10  ? 235 ASP A C   1 
ATOM   1705 O  O   . ASP A  1  222 ? 28.542  -6.349  37.026 1.00 39.65  ? 235 ASP A O   1 
ATOM   1706 C  CB  . ASP A  1  222 ? 27.380  -9.069  35.576 1.00 40.77  ? 235 ASP A CB  1 
ATOM   1707 C  CG  . ASP A  1  222 ? 26.743  -10.410 35.908 1.00 42.14  ? 235 ASP A CG  1 
ATOM   1708 O  OD1 . ASP A  1  222 ? 25.887  -10.451 36.827 1.00 41.21  ? 235 ASP A OD1 1 
ATOM   1709 O  OD2 . ASP A  1  222 ? 27.166  -11.419 35.282 1.00 43.55  ? 235 ASP A OD2 1 
ATOM   1710 N  N   . ALA A  1  223 ? 27.640  -5.932  35.007 1.00 32.45  ? 236 ALA A N   1 
ATOM   1711 C  CA  . ALA A  1  223 ? 28.386  -4.701  34.830 1.00 32.18  ? 236 ALA A CA  1 
ATOM   1712 C  C   . ALA A  1  223 ? 28.080  -3.718  35.960 1.00 31.55  ? 236 ALA A C   1 
ATOM   1713 O  O   . ALA A  1  223 ? 28.997  -3.171  36.560 1.00 34.75  ? 236 ALA A O   1 
ATOM   1714 C  CB  . ALA A  1  223 ? 28.109  -4.105  33.471 1.00 33.32  ? 236 ALA A CB  1 
ATOM   1715 N  N   . ALA A  1  224 ? 26.804  -3.485  36.263 1.00 30.83  ? 237 ALA A N   1 
ATOM   1716 C  CA  . ALA A  1  224 ? 26.455  -2.531  37.309 1.00 32.13  ? 237 ALA A CA  1 
ATOM   1717 C  C   . ALA A  1  224 ? 27.007  -2.993  38.656 1.00 30.98  ? 237 ALA A C   1 
ATOM   1718 O  O   . ALA A  1  224 ? 27.491  -2.194  39.456 1.00 29.92  ? 237 ALA A O   1 
ATOM   1719 C  CB  . ALA A  1  224 ? 24.954  -2.348  37.380 1.00 33.62  ? 237 ALA A CB  1 
ATOM   1720 N  N   . SER A  1  225 ? 26.931  -4.297  38.905 1.00 29.54  ? 238 SER A N   1 
ATOM   1721 C  CA  . SER A  1  225 ? 27.347  -4.848  40.176 1.00 31.45  ? 238 SER A CA  1 
ATOM   1722 C  C   . SER A  1  225 ? 28.813  -4.511  40.439 1.00 32.85  ? 238 SER A C   1 
ATOM   1723 O  O   . SER A  1  225 ? 29.166  -4.102  41.537 1.00 34.86  ? 238 SER A O   1 
ATOM   1724 C  CB  . SER A  1  225 ? 27.085  -6.330  40.225 1.00 30.63  ? 238 SER A CB  1 
ATOM   1725 O  OG  . SER A  1  225 ? 27.477  -6.865  41.477 1.00 35.53  ? 238 SER A OG  1 
ATOM   1726 N  N   . ILE A  1  226 ? 29.657  -4.659  39.417 1.00 31.57  ? 239 ILE A N   1 
ATOM   1727 C  CA  . ILE A  1  226 ? 31.088  -4.459  39.563 1.00 31.02  ? 239 ILE A CA  1 
ATOM   1728 C  C   . ILE A  1  226 ? 31.417  -2.966  39.455 1.00 31.28  ? 239 ILE A C   1 
ATOM   1729 O  O   . ILE A  1  226 ? 32.037  -2.415  40.351 1.00 29.95  ? 239 ILE A O   1 
ATOM   1730 C  CB  . ILE A  1  226 ? 31.841  -5.323  38.535 1.00 30.31  ? 239 ILE A CB  1 
ATOM   1731 C  CG1 . ILE A  1  226 ? 31.746  -6.795  38.873 1.00 29.46  ? 239 ILE A CG1 1 
ATOM   1732 C  CG2 . ILE A  1  226 ? 33.297  -4.901  38.381 1.00 30.74  ? 239 ILE A CG2 1 
ATOM   1733 C  CD1 . ILE A  1  226 ? 31.907  -7.693  37.661 1.00 31.34  ? 239 ILE A CD1 1 
ATOM   1734 N  N   . PHE A  1  227 ? 31.002  -2.314  38.361 1.00 31.35  ? 240 PHE A N   1 
ATOM   1735 C  CA  . PHE A  1  227 ? 31.381  -0.936  38.081 1.00 30.67  ? 240 PHE A CA  1 
ATOM   1736 C  C   . PHE A  1  227 ? 30.840  0.045   39.125 1.00 27.89  ? 240 PHE A C   1 
ATOM   1737 O  O   . PHE A  1  227 ? 31.513  1.009   39.474 1.00 29.12  ? 240 PHE A O   1 
ATOM   1738 C  CB  . PHE A  1  227 ? 30.888  -0.486  36.705 1.00 32.30  ? 240 PHE A CB  1 
ATOM   1739 C  CG  . PHE A  1  227 ? 31.743  -0.948  35.536 1.00 35.68  ? 240 PHE A CG  1 
ATOM   1740 C  CD1 . PHE A  1  227 ? 32.946  -0.321  35.247 1.00 38.87  ? 240 PHE A CD1 1 
ATOM   1741 C  CD2 . PHE A  1  227 ? 31.317  -1.965  34.693 1.00 38.20  ? 240 PHE A CD2 1 
ATOM   1742 C  CE1 . PHE A  1  227 ? 33.709  -0.716  34.156 1.00 40.10  ? 240 PHE A CE1 1 
ATOM   1743 C  CE2 . PHE A  1  227 ? 32.086  -2.361  33.611 1.00 38.07  ? 240 PHE A CE2 1 
ATOM   1744 C  CZ  . PHE A  1  227 ? 33.281  -1.741  33.346 1.00 39.73  ? 240 PHE A CZ  1 
ATOM   1745 N  N   . ARG A  1  228 ? 29.608  -0.167  39.585 1.00 26.73  ? 241 ARG A N   1 
ATOM   1746 C  CA  . ARG A  1  228 ? 28.986  0.758   40.517 1.00 26.95  ? 241 ARG A CA  1 
ATOM   1747 C  C   . ARG A  1  228 ? 29.111  0.275   41.966 1.00 26.03  ? 241 ARG A C   1 
ATOM   1748 O  O   . ARG A  1  228 ? 29.446  1.070   42.827 1.00 25.36  ? 241 ARG A O   1 
ATOM   1749 C  CB  . ARG A  1  228 ? 27.508  0.983   40.188 1.00 28.51  ? 241 ARG A CB  1 
ATOM   1750 C  CG  . ARG A  1  228 ? 26.836  1.943   41.165 1.00 29.85  ? 241 ARG A CG  1 
ATOM   1751 C  CD  . ARG A  1  228 ? 25.441  2.401   40.814 1.00 29.57  ? 241 ARG A CD  1 
ATOM   1752 N  NE  . ARG A  1  228 ? 24.484  1.294   40.676 1.00 30.31  ? 241 ARG A NE  1 
ATOM   1753 C  CZ  . ARG A  1  228 ? 23.723  1.035   39.609 1.00 29.88  ? 241 ARG A CZ  1 
ATOM   1754 N  NH1 . ARG A  1  228 ? 23.757  1.806   38.530 1.00 31.67  ? 241 ARG A NH1 1 
ATOM   1755 N  NH2 . ARG A  1  228 ? 22.904  -0.004  39.617 1.00 27.64  ? 241 ARG A NH2 1 
ATOM   1756 N  N   . ASP A  1  229 ? 28.800  -0.996  42.249 1.00 27.70  ? 242 ASP A N   1 
ATOM   1757 C  CA  . ASP A  1  229 ? 28.623  -1.424  43.625 1.00 30.56  ? 242 ASP A CA  1 
ATOM   1758 C  C   . ASP A  1  229 ? 29.861  -2.119  44.194 1.00 30.92  ? 242 ASP A C   1 
ATOM   1759 O  O   . ASP A  1  229 ? 29.892  -2.401  45.388 1.00 32.40  ? 242 ASP A O   1 
ATOM   1760 C  CB  . ASP A  1  229 ? 27.422  -2.332  43.799 1.00 34.78  ? 242 ASP A CB  1 
ATOM   1761 C  CG  . ASP A  1  229 ? 26.056  -1.759  43.479 1.00 36.71  ? 242 ASP A CG  1 
ATOM   1762 O  OD1 . ASP A  1  229 ? 25.822  -0.541  43.705 1.00 37.68  ? 242 ASP A OD1 1 
ATOM   1763 O  OD2 . ASP A  1  229 ? 25.223  -2.581  43.087 1.00 40.04  ? 242 ASP A OD2 1 
ATOM   1764 N  N   . MET A  1  230 ? 30.850  -2.420  43.345 1.00 32.46  ? 243 MET A N   1 
ATOM   1765 C  CA  A MET A  1  230 ? 32.096  -3.053  43.759 0.50 31.86  ? 243 MET A CA  1 
ATOM   1766 C  CA  B MET A  1  230 ? 32.094  -3.058  43.755 0.50 32.24  ? 243 MET A CA  1 
ATOM   1767 C  C   . MET A  1  230 ? 31.825  -4.459  44.294 1.00 31.62  ? 243 MET A C   1 
ATOM   1768 O  O   . MET A  1  230 ? 32.424  -4.870  45.273 1.00 32.79  ? 243 MET A O   1 
ATOM   1769 C  CB  A MET A  1  230 ? 32.802  -2.236  44.847 0.50 32.92  ? 243 MET A CB  1 
ATOM   1770 C  CB  B MET A  1  230 ? 32.805  -2.237  44.832 0.50 33.88  ? 243 MET A CB  1 
ATOM   1771 C  CG  A MET A  1  230 ? 33.030  -0.769  44.518 0.50 33.39  ? 243 MET A CG  1 
ATOM   1772 C  CG  B MET A  1  230 ? 33.144  -0.836  44.389 0.50 34.85  ? 243 MET A CG  1 
ATOM   1773 S  SD  A MET A  1  230 ? 33.292  0.245   45.992 0.50 31.59  ? 243 MET A SD  1 
ATOM   1774 S  SD  B MET A  1  230 ? 34.026  0.098   45.655 0.50 34.29  ? 243 MET A SD  1 
ATOM   1775 C  CE  A MET A  1  230 ? 33.370  1.876   45.227 0.50 28.88  ? 243 MET A CE  1 
ATOM   1776 C  CE  B MET A  1  230 ? 32.740  0.445   46.863 0.50 31.48  ? 243 MET A CE  1 
ATOM   1777 N  N   . ARG A  1  231 ? 30.928  -5.192  43.633 1.00 33.20  ? 244 ARG A N   1 
ATOM   1778 C  CA  . ARG A  1  231 ? 30.438  -6.476  44.104 1.00 32.44  ? 244 ARG A CA  1 
ATOM   1779 C  C   . ARG A  1  231 ? 30.536  -7.512  42.984 1.00 31.23  ? 244 ARG A C   1 
ATOM   1780 O  O   . ARG A  1  231 ? 30.082  -7.277  41.875 1.00 28.82  ? 244 ARG A O   1 
ATOM   1781 C  CB  . ARG A  1  231 ? 28.981  -6.303  44.537 1.00 34.08  ? 244 ARG A CB  1 
ATOM   1782 C  CG  . ARG A  1  231 ? 28.420  -7.467  45.342 1.00 41.28  ? 244 ARG A CG  1 
ATOM   1783 C  CD  . ARG A  1  231 ? 26.984  -7.261  45.800 1.00 46.34  ? 244 ARG A CD  1 
ATOM   1784 N  NE  . ARG A  1  231 ? 26.070  -7.234  44.648 1.00 60.61  ? 244 ARG A NE  1 
ATOM   1785 C  CZ  . ARG A  1  231 ? 25.722  -8.278  43.869 1.00 72.95  ? 244 ARG A CZ  1 
ATOM   1786 N  NH1 . ARG A  1  231 ? 25.995  -9.523  44.236 1.00 83.72  ? 244 ARG A NH1 1 
ATOM   1787 N  NH2 . ARG A  1  231 ? 25.071  -8.082  42.732 1.00 70.23  ? 244 ARG A NH2 1 
ATOM   1788 N  N   . PHE A  1  232 ? 31.129  -8.670  43.283 1.00 31.32  ? 245 PHE A N   1 
ATOM   1789 C  CA  . PHE A  1  232 ? 31.080  -9.793  42.372 1.00 30.02  ? 245 PHE A CA  1 
ATOM   1790 C  C   . PHE A  1  232 ? 29.631  -10.226 42.174 1.00 29.90  ? 245 PHE A C   1 
ATOM   1791 O  O   . PHE A  1  232 ? 28.839  -10.244 43.113 1.00 31.31  ? 245 PHE A O   1 
ATOM   1792 C  CB  . PHE A  1  232 ? 31.815  -11.018 42.903 1.00 30.19  ? 245 PHE A CB  1 
ATOM   1793 C  CG  . PHE A  1  232 ? 33.325  -10.934 42.898 1.00 32.45  ? 245 PHE A CG  1 
ATOM   1794 C  CD1 . PHE A  1  232 ? 34.031  -10.852 41.707 1.00 33.38  ? 245 PHE A CD1 1 
ATOM   1795 C  CD2 . PHE A  1  232 ? 34.041  -10.997 44.087 1.00 35.39  ? 245 PHE A CD2 1 
ATOM   1796 C  CE1 . PHE A  1  232 ? 35.417  -10.807 41.714 1.00 34.08  ? 245 PHE A CE1 1 
ATOM   1797 C  CE2 . PHE A  1  232 ? 35.428  -10.947 44.083 1.00 33.84  ? 245 PHE A CE2 1 
ATOM   1798 C  CZ  . PHE A  1  232 ? 36.113  -10.862 42.901 1.00 32.95  ? 245 PHE A CZ  1 
ATOM   1799 N  N   . PRO A  1  233 ? 29.246  -10.616 40.946 1.00 31.09  ? 246 PRO A N   1 
ATOM   1800 C  CA  . PRO A  1  233 ? 28.008  -11.373 40.750 1.00 32.59  ? 246 PRO A CA  1 
ATOM   1801 C  C   . PRO A  1  233 ? 27.924  -12.572 41.698 1.00 33.76  ? 246 PRO A C   1 
ATOM   1802 O  O   . PRO A  1  233 ? 28.942  -13.094 42.157 1.00 30.78  ? 246 PRO A O   1 
ATOM   1803 C  CB  . PRO A  1  233 ? 28.107  -11.809 39.282 1.00 30.60  ? 246 PRO A CB  1 
ATOM   1804 C  CG  . PRO A  1  233 ? 28.992  -10.771 38.628 1.00 30.42  ? 246 PRO A CG  1 
ATOM   1805 C  CD  . PRO A  1  233 ? 29.956  -10.311 39.692 1.00 30.88  ? 246 PRO A CD  1 
ATOM   1806 N  N   . ASP A  1  234 ? 26.692  -13.002 41.993 1.00 34.40  ? 247 ASP A N   1 
ATOM   1807 C  CA  . ASP A  1  234 ? 26.477  -14.173 42.835 1.00 36.26  ? 247 ASP A CA  1 
ATOM   1808 C  C   . ASP A  1  234 ? 27.126  -15.381 42.163 1.00 32.36  ? 247 ASP A C   1 
ATOM   1809 O  O   . ASP A  1  234 ? 27.036  -15.554 40.962 1.00 34.92  ? 247 ASP A O   1 
ATOM   1810 C  CB  . ASP A  1  234 ? 25.011  -14.421 43.166 1.00 37.94  ? 247 ASP A CB  1 
ATOM   1811 C  CG  . ASP A  1  234 ? 24.292  -13.386 44.026 1.00 40.09  ? 247 ASP A CG  1 
ATOM   1812 O  OD1 . ASP A  1  234 ? 24.936  -12.447 44.558 1.00 39.16  ? 247 ASP A OD1 1 
ATOM   1813 O  OD2 . ASP A  1  234 ? 23.063  -13.520 44.145 1.00 44.96  ? 247 ASP A OD2 1 
ATOM   1814 N  N   . ASP A  1  235 ? 27.834  -16.187 42.943 1.00 32.28  ? 248 ASP A N   1 
ATOM   1815 C  CA  . ASP A  1  235 ? 28.402  -17.437 42.467 1.00 34.95  ? 248 ASP A CA  1 
ATOM   1816 C  C   . ASP A  1  235 ? 29.431  -17.184 41.359 1.00 34.95  ? 248 ASP A C   1 
ATOM   1817 O  O   . ASP A  1  235 ? 29.600  -18.005 40.456 1.00 33.92  ? 248 ASP A O   1 
ATOM   1818 C  CB  . ASP A  1  235 ? 27.304  -18.388 42.026 1.00 36.07  ? 248 ASP A CB  1 
ATOM   1819 C  CG  . ASP A  1  235 ? 27.751  -19.836 41.886 1.00 42.98  ? 248 ASP A CG  1 
ATOM   1820 O  OD1 . ASP A  1  235 ? 28.288  -20.382 42.868 1.00 48.28  ? 248 ASP A OD1 1 
ATOM   1821 O  OD2 . ASP A  1  235 ? 27.583  -20.400 40.787 1.00 46.08  ? 248 ASP A OD2 1 
ATOM   1822 N  N   . PHE A  1  236 ? 30.135  -16.050 41.425 1.00 32.36  ? 249 PHE A N   1 
ATOM   1823 C  CA  . PHE A  1  236 ? 31.045  -15.672 40.358 1.00 31.34  ? 249 PHE A CA  1 
ATOM   1824 C  C   . PHE A  1  236 ? 32.262  -16.582 40.347 1.00 30.58  ? 249 PHE A C   1 
ATOM   1825 O  O   . PHE A  1  236 ? 32.916  -16.770 41.370 1.00 31.95  ? 249 PHE A O   1 
ATOM   1826 C  CB  . PHE A  1  236 ? 31.536  -14.234 40.505 1.00 31.93  ? 249 PHE A CB  1 
ATOM   1827 C  CG  . PHE A  1  236 ? 32.438  -13.792 39.364 1.00 32.24  ? 249 PHE A CG  1 
ATOM   1828 C  CD1 . PHE A  1  236 ? 31.914  -13.522 38.107 1.00 32.38  ? 249 PHE A CD1 1 
ATOM   1829 C  CD2 . PHE A  1  236 ? 33.798  -13.608 39.567 1.00 31.52  ? 249 PHE A CD2 1 
ATOM   1830 C  CE1 . PHE A  1  236 ? 32.741  -13.124 37.074 1.00 35.01  ? 249 PHE A CE1 1 
ATOM   1831 C  CE2 . PHE A  1  236 ? 34.623  -13.199 38.534 1.00 32.44  ? 249 PHE A CE2 1 
ATOM   1832 C  CZ  . PHE A  1  236 ? 34.096  -12.951 37.294 1.00 35.10  ? 249 PHE A CZ  1 
ATOM   1833 N  N   . HIS A  1  237 ? 32.543  -17.128 39.162 1.00 31.79  ? 250 HIS A N   1 
ATOM   1834 C  CA  . HIS A  1  237 ? 33.726  -17.932 38.909 1.00 32.03  ? 250 HIS A CA  1 
ATOM   1835 C  C   . HIS A  1  237 ? 34.639  -17.156 37.965 1.00 32.48  ? 250 HIS A C   1 
ATOM   1836 O  O   . HIS A  1  237 ? 34.198  -16.713 36.907 1.00 33.70  ? 250 HIS A O   1 
ATOM   1837 C  CB  . HIS A  1  237 ? 33.359  -19.291 38.297 1.00 31.54  ? 250 HIS A CB  1 
ATOM   1838 C  CG  . HIS A  1  237 ? 32.722  -20.249 39.235 1.00 32.39  ? 250 HIS A CG  1 
ATOM   1839 N  ND1 . HIS A  1  237 ? 31.681  -19.893 40.064 1.00 36.42  ? 250 HIS A ND1 1 
ATOM   1840 C  CD2 . HIS A  1  237 ? 32.972  -21.549 39.470 1.00 32.40  ? 250 HIS A CD2 1 
ATOM   1841 C  CE1 . HIS A  1  237 ? 31.330  -20.950 40.787 1.00 36.99  ? 250 HIS A CE1 1 
ATOM   1842 N  NE2 . HIS A  1  237 ? 32.109  -21.965 40.448 1.00 34.89  ? 250 HIS A NE2 1 
ATOM   1843 N  N   . ARG A  1  238 ? 35.914  -17.026 38.342 1.00 32.42  ? 251 ARG A N   1 
ATOM   1844 C  CA  . ARG A  1  238 ? 36.884  -16.302 37.535 1.00 32.65  ? 251 ARG A CA  1 
ATOM   1845 C  C   . ARG A  1  238 ? 37.177  -17.036 36.228 1.00 31.16  ? 251 ARG A C   1 
ATOM   1846 O  O   . ARG A  1  238 ? 36.865  -18.217 36.085 1.00 29.86  ? 251 ARG A O   1 
ATOM   1847 C  CB  . ARG A  1  238 ? 38.191  -16.145 38.312 1.00 35.47  ? 251 ARG A CB  1 
ATOM   1848 C  CG  . ARG A  1  238 ? 38.942  -17.459 38.479 1.00 36.30  ? 251 ARG A CG  1 
ATOM   1849 C  CD  . ARG A  1  238 ? 40.203  -17.318 39.320 1.00 37.79  ? 251 ARG A CD  1 
ATOM   1850 N  NE  . ARG A  1  238 ? 41.044  -18.500 39.119 1.00 36.51  ? 251 ARG A NE  1 
ATOM   1851 C  CZ  . ARG A  1  238 ? 42.153  -18.799 39.783 1.00 38.20  ? 251 ARG A CZ  1 
ATOM   1852 N  NH1 . ARG A  1  238 ? 42.663  -17.940 40.657 1.00 38.06  ? 251 ARG A NH1 1 
ATOM   1853 N  NH2 . ARG A  1  238 ? 42.752  -19.956 39.552 1.00 34.48  ? 251 ARG A NH2 1 
ATOM   1854 N  N   . SER A  1  239 ? 37.807  -16.301 35.298 1.00 31.71  ? 252 SER A N   1 
ATOM   1855 C  CA  . SER A  1  239 ? 38.313  -16.820 34.031 1.00 29.58  ? 252 SER A CA  1 
ATOM   1856 C  C   . SER A  1  239 ? 39.052  -18.147 34.220 1.00 31.98  ? 252 SER A C   1 
ATOM   1857 O  O   . SER A  1  239 ? 39.748  -18.349 35.207 1.00 33.73  ? 252 SER A O   1 
ATOM   1858 C  CB  . SER A  1  239 ? 39.225  -15.796 33.402 1.00 28.20  ? 252 SER A CB  1 
ATOM   1859 O  OG  . SER A  1  239 ? 39.870  -16.284 32.237 1.00 28.95  ? 252 SER A OG  1 
ATOM   1860 N  N   . ALA A  1  240 ? 38.897  -19.056 33.256 1.00 35.38  ? 253 ALA A N   1 
ATOM   1861 C  CA  . ALA A  1  240 ? 39.438  -20.404 33.365 1.00 37.37  ? 253 ALA A CA  1 
ATOM   1862 C  C   . ALA A  1  240 ? 40.912  -20.429 32.979 1.00 35.23  ? 253 ALA A C   1 
ATOM   1863 O  O   . ALA A  1  240 ? 41.578  -21.432 33.221 1.00 36.16  ? 253 ALA A O   1 
ATOM   1864 C  CB  . ALA A  1  240 ? 38.658  -21.346 32.481 1.00 39.97  ? 253 ALA A CB  1 
ATOM   1865 N  N   . VAL A  1  241 ? 41.384  -19.348 32.350 1.00 34.75  ? 254 VAL A N   1 
ATOM   1866 C  CA  . VAL A  1  241 ? 42.789  -19.177 32.020 1.00 36.24  ? 254 VAL A CA  1 
ATOM   1867 C  C   . VAL A  1  241 ? 43.233  -17.793 32.476 1.00 36.06  ? 254 VAL A C   1 
ATOM   1868 O  O   . VAL A  1  241 ? 42.434  -16.859 32.503 1.00 37.64  ? 254 VAL A O   1 
ATOM   1869 C  CB  . VAL A  1  241 ? 43.031  -19.335 30.508 1.00 37.20  ? 254 VAL A CB  1 
ATOM   1870 C  CG1 . VAL A  1  241 ? 42.644  -20.726 30.020 1.00 37.99  ? 254 VAL A CG1 1 
ATOM   1871 C  CG2 . VAL A  1  241 ? 42.302  -18.278 29.690 1.00 34.34  ? 254 VAL A CG2 1 
ATOM   1872 N  N   . PRO A  1  242 ? 44.526  -17.599 32.808 1.00 36.08  ? 255 PRO A N   1 
ATOM   1873 C  CA  . PRO A  1  242 ? 45.056  -16.258 33.051 1.00 33.64  ? 255 PRO A CA  1 
ATOM   1874 C  C   . PRO A  1  242 ? 44.777  -15.395 31.834 1.00 32.44  ? 255 PRO A C   1 
ATOM   1875 O  O   . PRO A  1  242 ? 44.965  -15.861 30.716 1.00 34.31  ? 255 PRO A O   1 
ATOM   1876 C  CB  . PRO A  1  242 ? 46.541  -16.515 33.252 1.00 35.58  ? 255 PRO A CB  1 
ATOM   1877 C  CG  . PRO A  1  242 ? 46.584  -17.936 33.793 1.00 35.66  ? 255 PRO A CG  1 
ATOM   1878 C  CD  . PRO A  1  242 ? 45.530  -18.656 32.980 1.00 35.78  ? 255 PRO A CD  1 
ATOM   1879 N  N   . ALA A  1  243 ? 44.289  -14.170 32.048 1.00 31.05  ? 256 ALA A N   1 
ATOM   1880 C  CA  . ALA A  1  243 ? 43.948  -13.313 30.923 1.00 32.16  ? 256 ALA A CA  1 
ATOM   1881 C  C   . ALA A  1  243 ? 44.221  -11.851 31.240 1.00 31.39  ? 256 ALA A C   1 
ATOM   1882 O  O   . ALA A  1  243 ? 44.506  -11.486 32.371 1.00 34.21  ? 256 ALA A O   1 
ATOM   1883 C  CB  . ALA A  1  243 ? 42.500  -13.512 30.534 1.00 33.61  ? 256 ALA A CB  1 
ATOM   1884 N  N   . SER A  1  244 ? 44.120  -11.024 30.208 1.00 31.93  ? 257 SER A N   1 
ATOM   1885 C  CA  . SER A  1  244 ? 44.276  -9.589  30.337 1.00 33.79  ? 257 SER A CA  1 
ATOM   1886 C  C   . SER A  1  244 ? 43.603  -8.905  29.151 1.00 33.99  ? 257 SER A C   1 
ATOM   1887 O  O   . SER A  1  244 ? 42.382  -8.782  29.132 1.00 32.96  ? 257 SER A O   1 
ATOM   1888 C  CB  . SER A  1  244 ? 45.723  -9.223  30.464 1.00 33.93  ? 257 SER A CB  1 
ATOM   1889 O  OG  . SER A  1  244 ? 46.465  -9.791  29.393 1.00 34.89  ? 257 SER A OG  1 
ATOM   1890 N  N   . ASN A  1  245 ? 44.392  -8.539  28.136 1.00 35.20  ? 258 ASN A N   1 
ATOM   1891 C  CA  . ASN A  1  245 ? 43.967  -7.560  27.146 1.00 38.59  ? 258 ASN A CA  1 
ATOM   1892 C  C   . ASN A  1  245 ? 43.757  -8.201  25.767 1.00 38.86  ? 258 ASN A C   1 
ATOM   1893 O  O   . ASN A  1  245 ? 43.910  -7.523  24.751 1.00 39.50  ? 258 ASN A O   1 
ATOM   1894 C  CB  . ASN A  1  245 ? 44.959  -6.400  27.078 1.00 39.60  ? 258 ASN A CB  1 
ATOM   1895 C  CG  . ASN A  1  245 ? 46.294  -6.812  26.497 1.00 43.35  ? 258 ASN A CG  1 
ATOM   1896 O  OD1 . ASN A  1  245 ? 46.642  -7.997  26.506 1.00 46.36  ? 258 ASN A OD1 1 
ATOM   1897 N  ND2 . ASN A  1  245 ? 47.080  -5.860  26.016 1.00 48.12  ? 258 ASN A ND2 1 
ATOM   1898 N  N   . GLU A  1  246 ? 43.382  -9.489  25.731 1.00 35.91  ? 259 GLU A N   1 
ATOM   1899 C  CA  . GLU A  1  246 ? 43.060  -10.155 24.480 1.00 36.16  ? 259 GLU A CA  1 
ATOM   1900 C  C   . GLU A  1  246 ? 41.894  -9.427  23.815 1.00 35.98  ? 259 GLU A C   1 
ATOM   1901 O  O   . GLU A  1  246 ? 40.863  -9.218  24.449 1.00 34.09  ? 259 GLU A O   1 
ATOM   1902 C  CB  . GLU A  1  246 ? 42.674  -11.618 24.698 1.00 40.00  ? 259 GLU A CB  1 
ATOM   1903 C  CG  . GLU A  1  246 ? 43.819  -12.485 25.219 1.00 45.93  ? 259 GLU A CG  1 
ATOM   1904 C  CD  . GLU A  1  246 ? 44.145  -12.402 26.709 1.00 49.97  ? 259 GLU A CD  1 
ATOM   1905 O  OE1 . GLU A  1  246 ? 43.501  -11.602 27.419 1.00 48.51  ? 259 GLU A OE1 1 
ATOM   1906 O  OE2 . GLU A  1  246 ? 45.017  -13.177 27.170 1.00 48.92  ? 259 GLU A OE2 1 
ATOM   1907 N  N   . GLY A  1  247 ? 42.081  -9.038  22.542 1.00 34.49  ? 260 GLY A N   1 
ATOM   1908 C  CA  . GLY A  1  247 ? 41.041  -8.395  21.761 1.00 33.47  ? 260 GLY A CA  1 
ATOM   1909 C  C   . GLY A  1  247 ? 41.271  -6.894  21.605 1.00 36.74  ? 260 GLY A C   1 
ATOM   1910 O  O   . GLY A  1  247 ? 40.587  -6.255  20.813 1.00 36.91  ? 260 GLY A O   1 
ATOM   1911 N  N   . ALA A  1  248 ? 42.234  -6.328  22.343 1.00 39.71  ? 261 ALA A N   1 
ATOM   1912 C  CA  . ALA A  1  248 ? 42.477  -4.890  22.303 1.00 40.50  ? 261 ALA A CA  1 
ATOM   1913 C  C   . ALA A  1  248 ? 42.916  -4.431  20.910 1.00 40.65  ? 261 ALA A C   1 
ATOM   1914 O  O   . ALA A  1  248 ? 42.575  -3.329  20.494 1.00 39.41  ? 261 ALA A O   1 
ATOM   1915 C  CB  . ALA A  1  248 ? 43.492  -4.516  23.362 1.00 40.13  ? 261 ALA A CB  1 
ATOM   1916 N  N   . ASP A  1  249 ? 43.675  -5.276  20.204 1.00 43.76  ? 262 ASP A N   1 
ATOM   1917 C  CA  . ASP A  1  249 ? 44.049  -5.058  18.810 1.00 51.86  ? 262 ASP A CA  1 
ATOM   1918 C  C   . ASP A  1  249 ? 42.813  -4.801  17.938 1.00 48.84  ? 262 ASP A C   1 
ATOM   1919 O  O   . ASP A  1  249 ? 42.812  -3.901  17.099 1.00 46.90  ? 262 ASP A O   1 
ATOM   1920 C  CB  . ASP A  1  249 ? 44.898  -6.209  18.269 1.00 59.58  ? 262 ASP A CB  1 
ATOM   1921 C  CG  . ASP A  1  249 ? 44.380  -7.631  18.497 1.00 70.95  ? 262 ASP A CG  1 
ATOM   1922 O  OD1 . ASP A  1  249 ? 43.334  -7.800  19.176 1.00 72.74  ? 262 ASP A OD1 1 
ATOM   1923 O  OD2 . ASP A  1  249 ? 45.022  -8.575  17.988 1.00 76.81  ? 262 ASP A OD2 1 
ATOM   1924 N  N   . GLN A  1  250 ? 41.756  -5.601  18.132 1.00 43.50  ? 263 GLN A N   1 
ATOM   1925 C  CA  . GLN A  1  250 ? 40.554  -5.504  17.320 1.00 40.66  ? 263 GLN A CA  1 
ATOM   1926 C  C   . GLN A  1  250 ? 39.768  -4.235  17.635 1.00 39.99  ? 263 GLN A C   1 
ATOM   1927 O  O   . GLN A  1  250 ? 39.141  -3.679  16.745 1.00 40.46  ? 263 GLN A O   1 
ATOM   1928 C  CB  . GLN A  1  250 ? 39.672  -6.734  17.510 1.00 39.45  ? 263 GLN A CB  1 
ATOM   1929 C  CG  . GLN A  1  250 ? 40.294  -8.000  16.926 1.00 42.22  ? 263 GLN A CG  1 
ATOM   1930 C  CD  . GLN A  1  250 ? 39.466  -9.241  17.185 1.00 45.06  ? 263 GLN A CD  1 
ATOM   1931 O  OE1 . GLN A  1  250 ? 38.273  -9.281  16.876 1.00 47.69  ? 263 GLN A OE1 1 
ATOM   1932 N  NE2 . GLN A  1  250 ? 40.061  -10.254 17.802 1.00 46.61  ? 263 GLN A NE2 1 
ATOM   1933 N  N   . VAL A  1  251 ? 39.799  -3.789  18.893 1.00 38.40  ? 264 VAL A N   1 
ATOM   1934 C  CA  . VAL A  1  251 ? 39.099  -2.582  19.299 1.00 37.42  ? 264 VAL A CA  1 
ATOM   1935 C  C   . VAL A  1  251 ? 39.691  -1.368  18.587 1.00 38.46  ? 264 VAL A C   1 
ATOM   1936 O  O   . VAL A  1  251 ? 38.955  -0.469  18.182 1.00 44.53  ? 264 VAL A O   1 
ATOM   1937 C  CB  . VAL A  1  251 ? 39.143  -2.416  20.828 1.00 35.95  ? 264 VAL A CB  1 
ATOM   1938 C  CG1 . VAL A  1  251 ? 38.649  -1.053  21.285 1.00 36.11  ? 264 VAL A CG1 1 
ATOM   1939 C  CG2 . VAL A  1  251 ? 38.351  -3.505  21.520 1.00 36.36  ? 264 VAL A CG2 1 
ATOM   1940 N  N   . LEU A  1  252 ? 41.021  -1.333  18.466 1.00 42.56  ? 265 LEU A N   1 
ATOM   1941 C  CA  . LEU A  1  252 ? 41.701  -0.258  17.760 1.00 44.59  ? 265 LEU A CA  1 
ATOM   1942 C  C   . LEU A  1  252 ? 41.415  -0.339  16.261 1.00 41.99  ? 265 LEU A C   1 
ATOM   1943 O  O   . LEU A  1  252 ? 41.264  0.690   15.605 1.00 47.39  ? 265 LEU A O   1 
ATOM   1944 C  CB  . LEU A  1  252 ? 43.201  -0.323  18.029 1.00 45.82  ? 265 LEU A CB  1 
ATOM   1945 C  CG  . LEU A  1  252 ? 44.047  0.787   17.390 1.00 46.40  ? 265 LEU A CG  1 
ATOM   1946 C  CD1 . LEU A  1  252 ? 43.763  2.171   17.978 1.00 44.54  ? 265 LEU A CD1 1 
ATOM   1947 C  CD2 . LEU A  1  252 ? 45.530  0.434   17.505 1.00 43.20  ? 265 LEU A CD2 1 
ATOM   1948 N  N   . ALA A  1  253 ? 41.346  -1.560  15.725 1.00 38.67  ? 266 ALA A N   1 
ATOM   1949 C  CA  . ALA A  1  253 ? 41.171  -1.758  14.296 1.00 41.72  ? 266 ALA A CA  1 
ATOM   1950 C  C   . ALA A  1  253 ? 39.815  -1.229  13.836 1.00 45.39  ? 266 ALA A C   1 
ATOM   1951 O  O   . ALA A  1  253 ? 39.697  -0.721  12.727 1.00 50.28  ? 266 ALA A O   1 
ATOM   1952 C  CB  . ALA A  1  253 ? 41.342  -3.223  13.941 1.00 42.28  ? 266 ALA A CB  1 
ATOM   1953 N  N   . ALA A  1  254 ? 38.800  -1.338  14.697 1.00 48.31  ? 267 ALA A N   1 
ATOM   1954 C  CA  . ALA A  1  254 ? 37.438  -0.938  14.374 1.00 45.88  ? 267 ALA A CA  1 
ATOM   1955 C  C   . ALA A  1  254 ? 37.333  0.563   14.107 1.00 46.14  ? 267 ALA A C   1 
ATOM   1956 O  O   . ALA A  1  254 ? 36.457  0.968   13.348 1.00 50.35  ? 267 ALA A O   1 
ATOM   1957 C  CB  . ALA A  1  254 ? 36.511  -1.355  15.500 1.00 46.00  ? 267 ALA A CB  1 
ATOM   1958 N  N   . HIS A  1  255 ? 38.172  1.379   14.763 1.00 45.46  ? 268 HIS A N   1 
ATOM   1959 C  CA  . HIS A  1  255 ? 38.235  2.814   14.508 1.00 49.25  ? 268 HIS A CA  1 
ATOM   1960 C  C   . HIS A  1  255 ? 39.659  3.317   14.739 1.00 47.81  ? 268 HIS A C   1 
ATOM   1961 O  O   . HIS A  1  255 ? 39.962  3.878   15.793 1.00 53.94  ? 268 HIS A O   1 
ATOM   1962 C  CB  . HIS A  1  255 ? 37.237  3.608   15.361 1.00 50.52  ? 268 HIS A CB  1 
ATOM   1963 C  CG  . HIS A  1  255 ? 35.808  3.349   15.034 1.00 55.69  ? 268 HIS A CG  1 
ATOM   1964 N  ND1 . HIS A  1  255 ? 35.180  3.968   13.979 1.00 60.59  ? 268 HIS A ND1 1 
ATOM   1965 C  CD2 . HIS A  1  255 ? 34.893  2.545   15.596 1.00 57.79  ? 268 HIS A CD2 1 
ATOM   1966 C  CE1 . HIS A  1  255 ? 33.923  3.549   13.924 1.00 65.47  ? 268 HIS A CE1 1 
ATOM   1967 N  NE2 . HIS A  1  255 ? 33.727  2.690   14.905 1.00 57.81  ? 268 HIS A NE2 1 
ATOM   1968 N  N   . PRO A  1  256 ? 40.565  3.124   13.753 1.00 45.56  ? 269 PRO A N   1 
ATOM   1969 C  CA  . PRO A  1  256 ? 41.974  3.500   13.900 1.00 43.76  ? 269 PRO A CA  1 
ATOM   1970 C  C   . PRO A  1  256 ? 42.120  4.915   14.441 1.00 41.52  ? 269 PRO A C   1 
ATOM   1971 O  O   . PRO A  1  256 ? 41.381  5.816   14.053 1.00 41.21  ? 269 PRO A O   1 
ATOM   1972 C  CB  . PRO A  1  256 ? 42.524  3.362   12.482 1.00 44.17  ? 269 PRO A CB  1 
ATOM   1973 C  CG  . PRO A  1  256 ? 41.657  2.283   11.867 1.00 44.59  ? 269 PRO A CG  1 
ATOM   1974 C  CD  . PRO A  1  256 ? 40.273  2.506   12.451 1.00 42.03  ? 269 PRO A CD  1 
ATOM   1975 N  N   . TRP A  1  257 ? 43.065  5.085   15.368 1.00 40.99  ? 270 TRP A N   1 
ATOM   1976 C  CA  . TRP A  1  257 ? 43.209  6.339   16.084 1.00 38.87  ? 270 TRP A CA  1 
ATOM   1977 C  C   . TRP A  1  257 ? 44.665  6.547   16.499 1.00 39.48  ? 270 TRP A C   1 
ATOM   1978 O  O   . TRP A  1  257 ? 45.415  5.600   16.711 1.00 40.03  ? 270 TRP A O   1 
ATOM   1979 C  CB  . TRP A  1  257 ? 42.252  6.386   17.286 1.00 35.75  ? 270 TRP A CB  1 
ATOM   1980 C  CG  . TRP A  1  257 ? 42.146  7.760   17.881 1.00 34.21  ? 270 TRP A CG  1 
ATOM   1981 C  CD1 . TRP A  1  257 ? 42.822  8.219   18.963 1.00 37.71  ? 270 TRP A CD1 1 
ATOM   1982 C  CD2 . TRP A  1  257 ? 41.394  8.880   17.370 1.00 35.59  ? 270 TRP A CD2 1 
ATOM   1983 N  NE1 . TRP A  1  257 ? 42.526  9.535   19.179 1.00 40.04  ? 270 TRP A NE1 1 
ATOM   1984 C  CE2 . TRP A  1  257 ? 41.664  9.971   18.215 1.00 35.15  ? 270 TRP A CE2 1 
ATOM   1985 C  CE3 . TRP A  1  257 ? 40.528  9.069   16.283 1.00 40.14  ? 270 TRP A CE3 1 
ATOM   1986 C  CZ2 . TRP A  1  257 ? 41.104  11.228  18.017 1.00 37.95  ? 270 TRP A CZ2 1 
ATOM   1987 C  CZ3 . TRP A  1  257 ? 39.982  10.318  16.075 1.00 38.58  ? 270 TRP A CZ3 1 
ATOM   1988 C  CH2 . TRP A  1  257 ? 40.275  11.385  16.928 1.00 39.34  ? 270 TRP A CH2 1 
ATOM   1989 N  N   . VAL A  1  258 ? 45.051  7.816   16.602 1.00 42.79  ? 271 VAL A N   1 
ATOM   1990 C  CA  . VAL A  1  258 ? 46.435  8.200   16.788 1.00 44.26  ? 271 VAL A CA  1 
ATOM   1991 C  C   . VAL A  1  258 ? 46.536  9.023   18.069 1.00 42.02  ? 271 VAL A C   1 
ATOM   1992 O  O   . VAL A  1  258 ? 45.693  9.876   18.328 1.00 42.98  ? 271 VAL A O   1 
ATOM   1993 C  CB  . VAL A  1  258 ? 46.890  8.976   15.531 1.00 47.07  ? 271 VAL A CB  1 
ATOM   1994 C  CG1 . VAL A  1  258 ? 48.248  9.639   15.692 1.00 52.66  ? 271 VAL A CG1 1 
ATOM   1995 C  CG2 . VAL A  1  258 ? 46.912  8.076   14.305 1.00 46.24  ? 271 VAL A CG2 1 
ATOM   1996 N  N   . PRO A  1  259 ? 47.554  8.772   18.917 1.00 39.35  ? 272 PRO A N   1 
ATOM   1997 C  CA  . PRO A  1  259 ? 47.717  9.517   20.160 1.00 40.66  ? 272 PRO A CA  1 
ATOM   1998 C  C   . PRO A  1  259 ? 47.822  11.016  19.915 1.00 41.54  ? 272 PRO A C   1 
ATOM   1999 O  O   . PRO A  1  259 ? 48.338  11.441  18.892 1.00 50.34  ? 272 PRO A O   1 
ATOM   2000 C  CB  . PRO A  1  259 ? 49.006  8.937   20.798 1.00 43.07  ? 272 PRO A CB  1 
ATOM   2001 C  CG  . PRO A  1  259 ? 49.681  8.171   19.691 1.00 43.42  ? 272 PRO A CG  1 
ATOM   2002 C  CD  . PRO A  1  259 ? 48.573  7.726   18.744 1.00 41.22  ? 272 PRO A CD  1 
ATOM   2003 N  N   . GLY A  1  260 ? 47.349  11.804  20.884 1.00 43.98  ? 273 GLY A N   1 
ATOM   2004 C  CA  . GLY A  1  260 ? 47.404  13.252  20.796 1.00 44.94  ? 273 GLY A CA  1 
ATOM   2005 C  C   . GLY A  1  260 ? 46.519  13.902  21.854 1.00 48.05  ? 273 GLY A C   1 
ATOM   2006 O  O   . GLY A  1  260 ? 46.290  13.323  22.911 1.00 45.26  ? 273 GLY A O   1 
ATOM   2007 N  N   . GLY A  1  261 ? 46.012  15.100  21.545 1.00 52.15  ? 274 GLY A N   1 
ATOM   2008 C  CA  . GLY A  1  261 ? 45.172  15.838  22.469 1.00 52.82  ? 274 GLY A CA  1 
ATOM   2009 C  C   . GLY A  1  261 ? 44.637  17.127  21.849 1.00 55.50  ? 274 GLY A C   1 
ATOM   2010 O  O   . GLY A  1  261 ? 45.033  17.513  20.749 1.00 53.83  ? 274 GLY A O   1 
ATOM   2011 N  N   . ASN A  1  262 ? 43.704  17.769  22.568 1.00 50.02  ? 275 ASN A N   1 
ATOM   2012 C  CA  . ASN A  1  262 ? 43.238  19.096  22.215 1.00 48.16  ? 275 ASN A CA  1 
ATOM   2013 C  C   . ASN A  1  262 ? 44.364  20.088  22.506 1.00 53.89  ? 275 ASN A C   1 
ATOM   2014 O  O   . ASN A  1  262 ? 44.881  20.106  23.619 1.00 57.34  ? 275 ASN A O   1 
ATOM   2015 C  CB  . ASN A  1  262 ? 41.969  19.459  22.979 1.00 44.60  ? 275 ASN A CB  1 
ATOM   2016 C  CG  . ASN A  1  262 ? 40.704  18.948  22.324 1.00 45.68  ? 275 ASN A CG  1 
ATOM   2017 O  OD1 . ASN A  1  262 ? 40.705  18.624  21.132 1.00 46.49  ? 275 ASN A OD1 1 
ATOM   2018 N  ND2 . ASN A  1  262 ? 39.609  18.864  23.073 1.00 46.09  ? 275 ASN A ND2 1 
ATOM   2019 N  N   . ALA A  1  263 ? 44.713  20.924  21.515 1.00 55.47  ? 276 ALA A N   1 
ATOM   2020 C  CA  . ALA A  1  263 ? 45.753  21.929  21.672 1.00 55.00  ? 276 ALA A CA  1 
ATOM   2021 C  C   . ALA A  1  263 ? 45.154  23.281  22.061 1.00 55.07  ? 276 ALA A C   1 
ATOM   2022 O  O   . ALA A  1  263 ? 43.994  23.569  21.760 1.00 52.01  ? 276 ALA A O   1 
ATOM   2023 C  CB  . ALA A  1  263 ? 46.539  22.032  20.385 1.00 57.37  ? 276 ALA A CB  1 
ATOM   2024 N  N   . ASP A  1  264 ? 45.963  24.100  22.747 1.00 61.13  ? 277 ASP A N   1 
ATOM   2025 C  CA  . ASP A  1  264 ? 45.673  25.506  23.010 1.00 71.80  ? 277 ASP A CA  1 
ATOM   2026 C  C   . ASP A  1  264 ? 44.353  25.683  23.758 1.00 68.73  ? 277 ASP A C   1 
ATOM   2027 O  O   . ASP A  1  264 ? 43.608  26.610  23.464 1.00 66.05  ? 277 ASP A O   1 
ATOM   2028 C  CB  . ASP A  1  264 ? 45.696  26.338  21.734 1.00 80.95  ? 277 ASP A CB  1 
ATOM   2029 C  CG  . ASP A  1  264 ? 47.004  26.306  20.955 1.00 93.22  ? 277 ASP A CG  1 
ATOM   2030 O  OD1 . ASP A  1  264 ? 48.062  26.564  21.571 1.00 102.90 ? 277 ASP A OD1 1 
ATOM   2031 O  OD2 . ASP A  1  264 ? 46.957  26.011  19.740 1.00 94.25  ? 277 ASP A OD2 1 
ATOM   2032 N  N   . ASN A  1  265 ? 44.076  24.792  24.719 1.00 71.89  ? 278 ASN A N   1 
ATOM   2033 C  CA  . ASN A  1  265 ? 42.977  24.955  25.653 1.00 69.62  ? 278 ASN A CA  1 
ATOM   2034 C  C   . ASN A  1  265 ? 41.658  25.189  24.911 1.00 58.01  ? 278 ASN A C   1 
ATOM   2035 O  O   . ASN A  1  265 ? 40.849  26.005  25.333 1.00 57.04  ? 278 ASN A O   1 
ATOM   2036 C  CB  . ASN A  1  265 ? 43.311  26.071  26.641 1.00 73.31  ? 278 ASN A CB  1 
ATOM   2037 C  CG  . ASN A  1  265 ? 42.551  25.931  27.938 1.00 85.92  ? 278 ASN A CG  1 
ATOM   2038 O  OD1 . ASN A  1  265 ? 42.544  24.848  28.536 1.00 94.93  ? 278 ASN A OD1 1 
ATOM   2039 N  ND2 . ASN A  1  265 ? 41.904  26.998  28.384 1.00 93.53  ? 278 ASN A ND2 1 
ATOM   2040 N  N   . GLN A  1  266 ? 41.431  24.448  23.823 1.00 55.62  ? 279 GLN A N   1 
ATOM   2041 C  CA  . GLN A  1  266 ? 40.224  24.581  23.019 1.00 60.44  ? 279 GLN A CA  1 
ATOM   2042 C  C   . GLN A  1  266 ? 39.632  23.218  22.670 1.00 56.57  ? 279 GLN A C   1 
ATOM   2043 O  O   . GLN A  1  266 ? 40.371  22.265  22.463 1.00 61.00  ? 279 GLN A O   1 
ATOM   2044 C  CB  . GLN A  1  266 ? 40.549  25.228  21.675 1.00 70.38  ? 279 GLN A CB  1 
ATOM   2045 C  CG  . GLN A  1  266 ? 40.688  26.744  21.737 1.00 77.92  ? 279 GLN A CG  1 
ATOM   2046 C  CD  . GLN A  1  266 ? 41.072  27.335  20.400 1.00 83.06  ? 279 GLN A CD  1 
ATOM   2047 O  OE1 . GLN A  1  266 ? 41.384  26.615  19.440 1.00 78.52  ? 279 GLN A OE1 1 
ATOM   2048 N  NE2 . GLN A  1  266 ? 41.025  28.657  20.320 1.00 88.32  ? 279 GLN A NE2 1 
ATOM   2049 N  N   . VAL A  1  267 ? 38.305  23.159  22.509 1.00 49.86  ? 280 VAL A N   1 
ATOM   2050 C  CA  . VAL A  1  267 ? 37.637  21.929  22.101 1.00 51.17  ? 280 VAL A CA  1 
ATOM   2051 C  C   . VAL A  1  267 ? 37.727  21.760  20.581 1.00 51.79  ? 280 VAL A C   1 
ATOM   2052 O  O   . VAL A  1  267 ? 38.217  22.635  19.879 1.00 59.30  ? 280 VAL A O   1 
ATOM   2053 C  CB  . VAL A  1  267 ? 36.180  21.887  22.602 1.00 56.53  ? 280 VAL A CB  1 
ATOM   2054 C  CG1 . VAL A  1  267 ? 36.115  21.806  24.120 1.00 59.37  ? 280 VAL A CG1 1 
ATOM   2055 C  CG2 . VAL A  1  267 ? 35.363  23.076  22.113 1.00 59.97  ? 280 VAL A CG2 1 
ATOM   2056 N  N   . ASN A  1  268 ? 37.283  20.595  20.096 1.00 50.32  ? 281 ASN A N   1 
ATOM   2057 C  CA  . ASN A  1  268 ? 37.327  20.200  18.694 1.00 54.68  ? 281 ASN A CA  1 
ATOM   2058 C  C   . ASN A  1  268 ? 38.620  20.636  18.005 1.00 51.45  ? 281 ASN A C   1 
ATOM   2059 O  O   . ASN A  1  268 ? 38.588  21.109  16.878 1.00 53.48  ? 281 ASN A O   1 
ATOM   2060 C  CB  . ASN A  1  268 ? 36.097  20.680  17.934 1.00 54.44  ? 281 ASN A CB  1 
ATOM   2061 C  CG  . ASN A  1  268 ? 34.833  20.069  18.486 1.00 54.06  ? 281 ASN A CG  1 
ATOM   2062 O  OD1 . ASN A  1  268 ? 34.547  18.887  18.259 1.00 59.24  ? 281 ASN A OD1 1 
ATOM   2063 N  ND2 . ASN A  1  268 ? 34.065  20.861  19.212 1.00 53.82  ? 281 ASN A ND2 1 
ATOM   2064 N  N   . ASN A  1  269 ? 39.755  20.379  18.652 1.00 51.43  ? 282 ASN A N   1 
ATOM   2065 C  CA  . ASN A  1  269 ? 41.038  20.871  18.181 1.00 52.52  ? 282 ASN A CA  1 
ATOM   2066 C  C   . ASN A  1  269 ? 42.123  19.815  18.416 1.00 46.51  ? 282 ASN A C   1 
ATOM   2067 O  O   . ASN A  1  269 ? 43.181  20.097  18.984 1.00 44.34  ? 282 ASN A O   1 
ATOM   2068 C  CB  . ASN A  1  269 ? 41.355  22.206  18.849 1.00 57.17  ? 282 ASN A CB  1 
ATOM   2069 C  CG  . ASN A  1  269 ? 42.528  22.904  18.204 1.00 57.92  ? 282 ASN A CG  1 
ATOM   2070 O  OD1 . ASN A  1  269 ? 42.775  22.727  17.004 1.00 50.41  ? 282 ASN A OD1 1 
ATOM   2071 N  ND2 . ASN A  1  269 ? 43.252  23.694  18.987 1.00 61.47  ? 282 ASN A ND2 1 
ATOM   2072 N  N   . TYR A  1  270 ? 41.865  18.592  17.949 1.00 42.87  ? 283 TYR A N   1 
ATOM   2073 C  CA  . TYR A  1  270 ? 42.731  17.468  18.263 1.00 45.56  ? 283 TYR A CA  1 
ATOM   2074 C  C   . TYR A  1  270 ? 43.941  17.471  17.327 1.00 44.70  ? 283 TYR A C   1 
ATOM   2075 O  O   . TYR A  1  270 ? 43.797  17.468  16.111 1.00 40.52  ? 283 TYR A O   1 
ATOM   2076 C  CB  . TYR A  1  270 ? 41.918  16.168  18.200 1.00 46.35  ? 283 TYR A CB  1 
ATOM   2077 C  CG  . TYR A  1  270 ? 42.641  14.928  18.716 1.00 47.27  ? 283 TYR A CG  1 
ATOM   2078 C  CD1 . TYR A  1  270 ? 42.593  14.569  20.059 1.00 47.05  ? 283 TYR A CD1 1 
ATOM   2079 C  CD2 . TYR A  1  270 ? 43.380  14.113  17.864 1.00 47.83  ? 283 TYR A CD2 1 
ATOM   2080 C  CE1 . TYR A  1  270 ? 43.258  13.447  20.534 1.00 47.82  ? 283 TYR A CE1 1 
ATOM   2081 C  CE2 . TYR A  1  270 ? 44.043  12.985  18.326 1.00 46.71  ? 283 TYR A CE2 1 
ATOM   2082 C  CZ  . TYR A  1  270 ? 43.987  12.654  19.666 1.00 45.41  ? 283 TYR A CZ  1 
ATOM   2083 O  OH  . TYR A  1  270 ? 44.632  11.544  20.124 1.00 46.00  ? 283 TYR A OH  1 
ATOM   2084 N  N   . VAL A  1  271 ? 45.139  17.442  17.925 1.00 46.01  ? 284 VAL A N   1 
ATOM   2085 C  CA  . VAL A  1  271 ? 46.406  17.422  17.208 1.00 47.76  ? 284 VAL A CA  1 
ATOM   2086 C  C   . VAL A  1  271 ? 47.141  16.122  17.526 1.00 47.51  ? 284 VAL A C   1 
ATOM   2087 O  O   . VAL A  1  271 ? 47.269  15.768  18.699 1.00 48.27  ? 284 VAL A O   1 
ATOM   2088 C  CB  . VAL A  1  271 ? 47.255  18.637  17.635 1.00 48.82  ? 284 VAL A CB  1 
ATOM   2089 C  CG1 . VAL A  1  271 ? 48.667  18.606  17.064 1.00 48.78  ? 284 VAL A CG1 1 
ATOM   2090 C  CG2 . VAL A  1  271 ? 46.571  19.960  17.307 1.00 49.05  ? 284 VAL A CG2 1 
ATOM   2091 N  N   . GLU A  1  272 ? 47.682  15.464  16.494 1.00 45.90  ? 285 GLU A N   1 
ATOM   2092 C  CA  A GLU A  1  272 ? 48.430  14.230  16.680 0.50 49.50  ? 285 GLU A CA  1 
ATOM   2093 C  CA  B GLU A  1  272 ? 48.438  14.232  16.672 0.50 49.37  ? 285 GLU A CA  1 
ATOM   2094 C  C   . GLU A  1  272 ? 49.748  14.546  17.397 1.00 51.40  ? 285 GLU A C   1 
ATOM   2095 O  O   . GLU A  1  272 ? 50.297  15.643  17.269 1.00 50.51  ? 285 GLU A O   1 
ATOM   2096 C  CB  A GLU A  1  272 ? 48.581  13.521  15.329 0.50 52.55  ? 285 GLU A CB  1 
ATOM   2097 C  CB  B GLU A  1  272 ? 48.702  13.512  15.343 0.50 52.33  ? 285 GLU A CB  1 
ATOM   2098 C  CG  A GLU A  1  272 ? 47.249  13.282  14.610 0.50 54.09  ? 285 GLU A CG  1 
ATOM   2099 C  CG  B GLU A  1  272 ? 49.896  12.557  15.418 0.50 53.00  ? 285 GLU A CG  1 
ATOM   2100 C  CD  A GLU A  1  272 ? 47.231  12.536  13.277 0.50 51.55  ? 285 GLU A CD  1 
ATOM   2101 C  CD  B GLU A  1  272 ? 50.351  11.824  14.164 0.50 53.13  ? 285 GLU A CD  1 
ATOM   2102 O  OE1 A GLU A  1  272 ? 48.275  12.088  12.753 0.50 44.55  ? 285 GLU A OE1 1 
ATOM   2103 O  OE1 B GLU A  1  272 ? 49.714  11.909  13.087 0.50 54.50  ? 285 GLU A OE1 1 
ATOM   2104 O  OE2 A GLU A  1  272 ? 46.105  12.391  12.757 0.50 50.55  ? 285 GLU A OE2 1 
ATOM   2105 O  OE2 B GLU A  1  272 ? 51.397  11.153  14.296 0.50 49.37  ? 285 GLU A OE2 1 
ATOM   2106 N  N   . ASP A  1  273 ? 50.237  13.579  18.191 1.00 53.80  ? 286 ASP A N   1 
ATOM   2107 C  CA  . ASP A  1  273 ? 51.569  13.636  18.775 1.00 55.49  ? 286 ASP A CA  1 
ATOM   2108 C  C   . ASP A  1  273 ? 52.398  12.493  18.199 1.00 53.03  ? 286 ASP A C   1 
ATOM   2109 O  O   . ASP A  1  273 ? 52.175  11.342  18.559 1.00 48.03  ? 286 ASP A O   1 
ATOM   2110 C  CB  . ASP A  1  273 ? 51.554  13.547  20.293 1.00 53.13  ? 286 ASP A CB  1 
ATOM   2111 C  CG  . ASP A  1  273 ? 52.927  13.574  20.949 1.00 54.69  ? 286 ASP A CG  1 
ATOM   2112 O  OD1 . ASP A  1  273 ? 53.944  13.580  20.209 1.00 59.34  ? 286 ASP A OD1 1 
ATOM   2113 O  OD2 . ASP A  1  273 ? 52.967  13.608  22.192 1.00 50.15  ? 286 ASP A OD2 1 
ATOM   2114 N  N   . PRO A  1  274 ? 53.375  12.764  17.301 1.00 60.82  ? 287 PRO A N   1 
ATOM   2115 C  CA  . PRO A  1  274 ? 54.173  11.694  16.693 1.00 62.89  ? 287 PRO A CA  1 
ATOM   2116 C  C   . PRO A  1  274 ? 55.262  11.085  17.586 1.00 61.47  ? 287 PRO A C   1 
ATOM   2117 O  O   . PRO A  1  274 ? 55.825  10.056  17.223 1.00 54.15  ? 287 PRO A O   1 
ATOM   2118 C  CB  . PRO A  1  274 ? 54.745  12.404  15.452 1.00 57.37  ? 287 PRO A CB  1 
ATOM   2119 C  CG  . PRO A  1  274 ? 54.940  13.831  15.912 1.00 58.67  ? 287 PRO A CG  1 
ATOM   2120 C  CD  . PRO A  1  274 ? 53.760  14.103  16.823 1.00 58.73  ? 287 PRO A CD  1 
ATOM   2121 N  N   . ASP A  1  275 ? 55.526  11.701  18.754 1.00 61.08  ? 288 ASP A N   1 
ATOM   2122 C  CA  . ASP A  1  275 ? 56.507  11.213  19.722 1.00 59.88  ? 288 ASP A CA  1 
ATOM   2123 C  C   . ASP A  1  275 ? 55.922  10.259  20.769 1.00 54.17  ? 288 ASP A C   1 
ATOM   2124 O  O   . ASP A  1  275 ? 56.679  9.572   21.451 1.00 50.11  ? 288 ASP A O   1 
ATOM   2125 C  CB  . ASP A  1  275 ? 57.152  12.364  20.476 1.00 64.14  ? 288 ASP A CB  1 
ATOM   2126 C  CG  . ASP A  1  275 ? 58.011  13.288  19.629 1.00 67.79  ? 288 ASP A CG  1 
ATOM   2127 O  OD1 . ASP A  1  275 ? 58.282  12.915  18.459 1.00 61.56  ? 288 ASP A OD1 1 
ATOM   2128 O  OD2 . ASP A  1  275 ? 58.366  14.369  20.146 1.00 68.88  ? 288 ASP A OD2 1 
ATOM   2129 N  N   . SER A  1  276 ? 54.594  10.215  20.910 1.00 48.90  ? 289 SER A N   1 
ATOM   2130 C  CA  . SER A  1  276 ? 53.949  9.353   21.887 1.00 47.19  ? 289 SER A CA  1 
ATOM   2131 C  C   . SER A  1  276 ? 54.215  7.882   21.589 1.00 43.38  ? 289 SER A C   1 
ATOM   2132 O  O   . SER A  1  276 ? 54.426  7.492   20.451 1.00 44.57  ? 289 SER A O   1 
ATOM   2133 C  CB  . SER A  1  276 ? 52.459  9.607   21.929 1.00 51.09  ? 289 SER A CB  1 
ATOM   2134 O  OG  . SER A  1  276 ? 51.769  8.543   22.574 1.00 48.19  ? 289 SER A OG  1 
ATOM   2135 N  N   . ALA A  1  277 ? 54.147  7.063   22.635 1.00 43.96  ? 290 ALA A N   1 
ATOM   2136 C  CA  . ALA A  1  277 ? 54.055  5.624   22.467 1.00 44.81  ? 290 ALA A CA  1 
ATOM   2137 C  C   . ALA A  1  277 ? 52.773  5.281   21.724 1.00 41.15  ? 290 ALA A C   1 
ATOM   2138 O  O   . ALA A  1  277 ? 51.798  6.023   21.783 1.00 41.48  ? 290 ALA A O   1 
ATOM   2139 C  CB  . ALA A  1  277 ? 54.063  4.946   23.814 1.00 48.29  ? 290 ALA A CB  1 
ATOM   2140 N  N   . ASP A  1  278 ? 52.801  4.146   21.024 1.00 40.88  ? 291 ASP A N   1 
ATOM   2141 C  CA  . ASP A  1  278 ? 51.621  3.556   20.406 1.00 41.56  ? 291 ASP A CA  1 
ATOM   2142 C  C   . ASP A  1  278 ? 51.841  2.051   20.425 1.00 42.30  ? 291 ASP A C   1 
ATOM   2143 O  O   . ASP A  1  278 ? 52.788  1.588   21.066 1.00 44.24  ? 291 ASP A O   1 
ATOM   2144 C  CB  . ASP A  1  278 ? 51.319  4.144   19.032 1.00 42.50  ? 291 ASP A CB  1 
ATOM   2145 C  CG  . ASP A  1  278 ? 52.342  3.873   17.930 1.00 44.84  ? 291 ASP A CG  1 
ATOM   2146 O  OD1 . ASP A  1  278 ? 53.070  2.866   18.024 1.00 44.21  ? 291 ASP A OD1 1 
ATOM   2147 O  OD2 . ASP A  1  278 ? 52.436  4.724   17.009 1.00 52.33  ? 291 ASP A OD2 1 
ATOM   2148 N  N   . PHE A  1  279 ? 51.015  1.305   19.683 1.00 40.28  ? 292 PHE A N   1 
ATOM   2149 C  CA  . PHE A  1  279 ? 50.998  -0.142  19.833 1.00 42.64  ? 292 PHE A CA  1 
ATOM   2150 C  C   . PHE A  1  279 ? 52.132  -0.828  19.073 1.00 42.50  ? 292 PHE A C   1 
ATOM   2151 O  O   . PHE A  1  279 ? 52.390  -1.998  19.328 1.00 43.37  ? 292 PHE A O   1 
ATOM   2152 C  CB  . PHE A  1  279 ? 49.619  -0.687  19.459 1.00 42.67  ? 292 PHE A CB  1 
ATOM   2153 C  CG  . PHE A  1  279 ? 48.664  -0.578  20.633 1.00 42.89  ? 292 PHE A CG  1 
ATOM   2154 C  CD1 . PHE A  1  279 ? 48.746  -1.472  21.694 1.00 47.23  ? 292 PHE A CD1 1 
ATOM   2155 C  CD2 . PHE A  1  279 ? 47.739  0.444   20.704 1.00 44.76  ? 292 PHE A CD2 1 
ATOM   2156 C  CE1 . PHE A  1  279 ? 47.880  -1.381  22.772 1.00 48.04  ? 292 PHE A CE1 1 
ATOM   2157 C  CE2 . PHE A  1  279 ? 46.871  0.533   21.784 1.00 48.90  ? 292 PHE A CE2 1 
ATOM   2158 C  CZ  . PHE A  1  279 ? 46.952  -0.369  22.823 1.00 47.57  ? 292 PHE A CZ  1 
ATOM   2159 N  N   . THR A  1  280 ? 52.806  -0.123  18.160 1.00 46.50  ? 293 THR A N   1 
ATOM   2160 C  CA  . THR A  1  280 ? 53.973  -0.677  17.482 1.00 51.62  ? 293 THR A CA  1 
ATOM   2161 C  C   . THR A  1  280 ? 55.244  -0.029  18.032 1.00 53.59  ? 293 THR A C   1 
ATOM   2162 O  O   . THR A  1  280 ? 56.322  -0.306  17.525 1.00 54.00  ? 293 THR A O   1 
ATOM   2163 C  CB  . THR A  1  280 ? 53.853  -0.474  15.967 1.00 52.52  ? 293 THR A CB  1 
ATOM   2164 O  OG1 . THR A  1  280 ? 53.828  0.939   15.775 1.00 56.79  ? 293 THR A OG1 1 
ATOM   2165 C  CG2 . THR A  1  280 ? 52.598  -1.084  15.368 1.00 51.43  ? 293 THR A CG2 1 
ATOM   2166 N  N   . HIS A  1  281 ? 55.112  0.837   19.055 1.00 55.22  ? 294 HIS A N   1 
ATOM   2167 C  CA  . HIS A  1  281 ? 56.233  1.574   19.627 1.00 49.68  ? 294 HIS A CA  1 
ATOM   2168 C  C   . HIS A  1  281 ? 56.113  1.603   21.154 1.00 48.24  ? 294 HIS A C   1 
ATOM   2169 O  O   . HIS A  1  281 ? 56.136  2.656   21.790 1.00 46.81  ? 294 HIS A O   1 
ATOM   2170 C  CB  . HIS A  1  281 ? 56.351  2.985   19.039 1.00 54.20  ? 294 HIS A CB  1 
ATOM   2171 C  CG  . HIS A  1  281 ? 56.679  3.054   17.582 1.00 62.70  ? 294 HIS A CG  1 
ATOM   2172 N  ND1 . HIS A  1  281 ? 57.973  3.113   17.114 1.00 71.66  ? 294 HIS A ND1 1 
ATOM   2173 C  CD2 . HIS A  1  281 ? 55.899  3.109   16.499 1.00 66.56  ? 294 HIS A CD2 1 
ATOM   2174 C  CE1 . HIS A  1  281 ? 57.967  3.186   15.790 1.00 71.41  ? 294 HIS A CE1 1 
ATOM   2175 N  NE2 . HIS A  1  281 ? 56.716  3.174   15.397 1.00 75.57  ? 294 HIS A NE2 1 
ATOM   2176 N  N   . LEU A  1  282 ? 56.017  0.409   21.747 1.00 48.08  ? 295 LEU A N   1 
ATOM   2177 C  CA  . LEU A  1  282 ? 55.704  0.261   23.157 1.00 46.74  ? 295 LEU A CA  1 
ATOM   2178 C  C   . LEU A  1  282 ? 56.846  0.688   24.073 1.00 50.99  ? 295 LEU A C   1 
ATOM   2179 O  O   . LEU A  1  282 ? 56.569  1.145   25.179 1.00 54.99  ? 295 LEU A O   1 
ATOM   2180 C  CB  . LEU A  1  282 ? 55.310  -1.188  23.414 1.00 45.24  ? 295 LEU A CB  1 
ATOM   2181 C  CG  . LEU A  1  282 ? 53.887  -1.579  23.023 1.00 44.05  ? 295 LEU A CG  1 
ATOM   2182 C  CD1 . LEU A  1  282 ? 53.657  -3.075  23.191 1.00 44.88  ? 295 LEU A CD1 1 
ATOM   2183 C  CD2 . LEU A  1  282 ? 52.912  -0.777  23.861 1.00 45.15  ? 295 LEU A CD2 1 
ATOM   2184 N  N   . CYS A  1  283 ? 58.108  0.497   23.668 1.00 53.46  ? 296 CYS A N   1 
ATOM   2185 C  CA  . CYS A  1  283 ? 59.232  0.808   24.545 1.00 57.50  ? 296 CYS A CA  1 
ATOM   2186 C  C   . CYS A  1  283 ? 59.268  2.298   24.883 1.00 48.56  ? 296 CYS A C   1 
ATOM   2187 O  O   . CYS A  1  283 ? 59.864  2.670   25.894 1.00 45.42  ? 296 CYS A O   1 
ATOM   2188 C  CB  . CYS A  1  283 ? 60.588  0.369   23.984 1.00 63.13  ? 296 CYS A CB  1 
ATOM   2189 S  SG  . CYS A  1  283 ? 60.963  -1.405  24.144 1.00 82.90  ? 296 CYS A SG  1 
ATOM   2190 N  N   . ARG A  1  284 ? 58.637  3.145   24.052 1.00 44.31  ? 297 ARG A N   1 
ATOM   2191 C  CA  . ARG A  1  284 ? 58.560  4.564   24.360 1.00 44.46  ? 297 ARG A CA  1 
ATOM   2192 C  C   . ARG A  1  284 ? 57.831  4.786   25.686 1.00 43.22  ? 297 ARG A C   1 
ATOM   2193 O  O   . ARG A  1  284 ? 58.165  5.714   26.426 1.00 46.17  ? 297 ARG A O   1 
ATOM   2194 C  CB  . ARG A  1  284 ? 57.854  5.366   23.267 1.00 45.46  ? 297 ARG A CB  1 
ATOM   2195 C  CG  . ARG A  1  284 ? 58.629  5.448   21.963 1.00 51.39  ? 297 ARG A CG  1 
ATOM   2196 C  CD  . ARG A  1  284 ? 58.004  6.464   21.018 1.00 56.33  ? 297 ARG A CD  1 
ATOM   2197 N  NE  . ARG A  1  284 ? 58.451  6.247   19.641 1.00 62.41  ? 297 ARG A NE  1 
ATOM   2198 C  CZ  . ARG A  1  284 ? 57.899  6.742   18.547 1.00 63.20  ? 297 ARG A CZ  1 
ATOM   2199 N  NH1 . ARG A  1  284 ? 56.942  7.634   18.651 1.00 58.62  ? 297 ARG A NH1 1 
ATOM   2200 N  NH2 . ARG A  1  284 ? 58.319  6.370   17.351 1.00 69.36  ? 297 ARG A NH2 1 
ATOM   2201 N  N   . LEU A  1  285 ? 56.829  3.940   25.968 1.00 41.76  ? 298 LEU A N   1 
ATOM   2202 C  CA  . LEU A  1  285 ? 56.083  4.021   27.212 1.00 43.39  ? 298 LEU A CA  1 
ATOM   2203 C  C   . LEU A  1  285 ? 57.039  3.806   28.383 1.00 37.77  ? 298 LEU A C   1 
ATOM   2204 O  O   . LEU A  1  285 ? 57.010  4.567   29.337 1.00 34.88  ? 298 LEU A O   1 
ATOM   2205 C  CB  . LEU A  1  285 ? 54.919  3.031   27.218 1.00 47.43  ? 298 LEU A CB  1 
ATOM   2206 C  CG  . LEU A  1  285 ? 53.876  3.215   28.333 1.00 49.17  ? 298 LEU A CG  1 
ATOM   2207 C  CD1 . LEU A  1  285 ? 52.600  2.500   27.968 1.00 54.06  ? 298 LEU A CD1 1 
ATOM   2208 C  CD2 . LEU A  1  285 ? 54.332  2.688   29.684 1.00 47.82  ? 298 LEU A CD2 1 
ATOM   2209 N  N   . TYR A  1  286 ? 57.919  2.808   28.273 1.00 41.65  ? 299 TYR A N   1 
ATOM   2210 C  CA  . TYR A  1  286 ? 58.907  2.517   29.307 1.00 40.36  ? 299 TYR A CA  1 
ATOM   2211 C  C   . TYR A  1  286 ? 59.773  3.747   29.550 1.00 39.98  ? 299 TYR A C   1 
ATOM   2212 O  O   . TYR A  1  286 ? 59.901  4.189   30.690 1.00 42.50  ? 299 TYR A O   1 
ATOM   2213 C  CB  . TYR A  1  286 ? 59.746  1.288   28.937 1.00 41.51  ? 299 TYR A CB  1 
ATOM   2214 C  CG  . TYR A  1  286 ? 60.875  0.985   29.910 1.00 41.94  ? 299 TYR A CG  1 
ATOM   2215 C  CD1 . TYR A  1  286 ? 60.611  0.638   31.230 1.00 40.83  ? 299 TYR A CD1 1 
ATOM   2216 C  CD2 . TYR A  1  286 ? 62.208  1.048   29.512 1.00 42.50  ? 299 TYR A CD2 1 
ATOM   2217 C  CE1 . TYR A  1  286 ? 61.637  0.379   32.129 1.00 39.93  ? 299 TYR A CE1 1 
ATOM   2218 C  CE2 . TYR A  1  286 ? 63.243  0.769   30.398 1.00 42.20  ? 299 TYR A CE2 1 
ATOM   2219 C  CZ  . TYR A  1  286 ? 62.961  0.450   31.717 1.00 41.25  ? 299 TYR A CZ  1 
ATOM   2220 O  OH  . TYR A  1  286 ? 63.976  0.210   32.609 1.00 39.19  ? 299 TYR A OH  1 
ATOM   2221 N  N   . GLU A  1  287 ? 60.340  4.310   28.478 1.00 44.33  ? 300 GLU A N   1 
ATOM   2222 C  CA  . GLU A  1  287 ? 61.257  5.441   28.586 1.00 47.66  ? 300 GLU A CA  1 
ATOM   2223 C  C   . GLU A  1  287 ? 60.539  6.648   29.195 1.00 42.62  ? 300 GLU A C   1 
ATOM   2224 O  O   . GLU A  1  287 ? 61.066  7.274   30.106 1.00 40.27  ? 300 GLU A O   1 
ATOM   2225 C  CB  . GLU A  1  287 ? 61.905  5.746   27.236 1.00 53.93  ? 300 GLU A CB  1 
ATOM   2226 C  CG  . GLU A  1  287 ? 62.844  4.633   26.768 1.00 68.64  ? 300 GLU A CG  1 
ATOM   2227 C  CD  . GLU A  1  287 ? 63.174  4.545   25.281 1.00 81.03  ? 300 GLU A CD  1 
ATOM   2228 O  OE1 . GLU A  1  287 ? 62.314  4.849   24.422 1.00 77.88  ? 300 GLU A OE1 1 
ATOM   2229 O  OE2 . GLU A  1  287 ? 64.309  4.111   24.969 1.00 94.82  ? 300 GLU A OE2 1 
ATOM   2230 N  N   . PHE A  1  288 ? 59.325  6.943   28.718 1.00 38.18  ? 301 PHE A N   1 
ATOM   2231 C  CA  . PHE A  1  288 ? 58.537  8.053   29.225 1.00 37.86  ? 301 PHE A CA  1 
ATOM   2232 C  C   . PHE A  1  288 ? 58.324  7.929   30.738 1.00 38.10  ? 301 PHE A C   1 
ATOM   2233 O  O   . PHE A  1  288 ? 58.471  8.907   31.466 1.00 35.79  ? 301 PHE A O   1 
ATOM   2234 C  CB  . PHE A  1  288 ? 57.203  8.108   28.471 1.00 42.12  ? 301 PHE A CB  1 
ATOM   2235 C  CG  . PHE A  1  288 ? 56.352  9.301   28.886 1.00 46.89  ? 301 PHE A CG  1 
ATOM   2236 C  CD1 . PHE A  1  288 ? 56.475  10.520  28.226 1.00 45.59  ? 301 PHE A CD1 1 
ATOM   2237 C  CD2 . PHE A  1  288 ? 55.464  9.215   29.965 1.00 49.08  ? 301 PHE A CD2 1 
ATOM   2238 C  CE1 . PHE A  1  288 ? 55.722  11.615  28.622 1.00 46.29  ? 301 PHE A CE1 1 
ATOM   2239 C  CE2 . PHE A  1  288 ? 54.726  10.318  30.366 1.00 45.97  ? 301 PHE A CE2 1 
ATOM   2240 C  CZ  . PHE A  1  288 ? 54.855  11.513  29.692 1.00 47.33  ? 301 PHE A CZ  1 
ATOM   2241 N  N   . VAL A  1  289 ? 57.966  6.731   31.218 1.00 37.42  ? 302 VAL A N   1 
ATOM   2242 C  CA  . VAL A  1  289 ? 57.632  6.522   32.623 1.00 37.82  ? 302 VAL A CA  1 
ATOM   2243 C  C   . VAL A  1  289 ? 58.882  6.667   33.488 1.00 36.02  ? 302 VAL A C   1 
ATOM   2244 O  O   . VAL A  1  289 ? 58.819  7.229   34.576 1.00 35.66  ? 302 VAL A O   1 
ATOM   2245 C  CB  . VAL A  1  289 ? 56.949  5.160   32.867 1.00 36.01  ? 302 VAL A CB  1 
ATOM   2246 C  CG1 . VAL A  1  289 ? 56.891  4.782   34.342 1.00 37.95  ? 302 VAL A CG1 1 
ATOM   2247 C  CG2 . VAL A  1  289 ? 55.554  5.138   32.277 1.00 35.42  ? 302 VAL A CG2 1 
ATOM   2248 N  N   . VAL A  1  290 ? 60.009  6.127   33.021 1.00 37.74  ? 303 VAL A N   1 
ATOM   2249 C  CA  . VAL A  1  290 ? 61.269  6.297   33.733 1.00 35.97  ? 303 VAL A CA  1 
ATOM   2250 C  C   . VAL A  1  290 ? 61.610  7.788   33.823 1.00 34.02  ? 303 VAL A C   1 
ATOM   2251 O  O   . VAL A  1  290 ? 62.020  8.267   34.870 1.00 32.55  ? 303 VAL A O   1 
ATOM   2252 C  CB  . VAL A  1  290 ? 62.389  5.483   33.067 1.00 36.29  ? 303 VAL A CB  1 
ATOM   2253 C  CG1 . VAL A  1  290 ? 63.764  5.850   33.612 1.00 37.47  ? 303 VAL A CG1 1 
ATOM   2254 C  CG2 . VAL A  1  290 ? 62.144  3.989   33.214 1.00 35.22  ? 303 VAL A CG2 1 
ATOM   2255 N  N   . GLY A  1  291 ? 61.404  8.519   32.723 1.00 34.65  ? 304 GLY A N   1 
ATOM   2256 C  CA  . GLY A  1  291 ? 61.464  9.975   32.710 1.00 34.81  ? 304 GLY A CA  1 
ATOM   2257 C  C   . GLY A  1  291 ? 60.615  10.599  33.812 1.00 38.33  ? 304 GLY A C   1 
ATOM   2258 O  O   . GLY A  1  291 ? 61.112  11.400  34.589 1.00 41.71  ? 304 GLY A O   1 
ATOM   2259 N  N   . SER A  1  292 ? 59.345  10.191  33.904 1.00 41.44  ? 305 SER A N   1 
ATOM   2260 C  CA  . SER A  1  292 ? 58.429  10.775  34.870 1.00 40.41  ? 305 SER A CA  1 
ATOM   2261 C  C   . SER A  1  292 ? 58.889  10.482  36.290 1.00 35.24  ? 305 SER A C   1 
ATOM   2262 O  O   . SER A  1  292 ? 58.687  11.295  37.177 1.00 34.26  ? 305 SER A O   1 
ATOM   2263 C  CB  . SER A  1  292 ? 57.009  10.299  34.668 1.00 41.85  ? 305 SER A CB  1 
ATOM   2264 O  OG  . SER A  1  292 ? 56.575  10.420  33.322 1.00 41.78  ? 305 SER A OG  1 
ATOM   2265 N  N   . VAL A  1  293 ? 59.483  9.312   36.510 1.00 37.94  ? 306 VAL A N   1 
ATOM   2266 C  CA  . VAL A  1  293 ? 59.942  8.949   37.841 1.00 41.34  ? 306 VAL A CA  1 
ATOM   2267 C  C   . VAL A  1  293 ? 61.117  9.844   38.241 1.00 40.66  ? 306 VAL A C   1 
ATOM   2268 O  O   . VAL A  1  293 ? 61.222  10.222  39.404 1.00 41.31  ? 306 VAL A O   1 
ATOM   2269 C  CB  . VAL A  1  293 ? 60.287  7.449   37.940 1.00 41.32  ? 306 VAL A CB  1 
ATOM   2270 C  CG1 . VAL A  1  293 ? 61.075  7.120   39.209 1.00 39.41  ? 306 VAL A CG1 1 
ATOM   2271 C  CG2 . VAL A  1  293 ? 59.024  6.602   37.870 1.00 39.72  ? 306 VAL A CG2 1 
ATOM   2272 N  N   . GLN A  1  294 ? 61.985  10.191  37.281 1.00 38.48  ? 307 GLN A N   1 
ATOM   2273 C  CA  . GLN A  1  294 ? 63.089  11.105  37.538 1.00 38.58  ? 307 GLN A CA  1 
ATOM   2274 C  C   . GLN A  1  294 ? 62.575  12.482  37.969 1.00 40.31  ? 307 GLN A C   1 
ATOM   2275 O  O   . GLN A  1  294 ? 63.166  13.096  38.860 1.00 43.64  ? 307 GLN A O   1 
ATOM   2276 C  CB  . GLN A  1  294 ? 64.021  11.201  36.334 1.00 38.06  ? 307 GLN A CB  1 
ATOM   2277 C  CG  . GLN A  1  294 ? 64.811  9.920   36.080 1.00 39.43  ? 307 GLN A CG  1 
ATOM   2278 C  CD  . GLN A  1  294 ? 65.656  9.984   34.827 1.00 40.29  ? 307 GLN A CD  1 
ATOM   2279 O  OE1 . GLN A  1  294 ? 65.173  9.847   33.693 1.00 39.29  ? 307 GLN A OE1 1 
ATOM   2280 N  NE2 . GLN A  1  294 ? 66.947  10.198  35.025 1.00 39.37  ? 307 GLN A NE2 1 
ATOM   2281 N  N   . GLU A  1  295 ? 61.476  12.960  37.357 1.00 40.80  ? 308 GLU A N   1 
ATOM   2282 C  CA  . GLU A  1  295 ? 60.885  14.238  37.724 1.00 39.77  ? 308 GLU A CA  1 
ATOM   2283 C  C   . GLU A  1  295 ? 60.357  14.192  39.159 1.00 39.71  ? 308 GLU A C   1 
ATOM   2284 O  O   . GLU A  1  295 ? 60.495  15.177  39.867 1.00 42.92  ? 308 GLU A O   1 
ATOM   2285 C  CB  . GLU A  1  295 ? 59.762  14.690  36.796 1.00 45.08  ? 308 GLU A CB  1 
ATOM   2286 C  CG  . GLU A  1  295 ? 60.186  14.945  35.354 1.00 55.75  ? 308 GLU A CG  1 
ATOM   2287 C  CD  . GLU A  1  295 ? 59.029  15.077  34.355 1.00 69.52  ? 308 GLU A CD  1 
ATOM   2288 O  OE1 . GLU A  1  295 ? 57.850  15.166  34.787 1.00 71.02  ? 308 GLU A OE1 1 
ATOM   2289 O  OE2 . GLU A  1  295 ? 59.295  15.066  33.125 1.00 70.99  ? 308 GLU A OE2 1 
ATOM   2290 N  N   . LEU A  1  296 ? 59.781  13.058  39.591 1.00 37.58  ? 309 LEU A N   1 
ATOM   2291 C  CA  . LEU A  1  296 ? 59.244  12.914  40.942 1.00 39.31  ? 309 LEU A CA  1 
ATOM   2292 C  C   . LEU A  1  296 ? 60.376  12.754  41.953 1.00 38.79  ? 309 LEU A C   1 
ATOM   2293 O  O   . LEU A  1  296 ? 60.251  13.200  43.089 1.00 38.43  ? 309 LEU A O   1 
ATOM   2294 C  CB  . LEU A  1  296 ? 58.286  11.724  41.055 1.00 39.09  ? 309 LEU A CB  1 
ATOM   2295 C  CG  . LEU A  1  296 ? 57.001  11.809  40.218 1.00 39.08  ? 309 LEU A CG  1 
ATOM   2296 C  CD1 . LEU A  1  296 ? 56.283  10.484  40.272 1.00 42.59  ? 309 LEU A CD1 1 
ATOM   2297 C  CD2 . LEU A  1  296 ? 56.045  12.920  40.620 1.00 35.26  ? 309 LEU A CD2 1 
ATOM   2298 N  N   . TYR A  1  297 ? 61.442  12.046  41.557 1.00 38.26  ? 310 TYR A N   1 
ATOM   2299 C  CA  . TYR A  1  297 ? 62.553  11.739  42.446 1.00 38.40  ? 310 TYR A CA  1 
ATOM   2300 C  C   . TYR A  1  297 ? 63.856  12.229  41.815 1.00 37.48  ? 310 TYR A C   1 
ATOM   2301 O  O   . TYR A  1  297 ? 64.631  11.445  41.271 1.00 34.31  ? 310 TYR A O   1 
ATOM   2302 C  CB  . TYR A  1  297 ? 62.561  10.231  42.723 1.00 36.33  ? 310 TYR A CB  1 
ATOM   2303 C  CG  . TYR A  1  297 ? 61.325  9.734   43.450 1.00 36.21  ? 310 TYR A CG  1 
ATOM   2304 C  CD1 . TYR A  1  297 ? 61.203  9.880   44.825 1.00 38.80  ? 310 TYR A CD1 1 
ATOM   2305 C  CD2 . TYR A  1  297 ? 60.287  9.109   42.763 1.00 36.96  ? 310 TYR A CD2 1 
ATOM   2306 C  CE1 . TYR A  1  297 ? 60.070  9.438   45.493 1.00 40.78  ? 310 TYR A CE1 1 
ATOM   2307 C  CE2 . TYR A  1  297 ? 59.160  8.649   43.422 1.00 36.73  ? 310 TYR A CE2 1 
ATOM   2308 C  CZ  . TYR A  1  297 ? 59.047  8.817   44.791 1.00 38.99  ? 310 TYR A CZ  1 
ATOM   2309 O  OH  . TYR A  1  297 ? 57.932  8.383   45.456 1.00 39.78  ? 310 TYR A OH  1 
ATOM   2310 N  N   . PRO A  1  298 ? 64.134  13.548  41.849 1.00 40.98  ? 311 PRO A N   1 
ATOM   2311 C  CA  . PRO A  1  298 ? 65.325  14.090  41.198 1.00 44.20  ? 311 PRO A CA  1 
ATOM   2312 C  C   . PRO A  1  298 ? 66.660  13.721  41.840 1.00 41.59  ? 311 PRO A C   1 
ATOM   2313 O  O   . PRO A  1  298 ? 67.660  13.680  41.130 1.00 40.12  ? 311 PRO A O   1 
ATOM   2314 C  CB  . PRO A  1  298 ? 65.084  15.611  41.208 1.00 44.39  ? 311 PRO A CB  1 
ATOM   2315 C  CG  . PRO A  1  298 ? 64.111  15.850  42.336 1.00 43.63  ? 311 PRO A CG  1 
ATOM   2316 C  CD  . PRO A  1  298 ? 63.305  14.585  42.475 1.00 40.70  ? 311 PRO A CD  1 
ATOM   2317 N  N   . ASN A  1  299 ? 66.683  13.430  43.151 1.00 41.73  ? 312 ASN A N   1 
ATOM   2318 C  CA  . ASN A  1  299 ? 67.952  13.162  43.819 1.00 39.30  ? 312 ASN A CA  1 
ATOM   2319 C  C   . ASN A  1  299 ? 67.759  12.351  45.099 1.00 36.32  ? 312 ASN A C   1 
ATOM   2320 O  O   . ASN A  1  299 ? 68.149  12.776  46.177 1.00 41.61  ? 312 ASN A O   1 
ATOM   2321 C  CB  . ASN A  1  299 ? 68.698  14.470  44.081 1.00 39.78  ? 312 ASN A CB  1 
ATOM   2322 C  CG  . ASN A  1  299 ? 70.099  14.257  44.588 1.00 37.51  ? 312 ASN A CG  1 
ATOM   2323 O  OD1 . ASN A  1  299 ? 70.850  13.453  44.017 1.00 44.98  ? 312 ASN A OD1 1 
ATOM   2324 N  ND2 . ASN A  1  299 ? 70.457  14.952  45.654 1.00 34.85  ? 312 ASN A ND2 1 
ATOM   2325 N  N   . PRO A  1  300 ? 67.231  11.117  45.024 1.00 36.60  ? 313 PRO A N   1 
ATOM   2326 C  CA  . PRO A  1  300 ? 67.067  10.287  46.223 1.00 38.13  ? 313 PRO A CA  1 
ATOM   2327 C  C   . PRO A  1  300 ? 68.379  9.676   46.700 1.00 38.96  ? 313 PRO A C   1 
ATOM   2328 O  O   . PRO A  1  300 ? 69.248  9.425   45.870 1.00 43.80  ? 313 PRO A O   1 
ATOM   2329 C  CB  . PRO A  1  300 ? 66.074  9.230   45.700 1.00 35.79  ? 313 PRO A CB  1 
ATOM   2330 C  CG  . PRO A  1  300 ? 66.484  9.045   44.263 1.00 35.50  ? 313 PRO A CG  1 
ATOM   2331 C  CD  . PRO A  1  300 ? 66.782  10.452  43.790 1.00 36.66  ? 313 PRO A CD  1 
ATOM   2332 N  N   . THR A  1  301 ? 68.506  9.408   48.013 1.00 46.87  ? 314 THR A N   1 
ATOM   2333 C  CA  . THR A  1  301 ? 69.815  9.073   48.571 1.00 57.10  ? 314 THR A CA  1 
ATOM   2334 C  C   . THR A  1  301 ? 69.805  7.788   49.402 1.00 59.74  ? 314 THR A C   1 
ATOM   2335 O  O   . THR A  1  301 ? 70.828  7.110   49.464 1.00 85.75  ? 314 THR A O   1 
ATOM   2336 C  CB  . THR A  1  301 ? 70.418  10.218  49.395 1.00 55.96  ? 314 THR A CB  1 
ATOM   2337 O  OG1 . THR A  1  301 ? 69.456  10.636  50.355 1.00 56.88  ? 314 THR A OG1 1 
ATOM   2338 C  CG2 . THR A  1  301 ? 70.790  11.434  48.568 1.00 59.17  ? 314 THR A CG2 1 
ATOM   2339 N  N   . GLY A  1  302 ? 68.729  7.443   50.100 1.00 49.23  ? 315 GLY A N   1 
ATOM   2340 C  CA  . GLY A  1  302 ? 68.915  6.475   51.174 1.00 47.93  ? 315 GLY A CA  1 
ATOM   2341 C  C   . GLY A  1  302 ? 68.211  5.154   50.902 1.00 46.77  ? 315 GLY A C   1 
ATOM   2342 O  O   . GLY A  1  302 ? 68.456  4.513   49.886 1.00 45.14  ? 315 GLY A O   1 
ATOM   2343 N  N   . ILE A  1  303 ? 67.344  4.776   51.851 1.00 48.82  ? 316 ILE A N   1 
ATOM   2344 C  CA  . ILE A  1  303 ? 66.384  3.697   51.685 1.00 50.43  ? 316 ILE A CA  1 
ATOM   2345 C  C   . ILE A  1  303 ? 65.488  4.013   50.483 1.00 45.07  ? 316 ILE A C   1 
ATOM   2346 O  O   . ILE A  1  303 ? 65.043  3.110   49.776 1.00 43.55  ? 316 ILE A O   1 
ATOM   2347 C  CB  . ILE A  1  303 ? 65.601  3.488   53.000 1.00 55.35  ? 316 ILE A CB  1 
ATOM   2348 C  CG1 . ILE A  1  303 ? 66.562  3.061   54.131 1.00 76.24  ? 316 ILE A CG1 1 
ATOM   2349 C  CG2 . ILE A  1  303 ? 64.470  2.471   52.839 1.00 54.55  ? 316 ILE A CG2 1 
ATOM   2350 C  CD1 . ILE A  1  303 ? 66.036  3.248   55.553 1.00 91.29  ? 316 ILE A CD1 1 
ATOM   2351 N  N   . LEU A  1  304 ? 65.234  5.301   50.237 1.00 37.79  ? 317 LEU A N   1 
ATOM   2352 C  CA  . LEU A  1  304 ? 64.381  5.684   49.130 1.00 35.44  ? 317 LEU A CA  1 
ATOM   2353 C  C   . LEU A  1  304 ? 65.063  5.354   47.801 1.00 35.89  ? 317 LEU A C   1 
ATOM   2354 O  O   . LEU A  1  304 ? 64.402  4.892   46.872 1.00 36.37  ? 317 LEU A O   1 
ATOM   2355 C  CB  . LEU A  1  304 ? 63.997  7.158   49.255 1.00 33.59  ? 317 LEU A CB  1 
ATOM   2356 C  CG  . LEU A  1  304 ? 63.236  7.749   48.067 1.00 33.00  ? 317 LEU A CG  1 
ATOM   2357 C  CD1 . LEU A  1  304 ? 61.918  7.029   47.832 1.00 34.50  ? 317 LEU A CD1 1 
ATOM   2358 C  CD2 . LEU A  1  304 ? 63.008  9.242   48.245 1.00 30.09  ? 317 LEU A CD2 1 
ATOM   2359 N  N   . ARG A  1  305 ? 66.375  5.601   47.702 1.00 34.50  ? 318 ARG A N   1 
ATOM   2360 C  CA  A ARG A  1  305 ? 67.117  5.299   46.489 0.50 33.18  ? 318 ARG A CA  1 
ATOM   2361 C  CA  B ARG A  1  305 ? 67.123  5.299   46.491 0.50 36.53  ? 318 ARG A CA  1 
ATOM   2362 C  C   . ARG A  1  305 ? 67.089  3.792   46.258 1.00 36.02  ? 318 ARG A C   1 
ATOM   2363 O  O   . ARG A  1  305 ? 66.837  3.336   45.149 1.00 34.99  ? 318 ARG A O   1 
ATOM   2364 C  CB  A ARG A  1  305 ? 68.571  5.780   46.579 0.50 31.34  ? 318 ARG A CB  1 
ATOM   2365 C  CB  B ARG A  1  305 ? 68.582  5.772   46.580 0.50 39.64  ? 318 ARG A CB  1 
ATOM   2366 C  CG  A ARG A  1  305 ? 69.443  5.459   45.373 0.50 27.00  ? 318 ARG A CG  1 
ATOM   2367 C  CG  B ARG A  1  305 ? 69.432  5.464   45.353 0.50 39.17  ? 318 ARG A CG  1 
ATOM   2368 C  CD  A ARG A  1  305 ? 70.937  5.508   45.733 0.50 23.85  ? 318 ARG A CD  1 
ATOM   2369 C  CD  B ARG A  1  305 ? 70.955  5.532   45.590 0.50 39.36  ? 318 ARG A CD  1 
ATOM   2370 N  NE  A ARG A  1  305 ? 71.737  5.026   44.605 0.50 20.50  ? 318 ARG A NE  1 
ATOM   2371 N  NE  B ARG A  1  305 ? 71.636  5.703   44.298 0.50 39.28  ? 318 ARG A NE  1 
ATOM   2372 C  CZ  A ARG A  1  305 ? 72.352  3.889   44.650 0.50 16.99  ? 318 ARG A CZ  1 
ATOM   2373 C  CZ  B ARG A  1  305 ? 71.481  6.762   43.485 0.50 37.11  ? 318 ARG A CZ  1 
ATOM   2374 N  NH1 A ARG A  1  305 ? 72.319  3.217   45.775 0.50 15.56  ? 318 ARG A NH1 1 
ATOM   2375 N  NH1 B ARG A  1  305 ? 70.804  7.843   43.856 0.50 38.89  ? 318 ARG A NH1 1 
ATOM   2376 N  NH2 A ARG A  1  305 ? 73.001  3.473   43.596 0.50 16.63  ? 318 ARG A NH2 1 
ATOM   2377 N  NH2 B ARG A  1  305 ? 72.026  6.759   42.292 0.50 33.08  ? 318 ARG A NH2 1 
ATOM   2378 N  N   . ARG A  1  306 ? 67.368  3.034   47.320 1.00 39.20  ? 319 ARG A N   1 
ATOM   2379 C  CA  . ARG A  1  306 ? 67.410  1.583   47.248 1.00 40.42  ? 319 ARG A CA  1 
ATOM   2380 C  C   . ARG A  1  306 ? 66.080  1.043   46.712 1.00 37.46  ? 319 ARG A C   1 
ATOM   2381 O  O   . ARG A  1  306 ? 66.063  0.200   45.817 1.00 34.84  ? 319 ARG A O   1 
ATOM   2382 C  CB  . ARG A  1  306 ? 67.750  1.021   48.634 1.00 43.86  ? 319 ARG A CB  1 
ATOM   2383 C  CG  . ARG A  1  306 ? 68.084  -0.467  48.638 1.00 57.48  ? 319 ARG A CG  1 
ATOM   2384 C  CD  . ARG A  1  306 ? 68.115  -1.111  50.020 1.00 64.65  ? 319 ARG A CD  1 
ATOM   2385 N  NE  . ARG A  1  306 ? 66.757  -1.262  50.558 1.00 71.95  ? 319 ARG A NE  1 
ATOM   2386 C  CZ  . ARG A  1  306 ? 66.461  -1.467  51.843 1.00 74.24  ? 319 ARG A CZ  1 
ATOM   2387 N  NH1 . ARG A  1  306 ? 67.412  -1.759  52.714 1.00 68.53  ? 319 ARG A NH1 1 
ATOM   2388 N  NH2 . ARG A  1  306 ? 65.200  -1.459  52.240 1.00 77.57  ? 319 ARG A NH2 1 
ATOM   2389 N  N   . ASN A  1  307 ? 64.961  1.541   47.251 1.00 34.67  ? 320 ASN A N   1 
ATOM   2390 C  CA  . ASN A  1  307 ? 63.657  0.988   46.932 1.00 35.98  ? 320 ASN A CA  1 
ATOM   2391 C  C   . ASN A  1  307 ? 63.216  1.406   45.535 1.00 36.49  ? 320 ASN A C   1 
ATOM   2392 O  O   . ASN A  1  307 ? 62.528  0.633   44.875 1.00 40.44  ? 320 ASN A O   1 
ATOM   2393 C  CB  . ASN A  1  307 ? 62.644  1.314   48.016 1.00 38.05  ? 320 ASN A CB  1 
ATOM   2394 C  CG  . ASN A  1  307 ? 62.901  0.513   49.273 1.00 40.09  ? 320 ASN A CG  1 
ATOM   2395 O  OD1 . ASN A  1  307 ? 63.844  -0.284  49.328 1.00 39.66  ? 320 ASN A OD1 1 
ATOM   2396 N  ND2 . ASN A  1  307 ? 62.066  0.697   50.284 1.00 41.24  ? 320 ASN A ND2 1 
ATOM   2397 N  N   . LEU A  1  308 ? 63.642  2.594   45.079 1.00 37.46  ? 321 LEU A N   1 
ATOM   2398 C  CA  . LEU A  1  308 ? 63.424  3.014   43.702 1.00 37.73  ? 321 LEU A CA  1 
ATOM   2399 C  C   . LEU A  1  308 ? 64.118  2.067   42.728 1.00 36.40  ? 321 LEU A C   1 
ATOM   2400 O  O   . LEU A  1  308 ? 63.555  1.716   41.697 1.00 35.08  ? 321 LEU A O   1 
ATOM   2401 C  CB  . LEU A  1  308 ? 63.937  4.433   43.482 1.00 41.24  ? 321 LEU A CB  1 
ATOM   2402 C  CG  . LEU A  1  308 ? 62.915  5.556   43.633 1.00 44.55  ? 321 LEU A CG  1 
ATOM   2403 C  CD1 . LEU A  1  308 ? 63.618  6.884   43.674 1.00 47.61  ? 321 LEU A CD1 1 
ATOM   2404 C  CD2 . LEU A  1  308 ? 61.950  5.533   42.466 1.00 48.63  ? 321 LEU A CD2 1 
ATOM   2405 N  N   . ILE A  1  309 ? 65.372  1.722   43.029 1.00 35.76  ? 322 ILE A N   1 
ATOM   2406 C  CA  . ILE A  1  309 ? 66.154  0.891   42.135 1.00 38.47  ? 322 ILE A CA  1 
ATOM   2407 C  C   . ILE A  1  309 ? 65.482  -0.471  42.003 1.00 37.47  ? 322 ILE A C   1 
ATOM   2408 O  O   . ILE A  1  309 ? 65.384  -0.999  40.901 1.00 37.43  ? 322 ILE A O   1 
ATOM   2409 C  CB  . ILE A  1  309 ? 67.610  0.781   42.612 1.00 38.11  ? 322 ILE A CB  1 
ATOM   2410 C  CG1 . ILE A  1  309 ? 68.368  2.077   42.331 1.00 40.44  ? 322 ILE A CG1 1 
ATOM   2411 C  CG2 . ILE A  1  309 ? 68.318  -0.409  41.963 1.00 38.69  ? 322 ILE A CG2 1 
ATOM   2412 C  CD1 . ILE A  1  309 ? 69.692  2.189   43.076 1.00 41.09  ? 322 ILE A CD1 1 
ATOM   2413 N  N   . LYS A  1  310 ? 65.013  -1.014  43.129 1.00 37.05  ? 323 LYS A N   1 
ATOM   2414 C  CA  . LYS A  1  310 ? 64.371  -2.324  43.142 1.00 37.03  ? 323 LYS A CA  1 
ATOM   2415 C  C   . LYS A  1  310 ? 63.040  -2.315  42.387 1.00 35.92  ? 323 LYS A C   1 
ATOM   2416 O  O   . LYS A  1  310 ? 62.801  -3.189  41.549 1.00 34.75  ? 323 LYS A O   1 
ATOM   2417 C  CB  . LYS A  1  310 ? 64.185  -2.805  44.582 1.00 37.38  ? 323 LYS A CB  1 
ATOM   2418 C  CG  . LYS A  1  310 ? 65.465  -3.336  45.188 1.00 36.65  ? 323 LYS A CG  1 
ATOM   2419 C  CD  . LYS A  1  310 ? 65.364  -3.668  46.665 1.00 40.85  ? 323 LYS A CD  1 
ATOM   2420 C  CE  . LYS A  1  310 ? 66.473  -4.588  47.099 1.00 44.66  ? 323 LYS A CE  1 
ATOM   2421 N  NZ  . LYS A  1  310 ? 66.489  -4.614  48.565 1.00 51.12  ? 323 LYS A NZ  1 
ATOM   2422 N  N   . ASN A  1  311 ? 62.196  -1.318  42.681 1.00 33.11  ? 324 ASN A N   1 
ATOM   2423 C  CA  . ASN A  1  311 ? 60.886  -1.227  42.067 1.00 31.93  ? 324 ASN A CA  1 
ATOM   2424 C  C   . ASN A  1  311 ? 61.031  -1.033  40.559 1.00 32.47  ? 324 ASN A C   1 
ATOM   2425 O  O   . ASN A  1  311 ? 60.257  -1.588  39.792 1.00 33.55  ? 324 ASN A O   1 
ATOM   2426 C  CB  . ASN A  1  311 ? 60.023  -0.179  42.756 1.00 31.14  ? 324 ASN A CB  1 
ATOM   2427 C  CG  . ASN A  1  311 ? 59.348  -0.735  43.988 1.00 34.23  ? 324 ASN A CG  1 
ATOM   2428 O  OD1 . ASN A  1  311 ? 58.359  -1.472  43.883 1.00 39.28  ? 324 ASN A OD1 1 
ATOM   2429 N  ND2 . ASN A  1  311 ? 59.826  -0.378  45.170 1.00 35.31  ? 324 ASN A ND2 1 
ATOM   2430 N  N   . LEU A  1  312 ? 62.031  -0.268  40.128 1.00 35.14  ? 325 LEU A N   1 
ATOM   2431 C  CA  . LEU A  1  312 ? 62.249  -0.039  38.707 1.00 34.75  ? 325 LEU A CA  1 
ATOM   2432 C  C   . LEU A  1  312 ? 62.653  -1.348  38.040 1.00 33.77  ? 325 LEU A C   1 
ATOM   2433 O  O   . LEU A  1  312 ? 62.207  -1.630  36.934 1.00 35.96  ? 325 LEU A O   1 
ATOM   2434 C  CB  . LEU A  1  312 ? 63.305  1.037   38.470 1.00 35.74  ? 325 LEU A CB  1 
ATOM   2435 C  CG  . LEU A  1  312 ? 62.843  2.490   38.604 1.00 35.82  ? 325 LEU A CG  1 
ATOM   2436 C  CD1 . LEU A  1  312 ? 64.011  3.439   38.811 1.00 36.59  ? 325 LEU A CD1 1 
ATOM   2437 C  CD2 . LEU A  1  312 ? 62.062  2.908   37.381 1.00 38.06  ? 325 LEU A CD2 1 
ATOM   2438 N  N   . HIS A  1  313 ? 63.505  -2.128  38.712 1.00 32.98  ? 326 HIS A N   1 
ATOM   2439 C  CA  . HIS A  1  313 ? 63.931  -3.415  38.188 1.00 33.86  ? 326 HIS A CA  1 
ATOM   2440 C  C   . HIS A  1  313 ? 62.734  -4.362  38.114 1.00 32.16  ? 326 HIS A C   1 
ATOM   2441 O  O   . HIS A  1  313 ? 62.517  -4.982  37.084 1.00 30.39  ? 326 HIS A O   1 
ATOM   2442 C  CB  . HIS A  1  313 ? 65.117  -3.982  38.981 1.00 35.78  ? 326 HIS A CB  1 
ATOM   2443 C  CG  . HIS A  1  313 ? 65.571  -5.281  38.416 1.00 39.74  ? 326 HIS A CG  1 
ATOM   2444 N  ND1 . HIS A  1  313 ? 66.107  -5.360  37.147 1.00 38.83  ? 326 HIS A ND1 1 
ATOM   2445 C  CD2 . HIS A  1  313 ? 65.472  -6.545  38.870 1.00 41.35  ? 326 HIS A CD2 1 
ATOM   2446 C  CE1 . HIS A  1  313 ? 66.375  -6.628  36.874 1.00 39.60  ? 326 HIS A CE1 1 
ATOM   2447 N  NE2 . HIS A  1  313 ? 65.983  -7.366  37.897 1.00 41.12  ? 326 HIS A NE2 1 
ATOM   2448 N  N   . TYR A  1  314 ? 61.941  -4.450  39.191 1.00 35.56  ? 327 TYR A N   1 
ATOM   2449 C  CA  . TYR A  1  314 ? 60.741  -5.276  39.190 1.00 34.48  ? 327 TYR A CA  1 
ATOM   2450 C  C   . TYR A  1  314 ? 59.842  -4.927  38.002 1.00 36.12  ? 327 TYR A C   1 
ATOM   2451 O  O   . TYR A  1  314 ? 59.370  -5.819  37.299 1.00 37.45  ? 327 TYR A O   1 
ATOM   2452 C  CB  . TYR A  1  314 ? 59.929  -5.129  40.478 1.00 35.30  ? 327 TYR A CB  1 
ATOM   2453 C  CG  . TYR A  1  314 ? 60.679  -5.535  41.736 1.00 36.34  ? 327 TYR A CG  1 
ATOM   2454 C  CD1 . TYR A  1  314 ? 61.734  -6.439  41.691 1.00 35.25  ? 327 TYR A CD1 1 
ATOM   2455 C  CD2 . TYR A  1  314 ? 60.316  -5.015  42.976 1.00 36.91  ? 327 TYR A CD2 1 
ATOM   2456 C  CE1 . TYR A  1  314 ? 62.417  -6.805  42.839 1.00 36.50  ? 327 TYR A CE1 1 
ATOM   2457 C  CE2 . TYR A  1  314 ? 60.978  -5.385  44.131 1.00 38.60  ? 327 TYR A CE2 1 
ATOM   2458 C  CZ  . TYR A  1  314 ? 62.038  -6.274  44.062 1.00 40.06  ? 327 TYR A CZ  1 
ATOM   2459 O  OH  . TYR A  1  314 ? 62.695  -6.626  45.205 1.00 38.36  ? 327 TYR A OH  1 
ATOM   2460 N  N   . TRP A  1  315 ? 59.604  -3.634  37.774 1.00 35.77  ? 328 TRP A N   1 
ATOM   2461 C  CA  . TRP A  1  315 ? 58.728  -3.231  36.689 1.00 36.96  ? 328 TRP A CA  1 
ATOM   2462 C  C   . TRP A  1  315 ? 59.310  -3.715  35.364 1.00 36.88  ? 328 TRP A C   1 
ATOM   2463 O  O   . TRP A  1  315 ? 58.598  -4.256  34.524 1.00 35.93  ? 328 TRP A O   1 
ATOM   2464 C  CB  . TRP A  1  315 ? 58.516  -1.711  36.687 1.00 37.09  ? 328 TRP A CB  1 
ATOM   2465 C  CG  . TRP A  1  315 ? 57.415  -1.243  35.769 1.00 34.35  ? 328 TRP A CG  1 
ATOM   2466 C  CD1 . TRP A  1  315 ? 56.152  -1.742  35.651 1.00 33.84  ? 328 TRP A CD1 1 
ATOM   2467 C  CD2 . TRP A  1  315 ? 57.511  -0.176  34.804 1.00 35.30  ? 328 TRP A CD2 1 
ATOM   2468 N  NE1 . TRP A  1  315 ? 55.452  -1.059  34.687 1.00 33.13  ? 328 TRP A NE1 1 
ATOM   2469 C  CE2 . TRP A  1  315 ? 56.255  -0.088  34.157 1.00 34.54  ? 328 TRP A CE2 1 
ATOM   2470 C  CE3 . TRP A  1  315 ? 58.531  0.704   34.431 1.00 34.41  ? 328 TRP A CE3 1 
ATOM   2471 C  CZ2 . TRP A  1  315 ? 56.000  0.855   33.167 1.00 33.34  ? 328 TRP A CZ2 1 
ATOM   2472 C  CZ3 . TRP A  1  315 ? 58.277  1.625   33.441 1.00 35.47  ? 328 TRP A CZ3 1 
ATOM   2473 C  CH2 . TRP A  1  315 ? 57.031  1.698   32.823 1.00 35.10  ? 328 TRP A CH2 1 
ATOM   2474 N  N   . TRP A  1  316 ? 60.614  -3.522  35.185 1.00 35.37  ? 329 TRP A N   1 
ATOM   2475 C  CA  . TRP A  1  316 ? 61.253  -3.870  33.930 1.00 37.78  ? 329 TRP A CA  1 
ATOM   2476 C  C   . TRP A  1  316 ? 61.066  -5.360  33.636 1.00 36.69  ? 329 TRP A C   1 
ATOM   2477 O  O   . TRP A  1  316 ? 60.888  -5.728  32.487 1.00 32.34  ? 329 TRP A O   1 
ATOM   2478 C  CB  . TRP A  1  316 ? 62.742  -3.470  33.948 1.00 41.46  ? 329 TRP A CB  1 
ATOM   2479 C  CG  . TRP A  1  316 ? 63.477  -3.969  32.737 1.00 39.80  ? 329 TRP A CG  1 
ATOM   2480 C  CD1 . TRP A  1  316 ? 63.511  -3.385  31.507 1.00 40.77  ? 329 TRP A CD1 1 
ATOM   2481 C  CD2 . TRP A  1  316 ? 64.173  -5.221  32.610 1.00 39.93  ? 329 TRP A CD2 1 
ATOM   2482 N  NE1 . TRP A  1  316 ? 64.201  -4.176  30.629 1.00 39.62  ? 329 TRP A NE1 1 
ATOM   2483 C  CE2 . TRP A  1  316 ? 64.613  -5.310  31.275 1.00 37.88  ? 329 TRP A CE2 1 
ATOM   2484 C  CE3 . TRP A  1  316 ? 64.466  -6.269  33.487 1.00 44.66  ? 329 TRP A CE3 1 
ATOM   2485 C  CZ2 . TRP A  1  316 ? 65.332  -6.402  30.802 1.00 39.31  ? 329 TRP A CZ2 1 
ATOM   2486 C  CZ3 . TRP A  1  316 ? 65.182  -7.349  33.018 1.00 43.93  ? 329 TRP A CZ3 1 
ATOM   2487 C  CH2 . TRP A  1  316 ? 65.594  -7.420  31.689 1.00 40.30  ? 329 TRP A CH2 1 
ATOM   2488 N  N   . THR A  1  317 ? 61.102  -6.228  34.656 1.00 39.76  ? 330 THR A N   1 
ATOM   2489 C  CA  . THR A  1  317 ? 60.986  -7.662  34.410 1.00 41.73  ? 330 THR A CA  1 
ATOM   2490 C  C   . THR A  1  317 ? 59.657  -7.951  33.716 1.00 42.36  ? 330 THR A C   1 
ATOM   2491 O  O   . THR A  1  317 ? 59.585  -8.852  32.892 1.00 44.51  ? 330 THR A O   1 
ATOM   2492 C  CB  . THR A  1  317 ? 61.092  -8.518  35.675 1.00 40.81  ? 330 THR A CB  1 
ATOM   2493 O  OG1 . THR A  1  317 ? 59.986  -8.250  36.536 1.00 40.11  ? 330 THR A OG1 1 
ATOM   2494 C  CG2 . THR A  1  317 ? 62.385  -8.295  36.428 1.00 40.60  ? 330 THR A CG2 1 
ATOM   2495 N  N   . GLY A  1  318 ? 58.599  -7.217  34.079 1.00 40.34  ? 331 GLY A N   1 
ATOM   2496 C  CA  . GLY A  1  318 ? 57.315  -7.366  33.420 1.00 40.10  ? 331 GLY A CA  1 
ATOM   2497 C  C   . GLY A  1  318 ? 57.300  -6.715  32.033 1.00 37.76  ? 331 GLY A C   1 
ATOM   2498 O  O   . GLY A  1  318 ? 56.850  -7.312  31.067 1.00 36.17  ? 331 GLY A O   1 
ATOM   2499 N  N   . VAL A  1  319 ? 57.777  -5.475  31.952 1.00 38.52  ? 332 VAL A N   1 
ATOM   2500 C  CA  . VAL A  1  319 ? 57.759  -4.704  30.719 1.00 39.99  ? 332 VAL A CA  1 
ATOM   2501 C  C   . VAL A  1  319 ? 58.533  -5.430  29.623 1.00 40.63  ? 332 VAL A C   1 
ATOM   2502 O  O   . VAL A  1  319 ? 58.120  -5.417  28.471 1.00 41.62  ? 332 VAL A O   1 
ATOM   2503 C  CB  . VAL A  1  319 ? 58.355  -3.315  30.998 1.00 42.47  ? 332 VAL A CB  1 
ATOM   2504 C  CG1 . VAL A  1  319 ? 58.840  -2.608  29.741 1.00 41.15  ? 332 VAL A CG1 1 
ATOM   2505 C  CG2 . VAL A  1  319 ? 57.370  -2.448  31.767 1.00 44.53  ? 332 VAL A CG2 1 
ATOM   2506 N  N   . ASN A  1  320 ? 59.651  -6.056  29.999 1.00 43.26  ? 333 ASN A N   1 
ATOM   2507 C  CA  . ASN A  1  320 ? 60.542  -6.712  29.052 1.00 45.91  ? 333 ASN A CA  1 
ATOM   2508 C  C   . ASN A  1  320 ? 59.800  -7.803  28.286 1.00 44.34  ? 333 ASN A C   1 
ATOM   2509 O  O   . ASN A  1  320 ? 59.932  -7.893  27.067 1.00 39.14  ? 333 ASN A O   1 
ATOM   2510 C  CB  . ASN A  1  320 ? 61.773  -7.294  29.741 1.00 46.14  ? 333 ASN A CB  1 
ATOM   2511 C  CG  . ASN A  1  320 ? 62.833  -7.714  28.754 1.00 43.20  ? 333 ASN A CG  1 
ATOM   2512 O  OD1 . ASN A  1  320 ? 63.157  -6.969  27.823 1.00 45.32  ? 333 ASN A OD1 1 
ATOM   2513 N  ND2 . ASN A  1  320 ? 63.379  -8.902  28.930 1.00 39.69  ? 333 ASN A ND2 1 
ATOM   2514 N  N   . VAL A  1  321 ? 59.031  -8.615  29.016 1.00 40.95  ? 334 VAL A N   1 
ATOM   2515 C  CA  . VAL A  1  321 ? 58.226  -9.668  28.427 1.00 43.82  ? 334 VAL A CA  1 
ATOM   2516 C  C   . VAL A  1  321 ? 57.038  -9.054  27.692 1.00 42.51  ? 334 VAL A C   1 
ATOM   2517 O  O   . VAL A  1  321 ? 56.761  -9.423  26.563 1.00 49.20  ? 334 VAL A O   1 
ATOM   2518 C  CB  . VAL A  1  321 ? 57.725  -10.682 29.476 1.00 50.87  ? 334 VAL A CB  1 
ATOM   2519 C  CG1 . VAL A  1  321 ? 56.798  -11.742 28.875 1.00 49.60  ? 334 VAL A CG1 1 
ATOM   2520 C  CG2 . VAL A  1  321 ? 58.873  -11.322 30.251 1.00 48.59  ? 334 VAL A CG2 1 
ATOM   2521 N  N   . ALA A  1  322 ? 56.313  -8.139  28.332 1.00 43.91  ? 335 ALA A N   1 
ATOM   2522 C  CA  . ALA A  1  322 ? 55.045  -7.670  27.792 1.00 42.74  ? 335 ALA A CA  1 
ATOM   2523 C  C   . ALA A  1  322 ? 55.255  -6.866  26.512 1.00 43.58  ? 335 ALA A C   1 
ATOM   2524 O  O   . ALA A  1  322 ? 54.430  -6.938  25.613 1.00 49.44  ? 335 ALA A O   1 
ATOM   2525 C  CB  . ALA A  1  322 ? 54.296  -6.850  28.827 1.00 44.67  ? 335 ALA A CB  1 
ATOM   2526 N  N   . PHE A  1  323 ? 56.339  -6.082  26.435 1.00 46.61  ? 336 PHE A N   1 
ATOM   2527 C  CA  . PHE A  1  323 ? 56.564  -5.195  25.300 1.00 46.90  ? 336 PHE A CA  1 
ATOM   2528 C  C   . PHE A  1  323 ? 57.517  -5.814  24.267 1.00 48.78  ? 336 PHE A C   1 
ATOM   2529 O  O   . PHE A  1  323 ? 57.872  -5.153  23.292 1.00 51.62  ? 336 PHE A O   1 
ATOM   2530 C  CB  . PHE A  1  323 ? 57.112  -3.842  25.769 1.00 45.35  ? 336 PHE A CB  1 
ATOM   2531 C  CG  . PHE A  1  323 ? 56.178  -2.999  26.627 1.00 47.89  ? 336 PHE A CG  1 
ATOM   2532 C  CD1 . PHE A  1  323 ? 54.883  -3.409  26.909 1.00 51.89  ? 336 PHE A CD1 1 
ATOM   2533 C  CD2 . PHE A  1  323 ? 56.580  -1.767  27.112 1.00 50.41  ? 336 PHE A CD2 1 
ATOM   2534 C  CE1 . PHE A  1  323 ? 54.041  -2.632  27.683 1.00 52.33  ? 336 PHE A CE1 1 
ATOM   2535 C  CE2 . PHE A  1  323 ? 55.729  -0.994  27.887 1.00 52.65  ? 336 PHE A CE2 1 
ATOM   2536 C  CZ  . PHE A  1  323 ? 54.463  -1.429  28.173 1.00 51.45  ? 336 PHE A CZ  1 
ATOM   2537 N  N   . GLY A  1  324 ? 57.949  -7.061  24.478 1.00 48.63  ? 337 GLY A N   1 
ATOM   2538 C  CA  . GLY A  1  324 ? 58.719  -7.793  23.481 1.00 51.33  ? 337 GLY A CA  1 
ATOM   2539 C  C   . GLY A  1  324 ? 60.197  -7.392  23.423 1.00 53.09  ? 337 GLY A C   1 
ATOM   2540 O  O   . GLY A  1  324 ? 60.811  -7.484  22.366 1.00 49.71  ? 337 GLY A O   1 
ATOM   2541 N  N   . GLY A  1  325 ? 60.764  -6.974  24.564 1.00 56.02  ? 338 GLY A N   1 
ATOM   2542 C  CA  . GLY A  1  325 ? 62.174  -6.618  24.693 1.00 50.25  ? 338 GLY A CA  1 
ATOM   2543 C  C   . GLY A  1  325 ? 62.388  -5.103  24.773 1.00 52.52  ? 338 GLY A C   1 
ATOM   2544 O  O   . GLY A  1  325 ? 62.173  -4.407  23.790 1.00 51.52  ? 338 GLY A O   1 
ATOM   2545 N  N   . CYS A  1  326 ? 62.804  -4.598  25.950 1.00 58.26  ? 339 CYS A N   1 
ATOM   2546 C  CA  . CYS A  1  326 ? 63.252  -3.216  26.109 1.00 59.57  ? 339 CYS A CA  1 
ATOM   2547 C  C   . CYS A  1  326 ? 64.591  -3.188  26.839 1.00 51.84  ? 339 CYS A C   1 
ATOM   2548 O  O   . CYS A  1  326 ? 64.796  -3.967  27.761 1.00 49.87  ? 339 CYS A O   1 
ATOM   2549 C  CB  . CYS A  1  326 ? 62.299  -2.363  26.941 1.00 62.71  ? 339 CYS A CB  1 
ATOM   2550 S  SG  . CYS A  1  326 ? 60.707  -1.990  26.153 1.00 89.43  ? 339 CYS A SG  1 
ATOM   2551 N  N   . ASP A  1  327 ? 65.472  -2.260  26.455 1.00 51.48  ? 340 ASP A N   1 
ATOM   2552 C  CA  . ASP A  1  327 ? 66.742  -2.083  27.152 1.00 51.78  ? 340 ASP A CA  1 
ATOM   2553 C  C   . ASP A  1  327 ? 66.481  -1.405  28.495 1.00 45.33  ? 340 ASP A C   1 
ATOM   2554 O  O   . ASP A  1  327 ? 65.904  -0.312  28.548 1.00 42.61  ? 340 ASP A O   1 
ATOM   2555 C  CB  . ASP A  1  327 ? 67.748  -1.263  26.363 1.00 55.55  ? 340 ASP A CB  1 
ATOM   2556 C  CG  . ASP A  1  327 ? 68.159  -1.832  25.016 1.00 60.99  ? 340 ASP A CG  1 
ATOM   2557 O  OD1 . ASP A  1  327 ? 68.502  -3.026  24.962 1.00 59.09  ? 340 ASP A OD1 1 
ATOM   2558 O  OD2 . ASP A  1  327 ? 68.143  -1.063  24.042 1.00 69.69  ? 340 ASP A OD2 1 
ATOM   2559 N  N   . GLU A  1  328 ? 66.922  -2.065  29.575 1.00 39.98  ? 341 GLU A N   1 
ATOM   2560 C  CA  . GLU A  1  328 ? 66.706  -1.554  30.916 1.00 41.59  ? 341 GLU A CA  1 
ATOM   2561 C  C   . GLU A  1  328 ? 67.515  -0.273  31.115 1.00 40.85  ? 341 GLU A C   1 
ATOM   2562 O  O   . GLU A  1  328 ? 68.683  -0.221  30.750 1.00 39.70  ? 341 GLU A O   1 
ATOM   2563 C  CB  . GLU A  1  328 ? 67.043  -2.634  31.943 1.00 42.45  ? 341 GLU A CB  1 
ATOM   2564 C  CG  . GLU A  1  328 ? 66.763  -2.217  33.385 1.00 43.99  ? 341 GLU A CG  1 
ATOM   2565 C  CD  . GLU A  1  328 ? 66.925  -3.305  34.444 1.00 45.63  ? 341 GLU A CD  1 
ATOM   2566 O  OE1 . GLU A  1  328 ? 67.346  -4.425  34.098 1.00 49.14  ? 341 GLU A OE1 1 
ATOM   2567 O  OE2 . GLU A  1  328 ? 66.624  -3.034  35.627 1.00 45.22  ? 341 GLU A OE2 1 
ATOM   2568 N  N   . LEU A  1  329 ? 66.872  0.744   31.705 1.00 42.90  ? 342 LEU A N   1 
ATOM   2569 C  CA  . LEU A  1  329 ? 67.511  1.995   32.081 1.00 42.64  ? 342 LEU A CA  1 
ATOM   2570 C  C   . LEU A  1  329 ? 67.865  1.966   33.565 1.00 42.54  ? 342 LEU A C   1 
ATOM   2571 O  O   . LEU A  1  329 ? 67.148  1.334   34.350 1.00 40.00  ? 342 LEU A O   1 
ATOM   2572 C  CB  . LEU A  1  329 ? 66.554  3.145   31.785 1.00 42.55  ? 342 LEU A CB  1 
ATOM   2573 C  CG  . LEU A  1  329 ? 66.150  3.333   30.321 1.00 44.03  ? 342 LEU A CG  1 
ATOM   2574 C  CD1 . LEU A  1  329 ? 65.020  4.352   30.198 1.00 42.27  ? 342 LEU A CD1 1 
ATOM   2575 C  CD2 . LEU A  1  329 ? 67.341  3.754   29.491 1.00 45.20  ? 342 LEU A CD2 1 
ATOM   2576 N  N   . PHE A  1  330 ? 68.945  2.686   33.931 1.00 44.91  ? 343 PHE A N   1 
ATOM   2577 C  CA  . PHE A  1  330 ? 69.432  2.710   35.301 1.00 43.72  ? 343 PHE A CA  1 
ATOM   2578 C  C   . PHE A  1  330 ? 69.650  4.142   35.769 1.00 44.82  ? 343 PHE A C   1 
ATOM   2579 O  O   . PHE A  1  330 ? 70.769  4.541   36.065 1.00 49.24  ? 343 PHE A O   1 
ATOM   2580 C  CB  . PHE A  1  330 ? 70.733  1.917   35.406 1.00 41.87  ? 343 PHE A CB  1 
ATOM   2581 C  CG  . PHE A  1  330 ? 70.594  0.453   35.025 1.00 44.33  ? 343 PHE A CG  1 
ATOM   2582 C  CD1 . PHE A  1  330 ? 70.118  -0.498  35.937 1.00 48.72  ? 343 PHE A CD1 1 
ATOM   2583 C  CD2 . PHE A  1  330 ? 70.942  0.037   33.749 1.00 42.33  ? 343 PHE A CD2 1 
ATOM   2584 C  CE1 . PHE A  1  330 ? 69.965  -1.827  35.560 1.00 48.26  ? 343 PHE A CE1 1 
ATOM   2585 C  CE2 . PHE A  1  330 ? 70.822  -1.297  33.387 1.00 43.72  ? 343 PHE A CE2 1 
ATOM   2586 C  CZ  . PHE A  1  330 ? 70.338  -2.224  34.292 1.00 46.94  ? 343 PHE A CZ  1 
ATOM   2587 N  N   . PRO A  1  331 ? 68.587  4.952   35.926 1.00 46.50  ? 344 PRO A N   1 
ATOM   2588 C  CA  . PRO A  1  331 ? 68.770  6.364   36.265 1.00 42.41  ? 344 PRO A CA  1 
ATOM   2589 C  C   . PRO A  1  331 ? 69.364  6.629   37.644 1.00 39.17  ? 344 PRO A C   1 
ATOM   2590 O  O   . PRO A  1  331 ? 69.779  7.752   37.913 1.00 40.54  ? 344 PRO A O   1 
ATOM   2591 C  CB  . PRO A  1  331 ? 67.342  6.904   36.146 1.00 45.83  ? 344 PRO A CB  1 
ATOM   2592 C  CG  . PRO A  1  331 ? 66.501  5.701   36.543 1.00 45.97  ? 344 PRO A CG  1 
ATOM   2593 C  CD  . PRO A  1  331 ? 67.172  4.554   35.827 1.00 45.48  ? 344 PRO A CD  1 
ATOM   2594 N  N   . TYR A  1  332 ? 69.394  5.616   38.520 1.00 36.81  ? 345 TYR A N   1 
ATOM   2595 C  CA  . TYR A  1  332 ? 69.981  5.777   39.844 1.00 36.55  ? 345 TYR A CA  1 
ATOM   2596 C  C   . TYR A  1  332 ? 71.114  4.774   40.047 1.00 35.11  ? 345 TYR A C   1 
ATOM   2597 O  O   . TYR A  1  332 ? 71.527  4.519   41.178 1.00 32.54  ? 345 TYR A O   1 
ATOM   2598 C  CB  . TYR A  1  332 ? 68.917  5.643   40.938 1.00 36.50  ? 345 TYR A CB  1 
ATOM   2599 C  CG  . TYR A  1  332 ? 67.741  6.587   40.721 1.00 39.60  ? 345 TYR A CG  1 
ATOM   2600 C  CD1 . TYR A  1  332 ? 67.866  7.965   40.879 1.00 39.80  ? 345 TYR A CD1 1 
ATOM   2601 C  CD2 . TYR A  1  332 ? 66.500  6.092   40.339 1.00 44.00  ? 345 TYR A CD2 1 
ATOM   2602 C  CE1 . TYR A  1  332 ? 66.795  8.812   40.653 1.00 44.39  ? 345 TYR A CE1 1 
ATOM   2603 C  CE2 . TYR A  1  332 ? 65.418  6.928   40.121 1.00 45.38  ? 345 TYR A CE2 1 
ATOM   2604 C  CZ  . TYR A  1  332 ? 65.565  8.290   40.279 1.00 44.66  ? 345 TYR A CZ  1 
ATOM   2605 O  OH  . TYR A  1  332 ? 64.488  9.088   40.062 1.00 42.45  ? 345 TYR A OH  1 
ATOM   2606 N  N   . GLY A  1  333 ? 71.605  4.226   38.930 1.00 36.28  ? 346 GLY A N   1 
ATOM   2607 C  CA  . GLY A  1  333 ? 72.654  3.231   38.940 1.00 39.36  ? 346 GLY A CA  1 
ATOM   2608 C  C   . GLY A  1  333 ? 72.166  1.897   39.489 1.00 45.47  ? 346 GLY A C   1 
ATOM   2609 O  O   . GLY A  1  333 ? 70.963  1.613   39.515 1.00 53.18  ? 346 GLY A O   1 
ATOM   2610 N  N   . GLN A  1  334 ? 73.145  1.101   39.941 1.00 49.59  ? 347 GLN A N   1 
ATOM   2611 C  CA  A GLN A  1  334 ? 72.910  -0.200  40.538 0.50 52.53  ? 347 GLN A CA  1 
ATOM   2612 C  CA  B GLN A  1  334 ? 72.891  -0.199  40.541 0.50 53.78  ? 347 GLN A CA  1 
ATOM   2613 C  C   . GLN A  1  334 ? 73.035  -0.076  42.054 1.00 53.80  ? 347 GLN A C   1 
ATOM   2614 O  O   . GLN A  1  334 ? 73.505  0.943   42.556 1.00 54.14  ? 347 GLN A O   1 
ATOM   2615 C  CB  A GLN A  1  334 ? 73.904  -1.189  39.931 0.50 54.83  ? 347 GLN A CB  1 
ATOM   2616 C  CB  B GLN A  1  334 ? 73.793  -1.268  39.923 0.50 58.22  ? 347 GLN A CB  1 
ATOM   2617 C  CG  A GLN A  1  334 ? 73.538  -1.638  38.517 0.50 58.98  ? 347 GLN A CG  1 
ATOM   2618 C  CG  B GLN A  1  334 ? 73.362  -1.643  38.506 0.50 63.63  ? 347 GLN A CG  1 
ATOM   2619 C  CD  A GLN A  1  334 ? 73.980  -0.695  37.414 0.50 59.37  ? 347 GLN A CD  1 
ATOM   2620 C  CD  B GLN A  1  334 ? 73.495  -3.114  38.166 0.50 66.60  ? 347 GLN A CD  1 
ATOM   2621 O  OE1 A GLN A  1  334 ? 74.584  0.356   37.655 0.50 59.31  ? 347 GLN A OE1 1 
ATOM   2622 O  OE1 B GLN A  1  334 ? 73.825  -3.958  39.009 0.50 67.18  ? 347 GLN A OE1 1 
ATOM   2623 N  NE2 A GLN A  1  334 ? 73.704  -1.082  36.176 0.50 56.58  ? 347 GLN A NE2 1 
ATOM   2624 N  NE2 B GLN A  1  334 ? 73.215  -3.430  36.910 0.50 63.65  ? 347 GLN A NE2 1 
ATOM   2625 N  N   . LEU A  1  335 ? 72.616  -1.121  42.769 1.00 57.30  ? 348 LEU A N   1 
ATOM   2626 C  CA  . LEU A  1  335 ? 72.559  -1.096  44.226 1.00 66.09  ? 348 LEU A CA  1 
ATOM   2627 C  C   . LEU A  1  335 ? 73.947  -0.820  44.837 1.00 68.52  ? 348 LEU A C   1 
ATOM   2628 O  O   . LEU A  1  335 ? 74.804  -1.740  44.815 1.00 71.86  ? 348 LEU A O   1 
ATOM   2629 C  CB  . LEU A  1  335 ? 71.949  -2.399  44.741 1.00 65.06  ? 348 LEU A CB  1 
ATOM   2630 C  CG  . LEU A  1  335 ? 70.420  -2.474  44.689 1.00 62.22  ? 348 LEU A CG  1 
ATOM   2631 C  CD1 . LEU A  1  335 ? 69.869  -3.853  45.016 1.00 59.44  ? 348 LEU A CD1 1 
ATOM   2632 C  CD2 . LEU A  1  335 ? 69.837  -1.425  45.625 1.00 59.44  ? 348 LEU A CD2 1 
ATOM   2633 N  N   . GLN B  1  1   ? 0.144   19.190  57.349 1.00 116.70 ? 14  GLN B N   1 
ATOM   2634 C  CA  . GLN B  1  1   ? 0.302   18.439  58.627 1.00 120.53 ? 14  GLN B CA  1 
ATOM   2635 C  C   . GLN B  1  1   ? -0.583  17.188  58.595 1.00 113.26 ? 14  GLN B C   1 
ATOM   2636 O  O   . GLN B  1  1   ? -0.078  16.086  58.379 1.00 100.56 ? 14  GLN B O   1 
ATOM   2637 C  CB  . GLN B  1  1   ? 0.025   19.353  59.827 1.00 124.77 ? 14  GLN B CB  1 
ATOM   2638 C  CG  . GLN B  1  1   ? 0.832   20.649  59.841 1.00 118.93 ? 14  GLN B CG  1 
ATOM   2639 C  CD  . GLN B  1  1   ? 0.403   21.613  60.926 1.00 113.09 ? 14  GLN B CD  1 
ATOM   2640 O  OE1 . GLN B  1  1   ? -0.413  21.294  61.801 1.00 104.18 ? 14  GLN B OE1 1 
ATOM   2641 N  NE2 . GLN B  1  1   ? 0.966   22.812  60.879 1.00 108.59 ? 14  GLN B NE2 1 
ATOM   2642 N  N   . GLY B  1  2   ? -1.911  17.382  58.735 1.00 103.80 ? 15  GLY B N   1 
ATOM   2643 C  CA  . GLY B  1  2   ? -2.870  16.299  58.912 1.00 87.01  ? 15  GLY B CA  1 
ATOM   2644 C  C   . GLY B  1  2   ? -3.372  15.735  57.583 1.00 72.34  ? 15  GLY B C   1 
ATOM   2645 O  O   . GLY B  1  2   ? -3.530  16.471  56.623 1.00 65.81  ? 15  GLY B O   1 
ATOM   2646 N  N   . VAL B  1  3   ? -3.608  14.422  57.542 1.00 65.01  ? 16  VAL B N   1 
ATOM   2647 C  CA  . VAL B  1  3   ? -3.810  13.701  56.299 1.00 65.70  ? 16  VAL B CA  1 
ATOM   2648 C  C   . VAL B  1  3   ? -5.039  12.824  56.477 1.00 59.86  ? 16  VAL B C   1 
ATOM   2649 O  O   . VAL B  1  3   ? -5.338  12.393  57.587 1.00 55.04  ? 16  VAL B O   1 
ATOM   2650 C  CB  . VAL B  1  3   ? -2.549  12.866  55.975 1.00 77.14  ? 16  VAL B CB  1 
ATOM   2651 C  CG1 . VAL B  1  3   ? -2.722  11.954  54.769 1.00 72.85  ? 16  VAL B CG1 1 
ATOM   2652 C  CG2 . VAL B  1  3   ? -1.315  13.745  55.782 1.00 83.88  ? 16  VAL B CG2 1 
ATOM   2653 N  N   . ASP B  1  4   ? -5.737  12.566  55.370 1.00 62.93  ? 17  ASP B N   1 
ATOM   2654 C  CA  . ASP B  1  4   ? -6.887  11.685  55.366 1.00 72.82  ? 17  ASP B CA  1 
ATOM   2655 C  C   . ASP B  1  4   ? -6.451  10.313  54.849 1.00 73.58  ? 17  ASP B C   1 
ATOM   2656 O  O   . ASP B  1  4   ? -6.174  10.176  53.659 1.00 74.33  ? 17  ASP B O   1 
ATOM   2657 C  CB  . ASP B  1  4   ? -8.004  12.310  54.547 1.00 76.63  ? 17  ASP B CB  1 
ATOM   2658 C  CG  . ASP B  1  4   ? -9.393  11.803  54.887 1.00 85.30  ? 17  ASP B CG  1 
ATOM   2659 O  OD1 . ASP B  1  4   ? -9.524  10.580  55.146 1.00 90.65  ? 17  ASP B OD1 1 
ATOM   2660 O  OD2 . ASP B  1  4   ? -10.324 12.633  54.872 1.00 97.13  ? 17  ASP B OD2 1 
ATOM   2661 N  N   . PRO B  1  5   ? -6.388  9.248   55.693 1.00 67.95  ? 18  PRO B N   1 
ATOM   2662 C  CA  . PRO B  1  5   ? -5.753  7.990   55.294 1.00 60.93  ? 18  PRO B CA  1 
ATOM   2663 C  C   . PRO B  1  5   ? -6.625  7.114   54.402 1.00 52.23  ? 18  PRO B C   1 
ATOM   2664 O  O   . PRO B  1  5   ? -7.732  6.749   54.797 1.00 51.31  ? 18  PRO B O   1 
ATOM   2665 C  CB  . PRO B  1  5   ? -5.428  7.269   56.616 1.00 62.51  ? 18  PRO B CB  1 
ATOM   2666 C  CG  . PRO B  1  5   ? -6.155  8.034   57.691 1.00 62.51  ? 18  PRO B CG  1 
ATOM   2667 C  CD  . PRO B  1  5   ? -6.942  9.171   57.053 1.00 65.85  ? 18  PRO B CD  1 
ATOM   2668 N  N   . PRO B  1  6   ? -6.124  6.684   53.222 1.00 50.07  ? 19  PRO B N   1 
ATOM   2669 C  CA  . PRO B  1  6   ? -6.902  5.844   52.317 1.00 46.93  ? 19  PRO B CA  1 
ATOM   2670 C  C   . PRO B  1  6   ? -7.072  4.454   52.912 1.00 45.18  ? 19  PRO B C   1 
ATOM   2671 O  O   . PRO B  1  6   ? -6.300  4.035   53.764 1.00 46.98  ? 19  PRO B O   1 
ATOM   2672 C  CB  . PRO B  1  6   ? -6.102  5.799   51.008 1.00 48.65  ? 19  PRO B CB  1 
ATOM   2673 C  CG  . PRO B  1  6   ? -4.699  6.239   51.381 1.00 51.93  ? 19  PRO B CG  1 
ATOM   2674 C  CD  . PRO B  1  6   ? -4.757  6.917   52.740 1.00 51.54  ? 19  PRO B CD  1 
ATOM   2675 N  N   . PRO B  1  7   ? -8.085  3.686   52.476 1.00 50.58  ? 20  PRO B N   1 
ATOM   2676 C  CA  . PRO B  1  7   ? -8.185  2.288   52.881 1.00 51.02  ? 20  PRO B CA  1 
ATOM   2677 C  C   . PRO B  1  7   ? -7.030  1.481   52.288 1.00 48.47  ? 20  PRO B C   1 
ATOM   2678 O  O   . PRO B  1  7   ? -6.376  1.906   51.338 1.00 48.28  ? 20  PRO B O   1 
ATOM   2679 C  CB  . PRO B  1  7   ? -9.574  1.873   52.350 1.00 52.26  ? 20  PRO B CB  1 
ATOM   2680 C  CG  . PRO B  1  7   ? -9.827  2.810   51.174 1.00 52.55  ? 20  PRO B CG  1 
ATOM   2681 C  CD  . PRO B  1  7   ? -9.166  4.118   51.575 1.00 52.05  ? 20  PRO B CD  1 
ATOM   2682 N  N   . PRO B  1  8   ? -6.715  0.296   52.839 1.00 46.42  ? 21  PRO B N   1 
ATOM   2683 C  CA  . PRO B  1  8   ? -5.599  -0.492  52.329 1.00 45.25  ? 21  PRO B CA  1 
ATOM   2684 C  C   . PRO B  1  8   ? -5.840  -0.969  50.906 1.00 45.49  ? 21  PRO B C   1 
ATOM   2685 O  O   . PRO B  1  8   ? -6.960  -1.295  50.539 1.00 51.02  ? 21  PRO B O   1 
ATOM   2686 C  CB  . PRO B  1  8   ? -5.490  -1.655  53.304 1.00 43.97  ? 21  PRO B CB  1 
ATOM   2687 C  CG  . PRO B  1  8   ? -6.862  -1.758  53.899 1.00 43.06  ? 21  PRO B CG  1 
ATOM   2688 C  CD  . PRO B  1  8   ? -7.380  -0.332  53.988 1.00 44.29  ? 21  PRO B CD  1 
ATOM   2689 N  N   . PRO B  1  9   ? -4.784  -1.052  50.077 1.00 42.12  ? 22  PRO B N   1 
ATOM   2690 C  CA  . PRO B  1  9   ? -4.892  -1.671  48.760 1.00 42.41  ? 22  PRO B CA  1 
ATOM   2691 C  C   . PRO B  1  9   ? -5.380  -3.106  48.892 1.00 41.69  ? 22  PRO B C   1 
ATOM   2692 O  O   . PRO B  1  9   ? -5.179  -3.741  49.930 1.00 44.21  ? 22  PRO B O   1 
ATOM   2693 C  CB  . PRO B  1  9   ? -3.461  -1.615  48.201 1.00 43.72  ? 22  PRO B CB  1 
ATOM   2694 C  CG  . PRO B  1  9   ? -2.795  -0.504  48.976 1.00 43.94  ? 22  PRO B CG  1 
ATOM   2695 C  CD  . PRO B  1  9   ? -3.435  -0.551  50.363 1.00 45.33  ? 22  PRO B CD  1 
ATOM   2696 N  N   . GLY B  1  10  ? -5.984  -3.609  47.812 1.00 38.89  ? 23  GLY B N   1 
ATOM   2697 C  CA  . GLY B  1  10  ? -6.336  -5.019  47.719 1.00 40.06  ? 23  GLY B CA  1 
ATOM   2698 C  C   . GLY B  1  10  ? -5.172  -5.833  47.154 1.00 41.10  ? 23  GLY B C   1 
ATOM   2699 O  O   . GLY B  1  10  ? -4.057  -5.314  47.005 1.00 37.88  ? 23  GLY B O   1 
ATOM   2700 N  N   . PRO B  1  11  ? -5.393  -7.125  46.822 1.00 37.93  ? 24  PRO B N   1 
ATOM   2701 C  CA  . PRO B  1  11  ? -4.363  -7.946  46.187 1.00 40.48  ? 24  PRO B CA  1 
ATOM   2702 C  C   . PRO B  1  11  ? -3.912  -7.331  44.868 1.00 43.70  ? 24  PRO B C   1 
ATOM   2703 O  O   . PRO B  1  11  ? -4.660  -6.584  44.246 1.00 48.35  ? 24  PRO B O   1 
ATOM   2704 C  CB  . PRO B  1  11  ? -5.041  -9.307  45.979 1.00 41.06  ? 24  PRO B CB  1 
ATOM   2705 C  CG  . PRO B  1  11  ? -6.172  -9.308  46.994 1.00 40.63  ? 24  PRO B CG  1 
ATOM   2706 C  CD  . PRO B  1  11  ? -6.640  -7.862  47.047 1.00 39.56  ? 24  PRO B CD  1 
ATOM   2707 N  N   . PRO B  1  12  ? -2.675  -7.605  44.405 1.00 52.28  ? 25  PRO B N   1 
ATOM   2708 C  CA  . PRO B  1  12  ? -2.229  -7.091  43.107 1.00 54.85  ? 25  PRO B CA  1 
ATOM   2709 C  C   . PRO B  1  12  ? -2.952  -7.798  41.959 1.00 54.33  ? 25  PRO B C   1 
ATOM   2710 O  O   . PRO B  1  12  ? -3.386  -8.939  42.116 1.00 48.03  ? 25  PRO B O   1 
ATOM   2711 C  CB  . PRO B  1  12  ? -0.714  -7.368  43.154 1.00 54.10  ? 25  PRO B CB  1 
ATOM   2712 C  CG  . PRO B  1  12  ? -0.563  -8.555  44.075 1.00 51.54  ? 25  PRO B CG  1 
ATOM   2713 C  CD  . PRO B  1  12  ? -1.659  -8.412  45.102 1.00 51.89  ? 25  PRO B CD  1 
ATOM   2714 N  N   . SER B  1  13  ? -3.096  -7.107  40.820 1.00 57.72  ? 26  SER B N   1 
ATOM   2715 C  CA  . SER B  1  13  ? -3.785  -7.666  39.658 1.00 57.29  ? 26  SER B CA  1 
ATOM   2716 C  C   . SER B  1  13  ? -3.116  -8.956  39.196 1.00 59.95  ? 26  SER B C   1 
ATOM   2717 O  O   . SER B  1  13  ? -3.797  -9.953  38.952 1.00 51.92  ? 26  SER B O   1 
ATOM   2718 C  CB  . SER B  1  13  ? -3.834  -6.690  38.523 1.00 55.65  ? 26  SER B CB  1 
ATOM   2719 O  OG  . SER B  1  13  ? -4.434  -5.486  38.967 1.00 64.67  ? 26  SER B OG  1 
ATOM   2720 N  N   . PHE B  1  14  ? -1.778  -8.907  39.065 1.00 58.13  ? 27  PHE B N   1 
ATOM   2721 C  CA  . PHE B  1  14  ? -0.991  -10.065 38.660 1.00 54.07  ? 27  PHE B CA  1 
ATOM   2722 C  C   . PHE B  1  14  ? -0.327  -10.674 39.898 1.00 45.68  ? 27  PHE B C   1 
ATOM   2723 O  O   . PHE B  1  14  ? 0.326   -9.965  40.653 1.00 38.20  ? 27  PHE B O   1 
ATOM   2724 C  CB  . PHE B  1  14  ? 0.013   -9.627  37.591 1.00 54.21  ? 27  PHE B CB  1 
ATOM   2725 C  CG  . PHE B  1  14  ? 0.960   -10.741 37.176 1.00 57.43  ? 27  PHE B CG  1 
ATOM   2726 C  CD1 . PHE B  1  14  ? 0.486   -11.819 36.431 1.00 57.06  ? 27  PHE B CD1 1 
ATOM   2727 C  CD2 . PHE B  1  14  ? 2.309   -10.718 37.540 1.00 56.41  ? 27  PHE B CD2 1 
ATOM   2728 C  CE1 . PHE B  1  14  ? 1.337   -12.850 36.059 1.00 58.70  ? 27  PHE B CE1 1 
ATOM   2729 C  CE2 . PHE B  1  14  ? 3.157   -11.759 37.175 1.00 57.73  ? 27  PHE B CE2 1 
ATOM   2730 C  CZ  . PHE B  1  14  ? 2.670   -12.819 36.430 1.00 58.49  ? 27  PHE B CZ  1 
ATOM   2731 N  N   . THR B  1  15  ? -0.513  -11.985 40.106 1.00 45.78  ? 28  THR B N   1 
ATOM   2732 C  CA  . THR B  1  15  ? -0.052  -12.649 41.320 1.00 45.57  ? 28  THR B CA  1 
ATOM   2733 C  C   . THR B  1  15  ? 0.913   -13.787 40.986 1.00 42.99  ? 28  THR B C   1 
ATOM   2734 O  O   . THR B  1  15  ? 1.134   -14.646 41.840 1.00 43.47  ? 28  THR B O   1 
ATOM   2735 C  CB  . THR B  1  15  ? -1.228  -13.193 42.150 1.00 47.00  ? 28  THR B CB  1 
ATOM   2736 O  OG1 . THR B  1  15  ? -1.859  -14.260 41.446 1.00 45.54  ? 28  THR B OG1 1 
ATOM   2737 C  CG2 . THR B  1  15  ? -2.286  -12.154 42.469 1.00 44.34  ? 28  THR B CG2 1 
ATOM   2738 N  N   . GLY B  1  16  ? 1.475   -13.815 39.764 1.00 39.95  ? 29  GLY B N   1 
ATOM   2739 C  CA  . GLY B  1  16  ? 2.460   -14.829 39.393 1.00 41.07  ? 29  GLY B CA  1 
ATOM   2740 C  C   . GLY B  1  16  ? 3.883   -14.415 39.783 1.00 41.75  ? 29  GLY B C   1 
ATOM   2741 O  O   . GLY B  1  16  ? 4.058   -13.353 40.379 1.00 39.12  ? 29  GLY B O   1 
ATOM   2742 N  N   . THR B  1  17  ? 4.893   -15.254 39.458 1.00 44.59  ? 30  THR B N   1 
ATOM   2743 C  CA  . THR B  1  17  ? 6.296   -14.884 39.658 1.00 44.94  ? 30  THR B CA  1 
ATOM   2744 C  C   . THR B  1  17  ? 6.636   -13.783 38.679 1.00 40.42  ? 30  THR B C   1 
ATOM   2745 O  O   . THR B  1  17  ? 5.986   -13.629 37.652 1.00 39.44  ? 30  THR B O   1 
ATOM   2746 C  CB  . THR B  1  17  ? 7.345   -15.965 39.420 1.00 45.74  ? 30  THR B CB  1 
ATOM   2747 O  OG1 . THR B  1  17  ? 7.129   -16.328 38.070 1.00 47.17  ? 30  THR B OG1 1 
ATOM   2748 C  CG2 . THR B  1  17  ? 7.160   -17.224 40.233 1.00 56.13  ? 30  THR B CG2 1 
ATOM   2749 N  N   . LYS B  1  18  ? 7.710   -13.081 39.014 1.00 40.65  ? 31  LYS B N   1 
ATOM   2750 C  CA  . LYS B  1  18  ? 8.298   -12.103 38.126 1.00 42.41  ? 31  LYS B CA  1 
ATOM   2751 C  C   . LYS B  1  18  ? 9.653   -11.728 38.704 1.00 39.80  ? 31  LYS B C   1 
ATOM   2752 O  O   . LYS B  1  18  ? 9.924   -11.970 39.883 1.00 37.34  ? 31  LYS B O   1 
ATOM   2753 C  CB  . LYS B  1  18  ? 7.393   -10.883 37.925 1.00 43.36  ? 31  LYS B CB  1 
ATOM   2754 C  CG  . LYS B  1  18  ? 7.127   -10.050 39.144 1.00 49.23  ? 31  LYS B CG  1 
ATOM   2755 C  CD  . LYS B  1  18  ? 6.453   -8.716  38.861 1.00 57.43  ? 31  LYS B CD  1 
ATOM   2756 C  CE  . LYS B  1  18  ? 7.030   -7.647  39.746 1.00 68.41  ? 31  LYS B CE  1 
ATOM   2757 N  NZ  . LYS B  1  18  ? 6.257   -6.409  39.778 1.00 76.55  ? 31  LYS B NZ  1 
ATOM   2758 N  N   . LEU B  1  19  ? 10.492  -11.157 37.842 1.00 37.05  ? 32  LEU B N   1 
ATOM   2759 C  CA  . LEU B  1  19  ? 11.751  -10.589 38.277 1.00 36.22  ? 32  LEU B CA  1 
ATOM   2760 C  C   . LEU B  1  19  ? 11.444  -9.351  39.108 1.00 37.05  ? 32  LEU B C   1 
ATOM   2761 O  O   . LEU B  1  19  ? 10.752  -8.463  38.617 1.00 37.34  ? 32  LEU B O   1 
ATOM   2762 C  CB  . LEU B  1  19  ? 12.602  -10.236 37.062 1.00 34.96  ? 32  LEU B CB  1 
ATOM   2763 C  CG  . LEU B  1  19  ? 13.909  -9.505  37.367 1.00 34.48  ? 32  LEU B CG  1 
ATOM   2764 C  CD1 . LEU B  1  19  ? 14.917  -10.447 38.038 1.00 35.57  ? 32  LEU B CD1 1 
ATOM   2765 C  CD2 . LEU B  1  19  ? 14.456  -8.887  36.108 1.00 33.80  ? 32  LEU B CD2 1 
ATOM   2766 N  N   . VAL B  1  20  ? 11.953  -9.307  40.353 1.00 35.88  ? 33  VAL B N   1 
ATOM   2767 C  CA  . VAL B  1  20  ? 11.713  -8.165  41.216 1.00 35.81  ? 33  VAL B CA  1 
ATOM   2768 C  C   . VAL B  1  20  ? 12.997  -7.361  41.400 1.00 39.47  ? 33  VAL B C   1 
ATOM   2769 O  O   . VAL B  1  20  ? 12.917  -6.159  41.659 1.00 38.58  ? 33  VAL B O   1 
ATOM   2770 C  CB  . VAL B  1  20  ? 11.089  -8.537  42.569 1.00 37.78  ? 33  VAL B CB  1 
ATOM   2771 C  CG1 . VAL B  1  20  ? 9.705   -9.143  42.386 1.00 39.11  ? 33  VAL B CG1 1 
ATOM   2772 C  CG2 . VAL B  1  20  ? 11.971  -9.456  43.402 1.00 39.46  ? 33  VAL B CG2 1 
ATOM   2773 N  N   . ASN B  1  21  ? 14.156  -8.027  41.257 1.00 40.47  ? 34  ASN B N   1 
ATOM   2774 C  CA  . ASN B  1  21  ? 15.457  -7.375  41.232 1.00 38.79  ? 34  ASN B CA  1 
ATOM   2775 C  C   . ASN B  1  21  ? 15.754  -6.882  39.818 1.00 39.52  ? 34  ASN B C   1 
ATOM   2776 O  O   . ASN B  1  21  ? 16.556  -7.478  39.110 1.00 43.44  ? 34  ASN B O   1 
ATOM   2777 C  CB  . ASN B  1  21  ? 16.534  -8.352  41.688 1.00 39.13  ? 34  ASN B CB  1 
ATOM   2778 C  CG  . ASN B  1  21  ? 17.877  -7.705  41.936 1.00 35.15  ? 34  ASN B CG  1 
ATOM   2779 O  OD1 . ASN B  1  21  ? 18.067  -6.512  41.676 1.00 33.16  ? 34  ASN B OD1 1 
ATOM   2780 N  ND2 . ASN B  1  21  ? 18.809  -8.483  42.458 1.00 33.81  ? 34  ASN B ND2 1 
ATOM   2781 N  N   . ASP B  1  22  ? 15.092  -5.799  39.405 1.00 43.18  ? 35  ASP B N   1 
ATOM   2782 C  CA  . ASP B  1  22  ? 15.044  -5.399  38.008 1.00 47.34  ? 35  ASP B CA  1 
ATOM   2783 C  C   . ASP B  1  22  ? 15.697  -4.027  37.866 1.00 46.25  ? 35  ASP B C   1 
ATOM   2784 O  O   . ASP B  1  22  ? 16.274  -3.514  38.824 1.00 44.65  ? 35  ASP B O   1 
ATOM   2785 C  CB  . ASP B  1  22  ? 13.627  -5.518  37.452 1.00 53.44  ? 35  ASP B CB  1 
ATOM   2786 C  CG  . ASP B  1  22  ? 12.561  -4.590  38.028 1.00 56.68  ? 35  ASP B CG  1 
ATOM   2787 O  OD1 . ASP B  1  22  ? 12.888  -3.785  38.926 1.00 53.07  ? 35  ASP B OD1 1 
ATOM   2788 O  OD2 . ASP B  1  22  ? 11.400  -4.666  37.561 1.00 63.73  ? 35  ASP B OD2 1 
ATOM   2789 N  N   . ALA B  1  23  ? 15.616  -3.450  36.659 1.00 46.12  ? 36  ALA B N   1 
ATOM   2790 C  CA  . ALA B  1  23  ? 16.371  -2.250  36.338 1.00 45.13  ? 36  ALA B CA  1 
ATOM   2791 C  C   . ALA B  1  23  ? 15.835  -1.050  37.112 1.00 40.20  ? 36  ALA B C   1 
ATOM   2792 O  O   . ALA B  1  23  ? 16.587  -0.153  37.474 1.00 40.50  ? 36  ALA B O   1 
ATOM   2793 C  CB  . ALA B  1  23  ? 16.338  -1.998  34.845 1.00 48.00  ? 36  ALA B CB  1 
ATOM   2794 N  N   . ASP B  1  24  ? 14.529  -1.043  37.360 1.00 40.02  ? 37  ASP B N   1 
ATOM   2795 C  CA  . ASP B  1  24  ? 13.891  0.081   38.022 1.00 44.30  ? 37  ASP B CA  1 
ATOM   2796 C  C   . ASP B  1  24  ? 14.009  -0.009  39.542 1.00 41.57  ? 37  ASP B C   1 
ATOM   2797 O  O   . ASP B  1  24  ? 13.657  0.945   40.223 1.00 39.63  ? 37  ASP B O   1 
ATOM   2798 C  CB  . ASP B  1  24  ? 12.426  0.154   37.628 1.00 50.37  ? 37  ASP B CB  1 
ATOM   2799 C  CG  . ASP B  1  24  ? 11.789  1.531   37.685 1.00 54.52  ? 37  ASP B CG  1 
ATOM   2800 O  OD1 . ASP B  1  24  ? 12.453  2.503   37.219 1.00 55.53  ? 37  ASP B OD1 1 
ATOM   2801 O  OD2 . ASP B  1  24  ? 10.619  1.594   38.148 1.00 60.40  ? 37  ASP B OD2 1 
ATOM   2802 N  N   . HIS B  1  25  ? 14.480  -1.145  40.075 1.00 40.20  ? 38  HIS B N   1 
ATOM   2803 C  CA  . HIS B  1  25  ? 14.574  -1.340  41.515 1.00 40.84  ? 38  HIS B CA  1 
ATOM   2804 C  C   . HIS B  1  25  ? 15.992  -1.760  41.900 1.00 38.92  ? 38  HIS B C   1 
ATOM   2805 O  O   . HIS B  1  25  ? 16.198  -2.797  42.526 1.00 38.00  ? 38  HIS B O   1 
ATOM   2806 C  CB  . HIS B  1  25  ? 13.497  -2.323  41.984 1.00 42.86  ? 38  HIS B CB  1 
ATOM   2807 C  CG  . HIS B  1  25  ? 12.119  -1.820  41.725 1.00 46.42  ? 38  HIS B CG  1 
ATOM   2808 N  ND1 . HIS B  1  25  ? 11.352  -2.218  40.651 1.00 49.08  ? 38  HIS B ND1 1 
ATOM   2809 C  CD2 . HIS B  1  25  ? 11.391  -0.923  42.392 1.00 44.05  ? 38  HIS B CD2 1 
ATOM   2810 C  CE1 . HIS B  1  25  ? 10.205  -1.567  40.686 1.00 46.96  ? 38  HIS B CE1 1 
ATOM   2811 N  NE2 . HIS B  1  25  ? 10.208  -0.780  41.740 1.00 44.77  ? 38  HIS B NE2 1 
ATOM   2812 N  N   . PRO B  1  26  ? 17.022  -0.955  41.555 1.00 37.64  ? 39  PRO B N   1 
ATOM   2813 C  CA  . PRO B  1  26  ? 18.408  -1.312  41.870 1.00 37.26  ? 39  PRO B CA  1 
ATOM   2814 C  C   . PRO B  1  26  ? 18.700  -1.186  43.365 1.00 35.25  ? 39  PRO B C   1 
ATOM   2815 O  O   . PRO B  1  26  ? 18.174  -0.291  44.026 1.00 33.11  ? 39  PRO B O   1 
ATOM   2816 C  CB  . PRO B  1  26  ? 19.186  -0.273  41.046 1.00 35.09  ? 39  PRO B CB  1 
ATOM   2817 C  CG  . PRO B  1  26  ? 18.294  0.941   41.055 1.00 33.86  ? 39  PRO B CG  1 
ATOM   2818 C  CD  . PRO B  1  26  ? 16.910  0.354   40.892 1.00 34.37  ? 39  PRO B CD  1 
ATOM   2819 N  N   . TRP B  1  27  ? 19.545  -2.078  43.889 1.00 33.10  ? 40  TRP B N   1 
ATOM   2820 C  CA  . TRP B  1  27  ? 20.110  -1.881  45.212 1.00 32.70  ? 40  TRP B CA  1 
ATOM   2821 C  C   . TRP B  1  27  ? 20.965  -0.612  45.219 1.00 33.99  ? 40  TRP B C   1 
ATOM   2822 O  O   . TRP B  1  27  ? 21.695  -0.335  44.270 1.00 38.55  ? 40  TRP B O   1 
ATOM   2823 C  CB  . TRP B  1  27  ? 20.923  -3.107  45.640 1.00 31.08  ? 40  TRP B CB  1 
ATOM   2824 C  CG  . TRP B  1  27  ? 21.484  -3.010  47.034 1.00 30.80  ? 40  TRP B CG  1 
ATOM   2825 C  CD1 . TRP B  1  27  ? 20.923  -3.482  48.182 1.00 32.10  ? 40  TRP B CD1 1 
ATOM   2826 C  CD2 . TRP B  1  27  ? 22.724  -2.387  47.430 1.00 32.57  ? 40  TRP B CD2 1 
ATOM   2827 N  NE1 . TRP B  1  27  ? 21.731  -3.217  49.257 1.00 31.41  ? 40  TRP B NE1 1 
ATOM   2828 C  CE2 . TRP B  1  27  ? 22.838  -2.540  48.829 1.00 29.33  ? 40  TRP B CE2 1 
ATOM   2829 C  CE3 . TRP B  1  27  ? 23.745  -1.715  46.742 1.00 34.43  ? 40  TRP B CE3 1 
ATOM   2830 C  CZ2 . TRP B  1  27  ? 23.919  -2.034  49.541 1.00 28.65  ? 40  TRP B CZ2 1 
ATOM   2831 C  CZ3 . TRP B  1  27  ? 24.806  -1.201  47.458 1.00 33.30  ? 40  TRP B CZ3 1 
ATOM   2832 C  CH2 . TRP B  1  27  ? 24.884  -1.350  48.840 1.00 29.93  ? 40  TRP B CH2 1 
ATOM   2833 N  N   . GLN B  1  28  ? 20.857  0.167   46.298 1.00 34.87  ? 41  GLN B N   1 
ATOM   2834 C  CA  . GLN B  1  28  ? 21.694  1.335   46.502 1.00 34.59  ? 41  GLN B CA  1 
ATOM   2835 C  C   . GLN B  1  28  ? 22.073  1.435   47.971 1.00 33.83  ? 41  GLN B C   1 
ATOM   2836 O  O   . GLN B  1  28  ? 21.331  1.001   48.846 1.00 35.18  ? 41  GLN B O   1 
ATOM   2837 C  CB  . GLN B  1  28  ? 20.973  2.618   46.120 1.00 36.68  ? 41  GLN B CB  1 
ATOM   2838 C  CG  . GLN B  1  28  ? 20.634  2.706   44.640 1.00 39.48  ? 41  GLN B CG  1 
ATOM   2839 C  CD  . GLN B  1  28  ? 19.912  3.987   44.288 1.00 38.96  ? 41  GLN B CD  1 
ATOM   2840 O  OE1 . GLN B  1  28  ? 19.627  4.838   45.148 1.00 39.72  ? 41  GLN B OE1 1 
ATOM   2841 N  NE2 . GLN B  1  28  ? 19.602  4.107   43.006 1.00 37.49  ? 41  GLN B NE2 1 
ATOM   2842 N  N   . PRO B  1  29  ? 23.244  2.018   48.293 1.00 36.59  ? 42  PRO B N   1 
ATOM   2843 C  CA  . PRO B  1  29  ? 23.665  2.143   49.684 1.00 37.41  ? 42  PRO B CA  1 
ATOM   2844 C  C   . PRO B  1  29  ? 22.863  3.206   50.430 1.00 37.72  ? 42  PRO B C   1 
ATOM   2845 O  O   . PRO B  1  29  ? 22.197  4.044   49.834 1.00 37.63  ? 42  PRO B O   1 
ATOM   2846 C  CB  . PRO B  1  29  ? 25.157  2.485   49.586 1.00 36.13  ? 42  PRO B CB  1 
ATOM   2847 C  CG  . PRO B  1  29  ? 25.321  3.123   48.243 1.00 35.98  ? 42  PRO B CG  1 
ATOM   2848 C  CD  . PRO B  1  29  ? 24.219  2.576   47.347 1.00 37.10  ? 42  PRO B CD  1 
ATOM   2849 N  N   . LEU B  1  30  ? 22.947  3.156   51.754 1.00 37.96  ? 43  LEU B N   1 
ATOM   2850 C  CA  . LEU B  1  30  ? 22.281  4.115   52.610 1.00 38.49  ? 43  LEU B CA  1 
ATOM   2851 C  C   . LEU B  1  30  ? 22.907  5.490   52.413 1.00 41.27  ? 43  LEU B C   1 
ATOM   2852 O  O   . LEU B  1  30  ? 24.117  5.613   52.292 1.00 38.05  ? 43  LEU B O   1 
ATOM   2853 C  CB  . LEU B  1  30  ? 22.428  3.645   54.055 1.00 40.15  ? 43  LEU B CB  1 
ATOM   2854 C  CG  . LEU B  1  30  ? 21.748  2.312   54.380 1.00 42.71  ? 43  LEU B CG  1 
ATOM   2855 C  CD1 . LEU B  1  30  ? 21.988  1.959   55.821 1.00 42.42  ? 43  LEU B CD1 1 
ATOM   2856 C  CD2 . LEU B  1  30  ? 20.240  2.300   54.048 1.00 43.27  ? 43  LEU B CD2 1 
ATOM   2857 N  N   . ARG B  1  31  ? 22.058  6.516   52.364 1.00 46.66  ? 44  ARG B N   1 
ATOM   2858 C  CA  . ARG B  1  31  ? 22.489  7.897   52.484 1.00 47.96  ? 44  ARG B CA  1 
ATOM   2859 C  C   . ARG B  1  31  ? 22.270  8.374   53.919 1.00 50.56  ? 44  ARG B C   1 
ATOM   2860 O  O   . ARG B  1  31  ? 21.575  7.733   54.703 1.00 47.72  ? 44  ARG B O   1 
ATOM   2861 C  CB  . ARG B  1  31  ? 21.674  8.817   51.572 1.00 48.84  ? 44  ARG B CB  1 
ATOM   2862 C  CG  . ARG B  1  31  ? 21.679  8.508   50.081 1.00 52.41  ? 44  ARG B CG  1 
ATOM   2863 C  CD  . ARG B  1  31  ? 20.526  9.201   49.359 1.00 60.33  ? 44  ARG B CD  1 
ATOM   2864 N  NE  . ARG B  1  31  ? 19.253  8.894   50.035 1.00 73.74  ? 44  ARG B NE  1 
ATOM   2865 C  CZ  . ARG B  1  31  ? 18.025  8.842   49.528 1.00 76.73  ? 44  ARG B CZ  1 
ATOM   2866 N  NH1 . ARG B  1  31  ? 17.810  9.095   48.246 1.00 81.42  ? 44  ARG B NH1 1 
ATOM   2867 N  NH2 . ARG B  1  31  ? 17.013  8.504   50.309 1.00 72.12  ? 44  ARG B NH2 1 
ATOM   2868 N  N   . GLU B  1  32  ? 22.853  9.533   54.234 1.00 56.37  ? 45  GLU B N   1 
ATOM   2869 C  CA  . GLU B  1  32  ? 22.633  10.196  55.506 1.00 63.43  ? 45  GLU B CA  1 
ATOM   2870 C  C   . GLU B  1  32  ? 21.128  10.345  55.738 1.00 57.75  ? 45  GLU B C   1 
ATOM   2871 O  O   . GLU B  1  32  ? 20.418  10.884  54.893 1.00 49.86  ? 45  GLU B O   1 
ATOM   2872 C  CB  . GLU B  1  32  ? 23.318  11.562  55.465 1.00 77.17  ? 45  GLU B CB  1 
ATOM   2873 C  CG  . GLU B  1  32  ? 23.270  12.311  56.792 1.00 86.89  ? 45  GLU B CG  1 
ATOM   2874 C  CD  . GLU B  1  32  ? 23.891  13.701  56.773 1.00 98.73  ? 45  GLU B CD  1 
ATOM   2875 O  OE1 . GLU B  1  32  ? 24.332  14.193  55.712 1.00 99.39  ? 45  GLU B OE1 1 
ATOM   2876 O  OE2 . GLU B  1  32  ? 23.922  14.309  57.859 1.00 104.95 ? 45  GLU B OE2 1 
ATOM   2877 N  N   . GLY B  1  33  ? 20.653  9.860   56.889 1.00 51.97  ? 46  GLY B N   1 
ATOM   2878 C  CA  . GLY B  1  33  ? 19.271  10.051  57.295 1.00 50.95  ? 46  GLY B CA  1 
ATOM   2879 C  C   . GLY B  1  33  ? 18.388  8.841   56.993 1.00 51.29  ? 46  GLY B C   1 
ATOM   2880 O  O   . GLY B  1  33  ? 17.278  8.755   57.517 1.00 57.10  ? 46  GLY B O   1 
ATOM   2881 N  N   . ASP B  1  34  ? 18.866  7.926   56.139 1.00 52.11  ? 47  ASP B N   1 
ATOM   2882 C  CA  . ASP B  1  34  ? 18.089  6.759   55.745 1.00 48.68  ? 47  ASP B CA  1 
ATOM   2883 C  C   . ASP B  1  34  ? 17.926  5.826   56.939 1.00 41.77  ? 47  ASP B C   1 
ATOM   2884 O  O   . ASP B  1  34  ? 18.855  5.659   57.706 1.00 41.68  ? 47  ASP B O   1 
ATOM   2885 C  CB  . ASP B  1  34  ? 18.719  6.037   54.562 1.00 48.91  ? 47  ASP B CB  1 
ATOM   2886 C  CG  . ASP B  1  34  ? 18.603  6.745   53.212 1.00 55.91  ? 47  ASP B CG  1 
ATOM   2887 O  OD1 . ASP B  1  34  ? 18.011  7.858   53.156 1.00 59.84  ? 47  ASP B OD1 1 
ATOM   2888 O  OD2 . ASP B  1  34  ? 19.099  6.176   52.214 1.00 52.24  ? 47  ASP B OD2 1 
ATOM   2889 N  N   . ILE B  1  35  ? 16.746  5.220   57.081 1.00 38.17  ? 48  ILE B N   1 
ATOM   2890 C  CA  . ILE B  1  35  ? 16.429  4.434   58.253 1.00 37.45  ? 48  ILE B CA  1 
ATOM   2891 C  C   . ILE B  1  35  ? 16.162  2.985   57.863 1.00 33.45  ? 48  ILE B C   1 
ATOM   2892 O  O   . ILE B  1  35  ? 15.528  2.711   56.856 1.00 32.99  ? 48  ILE B O   1 
ATOM   2893 C  CB  . ILE B  1  35  ? 15.263  5.095   59.011 1.00 40.82  ? 48  ILE B CB  1 
ATOM   2894 C  CG1 . ILE B  1  35  ? 15.821  6.228   59.845 1.00 44.73  ? 48  ILE B CG1 1 
ATOM   2895 C  CG2 . ILE B  1  35  ? 14.509  4.098   59.898 1.00 41.36  ? 48  ILE B CG2 1 
ATOM   2896 C  CD1 . ILE B  1  35  ? 14.821  7.293   60.175 1.00 51.40  ? 48  ILE B CD1 1 
ATOM   2897 N  N   . ARG B  1  36  ? 16.669  2.074   58.692 1.00 33.28  ? 49  ARG B N   1 
ATOM   2898 C  CA  . ARG B  1  36  ? 16.492  0.641   58.542 1.00 33.36  ? 49  ARG B CA  1 
ATOM   2899 C  C   . ARG B  1  36  ? 16.287  0.066   59.946 1.00 33.96  ? 49  ARG B C   1 
ATOM   2900 O  O   . ARG B  1  36  ? 16.625  0.729   60.914 1.00 33.46  ? 49  ARG B O   1 
ATOM   2901 C  CB  . ARG B  1  36  ? 17.723  0.057   57.836 1.00 29.52  ? 49  ARG B CB  1 
ATOM   2902 C  CG  . ARG B  1  36  ? 17.973  0.552   56.420 1.00 29.43  ? 49  ARG B CG  1 
ATOM   2903 C  CD  . ARG B  1  36  ? 16.947  0.003   55.437 1.00 31.07  ? 49  ARG B CD  1 
ATOM   2904 N  NE  . ARG B  1  36  ? 17.207  0.410   54.053 1.00 30.62  ? 49  ARG B NE  1 
ATOM   2905 C  CZ  . ARG B  1  36  ? 16.950  1.613   53.540 1.00 33.76  ? 49  ARG B CZ  1 
ATOM   2906 N  NH1 . ARG B  1  36  ? 16.414  2.565   54.288 1.00 32.41  ? 49  ARG B NH1 1 
ATOM   2907 N  NH2 . ARG B  1  36  ? 17.218  1.864   52.262 1.00 35.21  ? 49  ARG B NH2 1 
ATOM   2908 N  N   . GLY B  1  37  ? 15.711  -1.139  60.062 1.00 33.57  ? 50  GLY B N   1 
ATOM   2909 C  CA  . GLY B  1  37  ? 15.323  -1.656  61.365 1.00 32.70  ? 50  GLY B CA  1 
ATOM   2910 C  C   . GLY B  1  37  ? 15.328  -3.182  61.430 1.00 33.44  ? 50  GLY B C   1 
ATOM   2911 O  O   . GLY B  1  37  ? 16.126  -3.850  60.784 1.00 31.42  ? 50  GLY B O   1 
ATOM   2912 N  N   . PRO B  1  38  ? 14.457  -3.792  62.258 1.00 33.50  ? 51  PRO B N   1 
ATOM   2913 C  CA  . PRO B  1  38  ? 14.561  -5.215  62.559 1.00 32.18  ? 51  PRO B CA  1 
ATOM   2914 C  C   . PRO B  1  38  ? 13.999  -6.159  61.508 1.00 34.05  ? 51  PRO B C   1 
ATOM   2915 O  O   . PRO B  1  38  ? 14.161  -7.363  61.671 1.00 36.89  ? 51  PRO B O   1 
ATOM   2916 C  CB  . PRO B  1  38  ? 13.747  -5.298  63.840 1.00 30.03  ? 51  PRO B CB  1 
ATOM   2917 C  CG  . PRO B  1  38  ? 12.654  -4.317  63.634 1.00 29.88  ? 51  PRO B CG  1 
ATOM   2918 C  CD  . PRO B  1  38  ? 13.333  -3.149  62.944 1.00 32.08  ? 51  PRO B CD  1 
ATOM   2919 N  N   . CYS B  1  39  ? 13.313  -5.617  60.480 1.00 32.58  ? 52  CYS B N   1 
ATOM   2920 C  CA  . CYS B  1  39  ? 12.681  -6.428  59.450 1.00 30.03  ? 52  CYS B CA  1 
ATOM   2921 C  C   . CYS B  1  39  ? 13.538  -6.481  58.184 1.00 32.36  ? 52  CYS B C   1 
ATOM   2922 O  O   . CYS B  1  39  ? 13.706  -5.484  57.472 1.00 28.75  ? 52  CYS B O   1 
ATOM   2923 C  CB  . CYS B  1  39  ? 11.295  -5.930  59.064 1.00 32.05  ? 52  CYS B CB  1 
ATOM   2924 S  SG  . CYS B  1  39  ? 10.450  -7.034  57.897 1.00 34.19  ? 52  CYS B SG  1 
ATOM   2925 N  N   . PRO B  1  40  ? 14.070  -7.677  57.840 1.00 30.99  ? 53  PRO B N   1 
ATOM   2926 C  CA  . PRO B  1  40  ? 14.853  -7.852  56.621 1.00 30.65  ? 53  PRO B CA  1 
ATOM   2927 C  C   . PRO B  1  40  ? 14.020  -7.672  55.358 1.00 30.64  ? 53  PRO B C   1 
ATOM   2928 O  O   . PRO B  1  40  ? 14.540  -7.252  54.323 1.00 29.08  ? 53  PRO B O   1 
ATOM   2929 C  CB  . PRO B  1  40  ? 15.420  -9.282  56.748 1.00 30.99  ? 53  PRO B CB  1 
ATOM   2930 C  CG  . PRO B  1  40  ? 14.492  -9.992  57.706 1.00 30.51  ? 53  PRO B CG  1 
ATOM   2931 C  CD  . PRO B  1  40  ? 13.925  -8.925  58.606 1.00 30.24  ? 53  PRO B CD  1 
ATOM   2932 N  N   . GLY B  1  41  ? 12.721  -7.981  55.465 1.00 31.54  ? 54  GLY B N   1 
ATOM   2933 C  CA  . GLY B  1  41  ? 11.802  -7.795  54.357 1.00 32.28  ? 54  GLY B CA  1 
ATOM   2934 C  C   . GLY B  1  41  ? 11.695  -6.322  53.977 1.00 32.14  ? 54  GLY B C   1 
ATOM   2935 O  O   . GLY B  1  41  ? 11.987  -5.940  52.843 1.00 33.97  ? 54  GLY B O   1 
ATOM   2936 N  N   . LEU B  1  42  ? 11.280  -5.507  54.949 1.00 31.76  ? 55  LEU B N   1 
ATOM   2937 C  CA  . LEU B  1  42  ? 11.079  -4.094  54.700 1.00 33.87  ? 55  LEU B CA  1 
ATOM   2938 C  C   . LEU B  1  42  ? 12.418  -3.436  54.371 1.00 35.00  ? 55  LEU B C   1 
ATOM   2939 O  O   . LEU B  1  42  ? 12.470  -2.522  53.551 1.00 34.14  ? 55  LEU B O   1 
ATOM   2940 C  CB  . LEU B  1  42  ? 10.406  -3.448  55.910 1.00 32.88  ? 55  LEU B CB  1 
ATOM   2941 C  CG  . LEU B  1  42  ? 8.986   -3.923  56.224 1.00 35.63  ? 55  LEU B CG  1 
ATOM   2942 C  CD1 . LEU B  1  42  ? 8.456   -3.220  57.452 1.00 38.56  ? 55  LEU B CD1 1 
ATOM   2943 C  CD2 . LEU B  1  42  ? 8.025   -3.681  55.076 1.00 37.67  ? 55  LEU B CD2 1 
ATOM   2944 N  N   . ASN B  1  43  ? 13.496  -3.890  55.022 1.00 33.52  ? 56  ASN B N   1 
ATOM   2945 C  CA  . ASN B  1  43  ? 14.810  -3.319  54.773 1.00 30.95  ? 56  ASN B CA  1 
ATOM   2946 C  C   . ASN B  1  43  ? 15.201  -3.536  53.309 1.00 31.53  ? 56  ASN B C   1 
ATOM   2947 O  O   . ASN B  1  43  ? 15.651  -2.599  52.658 1.00 32.21  ? 56  ASN B O   1 
ATOM   2948 C  CB  . ASN B  1  43  ? 15.852  -3.917  55.704 1.00 31.23  ? 56  ASN B CB  1 
ATOM   2949 C  CG  . ASN B  1  43  ? 15.773  -3.392  57.114 1.00 30.18  ? 56  ASN B CG  1 
ATOM   2950 O  OD1 . ASN B  1  43  ? 15.226  -2.322  57.365 1.00 33.68  ? 56  ASN B OD1 1 
ATOM   2951 N  ND2 . ASN B  1  43  ? 16.347  -4.119  58.049 1.00 29.11  ? 56  ASN B ND2 1 
ATOM   2952 N  N   . THR B  1  44  ? 14.988  -4.750  52.783 1.00 29.04  ? 57  THR B N   1 
ATOM   2953 C  CA  . THR B  1  44  ? 15.347  -5.040  51.406 1.00 29.83  ? 57  THR B CA  1 
ATOM   2954 C  C   . THR B  1  44  ? 14.489  -4.214  50.445 1.00 30.59  ? 57  THR B C   1 
ATOM   2955 O  O   . THR B  1  44  ? 14.990  -3.713  49.441 1.00 29.37  ? 57  THR B O   1 
ATOM   2956 C  CB  . THR B  1  44  ? 15.221  -6.538  51.140 1.00 30.06  ? 57  THR B CB  1 
ATOM   2957 O  OG1 . THR B  1  44  ? 16.152  -7.188  51.998 1.00 31.10  ? 57  THR B OG1 1 
ATOM   2958 C  CG2 . THR B  1  44  ? 15.573  -6.900  49.710 1.00 29.78  ? 57  THR B CG2 1 
ATOM   2959 N  N   . LEU B  1  45  ? 13.198  -4.060  50.751 1.00 30.94  ? 58  LEU B N   1 
ATOM   2960 C  CA  . LEU B  1  45  ? 12.313  -3.301  49.885 1.00 32.00  ? 58  LEU B CA  1 
ATOM   2961 C  C   . LEU B  1  45  ? 12.724  -1.830  49.838 1.00 32.06  ? 58  LEU B C   1 
ATOM   2962 O  O   . LEU B  1  45  ? 12.604  -1.189  48.789 1.00 30.82  ? 58  LEU B O   1 
ATOM   2963 C  CB  . LEU B  1  45  ? 10.867  -3.464  50.343 1.00 32.37  ? 58  LEU B CB  1 
ATOM   2964 C  CG  . LEU B  1  45  ? 10.307  -4.880  50.194 1.00 31.64  ? 58  LEU B CG  1 
ATOM   2965 C  CD1 . LEU B  1  45  ? 9.019   -5.044  50.982 1.00 31.87  ? 58  LEU B CD1 1 
ATOM   2966 C  CD2 . LEU B  1  45  ? 10.091  -5.193  48.737 1.00 30.04  ? 58  LEU B CD2 1 
ATOM   2967 N  N   . ALA B  1  46  ? 13.207  -1.293  50.964 1.00 28.57  ? 59  ALA B N   1 
ATOM   2968 C  CA  . ALA B  1  46  ? 13.642  0.095   50.996 1.00 28.57  ? 59  ALA B CA  1 
ATOM   2969 C  C   . ALA B  1  46  ? 14.928  0.270   50.190 1.00 30.78  ? 59  ALA B C   1 
ATOM   2970 O  O   . ALA B  1  46  ? 15.062  1.224   49.416 1.00 30.54  ? 59  ALA B O   1 
ATOM   2971 C  CB  . ALA B  1  46  ? 13.831  0.561   52.420 1.00 28.06  ? 59  ALA B CB  1 
ATOM   2972 N  N   . SER B  1  47  ? 15.870  -0.667  50.367 1.00 30.85  ? 60  SER B N   1 
ATOM   2973 C  CA  . SER B  1  47  ? 17.176  -0.535  49.745 1.00 31.43  ? 60  SER B CA  1 
ATOM   2974 C  C   . SER B  1  47  ? 17.131  -0.849  48.241 1.00 32.34  ? 60  SER B C   1 
ATOM   2975 O  O   . SER B  1  47  ? 18.111  -0.599  47.546 1.00 31.29  ? 60  SER B O   1 
ATOM   2976 C  CB  . SER B  1  47  ? 18.204  -1.344  50.491 1.00 31.71  ? 60  SER B CB  1 
ATOM   2977 O  OG  . SER B  1  47  ? 18.599  -0.657  51.678 1.00 30.76  ? 60  SER B OG  1 
ATOM   2978 N  N   . HIS B  1  48  ? 15.990  -1.338  47.733 1.00 30.83  ? 61  HIS B N   1 
ATOM   2979 C  CA  . HIS B  1  48  ? 15.783  -1.492  46.304 1.00 31.84  ? 61  HIS B CA  1 
ATOM   2980 C  C   . HIS B  1  48  ? 14.743  -0.518  45.737 1.00 33.12  ? 61  HIS B C   1 
ATOM   2981 O  O   . HIS B  1  48  ? 14.391  -0.613  44.564 1.00 29.52  ? 61  HIS B O   1 
ATOM   2982 C  CB  . HIS B  1  48  ? 15.333  -2.917  45.976 1.00 32.41  ? 61  HIS B CB  1 
ATOM   2983 C  CG  . HIS B  1  48  ? 16.432  -3.917  45.913 1.00 32.15  ? 61  HIS B CG  1 
ATOM   2984 N  ND1 . HIS B  1  48  ? 17.066  -4.242  44.732 1.00 33.91  ? 61  HIS B ND1 1 
ATOM   2985 C  CD2 . HIS B  1  48  ? 16.984  -4.683  46.866 1.00 31.10  ? 61  HIS B CD2 1 
ATOM   2986 C  CE1 . HIS B  1  48  ? 17.970  -5.183  44.981 1.00 36.20  ? 61  HIS B CE1 1 
ATOM   2987 N  NE2 . HIS B  1  48  ? 17.941  -5.463  46.279 1.00 32.06  ? 61  HIS B NE2 1 
ATOM   2988 N  N   . GLY B  1  49  ? 14.228  0.407   46.555 1.00 34.06  ? 62  GLY B N   1 
ATOM   2989 C  CA  . GLY B  1  49  ? 13.297  1.423   46.073 1.00 31.07  ? 62  GLY B CA  1 
ATOM   2990 C  C   . GLY B  1  49  ? 11.847  0.941   45.872 1.00 31.78  ? 62  GLY B C   1 
ATOM   2991 O  O   . GLY B  1  49  ? 11.069  1.654   45.261 1.00 31.87  ? 62  GLY B O   1 
ATOM   2992 N  N   . TYR B  1  50  ? 11.447  -0.234  46.389 1.00 33.80  ? 63  TYR B N   1 
ATOM   2993 C  CA  . TYR B  1  50  ? 10.036  -0.610  46.454 1.00 33.26  ? 63  TYR B CA  1 
ATOM   2994 C  C   . TYR B  1  50  ? 9.296   0.239   47.494 1.00 34.89  ? 63  TYR B C   1 
ATOM   2995 O  O   . TYR B  1  50  ? 8.123   0.555   47.304 1.00 36.53  ? 63  TYR B O   1 
ATOM   2996 C  CB  . TYR B  1  50  ? 9.842   -2.100  46.759 1.00 35.29  ? 63  TYR B CB  1 
ATOM   2997 C  CG  . TYR B  1  50  ? 10.035  -2.971  45.527 1.00 36.14  ? 63  TYR B CG  1 
ATOM   2998 C  CD1 . TYR B  1  50  ? 9.011   -3.129  44.603 1.00 37.88  ? 63  TYR B CD1 1 
ATOM   2999 C  CD2 . TYR B  1  50  ? 11.246  -3.594  45.263 1.00 36.67  ? 63  TYR B CD2 1 
ATOM   3000 C  CE1 . TYR B  1  50  ? 9.173   -3.899  43.463 1.00 38.23  ? 63  TYR B CE1 1 
ATOM   3001 C  CE2 . TYR B  1  50  ? 11.423  -4.362  44.124 1.00 39.84  ? 63  TYR B CE2 1 
ATOM   3002 C  CZ  . TYR B  1  50  ? 10.385  -4.513  43.218 1.00 37.56  ? 63  TYR B CZ  1 
ATOM   3003 O  OH  . TYR B  1  50  ? 10.546  -5.252  42.086 1.00 34.85  ? 63  TYR B OH  1 
ATOM   3004 N  N   . LEU B  1  51  ? 9.968   0.550   48.613 1.00 32.85  ? 64  LEU B N   1 
ATOM   3005 C  CA  . LEU B  1  51  ? 9.554   1.596   49.534 1.00 34.58  ? 64  LEU B CA  1 
ATOM   3006 C  C   . LEU B  1  51  ? 10.424  2.824   49.301 1.00 35.89  ? 64  LEU B C   1 
ATOM   3007 O  O   . LEU B  1  51  ? 11.483  2.718   48.697 1.00 37.81  ? 64  LEU B O   1 
ATOM   3008 C  CB  . LEU B  1  51  ? 9.742   1.146   50.981 1.00 36.49  ? 64  LEU B CB  1 
ATOM   3009 C  CG  . LEU B  1  51  ? 8.840   0.015   51.458 1.00 39.10  ? 64  LEU B CG  1 
ATOM   3010 C  CD1 . LEU B  1  51  ? 9.338   -0.534  52.767 1.00 40.85  ? 64  LEU B CD1 1 
ATOM   3011 C  CD2 . LEU B  1  51  ? 7.424   0.528   51.591 1.00 43.69  ? 64  LEU B CD2 1 
ATOM   3012 N  N   . PRO B  1  52  ? 10.059  4.008   49.844 1.00 35.79  ? 65  PRO B N   1 
ATOM   3013 C  CA  . PRO B  1  52  ? 10.990  5.136   49.903 1.00 35.33  ? 65  PRO B CA  1 
ATOM   3014 C  C   . PRO B  1  52  ? 12.305  4.712   50.542 1.00 34.86  ? 65  PRO B C   1 
ATOM   3015 O  O   . PRO B  1  52  ? 12.297  3.995   51.534 1.00 37.12  ? 65  PRO B O   1 
ATOM   3016 C  CB  . PRO B  1  52  ? 10.250  6.182   50.739 1.00 35.92  ? 65  PRO B CB  1 
ATOM   3017 C  CG  . PRO B  1  52  ? 8.782   5.828   50.574 1.00 35.71  ? 65  PRO B CG  1 
ATOM   3018 C  CD  . PRO B  1  52  ? 8.736   4.323   50.403 1.00 33.98  ? 65  PRO B CD  1 
ATOM   3019 N  N   . ARG B  1  53  ? 13.424  5.193   49.992 1.00 37.17  ? 66  ARG B N   1 
ATOM   3020 C  CA  . ARG B  1  53  ? 14.746  4.696   50.353 1.00 37.19  ? 66  ARG B CA  1 
ATOM   3021 C  C   . ARG B  1  53  ? 15.164  5.186   51.736 1.00 34.76  ? 66  ARG B C   1 
ATOM   3022 O  O   . ARG B  1  53  ? 16.081  4.622   52.322 1.00 36.36  ? 66  ARG B O   1 
ATOM   3023 C  CB  . ARG B  1  53  ? 15.787  5.065   49.291 1.00 37.73  ? 66  ARG B CB  1 
ATOM   3024 C  CG  . ARG B  1  53  ? 15.501  4.376   47.966 1.00 39.81  ? 66  ARG B CG  1 
ATOM   3025 C  CD  . ARG B  1  53  ? 16.610  4.525   46.932 1.00 39.10  ? 66  ARG B CD  1 
ATOM   3026 N  NE  . ARG B  1  53  ? 16.285  3.817   45.688 1.00 36.70  ? 66  ARG B NE  1 
ATOM   3027 C  CZ  . ARG B  1  53  ? 16.730  2.604   45.359 1.00 37.48  ? 66  ARG B CZ  1 
ATOM   3028 N  NH1 . ARG B  1  53  ? 17.398  1.861   46.228 1.00 38.47  ? 66  ARG B NH1 1 
ATOM   3029 N  NH2 . ARG B  1  53  ? 16.472  2.110   44.161 1.00 36.80  ? 66  ARG B NH2 1 
ATOM   3030 N  N   . ASP B  1  54  ? 14.487  6.215   52.251 1.00 38.13  ? 67  ASP B N   1 
ATOM   3031 C  CA  . ASP B  1  54  ? 14.760  6.752   53.576 1.00 39.28  ? 67  ASP B CA  1 
ATOM   3032 C  C   . ASP B  1  54  ? 14.092  5.919   54.665 1.00 35.82  ? 67  ASP B C   1 
ATOM   3033 O  O   . ASP B  1  54  ? 14.367  6.120   55.839 1.00 35.89  ? 67  ASP B O   1 
ATOM   3034 C  CB  . ASP B  1  54  ? 14.387  8.222   53.687 1.00 45.54  ? 67  ASP B CB  1 
ATOM   3035 C  CG  . ASP B  1  54  ? 12.916  8.573   53.539 1.00 48.88  ? 67  ASP B CG  1 
ATOM   3036 O  OD1 . ASP B  1  54  ? 12.094  7.639   53.408 1.00 50.05  ? 67  ASP B OD1 1 
ATOM   3037 O  OD2 . ASP B  1  54  ? 12.612  9.785   53.533 1.00 52.98  ? 67  ASP B OD2 1 
ATOM   3038 N  N   . GLY B  1  55  ? 13.229  4.978   54.280 1.00 37.70  ? 68  GLY B N   1 
ATOM   3039 C  CA  . GLY B  1  55  ? 12.734  3.976   55.211 1.00 39.62  ? 68  GLY B CA  1 
ATOM   3040 C  C   . GLY B  1  55  ? 11.555  4.489   56.033 1.00 38.73  ? 68  GLY B C   1 
ATOM   3041 O  O   . GLY B  1  55  ? 11.261  3.952   57.092 1.00 40.30  ? 68  GLY B O   1 
ATOM   3042 N  N   . VAL B  1  56  ? 10.890  5.528   55.520 1.00 37.42  ? 69  VAL B N   1 
ATOM   3043 C  CA  . VAL B  1  56  ? 9.698   6.094   56.117 1.00 35.90  ? 69  VAL B CA  1 
ATOM   3044 C  C   . VAL B  1  56  ? 8.605   6.057   55.063 1.00 36.09  ? 69  VAL B C   1 
ATOM   3045 O  O   . VAL B  1  56  ? 8.810   6.566   53.967 1.00 35.21  ? 69  VAL B O   1 
ATOM   3046 C  CB  . VAL B  1  56  ? 9.954   7.530   56.597 1.00 37.56  ? 69  VAL B CB  1 
ATOM   3047 C  CG1 . VAL B  1  56  ? 8.678   8.191   57.087 1.00 38.67  ? 69  VAL B CG1 1 
ATOM   3048 C  CG2 . VAL B  1  56  ? 11.017  7.566   57.689 1.00 38.84  ? 69  VAL B CG2 1 
ATOM   3049 N  N   . ALA B  1  57  ? 7.448   5.476   55.410 1.00 37.25  ? 70  ALA B N   1 
ATOM   3050 C  CA  . ALA B  1  57  ? 6.428   5.210   54.411 1.00 38.10  ? 70  ALA B CA  1 
ATOM   3051 C  C   . ALA B  1  57  ? 5.028   5.218   55.021 1.00 37.85  ? 70  ALA B C   1 
ATOM   3052 O  O   . ALA B  1  57  ? 4.883   5.054   56.225 1.00 39.63  ? 70  ALA B O   1 
ATOM   3053 C  CB  . ALA B  1  57  ? 6.733   3.888   53.763 1.00 36.59  ? 70  ALA B CB  1 
ATOM   3054 N  N   . THR B  1  58  ? 4.015   5.361   54.159 1.00 37.49  ? 71  THR B N   1 
ATOM   3055 C  CA  . THR B  1  58  ? 2.618   5.243   54.545 1.00 38.74  ? 71  THR B CA  1 
ATOM   3056 C  C   . THR B  1  58  ? 2.261   3.763   54.635 1.00 40.20  ? 71  THR B C   1 
ATOM   3057 O  O   . THR B  1  58  ? 2.863   2.938   53.955 1.00 38.95  ? 71  THR B O   1 
ATOM   3058 C  CB  . THR B  1  58  ? 1.674   5.921   53.546 1.00 38.64  ? 71  THR B CB  1 
ATOM   3059 O  OG1 . THR B  1  58  ? 1.720   5.144   52.353 1.00 40.17  ? 71  THR B OG1 1 
ATOM   3060 C  CG2 . THR B  1  58  ? 2.033   7.358   53.233 1.00 38.14  ? 71  THR B CG2 1 
ATOM   3061 N  N   . PRO B  1  59  ? 1.243   3.391   55.448 1.00 38.00  ? 72  PRO B N   1 
ATOM   3062 C  CA  . PRO B  1  59  ? 0.716   2.030   55.432 1.00 37.41  ? 72  PRO B CA  1 
ATOM   3063 C  C   . PRO B  1  59  ? 0.441   1.496   54.028 1.00 38.86  ? 72  PRO B C   1 
ATOM   3064 O  O   . PRO B  1  59  ? 0.770   0.353   53.732 1.00 43.38  ? 72  PRO B O   1 
ATOM   3065 C  CB  . PRO B  1  59  ? -0.559  2.168   56.263 1.00 37.53  ? 72  PRO B CB  1 
ATOM   3066 C  CG  . PRO B  1  59  ? -0.228  3.267   57.254 1.00 37.01  ? 72  PRO B CG  1 
ATOM   3067 C  CD  . PRO B  1  59  ? 0.592   4.246   56.456 1.00 37.05  ? 72  PRO B CD  1 
ATOM   3068 N  N   . ALA B  1  60  ? -0.160  2.319   53.165 1.00 37.94  ? 73  ALA B N   1 
ATOM   3069 C  CA  . ALA B  1  60  ? -0.554  1.868   51.834 1.00 38.28  ? 73  ALA B CA  1 
ATOM   3070 C  C   . ALA B  1  60  ? 0.668   1.532   50.983 1.00 36.99  ? 73  ALA B C   1 
ATOM   3071 O  O   . ALA B  1  60  ? 0.640   0.547   50.251 1.00 39.74  ? 73  ALA B O   1 
ATOM   3072 C  CB  . ALA B  1  60  ? -1.423  2.903   51.157 1.00 38.83  ? 73  ALA B CB  1 
ATOM   3073 N  N   . GLN B  1  61  ? 1.736   2.331   51.104 1.00 36.79  ? 74  GLN B N   1 
ATOM   3074 C  CA  . GLN B  1  61  ? 2.975   2.096   50.374 1.00 38.12  ? 74  GLN B CA  1 
ATOM   3075 C  C   . GLN B  1  61  ? 3.612   0.770   50.787 1.00 39.87  ? 74  GLN B C   1 
ATOM   3076 O  O   . GLN B  1  61  ? 4.137   0.044   49.940 1.00 40.15  ? 74  GLN B O   1 
ATOM   3077 C  CB  . GLN B  1  61  ? 3.985   3.216   50.625 1.00 36.67  ? 74  GLN B CB  1 
ATOM   3078 C  CG  . GLN B  1  61  ? 3.597   4.537   49.980 1.00 35.40  ? 74  GLN B CG  1 
ATOM   3079 C  CD  . GLN B  1  61  ? 4.583   5.643   50.272 1.00 36.86  ? 74  GLN B CD  1 
ATOM   3080 O  OE1 . GLN B  1  61  ? 5.023   5.859   51.405 1.00 31.94  ? 74  GLN B OE1 1 
ATOM   3081 N  NE2 . GLN B  1  61  ? 4.958   6.353   49.226 1.00 40.95  ? 74  GLN B NE2 1 
ATOM   3082 N  N   . ILE B  1  62  ? 3.580   0.496   52.100 1.00 36.96  ? 75  ILE B N   1 
ATOM   3083 C  CA  . ILE B  1  62  ? 4.165   -0.702  52.673 1.00 34.91  ? 75  ILE B CA  1 
ATOM   3084 C  C   . ILE B  1  62  ? 3.421   -1.926  52.156 1.00 34.08  ? 75  ILE B C   1 
ATOM   3085 O  O   . ILE B  1  62  ? 4.036   -2.924  51.806 1.00 40.59  ? 75  ILE B O   1 
ATOM   3086 C  CB  . ILE B  1  62  ? 4.176   -0.619  54.212 1.00 33.30  ? 75  ILE B CB  1 
ATOM   3087 C  CG1 . ILE B  1  62  ? 5.127   0.461   54.707 1.00 32.19  ? 75  ILE B CG1 1 
ATOM   3088 C  CG2 . ILE B  1  62  ? 4.514   -1.972  54.843 1.00 35.06  ? 75  ILE B CG2 1 
ATOM   3089 C  CD1 . ILE B  1  62  ? 5.142   0.656   56.213 1.00 33.03  ? 75  ILE B CD1 1 
ATOM   3090 N  N   . ILE B  1  63  ? 2.100   -1.855  52.108 1.00 34.36  ? 76  ILE B N   1 
ATOM   3091 C  CA  . ILE B  1  63  ? 1.314   -2.989  51.659 1.00 36.58  ? 76  ILE B CA  1 
ATOM   3092 C  C   . ILE B  1  63  ? 1.613   -3.240  50.188 1.00 37.26  ? 76  ILE B C   1 
ATOM   3093 O  O   . ILE B  1  63  ? 1.894   -4.382  49.821 1.00 39.58  ? 76  ILE B O   1 
ATOM   3094 C  CB  . ILE B  1  63  ? -0.190  -2.801  51.947 1.00 37.83  ? 76  ILE B CB  1 
ATOM   3095 C  CG1 . ILE B  1  63  ? -0.454  -2.869  53.441 1.00 38.82  ? 76  ILE B CG1 1 
ATOM   3096 C  CG2 . ILE B  1  63  ? -1.043  -3.830  51.207 1.00 37.73  ? 76  ILE B CG2 1 
ATOM   3097 C  CD1 . ILE B  1  63  ? -1.775  -2.261  53.858 1.00 42.79  ? 76  ILE B CD1 1 
ATOM   3098 N  N   . THR B  1  64  ? 1.583   -2.205  49.339 1.00 38.87  ? 77  THR B N   1 
ATOM   3099 C  CA  A THR B  1  64  ? 1.796   -2.440  47.918 0.50 41.04  ? 77  THR B CA  1 
ATOM   3100 C  CA  B THR B  1  64  ? 1.791   -2.455  47.923 0.50 40.05  ? 77  THR B CA  1 
ATOM   3101 C  C   . THR B  1  64  ? 3.223   -2.972  47.721 1.00 39.93  ? 77  THR B C   1 
ATOM   3102 O  O   . THR B  1  64  ? 3.439   -3.868  46.913 1.00 36.36  ? 77  THR B O   1 
ATOM   3103 C  CB  A THR B  1  64  ? 1.502   -1.201  47.065 0.50 42.05  ? 77  THR B CB  1 
ATOM   3104 C  CB  B THR B  1  64  ? 1.401   -1.263  47.040 0.50 40.63  ? 77  THR B CB  1 
ATOM   3105 O  OG1 A THR B  1  64  ? 2.499   -0.248  47.413 0.50 53.39  ? 77  THR B OG1 1 
ATOM   3106 O  OG1 B THR B  1  64  ? 1.933   -1.573  45.756 0.50 36.36  ? 77  THR B OG1 1 
ATOM   3107 C  CG2 A THR B  1  64  ? 0.122   -0.610  47.276 0.50 37.28  ? 77  THR B CG2 1 
ATOM   3108 C  CG2 B THR B  1  64  ? 1.959   0.084   47.456 0.50 44.03  ? 77  THR B CG2 1 
ATOM   3109 N  N   . ALA B  1  65  ? 4.196   -2.468  48.504 1.00 38.97  ? 78  ALA B N   1 
ATOM   3110 C  CA  . ALA B  1  65  ? 5.593   -2.885  48.378 1.00 37.03  ? 78  ALA B CA  1 
ATOM   3111 C  C   . ALA B  1  65  ? 5.824   -4.347  48.757 1.00 35.66  ? 78  ALA B C   1 
ATOM   3112 O  O   . ALA B  1  65  ? 6.589   -5.027  48.085 1.00 35.67  ? 78  ALA B O   1 
ATOM   3113 C  CB  . ALA B  1  65  ? 6.487   -2.008  49.214 1.00 37.70  ? 78  ALA B CB  1 
ATOM   3114 N  N   . THR B  1  66  ? 5.209   -4.829  49.843 1.00 33.52  ? 79  THR B N   1 
ATOM   3115 C  CA  . THR B  1  66  ? 5.380   -6.216  50.244 1.00 32.00  ? 79  THR B CA  1 
ATOM   3116 C  C   . THR B  1  66  ? 4.745   -7.139  49.207 1.00 32.32  ? 79  THR B C   1 
ATOM   3117 O  O   . THR B  1  66  ? 5.188   -8.266  49.027 1.00 32.89  ? 79  THR B O   1 
ATOM   3118 C  CB  . THR B  1  66  ? 4.807   -6.481  51.640 1.00 31.95  ? 79  THR B CB  1 
ATOM   3119 O  OG1 . THR B  1  66  ? 3.408   -6.252  51.590 1.00 30.70  ? 79  THR B OG1 1 
ATOM   3120 C  CG2 . THR B  1  66  ? 5.425   -5.614  52.721 1.00 32.23  ? 79  THR B CG2 1 
ATOM   3121 N  N   . GLN B  1  67  ? 3.691   -6.669  48.535 1.00 36.14  ? 80  GLN B N   1 
ATOM   3122 C  CA  . GLN B  1  67  ? 3.013   -7.465  47.525 1.00 38.56  ? 80  GLN B CA  1 
ATOM   3123 C  C   . GLN B  1  67  ? 3.844   -7.483  46.239 1.00 39.67  ? 80  GLN B C   1 
ATOM   3124 O  O   . GLN B  1  67  ? 4.113   -8.548  45.701 1.00 39.72  ? 80  GLN B O   1 
ATOM   3125 C  CB  . GLN B  1  67  ? 1.584   -6.954  47.334 1.00 40.97  ? 80  GLN B CB  1 
ATOM   3126 C  CG  . GLN B  1  67  ? 0.679   -7.181  48.544 1.00 42.26  ? 80  GLN B CG  1 
ATOM   3127 C  CD  . GLN B  1  67  ? -0.755  -6.690  48.401 1.00 45.46  ? 80  GLN B CD  1 
ATOM   3128 O  OE1 . GLN B  1  67  ? -1.646  -7.125  49.141 1.00 49.08  ? 80  GLN B OE1 1 
ATOM   3129 N  NE2 . GLN B  1  67  ? -1.029  -5.797  47.457 1.00 43.76  ? 80  GLN B NE2 1 
ATOM   3130 N  N   . GLU B  1  68  ? 4.258   -6.314  45.740 1.00 39.33  ? 81  GLU B N   1 
ATOM   3131 C  CA  . GLU B  1  68  ? 5.019   -6.235  44.503 1.00 43.33  ? 81  GLU B CA  1 
ATOM   3132 C  C   . GLU B  1  68  ? 6.358   -6.956  44.630 1.00 43.87  ? 81  GLU B C   1 
ATOM   3133 O  O   . GLU B  1  68  ? 6.768   -7.685  43.730 1.00 46.50  ? 81  GLU B O   1 
ATOM   3134 C  CB  . GLU B  1  68  ? 5.302   -4.782  44.124 1.00 48.70  ? 81  GLU B CB  1 
ATOM   3135 C  CG  . GLU B  1  68  ? 4.063   -4.013  43.671 1.00 57.24  ? 81  GLU B CG  1 
ATOM   3136 C  CD  . GLU B  1  68  ? 3.365   -4.605  42.457 1.00 65.02  ? 81  GLU B CD  1 
ATOM   3137 O  OE1 . GLU B  1  68  ? 2.144   -4.873  42.506 1.00 57.32  ? 81  GLU B OE1 1 
ATOM   3138 O  OE2 . GLU B  1  68  ? 4.084   -4.818  41.460 1.00 75.93  ? 81  GLU B OE2 1 
ATOM   3139 N  N   . GLY B  1  69  ? 7.042   -6.742  45.754 1.00 37.81  ? 82  GLY B N   1 
ATOM   3140 C  CA  . GLY B  1  69  ? 8.399   -7.223  45.917 1.00 34.03  ? 82  GLY B CA  1 
ATOM   3141 C  C   . GLY B  1  69  ? 8.465   -8.705  46.268 1.00 31.84  ? 82  GLY B C   1 
ATOM   3142 O  O   . GLY B  1  69  ? 9.409   -9.378  45.863 1.00 28.64  ? 82  GLY B O   1 
ATOM   3143 N  N   . PHE B  1  70  ? 7.503   -9.205  47.060 1.00 30.51  ? 83  PHE B N   1 
ATOM   3144 C  CA  . PHE B  1  70  ? 7.655   -10.526 47.651 1.00 30.63  ? 83  PHE B CA  1 
ATOM   3145 C  C   . PHE B  1  70  ? 6.425   -11.405 47.466 1.00 30.88  ? 83  PHE B C   1 
ATOM   3146 O  O   . PHE B  1  70  ? 6.481   -12.581 47.798 1.00 33.29  ? 83  PHE B O   1 
ATOM   3147 C  CB  . PHE B  1  70  ? 7.967   -10.427 49.141 1.00 32.03  ? 83  PHE B CB  1 
ATOM   3148 C  CG  . PHE B  1  70  ? 9.415   -10.100 49.467 1.00 33.43  ? 83  PHE B CG  1 
ATOM   3149 C  CD1 . PHE B  1  70  ? 10.419  -11.041 49.270 1.00 35.44  ? 83  PHE B CD1 1 
ATOM   3150 C  CD2 . PHE B  1  70  ? 9.767   -8.870  50.009 1.00 37.10  ? 83  PHE B CD2 1 
ATOM   3151 C  CE1 . PHE B  1  70  ? 11.743  -10.754 49.594 1.00 36.48  ? 83  PHE B CE1 1 
ATOM   3152 C  CE2 . PHE B  1  70  ? 11.092  -8.581  50.331 1.00 38.10  ? 83  PHE B CE2 1 
ATOM   3153 C  CZ  . PHE B  1  70  ? 12.078  -9.521  50.121 1.00 37.23  ? 83  PHE B CZ  1 
ATOM   3154 N  N   . ASN B  1  71  ? 5.336   -10.848 46.929 1.00 33.58  ? 84  ASN B N   1 
ATOM   3155 C  CA  . ASN B  1  71  ? 4.043   -11.520 46.857 1.00 33.19  ? 84  ASN B CA  1 
ATOM   3156 C  C   . ASN B  1  71  ? 3.562   -11.917 48.256 1.00 30.97  ? 84  ASN B C   1 
ATOM   3157 O  O   . ASN B  1  71  ? 2.996   -12.988 48.438 1.00 29.64  ? 84  ASN B O   1 
ATOM   3158 C  CB  . ASN B  1  71  ? 4.104   -12.708 45.903 1.00 35.22  ? 84  ASN B CB  1 
ATOM   3159 C  CG  . ASN B  1  71  ? 2.849   -12.891 45.077 1.00 37.26  ? 84  ASN B CG  1 
ATOM   3160 O  OD1 . ASN B  1  71  ? 1.793   -12.320 45.369 1.00 38.00  ? 84  ASN B OD1 1 
ATOM   3161 N  ND2 . ASN B  1  71  ? 2.946   -13.688 44.027 1.00 41.67  ? 84  ASN B ND2 1 
ATOM   3162 N  N   . PHE B  1  72  ? 3.798   -11.057 49.253 1.00 31.42  ? 85  PHE B N   1 
ATOM   3163 C  CA  . PHE B  1  72  ? 3.199   -11.232 50.565 1.00 33.58  ? 85  PHE B CA  1 
ATOM   3164 C  C   . PHE B  1  72  ? 1.680   -11.178 50.402 1.00 35.13  ? 85  PHE B C   1 
ATOM   3165 O  O   . PHE B  1  72  ? 1.162   -10.304 49.717 1.00 32.41  ? 85  PHE B O   1 
ATOM   3166 C  CB  . PHE B  1  72  ? 3.725   -10.124 51.487 1.00 35.44  ? 85  PHE B CB  1 
ATOM   3167 C  CG  . PHE B  1  72  ? 3.606   -10.361 52.986 1.00 34.23  ? 85  PHE B CG  1 
ATOM   3168 C  CD1 . PHE B  1  72  ? 3.832   -11.607 53.547 1.00 34.20  ? 85  PHE B CD1 1 
ATOM   3169 C  CD2 . PHE B  1  72  ? 3.325   -9.310  53.835 1.00 35.96  ? 85  PHE B CD2 1 
ATOM   3170 C  CE1 . PHE B  1  72  ? 3.744   -11.797 54.915 1.00 37.69  ? 85  PHE B CE1 1 
ATOM   3171 C  CE2 . PHE B  1  72  ? 3.234   -9.508  55.205 1.00 37.78  ? 85  PHE B CE2 1 
ATOM   3172 C  CZ  . PHE B  1  72  ? 3.435   -10.753 55.742 1.00 36.93  ? 85  PHE B CZ  1 
ATOM   3173 N  N   . GLU B  1  73  ? 0.963   -12.117 51.021 1.00 38.90  ? 86  GLU B N   1 
ATOM   3174 C  CA  . GLU B  1  73  ? -0.482  -12.199 50.880 1.00 40.47  ? 86  GLU B CA  1 
ATOM   3175 C  C   . GLU B  1  73  ? -1.140  -10.962 51.495 1.00 38.41  ? 86  GLU B C   1 
ATOM   3176 O  O   . GLU B  1  73  ? -0.697  -10.472 52.529 1.00 39.50  ? 86  GLU B O   1 
ATOM   3177 C  CB  . GLU B  1  73  ? -0.921  -13.525 51.501 1.00 46.68  ? 86  GLU B CB  1 
ATOM   3178 C  CG  . GLU B  1  73  ? -2.379  -13.891 51.236 1.00 51.60  ? 86  GLU B CG  1 
ATOM   3179 C  CD  . GLU B  1  73  ? -3.364  -13.279 52.222 1.00 59.60  ? 86  GLU B CD  1 
ATOM   3180 O  OE1 . GLU B  1  73  ? -4.347  -12.663 51.770 1.00 61.03  ? 86  GLU B OE1 1 
ATOM   3181 O  OE2 . GLU B  1  73  ? -3.136  -13.406 53.444 1.00 70.31  ? 86  GLU B OE2 1 
ATOM   3182 N  N   . ASN B  1  74  ? -2.205  -10.478 50.841 1.00 37.46  ? 87  ASN B N   1 
ATOM   3183 C  CA  . ASN B  1  74  ? -2.831  -9.186  51.108 1.00 38.67  ? 87  ASN B CA  1 
ATOM   3184 C  C   . ASN B  1  74  ? -3.245  -9.040  52.574 1.00 37.40  ? 87  ASN B C   1 
ATOM   3185 O  O   . ASN B  1  74  ? -2.949  -8.031  53.213 1.00 33.95  ? 87  ASN B O   1 
ATOM   3186 C  CB  . ASN B  1  74  ? -4.040  -8.992  50.198 1.00 40.36  ? 87  ASN B CB  1 
ATOM   3187 C  CG  . ASN B  1  74  ? -4.783  -7.688  50.410 1.00 42.74  ? 87  ASN B CG  1 
ATOM   3188 O  OD1 . ASN B  1  74  ? -5.980  -7.704  50.730 1.00 47.54  ? 87  ASN B OD1 1 
ATOM   3189 N  ND2 . ASN B  1  74  ? -4.127  -6.558  50.183 1.00 39.65  ? 87  ASN B ND2 1 
ATOM   3190 N  N   . ASN B  1  75  ? -3.956  -10.032 53.102 1.00 34.90  ? 88  ASN B N   1 
ATOM   3191 C  CA  . ASN B  1  75  ? -4.478  -9.920  54.453 1.00 41.29  ? 88  ASN B CA  1 
ATOM   3192 C  C   . ASN B  1  75  ? -3.347  -9.916  55.474 1.00 43.97  ? 88  ASN B C   1 
ATOM   3193 O  O   . ASN B  1  75  ? -3.422  -9.183  56.461 1.00 38.90  ? 88  ASN B O   1 
ATOM   3194 C  CB  . ASN B  1  75  ? -5.512  -10.995 54.766 1.00 43.38  ? 88  ASN B CB  1 
ATOM   3195 C  CG  . ASN B  1  75  ? -6.850  -10.651 54.162 1.00 44.92  ? 88  ASN B CG  1 
ATOM   3196 O  OD1 . ASN B  1  75  ? -7.466  -11.529 53.556 1.00 47.25  ? 88  ASN B OD1 1 
ATOM   3197 N  ND2 . ASN B  1  75  ? -7.294  -9.404  54.282 1.00 42.99  ? 88  ASN B ND2 1 
ATOM   3198 N  N   . ALA B  1  76  ? -2.319  -10.737 55.213 1.00 43.46  ? 89  ALA B N   1 
ATOM   3199 C  CA  . ALA B  1  76  ? -1.152  -10.830 56.070 1.00 38.10  ? 89  ALA B CA  1 
ATOM   3200 C  C   . ALA B  1  76  ? -0.421  -9.493  56.127 1.00 37.04  ? 89  ALA B C   1 
ATOM   3201 O  O   . ALA B  1  76  ? 0.094   -9.111  57.179 1.00 39.59  ? 89  ALA B O   1 
ATOM   3202 C  CB  . ALA B  1  76  ? -0.248  -11.920 55.571 1.00 36.72  ? 89  ALA B CB  1 
ATOM   3203 N  N   . ALA B  1  77  ? -0.380  -8.806  54.984 1.00 34.36  ? 90  ALA B N   1 
ATOM   3204 C  CA  . ALA B  1  77  ? 0.268   -7.511  54.876 1.00 35.26  ? 90  ALA B CA  1 
ATOM   3205 C  C   . ALA B  1  77  ? -0.502  -6.454  55.666 1.00 35.87  ? 90  ALA B C   1 
ATOM   3206 O  O   . ALA B  1  77  ? 0.101   -5.581  56.295 1.00 36.64  ? 90  ALA B O   1 
ATOM   3207 C  CB  . ALA B  1  77  ? 0.373   -7.146  53.415 1.00 36.03  ? 90  ALA B CB  1 
ATOM   3208 N  N   . ILE B  1  78  ? -1.837  -6.541  55.608 1.00 36.57  ? 91  ILE B N   1 
ATOM   3209 C  CA  . ILE B  1  78  ? -2.705  -5.618  56.317 1.00 37.54  ? 91  ILE B CA  1 
ATOM   3210 C  C   . ILE B  1  78  ? -2.524  -5.807  57.828 1.00 34.36  ? 91  ILE B C   1 
ATOM   3211 O  O   . ILE B  1  78  ? -2.365  -4.838  58.564 1.00 32.01  ? 91  ILE B O   1 
ATOM   3212 C  CB  . ILE B  1  78  ? -4.164  -5.786  55.838 1.00 39.84  ? 91  ILE B CB  1 
ATOM   3213 C  CG1 . ILE B  1  78  ? -4.355  -5.190  54.437 1.00 43.39  ? 91  ILE B CG1 1 
ATOM   3214 C  CG2 . ILE B  1  78  ? -5.162  -5.168  56.814 1.00 37.95  ? 91  ILE B CG2 1 
ATOM   3215 C  CD1 . ILE B  1  78  ? -5.628  -5.634  53.721 1.00 40.97  ? 91  ILE B CD1 1 
ATOM   3216 N  N   . VAL B  1  79  ? -2.500  -7.061  58.280 1.00 32.58  ? 92  VAL B N   1 
ATOM   3217 C  CA  . VAL B  1  79  ? -2.402  -7.364  59.697 1.00 34.56  ? 92  VAL B CA  1 
ATOM   3218 C  C   . VAL B  1  79  ? -1.090  -6.820  60.245 1.00 34.03  ? 92  VAL B C   1 
ATOM   3219 O  O   . VAL B  1  79  ? -1.083  -6.224  61.315 1.00 36.59  ? 92  VAL B O   1 
ATOM   3220 C  CB  . VAL B  1  79  ? -2.539  -8.871  59.995 1.00 37.24  ? 92  VAL B CB  1 
ATOM   3221 C  CG1 . VAL B  1  79  ? -2.090  -9.239  61.409 1.00 38.30  ? 92  VAL B CG1 1 
ATOM   3222 C  CG2 . VAL B  1  79  ? -3.958  -9.350  59.738 1.00 37.17  ? 92  VAL B CG2 1 
ATOM   3223 N  N   . ALA B  1  80  ? 0.014   -7.035  59.521 1.00 34.94  ? 93  ALA B N   1 
ATOM   3224 C  CA  . ALA B  1  80  ? 1.321   -6.619  60.008 1.00 32.71  ? 93  ALA B CA  1 
ATOM   3225 C  C   . ALA B  1  80  ? 1.467   -5.107  59.911 1.00 32.43  ? 93  ALA B C   1 
ATOM   3226 O  O   . ALA B  1  80  ? 2.005   -4.493  60.824 1.00 33.64  ? 93  ALA B O   1 
ATOM   3227 C  CB  . ALA B  1  80  ? 2.433   -7.315  59.260 1.00 32.51  ? 93  ALA B CB  1 
ATOM   3228 N  N   . THR B  1  81  ? 0.998   -4.502  58.820 1.00 31.31  ? 94  THR B N   1 
ATOM   3229 C  CA  . THR B  1  81  ? 1.303   -3.099  58.592 1.00 35.31  ? 94  THR B CA  1 
ATOM   3230 C  C   . THR B  1  81  ? 0.561   -2.209  59.595 1.00 38.90  ? 94  THR B C   1 
ATOM   3231 O  O   . THR B  1  81  ? 1.172   -1.311  60.169 1.00 40.75  ? 94  THR B O   1 
ATOM   3232 C  CB  . THR B  1  81  ? 0.976   -2.716  57.153 1.00 36.26  ? 94  THR B CB  1 
ATOM   3233 O  OG1 . THR B  1  81  ? 1.804   -3.515  56.318 1.00 36.35  ? 94  THR B OG1 1 
ATOM   3234 C  CG2 . THR B  1  81  ? 1.223   -1.244  56.886 1.00 34.87  ? 94  THR B CG2 1 
ATOM   3235 N  N   . TYR B  1  82  ? -0.745  -2.438  59.807 1.00 40.65  ? 95  TYR B N   1 
ATOM   3236 C  CA  . TYR B  1  82  ? -1.532  -1.559  60.671 1.00 39.71  ? 95  TYR B CA  1 
ATOM   3237 C  C   . TYR B  1  82  ? -1.225  -1.863  62.142 1.00 37.35  ? 95  TYR B C   1 
ATOM   3238 O  O   . TYR B  1  82  ? -1.285  -0.974  62.987 1.00 34.27  ? 95  TYR B O   1 
ATOM   3239 C  CB  . TYR B  1  82  ? -3.028  -1.613  60.331 1.00 40.38  ? 95  TYR B CB  1 
ATOM   3240 C  CG  . TYR B  1  82  ? -3.340  -0.964  58.989 1.00 38.60  ? 95  TYR B CG  1 
ATOM   3241 C  CD1 . TYR B  1  82  ? -3.371  0.418   58.850 1.00 36.41  ? 95  TYR B CD1 1 
ATOM   3242 C  CD2 . TYR B  1  82  ? -3.565  -1.728  57.855 1.00 37.37  ? 95  TYR B CD2 1 
ATOM   3243 C  CE1 . TYR B  1  82  ? -3.610  1.018   57.624 1.00 35.93  ? 95  TYR B CE1 1 
ATOM   3244 C  CE2 . TYR B  1  82  ? -3.803  -1.143  56.622 1.00 38.01  ? 95  TYR B CE2 1 
ATOM   3245 C  CZ  . TYR B  1  82  ? -3.819  0.237   56.500 1.00 38.84  ? 95  TYR B CZ  1 
ATOM   3246 O  OH  . TYR B  1  82  ? -4.062  0.819   55.283 1.00 43.17  ? 95  TYR B OH  1 
ATOM   3247 N  N   . LEU B  1  83  ? -0.851  -3.102  62.457 1.00 35.49  ? 96  LEU B N   1 
ATOM   3248 C  CA  . LEU B  1  83  ? -0.303  -3.380  63.773 1.00 36.27  ? 96  LEU B CA  1 
ATOM   3249 C  C   . LEU B  1  83  ? 0.887   -2.456  64.041 1.00 36.47  ? 96  LEU B C   1 
ATOM   3250 O  O   . LEU B  1  83  ? 0.943   -1.758  65.054 1.00 32.95  ? 96  LEU B O   1 
ATOM   3251 C  CB  . LEU B  1  83  ? 0.102   -4.846  63.868 1.00 35.96  ? 96  LEU B CB  1 
ATOM   3252 C  CG  . LEU B  1  83  ? 0.795   -5.243  65.172 1.00 36.92  ? 96  LEU B CG  1 
ATOM   3253 C  CD1 . LEU B  1  83  ? -0.172  -5.074  66.331 1.00 38.23  ? 96  LEU B CD1 1 
ATOM   3254 C  CD2 . LEU B  1  83  ? 1.326   -6.669  65.097 1.00 37.58  ? 96  LEU B CD2 1 
ATOM   3255 N  N   . GLY B  1  84  ? 1.847   -2.458  63.118 1.00 34.78  ? 97  GLY B N   1 
ATOM   3256 C  CA  . GLY B  1  84  ? 3.037   -1.647  63.282 1.00 33.44  ? 97  GLY B CA  1 
ATOM   3257 C  C   . GLY B  1  84  ? 2.710   -0.158  63.337 1.00 34.87  ? 97  GLY B C   1 
ATOM   3258 O  O   . GLY B  1  84  ? 3.309   0.585   64.117 1.00 37.69  ? 97  GLY B O   1 
ATOM   3259 N  N   . HIS B  1  85  ? 1.753   0.267   62.504 1.00 35.70  ? 98  HIS B N   1 
ATOM   3260 C  CA  . HIS B  1  85  ? 1.408   1.676   62.385 1.00 36.54  ? 98  HIS B CA  1 
ATOM   3261 C  C   . HIS B  1  85  ? 0.644   2.164   63.618 1.00 37.60  ? 98  HIS B C   1 
ATOM   3262 O  O   . HIS B  1  85  ? 0.933   3.242   64.124 1.00 40.32  ? 98  HIS B O   1 
ATOM   3263 C  CB  . HIS B  1  85  ? 0.596   1.917   61.115 1.00 34.03  ? 98  HIS B CB  1 
ATOM   3264 C  CG  . HIS B  1  85  ? 0.283   3.342   60.833 1.00 33.73  ? 98  HIS B CG  1 
ATOM   3265 N  ND1 . HIS B  1  85  ? 1.266   4.302   60.788 1.00 36.29  ? 98  HIS B ND1 1 
ATOM   3266 C  CD2 . HIS B  1  85  ? -0.867  3.964   60.510 1.00 36.30  ? 98  HIS B CD2 1 
ATOM   3267 C  CE1 . HIS B  1  85  ? 0.727   5.473   60.469 1.00 38.98  ? 98  HIS B CE1 1 
ATOM   3268 N  NE2 . HIS B  1  85  ? -0.573  5.295   60.309 1.00 40.55  ? 98  HIS B NE2 1 
ATOM   3269 N  N   . LEU B  1  86  ? -0.342  1.395   64.097 1.00 37.91  ? 99  LEU B N   1 
ATOM   3270 C  CA  . LEU B  1  86  ? -1.126  1.799   65.262 1.00 37.99  ? 99  LEU B CA  1 
ATOM   3271 C  C   . LEU B  1  86  ? -0.220  2.020   66.467 1.00 37.61  ? 99  LEU B C   1 
ATOM   3272 O  O   . LEU B  1  86  ? -0.352  3.033   67.148 1.00 36.32  ? 99  LEU B O   1 
ATOM   3273 C  CB  . LEU B  1  86  ? -2.186  0.748   65.574 1.00 38.54  ? 99  LEU B CB  1 
ATOM   3274 C  CG  . LEU B  1  86  ? -3.406  0.750   64.645 1.00 41.11  ? 99  LEU B CG  1 
ATOM   3275 C  CD1 . LEU B  1  86  ? -4.196  -0.539  64.748 1.00 39.31  ? 99  LEU B CD1 1 
ATOM   3276 C  CD2 . LEU B  1  86  ? -4.303  1.941   64.957 1.00 41.32  ? 99  LEU B CD2 1 
ATOM   3277 N  N   . LEU B  1  87  ? 0.708   1.075   66.691 1.00 40.42  ? 100 LEU B N   1 
ATOM   3278 C  CA  . LEU B  1  87  ? 1.578   1.081   67.859 1.00 39.43  ? 100 LEU B CA  1 
ATOM   3279 C  C   . LEU B  1  87  ? 2.763   2.031   67.693 1.00 40.59  ? 100 LEU B C   1 
ATOM   3280 O  O   . LEU B  1  87  ? 3.179   2.622   68.687 1.00 37.46  ? 100 LEU B O   1 
ATOM   3281 C  CB  . LEU B  1  87  ? 2.073   -0.338  68.115 1.00 36.28  ? 100 LEU B CB  1 
ATOM   3282 C  CG  . LEU B  1  87  ? 1.005   -1.357  68.505 1.00 39.08  ? 100 LEU B CG  1 
ATOM   3283 C  CD1 . LEU B  1  87  ? 1.661   -2.706  68.699 1.00 40.97  ? 100 LEU B CD1 1 
ATOM   3284 C  CD2 . LEU B  1  87  ? 0.242   -0.960  69.763 1.00 42.30  ? 100 LEU B CD2 1 
ATOM   3285 N  N   . ASN B  1  88  ? 3.315   2.153   66.472 1.00 39.71  ? 101 ASN B N   1 
ATOM   3286 C  CA  . ASN B  1  88  ? 4.619   2.784   66.312 1.00 40.02  ? 101 ASN B CA  1 
ATOM   3287 C  C   . ASN B  1  88  ? 4.653   3.899   65.270 1.00 40.09  ? 101 ASN B C   1 
ATOM   3288 O  O   . ASN B  1  88  ? 5.709   4.502   65.073 1.00 41.72  ? 101 ASN B O   1 
ATOM   3289 C  CB  . ASN B  1  88  ? 5.684   1.788   65.882 1.00 39.75  ? 101 ASN B CB  1 
ATOM   3290 C  CG  . ASN B  1  88  ? 5.814   0.619   66.825 1.00 40.44  ? 101 ASN B CG  1 
ATOM   3291 O  OD1 . ASN B  1  88  ? 5.924   0.798   68.041 1.00 46.05  ? 101 ASN B OD1 1 
ATOM   3292 N  ND2 . ASN B  1  88  ? 5.828   -0.587  66.287 1.00 39.48  ? 101 ASN B ND2 1 
ATOM   3293 N  N   . GLY B  1  89  ? 3.527   4.167   64.594 1.00 39.86  ? 102 GLY B N   1 
ATOM   3294 C  CA  . GLY B  1  89  ? 3.488   5.148   63.516 1.00 39.38  ? 102 GLY B CA  1 
ATOM   3295 C  C   . GLY B  1  89  ? 2.850   6.462   63.965 1.00 40.26  ? 102 GLY B C   1 
ATOM   3296 O  O   . GLY B  1  89  ? 2.351   6.572   65.080 1.00 40.88  ? 102 GLY B O   1 
ATOM   3297 N  N   . ASN B  1  90  ? 2.874   7.458   63.082 1.00 40.03  ? 103 ASN B N   1 
ATOM   3298 C  CA  . ASN B  1  90  ? 2.236   8.733   63.344 1.00 40.83  ? 103 ASN B CA  1 
ATOM   3299 C  C   . ASN B  1  90  ? 0.910   8.745   62.594 1.00 44.30  ? 103 ASN B C   1 
ATOM   3300 O  O   . ASN B  1  90  ? 0.899   8.795   61.369 1.00 41.69  ? 103 ASN B O   1 
ATOM   3301 C  CB  . ASN B  1  90  ? 3.157   9.875   62.935 1.00 43.56  ? 103 ASN B CB  1 
ATOM   3302 C  CG  . ASN B  1  90  ? 2.574   11.233  63.233 1.00 47.20  ? 103 ASN B CG  1 
ATOM   3303 O  OD1 . ASN B  1  90  ? 1.397   11.493  62.952 1.00 51.19  ? 103 ASN B OD1 1 
ATOM   3304 N  ND2 . ASN B  1  90  ? 3.388   12.111  63.797 1.00 49.16  ? 103 ASN B ND2 1 
ATOM   3305 N  N   . LEU B  1  91  ? -0.205  8.716   63.331 1.00 48.53  ? 104 LEU B N   1 
ATOM   3306 C  CA  . LEU B  1  91  ? -1.505  8.499   62.717 1.00 48.00  ? 104 LEU B CA  1 
ATOM   3307 C  C   . LEU B  1  91  ? -2.013  9.762   62.028 1.00 45.75  ? 104 LEU B C   1 
ATOM   3308 O  O   . LEU B  1  91  ? -2.826  9.678   61.116 1.00 51.72  ? 104 LEU B O   1 
ATOM   3309 C  CB  . LEU B  1  91  ? -2.451  7.993   63.795 1.00 50.69  ? 104 LEU B CB  1 
ATOM   3310 C  CG  . LEU B  1  91  ? -2.019  6.676   64.439 1.00 54.88  ? 104 LEU B CG  1 
ATOM   3311 C  CD1 . LEU B  1  91  ? -2.809  6.382   65.679 1.00 62.34  ? 104 LEU B CD1 1 
ATOM   3312 C  CD2 . LEU B  1  91  ? -2.200  5.571   63.429 1.00 56.75  ? 104 LEU B CD2 1 
ATOM   3313 N  N   . VAL B  1  92  ? -1.481  10.918  62.408 1.00 45.68  ? 105 VAL B N   1 
ATOM   3314 C  CA  . VAL B  1  92  ? -1.920  12.187  61.848 1.00 46.18  ? 105 VAL B CA  1 
ATOM   3315 C  C   . VAL B  1  92  ? -1.289  12.410  60.478 1.00 48.84  ? 105 VAL B C   1 
ATOM   3316 O  O   . VAL B  1  92  ? -1.989  12.840  59.561 1.00 47.40  ? 105 VAL B O   1 
ATOM   3317 C  CB  . VAL B  1  92  ? -1.550  13.327  62.815 1.00 45.66  ? 105 VAL B CB  1 
ATOM   3318 C  CG1 . VAL B  1  92  ? -1.716  14.702  62.186 1.00 41.98  ? 105 VAL B CG1 1 
ATOM   3319 C  CG2 . VAL B  1  92  ? -2.315  13.213  64.126 1.00 47.03  ? 105 VAL B CG2 1 
ATOM   3320 N  N   . THR B  1  93  ? 0.026   12.142  60.357 1.00 50.57  ? 106 THR B N   1 
ATOM   3321 C  CA  . THR B  1  93  ? 0.735   12.307  59.091 1.00 53.35  ? 106 THR B CA  1 
ATOM   3322 C  C   . THR B  1  93  ? 0.666   11.034  58.253 1.00 48.95  ? 106 THR B C   1 
ATOM   3323 O  O   . THR B  1  93  ? 0.975   11.077  57.072 1.00 47.88  ? 106 THR B O   1 
ATOM   3324 C  CB  . THR B  1  93  ? 2.198   12.701  59.291 1.00 55.48  ? 106 THR B CB  1 
ATOM   3325 O  OG1 . THR B  1  93  ? 2.844   11.620  59.960 1.00 59.50  ? 106 THR B OG1 1 
ATOM   3326 C  CG2 . THR B  1  93  ? 2.349   13.992  60.077 1.00 54.08  ? 106 THR B CG2 1 
ATOM   3327 N  N   . ASP B  1  94  ? 0.319   9.904   58.879 1.00 45.53  ? 107 ASP B N   1 
ATOM   3328 C  CA  . ASP B  1  94  ? 0.160   8.639   58.181 1.00 43.91  ? 107 ASP B CA  1 
ATOM   3329 C  C   . ASP B  1  94  ? 1.512   8.096   57.724 1.00 43.14  ? 107 ASP B C   1 
ATOM   3330 O  O   . ASP B  1  94  ? 1.600   7.495   56.666 1.00 45.32  ? 107 ASP B O   1 
ATOM   3331 C  CB  . ASP B  1  94  ? -0.813  8.762   57.021 1.00 45.33  ? 107 ASP B CB  1 
ATOM   3332 C  CG  . ASP B  1  94  ? -1.413  7.450   56.529 1.00 51.25  ? 107 ASP B CG  1 
ATOM   3333 O  OD1 . ASP B  1  94  ? -1.830  6.632   57.388 1.00 47.97  ? 107 ASP B OD1 1 
ATOM   3334 O  OD2 . ASP B  1  94  ? -1.495  7.272   55.286 1.00 56.88  ? 107 ASP B OD2 1 
ATOM   3335 N  N   . LEU B  1  95  ? 2.546   8.267   58.549 1.00 41.22  ? 108 LEU B N   1 
ATOM   3336 C  CA  . LEU B  1  95  ? 3.890   7.819   58.229 1.00 39.18  ? 108 LEU B CA  1 
ATOM   3337 C  C   . LEU B  1  95  ? 4.412   6.913   59.344 1.00 39.42  ? 108 LEU B C   1 
ATOM   3338 O  O   . LEU B  1  95  ? 4.234   7.200   60.522 1.00 40.44  ? 108 LEU B O   1 
ATOM   3339 C  CB  . LEU B  1  95  ? 4.789   9.040   58.045 1.00 38.63  ? 108 LEU B CB  1 
ATOM   3340 C  CG  . LEU B  1  95  ? 4.468   9.956   56.857 1.00 39.92  ? 108 LEU B CG  1 
ATOM   3341 C  CD1 . LEU B  1  95  ? 5.317   11.204  56.952 1.00 41.30  ? 108 LEU B CD1 1 
ATOM   3342 C  CD2 . LEU B  1  95  ? 4.694   9.298   55.511 1.00 39.14  ? 108 LEU B CD2 1 
ATOM   3343 N  N   . LEU B  1  96  ? 5.092   5.831   58.944 1.00 38.13  ? 109 LEU B N   1 
ATOM   3344 C  CA  . LEU B  1  96  ? 5.701   4.879   59.856 1.00 35.42  ? 109 LEU B CA  1 
ATOM   3345 C  C   . LEU B  1  96  ? 7.176   4.713   59.505 1.00 35.20  ? 109 LEU B C   1 
ATOM   3346 O  O   . LEU B  1  96  ? 7.509   4.495   58.350 1.00 38.02  ? 109 LEU B O   1 
ATOM   3347 C  CB  . LEU B  1  96  ? 4.936   3.568   59.699 1.00 34.98  ? 109 LEU B CB  1 
ATOM   3348 C  CG  . LEU B  1  96  ? 5.572   2.333   60.337 1.00 34.91  ? 109 LEU B CG  1 
ATOM   3349 C  CD1 . LEU B  1  96  ? 5.732   2.519   61.820 1.00 35.30  ? 109 LEU B CD1 1 
ATOM   3350 C  CD2 . LEU B  1  96  ? 4.767   1.092   60.021 1.00 34.28  ? 109 LEU B CD2 1 
ATOM   3351 N  N   . SER B  1  97  ? 8.047   4.830   60.512 1.00 36.19  ? 110 SER B N   1 
ATOM   3352 C  CA  . SER B  1  97  ? 9.461   4.520   60.376 1.00 37.12  ? 110 SER B CA  1 
ATOM   3353 C  C   . SER B  1  97  ? 9.659   3.014   60.499 1.00 37.61  ? 110 SER B C   1 
ATOM   3354 O  O   . SER B  1  97  ? 9.181   2.414   61.462 1.00 37.01  ? 110 SER B O   1 
ATOM   3355 C  CB  . SER B  1  97  ? 10.276  5.221   61.432 1.00 38.36  ? 110 SER B CB  1 
ATOM   3356 O  OG  . SER B  1  97  ? 11.591  4.677   61.525 1.00 39.12  ? 110 SER B OG  1 
ATOM   3357 N  N   . ILE B  1  98  ? 10.422  2.416   59.575 1.00 35.64  ? 111 ILE B N   1 
ATOM   3358 C  CA  . ILE B  1  98  ? 10.675  0.986   59.650 1.00 33.75  ? 111 ILE B CA  1 
ATOM   3359 C  C   . ILE B  1  98  ? 11.816  0.705   60.627 1.00 34.72  ? 111 ILE B C   1 
ATOM   3360 O  O   . ILE B  1  98  ? 12.188  -0.451  60.807 1.00 35.62  ? 111 ILE B O   1 
ATOM   3361 C  CB  . ILE B  1  98  ? 10.943  0.376   58.268 1.00 33.40  ? 111 ILE B CB  1 
ATOM   3362 C  CG1 . ILE B  1  98  ? 12.272  0.832   57.668 1.00 31.92  ? 111 ILE B CG1 1 
ATOM   3363 C  CG2 . ILE B  1  98  ? 9.775   0.654   57.330 1.00 35.65  ? 111 ILE B CG2 1 
ATOM   3364 C  CD1 . ILE B  1  98  ? 12.630  0.142   56.365 1.00 31.55  ? 111 ILE B CD1 1 
ATOM   3365 N  N   . GLY B  1  99  ? 12.351  1.756   61.265 1.00 37.49  ? 112 GLY B N   1 
ATOM   3366 C  CA  . GLY B  1  99  ? 13.421  1.605   62.240 1.00 40.96  ? 112 GLY B CA  1 
ATOM   3367 C  C   . GLY B  1  99  ? 13.140  2.408   63.507 1.00 44.22  ? 112 GLY B C   1 
ATOM   3368 O  O   . GLY B  1  99  ? 12.166  2.148   64.202 1.00 47.73  ? 112 GLY B O   1 
ATOM   3369 N  N   . GLY B  1  100 ? 14.008  3.376   63.804 1.00 40.94  ? 113 GLY B N   1 
ATOM   3370 C  CA  . GLY B  1  100 ? 13.902  4.159   65.019 1.00 40.43  ? 113 GLY B CA  1 
ATOM   3371 C  C   . GLY B  1  100 ? 13.252  5.515   64.763 1.00 41.62  ? 113 GLY B C   1 
ATOM   3372 O  O   . GLY B  1  100 ? 12.657  5.744   63.713 1.00 41.86  ? 113 GLY B O   1 
ATOM   3373 N  N   . ALA B  1  101 ? 13.363  6.399   65.762 1.00 47.04  ? 114 ALA B N   1 
ATOM   3374 C  CA  . ALA B  1  101 ? 12.719  7.701   65.731 1.00 50.20  ? 114 ALA B CA  1 
ATOM   3375 C  C   . ALA B  1  101 ? 13.367  8.596   64.678 1.00 50.88  ? 114 ALA B C   1 
ATOM   3376 O  O   . ALA B  1  101 ? 14.561  8.481   64.425 1.00 48.63  ? 114 ALA B O   1 
ATOM   3377 C  CB  . ALA B  1  101 ? 12.794  8.326   67.101 1.00 49.72  ? 114 ALA B CB  1 
ATOM   3378 N  N   . THR B  1  102 ? 12.577  9.497   64.085 1.00 49.30  ? 115 THR B N   1 
ATOM   3379 C  CA  . THR B  1  102 ? 13.088  10.385  63.058 1.00 50.73  ? 115 THR B CA  1 
ATOM   3380 C  C   . THR B  1  102 ? 12.151  11.576  62.894 1.00 49.27  ? 115 THR B C   1 
ATOM   3381 O  O   . THR B  1  102 ? 10.942  11.410  62.948 1.00 47.97  ? 115 THR B O   1 
ATOM   3382 C  CB  . THR B  1  102 ? 13.233  9.620   61.738 1.00 48.71  ? 115 THR B CB  1 
ATOM   3383 O  OG1 . THR B  1  102 ? 13.704  10.504  60.717 1.00 45.75  ? 115 THR B OG1 1 
ATOM   3384 C  CG2 . THR B  1  102 ? 11.920  9.104   61.175 1.00 49.60  ? 115 THR B CG2 1 
ATOM   3385 N  N   . PRO B  1  103 ? 12.673  12.793  62.609 1.00 53.59  ? 116 PRO B N   1 
ATOM   3386 C  CA  . PRO B  1  103 ? 11.828  13.924  62.218 1.00 52.93  ? 116 PRO B CA  1 
ATOM   3387 C  C   . PRO B  1  103 ? 10.986  13.692  60.962 1.00 56.62  ? 116 PRO B C   1 
ATOM   3388 O  O   . PRO B  1  103 ? 10.001  14.390  60.739 1.00 61.24  ? 116 PRO B O   1 
ATOM   3389 C  CB  . PRO B  1  103 ? 12.817  15.095  62.029 1.00 51.52  ? 116 PRO B CB  1 
ATOM   3390 C  CG  . PRO B  1  103 ? 14.179  14.450  61.906 1.00 51.31  ? 116 PRO B CG  1 
ATOM   3391 C  CD  . PRO B  1  103 ? 14.100  13.143  62.665 1.00 52.07  ? 116 PRO B CD  1 
ATOM   3392 N  N   . LYS B  1  104 ? 11.361  12.703  60.149 1.00 56.41  ? 117 LYS B N   1 
ATOM   3393 C  CA  . LYS B  1  104 ? 10.691  12.434  58.885 1.00 53.43  ? 117 LYS B CA  1 
ATOM   3394 C  C   . LYS B  1  104 ? 9.248   11.954  59.060 1.00 53.14  ? 117 LYS B C   1 
ATOM   3395 O  O   . LYS B  1  104 ? 8.491   12.008  58.100 1.00 47.03  ? 117 LYS B O   1 
ATOM   3396 C  CB  . LYS B  1  104 ? 11.488  11.382  58.114 1.00 53.07  ? 117 LYS B CB  1 
ATOM   3397 C  CG  . LYS B  1  104 ? 12.831  11.846  57.591 1.00 56.42  ? 117 LYS B CG  1 
ATOM   3398 C  CD  . LYS B  1  104 ? 13.778  10.707  57.230 1.00 58.18  ? 117 LYS B CD  1 
ATOM   3399 C  CE  . LYS B  1  104 ? 15.035  11.178  56.564 1.00 58.39  ? 117 LYS B CE  1 
ATOM   3400 N  NZ  . LYS B  1  104 ? 14.757  11.780  55.256 1.00 56.36  ? 117 LYS B NZ  1 
ATOM   3401 N  N   . THR B  1  105 ? 8.853   11.468  60.251 1.00 55.31  ? 118 THR B N   1 
ATOM   3402 C  CA  . THR B  1  105 ? 7.466   11.063  60.472 1.00 52.83  ? 118 THR B CA  1 
ATOM   3403 C  C   . THR B  1  105 ? 6.615   12.277  60.839 1.00 57.30  ? 118 THR B C   1 
ATOM   3404 O  O   . THR B  1  105 ? 5.391   12.167  60.911 1.00 54.71  ? 118 THR B O   1 
ATOM   3405 C  CB  . THR B  1  105 ? 7.326   9.971   61.534 1.00 48.40  ? 118 THR B CB  1 
ATOM   3406 O  OG1 . THR B  1  105 ? 8.008   10.354  62.722 1.00 44.53  ? 118 THR B OG1 1 
ATOM   3407 C  CG2 . THR B  1  105 ? 7.877   8.635   61.076 1.00 53.01  ? 118 THR B CG2 1 
ATOM   3408 N  N   . GLY B  1  106 ? 7.277   13.406  61.131 1.00 64.25  ? 119 GLY B N   1 
ATOM   3409 C  CA  . GLY B  1  106 ? 6.605   14.673  61.383 1.00 65.15  ? 119 GLY B CA  1 
ATOM   3410 C  C   . GLY B  1  106 ? 6.493   14.998  62.872 1.00 65.09  ? 119 GLY B C   1 
ATOM   3411 O  O   . GLY B  1  106 ? 7.043   14.284  63.711 1.00 59.94  ? 119 GLY B O   1 
ATOM   3412 N  N   . PRO B  1  107 ? 5.752   16.080  63.223 1.00 71.85  ? 120 PRO B N   1 
ATOM   3413 C  CA  . PRO B  1  107 ? 5.568   16.511  64.616 1.00 67.99  ? 120 PRO B CA  1 
ATOM   3414 C  C   . PRO B  1  107 ? 5.132   15.385  65.547 1.00 62.76  ? 120 PRO B C   1 
ATOM   3415 O  O   . PRO B  1  107 ? 4.115   14.749  65.304 1.00 57.11  ? 120 PRO B O   1 
ATOM   3416 C  CB  . PRO B  1  107 ? 4.482   17.594  64.515 1.00 65.00  ? 120 PRO B CB  1 
ATOM   3417 C  CG  . PRO B  1  107 ? 4.641   18.148  63.121 1.00 68.04  ? 120 PRO B CG  1 
ATOM   3418 C  CD  . PRO B  1  107 ? 5.049   16.956  62.272 1.00 69.64  ? 120 PRO B CD  1 
ATOM   3419 N  N   . PRO B  1  108 ? 5.862   15.111  66.648 1.00 63.55  ? 121 PRO B N   1 
ATOM   3420 C  CA  . PRO B  1  108 ? 5.569   13.926  67.455 1.00 65.90  ? 121 PRO B CA  1 
ATOM   3421 C  C   . PRO B  1  108 ? 4.189   14.034  68.104 1.00 68.09  ? 121 PRO B C   1 
ATOM   3422 O  O   . PRO B  1  108 ? 3.697   15.136  68.332 1.00 70.41  ? 121 PRO B O   1 
ATOM   3423 C  CB  . PRO B  1  108 ? 6.725   13.849  68.471 1.00 68.94  ? 121 PRO B CB  1 
ATOM   3424 C  CG  . PRO B  1  108 ? 7.332   15.246  68.482 1.00 69.81  ? 121 PRO B CG  1 
ATOM   3425 C  CD  . PRO B  1  108 ? 6.975   15.924  67.168 1.00 66.48  ? 121 PRO B CD  1 
ATOM   3426 N  N   . PRO B  1  109 ? 3.492   12.902  68.355 1.00 70.57  ? 122 PRO B N   1 
ATOM   3427 C  CA  . PRO B  1  109 ? 2.164   12.933  68.968 1.00 68.88  ? 122 PRO B CA  1 
ATOM   3428 C  C   . PRO B  1  109 ? 2.232   13.173  70.474 1.00 67.47  ? 122 PRO B C   1 
ATOM   3429 O  O   . PRO B  1  109 ? 3.308   13.107  71.056 1.00 63.53  ? 122 PRO B O   1 
ATOM   3430 C  CB  . PRO B  1  109 ? 1.627   11.527  68.615 1.00 65.14  ? 122 PRO B CB  1 
ATOM   3431 C  CG  . PRO B  1  109 ? 2.849   10.650  68.631 1.00 62.59  ? 122 PRO B CG  1 
ATOM   3432 C  CD  . PRO B  1  109 ? 3.926   11.532  68.030 1.00 68.58  ? 122 PRO B CD  1 
ATOM   3433 N  N   . PRO B  1  110 ? 1.087   13.437  71.147 1.00 71.15  ? 123 PRO B N   1 
ATOM   3434 C  CA  . PRO B  1  110 ? 1.056   13.617  72.601 1.00 67.44  ? 123 PRO B CA  1 
ATOM   3435 C  C   . PRO B  1  110 ? 1.356   12.328  73.363 1.00 61.11  ? 123 PRO B C   1 
ATOM   3436 O  O   . PRO B  1  110 ? 0.809   11.279  73.040 1.00 60.85  ? 123 PRO B O   1 
ATOM   3437 C  CB  . PRO B  1  110 ? -0.374  14.110  72.867 1.00 73.41  ? 123 PRO B CB  1 
ATOM   3438 C  CG  . PRO B  1  110 ? -1.181  13.529  71.731 1.00 76.35  ? 123 PRO B CG  1 
ATOM   3439 C  CD  . PRO B  1  110 ? -0.244  13.589  70.537 1.00 75.76  ? 123 PRO B CD  1 
ATOM   3440 N  N   . PRO B  1  111 ? 2.236   12.369  74.385 1.00 58.55  ? 124 PRO B N   1 
ATOM   3441 C  CA  . PRO B  1  111 ? 2.552   11.183  75.188 1.00 58.52  ? 124 PRO B CA  1 
ATOM   3442 C  C   . PRO B  1  111 ? 1.313   10.568  75.841 1.00 55.12  ? 124 PRO B C   1 
ATOM   3443 O  O   . PRO B  1  111 ? 0.329   11.266  76.056 1.00 52.19  ? 124 PRO B O   1 
ATOM   3444 C  CB  . PRO B  1  111 ? 3.557   11.707  76.250 1.00 57.12  ? 124 PRO B CB  1 
ATOM   3445 C  CG  . PRO B  1  111 ? 4.082   13.012  75.686 1.00 57.25  ? 124 PRO B CG  1 
ATOM   3446 C  CD  . PRO B  1  111 ? 2.992   13.564  74.799 1.00 56.03  ? 124 PRO B CD  1 
ATOM   3447 N  N   . PRO B  1  112 ? 1.311   9.258   76.202 1.00 50.90  ? 125 PRO B N   1 
ATOM   3448 C  CA  . PRO B  1  112 ? 2.481   8.369   76.054 1.00 47.12  ? 125 PRO B CA  1 
ATOM   3449 C  C   . PRO B  1  112 ? 2.778   7.798   74.663 1.00 48.76  ? 125 PRO B C   1 
ATOM   3450 O  O   . PRO B  1  112 ? 3.646   6.940   74.516 1.00 53.18  ? 125 PRO B O   1 
ATOM   3451 C  CB  . PRO B  1  112 ? 2.166   7.231   77.045 1.00 44.92  ? 125 PRO B CB  1 
ATOM   3452 C  CG  . PRO B  1  112 ? 0.658   7.161   77.032 1.00 46.53  ? 125 PRO B CG  1 
ATOM   3453 C  CD  . PRO B  1  112 ? 0.157   8.583   76.824 1.00 45.31  ? 125 PRO B CD  1 
ATOM   3454 N  N   . ALA B  1  113 ? 2.033   8.231   73.645 1.00 49.39  ? 126 ALA B N   1 
ATOM   3455 C  CA  . ALA B  1  113 ? 2.302   7.793   72.285 1.00 52.43  ? 126 ALA B CA  1 
ATOM   3456 C  C   . ALA B  1  113 ? 3.622   8.402   71.823 1.00 53.79  ? 126 ALA B C   1 
ATOM   3457 O  O   . ALA B  1  113 ? 3.986   9.486   72.287 1.00 51.75  ? 126 ALA B O   1 
ATOM   3458 C  CB  . ALA B  1  113 ? 1.156   8.164   71.368 1.00 51.35  ? 126 ALA B CB  1 
ATOM   3459 N  N   . HIS B  1  114 ? 4.295   7.707   70.895 1.00 54.45  ? 127 HIS B N   1 
ATOM   3460 C  CA  . HIS B  1  114 ? 5.678   8.006   70.563 1.00 52.64  ? 127 HIS B CA  1 
ATOM   3461 C  C   . HIS B  1  114 ? 5.898   8.117   69.053 1.00 55.23  ? 127 HIS B C   1 
ATOM   3462 O  O   . HIS B  1  114 ? 6.622   9.004   68.608 1.00 60.39  ? 127 HIS B O   1 
ATOM   3463 C  CB  . HIS B  1  114 ? 6.589   6.972   71.223 1.00 46.09  ? 127 HIS B CB  1 
ATOM   3464 C  CG  . HIS B  1  114 ? 6.113   5.573   71.067 1.00 48.15  ? 127 HIS B CG  1 
ATOM   3465 N  ND1 . HIS B  1  114 ? 6.301   4.873   69.896 1.00 51.54  ? 127 HIS B ND1 1 
ATOM   3466 C  CD2 . HIS B  1  114 ? 5.467   4.750   71.888 1.00 48.25  ? 127 HIS B CD2 1 
ATOM   3467 C  CE1 . HIS B  1  114 ? 5.803   3.650   70.021 1.00 48.63  ? 127 HIS B CE1 1 
ATOM   3468 N  NE2 . HIS B  1  114 ? 5.287   3.550   71.227 1.00 47.24  ? 127 HIS B NE2 1 
ATOM   3469 N  N   . ALA B  1  115 ? 5.306   7.212   68.265 1.00 54.72  ? 128 ALA B N   1 
ATOM   3470 C  CA  . ALA B  1  115 ? 5.590   7.124   66.836 1.00 54.48  ? 128 ALA B CA  1 
ATOM   3471 C  C   . ALA B  1  115 ? 7.087   6.909   66.593 1.00 51.17  ? 128 ALA B C   1 
ATOM   3472 O  O   . ALA B  1  115 ? 7.656   7.501   65.676 1.00 47.39  ? 128 ALA B O   1 
ATOM   3473 C  CB  . ALA B  1  115 ? 5.098   8.362   66.118 1.00 54.48  ? 128 ALA B CB  1 
ATOM   3474 N  N   . GLY B  1  116 ? 7.694   6.020   67.392 1.00 45.07  ? 129 GLY B N   1 
ATOM   3475 C  CA  . GLY B  1  116 ? 9.133   5.839   67.419 1.00 42.35  ? 129 GLY B CA  1 
ATOM   3476 C  C   . GLY B  1  116 ? 9.611   4.695   66.520 1.00 40.93  ? 129 GLY B C   1 
ATOM   3477 O  O   . GLY B  1  116 ? 10.785  4.352   66.557 1.00 40.46  ? 129 GLY B O   1 
ATOM   3478 N  N   . GLY B  1  117 ? 8.703   4.111   65.722 1.00 37.39  ? 130 GLY B N   1 
ATOM   3479 C  CA  . GLY B  1  117 ? 9.058   3.194   64.651 1.00 34.22  ? 130 GLY B CA  1 
ATOM   3480 C  C   . GLY B  1  117 ? 9.117   1.749   65.145 1.00 33.68  ? 130 GLY B C   1 
ATOM   3481 O  O   . GLY B  1  117 ? 8.933   1.501   66.330 1.00 32.28  ? 130 GLY B O   1 
ATOM   3482 N  N   . LEU B  1  118 ? 9.435   0.819   64.228 1.00 34.48  ? 131 LEU B N   1 
ATOM   3483 C  CA  . LEU B  1  118 ? 9.383   -0.616  64.481 1.00 36.46  ? 131 LEU B CA  1 
ATOM   3484 C  C   . LEU B  1  118 ? 10.454  -1.074  65.470 1.00 38.14  ? 131 LEU B C   1 
ATOM   3485 O  O   . LEU B  1  118 ? 10.389  -2.204  65.944 1.00 42.04  ? 131 LEU B O   1 
ATOM   3486 C  CB  . LEU B  1  118 ? 9.514   -1.383  63.165 1.00 36.54  ? 131 LEU B CB  1 
ATOM   3487 C  CG  . LEU B  1  118 ? 8.419   -1.139  62.122 1.00 38.85  ? 131 LEU B CG  1 
ATOM   3488 C  CD1 . LEU B  1  118 ? 8.695   -1.964  60.871 1.00 37.43  ? 131 LEU B CD1 1 
ATOM   3489 C  CD2 . LEU B  1  118 ? 7.030   -1.424  62.667 1.00 39.98  ? 131 LEU B CD2 1 
ATOM   3490 N  N   . ASN B  1  119 ? 11.441  -0.223  65.773 1.00 37.68  ? 132 ASN B N   1 
ATOM   3491 C  CA  . ASN B  1  119 ? 12.460  -0.559  66.752 1.00 39.27  ? 132 ASN B CA  1 
ATOM   3492 C  C   . ASN B  1  119 ? 11.894  -0.661  68.168 1.00 42.12  ? 132 ASN B C   1 
ATOM   3493 O  O   . ASN B  1  119 ? 12.520  -1.296  69.014 1.00 36.95  ? 132 ASN B O   1 
ATOM   3494 C  CB  . ASN B  1  119 ? 13.571  0.476   66.815 1.00 39.73  ? 132 ASN B CB  1 
ATOM   3495 C  CG  . ASN B  1  119 ? 14.542  0.363   65.667 1.00 39.16  ? 132 ASN B CG  1 
ATOM   3496 O  OD1 . ASN B  1  119 ? 14.400  -0.496  64.792 1.00 42.25  ? 132 ASN B OD1 1 
ATOM   3497 N  ND2 . ASN B  1  119 ? 15.534  1.235   65.662 1.00 37.40  ? 132 ASN B ND2 1 
ATOM   3498 N  N   . VAL B  1  120 ? 10.747  -0.021  68.434 1.00 41.97  ? 133 VAL B N   1 
ATOM   3499 C  CA  . VAL B  1  120 ? 10.215  0.051   69.786 1.00 46.06  ? 133 VAL B CA  1 
ATOM   3500 C  C   . VAL B  1  120 ? 9.904   -1.356  70.305 1.00 46.43  ? 133 VAL B C   1 
ATOM   3501 O  O   . VAL B  1  120 ? 9.116   -2.100  69.707 1.00 41.64  ? 133 VAL B O   1 
ATOM   3502 C  CB  . VAL B  1  120 ? 8.975   0.966   69.848 1.00 49.05  ? 133 VAL B CB  1 
ATOM   3503 C  CG1 . VAL B  1  120 ? 8.240   0.861   71.185 1.00 46.33  ? 133 VAL B CG1 1 
ATOM   3504 C  CG2 . VAL B  1  120 ? 9.326   2.421   69.533 1.00 48.90  ? 133 VAL B CG2 1 
ATOM   3505 N  N   . HIS B  1  121 ? 10.519  -1.685  71.454 1.00 41.89  ? 134 HIS B N   1 
ATOM   3506 C  CA  . HIS B  1  121 ? 10.429  -3.010  72.053 1.00 42.20  ? 134 HIS B CA  1 
ATOM   3507 C  C   . HIS B  1  121 ? 9.183   -3.093  72.931 1.00 43.34  ? 134 HIS B C   1 
ATOM   3508 O  O   . HIS B  1  121 ? 8.774   -2.092  73.509 1.00 37.43  ? 134 HIS B O   1 
ATOM   3509 C  CB  . HIS B  1  121 ? 11.658  -3.264  72.930 1.00 40.80  ? 134 HIS B CB  1 
ATOM   3510 C  CG  . HIS B  1  121 ? 11.630  -4.539  73.709 1.00 40.59  ? 134 HIS B CG  1 
ATOM   3511 N  ND1 . HIS B  1  121 ? 11.749  -5.764  73.092 1.00 39.43  ? 134 HIS B ND1 1 
ATOM   3512 C  CD2 . HIS B  1  121 ? 11.476  -4.799  75.023 1.00 40.89  ? 134 HIS B CD2 1 
ATOM   3513 C  CE1 . HIS B  1  121 ? 11.688  -6.730  74.009 1.00 39.98  ? 134 HIS B CE1 1 
ATOM   3514 N  NE2 . HIS B  1  121 ? 11.513  -6.166  75.186 1.00 41.82  ? 134 HIS B NE2 1 
ATOM   3515 N  N   . GLY B  1  122 ? 8.592   -4.288  73.050 1.00 44.42  ? 135 GLY B N   1 
ATOM   3516 C  CA  . GLY B  1  122 ? 7.679   -4.541  74.149 1.00 49.49  ? 135 GLY B CA  1 
ATOM   3517 C  C   . GLY B  1  122 ? 6.289   -5.012  73.725 1.00 52.50  ? 135 GLY B C   1 
ATOM   3518 O  O   . GLY B  1  122 ? 5.730   -5.854  74.417 1.00 54.56  ? 135 GLY B O   1 
ATOM   3519 N  N   . THR B  1  123 ? 5.713   -4.440  72.657 1.00 55.51  ? 136 THR B N   1 
ATOM   3520 C  CA  . THR B  1  123 ? 4.358   -4.786  72.252 1.00 55.53  ? 136 THR B CA  1 
ATOM   3521 C  C   . THR B  1  123 ? 4.359   -5.459  70.875 1.00 56.52  ? 136 THR B C   1 
ATOM   3522 O  O   . THR B  1  123 ? 3.571   -6.382  70.676 1.00 50.25  ? 136 THR B O   1 
ATOM   3523 C  CB  . THR B  1  123 ? 3.463   -3.548  72.270 1.00 60.41  ? 136 THR B CB  1 
ATOM   3524 O  OG1 . THR B  1  123 ? 3.559   -2.940  73.549 1.00 63.01  ? 136 THR B OG1 1 
ATOM   3525 C  CG2 . THR B  1  123 ? 2.012   -3.888  71.962 1.00 63.44  ? 136 THR B CG2 1 
ATOM   3526 N  N   . PHE B  1  124 ? 5.205   -4.987  69.933 1.00 53.30  ? 137 PHE B N   1 
ATOM   3527 C  CA  . PHE B  1  124 ? 5.375   -5.647  68.638 1.00 48.95  ? 137 PHE B CA  1 
ATOM   3528 C  C   . PHE B  1  124 ? 6.729   -6.369  68.593 1.00 46.76  ? 137 PHE B C   1 
ATOM   3529 O  O   . PHE B  1  124 ? 6.760   -7.596  68.725 1.00 47.26  ? 137 PHE B O   1 
ATOM   3530 C  CB  . PHE B  1  124 ? 5.212   -4.689  67.451 1.00 46.44  ? 137 PHE B CB  1 
ATOM   3531 C  CG  . PHE B  1  124 ? 5.068   -5.312  66.065 1.00 43.56  ? 137 PHE B CG  1 
ATOM   3532 C  CD1 . PHE B  1  124 ? 5.253   -6.675  65.836 1.00 44.09  ? 137 PHE B CD1 1 
ATOM   3533 C  CD2 . PHE B  1  124 ? 4.737   -4.523  64.971 1.00 47.71  ? 137 PHE B CD2 1 
ATOM   3534 C  CE1 . PHE B  1  124 ? 5.104   -7.220  64.562 1.00 44.82  ? 137 PHE B CE1 1 
ATOM   3535 C  CE2 . PHE B  1  124 ? 4.578   -5.077  63.703 1.00 43.12  ? 137 PHE B CE2 1 
ATOM   3536 C  CZ  . PHE B  1  124 ? 4.759   -6.421  63.503 1.00 41.05  ? 137 PHE B CZ  1 
ATOM   3537 N  N   . GLU B  1  125 ? 7.837   -5.632  68.383 1.00 42.00  ? 138 GLU B N   1 
ATOM   3538 C  CA  . GLU B  1  125 ? 9.163   -6.235  68.375 1.00 42.20  ? 138 GLU B CA  1 
ATOM   3539 C  C   . GLU B  1  125 ? 9.389   -6.965  69.701 1.00 40.78  ? 138 GLU B C   1 
ATOM   3540 O  O   . GLU B  1  125 ? 8.990   -6.472  70.753 1.00 45.52  ? 138 GLU B O   1 
ATOM   3541 C  CB  . GLU B  1  125 ? 10.266  -5.186  68.183 1.00 43.82  ? 138 GLU B CB  1 
ATOM   3542 C  CG  . GLU B  1  125 ? 11.659  -5.761  67.900 1.00 46.00  ? 138 GLU B CG  1 
ATOM   3543 C  CD  . GLU B  1  125 ? 12.433  -6.471  69.018 1.00 44.19  ? 138 GLU B CD  1 
ATOM   3544 O  OE1 . GLU B  1  125 ? 12.419  -5.916  70.132 1.00 40.47  ? 138 GLU B OE1 1 
ATOM   3545 O  OE2 . GLU B  1  125 ? 13.067  -7.544  68.788 1.00 41.56  ? 138 GLU B OE2 1 
ATOM   3546 N  N   . GLY B  1  126 ? 10.030  -8.140  69.638 1.00 40.69  ? 139 GLY B N   1 
ATOM   3547 C  CA  . GLY B  1  126 ? 10.400  -8.909  70.817 1.00 39.81  ? 139 GLY B CA  1 
ATOM   3548 C  C   . GLY B  1  126 ? 11.565  -9.878  70.571 1.00 37.70  ? 139 GLY B C   1 
ATOM   3549 O  O   . GLY B  1  126 ? 12.332  -9.745  69.610 1.00 40.26  ? 139 GLY B O   1 
ATOM   3550 N  N   . ASP B  1  127 ? 11.612  -10.897 71.432 1.00 36.82  ? 140 ASP B N   1 
ATOM   3551 C  CA  . ASP B  1  127 ? 12.813  -11.636 71.782 1.00 38.31  ? 140 ASP B CA  1 
ATOM   3552 C  C   . ASP B  1  127 ? 12.900  -12.939 70.979 1.00 34.80  ? 140 ASP B C   1 
ATOM   3553 O  O   . ASP B  1  127 ? 11.932  -13.360 70.367 1.00 37.37  ? 140 ASP B O   1 
ATOM   3554 C  CB  . ASP B  1  127 ? 12.826  -11.872 73.292 1.00 39.94  ? 140 ASP B CB  1 
ATOM   3555 C  CG  . ASP B  1  127 ? 12.897  -10.636 74.190 1.00 44.30  ? 140 ASP B CG  1 
ATOM   3556 O  OD1 . ASP B  1  127 ? 13.418  -9.592  73.744 1.00 47.44  ? 140 ASP B OD1 1 
ATOM   3557 O  OD2 . ASP B  1  127 ? 12.401  -10.707 75.335 1.00 48.53  ? 140 ASP B OD2 1 
ATOM   3558 N  N   . ALA B  1  128 ? 14.074  -13.574 70.996 1.00 35.39  ? 141 ALA B N   1 
ATOM   3559 C  CA  . ALA B  1  128 ? 14.310  -14.870 70.370 1.00 37.63  ? 141 ALA B CA  1 
ATOM   3560 C  C   . ALA B  1  128 ? 14.245  -14.782 68.841 1.00 36.74  ? 141 ALA B C   1 
ATOM   3561 O  O   . ALA B  1  128 ? 13.829  -15.720 68.166 1.00 37.38  ? 141 ALA B O   1 
ATOM   3562 C  CB  . ALA B  1  128 ? 13.352  -15.918 70.914 1.00 36.68  ? 141 ALA B CB  1 
ATOM   3563 N  N   . GLY B  1  129 ? 14.714  -13.667 68.287 1.00 38.76  ? 142 GLY B N   1 
ATOM   3564 C  CA  . GLY B  1  129 ? 14.816  -13.520 66.843 1.00 40.48  ? 142 GLY B CA  1 
ATOM   3565 C  C   . GLY B  1  129 ? 15.880  -14.451 66.274 1.00 38.44  ? 142 GLY B C   1 
ATOM   3566 O  O   . GLY B  1  129 ? 16.639  -15.039 67.032 1.00 44.19  ? 142 GLY B O   1 
ATOM   3567 N  N   . MET B  1  130 ? 15.930  -14.554 64.939 1.00 40.95  ? 143 MET B N   1 
ATOM   3568 C  CA  . MET B  1  130 ? 16.872  -15.409 64.224 1.00 38.09  ? 143 MET B CA  1 
ATOM   3569 C  C   . MET B  1  130 ? 18.226  -14.718 64.029 1.00 34.68  ? 143 MET B C   1 
ATOM   3570 O  O   . MET B  1  130 ? 19.264  -15.324 64.313 1.00 38.52  ? 143 MET B O   1 
ATOM   3571 C  CB  . MET B  1  130 ? 16.320  -15.790 62.847 1.00 42.45  ? 143 MET B CB  1 
ATOM   3572 C  CG  . MET B  1  130 ? 15.220  -16.858 62.852 1.00 48.27  ? 143 MET B CG  1 
ATOM   3573 S  SD  . MET B  1  130 ? 14.520  -17.238 61.224 1.00 48.08  ? 143 MET B SD  1 
ATOM   3574 C  CE  . MET B  1  130 ? 13.863  -15.616 60.826 1.00 48.08  ? 143 MET B CE  1 
ATOM   3575 N  N   . THR B  1  131 ? 18.225  -13.471 63.524 1.00 29.53  ? 144 THR B N   1 
ATOM   3576 C  CA  . THR B  1  131 ? 19.461  -12.744 63.256 1.00 28.98  ? 144 THR B CA  1 
ATOM   3577 C  C   . THR B  1  131 ? 19.521  -11.419 64.007 1.00 30.01  ? 144 THR B C   1 
ATOM   3578 O  O   . THR B  1  131 ? 20.423  -10.633 63.734 1.00 29.95  ? 144 THR B O   1 
ATOM   3579 C  CB  . THR B  1  131 ? 19.635  -12.473 61.756 1.00 28.77  ? 144 THR B CB  1 
ATOM   3580 O  OG1 . THR B  1  131 ? 18.750  -11.442 61.349 1.00 31.03  ? 144 THR B OG1 1 
ATOM   3581 C  CG2 . THR B  1  131 ? 19.353  -13.677 60.886 1.00 27.57  ? 144 THR B CG2 1 
ATOM   3582 N  N   . ARG B  1  132 ? 18.583  -11.164 64.933 1.00 35.50  ? 145 ARG B N   1 
ATOM   3583 C  CA  . ARG B  1  132 ? 18.649  -10.007 65.823 1.00 37.44  ? 145 ARG B CA  1 
ATOM   3584 C  C   . ARG B  1  132 ? 18.639  -10.447 67.290 1.00 34.47  ? 145 ARG B C   1 
ATOM   3585 O  O   . ARG B  1  132 ? 17.960  -11.402 67.641 1.00 37.59  ? 145 ARG B O   1 
ATOM   3586 C  CB  . ARG B  1  132 ? 17.512  -9.022  65.548 1.00 39.72  ? 145 ARG B CB  1 
ATOM   3587 C  CG  . ARG B  1  132 ? 17.808  -7.997  64.461 1.00 40.77  ? 145 ARG B CG  1 
ATOM   3588 C  CD  . ARG B  1  132 ? 17.632  -8.535  63.051 1.00 42.53  ? 145 ARG B CD  1 
ATOM   3589 N  NE  . ARG B  1  132 ? 17.923  -7.481  62.079 1.00 45.18  ? 145 ARG B NE  1 
ATOM   3590 C  CZ  . ARG B  1  132 ? 18.482  -7.650  60.883 1.00 45.11  ? 145 ARG B CZ  1 
ATOM   3591 N  NH1 . ARG B  1  132 ? 18.731  -8.857  60.402 1.00 43.80  ? 145 ARG B NH1 1 
ATOM   3592 N  NH2 . ARG B  1  132 ? 18.780  -6.600  60.152 1.00 44.43  ? 145 ARG B NH2 1 
ATOM   3593 N  N   . ALA B  1  133 ? 19.420  -9.742  68.123 1.00 34.28  ? 146 ALA B N   1 
ATOM   3594 C  CA  . ALA B  1  133 ? 19.601  -10.052 69.535 1.00 32.63  ? 146 ALA B CA  1 
ATOM   3595 C  C   . ALA B  1  133 ? 18.453  -9.419  70.315 1.00 33.87  ? 146 ALA B C   1 
ATOM   3596 O  O   . ALA B  1  133 ? 17.863  -8.427  69.883 1.00 31.25  ? 146 ALA B O   1 
ATOM   3597 N  N   . ASP B  1  134 ? 18.130  -10.012 71.470 1.00 36.93  ? 147 ASP B N   1 
ATOM   3598 C  CA  . ASP B  1  134 ? 17.129  -9.455  72.379 1.00 36.31  ? 147 ASP B CA  1 
ATOM   3599 C  C   . ASP B  1  134 ? 17.503  -8.023  72.765 1.00 38.09  ? 147 ASP B C   1 
ATOM   3600 O  O   . ASP B  1  134 ? 18.682  -7.672  72.823 1.00 44.09  ? 147 ASP B O   1 
ATOM   3601 C  CB  . ASP B  1  134 ? 16.941  -10.330 73.608 1.00 37.60  ? 147 ASP B CB  1 
ATOM   3602 C  CG  . ASP B  1  134 ? 16.422  -11.737 73.334 1.00 41.63  ? 147 ASP B CG  1 
ATOM   3603 O  OD1 . ASP B  1  134 ? 16.268  -12.094 72.152 1.00 42.28  ? 147 ASP B OD1 1 
ATOM   3604 O  OD2 . ASP B  1  134 ? 16.155  -12.472 74.299 1.00 46.50  ? 147 ASP B OD2 1 
ATOM   3605 N  N   . GLU B  1  135 ? 16.480  -7.213  73.068 1.00 43.50  ? 148 GLU B N   1 
ATOM   3606 C  CA  . GLU B  1  135 ? 16.654  -5.806  73.399 1.00 49.34  ? 148 GLU B CA  1 
ATOM   3607 C  C   . GLU B  1  135 ? 17.404  -5.635  74.720 1.00 49.99  ? 148 GLU B C   1 
ATOM   3608 O  O   . GLU B  1  135 ? 18.089  -4.630  74.902 1.00 49.54  ? 148 GLU B O   1 
ATOM   3609 C  CB  . GLU B  1  135 ? 15.294  -5.115  73.484 1.00 51.32  ? 148 GLU B CB  1 
ATOM   3610 C  CG  . GLU B  1  135 ? 15.380  -3.596  73.659 1.00 56.55  ? 148 GLU B CG  1 
ATOM   3611 C  CD  . GLU B  1  135 ? 15.314  -3.057  75.085 1.00 62.81  ? 148 GLU B CD  1 
ATOM   3612 O  OE1 . GLU B  1  135 ? 15.055  -3.829  76.041 1.00 60.31  ? 148 GLU B OE1 1 
ATOM   3613 O  OE2 . GLU B  1  135 ? 15.520  -1.830  75.235 1.00 67.87  ? 148 GLU B OE2 1 
ATOM   3614 N  N   . PHE B  1  136 ? 17.267  -6.612  75.628 1.00 47.66  ? 149 PHE B N   1 
ATOM   3615 C  CA  . PHE B  1  136 ? 17.942  -6.568  76.910 1.00 51.43  ? 149 PHE B CA  1 
ATOM   3616 C  C   . PHE B  1  136 ? 19.449  -6.376  76.732 1.00 51.66  ? 149 PHE B C   1 
ATOM   3617 O  O   . PHE B  1  136 ? 20.078  -5.737  77.574 1.00 49.54  ? 149 PHE B O   1 
ATOM   3618 C  CB  . PHE B  1  136 ? 17.678  -7.839  77.717 1.00 56.08  ? 149 PHE B CB  1 
ATOM   3619 C  CG  . PHE B  1  136 ? 18.472  -7.898  79.013 1.00 62.18  ? 149 PHE B CG  1 
ATOM   3620 C  CD1 . PHE B  1  136 ? 18.133  -7.068  80.086 1.00 66.51  ? 149 PHE B CD1 1 
ATOM   3621 C  CD2 . PHE B  1  136 ? 19.550  -8.775  79.152 1.00 59.61  ? 149 PHE B CD2 1 
ATOM   3622 C  CE1 . PHE B  1  136 ? 18.857  -7.122  81.265 1.00 63.38  ? 149 PHE B CE1 1 
ATOM   3623 C  CE2 . PHE B  1  136 ? 20.263  -8.824  80.339 1.00 60.74  ? 149 PHE B CE2 1 
ATOM   3624 C  CZ  . PHE B  1  136 ? 19.919  -7.996  81.387 1.00 62.92  ? 149 PHE B CZ  1 
ATOM   3625 N  N   . PHE B  1  137 ? 20.022  -6.941  75.656 1.00 47.07  ? 150 PHE B N   1 
ATOM   3626 C  CA  . PHE B  1  137 ? 21.460  -6.917  75.452 1.00 41.04  ? 150 PHE B CA  1 
ATOM   3627 C  C   . PHE B  1  137 ? 21.911  -5.631  74.764 1.00 37.90  ? 150 PHE B C   1 
ATOM   3628 O  O   . PHE B  1  137 ? 23.096  -5.461  74.545 1.00 37.52  ? 150 PHE B O   1 
ATOM   3629 C  CB  . PHE B  1  137 ? 21.871  -8.137  74.631 1.00 40.86  ? 150 PHE B CB  1 
ATOM   3630 C  CG  . PHE B  1  137 ? 21.451  -9.474  75.221 1.00 44.87  ? 150 PHE B CG  1 
ATOM   3631 C  CD1 . PHE B  1  137 ? 21.838  -9.840  76.502 1.00 47.84  ? 150 PHE B CD1 1 
ATOM   3632 C  CD2 . PHE B  1  137 ? 20.677  -10.366 74.489 1.00 49.85  ? 150 PHE B CD2 1 
ATOM   3633 C  CE1 . PHE B  1  137 ? 21.471  -11.078 77.028 1.00 53.66  ? 150 PHE B CE1 1 
ATOM   3634 C  CE2 . PHE B  1  137 ? 20.305  -11.595 75.020 1.00 53.77  ? 150 PHE B CE2 1 
ATOM   3635 C  CZ  . PHE B  1  137 ? 20.707  -11.953 76.282 1.00 52.10  ? 150 PHE B CZ  1 
ATOM   3636 N  N   . GLY B  1  138 ? 20.983  -4.747  74.384 1.00 37.91  ? 151 GLY B N   1 
ATOM   3637 C  CA  . GLY B  1  138 ? 21.348  -3.398  73.991 1.00 38.41  ? 151 GLY B CA  1 
ATOM   3638 C  C   . GLY B  1  138 ? 21.065  -3.069  72.524 1.00 45.10  ? 151 GLY B C   1 
ATOM   3639 O  O   . GLY B  1  138 ? 21.201  -1.903  72.148 1.00 46.40  ? 151 GLY B O   1 
ATOM   3640 N  N   . ASP B  1  139 ? 20.676  -4.048  71.687 1.00 46.94  ? 152 ASP B N   1 
ATOM   3641 C  CA  . ASP B  1  139 ? 20.436  -3.728  70.280 1.00 52.20  ? 152 ASP B CA  1 
ATOM   3642 C  C   . ASP B  1  139 ? 19.517  -4.754  69.628 1.00 49.30  ? 152 ASP B C   1 
ATOM   3643 O  O   . ASP B  1  139 ? 19.921  -5.895  69.400 1.00 48.16  ? 152 ASP B O   1 
ATOM   3644 C  CB  . ASP B  1  139 ? 21.733  -3.587  69.491 1.00 55.08  ? 152 ASP B CB  1 
ATOM   3645 C  CG  . ASP B  1  139 ? 21.585  -3.214  68.022 1.00 57.01  ? 152 ASP B CG  1 
ATOM   3646 O  OD1 . ASP B  1  139 ? 20.464  -3.310  67.496 1.00 65.85  ? 152 ASP B OD1 1 
ATOM   3647 O  OD2 . ASP B  1  139 ? 22.588  -2.811  67.421 1.00 59.81  ? 152 ASP B OD2 1 
ATOM   3648 N  N   . ASN B  1  140 ? 18.307  -4.301  69.269 1.00 45.90  ? 153 ASN B N   1 
ATOM   3649 C  CA  . ASN B  1  140 ? 17.260  -5.195  68.799 1.00 41.10  ? 153 ASN B CA  1 
ATOM   3650 C  C   . ASN B  1  140 ? 17.041  -5.084  67.289 1.00 40.14  ? 153 ASN B C   1 
ATOM   3651 O  O   . ASN B  1  140 ? 16.178  -5.789  66.766 1.00 40.28  ? 153 ASN B O   1 
ATOM   3652 C  CB  . ASN B  1  140 ? 15.955  -4.938  69.543 1.00 38.78  ? 153 ASN B CB  1 
ATOM   3653 C  CG  . ASN B  1  140 ? 15.377  -3.572  69.263 1.00 39.58  ? 153 ASN B CG  1 
ATOM   3654 O  OD1 . ASN B  1  140 ? 16.076  -2.672  68.785 1.00 40.64  ? 153 ASN B OD1 1 
ATOM   3655 N  ND2 . ASN B  1  140 ? 14.102  -3.389  69.571 1.00 43.61  ? 153 ASN B ND2 1 
ATOM   3656 N  N   . HIS B  1  141 ? 17.820  -4.236  66.598 1.00 42.10  ? 154 HIS B N   1 
ATOM   3657 C  CA  . HIS B  1  141 ? 17.581  -3.943  65.189 1.00 48.51  ? 154 HIS B CA  1 
ATOM   3658 C  C   . HIS B  1  141 ? 18.727  -4.407  64.273 1.00 44.23  ? 154 HIS B C   1 
ATOM   3659 O  O   . HIS B  1  141 ? 18.472  -4.854  63.159 1.00 49.33  ? 154 HIS B O   1 
ATOM   3660 C  CB  . HIS B  1  141 ? 17.199  -2.468  65.009 1.00 53.13  ? 154 HIS B CB  1 
ATOM   3661 C  CG  . HIS B  1  141 ? 18.213  -1.514  65.529 1.00 58.95  ? 154 HIS B CG  1 
ATOM   3662 N  ND1 . HIS B  1  141 ? 18.212  -1.080  66.837 1.00 54.33  ? 154 HIS B ND1 1 
ATOM   3663 C  CD2 . HIS B  1  141 ? 19.270  -0.928  64.935 1.00 62.61  ? 154 HIS B CD2 1 
ATOM   3664 C  CE1 . HIS B  1  141 ? 19.234  -0.258  67.019 1.00 54.51  ? 154 HIS B CE1 1 
ATOM   3665 N  NE2 . HIS B  1  141 ? 19.891  -0.158  65.882 1.00 57.16  ? 154 HIS B NE2 1 
ATOM   3666 N  N   . SER B  1  142 ? 19.976  -4.310  64.725 1.00 42.47  ? 155 SER B N   1 
ATOM   3667 C  CA  . SER B  1  142 ? 21.137  -4.652  63.912 1.00 40.66  ? 155 SER B CA  1 
ATOM   3668 C  C   . SER B  1  142 ? 21.232  -6.148  63.631 1.00 38.32  ? 155 SER B C   1 
ATOM   3669 O  O   . SER B  1  142 ? 20.934  -6.973  64.486 1.00 36.93  ? 155 SER B O   1 
ATOM   3670 C  CB  . SER B  1  142 ? 22.415  -4.205  64.574 1.00 42.31  ? 155 SER B CB  1 
ATOM   3671 O  OG  . SER B  1  142 ? 22.522  -2.791  64.525 1.00 48.21  ? 155 SER B OG  1 
ATOM   3672 N  N   . PHE B  1  143 ? 21.723  -6.471  62.429 1.00 38.95  ? 156 PHE B N   1 
ATOM   3673 C  CA  . PHE B  1  143 ? 22.178  -7.814  62.102 1.00 34.68  ? 156 PHE B CA  1 
ATOM   3674 C  C   . PHE B  1  143 ? 23.275  -8.243  63.069 1.00 32.05  ? 156 PHE B C   1 
ATOM   3675 O  O   . PHE B  1  143 ? 24.168  -7.458  63.346 1.00 31.11  ? 156 PHE B O   1 
ATOM   3676 C  CB  . PHE B  1  143 ? 22.721  -7.839  60.671 1.00 33.93  ? 156 PHE B CB  1 
ATOM   3677 C  CG  . PHE B  1  143 ? 23.282  -9.195  60.267 1.00 34.95  ? 156 PHE B CG  1 
ATOM   3678 C  CD1 . PHE B  1  143 ? 22.443  -10.213 59.825 1.00 34.66  ? 156 PHE B CD1 1 
ATOM   3679 C  CD2 . PHE B  1  143 ? 24.638  -9.455  60.338 1.00 34.55  ? 156 PHE B CD2 1 
ATOM   3680 C  CE1 . PHE B  1  143 ? 22.940  -11.458 59.458 1.00 34.87  ? 156 PHE B CE1 1 
ATOM   3681 C  CE2 . PHE B  1  143 ? 25.129  -10.700 59.972 1.00 38.24  ? 156 PHE B CE2 1 
ATOM   3682 C  CZ  . PHE B  1  143 ? 24.279  -11.700 59.532 1.00 39.26  ? 156 PHE B CZ  1 
ATOM   3683 N  N   . ASN B  1  144 ? 23.204  -9.491  63.543 1.00 32.38  ? 157 ASN B N   1 
ATOM   3684 C  CA  . ASN B  1  144 ? 24.143  -10.045 64.507 1.00 32.65  ? 157 ASN B CA  1 
ATOM   3685 C  C   . ASN B  1  144 ? 24.781  -11.306 63.925 1.00 32.40  ? 157 ASN B C   1 
ATOM   3686 O  O   . ASN B  1  144 ? 24.113  -12.311 63.711 1.00 29.14  ? 157 ASN B O   1 
ATOM   3687 C  CB  . ASN B  1  144 ? 23.425  -10.310 65.821 1.00 36.72  ? 157 ASN B CB  1 
ATOM   3688 C  CG  . ASN B  1  144 ? 24.255  -10.992 66.891 1.00 37.56  ? 157 ASN B CG  1 
ATOM   3689 O  OD1 . ASN B  1  144 ? 24.840  -12.045 66.623 1.00 31.45  ? 157 ASN B OD1 1 
ATOM   3690 N  ND2 . ASN B  1  144 ? 24.308  -10.450 68.110 1.00 44.71  ? 157 ASN B ND2 1 
ATOM   3691 N  N   . GLN B  1  145 ? 26.099  -11.247 63.685 1.00 35.74  ? 158 GLN B N   1 
ATOM   3692 C  CA  . GLN B  1  145 ? 26.826  -12.299 62.983 1.00 34.93  ? 158 GLN B CA  1 
ATOM   3693 C  C   . GLN B  1  145 ? 26.887  -13.583 63.810 1.00 32.26  ? 158 GLN B C   1 
ATOM   3694 O  O   . GLN B  1  145 ? 26.853  -14.673 63.254 1.00 31.54  ? 158 GLN B O   1 
ATOM   3695 C  CB  . GLN B  1  145 ? 28.216  -11.781 62.603 1.00 35.01  ? 158 GLN B CB  1 
ATOM   3696 C  CG  . GLN B  1  145 ? 29.047  -12.744 61.768 1.00 34.80  ? 158 GLN B CG  1 
ATOM   3697 C  CD  . GLN B  1  145 ? 28.431  -13.053 60.419 1.00 36.27  ? 158 GLN B CD  1 
ATOM   3698 O  OE1 . GLN B  1  145 ? 28.110  -12.166 59.621 1.00 32.33  ? 158 GLN B OE1 1 
ATOM   3699 N  NE2 . GLN B  1  145 ? 28.265  -14.337 60.149 1.00 37.41  ? 158 GLN B NE2 1 
ATOM   3700 N  N   . THR B  1  146 ? 26.978  -13.465 65.137 1.00 32.93  ? 159 THR B N   1 
ATOM   3701 C  CA  . THR B  1  146 ? 27.006  -14.638 66.003 1.00 35.78  ? 159 THR B CA  1 
ATOM   3702 C  C   . THR B  1  146 ? 25.712  -15.432 65.867 1.00 35.41  ? 159 THR B C   1 
ATOM   3703 O  O   . THR B  1  146 ? 25.731  -16.660 65.885 1.00 38.48  ? 159 THR B O   1 
ATOM   3704 C  CB  . THR B  1  146 ? 27.199  -14.260 67.471 1.00 37.95  ? 159 THR B CB  1 
ATOM   3705 O  OG1 . THR B  1  146 ? 28.370  -13.457 67.567 1.00 39.99  ? 159 THR B OG1 1 
ATOM   3706 C  CG2 . THR B  1  146 ? 27.352  -15.493 68.340 1.00 37.16  ? 159 THR B CG2 1 
ATOM   3707 N  N   . LEU B  1  147 ? 24.584  -14.726 65.783 1.00 33.69  ? 160 LEU B N   1 
ATOM   3708 C  CA  . LEU B  1  147 ? 23.298  -15.385 65.639 1.00 33.30  ? 160 LEU B CA  1 
ATOM   3709 C  C   . LEU B  1  147 ? 23.138  -15.988 64.244 1.00 32.14  ? 160 LEU B C   1 
ATOM   3710 O  O   . LEU B  1  147 ? 22.550  -17.058 64.089 1.00 33.16  ? 160 LEU B O   1 
ATOM   3711 C  CB  . LEU B  1  147 ? 22.194  -14.394 65.980 1.00 38.01  ? 160 LEU B CB  1 
ATOM   3712 C  CG  . LEU B  1  147 ? 21.949  -14.138 67.475 1.00 38.53  ? 160 LEU B CG  1 
ATOM   3713 C  CD1 . LEU B  1  147 ? 20.792  -13.144 67.646 1.00 39.42  ? 160 LEU B CD1 1 
ATOM   3714 C  CD2 . LEU B  1  147 ? 21.648  -15.438 68.218 1.00 36.64  ? 160 LEU B CD2 1 
ATOM   3715 N  N   . PHE B  1  148 ? 23.677  -15.313 63.226 1.00 31.99  ? 161 PHE B N   1 
ATOM   3716 C  CA  . PHE B  1  148 ? 23.658  -15.845 61.872 1.00 31.86  ? 161 PHE B CA  1 
ATOM   3717 C  C   . PHE B  1  148 ? 24.526  -17.100 61.767 1.00 33.37  ? 161 PHE B C   1 
ATOM   3718 O  O   . PHE B  1  148 ? 24.235  -17.983 60.957 1.00 32.29  ? 161 PHE B O   1 
ATOM   3719 C  CB  . PHE B  1  148 ? 24.131  -14.814 60.842 1.00 33.78  ? 161 PHE B CB  1 
ATOM   3720 C  CG  . PHE B  1  148 ? 23.958  -15.294 59.411 1.00 33.33  ? 161 PHE B CG  1 
ATOM   3721 C  CD1 . PHE B  1  148 ? 22.688  -15.423 58.856 1.00 34.78  ? 161 PHE B CD1 1 
ATOM   3722 C  CD2 . PHE B  1  148 ? 25.054  -15.659 58.643 1.00 32.59  ? 161 PHE B CD2 1 
ATOM   3723 C  CE1 . PHE B  1  148 ? 22.533  -15.883 57.559 1.00 34.76  ? 161 PHE B CE1 1 
ATOM   3724 C  CE2 . PHE B  1  148 ? 24.889  -16.123 57.349 1.00 35.73  ? 161 PHE B CE2 1 
ATOM   3725 C  CZ  . PHE B  1  148 ? 23.633  -16.224 56.808 1.00 35.37  ? 161 PHE B CZ  1 
ATOM   3726 N  N   . ASP B  1  149 ? 25.602  -17.164 62.571 1.00 31.43  ? 162 ASP B N   1 
ATOM   3727 C  CA  . ASP B  1  149 ? 26.467  -18.332 62.602 1.00 34.56  ? 162 ASP B CA  1 
ATOM   3728 C  C   . ASP B  1  149 ? 25.672  -19.546 63.095 1.00 34.89  ? 162 ASP B C   1 
ATOM   3729 O  O   . ASP B  1  149 ? 25.847  -20.655 62.593 1.00 33.52  ? 162 ASP B O   1 
ATOM   3730 C  CB  . ASP B  1  149 ? 27.731  -18.031 63.393 1.00 39.41  ? 162 ASP B CB  1 
ATOM   3731 C  CG  . ASP B  1  149 ? 28.736  -17.094 62.719 1.00 44.43  ? 162 ASP B CG  1 
ATOM   3732 O  OD1 . ASP B  1  149 ? 28.769  -17.051 61.472 1.00 41.14  ? 162 ASP B OD1 1 
ATOM   3733 O  OD2 . ASP B  1  149 ? 29.474  -16.373 63.435 1.00 49.35  ? 162 ASP B OD2 1 
ATOM   3734 N  N   . LYS B  1  150 ? 24.778  -19.320 64.069 1.00 36.23  ? 163 LYS B N   1 
ATOM   3735 C  CA  . LYS B  1  150 ? 23.916  -20.369 64.596 1.00 34.29  ? 163 LYS B CA  1 
ATOM   3736 C  C   . LYS B  1  150 ? 22.883  -20.810 63.558 1.00 32.69  ? 163 LYS B C   1 
ATOM   3737 O  O   . LYS B  1  150 ? 22.566  -21.992 63.466 1.00 31.78  ? 163 LYS B O   1 
ATOM   3738 C  CB  . LYS B  1  150 ? 23.264  -19.885 65.893 1.00 34.47  ? 163 LYS B CB  1 
ATOM   3739 C  CG  . LYS B  1  150 ? 22.411  -20.921 66.592 1.00 37.47  ? 163 LYS B CG  1 
ATOM   3740 C  CD  . LYS B  1  150 ? 21.774  -20.344 67.845 1.00 42.75  ? 163 LYS B CD  1 
ATOM   3741 C  CE  . LYS B  1  150 ? 20.738  -21.235 68.470 1.00 47.76  ? 163 LYS B CE  1 
ATOM   3742 N  NZ  . LYS B  1  150 ? 21.177  -21.787 69.749 1.00 49.16  ? 163 LYS B NZ  1 
ATOM   3743 N  N   . PHE B  1  151 ? 22.366  -19.860 62.771 1.00 31.88  ? 164 PHE B N   1 
ATOM   3744 C  CA  . PHE B  1  151 ? 21.490  -20.176 61.650 1.00 32.70  ? 164 PHE B CA  1 
ATOM   3745 C  C   . PHE B  1  151 ? 22.198  -21.120 60.674 1.00 32.08  ? 164 PHE B C   1 
ATOM   3746 O  O   . PHE B  1  151 ? 21.612  -22.102 60.219 1.00 31.78  ? 164 PHE B O   1 
ATOM   3747 C  CB  . PHE B  1  151 ? 21.071  -18.847 61.017 1.00 35.52  ? 164 PHE B CB  1 
ATOM   3748 C  CG  . PHE B  1  151 ? 20.105  -18.927 59.842 1.00 37.27  ? 164 PHE B CG  1 
ATOM   3749 C  CD1 . PHE B  1  151 ? 18.727  -18.948 60.059 1.00 39.49  ? 164 PHE B CD1 1 
ATOM   3750 C  CD2 . PHE B  1  151 ? 20.574  -18.929 58.529 1.00 33.99  ? 164 PHE B CD2 1 
ATOM   3751 C  CE1 . PHE B  1  151 ? 17.839  -18.990 58.990 1.00 38.00  ? 164 PHE B CE1 1 
ATOM   3752 C  CE2 . PHE B  1  151 ? 19.683  -18.981 57.467 1.00 34.47  ? 164 PHE B CE2 1 
ATOM   3753 C  CZ  . PHE B  1  151 ? 18.321  -19.014 57.696 1.00 37.21  ? 164 PHE B CZ  1 
ATOM   3754 N  N   . VAL B  1  152 ? 23.473  -20.832 60.381 1.00 31.40  ? 165 VAL B N   1 
ATOM   3755 C  CA  . VAL B  1  152 ? 24.247  -21.646 59.456 1.00 31.98  ? 165 VAL B CA  1 
ATOM   3756 C  C   . VAL B  1  152 ? 24.480  -23.027 60.073 1.00 33.16  ? 165 VAL B C   1 
ATOM   3757 O  O   . VAL B  1  152 ? 24.331  -24.050 59.403 1.00 31.05  ? 165 VAL B O   1 
ATOM   3758 C  CB  . VAL B  1  152 ? 25.576  -20.967 59.068 1.00 29.54  ? 165 VAL B CB  1 
ATOM   3759 C  CG1 . VAL B  1  152 ? 26.458  -21.870 58.212 1.00 28.41  ? 165 VAL B CG1 1 
ATOM   3760 C  CG2 . VAL B  1  152 ? 25.341  -19.621 58.378 1.00 30.40  ? 165 VAL B CG2 1 
ATOM   3761 N  N   . ASP B  1  153 ? 24.827  -23.048 61.365 1.00 35.41  ? 166 ASP B N   1 
ATOM   3762 C  CA  . ASP B  1  153 ? 25.106  -24.296 62.065 1.00 38.63  ? 166 ASP B CA  1 
ATOM   3763 C  C   . ASP B  1  153 ? 23.889  -25.229 61.992 1.00 37.67  ? 166 ASP B C   1 
ATOM   3764 O  O   . ASP B  1  153 ? 24.017  -26.394 61.609 1.00 32.84  ? 166 ASP B O   1 
ATOM   3765 C  CB  . ASP B  1  153 ? 25.629  -24.020 63.470 1.00 39.72  ? 166 ASP B CB  1 
ATOM   3766 C  CG  . ASP B  1  153 ? 25.922  -25.246 64.325 1.00 42.16  ? 166 ASP B CG  1 
ATOM   3767 O  OD1 . ASP B  1  153 ? 26.616  -26.160 63.822 1.00 40.61  ? 166 ASP B OD1 1 
ATOM   3768 O  OD2 . ASP B  1  153 ? 25.429  -25.280 65.488 1.00 44.34  ? 166 ASP B OD2 1 
ATOM   3769 N  N   . PHE B  1  154 ? 22.701  -24.704 62.336 1.00 37.23  ? 167 PHE B N   1 
ATOM   3770 C  CA  . PHE B  1  154 ? 21.499  -25.521 62.380 1.00 31.77  ? 167 PHE B CA  1 
ATOM   3771 C  C   . PHE B  1  154 ? 21.119  -25.963 60.977 1.00 29.44  ? 167 PHE B C   1 
ATOM   3772 O  O   . PHE B  1  154 ? 20.635  -27.078 60.804 1.00 28.98  ? 167 PHE B O   1 
ATOM   3773 C  CB  . PHE B  1  154 ? 20.359  -24.781 63.073 1.00 33.58  ? 167 PHE B CB  1 
ATOM   3774 C  CG  . PHE B  1  154 ? 20.328  -24.986 64.578 1.00 35.37  ? 167 PHE B CG  1 
ATOM   3775 C  CD1 . PHE B  1  154 ? 21.359  -24.525 65.383 1.00 39.96  ? 167 PHE B CD1 1 
ATOM   3776 C  CD2 . PHE B  1  154 ? 19.261  -25.632 65.185 1.00 39.16  ? 167 PHE B CD2 1 
ATOM   3777 C  CE1 . PHE B  1  154 ? 21.320  -24.698 66.755 1.00 39.21  ? 167 PHE B CE1 1 
ATOM   3778 C  CE2 . PHE B  1  154 ? 19.224  -25.798 66.558 1.00 38.71  ? 167 PHE B CE2 1 
ATOM   3779 C  CZ  . PHE B  1  154 ? 20.250  -25.321 67.336 1.00 39.45  ? 167 PHE B CZ  1 
ATOM   3780 N  N   . SER B  1  155 ? 21.356  -25.109 59.973 1.00 30.27  ? 168 SER B N   1 
ATOM   3781 C  CA  . SER B  1  155 ? 21.118  -25.500 58.586 1.00 29.00  ? 168 SER B CA  1 
ATOM   3782 C  C   . SER B  1  155 ? 22.027  -26.666 58.187 1.00 29.78  ? 168 SER B C   1 
ATOM   3783 O  O   . SER B  1  155 ? 21.624  -27.537 57.422 1.00 28.79  ? 168 SER B O   1 
ATOM   3784 C  CB  . SER B  1  155 ? 21.298  -24.323 57.656 1.00 30.79  ? 168 SER B CB  1 
ATOM   3785 O  OG  . SER B  1  155 ? 20.413  -23.260 57.976 1.00 31.40  ? 168 SER B OG  1 
ATOM   3786 N  N   . ASN B  1  156 ? 23.275  -26.656 58.688 1.00 32.63  ? 169 ASN B N   1 
ATOM   3787 C  CA  . ASN B  1  156 ? 24.222  -27.733 58.434 1.00 33.95  ? 169 ASN B CA  1 
ATOM   3788 C  C   . ASN B  1  156 ? 23.763  -29.017 59.132 1.00 33.44  ? 169 ASN B C   1 
ATOM   3789 O  O   . ASN B  1  156 ? 23.817  -30.089 58.545 1.00 32.75  ? 169 ASN B O   1 
ATOM   3790 C  CB  . ASN B  1  156 ? 25.635  -27.354 58.867 1.00 35.54  ? 169 ASN B CB  1 
ATOM   3791 C  CG  . ASN B  1  156 ? 26.326  -26.390 57.932 1.00 35.41  ? 169 ASN B CG  1 
ATOM   3792 O  OD1 . ASN B  1  156 ? 26.047  -26.340 56.719 1.00 40.63  ? 169 ASN B OD1 1 
ATOM   3793 N  ND2 . ASN B  1  156 ? 27.269  -25.654 58.493 1.00 34.20  ? 169 ASN B ND2 1 
ATOM   3794 N  N   . ARG B  1  157 ? 23.280  -28.901 60.374 1.00 32.83  ? 170 ARG B N   1 
ATOM   3795 C  CA  . ARG B  1  157 ? 22.961  -30.073 61.177 1.00 34.79  ? 170 ARG B CA  1 
ATOM   3796 C  C   . ARG B  1  157 ? 21.639  -30.729 60.772 1.00 36.31  ? 170 ARG B C   1 
ATOM   3797 O  O   . ARG B  1  157 ? 21.493  -31.930 60.967 1.00 32.64  ? 170 ARG B O   1 
ATOM   3798 C  CB  . ARG B  1  157 ? 22.934  -29.721 62.666 1.00 37.29  ? 170 ARG B CB  1 
ATOM   3799 C  CG  . ARG B  1  157 ? 24.151  -28.919 63.087 1.00 39.63  ? 170 ARG B CG  1 
ATOM   3800 C  CD  . ARG B  1  157 ? 24.480  -28.902 64.553 1.00 41.71  ? 170 ARG B CD  1 
ATOM   3801 N  NE  . ARG B  1  157 ? 23.352  -29.068 65.469 1.00 45.84  ? 170 ARG B NE  1 
ATOM   3802 C  CZ  . ARG B  1  157 ? 23.188  -28.374 66.592 1.00 55.02  ? 170 ARG B CZ  1 
ATOM   3803 N  NH1 . ARG B  1  157 ? 22.304  -28.802 67.480 1.00 60.20  ? 170 ARG B NH1 1 
ATOM   3804 N  NH2 . ARG B  1  157 ? 23.935  -27.315 66.872 1.00 50.19  ? 170 ARG B NH2 1 
ATOM   3805 N  N   . TYR B  1  158 ? 20.668  -29.958 60.238 1.00 39.28  ? 171 TYR B N   1 
ATOM   3806 C  CA  . TYR B  1  158 ? 19.333  -30.499 60.009 1.00 36.57  ? 171 TYR B CA  1 
ATOM   3807 C  C   . TYR B  1  158 ? 18.833  -30.331 58.576 1.00 38.36  ? 171 TYR B C   1 
ATOM   3808 O  O   . TYR B  1  158 ? 17.847  -30.986 58.220 1.00 40.84  ? 171 TYR B O   1 
ATOM   3809 C  CB  . TYR B  1  158 ? 18.336  -29.860 60.973 1.00 36.76  ? 171 TYR B CB  1 
ATOM   3810 C  CG  . TYR B  1  158 ? 18.702  -30.105 62.427 1.00 38.87  ? 171 TYR B CG  1 
ATOM   3811 C  CD1 . TYR B  1  158 ? 18.452  -31.335 63.028 1.00 41.49  ? 171 TYR B CD1 1 
ATOM   3812 C  CD2 . TYR B  1  158 ? 19.314  -29.119 63.194 1.00 39.27  ? 171 TYR B CD2 1 
ATOM   3813 C  CE1 . TYR B  1  158 ? 18.793  -31.574 64.351 1.00 40.34  ? 171 TYR B CE1 1 
ATOM   3814 C  CE2 . TYR B  1  158 ? 19.658  -29.344 64.518 1.00 41.57  ? 171 TYR B CE2 1 
ATOM   3815 C  CZ  . TYR B  1  158 ? 19.400  -30.579 65.097 1.00 40.76  ? 171 TYR B CZ  1 
ATOM   3816 O  OH  . TYR B  1  158 ? 19.735  -30.818 66.397 1.00 40.33  ? 171 TYR B OH  1 
ATOM   3817 N  N   . GLY B  1  159 ? 19.486  -29.486 57.760 1.00 37.12  ? 172 GLY B N   1 
ATOM   3818 C  CA  . GLY B  1  159 ? 18.960  -29.140 56.445 1.00 35.63  ? 172 GLY B CA  1 
ATOM   3819 C  C   . GLY B  1  159 ? 19.951  -29.367 55.304 1.00 36.09  ? 172 GLY B C   1 
ATOM   3820 O  O   . GLY B  1  159 ? 19.771  -28.838 54.202 1.00 37.31  ? 172 GLY B O   1 
ATOM   3821 N  N   . GLY B  1  160 ? 20.994  -30.162 55.552 1.00 36.71  ? 173 GLY B N   1 
ATOM   3822 C  CA  . GLY B  1  160 ? 21.962  -30.473 54.513 1.00 36.13  ? 173 GLY B CA  1 
ATOM   3823 C  C   . GLY B  1  160 ? 22.704  -29.231 54.013 1.00 34.46  ? 173 GLY B C   1 
ATOM   3824 O  O   . GLY B  1  160 ? 23.154  -29.207 52.865 1.00 34.40  ? 173 GLY B O   1 
ATOM   3825 N  N   . GLY B  1  161 ? 22.812  -28.210 54.879 1.00 34.78  ? 174 GLY B N   1 
ATOM   3826 C  CA  . GLY B  1  161 ? 23.492  -26.968 54.546 1.00 35.43  ? 174 GLY B CA  1 
ATOM   3827 C  C   . GLY B  1  161 ? 22.546  -25.882 54.038 1.00 35.88  ? 174 GLY B C   1 
ATOM   3828 O  O   . GLY B  1  161 ? 23.005  -24.788 53.720 1.00 32.52  ? 174 GLY B O   1 
ATOM   3829 N  N   . PHE B  1  162 ? 21.236  -26.186 54.001 1.00 37.98  ? 175 PHE B N   1 
ATOM   3830 C  CA  . PHE B  1  162 ? 20.205  -25.250 53.574 1.00 37.66  ? 175 PHE B CA  1 
ATOM   3831 C  C   . PHE B  1  162 ? 19.171  -25.056 54.684 1.00 38.43  ? 175 PHE B C   1 
ATOM   3832 O  O   . PHE B  1  162 ? 19.069  -25.879 55.588 1.00 40.51  ? 175 PHE B O   1 
ATOM   3833 C  CB  . PHE B  1  162 ? 19.539  -25.771 52.301 1.00 35.59  ? 175 PHE B CB  1 
ATOM   3834 C  CG  . PHE B  1  162 ? 20.463  -25.894 51.101 1.00 35.67  ? 175 PHE B CG  1 
ATOM   3835 C  CD1 . PHE B  1  162 ? 21.166  -27.064 50.864 1.00 34.42  ? 175 PHE B CD1 1 
ATOM   3836 C  CD2 . PHE B  1  162 ? 20.611  -24.840 50.203 1.00 37.55  ? 175 PHE B CD2 1 
ATOM   3837 C  CE1 . PHE B  1  162 ? 21.999  -27.176 49.757 1.00 35.58  ? 175 PHE B CE1 1 
ATOM   3838 C  CE2 . PHE B  1  162 ? 21.442  -24.961 49.097 1.00 39.01  ? 175 PHE B CE2 1 
ATOM   3839 C  CZ  . PHE B  1  162 ? 22.146  -26.125 48.883 1.00 35.65  ? 175 PHE B CZ  1 
ATOM   3840 N  N   . TYR B  1  163 ? 18.407  -23.957 54.614 1.00 37.73  ? 176 TYR B N   1 
ATOM   3841 C  CA  . TYR B  1  163 ? 17.339  -23.701 55.569 1.00 36.64  ? 176 TYR B CA  1 
ATOM   3842 C  C   . TYR B  1  163 ? 16.023  -24.237 55.012 1.00 36.86  ? 176 TYR B C   1 
ATOM   3843 O  O   . TYR B  1  163 ? 15.629  -23.855 53.922 1.00 38.90  ? 176 TYR B O   1 
ATOM   3844 C  CB  . TYR B  1  163 ? 17.264  -22.205 55.860 1.00 35.10  ? 176 TYR B CB  1 
ATOM   3845 C  CG  . TYR B  1  163 ? 16.316  -21.836 56.985 1.00 34.13  ? 176 TYR B CG  1 
ATOM   3846 C  CD1 . TYR B  1  163 ? 16.676  -22.002 58.321 1.00 34.74  ? 176 TYR B CD1 1 
ATOM   3847 C  CD2 . TYR B  1  163 ? 15.068  -21.310 56.712 1.00 34.63  ? 176 TYR B CD2 1 
ATOM   3848 C  CE1 . TYR B  1  163 ? 15.823  -21.650 59.355 1.00 33.78  ? 176 TYR B CE1 1 
ATOM   3849 C  CE2 . TYR B  1  163 ? 14.205  -20.940 57.737 1.00 36.53  ? 176 TYR B CE2 1 
ATOM   3850 C  CZ  . TYR B  1  163 ? 14.581  -21.110 59.061 1.00 35.74  ? 176 TYR B CZ  1 
ATOM   3851 O  OH  . TYR B  1  163 ? 13.704  -20.764 60.050 1.00 35.21  ? 176 TYR B OH  1 
ATOM   3852 N  N   . ASN B  1  164 ? 15.383  -25.148 55.759 1.00 39.23  ? 177 ASN B N   1 
ATOM   3853 C  CA  . ASN B  1  164 ? 14.133  -25.793 55.369 1.00 39.44  ? 177 ASN B CA  1 
ATOM   3854 C  C   . ASN B  1  164 ? 13.265  -25.928 56.628 1.00 37.46  ? 177 ASN B C   1 
ATOM   3855 O  O   . ASN B  1  164 ? 13.671  -25.524 57.720 1.00 36.28  ? 177 ASN B O   1 
ATOM   3856 C  CB  . ASN B  1  164 ? 14.401  -27.075 54.565 1.00 39.27  ? 177 ASN B CB  1 
ATOM   3857 C  CG  . ASN B  1  164 ? 14.743  -28.308 55.393 1.00 42.15  ? 177 ASN B CG  1 
ATOM   3858 O  OD1 . ASN B  1  164 ? 14.826  -28.202 56.616 1.00 41.75  ? 177 ASN B OD1 1 
ATOM   3859 N  ND2 . ASN B  1  164 ? 14.929  -29.498 54.796 1.00 43.15  ? 177 ASN B ND2 1 
ATOM   3860 N  N   . LEU B  1  165 ? 12.080  -26.522 56.491 1.00 40.39  ? 178 LEU B N   1 
ATOM   3861 C  CA  . LEU B  1  165 ? 11.108  -26.502 57.583 1.00 43.29  ? 178 LEU B CA  1 
ATOM   3862 C  C   . LEU B  1  165 ? 11.608  -27.249 58.824 1.00 37.62  ? 178 LEU B C   1 
ATOM   3863 O  O   . LEU B  1  165 ? 11.318  -26.837 59.940 1.00 34.68  ? 178 LEU B O   1 
ATOM   3864 C  CB  . LEU B  1  165 ? 9.761   -27.028 57.091 1.00 46.85  ? 178 LEU B CB  1 
ATOM   3865 C  CG  . LEU B  1  165 ? 8.530   -26.468 57.809 1.00 50.06  ? 178 LEU B CG  1 
ATOM   3866 C  CD1 . LEU B  1  165 ? 8.510   -24.946 57.804 1.00 49.79  ? 178 LEU B CD1 1 
ATOM   3867 C  CD2 . LEU B  1  165 ? 7.266   -27.016 57.173 1.00 51.19  ? 178 LEU B CD2 1 
ATOM   3868 N  N   . THR B  1  166 ? 12.382  -28.325 58.633 1.00 37.65  ? 179 THR B N   1 
ATOM   3869 C  CA  . THR B  1  166 ? 12.962  -29.069 59.743 1.00 37.67  ? 179 THR B CA  1 
ATOM   3870 C  C   . THR B  1  166 ? 13.887  -28.156 60.544 1.00 39.72  ? 179 THR B C   1 
ATOM   3871 O  O   . THR B  1  166 ? 13.814  -28.138 61.766 1.00 41.26  ? 179 THR B O   1 
ATOM   3872 C  CB  . THR B  1  166 ? 13.733  -30.282 59.225 1.00 38.85  ? 179 THR B CB  1 
ATOM   3873 O  OG1 . THR B  1  166 ? 12.945  -30.892 58.210 1.00 36.29  ? 179 THR B OG1 1 
ATOM   3874 C  CG2 . THR B  1  166 ? 14.033  -31.292 60.315 1.00 41.31  ? 179 THR B CG2 1 
ATOM   3875 N  N   . VAL B  1  167 ? 14.748  -27.406 59.837 1.00 38.39  ? 180 VAL B N   1 
ATOM   3876 C  CA  . VAL B  1  167 ? 15.713  -26.508 60.456 1.00 37.38  ? 180 VAL B CA  1 
ATOM   3877 C  C   . VAL B  1  167 ? 14.962  -25.466 61.279 1.00 37.72  ? 180 VAL B C   1 
ATOM   3878 O  O   . VAL B  1  167 ? 15.406  -25.092 62.369 1.00 36.50  ? 180 VAL B O   1 
ATOM   3879 C  CB  . VAL B  1  167 ? 16.620  -25.792 59.430 1.00 38.12  ? 180 VAL B CB  1 
ATOM   3880 C  CG1 . VAL B  1  167 ? 17.718  -24.979 60.098 1.00 34.72  ? 180 VAL B CG1 1 
ATOM   3881 C  CG2 . VAL B  1  167 ? 17.241  -26.756 58.441 1.00 39.27  ? 180 VAL B CG2 1 
ATOM   3882 N  N   . ALA B  1  168 ? 13.851  -24.965 60.720 1.00 37.90  ? 181 ALA B N   1 
ATOM   3883 C  CA  . ALA B  1  168 ? 13.091  -23.910 61.363 1.00 40.04  ? 181 ALA B CA  1 
ATOM   3884 C  C   . ALA B  1  168 ? 12.565  -24.392 62.717 1.00 40.45  ? 181 ALA B C   1 
ATOM   3885 O  O   . ALA B  1  168 ? 12.692  -23.684 63.716 1.00 38.10  ? 181 ALA B O   1 
ATOM   3886 C  CB  . ALA B  1  168 ? 11.987  -23.446 60.445 1.00 43.04  ? 181 ALA B CB  1 
ATOM   3887 N  N   . GLY B  1  169 ? 11.997  -25.603 62.745 1.00 41.12  ? 182 GLY B N   1 
ATOM   3888 C  CA  . GLY B  1  169 ? 11.505  -26.193 63.979 1.00 43.18  ? 182 GLY B CA  1 
ATOM   3889 C  C   . GLY B  1  169 ? 12.582  -26.231 65.065 1.00 45.75  ? 182 GLY B C   1 
ATOM   3890 O  O   . GLY B  1  169 ? 12.340  -25.833 66.207 1.00 51.76  ? 182 GLY B O   1 
ATOM   3891 N  N   . GLU B  1  170 ? 13.773  -26.713 64.684 1.00 43.06  ? 183 GLU B N   1 
ATOM   3892 C  CA  . GLU B  1  170 ? 14.888  -26.869 65.602 1.00 44.57  ? 183 GLU B CA  1 
ATOM   3893 C  C   . GLU B  1  170 ? 15.429  -25.507 66.039 1.00 40.84  ? 183 GLU B C   1 
ATOM   3894 O  O   . GLU B  1  170 ? 15.704  -25.302 67.214 1.00 40.30  ? 183 GLU B O   1 
ATOM   3895 C  CB  . GLU B  1  170 ? 16.004  -27.696 64.963 1.00 47.65  ? 183 GLU B CB  1 
ATOM   3896 C  CG  . GLU B  1  170 ? 15.643  -29.161 64.732 1.00 50.55  ? 183 GLU B CG  1 
ATOM   3897 C  CD  . GLU B  1  170 ? 15.120  -29.888 65.951 1.00 54.47  ? 183 GLU B CD  1 
ATOM   3898 O  OE1 . GLU B  1  170 ? 15.781  -29.851 67.002 1.00 59.03  ? 183 GLU B OE1 1 
ATOM   3899 O  OE2 . GLU B  1  170 ? 14.023  -30.466 65.848 1.00 58.54  ? 183 GLU B OE2 1 
ATOM   3900 N  N   . LEU B  1  171 ? 15.600  -24.575 65.098 1.00 39.73  ? 184 LEU B N   1 
ATOM   3901 C  CA  . LEU B  1  171 ? 16.243  -23.313 65.421 1.00 38.34  ? 184 LEU B CA  1 
ATOM   3902 C  C   . LEU B  1  171 ? 15.349  -22.482 66.343 1.00 35.54  ? 184 LEU B C   1 
ATOM   3903 O  O   . LEU B  1  171 ? 15.844  -21.840 67.261 1.00 35.47  ? 184 LEU B O   1 
ATOM   3904 C  CB  . LEU B  1  171 ? 16.611  -22.546 64.151 1.00 37.40  ? 184 LEU B CB  1 
ATOM   3905 C  CG  . LEU B  1  171 ? 17.256  -21.172 64.378 1.00 37.06  ? 184 LEU B CG  1 
ATOM   3906 C  CD1 . LEU B  1  171 ? 18.590  -21.313 65.080 1.00 38.55  ? 184 LEU B CD1 1 
ATOM   3907 C  CD2 . LEU B  1  171 ? 17.403  -20.389 63.095 1.00 39.67  ? 184 LEU B CD2 1 
ATOM   3908 N  N   . ARG B  1  172 ? 14.040  -22.474 66.080 1.00 37.23  ? 185 ARG B N   1 
ATOM   3909 C  CA  . ARG B  1  172 ? 13.096  -21.671 66.849 1.00 40.84  ? 185 ARG B CA  1 
ATOM   3910 C  C   . ARG B  1  172 ? 13.163  -22.074 68.325 1.00 37.74  ? 185 ARG B C   1 
ATOM   3911 O  O   . ARG B  1  172 ? 13.277  -21.215 69.199 1.00 34.31  ? 185 ARG B O   1 
ATOM   3912 C  CB  . ARG B  1  172 ? 11.701  -21.791 66.208 1.00 41.52  ? 185 ARG B CB  1 
ATOM   3913 C  CG  . ARG B  1  172 ? 10.475  -21.430 67.034 1.00 40.48  ? 185 ARG B CG  1 
ATOM   3914 C  CD  . ARG B  1  172 ? 10.512  -20.070 67.715 1.00 41.39  ? 185 ARG B CD  1 
ATOM   3915 N  NE  . ARG B  1  172 ? 10.805  -18.964 66.797 1.00 41.54  ? 185 ARG B NE  1 
ATOM   3916 C  CZ  . ARG B  1  172 ? 11.691  -17.990 66.999 1.00 41.45  ? 185 ARG B CZ  1 
ATOM   3917 N  NH1 . ARG B  1  172 ? 12.450  -17.985 68.085 1.00 41.77  ? 185 ARG B NH1 1 
ATOM   3918 N  NH2 . ARG B  1  172 ? 11.807  -17.005 66.114 1.00 41.98  ? 185 ARG B NH2 1 
ATOM   3919 N  N   . TYR B  1  173 ? 13.109  -23.386 68.583 1.00 36.38  ? 186 TYR B N   1 
ATOM   3920 C  CA  . TYR B  1  173 ? 13.160  -23.914 69.936 1.00 40.59  ? 186 TYR B CA  1 
ATOM   3921 C  C   . TYR B  1  173 ? 14.476  -23.504 70.602 1.00 42.23  ? 186 TYR B C   1 
ATOM   3922 O  O   . TYR B  1  173 ? 14.483  -23.015 71.729 1.00 45.86  ? 186 TYR B O   1 
ATOM   3923 C  CB  . TYR B  1  173 ? 12.968  -25.437 69.908 1.00 45.36  ? 186 TYR B CB  1 
ATOM   3924 C  CG  . TYR B  1  173 ? 12.953  -26.077 71.288 1.00 50.56  ? 186 TYR B CG  1 
ATOM   3925 C  CD1 . TYR B  1  173 ? 11.906  -25.830 72.164 1.00 58.13  ? 186 TYR B CD1 1 
ATOM   3926 C  CD2 . TYR B  1  173 ? 13.970  -26.922 71.720 1.00 54.18  ? 186 TYR B CD2 1 
ATOM   3927 C  CE1 . TYR B  1  173 ? 11.865  -26.393 73.431 1.00 60.36  ? 186 TYR B CE1 1 
ATOM   3928 C  CE2 . TYR B  1  173 ? 13.945  -27.489 72.985 1.00 59.42  ? 186 TYR B CE2 1 
ATOM   3929 C  CZ  . TYR B  1  173 ? 12.885  -27.230 73.841 1.00 61.37  ? 186 TYR B CZ  1 
ATOM   3930 O  OH  . TYR B  1  173 ? 12.830  -27.764 75.094 1.00 59.98  ? 186 TYR B OH  1 
ATOM   3931 N  N   . SER B  1  174 ? 15.590  -23.692 69.891 1.00 38.13  ? 187 SER B N   1 
ATOM   3932 C  CA  . SER B  1  174 ? 16.904  -23.460 70.461 1.00 38.77  ? 187 SER B CA  1 
ATOM   3933 C  C   . SER B  1  174 ? 17.091  -21.988 70.815 1.00 38.37  ? 187 SER B C   1 
ATOM   3934 O  O   . SER B  1  174 ? 17.653  -21.687 71.865 1.00 41.60  ? 187 SER B O   1 
ATOM   3935 C  CB  . SER B  1  174 ? 17.975  -23.961 69.543 1.00 42.15  ? 187 SER B CB  1 
ATOM   3936 O  OG  . SER B  1  174 ? 19.263  -23.752 70.101 1.00 45.59  ? 187 SER B OG  1 
ATOM   3937 N  N   . ARG B  1  175 ? 16.574  -21.074 69.980 1.00 37.67  ? 188 ARG B N   1 
ATOM   3938 C  CA  . ARG B  1  175 ? 16.659  -19.645 70.270 1.00 39.07  ? 188 ARG B CA  1 
ATOM   3939 C  C   . ARG B  1  175 ? 15.830  -19.289 71.505 1.00 39.32  ? 188 ARG B C   1 
ATOM   3940 O  O   . ARG B  1  175 ? 16.196  -18.387 72.262 1.00 39.45  ? 188 ARG B O   1 
ATOM   3941 C  CB  . ARG B  1  175 ? 16.237  -18.762 69.094 1.00 39.08  ? 188 ARG B CB  1 
ATOM   3942 C  CG  . ARG B  1  175 ? 17.194  -18.839 67.910 1.00 39.45  ? 188 ARG B CG  1 
ATOM   3943 C  CD  . ARG B  1  175 ? 18.525  -18.166 68.177 1.00 36.22  ? 188 ARG B CD  1 
ATOM   3944 N  NE  . ARG B  1  175 ? 18.308  -16.735 68.383 1.00 33.31  ? 188 ARG B NE  1 
ATOM   3945 C  CZ  . ARG B  1  175 ? 18.498  -16.051 69.501 1.00 35.80  ? 188 ARG B CZ  1 
ATOM   3946 N  NH1 . ARG B  1  175 ? 19.049  -16.601 70.571 1.00 36.30  ? 188 ARG B NH1 1 
ATOM   3947 N  NH2 . ARG B  1  175 ? 18.146  -14.777 69.545 1.00 38.68  ? 188 ARG B NH2 1 
ATOM   3948 N  N   . ILE B  1  176 ? 14.711  -19.987 71.705 1.00 38.89  ? 189 ILE B N   1 
ATOM   3949 C  CA  . ILE B  1  176 ? 13.916  -19.768 72.897 1.00 39.79  ? 189 ILE B CA  1 
ATOM   3950 C  C   . ILE B  1  176 ? 14.747  -20.150 74.118 1.00 38.88  ? 189 ILE B C   1 
ATOM   3951 O  O   . ILE B  1  176 ? 14.838  -19.367 75.058 1.00 36.43  ? 189 ILE B O   1 
ATOM   3952 C  CB  . ILE B  1  176 ? 12.577  -20.517 72.814 1.00 40.55  ? 189 ILE B CB  1 
ATOM   3953 C  CG1 . ILE B  1  176 ? 11.660  -19.865 71.788 1.00 36.67  ? 189 ILE B CG1 1 
ATOM   3954 C  CG2 . ILE B  1  176 ? 11.913  -20.591 74.194 1.00 41.78  ? 189 ILE B CG2 1 
ATOM   3955 C  CD1 . ILE B  1  176 ? 10.448  -20.696 71.434 1.00 36.00  ? 189 ILE B CD1 1 
ATOM   3956 N  N   . GLN B  1  177 ? 15.384  -21.328 74.069 1.00 41.54  ? 190 GLN B N   1 
ATOM   3957 C  CA  . GLN B  1  177 ? 16.253  -21.787 75.144 1.00 45.38  ? 190 GLN B CA  1 
ATOM   3958 C  C   . GLN B  1  177 ? 17.383  -20.782 75.415 1.00 45.97  ? 190 GLN B C   1 
ATOM   3959 O  O   . GLN B  1  177 ? 17.651  -20.484 76.575 1.00 46.64  ? 190 GLN B O   1 
ATOM   3960 C  CB  . GLN B  1  177 ? 16.798  -23.187 74.844 1.00 51.90  ? 190 GLN B CB  1 
ATOM   3961 C  CG  . GLN B  1  177 ? 15.737  -24.277 74.746 1.00 55.72  ? 190 GLN B CG  1 
ATOM   3962 C  CD  . GLN B  1  177 ? 14.832  -24.332 75.962 1.00 71.65  ? 190 GLN B CD  1 
ATOM   3963 O  OE1 . GLN B  1  177 ? 15.207  -23.953 77.080 1.00 73.61  ? 190 GLN B OE1 1 
ATOM   3964 N  NE2 . GLN B  1  177 ? 13.612  -24.807 75.762 1.00 77.93  ? 190 GLN B NE2 1 
ATOM   3965 N  N   . ASP B  1  178 ? 18.045  -20.266 74.365 1.00 43.24  ? 191 ASP B N   1 
ATOM   3966 C  CA  . ASP B  1  178 ? 19.080  -19.251 74.525 1.00 46.08  ? 191 ASP B CA  1 
ATOM   3967 C  C   . ASP B  1  178 ? 18.583  -18.077 75.370 1.00 45.34  ? 191 ASP B C   1 
ATOM   3968 O  O   . ASP B  1  178 ? 19.304  -17.583 76.237 1.00 45.33  ? 191 ASP B O   1 
ATOM   3969 C  CB  . ASP B  1  178 ? 19.556  -18.676 73.193 1.00 50.37  ? 191 ASP B CB  1 
ATOM   3970 C  CG  . ASP B  1  178 ? 20.370  -19.606 72.296 1.00 52.91  ? 191 ASP B CG  1 
ATOM   3971 O  OD1 . ASP B  1  178 ? 20.802  -20.677 72.794 1.00 52.74  ? 191 ASP B OD1 1 
ATOM   3972 O  OD2 . ASP B  1  178 ? 20.567  -19.256 71.099 1.00 47.47  ? 191 ASP B OD2 1 
ATOM   3973 N  N   . SER B  1  179 ? 17.361  -17.606 75.088 1.00 43.93  ? 192 SER B N   1 
ATOM   3974 C  CA  . SER B  1  179 ? 16.835  -16.418 75.743 1.00 42.07  ? 192 SER B CA  1 
ATOM   3975 C  C   . SER B  1  179 ? 16.415  -16.724 77.187 1.00 41.84  ? 192 SER B C   1 
ATOM   3976 O  O   . SER B  1  179 ? 16.604  -15.883 78.066 1.00 38.88  ? 192 SER B O   1 
ATOM   3977 C  CB  . SER B  1  179 ? 15.722  -15.788 74.925 1.00 39.57  ? 192 SER B CB  1 
ATOM   3978 O  OG  . SER B  1  179 ? 16.252  -15.039 73.841 1.00 36.02  ? 192 SER B OG  1 
ATOM   3979 N  N   . ILE B  1  180 ? 15.863  -17.925 77.435 1.00 42.44  ? 193 ILE B N   1 
ATOM   3980 C  CA  . ILE B  1  180 ? 15.507  -18.347 78.784 1.00 47.34  ? 193 ILE B CA  1 
ATOM   3981 C  C   . ILE B  1  180 ? 16.752  -18.307 79.668 1.00 49.09  ? 193 ILE B C   1 
ATOM   3982 O  O   . ILE B  1  180 ? 16.702  -17.830 80.799 1.00 43.92  ? 193 ILE B O   1 
ATOM   3983 C  CB  . ILE B  1  180 ? 14.856  -19.744 78.783 1.00 48.26  ? 193 ILE B CB  1 
ATOM   3984 C  CG1 . ILE B  1  180 ? 13.453  -19.709 78.182 1.00 48.59  ? 193 ILE B CG1 1 
ATOM   3985 C  CG2 . ILE B  1  180 ? 14.842  -20.346 80.186 1.00 47.61  ? 193 ILE B CG2 1 
ATOM   3986 C  CD1 . ILE B  1  180 ? 12.788  -21.069 78.074 1.00 50.08  ? 193 ILE B CD1 1 
ATOM   3987 N  N   . ALA B  1  181 ? 17.870  -18.800 79.124 1.00 51.08  ? 194 ALA B N   1 
ATOM   3988 C  CA  . ALA B  1  181 ? 19.085  -19.027 79.887 1.00 47.61  ? 194 ALA B CA  1 
ATOM   3989 C  C   . ALA B  1  181 ? 19.881  -17.746 80.093 1.00 45.34  ? 194 ALA B C   1 
ATOM   3990 O  O   . ALA B  1  181 ? 20.728  -17.717 80.978 1.00 50.85  ? 194 ALA B O   1 
ATOM   3991 C  CB  . ALA B  1  181 ? 19.940  -20.062 79.194 1.00 47.97  ? 194 ALA B CB  1 
ATOM   3992 N  N   . THR B  1  182 ? 19.666  -16.708 79.277 1.00 44.51  ? 195 THR B N   1 
ATOM   3993 C  CA  . THR B  1  182 ? 20.604  -15.590 79.294 1.00 47.32  ? 195 THR B CA  1 
ATOM   3994 C  C   . THR B  1  182 ? 19.906  -14.241 79.472 1.00 46.25  ? 195 THR B C   1 
ATOM   3995 O  O   . THR B  1  182 ? 20.585  -13.249 79.721 1.00 46.88  ? 195 THR B O   1 
ATOM   3996 C  CB  . THR B  1  182 ? 21.473  -15.598 78.028 1.00 49.22  ? 195 THR B CB  1 
ATOM   3997 O  OG1 . THR B  1  182 ? 20.637  -15.331 76.902 1.00 47.61  ? 195 THR B OG1 1 
ATOM   3998 C  CG2 . THR B  1  182 ? 22.209  -16.911 77.826 1.00 48.13  ? 195 THR B CG2 1 
ATOM   3999 N  N   . ASN B  1  183 ? 18.577  -14.179 79.319 1.00 44.89  ? 196 ASN B N   1 
ATOM   4000 C  CA  . ASN B  1  183 ? 17.870  -12.908 79.341 1.00 44.30  ? 196 ASN B CA  1 
ATOM   4001 C  C   . ASN B  1  183 ? 16.850  -12.937 80.474 1.00 44.51  ? 196 ASN B C   1 
ATOM   4002 O  O   . ASN B  1  183 ? 15.812  -13.582 80.373 1.00 46.31  ? 196 ASN B O   1 
ATOM   4003 C  CB  . ASN B  1  183 ? 17.211  -12.601 77.999 1.00 43.33  ? 196 ASN B CB  1 
ATOM   4004 C  CG  . ASN B  1  183 ? 16.436  -11.295 77.994 1.00 45.02  ? 196 ASN B CG  1 
ATOM   4005 O  OD1 . ASN B  1  183 ? 16.407  -10.560 78.988 1.00 44.49  ? 196 ASN B OD1 1 
ATOM   4006 N  ND2 . ASN B  1  183 ? 15.796  -10.971 76.877 1.00 45.38  ? 196 ASN B ND2 1 
ATOM   4007 N  N   . PRO B  1  184 ? 17.101  -12.233 81.588 1.00 47.69  ? 197 PRO B N   1 
ATOM   4008 C  CA  . PRO B  1  184 ? 16.156  -12.240 82.708 1.00 53.41  ? 197 PRO B CA  1 
ATOM   4009 C  C   . PRO B  1  184 ? 14.818  -11.543 82.432 1.00 51.72  ? 197 PRO B C   1 
ATOM   4010 O  O   . PRO B  1  184 ? 13.841  -11.815 83.128 1.00 49.04  ? 197 PRO B O   1 
ATOM   4011 C  CB  . PRO B  1  184 ? 16.977  -11.544 83.811 1.00 50.01  ? 197 PRO B CB  1 
ATOM   4012 C  CG  . PRO B  1  184 ? 17.881  -10.594 83.046 1.00 50.80  ? 197 PRO B CG  1 
ATOM   4013 C  CD  . PRO B  1  184 ? 18.280  -11.383 81.815 1.00 49.38  ? 197 PRO B CD  1 
ATOM   4014 N  N   . GLU B  1  185 ? 14.781  -10.661 81.414 1.00 47.38  ? 198 GLU B N   1 
ATOM   4015 C  CA  . GLU B  1  185 ? 13.576  -9.930  81.051 1.00 46.21  ? 198 GLU B CA  1 
ATOM   4016 C  C   . GLU B  1  185 ? 12.836  -10.609 79.891 1.00 43.07  ? 198 GLU B C   1 
ATOM   4017 O  O   . GLU B  1  185 ? 11.920  -10.028 79.315 1.00 42.41  ? 198 GLU B O   1 
ATOM   4018 C  CB  . GLU B  1  185 ? 13.933  -8.485  80.698 1.00 48.60  ? 198 GLU B CB  1 
ATOM   4019 C  CG  . GLU B  1  185 ? 14.237  -7.600  81.905 1.00 51.96  ? 198 GLU B CG  1 
ATOM   4020 C  CD  . GLU B  1  185 ? 14.801  -6.228  81.547 1.00 55.06  ? 198 GLU B CD  1 
ATOM   4021 O  OE1 . GLU B  1  185 ? 14.823  -5.879  80.357 1.00 52.56  ? 198 GLU B OE1 1 
ATOM   4022 O  OE2 . GLU B  1  185 ? 15.249  -5.497  82.450 1.00 62.26  ? 198 GLU B OE2 1 
ATOM   4023 N  N   . PHE B  1  186 ? 13.207  -11.850 79.566 1.00 41.34  ? 199 PHE B N   1 
ATOM   4024 C  CA  . PHE B  1  186 ? 12.683  -12.540 78.399 1.00 42.46  ? 199 PHE B CA  1 
ATOM   4025 C  C   . PHE B  1  186 ? 11.168  -12.685 78.490 1.00 47.90  ? 199 PHE B C   1 
ATOM   4026 O  O   . PHE B  1  186 ? 10.660  -13.310 79.418 1.00 50.93  ? 199 PHE B O   1 
ATOM   4027 C  CB  . PHE B  1  186 ? 13.302  -13.933 78.270 1.00 41.58  ? 199 PHE B CB  1 
ATOM   4028 C  CG  . PHE B  1  186 ? 12.776  -14.791 77.127 1.00 40.11  ? 199 PHE B CG  1 
ATOM   4029 C  CD1 . PHE B  1  186 ? 12.671  -14.293 75.836 1.00 42.11  ? 199 PHE B CD1 1 
ATOM   4030 C  CD2 . PHE B  1  186 ? 12.388  -16.104 77.350 1.00 38.46  ? 199 PHE B CD2 1 
ATOM   4031 C  CE1 . PHE B  1  186 ? 12.205  -15.090 74.802 1.00 38.43  ? 199 PHE B CE1 1 
ATOM   4032 C  CE2 . PHE B  1  186 ? 11.928  -16.896 76.314 1.00 37.65  ? 199 PHE B CE2 1 
ATOM   4033 C  CZ  . PHE B  1  186 ? 11.838  -16.386 75.041 1.00 36.39  ? 199 PHE B CZ  1 
ATOM   4034 N  N   . GLN B  1  187 ? 10.477  -12.124 77.488 1.00 49.15  ? 200 GLN B N   1 
ATOM   4035 C  CA  . GLN B  1  187 ? 9.038   -12.258 77.317 1.00 46.03  ? 200 GLN B CA  1 
ATOM   4036 C  C   . GLN B  1  187 ? 8.765   -12.993 76.007 1.00 46.23  ? 200 GLN B C   1 
ATOM   4037 O  O   . GLN B  1  187 ? 9.442   -12.746 75.008 1.00 45.84  ? 200 GLN B O   1 
ATOM   4038 C  CB  . GLN B  1  187 ? 8.420   -10.859 77.277 1.00 49.84  ? 200 GLN B CB  1 
ATOM   4039 C  CG  . GLN B  1  187 ? 8.447   -10.115 78.611 1.00 53.47  ? 200 GLN B CG  1 
ATOM   4040 C  CD  . GLN B  1  187 ? 7.540   -10.750 79.646 1.00 55.88  ? 200 GLN B CD  1 
ATOM   4041 O  OE1 . GLN B  1  187 ? 6.313   -10.613 79.593 1.00 59.48  ? 200 GLN B OE1 1 
ATOM   4042 N  NE2 . GLN B  1  187 ? 8.129   -11.481 80.584 1.00 57.76  ? 200 GLN B NE2 1 
ATOM   4043 N  N   . PHE B  1  188 ? 7.770   -13.888 76.010 1.00 42.59  ? 201 PHE B N   1 
ATOM   4044 C  CA  . PHE B  1  188 ? 7.405   -14.616 74.805 1.00 37.06  ? 201 PHE B CA  1 
ATOM   4045 C  C   . PHE B  1  188 ? 5.901   -14.866 74.811 1.00 37.68  ? 201 PHE B C   1 
ATOM   4046 O  O   . PHE B  1  188 ? 5.445   -16.006 74.866 1.00 33.16  ? 201 PHE B O   1 
ATOM   4047 C  CB  . PHE B  1  188 ? 8.232   -15.899 74.739 1.00 33.94  ? 201 PHE B CB  1 
ATOM   4048 C  CG  . PHE B  1  188 ? 8.361   -16.491 73.347 1.00 35.94  ? 201 PHE B CG  1 
ATOM   4049 C  CD1 . PHE B  1  188 ? 9.101   -15.834 72.376 1.00 38.44  ? 201 PHE B CD1 1 
ATOM   4050 C  CD2 . PHE B  1  188 ? 7.791   -17.710 73.020 1.00 36.47  ? 201 PHE B CD2 1 
ATOM   4051 C  CE1 . PHE B  1  188 ? 9.239   -16.356 71.111 1.00 39.82  ? 201 PHE B CE1 1 
ATOM   4052 C  CE2 . PHE B  1  188 ? 7.921   -18.226 71.740 1.00 39.45  ? 201 PHE B CE2 1 
ATOM   4053 C  CZ  . PHE B  1  188 ? 8.642   -17.552 70.793 1.00 40.90  ? 201 PHE B CZ  1 
ATOM   4054 N  N   . LYS B  1  189 ? 5.132   -13.779 74.750 1.00 41.75  ? 202 LYS B N   1 
ATOM   4055 C  CA  . LYS B  1  189 ? 3.685   -13.870 74.861 1.00 45.14  ? 202 LYS B CA  1 
ATOM   4056 C  C   . LYS B  1  189 ? 3.014   -12.895 73.892 1.00 42.30  ? 202 LYS B C   1 
ATOM   4057 O  O   . LYS B  1  189 ? 3.644   -12.001 73.339 1.00 44.58  ? 202 LYS B O   1 
ATOM   4058 C  CB  . LYS B  1  189 ? 3.259   -13.608 76.309 1.00 46.19  ? 202 LYS B CB  1 
ATOM   4059 C  CG  . LYS B  1  189 ? 3.701   -12.269 76.895 1.00 53.69  ? 202 LYS B CG  1 
ATOM   4060 C  CD  . LYS B  1  189 ? 3.358   -12.076 78.374 1.00 59.32  ? 202 LYS B CD  1 
ATOM   4061 C  CE  . LYS B  1  189 ? 3.972   -13.122 79.245 1.00 69.14  ? 202 LYS B CE  1 
ATOM   4062 N  NZ  . LYS B  1  189 ? 3.740   -12.937 80.680 1.00 71.19  ? 202 LYS B NZ  1 
ATOM   4063 N  N   . ASN B  1  190 ? 1.714   -13.103 73.683 1.00 41.40  ? 203 ASN B N   1 
ATOM   4064 C  CA  . ASN B  1  190 ? 0.869   -12.169 72.963 1.00 41.36  ? 203 ASN B CA  1 
ATOM   4065 C  C   . ASN B  1  190 ? 1.368   -12.026 71.530 1.00 38.45  ? 203 ASN B C   1 
ATOM   4066 O  O   . ASN B  1  190 ? 1.487   -13.016 70.817 1.00 43.00  ? 203 ASN B O   1 
ATOM   4067 C  CB  . ASN B  1  190 ? 0.741   -10.858 73.731 1.00 43.16  ? 203 ASN B CB  1 
ATOM   4068 C  CG  . ASN B  1  190 ? 0.096   -11.070 75.082 1.00 46.11  ? 203 ASN B CG  1 
ATOM   4069 O  OD1 . ASN B  1  190 ? -0.869  -11.838 75.215 1.00 43.71  ? 203 ASN B OD1 1 
ATOM   4070 N  ND2 . ASN B  1  190 ? 0.626   -10.397 76.091 1.00 47.30  ? 203 ASN B ND2 1 
ATOM   4071 N  N   . VAL B  1  191 ? 1.647   -10.797 71.100 1.00 34.52  ? 204 VAL B N   1 
ATOM   4072 C  CA  . VAL B  1  191 ? 2.028   -10.564 69.724 1.00 34.89  ? 204 VAL B CA  1 
ATOM   4073 C  C   . VAL B  1  191 ? 3.271   -11.388 69.408 1.00 37.27  ? 204 VAL B C   1 
ATOM   4074 O  O   . VAL B  1  191 ? 3.328   -12.060 68.382 1.00 39.38  ? 204 VAL B O   1 
ATOM   4075 C  CB  . VAL B  1  191 ? 2.281   -9.074  69.442 1.00 37.86  ? 204 VAL B CB  1 
ATOM   4076 C  CG1 . VAL B  1  191 ? 2.744   -8.841  68.011 1.00 39.34  ? 204 VAL B CG1 1 
ATOM   4077 C  CG2 . VAL B  1  191 ? 1.060   -8.214  69.740 1.00 40.45  ? 204 VAL B CG2 1 
ATOM   4078 N  N   . ARG B  1  192 ? 4.269   -11.345 70.297 1.00 36.76  ? 205 ARG B N   1 
ATOM   4079 C  CA  . ARG B  1  192 ? 5.544   -11.958 69.994 1.00 35.16  ? 205 ARG B CA  1 
ATOM   4080 C  C   . ARG B  1  192 ? 5.389   -13.463 69.792 1.00 32.99  ? 205 ARG B C   1 
ATOM   4081 O  O   . ARG B  1  192 ? 6.032   -14.052 68.931 1.00 31.99  ? 205 ARG B O   1 
ATOM   4082 C  CB  . ARG B  1  192 ? 6.590   -11.686 71.079 1.00 38.77  ? 205 ARG B CB  1 
ATOM   4083 C  CG  . ARG B  1  192 ? 7.958   -12.264 70.731 1.00 39.77  ? 205 ARG B CG  1 
ATOM   4084 C  CD  . ARG B  1  192 ? 8.413   -11.838 69.350 1.00 40.39  ? 205 ARG B CD  1 
ATOM   4085 N  NE  . ARG B  1  192 ? 9.668   -12.465 68.936 1.00 42.81  ? 205 ARG B NE  1 
ATOM   4086 C  CZ  . ARG B  1  192 ? 10.064  -12.607 67.669 1.00 44.59  ? 205 ARG B CZ  1 
ATOM   4087 N  NH1 . ARG B  1  192 ? 9.313   -12.170 66.670 1.00 41.91  ? 205 ARG B NH1 1 
ATOM   4088 N  NH2 . ARG B  1  192 ? 11.210  -13.212 67.413 1.00 45.97  ? 205 ARG B NH2 1 
ATOM   4089 N  N   . PHE B  1  193 ? 4.545   -14.094 70.595 1.00 35.83  ? 206 PHE B N   1 
ATOM   4090 C  CA  . PHE B  1  193 ? 4.411   -15.534 70.522 1.00 36.83  ? 206 PHE B CA  1 
ATOM   4091 C  C   . PHE B  1  193 ? 3.884   -15.927 69.144 1.00 38.30  ? 206 PHE B C   1 
ATOM   4092 O  O   . PHE B  1  193 ? 4.323   -16.931 68.590 1.00 45.41  ? 206 PHE B O   1 
ATOM   4093 C  CB  . PHE B  1  193 ? 3.517   -16.062 71.641 1.00 36.19  ? 206 PHE B CB  1 
ATOM   4094 C  CG  . PHE B  1  193 ? 3.356   -17.568 71.567 1.00 35.14  ? 206 PHE B CG  1 
ATOM   4095 C  CD1 . PHE B  1  193 ? 4.321   -18.409 72.085 1.00 33.66  ? 206 PHE B CD1 1 
ATOM   4096 C  CD2 . PHE B  1  193 ? 2.251   -18.131 70.945 1.00 39.16  ? 206 PHE B CD2 1 
ATOM   4097 C  CE1 . PHE B  1  193 ? 4.175   -19.784 71.999 1.00 37.90  ? 206 PHE B CE1 1 
ATOM   4098 C  CE2 . PHE B  1  193 ? 2.110   -19.506 70.855 1.00 41.09  ? 206 PHE B CE2 1 
ATOM   4099 C  CZ  . PHE B  1  193 ? 3.069   -20.330 71.394 1.00 42.01  ? 206 PHE B CZ  1 
ATOM   4100 N  N   . ILE B  1  194 ? 2.968   -15.131 68.585 1.00 36.43  ? 207 ILE B N   1 
ATOM   4101 C  CA  . ILE B  1  194 ? 2.411   -15.439 67.277 1.00 41.54  ? 207 ILE B CA  1 
ATOM   4102 C  C   . ILE B  1  194 ? 3.417   -15.085 66.179 1.00 39.82  ? 207 ILE B C   1 
ATOM   4103 O  O   . ILE B  1  194 ? 3.661   -15.897 65.298 1.00 39.61  ? 207 ILE B O   1 
ATOM   4104 C  CB  . ILE B  1  194 ? 1.055   -14.743 67.076 1.00 44.88  ? 207 ILE B CB  1 
ATOM   4105 C  CG1 . ILE B  1  194 ? 0.069   -15.137 68.189 1.00 46.93  ? 207 ILE B CG1 1 
ATOM   4106 C  CG2 . ILE B  1  194 ? 0.497   -15.038 65.679 1.00 45.58  ? 207 ILE B CG2 1 
ATOM   4107 C  CD1 . ILE B  1  194 ? -0.519  -16.527 68.004 1.00 50.79  ? 207 ILE B CD1 1 
ATOM   4108 N  N   . THR B  1  195 ? 4.027   -13.895 66.243 1.00 39.62  ? 208 THR B N   1 
ATOM   4109 C  CA  . THR B  1  195 ? 4.890   -13.450 65.166 1.00 39.41  ? 208 THR B CA  1 
ATOM   4110 C  C   . THR B  1  195 ? 6.159   -14.301 65.099 1.00 43.25  ? 208 THR B C   1 
ATOM   4111 O  O   . THR B  1  195 ? 6.676   -14.518 64.011 1.00 44.65  ? 208 THR B O   1 
ATOM   4112 C  CB  . THR B  1  195 ? 5.196   -11.957 65.264 1.00 39.45  ? 208 THR B CB  1 
ATOM   4113 O  OG1 . THR B  1  195 ? 5.951   -11.624 66.419 1.00 39.85  ? 208 THR B OG1 1 
ATOM   4114 C  CG2 . THR B  1  195 ? 3.934   -11.121 65.270 1.00 41.11  ? 208 THR B CG2 1 
ATOM   4115 N  N   . ALA B  1  196 ? 6.633   -14.832 66.236 1.00 44.91  ? 209 ALA B N   1 
ATOM   4116 C  CA  . ALA B  1  196 ? 7.883   -15.584 66.272 1.00 41.30  ? 209 ALA B CA  1 
ATOM   4117 C  C   . ALA B  1  196 ? 7.818   -16.879 65.468 1.00 39.66  ? 209 ALA B C   1 
ATOM   4118 O  O   . ALA B  1  196 ? 8.848   -17.373 65.047 1.00 45.80  ? 209 ALA B O   1 
ATOM   4119 C  CB  . ALA B  1  196 ? 8.278   -15.891 67.693 1.00 40.85  ? 209 ALA B CB  1 
ATOM   4120 N  N   . TYR B  1  197 ? 6.636   -17.462 65.282 1.00 41.16  ? 210 TYR B N   1 
ATOM   4121 C  CA  . TYR B  1  197 ? 6.543   -18.705 64.533 1.00 40.58  ? 210 TYR B CA  1 
ATOM   4122 C  C   . TYR B  1  197 ? 6.427   -18.386 63.045 1.00 43.64  ? 210 TYR B C   1 
ATOM   4123 O  O   . TYR B  1  197 ? 7.043   -19.073 62.232 1.00 42.45  ? 210 TYR B O   1 
ATOM   4124 C  CB  . TYR B  1  197 ? 5.429   -19.588 65.101 1.00 38.02  ? 210 TYR B CB  1 
ATOM   4125 C  CG  . TYR B  1  197 ? 5.898   -20.265 66.376 1.00 36.31  ? 210 TYR B CG  1 
ATOM   4126 C  CD1 . TYR B  1  197 ? 6.595   -21.463 66.323 1.00 36.92  ? 210 TYR B CD1 1 
ATOM   4127 C  CD2 . TYR B  1  197 ? 5.718   -19.670 67.616 1.00 35.02  ? 210 TYR B CD2 1 
ATOM   4128 C  CE1 . TYR B  1  197 ? 7.082   -22.065 67.470 1.00 36.07  ? 210 TYR B CE1 1 
ATOM   4129 C  CE2 . TYR B  1  197 ? 6.217   -20.253 68.769 1.00 37.23  ? 210 TYR B CE2 1 
ATOM   4130 C  CZ  . TYR B  1  197 ? 6.890   -21.458 68.696 1.00 36.80  ? 210 TYR B CZ  1 
ATOM   4131 O  OH  . TYR B  1  197 ? 7.393   -22.048 69.819 1.00 43.63  ? 210 TYR B OH  1 
ATOM   4132 N  N   . GLY B  1  198 ? 5.669   -17.333 62.702 1.00 43.77  ? 211 GLY B N   1 
ATOM   4133 C  CA  . GLY B  1  198 ? 5.512   -16.899 61.321 1.00 41.65  ? 211 GLY B CA  1 
ATOM   4134 C  C   . GLY B  1  198 ? 6.839   -16.482 60.686 1.00 38.29  ? 211 GLY B C   1 
ATOM   4135 O  O   . GLY B  1  198 ? 7.126   -16.823 59.542 1.00 35.09  ? 211 GLY B O   1 
ATOM   4136 N  N   . GLU B  1  199 ? 7.650   -15.739 61.439 1.00 39.13  ? 212 GLU B N   1 
ATOM   4137 C  CA  . GLU B  1  199 ? 8.887   -15.191 60.911 1.00 39.22  ? 212 GLU B CA  1 
ATOM   4138 C  C   . GLU B  1  199 ? 9.845   -16.326 60.519 1.00 36.48  ? 212 GLU B C   1 
ATOM   4139 O  O   . GLU B  1  199 ? 10.679  -16.149 59.648 1.00 37.04  ? 212 GLU B O   1 
ATOM   4140 C  CB  . GLU B  1  199 ? 9.483   -14.165 61.885 1.00 43.35  ? 212 GLU B CB  1 
ATOM   4141 C  CG  . GLU B  1  199 ? 10.238  -14.795 63.062 1.00 51.41  ? 212 GLU B CG  1 
ATOM   4142 C  CD  . GLU B  1  199 ? 10.904  -13.851 64.088 1.00 53.13  ? 212 GLU B CD  1 
ATOM   4143 O  OE1 . GLU B  1  199 ? 10.612  -12.615 64.124 1.00 45.88  ? 212 GLU B OE1 1 
ATOM   4144 O  OE2 . GLU B  1  199 ? 11.740  -14.370 64.884 1.00 48.40  ? 212 GLU B OE2 1 
ATOM   4145 N  N   . THR B  1  200 ? 9.733   -17.503 61.136 1.00 35.75  ? 213 THR B N   1 
ATOM   4146 C  CA  . THR B  1  200 ? 10.696  -18.564 60.883 1.00 36.07  ? 213 THR B CA  1 
ATOM   4147 C  C   . THR B  1  200 ? 10.386  -19.280 59.571 1.00 36.56  ? 213 THR B C   1 
ATOM   4148 O  O   . THR B  1  200 ? 11.239  -20.018 59.090 1.00 41.19  ? 213 THR B O   1 
ATOM   4149 C  CB  . THR B  1  200 ? 10.744  -19.581 62.025 1.00 39.86  ? 213 THR B CB  1 
ATOM   4150 O  OG1 . THR B  1  200 ? 9.545   -20.354 61.988 1.00 44.39  ? 213 THR B OG1 1 
ATOM   4151 C  CG2 . THR B  1  200 ? 10.953  -18.909 63.371 1.00 41.27  ? 213 THR B CG2 1 
ATOM   4152 N  N   . VAL B  1  201 ? 9.182   -19.104 59.004 1.00 35.67  ? 214 VAL B N   1 
ATOM   4153 C  CA  . VAL B  1  201 ? 8.870   -19.743 57.736 1.00 32.80  ? 214 VAL B CA  1 
ATOM   4154 C  C   . VAL B  1  201 ? 8.886   -18.736 56.593 1.00 31.91  ? 214 VAL B C   1 
ATOM   4155 O  O   . VAL B  1  201 ? 8.884   -19.152 55.440 1.00 32.74  ? 214 VAL B O   1 
ATOM   4156 C  CB  . VAL B  1  201 ? 7.547   -20.528 57.753 1.00 33.59  ? 214 VAL B CB  1 
ATOM   4157 C  CG1 . VAL B  1  201 ? 7.598   -21.662 58.764 1.00 31.89  ? 214 VAL B CG1 1 
ATOM   4158 C  CG2 . VAL B  1  201 ? 6.332   -19.645 57.987 1.00 33.98  ? 214 VAL B CG2 1 
ATOM   4159 N  N   . PHE B  1  202 ? 8.941   -17.432 56.886 1.00 34.19  ? 215 PHE B N   1 
ATOM   4160 C  CA  . PHE B  1  202 ? 8.981   -16.434 55.825 1.00 35.66  ? 215 PHE B CA  1 
ATOM   4161 C  C   . PHE B  1  202 ? 10.175  -16.693 54.908 1.00 35.55  ? 215 PHE B C   1 
ATOM   4162 O  O   . PHE B  1  202 ? 10.055  -16.586 53.689 1.00 36.51  ? 215 PHE B O   1 
ATOM   4163 C  CB  . PHE B  1  202 ? 8.991   -14.992 56.344 1.00 33.77  ? 215 PHE B CB  1 
ATOM   4164 C  CG  . PHE B  1  202 ? 7.686   -14.492 56.942 1.00 36.00  ? 215 PHE B CG  1 
ATOM   4165 C  CD1 . PHE B  1  202 ? 6.507   -15.223 56.847 1.00 40.72  ? 215 PHE B CD1 1 
ATOM   4166 C  CD2 . PHE B  1  202 ? 7.630   -13.259 57.565 1.00 38.63  ? 215 PHE B CD2 1 
ATOM   4167 C  CE1 . PHE B  1  202 ? 5.323   -14.748 57.396 1.00 41.38  ? 215 PHE B CE1 1 
ATOM   4168 C  CE2 . PHE B  1  202 ? 6.447   -12.792 58.110 1.00 42.76  ? 215 PHE B CE2 1 
ATOM   4169 C  CZ  . PHE B  1  202 ? 5.295   -13.534 58.028 1.00 41.78  ? 215 PHE B CZ  1 
ATOM   4170 N  N   . PRO B  1  203 ? 11.372  -17.018 55.432 1.00 37.37  ? 216 PRO B N   1 
ATOM   4171 C  CA  . PRO B  1  203 ? 12.518  -17.286 54.568 1.00 38.44  ? 216 PRO B CA  1 
ATOM   4172 C  C   . PRO B  1  203 ? 12.284  -18.409 53.560 1.00 36.93  ? 216 PRO B C   1 
ATOM   4173 O  O   . PRO B  1  203 ? 12.803  -18.358 52.451 1.00 41.89  ? 216 PRO B O   1 
ATOM   4174 C  CB  . PRO B  1  203 ? 13.628  -17.620 55.568 1.00 40.25  ? 216 PRO B CB  1 
ATOM   4175 C  CG  . PRO B  1  203 ? 13.238  -16.890 56.829 1.00 41.56  ? 216 PRO B CG  1 
ATOM   4176 C  CD  . PRO B  1  203 ? 11.725  -17.054 56.855 1.00 42.06  ? 216 PRO B CD  1 
ATOM   4177 N  N   . ILE B  1  204 ? 11.491  -19.410 53.936 1.00 36.03  ? 217 ILE B N   1 
ATOM   4178 C  CA  . ILE B  1  204 ? 11.177  -20.522 53.047 1.00 38.40  ? 217 ILE B CA  1 
ATOM   4179 C  C   . ILE B  1  204 ? 10.167  -20.081 51.983 1.00 38.56  ? 217 ILE B C   1 
ATOM   4180 O  O   . ILE B  1  204 ? 10.336  -20.347 50.798 1.00 38.84  ? 217 ILE B O   1 
ATOM   4181 C  CB  . ILE B  1  204 ? 10.654  -21.721 53.861 1.00 39.83  ? 217 ILE B CB  1 
ATOM   4182 C  CG1 . ILE B  1  204 ? 11.690  -22.182 54.876 1.00 41.23  ? 217 ILE B CG1 1 
ATOM   4183 C  CG2 . ILE B  1  204 ? 10.222  -22.868 52.950 1.00 38.73  ? 217 ILE B CG2 1 
ATOM   4184 C  CD1 . ILE B  1  204 ? 11.164  -23.148 55.915 1.00 42.12  ? 217 ILE B CD1 1 
ATOM   4185 N  N   . ASN B  1  205 ? 9.089   -19.423 52.415 1.00 40.23  ? 218 ASN B N   1 
ATOM   4186 C  CA  . ASN B  1  205 ? 7.957   -19.159 51.543 1.00 35.34  ? 218 ASN B CA  1 
ATOM   4187 C  C   . ASN B  1  205 ? 8.193   -17.916 50.694 1.00 35.35  ? 218 ASN B C   1 
ATOM   4188 O  O   . ASN B  1  205 ? 7.598   -17.823 49.616 1.00 40.87  ? 218 ASN B O   1 
ATOM   4189 C  CB  . ASN B  1  205 ? 6.658   -19.018 52.324 1.00 34.25  ? 218 ASN B CB  1 
ATOM   4190 C  CG  . ASN B  1  205 ? 6.368   -20.221 53.190 1.00 34.48  ? 218 ASN B CG  1 
ATOM   4191 O  OD1 . ASN B  1  205 ? 6.747   -21.345 52.850 1.00 35.04  ? 218 ASN B OD1 1 
ATOM   4192 N  ND2 . ASN B  1  205 ? 5.721   -20.007 54.324 1.00 37.10  ? 218 ASN B ND2 1 
ATOM   4193 N  N   . LEU B  1  206 ? 9.048   -16.981 51.159 1.00 31.61  ? 219 LEU B N   1 
ATOM   4194 C  CA  . LEU B  1  206 ? 9.185   -15.692 50.489 1.00 29.68  ? 219 LEU B CA  1 
ATOM   4195 C  C   . LEU B  1  206 ? 10.603  -15.382 50.014 1.00 32.60  ? 219 LEU B C   1 
ATOM   4196 O  O   . LEU B  1  206 ? 10.737  -14.594 49.087 1.00 33.92  ? 219 LEU B O   1 
ATOM   4197 C  CB  . LEU B  1  206 ? 8.675   -14.603 51.419 1.00 28.93  ? 219 LEU B CB  1 
ATOM   4198 C  CG  . LEU B  1  206 ? 7.195   -14.726 51.793 1.00 29.84  ? 219 LEU B CG  1 
ATOM   4199 C  CD1 . LEU B  1  206 ? 6.841   -13.816 52.951 1.00 29.34  ? 219 LEU B CD1 1 
ATOM   4200 C  CD2 . LEU B  1  206 ? 6.302   -14.451 50.582 1.00 29.11  ? 219 LEU B CD2 1 
ATOM   4201 N  N   . PHE B  1  207 ? 11.644  -15.940 50.656 1.00 37.60  ? 220 PHE B N   1 
ATOM   4202 C  CA  . PHE B  1  207 ? 13.025  -15.618 50.316 1.00 35.40  ? 220 PHE B CA  1 
ATOM   4203 C  C   . PHE B  1  207 ? 13.593  -16.642 49.340 1.00 37.69  ? 220 PHE B C   1 
ATOM   4204 O  O   . PHE B  1  207 ? 14.639  -16.407 48.728 1.00 40.26  ? 220 PHE B O   1 
ATOM   4205 C  CB  . PHE B  1  207 ? 13.982  -15.575 51.509 1.00 34.69  ? 220 PHE B CB  1 
ATOM   4206 C  CG  . PHE B  1  207 ? 13.758  -14.450 52.507 1.00 36.53  ? 220 PHE B CG  1 
ATOM   4207 C  CD1 . PHE B  1  207 ? 12.949  -13.354 52.207 1.00 37.82  ? 220 PHE B CD1 1 
ATOM   4208 C  CD2 . PHE B  1  207 ? 14.381  -14.487 53.744 1.00 34.90  ? 220 PHE B CD2 1 
ATOM   4209 C  CE1 . PHE B  1  207 ? 12.767  -12.336 53.130 1.00 35.98  ? 220 PHE B CE1 1 
ATOM   4210 C  CE2 . PHE B  1  207 ? 14.185  -13.469 54.659 1.00 35.38  ? 220 PHE B CE2 1 
ATOM   4211 C  CZ  . PHE B  1  207 ? 13.378  -12.402 54.355 1.00 35.04  ? 220 PHE B CZ  1 
ATOM   4212 N  N   . VAL B  1  208 ? 12.930  -17.797 49.227 1.00 35.45  ? 221 VAL B N   1 
ATOM   4213 C  CA  . VAL B  1  208 ? 13.295  -18.769 48.214 1.00 32.57  ? 221 VAL B CA  1 
ATOM   4214 C  C   . VAL B  1  208 ? 12.669  -18.331 46.898 1.00 31.88  ? 221 VAL B C   1 
ATOM   4215 O  O   . VAL B  1  208 ? 11.492  -17.993 46.846 1.00 31.44  ? 221 VAL B O   1 
ATOM   4216 C  CB  . VAL B  1  208 ? 12.885  -20.199 48.597 1.00 29.67  ? 221 VAL B CB  1 
ATOM   4217 C  CG1 . VAL B  1  208 ? 13.168  -21.185 47.479 1.00 30.78  ? 221 VAL B CG1 1 
ATOM   4218 C  CG2 . VAL B  1  208 ? 13.595  -20.642 49.865 1.00 29.69  ? 221 VAL B CG2 1 
ATOM   4219 N  N   . ASP B  1  209 ? 13.486  -18.364 45.845 1.00 33.79  ? 222 ASP B N   1 
ATOM   4220 C  CA  . ASP B  1  209 ? 13.087  -17.965 44.509 1.00 35.73  ? 222 ASP B CA  1 
ATOM   4221 C  C   . ASP B  1  209 ? 11.806  -18.691 44.108 1.00 35.61  ? 222 ASP B C   1 
ATOM   4222 O  O   . ASP B  1  209 ? 11.640  -19.874 44.387 1.00 33.87  ? 222 ASP B O   1 
ATOM   4223 C  CB  . ASP B  1  209 ? 14.226  -18.214 43.530 1.00 37.80  ? 222 ASP B CB  1 
ATOM   4224 C  CG  . ASP B  1  209 ? 14.063  -17.564 42.168 1.00 35.71  ? 222 ASP B CG  1 
ATOM   4225 O  OD1 . ASP B  1  209 ? 13.282  -18.117 41.375 1.00 34.70  ? 222 ASP B OD1 1 
ATOM   4226 O  OD2 . ASP B  1  209 ? 14.693  -16.500 41.937 1.00 33.68  ? 222 ASP B OD2 1 
ATOM   4227 N  N   . GLY B  1  210 ? 10.919  -17.964 43.419 1.00 39.24  ? 223 GLY B N   1 
ATOM   4228 C  CA  . GLY B  1  210 ? 9.587   -18.452 43.095 1.00 40.73  ? 223 GLY B CA  1 
ATOM   4229 C  C   . GLY B  1  210 ? 9.582   -19.514 41.997 1.00 41.62  ? 223 GLY B C   1 
ATOM   4230 O  O   . GLY B  1  210 ? 8.604   -20.243 41.855 1.00 45.61  ? 223 GLY B O   1 
ATOM   4231 N  N   . ARG B  1  211 ? 10.670  -19.592 41.222 1.00 41.10  ? 224 ARG B N   1 
ATOM   4232 C  CA  . ARG B  1  211 ? 10.794  -20.602 40.186 1.00 38.71  ? 224 ARG B CA  1 
ATOM   4233 C  C   . ARG B  1  211 ? 11.152  -21.959 40.783 1.00 37.91  ? 224 ARG B C   1 
ATOM   4234 O  O   . ARG B  1  211 ? 11.036  -22.959 40.094 1.00 41.11  ? 224 ARG B O   1 
ATOM   4235 C  CB  . ARG B  1  211 ? 11.815  -20.195 39.126 1.00 38.11  ? 224 ARG B CB  1 
ATOM   4236 C  CG  . ARG B  1  211 ? 11.430  -18.937 38.365 1.00 37.71  ? 224 ARG B CG  1 
ATOM   4237 C  CD  . ARG B  1  211 ? 12.637  -18.372 37.635 1.00 40.65  ? 224 ARG B CD  1 
ATOM   4238 N  NE  . ARG B  1  211 ? 13.642  -17.849 38.565 1.00 41.64  ? 224 ARG B NE  1 
ATOM   4239 C  CZ  . ARG B  1  211 ? 14.720  -17.162 38.223 1.00 40.69  ? 224 ARG B CZ  1 
ATOM   4240 N  NH1 . ARG B  1  211 ? 14.975  -16.929 36.954 1.00 36.50  ? 224 ARG B NH1 1 
ATOM   4241 N  NH2 . ARG B  1  211 ? 15.531  -16.690 39.155 1.00 41.69  ? 224 ARG B NH2 1 
ATOM   4242 N  N   . VAL B  1  212 ? 11.546  -22.017 42.057 1.00 41.20  ? 225 VAL B N   1 
ATOM   4243 C  CA  . VAL B  1  212 ? 11.766  -23.293 42.729 1.00 43.52  ? 225 VAL B CA  1 
ATOM   4244 C  C   . VAL B  1  212 ? 10.415  -23.801 43.231 1.00 49.80  ? 225 VAL B C   1 
ATOM   4245 O  O   . VAL B  1  212 ? 9.866   -23.249 44.177 1.00 49.78  ? 225 VAL B O   1 
ATOM   4246 C  CB  . VAL B  1  212 ? 12.768  -23.137 43.894 1.00 42.00  ? 225 VAL B CB  1 
ATOM   4247 C  CG1 . VAL B  1  212 ? 13.013  -24.433 44.644 1.00 38.89  ? 225 VAL B CG1 1 
ATOM   4248 C  CG2 . VAL B  1  212 ? 14.096  -22.559 43.441 1.00 43.10  ? 225 VAL B CG2 1 
ATOM   4249 N  N   . THR B  1  213 ? 9.879   -24.862 42.616 1.00 56.02  ? 226 THR B N   1 
ATOM   4250 C  CA  . THR B  1  213 ? 8.549   -25.348 42.980 1.00 61.97  ? 226 THR B CA  1 
ATOM   4251 C  C   . THR B  1  213 ? 8.662   -26.558 43.910 1.00 61.83  ? 226 THR B C   1 
ATOM   4252 O  O   . THR B  1  213 ? 7.692   -26.933 44.558 1.00 54.40  ? 226 THR B O   1 
ATOM   4253 C  CB  . THR B  1  213 ? 7.717   -25.684 41.733 1.00 61.03  ? 226 THR B CB  1 
ATOM   4254 O  OG1 . THR B  1  213 ? 8.307   -26.830 41.127 1.00 53.42  ? 226 THR B OG1 1 
ATOM   4255 C  CG2 . THR B  1  213 ? 7.662   -24.547 40.722 1.00 60.27  ? 226 THR B CG2 1 
ATOM   4256 N  N   . THR B  1  214 ? 9.849   -27.157 43.999 1.00 67.61  ? 227 THR B N   1 
ATOM   4257 C  CA  . THR B  1  214 ? 10.000  -28.437 44.670 1.00 74.53  ? 227 THR B CA  1 
ATOM   4258 C  C   . THR B  1  214 ? 11.211  -28.407 45.608 1.00 75.74  ? 227 THR B C   1 
ATOM   4259 O  O   . THR B  1  214 ? 12.271  -27.904 45.237 1.00 87.44  ? 227 THR B O   1 
ATOM   4260 C  CB  . THR B  1  214 ? 10.090  -29.490 43.565 1.00 80.66  ? 227 THR B CB  1 
ATOM   4261 O  OG1 . THR B  1  214 ? 10.124  -30.726 44.269 1.00 85.23  ? 227 THR B OG1 1 
ATOM   4262 C  CG2 . THR B  1  214 ? 11.296  -29.331 42.651 1.00 80.63  ? 227 THR B CG2 1 
ATOM   4263 N  N   . ASP B  1  215 ? 11.039  -28.928 46.833 1.00 69.90  ? 228 ASP B N   1 
ATOM   4264 C  CA  . ASP B  1  215 ? 12.141  -29.039 47.783 1.00 76.12  ? 228 ASP B CA  1 
ATOM   4265 C  C   . ASP B  1  215 ? 12.664  -27.630 48.089 1.00 59.37  ? 228 ASP B C   1 
ATOM   4266 O  O   . ASP B  1  215 ? 13.844  -27.343 47.929 1.00 56.00  ? 228 ASP B O   1 
ATOM   4267 C  CB  . ASP B  1  215 ? 13.189  -30.023 47.262 1.00 93.24  ? 228 ASP B CB  1 
ATOM   4268 C  CG  . ASP B  1  215 ? 14.363  -30.379 48.174 1.00 104.38 ? 228 ASP B CG  1 
ATOM   4269 O  OD1 . ASP B  1  215 ? 14.120  -30.614 49.377 1.00 98.80  ? 228 ASP B OD1 1 
ATOM   4270 O  OD2 . ASP B  1  215 ? 15.520  -30.457 47.670 1.00 96.11  ? 228 ASP B OD2 1 
ATOM   4271 N  N   . ARG B  1  216 ? 11.765  -26.741 48.516 1.00 50.27  ? 229 ARG B N   1 
ATOM   4272 C  CA  . ARG B  1  216 ? 12.107  -25.346 48.735 1.00 42.56  ? 229 ARG B CA  1 
ATOM   4273 C  C   . ARG B  1  216 ? 13.001  -25.235 49.971 1.00 43.97  ? 229 ARG B C   1 
ATOM   4274 O  O   . ARG B  1  216 ? 12.685  -25.731 51.051 1.00 46.13  ? 229 ARG B O   1 
ATOM   4275 C  CB  . ARG B  1  216 ? 10.859  -24.458 48.826 1.00 41.44  ? 229 ARG B CB  1 
ATOM   4276 C  CG  . ARG B  1  216 ? 10.166  -24.248 47.487 1.00 44.17  ? 229 ARG B CG  1 
ATOM   4277 C  CD  . ARG B  1  216 ? 8.790   -23.584 47.578 1.00 43.77  ? 229 ARG B CD  1 
ATOM   4278 N  NE  . ARG B  1  216 ? 8.831   -22.192 48.035 1.00 45.27  ? 229 ARG B NE  1 
ATOM   4279 C  CZ  . ARG B  1  216 ? 9.332   -21.163 47.348 1.00 53.16  ? 229 ARG B CZ  1 
ATOM   4280 N  NH1 . ARG B  1  216 ? 9.687   -21.305 46.076 1.00 55.46  ? 229 ARG B NH1 1 
ATOM   4281 N  NH2 . ARG B  1  216 ? 9.462   -19.971 47.923 1.00 51.64  ? 229 ARG B NH2 1 
ATOM   4282 N  N   . LYS B  1  217 ? 14.140  -24.574 49.784 1.00 40.21  ? 230 LYS B N   1 
ATOM   4283 C  CA  . LYS B  1  217 ? 15.154  -24.448 50.808 1.00 39.83  ? 230 LYS B CA  1 
ATOM   4284 C  C   . LYS B  1  217 ? 16.025  -23.252 50.449 1.00 38.66  ? 230 LYS B C   1 
ATOM   4285 O  O   . LYS B  1  217 ? 16.246  -22.976 49.268 1.00 41.50  ? 230 LYS B O   1 
ATOM   4286 C  CB  . LYS B  1  217 ? 15.983  -25.733 50.864 1.00 44.20  ? 230 LYS B CB  1 
ATOM   4287 C  CG  . LYS B  1  217 ? 16.762  -26.030 49.589 1.00 44.82  ? 230 LYS B CG  1 
ATOM   4288 C  CD  . LYS B  1  217 ? 17.463  -27.384 49.547 1.00 47.88  ? 230 LYS B CD  1 
ATOM   4289 C  CE  . LYS B  1  217 ? 18.236  -27.531 48.262 1.00 54.87  ? 230 LYS B CE  1 
ATOM   4290 N  NZ  . LYS B  1  217 ? 19.123  -28.694 48.237 1.00 56.30  ? 230 LYS B NZ  1 
ATOM   4291 N  N   . LEU B  1  218 ? 16.512  -22.547 51.473 1.00 37.50  ? 231 LEU B N   1 
ATOM   4292 C  CA  . LEU B  1  218 ? 17.221  -21.295 51.268 1.00 36.92  ? 231 LEU B CA  1 
ATOM   4293 C  C   . LEU B  1  218 ? 18.717  -21.515 51.462 1.00 35.65  ? 231 LEU B C   1 
ATOM   4294 O  O   . LEU B  1  218 ? 19.122  -22.088 52.468 1.00 35.71  ? 231 LEU B O   1 
ATOM   4295 C  CB  . LEU B  1  218 ? 16.675  -20.270 52.255 1.00 34.04  ? 231 LEU B CB  1 
ATOM   4296 C  CG  . LEU B  1  218 ? 17.223  -18.850 52.103 1.00 34.33  ? 231 LEU B CG  1 
ATOM   4297 C  CD1 . LEU B  1  218 ? 16.757  -18.187 50.814 1.00 34.90  ? 231 LEU B CD1 1 
ATOM   4298 C  CD2 . LEU B  1  218 ? 16.852  -17.987 53.289 1.00 33.87  ? 231 LEU B CD2 1 
ATOM   4299 N  N   . SER B  1  219 ? 19.527  -21.049 50.501 1.00 35.34  ? 232 SER B N   1 
ATOM   4300 C  CA  . SER B  1  219 ? 20.980  -21.123 50.620 1.00 32.22  ? 232 SER B CA  1 
ATOM   4301 C  C   . SER B  1  219 ? 21.473  -20.080 51.625 1.00 32.07  ? 232 SER B C   1 
ATOM   4302 O  O   . SER B  1  219 ? 20.813  -19.071 51.865 1.00 34.09  ? 232 SER B O   1 
ATOM   4303 C  CB  . SER B  1  219 ? 21.631  -20.932 49.294 1.00 29.33  ? 232 SER B CB  1 
ATOM   4304 O  OG  . SER B  1  219 ? 21.534  -19.571 48.896 1.00 28.92  ? 232 SER B OG  1 
ATOM   4305 N  N   . MET B  1  220 ? 22.659  -20.300 52.196 1.00 32.05  ? 233 MET B N   1 
ATOM   4306 C  CA  . MET B  1  220 ? 23.203  -19.339 53.141 1.00 33.69  ? 233 MET B CA  1 
ATOM   4307 C  C   . MET B  1  220 ? 23.671  -18.066 52.428 1.00 34.41  ? 233 MET B C   1 
ATOM   4308 O  O   . MET B  1  220 ? 23.700  -16.999 53.034 1.00 36.68  ? 233 MET B O   1 
ATOM   4309 C  CB  . MET B  1  220 ? 24.348  -19.954 53.943 1.00 33.30  ? 233 MET B CB  1 
ATOM   4310 C  CG  . MET B  1  220 ? 23.941  -21.158 54.785 1.00 36.23  ? 233 MET B CG  1 
ATOM   4311 S  SD  . MET B  1  220 ? 22.604  -20.890 55.975 1.00 38.88  ? 233 MET B SD  1 
ATOM   4312 C  CE  . MET B  1  220 ? 21.203  -21.546 55.064 1.00 37.89  ? 233 MET B CE  1 
ATOM   4313 N  N   . GLU B  1  221 ? 24.025  -18.163 51.141 1.00 33.50  ? 234 GLU B N   1 
ATOM   4314 C  CA  . GLU B  1  221 ? 24.452  -17.002 50.372 1.00 35.66  ? 234 GLU B CA  1 
ATOM   4315 C  C   . GLU B  1  221 ? 23.286  -16.019 50.240 1.00 35.79  ? 234 GLU B C   1 
ATOM   4316 O  O   . GLU B  1  221 ? 23.457  -14.815 50.416 1.00 34.10  ? 234 GLU B O   1 
ATOM   4317 C  CB  . GLU B  1  221 ? 24.982  -17.381 48.985 1.00 36.84  ? 234 GLU B CB  1 
ATOM   4318 C  CG  . GLU B  1  221 ? 26.236  -18.253 48.992 1.00 41.69  ? 234 GLU B CG  1 
ATOM   4319 C  CD  . GLU B  1  221 ? 26.139  -19.755 49.297 1.00 49.14  ? 234 GLU B CD  1 
ATOM   4320 O  OE1 . GLU B  1  221 ? 25.096  -20.335 49.659 1.00 51.71  ? 234 GLU B OE1 1 
ATOM   4321 O  OE2 . GLU B  1  221 ? 27.188  -20.408 49.117 1.00 52.21  ? 234 GLU B OE2 1 
ATOM   4322 N  N   . ASP B  1  222 ? 22.095  -16.561 49.939 1.00 37.90  ? 235 ASP B N   1 
ATOM   4323 C  CA  . ASP B  1  222 ? 20.880  -15.778 49.763 1.00 37.91  ? 235 ASP B CA  1 
ATOM   4324 C  C   . ASP B  1  222 ? 20.383  -15.258 51.102 1.00 34.49  ? 235 ASP B C   1 
ATOM   4325 O  O   . ASP B  1  222 ? 19.978  -14.106 51.197 1.00 35.51  ? 235 ASP B O   1 
ATOM   4326 C  CB  . ASP B  1  222 ? 19.801  -16.566 49.034 1.00 43.18  ? 235 ASP B CB  1 
ATOM   4327 C  CG  . ASP B  1  222 ? 20.068  -16.860 47.560 1.00 47.86  ? 235 ASP B CG  1 
ATOM   4328 O  OD1 . ASP B  1  222 ? 21.033  -16.272 46.999 1.00 45.46  ? 235 ASP B OD1 1 
ATOM   4329 O  OD2 . ASP B  1  222 ? 19.339  -17.716 47.004 1.00 52.94  ? 235 ASP B OD2 1 
ATOM   4330 N  N   . ALA B  1  223 ? 20.435  -16.099 52.137 1.00 34.89  ? 236 ALA B N   1 
ATOM   4331 C  CA  . ALA B  1  223 ? 20.118  -15.648 53.485 1.00 34.82  ? 236 ALA B CA  1 
ATOM   4332 C  C   . ALA B  1  223 ? 20.993  -14.453 53.879 1.00 35.85  ? 236 ALA B C   1 
ATOM   4333 O  O   . ALA B  1  223 ? 20.479  -13.447 54.358 1.00 35.48  ? 236 ALA B O   1 
ATOM   4334 C  CB  . ALA B  1  223 ? 20.257  -16.793 54.463 1.00 33.64  ? 236 ALA B CB  1 
ATOM   4335 N  N   . ALA B  1  224 ? 22.312  -14.541 53.670 1.00 34.63  ? 237 ALA B N   1 
ATOM   4336 C  CA  . ALA B  1  224 ? 23.187  -13.451 54.062 1.00 36.34  ? 237 ALA B CA  1 
ATOM   4337 C  C   . ALA B  1  224 ? 22.847  -12.188 53.270 1.00 36.71  ? 237 ALA B C   1 
ATOM   4338 O  O   . ALA B  1  224 ? 22.860  -11.074 53.800 1.00 37.01  ? 237 ALA B O   1 
ATOM   4339 C  CB  . ALA B  1  224 ? 24.628  -13.846 53.871 1.00 38.23  ? 237 ALA B CB  1 
ATOM   4340 N  N   . SER B  1  225 ? 22.546  -12.362 51.985 1.00 34.57  ? 238 SER B N   1 
ATOM   4341 C  CA  . SER B  1  225 ? 22.293  -11.218 51.127 1.00 33.57  ? 238 SER B CA  1 
ATOM   4342 C  C   . SER B  1  225 ? 21.120  -10.395 51.666 1.00 30.63  ? 238 SER B C   1 
ATOM   4343 O  O   . SER B  1  225 ? 21.180  -9.164  51.718 1.00 29.75  ? 238 SER B O   1 
ATOM   4344 C  CB  . SER B  1  225 ? 22.066  -11.657 49.703 1.00 34.00  ? 238 SER B CB  1 
ATOM   4345 O  OG  . SER B  1  225 ? 21.830  -10.543 48.857 1.00 33.09  ? 238 SER B OG  1 
ATOM   4346 N  N   . ILE B  1  226 ? 20.061  -11.089 52.092 1.00 30.59  ? 239 ILE B N   1 
ATOM   4347 C  CA  . ILE B  1  226 ? 18.834  -10.440 52.531 1.00 31.95  ? 239 ILE B CA  1 
ATOM   4348 C  C   . ILE B  1  226 ? 18.984  -9.987  53.984 1.00 31.71  ? 239 ILE B C   1 
ATOM   4349 O  O   . ILE B  1  226 ? 18.809  -8.803  54.277 1.00 33.78  ? 239 ILE B O   1 
ATOM   4350 C  CB  . ILE B  1  226 ? 17.636  -11.381 52.314 1.00 32.73  ? 239 ILE B CB  1 
ATOM   4351 C  CG1 . ILE B  1  226 ? 17.334  -11.546 50.835 1.00 33.88  ? 239 ILE B CG1 1 
ATOM   4352 C  CG2 . ILE B  1  226 ? 16.394  -10.912 53.065 1.00 35.56  ? 239 ILE B CG2 1 
ATOM   4353 C  CD1 . ILE B  1  226 ? 16.596  -12.832 50.514 1.00 34.41  ? 239 ILE B CD1 1 
ATOM   4354 N  N   . PHE B  1  227 ? 19.323  -10.921 54.884 1.00 31.71  ? 240 PHE B N   1 
ATOM   4355 C  CA  . PHE B  1  227 ? 19.356  -10.633 56.314 1.00 33.71  ? 240 PHE B CA  1 
ATOM   4356 C  C   . PHE B  1  227 ? 20.426  -9.599  56.678 1.00 34.07  ? 240 PHE B C   1 
ATOM   4357 O  O   . PHE B  1  227 ? 20.210  -8.769  57.563 1.00 35.66  ? 240 PHE B O   1 
ATOM   4358 C  CB  . PHE B  1  227 ? 19.619  -11.889 57.136 1.00 31.54  ? 240 PHE B CB  1 
ATOM   4359 C  CG  . PHE B  1  227 ? 18.424  -12.798 57.336 1.00 31.31  ? 240 PHE B CG  1 
ATOM   4360 C  CD1 . PHE B  1  227 ? 17.458  -12.487 58.277 1.00 31.37  ? 240 PHE B CD1 1 
ATOM   4361 C  CD2 . PHE B  1  227 ? 18.304  -13.991 56.646 1.00 35.13  ? 240 PHE B CD2 1 
ATOM   4362 C  CE1 . PHE B  1  227 ? 16.387  -13.334 58.506 1.00 30.78  ? 240 PHE B CE1 1 
ATOM   4363 C  CE2 . PHE B  1  227 ? 17.229  -14.836 56.870 1.00 37.91  ? 240 PHE B CE2 1 
ATOM   4364 C  CZ  . PHE B  1  227 ? 16.270  -14.505 57.802 1.00 34.29  ? 240 PHE B CZ  1 
ATOM   4365 N  N   . ARG B  1  228 ? 21.589  -9.651  56.022 1.00 33.35  ? 241 ARG B N   1 
ATOM   4366 C  CA  . ARG B  1  228 ? 22.692  -8.769  56.380 1.00 33.60  ? 241 ARG B CA  1 
ATOM   4367 C  C   . ARG B  1  228 ? 22.760  -7.552  55.464 1.00 31.97  ? 241 ARG B C   1 
ATOM   4368 O  O   . ARG B  1  228 ? 22.894  -6.440  55.949 1.00 28.28  ? 241 ARG B O   1 
ATOM   4369 C  CB  . ARG B  1  228 ? 24.036  -9.506  56.365 1.00 35.42  ? 241 ARG B CB  1 
ATOM   4370 C  CG  . ARG B  1  228 ? 25.210  -8.608  56.710 1.00 35.77  ? 241 ARG B CG  1 
ATOM   4371 C  CD  . ARG B  1  228 ? 26.512  -9.350  56.990 1.00 34.41  ? 241 ARG B CD  1 
ATOM   4372 N  NE  . ARG B  1  228 ? 27.044  -10.053 55.824 1.00 34.59  ? 241 ARG B NE  1 
ATOM   4373 C  CZ  . ARG B  1  228 ? 27.382  -11.340 55.775 1.00 37.69  ? 241 ARG B CZ  1 
ATOM   4374 N  NH1 . ARG B  1  228 ? 27.252  -12.142 56.832 1.00 39.68  ? 241 ARG B NH1 1 
ATOM   4375 N  NH2 . ARG B  1  228 ? 27.865  -11.847 54.645 1.00 35.74  ? 241 ARG B NH2 1 
ATOM   4376 N  N   . ASP B  1  229 ? 22.699  -7.755  54.144 1.00 33.43  ? 242 ASP B N   1 
ATOM   4377 C  CA  . ASP B  1  229 ? 23.041  -6.680  53.223 1.00 35.05  ? 242 ASP B CA  1 
ATOM   4378 C  C   . ASP B  1  229 ? 21.816  -5.953  52.672 1.00 37.28  ? 242 ASP B C   1 
ATOM   4379 O  O   . ASP B  1  229 ? 21.984  -4.929  52.001 1.00 35.98  ? 242 ASP B O   1 
ATOM   4380 C  CB  . ASP B  1  229 ? 23.888  -7.170  52.066 1.00 35.43  ? 242 ASP B CB  1 
ATOM   4381 C  CG  . ASP B  1  229 ? 25.264  -7.702  52.414 1.00 36.77  ? 242 ASP B CG  1 
ATOM   4382 O  OD1 . ASP B  1  229 ? 25.901  -7.174  53.361 1.00 41.18  ? 242 ASP B OD1 1 
ATOM   4383 O  OD2 . ASP B  1  229 ? 25.708  -8.587  51.673 1.00 39.55  ? 242 ASP B OD2 1 
ATOM   4384 N  N   . MET B  1  230 ? 20.607  -6.488  52.931 1.00 39.07  ? 243 MET B N   1 
ATOM   4385 C  CA  A MET B  1  230 ? 19.361  -5.872  52.492 0.50 38.63  ? 243 MET B CA  1 
ATOM   4386 C  CA  B MET B  1  230 ? 19.367  -5.865  52.489 0.50 38.94  ? 243 MET B CA  1 
ATOM   4387 C  C   . MET B  1  230 ? 19.283  -5.876  50.964 1.00 38.73  ? 243 MET B C   1 
ATOM   4388 O  O   . MET B  1  230 ? 18.833  -4.901  50.363 1.00 35.41  ? 243 MET B O   1 
ATOM   4389 C  CB  A MET B  1  230 ? 19.237  -4.419  52.978 0.50 37.72  ? 243 MET B CB  1 
ATOM   4390 C  CB  B MET B  1  230 ? 19.276  -4.413  52.975 0.50 38.42  ? 243 MET B CB  1 
ATOM   4391 C  CG  A MET B  1  230 ? 19.402  -4.245  54.472 0.50 37.23  ? 243 MET B CG  1 
ATOM   4392 C  CG  B MET B  1  230 ? 19.320  -4.292  54.475 0.50 38.25  ? 243 MET B CG  1 
ATOM   4393 S  SD  A MET B  1  230 ? 19.744  -2.535  54.932 0.50 36.13  ? 243 MET B SD  1 
ATOM   4394 S  SD  B MET B  1  230 ? 19.164  -2.587  55.033 0.50 37.44  ? 243 MET B SD  1 
ATOM   4395 C  CE  A MET B  1  230 ? 19.993  -2.785  56.699 0.50 37.26  ? 243 MET B CE  1 
ATOM   4396 C  CE  B MET B  1  230 ? 20.814  -1.948  54.719 0.50 37.40  ? 243 MET B CE  1 
ATOM   4397 N  N   . ARG B  1  231 ? 19.713  -6.991  50.355 1.00 37.10  ? 244 ARG B N   1 
ATOM   4398 C  CA  . ARG B  1  231 ? 19.867  -7.082  48.913 1.00 34.06  ? 244 ARG B CA  1 
ATOM   4399 C  C   . ARG B  1  231 ? 19.174  -8.341  48.407 1.00 32.81  ? 244 ARG B C   1 
ATOM   4400 O  O   . ARG B  1  231 ? 19.397  -9.425  48.939 1.00 32.48  ? 244 ARG B O   1 
ATOM   4401 C  CB  . ARG B  1  231 ? 21.360  -7.115  48.588 1.00 35.97  ? 244 ARG B CB  1 
ATOM   4402 C  CG  . ARG B  1  231 ? 21.688  -6.903  47.112 1.00 40.06  ? 244 ARG B CG  1 
ATOM   4403 C  CD  . ARG B  1  231 ? 23.194  -6.938  46.805 1.00 39.92  ? 244 ARG B CD  1 
ATOM   4404 N  NE  . ARG B  1  231 ? 23.742  -8.280  47.045 1.00 48.19  ? 244 ARG B NE  1 
ATOM   4405 C  CZ  . ARG B  1  231 ? 23.533  -9.385  46.293 1.00 61.05  ? 244 ARG B CZ  1 
ATOM   4406 N  NH1 . ARG B  1  231 ? 22.971  -9.294  45.095 1.00 78.95  ? 244 ARG B NH1 1 
ATOM   4407 N  NH2 . ARG B  1  231 ? 23.893  -10.594 46.710 1.00 55.70  ? 244 ARG B NH2 1 
ATOM   4408 N  N   . PHE B  1  232 ? 18.329  -8.195  47.376 1.00 31.10  ? 245 PHE B N   1 
ATOM   4409 C  CA  . PHE B  1  232 ? 17.793  -9.353  46.690 1.00 30.15  ? 245 PHE B CA  1 
ATOM   4410 C  C   . PHE B  1  232 ? 18.932  -10.143 46.061 1.00 31.67  ? 245 PHE B C   1 
ATOM   4411 O  O   . PHE B  1  232 ? 19.877  -9.555  45.532 1.00 33.86  ? 245 PHE B O   1 
ATOM   4412 C  CB  . PHE B  1  232 ? 16.853  -8.989  45.544 1.00 31.68  ? 245 PHE B CB  1 
ATOM   4413 C  CG  . PHE B  1  232 ? 15.489  -8.465  45.968 1.00 32.57  ? 245 PHE B CG  1 
ATOM   4414 C  CD1 . PHE B  1  232 ? 14.594  -9.288  46.634 1.00 33.82  ? 245 PHE B CD1 1 
ATOM   4415 C  CD2 . PHE B  1  232 ? 15.091  -7.170  45.657 1.00 33.36  ? 245 PHE B CD2 1 
ATOM   4416 C  CE1 . PHE B  1  232 ? 13.345  -8.818  47.008 1.00 36.92  ? 245 PHE B CE1 1 
ATOM   4417 C  CE2 . PHE B  1  232 ? 13.834  -6.710  46.009 1.00 35.19  ? 245 PHE B CE2 1 
ATOM   4418 C  CZ  . PHE B  1  232 ? 12.964  -7.532  46.691 1.00 35.77  ? 245 PHE B CZ  1 
ATOM   4419 N  N   . PRO B  1  233 ? 18.881  -11.492 46.083 1.00 27.55  ? 246 PRO B N   1 
ATOM   4420 C  CA  . PRO B  1  233 ? 19.743  -12.289 45.213 1.00 27.74  ? 246 PRO B CA  1 
ATOM   4421 C  C   . PRO B  1  233 ? 19.683  -11.806 43.767 1.00 31.04  ? 246 PRO B C   1 
ATOM   4422 O  O   . PRO B  1  233 ? 18.683  -11.221 43.338 1.00 33.33  ? 246 PRO B O   1 
ATOM   4423 C  CB  . PRO B  1  233 ? 19.194  -13.704 45.376 1.00 26.83  ? 246 PRO B CB  1 
ATOM   4424 C  CG  . PRO B  1  233 ? 18.541  -13.719 46.742 1.00 27.08  ? 246 PRO B CG  1 
ATOM   4425 C  CD  . PRO B  1  233 ? 18.038  -12.301 46.970 1.00 26.91  ? 246 PRO B CD  1 
ATOM   4426 N  N   . ASP B  1  234 ? 20.764  -12.052 43.021 1.00 33.48  ? 247 ASP B N   1 
ATOM   4427 C  CA  . ASP B  1  234 ? 20.789  -11.761 41.593 1.00 38.72  ? 247 ASP B CA  1 
ATOM   4428 C  C   . ASP B  1  234 ? 19.629  -12.501 40.912 1.00 38.99  ? 247 ASP B C   1 
ATOM   4429 O  O   . ASP B  1  234 ? 19.348  -13.661 41.212 1.00 39.15  ? 247 ASP B O   1 
ATOM   4430 C  CB  . ASP B  1  234 ? 22.125  -12.141 40.964 1.00 40.89  ? 247 ASP B CB  1 
ATOM   4431 C  CG  . ASP B  1  234 ? 23.359  -11.326 41.337 1.00 42.00  ? 247 ASP B CG  1 
ATOM   4432 O  OD1 . ASP B  1  234 ? 23.286  -10.413 42.192 1.00 44.13  ? 247 ASP B OD1 1 
ATOM   4433 O  OD2 . ASP B  1  234 ? 24.402  -11.607 40.736 1.00 48.82  ? 247 ASP B OD2 1 
ATOM   4434 N  N   . ASP B  1  235 ? 18.914  -11.796 40.035 1.00 40.06  ? 248 ASP B N   1 
ATOM   4435 C  CA  . ASP B  1  235 ? 17.866  -12.396 39.227 1.00 41.55  ? 248 ASP B CA  1 
ATOM   4436 C  C   . ASP B  1  235 ? 16.733  -12.967 40.091 1.00 38.78  ? 248 ASP B C   1 
ATOM   4437 O  O   . ASP B  1  235 ? 16.093  -13.954 39.717 1.00 34.30  ? 248 ASP B O   1 
ATOM   4438 C  CB  . ASP B  1  235 ? 18.449  -13.449 38.294 1.00 40.77  ? 248 ASP B CB  1 
ATOM   4439 C  CG  . ASP B  1  235 ? 17.538  -13.800 37.125 1.00 41.61  ? 248 ASP B CG  1 
ATOM   4440 O  OD1 . ASP B  1  235 ? 17.123  -12.851 36.406 1.00 40.52  ? 248 ASP B OD1 1 
ATOM   4441 O  OD2 . ASP B  1  235 ? 17.226  -15.000 36.965 1.00 37.47  ? 248 ASP B OD2 1 
ATOM   4442 N  N   . PHE B  1  236 ? 16.462  -12.343 41.243 1.00 36.98  ? 249 PHE B N   1 
ATOM   4443 C  CA  . PHE B  1  236 ? 15.489  -12.902 42.168 1.00 33.99  ? 249 PHE B CA  1 
ATOM   4444 C  C   . PHE B  1  236 ? 14.072  -12.749 41.623 1.00 32.30  ? 249 PHE B C   1 
ATOM   4445 O  O   . PHE B  1  236 ? 13.653  -11.663 41.226 1.00 28.80  ? 249 PHE B O   1 
ATOM   4446 C  CB  . PHE B  1  236 ? 15.557  -12.226 43.532 1.00 34.26  ? 249 PHE B CB  1 
ATOM   4447 C  CG  . PHE B  1  236 ? 14.588  -12.811 44.543 1.00 33.46  ? 249 PHE B CG  1 
ATOM   4448 C  CD1 . PHE B  1  236 ? 14.852  -14.037 45.136 1.00 33.80  ? 249 PHE B CD1 1 
ATOM   4449 C  CD2 . PHE B  1  236 ? 13.458  -12.111 44.940 1.00 34.68  ? 249 PHE B CD2 1 
ATOM   4450 C  CE1 . PHE B  1  236 ? 13.991  -14.571 46.077 1.00 34.47  ? 249 PHE B CE1 1 
ATOM   4451 C  CE2 . PHE B  1  236 ? 12.594  -12.647 45.878 1.00 35.62  ? 249 PHE B CE2 1 
ATOM   4452 C  CZ  . PHE B  1  236 ? 12.870  -13.869 46.455 1.00 35.79  ? 249 PHE B CZ  1 
ATOM   4453 N  N   . HIS B  1  237 ? 13.349  -13.871 41.620 1.00 34.21  ? 250 HIS B N   1 
ATOM   4454 C  CA  . HIS B  1  237 ? 11.943  -13.920 41.255 1.00 33.74  ? 250 HIS B CA  1 
ATOM   4455 C  C   . HIS B  1  237 ? 11.136  -14.234 42.514 1.00 32.58  ? 250 HIS B C   1 
ATOM   4456 O  O   . HIS B  1  237 ? 11.420  -15.210 43.212 1.00 26.14  ? 250 HIS B O   1 
ATOM   4457 C  CB  . HIS B  1  237 ? 11.683  -14.981 40.175 1.00 34.92  ? 250 HIS B CB  1 
ATOM   4458 C  CG  . HIS B  1  237 ? 12.201  -14.632 38.822 1.00 38.51  ? 250 HIS B CG  1 
ATOM   4459 N  ND1 . HIS B  1  237 ? 13.474  -14.140 38.606 1.00 43.18  ? 250 HIS B ND1 1 
ATOM   4460 C  CD2 . HIS B  1  237 ? 11.623  -14.712 37.622 1.00 37.40  ? 250 HIS B CD2 1 
ATOM   4461 C  CE1 . HIS B  1  237 ? 13.639  -13.915 37.310 1.00 42.98  ? 250 HIS B CE1 1 
ATOM   4462 N  NE2 . HIS B  1  237 ? 12.521  -14.248 36.696 1.00 42.23  ? 250 HIS B NE2 1 
ATOM   4463 N  N   . ARG B  1  238 ? 10.117  -13.408 42.780 1.00 34.45  ? 251 ARG B N   1 
ATOM   4464 C  CA  . ARG B  1  238 ? 9.247   -13.594 43.929 1.00 35.98  ? 251 ARG B CA  1 
ATOM   4465 C  C   . ARG B  1  238 ? 8.418   -14.873 43.799 1.00 35.96  ? 251 ARG B C   1 
ATOM   4466 O  O   . ARG B  1  238 ? 8.308   -15.445 42.715 1.00 39.79  ? 251 ARG B O   1 
ATOM   4467 C  CB  . ARG B  1  238 ? 8.280   -12.418 44.066 1.00 36.39  ? 251 ARG B CB  1 
ATOM   4468 C  CG  . ARG B  1  238 ? 7.207   -12.382 42.989 1.00 37.86  ? 251 ARG B CG  1 
ATOM   4469 C  CD  . ARG B  1  238 ? 6.305   -11.167 43.084 1.00 38.62  ? 251 ARG B CD  1 
ATOM   4470 N  NE  . ARG B  1  238 ? 5.110   -11.401 42.264 1.00 42.63  ? 251 ARG B NE  1 
ATOM   4471 C  CZ  . ARG B  1  238 ? 4.166   -10.516 41.989 1.00 41.75  ? 251 ARG B CZ  1 
ATOM   4472 N  NH1 . ARG B  1  238 ? 4.171   -9.338  42.579 1.00 43.87  ? 251 ARG B NH1 1 
ATOM   4473 N  NH2 . ARG B  1  238 ? 3.223   -10.823 41.121 1.00 43.42  ? 251 ARG B NH2 1 
ATOM   4474 N  N   . SER B  1  239 ? 7.827   -15.278 44.933 1.00 34.66  ? 252 SER B N   1 
ATOM   4475 C  CA  . SER B  1  239 ? 6.912   -16.406 45.038 1.00 37.55  ? 252 SER B CA  1 
ATOM   4476 C  C   . SER B  1  239 ? 5.861   -16.373 43.926 1.00 36.65  ? 252 SER B C   1 
ATOM   4477 O  O   . SER B  1  239 ? 5.394   -15.309 43.536 1.00 34.47  ? 252 SER B O   1 
ATOM   4478 C  CB  . SER B  1  239 ? 6.260   -16.403 46.399 1.00 38.15  ? 252 SER B CB  1 
ATOM   4479 O  OG  . SER B  1  239 ? 5.265   -17.410 46.503 1.00 36.23  ? 252 SER B OG  1 
ATOM   4480 N  N   . ALA B  1  240 ? 5.499   -17.553 43.412 1.00 38.47  ? 253 ALA B N   1 
ATOM   4481 C  CA  . ALA B  1  240 ? 4.598   -17.644 42.267 1.00 44.09  ? 253 ALA B CA  1 
ATOM   4482 C  C   . ALA B  1  240 ? 3.145   -17.477 42.704 1.00 44.90  ? 253 ALA B C   1 
ATOM   4483 O  O   . ALA B  1  240 ? 2.277   -17.305 41.860 1.00 46.48  ? 253 ALA B O   1 
ATOM   4484 C  CB  . ALA B  1  240 ? 4.782   -18.970 41.569 1.00 44.12  ? 253 ALA B CB  1 
ATOM   4485 N  N   . VAL B  1  241 ? 2.905   -17.593 44.017 1.00 41.19  ? 254 VAL B N   1 
ATOM   4486 C  CA  . VAL B  1  241 ? 1.602   -17.384 44.609 1.00 42.43  ? 254 VAL B CA  1 
ATOM   4487 C  C   . VAL B  1  241 ? 1.753   -16.456 45.807 1.00 44.77  ? 254 VAL B C   1 
ATOM   4488 O  O   . VAL B  1  241 ? 2.786   -16.452 46.464 1.00 51.21  ? 254 VAL B O   1 
ATOM   4489 C  CB  . VAL B  1  241 ? 0.977   -18.720 45.051 1.00 43.50  ? 254 VAL B CB  1 
ATOM   4490 C  CG1 . VAL B  1  241 ? 0.729   -19.648 43.862 1.00 41.18  ? 254 VAL B CG1 1 
ATOM   4491 C  CG2 . VAL B  1  241 ? 1.799   -19.423 46.129 1.00 41.45  ? 254 VAL B CG2 1 
ATOM   4492 N  N   . PRO B  1  242 ? 0.712   -15.672 46.162 1.00 46.56  ? 255 PRO B N   1 
ATOM   4493 C  CA  . PRO B  1  242 ? 0.716   -14.917 47.413 1.00 44.19  ? 255 PRO B CA  1 
ATOM   4494 C  C   . PRO B  1  242 ? 0.973   -15.885 48.563 1.00 44.84  ? 255 PRO B C   1 
ATOM   4495 O  O   . PRO B  1  242 ? 0.420   -16.983 48.576 1.00 44.28  ? 255 PRO B O   1 
ATOM   4496 C  CB  . PRO B  1  242 ? -0.678  -14.304 47.453 1.00 41.62  ? 255 PRO B CB  1 
ATOM   4497 C  CG  . PRO B  1  242 ? -1.065  -14.197 46.004 1.00 41.70  ? 255 PRO B CG  1 
ATOM   4498 C  CD  . PRO B  1  242 ? -0.519  -15.470 45.381 1.00 43.13  ? 255 PRO B CD  1 
ATOM   4499 N  N   . ALA B  1  243 ? 1.850   -15.498 49.494 1.00 43.31  ? 256 ALA B N   1 
ATOM   4500 C  CA  . ALA B  1  243 ? 2.195   -16.386 50.594 1.00 41.05  ? 256 ALA B CA  1 
ATOM   4501 C  C   . ALA B  1  243 ? 2.491   -15.590 51.857 1.00 34.87  ? 256 ALA B C   1 
ATOM   4502 O  O   . ALA B  1  243 ? 2.618   -14.372 51.824 1.00 32.85  ? 256 ALA B O   1 
ATOM   4503 C  CB  . ALA B  1  243 ? 3.382   -17.249 50.213 1.00 43.46  ? 256 ALA B CB  1 
ATOM   4504 N  N   . SER B  1  244 ? 2.606   -16.319 52.962 1.00 35.45  ? 257 SER B N   1 
ATOM   4505 C  CA  . SER B  1  244 ? 2.961   -15.753 54.252 1.00 39.98  ? 257 SER B CA  1 
ATOM   4506 C  C   . SER B  1  244 ? 3.501   -16.860 55.155 1.00 38.82  ? 257 SER B C   1 
ATOM   4507 O  O   . SER B  1  244 ? 4.652   -17.261 55.002 1.00 38.57  ? 257 SER B O   1 
ATOM   4508 C  CB  . SER B  1  244 ? 1.790   -15.036 54.872 1.00 39.09  ? 257 SER B CB  1 
ATOM   4509 O  OG  . SER B  1  244 ? 0.673   -15.904 54.903 1.00 38.74  ? 257 SER B OG  1 
ATOM   4510 N  N   . ASN B  1  245 ? 2.645   -17.399 56.032 1.00 38.86  ? 258 ASN B N   1 
ATOM   4511 C  CA  . ASN B  1  245 ? 3.109   -18.170 57.176 1.00 41.70  ? 258 ASN B CA  1 
ATOM   4512 C  C   . ASN B  1  245 ? 2.747   -19.652 57.059 1.00 37.78  ? 258 ASN B C   1 
ATOM   4513 O  O   . ASN B  1  245 ? 2.586   -20.327 58.074 1.00 36.31  ? 258 ASN B O   1 
ATOM   4514 C  CB  . ASN B  1  245 ? 2.588   -17.580 58.487 1.00 45.63  ? 258 ASN B CB  1 
ATOM   4515 C  CG  . ASN B  1  245 ? 1.094   -17.724 58.640 1.00 47.99  ? 258 ASN B CG  1 
ATOM   4516 O  OD1 . ASN B  1  245 ? 0.378   -17.889 57.649 1.00 44.33  ? 258 ASN B OD1 1 
ATOM   4517 N  ND2 . ASN B  1  245 ? 0.605   -17.650 59.871 1.00 52.40  ? 258 ASN B ND2 1 
ATOM   4518 N  N   . GLU B  1  246 ? 2.662   -20.168 55.832 1.00 39.15  ? 259 GLU B N   1 
ATOM   4519 C  CA  . GLU B  1  246 ? 2.440   -21.591 55.610 1.00 42.83  ? 259 GLU B CA  1 
ATOM   4520 C  C   . GLU B  1  246 ? 3.578   -22.383 56.251 1.00 43.89  ? 259 GLU B C   1 
ATOM   4521 O  O   . GLU B  1  246 ? 4.750   -22.106 55.983 1.00 47.92  ? 259 GLU B O   1 
ATOM   4522 C  CB  . GLU B  1  246 ? 2.382   -21.928 54.115 1.00 44.01  ? 259 GLU B CB  1 
ATOM   4523 C  CG  . GLU B  1  246 ? 1.205   -21.315 53.359 1.00 46.00  ? 259 GLU B CG  1 
ATOM   4524 C  CD  . GLU B  1  246 ? 1.261   -19.825 53.038 1.00 50.49  ? 259 GLU B CD  1 
ATOM   4525 O  OE1 . GLU B  1  246 ? 2.325   -19.205 53.299 1.00 45.30  ? 259 GLU B OE1 1 
ATOM   4526 O  OE2 . GLU B  1  246 ? 0.230   -19.266 52.579 1.00 50.40  ? 259 GLU B OE2 1 
ATOM   4527 N  N   . GLY B  1  247 ? 3.221   -23.346 57.111 1.00 40.55  ? 260 GLY B N   1 
ATOM   4528 C  CA  . GLY B  1  247 ? 4.184   -24.227 57.750 1.00 35.93  ? 260 GLY B CA  1 
ATOM   4529 C  C   . GLY B  1  247 ? 4.438   -23.864 59.212 1.00 37.57  ? 260 GLY B C   1 
ATOM   4530 O  O   . GLY B  1  247 ? 5.089   -24.625 59.925 1.00 41.73  ? 260 GLY B O   1 
ATOM   4531 N  N   . ALA B  1  248 ? 3.920   -22.718 59.670 1.00 35.82  ? 261 ALA B N   1 
ATOM   4532 C  CA  . ALA B  1  248 ? 4.169   -22.273 61.033 1.00 36.20  ? 261 ALA B CA  1 
ATOM   4533 C  C   . ALA B  1  248 ? 3.603   -23.257 62.066 1.00 39.02  ? 261 ALA B C   1 
ATOM   4534 O  O   . ALA B  1  248 ? 4.196   -23.434 63.133 1.00 35.50  ? 261 ALA B O   1 
ATOM   4535 C  CB  . ALA B  1  248 ? 3.611   -20.886 61.225 1.00 36.61  ? 261 ALA B CB  1 
ATOM   4536 N  N   . ASP B  1  249 ? 2.464   -23.893 61.753 1.00 41.71  ? 262 ASP B N   1 
ATOM   4537 C  CA  . ASP B  1  249 ? 1.902   -24.901 62.642 1.00 49.78  ? 262 ASP B CA  1 
ATOM   4538 C  C   . ASP B  1  249 ? 2.878   -26.077 62.814 1.00 48.64  ? 262 ASP B C   1 
ATOM   4539 O  O   . ASP B  1  249 ? 2.979   -26.615 63.903 1.00 46.54  ? 262 ASP B O   1 
ATOM   4540 C  CB  . ASP B  1  249 ? 0.505   -25.312 62.189 1.00 57.64  ? 262 ASP B CB  1 
ATOM   4541 C  CG  . ASP B  1  249 ? 0.413   -25.926 60.794 1.00 69.27  ? 262 ASP B CG  1 
ATOM   4542 O  OD1 . ASP B  1  249 ? 1.438   -25.905 60.045 1.00 69.14  ? 262 ASP B OD1 1 
ATOM   4543 O  OD2 . ASP B  1  249 ? -0.692  -26.421 60.455 1.00 68.99  ? 262 ASP B OD2 1 
ATOM   4544 N  N   . GLN B  1  250 ? 3.604   -26.481 61.760 1.00 46.00  ? 263 GLN B N   1 
ATOM   4545 C  CA  . GLN B  1  250 ? 4.545   -27.593 61.858 1.00 45.36  ? 263 GLN B CA  1 
ATOM   4546 C  C   . GLN B  1  250 ? 5.767   -27.232 62.702 1.00 42.40  ? 263 GLN B C   1 
ATOM   4547 O  O   . GLN B  1  250 ? 6.321   -28.097 63.375 1.00 39.14  ? 263 GLN B O   1 
ATOM   4548 C  CB  . GLN B  1  250 ? 4.991   -28.061 60.476 1.00 45.68  ? 263 GLN B CB  1 
ATOM   4549 C  CG  . GLN B  1  250 ? 3.868   -28.721 59.681 1.00 50.39  ? 263 GLN B CG  1 
ATOM   4550 C  CD  . GLN B  1  250 ? 4.273   -29.051 58.262 1.00 54.38  ? 263 GLN B CD  1 
ATOM   4551 O  OE1 . GLN B  1  250 ? 5.258   -29.759 58.044 1.00 56.25  ? 263 GLN B OE1 1 
ATOM   4552 N  NE2 . GLN B  1  250 ? 3.571   -28.502 57.278 1.00 57.84  ? 263 GLN B NE2 1 
ATOM   4553 N  N   . VAL B  1  251 ? 6.185   -25.961 62.657 1.00 38.68  ? 264 VAL B N   1 
ATOM   4554 C  CA  . VAL B  1  251 ? 7.326   -25.501 63.425 1.00 37.04  ? 264 VAL B CA  1 
ATOM   4555 C  C   . VAL B  1  251 ? 7.018   -25.617 64.915 1.00 42.04  ? 264 VAL B C   1 
ATOM   4556 O  O   . VAL B  1  251 ? 7.890   -25.979 65.702 1.00 47.20  ? 264 VAL B O   1 
ATOM   4557 C  CB  . VAL B  1  251 ? 7.698   -24.059 63.028 1.00 35.01  ? 264 VAL B CB  1 
ATOM   4558 C  CG1 . VAL B  1  251 ? 8.702   -23.414 63.972 1.00 32.39  ? 264 VAL B CG1 1 
ATOM   4559 C  CG2 . VAL B  1  251 ? 8.215   -23.991 61.600 1.00 37.12  ? 264 VAL B CG2 1 
ATOM   4560 N  N   . LEU B  1  252 ? 5.785   -25.267 65.301 1.00 45.43  ? 265 LEU B N   1 
ATOM   4561 C  CA  . LEU B  1  252 ? 5.350   -25.366 66.685 1.00 45.95  ? 265 LEU B CA  1 
ATOM   4562 C  C   . LEU B  1  252 ? 5.222   -26.836 67.093 1.00 46.85  ? 265 LEU B C   1 
ATOM   4563 O  O   . LEU B  1  252 ? 5.526   -27.185 68.228 1.00 49.30  ? 265 LEU B O   1 
ATOM   4564 C  CB  . LEU B  1  252 ? 4.022   -24.634 66.864 1.00 45.05  ? 265 LEU B CB  1 
ATOM   4565 C  CG  . LEU B  1  252 ? 3.448   -24.615 68.284 1.00 46.60  ? 265 LEU B CG  1 
ATOM   4566 C  CD1 . LEU B  1  252 ? 4.295   -23.786 69.227 1.00 47.09  ? 265 LEU B CD1 1 
ATOM   4567 C  CD2 . LEU B  1  252 ? 2.022   -24.093 68.282 1.00 46.93  ? 265 LEU B CD2 1 
ATOM   4568 N  N   . ALA B  1  253 ? 4.760   -27.686 66.169 1.00 42.83  ? 266 ALA B N   1 
ATOM   4569 C  CA  . ALA B  1  253 ? 4.513   -29.087 66.466 1.00 44.32  ? 266 ALA B CA  1 
ATOM   4570 C  C   . ALA B  1  253 ? 5.815   -29.814 66.803 1.00 49.29  ? 266 ALA B C   1 
ATOM   4571 O  O   . ALA B  1  253 ? 5.814   -30.715 67.636 1.00 55.35  ? 266 ALA B O   1 
ATOM   4572 C  CB  . ALA B  1  253 ? 3.788   -29.749 65.313 1.00 40.48  ? 266 ALA B CB  1 
ATOM   4573 N  N   . ALA B  1  254 ? 6.924   -29.408 66.172 1.00 53.43  ? 267 ALA B N   1 
ATOM   4574 C  CA  . ALA B  1  254 ? 8.221   -30.043 66.365 1.00 48.12  ? 267 ALA B CA  1 
ATOM   4575 C  C   . ALA B  1  254 ? 8.714   -29.913 67.811 1.00 48.69  ? 267 ALA B C   1 
ATOM   4576 O  O   . ALA B  1  254 ? 9.440   -30.780 68.287 1.00 46.90  ? 267 ALA B O   1 
ATOM   4577 C  CB  . ALA B  1  254 ? 9.218   -29.448 65.397 1.00 42.72  ? 267 ALA B CB  1 
ATOM   4578 N  N   . HIS B  1  255 ? 8.361   -28.810 68.489 1.00 49.31  ? 268 HIS B N   1 
ATOM   4579 C  CA  . HIS B  1  255 ? 8.704   -28.598 69.892 1.00 53.70  ? 268 HIS B CA  1 
ATOM   4580 C  C   . HIS B  1  255 ? 7.609   -27.765 70.560 1.00 56.36  ? 268 HIS B C   1 
ATOM   4581 O  O   . HIS B  1  255 ? 7.770   -26.553 70.742 1.00 51.14  ? 268 HIS B O   1 
ATOM   4582 C  CB  . HIS B  1  255 ? 10.076  -27.930 70.059 1.00 53.30  ? 268 HIS B CB  1 
ATOM   4583 C  CG  . HIS B  1  255 ? 11.228  -28.770 69.627 1.00 52.72  ? 268 HIS B CG  1 
ATOM   4584 N  ND1 . HIS B  1  255 ? 11.753  -29.758 70.431 1.00 54.83  ? 268 HIS B ND1 1 
ATOM   4585 C  CD2 . HIS B  1  255 ? 11.935  -28.798 68.484 1.00 54.41  ? 268 HIS B CD2 1 
ATOM   4586 C  CE1 . HIS B  1  255 ? 12.745  -30.359 69.786 1.00 59.90  ? 268 HIS B CE1 1 
ATOM   4587 N  NE2 . HIS B  1  255 ? 12.868  -29.797 68.599 1.00 59.12  ? 268 HIS B NE2 1 
ATOM   4588 N  N   . PRO B  1  256 ? 6.470   -28.404 70.939 1.00 50.84  ? 269 PRO B N   1 
ATOM   4589 C  CA  . PRO B  1  256 ? 5.337   -27.707 71.543 1.00 48.19  ? 269 PRO B CA  1 
ATOM   4590 C  C   . PRO B  1  256 ? 5.785   -26.766 72.652 1.00 46.30  ? 269 PRO B C   1 
ATOM   4591 O  O   . PRO B  1  256 ? 6.659   -27.105 73.441 1.00 41.33  ? 269 PRO B O   1 
ATOM   4592 C  CB  . PRO B  1  256 ? 4.470   -28.846 72.069 1.00 47.61  ? 269 PRO B CB  1 
ATOM   4593 C  CG  . PRO B  1  256 ? 4.735   -29.961 71.092 1.00 50.04  ? 269 PRO B CG  1 
ATOM   4594 C  CD  . PRO B  1  256 ? 6.218   -29.845 70.794 1.00 48.94  ? 269 PRO B CD  1 
ATOM   4595 N  N   . TRP B  1  257 ? 5.185   -25.576 72.672 1.00 46.01  ? 270 TRP B N   1 
ATOM   4596 C  CA  . TRP B  1  257 ? 5.627   -24.515 73.553 1.00 44.82  ? 270 TRP B CA  1 
ATOM   4597 C  C   . TRP B  1  257 ? 4.458   -23.590 73.890 1.00 43.88  ? 270 TRP B C   1 
ATOM   4598 O  O   . TRP B  1  257 ? 3.506   -23.425 73.123 1.00 44.43  ? 270 TRP B O   1 
ATOM   4599 C  CB  . TRP B  1  257 ? 6.809   -23.756 72.924 1.00 43.92  ? 270 TRP B CB  1 
ATOM   4600 C  CG  . TRP B  1  257 ? 7.490   -22.842 73.903 1.00 40.71  ? 270 TRP B CG  1 
ATOM   4601 C  CD1 . TRP B  1  257 ? 7.287   -21.504 74.035 1.00 40.08  ? 270 TRP B CD1 1 
ATOM   4602 C  CD2 . TRP B  1  257 ? 8.408   -23.219 74.950 1.00 40.14  ? 270 TRP B CD2 1 
ATOM   4603 N  NE1 . TRP B  1  257 ? 8.040   -21.015 75.062 1.00 44.22  ? 270 TRP B NE1 1 
ATOM   4604 C  CE2 . TRP B  1  257 ? 8.731   -22.039 75.645 1.00 41.56  ? 270 TRP B CE2 1 
ATOM   4605 C  CE3 . TRP B  1  257 ? 8.983   -24.425 75.366 1.00 43.15  ? 270 TRP B CE3 1 
ATOM   4606 C  CZ2 . TRP B  1  257 ? 9.601   -22.030 76.730 1.00 47.10  ? 270 TRP B CZ2 1 
ATOM   4607 C  CZ3 . TRP B  1  257 ? 9.844   -24.422 76.441 1.00 44.18  ? 270 TRP B CZ3 1 
ATOM   4608 C  CH2 . TRP B  1  257 ? 10.147  -23.237 77.113 1.00 47.82  ? 270 TRP B CH2 1 
ATOM   4609 N  N   . VAL B  1  258 ? 4.549   -22.987 75.070 1.00 43.44  ? 271 VAL B N   1 
ATOM   4610 C  CA  . VAL B  1  258 ? 3.443   -22.259 75.655 1.00 49.16  ? 271 VAL B CA  1 
ATOM   4611 C  C   . VAL B  1  258 ? 3.914   -20.837 75.926 1.00 44.64  ? 271 VAL B C   1 
ATOM   4612 O  O   . VAL B  1  258 ? 5.022   -20.634 76.406 1.00 42.00  ? 271 VAL B O   1 
ATOM   4613 C  CB  . VAL B  1  258 ? 2.981   -22.992 76.934 1.00 54.81  ? 271 VAL B CB  1 
ATOM   4614 C  CG1 . VAL B  1  258 ? 1.923   -22.225 77.707 1.00 62.54  ? 271 VAL B CG1 1 
ATOM   4615 C  CG2 . VAL B  1  258 ? 2.464   -24.391 76.630 1.00 54.66  ? 271 VAL B CG2 1 
ATOM   4616 N  N   . PRO B  1  259 ? 3.097   -19.808 75.604 1.00 47.53  ? 272 PRO B N   1 
ATOM   4617 C  CA  . PRO B  1  259 ? 3.471   -18.420 75.867 1.00 46.94  ? 272 PRO B CA  1 
ATOM   4618 C  C   . PRO B  1  259 ? 3.790   -18.187 77.338 1.00 47.74  ? 272 PRO B C   1 
ATOM   4619 O  O   . PRO B  1  259 ? 3.213   -18.828 78.204 1.00 49.49  ? 272 PRO B O   1 
ATOM   4620 C  CB  . PRO B  1  259 ? 2.261   -17.597 75.398 1.00 47.39  ? 272 PRO B CB  1 
ATOM   4621 C  CG  . PRO B  1  259 ? 1.131   -18.597 75.256 1.00 45.58  ? 272 PRO B CG  1 
ATOM   4622 C  CD  . PRO B  1  259 ? 1.789   -19.925 74.937 1.00 47.07  ? 272 PRO B CD  1 
ATOM   4623 N  N   . GLY B  1  260 ? 4.711   -17.256 77.599 1.00 47.98  ? 273 GLY B N   1 
ATOM   4624 C  CA  . GLY B  1  260 ? 5.093   -16.911 78.952 1.00 44.48  ? 273 GLY B CA  1 
ATOM   4625 C  C   . GLY B  1  260 ? 6.361   -16.065 78.958 1.00 46.32  ? 273 GLY B C   1 
ATOM   4626 O  O   . GLY B  1  260 ? 6.635   -15.337 78.013 1.00 42.90  ? 273 GLY B O   1 
ATOM   4627 N  N   . GLY B  1  261 ? 7.130   -16.168 80.046 1.00 50.77  ? 274 GLY B N   1 
ATOM   4628 C  CA  . GLY B  1  261 ? 8.340   -15.376 80.198 1.00 53.91  ? 274 GLY B CA  1 
ATOM   4629 C  C   . GLY B  1  261 ? 9.098   -15.737 81.472 1.00 56.80  ? 274 GLY B C   1 
ATOM   4630 O  O   . GLY B  1  261 ? 8.588   -16.470 82.317 1.00 55.56  ? 274 GLY B O   1 
ATOM   4631 N  N   . ASN B  1  262 ? 10.335  -15.234 81.573 1.00 55.15  ? 275 ASN B N   1 
ATOM   4632 C  CA  . ASN B  1  262 ? 11.118  -15.333 82.789 1.00 54.31  ? 275 ASN B CA  1 
ATOM   4633 C  C   . ASN B  1  262 ? 10.509  -14.403 83.832 1.00 56.39  ? 275 ASN B C   1 
ATOM   4634 O  O   . ASN B  1  262 ? 10.327  -13.228 83.552 1.00 56.56  ? 275 ASN B O   1 
ATOM   4635 C  CB  . ASN B  1  262 ? 12.583  -14.975 82.552 1.00 51.23  ? 275 ASN B CB  1 
ATOM   4636 C  CG  . ASN B  1  262 ? 13.410  -16.128 82.031 1.00 48.64  ? 275 ASN B CG  1 
ATOM   4637 O  OD1 . ASN B  1  262 ? 13.026  -17.294 82.155 1.00 40.68  ? 275 ASN B OD1 1 
ATOM   4638 N  ND2 . ASN B  1  262 ? 14.574  -15.828 81.472 1.00 51.81  ? 275 ASN B ND2 1 
ATOM   4639 N  N   . ALA B  1  263 ? 10.221  -14.930 85.030 1.00 62.42  ? 276 ALA B N   1 
ATOM   4640 C  CA  . ALA B  1  263 ? 9.617   -14.150 86.101 1.00 66.79  ? 276 ALA B CA  1 
ATOM   4641 C  C   . ALA B  1  263 ? 10.689  -13.593 87.043 1.00 71.41  ? 276 ALA B C   1 
ATOM   4642 O  O   . ALA B  1  263 ? 11.747  -14.193 87.208 1.00 70.64  ? 276 ALA B O   1 
ATOM   4643 C  CB  . ALA B  1  263 ? 8.604   -15.008 86.839 1.00 67.11  ? 276 ALA B CB  1 
ATOM   4644 N  N   . ASP B  1  264 ? 10.389  -12.432 87.646 1.00 76.12  ? 277 ASP B N   1 
ATOM   4645 C  CA  . ASP B  1  264 ? 11.144  -11.873 88.764 1.00 83.42  ? 277 ASP B CA  1 
ATOM   4646 C  C   . ASP B  1  264 ? 12.610  -11.630 88.399 1.00 73.78  ? 277 ASP B C   1 
ATOM   4647 O  O   . ASP B  1  264 ? 13.500  -11.912 89.196 1.00 82.14  ? 277 ASP B O   1 
ATOM   4648 C  CB  . ASP B  1  264 ? 11.018  -12.727 90.022 1.00 90.02  ? 277 ASP B CB  1 
ATOM   4649 C  CG  . ASP B  1  264 ? 9.596   -12.942 90.528 1.00 90.23  ? 277 ASP B CG  1 
ATOM   4650 O  OD1 . ASP B  1  264 ? 8.876   -11.933 90.707 1.00 84.36  ? 277 ASP B OD1 1 
ATOM   4651 O  OD2 . ASP B  1  264 ? 9.212   -14.117 90.729 1.00 80.86  ? 277 ASP B OD2 1 
ATOM   4652 N  N   . ASN B  1  265 ? 12.852  -11.114 87.191 1.00 62.59  ? 278 ASN B N   1 
ATOM   4653 C  CA  A ASN B  1  265 ? 14.165  -10.641 86.783 0.50 59.45  ? 278 ASN B CA  1 
ATOM   4654 C  CA  B ASN B  1  265 ? 14.167  -10.642 86.778 0.50 57.54  ? 278 ASN B CA  1 
ATOM   4655 C  C   . ASN B  1  265 ? 15.220  -11.731 86.990 1.00 56.10  ? 278 ASN B C   1 
ATOM   4656 O  O   . ASN B  1  265 ? 16.340  -11.434 87.395 1.00 55.13  ? 278 ASN B O   1 
ATOM   4657 C  CB  A ASN B  1  265 ? 14.533  -9.348  87.507 0.50 58.12  ? 278 ASN B CB  1 
ATOM   4658 C  CB  B ASN B  1  265 ? 14.531  -9.343  87.497 0.50 53.91  ? 278 ASN B CB  1 
ATOM   4659 C  CG  A ASN B  1  265 ? 13.807  -8.133  86.978 0.50 57.43  ? 278 ASN B CG  1 
ATOM   4660 C  CG  B ASN B  1  265 ? 15.719  -8.625  86.893 0.50 50.00  ? 278 ASN B CG  1 
ATOM   4661 O  OD1 A ASN B  1  265 ? 13.369  -8.103  85.822 0.50 56.21  ? 278 ASN B OD1 1 
ATOM   4662 O  OD1 B ASN B  1  265 ? 15.833  -8.502  85.664 0.50 50.53  ? 278 ASN B OD1 1 
ATOM   4663 N  ND2 A ASN B  1  265 ? 13.720  -7.095  87.795 0.50 57.79  ? 278 ASN B ND2 1 
ATOM   4664 N  ND2 B ASN B  1  265 ? 16.604  -8.120  87.741 0.50 49.28  ? 278 ASN B ND2 1 
ATOM   4665 N  N   . GLN B  1  266 ? 14.874  -12.989 86.675 1.00 54.39  ? 279 GLN B N   1 
ATOM   4666 C  CA  . GLN B  1  266 ? 15.800  -14.102 86.820 1.00 59.84  ? 279 GLN B CA  1 
ATOM   4667 C  C   . GLN B  1  266 ? 15.813  -14.982 85.572 1.00 58.57  ? 279 GLN B C   1 
ATOM   4668 O  O   . GLN B  1  266 ? 14.782  -15.188 84.948 1.00 65.19  ? 279 GLN B O   1 
ATOM   4669 C  CB  . GLN B  1  266 ? 15.374  -15.012 87.967 1.00 68.41  ? 279 GLN B CB  1 
ATOM   4670 C  CG  . GLN B  1  266 ? 15.703  -14.480 89.354 1.00 79.83  ? 279 GLN B CG  1 
ATOM   4671 C  CD  . GLN B  1  266 ? 15.147  -15.355 90.458 1.00 88.74  ? 279 GLN B CD  1 
ATOM   4672 O  OE1 . GLN B  1  266 ? 14.501  -16.381 90.217 1.00 77.50  ? 279 GLN B OE1 1 
ATOM   4673 N  NE2 . GLN B  1  266 ? 15.402  -14.956 91.694 1.00 100.07 ? 279 GLN B NE2 1 
ATOM   4674 N  N   . VAL B  1  267 ? 16.975  -15.568 85.273 1.00 52.53  ? 280 VAL B N   1 
ATOM   4675 C  CA  . VAL B  1  267 ? 17.113  -16.508 84.174 1.00 54.15  ? 280 VAL B CA  1 
ATOM   4676 C  C   . VAL B  1  267 ? 16.615  -17.890 84.596 1.00 52.67  ? 280 VAL B C   1 
ATOM   4677 O  O   . VAL B  1  267 ? 16.270  -18.110 85.748 1.00 53.68  ? 280 VAL B O   1 
ATOM   4678 C  CB  . VAL B  1  267 ? 18.565  -16.546 83.654 1.00 58.72  ? 280 VAL B CB  1 
ATOM   4679 C  CG1 . VAL B  1  267 ? 18.974  -15.217 83.023 1.00 60.29  ? 280 VAL B CG1 1 
ATOM   4680 C  CG2 . VAL B  1  267 ? 19.569  -16.940 84.731 1.00 62.19  ? 280 VAL B CG2 1 
ATOM   4681 N  N   . ASN B  1  268 ? 16.541  -18.802 83.622 1.00 58.15  ? 281 ASN B N   1 
ATOM   4682 C  CA  . ASN B  1  268 ? 16.035  -20.164 83.782 1.00 62.44  ? 281 ASN B CA  1 
ATOM   4683 C  C   . ASN B  1  268 ? 14.816  -20.224 84.703 1.00 58.52  ? 281 ASN B C   1 
ATOM   4684 O  O   . ASN B  1  268 ? 14.715  -21.127 85.524 1.00 56.22  ? 281 ASN B O   1 
ATOM   4685 C  CB  . ASN B  1  268 ? 17.130  -21.123 84.237 1.00 61.14  ? 281 ASN B CB  1 
ATOM   4686 C  CG  . ASN B  1  268 ? 18.232  -21.222 83.209 1.00 62.54  ? 281 ASN B CG  1 
ATOM   4687 O  OD1 . ASN B  1  268 ? 18.068  -21.866 82.164 1.00 60.33  ? 281 ASN B OD1 1 
ATOM   4688 N  ND2 . ASN B  1  268 ? 19.361  -20.585 83.480 1.00 61.69  ? 281 ASN B ND2 1 
ATOM   4689 N  N   . ASN B  1  269 ? 13.858  -19.315 84.497 1.00 57.41  ? 282 ASN B N   1 
ATOM   4690 C  CA  . ASN B  1  269 ? 12.721  -19.174 85.386 1.00 55.68  ? 282 ASN B CA  1 
ATOM   4691 C  C   . ASN B  1  269 ? 11.453  -18.898 84.571 1.00 54.51  ? 282 ASN B C   1 
ATOM   4692 O  O   . ASN B  1  269 ? 10.715  -17.947 84.843 1.00 47.03  ? 282 ASN B O   1 
ATOM   4693 C  CB  . ASN B  1  269 ? 13.009  -18.095 86.424 1.00 56.00  ? 282 ASN B CB  1 
ATOM   4694 C  CG  . ASN B  1  269 ? 11.989  -18.079 87.544 1.00 53.70  ? 282 ASN B CG  1 
ATOM   4695 O  OD1 . ASN B  1  269 ? 11.413  -19.118 87.884 1.00 45.59  ? 282 ASN B OD1 1 
ATOM   4696 N  ND2 . ASN B  1  269 ? 11.767  -16.919 88.142 1.00 50.67  ? 282 ASN B ND2 1 
ATOM   4697 N  N   . TYR B  1  270 ? 11.188  -19.749 83.573 1.00 51.63  ? 283 TYR B N   1 
ATOM   4698 C  CA  . TYR B  1  270 ? 10.105  -19.492 82.638 1.00 54.36  ? 283 TYR B CA  1 
ATOM   4699 C  C   . TYR B  1  270 ? 8.771   -19.934 83.243 1.00 55.77  ? 283 TYR B C   1 
ATOM   4700 O  O   . TYR B  1  270 ? 8.621   -21.082 83.652 1.00 54.65  ? 283 TYR B O   1 
ATOM   4701 C  CB  . TYR B  1  270 ? 10.411  -20.201 81.317 1.00 55.96  ? 283 TYR B CB  1 
ATOM   4702 C  CG  . TYR B  1  270 ? 9.483   -19.837 80.165 1.00 56.77  ? 283 TYR B CG  1 
ATOM   4703 C  CD1 . TYR B  1  270 ? 9.744   -18.746 79.340 1.00 59.67  ? 283 TYR B CD1 1 
ATOM   4704 C  CD2 . TYR B  1  270 ? 8.358   -20.602 79.887 1.00 56.78  ? 283 TYR B CD2 1 
ATOM   4705 C  CE1 . TYR B  1  270 ? 8.909   -18.421 78.283 1.00 57.60  ? 283 TYR B CE1 1 
ATOM   4706 C  CE2 . TYR B  1  270 ? 7.519   -20.295 78.828 1.00 57.80  ? 283 TYR B CE2 1 
ATOM   4707 C  CZ  . TYR B  1  270 ? 7.790   -19.197 78.027 1.00 56.66  ? 283 TYR B CZ  1 
ATOM   4708 O  OH  . TYR B  1  270 ? 6.941   -18.892 77.006 1.00 45.81  ? 283 TYR B OH  1 
ATOM   4709 N  N   . VAL B  1  271 ? 7.802   -19.009 83.267 1.00 54.09  ? 284 VAL B N   1 
ATOM   4710 C  CA  . VAL B  1  271 ? 6.467   -19.251 83.793 1.00 51.58  ? 284 VAL B CA  1 
ATOM   4711 C  C   . VAL B  1  271 ? 5.453   -19.079 82.668 1.00 51.01  ? 284 VAL B C   1 
ATOM   4712 O  O   . VAL B  1  271 ? 5.470   -18.056 81.985 1.00 49.26  ? 284 VAL B O   1 
ATOM   4713 C  CB  . VAL B  1  271 ? 6.151   -18.261 84.931 1.00 55.78  ? 284 VAL B CB  1 
ATOM   4714 C  CG1 . VAL B  1  271 ? 4.717   -18.408 85.437 1.00 54.85  ? 284 VAL B CG1 1 
ATOM   4715 C  CG2 . VAL B  1  271 ? 7.157   -18.354 86.076 1.00 57.06  ? 284 VAL B CG2 1 
ATOM   4716 N  N   . GLU B  1  272 ? 4.535   -20.047 82.540 1.00 52.63  ? 285 GLU B N   1 
ATOM   4717 C  CA  A GLU B  1  272 ? 3.487   -19.994 81.533 0.50 51.38  ? 285 GLU B CA  1 
ATOM   4718 C  CA  B GLU B  1  272 ? 3.472   -20.004 81.541 0.50 53.06  ? 285 GLU B CA  1 
ATOM   4719 C  C   . GLU B  1  272 ? 2.515   -18.852 81.854 1.00 52.56  ? 285 GLU B C   1 
ATOM   4720 O  O   . GLU B  1  272 ? 2.307   -18.506 83.014 1.00 50.28  ? 285 GLU B O   1 
ATOM   4721 C  CB  A GLU B  1  272 ? 2.831   -21.374 81.422 0.50 49.18  ? 285 GLU B CB  1 
ATOM   4722 C  CB  B GLU B  1  272 ? 2.735   -21.349 81.456 0.50 53.18  ? 285 GLU B CB  1 
ATOM   4723 C  CG  A GLU B  1  272 ? 3.831   -22.496 81.131 0.50 48.32  ? 285 GLU B CG  1 
ATOM   4724 C  CG  B GLU B  1  272 ? 1.308   -21.256 80.907 0.50 54.45  ? 285 GLU B CG  1 
ATOM   4725 C  CD  A GLU B  1  272 ? 3.260   -23.899 80.955 0.50 47.40  ? 285 GLU B CD  1 
ATOM   4726 C  CD  B GLU B  1  272 ? 0.525   -22.560 80.780 0.50 55.90  ? 285 GLU B CD  1 
ATOM   4727 O  OE1 A GLU B  1  272 ? 2.030   -24.071 81.056 0.50 48.01  ? 285 GLU B OE1 1 
ATOM   4728 O  OE1 B GLU B  1  272 ? 1.072   -23.654 81.049 0.50 58.85  ? 285 GLU B OE1 1 
ATOM   4729 O  OE2 A GLU B  1  272 ? 4.048   -24.829 80.690 0.50 43.43  ? 285 GLU B OE2 1 
ATOM   4730 O  OE2 B GLU B  1  272 ? -0.664  -22.474 80.410 0.50 52.43  ? 285 GLU B OE2 1 
ATOM   4731 N  N   . ASP B  1  273 ? 1.953   -18.243 80.798 1.00 57.57  ? 286 ASP B N   1 
ATOM   4732 C  CA  . ASP B  1  273 ? 0.883   -17.264 80.917 1.00 56.85  ? 286 ASP B CA  1 
ATOM   4733 C  C   . ASP B  1  273 ? -0.367  -17.832 80.247 1.00 59.41  ? 286 ASP B C   1 
ATOM   4734 O  O   . ASP B  1  273 ? -0.428  -17.910 79.026 1.00 57.32  ? 286 ASP B O   1 
ATOM   4735 C  CB  . ASP B  1  273 ? 1.233   -15.925 80.289 1.00 52.19  ? 286 ASP B CB  1 
ATOM   4736 C  CG  . ASP B  1  273 ? 0.128   -14.877 80.349 1.00 51.10  ? 286 ASP B CG  1 
ATOM   4737 O  OD1 . ASP B  1  273 ? -0.978  -15.208 80.813 1.00 53.22  ? 286 ASP B OD1 1 
ATOM   4738 O  OD2 . ASP B  1  273 ? 0.387   -13.727 79.959 1.00 53.34  ? 286 ASP B OD2 1 
ATOM   4739 N  N   . PRO B  1  274 ? -1.404  -18.246 81.014 1.00 69.78  ? 287 PRO B N   1 
ATOM   4740 C  CA  . PRO B  1  274 ? -2.606  -18.839 80.416 1.00 64.44  ? 287 PRO B CA  1 
ATOM   4741 C  C   . PRO B  1  274 ? -3.578  -17.850 79.766 1.00 59.47  ? 287 PRO B C   1 
ATOM   4742 O  O   . PRO B  1  274 ? -4.494  -18.288 79.076 1.00 60.59  ? 287 PRO B O   1 
ATOM   4743 C  CB  . PRO B  1  274 ? -3.214  -19.558 81.634 1.00 65.57  ? 287 PRO B CB  1 
ATOM   4744 C  CG  . PRO B  1  274 ? -2.864  -18.659 82.807 1.00 66.32  ? 287 PRO B CG  1 
ATOM   4745 C  CD  . PRO B  1  274 ? -1.470  -18.160 82.486 1.00 68.69  ? 287 PRO B CD  1 
ATOM   4746 N  N   . ASP B  1  275 ? -3.363  -16.535 79.971 1.00 57.32  ? 288 ASP B N   1 
ATOM   4747 C  CA  . ASP B  1  275 ? -4.197  -15.477 79.409 1.00 56.99  ? 288 ASP B CA  1 
ATOM   4748 C  C   . ASP B  1  275 ? -3.713  -14.974 78.044 1.00 57.13  ? 288 ASP B C   1 
ATOM   4749 O  O   . ASP B  1  275 ? -4.452  -14.286 77.342 1.00 56.50  ? 288 ASP B O   1 
ATOM   4750 C  CB  . ASP B  1  275 ? -4.263  -14.279 80.339 1.00 59.28  ? 288 ASP B CB  1 
ATOM   4751 C  CG  . ASP B  1  275 ? -5.140  -14.483 81.567 1.00 70.63  ? 288 ASP B CG  1 
ATOM   4752 O  OD1 . ASP B  1  275 ? -5.440  -15.656 81.910 1.00 70.71  ? 288 ASP B OD1 1 
ATOM   4753 O  OD2 . ASP B  1  275 ? -5.563  -13.450 82.147 1.00 70.63  ? 288 ASP B OD2 1 
ATOM   4754 N  N   . SER B  1  276 ? -2.466  -15.287 77.676 1.00 55.97  ? 289 SER B N   1 
ATOM   4755 C  CA  . SER B  1  276 ? -1.901  -14.865 76.405 1.00 51.99  ? 289 SER B CA  1 
ATOM   4756 C  C   . SER B  1  276 ? -2.672  -15.459 75.233 1.00 47.21  ? 289 SER B C   1 
ATOM   4757 O  O   . SER B  1  276 ? -3.260  -16.539 75.341 1.00 44.60  ? 289 SER B O   1 
ATOM   4758 C  CB  . SER B  1  276 ? -0.440  -15.257 76.312 1.00 53.18  ? 289 SER B CB  1 
ATOM   4759 O  OG  . SER B  1  276 ? 0.030   -15.202 74.974 1.00 49.24  ? 289 SER B OG  1 
ATOM   4760 N  N   . ALA B  1  277 ? -2.604  -14.762 74.098 1.00 42.62  ? 290 ALA B N   1 
ATOM   4761 C  CA  . ALA B  1  277 ? -2.981  -15.358 72.827 1.00 44.81  ? 290 ALA B CA  1 
ATOM   4762 C  C   . ALA B  1  277 ? -2.104  -16.570 72.528 1.00 47.10  ? 290 ALA B C   1 
ATOM   4763 O  O   . ALA B  1  277 ? -0.958  -16.622 72.970 1.00 47.15  ? 290 ALA B O   1 
ATOM   4764 C  CB  . ALA B  1  277 ? -2.834  -14.331 71.733 1.00 46.05  ? 290 ALA B CB  1 
ATOM   4765 N  N   . ASP B  1  278 ? -2.658  -17.533 71.786 1.00 46.76  ? 291 ASP B N   1 
ATOM   4766 C  CA  . ASP B  1  278 ? -1.892  -18.619 71.193 1.00 50.62  ? 291 ASP B CA  1 
ATOM   4767 C  C   . ASP B  1  278 ? -2.561  -18.974 69.865 1.00 50.06  ? 291 ASP B C   1 
ATOM   4768 O  O   . ASP B  1  278 ? -3.399  -18.210 69.397 1.00 41.33  ? 291 ASP B O   1 
ATOM   4769 C  CB  . ASP B  1  278 ? -1.727  -19.778 72.164 1.00 52.17  ? 291 ASP B CB  1 
ATOM   4770 C  CG  . ASP B  1  278 ? -2.980  -20.576 72.490 1.00 54.61  ? 291 ASP B CG  1 
ATOM   4771 O  OD1 . ASP B  1  278 ? -3.979  -20.472 71.736 1.00 52.95  ? 291 ASP B OD1 1 
ATOM   4772 O  OD2 . ASP B  1  278 ? -2.956  -21.299 73.500 1.00 55.39  ? 291 ASP B OD2 1 
ATOM   4773 N  N   . PHE B  1  279 ? -2.218  -20.123 69.270 1.00 49.58  ? 292 PHE B N   1 
ATOM   4774 C  CA  . PHE B  1  279 ? -2.624  -20.394 67.898 1.00 49.71  ? 292 PHE B CA  1 
ATOM   4775 C  C   . PHE B  1  279 ? -4.067  -20.887 67.803 1.00 53.30  ? 292 PHE B C   1 
ATOM   4776 O  O   . PHE B  1  279 ? -4.625  -20.887 66.713 1.00 51.95  ? 292 PHE B O   1 
ATOM   4777 C  CB  . PHE B  1  279 ? -1.630  -21.338 67.222 1.00 50.59  ? 292 PHE B CB  1 
ATOM   4778 C  CG  . PHE B  1  279 ? -0.438  -20.551 66.706 1.00 56.25  ? 292 PHE B CG  1 
ATOM   4779 C  CD1 . PHE B  1  279 ? -0.544  -19.817 65.530 1.00 62.76  ? 292 PHE B CD1 1 
ATOM   4780 C  CD2 . PHE B  1  279 ? 0.753   -20.495 67.420 1.00 55.76  ? 292 PHE B CD2 1 
ATOM   4781 C  CE1 . PHE B  1  279 ? 0.519   -19.056 65.072 1.00 66.63  ? 292 PHE B CE1 1 
ATOM   4782 C  CE2 . PHE B  1  279 ? 1.811   -19.741 66.954 1.00 58.13  ? 292 PHE B CE2 1 
ATOM   4783 C  CZ  . PHE B  1  279 ? 1.694   -19.024 65.785 1.00 62.94  ? 292 PHE B CZ  1 
ATOM   4784 N  N   . THR B  1  280 ? -4.678  -21.279 68.927 1.00 58.48  ? 293 THR B N   1 
ATOM   4785 C  CA  . THR B  1  280 ? -6.087  -21.642 68.948 1.00 56.36  ? 293 THR B CA  1 
ATOM   4786 C  C   . THR B  1  280 ? -6.902  -20.530 69.611 1.00 54.30  ? 293 THR B C   1 
ATOM   4787 O  O   . THR B  1  280 ? -8.100  -20.698 69.804 1.00 52.99  ? 293 THR B O   1 
ATOM   4788 C  CB  . THR B  1  280 ? -6.276  -22.977 69.670 1.00 56.08  ? 293 THR B CB  1 
ATOM   4789 O  OG1 . THR B  1  280 ? -5.848  -22.742 71.006 1.00 56.00  ? 293 THR B OG1 1 
ATOM   4790 C  CG2 . THR B  1  280 ? -5.487  -24.119 69.048 1.00 56.13  ? 293 THR B CG2 1 
ATOM   4791 N  N   . HIS B  1  281 ? -6.256  -19.408 69.957 1.00 52.49  ? 294 HIS B N   1 
ATOM   4792 C  CA  . HIS B  1  281 ? -6.898  -18.293 70.643 1.00 53.15  ? 294 HIS B CA  1 
ATOM   4793 C  C   . HIS B  1  281 ? -6.394  -16.978 70.036 1.00 49.84  ? 294 HIS B C   1 
ATOM   4794 O  O   . HIS B  1  281 ? -5.926  -16.096 70.753 1.00 52.16  ? 294 HIS B O   1 
ATOM   4795 C  CB  . HIS B  1  281 ? -6.683  -18.353 72.170 1.00 54.74  ? 294 HIS B CB  1 
ATOM   4796 C  CG  . HIS B  1  281 ? -7.301  -19.526 72.873 1.00 61.81  ? 294 HIS B CG  1 
ATOM   4797 N  ND1 . HIS B  1  281 ? -8.593  -19.539 73.361 1.00 64.93  ? 294 HIS B ND1 1 
ATOM   4798 C  CD2 . HIS B  1  281 ? -6.794  -20.733 73.167 1.00 63.94  ? 294 HIS B CD2 1 
ATOM   4799 C  CE1 . HIS B  1  281 ? -8.842  -20.708 73.935 1.00 67.88  ? 294 HIS B CE1 1 
ATOM   4800 N  NE2 . HIS B  1  281 ? -7.760  -21.444 73.832 1.00 72.72  ? 294 HIS B NE2 1 
ATOM   4801 N  N   . LEU B  1  282 ? -6.518  -16.831 68.711 1.00 46.60  ? 295 LEU B N   1 
ATOM   4802 C  CA  . LEU B  1  282 ? -5.933  -15.711 67.988 1.00 46.21  ? 295 LEU B CA  1 
ATOM   4803 C  C   . LEU B  1  282 ? -6.614  -14.376 68.285 1.00 49.13  ? 295 LEU B C   1 
ATOM   4804 O  O   . LEU B  1  282 ? -5.956  -13.337 68.255 1.00 55.85  ? 295 LEU B O   1 
ATOM   4805 C  CB  . LEU B  1  282 ? -5.940  -15.981 66.484 1.00 46.21  ? 295 LEU B CB  1 
ATOM   4806 C  CG  . LEU B  1  282 ? -4.846  -16.928 65.980 1.00 46.03  ? 295 LEU B CG  1 
ATOM   4807 C  CD1 . LEU B  1  282 ? -4.992  -17.223 64.500 1.00 47.19  ? 295 LEU B CD1 1 
ATOM   4808 C  CD2 . LEU B  1  282 ? -3.500  -16.277 66.228 1.00 48.62  ? 295 LEU B CD2 1 
ATOM   4809 N  N   . CYS B  1  283 ? -7.926  -14.385 68.524 1.00 50.77  ? 296 CYS B N   1 
ATOM   4810 C  CA  . CYS B  1  283 ? -8.653  -13.141 68.729 1.00 56.35  ? 296 CYS B CA  1 
ATOM   4811 C  C   . CYS B  1  283 ? -8.177  -12.423 69.989 1.00 53.12  ? 296 CYS B C   1 
ATOM   4812 O  O   . CYS B  1  283 ? -8.388  -11.224 70.112 1.00 49.37  ? 296 CYS B O   1 
ATOM   4813 C  CB  . CYS B  1  283 ? -10.169 -13.325 68.749 1.00 66.40  ? 296 CYS B CB  1 
ATOM   4814 S  SG  . CYS B  1  283 ? -10.891 -13.668 67.117 1.00 87.10  ? 296 CYS B SG  1 
ATOM   4815 N  N   . ARG B  1  284 ? -7.528  -13.135 70.915 1.00 53.60  ? 297 ARG B N   1 
ATOM   4816 C  CA  . ARG B  1  284 ? -6.961  -12.488 72.089 1.00 52.64  ? 297 ARG B CA  1 
ATOM   4817 C  C   . ARG B  1  284 ? -5.900  -11.473 71.684 1.00 50.13  ? 297 ARG B C   1 
ATOM   4818 O  O   . ARG B  1  284 ? -5.754  -10.439 72.338 1.00 50.30  ? 297 ARG B O   1 
ATOM   4819 C  CB  . ARG B  1  284 ? -6.349  -13.476 73.079 1.00 53.25  ? 297 ARG B CB  1 
ATOM   4820 C  CG  . ARG B  1  284 ? -7.364  -14.362 73.776 1.00 57.75  ? 297 ARG B CG  1 
ATOM   4821 C  CD  . ARG B  1  284 ? -6.726  -15.116 74.928 1.00 61.71  ? 297 ARG B CD  1 
ATOM   4822 N  NE  . ARG B  1  284 ? -7.582  -16.216 75.380 1.00 65.09  ? 297 ARG B NE  1 
ATOM   4823 C  CZ  . ARG B  1  284 ? -7.187  -17.243 76.118 1.00 64.76  ? 297 ARG B CZ  1 
ATOM   4824 N  NH1 . ARG B  1  284 ? -5.972  -17.278 76.627 1.00 66.93  ? 297 ARG B NH1 1 
ATOM   4825 N  NH2 . ARG B  1  284 ? -8.021  -18.245 76.336 1.00 64.22  ? 297 ARG B NH2 1 
ATOM   4826 N  N   . LEU B  1  285 ? -5.164  -11.779 70.610 1.00 47.71  ? 298 LEU B N   1 
ATOM   4827 C  CA  . LEU B  1  285 ? -4.160  -10.865 70.094 1.00 46.33  ? 298 LEU B CA  1 
ATOM   4828 C  C   . LEU B  1  285 ? -4.842  -9.559  69.687 1.00 43.31  ? 298 LEU B C   1 
ATOM   4829 O  O   . LEU B  1  285 ? -4.363  -8.480  70.033 1.00 45.88  ? 298 LEU B O   1 
ATOM   4830 C  CB  . LEU B  1  285 ? -3.390  -11.500 68.936 1.00 48.57  ? 298 LEU B CB  1 
ATOM   4831 C  CG  . LEU B  1  285 ? -2.100  -10.788 68.510 1.00 46.31  ? 298 LEU B CG  1 
ATOM   4832 C  CD1 . LEU B  1  285 ? -1.253  -11.744 67.721 1.00 47.46  ? 298 LEU B CD1 1 
ATOM   4833 C  CD2 . LEU B  1  285 ? -2.333  -9.548  67.679 1.00 48.38  ? 298 LEU B CD2 1 
ATOM   4834 N  N   . TYR B  1  286 ? -5.981  -9.669  68.992 1.00 39.94  ? 299 TYR B N   1 
ATOM   4835 C  CA  . TYR B  1  286 ? -6.746  -8.507  68.560 1.00 40.47  ? 299 TYR B CA  1 
ATOM   4836 C  C   . TYR B  1  286 ? -7.122  -7.656  69.775 1.00 42.52  ? 299 TYR B C   1 
ATOM   4837 O  O   . TYR B  1  286 ? -6.832  -6.458  69.804 1.00 42.55  ? 299 TYR B O   1 
ATOM   4838 C  CB  . TYR B  1  286 ? -7.958  -8.940  67.719 1.00 37.89  ? 299 TYR B CB  1 
ATOM   4839 C  CG  . TYR B  1  286 ? -8.869  -7.787  67.328 1.00 38.17  ? 299 TYR B CG  1 
ATOM   4840 C  CD1 . TYR B  1  286 ? -8.418  -6.764  66.503 1.00 36.34  ? 299 TYR B CD1 1 
ATOM   4841 C  CD2 . TYR B  1  286 ? -10.174 -7.707  67.802 1.00 42.17  ? 299 TYR B CD2 1 
ATOM   4842 C  CE1 . TYR B  1  286 ? -9.235  -5.693  66.170 1.00 41.01  ? 299 TYR B CE1 1 
ATOM   4843 C  CE2 . TYR B  1  286 ? -11.009 -6.648  67.461 1.00 42.64  ? 299 TYR B CE2 1 
ATOM   4844 C  CZ  . TYR B  1  286 ? -10.539 -5.634  66.643 1.00 44.19  ? 299 TYR B CZ  1 
ATOM   4845 O  OH  . TYR B  1  286 ? -11.328 -4.569  66.297 1.00 43.47  ? 299 TYR B OH  1 
ATOM   4846 N  N   . GLU B  1  287 ? -7.741  -8.286  70.781 1.00 44.93  ? 300 GLU B N   1 
ATOM   4847 C  CA  . GLU B  1  287 ? -8.224  -7.582  71.962 1.00 47.93  ? 300 GLU B CA  1 
ATOM   4848 C  C   . GLU B  1  287 ? -7.063  -6.921  72.704 1.00 44.98  ? 300 GLU B C   1 
ATOM   4849 O  O   . GLU B  1  287 ? -7.156  -5.747  73.064 1.00 47.99  ? 300 GLU B O   1 
ATOM   4850 C  CB  . GLU B  1  287 ? -9.026  -8.528  72.855 1.00 52.26  ? 300 GLU B CB  1 
ATOM   4851 C  CG  . GLU B  1  287 ? -10.363 -8.940  72.243 1.00 62.90  ? 300 GLU B CG  1 
ATOM   4852 C  CD  . GLU B  1  287 ? -11.003 -10.238 72.733 1.00 77.35  ? 300 GLU B CD  1 
ATOM   4853 O  OE1 . GLU B  1  287 ? -10.308 -11.196 73.159 1.00 80.44  ? 300 GLU B OE1 1 
ATOM   4854 O  OE2 . GLU B  1  287 ? -12.256 -10.288 72.687 1.00 90.32  ? 300 GLU B OE2 1 
ATOM   4855 N  N   . PHE B  1  288 ? -5.964  -7.666  72.902 1.00 41.61  ? 301 PHE B N   1 
ATOM   4856 C  CA  . PHE B  1  288 ? -4.786  -7.146  73.579 1.00 38.43  ? 301 PHE B CA  1 
ATOM   4857 C  C   . PHE B  1  288 ? -4.280  -5.868  72.901 1.00 37.39  ? 301 PHE B C   1 
ATOM   4858 O  O   . PHE B  1  288 ? -3.977  -4.892  73.577 1.00 36.16  ? 301 PHE B O   1 
ATOM   4859 C  CB  . PHE B  1  288 ? -3.708  -8.235  73.606 1.00 41.01  ? 301 PHE B CB  1 
ATOM   4860 C  CG  . PHE B  1  288 ? -2.461  -7.813  74.364 1.00 43.21  ? 301 PHE B CG  1 
ATOM   4861 C  CD1 . PHE B  1  288 ? -2.351  -8.056  75.732 1.00 44.87  ? 301 PHE B CD1 1 
ATOM   4862 C  CD2 . PHE B  1  288 ? -1.425  -7.132  73.729 1.00 42.98  ? 301 PHE B CD2 1 
ATOM   4863 C  CE1 . PHE B  1  288 ? -1.230  -7.636  76.439 1.00 43.55  ? 301 PHE B CE1 1 
ATOM   4864 C  CE2 . PHE B  1  288 ? -0.313  -6.710  74.441 1.00 43.11  ? 301 PHE B CE2 1 
ATOM   4865 C  CZ  . PHE B  1  288 ? -0.217  -6.960  75.794 1.00 42.29  ? 301 PHE B CZ  1 
ATOM   4866 N  N   . VAL B  1  289 ? -4.179  -5.875  71.562 1.00 35.52  ? 302 VAL B N   1 
ATOM   4867 C  CA  . VAL B  1  289 ? -3.596  -4.766  70.828 1.00 36.47  ? 302 VAL B CA  1 
ATOM   4868 C  C   . VAL B  1  289 ? -4.515  -3.551  70.897 1.00 36.06  ? 302 VAL B C   1 
ATOM   4869 O  O   . VAL B  1  289 ? -4.038  -2.423  71.010 1.00 32.89  ? 302 VAL B O   1 
ATOM   4870 C  CB  . VAL B  1  289 ? -3.272  -5.126  69.363 1.00 38.42  ? 302 VAL B CB  1 
ATOM   4871 C  CG1 . VAL B  1  289 ? -2.952  -3.902  68.510 1.00 34.96  ? 302 VAL B CG1 1 
ATOM   4872 C  CG2 . VAL B  1  289 ? -2.131  -6.127  69.264 1.00 39.46  ? 302 VAL B CG2 1 
ATOM   4873 N  N   . VAL B  1  290 ? -5.827  -3.772  70.788 1.00 38.38  ? 303 VAL B N   1 
ATOM   4874 C  CA  . VAL B  1  290 ? -6.784  -2.683  70.941 1.00 42.81  ? 303 VAL B CA  1 
ATOM   4875 C  C   . VAL B  1  290 ? -6.624  -2.050  72.328 1.00 42.21  ? 303 VAL B C   1 
ATOM   4876 O  O   . VAL B  1  290 ? -6.594  -0.813  72.453 1.00 41.14  ? 303 VAL B O   1 
ATOM   4877 C  CB  . VAL B  1  290 ? -8.224  -3.168  70.676 1.00 44.90  ? 303 VAL B CB  1 
ATOM   4878 C  CG1 . VAL B  1  290 ? -9.269  -2.158  71.133 1.00 44.07  ? 303 VAL B CG1 1 
ATOM   4879 C  CG2 . VAL B  1  290 ? -8.424  -3.531  69.203 1.00 40.62  ? 303 VAL B CG2 1 
ATOM   4880 N  N   . GLY B  1  291 ? -6.488  -2.907  73.355 1.00 41.45  ? 304 GLY B N   1 
ATOM   4881 C  CA  . GLY B  1  291 ? -6.121  -2.459  74.689 1.00 39.97  ? 304 GLY B CA  1 
ATOM   4882 C  C   . GLY B  1  291 ? -4.871  -1.569  74.690 1.00 40.23  ? 304 GLY B C   1 
ATOM   4883 O  O   . GLY B  1  291 ? -4.892  -0.470  75.230 1.00 43.10  ? 304 GLY B O   1 
ATOM   4884 N  N   . SER B  1  292 ? -3.790  -2.029  74.050 1.00 40.12  ? 305 SER B N   1 
ATOM   4885 C  CA  . SER B  1  292 ? -2.528  -1.304  74.049 1.00 36.54  ? 305 SER B CA  1 
ATOM   4886 C  C   . SER B  1  292 ? -2.680  0.050   73.368 1.00 36.41  ? 305 SER B C   1 
ATOM   4887 O  O   . SER B  1  292 ? -2.028  1.018   73.772 1.00 36.57  ? 305 SER B O   1 
ATOM   4888 C  CB  . SER B  1  292 ? -1.425  -2.088  73.389 1.00 39.15  ? 305 SER B CB  1 
ATOM   4889 O  OG  . SER B  1  292 ? -1.308  -3.403  73.923 1.00 43.35  ? 305 SER B OG  1 
ATOM   4890 N  N   . VAL B  1  293 ? -3.521  0.114   72.326 1.00 36.82  ? 306 VAL B N   1 
ATOM   4891 C  CA  . VAL B  1  293 ? -3.713  1.361   71.610 1.00 39.43  ? 306 VAL B CA  1 
ATOM   4892 C  C   . VAL B  1  293 ? -4.402  2.383   72.518 1.00 43.68  ? 306 VAL B C   1 
ATOM   4893 O  O   . VAL B  1  293 ? -4.078  3.576   72.470 1.00 39.19  ? 306 VAL B O   1 
ATOM   4894 C  CB  . VAL B  1  293 ? -4.475  1.139   70.291 1.00 40.07  ? 306 VAL B CB  1 
ATOM   4895 C  CG1 . VAL B  1  293 ? -4.984  2.442   69.688 1.00 40.49  ? 306 VAL B CG1 1 
ATOM   4896 C  CG2 . VAL B  1  293 ? -3.609  0.411   69.272 1.00 41.27  ? 306 VAL B CG2 1 
ATOM   4897 N  N   . GLN B  1  294 ? -5.345  1.904   73.348 1.00 49.33  ? 307 GLN B N   1 
ATOM   4898 C  CA  . GLN B  1  294 ? -6.037  2.764   74.298 1.00 48.51  ? 307 GLN B CA  1 
ATOM   4899 C  C   . GLN B  1  294 ? -5.051  3.361   75.299 1.00 49.35  ? 307 GLN B C   1 
ATOM   4900 O  O   . GLN B  1  294 ? -5.187  4.522   75.652 1.00 52.64  ? 307 GLN B O   1 
ATOM   4901 C  CB  . GLN B  1  294 ? -7.172  2.025   75.003 1.00 46.86  ? 307 GLN B CB  1 
ATOM   4902 C  CG  . GLN B  1  294 ? -8.327  1.715   74.065 1.00 50.66  ? 307 GLN B CG  1 
ATOM   4903 C  CD  . GLN B  1  294 ? -9.426  0.907   74.707 1.00 55.54  ? 307 GLN B CD  1 
ATOM   4904 O  OE1 . GLN B  1  294 ? -9.374  -0.328  74.817 1.00 55.29  ? 307 GLN B OE1 1 
ATOM   4905 N  NE2 . GLN B  1  294 ? -10.473 1.631   75.065 1.00 60.21  ? 307 GLN B NE2 1 
ATOM   4906 N  N   . GLU B  1  295 ? -4.060  2.582   75.748 1.00 48.85  ? 308 GLU B N   1 
ATOM   4907 C  CA  . GLU B  1  295 ? -3.066  3.084   76.691 1.00 48.31  ? 308 GLU B CA  1 
ATOM   4908 C  C   . GLU B  1  295 ? -2.216  4.178   76.045 1.00 49.65  ? 308 GLU B C   1 
ATOM   4909 O  O   . GLU B  1  295 ? -1.886  5.137   76.726 1.00 52.86  ? 308 GLU B O   1 
ATOM   4910 C  CB  . GLU B  1  295 ? -2.189  1.976   77.266 1.00 52.48  ? 308 GLU B CB  1 
ATOM   4911 C  CG  . GLU B  1  295 ? -2.974  0.983   78.124 1.00 61.46  ? 308 GLU B CG  1 
ATOM   4912 C  CD  . GLU B  1  295 ? -2.189  -0.190  78.693 1.00 73.58  ? 308 GLU B CD  1 
ATOM   4913 O  OE1 . GLU B  1  295 ? -0.945  -0.085  78.744 1.00 86.07  ? 308 GLU B OE1 1 
ATOM   4914 O  OE2 . GLU B  1  295 ? -2.811  -1.212  79.071 1.00 75.72  ? 308 GLU B OE2 1 
ATOM   4915 N  N   . LEU B  1  296 ? -1.881  4.049   74.749 1.00 50.11  ? 309 LEU B N   1 
ATOM   4916 C  CA  . LEU B  1  296 ? -1.095  5.056   74.039 1.00 48.55  ? 309 LEU B CA  1 
ATOM   4917 C  C   . LEU B  1  296 ? -1.922  6.310   73.766 1.00 46.63  ? 309 LEU B C   1 
ATOM   4918 O  O   . LEU B  1  296 ? -1.390  7.422   73.771 1.00 43.20  ? 309 LEU B O   1 
ATOM   4919 C  CB  . LEU B  1  296 ? -0.564  4.520   72.706 1.00 49.17  ? 309 LEU B CB  1 
ATOM   4920 C  CG  . LEU B  1  296 ? 0.448   3.377   72.765 1.00 48.32  ? 309 LEU B CG  1 
ATOM   4921 C  CD1 . LEU B  1  296 ? 0.634   2.837   71.360 1.00 47.45  ? 309 LEU B CD1 1 
ATOM   4922 C  CD2 . LEU B  1  296 ? 1.767   3.851   73.370 1.00 47.75  ? 309 LEU B CD2 1 
ATOM   4923 N  N   . TYR B  1  297 ? -3.205  6.111   73.445 1.00 48.46  ? 310 TYR B N   1 
ATOM   4924 C  CA  . TYR B  1  297 ? -4.089  7.208   73.088 1.00 52.78  ? 310 TYR B CA  1 
ATOM   4925 C  C   . TYR B  1  297 ? -5.316  7.196   74.000 1.00 56.11  ? 310 TYR B C   1 
ATOM   4926 O  O   . TYR B  1  297 ? -6.386  6.746   73.599 1.00 50.07  ? 310 TYR B O   1 
ATOM   4927 C  CB  . TYR B  1  297 ? -4.463  7.043   71.620 1.00 48.58  ? 310 TYR B CB  1 
ATOM   4928 C  CG  . TYR B  1  297 ? -3.285  7.165   70.673 1.00 46.56  ? 310 TYR B CG  1 
ATOM   4929 C  CD1 . TYR B  1  297 ? -2.793  8.409   70.299 1.00 47.35  ? 310 TYR B CD1 1 
ATOM   4930 C  CD2 . TYR B  1  297 ? -2.705  6.035   70.113 1.00 45.78  ? 310 TYR B CD2 1 
ATOM   4931 C  CE1 . TYR B  1  297 ? -1.738  8.525   69.410 1.00 46.82  ? 310 TYR B CE1 1 
ATOM   4932 C  CE2 . TYR B  1  297 ? -1.644  6.139   69.229 1.00 46.58  ? 310 TYR B CE2 1 
ATOM   4933 C  CZ  . TYR B  1  297 ? -1.168  7.386   68.868 1.00 45.79  ? 310 TYR B CZ  1 
ATOM   4934 O  OH  . TYR B  1  297 ? -0.131  7.489   67.997 1.00 42.90  ? 310 TYR B OH  1 
ATOM   4935 N  N   . PRO B  1  298 ? -5.190  7.645   75.270 1.00 56.10  ? 311 PRO B N   1 
ATOM   4936 C  CA  . PRO B  1  298 ? -6.284  7.510   76.235 1.00 55.26  ? 311 PRO B CA  1 
ATOM   4937 C  C   . PRO B  1  298 ? -7.486  8.415   75.971 1.00 55.84  ? 311 PRO B C   1 
ATOM   4938 O  O   . PRO B  1  298 ? -8.602  8.035   76.294 1.00 54.70  ? 311 PRO B O   1 
ATOM   4939 C  CB  . PRO B  1  298 ? -5.637  7.776   77.597 1.00 53.84  ? 311 PRO B CB  1 
ATOM   4940 C  CG  . PRO B  1  298 ? -4.385  8.569   77.274 1.00 57.80  ? 311 PRO B CG  1 
ATOM   4941 C  CD  . PRO B  1  298 ? -3.982  8.259   75.836 1.00 58.08  ? 311 PRO B CD  1 
ATOM   4942 N  N   . ASN B  1  299 ? -7.269  9.566   75.320 1.00 56.49  ? 312 ASN B N   1 
ATOM   4943 C  CA  . ASN B  1  299 ? -8.322  10.543  75.114 1.00 57.82  ? 312 ASN B CA  1 
ATOM   4944 C  C   . ASN B  1  299 ? -7.993  11.432  73.915 1.00 54.47  ? 312 ASN B C   1 
ATOM   4945 O  O   . ASN B  1  299 ? -7.871  12.645  74.045 1.00 55.48  ? 312 ASN B O   1 
ATOM   4946 C  CB  . ASN B  1  299 ? -8.538  11.371  76.377 1.00 65.64  ? 312 ASN B CB  1 
ATOM   4947 C  CG  . ASN B  1  299 ? -9.297  10.654  77.469 1.00 77.14  ? 312 ASN B CG  1 
ATOM   4948 O  OD1 . ASN B  1  299 ? -10.280 9.943   77.195 1.00 91.30  ? 312 ASN B OD1 1 
ATOM   4949 N  ND2 . ASN B  1  299 ? -8.873  10.847  78.716 1.00 82.41  ? 312 ASN B ND2 1 
ATOM   4950 N  N   . PRO B  1  300 ? -7.895  10.882  72.686 1.00 54.83  ? 313 PRO B N   1 
ATOM   4951 C  CA  . PRO B  1  300 ? -7.597  11.697  71.503 1.00 58.62  ? 313 PRO B CA  1 
ATOM   4952 C  C   . PRO B  1  300 ? -8.803  12.516  71.049 1.00 66.16  ? 313 PRO B C   1 
ATOM   4953 O  O   . PRO B  1  300 ? -9.939  12.097  71.294 1.00 69.84  ? 313 PRO B O   1 
ATOM   4954 C  CB  . PRO B  1  300 ? -7.241  10.600  70.489 1.00 59.22  ? 313 PRO B CB  1 
ATOM   4955 C  CG  . PRO B  1  300 ? -8.170  9.442   70.855 1.00 56.95  ? 313 PRO B CG  1 
ATOM   4956 C  CD  . PRO B  1  300 ? -8.125  9.460   72.373 1.00 57.55  ? 313 PRO B CD  1 
ATOM   4957 N  N   . THR B  1  301 ? -8.577  13.641  70.350 1.00 69.55  ? 314 THR B N   1 
ATOM   4958 C  CA  . THR B  1  301 ? -9.673  14.582  70.141 1.00 75.89  ? 314 THR B CA  1 
ATOM   4959 C  C   . THR B  1  301 ? -9.927  14.934  68.675 1.00 71.38  ? 314 THR B C   1 
ATOM   4960 O  O   . THR B  1  301 ? -11.076 15.170  68.325 1.00 88.86  ? 314 THR B O   1 
ATOM   4961 C  CB  . THR B  1  301 ? -9.485  15.861  70.968 1.00 77.67  ? 314 THR B CB  1 
ATOM   4962 O  OG1 . THR B  1  301 ? -8.193  16.390  70.675 1.00 74.82  ? 314 THR B OG1 1 
ATOM   4963 C  CG2 . THR B  1  301 ? -9.619  15.630  72.463 1.00 77.46  ? 314 THR B CG2 1 
ATOM   4964 N  N   . GLY B  1  302 ? -8.914  15.043  67.827 1.00 57.11  ? 315 GLY B N   1 
ATOM   4965 C  CA  . GLY B  1  302 ? -9.145  15.809  66.613 1.00 61.17  ? 315 GLY B CA  1 
ATOM   4966 C  C   . GLY B  1  302 ? -9.114  14.943  65.357 1.00 67.68  ? 315 GLY B C   1 
ATOM   4967 O  O   . GLY B  1  302 ? -9.845  13.948  65.236 1.00 61.04  ? 315 GLY B O   1 
ATOM   4968 N  N   . ILE B  1  303 ? -8.238  15.367  64.434 1.00 70.25  ? 316 ILE B N   1 
ATOM   4969 C  CA  . ILE B  1  303 ? -7.815  14.570  63.296 1.00 67.52  ? 316 ILE B CA  1 
ATOM   4970 C  C   . ILE B  1  303 ? -7.216  13.259  63.810 1.00 57.88  ? 316 ILE B C   1 
ATOM   4971 O  O   . ILE B  1  303 ? -7.356  12.222  63.176 1.00 53.90  ? 316 ILE B O   1 
ATOM   4972 C  CB  . ILE B  1  303 ? -6.832  15.376  62.423 1.00 78.47  ? 316 ILE B CB  1 
ATOM   4973 C  CG1 . ILE B  1  303 ? -7.460  16.691  61.916 1.00 98.40  ? 316 ILE B CG1 1 
ATOM   4974 C  CG2 . ILE B  1  303 ? -6.324  14.538  61.254 1.00 74.44  ? 316 ILE B CG2 1 
ATOM   4975 C  CD1 . ILE B  1  303 ? -6.461  17.756  61.483 1.00 100.08 ? 316 ILE B CD1 1 
ATOM   4976 N  N   . LEU B  1  304 ? -6.560  13.302  64.971 1.00 53.23  ? 317 LEU B N   1 
ATOM   4977 C  CA  . LEU B  1  304 ? -5.968  12.113  65.555 1.00 50.42  ? 317 LEU B CA  1 
ATOM   4978 C  C   . LEU B  1  304 ? -7.036  11.087  65.927 1.00 53.04  ? 317 LEU B C   1 
ATOM   4979 O  O   . LEU B  1  304 ? -6.825  9.900   65.705 1.00 51.36  ? 317 LEU B O   1 
ATOM   4980 C  CB  . LEU B  1  304 ? -5.116  12.515  66.761 1.00 48.20  ? 317 LEU B CB  1 
ATOM   4981 C  CG  . LEU B  1  304 ? -4.544  11.364  67.592 1.00 48.32  ? 317 LEU B CG  1 
ATOM   4982 C  CD1 . LEU B  1  304 ? -3.606  10.546  66.746 1.00 46.62  ? 317 LEU B CD1 1 
ATOM   4983 C  CD2 . LEU B  1  304 ? -3.845  11.890  68.834 1.00 51.05  ? 317 LEU B CD2 1 
ATOM   4984 N  N   . ARG B  1  305 ? -8.159  11.540  66.513 1.00 53.52  ? 318 ARG B N   1 
ATOM   4985 C  CA  . ARG B  1  305 ? -9.246  10.652  66.890 1.00 49.85  ? 318 ARG B CA  1 
ATOM   4986 C  C   . ARG B  1  305 ? -9.799  9.999   65.627 1.00 44.88  ? 318 ARG B C   1 
ATOM   4987 O  O   . ARG B  1  305 ? -10.016 8.784   65.570 1.00 44.61  ? 318 ARG B O   1 
ATOM   4988 C  CB  . ARG B  1  305 ? -10.354 11.401  67.652 1.00 53.27  ? 318 ARG B CB  1 
ATOM   4989 C  CG  . ARG B  1  305 ? -11.576 10.533  67.990 1.00 54.84  ? 318 ARG B CG  1 
ATOM   4990 C  CD  . ARG B  1  305 ? -12.624 11.119  68.952 1.00 53.87  ? 318 ARG B CD  1 
ATOM   4991 N  NE  . ARG B  1  305 ? -12.306 10.841  70.365 1.00 55.32  ? 318 ARG B NE  1 
ATOM   4992 C  CZ  . ARG B  1  305 ? -12.873 9.930   71.175 1.00 50.02  ? 318 ARG B CZ  1 
ATOM   4993 N  NH1 . ARG B  1  305 ? -12.354 9.700   72.372 1.00 53.89  ? 318 ARG B NH1 1 
ATOM   4994 N  NH2 . ARG B  1  305 ? -13.902 9.192   70.794 1.00 45.28  ? 318 ARG B NH2 1 
ATOM   4995 N  N   . ARG B  1  306 ? -10.036 10.830  64.619 1.00 43.97  ? 319 ARG B N   1 
ATOM   4996 C  CA  . ARG B  1  306 ? -10.635 10.362  63.382 1.00 51.59  ? 319 ARG B CA  1 
ATOM   4997 C  C   . ARG B  1  306 ? -9.756  9.280   62.746 1.00 48.33  ? 319 ARG B C   1 
ATOM   4998 O  O   . ARG B  1  306 ? -10.256 8.235   62.324 1.00 50.98  ? 319 ARG B O   1 
ATOM   4999 C  CB  . ARG B  1  306 ? -10.853 11.591  62.493 1.00 62.82  ? 319 ARG B CB  1 
ATOM   5000 C  CG  . ARG B  1  306 ? -11.661 11.350  61.229 1.00 80.62  ? 319 ARG B CG  1 
ATOM   5001 C  CD  . ARG B  1  306 ? -11.489 12.465  60.192 1.00 93.30  ? 319 ARG B CD  1 
ATOM   5002 N  NE  . ARG B  1  306 ? -10.146 12.455  59.595 1.00 111.16 ? 319 ARG B NE  1 
ATOM   5003 C  CZ  . ARG B  1  306 ? -9.726  13.236  58.607 1.00 115.31 ? 319 ARG B CZ  1 
ATOM   5004 N  NH1 . ARG B  1  306 ? -10.517 14.195  58.151 1.00 121.57 ? 319 ARG B NH1 1 
ATOM   5005 N  NH2 . ARG B  1  306 ? -8.484  13.119  58.159 1.00 115.31 ? 319 ARG B NH2 1 
ATOM   5006 N  N   . ASN B  1  307 ? -8.442  9.522   62.702 1.00 45.95  ? 320 ASN B N   1 
ATOM   5007 C  CA  . ASN B  1  307 ? -7.523  8.622   62.022 1.00 48.62  ? 320 ASN B CA  1 
ATOM   5008 C  C   . ASN B  1  307 ? -7.320  7.335   62.820 1.00 48.21  ? 320 ASN B C   1 
ATOM   5009 O  O   . ASN B  1  307 ? -7.079  6.295   62.215 1.00 40.21  ? 320 ASN B O   1 
ATOM   5010 C  CB  . ASN B  1  307 ? -6.213  9.315   61.665 1.00 47.26  ? 320 ASN B CB  1 
ATOM   5011 C  CG  . ASN B  1  307 ? -6.397  10.301  60.539 1.00 48.98  ? 320 ASN B CG  1 
ATOM   5012 O  OD1 . ASN B  1  307 ? -7.508  10.437  60.011 1.00 55.90  ? 320 ASN B OD1 1 
ATOM   5013 N  ND2 . ASN B  1  307 ? -5.321  10.984  60.161 1.00 51.02  ? 320 ASN B ND2 1 
ATOM   5014 N  N   . LEU B  1  308 ? -7.428  7.394   64.154 1.00 47.36  ? 321 LEU B N   1 
ATOM   5015 C  CA  . LEU B  1  308 ? -7.410  6.195   64.983 1.00 49.08  ? 321 LEU B CA  1 
ATOM   5016 C  C   . LEU B  1  308 ? -8.581  5.277   64.639 1.00 48.11  ? 321 LEU B C   1 
ATOM   5017 O  O   . LEU B  1  308 ? -8.430  4.057   64.556 1.00 47.88  ? 321 LEU B O   1 
ATOM   5018 C  CB  . LEU B  1  308 ? -7.451  6.550   66.464 1.00 51.93  ? 321 LEU B CB  1 
ATOM   5019 C  CG  . LEU B  1  308 ? -6.096  6.671   67.162 1.00 54.91  ? 321 LEU B CG  1 
ATOM   5020 C  CD1 . LEU B  1  308 ? -6.252  7.362   68.498 1.00 60.20  ? 321 LEU B CD1 1 
ATOM   5021 C  CD2 . LEU B  1  308 ? -5.485  5.306   67.355 1.00 54.92  ? 321 LEU B CD2 1 
ATOM   5022 N  N   . ILE B  1  309 ? -9.761  5.867   64.485 1.00 49.00  ? 322 ILE B N   1 
ATOM   5023 C  CA  . ILE B  1  309 ? -10.958 5.093   64.221 1.00 48.84  ? 322 ILE B CA  1 
ATOM   5024 C  C   . ILE B  1  309 ? -10.802 4.368   62.884 1.00 46.11  ? 322 ILE B C   1 
ATOM   5025 O  O   . ILE B  1  309 ? -11.128 3.191   62.762 1.00 50.17  ? 322 ILE B O   1 
ATOM   5026 C  CB  . ILE B  1  309 ? -12.200 5.998   64.263 1.00 47.44  ? 322 ILE B CB  1 
ATOM   5027 C  CG1 . ILE B  1  309 ? -12.505 6.436   65.688 1.00 48.60  ? 322 ILE B CG1 1 
ATOM   5028 C  CG2 . ILE B  1  309 ? -13.387 5.290   63.623 1.00 47.20  ? 322 ILE B CG2 1 
ATOM   5029 C  CD1 . ILE B  1  309 ? -13.420 7.640   65.810 1.00 48.36  ? 322 ILE B CD1 1 
ATOM   5030 N  N   . LYS B  1  310 ? -10.294 5.086   61.886 1.00 46.05  ? 323 LYS B N   1 
ATOM   5031 C  CA  . LYS B  1  310 ? -10.113 4.533   60.551 1.00 48.90  ? 323 LYS B CA  1 
ATOM   5032 C  C   . LYS B  1  310 ? -9.039  3.436   60.520 1.00 44.19  ? 323 LYS B C   1 
ATOM   5033 O  O   . LYS B  1  310 ? -9.267  2.364   59.964 1.00 38.00  ? 323 LYS B O   1 
ATOM   5034 C  CB  . LYS B  1  310 ? -9.769  5.652   59.567 1.00 51.11  ? 323 LYS B CB  1 
ATOM   5035 C  CG  . LYS B  1  310 ? -10.947 6.510   59.165 1.00 58.65  ? 323 LYS B CG  1 
ATOM   5036 C  CD  . LYS B  1  310 ? -10.515 7.732   58.363 1.00 63.17  ? 323 LYS B CD  1 
ATOM   5037 C  CE  . LYS B  1  310 ? -11.615 8.355   57.573 1.00 65.75  ? 323 LYS B CE  1 
ATOM   5038 N  NZ  . LYS B  1  310 ? -11.158 9.676   57.139 1.00 69.21  ? 323 LYS B NZ  1 
ATOM   5039 N  N   . ASN B  1  311 ? -7.875  3.705   61.127 1.00 40.19  ? 324 ASN B N   1 
ATOM   5040 C  CA  . ASN B  1  311 ? -6.775  2.758   61.133 1.00 37.70  ? 324 ASN B CA  1 
ATOM   5041 C  C   . ASN B  1  311 ? -7.186  1.487   61.870 1.00 37.77  ? 324 ASN B C   1 
ATOM   5042 O  O   . ASN B  1  311 ? -6.817  0.393   61.454 1.00 41.96  ? 324 ASN B O   1 
ATOM   5043 C  CB  . ASN B  1  311 ? -5.489  3.392   61.647 1.00 36.64  ? 324 ASN B CB  1 
ATOM   5044 C  CG  . ASN B  1  311 ? -4.753  4.138   60.553 1.00 38.19  ? 324 ASN B CG  1 
ATOM   5045 O  OD1 . ASN B  1  311 ? -4.095  3.513   59.714 1.00 42.40  ? 324 ASN B OD1 1 
ATOM   5046 N  ND2 . ASN B  1  311 ? -4.820  5.462   60.544 1.00 36.40  ? 324 ASN B ND2 1 
ATOM   5047 N  N   . LEU B  1  312 ? -7.969  1.617   62.942 1.00 37.55  ? 325 LEU B N   1 
ATOM   5048 C  CA  . LEU B  1  312 ? -8.425  0.445   63.673 1.00 38.13  ? 325 LEU B CA  1 
ATOM   5049 C  C   . LEU B  1  312 ? -9.357  -0.387  62.796 1.00 38.84  ? 325 LEU B C   1 
ATOM   5050 O  O   . LEU B  1  312 ? -9.301  -1.614  62.825 1.00 39.54  ? 325 LEU B O   1 
ATOM   5051 C  CB  . LEU B  1  312 ? -9.114  0.855   64.973 1.00 42.02  ? 325 LEU B CB  1 
ATOM   5052 C  CG  . LEU B  1  312 ? -8.191  1.218   66.140 1.00 39.64  ? 325 LEU B CG  1 
ATOM   5053 C  CD1 . LEU B  1  312 ? -8.940  2.019   67.171 1.00 42.76  ? 325 LEU B CD1 1 
ATOM   5054 C  CD2 . LEU B  1  312 ? -7.621  -0.030  66.779 1.00 37.95  ? 325 LEU B CD2 1 
ATOM   5055 N  N   . HIS B  1  313 ? -10.230 0.292   62.040 1.00 39.43  ? 326 HIS B N   1 
ATOM   5056 C  CA  . HIS B  1  313 ? -11.141 -0.387  61.136 1.00 39.33  ? 326 HIS B CA  1 
ATOM   5057 C  C   . HIS B  1  313 ? -10.339 -1.100  60.038 1.00 39.43  ? 326 HIS B C   1 
ATOM   5058 O  O   . HIS B  1  313 ? -10.571 -2.276  59.747 1.00 40.08  ? 326 HIS B O   1 
ATOM   5059 C  CB  . HIS B  1  313 ? -12.226 0.569   60.606 1.00 39.28  ? 326 HIS B CB  1 
ATOM   5060 C  CG  . HIS B  1  313 ? -13.164 -0.137  59.691 1.00 39.29  ? 326 HIS B CG  1 
ATOM   5061 N  ND1 . HIS B  1  313 ? -13.971 -1.163  60.148 1.00 39.87  ? 326 HIS B ND1 1 
ATOM   5062 C  CD2 . HIS B  1  313 ? -13.334 -0.071  58.361 1.00 36.41  ? 326 HIS B CD2 1 
ATOM   5063 C  CE1 . HIS B  1  313 ? -14.610 -1.688  59.115 1.00 41.02  ? 326 HIS B CE1 1 
ATOM   5064 N  NE2 . HIS B  1  313 ? -14.234 -1.037  58.023 1.00 38.53  ? 326 HIS B NE2 1 
ATOM   5065 N  N   . TYR B  1  314 ? -9.381  -0.393  59.429 1.00 35.48  ? 327 TYR B N   1 
ATOM   5066 C  CA  . TYR B  1  314 ? -8.541  -1.004  58.407 1.00 36.91  ? 327 TYR B CA  1 
ATOM   5067 C  C   . TYR B  1  314 ? -7.861  -2.270  58.933 1.00 35.09  ? 327 TYR B C   1 
ATOM   5068 O  O   . TYR B  1  314 ? -7.854  -3.291  58.250 1.00 31.38  ? 327 TYR B O   1 
ATOM   5069 C  CB  . TYR B  1  314 ? -7.474  -0.019  57.949 1.00 38.26  ? 327 TYR B CB  1 
ATOM   5070 C  CG  . TYR B  1  314 ? -7.999  1.249   57.298 1.00 39.02  ? 327 TYR B CG  1 
ATOM   5071 C  CD1 . TYR B  1  314 ? -9.273  1.302   56.740 1.00 40.72  ? 327 TYR B CD1 1 
ATOM   5072 C  CD2 . TYR B  1  314 ? -7.214  2.392   57.249 1.00 38.40  ? 327 TYR B CD2 1 
ATOM   5073 C  CE1 . TYR B  1  314 ? -9.750  2.458   56.146 1.00 40.92  ? 327 TYR B CE1 1 
ATOM   5074 C  CE2 . TYR B  1  314 ? -7.679  3.556   56.661 1.00 42.65  ? 327 TYR B CE2 1 
ATOM   5075 C  CZ  . TYR B  1  314 ? -8.948  3.585   56.105 1.00 42.29  ? 327 TYR B CZ  1 
ATOM   5076 O  OH  . TYR B  1  314 ? -9.382  4.732   55.509 1.00 43.55  ? 327 TYR B OH  1 
ATOM   5077 N  N   . TRP B  1  315 ? -7.306  -2.209  60.148 1.00 33.08  ? 328 TRP B N   1 
ATOM   5078 C  CA  . TRP B  1  315 ? -6.639  -3.365  60.719 1.00 34.87  ? 328 TRP B CA  1 
ATOM   5079 C  C   . TRP B  1  315 ? -7.626  -4.522  60.830 1.00 35.13  ? 328 TRP B C   1 
ATOM   5080 O  O   . TRP B  1  315 ? -7.321  -5.653  60.458 1.00 39.28  ? 328 TRP B O   1 
ATOM   5081 C  CB  . TRP B  1  315 ? -6.005  -3.030  62.078 1.00 36.62  ? 328 TRP B CB  1 
ATOM   5082 C  CG  . TRP B  1  315 ? -5.070  -4.096  62.608 1.00 37.95  ? 328 TRP B CG  1 
ATOM   5083 C  CD1 . TRP B  1  315 ? -4.083  -4.753  61.931 1.00 36.02  ? 328 TRP B CD1 1 
ATOM   5084 C  CD2 . TRP B  1  315 ? -5.051  -4.635  63.948 1.00 37.62  ? 328 TRP B CD2 1 
ATOM   5085 N  NE1 . TRP B  1  315 ? -3.466  -5.663  62.743 1.00 37.39  ? 328 TRP B NE1 1 
ATOM   5086 C  CE2 . TRP B  1  315 ? -4.030  -5.611  63.987 1.00 38.83  ? 328 TRP B CE2 1 
ATOM   5087 C  CE3 . TRP B  1  315 ? -5.775  -4.373  65.115 1.00 39.87  ? 328 TRP B CE3 1 
ATOM   5088 C  CZ2 . TRP B  1  315 ? -3.730  -6.332  65.140 1.00 39.44  ? 328 TRP B CZ2 1 
ATOM   5089 C  CZ3 . TRP B  1  315 ? -5.473  -5.079  66.258 1.00 41.01  ? 328 TRP B CZ3 1 
ATOM   5090 C  CH2 . TRP B  1  315 ? -4.459  -6.041  66.271 1.00 40.16  ? 328 TRP B CH2 1 
ATOM   5091 N  N   . TRP B  1  316 ? -8.818  -4.226  61.341 1.00 36.97  ? 329 TRP B N   1 
ATOM   5092 C  CA  . TRP B  1  316 ? -9.813  -5.254  61.572 1.00 34.02  ? 329 TRP B CA  1 
ATOM   5093 C  C   . TRP B  1  316 ? -10.145 -5.982  60.267 1.00 32.40  ? 329 TRP B C   1 
ATOM   5094 O  O   . TRP B  1  316 ? -10.362 -7.196  60.288 1.00 32.53  ? 329 TRP B O   1 
ATOM   5095 C  CB  . TRP B  1  316 ? -11.074 -4.667  62.233 1.00 33.49  ? 329 TRP B CB  1 
ATOM   5096 C  CG  . TRP B  1  316 ? -12.156 -5.702  62.348 1.00 34.27  ? 329 TRP B CG  1 
ATOM   5097 C  CD1 . TRP B  1  316 ? -12.275 -6.645  63.319 1.00 34.39  ? 329 TRP B CD1 1 
ATOM   5098 C  CD2 . TRP B  1  316 ? -13.209 -5.959  61.396 1.00 36.73  ? 329 TRP B CD2 1 
ATOM   5099 N  NE1 . TRP B  1  316 ? -13.342 -7.456  63.059 1.00 36.74  ? 329 TRP B NE1 1 
ATOM   5100 C  CE2 . TRP B  1  316 ? -13.935 -7.063  61.890 1.00 37.27  ? 329 TRP B CE2 1 
ATOM   5101 C  CE3 . TRP B  1  316 ? -13.611 -5.361  60.194 1.00 39.80  ? 329 TRP B CE3 1 
ATOM   5102 C  CZ2 . TRP B  1  316 ? -15.043 -7.586  61.225 1.00 39.71  ? 329 TRP B CZ2 1 
ATOM   5103 C  CZ3 . TRP B  1  316 ? -14.713 -5.878  59.540 1.00 40.61  ? 329 TRP B CZ3 1 
ATOM   5104 C  CH2 . TRP B  1  316 ? -15.407 -6.986  60.041 1.00 38.89  ? 329 TRP B CH2 1 
ATOM   5105 N  N   . THR B  1  317 ? -10.193 -5.267  59.133 1.00 33.10  ? 330 THR B N   1 
ATOM   5106 C  CA  . THR B  1  317 ? -10.565 -5.916  57.876 1.00 40.30  ? 330 THR B CA  1 
ATOM   5107 C  C   . THR B  1  317 ? -9.606  -7.068  57.581 1.00 36.90  ? 330 THR B C   1 
ATOM   5108 O  O   . THR B  1  317 ? -10.016 -8.086  57.045 1.00 43.50  ? 330 THR B O   1 
ATOM   5109 C  CB  . THR B  1  317 ? -10.612 -4.975  56.669 1.00 39.88  ? 330 THR B CB  1 
ATOM   5110 O  OG1 . THR B  1  317 ? -9.301  -4.485  56.412 1.00 42.46  ? 330 THR B OG1 1 
ATOM   5111 C  CG2 . THR B  1  317 ? -11.552 -3.802  56.877 1.00 41.72  ? 330 THR B CG2 1 
ATOM   5112 N  N   . GLY B  1  318 ? -8.329  -6.889  57.914 1.00 35.54  ? 331 GLY B N   1 
ATOM   5113 C  CA  . GLY B  1  318 ? -7.346  -7.939  57.727 1.00 34.96  ? 331 GLY B CA  1 
ATOM   5114 C  C   . GLY B  1  318 ? -7.453  -9.016  58.798 1.00 34.34  ? 331 GLY B C   1 
ATOM   5115 O  O   . GLY B  1  318 ? -7.439  -10.202 58.480 1.00 35.48  ? 331 GLY B O   1 
ATOM   5116 N  N   . VAL B  1  319 ? -7.528  -8.586  60.063 1.00 35.06  ? 332 VAL B N   1 
ATOM   5117 C  CA  . VAL B  1  319 ? -7.568  -9.491  61.201 1.00 36.15  ? 332 VAL B CA  1 
ATOM   5118 C  C   . VAL B  1  319 ? -8.726  -10.467 61.061 1.00 35.51  ? 332 VAL B C   1 
ATOM   5119 O  O   . VAL B  1  319 ? -8.578  -11.648 61.382 1.00 40.66  ? 332 VAL B O   1 
ATOM   5120 C  CB  . VAL B  1  319 ? -7.676  -8.677  62.499 1.00 38.97  ? 332 VAL B CB  1 
ATOM   5121 C  CG1 . VAL B  1  319 ? -8.161  -9.513  63.668 1.00 42.70  ? 332 VAL B CG1 1 
ATOM   5122 C  CG2 . VAL B  1  319 ? -6.352  -8.037  62.858 1.00 40.59  ? 332 VAL B CG2 1 
ATOM   5123 N  N   . ASN B  1  320 ? -9.872  -9.951  60.604 1.00 35.75  ? 333 ASN B N   1 
ATOM   5124 C  CA  . ASN B  1  320 ? -11.094 -10.728 60.536 1.00 41.20  ? 333 ASN B CA  1 
ATOM   5125 C  C   . ASN B  1  320 ? -10.901 -11.968 59.667 1.00 43.09  ? 333 ASN B C   1 
ATOM   5126 O  O   . ASN B  1  320 ? -11.304 -13.065 60.062 1.00 41.88  ? 333 ASN B O   1 
ATOM   5127 C  CB  . ASN B  1  320 ? -12.263 -9.891  60.031 1.00 45.19  ? 333 ASN B CB  1 
ATOM   5128 C  CG  . ASN B  1  320 ? -13.583 -10.592 60.254 1.00 47.13  ? 333 ASN B CG  1 
ATOM   5129 O  OD1 . ASN B  1  320 ? -13.833 -11.120 61.340 1.00 49.94  ? 333 ASN B OD1 1 
ATOM   5130 N  ND2 . ASN B  1  320 ? -14.433 -10.633 59.246 1.00 50.27  ? 333 ASN B ND2 1 
ATOM   5131 N  N   . VAL B  1  321 ? -10.285 -11.769 58.493 1.00 42.99  ? 334 VAL B N   1 
ATOM   5132 C  CA  . VAL B  1  321 ? -10.008 -12.860 57.572 1.00 43.52  ? 334 VAL B CA  1 
ATOM   5133 C  C   . VAL B  1  321 ? -8.871  -13.721 58.119 1.00 44.51  ? 334 VAL B C   1 
ATOM   5134 O  O   . VAL B  1  321 ? -8.973  -14.939 58.136 1.00 48.02  ? 334 VAL B O   1 
ATOM   5135 C  CB  . VAL B  1  321 ? -9.646  -12.389 56.151 1.00 44.21  ? 334 VAL B CB  1 
ATOM   5136 C  CG1 . VAL B  1  321 ? -9.424  -13.582 55.231 1.00 41.82  ? 334 VAL B CG1 1 
ATOM   5137 C  CG2 . VAL B  1  321 ? -10.684 -11.438 55.566 1.00 43.70  ? 334 VAL B CG2 1 
ATOM   5138 N  N   . ALA B  1  322 ? -7.776  -13.092 58.545 1.00 46.75  ? 335 ALA B N   1 
ATOM   5139 C  CA  . ALA B  1  322 ? -6.573  -13.833 58.890 1.00 46.98  ? 335 ALA B CA  1 
ATOM   5140 C  C   . ALA B  1  322 ? -6.779  -14.697 60.132 1.00 49.30  ? 335 ALA B C   1 
ATOM   5141 O  O   . ALA B  1  322 ? -6.212  -15.782 60.208 1.00 52.43  ? 335 ALA B O   1 
ATOM   5142 C  CB  . ALA B  1  322 ? -5.415  -12.885 59.089 1.00 48.16  ? 335 ALA B CB  1 
ATOM   5143 N  N   . PHE B  1  323 ? -7.562  -14.214 61.110 1.00 49.73  ? 336 PHE B N   1 
ATOM   5144 C  CA  . PHE B  1  323 ? -7.727  -14.932 62.366 1.00 50.92  ? 336 PHE B CA  1 
ATOM   5145 C  C   . PHE B  1  323 ? -9.003  -15.776 62.387 1.00 53.87  ? 336 PHE B C   1 
ATOM   5146 O  O   . PHE B  1  323 ? -9.299  -16.395 63.405 1.00 54.04  ? 336 PHE B O   1 
ATOM   5147 C  CB  . PHE B  1  323 ? -7.732  -13.975 63.557 1.00 47.90  ? 336 PHE B CB  1 
ATOM   5148 C  CG  . PHE B  1  323 ? -6.433  -13.235 63.834 1.00 47.75  ? 336 PHE B CG  1 
ATOM   5149 C  CD1 . PHE B  1  323 ? -5.296  -13.433 63.060 1.00 51.09  ? 336 PHE B CD1 1 
ATOM   5150 C  CD2 . PHE B  1  323 ? -6.344  -12.353 64.907 1.00 45.12  ? 336 PHE B CD2 1 
ATOM   5151 C  CE1 . PHE B  1  323 ? -4.127  -12.729 63.332 1.00 50.36  ? 336 PHE B CE1 1 
ATOM   5152 C  CE2 . PHE B  1  323 ? -5.172  -11.661 65.175 1.00 44.20  ? 336 PHE B CE2 1 
ATOM   5153 C  CZ  . PHE B  1  323 ? -4.067  -11.845 64.384 1.00 46.23  ? 336 PHE B CZ  1 
ATOM   5154 N  N   . GLY B  1  324 ? -9.759  -15.799 61.282 1.00 54.53  ? 337 GLY B N   1 
ATOM   5155 C  CA  . GLY B  1  324 ? -10.914 -16.678 61.156 1.00 54.45  ? 337 GLY B CA  1 
ATOM   5156 C  C   . GLY B  1  324 ? -12.155 -16.163 61.889 1.00 55.24  ? 337 GLY B C   1 
ATOM   5157 O  O   . GLY B  1  324 ? -12.972 -16.974 62.325 1.00 56.75  ? 337 GLY B O   1 
ATOM   5158 N  N   . GLY B  1  325 ? -12.298 -14.830 62.000 1.00 54.21  ? 338 GLY B N   1 
ATOM   5159 C  CA  . GLY B  1  325 ? -13.493 -14.187 62.538 1.00 50.35  ? 338 GLY B CA  1 
ATOM   5160 C  C   . GLY B  1  325 ? -13.266 -13.622 63.942 1.00 49.39  ? 338 GLY B C   1 
ATOM   5161 O  O   . GLY B  1  325 ? -13.098 -14.392 64.881 1.00 44.70  ? 338 GLY B O   1 
ATOM   5162 N  N   . CYS B  1  326 ? -13.242 -12.285 64.077 1.00 50.13  ? 339 CYS B N   1 
ATOM   5163 C  CA  . CYS B  1  326 ? -13.184 -11.620 65.378 1.00 56.50  ? 339 CYS B CA  1 
ATOM   5164 C  C   . CYS B  1  326 ? -14.216 -10.496 65.425 1.00 56.86  ? 339 CYS B C   1 
ATOM   5165 O  O   . CYS B  1  326 ? -14.423 -9.804  64.428 1.00 53.02  ? 339 CYS B O   1 
ATOM   5166 C  CB  . CYS B  1  326 ? -11.848 -10.931 65.662 1.00 61.08  ? 339 CYS B CB  1 
ATOM   5167 S  SG  . CYS B  1  326 ? -10.425 -12.033 65.878 1.00 80.84  ? 339 CYS B SG  1 
ATOM   5168 N  N   . ASP B  1  327 ? -14.834 -10.300 66.596 1.00 53.74  ? 340 ASP B N   1 
ATOM   5169 C  CA  . ASP B  1  327 ? -15.807 -9.234  66.775 1.00 57.17  ? 340 ASP B CA  1 
ATOM   5170 C  C   . ASP B  1  327 ? -15.086 -7.891  66.831 1.00 47.78  ? 340 ASP B C   1 
ATOM   5171 O  O   . ASP B  1  327 ? -14.211 -7.701  67.666 1.00 45.78  ? 340 ASP B O   1 
ATOM   5172 C  CB  . ASP B  1  327 ? -16.671 -9.444  68.011 1.00 63.80  ? 340 ASP B CB  1 
ATOM   5173 C  CG  . ASP B  1  327 ? -17.566 -10.678 67.967 1.00 68.91  ? 340 ASP B CG  1 
ATOM   5174 O  OD1 . ASP B  1  327 ? -18.265 -10.858 66.946 1.00 77.42  ? 340 ASP B OD1 1 
ATOM   5175 O  OD2 . ASP B  1  327 ? -17.564 -11.452 68.948 1.00 62.41  ? 340 ASP B OD2 1 
ATOM   5176 N  N   . GLU B  1  328 ? -15.465 -6.970  65.941 1.00 42.87  ? 341 GLU B N   1 
ATOM   5177 C  CA  . GLU B  1  328 ? -14.813 -5.677  65.858 1.00 40.90  ? 341 GLU B CA  1 
ATOM   5178 C  C   . GLU B  1  328 ? -15.106 -4.859  67.115 1.00 39.00  ? 341 GLU B C   1 
ATOM   5179 O  O   . GLU B  1  328 ? -16.242 -4.791  67.543 1.00 39.30  ? 341 GLU B O   1 
ATOM   5180 C  CB  . GLU B  1  328 ? -15.235 -4.948  64.583 1.00 41.00  ? 341 GLU B CB  1 
ATOM   5181 C  CG  . GLU B  1  328 ? -14.507 -3.617  64.391 1.00 43.44  ? 341 GLU B CG  1 
ATOM   5182 C  CD  . GLU B  1  328 ? -14.739 -2.902  63.075 1.00 46.10  ? 341 GLU B CD  1 
ATOM   5183 O  OE1 . GLU B  1  328 ? -15.564 -3.391  62.253 1.00 48.27  ? 341 GLU B OE1 1 
ATOM   5184 O  OE2 . GLU B  1  328 ? -14.054 -1.858  62.882 1.00 45.77  ? 341 GLU B OE2 1 
ATOM   5185 N  N   . LEU B  1  329 ? -14.058 -4.249  67.683 1.00 38.75  ? 342 LEU B N   1 
ATOM   5186 C  CA  . LEU B  1  329 ? -14.164 -3.338  68.809 1.00 41.56  ? 342 LEU B CA  1 
ATOM   5187 C  C   . LEU B  1  329 ? -14.093 -1.900  68.304 1.00 40.37  ? 342 LEU B C   1 
ATOM   5188 O  O   . LEU B  1  329 ? -13.433 -1.631  67.312 1.00 41.14  ? 342 LEU B O   1 
ATOM   5189 C  CB  . LEU B  1  329 ? -13.023 -3.616  69.787 1.00 45.75  ? 342 LEU B CB  1 
ATOM   5190 C  CG  . LEU B  1  329 ? -12.974 -5.026  70.385 1.00 49.93  ? 342 LEU B CG  1 
ATOM   5191 C  CD1 . LEU B  1  329 ? -11.690 -5.236  71.169 1.00 49.34  ? 342 LEU B CD1 1 
ATOM   5192 C  CD2 . LEU B  1  329 ? -14.216 -5.350  71.229 1.00 49.43  ? 342 LEU B CD2 1 
ATOM   5193 N  N   . PHE B  1  330 ? -14.742 -0.974  69.015 1.00 43.13  ? 343 PHE B N   1 
ATOM   5194 C  CA  . PHE B  1  330 ? -14.812 0.427   68.618 1.00 44.03  ? 343 PHE B CA  1 
ATOM   5195 C  C   . PHE B  1  330 ? -14.497 1.302   69.828 1.00 48.33  ? 343 PHE B C   1 
ATOM   5196 O  O   . PHE B  1  330 ? -15.356 2.004   70.358 1.00 48.06  ? 343 PHE B O   1 
ATOM   5197 C  CB  . PHE B  1  330 ? -16.207 0.789   68.105 1.00 44.37  ? 343 PHE B CB  1 
ATOM   5198 C  CG  . PHE B  1  330 ? -16.697 -0.072  66.960 1.00 40.23  ? 343 PHE B CG  1 
ATOM   5199 C  CD1 . PHE B  1  330 ? -16.368 0.262   65.655 1.00 40.95  ? 343 PHE B CD1 1 
ATOM   5200 C  CD2 . PHE B  1  330 ? -17.465 -1.209  67.193 1.00 41.10  ? 343 PHE B CD2 1 
ATOM   5201 C  CE1 . PHE B  1  330 ? -16.823 -0.511  64.602 1.00 40.12  ? 343 PHE B CE1 1 
ATOM   5202 C  CE2 . PHE B  1  330 ? -17.917 -1.981  66.135 1.00 43.57  ? 343 PHE B CE2 1 
ATOM   5203 C  CZ  . PHE B  1  330 ? -17.584 -1.635  64.842 1.00 42.57  ? 343 PHE B CZ  1 
ATOM   5204 N  N   . PRO B  1  331 ? -13.240 1.302   70.312 1.00 51.78  ? 344 PRO B N   1 
ATOM   5205 C  CA  . PRO B  1  331 ? -12.917 2.013   71.544 1.00 53.53  ? 344 PRO B CA  1 
ATOM   5206 C  C   . PRO B  1  331 ? -13.065 3.529   71.496 1.00 48.97  ? 344 PRO B C   1 
ATOM   5207 O  O   . PRO B  1  331 ? -13.032 4.164   72.543 1.00 57.66  ? 344 PRO B O   1 
ATOM   5208 C  CB  . PRO B  1  331 ? -11.466 1.566   71.745 1.00 55.27  ? 344 PRO B CB  1 
ATOM   5209 C  CG  . PRO B  1  331 ? -10.950 1.404   70.350 1.00 53.64  ? 344 PRO B CG  1 
ATOM   5210 C  CD  . PRO B  1  331 ? -12.078 0.640   69.705 1.00 50.81  ? 344 PRO B CD  1 
ATOM   5211 N  N   . TYR B  1  332 ? -13.216 4.107   70.302 1.00 45.02  ? 345 TYR B N   1 
ATOM   5212 C  CA  . TYR B  1  332 ? -13.424 5.544   70.186 1.00 48.45  ? 345 TYR B CA  1 
ATOM   5213 C  C   . TYR B  1  332 ? -14.729 5.834   69.450 1.00 49.17  ? 345 TYR B C   1 
ATOM   5214 O  O   . TYR B  1  332 ? -14.938 6.953   68.980 1.00 57.55  ? 345 TYR B O   1 
ATOM   5215 C  CB  . TYR B  1  332 ? -12.245 6.220   69.479 1.00 51.71  ? 345 TYR B CB  1 
ATOM   5216 C  CG  . TYR B  1  332 ? -10.904 5.888   70.105 1.00 50.16  ? 345 TYR B CG  1 
ATOM   5217 C  CD1 . TYR B  1  332 ? -10.544 6.449   71.318 1.00 50.18  ? 345 TYR B CD1 1 
ATOM   5218 C  CD2 . TYR B  1  332 ? -10.009 5.015   69.496 1.00 53.05  ? 345 TYR B CD2 1 
ATOM   5219 C  CE1 . TYR B  1  332 ? -9.328  6.160   71.910 1.00 53.90  ? 345 TYR B CE1 1 
ATOM   5220 C  CE2 . TYR B  1  332 ? -8.790  4.716   70.078 1.00 55.80  ? 345 TYR B CE2 1 
ATOM   5221 C  CZ  . TYR B  1  332 ? -8.449  5.290   71.288 1.00 56.09  ? 345 TYR B CZ  1 
ATOM   5222 O  OH  . TYR B  1  332 ? -7.248  4.976   71.849 1.00 53.87  ? 345 TYR B OH  1 
ATOM   5223 N  N   . GLY B  1  333 ? -15.598 4.819   69.367 1.00 50.11  ? 346 GLY B N   1 
ATOM   5224 C  CA  . GLY B  1  333 ? -16.858 4.927   68.649 1.00 51.37  ? 346 GLY B CA  1 
ATOM   5225 C  C   . GLY B  1  333 ? -16.664 4.957   67.133 1.00 56.03  ? 346 GLY B C   1 
ATOM   5226 O  O   . GLY B  1  333 ? -15.591 4.606   66.636 1.00 60.71  ? 346 GLY B O   1 
ATOM   5227 N  N   . GLN B  1  334 ? -17.741 5.336   66.423 1.00 58.67  ? 347 GLN B N   1 
ATOM   5228 C  CA  A GLN B  1  334 ? -17.776 5.357   64.969 0.50 59.32  ? 347 GLN B CA  1 
ATOM   5229 C  CA  B GLN B  1  334 ? -17.773 5.353   64.966 0.50 57.24  ? 347 GLN B CA  1 
ATOM   5230 C  C   . GLN B  1  334 ? -17.662 6.790   64.467 1.00 59.87  ? 347 GLN B C   1 
ATOM   5231 O  O   . GLN B  1  334 ? -17.748 7.720   65.251 1.00 65.51  ? 347 GLN B O   1 
ATOM   5232 C  CB  A GLN B  1  334 ? -19.051 4.658   64.500 0.50 60.28  ? 347 GLN B CB  1 
ATOM   5233 C  CB  B GLN B  1  334 ? -19.030 4.639   64.470 0.50 55.26  ? 347 GLN B CB  1 
ATOM   5234 C  CG  A GLN B  1  334 ? -18.871 3.149   64.407 0.50 61.66  ? 347 GLN B CG  1 
ATOM   5235 C  CG  B GLN B  1  334 ? -18.959 3.125   64.653 0.50 53.63  ? 347 GLN B CG  1 
ATOM   5236 C  CD  A GLN B  1  334 ? -18.372 2.732   63.038 0.50 63.01  ? 347 GLN B CD  1 
ATOM   5237 C  CD  B GLN B  1  334 ? -20.291 2.425   64.526 0.50 51.00  ? 347 GLN B CD  1 
ATOM   5238 O  OE1 A GLN B  1  334 ? -17.392 3.277   62.505 0.50 64.51  ? 347 GLN B OE1 1 
ATOM   5239 O  OE1 B GLN B  1  334 ? -21.333 3.051   64.313 0.50 51.52  ? 347 GLN B OE1 1 
ATOM   5240 N  NE2 A GLN B  1  334 ? -19.066 1.774   62.440 0.50 59.10  ? 347 GLN B NE2 1 
ATOM   5241 N  NE2 B GLN B  1  334 ? -20.262 1.107   64.654 0.50 50.56  ? 347 GLN B NE2 1 
ATOM   5242 N  N   . LEU B  1  335 ? -17.464 6.932   63.145 1.00 70.49  ? 348 LEU B N   1 
ATOM   5243 C  CA  . LEU B  1  335 ? -17.241 8.218   62.487 1.00 80.84  ? 348 LEU B CA  1 
ATOM   5244 C  C   . LEU B  1  335 ? -18.522 8.820   61.857 1.00 79.40  ? 348 LEU B C   1 
ATOM   5245 O  O   . LEU B  1  335 ? -19.651 8.429   62.205 1.00 75.57  ? 348 LEU B O   1 
ATOM   5246 C  CB  . LEU B  1  335 ? -16.177 8.074   61.390 1.00 80.29  ? 348 LEU B CB  1 
ATOM   5247 C  CG  . LEU B  1  335 ? -14.715 8.265   61.808 1.00 89.20  ? 348 LEU B CG  1 
ATOM   5248 C  CD1 . LEU B  1  335 ? -13.849 8.320   60.560 1.00 83.60  ? 348 LEU B CD1 1 
ATOM   5249 C  CD2 . LEU B  1  335 ? -14.461 9.506   62.676 1.00 93.98  ? 348 LEU B CD2 1 
ATOM   5250 N  N   . GLN C  1  1   ? 2.508   -17.419 26.081 1.00 139.95 ? 14  GLN C N   1 
ATOM   5251 C  CA  . GLN C  1  1   ? 2.879   -16.021 26.438 1.00 135.33 ? 14  GLN C CA  1 
ATOM   5252 C  C   . GLN C  1  1   ? 2.954   -15.177 25.156 1.00 123.97 ? 14  GLN C C   1 
ATOM   5253 O  O   . GLN C  1  1   ? 2.034   -14.412 24.865 1.00 109.86 ? 14  GLN C O   1 
ATOM   5254 C  CB  . GLN C  1  1   ? 4.102   -16.001 27.374 1.00 132.05 ? 14  GLN C CB  1 
ATOM   5255 C  CG  . GLN C  1  1   ? 5.490   -16.192 26.755 1.00 126.35 ? 14  GLN C CG  1 
ATOM   5256 C  CD  . GLN C  1  1   ? 5.752   -17.573 26.187 1.00 125.44 ? 14  GLN C CD  1 
ATOM   5257 O  OE1 . GLN C  1  1   ? 5.101   -18.558 26.552 1.00 127.91 ? 14  GLN C OE1 1 
ATOM   5258 N  NE2 . GLN C  1  1   ? 6.728   -17.661 25.293 1.00 113.22 ? 14  GLN C NE2 1 
ATOM   5259 N  N   . GLY C  1  2   ? 4.011   -15.382 24.357 1.00 104.83 ? 15  GLY C N   1 
ATOM   5260 C  CA  . GLY C  1  2   ? 4.502   -14.383 23.421 1.00 85.11  ? 15  GLY C CA  1 
ATOM   5261 C  C   . GLY C  1  2   ? 3.990   -14.615 22.006 1.00 69.04  ? 15  GLY C C   1 
ATOM   5262 O  O   . GLY C  1  2   ? 3.645   -15.723 21.621 1.00 62.90  ? 15  GLY C O   1 
ATOM   5263 N  N   . VAL C  1  3   ? 4.022   -13.547 21.211 1.00 60.99  ? 16  VAL C N   1 
ATOM   5264 C  CA  . VAL C  1  3   ? 3.439   -13.525 19.883 1.00 59.50  ? 16  VAL C CA  1 
ATOM   5265 C  C   . VAL C  1  3   ? 4.479   -12.951 18.930 1.00 57.91  ? 16  VAL C C   1 
ATOM   5266 O  O   . VAL C  1  3   ? 5.304   -12.145 19.338 1.00 57.13  ? 16  VAL C O   1 
ATOM   5267 C  CB  . VAL C  1  3   ? 2.156   -12.668 19.926 1.00 63.45  ? 16  VAL C CB  1 
ATOM   5268 C  CG1 . VAL C  1  3   ? 1.538   -12.456 18.552 1.00 64.65  ? 16  VAL C CG1 1 
ATOM   5269 C  CG2 . VAL C  1  3   ? 1.112   -13.256 20.872 1.00 67.24  ? 16  VAL C CG2 1 
ATOM   5270 N  N   . ASP C  1  4   ? 4.431   -13.377 17.665 1.00 62.39  ? 17  ASP C N   1 
ATOM   5271 C  CA  . ASP C  1  4   ? 5.283   -12.829 16.623 1.00 61.81  ? 17  ASP C CA  1 
ATOM   5272 C  C   . ASP C  1  4   ? 4.490   -11.787 15.828 1.00 58.12  ? 17  ASP C C   1 
ATOM   5273 O  O   . ASP C  1  4   ? 3.582   -12.156 15.089 1.00 62.08  ? 17  ASP C O   1 
ATOM   5274 C  CB  . ASP C  1  4   ? 5.816   -13.950 15.747 1.00 70.46  ? 17  ASP C CB  1 
ATOM   5275 C  CG  . ASP C  1  4   ? 7.091   -13.608 14.987 1.00 84.94  ? 17  ASP C CG  1 
ATOM   5276 O  OD1 . ASP C  1  4   ? 7.229   -12.442 14.554 1.00 90.61  ? 17  ASP C OD1 1 
ATOM   5277 O  OD2 . ASP C  1  4   ? 7.937   -14.507 14.835 1.00 93.38  ? 17  ASP C OD2 1 
ATOM   5278 N  N   . PRO C  1  5   ? 4.780   -10.465 15.936 1.00 52.84  ? 18  PRO C N   1 
ATOM   5279 C  CA  . PRO C  1  5   ? 3.884   -9.437  15.395 1.00 53.25  ? 18  PRO C CA  1 
ATOM   5280 C  C   . PRO C  1  5   ? 3.995   -9.234  13.882 1.00 53.75  ? 18  PRO C C   1 
ATOM   5281 O  O   . PRO C  1  5   ? 5.077   -8.954  13.364 1.00 45.34  ? 18  PRO C O   1 
ATOM   5282 C  CB  . PRO C  1  5   ? 4.257   -8.157  16.160 1.00 54.62  ? 18  PRO C CB  1 
ATOM   5283 C  CG  . PRO C  1  5   ? 5.605   -8.453  16.833 1.00 53.34  ? 18  PRO C CG  1 
ATOM   5284 C  CD  . PRO C  1  5   ? 5.990   -9.889  16.539 1.00 51.37  ? 18  PRO C CD  1 
ATOM   5285 N  N   . PRO C  1  6   ? 2.864   -9.311  13.142 1.00 55.96  ? 19  PRO C N   1 
ATOM   5286 C  CA  . PRO C  1  6   ? 2.885   -9.184  11.685 1.00 53.23  ? 19  PRO C CA  1 
ATOM   5287 C  C   . PRO C  1  6   ? 3.179   -7.741  11.300 1.00 47.95  ? 19  PRO C C   1 
ATOM   5288 O  O   . PRO C  1  6   ? 2.977   -6.827  12.095 1.00 47.83  ? 19  PRO C O   1 
ATOM   5289 C  CB  . PRO C  1  6   ? 1.492   -9.610  11.209 1.00 52.79  ? 19  PRO C CB  1 
ATOM   5290 C  CG  . PRO C  1  6   ? 0.604   -9.518  12.439 1.00 55.73  ? 19  PRO C CG  1 
ATOM   5291 C  CD  . PRO C  1  6   ? 1.500   -9.457  13.675 1.00 56.07  ? 19  PRO C CD  1 
ATOM   5292 N  N   . PRO C  1  7   ? 3.660   -7.485  10.071 1.00 42.55  ? 20  PRO C N   1 
ATOM   5293 C  CA  . PRO C  1  7   ? 3.790   -6.112  9.592  1.00 40.13  ? 20  PRO C CA  1 
ATOM   5294 C  C   . PRO C  1  7   ? 2.408   -5.484  9.422  1.00 37.26  ? 20  PRO C C   1 
ATOM   5295 O  O   . PRO C  1  7   ? 1.399   -6.175  9.324  1.00 34.67  ? 20  PRO C O   1 
ATOM   5296 C  CB  . PRO C  1  7   ? 4.580   -6.238  8.283  1.00 42.03  ? 20  PRO C CB  1 
ATOM   5297 C  CG  . PRO C  1  7   ? 4.325   -7.665  7.837  1.00 45.27  ? 20  PRO C CG  1 
ATOM   5298 C  CD  . PRO C  1  7   ? 4.125   -8.487  9.105  1.00 44.63  ? 20  PRO C CD  1 
ATOM   5299 N  N   . PRO C  1  8   ? 2.302   -4.139  9.443  1.00 34.98  ? 21  PRO C N   1 
ATOM   5300 C  CA  . PRO C  1  8   ? 1.015   -3.478  9.337  1.00 33.00  ? 21  PRO C CA  1 
ATOM   5301 C  C   . PRO C  1  8   ? 0.372   -3.736  7.982  1.00 37.11  ? 21  PRO C C   1 
ATOM   5302 O  O   . PRO C  1  8   ? 1.045   -3.837  6.959  1.00 41.29  ? 21  PRO C O   1 
ATOM   5303 C  CB  . PRO C  1  8   ? 1.353   -2.007  9.519  1.00 34.37  ? 21  PRO C CB  1 
ATOM   5304 C  CG  . PRO C  1  8   ? 2.795   -1.904  9.134  1.00 36.74  ? 21  PRO C CG  1 
ATOM   5305 C  CD  . PRO C  1  8   ? 3.414   -3.194  9.580  1.00 37.49  ? 21  PRO C CD  1 
ATOM   5306 N  N   . PRO C  1  9   ? -0.966  -3.805  7.934  1.00 36.69  ? 22  PRO C N   1 
ATOM   5307 C  CA  . PRO C  1  9   ? -1.685  -3.839  6.665  1.00 35.89  ? 22  PRO C CA  1 
ATOM   5308 C  C   . PRO C  1  9   ? -1.320  -2.641  5.797  1.00 34.21  ? 22  PRO C C   1 
ATOM   5309 O  O   . PRO C  1  9   ? -0.958  -1.588  6.324  1.00 32.50  ? 22  PRO C O   1 
ATOM   5310 C  CB  . PRO C  1  9   ? -3.167  -3.797  7.089  1.00 36.72  ? 22  PRO C CB  1 
ATOM   5311 C  CG  . PRO C  1  9   ? -3.166  -4.286  8.524  1.00 38.29  ? 22  PRO C CG  1 
ATOM   5312 C  CD  . PRO C  1  9   ? -1.851  -3.836  9.101  1.00 37.36  ? 22  PRO C CD  1 
ATOM   5313 N  N   . GLY C  1  10  ? -1.456  -2.812  4.471  1.00 31.31  ? 23  GLY C N   1 
ATOM   5314 C  CA  . GLY C  1  10  ? -1.361  -1.698  3.546  1.00 31.62  ? 23  GLY C CA  1 
ATOM   5315 C  C   . GLY C  1  10  ? -2.715  -1.011  3.373  1.00 34.90  ? 23  GLY C C   1 
ATOM   5316 O  O   . GLY C  1  10  ? -3.661  -1.291  4.115  1.00 32.51  ? 23  GLY C O   1 
ATOM   5317 N  N   . PRO C  1  11  ? -2.853  -0.073  2.403  1.00 38.85  ? 24  PRO C N   1 
ATOM   5318 C  CA  . PRO C  1  11  ? -4.133  0.594   2.144  1.00 41.94  ? 24  PRO C CA  1 
ATOM   5319 C  C   . PRO C  1  11  ? -5.205  -0.429  1.786  1.00 40.33  ? 24  PRO C C   1 
ATOM   5320 O  O   . PRO C  1  11  ? -4.879  -1.521  1.324  1.00 38.30  ? 24  PRO C O   1 
ATOM   5321 C  CB  . PRO C  1  11  ? -3.832  1.562   0.991  1.00 38.40  ? 24  PRO C CB  1 
ATOM   5322 C  CG  . PRO C  1  11  ? -2.336  1.767   1.064  1.00 35.31  ? 24  PRO C CG  1 
ATOM   5323 C  CD  . PRO C  1  11  ? -1.784  0.431   1.528  1.00 35.94  ? 24  PRO C CD  1 
ATOM   5324 N  N   . PRO C  1  12  ? -6.502  -0.125  2.015  1.00 41.13  ? 25  PRO C N   1 
ATOM   5325 C  CA  . PRO C  1  12  ? -7.566  -1.071  1.658  1.00 42.88  ? 25  PRO C CA  1 
ATOM   5326 C  C   . PRO C  1  12  ? -7.705  -1.169  0.143  1.00 40.25  ? 25  PRO C C   1 
ATOM   5327 O  O   . PRO C  1  12  ? -7.363  -0.216  -0.562 1.00 42.24  ? 25  PRO C O   1 
ATOM   5328 C  CB  . PRO C  1  12  ? -8.810  -0.477  2.337  1.00 43.80  ? 25  PRO C CB  1 
ATOM   5329 C  CG  . PRO C  1  12  ? -8.502  1.017   2.458  1.00 42.58  ? 25  PRO C CG  1 
ATOM   5330 C  CD  . PRO C  1  12  ? -6.993  1.135   2.607  1.00 39.18  ? 25  PRO C CD  1 
ATOM   5331 N  N   . SER C  1  13  ? -8.177  -2.324  -0.353 1.00 43.28  ? 26  SER C N   1 
ATOM   5332 C  CA  . SER C  1  13  ? -8.335  -2.554  -1.788 1.00 46.06  ? 26  SER C CA  1 
ATOM   5333 C  C   . SER C  1  13  ? -9.202  -1.471  -2.425 1.00 43.08  ? 26  SER C C   1 
ATOM   5334 O  O   . SER C  1  13  ? -8.838  -0.893  -3.452 1.00 44.26  ? 26  SER C O   1 
ATOM   5335 C  CB  . SER C  1  13  ? -8.942  -3.899  -2.060 1.00 46.31  ? 26  SER C CB  1 
ATOM   5336 O  OG  . SER C  1  13  ? -8.205  -4.906  -1.390 1.00 54.30  ? 26  SER C OG  1 
ATOM   5337 N  N   . PHE C  1  14  ? -10.355 -1.221  -1.789 1.00 41.63  ? 27  PHE C N   1 
ATOM   5338 C  CA  . PHE C  1  14  ? -11.314 -0.239  -2.256 1.00 41.68  ? 27  PHE C CA  1 
ATOM   5339 C  C   . PHE C  1  14  ? -11.209 0.995   -1.367 1.00 38.60  ? 27  PHE C C   1 
ATOM   5340 O  O   . PHE C  1  14  ? -11.286 0.860   -0.153 1.00 40.76  ? 27  PHE C O   1 
ATOM   5341 C  CB  . PHE C  1  14  ? -12.707 -0.888  -2.270 1.00 38.99  ? 27  PHE C CB  1 
ATOM   5342 C  CG  . PHE C  1  14  ? -13.790 0.104   -2.652 1.00 39.82  ? 27  PHE C CG  1 
ATOM   5343 C  CD1 . PHE C  1  14  ? -13.882 0.596   -3.955 1.00 37.64  ? 27  PHE C CD1 1 
ATOM   5344 C  CD2 . PHE C  1  14  ? -14.708 0.546   -1.702 1.00 40.37  ? 27  PHE C CD2 1 
ATOM   5345 C  CE1 . PHE C  1  14  ? -14.851 1.530   -4.287 1.00 35.89  ? 27  PHE C CE1 1 
ATOM   5346 C  CE2 . PHE C  1  14  ? -15.694 1.455   -2.050 1.00 41.89  ? 27  PHE C CE2 1 
ATOM   5347 C  CZ  . PHE C  1  14  ? -15.761 1.954   -3.342 1.00 38.31  ? 27  PHE C CZ  1 
ATOM   5348 N  N   . THR C  1  15  ? -11.032 2.184   -1.965 1.00 39.03  ? 28  THR C N   1 
ATOM   5349 C  CA  . THR C  1  15  ? -10.824 3.408   -1.195 1.00 37.08  ? 28  THR C CA  1 
ATOM   5350 C  C   . THR C  1  15  ? -11.914 4.444   -1.470 1.00 37.60  ? 28  THR C C   1 
ATOM   5351 O  O   . THR C  1  15  ? -11.714 5.609   -1.155 1.00 36.90  ? 28  THR C O   1 
ATOM   5352 C  CB  . THR C  1  15  ? -9.446  4.017   -1.490 1.00 40.03  ? 28  THR C CB  1 
ATOM   5353 O  OG1 . THR C  1  15  ? -9.400  4.534   -2.820 1.00 42.08  ? 28  THR C OG1 1 
ATOM   5354 C  CG2 . THR C  1  15  ? -8.293  3.056   -1.237 1.00 37.88  ? 28  THR C CG2 1 
ATOM   5355 N  N   . GLY C  1  16  ? -13.054 4.048   -2.052 1.00 38.45  ? 29  GLY C N   1 
ATOM   5356 C  CA  . GLY C  1  16  ? -14.179 4.960   -2.241 1.00 40.07  ? 29  GLY C CA  1 
ATOM   5357 C  C   . GLY C  1  16  ? -15.100 5.015   -1.015 1.00 45.53  ? 29  GLY C C   1 
ATOM   5358 O  O   . GLY C  1  16  ? -14.813 4.378   -0.007 1.00 43.52  ? 29  GLY C O   1 
ATOM   5359 N  N   . THR C  1  17  ? -16.205 5.784   -1.104 1.00 52.60  ? 30  THR C N   1 
ATOM   5360 C  CA  . THR C  1  17  ? -17.229 5.816   -0.060 1.00 53.36  ? 30  THR C CA  1 
ATOM   5361 C  C   . THR C  1  17  ? -17.939 4.480   -0.046 1.00 46.32  ? 30  THR C C   1 
ATOM   5362 O  O   . THR C  1  17  ? -17.946 3.760   -1.049 1.00 36.63  ? 30  THR C O   1 
ATOM   5363 C  CB  . THR C  1  17  ? -18.334 6.855   -0.238 1.00 59.30  ? 30  THR C CB  1 
ATOM   5364 O  OG1 . THR C  1  17  ? -18.907 6.505   -1.491 1.00 63.49  ? 30  THR C OG1 1 
ATOM   5365 C  CG2 . THR C  1  17  ? -17.848 8.279   -0.339 1.00 70.51  ? 30  THR C CG2 1 
ATOM   5366 N  N   . LYS C  1  18  ? -18.587 4.241   1.090  1.00 43.63  ? 31  LYS C N   1 
ATOM   5367 C  CA  . LYS C  1  18  ? -19.497 3.128   1.251  1.00 44.20  ? 31  LYS C CA  1 
ATOM   5368 C  C   . LYS C  1  18  ? -20.230 3.283   2.579  1.00 46.22  ? 31  LYS C C   1 
ATOM   5369 O  O   . LYS C  1  18  ? -19.827 4.076   3.429  1.00 41.40  ? 31  LYS C O   1 
ATOM   5370 C  CB  . LYS C  1  18  ? -18.761 1.789   1.192  1.00 45.06  ? 31  LYS C CB  1 
ATOM   5371 C  CG  . LYS C  1  18  ? -17.762 1.495   2.291  1.00 49.71  ? 31  LYS C CG  1 
ATOM   5372 C  CD  . LYS C  1  18  ? -17.287 0.048   2.149  1.00 56.80  ? 31  LYS C CD  1 
ATOM   5373 C  CE  . LYS C  1  18  ? -17.117 -0.670  3.442  1.00 65.01  ? 31  LYS C CE  1 
ATOM   5374 N  NZ  . LYS C  1  18  ? -16.251 -1.838  3.278  1.00 71.11  ? 31  LYS C NZ  1 
ATOM   5375 N  N   . LEU C  1  19  ? -21.338 2.553   2.714  1.00 47.44  ? 32  LEU C N   1 
ATOM   5376 C  CA  . LEU C  1  19  ? -22.075 2.509   3.960  1.00 46.41  ? 32  LEU C CA  1 
ATOM   5377 C  C   . LEU C  1  19  ? -21.229 1.744   4.964  1.00 42.61  ? 32  LEU C C   1 
ATOM   5378 O  O   . LEU C  1  19  ? -20.849 0.611   4.678  1.00 44.11  ? 32  LEU C O   1 
ATOM   5379 C  CB  . LEU C  1  19  ? -23.425 1.825   3.750  1.00 46.75  ? 32  LEU C CB  1 
ATOM   5380 C  CG  . LEU C  1  19  ? -24.257 1.592   5.017  1.00 45.93  ? 32  LEU C CG  1 
ATOM   5381 C  CD1 . LEU C  1  19  ? -24.805 2.903   5.556  1.00 43.81  ? 32  LEU C CD1 1 
ATOM   5382 C  CD2 . LEU C  1  19  ? -25.362 0.599   4.769  1.00 45.80  ? 32  LEU C CD2 1 
ATOM   5383 N  N   . VAL C  1  20  ? -20.950 2.361   6.122  1.00 41.02  ? 33  VAL C N   1 
ATOM   5384 C  CA  . VAL C  1  20  ? -20.139 1.701   7.141  1.00 44.27  ? 33  VAL C CA  1 
ATOM   5385 C  C   . VAL C  1  20  ? -21.006 1.337   8.342  1.00 43.26  ? 33  VAL C C   1 
ATOM   5386 O  O   . VAL C  1  20  ? -20.668 0.408   9.066  1.00 42.28  ? 33  VAL C O   1 
ATOM   5387 C  CB  . VAL C  1  20  ? -18.899 2.512   7.573  1.00 43.80  ? 33  VAL C CB  1 
ATOM   5388 C  CG1 . VAL C  1  20  ? -17.930 2.678   6.415  1.00 44.83  ? 33  VAL C CG1 1 
ATOM   5389 C  CG2 . VAL C  1  20  ? -19.250 3.870   8.167  1.00 41.51  ? 33  VAL C CG2 1 
ATOM   5390 N  N   . ASN C  1  21  ? -22.098 2.091   8.541  1.00 43.06  ? 34  ASN C N   1 
ATOM   5391 C  CA  . ASN C  1  21  ? -23.105 1.796   9.546  1.00 41.51  ? 34  ASN C CA  1 
ATOM   5392 C  C   . ASN C  1  21  ? -24.097 0.787   8.980  1.00 44.89  ? 34  ASN C C   1 
ATOM   5393 O  O   . ASN C  1  21  ? -25.209 1.159   8.634  1.00 47.77  ? 34  ASN C O   1 
ATOM   5394 C  CB  . ASN C  1  21  ? -23.821 3.079   9.954  1.00 38.91  ? 34  ASN C CB  1 
ATOM   5395 C  CG  . ASN C  1  21  ? -24.688 2.904   11.183 1.00 39.31  ? 34  ASN C CG  1 
ATOM   5396 O  OD1 . ASN C  1  21  ? -24.896 1.785   11.678 1.00 37.13  ? 34  ASN C OD1 1 
ATOM   5397 N  ND2 . ASN C  1  21  ? -25.217 4.012   11.682 1.00 35.71  ? 34  ASN C ND2 1 
ATOM   5398 N  N   . ASP C  1  22  ? -23.682 -0.476  8.875  1.00 47.87  ? 35  ASP C N   1 
ATOM   5399 C  CA  . ASP C  1  22  ? -24.406 -1.457  8.085  1.00 56.12  ? 35  ASP C CA  1 
ATOM   5400 C  C   . ASP C  1  22  ? -24.883 -2.581  9.001  1.00 56.68  ? 35  ASP C C   1 
ATOM   5401 O  O   . ASP C  1  22  ? -24.768 -2.483  10.213 1.00 60.26  ? 35  ASP C O   1 
ATOM   5402 C  CB  . ASP C  1  22  ? -23.586 -1.896  6.877  1.00 60.40  ? 35  ASP C CB  1 
ATOM   5403 C  CG  . ASP C  1  22  ? -22.293 -2.651  7.148  1.00 65.88  ? 35  ASP C CG  1 
ATOM   5404 O  OD1 . ASP C  1  22  ? -21.958 -2.865  8.327  1.00 84.32  ? 35  ASP C OD1 1 
ATOM   5405 O  OD2 . ASP C  1  22  ? -21.630 -3.040  6.174  1.00 69.80  ? 35  ASP C OD2 1 
ATOM   5406 N  N   . ALA C  1  23  ? -25.444 -3.638  8.409  1.00 61.89  ? 36  ALA C N   1 
ATOM   5407 C  CA  . ALA C  1  23  ? -26.113 -4.682  9.169  1.00 64.56  ? 36  ALA C CA  1 
ATOM   5408 C  C   . ALA C  1  23  ? -25.105 -5.489  9.980  1.00 62.84  ? 36  ALA C C   1 
ATOM   5409 O  O   . ALA C  1  23  ? -25.422 -5.951  11.075 1.00 64.18  ? 36  ALA C O   1 
ATOM   5410 C  CB  . ALA C  1  23  ? -26.893 -5.583  8.237  1.00 69.38  ? 36  ALA C CB  1 
ATOM   5411 N  N   . ASP C  1  24  ? -23.899 -5.652  9.431  1.00 58.95  ? 37  ASP C N   1 
ATOM   5412 C  CA  . ASP C  1  24  ? -22.866 -6.453  10.066 1.00 62.63  ? 37  ASP C CA  1 
ATOM   5413 C  C   . ASP C  1  24  ? -22.110 -5.672  11.145 1.00 51.97  ? 37  ASP C C   1 
ATOM   5414 O  O   . ASP C  1  24  ? -21.329 -6.268  11.867 1.00 45.10  ? 37  ASP C O   1 
ATOM   5415 C  CB  . ASP C  1  24  ? -21.869 -6.975  9.043  1.00 68.83  ? 37  ASP C CB  1 
ATOM   5416 C  CG  . ASP C  1  24  ? -22.352 -8.093  8.133  1.00 69.12  ? 37  ASP C CG  1 
ATOM   5417 O  OD1 . ASP C  1  24  ? -23.103 -8.964  8.614  1.00 78.06  ? 37  ASP C OD1 1 
ATOM   5418 O  OD2 . ASP C  1  24  ? -21.912 -8.121  6.973  1.00 67.44  ? 37  ASP C OD2 1 
ATOM   5419 N  N   . HIS C  1  25  ? -22.321 -4.351  11.237 1.00 48.70  ? 38  HIS C N   1 
ATOM   5420 C  CA  . HIS C  1  25  ? -21.603 -3.513  12.185 1.00 46.24  ? 38  HIS C CA  1 
ATOM   5421 C  C   . HIS C  1  25  ? -22.594 -2.684  12.998 1.00 41.35  ? 38  HIS C C   1 
ATOM   5422 O  O   . HIS C  1  25  ? -22.517 -1.451  13.045 1.00 35.93  ? 38  HIS C O   1 
ATOM   5423 C  CB  . HIS C  1  25  ? -20.555 -2.660  11.460 1.00 51.77  ? 38  HIS C CB  1 
ATOM   5424 C  CG  . HIS C  1  25  ? -19.516 -3.489  10.785 1.00 53.58  ? 38  HIS C CG  1 
ATOM   5425 N  ND1 . HIS C  1  25  ? -19.531 -3.764  9.435  1.00 53.67  ? 38  HIS C ND1 1 
ATOM   5426 C  CD2 . HIS C  1  25  ? -18.445 -4.122  11.288 1.00 54.48  ? 38  HIS C CD2 1 
ATOM   5427 C  CE1 . HIS C  1  25  ? -18.497 -4.542  9.147  1.00 57.38  ? 38  HIS C CE1 1 
ATOM   5428 N  NE2 . HIS C  1  25  ? -17.823 -4.771  10.254 1.00 51.79  ? 38  HIS C NE2 1 
ATOM   5429 N  N   . PRO C  1  26  ? -23.531 -3.344  13.716 1.00 42.98  ? 39  PRO C N   1 
ATOM   5430 C  CA  . PRO C  1  26  ? -24.522 -2.617  14.512 1.00 41.91  ? 39  PRO C CA  1 
ATOM   5431 C  C   . PRO C  1  26  ? -23.893 -1.979  15.750 1.00 44.31  ? 39  PRO C C   1 
ATOM   5432 O  O   . PRO C  1  26  ? -23.011 -2.577  16.366 1.00 41.16  ? 39  PRO C O   1 
ATOM   5433 C  CB  . PRO C  1  26  ? -25.508 -3.739  14.876 1.00 38.67  ? 39  PRO C CB  1 
ATOM   5434 C  CG  . PRO C  1  26  ? -24.637 -4.978  14.988 1.00 39.69  ? 39  PRO C CG  1 
ATOM   5435 C  CD  . PRO C  1  26  ? -23.655 -4.813  13.838 1.00 41.97  ? 39  PRO C CD  1 
ATOM   5436 N  N   . TRP C  1  27  ? -24.365 -0.783  16.122 1.00 42.82  ? 40  TRP C N   1 
ATOM   5437 C  CA  . TRP C  1  27  ? -24.069 -0.242  17.435 1.00 46.21  ? 40  TRP C CA  1 
ATOM   5438 C  C   . TRP C  1  27  ? -24.639 -1.161  18.517 1.00 44.45  ? 40  TRP C C   1 
ATOM   5439 O  O   . TRP C  1  27  ? -25.740 -1.674  18.389 1.00 50.73  ? 40  TRP C O   1 
ATOM   5440 C  CB  . TRP C  1  27  ? -24.626 1.183   17.564 1.00 51.97  ? 40  TRP C CB  1 
ATOM   5441 C  CG  . TRP C  1  27  ? -24.269 1.853   18.865 1.00 59.00  ? 40  TRP C CG  1 
ATOM   5442 C  CD1 . TRP C  1  27  ? -23.204 2.665   19.118 1.00 55.24  ? 40  TRP C CD1 1 
ATOM   5443 C  CD2 . TRP C  1  27  ? -24.991 1.753   20.111 1.00 63.88  ? 40  TRP C CD2 1 
ATOM   5444 N  NE1 . TRP C  1  27  ? -23.228 3.102   20.414 1.00 56.73  ? 40  TRP C NE1 1 
ATOM   5445 C  CE2 . TRP C  1  27  ? -24.301 2.548   21.054 1.00 64.21  ? 40  TRP C CE2 1 
ATOM   5446 C  CE3 . TRP C  1  27  ? -26.145 1.081   20.518 1.00 61.90  ? 40  TRP C CE3 1 
ATOM   5447 C  CZ2 . TRP C  1  27  ? -24.729 2.694   22.369 1.00 57.60  ? 40  TRP C CZ2 1 
ATOM   5448 C  CZ3 . TRP C  1  27  ? -26.556 1.208   21.822 1.00 61.47  ? 40  TRP C CZ3 1 
ATOM   5449 C  CH2 . TRP C  1  27  ? -25.858 2.005   22.732 1.00 59.72  ? 40  TRP C CH2 1 
ATOM   5450 N  N   . GLN C  1  28  ? -23.874 -1.367  19.586 1.00 44.11  ? 41  GLN C N   1 
ATOM   5451 C  CA  . GLN C  1  28  ? -24.332 -2.119  20.742 1.00 43.02  ? 41  GLN C CA  1 
ATOM   5452 C  C   . GLN C  1  28  ? -23.815 -1.463  22.012 1.00 43.31  ? 41  GLN C C   1 
ATOM   5453 O  O   . GLN C  1  28  ? -22.752 -0.858  22.008 1.00 42.68  ? 41  GLN C O   1 
ATOM   5454 C  CB  . GLN C  1  28  ? -23.845 -3.560  20.736 1.00 37.79  ? 41  GLN C CB  1 
ATOM   5455 C  CG  . GLN C  1  28  ? -24.391 -4.375  19.577 1.00 36.51  ? 41  GLN C CG  1 
ATOM   5456 C  CD  . GLN C  1  28  ? -23.867 -5.795  19.577 1.00 39.51  ? 41  GLN C CD  1 
ATOM   5457 O  OE1 . GLN C  1  28  ? -23.070 -6.201  20.431 1.00 41.67  ? 41  GLN C OE1 1 
ATOM   5458 N  NE2 . GLN C  1  28  ? -24.296 -6.568  18.589 1.00 43.38  ? 41  GLN C NE2 1 
ATOM   5459 N  N   . PRO C  1  29  ? -24.563 -1.556  23.128 1.00 49.27  ? 42  PRO C N   1 
ATOM   5460 C  CA  . PRO C  1  29  ? -24.142 -0.904  24.364 1.00 48.09  ? 42  PRO C CA  1 
ATOM   5461 C  C   . PRO C  1  29  ? -22.981 -1.634  25.012 1.00 42.28  ? 42  PRO C C   1 
ATOM   5462 O  O   . PRO C  1  29  ? -22.741 -2.815  24.745 1.00 40.17  ? 42  PRO C O   1 
ATOM   5463 C  CB  . PRO C  1  29  ? -25.401 -0.880  25.236 1.00 53.13  ? 42  PRO C CB  1 
ATOM   5464 C  CG  . PRO C  1  29  ? -26.256 -2.006  24.693 1.00 55.65  ? 42  PRO C CG  1 
ATOM   5465 C  CD  . PRO C  1  29  ? -25.854 -2.246  23.245 1.00 52.70  ? 42  PRO C CD  1 
ATOM   5466 N  N   . LEU C  1  30  ? -22.268 -0.890  25.856 1.00 41.75  ? 43  LEU C N   1 
ATOM   5467 C  CA  . LEU C  1  30  ? -21.128 -1.421  26.577 1.00 44.78  ? 43  LEU C CA  1 
ATOM   5468 C  C   . LEU C  1  30  ? -21.590 -2.511  27.534 1.00 43.69  ? 43  LEU C C   1 
ATOM   5469 O  O   . LEU C  1  30  ? -22.615 -2.359  28.193 1.00 42.79  ? 43  LEU C O   1 
ATOM   5470 C  CB  . LEU C  1  30  ? -20.484 -0.258  27.324 1.00 48.59  ? 43  LEU C CB  1 
ATOM   5471 C  CG  . LEU C  1  30  ? -19.939 0.879   26.453 1.00 50.32  ? 43  LEU C CG  1 
ATOM   5472 C  CD1 . LEU C  1  30  ? -19.543 2.084   27.289 1.00 46.34  ? 43  LEU C CD1 1 
ATOM   5473 C  CD2 . LEU C  1  30  ? -18.784 0.315   25.629 1.00 49.77  ? 43  LEU C CD2 1 
ATOM   5474 N  N   . ARG C  1  31  ? -20.824 -3.603  27.587 1.00 47.71  ? 44  ARG C N   1 
ATOM   5475 C  CA  . ARG C  1  31  ? -20.972 -4.606  28.627 1.00 48.25  ? 44  ARG C CA  1 
ATOM   5476 C  C   . ARG C  1  31  ? -19.940 -4.351  29.728 1.00 48.17  ? 44  ARG C C   1 
ATOM   5477 O  O   . ARG C  1  31  ? -18.972 -3.635  29.517 1.00 51.02  ? 44  ARG C O   1 
ATOM   5478 C  CB  . ARG C  1  31  ? -20.747 -6.018  28.079 1.00 50.73  ? 44  ARG C CB  1 
ATOM   5479 C  CG  . ARG C  1  31  ? -21.643 -6.486  26.942 1.00 54.14  ? 44  ARG C CG  1 
ATOM   5480 C  CD  . ARG C  1  31  ? -21.054 -7.701  26.250 1.00 58.99  ? 44  ARG C CD  1 
ATOM   5481 N  NE  . ARG C  1  31  ? -19.777 -7.283  25.651 1.00 77.17  ? 44  ARG C NE  1 
ATOM   5482 C  CZ  . ARG C  1  31  ? -18.922 -7.980  24.888 1.00 83.42  ? 44  ARG C CZ  1 
ATOM   5483 N  NH1 . ARG C  1  31  ? -19.211 -9.214  24.512 1.00 84.64  ? 44  ARG C NH1 1 
ATOM   5484 N  NH2 . ARG C  1  31  ? -17.774 -7.437  24.492 1.00 80.40  ? 44  ARG C NH2 1 
ATOM   5485 N  N   . GLU C  1  32  ? -20.177 -4.926  30.910 1.00 51.60  ? 45  GLU C N   1 
ATOM   5486 C  CA  . GLU C  1  32  ? -19.191 -5.009  31.977 1.00 53.06  ? 45  GLU C CA  1 
ATOM   5487 C  C   . GLU C  1  32  ? -17.828 -5.420  31.413 1.00 52.98  ? 45  GLU C C   1 
ATOM   5488 O  O   . GLU C  1  32  ? -17.704 -6.475  30.780 1.00 44.99  ? 45  GLU C O   1 
ATOM   5489 C  CB  . GLU C  1  32  ? -19.625 -6.037  33.033 1.00 53.06  ? 45  GLU C CB  1 
ATOM   5490 C  CG  . GLU C  1  32  ? -20.046 -5.414  34.362 1.00 57.18  ? 45  GLU C CG  1 
ATOM   5491 C  CD  . GLU C  1  32  ? -18.983 -4.544  35.016 1.00 53.54  ? 45  GLU C CD  1 
ATOM   5492 O  OE1 . GLU C  1  32  ? -17.874 -5.089  35.044 1.00 54.76  ? 45  GLU C OE1 1 
ATOM   5493 O  OE2 . GLU C  1  32  ? -19.206 -3.398  35.505 1.00 52.00  ? 45  GLU C OE2 1 
ATOM   5494 N  N   . GLY C  1  33  ? -16.812 -4.574  31.653 1.00 50.28  ? 46  GLY C N   1 
ATOM   5495 C  CA  . GLY C  1  33  ? -15.440 -4.912  31.313 1.00 53.98  ? 46  GLY C CA  1 
ATOM   5496 C  C   . GLY C  1  33  ? -14.996 -4.367  29.956 1.00 50.78  ? 46  GLY C C   1 
ATOM   5497 O  O   . GLY C  1  33  ? -13.816 -4.391  29.646 1.00 60.58  ? 46  GLY C O   1 
ATOM   5498 N  N   . ASP C  1  34  ? -15.940 -3.876  29.151 1.00 48.76  ? 47  ASP C N   1 
ATOM   5499 C  CA  . ASP C  1  34  ? -15.627 -3.242  27.882 1.00 46.71  ? 47  ASP C CA  1 
ATOM   5500 C  C   . ASP C  1  34  ? -14.893 -1.938  28.165 1.00 42.92  ? 47  ASP C C   1 
ATOM   5501 O  O   . ASP C  1  34  ? -15.219 -1.227  29.100 1.00 36.65  ? 47  ASP C O   1 
ATOM   5502 C  CB  . ASP C  1  34  ? -16.872 -3.002  27.040 1.00 46.44  ? 47  ASP C CB  1 
ATOM   5503 C  CG  . ASP C  1  34  ? -17.505 -4.245  26.424 1.00 51.79  ? 47  ASP C CG  1 
ATOM   5504 O  OD1 . ASP C  1  34  ? -16.959 -5.363  26.628 1.00 53.11  ? 47  ASP C OD1 1 
ATOM   5505 O  OD2 . ASP C  1  34  ? -18.538 -4.090  25.728 1.00 54.45  ? 47  ASP C OD2 1 
ATOM   5506 N  N   . ILE C  1  35  ? -13.912 -1.621  27.317 1.00 41.69  ? 48  ILE C N   1 
ATOM   5507 C  CA  . ILE C  1  35  ? -13.035 -0.499  27.576 1.00 40.37  ? 48  ILE C CA  1 
ATOM   5508 C  C   . ILE C  1  35  ? -13.194 0.518   26.457 1.00 38.57  ? 48  ILE C C   1 
ATOM   5509 O  O   . ILE C  1  35  ? -13.294 0.151   25.291 1.00 40.90  ? 48  ILE C O   1 
ATOM   5510 C  CB  . ILE C  1  35  ? -11.595 -0.993  27.744 1.00 45.43  ? 48  ILE C CB  1 
ATOM   5511 C  CG1 . ILE C  1  35  ? -11.413 -1.643  29.093 1.00 47.83  ? 48  ILE C CG1 1 
ATOM   5512 C  CG2 . ILE C  1  35  ? -10.591 0.133   27.535 1.00 49.54  ? 48  ILE C CG2 1 
ATOM   5513 C  CD1 . ILE C  1  35  ? -10.335 -2.716  29.114 1.00 53.77  ? 48  ILE C CD1 1 
ATOM   5514 N  N   . ARG C  1  36  ? -13.265 1.788   26.864 1.00 35.53  ? 49  ARG C N   1 
ATOM   5515 C  CA  . ARG C  1  36  ? -13.334 2.920   25.964 1.00 36.77  ? 49  ARG C CA  1 
ATOM   5516 C  C   . ARG C  1  36  ? -12.437 4.011   26.547 1.00 39.37  ? 49  ARG C C   1 
ATOM   5517 O  O   . ARG C  1  36  ? -12.106 3.943   27.736 1.00 40.58  ? 49  ARG C O   1 
ATOM   5518 C  CB  . ARG C  1  36  ? -14.799 3.353   25.841 1.00 37.62  ? 49  ARG C CB  1 
ATOM   5519 C  CG  . ARG C  1  36  ? -15.737 2.333   25.206 1.00 36.63  ? 49  ARG C CG  1 
ATOM   5520 C  CD  . ARG C  1  36  ? -15.494 2.142   23.717 1.00 33.64  ? 49  ARG C CD  1 
ATOM   5521 N  NE  . ARG C  1  36  ? -16.461 1.227   23.113 1.00 31.64  ? 49  ARG C NE  1 
ATOM   5522 C  CZ  . ARG C  1  36  ? -16.423 -0.099  23.224 1.00 31.38  ? 49  ARG C CZ  1 
ATOM   5523 N  NH1 . ARG C  1  36  ? -15.462 -0.696  23.903 1.00 30.29  ? 49  ARG C NH1 1 
ATOM   5524 N  NH2 . ARG C  1  36  ? -17.340 -0.841  22.631 1.00 30.19  ? 49  ARG C NH2 1 
ATOM   5525 N  N   . GLY C  1  37  ? -12.046 5.003   25.729 1.00 37.15  ? 50  GLY C N   1 
ATOM   5526 C  CA  . GLY C  1  37  ? -11.041 5.959   26.164 1.00 37.64  ? 50  GLY C CA  1 
ATOM   5527 C  C   . GLY C  1  37  ? -11.160 7.315   25.484 1.00 35.91  ? 50  GLY C C   1 
ATOM   5528 O  O   . GLY C  1  37  ? -12.239 7.758   25.147 1.00 36.97  ? 50  GLY C O   1 
ATOM   5529 N  N   . PRO C  1  38  ? -10.042 8.035   25.277 1.00 38.04  ? 51  PRO C N   1 
ATOM   5530 C  CA  . PRO C  1  38  ? -10.107 9.436   24.851 1.00 38.42  ? 51  PRO C CA  1 
ATOM   5531 C  C   . PRO C  1  38  ? -10.330 9.665   23.363 1.00 38.87  ? 51  PRO C C   1 
ATOM   5532 O  O   . PRO C  1  38  ? -10.492 10.823  22.979 1.00 34.55  ? 51  PRO C O   1 
ATOM   5533 C  CB  . PRO C  1  38  ? -8.737  9.947   25.263 1.00 38.24  ? 51  PRO C CB  1 
ATOM   5534 C  CG  . PRO C  1  38  ? -7.850  8.751   25.008 1.00 38.44  ? 51  PRO C CG  1 
ATOM   5535 C  CD  . PRO C  1  38  ? -8.669  7.533   25.428 1.00 37.06  ? 51  PRO C CD  1 
ATOM   5536 N  N   . CYS C  1  39  ? -10.296 8.583   22.552 1.00 39.92  ? 52  CYS C N   1 
ATOM   5537 C  CA  . CYS C  1  39  ? -10.445 8.693   21.103 1.00 37.23  ? 52  CYS C CA  1 
ATOM   5538 C  C   . CYS C  1  39  ? -11.866 8.340   20.663 1.00 34.26  ? 52  CYS C C   1 
ATOM   5539 O  O   . CYS C  1  39  ? -12.294 7.185   20.739 1.00 33.82  ? 52  CYS C O   1 
ATOM   5540 C  CB  . CYS C  1  39  ? -9.476  7.807   20.326 1.00 36.85  ? 52  CYS C CB  1 
ATOM   5541 S  SG  . CYS C  1  39  ? -9.588  8.046   18.530 1.00 39.05  ? 52  CYS C SG  1 
ATOM   5542 N  N   . PRO C  1  40  ? -12.628 9.323   20.139 1.00 33.10  ? 53  PRO C N   1 
ATOM   5543 C  CA  . PRO C  1  40  ? -13.985 9.071   19.656 1.00 35.41  ? 53  PRO C CA  1 
ATOM   5544 C  C   . PRO C  1  40  ? -14.010 8.178   18.417 1.00 38.84  ? 53  PRO C C   1 
ATOM   5545 O  O   . PRO C  1  40  ? -14.972 7.447   18.196 1.00 41.70  ? 53  PRO C O   1 
ATOM   5546 C  CB  . PRO C  1  40  ? -14.539 10.479  19.379 1.00 35.70  ? 53  PRO C CB  1 
ATOM   5547 C  CG  . PRO C  1  40  ? -13.323 11.354  19.167 1.00 34.18  ? 53  PRO C CG  1 
ATOM   5548 C  CD  . PRO C  1  40  ? -12.207 10.720  19.967 1.00 34.26  ? 53  PRO C CD  1 
ATOM   5549 N  N   . GLY C  1  41  ? -12.938 8.241   17.619 1.00 38.31  ? 54  GLY C N   1 
ATOM   5550 C  CA  . GLY C  1  41  ? -12.803 7.376   16.462 1.00 36.12  ? 54  GLY C CA  1 
ATOM   5551 C  C   . GLY C  1  41  ? -12.745 5.902   16.857 1.00 37.66  ? 54  GLY C C   1 
ATOM   5552 O  O   . GLY C  1  41  ? -13.569 5.105   16.422 1.00 35.10  ? 54  GLY C O   1 
ATOM   5553 N  N   . LEU C  1  42  ? -11.764 5.552   17.694 1.00 39.13  ? 55  LEU C N   1 
ATOM   5554 C  CA  . LEU C  1  42  ? -11.587 4.171   18.108 1.00 41.26  ? 55  LEU C CA  1 
ATOM   5555 C  C   . LEU C  1  42  ? -12.786 3.719   18.943 1.00 40.52  ? 55  LEU C C   1 
ATOM   5556 O  O   . LEU C  1  42  ? -13.203 2.562   18.871 1.00 39.69  ? 55  LEU C O   1 
ATOM   5557 C  CB  . LEU C  1  42  ? -10.281 4.022   18.884 1.00 44.40  ? 55  LEU C CB  1 
ATOM   5558 C  CG  . LEU C  1  42  ? -8.988  4.328   18.124 1.00 43.71  ? 55  LEU C CG  1 
ATOM   5559 C  CD1 . LEU C  1  42  ? -7.838  4.183   19.088 1.00 43.95  ? 55  LEU C CD1 1 
ATOM   5560 C  CD2 . LEU C  1  42  ? -8.784  3.432   16.931 1.00 42.12  ? 55  LEU C CD2 1 
ATOM   5561 N  N   . ASN C  1  43  ? -13.355 4.640   19.720 1.00 39.38  ? 56  ASN C N   1 
ATOM   5562 C  CA  . ASN C  1  43  ? -14.516 4.304   20.532 1.00 43.55  ? 56  ASN C CA  1 
ATOM   5563 C  C   . ASN C  1  43  ? -15.680 3.877   19.634 1.00 40.77  ? 56  ASN C C   1 
ATOM   5564 O  O   . ASN C  1  43  ? -16.302 2.845   19.876 1.00 37.42  ? 56  ASN C O   1 
ATOM   5565 C  CB  . ASN C  1  43  ? -14.911 5.451   21.455 1.00 43.67  ? 56  ASN C CB  1 
ATOM   5566 C  CG  . ASN C  1  43  ? -13.971 5.621   22.627 1.00 41.32  ? 56  ASN C CG  1 
ATOM   5567 O  OD1 . ASN C  1  43  ? -13.244 4.694   23.014 1.00 42.79  ? 56  ASN C OD1 1 
ATOM   5568 N  ND2 . ASN C  1  43  ? -13.988 6.809   23.212 1.00 41.32  ? 56  ASN C ND2 1 
ATOM   5569 N  N   . THR C  1  44  ? -15.939 4.653   18.575 1.00 36.85  ? 57  THR C N   1 
ATOM   5570 C  CA  . THR C  1  44  ? -17.024 4.337   17.661 1.00 36.28  ? 57  THR C CA  1 
ATOM   5571 C  C   . THR C  1  44  ? -16.764 3.003   16.949 1.00 37.81  ? 57  THR C C   1 
ATOM   5572 O  O   . THR C  1  44  ? -17.688 2.211   16.764 1.00 38.71  ? 57  THR C O   1 
ATOM   5573 C  CB  . THR C  1  44  ? -17.222 5.485   16.679 1.00 39.54  ? 57  THR C CB  1 
ATOM   5574 O  OG1 . THR C  1  44  ? -17.560 6.639   17.447 1.00 41.44  ? 57  THR C OG1 1 
ATOM   5575 C  CG2 . THR C  1  44  ? -18.342 5.209   15.692 1.00 41.85  ? 57  THR C CG2 1 
ATOM   5576 N  N   . LEU C  1  45  ? -15.511 2.739   16.562 1.00 33.81  ? 58  LEU C N   1 
ATOM   5577 C  CA  . LEU C  1  45  ? -15.200 1.508   15.854 1.00 34.88  ? 58  LEU C CA  1 
ATOM   5578 C  C   . LEU C  1  45  ? -15.413 0.294   16.754 1.00 34.89  ? 58  LEU C C   1 
ATOM   5579 O  O   . LEU C  1  45  ? -15.834 -0.767  16.289 1.00 34.16  ? 58  LEU C O   1 
ATOM   5580 C  CB  . LEU C  1  45  ? -13.776 1.562   15.313 1.00 35.68  ? 58  LEU C CB  1 
ATOM   5581 C  CG  . LEU C  1  45  ? -13.533 2.618   14.236 1.00 37.81  ? 58  LEU C CG  1 
ATOM   5582 C  CD1 . LEU C  1  45  ? -12.060 2.886   14.040 1.00 38.10  ? 58  LEU C CD1 1 
ATOM   5583 C  CD2 . LEU C  1  45  ? -14.193 2.166   12.943 1.00 38.61  ? 58  LEU C CD2 1 
ATOM   5584 N  N   . ALA C  1  46  ? -15.126 0.443   18.049 1.00 39.45  ? 59  ALA C N   1 
ATOM   5585 C  CA  . ALA C  1  46  ? -15.324 -0.661  18.978 1.00 42.43  ? 59  ALA C CA  1 
ATOM   5586 C  C   . ALA C  1  46  ? -16.816 -0.912  19.200 1.00 41.33  ? 59  ALA C C   1 
ATOM   5587 O  O   . ALA C  1  46  ? -17.267 -2.060  19.199 1.00 37.97  ? 59  ALA C O   1 
ATOM   5588 C  CB  . ALA C  1  46  ? -14.614 -0.379  20.274 1.00 43.51  ? 59  ALA C CB  1 
ATOM   5589 N  N   . SER C  1  47  ? -17.579 0.172   19.361 1.00 39.04  ? 60  SER C N   1 
ATOM   5590 C  CA  . SER C  1  47  ? -18.993 0.048   19.689 1.00 42.16  ? 60  SER C CA  1 
ATOM   5591 C  C   . SER C  1  47  ? -19.831 -0.365  18.470 1.00 44.48  ? 60  SER C C   1 
ATOM   5592 O  O   . SER C  1  47  ? -20.995 -0.704  18.630 1.00 40.23  ? 60  SER C O   1 
ATOM   5593 C  CB  . SER C  1  47  ? -19.496 1.314   20.351 1.00 38.94  ? 60  SER C CB  1 
ATOM   5594 O  OG  . SER C  1  47  ? -19.091 1.351   21.718 1.00 40.15  ? 60  SER C OG  1 
ATOM   5595 N  N   . HIS C  1  48  ? -19.231 -0.401  17.267 1.00 45.94  ? 61  HIS C N   1 
ATOM   5596 C  CA  . HIS C  1  48  ? -19.887 -0.953  16.084 1.00 42.13  ? 61  HIS C CA  1 
ATOM   5597 C  C   . HIS C  1  48  ? -19.264 -2.272  15.618 1.00 37.22  ? 61  HIS C C   1 
ATOM   5598 O  O   . HIS C  1  48  ? -19.659 -2.783  14.567 1.00 31.80  ? 61  HIS C O   1 
ATOM   5599 C  CB  . HIS C  1  48  ? -19.847 0.035   14.917 1.00 37.90  ? 61  HIS C CB  1 
ATOM   5600 C  CG  . HIS C  1  48  ? -20.882 1.103   14.985 1.00 39.38  ? 61  HIS C CG  1 
ATOM   5601 N  ND1 . HIS C  1  48  ? -22.103 0.981   14.344 1.00 37.62  ? 61  HIS C ND1 1 
ATOM   5602 C  CD2 . HIS C  1  48  ? -20.871 2.320   15.560 1.00 35.46  ? 61  HIS C CD2 1 
ATOM   5603 C  CE1 . HIS C  1  48  ? -22.792 2.104   14.539 1.00 37.72  ? 61  HIS C CE1 1 
ATOM   5604 N  NE2 . HIS C  1  48  ? -22.063 2.935   15.263 1.00 34.20  ? 61  HIS C NE2 1 
ATOM   5605 N  N   . GLY C  1  49  ? -18.287 -2.810  16.362 1.00 36.23  ? 62  GLY C N   1 
ATOM   5606 C  CA  . GLY C  1  49  ? -17.706 -4.103  16.030 1.00 37.52  ? 62  GLY C CA  1 
ATOM   5607 C  C   . GLY C  1  49  ? -16.694 -4.086  14.873 1.00 36.96  ? 62  GLY C C   1 
ATOM   5608 O  O   . GLY C  1  49  ? -16.343 -5.152  14.376 1.00 33.67  ? 62  GLY C O   1 
ATOM   5609 N  N   . TYR C  1  50  ? -16.185 -2.910  14.461 1.00 37.05  ? 63  TYR C N   1 
ATOM   5610 C  CA  . TYR C  1  50  ? -15.029 -2.843  13.569 1.00 39.41  ? 63  TYR C CA  1 
ATOM   5611 C  C   . TYR C  1  50  ? -13.760 -3.285  14.307 1.00 39.14  ? 63  TYR C C   1 
ATOM   5612 O  O   . TYR C  1  50  ? -12.876 -3.862  13.698 1.00 43.89  ? 63  TYR C O   1 
ATOM   5613 C  CB  . TYR C  1  50  ? -14.859 -1.447  12.960 1.00 38.19  ? 63  TYR C CB  1 
ATOM   5614 C  CG  . TYR C  1  50  ? -15.792 -1.201  11.785 1.00 40.19  ? 63  TYR C CG  1 
ATOM   5615 C  CD1 . TYR C  1  50  ? -15.486 -1.681  10.516 1.00 42.57  ? 63  TYR C CD1 1 
ATOM   5616 C  CD2 . TYR C  1  50  ? -16.995 -0.529  11.946 1.00 41.39  ? 63  TYR C CD2 1 
ATOM   5617 C  CE1 . TYR C  1  50  ? -16.336 -1.484  9.441  1.00 40.63  ? 63  TYR C CE1 1 
ATOM   5618 C  CE2 . TYR C  1  50  ? -17.859 -0.333  10.881 1.00 42.98  ? 63  TYR C CE2 1 
ATOM   5619 C  CZ  . TYR C  1  50  ? -17.528 -0.812  9.625  1.00 42.84  ? 63  TYR C CZ  1 
ATOM   5620 O  OH  . TYR C  1  50  ? -18.374 -0.641  8.571  1.00 46.69  ? 63  TYR C OH  1 
ATOM   5621 N  N   . LEU C  1  51  ? -13.649 -2.935  15.591 1.00 40.94  ? 64  LEU C N   1 
ATOM   5622 C  CA  . LEU C  1  51  ? -12.684 -3.512  16.520 1.00 43.10  ? 64  LEU C CA  1 
ATOM   5623 C  C   . LEU C  1  51  ? -13.402 -4.506  17.423 1.00 43.31  ? 64  LEU C C   1 
ATOM   5624 O  O   . LEU C  1  51  ? -14.621 -4.463  17.515 1.00 47.03  ? 64  LEU C O   1 
ATOM   5625 C  CB  . LEU C  1  51  ? -12.079 -2.421  17.405 1.00 41.37  ? 64  LEU C CB  1 
ATOM   5626 C  CG  . LEU C  1  51  ? -11.201 -1.380  16.724 1.00 41.09  ? 64  LEU C CG  1 
ATOM   5627 C  CD1 . LEU C  1  51  ? -10.964 -0.217  17.648 1.00 40.04  ? 64  LEU C CD1 1 
ATOM   5628 C  CD2 . LEU C  1  51  ? -9.904  -2.047  16.308 1.00 40.38  ? 64  LEU C CD2 1 
ATOM   5629 N  N   . PRO C  1  52  ? -12.675 -5.349  18.191 1.00 47.38  ? 65  PRO C N   1 
ATOM   5630 C  CA  . PRO C  1  52  ? -13.281 -6.091  19.299 1.00 45.68  ? 65  PRO C CA  1 
ATOM   5631 C  C   . PRO C  1  52  ? -14.024 -5.143  20.232 1.00 47.28  ? 65  PRO C C   1 
ATOM   5632 O  O   . PRO C  1  52  ? -13.511 -4.073  20.554 1.00 43.55  ? 65  PRO C O   1 
ATOM   5633 C  CB  . PRO C  1  52  ? -12.094 -6.766  19.998 1.00 46.28  ? 65  PRO C CB  1 
ATOM   5634 C  CG  . PRO C  1  52  ? -11.015 -6.847  18.929 1.00 47.38  ? 65  PRO C CG  1 
ATOM   5635 C  CD  . PRO C  1  52  ? -11.236 -5.631  18.036 1.00 47.49  ? 65  PRO C CD  1 
ATOM   5636 N  N   . ARG C  1  53  ? -15.223 -5.557  20.667 1.00 46.64  ? 66  ARG C N   1 
ATOM   5637 C  CA  . ARG C  1  53  ? -16.143 -4.693  21.388 1.00 45.27  ? 66  ARG C CA  1 
ATOM   5638 C  C   . ARG C  1  53  ? -15.654 -4.405  22.809 1.00 42.89  ? 66  ARG C C   1 
ATOM   5639 O  O   . ARG C  1  53  ? -16.112 -3.427  23.412 1.00 31.15  ? 66  ARG C O   1 
ATOM   5640 C  CB  . ARG C  1  53  ? -17.560 -5.278  21.382 1.00 47.78  ? 66  ARG C CB  1 
ATOM   5641 C  CG  . ARG C  1  53  ? -18.139 -5.371  19.976 1.00 46.93  ? 66  ARG C CG  1 
ATOM   5642 C  CD  . ARG C  1  53  ? -19.613 -5.733  19.922 1.00 44.22  ? 66  ARG C CD  1 
ATOM   5643 N  NE  . ARG C  1  53  ? -20.125 -5.753  18.543 1.00 42.70  ? 66  ARG C NE  1 
ATOM   5644 C  CZ  . ARG C  1  53  ? -20.787 -4.756  17.956 1.00 43.53  ? 66  ARG C CZ  1 
ATOM   5645 N  NH1 . ARG C  1  53  ? -20.921 -3.574  18.548 1.00 40.16  ? 66  ARG C NH1 1 
ATOM   5646 N  NH2 . ARG C  1  53  ? -21.292 -4.928  16.743 1.00 49.11  ? 66  ARG C NH2 1 
ATOM   5647 N  N   . ASP C  1  54  ? -14.709 -5.223  23.308 1.00 42.54  ? 67  ASP C N   1 
ATOM   5648 C  CA  . ASP C  1  54  ? -14.138 -5.014  24.632 1.00 47.95  ? 67  ASP C CA  1 
ATOM   5649 C  C   . ASP C  1  54  ? -13.056 -3.933  24.622 1.00 43.90  ? 67  ASP C C   1 
ATOM   5650 O  O   . ASP C  1  54  ? -12.602 -3.519  25.682 1.00 48.59  ? 67  ASP C O   1 
ATOM   5651 C  CB  . ASP C  1  54  ? -13.631 -6.311  25.250 1.00 49.17  ? 67  ASP C CB  1 
ATOM   5652 C  CG  . ASP C  1  54  ? -12.450 -6.981  24.559 1.00 54.66  ? 67  ASP C CG  1 
ATOM   5653 O  OD1 . ASP C  1  54  ? -11.950 -6.423  23.548 1.00 57.58  ? 67  ASP C OD1 1 
ATOM   5654 O  OD2 . ASP C  1  54  ? -12.006 -8.036  25.067 1.00 59.71  ? 67  ASP C OD2 1 
ATOM   5655 N  N   . GLY C  1  55  ? -12.642 -3.477  23.442 1.00 42.58  ? 68  GLY C N   1 
ATOM   5656 C  CA  . GLY C  1  55  ? -11.794 -2.296  23.334 1.00 41.44  ? 68  GLY C CA  1 
ATOM   5657 C  C   . GLY C  1  55  ? -10.311 -2.614  23.546 1.00 38.63  ? 68  GLY C C   1 
ATOM   5658 O  O   . GLY C  1  55  ? -9.532  -1.723  23.885 1.00 35.60  ? 68  GLY C O   1 
ATOM   5659 N  N   . VAL C  1  56  ? -9.953  -3.887  23.340 1.00 33.92  ? 69  VAL C N   1 
ATOM   5660 C  CA  . VAL C  1  56  ? -8.587  -4.358  23.388 1.00 35.94  ? 69  VAL C CA  1 
ATOM   5661 C  C   . VAL C  1  56  ? -8.288  -5.017  22.050 1.00 38.67  ? 69  VAL C C   1 
ATOM   5662 O  O   . VAL C  1  56  ? -9.016  -5.912  21.640 1.00 43.09  ? 69  VAL C O   1 
ATOM   5663 C  CB  . VAL C  1  56  ? -8.374  -5.349  24.543 1.00 37.56  ? 69  VAL C CB  1 
ATOM   5664 C  CG1 . VAL C  1  56  ? -6.989  -5.998  24.502 1.00 39.30  ? 69  VAL C CG1 1 
ATOM   5665 C  CG2 . VAL C  1  56  ? -8.610  -4.674  25.890 1.00 38.57  ? 69  VAL C CG2 1 
ATOM   5666 N  N   . ALA C  1  57  ? -7.212  -4.588  21.383 1.00 42.87  ? 70  ALA C N   1 
ATOM   5667 C  CA  . ALA C  1  57  ? -6.979  -5.000  20.007 1.00 42.39  ? 70  ALA C CA  1 
ATOM   5668 C  C   . ALA C  1  57  ? -5.492  -5.000  19.669 1.00 39.83  ? 70  ALA C C   1 
ATOM   5669 O  O   . ALA C  1  57  ? -4.698  -4.355  20.349 1.00 43.24  ? 70  ALA C O   1 
ATOM   5670 C  CB  . ALA C  1  57  ? -7.744  -4.087  19.085 1.00 42.22  ? 70  ALA C CB  1 
ATOM   5671 N  N   . THR C  1  58  ? -5.143  -5.736  18.601 1.00 38.13  ? 71  THR C N   1 
ATOM   5672 C  CA  . THR C  1  58  ? -3.795  -5.727  18.048 1.00 37.07  ? 71  THR C CA  1 
ATOM   5673 C  C   . THR C  1  58  ? -3.606  -4.470  17.206 1.00 36.45  ? 71  THR C C   1 
ATOM   5674 O  O   . THR C  1  58  ? -4.570  -3.933  16.672 1.00 39.27  ? 71  THR C O   1 
ATOM   5675 C  CB  . THR C  1  58  ? -3.519  -6.959  17.191 1.00 34.36  ? 71  THR C CB  1 
ATOM   5676 O  OG1 . THR C  1  58  ? -4.313  -6.790  16.021 1.00 34.09  ? 71  THR C OG1 1 
ATOM   5677 C  CG2 . THR C  1  58  ? -3.830  -8.263  17.904 1.00 34.77  ? 71  THR C CG2 1 
ATOM   5678 N  N   . PRO C  1  59  ? -2.356  -3.982  17.037 1.00 39.19  ? 72  PRO C N   1 
ATOM   5679 C  CA  . PRO C  1  59  ? -2.082  -2.901  16.090 1.00 39.60  ? 72  PRO C CA  1 
ATOM   5680 C  C   . PRO C  1  59  ? -2.704  -3.119  14.712 1.00 36.51  ? 72  PRO C C   1 
ATOM   5681 O  O   . PRO C  1  59  ? -3.281  -2.200  14.146 1.00 34.34  ? 72  PRO C O   1 
ATOM   5682 C  CB  . PRO C  1  59  ? -0.545  -2.910  16.039 1.00 39.92  ? 72  PRO C CB  1 
ATOM   5683 C  CG  . PRO C  1  59  ? -0.136  -3.349  17.418 1.00 38.97  ? 72  PRO C CG  1 
ATOM   5684 C  CD  . PRO C  1  59  ? -1.151  -4.421  17.767 1.00 40.54  ? 72  PRO C CD  1 
ATOM   5685 N  N   . ALA C  1  60  ? -2.596  -4.342  14.186 1.00 36.99  ? 73  ALA C N   1 
ATOM   5686 C  CA  . ALA C  1  60  ? -3.076  -4.643  12.848 1.00 38.90  ? 73  ALA C CA  1 
ATOM   5687 C  C   . ALA C  1  60  ? -4.593  -4.487  12.755 1.00 38.11  ? 73  ALA C C   1 
ATOM   5688 O  O   . ALA C  1  60  ? -5.091  -3.979  11.755 1.00 38.68  ? 73  ALA C O   1 
ATOM   5689 C  CB  . ALA C  1  60  ? -2.643  -6.029  12.440 1.00 39.53  ? 73  ALA C CB  1 
ATOM   5690 N  N   . GLN C  1  61  ? -5.316  -4.919  13.796 1.00 36.29  ? 74  GLN C N   1 
ATOM   5691 C  CA  . GLN C  1  61  ? -6.764  -4.798  13.832 1.00 35.92  ? 74  GLN C CA  1 
ATOM   5692 C  C   . GLN C  1  61  ? -7.202  -3.337  13.830 1.00 36.69  ? 74  GLN C C   1 
ATOM   5693 O  O   . GLN C  1  61  ? -8.192  -2.983  13.186 1.00 39.27  ? 74  GLN C O   1 
ATOM   5694 C  CB  . GLN C  1  61  ? -7.328  -5.463  15.082 1.00 37.15  ? 74  GLN C CB  1 
ATOM   5695 C  CG  . GLN C  1  61  ? -7.248  -6.982  15.047 1.00 37.75  ? 74  GLN C CG  1 
ATOM   5696 C  CD  . GLN C  1  61  ? -7.784  -7.597  16.318 1.00 42.98  ? 74  GLN C CD  1 
ATOM   5697 O  OE1 . GLN C  1  61  ? -7.475  -7.185  17.450 1.00 45.50  ? 74  GLN C OE1 1 
ATOM   5698 N  NE2 . GLN C  1  61  ? -8.629  -8.591  16.120 1.00 47.08  ? 74  GLN C NE2 1 
ATOM   5699 N  N   . ILE C  1  62  ? -6.468  -2.511  14.585 1.00 37.62  ? 75  ILE C N   1 
ATOM   5700 C  CA  . ILE C  1  62  ? -6.753  -1.088  14.711 1.00 37.38  ? 75  ILE C CA  1 
ATOM   5701 C  C   . ILE C  1  62  ? -6.573  -0.410  13.350 1.00 38.16  ? 75  ILE C C   1 
ATOM   5702 O  O   . ILE C  1  62  ? -7.388  0.419   12.947 1.00 36.07  ? 75  ILE C O   1 
ATOM   5703 C  CB  . ILE C  1  62  ? -5.882  -0.463  15.818 1.00 34.05  ? 75  ILE C CB  1 
ATOM   5704 C  CG1 . ILE C  1  62  ? -6.295  -1.000  17.199 1.00 34.05  ? 75  ILE C CG1 1 
ATOM   5705 C  CG2 . ILE C  1  62  ? -5.915  1.066   15.765 1.00 32.76  ? 75  ILE C CG2 1 
ATOM   5706 C  CD1 . ILE C  1  62  ? -5.479  -0.489  18.380 1.00 32.54  ? 75  ILE C CD1 1 
ATOM   5707 N  N   . ILE C  1  63  ? -5.499  -0.763  12.640 1.00 35.16  ? 76  ILE C N   1 
ATOM   5708 C  CA  . ILE C  1  63  ? -5.241  -0.148  11.354 1.00 34.29  ? 76  ILE C CA  1 
ATOM   5709 C  C   . ILE C  1  63  ? -6.342  -0.541  10.379 1.00 34.13  ? 76  ILE C C   1 
ATOM   5710 O  O   . ILE C  1  63  ? -6.885  0.339   9.718  1.00 34.37  ? 76  ILE C O   1 
ATOM   5711 C  CB  . ILE C  1  63  ? -3.830  -0.489  10.838 1.00 36.02  ? 76  ILE C CB  1 
ATOM   5712 C  CG1 . ILE C  1  63  ? -2.771  0.206   11.674 1.00 38.07  ? 76  ILE C CG1 1 
ATOM   5713 C  CG2 . ILE C  1  63  ? -3.660  -0.130  9.363  1.00 38.50  ? 76  ILE C CG2 1 
ATOM   5714 C  CD1 . ILE C  1  63  ? -1.414  -0.453  11.579 1.00 38.51  ? 76  ILE C CD1 1 
ATOM   5715 N  N   . THR C  1  64  ? -6.686  -1.835  10.284 1.00 34.80  ? 77  THR C N   1 
ATOM   5716 C  CA  A THR C  1  64  ? -7.691  -2.242  9.315  0.50 37.10  ? 77  THR C CA  1 
ATOM   5717 C  CA  B THR C  1  64  ? -7.697  -2.251  9.321  0.50 35.64  ? 77  THR C CA  1 
ATOM   5718 C  C   . THR C  1  64  ? -9.029  -1.581  9.675  1.00 35.46  ? 77  THR C C   1 
ATOM   5719 O  O   . THR C  1  64  ? -9.749  -1.130  8.781  1.00 32.96  ? 77  THR C O   1 
ATOM   5720 C  CB  A THR C  1  64  ? -7.804  -3.765  9.184  0.50 38.27  ? 77  THR C CB  1 
ATOM   5721 C  CB  B THR C  1  64  ? -7.805  -3.773  9.143  0.50 35.71  ? 77  THR C CB  1 
ATOM   5722 O  OG1 A THR C  1  64  ? -8.328  -4.212  10.425 0.50 47.97  ? 77  THR C OG1 1 
ATOM   5723 O  OG1 B THR C  1  64  ? -9.159  -4.008  8.768  0.50 31.19  ? 77  THR C OG1 1 
ATOM   5724 C  CG2 A THR C  1  64  ? -6.496  -4.478  8.899  0.50 35.02  ? 77  THR C CG2 1 
ATOM   5725 C  CG2 B THR C  1  64  ? -7.554  -4.605  10.384 0.50 38.46  ? 77  THR C CG2 1 
ATOM   5726 N  N   . ALA C  1  65  ? -9.333  -1.447  10.980 1.00 34.90  ? 78  ALA C N   1 
ATOM   5727 C  CA  . ALA C  1  65  ? -10.591 -0.852  11.434 1.00 32.03  ? 78  ALA C CA  1 
ATOM   5728 C  C   . ALA C  1  65  ? -10.702 0.637   11.089 1.00 31.68  ? 78  ALA C C   1 
ATOM   5729 O  O   . ALA C  1  65  ? -11.762 1.096   10.698 1.00 30.38  ? 78  ALA C O   1 
ATOM   5730 C  CB  . ALA C  1  65  ? -10.768 -1.047  12.922 1.00 31.03  ? 78  ALA C CB  1 
ATOM   5731 N  N   . THR C  1  66  ? -9.632  1.416   11.273 1.00 35.94  ? 79  THR C N   1 
ATOM   5732 C  CA  . THR C  1  66  ? -9.677  2.842   10.964 1.00 34.86  ? 79  THR C CA  1 
ATOM   5733 C  C   . THR C  1  66  ? -9.828  3.038   9.455  1.00 35.14  ? 79  THR C C   1 
ATOM   5734 O  O   . THR C  1  66  ? -10.400 4.030   9.017  1.00 34.41  ? 79  THR C O   1 
ATOM   5735 C  CB  . THR C  1  66  ? -8.453  3.588   11.493 1.00 31.86  ? 79  THR C CB  1 
ATOM   5736 O  OG1 . THR C  1  66  ? -7.313  3.075   10.818 1.00 29.68  ? 79  THR C OG1 1 
ATOM   5737 C  CG2 . THR C  1  66  ? -8.265  3.428   12.987 1.00 31.02  ? 79  THR C CG2 1 
ATOM   5738 N  N   . GLN C  1  67  ? -9.301  2.099   8.661  1.00 33.74  ? 80  GLN C N   1 
ATOM   5739 C  CA  . GLN C  1  67  ? -9.395  2.199   7.211  1.00 34.76  ? 80  GLN C CA  1 
ATOM   5740 C  C   . GLN C  1  67  ? -10.808 1.806   6.752  1.00 34.28  ? 80  GLN C C   1 
ATOM   5741 O  O   . GLN C  1  67  ? -11.443 2.549   6.015  1.00 34.42  ? 80  GLN C O   1 
ATOM   5742 C  CB  . GLN C  1  67  ? -8.279  1.370   6.572  1.00 32.23  ? 80  GLN C CB  1 
ATOM   5743 C  CG  . GLN C  1  67  ? -6.893  1.959   6.796  1.00 34.11  ? 80  GLN C CG  1 
ATOM   5744 C  CD  . GLN C  1  67  ? -5.730  1.188   6.199  1.00 33.38  ? 80  GLN C CD  1 
ATOM   5745 O  OE1 . GLN C  1  67  ? -4.630  1.724   6.043  1.00 35.51  ? 80  GLN C OE1 1 
ATOM   5746 N  NE2 . GLN C  1  67  ? -5.925  -0.070  5.841  1.00 35.78  ? 80  GLN C NE2 1 
ATOM   5747 N  N   . GLU C  1  68  ? -11.303 0.641   7.186  1.00 34.68  ? 81  GLU C N   1 
ATOM   5748 C  CA  . GLU C  1  68  ? -12.614 0.170   6.777  1.00 39.63  ? 81  GLU C CA  1 
ATOM   5749 C  C   . GLU C  1  68  ? -13.712 1.126   7.248  1.00 40.75  ? 81  GLU C C   1 
ATOM   5750 O  O   . GLU C  1  68  ? -14.636 1.437   6.507  1.00 41.48  ? 81  GLU C O   1 
ATOM   5751 C  CB  . GLU C  1  68  ? -12.932 -1.205  7.358  1.00 46.32  ? 81  GLU C CB  1 
ATOM   5752 C  CG  . GLU C  1  68  ? -12.099 -2.337  6.774  1.00 58.23  ? 81  GLU C CG  1 
ATOM   5753 C  CD  . GLU C  1  68  ? -12.272 -2.531  5.278  1.00 69.50  ? 81  GLU C CD  1 
ATOM   5754 O  OE1 . GLU C  1  68  ? -11.201 -2.616  4.623  1.00 67.10  ? 81  GLU C OE1 1 
ATOM   5755 O  OE2 . GLU C  1  68  ? -13.439 -2.570  4.786  1.00 74.84  ? 81  GLU C OE2 1 
ATOM   5756 N  N   . GLY C  1  69  ? -13.619 1.584   8.493  1.00 38.93  ? 82  GLY C N   1 
ATOM   5757 C  CA  . GLY C  1  69  ? -14.693 2.354   9.092  1.00 36.57  ? 82  GLY C CA  1 
ATOM   5758 C  C   . GLY C  1  69  ? -14.689 3.818   8.667  1.00 33.76  ? 82  GLY C C   1 
ATOM   5759 O  O   . GLY C  1  69  ? -15.747 4.411   8.580  1.00 36.74  ? 82  GLY C O   1 
ATOM   5760 N  N   . PHE C  1  70  ? -13.517 4.417   8.445  1.00 33.83  ? 83  PHE C N   1 
ATOM   5761 C  CA  . PHE C  1  70  ? -13.438 5.866   8.308  1.00 35.25  ? 83  PHE C CA  1 
ATOM   5762 C  C   . PHE C  1  70  ? -12.622 6.312   7.099  1.00 32.85  ? 83  PHE C C   1 
ATOM   5763 O  O   . PHE C  1  70  ? -12.586 7.508   6.816  1.00 30.85  ? 83  PHE C O   1 
ATOM   5764 C  CB  . PHE C  1  70  ? -12.819 6.504   9.555  1.00 38.32  ? 83  PHE C CB  1 
ATOM   5765 C  CG  . PHE C  1  70  ? -13.772 6.653   10.725 1.00 41.32  ? 83  PHE C CG  1 
ATOM   5766 C  CD1 . PHE C  1  70  ? -14.786 7.600   10.682 1.00 42.28  ? 83  PHE C CD1 1 
ATOM   5767 C  CD2 . PHE C  1  70  ? -13.627 5.882   11.872 1.00 43.60  ? 83  PHE C CD2 1 
ATOM   5768 C  CE1 . PHE C  1  70  ? -15.659 7.749   11.747 1.00 43.61  ? 83  PHE C CE1 1 
ATOM   5769 C  CE2 . PHE C  1  70  ? -14.507 6.034   12.927 1.00 45.20  ? 83  PHE C CE2 1 
ATOM   5770 C  CZ  . PHE C  1  70  ? -15.514 6.972   12.866 1.00 44.57  ? 83  PHE C CZ  1 
ATOM   5771 N  N   . ASN C  1  71  ? -11.972 5.362   6.417  1.00 33.87  ? 84  ASN C N   1 
ATOM   5772 C  CA  . ASN C  1  71  ? -11.019 5.658   5.358  1.00 35.40  ? 84  ASN C CA  1 
ATOM   5773 C  C   . ASN C  1  71  ? -9.875  6.536   5.872  1.00 33.61  ? 84  ASN C C   1 
ATOM   5774 O  O   . ASN C  1  71  ? -9.420  7.443   5.190  1.00 31.55  ? 84  ASN C O   1 
ATOM   5775 C  CB  . ASN C  1  71  ? -11.736 6.275   4.166  1.00 38.81  ? 84  ASN C CB  1 
ATOM   5776 C  CG  . ASN C  1  71  ? -11.186 5.824   2.832  1.00 38.84  ? 84  ASN C CG  1 
ATOM   5777 O  OD1 . ASN C  1  71  ? -10.087 5.262   2.732  1.00 42.09  ? 84  ASN C OD1 1 
ATOM   5778 N  ND2 . ASN C  1  71  ? -11.940 6.088   1.784  1.00 42.18  ? 84  ASN C ND2 1 
ATOM   5779 N  N   . PHE C  1  72  ? -9.399  6.258   7.089  1.00 35.96  ? 85  PHE C N   1 
ATOM   5780 C  CA  . PHE C  1  72  ? -8.199  6.905   7.596  1.00 33.42  ? 85  PHE C CA  1 
ATOM   5781 C  C   . PHE C  1  72  ? -7.038  6.488   6.697  1.00 31.69  ? 85  PHE C C   1 
ATOM   5782 O  O   . PHE C  1  72  ? -6.923  5.311   6.359  1.00 30.44  ? 85  PHE C O   1 
ATOM   5783 C  CB  . PHE C  1  72  ? -8.018  6.470   9.056  1.00 34.76  ? 85  PHE C CB  1 
ATOM   5784 C  CG  . PHE C  1  72  ? -7.106  7.327   9.921  1.00 34.49  ? 85  PHE C CG  1 
ATOM   5785 C  CD1 . PHE C  1  72  ? -7.110  8.713   9.833  1.00 34.69  ? 85  PHE C CD1 1 
ATOM   5786 C  CD2 . PHE C  1  72  ? -6.288  6.738   10.873 1.00 34.79  ? 85  PHE C CD2 1 
ATOM   5787 C  CE1 . PHE C  1  72  ? -6.279  9.480   10.635 1.00 34.34  ? 85  PHE C CE1 1 
ATOM   5788 C  CE2 . PHE C  1  72  ? -5.468  7.514   11.683 1.00 34.22  ? 85  PHE C CE2 1 
ATOM   5789 C  CZ  . PHE C  1  72  ? -5.464  8.879   11.561 1.00 32.77  ? 85  PHE C CZ  1 
ATOM   5790 N  N   . GLU C  1  73  ? -6.189  7.446   6.306  1.00 33.35  ? 86  GLU C N   1 
ATOM   5791 C  CA  . GLU C  1  73  ? -5.084  7.167   5.395  1.00 35.41  ? 86  GLU C CA  1 
ATOM   5792 C  C   . GLU C  1  73  ? -4.080  6.223   6.060  1.00 34.17  ? 86  GLU C C   1 
ATOM   5793 O  O   . GLU C  1  73  ? -3.813  6.343   7.241  1.00 34.69  ? 86  GLU C O   1 
ATOM   5794 C  CB  . GLU C  1  73  ? -4.500  8.504   4.948  1.00 41.69  ? 86  GLU C CB  1 
ATOM   5795 C  CG  . GLU C  1  73  ? -3.491  8.388   3.803  1.00 48.97  ? 86  GLU C CG  1 
ATOM   5796 C  CD  . GLU C  1  73  ? -2.060  8.083   4.235  1.00 56.13  ? 86  GLU C CD  1 
ATOM   5797 O  OE1 . GLU C  1  73  ? -1.438  7.131   3.696  1.00 53.66  ? 86  GLU C OE1 1 
ATOM   5798 O  OE2 . GLU C  1  73  ? -1.574  8.807   5.140  1.00 60.54  ? 86  GLU C OE2 1 
ATOM   5799 N  N   . ASN C  1  74  ? -3.527  5.288   5.285  1.00 33.94  ? 87  ASN C N   1 
ATOM   5800 C  CA  . ASN C  1  74  ? -2.741  4.155   5.767  1.00 32.46  ? 87  ASN C CA  1 
ATOM   5801 C  C   . ASN C  1  74  ? -1.557  4.601   6.617  1.00 33.15  ? 87  ASN C C   1 
ATOM   5802 O  O   . ASN C  1  74  ? -1.342  4.082   7.698  1.00 29.69  ? 87  ASN C O   1 
ATOM   5803 C  CB  . ASN C  1  74  ? -2.237  3.336   4.579  1.00 32.92  ? 87  ASN C CB  1 
ATOM   5804 C  CG  . ASN C  1  74  ? -1.397  2.141   4.949  1.00 30.69  ? 87  ASN C CG  1 
ATOM   5805 O  OD1 . ASN C  1  74  ? -0.237  2.045   4.538  1.00 32.90  ? 87  ASN C OD1 1 
ATOM   5806 N  ND2 . ASN C  1  74  ? -1.971  1.196   5.670  1.00 30.43  ? 87  ASN C ND2 1 
ATOM   5807 N  N   . ASN C  1  75  ? -0.764  5.547   6.117  1.00 36.26  ? 88  ASN C N   1 
ATOM   5808 C  CA  . ASN C  1  75  ? 0.434   5.959   6.826  1.00 37.23  ? 88  ASN C CA  1 
ATOM   5809 C  C   . ASN C  1  75  ? 0.072   6.678   8.121  1.00 38.19  ? 88  ASN C C   1 
ATOM   5810 O  O   . ASN C  1  75  ? 0.753   6.501   9.122  1.00 38.25  ? 88  ASN C O   1 
ATOM   5811 C  CB  . ASN C  1  75  ? 1.380   6.758   5.939  1.00 38.11  ? 88  ASN C CB  1 
ATOM   5812 C  CG  . ASN C  1  75  ? 2.157   5.845   5.007  1.00 38.37  ? 88  ASN C CG  1 
ATOM   5813 O  OD1 . ASN C  1  75  ? 2.265   6.135   3.813  1.00 40.16  ? 88  ASN C OD1 1 
ATOM   5814 N  ND2 . ASN C  1  75  ? 2.645   4.708   5.486  1.00 33.07  ? 88  ASN C ND2 1 
ATOM   5815 N  N   . ALA C  1  76  ? -0.998  7.474   8.094  1.00 36.80  ? 89  ALA C N   1 
ATOM   5816 C  CA  . ALA C  1  76  ? -1.484  8.189   9.263  1.00 35.15  ? 89  ALA C CA  1 
ATOM   5817 C  C   . ALA C  1  76  ? -1.933  7.208   10.342 1.00 32.85  ? 89  ALA C C   1 
ATOM   5818 O  O   . ALA C  1  76  ? -1.735  7.455   11.527 1.00 33.92  ? 89  ALA C O   1 
ATOM   5819 C  CB  . ALA C  1  76  ? -2.633  9.090   8.863  1.00 37.72  ? 89  ALA C CB  1 
ATOM   5820 N  N   . ALA C  1  77  ? -2.538  6.102   9.912  1.00 30.89  ? 90  ALA C N   1 
ATOM   5821 C  CA  . ALA C  1  77  ? -2.997  5.055   10.808 1.00 32.97  ? 90  ALA C CA  1 
ATOM   5822 C  C   . ALA C  1  77  ? -1.815  4.341   11.448 1.00 34.11  ? 90  ALA C C   1 
ATOM   5823 O  O   . ALA C  1  77  ? -1.867  3.981   12.622 1.00 36.95  ? 90  ALA C O   1 
ATOM   5824 C  CB  . ALA C  1  77  ? -3.865  4.077   10.044 1.00 34.00  ? 90  ALA C CB  1 
ATOM   5825 N  N   . ILE C  1  78  ? -0.761  4.129   10.652 1.00 33.94  ? 91  ILE C N   1 
ATOM   5826 C  CA  . ILE C  1  78  ? 0.439   3.461   11.126 1.00 33.56  ? 91  ILE C CA  1 
ATOM   5827 C  C   . ILE C  1  78  ? 1.132   4.351   12.155 1.00 31.31  ? 91  ILE C C   1 
ATOM   5828 O  O   . ILE C  1  78  ? 1.503   3.872   13.212 1.00 31.52  ? 91  ILE C O   1 
ATOM   5829 C  CB  . ILE C  1  78  ? 1.318   3.063   9.927  1.00 35.79  ? 91  ILE C CB  1 
ATOM   5830 C  CG1 . ILE C  1  78  ? 0.714   1.849   9.210  1.00 35.38  ? 91  ILE C CG1 1 
ATOM   5831 C  CG2 . ILE C  1  78  ? 2.756   2.775   10.345 1.00 36.56  ? 91  ILE C CG2 1 
ATOM   5832 C  CD1 . ILE C  1  78  ? 1.274   1.599   7.828  1.00 34.25  ? 91  ILE C CD1 1 
ATOM   5833 N  N   . VAL C  1  79  ? 1.236   5.653   11.873 1.00 29.76  ? 92  VAL C N   1 
ATOM   5834 C  CA  . VAL C  1  79  ? 1.919   6.584   12.751 1.00 30.12  ? 92  VAL C CA  1 
ATOM   5835 C  C   . VAL C  1  79  ? 1.214   6.607   14.100 1.00 32.36  ? 92  VAL C C   1 
ATOM   5836 O  O   . VAL C  1  79  ? 1.888   6.572   15.127 1.00 31.33  ? 92  VAL C O   1 
ATOM   5837 C  CB  . VAL C  1  79  ? 2.036   8.006   12.163 1.00 32.12  ? 92  VAL C CB  1 
ATOM   5838 C  CG1 . VAL C  1  79  ? 2.429   9.057   13.193 1.00 33.81  ? 92  VAL C CG1 1 
ATOM   5839 C  CG2 . VAL C  1  79  ? 3.015   8.066   11.011 1.00 32.94  ? 92  VAL C CG2 1 
ATOM   5840 N  N   . ALA C  1  80  ? -0.125  6.682   14.094 1.00 30.75  ? 93  ALA C N   1 
ATOM   5841 C  CA  . ALA C  1  80  ? -0.868  6.810   15.338 1.00 29.98  ? 93  ALA C CA  1 
ATOM   5842 C  C   . ALA C  1  80  ? -0.882  5.483   16.085 1.00 29.17  ? 93  ALA C C   1 
ATOM   5843 O  O   . ALA C  1  80  ? -0.729  5.471   17.299 1.00 28.17  ? 93  ALA C O   1 
ATOM   5844 C  CB  . ALA C  1  80  ? -2.268  7.312   15.094 1.00 29.98  ? 93  ALA C CB  1 
ATOM   5845 N  N   . THR C  1  81  ? -1.051  4.368   15.374 1.00 29.25  ? 94  THR C N   1 
ATOM   5846 C  CA  . THR C  1  81  ? -1.276  3.103   16.050 1.00 29.46  ? 94  THR C CA  1 
ATOM   5847 C  C   . THR C  1  81  ? -0.013  2.648   16.782 1.00 33.34  ? 94  THR C C   1 
ATOM   5848 O  O   . THR C  1  81  ? -0.093  2.261   17.950 1.00 34.64  ? 94  THR C O   1 
ATOM   5849 C  CB  . THR C  1  81  ? -1.765  2.054   15.062 1.00 29.33  ? 94  THR C CB  1 
ATOM   5850 O  OG1 . THR C  1  81  ? -3.008  2.514   14.549 1.00 26.48  ? 94  THR C OG1 1 
ATOM   5851 C  CG2 . THR C  1  81  ? -1.991  0.711   15.729 1.00 31.42  ? 94  THR C CG2 1 
ATOM   5852 N  N   . TYR C  1  82  ? 1.147   2.681   16.110 1.00 33.44  ? 95  TYR C N   1 
ATOM   5853 C  CA  . TYR C  1  82  ? 2.378   2.155   16.693 1.00 32.41  ? 95  TYR C CA  1 
ATOM   5854 C  C   . TYR C  1  82  ? 2.938   3.145   17.715 1.00 32.20  ? 95  TYR C C   1 
ATOM   5855 O  O   . TYR C  1  82  ? 3.565   2.732   18.684 1.00 33.79  ? 95  TYR C O   1 
ATOM   5856 C  CB  . TYR C  1  82  ? 3.389   1.746   15.610 1.00 33.92  ? 95  TYR C CB  1 
ATOM   5857 C  CG  . TYR C  1  82  ? 2.930   0.504   14.855 1.00 33.43  ? 95  TYR C CG  1 
ATOM   5858 C  CD1 . TYR C  1  82  ? 3.018   -0.755  15.423 1.00 33.19  ? 95  TYR C CD1 1 
ATOM   5859 C  CD2 . TYR C  1  82  ? 2.356   0.597   13.596 1.00 35.52  ? 95  TYR C CD2 1 
ATOM   5860 C  CE1 . TYR C  1  82  ? 2.589   -1.887  14.748 1.00 34.55  ? 95  TYR C CE1 1 
ATOM   5861 C  CE2 . TYR C  1  82  ? 1.912   -0.524  12.916 1.00 35.17  ? 95  TYR C CE2 1 
ATOM   5862 C  CZ  . TYR C  1  82  ? 2.021   -1.774  13.494 1.00 35.22  ? 95  TYR C CZ  1 
ATOM   5863 O  OH  . TYR C  1  82  ? 1.582   -2.890  12.830 1.00 32.69  ? 95  TYR C OH  1 
ATOM   5864 N  N   . LEU C  1  83  ? 2.683   4.442   17.538 1.00 31.69  ? 96  LEU C N   1 
ATOM   5865 C  CA  . LEU C  1  83  ? 2.962   5.396   18.596 1.00 32.87  ? 96  LEU C CA  1 
ATOM   5866 C  C   . LEU C  1  83  ? 2.246   4.959   19.871 1.00 35.49  ? 96  LEU C C   1 
ATOM   5867 O  O   . LEU C  1  83  ? 2.855   4.826   20.928 1.00 39.58  ? 96  LEU C O   1 
ATOM   5868 C  CB  . LEU C  1  83  ? 2.514   6.793   18.169 1.00 34.04  ? 96  LEU C CB  1 
ATOM   5869 C  CG  . LEU C  1  83  ? 2.619   7.886   19.232 1.00 33.15  ? 96  LEU C CG  1 
ATOM   5870 C  CD1 . LEU C  1  83  ? 4.067   8.103   19.581 1.00 32.85  ? 96  LEU C CD1 1 
ATOM   5871 C  CD2 . LEU C  1  83  ? 1.967   9.160   18.730 1.00 33.63  ? 96  LEU C CD2 1 
ATOM   5872 N  N   . GLY C  1  84  ? 0.933   4.748   19.772 1.00 35.83  ? 97  GLY C N   1 
ATOM   5873 C  CA  . GLY C  1  84  ? 0.149   4.365   20.935 1.00 35.86  ? 97  GLY C CA  1 
ATOM   5874 C  C   . GLY C  1  84  ? 0.596   3.020   21.503 1.00 33.87  ? 97  GLY C C   1 
ATOM   5875 O  O   . GLY C  1  84  ? 0.634   2.852   22.711 1.00 36.02  ? 97  GLY C O   1 
ATOM   5876 N  N   . HIS C  1  85  ? 0.941   2.073   20.625 1.00 31.80  ? 98  HIS C N   1 
ATOM   5877 C  CA  . HIS C  1  85  ? 1.307   0.726   21.036 1.00 31.74  ? 98  HIS C CA  1 
ATOM   5878 C  C   . HIS C  1  85  ? 2.690   0.707   21.700 1.00 33.17  ? 98  HIS C C   1 
ATOM   5879 O  O   . HIS C  1  85  ? 2.871   0.060   22.721 1.00 31.90  ? 98  HIS C O   1 
ATOM   5880 C  CB  . HIS C  1  85  ? 1.294   -0.221  19.837 1.00 30.58  ? 98  HIS C CB  1 
ATOM   5881 C  CG  . HIS C  1  85  ? 1.492   -1.652  20.175 1.00 31.28  ? 98  HIS C CG  1 
ATOM   5882 N  ND1 . HIS C  1  85  ? 0.775   -2.299  21.153 1.00 30.89  ? 98  HIS C ND1 1 
ATOM   5883 C  CD2 . HIS C  1  85  ? 2.306   -2.587  19.629 1.00 34.35  ? 98  HIS C CD2 1 
ATOM   5884 C  CE1 . HIS C  1  85  ? 1.168   -3.575  21.204 1.00 32.94  ? 98  HIS C CE1 1 
ATOM   5885 N  NE2 . HIS C  1  85  ? 2.101   -3.777  20.291 1.00 32.22  ? 98  HIS C NE2 1 
ATOM   5886 N  N   . LEU C  1  86  ? 3.675   1.396   21.122 1.00 32.84  ? 99  LEU C N   1 
ATOM   5887 C  CA  . LEU C  1  86  ? 5.015   1.428   21.695 1.00 33.98  ? 99  LEU C CA  1 
ATOM   5888 C  C   . LEU C  1  86  ? 4.986   1.975   23.122 1.00 33.29  ? 99  LEU C C   1 
ATOM   5889 O  O   . LEU C  1  86  ? 5.617   1.410   24.006 1.00 32.73  ? 99  LEU C O   1 
ATOM   5890 C  CB  . LEU C  1  86  ? 5.944   2.248   20.799 1.00 31.08  ? 99  LEU C CB  1 
ATOM   5891 C  CG  . LEU C  1  86  ? 6.423   1.528   19.534 1.00 31.31  ? 99  LEU C CG  1 
ATOM   5892 C  CD1 . LEU C  1  86  ? 6.998   2.503   18.523 1.00 30.88  ? 99  LEU C CD1 1 
ATOM   5893 C  CD2 . LEU C  1  86  ? 7.441   0.451   19.876 1.00 30.80  ? 99  LEU C CD2 1 
ATOM   5894 N  N   . LEU C  1  87  ? 4.251   3.076   23.322 1.00 34.35  ? 100 LEU C N   1 
ATOM   5895 C  CA  . LEU C  1  87  ? 4.199   3.789   24.590 1.00 32.45  ? 100 LEU C CA  1 
ATOM   5896 C  C   . LEU C  1  87  ? 3.241   3.126   25.579 1.00 33.88  ? 100 LEU C C   1 
ATOM   5897 O  O   . LEU C  1  87  ? 3.520   3.116   26.775 1.00 32.01  ? 100 LEU C O   1 
ATOM   5898 C  CB  . LEU C  1  87  ? 3.801   5.240   24.343 1.00 29.87  ? 100 LEU C CB  1 
ATOM   5899 C  CG  . LEU C  1  87  ? 4.805   6.063   23.536 1.00 31.39  ? 100 LEU C CG  1 
ATOM   5900 C  CD1 . LEU C  1  87  ? 4.294   7.466   23.348 1.00 33.67  ? 100 LEU C CD1 1 
ATOM   5901 C  CD2 . LEU C  1  87  ? 6.187   6.106   24.167 1.00 31.58  ? 100 LEU C CD2 1 
ATOM   5902 N  N   . ASN C  1  88  ? 2.117   2.581   25.094 1.00 34.20  ? 101 ASN C N   1 
ATOM   5903 C  CA  . ASN C  1  88  ? 1.022   2.227   25.987 1.00 35.10  ? 101 ASN C CA  1 
ATOM   5904 C  C   . ASN C  1  88  ? 0.537   0.785   25.825 1.00 35.69  ? 101 ASN C C   1 
ATOM   5905 O  O   . ASN C  1  88  ? -0.388  0.390   26.532 1.00 34.90  ? 101 ASN C O   1 
ATOM   5906 C  CB  . ASN C  1  88  ? -0.197  3.105   25.767 1.00 35.16  ? 101 ASN C CB  1 
ATOM   5907 C  CG  . ASN C  1  88  ? 0.107   4.576   25.911 1.00 39.16  ? 101 ASN C CG  1 
ATOM   5908 O  OD1 . ASN C  1  88  ? 0.735   5.017   26.883 1.00 43.30  ? 101 ASN C OD1 1 
ATOM   5909 N  ND2 . ASN C  1  88  ? -0.363  5.366   24.963 1.00 41.88  ? 101 ASN C ND2 1 
ATOM   5910 N  N   . GLY C  1  89  ? 1.136   0.003   24.922 1.00 32.06  ? 102 GLY C N   1 
ATOM   5911 C  CA  . GLY C  1  89  ? 0.648   -1.340  24.646 1.00 31.42  ? 102 GLY C CA  1 
ATOM   5912 C  C   . GLY C  1  89  ? 1.576   -2.400  25.221 1.00 33.25  ? 102 GLY C C   1 
ATOM   5913 O  O   . GLY C  1  89  ? 2.636   -2.076  25.750 1.00 37.93  ? 102 GLY C O   1 
ATOM   5914 N  N   . ASN C  1  90  ? 1.172   -3.667  25.108 1.00 31.77  ? 103 ASN C N   1 
ATOM   5915 C  CA  . ASN C  1  90  ? 1.992   -4.770  25.556 1.00 33.11  ? 103 ASN C CA  1 
ATOM   5916 C  C   . ASN C  1  90  ? 2.648   -5.388  24.331 1.00 35.29  ? 103 ASN C C   1 
ATOM   5917 O  O   . ASN C  1  90  ? 1.963   -6.002  23.517 1.00 39.09  ? 103 ASN C O   1 
ATOM   5918 C  CB  . ASN C  1  90  ? 1.151   -5.760  26.351 1.00 36.79  ? 103 ASN C CB  1 
ATOM   5919 C  CG  . ASN C  1  90  ? 1.959   -6.921  26.896 1.00 39.89  ? 103 ASN C CG  1 
ATOM   5920 O  OD1 . ASN C  1  90  ? 2.781   -7.515  26.185 1.00 38.03  ? 103 ASN C OD1 1 
ATOM   5921 N  ND2 . ASN C  1  90  ? 1.734   -7.267  28.158 1.00 42.03  ? 103 ASN C ND2 1 
ATOM   5922 N  N   . LEU C  1  91  ? 3.971   -5.246  24.210 1.00 37.79  ? 104 LEU C N   1 
ATOM   5923 C  CA  . LEU C  1  91  ? 4.653   -5.608  22.972 1.00 38.66  ? 104 LEU C CA  1 
ATOM   5924 C  C   . LEU C  1  91  ? 4.790   -7.120  22.824 1.00 35.95  ? 104 LEU C C   1 
ATOM   5925 O  O   . LEU C  1  91  ? 4.930   -7.639  21.723 1.00 35.42  ? 104 LEU C O   1 
ATOM   5926 C  CB  . LEU C  1  91  ? 5.997   -4.894  22.955 1.00 42.91  ? 104 LEU C CB  1 
ATOM   5927 C  CG  . LEU C  1  91  ? 5.871   -3.371  22.949 1.00 50.24  ? 104 LEU C CG  1 
ATOM   5928 C  CD1 . LEU C  1  91  ? 7.213   -2.726  23.168 1.00 58.60  ? 104 LEU C CD1 1 
ATOM   5929 C  CD2 . LEU C  1  91  ? 5.265   -2.893  21.640 1.00 57.90  ? 104 LEU C CD2 1 
ATOM   5930 N  N   . VAL C  1  92  ? 4.711   -7.833  23.945 1.00 36.74  ? 105 VAL C N   1 
ATOM   5931 C  CA  . VAL C  1  92  ? 4.906   -9.269  23.946 1.00 39.82  ? 105 VAL C CA  1 
ATOM   5932 C  C   . VAL C  1  92  ? 3.636   -9.979  23.489 1.00 43.07  ? 105 VAL C C   1 
ATOM   5933 O  O   . VAL C  1  92  ? 3.717   -10.917 22.698 1.00 46.71  ? 105 VAL C O   1 
ATOM   5934 C  CB  . VAL C  1  92  ? 5.382   -9.723  25.333 1.00 41.21  ? 105 VAL C CB  1 
ATOM   5935 C  CG1 . VAL C  1  92  ? 5.343   -11.236 25.458 1.00 41.88  ? 105 VAL C CG1 1 
ATOM   5936 C  CG2 . VAL C  1  92  ? 6.792   -9.194  25.621 1.00 42.07  ? 105 VAL C CG2 1 
ATOM   5937 N  N   . THR C  1  93  ? 2.474   -9.543  23.997 1.00 44.07  ? 106 THR C N   1 
ATOM   5938 C  CA  . THR C  1  93  ? 1.193   -10.122 23.606 1.00 43.21  ? 106 THR C CA  1 
ATOM   5939 C  C   . THR C  1  93  ? 0.618   -9.422  22.376 1.00 42.41  ? 106 THR C C   1 
ATOM   5940 O  O   . THR C  1  93  ? -0.310  -9.939  21.769 1.00 48.38  ? 106 THR C O   1 
ATOM   5941 C  CB  . THR C  1  93  ? 0.172   -10.071 24.745 1.00 42.94  ? 106 THR C CB  1 
ATOM   5942 O  OG1 . THR C  1  93  ? -0.096  -8.703  25.033 1.00 40.02  ? 106 THR C OG1 1 
ATOM   5943 C  CG2 . THR C  1  93  ? 0.641   -10.804 25.988 1.00 44.39  ? 106 THR C CG2 1 
ATOM   5944 N  N   . ASP C  1  94  ? 1.116   -8.226  22.057 1.00 40.04  ? 107 ASP C N   1 
ATOM   5945 C  CA  . ASP C  1  94  ? 0.694   -7.495  20.871 1.00 39.23  ? 107 ASP C CA  1 
ATOM   5946 C  C   . ASP C  1  94  ? -0.724  -6.964  21.039 1.00 36.63  ? 107 ASP C C   1 
ATOM   5947 O  O   . ASP C  1  94  ? -1.481  -6.905  20.071 1.00 40.43  ? 107 ASP C O   1 
ATOM   5948 C  CB  . ASP C  1  94  ? 0.828   -8.343  19.610 1.00 40.43  ? 107 ASP C CB  1 
ATOM   5949 C  CG  . ASP C  1  94  ? 0.861   -7.581  18.292 1.00 39.13  ? 107 ASP C CG  1 
ATOM   5950 O  OD1 . ASP C  1  94  ? 1.582   -6.557  18.219 1.00 40.96  ? 107 ASP C OD1 1 
ATOM   5951 O  OD2 . ASP C  1  94  ? 0.191   -8.040  17.342 1.00 37.57  ? 107 ASP C OD2 1 
ATOM   5952 N  N   . LEU C  1  95  ? -1.059  -6.522  22.256 1.00 35.10  ? 108 LEU C N   1 
ATOM   5953 C  CA  . LEU C  1  95  ? -2.383  -6.004  22.553 1.00 35.09  ? 108 LEU C CA  1 
ATOM   5954 C  C   . LEU C  1  95  ? -2.276  -4.600  23.136 1.00 32.42  ? 108 LEU C C   1 
ATOM   5955 O  O   . LEU C  1  95  ? -1.424  -4.338  23.974 1.00 33.74  ? 108 LEU C O   1 
ATOM   5956 C  CB  . LEU C  1  95  ? -3.092  -6.961  23.514 1.00 37.85  ? 108 LEU C CB  1 
ATOM   5957 C  CG  . LEU C  1  95  ? -3.401  -8.364  22.982 1.00 37.78  ? 108 LEU C CG  1 
ATOM   5958 C  CD1 . LEU C  1  95  ? -3.845  -9.259  24.124 1.00 38.63  ? 108 LEU C CD1 1 
ATOM   5959 C  CD2 . LEU C  1  95  ? -4.473  -8.291  21.902 1.00 37.87  ? 108 LEU C CD2 1 
ATOM   5960 N  N   . LEU C  1  96  ? -3.195  -3.729  22.708 1.00 33.85  ? 109 LEU C N   1 
ATOM   5961 C  CA  . LEU C  1  96  ? -3.291  -2.362  23.181 1.00 34.02  ? 109 LEU C CA  1 
ATOM   5962 C  C   . LEU C  1  96  ? -4.712  -2.097  23.684 1.00 38.79  ? 109 LEU C C   1 
ATOM   5963 O  O   . LEU C  1  96  ? -5.686  -2.419  23.002 1.00 39.36  ? 109 LEU C O   1 
ATOM   5964 C  CB  . LEU C  1  96  ? -2.946  -1.467  21.994 1.00 32.71  ? 109 LEU C CB  1 
ATOM   5965 C  CG  . LEU C  1  96  ? -3.231  0.025   22.165 1.00 32.63  ? 109 LEU C CG  1 
ATOM   5966 C  CD1 . LEU C  1  96  ? -2.441  0.566   23.369 1.00 36.37  ? 109 LEU C CD1 1 
ATOM   5967 C  CD2 . LEU C  1  96  ? -2.869  0.813   20.924 1.00 30.49  ? 109 LEU C CD2 1 
ATOM   5968 N  N   . SER C  1  97  ? -4.823  -1.520  24.887 1.00 36.53  ? 110 SER C N   1 
ATOM   5969 C  CA  . SER C  1  97  ? -6.092  -1.034  25.405 1.00 36.03  ? 110 SER C CA  1 
ATOM   5970 C  C   . SER C  1  97  ? -6.363  0.347   24.841 1.00 34.48  ? 110 SER C C   1 
ATOM   5971 O  O   . SER C  1  97  ? -5.497  1.214   24.926 1.00 36.55  ? 110 SER C O   1 
ATOM   5972 C  CB  . SER C  1  97  ? -6.075  -0.962  26.913 1.00 38.70  ? 110 SER C CB  1 
ATOM   5973 O  OG  . SER C  1  97  ? -7.187  -0.220  27.397 1.00 41.00  ? 110 SER C OG  1 
ATOM   5974 N  N   . ILE C  1  98  ? -7.581  0.584   24.341 1.00 35.60  ? 111 ILE C N   1 
ATOM   5975 C  CA  . ILE C  1  98  ? -7.908  1.899   23.811 1.00 38.49  ? 111 ILE C CA  1 
ATOM   5976 C  C   . ILE C  1  98  ? -8.332  2.835   24.938 1.00 38.33  ? 111 ILE C C   1 
ATOM   5977 O  O   . ILE C  1  98  ? -8.684  3.991   24.683 1.00 42.75  ? 111 ILE C O   1 
ATOM   5978 C  CB  . ILE C  1  98  ? -8.965  1.830   22.695 1.00 40.58  ? 111 ILE C CB  1 
ATOM   5979 C  CG1 . ILE C  1  98  ? -10.338 1.425   23.210 1.00 43.03  ? 111 ILE C CG1 1 
ATOM   5980 C  CG2 . ILE C  1  98  ? -8.483  0.923   21.564 1.00 41.19  ? 111 ILE C CG2 1 
ATOM   5981 C  CD1 . ILE C  1  98  ? -11.433 1.507   22.156 1.00 44.99  ? 111 ILE C CD1 1 
ATOM   5982 N  N   . GLY C  1  99  ? -8.294  2.332   26.177 1.00 40.03  ? 112 GLY C N   1 
ATOM   5983 C  CA  . GLY C  1  99  ? -8.637  3.123   27.346 1.00 39.98  ? 112 GLY C CA  1 
ATOM   5984 C  C   . GLY C  1  99  ? -7.606  2.946   28.457 1.00 41.29  ? 112 GLY C C   1 
ATOM   5985 O  O   . GLY C  1  99  ? -6.437  3.299   28.284 1.00 39.75  ? 112 GLY C O   1 
ATOM   5986 N  N   . GLY C  1  100 ? -8.062  2.426   29.605 1.00 41.68  ? 113 GLY C N   1 
ATOM   5987 C  CA  . GLY C  1  100 ? -7.213  2.290   30.778 1.00 43.20  ? 113 GLY C CA  1 
ATOM   5988 C  C   . GLY C  1  100 ? -6.645  0.876   30.914 1.00 42.36  ? 113 GLY C C   1 
ATOM   5989 O  O   . GLY C  1  100 ? -6.792  0.054   30.008 1.00 41.28  ? 113 GLY C O   1 
ATOM   5990 N  N   . ALA C  1  101 ? -6.020  0.613   32.068 1.00 43.17  ? 114 ALA C N   1 
ATOM   5991 C  CA  . ALA C  1  101 ? -5.306  -0.633  32.303 1.00 47.30  ? 114 ALA C CA  1 
ATOM   5992 C  C   . ALA C  1  101 ? -6.291  -1.788  32.423 1.00 48.05  ? 114 ALA C C   1 
ATOM   5993 O  O   . ALA C  1  101 ? -7.412  -1.599  32.885 1.00 57.49  ? 114 ALA C O   1 
ATOM   5994 C  CB  . ALA C  1  101 ? -4.455  -0.512  33.546 1.00 47.39  ? 114 ALA C CB  1 
ATOM   5995 N  N   . THR C  1  102 ? -5.869  -2.985  32.014 1.00 45.68  ? 115 THR C N   1 
ATOM   5996 C  CA  . THR C  1  102 ? -6.772  -4.120  32.043 1.00 52.24  ? 115 THR C CA  1 
ATOM   5997 C  C   . THR C  1  102 ? -5.960  -5.403  32.016 1.00 51.17  ? 115 THR C C   1 
ATOM   5998 O  O   . THR C  1  102 ? -4.970  -5.477  31.308 1.00 52.69  ? 115 THR C O   1 
ATOM   5999 C  CB  . THR C  1  102 ? -7.756  -4.052  30.868 1.00 57.10  ? 115 THR C CB  1 
ATOM   6000 O  OG1 . THR C  1  102 ? -8.611  -5.190  30.888 1.00 56.34  ? 115 THR C OG1 1 
ATOM   6001 C  CG2 . THR C  1  102 ? -7.091  -4.159  29.513 1.00 59.88  ? 115 THR C CG2 1 
ATOM   6002 N  N   . PRO C  1  103 ? -6.385  -6.465  32.736 1.00 55.96  ? 116 PRO C N   1 
ATOM   6003 C  CA  . PRO C  1  103 ? -5.740  -7.774  32.601 1.00 57.51  ? 116 PRO C CA  1 
ATOM   6004 C  C   . PRO C  1  103 ? -5.839  -8.377  31.199 1.00 54.78  ? 116 PRO C C   1 
ATOM   6005 O  O   . PRO C  1  103 ? -5.088  -9.288  30.880 1.00 50.70  ? 116 PRO C O   1 
ATOM   6006 C  CB  . PRO C  1  103 ? -6.437  -8.654  33.665 1.00 60.39  ? 116 PRO C CB  1 
ATOM   6007 C  CG  . PRO C  1  103 ? -7.741  -7.934  33.969 1.00 63.29  ? 116 PRO C CG  1 
ATOM   6008 C  CD  . PRO C  1  103 ? -7.480  -6.454  33.722 1.00 59.47  ? 116 PRO C CD  1 
ATOM   6009 N  N   . LYS C  1  104 ? -6.745  -7.853  30.359 1.00 56.29  ? 117 LYS C N   1 
ATOM   6010 C  CA  . LYS C  1  104 ? -6.950  -8.373  29.017 1.00 55.33  ? 117 LYS C CA  1 
ATOM   6011 C  C   . LYS C  1  104 ? -5.722  -8.204  28.115 1.00 53.71  ? 117 LYS C C   1 
ATOM   6012 O  O   . LYS C  1  104 ? -5.610  -8.910  27.114 1.00 52.93  ? 117 LYS C O   1 
ATOM   6013 C  CB  . LYS C  1  104 ? -8.148  -7.656  28.385 1.00 62.76  ? 117 LYS C CB  1 
ATOM   6014 C  CG  . LYS C  1  104 ? -9.512  -7.965  28.978 1.00 64.91  ? 117 LYS C CG  1 
ATOM   6015 C  CD  . LYS C  1  104 ? -10.550 -6.911  28.613 1.00 71.01  ? 117 LYS C CD  1 
ATOM   6016 C  CE  . LYS C  1  104 ? -11.917 -7.178  29.141 1.00 74.46  ? 117 LYS C CE  1 
ATOM   6017 N  NZ  . LYS C  1  104 ? -12.514 -8.305  28.429 1.00 80.02  ? 117 LYS C NZ  1 
ATOM   6018 N  N   . THR C  1  105 ? -4.815  -7.259  28.427 1.00 53.09  ? 118 THR C N   1 
ATOM   6019 C  CA  . THR C  1  105 ? -3.605  -7.081  27.626 1.00 48.84  ? 118 THR C CA  1 
ATOM   6020 C  C   . THR C  1  105 ? -2.531  -8.073  28.062 1.00 46.85  ? 118 THR C C   1 
ATOM   6021 O  O   . THR C  1  105 ? -1.522  -8.216  27.378 1.00 45.66  ? 118 THR C O   1 
ATOM   6022 C  CB  . THR C  1  105 ? -3.065  -5.648  27.654 1.00 43.59  ? 118 THR C CB  1 
ATOM   6023 O  OG1 . THR C  1  105 ? -2.873  -5.223  28.996 1.00 39.22  ? 118 THR C OG1 1 
ATOM   6024 C  CG2 . THR C  1  105 ? -3.990  -4.653  26.968 1.00 42.34  ? 118 THR C CG2 1 
ATOM   6025 N  N   . GLY C  1  106 ? -2.758  -8.739  29.201 1.00 49.31  ? 119 GLY C N   1 
ATOM   6026 C  CA  . GLY C  1  106 ? -1.917  -9.836  29.658 1.00 51.81  ? 119 GLY C CA  1 
ATOM   6027 C  C   . GLY C  1  106 ? -0.948  -9.417  30.765 1.00 52.43  ? 119 GLY C C   1 
ATOM   6028 O  O   . GLY C  1  106 ? -1.003  -8.286  31.256 1.00 48.29  ? 119 GLY C O   1 
ATOM   6029 N  N   . PRO C  1  107 ? -0.017  -10.325 31.158 1.00 50.91  ? 120 PRO C N   1 
ATOM   6030 C  CA  . PRO C  1  107 ? 0.966   -10.054 32.213 1.00 53.03  ? 120 PRO C CA  1 
ATOM   6031 C  C   . PRO C  1  107 ? 1.706   -8.736  32.010 1.00 53.40  ? 120 PRO C C   1 
ATOM   6032 O  O   . PRO C  1  107 ? 2.317   -8.526  30.968 1.00 56.62  ? 120 PRO C O   1 
ATOM   6033 C  CB  . PRO C  1  107 ? 1.938   -11.248 32.112 1.00 53.77  ? 120 PRO C CB  1 
ATOM   6034 C  CG  . PRO C  1  107 ? 1.140   -12.354 31.460 1.00 52.50  ? 120 PRO C CG  1 
ATOM   6035 C  CD  . PRO C  1  107 ? 0.130   -11.664 30.566 1.00 49.72  ? 120 PRO C CD  1 
ATOM   6036 N  N   . PRO C  1  108 ? 1.719   -7.819  32.998 1.00 59.42  ? 121 PRO C N   1 
ATOM   6037 C  CA  . PRO C  1  108 ? 2.287   -6.488  32.779 1.00 56.23  ? 121 PRO C CA  1 
ATOM   6038 C  C   . PRO C  1  108 ? 3.782   -6.584  32.473 1.00 55.62  ? 121 PRO C C   1 
ATOM   6039 O  O   . PRO C  1  108 ? 4.451   -7.523  32.907 1.00 49.62  ? 121 PRO C O   1 
ATOM   6040 C  CB  . PRO C  1  108 ? 1.988   -5.694  34.064 1.00 55.04  ? 121 PRO C CB  1 
ATOM   6041 C  CG  . PRO C  1  108 ? 1.660   -6.753  35.107 1.00 58.63  ? 121 PRO C CG  1 
ATOM   6042 C  CD  . PRO C  1  108 ? 1.224   -8.020  34.368 1.00 61.91  ? 121 PRO C CD  1 
ATOM   6043 N  N   . PRO C  1  109 ? 4.339   -5.652  31.660 1.00 54.74  ? 122 PRO C N   1 
ATOM   6044 C  CA  . PRO C  1  109 ? 5.769   -5.648  31.357 1.00 53.64  ? 122 PRO C CA  1 
ATOM   6045 C  C   . PRO C  1  109 ? 6.595   -5.111  32.521 1.00 53.84  ? 122 PRO C C   1 
ATOM   6046 O  O   . PRO C  1  109 ? 6.035   -4.562  33.468 1.00 57.88  ? 122 PRO C O   1 
ATOM   6047 C  CB  . PRO C  1  109 ? 5.812   -4.720  30.132 1.00 49.42  ? 122 PRO C CB  1 
ATOM   6048 C  CG  . PRO C  1  109 ? 4.702   -3.736  30.372 1.00 46.90  ? 122 PRO C CG  1 
ATOM   6049 C  CD  . PRO C  1  109 ? 3.613   -4.574  30.977 1.00 48.25  ? 122 PRO C CD  1 
ATOM   6050 N  N   . PRO C  1  110 ? 7.942   -5.232  32.476 1.00 56.75  ? 123 PRO C N   1 
ATOM   6051 C  CA  . PRO C  1  110 ? 8.814   -4.693  33.526 1.00 56.74  ? 123 PRO C CA  1 
ATOM   6052 C  C   . PRO C  1  110 ? 8.814   -3.173  33.559 1.00 48.24  ? 123 PRO C C   1 
ATOM   6053 O  O   . PRO C  1  110 ? 8.939   -2.548  32.515 1.00 47.18  ? 123 PRO C O   1 
ATOM   6054 C  CB  . PRO C  1  110 ? 10.209  -5.242  33.182 1.00 57.27  ? 123 PRO C CB  1 
ATOM   6055 C  CG  . PRO C  1  110 ? 10.140  -5.495  31.698 1.00 57.08  ? 123 PRO C CG  1 
ATOM   6056 C  CD  . PRO C  1  110 ? 8.704   -5.931  31.430 1.00 57.74  ? 123 PRO C CD  1 
ATOM   6057 N  N   . PRO C  1  111 ? 8.661   -2.544  34.746 1.00 45.36  ? 124 PRO C N   1 
ATOM   6058 C  CA  . PRO C  1  111 ? 8.667   -1.081  34.850 1.00 42.78  ? 124 PRO C CA  1 
ATOM   6059 C  C   . PRO C  1  111 ? 9.977   -0.492  34.333 1.00 40.06  ? 124 PRO C C   1 
ATOM   6060 O  O   . PRO C  1  111 ? 10.995  -1.179  34.339 1.00 36.26  ? 124 PRO C O   1 
ATOM   6061 C  CB  . PRO C  1  111 ? 8.458   -0.802  36.358 1.00 43.97  ? 124 PRO C CB  1 
ATOM   6062 C  CG  . PRO C  1  111 ? 7.869   -2.087  36.907 1.00 44.90  ? 124 PRO C CG  1 
ATOM   6063 C  CD  . PRO C  1  111 ? 8.391   -3.206  36.030 1.00 44.19  ? 124 PRO C CD  1 
ATOM   6064 N  N   . PRO C  1  112 ? 10.034  0.790   33.902 1.00 38.67  ? 125 PRO C N   1 
ATOM   6065 C  CA  . PRO C  1  112 ? 8.906   1.732   33.947 1.00 41.72  ? 125 PRO C CA  1 
ATOM   6066 C  C   . PRO C  1  112 ? 7.803   1.602   32.894 1.00 42.04  ? 125 PRO C C   1 
ATOM   6067 O  O   . PRO C  1  112 ? 6.877   2.415   32.879 1.00 39.48  ? 125 PRO C O   1 
ATOM   6068 C  CB  . PRO C  1  112 ? 9.553   3.135   33.818 1.00 39.80  ? 125 PRO C CB  1 
ATOM   6069 C  CG  . PRO C  1  112 ? 11.037  2.888   33.659 1.00 42.54  ? 125 PRO C CG  1 
ATOM   6070 C  CD  . PRO C  1  112 ? 11.249  1.404   33.365 1.00 39.51  ? 125 PRO C CD  1 
ATOM   6071 N  N   . ALA C  1  113 ? 7.901   0.596   32.019 1.00 40.98  ? 126 ALA C N   1 
ATOM   6072 C  CA  . ALA C  1  113 ? 6.847   0.335   31.057 1.00 44.46  ? 126 ALA C CA  1 
ATOM   6073 C  C   . ALA C  1  113 ? 5.605   -0.144  31.802 1.00 46.54  ? 126 ALA C C   1 
ATOM   6074 O  O   . ALA C  1  113 ? 5.722   -0.754  32.856 1.00 50.27  ? 126 ALA C O   1 
ATOM   6075 C  CB  . ALA C  1  113 ? 7.314   -0.676  30.027 1.00 45.14  ? 126 ALA C CB  1 
ATOM   6076 N  N   . HIS C  1  114 ? 4.424   0.121   31.233 1.00 45.37  ? 127 HIS C N   1 
ATOM   6077 C  CA  . HIS C  1  114 ? 3.164   -0.040  31.947 1.00 42.95  ? 127 HIS C CA  1 
ATOM   6078 C  C   . HIS C  1  114 ? 2.127   -0.793  31.114 1.00 45.51  ? 127 HIS C C   1 
ATOM   6079 O  O   . HIS C  1  114 ? 1.395   -1.624  31.644 1.00 47.38  ? 127 HIS C O   1 
ATOM   6080 C  CB  . HIS C  1  114 ? 2.643   1.323   32.411 1.00 41.47  ? 127 HIS C CB  1 
ATOM   6081 C  CG  . HIS C  1  114 ? 2.777   2.382   31.375 1.00 43.81  ? 127 HIS C CG  1 
ATOM   6082 N  ND1 . HIS C  1  114 ? 1.859   2.480   30.356 1.00 41.87  ? 127 HIS C ND1 1 
ATOM   6083 C  CD2 . HIS C  1  114 ? 3.687   3.354   31.166 1.00 40.91  ? 127 HIS C CD2 1 
ATOM   6084 C  CE1 . HIS C  1  114 ? 2.209   3.494   29.577 1.00 40.73  ? 127 HIS C CE1 1 
ATOM   6085 N  NE2 . HIS C  1  114 ? 3.305   4.046   30.053 1.00 40.18  ? 127 HIS C NE2 1 
ATOM   6086 N  N   . ALA C  1  115 ? 2.047   -0.498  29.811 1.00 47.87  ? 128 ALA C N   1 
ATOM   6087 C  CA  . ALA C  1  115 ? 1.005   -1.050  28.957 1.00 42.16  ? 128 ALA C CA  1 
ATOM   6088 C  C   . ALA C  1  115 ? -0.375  -0.683  29.495 1.00 36.17  ? 128 ALA C C   1 
ATOM   6089 O  O   . ALA C  1  115 ? -1.280  -1.504  29.459 1.00 33.95  ? 128 ALA C O   1 
ATOM   6090 C  CB  . ALA C  1  115 ? 1.153   -2.554  28.812 1.00 42.84  ? 128 ALA C CB  1 
ATOM   6091 N  N   . GLY C  1  116 ? -0.534  0.574   29.919 1.00 35.55  ? 129 GLY C N   1 
ATOM   6092 C  CA  . GLY C  1  116 ? -1.728  1.014   30.623 1.00 36.21  ? 129 GLY C CA  1 
ATOM   6093 C  C   . GLY C  1  116 ? -2.756  1.682   29.710 1.00 39.07  ? 129 GLY C C   1 
ATOM   6094 O  O   . GLY C  1  116 ? -3.731  2.242   30.208 1.00 40.59  ? 129 GLY C O   1 
ATOM   6095 N  N   . GLY C  1  117 ? -2.515  1.641   28.386 1.00 37.24  ? 130 GLY C N   1 
ATOM   6096 C  CA  . GLY C  1  117 ? -3.500  2.021   27.391 1.00 32.09  ? 130 GLY C CA  1 
ATOM   6097 C  C   . GLY C  1  117 ? -3.450  3.511   27.070 1.00 30.71  ? 130 GLY C C   1 
ATOM   6098 O  O   . GLY C  1  117 ? -2.657  4.237   27.663 1.00 27.95  ? 130 GLY C O   1 
ATOM   6099 N  N   . LEU C  1  118 ? -4.349  3.952   26.167 1.00 28.64  ? 131 LEU C N   1 
ATOM   6100 C  CA  . LEU C  1  118 ? -4.322  5.302   25.625 1.00 30.75  ? 131 LEU C CA  1 
ATOM   6101 C  C   . LEU C  1  118 ? -4.691  6.356   26.663 1.00 31.95  ? 131 LEU C C   1 
ATOM   6102 O  O   . LEU C  1  118 ? -4.501  7.537   26.411 1.00 32.32  ? 131 LEU C O   1 
ATOM   6103 C  CB  . LEU C  1  118 ? -5.263  5.372   24.423 1.00 32.50  ? 131 LEU C CB  1 
ATOM   6104 C  CG  . LEU C  1  118 ? -4.899  4.477   23.232 1.00 34.46  ? 131 LEU C CG  1 
ATOM   6105 C  CD1 . LEU C  1  118 ? -5.915  4.599   22.120 1.00 33.88  ? 131 LEU C CD1 1 
ATOM   6106 C  CD2 . LEU C  1  118 ? -3.504  4.823   22.700 1.00 33.43  ? 131 LEU C CD2 1 
ATOM   6107 N  N   . ASN C  1  119 ? -5.239  5.944   27.813 1.00 35.99  ? 132 ASN C N   1 
ATOM   6108 C  CA  . ASN C  1  119 ? -5.569  6.877   28.878 1.00 39.77  ? 132 ASN C CA  1 
ATOM   6109 C  C   . ASN C  1  119 ? -4.331  7.507   29.504 1.00 39.58  ? 132 ASN C C   1 
ATOM   6110 O  O   . ASN C  1  119 ? -4.450  8.563   30.111 1.00 38.46  ? 132 ASN C O   1 
ATOM   6111 C  CB  . ASN C  1  119 ? -6.330  6.221   30.022 1.00 43.77  ? 132 ASN C CB  1 
ATOM   6112 C  CG  . ASN C  1  119 ? -7.782  5.983   29.689 1.00 48.36  ? 132 ASN C CG  1 
ATOM   6113 O  OD1 . ASN C  1  119 ? -8.245  6.297   28.587 1.00 46.92  ? 132 ASN C OD1 1 
ATOM   6114 N  ND2 . ASN C  1  119 ? -8.523  5.421   30.630 1.00 51.25  ? 132 ASN C ND2 1 
ATOM   6115 N  N   . VAL C  1  120 ? -3.165  6.858   29.384 1.00 39.76  ? 133 VAL C N   1 
ATOM   6116 C  CA  . VAL C  1  120 ? -1.959  7.318   30.056 1.00 39.35  ? 133 VAL C CA  1 
ATOM   6117 C  C   . VAL C  1  120 ? -1.583  8.717   29.567 1.00 40.44  ? 133 VAL C C   1 
ATOM   6118 O  O   . VAL C  1  120 ? -1.361  8.929   28.383 1.00 44.76  ? 133 VAL C O   1 
ATOM   6119 C  CB  . VAL C  1  120 ? -0.806  6.320   29.859 1.00 39.47  ? 133 VAL C CB  1 
ATOM   6120 C  CG1 . VAL C  1  120 ? 0.524   6.876   30.350 1.00 40.37  ? 133 VAL C CG1 1 
ATOM   6121 C  CG2 . VAL C  1  120 ? -1.102  4.988   30.530 1.00 38.30  ? 133 VAL C CG2 1 
ATOM   6122 N  N   . HIS C  1  121 ? -1.469  9.651   30.517 1.00 42.85  ? 134 HIS C N   1 
ATOM   6123 C  CA  . HIS C  1  121 ? -1.193  11.053  30.246 1.00 44.29  ? 134 HIS C CA  1 
ATOM   6124 C  C   . HIS C  1  121 ? 0.310   11.279  30.112 1.00 48.29  ? 134 HIS C C   1 
ATOM   6125 O  O   . HIS C  1  121 ? 1.082   10.594  30.770 1.00 47.33  ? 134 HIS C O   1 
ATOM   6126 C  CB  . HIS C  1  121 ? -1.703  11.912  31.413 1.00 43.24  ? 134 HIS C CB  1 
ATOM   6127 C  CG  . HIS C  1  121 ? -1.399  13.369  31.297 1.00 43.60  ? 134 HIS C CG  1 
ATOM   6128 N  ND1 . HIS C  1  121 ? -1.983  14.175  30.339 1.00 49.16  ? 134 HIS C ND1 1 
ATOM   6129 C  CD2 . HIS C  1  121 ? -0.564  14.156  31.982 1.00 43.46  ? 134 HIS C CD2 1 
ATOM   6130 C  CE1 . HIS C  1  121 ? -1.512  15.407  30.456 1.00 49.55  ? 134 HIS C CE1 1 
ATOM   6131 N  NE2 . HIS C  1  121 ? -0.637  15.421  31.440 1.00 49.37  ? 134 HIS C NE2 1 
ATOM   6132 N  N   . GLY C  1  122 ? 0.726   12.247  29.287 1.00 52.36  ? 135 GLY C N   1 
ATOM   6133 C  CA  . GLY C  1  122 ? 2.068   12.784  29.430 1.00 56.72  ? 135 GLY C CA  1 
ATOM   6134 C  C   . GLY C  1  122 ? 2.923   12.716  28.167 1.00 58.00  ? 135 GLY C C   1 
ATOM   6135 O  O   . GLY C  1  122 ? 3.644   13.676  27.912 1.00 53.73  ? 135 GLY C O   1 
ATOM   6136 N  N   . THR C  1  123 ? 2.907   11.596  27.418 1.00 59.92  ? 136 THR C N   1 
ATOM   6137 C  CA  A THR C  1  123 ? 3.765   11.462  26.247 0.50 65.04  ? 136 THR C CA  1 
ATOM   6138 C  CA  B THR C  1  123 ? 3.766   11.476  26.243 0.50 62.81  ? 136 THR C CA  1 
ATOM   6139 C  C   . THR C  1  123 ? 2.922   11.353  24.971 1.00 61.45  ? 136 THR C C   1 
ATOM   6140 O  O   . THR C  1  123 ? 3.357   11.825  23.918 1.00 56.44  ? 136 THR C O   1 
ATOM   6141 C  CB  A THR C  1  123 ? 4.725   10.278  26.418 0.50 69.30  ? 136 THR C CB  1 
ATOM   6142 C  CB  B THR C  1  123 ? 4.769   10.320  26.369 0.50 63.80  ? 136 THR C CB  1 
ATOM   6143 O  OG1 A THR C  1  123 ? 3.908   9.110   26.425 0.50 76.18  ? 136 THR C OG1 1 
ATOM   6144 O  OG1 B THR C  1  123 ? 5.528   10.473  27.568 0.50 64.14  ? 136 THR C OG1 1 
ATOM   6145 C  CG2 A THR C  1  123 ? 5.493   10.299  27.731 0.50 67.13  ? 136 THR C CG2 1 
ATOM   6146 C  CG2 B THR C  1  123 ? 5.737   10.257  25.197 0.50 60.87  ? 136 THR C CG2 1 
ATOM   6147 N  N   . PHE C  1  124 ? 1.733   10.715  25.050 1.00 57.21  ? 137 PHE C N   1 
ATOM   6148 C  CA  . PHE C  1  124 ? 0.784   10.716  23.932 1.00 52.56  ? 137 PHE C CA  1 
ATOM   6149 C  C   . PHE C  1  124 ? -0.422  11.604  24.273 1.00 50.83  ? 137 PHE C C   1 
ATOM   6150 O  O   . PHE C  1  124 ? -0.505  12.727  23.773 1.00 51.67  ? 137 PHE C O   1 
ATOM   6151 C  CB  . PHE C  1  124 ? 0.360   9.313   23.469 1.00 48.13  ? 137 PHE C CB  1 
ATOM   6152 C  CG  . PHE C  1  124 ? -0.352  9.209   22.119 1.00 44.67  ? 137 PHE C CG  1 
ATOM   6153 C  CD1 . PHE C  1  124 ? -0.785  10.326  21.408 1.00 45.41  ? 137 PHE C CD1 1 
ATOM   6154 C  CD2 . PHE C  1  124 ? -0.633  7.965   21.573 1.00 44.66  ? 137 PHE C CD2 1 
ATOM   6155 C  CE1 . PHE C  1  124 ? -1.437  10.198  20.185 1.00 43.45  ? 137 PHE C CE1 1 
ATOM   6156 C  CE2 . PHE C  1  124 ? -1.282  7.838   20.353 1.00 44.89  ? 137 PHE C CE2 1 
ATOM   6157 C  CZ  . PHE C  1  124 ? -1.684  8.959   19.658 1.00 43.28  ? 137 PHE C CZ  1 
ATOM   6158 N  N   . GLU C  1  125 ? -1.375  11.095  25.075 1.00 48.52  ? 138 GLU C N   1 
ATOM   6159 C  CA  . GLU C  1  125 ? -2.541  11.873  25.484 1.00 52.24  ? 138 GLU C CA  1 
ATOM   6160 C  C   . GLU C  1  125 ? -2.083  13.174  26.149 1.00 50.48  ? 138 GLU C C   1 
ATOM   6161 O  O   . GLU C  1  125 ? -1.110  13.178  26.891 1.00 55.26  ? 138 GLU C O   1 
ATOM   6162 C  CB  . GLU C  1  125 ? -3.446  11.111  26.458 1.00 54.55  ? 138 GLU C CB  1 
ATOM   6163 C  CG  . GLU C  1  125 ? -4.818  11.748  26.710 1.00 61.73  ? 138 GLU C CG  1 
ATOM   6164 C  CD  . GLU C  1  125 ? -4.919  13.032  27.539 1.00 63.06  ? 138 GLU C CD  1 
ATOM   6165 O  OE1 . GLU C  1  125 ? -4.213  13.072  28.581 1.00 57.28  ? 138 GLU C OE1 1 
ATOM   6166 O  OE2 . GLU C  1  125 ? -5.704  13.966  27.176 1.00 61.56  ? 138 GLU C OE2 1 
ATOM   6167 N  N   . GLY C  1  126 ? -2.786  14.280  25.869 1.00 48.68  ? 139 GLY C N   1 
ATOM   6168 C  CA  . GLY C  1  126 ? -2.507  15.556  26.502 1.00 46.57  ? 139 GLY C CA  1 
ATOM   6169 C  C   . GLY C  1  126 ? -3.692  16.526  26.484 1.00 49.74  ? 139 GLY C C   1 
ATOM   6170 O  O   . GLY C  1  126 ? -4.861  16.140  26.327 1.00 46.83  ? 139 GLY C O   1 
ATOM   6171 N  N   . ASP C  1  127 ? -3.321  17.814  26.598 1.00 50.86  ? 140 ASP C N   1 
ATOM   6172 C  CA  . ASP C  1  127 ? -4.173  18.864  27.135 1.00 56.00  ? 140 ASP C CA  1 
ATOM   6173 C  C   . ASP C  1  127 ? -4.828  19.648  25.999 1.00 52.28  ? 140 ASP C C   1 
ATOM   6174 O  O   . ASP C  1  127 ? -4.424  19.536  24.848 1.00 52.65  ? 140 ASP C O   1 
ATOM   6175 C  CB  . ASP C  1  127 ? -3.357  19.744  28.076 1.00 56.46  ? 140 ASP C CB  1 
ATOM   6176 C  CG  . ASP C  1  127 ? -2.799  19.080  29.334 1.00 56.70  ? 140 ASP C CG  1 
ATOM   6177 O  OD1 . ASP C  1  127 ? -3.407  18.071  29.808 1.00 49.61  ? 140 ASP C OD1 1 
ATOM   6178 O  OD2 . ASP C  1  127 ? -1.734  19.556  29.823 1.00 53.82  ? 140 ASP C OD2 1 
ATOM   6179 N  N   . ALA C  1  128 ? -5.855  20.434  26.346 1.00 51.53  ? 141 ALA C N   1 
ATOM   6180 C  CA  . ALA C  1  128 ? -6.556  21.317  25.420 1.00 50.38  ? 141 ALA C CA  1 
ATOM   6181 C  C   . ALA C  1  128 ? -7.355  20.524  24.386 1.00 51.40  ? 141 ALA C C   1 
ATOM   6182 O  O   . ALA C  1  128 ? -7.498  20.958  23.246 1.00 51.70  ? 141 ALA C O   1 
ATOM   6183 C  CB  . ALA C  1  128 ? -5.591  22.284  24.779 1.00 47.48  ? 141 ALA C CB  1 
ATOM   6184 N  N   . GLY C  1  129 ? -7.929  19.391  24.810 1.00 53.27  ? 142 GLY C N   1 
ATOM   6185 C  CA  . GLY C  1  129 ? -8.833  18.630  23.962 1.00 59.07  ? 142 GLY C CA  1 
ATOM   6186 C  C   . GLY C  1  129 ? -10.123 19.405  23.690 1.00 61.68  ? 142 GLY C C   1 
ATOM   6187 O  O   . GLY C  1  129 ? -10.376 20.423  24.325 1.00 73.99  ? 142 GLY C O   1 
ATOM   6188 N  N   . MET C  1  130 ? -10.930 18.900  22.750 1.00 63.33  ? 143 MET C N   1 
ATOM   6189 C  CA  . MET C  1  130 ? -12.177 19.537  22.342 1.00 63.49  ? 143 MET C CA  1 
ATOM   6190 C  C   . MET C  1  130 ? -13.343 19.124  23.247 1.00 59.66  ? 143 MET C C   1 
ATOM   6191 O  O   . MET C  1  130 ? -14.108 19.979  23.696 1.00 64.19  ? 143 MET C O   1 
ATOM   6192 C  CB  . MET C  1  130 ? -12.520 19.181  20.891 1.00 67.33  ? 143 MET C CB  1 
ATOM   6193 C  CG  . MET C  1  130 ? -11.689 19.936  19.846 1.00 72.01  ? 143 MET C CG  1 
ATOM   6194 S  SD  . MET C  1  130 ? -12.006 19.425  18.141 1.00 69.94  ? 143 MET C SD  1 
ATOM   6195 C  CE  . MET C  1  130 ? -11.731 17.648  18.204 1.00 59.71  ? 143 MET C CE  1 
ATOM   6196 N  N   . THR C  1  131 ? -13.496 17.811  23.478 1.00 50.53  ? 144 THR C N   1 
ATOM   6197 C  CA  . THR C  1  131 ? -14.573 17.277  24.293 1.00 49.24  ? 144 THR C CA  1 
ATOM   6198 C  C   . THR C  1  131 ? -14.062 16.500  25.510 1.00 49.74  ? 144 THR C C   1 
ATOM   6199 O  O   . THR C  1  131 ? -14.886 15.860  26.177 1.00 50.77  ? 144 THR C O   1 
ATOM   6200 C  CB  . THR C  1  131 ? -15.471 16.368  23.453 1.00 53.03  ? 144 THR C CB  1 
ATOM   6201 O  OG1 . THR C  1  131 ? -14.793 15.141  23.196 1.00 46.92  ? 144 THR C OG1 1 
ATOM   6202 C  CG2 . THR C  1  131 ? -15.873 17.000  22.136 1.00 56.35  ? 144 THR C CG2 1 
ATOM   6203 N  N   . ARG C  1  132 ? -12.746 16.542  25.799 1.00 47.70  ? 145 ARG C N   1 
ATOM   6204 C  CA  . ARG C  1  132 ? -12.199 15.947  27.017 1.00 49.29  ? 145 ARG C CA  1 
ATOM   6205 C  C   . ARG C  1  132 ? -11.414 16.986  27.823 1.00 48.76  ? 145 ARG C C   1 
ATOM   6206 O  O   . ARG C  1  132 ? -10.734 17.830  27.240 1.00 50.17  ? 145 ARG C O   1 
ATOM   6207 C  CB  . ARG C  1  132 ? -11.304 14.742  26.715 1.00 49.17  ? 145 ARG C CB  1 
ATOM   6208 C  CG  . ARG C  1  132 ? -12.038 13.414  26.607 1.00 50.12  ? 145 ARG C CG  1 
ATOM   6209 C  CD  . ARG C  1  132 ? -12.712 13.193  25.264 1.00 51.86  ? 145 ARG C CD  1 
ATOM   6210 N  NE  . ARG C  1  132 ? -13.371 11.882  25.242 1.00 51.67  ? 145 ARG C NE  1 
ATOM   6211 C  CZ  . ARG C  1  132 ? -14.517 11.601  24.648 1.00 52.74  ? 145 ARG C CZ  1 
ATOM   6212 N  NH1 . ARG C  1  132 ? -15.114 12.495  23.873 1.00 53.69  ? 145 ARG C NH1 1 
ATOM   6213 N  NH2 . ARG C  1  132 ? -15.053 10.405  24.812 1.00 55.62  ? 145 ARG C NH2 1 
ATOM   6214 N  N   . ALA C  1  133 ? -11.515 16.901  29.163 1.00 49.50  ? 146 ALA C N   1 
ATOM   6215 C  CA  . ALA C  1  133 ? -10.874 17.836  30.076 1.00 49.93  ? 146 ALA C CA  1 
ATOM   6216 C  C   . ALA C  1  133 ? -9.416  17.426  30.284 1.00 49.58  ? 146 ALA C C   1 
ATOM   6217 O  O   . ALA C  1  133 ? -9.075  16.243  30.175 1.00 44.27  ? 146 ALA C O   1 
ATOM   6218 N  N   . ASP C  1  134 ? -8.565  18.419  30.588 1.00 46.75  ? 147 ASP C N   1 
ATOM   6219 C  CA  . ASP C  1  134 ? -7.182  18.157  30.956 1.00 48.30  ? 147 ASP C CA  1 
ATOM   6220 C  C   . ASP C  1  134 ? -7.112  17.182  32.136 1.00 56.03  ? 147 ASP C C   1 
ATOM   6221 O  O   . ASP C  1  134 ? -8.017  17.118  32.975 1.00 62.83  ? 147 ASP C O   1 
ATOM   6222 C  CB  . ASP C  1  134 ? -6.436  19.442  31.271 1.00 46.14  ? 147 ASP C CB  1 
ATOM   6223 C  CG  . ASP C  1  134 ? -6.268  20.403  30.106 1.00 50.18  ? 147 ASP C CG  1 
ATOM   6224 O  OD1 . ASP C  1  134 ? -6.862  20.141  29.044 1.00 57.09  ? 147 ASP C OD1 1 
ATOM   6225 O  OD2 . ASP C  1  134 ? -5.532  21.402  30.259 1.00 50.88  ? 147 ASP C OD2 1 
ATOM   6226 N  N   . GLU C  1  135 ? -6.008  16.426  32.191 1.00 57.68  ? 148 GLU C N   1 
ATOM   6227 C  CA  . GLU C  1  135 ? -5.843  15.351  33.157 1.00 60.43  ? 148 GLU C CA  1 
ATOM   6228 C  C   . GLU C  1  135 ? -5.699  15.909  34.574 1.00 62.04  ? 148 GLU C C   1 
ATOM   6229 O  O   . GLU C  1  135 ? -6.060  15.250  35.546 1.00 53.99  ? 148 GLU C O   1 
ATOM   6230 C  CB  . GLU C  1  135 ? -4.619  14.513  32.788 1.00 61.63  ? 148 GLU C CB  1 
ATOM   6231 C  CG  . GLU C  1  135 ? -4.508  13.238  33.620 1.00 63.09  ? 148 GLU C CG  1 
ATOM   6232 C  CD  . GLU C  1  135 ? -3.619  13.305  34.848 1.00 67.35  ? 148 GLU C CD  1 
ATOM   6233 O  OE1 . GLU C  1  135 ? -2.911  14.327  35.087 1.00 69.35  ? 148 GLU C OE1 1 
ATOM   6234 O  OE2 . GLU C  1  135 ? -3.662  12.276  35.561 1.00 67.81  ? 148 GLU C OE2 1 
ATOM   6235 N  N   . PHE C  1  136 ? -5.157  17.123  34.684 1.00 60.23  ? 149 PHE C N   1 
ATOM   6236 C  CA  . PHE C  1  136 ? -5.008  17.797  35.961 1.00 67.43  ? 149 PHE C CA  1 
ATOM   6237 C  C   . PHE C  1  136 ? -6.334  17.869  36.722 1.00 63.35  ? 149 PHE C C   1 
ATOM   6238 O  O   . PHE C  1  136 ? -6.326  17.823  37.941 1.00 68.61  ? 149 PHE C O   1 
ATOM   6239 C  CB  . PHE C  1  136 ? -4.460  19.214  35.755 1.00 75.81  ? 149 PHE C CB  1 
ATOM   6240 C  CG  . PHE C  1  136 ? -4.362  19.997  37.056 1.00 86.02  ? 149 PHE C CG  1 
ATOM   6241 C  CD1 . PHE C  1  136 ? -3.412  19.663  38.018 1.00 89.08  ? 149 PHE C CD1 1 
ATOM   6242 C  CD2 . PHE C  1  136 ? -5.231  21.046  37.324 1.00 87.51  ? 149 PHE C CD2 1 
ATOM   6243 C  CE1 . PHE C  1  136 ? -3.322  20.365  39.209 1.00 85.77  ? 149 PHE C CE1 1 
ATOM   6244 C  CE2 . PHE C  1  136 ? -5.139  21.751  38.517 1.00 87.07  ? 149 PHE C CE2 1 
ATOM   6245 C  CZ  . PHE C  1  136 ? -4.181  21.414  39.452 1.00 86.49  ? 149 PHE C CZ  1 
ATOM   6246 N  N   . PHE C  1  137 ? -7.460  17.999  36.015 1.00 60.25  ? 150 PHE C N   1 
ATOM   6247 C  CA  . PHE C  1  137 ? -8.756  18.163  36.653 1.00 55.20  ? 150 PHE C CA  1 
ATOM   6248 C  C   . PHE C  1  137 ? -9.396  16.812  36.987 1.00 58.27  ? 150 PHE C C   1 
ATOM   6249 O  O   . PHE C  1  137 ? -10.513 16.782  37.503 1.00 62.13  ? 150 PHE C O   1 
ATOM   6250 C  CB  . PHE C  1  137 ? -9.700  18.956  35.749 1.00 55.44  ? 150 PHE C CB  1 
ATOM   6251 C  CG  . PHE C  1  137 ? -9.159  20.284  35.246 1.00 61.24  ? 150 PHE C CG  1 
ATOM   6252 C  CD1 . PHE C  1  137 ? -8.670  21.241  36.127 1.00 63.74  ? 150 PHE C CD1 1 
ATOM   6253 C  CD2 . PHE C  1  137 ? -9.123  20.560  33.880 1.00 62.48  ? 150 PHE C CD2 1 
ATOM   6254 C  CE1 . PHE C  1  137 ? -8.171  22.450  35.650 1.00 69.43  ? 150 PHE C CE1 1 
ATOM   6255 C  CE2 . PHE C  1  137 ? -8.637  21.776  33.409 1.00 61.85  ? 150 PHE C CE2 1 
ATOM   6256 C  CZ  . PHE C  1  137 ? -8.143  22.716  34.293 1.00 65.00  ? 150 PHE C CZ  1 
ATOM   6257 N  N   . GLY C  1  138 ? -8.739  15.690  36.662 1.00 58.94  ? 151 GLY C N   1 
ATOM   6258 C  CA  . GLY C  1  138 ? -9.099  14.411  37.258 1.00 55.67  ? 151 GLY C CA  1 
ATOM   6259 C  C   . GLY C  1  138 ? -9.662  13.380  36.280 1.00 57.30  ? 151 GLY C C   1 
ATOM   6260 O  O   . GLY C  1  138 ? -9.888  12.245  36.684 1.00 56.76  ? 151 GLY C O   1 
ATOM   6261 N  N   . ASP C  1  139 ? -9.903  13.745  35.013 1.00 66.34  ? 152 ASP C N   1 
ATOM   6262 C  CA  . ASP C  1  139 ? -10.473 12.793  34.062 1.00 71.54  ? 152 ASP C CA  1 
ATOM   6263 C  C   . ASP C  1  139 ? -10.194 13.227  32.625 1.00 69.26  ? 152 ASP C C   1 
ATOM   6264 O  O   . ASP C  1  139 ? -10.763 14.208  32.143 1.00 63.52  ? 152 ASP C O   1 
ATOM   6265 C  CB  . ASP C  1  139 ? -11.966 12.577  34.274 1.00 72.69  ? 152 ASP C CB  1 
ATOM   6266 C  CG  . ASP C  1  139 ? -12.609 11.531  33.370 1.00 73.89  ? 152 ASP C CG  1 
ATOM   6267 O  OD1 . ASP C  1  139 ? -11.985 11.159  32.358 1.00 78.73  ? 152 ASP C OD1 1 
ATOM   6268 O  OD2 . ASP C  1  139 ? -13.727 11.080  33.684 1.00 70.87  ? 152 ASP C OD2 1 
ATOM   6269 N  N   . ASN C  1  140 ? -9.355  12.440  31.936 1.00 65.40  ? 153 ASN C N   1 
ATOM   6270 C  CA  . ASN C  1  140 ? -8.855  12.811  30.622 1.00 62.31  ? 153 ASN C CA  1 
ATOM   6271 C  C   . ASN C  1  140 ? -9.515  11.989  29.515 1.00 56.61  ? 153 ASN C C   1 
ATOM   6272 O  O   . ASN C  1  140 ? -9.190  12.206  28.352 1.00 62.99  ? 153 ASN C O   1 
ATOM   6273 C  CB  . ASN C  1  140 ? -7.338  12.664  30.553 1.00 59.18  ? 153 ASN C CB  1 
ATOM   6274 C  CG  . ASN C  1  140 ? -6.878  11.228  30.693 1.00 59.17  ? 153 ASN C CG  1 
ATOM   6275 O  OD1 . ASN C  1  140 ? -7.621  10.365  31.171 1.00 60.15  ? 153 ASN C OD1 1 
ATOM   6276 N  ND2 . ASN C  1  140 ? -5.651  10.940  30.292 1.00 58.78  ? 153 ASN C ND2 1 
ATOM   6277 N  N   . HIS C  1  141 ? -10.438 11.077  29.863 1.00 58.21  ? 154 HIS C N   1 
ATOM   6278 C  CA  . HIS C  1  141 ? -10.991 10.138  28.893 1.00 62.69  ? 154 HIS C CA  1 
ATOM   6279 C  C   . HIS C  1  141 ? -12.490 10.349  28.658 1.00 62.87  ? 154 HIS C C   1 
ATOM   6280 O  O   . HIS C  1  141 ? -12.945 10.189  27.531 1.00 63.04  ? 154 HIS C O   1 
ATOM   6281 C  CB  . HIS C  1  141 ? -10.616 8.698   29.272 1.00 66.96  ? 154 HIS C CB  1 
ATOM   6282 C  CG  . HIS C  1  141 ? -11.059 8.285   30.623 1.00 68.92  ? 154 HIS C CG  1 
ATOM   6283 N  ND1 . HIS C  1  141 ? -10.286 8.504   31.741 1.00 63.74  ? 154 HIS C ND1 1 
ATOM   6284 C  CD2 . HIS C  1  141 ? -12.179 7.687   31.037 1.00 73.08  ? 154 HIS C CD2 1 
ATOM   6285 C  CE1 . HIS C  1  141 ? -10.932 8.044   32.799 1.00 69.95  ? 154 HIS C CE1 1 
ATOM   6286 N  NE2 . HIS C  1  141 ? -12.085 7.551   32.396 1.00 69.22  ? 154 HIS C NE2 1 
ATOM   6287 N  N   . SER C  1  142 ? -13.250 10.709  29.702 1.00 63.00  ? 155 SER C N   1 
ATOM   6288 C  CA  . SER C  1  142 ? -14.696 10.852  29.604 1.00 58.88  ? 155 SER C CA  1 
ATOM   6289 C  C   . SER C  1  142 ? -15.093 12.049  28.749 1.00 55.57  ? 155 SER C C   1 
ATOM   6290 O  O   . SER C  1  142 ? -14.451 13.101  28.789 1.00 49.91  ? 155 SER C O   1 
ATOM   6291 C  CB  . SER C  1  142 ? -15.323 10.985  30.958 1.00 59.33  ? 155 SER C CB  1 
ATOM   6292 O  OG  . SER C  1  142 ? -15.267 9.740   31.634 1.00 63.05  ? 155 SER C OG  1 
ATOM   6293 N  N   . PHE C  1  143 ? -16.205 11.876  28.024 1.00 52.81  ? 156 PHE C N   1 
ATOM   6294 C  CA  . PHE C  1  143 ? -16.901 12.991  27.406 1.00 58.28  ? 156 PHE C CA  1 
ATOM   6295 C  C   . PHE C  1  143 ? -17.303 14.016  28.466 1.00 57.25  ? 156 PHE C C   1 
ATOM   6296 O  O   . PHE C  1  143 ? -17.807 13.638  29.515 1.00 55.00  ? 156 PHE C O   1 
ATOM   6297 C  CB  . PHE C  1  143 ? -18.147 12.471  26.683 1.00 59.10  ? 156 PHE C CB  1 
ATOM   6298 C  CG  . PHE C  1  143 ? -18.983 13.581  26.066 1.00 61.02  ? 156 PHE C CG  1 
ATOM   6299 C  CD1 . PHE C  1  143 ? -18.654 14.115  24.825 1.00 64.38  ? 156 PHE C CD1 1 
ATOM   6300 C  CD2 . PHE C  1  143 ? -20.094 14.095  26.733 1.00 66.65  ? 156 PHE C CD2 1 
ATOM   6301 C  CE1 . PHE C  1  143 ? -19.427 15.114  24.259 1.00 66.16  ? 156 PHE C CE1 1 
ATOM   6302 C  CE2 . PHE C  1  143 ? -20.856 15.104  26.167 1.00 69.25  ? 156 PHE C CE2 1 
ATOM   6303 C  CZ  . PHE C  1  143 ? -20.520 15.610  24.933 1.00 66.44  ? 156 PHE C CZ  1 
ATOM   6304 N  N   . ASN C  1  144 ? -17.114 15.303  28.153 1.00 57.85  ? 157 ASN C N   1 
ATOM   6305 C  CA  . ASN C  1  144 ? -17.380 16.401  29.068 1.00 61.47  ? 157 ASN C CA  1 
ATOM   6306 C  C   . ASN C  1  144 ? -18.371 17.369  28.418 1.00 63.55  ? 157 ASN C C   1 
ATOM   6307 O  O   . ASN C  1  144 ? -18.041 18.048  27.443 1.00 56.06  ? 157 ASN C O   1 
ATOM   6308 C  CB  . ASN C  1  144 ? -16.059 17.065  29.438 1.00 71.79  ? 157 ASN C CB  1 
ATOM   6309 C  CG  . ASN C  1  144 ? -16.185 18.325  30.266 1.00 77.94  ? 157 ASN C CG  1 
ATOM   6310 O  OD1 . ASN C  1  144 ? -16.911 19.254  29.885 1.00 76.15  ? 157 ASN C OD1 1 
ATOM   6311 N  ND2 . ASN C  1  144 ? -15.496 18.348  31.403 1.00 81.96  ? 157 ASN C ND2 1 
ATOM   6312 N  N   . GLN C  1  145 ? -19.567 17.466  29.019 1.00 69.04  ? 158 GLN C N   1 
ATOM   6313 C  CA  . GLN C  1  145 ? -20.692 18.212  28.468 1.00 64.35  ? 158 GLN C CA  1 
ATOM   6314 C  C   . GLN C  1  145 ? -20.394 19.715  28.418 1.00 58.31  ? 158 GLN C C   1 
ATOM   6315 O  O   . GLN C  1  145 ? -20.811 20.389  27.479 1.00 61.71  ? 158 GLN C O   1 
ATOM   6316 C  CB  . GLN C  1  145 ? -21.940 17.915  29.305 1.00 63.97  ? 158 GLN C CB  1 
ATOM   6317 C  CG  . GLN C  1  145 ? -23.220 18.571  28.795 1.00 64.86  ? 158 GLN C CG  1 
ATOM   6318 C  CD  . GLN C  1  145 ? -23.643 18.067  27.433 1.00 58.01  ? 158 GLN C CD  1 
ATOM   6319 O  OE1 . GLN C  1  145 ? -23.871 16.867  27.237 1.00 51.56  ? 158 GLN C OE1 1 
ATOM   6320 N  NE2 . GLN C  1  145 ? -23.778 18.977  26.480 1.00 54.20  ? 158 GLN C NE2 1 
ATOM   6321 N  N   . THR C  1  146 ? -19.681 20.239  29.423 1.00 57.35  ? 159 THR C N   1 
ATOM   6322 C  CA  . THR C  1  146 ? -19.362 21.659  29.470 1.00 61.13  ? 159 THR C CA  1 
ATOM   6323 C  C   . THR C  1  146 ? -18.492 22.039  28.279 1.00 66.42  ? 159 THR C C   1 
ATOM   6324 O  O   . THR C  1  146 ? -18.642 23.120  27.717 1.00 63.38  ? 159 THR C O   1 
ATOM   6325 C  CB  . THR C  1  146 ? -18.644 22.034  30.767 1.00 64.42  ? 159 THR C CB  1 
ATOM   6326 O  OG1 . THR C  1  146 ? -19.409 21.548  31.874 1.00 61.27  ? 159 THR C OG1 1 
ATOM   6327 C  CG2 . THR C  1  146 ? -18.396 23.535  30.842 1.00 60.19  ? 159 THR C CG2 1 
ATOM   6328 N  N   . LEU C  1  147 ? -17.537 21.169  27.936 1.00 78.41  ? 160 LEU C N   1 
ATOM   6329 C  CA  . LEU C  1  147 ? -16.638 21.441  26.826 1.00 75.10  ? 160 LEU C CA  1 
ATOM   6330 C  C   . LEU C  1  147 ? -17.365 21.285  25.493 1.00 70.55  ? 160 LEU C C   1 
ATOM   6331 O  O   . LEU C  1  147 ? -17.087 22.038  24.560 1.00 66.25  ? 160 LEU C O   1 
ATOM   6332 C  CB  . LEU C  1  147 ? -15.419 20.528  26.918 1.00 78.77  ? 160 LEU C CB  1 
ATOM   6333 C  CG  . LEU C  1  147 ? -14.354 20.944  27.933 1.00 78.52  ? 160 LEU C CG  1 
ATOM   6334 C  CD1 . LEU C  1  147 ? -13.217 19.932  27.929 1.00 82.31  ? 160 LEU C CD1 1 
ATOM   6335 C  CD2 . LEU C  1  147 ? -13.845 22.344  27.627 1.00 71.81  ? 160 LEU C CD2 1 
ATOM   6336 N  N   . PHE C  1  148 ? -18.294 20.321  25.413 1.00 60.90  ? 161 PHE C N   1 
ATOM   6337 C  CA  . PHE C  1  148 ? -19.102 20.148  24.216 1.00 62.19  ? 161 PHE C CA  1 
ATOM   6338 C  C   . PHE C  1  148 ? -20.020 21.352  24.007 1.00 65.64  ? 161 PHE C C   1 
ATOM   6339 O  O   . PHE C  1  148 ? -20.334 21.683  22.864 1.00 66.42  ? 161 PHE C O   1 
ATOM   6340 C  CB  . PHE C  1  148 ? -19.946 18.872  24.253 1.00 66.86  ? 161 PHE C CB  1 
ATOM   6341 C  CG  . PHE C  1  148 ? -20.687 18.611  22.947 1.00 71.25  ? 161 PHE C CG  1 
ATOM   6342 C  CD1 . PHE C  1  148 ? -19.994 18.215  21.807 1.00 73.64  ? 161 PHE C CD1 1 
ATOM   6343 C  CD2 . PHE C  1  148 ? -22.063 18.772  22.859 1.00 71.12  ? 161 PHE C CD2 1 
ATOM   6344 C  CE1 . PHE C  1  148 ? -20.660 17.968  20.614 1.00 74.52  ? 161 PHE C CE1 1 
ATOM   6345 C  CE2 . PHE C  1  148 ? -22.726 18.523  21.664 1.00 75.24  ? 161 PHE C CE2 1 
ATOM   6346 C  CZ  . PHE C  1  148 ? -22.026 18.117  20.543 1.00 75.90  ? 161 PHE C CZ  1 
ATOM   6347 N  N   . ASP C  1  149 ? -20.459 21.985  25.106 1.00 66.04  ? 162 ASP C N   1 
ATOM   6348 C  CA  . ASP C  1  149 ? -21.291 23.175  25.034 1.00 66.15  ? 162 ASP C CA  1 
ATOM   6349 C  C   . ASP C  1  149 ? -20.515 24.304  24.358 1.00 66.09  ? 162 ASP C C   1 
ATOM   6350 O  O   . ASP C  1  149 ? -21.087 25.057  23.563 1.00 67.38  ? 162 ASP C O   1 
ATOM   6351 C  CB  . ASP C  1  149 ? -21.825 23.551  26.410 1.00 69.78  ? 162 ASP C CB  1 
ATOM   6352 C  CG  . ASP C  1  149 ? -22.904 22.632  26.967 1.00 79.50  ? 162 ASP C CG  1 
ATOM   6353 O  OD1 . ASP C  1  149 ? -23.619 22.003  26.155 1.00 75.21  ? 162 ASP C OD1 1 
ATOM   6354 O  OD2 . ASP C  1  149 ? -23.005 22.529  28.211 1.00 87.42  ? 162 ASP C OD2 1 
ATOM   6355 N  N   . LYS C  1  150 ? -19.210 24.393  24.660 1.00 64.94  ? 163 LYS C N   1 
ATOM   6356 C  CA  . LYS C  1  150 ? -18.338 25.394  24.063 1.00 66.35  ? 163 LYS C CA  1 
ATOM   6357 C  C   . LYS C  1  150 ? -18.131 25.105  22.575 1.00 69.57  ? 163 LYS C C   1 
ATOM   6358 O  O   . LYS C  1  150 ? -18.065 26.033  21.774 1.00 68.87  ? 163 LYS C O   1 
ATOM   6359 C  CB  . LYS C  1  150 ? -17.017 25.447  24.838 1.00 68.83  ? 163 LYS C CB  1 
ATOM   6360 C  CG  . LYS C  1  150 ? -16.024 26.495  24.371 1.00 72.97  ? 163 LYS C CG  1 
ATOM   6361 C  CD  . LYS C  1  150 ? -14.718 26.408  25.157 1.00 75.02  ? 163 LYS C CD  1 
ATOM   6362 C  CE  . LYS C  1  150 ? -13.616 27.265  24.602 1.00 77.29  ? 163 LYS C CE  1 
ATOM   6363 N  NZ  . LYS C  1  150 ? -13.277 28.412  25.440 1.00 78.08  ? 163 LYS C NZ  1 
ATOM   6364 N  N   . PHE C  1  151 ? -18.031 23.819  22.211 1.00 71.90  ? 164 PHE C N   1 
ATOM   6365 C  CA  . PHE C  1  151 ? -17.956 23.404  20.818 1.00 70.65  ? 164 PHE C CA  1 
ATOM   6366 C  C   . PHE C  1  151 ? -19.195 23.896  20.068 1.00 68.74  ? 164 PHE C C   1 
ATOM   6367 O  O   . PHE C  1  151 ? -19.087 24.411  18.957 1.00 65.28  ? 164 PHE C O   1 
ATOM   6368 C  CB  . PHE C  1  151 ? -17.794 21.878  20.805 1.00 74.13  ? 164 PHE C CB  1 
ATOM   6369 C  CG  . PHE C  1  151 ? -17.686 21.206  19.444 1.00 74.49  ? 164 PHE C CG  1 
ATOM   6370 C  CD1 . PHE C  1  151 ? -16.460 21.096  18.799 1.00 73.29  ? 164 PHE C CD1 1 
ATOM   6371 C  CD2 . PHE C  1  151 ? -18.812 20.669  18.823 1.00 75.24  ? 164 PHE C CD2 1 
ATOM   6372 C  CE1 . PHE C  1  151 ? -16.364 20.480  17.563 1.00 71.51  ? 164 PHE C CE1 1 
ATOM   6373 C  CE2 . PHE C  1  151 ? -18.711 20.050  17.586 1.00 70.74  ? 164 PHE C CE2 1 
ATOM   6374 C  CZ  . PHE C  1  151 ? -17.487 19.966  16.957 1.00 70.57  ? 164 PHE C CZ  1 
ATOM   6375 N  N   . VAL C  1  152 ? -20.374 23.739  20.687 1.00 64.79  ? 165 VAL C N   1 
ATOM   6376 C  CA  . VAL C  1  152 ? -21.625 24.140  20.060 1.00 61.62  ? 165 VAL C CA  1 
ATOM   6377 C  C   . VAL C  1  152 ? -21.661 25.662  19.942 1.00 62.87  ? 165 VAL C C   1 
ATOM   6378 O  O   . VAL C  1  152 ? -22.034 26.202  18.899 1.00 61.56  ? 165 VAL C O   1 
ATOM   6379 C  CB  . VAL C  1  152 ? -22.851 23.607  20.817 1.00 61.48  ? 165 VAL C CB  1 
ATOM   6380 C  CG1 . VAL C  1  152 ? -24.154 24.107  20.206 1.00 60.79  ? 165 VAL C CG1 1 
ATOM   6381 C  CG2 . VAL C  1  152 ? -22.862 22.085  20.859 1.00 61.51  ? 165 VAL C CG2 1 
ATOM   6382 N  N   . ASP C  1  153 ? -21.242 26.345  21.009 1.00 65.43  ? 166 ASP C N   1 
ATOM   6383 C  CA  . ASP C  1  153 ? -21.244 27.796  21.017 1.00 77.85  ? 166 ASP C CA  1 
ATOM   6384 C  C   . ASP C  1  153 ? -20.379 28.338  19.876 1.00 73.24  ? 166 ASP C C   1 
ATOM   6385 O  O   . ASP C  1  153 ? -20.833 29.188  19.115 1.00 77.12  ? 166 ASP C O   1 
ATOM   6386 C  CB  . ASP C  1  153 ? -20.893 28.360  22.388 1.00 86.54  ? 166 ASP C CB  1 
ATOM   6387 C  CG  . ASP C  1  153 ? -21.015 29.880  22.487 1.00 86.10  ? 166 ASP C CG  1 
ATOM   6388 O  OD1 . ASP C  1  153 ? -22.068 30.411  22.071 1.00 81.70  ? 166 ASP C OD1 1 
ATOM   6389 O  OD2 . ASP C  1  153 ? -20.070 30.531  22.970 1.00 83.09  ? 166 ASP C OD2 1 
ATOM   6390 N  N   . PHE C  1  154 ? -19.142 27.843  19.748 1.00 75.85  ? 167 PHE C N   1 
ATOM   6391 C  CA  . PHE C  1  154 ? -18.216 28.331  18.730 1.00 72.60  ? 167 PHE C CA  1 
ATOM   6392 C  C   . PHE C  1  154 ? -18.736 27.977  17.335 1.00 69.79  ? 167 PHE C C   1 
ATOM   6393 O  O   . PHE C  1  154 ? -18.560 28.756  16.408 1.00 61.85  ? 167 PHE C O   1 
ATOM   6394 C  CB  . PHE C  1  154 ? -16.796 27.803  18.947 1.00 68.58  ? 167 PHE C CB  1 
ATOM   6395 C  CG  . PHE C  1  154 ? -15.937 28.666  19.861 1.00 66.02  ? 167 PHE C CG  1 
ATOM   6396 C  CD1 . PHE C  1  154 ? -16.263 28.823  21.201 1.00 66.46  ? 167 PHE C CD1 1 
ATOM   6397 C  CD2 . PHE C  1  154 ? -14.768 29.262  19.393 1.00 64.41  ? 167 PHE C CD2 1 
ATOM   6398 C  CE1 . PHE C  1  154 ? -15.471 29.603  22.038 1.00 69.64  ? 167 PHE C CE1 1 
ATOM   6399 C  CE2 . PHE C  1  154 ? -13.975 30.031  20.236 1.00 67.39  ? 167 PHE C CE2 1 
ATOM   6400 C  CZ  . PHE C  1  154 ? -14.330 30.207  21.555 1.00 67.84  ? 167 PHE C CZ  1 
ATOM   6401 N  N   . SER C  1  155 ? -19.399 26.826  17.183 1.00 69.60  ? 168 SER C N   1 
ATOM   6402 C  CA  . SER C  1  155 ? -20.018 26.476  15.912 1.00 78.20  ? 168 SER C CA  1 
ATOM   6403 C  C   . SER C  1  155 ? -21.126 27.471  15.554 1.00 80.88  ? 168 SER C C   1 
ATOM   6404 O  O   . SER C  1  155 ? -21.321 27.791  14.378 1.00 74.39  ? 168 SER C O   1 
ATOM   6405 C  CB  . SER C  1  155 ? -20.562 25.066  15.926 1.00 81.01  ? 168 SER C CB  1 
ATOM   6406 O  OG  . SER C  1  155 ? -19.539 24.116  16.200 1.00 81.76  ? 168 SER C OG  1 
ATOM   6407 N  N   . ASN C  1  156 ? -21.870 27.930  16.574 1.00 79.88  ? 169 ASN C N   1 
ATOM   6408 C  CA  . ASN C  1  156 ? -22.920 28.922  16.385 1.00 71.99  ? 169 ASN C CA  1 
ATOM   6409 C  C   . ASN C  1  156 ? -22.298 30.265  16.002 1.00 71.21  ? 169 ASN C C   1 
ATOM   6410 O  O   . ASN C  1  156 ? -22.790 30.941  15.111 1.00 70.27  ? 169 ASN C O   1 
ATOM   6411 C  CB  . ASN C  1  156 ? -23.806 29.052  17.620 1.00 68.53  ? 169 ASN C CB  1 
ATOM   6412 C  CG  . ASN C  1  156 ? -24.781 27.905  17.780 1.00 72.59  ? 169 ASN C CG  1 
ATOM   6413 O  OD1 . ASN C  1  156 ? -25.194 27.274  16.800 1.00 72.23  ? 169 ASN C OD1 1 
ATOM   6414 N  ND2 . ASN C  1  156 ? -25.207 27.635  19.004 1.00 70.55  ? 169 ASN C ND2 1 
ATOM   6415 N  N   . ARG C  1  157 ? -21.193 30.635  16.655 1.00 72.50  ? 170 ARG C N   1 
ATOM   6416 C  CA  . ARG C  1  157 ? -20.613 31.961  16.507 1.00 77.23  ? 170 ARG C CA  1 
ATOM   6417 C  C   . ARG C  1  157 ? -19.824 32.098  15.203 1.00 74.41  ? 170 ARG C C   1 
ATOM   6418 O  O   . ARG C  1  157 ? -19.722 33.206  14.696 1.00 72.85  ? 170 ARG C O   1 
ATOM   6419 C  CB  . ARG C  1  157 ? -19.713 32.308  17.701 1.00 81.94  ? 170 ARG C CB  1 
ATOM   6420 C  CG  . ARG C  1  157 ? -19.698 33.785  18.079 1.00 83.66  ? 170 ARG C CG  1 
ATOM   6421 C  CD  . ARG C  1  157 ? -18.597 34.145  19.053 1.00 83.33  ? 170 ARG C CD  1 
ATOM   6422 N  NE  . ARG C  1  157 ? -18.677 33.303  20.251 1.00 84.82  ? 170 ARG C NE  1 
ATOM   6423 C  CZ  . ARG C  1  157 ? -17.726 33.100  21.167 1.00 83.80  ? 170 ARG C CZ  1 
ATOM   6424 N  NH1 . ARG C  1  157 ? -16.513 33.623  21.053 1.00 76.85  ? 170 ARG C NH1 1 
ATOM   6425 N  NH2 . ARG C  1  157 ? -18.008 32.325  22.204 1.00 81.31  ? 170 ARG C NH2 1 
ATOM   6426 N  N   . TYR C  1  158 ? -19.246 31.010  14.669 1.00 77.92  ? 171 TYR C N   1 
ATOM   6427 C  CA  . TYR C  1  158 ? -18.344 31.133  13.528 1.00 74.47  ? 171 TYR C CA  1 
ATOM   6428 C  C   . TYR C  1  158 ? -18.719 30.238  12.346 1.00 69.63  ? 171 TYR C C   1 
ATOM   6429 O  O   . TYR C  1  158 ? -18.185 30.455  11.262 1.00 66.27  ? 171 TYR C O   1 
ATOM   6430 C  CB  . TYR C  1  158 ? -16.910 30.818  13.957 1.00 77.74  ? 171 TYR C CB  1 
ATOM   6431 C  CG  . TYR C  1  158 ? -16.403 31.752  15.040 1.00 79.47  ? 171 TYR C CG  1 
ATOM   6432 C  CD1 . TYR C  1  158 ? -15.993 33.040  14.727 1.00 83.89  ? 171 TYR C CD1 1 
ATOM   6433 C  CD2 . TYR C  1  158 ? -16.355 31.354  16.370 1.00 78.03  ? 171 TYR C CD2 1 
ATOM   6434 C  CE1 . TYR C  1  158 ? -15.536 33.910  15.705 1.00 83.73  ? 171 TYR C CE1 1 
ATOM   6435 C  CE2 . TYR C  1  158 ? -15.915 32.217  17.359 1.00 77.82  ? 171 TYR C CE2 1 
ATOM   6436 C  CZ  . TYR C  1  158 ? -15.501 33.496  17.026 1.00 80.40  ? 171 TYR C CZ  1 
ATOM   6437 O  OH  . TYR C  1  158 ? -15.048 34.345  17.992 1.00 82.45  ? 171 TYR C OH  1 
ATOM   6438 N  N   . GLY C  1  159 ? -19.614 29.254  12.534 1.00 69.63  ? 172 GLY C N   1 
ATOM   6439 C  CA  . GLY C  1  159 ? -19.869 28.261  11.497 1.00 72.50  ? 172 GLY C CA  1 
ATOM   6440 C  C   . GLY C  1  159 ? -21.345 28.118  11.126 1.00 73.08  ? 172 GLY C C   1 
ATOM   6441 O  O   . GLY C  1  159 ? -21.735 27.123  10.517 1.00 69.27  ? 172 GLY C O   1 
ATOM   6442 N  N   . GLY C  1  160 ? -22.166 29.112  11.485 1.00 70.15  ? 173 GLY C N   1 
ATOM   6443 C  CA  . GLY C  1  160 ? -23.584 29.088  11.161 1.00 65.11  ? 173 GLY C CA  1 
ATOM   6444 C  C   . GLY C  1  160 ? -24.308 27.901  11.796 1.00 66.02  ? 173 GLY C C   1 
ATOM   6445 O  O   . GLY C  1  160 ? -25.323 27.443  11.269 1.00 62.85  ? 173 GLY C O   1 
ATOM   6446 N  N   . GLY C  1  161 ? -23.775 27.412  12.929 1.00 64.54  ? 174 GLY C N   1 
ATOM   6447 C  CA  . GLY C  1  161 ? -24.366 26.298  13.658 1.00 64.60  ? 174 GLY C CA  1 
ATOM   6448 C  C   . GLY C  1  161 ? -23.774 24.943  13.264 1.00 65.34  ? 174 GLY C C   1 
ATOM   6449 O  O   . GLY C  1  161 ? -24.280 23.902  13.702 1.00 56.99  ? 174 GLY C O   1 
ATOM   6450 N  N   . PHE C  1  162 ? -22.732 24.976  12.416 1.00 72.14  ? 175 PHE C N   1 
ATOM   6451 C  CA  . PHE C  1  162 ? -22.005 23.786  11.994 1.00 75.34  ? 175 PHE C CA  1 
ATOM   6452 C  C   . PHE C  1  162 ? -20.525 23.942  12.352 1.00 73.71  ? 175 PHE C C   1 
ATOM   6453 O  O   . PHE C  1  162 ? -20.032 25.055  12.538 1.00 72.48  ? 175 PHE C O   1 
ATOM   6454 C  CB  . PHE C  1  162 ? -22.191 23.549  10.491 1.00 74.39  ? 175 PHE C CB  1 
ATOM   6455 C  CG  . PHE C  1  162 ? -23.630 23.290  10.065 1.00 79.61  ? 175 PHE C CG  1 
ATOM   6456 C  CD1 . PHE C  1  162 ? -24.470 24.340  9.705  1.00 79.24  ? 175 PHE C CD1 1 
ATOM   6457 C  CD2 . PHE C  1  162 ? -24.144 21.993  10.031 1.00 81.88  ? 175 PHE C CD2 1 
ATOM   6458 C  CE1 . PHE C  1  162 ? -25.784 24.090  9.324  1.00 81.59  ? 175 PHE C CE1 1 
ATOM   6459 C  CE2 . PHE C  1  162 ? -25.456 21.752  9.650  1.00 80.25  ? 175 PHE C CE2 1 
ATOM   6460 C  CZ  . PHE C  1  162 ? -26.276 22.798  9.304  1.00 79.32  ? 175 PHE C CZ  1 
ATOM   6461 N  N   . TYR C  1  163 ? -19.813 22.810  12.438 1.00 67.99  ? 176 TYR C N   1 
ATOM   6462 C  CA  . TYR C  1  163 ? -18.375 22.822  12.661 1.00 66.34  ? 176 TYR C CA  1 
ATOM   6463 C  C   . TYR C  1  163 ? -17.653 22.780  11.313 1.00 64.78  ? 176 TYR C C   1 
ATOM   6464 O  O   . TYR C  1  163 ? -17.880 21.866  10.525 1.00 62.82  ? 176 TYR C O   1 
ATOM   6465 C  CB  . TYR C  1  163 ? -18.002 21.638  13.555 1.00 66.44  ? 176 TYR C CB  1 
ATOM   6466 C  CG  . TYR C  1  163 ? -16.545 21.647  13.999 1.00 67.18  ? 176 TYR C CG  1 
ATOM   6467 C  CD1 . TYR C  1  163 ? -16.103 22.477  15.023 1.00 69.37  ? 176 TYR C CD1 1 
ATOM   6468 C  CD2 . TYR C  1  163 ? -15.610 20.820  13.392 1.00 71.37  ? 176 TYR C CD2 1 
ATOM   6469 C  CE1 . TYR C  1  163 ? -14.775 22.483  15.423 1.00 70.87  ? 176 TYR C CE1 1 
ATOM   6470 C  CE2 . TYR C  1  163 ? -14.280 20.820  13.780 1.00 69.05  ? 176 TYR C CE2 1 
ATOM   6471 C  CZ  . TYR C  1  163 ? -13.859 21.653  14.797 1.00 67.25  ? 176 TYR C CZ  1 
ATOM   6472 O  OH  . TYR C  1  163 ? -12.542 21.636  15.148 1.00 60.35  ? 176 TYR C OH  1 
ATOM   6473 N  N   . ASN C  1  164 ? -16.801 23.785  11.062 1.00 64.12  ? 177 ASN C N   1 
ATOM   6474 C  CA  . ASN C  1  164 ? -16.046 23.899  9.822  1.00 65.74  ? 177 ASN C CA  1 
ATOM   6475 C  C   . ASN C  1  164 ? -14.659 24.465  10.141 1.00 62.90  ? 177 ASN C C   1 
ATOM   6476 O  O   . ASN C  1  164 ? -14.345 24.696  11.300 1.00 61.91  ? 177 ASN C O   1 
ATOM   6477 C  CB  . ASN C  1  164 ? -16.854 24.649  8.766  1.00 68.09  ? 177 ASN C CB  1 
ATOM   6478 C  CG  . ASN C  1  164 ? -16.831 26.156  8.881  1.00 75.58  ? 177 ASN C CG  1 
ATOM   6479 O  OD1 . ASN C  1  164 ? -16.209 26.727  9.796  1.00 73.02  ? 177 ASN C OD1 1 
ATOM   6480 N  ND2 . ASN C  1  164 ? -17.470 26.797  7.908  1.00 81.35  ? 177 ASN C ND2 1 
ATOM   6481 N  N   . LEU C  1  165 ? -13.833 24.703  9.119  1.00 62.28  ? 178 LEU C N   1 
ATOM   6482 C  CA  . LEU C  1  165 ? -12.426 24.993  9.340  1.00 65.50  ? 178 LEU C CA  1 
ATOM   6483 C  C   . LEU C  1  165 ? -12.239 26.294  10.118 1.00 67.81  ? 178 LEU C C   1 
ATOM   6484 O  O   . LEU C  1  165 ? -11.325 26.399  10.931 1.00 74.22  ? 178 LEU C O   1 
ATOM   6485 C  CB  . LEU C  1  165 ? -11.654 25.014  8.020  1.00 67.15  ? 178 LEU C CB  1 
ATOM   6486 C  CG  . LEU C  1  165 ? -10.186 24.580  8.113  1.00 73.92  ? 178 LEU C CG  1 
ATOM   6487 C  CD1 . LEU C  1  165 ? -10.008 23.239  8.841  1.00 74.23  ? 178 LEU C CD1 1 
ATOM   6488 C  CD2 . LEU C  1  165 ? -9.588  24.499  6.718  1.00 73.76  ? 178 LEU C CD2 1 
ATOM   6489 N  N   . THR C  1  166 ? -13.110 27.282  9.884  1.00 71.98  ? 179 THR C N   1 
ATOM   6490 C  CA  . THR C  1  166 ? -13.033 28.548  10.597 1.00 76.08  ? 179 THR C CA  1 
ATOM   6491 C  C   . THR C  1  166 ? -13.256 28.306  12.089 1.00 66.03  ? 179 THR C C   1 
ATOM   6492 O  O   . THR C  1  166 ? -12.507 28.826  12.907 1.00 62.12  ? 179 THR C O   1 
ATOM   6493 C  CB  . THR C  1  166 ? -14.051 29.541  10.039 1.00 81.65  ? 179 THR C CB  1 
ATOM   6494 O  OG1 . THR C  1  166 ? -14.004 29.440  8.618  1.00 79.62  ? 179 THR C OG1 1 
ATOM   6495 C  CG2 . THR C  1  166 ? -13.731 30.965  10.458 1.00 80.82  ? 179 THR C CG2 1 
ATOM   6496 N  N   . VAL C  1  167 ? -14.277 27.505  12.423 1.00 58.47  ? 180 VAL C N   1 
ATOM   6497 C  CA  . VAL C  1  167 ? -14.611 27.180  13.806 1.00 61.41  ? 180 VAL C CA  1 
ATOM   6498 C  C   . VAL C  1  167 ? -13.414 26.507  14.475 1.00 67.28  ? 180 VAL C C   1 
ATOM   6499 O  O   . VAL C  1  167 ? -13.117 26.769  15.640 1.00 66.42  ? 180 VAL C O   1 
ATOM   6500 C  CB  . VAL C  1  167 ? -15.850 26.268  13.931 1.00 60.01  ? 180 VAL C CB  1 
ATOM   6501 C  CG1 . VAL C  1  167 ? -16.289 26.073  15.378 1.00 60.89  ? 180 VAL C CG1 1 
ATOM   6502 C  CG2 . VAL C  1  167 ? -17.030 26.774  13.109 1.00 67.78  ? 180 VAL C CG2 1 
ATOM   6503 N  N   . ALA C  1  168 ? -12.755 25.609  13.735 1.00 74.77  ? 181 ALA C N   1 
ATOM   6504 C  CA  . ALA C  1  168 ? -11.643 24.841  14.271 1.00 71.60  ? 181 ALA C CA  1 
ATOM   6505 C  C   . ALA C  1  168 ? -10.510 25.775  14.682 1.00 65.88  ? 181 ALA C C   1 
ATOM   6506 O  O   . ALA C  1  168 ? -9.969  25.638  15.773 1.00 69.69  ? 181 ALA C O   1 
ATOM   6507 C  CB  . ALA C  1  168 ? -11.178 23.804  13.265 1.00 75.79  ? 181 ALA C CB  1 
ATOM   6508 N  N   . GLY C  1  169 ? -10.169 26.735  13.817 1.00 64.93  ? 182 GLY C N   1 
ATOM   6509 C  CA  . GLY C  1  169 ? -9.121  27.701  14.117 1.00 71.50  ? 182 GLY C CA  1 
ATOM   6510 C  C   . GLY C  1  169 ? -9.401  28.441  15.424 1.00 78.35  ? 182 GLY C C   1 
ATOM   6511 O  O   . GLY C  1  169 ? -8.513  28.567  16.262 1.00 85.14  ? 182 GLY C O   1 
ATOM   6512 N  N   . GLU C  1  170 ? -10.649 28.902  15.581 1.00 79.58  ? 183 GLU C N   1 
ATOM   6513 C  CA  . GLU C  1  170 ? -11.067 29.683  16.732 1.00 74.08  ? 183 GLU C CA  1 
ATOM   6514 C  C   . GLU C  1  170 ? -11.110 28.805  17.979 1.00 68.03  ? 183 GLU C C   1 
ATOM   6515 O  O   . GLU C  1  170 ? -10.644 29.226  19.031 1.00 71.43  ? 183 GLU C O   1 
ATOM   6516 C  CB  . GLU C  1  170 ? -12.436 30.337  16.503 1.00 74.95  ? 183 GLU C CB  1 
ATOM   6517 C  CG  . GLU C  1  170 ? -12.444 31.433  15.442 1.00 78.30  ? 183 GLU C CG  1 
ATOM   6518 C  CD  . GLU C  1  170 ? -11.345 32.477  15.587 1.00 80.22  ? 183 GLU C CD  1 
ATOM   6519 O  OE1 . GLU C  1  170 ? -11.310 33.088  16.669 1.00 87.09  ? 183 GLU C OE1 1 
ATOM   6520 O  OE2 . GLU C  1  170 ? -10.531 32.675  14.653 1.00 71.41  ? 183 GLU C OE2 1 
ATOM   6521 N  N   . LEU C  1  171 ? -11.679 27.600  17.873 1.00 61.16  ? 184 LEU C N   1 
ATOM   6522 C  CA  . LEU C  1  171 ? -11.877 26.771  19.050 1.00 64.81  ? 184 LEU C CA  1 
ATOM   6523 C  C   . LEU C  1  171 ? -10.532 26.293  19.603 1.00 66.41  ? 184 LEU C C   1 
ATOM   6524 O  O   . LEU C  1  171 ? -10.341 26.272  20.813 1.00 66.11  ? 184 LEU C O   1 
ATOM   6525 C  CB  . LEU C  1  171 ? -12.800 25.591  18.754 1.00 64.22  ? 184 LEU C CB  1 
ATOM   6526 C  CG  . LEU C  1  171 ? -13.070 24.668  19.950 1.00 67.66  ? 184 LEU C CG  1 
ATOM   6527 C  CD1 . LEU C  1  171 ? -13.770 25.397  21.081 1.00 68.11  ? 184 LEU C CD1 1 
ATOM   6528 C  CD2 . LEU C  1  171 ? -13.879 23.453  19.564 1.00 70.77  ? 184 LEU C CD2 1 
ATOM   6529 N  N   . ARG C  1  172 ? -9.612  25.900  18.714 1.00 67.46  ? 185 ARG C N   1 
ATOM   6530 C  CA  . ARG C  1  172 ? -8.306  25.385  19.110 1.00 68.96  ? 185 ARG C CA  1 
ATOM   6531 C  C   . ARG C  1  172 ? -7.581  26.426  19.966 1.00 71.06  ? 185 ARG C C   1 
ATOM   6532 O  O   . ARG C  1  172 ? -7.082  26.100  21.044 1.00 63.83  ? 185 ARG C O   1 
ATOM   6533 C  CB  . ARG C  1  172 ? -7.532  24.933  17.860 1.00 66.32  ? 185 ARG C CB  1 
ATOM   6534 C  CG  . ARG C  1  172 ? -6.016  24.775  17.930 1.00 65.12  ? 185 ARG C CG  1 
ATOM   6535 C  CD  . ARG C  1  172 ? -5.519  23.886  19.054 1.00 61.38  ? 185 ARG C CD  1 
ATOM   6536 N  NE  . ARG C  1  172 ? -6.144  22.562  19.111 1.00 57.07  ? 185 ARG C NE  1 
ATOM   6537 C  CZ  . ARG C  1  172 ? -6.649  21.978  20.201 1.00 58.23  ? 185 ARG C CZ  1 
ATOM   6538 N  NH1 . ARG C  1  172 ? -6.666  22.620  21.362 1.00 58.28  ? 185 ARG C NH1 1 
ATOM   6539 N  NH2 . ARG C  1  172 ? -7.140  20.743  20.135 1.00 53.38  ? 185 ARG C NH2 1 
ATOM   6540 N  N   . TYR C  1  173 ? -7.543  27.675  19.481 1.00 71.41  ? 186 TYR C N   1 
ATOM   6541 C  CA  . TYR C  1  173 ? -6.876  28.762  20.180 1.00 76.72  ? 186 TYR C CA  1 
ATOM   6542 C  C   . TYR C  1  173 ? -7.517  28.973  21.553 1.00 74.28  ? 186 TYR C C   1 
ATOM   6543 O  O   . TYR C  1  173 ? -6.825  29.056  22.566 1.00 75.03  ? 186 TYR C O   1 
ATOM   6544 C  CB  . TYR C  1  173 ? -6.905  30.038  19.330 1.00 83.17  ? 186 TYR C CB  1 
ATOM   6545 C  CG  . TYR C  1  173 ? -6.146  31.199  19.956 1.00 93.30  ? 186 TYR C CG  1 
ATOM   6546 C  CD1 . TYR C  1  173 ? -4.763  31.150  20.096 1.00 96.38  ? 186 TYR C CD1 1 
ATOM   6547 C  CD2 . TYR C  1  173 ? -6.800  32.341  20.405 1.00 99.15  ? 186 TYR C CD2 1 
ATOM   6548 C  CE1 . TYR C  1  173 ? -4.052  32.192  20.668 1.00 93.09  ? 186 TYR C CE1 1 
ATOM   6549 C  CE2 . TYR C  1  173 ? -6.102  33.392  20.980 1.00 97.00  ? 186 TYR C CE2 1 
ATOM   6550 C  CZ  . TYR C  1  173 ? -4.724  33.317  21.105 1.00 94.12  ? 186 TYR C CZ  1 
ATOM   6551 O  OH  . TYR C  1  173 ? -4.008  34.327  21.671 1.00 97.84  ? 186 TYR C OH  1 
ATOM   6552 N  N   . SER C  1  174 ? -8.849  29.033  21.580 1.00 70.09  ? 187 SER C N   1 
ATOM   6553 C  CA  . SER C  1  174 ? -9.575  29.349  22.795 1.00 65.73  ? 187 SER C CA  1 
ATOM   6554 C  C   . SER C  1  174 ? -9.345  28.271  23.854 1.00 68.92  ? 187 SER C C   1 
ATOM   6555 O  O   . SER C  1  174 ? -9.180  28.594  25.027 1.00 74.21  ? 187 SER C O   1 
ATOM   6556 C  CB  . SER C  1  174 ? -11.037 29.558  22.494 1.00 67.95  ? 187 SER C CB  1 
ATOM   6557 O  OG  . SER C  1  174 ? -11.764 29.862  23.671 1.00 73.28  ? 187 SER C OG  1 
ATOM   6558 N  N   . ARG C  1  175 ? -9.292  26.995  23.443 1.00 68.54  ? 188 ARG C N   1 
ATOM   6559 C  CA  . ARG C  1  175 ? -9.048  25.903  24.379 1.00 66.05  ? 188 ARG C CA  1 
ATOM   6560 C  C   . ARG C  1  175 ? -7.629  25.981  24.939 1.00 66.22  ? 188 ARG C C   1 
ATOM   6561 O  O   . ARG C  1  175 ? -7.395  25.607  26.086 1.00 72.11  ? 188 ARG C O   1 
ATOM   6562 C  CB  . ARG C  1  175 ? -9.275  24.522  23.751 1.00 65.57  ? 188 ARG C CB  1 
ATOM   6563 C  CG  . ARG C  1  175 ? -10.732 24.239  23.411 1.00 63.53  ? 188 ARG C CG  1 
ATOM   6564 C  CD  . ARG C  1  175 ? -11.601 24.051  24.627 1.00 64.65  ? 188 ARG C CD  1 
ATOM   6565 N  NE  . ARG C  1  175 ? -11.157 22.851  25.341 1.00 68.29  ? 188 ARG C NE  1 
ATOM   6566 C  CZ  . ARG C  1  175 ? -10.602 22.793  26.548 1.00 68.82  ? 188 ARG C CZ  1 
ATOM   6567 N  NH1 . ARG C  1  175 ? -10.502 23.861  27.318 1.00 69.23  ? 188 ARG C NH1 1 
ATOM   6568 N  NH2 . ARG C  1  175 ? -10.147 21.636  26.991 1.00 73.38  ? 188 ARG C NH2 1 
ATOM   6569 N  N   . ILE C  1  176 ? -6.679  26.459  24.133 1.00 67.61  ? 189 ILE C N   1 
ATOM   6570 C  CA  . ILE C  1  176 ? -5.323  26.651  24.618 1.00 69.42  ? 189 ILE C CA  1 
ATOM   6571 C  C   . ILE C  1  176 ? -5.352  27.694  25.736 1.00 75.18  ? 189 ILE C C   1 
ATOM   6572 O  O   . ILE C  1  176 ? -4.801  27.460  26.811 1.00 75.04  ? 189 ILE C O   1 
ATOM   6573 C  CB  . ILE C  1  176 ? -4.367  27.009  23.468 1.00 62.23  ? 189 ILE C CB  1 
ATOM   6574 C  CG1 . ILE C  1  176 ? -4.132  25.806  22.568 1.00 59.71  ? 189 ILE C CG1 1 
ATOM   6575 C  CG2 . ILE C  1  176 ? -3.050  27.570  24.001 1.00 64.77  ? 189 ILE C CG2 1 
ATOM   6576 C  CD1 . ILE C  1  176 ? -3.443  26.133  21.253 1.00 59.57  ? 189 ILE C CD1 1 
ATOM   6577 N  N   . GLN C  1  177 ? -6.041  28.816  25.492 1.00 78.08  ? 190 GLN C N   1 
ATOM   6578 C  CA  . GLN C  1  177 ? -6.190  29.875  26.482 1.00 76.59  ? 190 GLN C CA  1 
ATOM   6579 C  C   . GLN C  1  177 ? -6.843  29.345  27.762 1.00 70.61  ? 190 GLN C C   1 
ATOM   6580 O  O   . GLN C  1  177 ? -6.367  29.661  28.849 1.00 76.72  ? 190 GLN C O   1 
ATOM   6581 C  CB  . GLN C  1  177 ? -6.954  31.067  25.901 1.00 82.46  ? 190 GLN C CB  1 
ATOM   6582 C  CG  . GLN C  1  177 ? -6.257  31.745  24.723 1.00 85.10  ? 190 GLN C CG  1 
ATOM   6583 C  CD  . GLN C  1  177 ? -4.828  32.152  25.021 1.00 87.14  ? 190 GLN C CD  1 
ATOM   6584 O  OE1 . GLN C  1  177 ? -4.458  32.420  26.169 1.00 96.58  ? 190 GLN C OE1 1 
ATOM   6585 N  NE2 . GLN C  1  177 ? -4.002  32.206  23.990 1.00 85.41  ? 190 GLN C NE2 1 
ATOM   6586 N  N   . ASP C  1  178 ? -7.915  28.546  27.644 1.00 63.12  ? 191 ASP C N   1 
ATOM   6587 C  CA  . ASP C  1  178 ? -8.562  27.935  28.800 1.00 66.14  ? 191 ASP C CA  1 
ATOM   6588 C  C   . ASP C  1  178 ? -7.547  27.207  29.680 1.00 69.83  ? 191 ASP C C   1 
ATOM   6589 O  O   . ASP C  1  178 ? -7.587  27.318  30.910 1.00 66.13  ? 191 ASP C O   1 
ATOM   6590 C  CB  . ASP C  1  178 ? -9.644  26.934  28.418 1.00 67.84  ? 191 ASP C CB  1 
ATOM   6591 C  CG  . ASP C  1  178 ? -10.915 27.504  27.798 1.00 75.14  ? 191 ASP C CG  1 
ATOM   6592 O  OD1 . ASP C  1  178 ? -11.092 28.742  27.843 1.00 73.58  ? 191 ASP C OD1 1 
ATOM   6593 O  OD2 . ASP C  1  178 ? -11.733 26.705  27.268 1.00 79.83  ? 191 ASP C OD2 1 
ATOM   6594 N  N   . SER C  1  179 ? -6.653  26.440  29.046 1.00 69.83  ? 192 SER C N   1 
ATOM   6595 C  CA  . SER C  1  179 ? -5.723  25.597  29.780 1.00 68.09  ? 192 SER C CA  1 
ATOM   6596 C  C   . SER C  1  179 ? -4.600  26.431  30.408 1.00 65.67  ? 192 SER C C   1 
ATOM   6597 O  O   . SER C  1  179 ? -4.166  26.129  31.519 1.00 61.15  ? 192 SER C O   1 
ATOM   6598 C  CB  . SER C  1  179 ? -5.204  24.477  28.902 1.00 66.14  ? 192 SER C CB  1 
ATOM   6599 O  OG  . SER C  1  179 ? -6.170  23.441  28.772 1.00 58.11  ? 192 SER C OG  1 
ATOM   6600 N  N   . ILE C  1  180 ? -4.140  27.481  29.707 1.00 64.82  ? 193 ILE C N   1 
ATOM   6601 C  CA  . ILE C  1  180 ? -3.131  28.384  30.246 1.00 65.29  ? 193 ILE C CA  1 
ATOM   6602 C  C   . ILE C  1  180 ? -3.643  28.990  31.553 1.00 75.05  ? 193 ILE C C   1 
ATOM   6603 O  O   . ILE C  1  180 ? -2.910  29.072  32.538 1.00 84.34  ? 193 ILE C O   1 
ATOM   6604 C  CB  . ILE C  1  180 ? -2.750  29.476  29.228 1.00 66.45  ? 193 ILE C CB  1 
ATOM   6605 C  CG1 . ILE C  1  180 ? -1.942  28.900  28.064 1.00 64.90  ? 193 ILE C CG1 1 
ATOM   6606 C  CG2 . ILE C  1  180 ? -2.003  30.628  29.908 1.00 69.81  ? 193 ILE C CG2 1 
ATOM   6607 C  CD1 . ILE C  1  180 ? -1.616  29.903  26.968 1.00 63.19  ? 193 ILE C CD1 1 
ATOM   6608 N  N   . ALA C  1  181 ? -4.918  29.393  31.550 1.00 81.17  ? 194 ALA C N   1 
ATOM   6609 C  CA  . ALA C  1  181 ? -5.496  30.176  32.629 1.00 77.24  ? 194 ALA C CA  1 
ATOM   6610 C  C   . ALA C  1  181 ? -5.886  29.312  33.824 1.00 73.57  ? 194 ALA C C   1 
ATOM   6611 O  O   . ALA C  1  181 ? -6.063  29.847  34.914 1.00 81.03  ? 194 ALA C O   1 
ATOM   6612 C  CB  . ALA C  1  181 ? -6.701  30.933  32.122 1.00 79.38  ? 194 ALA C CB  1 
ATOM   6613 N  N   . THR C  1  182 ? -6.068  28.000  33.635 1.00 71.45  ? 195 THR C N   1 
ATOM   6614 C  CA  . THR C  1  182 ? -6.702  27.213  34.685 1.00 73.93  ? 195 THR C CA  1 
ATOM   6615 C  C   . THR C  1  182 ? -5.895  25.968  35.060 1.00 71.22  ? 195 THR C C   1 
ATOM   6616 O  O   . THR C  1  182 ? -6.207  25.333  36.061 1.00 72.57  ? 195 THR C O   1 
ATOM   6617 C  CB  . THR C  1  182 ? -8.130  26.841  34.277 1.00 79.41  ? 195 THR C CB  1 
ATOM   6618 O  OG1 . THR C  1  182 ? -8.063  25.951  33.166 1.00 89.87  ? 195 THR C OG1 1 
ATOM   6619 C  CG2 . THR C  1  182 ? -8.979  28.049  33.916 1.00 77.74  ? 195 THR C CG2 1 
ATOM   6620 N  N   . ASN C  1  183 ? -4.880  25.598  34.271 1.00 71.90  ? 196 ASN C N   1 
ATOM   6621 C  CA  . ASN C  1  183 ? -4.159  24.354  34.503 1.00 70.03  ? 196 ASN C CA  1 
ATOM   6622 C  C   . ASN C  1  183 ? -2.691  24.684  34.717 1.00 62.48  ? 196 ASN C C   1 
ATOM   6623 O  O   . ASN C  1  183 ? -1.977  24.998  33.774 1.00 60.17  ? 196 ASN C O   1 
ATOM   6624 C  CB  . ASN C  1  183 ? -4.344  23.348  33.368 1.00 74.10  ? 196 ASN C CB  1 
ATOM   6625 C  CG  . ASN C  1  183 ? -3.586  22.053  33.581 1.00 75.30  ? 196 ASN C CG  1 
ATOM   6626 O  OD1 . ASN C  1  183 ? -2.938  21.855  34.616 1.00 78.98  ? 196 ASN C OD1 1 
ATOM   6627 N  ND2 . ASN C  1  183 ? -3.660  21.150  32.611 1.00 74.70  ? 196 ASN C ND2 1 
ATOM   6628 N  N   . PRO C  1  184 ? -2.189  24.613  35.964 1.00 64.99  ? 197 PRO C N   1 
ATOM   6629 C  CA  . PRO C  1  184 ? -0.784  24.929  36.221 1.00 68.09  ? 197 PRO C CA  1 
ATOM   6630 C  C   . PRO C  1  184 ? 0.222   23.938  35.628 1.00 73.08  ? 197 PRO C C   1 
ATOM   6631 O  O   . PRO C  1  184 ? 1.384   24.300  35.424 1.00 68.44  ? 197 PRO C O   1 
ATOM   6632 C  CB  . PRO C  1  184 ? -0.758  24.955  37.753 1.00 67.54  ? 197 PRO C CB  1 
ATOM   6633 C  CG  . PRO C  1  184 ? -1.831  23.964  38.167 1.00 66.38  ? 197 PRO C CG  1 
ATOM   6634 C  CD  . PRO C  1  184 ? -2.936  24.207  37.168 1.00 65.11  ? 197 PRO C CD  1 
ATOM   6635 N  N   . GLU C  1  185 ? -0.233  22.705  35.331 1.00 73.98  ? 198 GLU C N   1 
ATOM   6636 C  CA  . GLU C  1  185 ? 0.624   21.660  34.781 1.00 70.86  ? 198 GLU C CA  1 
ATOM   6637 C  C   . GLU C  1  185 ? 0.513   21.593  33.254 1.00 65.39  ? 198 GLU C C   1 
ATOM   6638 O  O   . GLU C  1  185 ? 1.047   20.676  32.641 1.00 64.58  ? 198 GLU C O   1 
ATOM   6639 C  CB  . GLU C  1  185 ? 0.273   20.303  35.391 1.00 71.24  ? 198 GLU C CB  1 
ATOM   6640 C  CG  . GLU C  1  185 ? 0.708   20.120  36.841 1.00 73.67  ? 198 GLU C CG  1 
ATOM   6641 C  CD  . GLU C  1  185 ? 0.163   18.857  37.501 1.00 84.64  ? 198 GLU C CD  1 
ATOM   6642 O  OE1 . GLU C  1  185 ? -0.538  18.079  36.820 1.00 84.49  ? 198 GLU C OE1 1 
ATOM   6643 O  OE2 . GLU C  1  185 ? 0.419   18.635  38.706 1.00 91.04  ? 198 GLU C OE2 1 
ATOM   6644 N  N   . PHE C  1  186 ? -0.120  22.598  32.637 1.00 61.48  ? 199 PHE C N   1 
ATOM   6645 C  CA  . PHE C  1  186 ? -0.418  22.580  31.216 1.00 59.53  ? 199 PHE C CA  1 
ATOM   6646 C  C   . PHE C  1  186 ? 0.858   22.452  30.393 1.00 60.20  ? 199 PHE C C   1 
ATOM   6647 O  O   . PHE C  1  186 ? 1.731   23.318  30.462 1.00 60.59  ? 199 PHE C O   1 
ATOM   6648 C  CB  . PHE C  1  186 ? -1.144  23.864  30.805 1.00 60.69  ? 199 PHE C CB  1 
ATOM   6649 C  CG  . PHE C  1  186 ? -1.454  24.003  29.320 1.00 56.53  ? 199 PHE C CG  1 
ATOM   6650 C  CD1 . PHE C  1  186 ? -2.053  22.970  28.607 1.00 52.69  ? 199 PHE C CD1 1 
ATOM   6651 C  CD2 . PHE C  1  186 ? -1.141  25.172  28.639 1.00 54.67  ? 199 PHE C CD2 1 
ATOM   6652 C  CE1 . PHE C  1  186 ? -2.340  23.117  27.261 1.00 50.52  ? 199 PHE C CE1 1 
ATOM   6653 C  CE2 . PHE C  1  186 ? -1.418  25.301  27.290 1.00 52.50  ? 199 PHE C CE2 1 
ATOM   6654 C  CZ  . PHE C  1  186 ? -2.009  24.274  26.605 1.00 52.59  ? 199 PHE C CZ  1 
ATOM   6655 N  N   . GLN C  1  187 ? 0.911   21.374  29.595 1.00 59.32  ? 200 GLN C N   1 
ATOM   6656 C  CA  . GLN C  1  187 ? 1.960   21.134  28.616 1.00 57.60  ? 200 GLN C CA  1 
ATOM   6657 C  C   . GLN C  1  187 ? 1.354   21.135  27.213 1.00 56.31  ? 200 GLN C C   1 
ATOM   6658 O  O   . GLN C  1  187 ? 0.268   20.601  27.008 1.00 60.46  ? 200 GLN C O   1 
ATOM   6659 C  CB  . GLN C  1  187 ? 2.600   19.780  28.923 1.00 58.87  ? 200 GLN C CB  1 
ATOM   6660 C  CG  . GLN C  1  187 ? 3.438   19.753  30.197 1.00 61.04  ? 200 GLN C CG  1 
ATOM   6661 C  CD  . GLN C  1  187 ? 4.690   20.596  30.081 1.00 63.30  ? 200 GLN C CD  1 
ATOM   6662 O  OE1 . GLN C  1  187 ? 5.670   20.208  29.442 1.00 62.08  ? 200 GLN C OE1 1 
ATOM   6663 N  NE2 . GLN C  1  187 ? 4.672   21.772  30.688 1.00 69.33  ? 200 GLN C NE2 1 
ATOM   6664 N  N   . PHE C  1  188 ? 2.056   21.726  26.242 1.00 51.35  ? 201 PHE C N   1 
ATOM   6665 C  CA  . PHE C  1  188 ? 1.599   21.722  24.858 1.00 47.80  ? 201 PHE C CA  1 
ATOM   6666 C  C   . PHE C  1  188 ? 2.811   21.638  23.935 1.00 44.18  ? 201 PHE C C   1 
ATOM   6667 O  O   . PHE C  1  188 ? 3.097   22.568  23.186 1.00 44.10  ? 201 PHE C O   1 
ATOM   6668 C  CB  . PHE C  1  188 ? 0.750   22.972  24.619 1.00 48.76  ? 201 PHE C CB  1 
ATOM   6669 C  CG  . PHE C  1  188 ? -0.212  22.882  23.442 1.00 50.40  ? 201 PHE C CG  1 
ATOM   6670 C  CD1 . PHE C  1  188 ? -1.348  22.082  23.517 1.00 50.99  ? 201 PHE C CD1 1 
ATOM   6671 C  CD2 . PHE C  1  188 ? -0.028  23.640  22.290 1.00 47.76  ? 201 PHE C CD2 1 
ATOM   6672 C  CE1 . PHE C  1  188 ? -2.248  22.024  22.466 1.00 47.64  ? 201 PHE C CE1 1 
ATOM   6673 C  CE2 . PHE C  1  188 ? -0.933  23.575  21.246 1.00 45.16  ? 201 PHE C CE2 1 
ATOM   6674 C  CZ  . PHE C  1  188 ? -2.029  22.755  21.328 1.00 45.30  ? 201 PHE C CZ  1 
ATOM   6675 N  N   . LYS C  1  189 ? 3.526   20.511  23.999 1.00 45.00  ? 202 LYS C N   1 
ATOM   6676 C  CA  . LYS C  1  189 ? 4.760   20.355  23.245 1.00 50.67  ? 202 LYS C CA  1 
ATOM   6677 C  C   . LYS C  1  189 ? 4.884   18.936  22.689 1.00 47.76  ? 202 LYS C C   1 
ATOM   6678 O  O   . LYS C  1  189 ? 4.153   18.028  23.087 1.00 42.58  ? 202 LYS C O   1 
ATOM   6679 C  CB  . LYS C  1  189 ? 5.959   20.697  24.141 1.00 58.59  ? 202 LYS C CB  1 
ATOM   6680 C  CG  . LYS C  1  189 ? 6.070   19.855  25.410 1.00 65.84  ? 202 LYS C CG  1 
ATOM   6681 C  CD  . LYS C  1  189 ? 7.414   20.012  26.101 1.00 67.90  ? 202 LYS C CD  1 
ATOM   6682 C  CE  . LYS C  1  189 ? 7.540   21.344  26.745 1.00 71.33  ? 202 LYS C CE  1 
ATOM   6683 N  NZ  . LYS C  1  189 ? 7.752   21.195  28.185 1.00 77.65  ? 202 LYS C NZ  1 
ATOM   6684 N  N   . ASN C  1  190 ? 5.811   18.774  21.736 1.00 46.87  ? 203 ASN C N   1 
ATOM   6685 C  CA  . ASN C  1  190 ? 6.191   17.468  21.228 1.00 47.87  ? 203 ASN C CA  1 
ATOM   6686 C  C   . ASN C  1  190 ? 4.985   16.776  20.594 1.00 47.30  ? 203 ASN C C   1 
ATOM   6687 O  O   . ASN C  1  190 ? 4.371   17.333  19.693 1.00 43.28  ? 203 ASN C O   1 
ATOM   6688 C  CB  . ASN C  1  190 ? 6.882   16.659  22.317 1.00 50.03  ? 203 ASN C CB  1 
ATOM   6689 C  CG  . ASN C  1  190 ? 8.165   17.313  22.753 1.00 53.02  ? 203 ASN C CG  1 
ATOM   6690 O  OD1 . ASN C  1  190 ? 8.925   17.794  21.900 1.00 58.02  ? 203 ASN C OD1 1 
ATOM   6691 N  ND2 . ASN C  1  190 ? 8.419   17.334  24.055 1.00 50.34  ? 203 ASN C ND2 1 
ATOM   6692 N  N   . VAL C  1  191 ? 4.654   15.566  21.053 1.00 45.71  ? 204 VAL C N   1 
ATOM   6693 C  CA  . VAL C  1  191 ? 3.588   14.804  20.429 1.00 46.14  ? 204 VAL C CA  1 
ATOM   6694 C  C   . VAL C  1  191 ? 2.294   15.617  20.483 1.00 46.18  ? 204 VAL C C   1 
ATOM   6695 O  O   . VAL C  1  191 ? 1.589   15.750  19.488 1.00 50.88  ? 204 VAL C O   1 
ATOM   6696 C  CB  . VAL C  1  191 ? 3.391   13.428  21.089 1.00 45.32  ? 204 VAL C CB  1 
ATOM   6697 C  CG1 . VAL C  1  191 ? 2.230   12.671  20.458 1.00 45.91  ? 204 VAL C CG1 1 
ATOM   6698 C  CG2 . VAL C  1  191 ? 4.660   12.585  21.051 1.00 46.83  ? 204 VAL C CG2 1 
ATOM   6699 N  N   . ARG C  1  192 ? 1.986   16.176  21.652 1.00 45.18  ? 205 ARG C N   1 
ATOM   6700 C  CA  . ARG C  1  192 ? 0.700   16.816  21.834 1.00 43.60  ? 205 ARG C CA  1 
ATOM   6701 C  C   . ARG C  1  192 ? 0.554   18.009  20.895 1.00 42.74  ? 205 ARG C C   1 
ATOM   6702 O  O   . ARG C  1  192 ? -0.522  18.264  20.376 1.00 39.23  ? 205 ARG C O   1 
ATOM   6703 C  CB  . ARG C  1  192 ? 0.490   17.262  23.282 1.00 47.52  ? 205 ARG C CB  1 
ATOM   6704 C  CG  . ARG C  1  192 ? -0.886  17.877  23.494 1.00 50.51  ? 205 ARG C CG  1 
ATOM   6705 C  CD  . ARG C  1  192 ? -2.005  16.985  22.988 1.00 54.90  ? 205 ARG C CD  1 
ATOM   6706 N  NE  . ARG C  1  192 ? -3.329  17.608  23.077 1.00 62.43  ? 205 ARG C NE  1 
ATOM   6707 C  CZ  . ARG C  1  192 ? -4.390  17.251  22.364 1.00 64.05  ? 205 ARG C CZ  1 
ATOM   6708 N  NH1 . ARG C  1  192 ? -4.297  16.275  21.476 1.00 63.00  ? 205 ARG C NH1 1 
ATOM   6709 N  NH2 . ARG C  1  192 ? -5.538  17.883  22.534 1.00 71.10  ? 205 ARG C NH2 1 
ATOM   6710 N  N   . PHE C  1  193 ? 1.637   18.757  20.683 1.00 47.68  ? 206 PHE C N   1 
ATOM   6711 C  CA  . PHE C  1  193 ? 1.548   19.954  19.866 1.00 48.38  ? 206 PHE C CA  1 
ATOM   6712 C  C   . PHE C  1  193 ? 1.144   19.573  18.448 1.00 47.86  ? 206 PHE C C   1 
ATOM   6713 O  O   . PHE C  1  193 ? 0.368   20.288  17.830 1.00 48.20  ? 206 PHE C O   1 
ATOM   6714 C  CB  . PHE C  1  193 ? 2.856   20.738  19.883 1.00 46.62  ? 206 PHE C CB  1 
ATOM   6715 C  CG  . PHE C  1  193 ? 2.795   21.982  19.018 1.00 48.98  ? 206 PHE C CG  1 
ATOM   6716 C  CD1 . PHE C  1  193 ? 2.223   23.152  19.494 1.00 49.54  ? 206 PHE C CD1 1 
ATOM   6717 C  CD2 . PHE C  1  193 ? 3.289   21.965  17.723 1.00 53.86  ? 206 PHE C CD2 1 
ATOM   6718 C  CE1 . PHE C  1  193 ? 2.167   24.283  18.698 1.00 53.75  ? 206 PHE C CE1 1 
ATOM   6719 C  CE2 . PHE C  1  193 ? 3.231   23.100  16.930 1.00 57.01  ? 206 PHE C CE2 1 
ATOM   6720 C  CZ  . PHE C  1  193 ? 2.674   24.257  17.418 1.00 55.77  ? 206 PHE C CZ  1 
ATOM   6721 N  N   . ILE C  1  194 ? 1.660   18.442  17.946 1.00 47.75  ? 207 ILE C N   1 
ATOM   6722 C  CA  . ILE C  1  194 ? 1.342   17.998  16.601 1.00 47.15  ? 207 ILE C CA  1 
ATOM   6723 C  C   . ILE C  1  194 ? -0.060  17.397  16.563 1.00 47.49  ? 207 ILE C C   1 
ATOM   6724 O  O   . ILE C  1  194 ? -0.844  17.756  15.691 1.00 51.39  ? 207 ILE C O   1 
ATOM   6725 C  CB  . ILE C  1  194 ? 2.412   17.033  16.071 1.00 48.12  ? 207 ILE C CB  1 
ATOM   6726 C  CG1 . ILE C  1  194 ? 3.804   17.690  16.096 1.00 51.71  ? 207 ILE C CG1 1 
ATOM   6727 C  CG2 . ILE C  1  194 ? 2.055   16.516  14.674 1.00 48.69  ? 207 ILE C CG2 1 
ATOM   6728 C  CD1 . ILE C  1  194 ? 3.909   18.972  15.283 1.00 54.78  ? 207 ILE C CD1 1 
ATOM   6729 N  N   . THR C  1  195 ? -0.393  16.518  17.512 1.00 47.00  ? 208 THR C N   1 
ATOM   6730 C  CA  . THR C  1  195 ? -1.666  15.817  17.451 1.00 48.37  ? 208 THR C CA  1 
ATOM   6731 C  C   . THR C  1  195 ? -2.828  16.784  17.680 1.00 50.60  ? 208 THR C C   1 
ATOM   6732 O  O   . THR C  1  195 ? -3.887  16.587  17.109 1.00 52.48  ? 208 THR C O   1 
ATOM   6733 C  CB  . THR C  1  195 ? -1.702  14.614  18.395 1.00 47.70  ? 208 THR C CB  1 
ATOM   6734 O  OG1 . THR C  1  195 ? -1.632  14.982  19.768 1.00 51.07  ? 208 THR C OG1 1 
ATOM   6735 C  CG2 . THR C  1  195 ? -0.572  13.644  18.100 1.00 49.13  ? 208 THR C CG2 1 
ATOM   6736 N  N   . ALA C  1  196 ? -2.626  17.851  18.460 1.00 54.51  ? 209 ALA C N   1 
ATOM   6737 C  CA  . ALA C  1  196 ? -3.700  18.775  18.804 1.00 52.48  ? 209 ALA C CA  1 
ATOM   6738 C  C   . ALA C  1  196 ? -4.239  19.531  17.593 1.00 51.81  ? 209 ALA C C   1 
ATOM   6739 O  O   . ALA C  1  196 ? -5.377  19.980  17.625 1.00 61.08  ? 209 ALA C O   1 
ATOM   6740 C  CB  . ALA C  1  196 ? -3.254  19.765  19.860 1.00 53.02  ? 209 ALA C CB  1 
ATOM   6741 N  N   . TYR C  1  197 ? -3.438  19.720  16.546 1.00 51.94  ? 210 TYR C N   1 
ATOM   6742 C  CA  . TYR C  1  197 ? -3.925  20.449  15.385 1.00 52.86  ? 210 TYR C CA  1 
ATOM   6743 C  C   . TYR C  1  197 ? -4.647  19.485  14.451 1.00 50.18  ? 210 TYR C C   1 
ATOM   6744 O  O   . TYR C  1  197 ? -5.682  19.834  13.898 1.00 53.48  ? 210 TYR C O   1 
ATOM   6745 C  CB  . TYR C  1  197 ? -2.784  21.248  14.750 1.00 56.49  ? 210 TYR C CB  1 
ATOM   6746 C  CG  . TYR C  1  197 ? -2.528  22.514  15.551 1.00 62.59  ? 210 TYR C CG  1 
ATOM   6747 C  CD1 . TYR C  1  197 ? -3.267  23.672  15.321 1.00 64.69  ? 210 TYR C CD1 1 
ATOM   6748 C  CD2 . TYR C  1  197 ? -1.608  22.527  16.588 1.00 64.24  ? 210 TYR C CD2 1 
ATOM   6749 C  CE1 . TYR C  1  197 ? -3.068  24.817  16.075 1.00 66.80  ? 210 TYR C CE1 1 
ATOM   6750 C  CE2 . TYR C  1  197 ? -1.392  23.670  17.341 1.00 65.88  ? 210 TYR C CE2 1 
ATOM   6751 C  CZ  . TYR C  1  197 ? -2.134  24.815  17.093 1.00 68.02  ? 210 TYR C CZ  1 
ATOM   6752 O  OH  . TYR C  1  197 ? -1.953  25.951  17.827 1.00 70.50  ? 210 TYR C OH  1 
ATOM   6753 N  N   . GLY C  1  198 ? -4.114  18.272  14.303 1.00 50.70  ? 211 GLY C N   1 
ATOM   6754 C  CA  . GLY C  1  198 ? -4.730  17.255  13.469 1.00 53.00  ? 211 GLY C CA  1 
ATOM   6755 C  C   . GLY C  1  198 ? -6.114  16.847  13.967 1.00 51.81  ? 211 GLY C C   1 
ATOM   6756 O  O   . GLY C  1  198 ? -7.022  16.651  13.175 1.00 50.68  ? 211 GLY C O   1 
ATOM   6757 N  N   . GLU C  1  199 ? -6.272  16.706  15.281 1.00 55.41  ? 212 GLU C N   1 
ATOM   6758 C  CA  . GLU C  1  199 ? -7.521  16.216  15.843 1.00 58.86  ? 212 GLU C CA  1 
ATOM   6759 C  C   . GLU C  1  199 ? -8.645  17.215  15.548 1.00 52.25  ? 212 GLU C C   1 
ATOM   6760 O  O   . GLU C  1  199 ? -9.799  16.817  15.478 1.00 49.17  ? 212 GLU C O   1 
ATOM   6761 C  CB  . GLU C  1  199 ? -7.357  15.893  17.335 1.00 63.92  ? 212 GLU C CB  1 
ATOM   6762 C  CG  . GLU C  1  199 ? -7.365  17.127  18.245 1.00 72.90  ? 212 GLU C CG  1 
ATOM   6763 C  CD  . GLU C  1  199 ? -7.243  16.903  19.757 1.00 79.38  ? 212 GLU C CD  1 
ATOM   6764 O  OE1 . GLU C  1  199 ? -6.815  15.778  20.180 1.00 73.77  ? 212 GLU C OE1 1 
ATOM   6765 O  OE2 . GLU C  1  199 ? -7.558  17.871  20.520 1.00 62.39  ? 212 GLU C OE2 1 
ATOM   6766 N  N   . THR C  1  200 ? -8.326  18.501  15.342 1.00 48.34  ? 213 THR C N   1 
ATOM   6767 C  CA  . THR C  1  200 ? -9.372  19.497  15.181 1.00 52.00  ? 213 THR C CA  1 
ATOM   6768 C  C   . THR C  1  200 ? -9.931  19.465  13.765 1.00 52.76  ? 213 THR C C   1 
ATOM   6769 O  O   . THR C  1  200 ? -10.988 20.047  13.544 1.00 60.22  ? 213 THR C O   1 
ATOM   6770 C  CB  . THR C  1  200 ? -8.902  20.909  15.536 1.00 56.89  ? 213 THR C CB  1 
ATOM   6771 O  OG1 . THR C  1  200 ? -8.048  21.374  14.495 1.00 61.13  ? 213 THR C OG1 1 
ATOM   6772 C  CG2 . THR C  1  200 ? -8.190  20.978  16.872 1.00 54.47  ? 213 THR C CG2 1 
ATOM   6773 N  N   . VAL C  1  201 ? -9.237  18.824  12.811 1.00 48.88  ? 214 VAL C N   1 
ATOM   6774 C  CA  . VAL C  1  201 ? -9.761  18.729  11.457 1.00 42.47  ? 214 VAL C CA  1 
ATOM   6775 C  C   . VAL C  1  201 ? -10.314 17.336  11.168 1.00 40.94  ? 214 VAL C C   1 
ATOM   6776 O  O   . VAL C  1  201 ? -11.015 17.177  10.180 1.00 37.16  ? 214 VAL C O   1 
ATOM   6777 C  CB  . VAL C  1  201 ? -8.752  19.150  10.381 1.00 45.49  ? 214 VAL C CB  1 
ATOM   6778 C  CG1 . VAL C  1  201 ? -8.330  20.595  10.578 1.00 47.34  ? 214 VAL C CG1 1 
ATOM   6779 C  CG2 . VAL C  1  201 ? -7.533  18.243  10.316 1.00 50.58  ? 214 VAL C CG2 1 
ATOM   6780 N  N   . PHE C  1  202 ? -10.050 16.343  12.024 1.00 39.06  ? 215 PHE C N   1 
ATOM   6781 C  CA  . PHE C  1  202 ? -10.578 15.009  11.790 1.00 44.46  ? 215 PHE C CA  1 
ATOM   6782 C  C   . PHE C  1  202 ? -12.103 15.048  11.698 1.00 49.61  ? 215 PHE C C   1 
ATOM   6783 O  O   . PHE C  1  202 ? -12.682 14.379  10.851 1.00 57.68  ? 215 PHE C O   1 
ATOM   6784 C  CB  . PHE C  1  202 ? -10.149 13.984  12.844 1.00 47.73  ? 215 PHE C CB  1 
ATOM   6785 C  CG  . PHE C  1  202 ? -8.694  13.547  12.793 1.00 47.81  ? 215 PHE C CG  1 
ATOM   6786 C  CD1 . PHE C  1  202 ? -7.855  13.916  11.745 1.00 46.99  ? 215 PHE C CD1 1 
ATOM   6787 C  CD2 . PHE C  1  202 ? -8.186  12.725  13.786 1.00 47.22  ? 215 PHE C CD2 1 
ATOM   6788 C  CE1 . PHE C  1  202 ? -6.528  13.514  11.728 1.00 49.08  ? 215 PHE C CE1 1 
ATOM   6789 C  CE2 . PHE C  1  202 ? -6.867  12.307  13.748 1.00 50.72  ? 215 PHE C CE2 1 
ATOM   6790 C  CZ  . PHE C  1  202 ? -6.036  12.716  12.734 1.00 50.32  ? 215 PHE C CZ  1 
ATOM   6791 N  N   . PRO C  1  203 ? -12.825 15.797  12.556 1.00 51.21  ? 216 PRO C N   1 
ATOM   6792 C  CA  . PRO C  1  203 ? -14.279 15.859  12.444 1.00 51.74  ? 216 PRO C CA  1 
ATOM   6793 C  C   . PRO C  1  203 ? -14.784 16.330  11.079 1.00 48.90  ? 216 PRO C C   1 
ATOM   6794 O  O   . PRO C  1  203 ? -15.826 15.877  10.617 1.00 43.95  ? 216 PRO C O   1 
ATOM   6795 C  CB  . PRO C  1  203 ? -14.667 16.819  13.581 1.00 52.72  ? 216 PRO C CB  1 
ATOM   6796 C  CG  . PRO C  1  203 ? -13.536 16.696  14.569 1.00 50.35  ? 216 PRO C CG  1 
ATOM   6797 C  CD  . PRO C  1  203 ? -12.309 16.559  13.700 1.00 51.82  ? 216 PRO C CD  1 
ATOM   6798 N  N   . ILE C  1  204 ? -14.034 17.225  10.434 1.00 45.83  ? 217 ILE C N   1 
ATOM   6799 C  CA  . ILE C  1  204 ? -14.397 17.727  9.117  1.00 45.63  ? 217 ILE C CA  1 
ATOM   6800 C  C   . ILE C  1  204 ? -14.103 16.668  8.053  1.00 41.93  ? 217 ILE C C   1 
ATOM   6801 O  O   . ILE C  1  204 ? -14.939 16.389  7.208  1.00 44.12  ? 217 ILE C O   1 
ATOM   6802 C  CB  . ILE C  1  204 ? -13.641 19.037  8.829  1.00 47.47  ? 217 ILE C CB  1 
ATOM   6803 C  CG1 . ILE C  1  204 ? -13.965 20.102  9.870  1.00 47.05  ? 217 ILE C CG1 1 
ATOM   6804 C  CG2 . ILE C  1  204 ? -13.906 19.533  7.410  1.00 46.87  ? 217 ILE C CG2 1 
ATOM   6805 C  CD1 . ILE C  1  204 ? -13.043 21.310  9.825  1.00 49.85  ? 217 ILE C CD1 1 
ATOM   6806 N  N   . ASN C  1  205 ? -12.899 16.089  8.088  1.00 42.15  ? 218 ASN C N   1 
ATOM   6807 C  CA  . ASN C  1  205 ? -12.435 15.243  7.004  1.00 39.84  ? 218 ASN C CA  1 
ATOM   6808 C  C   . ASN C  1  205 ? -12.964 13.820  7.140  1.00 39.84  ? 218 ASN C C   1 
ATOM   6809 O  O   . ASN C  1  205 ? -13.082 13.142  6.121  1.00 40.31  ? 218 ASN C O   1 
ATOM   6810 C  CB  . ASN C  1  205 ? -10.920 15.222  6.892  1.00 40.28  ? 218 ASN C CB  1 
ATOM   6811 C  CG  . ASN C  1  205 ? -10.320 16.601  6.776  1.00 41.96  ? 218 ASN C CG  1 
ATOM   6812 O  OD1 . ASN C  1  205 ? -10.943 17.516  6.231  1.00 42.36  ? 218 ASN C OD1 1 
ATOM   6813 N  ND2 . ASN C  1  205 ? -9.109  16.771  7.286  1.00 44.79  ? 218 ASN C ND2 1 
ATOM   6814 N  N   . LEU C  1  206 ? -13.302 13.380  8.365  1.00 37.96  ? 219 LEU C N   1 
ATOM   6815 C  CA  . LEU C  1  206 ? -13.651 11.984  8.597  1.00 38.16  ? 219 LEU C CA  1 
ATOM   6816 C  C   . LEU C  1  206 ? -15.047 11.768  9.185  1.00 41.52  ? 219 LEU C C   1 
ATOM   6817 O  O   . LEU C  1  206 ? -15.597 10.680  9.002  1.00 43.65  ? 219 LEU C O   1 
ATOM   6818 C  CB  . LEU C  1  206 ? -12.582 11.368  9.491  1.00 40.12  ? 219 LEU C CB  1 
ATOM   6819 C  CG  . LEU C  1  206 ? -11.173 11.347  8.898  1.00 44.21  ? 219 LEU C CG  1 
ATOM   6820 C  CD1 . LEU C  1  206 ? -10.176 10.933  9.970  1.00 47.01  ? 219 LEU C CD1 1 
ATOM   6821 C  CD2 . LEU C  1  206 ? -11.084 10.402  7.704  1.00 45.21  ? 219 LEU C CD2 1 
ATOM   6822 N  N   . PHE C  1  207 ? -15.598 12.746  9.929  1.00 45.21  ? 220 PHE C N   1 
ATOM   6823 C  CA  . PHE C  1  207 ? -16.888 12.574  10.588 1.00 43.41  ? 220 PHE C CA  1 
ATOM   6824 C  C   . PHE C  1  207 ? -18.023 13.116  9.723  1.00 42.60  ? 220 PHE C C   1 
ATOM   6825 O  O   . PHE C  1  207 ? -19.180 12.805  9.964  1.00 45.29  ? 220 PHE C O   1 
ATOM   6826 C  CB  . PHE C  1  207 ? -16.985 13.265  11.948 1.00 43.79  ? 220 PHE C CB  1 
ATOM   6827 C  CG  . PHE C  1  207 ? -16.112 12.690  13.054 1.00 45.98  ? 220 PHE C CG  1 
ATOM   6828 C  CD1 . PHE C  1  207 ? -15.526 11.431  12.946 1.00 46.12  ? 220 PHE C CD1 1 
ATOM   6829 C  CD2 . PHE C  1  207 ? -15.911 13.414  14.224 1.00 44.77  ? 220 PHE C CD2 1 
ATOM   6830 C  CE1 . PHE C  1  207 ? -14.735 10.931  13.967 1.00 45.85  ? 220 PHE C CE1 1 
ATOM   6831 C  CE2 . PHE C  1  207 ? -15.122 12.913  15.245 1.00 44.70  ? 220 PHE C CE2 1 
ATOM   6832 C  CZ  . PHE C  1  207 ? -14.533 11.675  15.114 1.00 45.05  ? 220 PHE C CZ  1 
ATOM   6833 N  N   . VAL C  1  208 ? -17.694 13.955  8.744  1.00 44.77  ? 221 VAL C N   1 
ATOM   6834 C  CA  . VAL C  1  208 ? -18.674 14.397  7.770  1.00 43.84  ? 221 VAL C CA  1 
ATOM   6835 C  C   . VAL C  1  208 ? -18.846 13.300  6.723  1.00 47.75  ? 221 VAL C C   1 
ATOM   6836 O  O   . VAL C  1  208 ? -17.871 12.742  6.213  1.00 47.05  ? 221 VAL C O   1 
ATOM   6837 C  CB  . VAL C  1  208 ? -18.263 15.724  7.116  1.00 41.34  ? 221 VAL C CB  1 
ATOM   6838 C  CG1 . VAL C  1  208 ? -19.226 16.133  6.015  1.00 45.10  ? 221 VAL C CG1 1 
ATOM   6839 C  CG2 . VAL C  1  208 ? -18.164 16.833  8.138  1.00 43.13  ? 221 VAL C CG2 1 
ATOM   6840 N  N   . ASP C  1  209 ? -20.109 13.014  6.414  1.00 48.11  ? 222 ASP C N   1 
ATOM   6841 C  CA  . ASP C  1  209 ? -20.481 11.996  5.450  1.00 50.10  ? 222 ASP C CA  1 
ATOM   6842 C  C   . ASP C  1  209 ? -19.726 12.198  4.136  1.00 49.35  ? 222 ASP C C   1 
ATOM   6843 O  O   . ASP C  1  209 ? -19.560 13.326  3.672  1.00 46.13  ? 222 ASP C O   1 
ATOM   6844 C  CB  . ASP C  1  209 ? -21.989 12.003  5.255  1.00 49.33  ? 222 ASP C CB  1 
ATOM   6845 C  CG  . ASP C  1  209 ? -22.539 10.785  4.532  1.00 51.34  ? 222 ASP C CG  1 
ATOM   6846 O  OD1 . ASP C  1  209 ? -22.389 10.739  3.295  1.00 53.73  ? 222 ASP C OD1 1 
ATOM   6847 O  OD2 . ASP C  1  209 ? -23.068 9.878   5.214  1.00 43.94  ? 222 ASP C OD2 1 
ATOM   6848 N  N   . GLY C  1  210 ? -19.297 11.078  3.535  1.00 49.96  ? 223 GLY C N   1 
ATOM   6849 C  CA  . GLY C  1  210 ? -18.423 11.093  2.368  1.00 55.64  ? 223 GLY C CA  1 
ATOM   6850 C  C   . GLY C  1  210 ? -19.144 11.501  1.081  1.00 55.41  ? 223 GLY C C   1 
ATOM   6851 O  O   . GLY C  1  210 ? -18.485 11.874  0.114  1.00 50.32  ? 223 GLY C O   1 
ATOM   6852 N  N   . ARG C  1  211 ? -20.483 11.453  1.085  1.00 50.72  ? 224 ARG C N   1 
ATOM   6853 C  CA  . ARG C  1  211 ? -21.271 11.899  -0.049 1.00 46.73  ? 224 ARG C CA  1 
ATOM   6854 C  C   . ARG C  1  211 ? -21.325 13.425  -0.118 1.00 48.44  ? 224 ARG C C   1 
ATOM   6855 O  O   . ARG C  1  211 ? -21.704 13.962  -1.152 1.00 55.61  ? 224 ARG C O   1 
ATOM   6856 C  CB  . ARG C  1  211 ? -22.682 11.300  -0.016 1.00 42.78  ? 224 ARG C CB  1 
ATOM   6857 C  CG  . ARG C  1  211 ? -22.676 9.788   -0.189 1.00 42.21  ? 224 ARG C CG  1 
ATOM   6858 C  CD  . ARG C  1  211 ? -23.974 9.138   0.227  1.00 45.70  ? 224 ARG C CD  1 
ATOM   6859 N  NE  . ARG C  1  211 ? -24.233 9.316   1.660  1.00 55.58  ? 224 ARG C NE  1 
ATOM   6860 C  CZ  . ARG C  1  211 ? -25.240 8.780   2.345  1.00 57.93  ? 224 ARG C CZ  1 
ATOM   6861 N  NH1 . ARG C  1  211 ? -26.145 8.050   1.731  1.00 56.64  ? 224 ARG C NH1 1 
ATOM   6862 N  NH2 . ARG C  1  211 ? -25.342 8.965   3.648  1.00 60.40  ? 224 ARG C NH2 1 
ATOM   6863 N  N   . VAL C  1  212 ? -20.950 14.129  0.958  1.00 46.71  ? 225 VAL C N   1 
ATOM   6864 C  CA  . VAL C  1  212 ? -20.890 15.585  0.927  1.00 49.60  ? 225 VAL C CA  1 
ATOM   6865 C  C   . VAL C  1  212 ? -19.554 16.000  0.317  1.00 54.10  ? 225 VAL C C   1 
ATOM   6866 O  O   . VAL C  1  212 ? -18.515 15.830  0.938  1.00 60.28  ? 225 VAL C O   1 
ATOM   6867 C  CB  . VAL C  1  212 ? -21.068 16.173  2.343  1.00 47.86  ? 225 VAL C CB  1 
ATOM   6868 C  CG1 . VAL C  1  212 ? -20.922 17.693  2.392  1.00 45.95  ? 225 VAL C CG1 1 
ATOM   6869 C  CG2 . VAL C  1  212 ? -22.390 15.739  2.960  1.00 48.61  ? 225 VAL C CG2 1 
ATOM   6870 N  N   . THR C  1  213 ? -19.582 16.558  -0.896 1.00 64.10  ? 226 THR C N   1 
ATOM   6871 C  CA  . THR C  1  213 ? -18.364 16.863  -1.635 1.00 69.32  ? 226 THR C CA  1 
ATOM   6872 C  C   . THR C  1  213 ? -18.005 18.339  -1.503 1.00 67.18  ? 226 THR C C   1 
ATOM   6873 O  O   . THR C  1  213 ? -16.893 18.725  -1.830 1.00 67.50  ? 226 THR C O   1 
ATOM   6874 C  CB  . THR C  1  213 ? -18.548 16.479  -3.107 1.00 72.12  ? 226 THR C CB  1 
ATOM   6875 O  OG1 . THR C  1  213 ? -19.627 17.288  -3.582 1.00 73.85  ? 226 THR C OG1 1 
ATOM   6876 C  CG2 . THR C  1  213 ? -18.827 14.996  -3.296 1.00 68.66  ? 226 THR C CG2 1 
ATOM   6877 N  N   . THR C  1  214 ? -18.943 19.166  -1.040 1.00 76.56  ? 227 THR C N   1 
ATOM   6878 C  CA  . THR C  1  214 ? -18.781 20.606  -1.126 1.00 80.90  ? 227 THR C CA  1 
ATOM   6879 C  C   . THR C  1  214 ? -19.190 21.246  0.202  1.00 77.60  ? 227 THR C C   1 
ATOM   6880 O  O   . THR C  1  214 ? -20.214 20.876  0.783  1.00 72.65  ? 227 THR C O   1 
ATOM   6881 C  CB  . THR C  1  214 ? -19.604 21.082  -2.326 1.00 87.43  ? 227 THR C CB  1 
ATOM   6882 O  OG1 . THR C  1  214 ? -19.317 22.472  -2.410 1.00 88.84  ? 227 THR C OG1 1 
ATOM   6883 C  CG2 . THR C  1  214 ? -21.097 20.810  -2.202 1.00 84.38  ? 227 THR C CG2 1 
ATOM   6884 N  N   . ASP C  1  215 ? -18.370 22.196  0.683  1.00 77.57  ? 228 ASP C N   1 
ATOM   6885 C  CA  . ASP C  1  215 ? -18.719 22.986  1.855  1.00 85.85  ? 228 ASP C CA  1 
ATOM   6886 C  C   . ASP C  1  215 ? -18.882 22.046  3.053  1.00 77.39  ? 228 ASP C C   1 
ATOM   6887 O  O   . ASP C  1  215 ? -19.926 22.031  3.700  1.00 77.10  ? 228 ASP C O   1 
ATOM   6888 C  CB  . ASP C  1  215 ? -19.942 23.852  1.557  1.00 99.05  ? 228 ASP C CB  1 
ATOM   6889 C  CG  . ASP C  1  215 ? -20.346 24.889  2.600  1.00 106.36 ? 228 ASP C CG  1 
ATOM   6890 O  OD1 . ASP C  1  215 ? -19.440 25.560  3.132  1.00 120.31 ? 228 ASP C OD1 1 
ATOM   6891 O  OD2 . ASP C  1  215 ? -21.570 25.047  2.839  1.00 99.41  ? 228 ASP C OD2 1 
ATOM   6892 N  N   . ARG C  1  216 ? -17.844 21.244  3.320  1.00 68.64  ? 229 ARG C N   1 
ATOM   6893 C  CA  . ARG C  1  216 ? -17.933 20.177  4.301  1.00 65.40  ? 229 ARG C CA  1 
ATOM   6894 C  C   . ARG C  1  216 ? -17.982 20.777  5.703  1.00 62.49  ? 229 ARG C C   1 
ATOM   6895 O  O   . ARG C  1  216 ? -17.140 21.591  6.074  1.00 55.41  ? 229 ARG C O   1 
ATOM   6896 C  CB  . ARG C  1  216 ? -16.791 19.169  4.117  1.00 66.73  ? 229 ARG C CB  1 
ATOM   6897 C  CG  . ARG C  1  216 ? -16.974 18.246  2.920  1.00 63.89  ? 229 ARG C CG  1 
ATOM   6898 C  CD  . ARG C  1  216 ? -15.748 17.411  2.592  1.00 59.17  ? 229 ARG C CD  1 
ATOM   6899 N  NE  . ARG C  1  216 ? -15.442 16.424  3.631  1.00 57.59  ? 229 ARG C NE  1 
ATOM   6900 C  CZ  . ARG C  1  216 ? -16.139 15.320  3.898  1.00 59.18  ? 229 ARG C CZ  1 
ATOM   6901 N  NH1 . ARG C  1  216 ? -17.150 14.946  3.130  1.00 55.07  ? 229 ARG C NH1 1 
ATOM   6902 N  NH2 . ARG C  1  216 ? -15.807 14.568  4.936  1.00 60.72  ? 229 ARG C NH2 1 
ATOM   6903 N  N   . LYS C  1  217 ? -18.989 20.350  6.469  1.00 60.55  ? 230 LYS C N   1 
ATOM   6904 C  CA  . LYS C  1  217 ? -19.260 20.900  7.783  1.00 59.34  ? 230 LYS C CA  1 
ATOM   6905 C  C   . LYS C  1  217 ? -20.078 19.876  8.564  1.00 56.68  ? 230 LYS C C   1 
ATOM   6906 O  O   . LYS C  1  217 ? -20.884 19.157  7.978  1.00 55.54  ? 230 LYS C O   1 
ATOM   6907 C  CB  . LYS C  1  217 ? -20.015 22.222  7.633  1.00 68.10  ? 230 LYS C CB  1 
ATOM   6908 C  CG  . LYS C  1  217 ? -21.390 22.062  6.992  1.00 78.36  ? 230 LYS C CG  1 
ATOM   6909 C  CD  . LYS C  1  217 ? -22.174 23.331  6.678  1.00 84.01  ? 230 LYS C CD  1 
ATOM   6910 C  CE  . LYS C  1  217 ? -23.528 22.958  6.118  1.00 84.12  ? 230 LYS C CE  1 
ATOM   6911 N  NZ  . LYS C  1  217 ? -24.433 24.100  5.984  1.00 81.04  ? 230 LYS C NZ  1 
ATOM   6912 N  N   . LEU C  1  218 ? -19.857 19.818  9.881  1.00 53.73  ? 231 LEU C N   1 
ATOM   6913 C  CA  . LEU C  1  218 ? -20.415 18.761  10.709 1.00 56.35  ? 231 LEU C CA  1 
ATOM   6914 C  C   . LEU C  1  218 ? -21.560 19.326  11.543 1.00 56.32  ? 231 LEU C C   1 
ATOM   6915 O  O   . LEU C  1  218 ? -21.395 20.353  12.196 1.00 56.18  ? 231 LEU C O   1 
ATOM   6916 C  CB  . LEU C  1  218 ? -19.305 18.201  11.599 1.00 54.65  ? 231 LEU C CB  1 
ATOM   6917 C  CG  . LEU C  1  218 ? -19.693 17.012  12.483 1.00 52.49  ? 231 LEU C CG  1 
ATOM   6918 C  CD1 . LEU C  1  218 ? -19.952 15.755  11.682 1.00 52.53  ? 231 LEU C CD1 1 
ATOM   6919 C  CD2 . LEU C  1  218 ? -18.639 16.763  13.527 1.00 53.45  ? 231 LEU C CD2 1 
ATOM   6920 N  N   . SER C  1  219 ? -22.707 18.639  11.533 1.00 58.06  ? 232 SER C N   1 
ATOM   6921 C  CA  . SER C  1  219 ? -23.849 19.044  12.340 1.00 60.76  ? 232 SER C CA  1 
ATOM   6922 C  C   . SER C  1  219 ? -23.595 18.701  13.808 1.00 62.57  ? 232 SER C C   1 
ATOM   6923 O  O   . SER C  1  219 ? -22.807 17.812  14.106 1.00 60.41  ? 232 SER C O   1 
ATOM   6924 C  CB  . SER C  1  219 ? -25.114 18.393  11.844 1.00 55.11  ? 232 SER C CB  1 
ATOM   6925 O  OG  . SER C  1  219 ? -25.144 17.016  12.194 1.00 55.89  ? 232 SER C OG  1 
ATOM   6926 N  N   . MET C  1  220 ? -24.295 19.376  14.726 1.00 61.07  ? 233 MET C N   1 
ATOM   6927 C  CA  . MET C  1  220 ? -24.116 19.098  16.141 1.00 56.95  ? 233 MET C CA  1 
ATOM   6928 C  C   . MET C  1  220 ? -24.737 17.758  16.521 1.00 55.70  ? 233 MET C C   1 
ATOM   6929 O  O   . MET C  1  220 ? -24.299 17.130  17.485 1.00 62.98  ? 233 MET C O   1 
ATOM   6930 C  CB  . MET C  1  220 ? -24.716 20.207  17.004 1.00 59.00  ? 233 MET C CB  1 
ATOM   6931 C  CG  . MET C  1  220 ? -24.110 21.578  16.771 1.00 65.77  ? 233 MET C CG  1 
ATOM   6932 S  SD  . MET C  1  220 ? -22.330 21.700  17.040 1.00 70.87  ? 233 MET C SD  1 
ATOM   6933 C  CE  . MET C  1  220 ? -21.650 21.490  15.388 1.00 76.16  ? 233 MET C CE  1 
ATOM   6934 N  N   . GLU C  1  221 ? -25.739 17.307  15.764 1.00 59.66  ? 234 GLU C N   1 
ATOM   6935 C  CA  . GLU C  1  221 ? -26.388 16.031  16.046 1.00 71.17  ? 234 GLU C CA  1 
ATOM   6936 C  C   . GLU C  1  221 ? -25.391 14.900  15.800 1.00 68.15  ? 234 GLU C C   1 
ATOM   6937 O  O   . GLU C  1  221 ? -25.293 13.970  16.598 1.00 67.24  ? 234 GLU C O   1 
ATOM   6938 C  CB  . GLU C  1  221 ? -27.656 15.826  15.206 1.00 82.63  ? 234 GLU C CB  1 
ATOM   6939 C  CG  . GLU C  1  221 ? -28.773 16.840  15.470 1.00 88.29  ? 234 GLU C CG  1 
ATOM   6940 C  CD  . GLU C  1  221 ? -28.615 18.306  15.031 1.00 92.57  ? 234 GLU C CD  1 
ATOM   6941 O  OE1 . GLU C  1  221 ? -27.713 18.679  14.236 1.00 78.27  ? 234 GLU C OE1 1 
ATOM   6942 O  OE2 . GLU C  1  221 ? -29.392 19.119  15.569 1.00 93.01  ? 234 GLU C OE2 1 
ATOM   6943 N  N   . ASP C  1  222 ? -24.648 15.006  14.688 1.00 66.91  ? 235 ASP C N   1 
ATOM   6944 C  CA  . ASP C  1  222 ? -23.649 14.020  14.300 1.00 66.50  ? 235 ASP C CA  1 
ATOM   6945 C  C   . ASP C  1  222 ? -22.437 14.096  15.229 1.00 53.79  ? 235 ASP C C   1 
ATOM   6946 O  O   . ASP C  1  222 ? -21.916 13.066  15.643 1.00 47.78  ? 235 ASP C O   1 
ATOM   6947 C  CB  . ASP C  1  222 ? -23.256 14.168  12.836 1.00 67.92  ? 235 ASP C CB  1 
ATOM   6948 C  CG  . ASP C  1  222 ? -24.324 13.807  11.811 1.00 64.25  ? 235 ASP C CG  1 
ATOM   6949 O  OD1 . ASP C  1  222 ? -25.348 13.211  12.213 1.00 62.94  ? 235 ASP C OD1 1 
ATOM   6950 O  OD2 . ASP C  1  222 ? -24.140 14.174  10.627 1.00 60.39  ? 235 ASP C OD2 1 
ATOM   6951 N  N   . ALA C  1  223 ? -21.999 15.313  15.559 1.00 46.41  ? 236 ALA C N   1 
ATOM   6952 C  CA  . ALA C  1  223 ? -20.945 15.493  16.546 1.00 47.84  ? 236 ALA C CA  1 
ATOM   6953 C  C   . ALA C  1  223 ? -21.299 14.796  17.866 1.00 52.43  ? 236 ALA C C   1 
ATOM   6954 O  O   . ALA C  1  223 ? -20.494 14.040  18.402 1.00 54.57  ? 236 ALA C O   1 
ATOM   6955 C  CB  . ALA C  1  223 ? -20.645 16.966  16.749 1.00 42.94  ? 236 ALA C CB  1 
ATOM   6956 N  N   . ALA C  1  224 ? -22.507 15.027  18.389 1.00 56.50  ? 237 ALA C N   1 
ATOM   6957 C  CA  . ALA C  1  224 ? -22.891 14.419  19.654 1.00 56.23  ? 237 ALA C CA  1 
ATOM   6958 C  C   . ALA C  1  224 ? -22.901 12.895  19.535 1.00 53.72  ? 237 ALA C C   1 
ATOM   6959 O  O   . ALA C  1  224 ? -22.482 12.178  20.444 1.00 58.22  ? 237 ALA C O   1 
ATOM   6960 C  CB  . ALA C  1  224 ? -24.236 14.944  20.093 1.00 60.93  ? 237 ALA C CB  1 
ATOM   6961 N  N   . SER C  1  225 ? -23.391 12.401  18.398 1.00 52.25  ? 238 SER C N   1 
ATOM   6962 C  CA  . SER C  1  225 ? -23.538 10.968  18.215 1.00 53.69  ? 238 SER C CA  1 
ATOM   6963 C  C   . SER C  1  225 ? -22.180 10.275  18.349 1.00 53.57  ? 238 SER C C   1 
ATOM   6964 O  O   . SER C  1  225 ? -22.068 9.237   18.997 1.00 46.08  ? 238 SER C O   1 
ATOM   6965 C  CB  . SER C  1  225 ? -24.197 10.661  16.897 1.00 50.86  ? 238 SER C CB  1 
ATOM   6966 O  OG  . SER C  1  225 ? -24.361 9.258   16.736 1.00 48.58  ? 238 SER C OG  1 
ATOM   6967 N  N   . ILE C  1  226 ? -21.144 10.873  17.752 1.00 52.38  ? 239 ILE C N   1 
ATOM   6968 C  CA  . ILE C  1  226 ? -19.823 10.271  17.709 1.00 50.39  ? 239 ILE C CA  1 
ATOM   6969 C  C   . ILE C  1  226 ? -19.081 10.572  19.010 1.00 46.47  ? 239 ILE C C   1 
ATOM   6970 O  O   . ILE C  1  226 ? -18.628 9.640   19.684 1.00 45.79  ? 239 ILE C O   1 
ATOM   6971 C  CB  . ILE C  1  226 ? -19.061 10.751  16.458 1.00 53.03  ? 239 ILE C CB  1 
ATOM   6972 C  CG1 . ILE C  1  226 ? -19.661 10.166  15.193 1.00 53.89  ? 239 ILE C CG1 1 
ATOM   6973 C  CG2 . ILE C  1  226 ? -17.575 10.418  16.542 1.00 54.60  ? 239 ILE C CG2 1 
ATOM   6974 C  CD1 . ILE C  1  226 ? -19.409 11.010  13.964 1.00 53.03  ? 239 ILE C CD1 1 
ATOM   6975 N  N   . PHE C  1  227 ? -18.960 11.862  19.353 1.00 43.29  ? 240 PHE C N   1 
ATOM   6976 C  CA  . PHE C  1  227 ? -18.139 12.287  20.478 1.00 47.98  ? 240 PHE C CA  1 
ATOM   6977 C  C   . PHE C  1  227 ? -18.673 11.774  21.814 1.00 51.74  ? 240 PHE C C   1 
ATOM   6978 O  O   . PHE C  1  227 ? -17.886 11.430  22.697 1.00 50.48  ? 240 PHE C O   1 
ATOM   6979 C  CB  . PHE C  1  227 ? -18.051 13.808  20.585 1.00 46.58  ? 240 PHE C CB  1 
ATOM   6980 C  CG  . PHE C  1  227 ? -17.056 14.445  19.634 1.00 47.98  ? 240 PHE C CG  1 
ATOM   6981 C  CD1 . PHE C  1  227 ? -15.693 14.389  19.894 1.00 48.66  ? 240 PHE C CD1 1 
ATOM   6982 C  CD2 . PHE C  1  227 ? -17.488 15.158  18.528 1.00 55.39  ? 240 PHE C CD2 1 
ATOM   6983 C  CE1 . PHE C  1  227 ? -14.794 15.018  19.057 1.00 51.02  ? 240 PHE C CE1 1 
ATOM   6984 C  CE2 . PHE C  1  227 ? -16.579 15.786  17.690 1.00 57.50  ? 240 PHE C CE2 1 
ATOM   6985 C  CZ  . PHE C  1  227 ? -15.241 15.737  17.971 1.00 52.98  ? 240 PHE C CZ  1 
ATOM   6986 N  N   . ARG C  1  228 ? -20.003 11.744  21.975 1.00 53.21  ? 241 ARG C N   1 
ATOM   6987 C  CA  . ARG C  1  228 ? -20.588 11.325  23.234 1.00 54.89  ? 241 ARG C CA  1 
ATOM   6988 C  C   . ARG C  1  228 ? -21.000 9.856   23.194 1.00 50.79  ? 241 ARG C C   1 
ATOM   6989 O  O   . ARG C  1  228 ? -20.671 9.111   24.106 1.00 59.05  ? 241 ARG C O   1 
ATOM   6990 C  CB  . ARG C  1  228 ? -21.791 12.188  23.629 1.00 64.64  ? 241 ARG C CB  1 
ATOM   6991 C  CG  . ARG C  1  228 ? -22.436 11.752  24.939 1.00 67.54  ? 241 ARG C CG  1 
ATOM   6992 C  CD  . ARG C  1  228 ? -23.630 12.635  25.280 1.00 71.65  ? 241 ARG C CD  1 
ATOM   6993 N  NE  . ARG C  1  228 ? -24.779 12.140  24.511 1.00 72.25  ? 241 ARG C NE  1 
ATOM   6994 C  CZ  . ARG C  1  228 ? -25.591 12.841  23.715 1.00 73.89  ? 241 ARG C CZ  1 
ATOM   6995 N  NH1 . ARG C  1  228 ? -25.487 14.158  23.631 1.00 66.59  ? 241 ARG C NH1 1 
ATOM   6996 N  NH2 . ARG C  1  228 ? -26.521 12.209  23.017 1.00 74.43  ? 241 ARG C NH2 1 
ATOM   6997 N  N   . ASP C  1  229 ? -21.746 9.439   22.169 1.00 47.07  ? 242 ASP C N   1 
ATOM   6998 C  CA  . ASP C  1  229 ? -22.450 8.169   22.232 1.00 52.01  ? 242 ASP C CA  1 
ATOM   6999 C  C   . ASP C  1  229 ? -21.716 7.040   21.520 1.00 49.46  ? 242 ASP C C   1 
ATOM   7000 O  O   . ASP C  1  229 ? -22.158 5.898   21.618 1.00 41.54  ? 242 ASP C O   1 
ATOM   7001 C  CB  . ASP C  1  229 ? -23.880 8.307   21.734 1.00 65.25  ? 242 ASP C CB  1 
ATOM   7002 C  CG  . ASP C  1  229 ? -24.805 9.089   22.665 1.00 77.98  ? 242 ASP C CG  1 
ATOM   7003 O  OD1 . ASP C  1  229 ? -24.664 8.923   23.898 1.00 86.15  ? 242 ASP C OD1 1 
ATOM   7004 O  OD2 . ASP C  1  229 ? -25.659 9.866   22.167 1.00 87.45  ? 242 ASP C OD2 1 
ATOM   7005 N  N   . MET C  1  230 ? -20.623 7.371   20.804 1.00 50.78  ? 243 MET C N   1 
ATOM   7006 C  CA  A MET C  1  230 ? -19.777 6.385   20.145 0.50 47.24  ? 243 MET C CA  1 
ATOM   7007 C  CA  B MET C  1  230 ? -19.776 6.387   20.144 0.50 49.72  ? 243 MET C CA  1 
ATOM   7008 C  C   . MET C  1  230 ? -20.563 5.690   19.037 1.00 47.22  ? 243 MET C C   1 
ATOM   7009 O  O   . MET C  1  230 ? -20.433 4.480   18.853 1.00 45.94  ? 243 MET C O   1 
ATOM   7010 C  CB  A MET C  1  230 ? -19.278 5.318   21.131 0.50 46.93  ? 243 MET C CB  1 
ATOM   7011 C  CB  B MET C  1  230 ? -19.264 5.322   21.127 0.50 53.26  ? 243 MET C CB  1 
ATOM   7012 C  CG  A MET C  1  230 ? -18.562 5.876   22.345 0.50 46.21  ? 243 MET C CG  1 
ATOM   7013 C  CG  B MET C  1  230 ? -18.448 5.866   22.288 0.50 56.60  ? 243 MET C CG  1 
ATOM   7014 S  SD  A MET C  1  230 ? -18.382 4.656   23.659 0.50 44.23  ? 243 MET C SD  1 
ATOM   7015 S  SD  B MET C  1  230 ? -17.873 4.575   23.411 0.50 60.06  ? 243 MET C SD  1 
ATOM   7016 C  CE  A MET C  1  230 ? -17.708 5.686   24.968 0.50 42.41  ? 243 MET C CE  1 
ATOM   7017 C  CE  B MET C  1  230 ? -19.428 4.147   24.196 0.50 65.79  ? 243 MET C CE  1 
ATOM   7018 N  N   . ARG C  1  231 ? -21.367 6.463   18.297 1.00 49.67  ? 244 ARG C N   1 
ATOM   7019 C  CA  . ARG C  1  231 ? -22.297 5.907   17.328 1.00 53.12  ? 244 ARG C CA  1 
ATOM   7020 C  C   . ARG C  1  231 ? -22.170 6.650   16.007 1.00 47.21  ? 244 ARG C C   1 
ATOM   7021 O  O   . ARG C  1  231 ? -22.187 7.885   15.976 1.00 40.03  ? 244 ARG C O   1 
ATOM   7022 C  CB  . ARG C  1  231 ? -23.719 6.079   17.876 1.00 58.57  ? 244 ARG C CB  1 
ATOM   7023 C  CG  . ARG C  1  231 ? -24.816 5.305   17.167 1.00 59.57  ? 244 ARG C CG  1 
ATOM   7024 C  CD  . ARG C  1  231 ? -26.144 5.722   17.782 1.00 63.01  ? 244 ARG C CD  1 
ATOM   7025 N  NE  . ARG C  1  231 ? -27.112 4.649   17.535 1.00 73.98  ? 244 ARG C NE  1 
ATOM   7026 C  CZ  . ARG C  1  231 ? -27.677 3.863   18.448 1.00 80.01  ? 244 ARG C CZ  1 
ATOM   7027 N  NH1 . ARG C  1  231 ? -27.471 4.092   19.748 1.00 79.73  ? 244 ARG C NH1 1 
ATOM   7028 N  NH2 . ARG C  1  231 ? -28.460 2.858   18.043 1.00 65.22  ? 244 ARG C NH2 1 
ATOM   7029 N  N   . PHE C  1  232 ? -22.053 5.886   14.916 1.00 46.14  ? 245 PHE C N   1 
ATOM   7030 C  CA  . PHE C  1  232 ? -22.124 6.484   13.592 1.00 43.92  ? 245 PHE C CA  1 
ATOM   7031 C  C   . PHE C  1  232 ? -23.497 7.113   13.387 1.00 44.12  ? 245 PHE C C   1 
ATOM   7032 O  O   . PHE C  1  232 ? -24.511 6.563   13.816 1.00 44.23  ? 245 PHE C O   1 
ATOM   7033 C  CB  . PHE C  1  232 ? -21.955 5.454   12.478 1.00 42.87  ? 245 PHE C CB  1 
ATOM   7034 C  CG  . PHE C  1  232 ? -20.551 4.903   12.295 1.00 40.57  ? 245 PHE C CG  1 
ATOM   7035 C  CD1 . PHE C  1  232 ? -19.516 5.736   11.892 1.00 38.88  ? 245 PHE C CD1 1 
ATOM   7036 C  CD2 . PHE C  1  232 ? -20.288 3.549   12.475 1.00 40.15  ? 245 PHE C CD2 1 
ATOM   7037 C  CE1 . PHE C  1  232 ? -18.247 5.232   11.707 1.00 39.51  ? 245 PHE C CE1 1 
ATOM   7038 C  CE2 . PHE C  1  232 ? -19.016 3.045   12.275 1.00 40.12  ? 245 PHE C CE2 1 
ATOM   7039 C  CZ  . PHE C  1  232 ? -17.999 3.885   11.896 1.00 40.66  ? 245 PHE C CZ  1 
ATOM   7040 N  N   . PRO C  1  233 ? -23.577 8.268   12.703 1.00 45.13  ? 246 PRO C N   1 
ATOM   7041 C  CA  . PRO C  1  233 ? -24.850 8.747   12.165 1.00 48.61  ? 246 PRO C CA  1 
ATOM   7042 C  C   . PRO C  1  233 ? -25.587 7.652   11.403 1.00 49.11  ? 246 PRO C C   1 
ATOM   7043 O  O   . PRO C  1  233 ? -24.960 6.733   10.885 1.00 47.97  ? 246 PRO C O   1 
ATOM   7044 C  CB  . PRO C  1  233 ? -24.439 9.915   11.260 1.00 45.51  ? 246 PRO C CB  1 
ATOM   7045 C  CG  . PRO C  1  233 ? -23.167 10.431  11.897 1.00 45.66  ? 246 PRO C CG  1 
ATOM   7046 C  CD  . PRO C  1  233 ? -22.472 9.206   12.481 1.00 46.18  ? 246 PRO C CD  1 
ATOM   7047 N  N   . ASP C  1  234 ? -26.915 7.760   11.324 1.00 57.67  ? 247 ASP C N   1 
ATOM   7048 C  CA  . ASP C  1  234 ? -27.712 6.840   10.523 1.00 62.06  ? 247 ASP C CA  1 
ATOM   7049 C  C   . ASP C  1  234 ? -27.244 6.927   9.073  1.00 55.55  ? 247 ASP C C   1 
ATOM   7050 O  O   . ASP C  1  234 ? -26.988 8.019   8.554  1.00 46.26  ? 247 ASP C O   1 
ATOM   7051 C  CB  . ASP C  1  234 ? -29.207 7.114   10.673 1.00 67.60  ? 247 ASP C CB  1 
ATOM   7052 C  CG  . ASP C  1  234 ? -29.720 7.106   12.109 1.00 76.08  ? 247 ASP C CG  1 
ATOM   7053 O  OD1 . ASP C  1  234 ? -29.269 6.222   12.861 1.00 89.31  ? 247 ASP C OD1 1 
ATOM   7054 O  OD2 . ASP C  1  234 ? -30.530 7.994   12.475 1.00 78.36  ? 247 ASP C OD2 1 
ATOM   7055 N  N   . ASP C  1  235 ? -27.075 5.755   8.449  1.00 52.82  ? 248 ASP C N   1 
ATOM   7056 C  CA  . ASP C  1  235 ? -26.736 5.690   7.037  1.00 59.67  ? 248 ASP C CA  1 
ATOM   7057 C  C   . ASP C  1  235 ? -25.391 6.373   6.741  1.00 52.58  ? 248 ASP C C   1 
ATOM   7058 O  O   . ASP C  1  235 ? -25.184 6.937   5.670  1.00 50.72  ? 248 ASP C O   1 
ATOM   7059 C  CB  . ASP C  1  235 ? -27.871 6.279   6.209  1.00 59.25  ? 248 ASP C CB  1 
ATOM   7060 C  CG  . ASP C  1  235 ? -27.816 5.925   4.734  1.00 60.19  ? 248 ASP C CG  1 
ATOM   7061 O  OD1 . ASP C  1  235 ? -27.795 4.705   4.451  1.00 53.47  ? 248 ASP C OD1 1 
ATOM   7062 O  OD2 . ASP C  1  235 ? -27.765 6.868   3.903  1.00 55.91  ? 248 ASP C OD2 1 
ATOM   7063 N  N   . PHE C  1  236 ? -24.455 6.310   7.683  1.00 51.98  ? 249 PHE C N   1 
ATOM   7064 C  CA  . PHE C  1  236 ? -23.197 7.019   7.536  1.00 49.33  ? 249 PHE C CA  1 
ATOM   7065 C  C   . PHE C  1  236 ? -22.332 6.354   6.466  1.00 47.66  ? 249 PHE C C   1 
ATOM   7066 O  O   . PHE C  1  236 ? -22.094 5.139   6.495  1.00 39.29  ? 249 PHE C O   1 
ATOM   7067 C  CB  . PHE C  1  236 ? -22.405 7.055   8.840  1.00 45.03  ? 249 PHE C CB  1 
ATOM   7068 C  CG  . PHE C  1  236 ? -21.102 7.822   8.737  1.00 41.47  ? 249 PHE C CG  1 
ATOM   7069 C  CD1 . PHE C  1  236 ? -21.107 9.209   8.685  1.00 42.19  ? 249 PHE C CD1 1 
ATOM   7070 C  CD2 . PHE C  1  236 ? -19.877 7.163   8.728  1.00 42.43  ? 249 PHE C CD2 1 
ATOM   7071 C  CE1 . PHE C  1  236 ? -19.917 9.920   8.622  1.00 43.71  ? 249 PHE C CE1 1 
ATOM   7072 C  CE2 . PHE C  1  236 ? -18.689 7.882   8.651  1.00 41.19  ? 249 PHE C CE2 1 
ATOM   7073 C  CZ  . PHE C  1  236 ? -18.710 9.261   8.587  1.00 40.10  ? 249 PHE C CZ  1 
ATOM   7074 N  N   . HIS C  1  237 ? -21.865 7.194   5.533  1.00 48.64  ? 250 HIS C N   1 
ATOM   7075 C  CA  . HIS C  1  237 ? -20.923 6.793   4.501  1.00 48.69  ? 250 HIS C CA  1 
ATOM   7076 C  C   . HIS C  1  237 ? -19.585 7.468   4.780  1.00 44.06  ? 250 HIS C C   1 
ATOM   7077 O  O   . HIS C  1  237 ? -19.532 8.689   4.944  1.00 37.41  ? 250 HIS C O   1 
ATOM   7078 C  CB  . HIS C  1  237 ? -21.434 7.172   3.107  1.00 52.51  ? 250 HIS C CB  1 
ATOM   7079 C  CG  . HIS C  1  237 ? -22.584 6.347   2.625  1.00 58.38  ? 250 HIS C CG  1 
ATOM   7080 N  ND1 . HIS C  1  237 ? -23.689 6.080   3.397  1.00 59.71  ? 250 HIS C ND1 1 
ATOM   7081 C  CD2 . HIS C  1  237 ? -22.800 5.745   1.451  1.00 57.17  ? 250 HIS C CD2 1 
ATOM   7082 C  CE1 . HIS C  1  237 ? -24.528 5.330   2.704  1.00 61.83  ? 250 HIS C CE1 1 
ATOM   7083 N  NE2 . HIS C  1  237 ? -24.000 5.108   1.522  1.00 55.54  ? 250 HIS C NE2 1 
ATOM   7084 N  N   . ARG C  1  238 ? -18.511 6.665   4.815  1.00 41.97  ? 251 ARG C N   1 
ATOM   7085 C  CA  . ARG C  1  238 ? -17.176 7.176   5.092  1.00 41.66  ? 251 ARG C CA  1 
ATOM   7086 C  C   . ARG C  1  238 ? -16.686 8.076   3.962  1.00 40.31  ? 251 ARG C C   1 
ATOM   7087 O  O   . ARG C  1  238 ? -17.242 8.061   2.863  1.00 45.77  ? 251 ARG C O   1 
ATOM   7088 C  CB  . ARG C  1  238 ? -16.181 6.027   5.267  1.00 42.10  ? 251 ARG C CB  1 
ATOM   7089 C  CG  . ARG C  1  238 ? -15.898 5.298   3.961  1.00 42.45  ? 251 ARG C CG  1 
ATOM   7090 C  CD  . ARG C  1  238 ? -14.972 4.104   4.129  1.00 41.51  ? 251 ARG C CD  1 
ATOM   7091 N  NE  . ARG C  1  238 ? -14.478 3.708   2.811  1.00 42.98  ? 251 ARG C NE  1 
ATOM   7092 C  CZ  . ARG C  1  238 ? -13.784 2.618   2.536  1.00 42.32  ? 251 ARG C CZ  1 
ATOM   7093 N  NH1 . ARG C  1  238 ? -13.418 1.790   3.509  1.00 37.64  ? 251 ARG C NH1 1 
ATOM   7094 N  NH2 . ARG C  1  238 ? -13.480 2.359   1.262  1.00 40.48  ? 251 ARG C NH2 1 
ATOM   7095 N  N   . SER C  1  239 ? -15.608 8.816   4.258  1.00 41.74  ? 252 SER C N   1 
ATOM   7096 C  CA  . SER C  1  239 ? -14.912 9.677   3.313  1.00 41.79  ? 252 SER C CA  1 
ATOM   7097 C  C   . SER C  1  239 ? -14.663 8.950   1.992  1.00 42.56  ? 252 SER C C   1 
ATOM   7098 O  O   . SER C  1  239 ? -14.385 7.753   1.988  1.00 40.41  ? 252 SER C O   1 
ATOM   7099 C  CB  . SER C  1  239 ? -13.619 10.171  3.906  1.00 40.93  ? 252 SER C CB  1 
ATOM   7100 O  OG  . SER C  1  239 ? -12.853 10.914  2.965  1.00 43.82  ? 252 SER C OG  1 
ATOM   7101 N  N   . ALA C  1  240 ? -14.766 9.686   0.873  1.00 41.10  ? 253 ALA C N   1 
ATOM   7102 C  CA  . ALA C  1  240 ? -14.662 9.084   -0.446 1.00 44.04  ? 253 ALA C CA  1 
ATOM   7103 C  C   . ALA C  1  240 ? -13.201 8.858   -0.832 1.00 41.82  ? 253 ALA C C   1 
ATOM   7104 O  O   . ALA C  1  240 ? -12.930 8.172   -1.807 1.00 44.00  ? 253 ALA C O   1 
ATOM   7105 C  CB  . ALA C  1  240 ? -15.342 9.969   -1.460 1.00 43.96  ? 253 ALA C CB  1 
ATOM   7106 N  N   . VAL C  1  241 ? -12.291 9.494   -0.096 1.00 39.76  ? 254 VAL C N   1 
ATOM   7107 C  CA  . VAL C  1  241 ? -10.860 9.322   -0.282 1.00 46.01  ? 254 VAL C CA  1 
ATOM   7108 C  C   . VAL C  1  241 ? -10.224 9.057   1.073  1.00 42.96  ? 254 VAL C C   1 
ATOM   7109 O  O   . VAL C  1  241 ? -10.712 9.536   2.089  1.00 42.80  ? 254 VAL C O   1 
ATOM   7110 C  CB  . VAL C  1  241 ? -10.198 10.548  -0.936 1.00 49.26  ? 254 VAL C CB  1 
ATOM   7111 C  CG1 . VAL C  1  241 ? -10.731 10.768  -2.338 1.00 61.30  ? 254 VAL C CG1 1 
ATOM   7112 C  CG2 . VAL C  1  241 ? -10.365 11.806  -0.091 1.00 48.69  ? 254 VAL C CG2 1 
ATOM   7113 N  N   . PRO C  1  242 ? -9.091  8.328   1.122  1.00 40.14  ? 255 PRO C N   1 
ATOM   7114 C  CA  . PRO C  1  242 ? -8.314  8.218   2.348  1.00 37.90  ? 255 PRO C CA  1 
ATOM   7115 C  C   . PRO C  1  242 ? -7.981  9.627   2.815  1.00 36.84  ? 255 PRO C C   1 
ATOM   7116 O  O   . PRO C  1  242 ? -7.604  10.477  2.007  1.00 32.70  ? 255 PRO C O   1 
ATOM   7117 C  CB  . PRO C  1  242 ? -7.079  7.432   1.913  1.00 38.11  ? 255 PRO C CB  1 
ATOM   7118 C  CG  . PRO C  1  242 ? -7.555  6.632   0.753  1.00 39.59  ? 255 PRO C CG  1 
ATOM   7119 C  CD  . PRO C  1  242 ? -8.486  7.582   0.012  1.00 40.89  ? 255 PRO C CD  1 
ATOM   7120 N  N   . ALA C  1  243 ? -8.141  9.875   4.118  1.00 38.38  ? 256 ALA C N   1 
ATOM   7121 C  CA  . ALA C  1  243 ? -7.895  11.211  4.625  1.00 41.13  ? 256 ALA C CA  1 
ATOM   7122 C  C   . ALA C  1  243 ? -7.328  11.148  6.032  1.00 38.34  ? 256 ALA C C   1 
ATOM   7123 O  O   . ALA C  1  243 ? -7.319  10.095  6.661  1.00 35.37  ? 256 ALA C O   1 
ATOM   7124 C  CB  . ALA C  1  243 ? -9.163  12.042  4.572  1.00 42.13  ? 256 ALA C CB  1 
ATOM   7125 N  N   . SER C  1  244 ? -6.863  12.317  6.477  1.00 39.16  ? 257 SER C N   1 
ATOM   7126 C  CA  . SER C  1  244 ? -6.408  12.496  7.840  1.00 39.88  ? 257 SER C CA  1 
ATOM   7127 C  C   . SER C  1  244 ? -6.478  13.981  8.190  1.00 39.86  ? 257 SER C C   1 
ATOM   7128 O  O   . SER C  1  244 ? -7.557  14.488  8.471  1.00 38.54  ? 257 SER C O   1 
ATOM   7129 C  CB  . SER C  1  244 ? -5.027  11.924  8.020  1.00 39.83  ? 257 SER C CB  1 
ATOM   7130 O  OG  . SER C  1  244 ? -4.160  12.459  7.030  1.00 37.03  ? 257 SER C OG  1 
ATOM   7131 N  N   . ASN C  1  245 ? -5.342  14.683  8.090  1.00 42.42  ? 258 ASN C N   1 
ATOM   7132 C  CA  . ASN C  1  245 ? -5.169  15.965  8.752  1.00 42.28  ? 258 ASN C CA  1 
ATOM   7133 C  C   . ASN C  1  245 ? -5.089  17.122  7.753  1.00 43.96  ? 258 ASN C C   1 
ATOM   7134 O  O   . ASN C  1  245 ? -4.464  18.136  8.040  1.00 45.72  ? 258 ASN C O   1 
ATOM   7135 C  CB  . ASN C  1  245 ? -3.944  15.937  9.660  1.00 44.06  ? 258 ASN C CB  1 
ATOM   7136 C  CG  . ASN C  1  245 ? -2.645  15.840  8.901  1.00 43.71  ? 258 ASN C CG  1 
ATOM   7137 O  OD1 . ASN C  1  245 ? -2.623  15.398  7.752  1.00 47.80  ? 258 ASN C OD1 1 
ATOM   7138 N  ND2 . ASN C  1  245 ? -1.547  16.207  9.530  1.00 44.37  ? 258 ASN C ND2 1 
ATOM   7139 N  N   . GLU C  1  246 ? -5.756  16.993  6.603  1.00 46.33  ? 259 GLU C N   1 
ATOM   7140 C  CA  . GLU C  1  246 ? -5.850  18.082  5.644  1.00 48.24  ? 259 GLU C CA  1 
ATOM   7141 C  C   . GLU C  1  246 ? -6.524  19.282  6.310  1.00 47.79  ? 259 GLU C C   1 
ATOM   7142 O  O   . GLU C  1  246 ? -7.604  19.149  6.883  1.00 46.30  ? 259 GLU C O   1 
ATOM   7143 C  CB  . GLU C  1  246 ? -6.654  17.661  4.413  1.00 49.48  ? 259 GLU C CB  1 
ATOM   7144 C  CG  . GLU C  1  246 ? -5.982  16.567  3.582  1.00 47.90  ? 259 GLU C CG  1 
ATOM   7145 C  CD  . GLU C  1  246 ? -6.149  15.133  4.068  1.00 50.32  ? 259 GLU C CD  1 
ATOM   7146 O  OE1 . GLU C  1  246 ? -6.765  14.914  5.143  1.00 54.76  ? 259 GLU C OE1 1 
ATOM   7147 O  OE2 . GLU C  1  246 ? -5.661  14.220  3.355  1.00 43.83  ? 259 GLU C OE2 1 
ATOM   7148 N  N   . GLY C  1  247 ? -5.870  20.448  6.243  1.00 48.35  ? 260 GLY C N   1 
ATOM   7149 C  CA  . GLY C  1  247 ? -6.420  21.678  6.791  1.00 50.75  ? 260 GLY C CA  1 
ATOM   7150 C  C   . GLY C  1  247 ? -5.766  22.089  8.112  1.00 54.00  ? 260 GLY C C   1 
ATOM   7151 O  O   . GLY C  1  247 ? -5.985  23.204  8.587  1.00 56.83  ? 260 GLY C O   1 
ATOM   7152 N  N   . ALA C  1  248 ? -4.951  21.205  8.701  1.00 54.96  ? 261 ALA C N   1 
ATOM   7153 C  CA  . ALA C  1  248 ? -4.325  21.487  9.984  1.00 54.99  ? 261 ALA C CA  1 
ATOM   7154 C  C   . ALA C  1  248 ? -3.387  22.696  9.892  1.00 57.40  ? 261 ALA C C   1 
ATOM   7155 O  O   . ALA C  1  248 ? -3.277  23.459  10.848 1.00 57.72  ? 261 ALA C O   1 
ATOM   7156 C  CB  . ALA C  1  248 ? -3.606  20.255  10.488 1.00 54.30  ? 261 ALA C CB  1 
ATOM   7157 N  N   . ASP C  1  249 ? -2.713  22.857  8.746  1.00 63.14  ? 262 ASP C N   1 
ATOM   7158 C  CA  . ASP C  1  249 ? -1.898  24.026  8.435  1.00 68.13  ? 262 ASP C CA  1 
ATOM   7159 C  C   . ASP C  1  249 ? -2.689  25.326  8.630  1.00 66.25  ? 262 ASP C C   1 
ATOM   7160 O  O   . ASP C  1  249 ? -2.186  26.291  9.202  1.00 66.06  ? 262 ASP C O   1 
ATOM   7161 C  CB  . ASP C  1  249 ? -1.302  23.931  7.031  1.00 80.07  ? 262 ASP C CB  1 
ATOM   7162 C  CG  . ASP C  1  249 ? -2.245  23.578  5.876  1.00 91.32  ? 262 ASP C CG  1 
ATOM   7163 O  OD1 . ASP C  1  249 ? -3.446  23.329  6.122  1.00 86.12  ? 262 ASP C OD1 1 
ATOM   7164 O  OD2 . ASP C  1  249 ? -1.773  23.541  4.719  1.00 95.71  ? 262 ASP C OD2 1 
ATOM   7165 N  N   . GLN C  1  250 ? -3.936  25.357  8.146  1.00 69.12  ? 263 GLN C N   1 
ATOM   7166 C  CA  . GLN C  1  250 ? -4.751  26.560  8.191  1.00 66.96  ? 263 GLN C CA  1 
ATOM   7167 C  C   . GLN C  1  250 ? -5.205  26.865  9.612  1.00 61.58  ? 263 GLN C C   1 
ATOM   7168 O  O   . GLN C  1  250 ? -5.353  28.031  9.957  1.00 69.31  ? 263 GLN C O   1 
ATOM   7169 C  CB  . GLN C  1  250 ? -5.977  26.431  7.291  1.00 70.78  ? 263 GLN C CB  1 
ATOM   7170 C  CG  . GLN C  1  250 ? -5.639  26.379  5.808  1.00 72.70  ? 263 GLN C CG  1 
ATOM   7171 C  CD  . GLN C  1  250 ? -6.855  26.448  4.913  1.00 70.13  ? 263 GLN C CD  1 
ATOM   7172 O  OE1 . GLN C  1  250 ? -7.870  27.094  5.202  1.00 70.86  ? 263 GLN C OE1 1 
ATOM   7173 N  NE2 . GLN C  1  250 ? -6.728  25.812  3.765  1.00 71.67  ? 263 GLN C NE2 1 
ATOM   7174 N  N   . VAL C  1  251 ? -5.442  25.825  10.416 1.00 62.07  ? 264 VAL C N   1 
ATOM   7175 C  CA  . VAL C  1  251 ? -5.882  26.000  11.792 1.00 64.51  ? 264 VAL C CA  1 
ATOM   7176 C  C   . VAL C  1  251 ? -4.792  26.706  12.599 1.00 61.42  ? 264 VAL C C   1 
ATOM   7177 O  O   . VAL C  1  251 ? -5.095  27.553  13.438 1.00 65.44  ? 264 VAL C O   1 
ATOM   7178 C  CB  . VAL C  1  251 ? -6.267  24.644  12.417 1.00 68.19  ? 264 VAL C CB  1 
ATOM   7179 C  CG1 . VAL C  1  251 ? -6.531  24.745  13.912 1.00 69.94  ? 264 VAL C CG1 1 
ATOM   7180 C  CG2 . VAL C  1  251 ? -7.490  24.039  11.741 1.00 70.14  ? 264 VAL C CG2 1 
ATOM   7181 N  N   . LEU C  1  252 ? -3.531  26.340  12.349 1.00 62.95  ? 265 LEU C N   1 
ATOM   7182 C  CA  . LEU C  1  252 ? -2.398  26.965  13.013 1.00 64.62  ? 265 LEU C CA  1 
ATOM   7183 C  C   . LEU C  1  252 ? -2.219  28.399  12.518 1.00 69.87  ? 265 LEU C C   1 
ATOM   7184 O  O   . LEU C  1  252 ? -1.866  29.282  13.296 1.00 76.27  ? 265 LEU C O   1 
ATOM   7185 C  CB  . LEU C  1  252 ? -1.130  26.144  12.773 1.00 62.80  ? 265 LEU C CB  1 
ATOM   7186 C  CG  . LEU C  1  252 ? 0.158   26.678  13.408 1.00 59.77  ? 265 LEU C CG  1 
ATOM   7187 C  CD1 . LEU C  1  252 ? 0.076   26.504  14.914 1.00 59.80  ? 265 LEU C CD1 1 
ATOM   7188 C  CD2 . LEU C  1  252 ? 1.395   26.013  12.838 1.00 59.89  ? 265 LEU C CD2 1 
ATOM   7189 N  N   . ALA C  1  253 ? -2.447  28.624  11.219 1.00 77.40  ? 266 ALA C N   1 
ATOM   7190 C  CA  . ALA C  1  253 ? -2.221  29.929  10.617 1.00 73.94  ? 266 ALA C CA  1 
ATOM   7191 C  C   . ALA C  1  253 ? -3.183  30.972  11.200 1.00 71.08  ? 266 ALA C C   1 
ATOM   7192 O  O   . ALA C  1  253 ? -2.816  32.131  11.338 1.00 70.56  ? 266 ALA C O   1 
ATOM   7193 C  CB  . ALA C  1  253 ? -2.347  29.822  9.115  1.00 72.77  ? 266 ALA C CB  1 
ATOM   7194 N  N   . ALA C  1  254 ? -4.400  30.548  11.561 1.00 68.07  ? 267 ALA C N   1 
ATOM   7195 C  CA  . ALA C  1  254 ? -5.431  31.437  12.077 1.00 68.98  ? 267 ALA C CA  1 
ATOM   7196 C  C   . ALA C  1  254 ? -5.024  32.075  13.407 1.00 75.50  ? 267 ALA C C   1 
ATOM   7197 O  O   . ALA C  1  254 ? -5.473  33.176  13.709 1.00 81.08  ? 267 ALA C O   1 
ATOM   7198 C  CB  . ALA C  1  254 ? -6.736  30.681  12.224 1.00 64.06  ? 267 ALA C CB  1 
ATOM   7199 N  N   . HIS C  1  255 ? -4.229  31.365  14.221 1.00 81.04  ? 268 HIS C N   1 
ATOM   7200 C  CA  . HIS C  1  255 ? -3.706  31.896  15.476 1.00 79.89  ? 268 HIS C CA  1 
ATOM   7201 C  C   . HIS C  1  255 ? -2.333  31.285  15.754 1.00 72.83  ? 268 HIS C C   1 
ATOM   7202 O  O   . HIS C  1  255 ? -2.223  30.347  16.546 1.00 74.52  ? 268 HIS C O   1 
ATOM   7203 C  CB  . HIS C  1  255 ? -4.676  31.634  16.638 1.00 85.57  ? 268 HIS C CB  1 
ATOM   7204 C  CG  . HIS C  1  255 ? -5.946  32.411  16.567 1.00 88.93  ? 268 HIS C CG  1 
ATOM   7205 N  ND1 . HIS C  1  255 ? -6.037  33.738  16.927 1.00 88.62  ? 268 HIS C ND1 1 
ATOM   7206 C  CD2 . HIS C  1  255 ? -7.167  32.055  16.147 1.00 92.79  ? 268 HIS C CD2 1 
ATOM   7207 C  CE1 . HIS C  1  255 ? -7.283  34.153  16.742 1.00 90.27  ? 268 HIS C CE1 1 
ATOM   7208 N  NE2 . HIS C  1  255 ? -7.990  33.145  16.277 1.00 91.83  ? 268 HIS C NE2 1 
ATOM   7209 N  N   . PRO C  1  256 ? -1.261  31.781  15.094 1.00 66.58  ? 269 PRO C N   1 
ATOM   7210 C  CA  . PRO C  1  256 ? 0.080   31.204  15.216 1.00 69.69  ? 269 PRO C CA  1 
ATOM   7211 C  C   . PRO C  1  256 ? 0.457   30.965  16.670 1.00 70.72  ? 269 PRO C C   1 
ATOM   7212 O  O   . PRO C  1  256 ? 0.174   31.795  17.528 1.00 75.10  ? 269 PRO C O   1 
ATOM   7213 C  CB  . PRO C  1  256 ? 0.995   32.225  14.540 1.00 68.76  ? 269 PRO C CB  1 
ATOM   7214 C  CG  . PRO C  1  256 ? 0.093   32.863  13.506 1.00 71.70  ? 269 PRO C CG  1 
ATOM   7215 C  CD  . PRO C  1  256 ? -1.292  32.912  14.160 1.00 70.07  ? 269 PRO C CD  1 
ATOM   7216 N  N   . TRP C  1  257 ? 1.065   29.805  16.928 1.00 68.86  ? 270 TRP C N   1 
ATOM   7217 C  CA  . TRP C  1  257 ? 1.334   29.381  18.286 1.00 68.24  ? 270 TRP C CA  1 
ATOM   7218 C  C   . TRP C  1  257 ? 2.585   28.510  18.332 1.00 65.18  ? 270 TRP C C   1 
ATOM   7219 O  O   . TRP C  1  257 ? 2.932   27.824  17.372 1.00 62.92  ? 270 TRP C O   1 
ATOM   7220 C  CB  . TRP C  1  257 ? 0.109   28.671  18.874 1.00 69.14  ? 270 TRP C CB  1 
ATOM   7221 C  CG  . TRP C  1  257 ? 0.218   28.468  20.359 1.00 79.48  ? 270 TRP C CG  1 
ATOM   7222 C  CD1 . TRP C  1  257 ? 0.604   27.327  20.992 1.00 81.08  ? 270 TRP C CD1 1 
ATOM   7223 C  CD2 . TRP C  1  257 ? 0.010   29.456  21.392 1.00 84.46  ? 270 TRP C CD2 1 
ATOM   7224 N  NE1 . TRP C  1  257 ? 0.610   27.518  22.347 1.00 79.07  ? 270 TRP C NE1 1 
ATOM   7225 C  CE2 . TRP C  1  257 ? 0.253   28.811  22.621 1.00 81.09  ? 270 TRP C CE2 1 
ATOM   7226 C  CE3 . TRP C  1  257 ? -0.370  30.804  21.401 1.00 81.37  ? 270 TRP C CE3 1 
ATOM   7227 C  CZ2 . TRP C  1  257 ? 0.138   29.472  23.838 1.00 83.35  ? 270 TRP C CZ2 1 
ATOM   7228 C  CZ3 . TRP C  1  257 ? -0.487  31.455  22.608 1.00 79.83  ? 270 TRP C CZ3 1 
ATOM   7229 C  CH2 . TRP C  1  257 ? -0.233  30.795  23.808 1.00 84.46  ? 270 TRP C CH2 1 
ATOM   7230 N  N   . VAL C  1  258 ? 3.263   28.571  19.476 1.00 67.08  ? 271 VAL C N   1 
ATOM   7231 C  CA  . VAL C  1  258 ? 4.570   27.965  19.623 1.00 67.98  ? 271 VAL C CA  1 
ATOM   7232 C  C   . VAL C  1  258 ? 4.488   26.958  20.766 1.00 62.76  ? 271 VAL C C   1 
ATOM   7233 O  O   . VAL C  1  258 ? 3.887   27.241  21.803 1.00 63.28  ? 271 VAL C O   1 
ATOM   7234 C  CB  . VAL C  1  258 ? 5.610   29.077  19.861 1.00 74.87  ? 271 VAL C CB  1 
ATOM   7235 C  CG1 . VAL C  1  258 ? 6.988   28.540  20.231 1.00 77.25  ? 271 VAL C CG1 1 
ATOM   7236 C  CG2 . VAL C  1  258 ? 5.718   30.003  18.653 1.00 74.46  ? 271 VAL C CG2 1 
ATOM   7237 N  N   . PRO C  1  259 ? 5.058   25.745  20.594 1.00 59.78  ? 272 PRO C N   1 
ATOM   7238 C  CA  . PRO C  1  259 ? 5.028   24.730  21.650 1.00 62.70  ? 272 PRO C CA  1 
ATOM   7239 C  C   . PRO C  1  259 ? 5.630   25.248  22.953 1.00 64.42  ? 272 PRO C C   1 
ATOM   7240 O  O   . PRO C  1  259 ? 6.533   26.080  22.926 1.00 60.68  ? 272 PRO C O   1 
ATOM   7241 C  CB  . PRO C  1  259 ? 5.840   23.552  21.061 1.00 64.77  ? 272 PRO C CB  1 
ATOM   7242 C  CG  . PRO C  1  259 ? 6.595   24.139  19.872 1.00 60.48  ? 272 PRO C CG  1 
ATOM   7243 C  CD  . PRO C  1  259 ? 5.740   25.281  19.375 1.00 60.08  ? 272 PRO C CD  1 
ATOM   7244 N  N   . GLY C  1  260 ? 5.124   24.739  24.081 1.00 59.52  ? 273 GLY C N   1 
ATOM   7245 C  CA  . GLY C  1  260 ? 5.624   25.111  25.393 1.00 59.52  ? 273 GLY C CA  1 
ATOM   7246 C  C   . GLY C  1  260 ? 4.678   24.640  26.497 1.00 63.36  ? 273 GLY C C   1 
ATOM   7247 O  O   . GLY C  1  260 ? 3.975   23.640  26.337 1.00 66.92  ? 273 GLY C O   1 
ATOM   7248 N  N   . GLY C  1  261 ? 4.657   25.378  27.611 1.00 65.67  ? 274 GLY C N   1 
ATOM   7249 C  CA  . GLY C  1  261 ? 3.814   25.026  28.742 1.00 70.45  ? 274 GLY C CA  1 
ATOM   7250 C  C   . GLY C  1  261 ? 3.890   26.067  29.857 1.00 70.46  ? 274 GLY C C   1 
ATOM   7251 O  O   . GLY C  1  261 ? 4.705   26.987  29.806 1.00 68.70  ? 274 GLY C O   1 
ATOM   7252 N  N   . ASN C  1  262 ? 3.004   25.914  30.845 1.00 69.29  ? 275 ASN C N   1 
ATOM   7253 C  CA  . ASN C  1  262 ? 3.061   26.700  32.067 1.00 69.65  ? 275 ASN C CA  1 
ATOM   7254 C  C   . ASN C  1  262 ? 4.261   26.235  32.886 1.00 76.76  ? 275 ASN C C   1 
ATOM   7255 O  O   . ASN C  1  262 ? 4.391   25.041  33.143 1.00 88.87  ? 275 ASN C O   1 
ATOM   7256 C  CB  . ASN C  1  262 ? 1.774   26.563  32.878 1.00 68.47  ? 275 ASN C CB  1 
ATOM   7257 C  CG  . ASN C  1  262 ? 0.673   27.498  32.423 1.00 66.48  ? 275 ASN C CG  1 
ATOM   7258 O  OD1 . ASN C  1  262 ? 0.941   28.502  31.750 1.00 65.92  ? 275 ASN C OD1 1 
ATOM   7259 N  ND2 . ASN C  1  262 ? -0.564  27.207  32.806 1.00 63.62  ? 275 ASN C ND2 1 
ATOM   7260 N  N   . ALA C  1  263 ? 5.118   27.177  33.301 1.00 75.88  ? 276 ALA C N   1 
ATOM   7261 C  CA  . ALA C  1  263 ? 6.302   26.858  34.089 1.00 81.00  ? 276 ALA C CA  1 
ATOM   7262 C  C   . ALA C  1  263 ? 6.017   26.986  35.590 1.00 86.74  ? 276 ALA C C   1 
ATOM   7263 O  O   . ALA C  1  263 ? 5.169   27.777  36.010 1.00 82.32  ? 276 ALA C O   1 
ATOM   7264 C  CB  . ALA C  1  263 ? 7.449   27.745  33.661 1.00 75.05  ? 276 ALA C CB  1 
ATOM   7265 N  N   . ASP C  1  264 ? 6.719   26.160  36.383 1.00 90.12  ? 277 ASP C N   1 
ATOM   7266 C  CA  . ASP C  1  264 ? 6.787   26.281  37.833 1.00 89.93  ? 277 ASP C CA  1 
ATOM   7267 C  C   . ASP C  1  264 ? 5.405   26.200  38.478 1.00 86.77  ? 277 ASP C C   1 
ATOM   7268 O  O   . ASP C  1  264 ? 5.108   26.961  39.396 1.00 94.97  ? 277 ASP C O   1 
ATOM   7269 C  CB  . ASP C  1  264 ? 7.519   27.548  38.248 1.00 92.99  ? 277 ASP C CB  1 
ATOM   7270 C  CG  . ASP C  1  264 ? 8.957   27.643  37.760 1.00 100.50 ? 277 ASP C CG  1 
ATOM   7271 O  OD1 . ASP C  1  264 ? 9.720   26.687  38.022 1.00 106.11 ? 277 ASP C OD1 1 
ATOM   7272 O  OD2 . ASP C  1  264 ? 9.309   28.667  37.127 1.00 100.85 ? 277 ASP C OD2 1 
ATOM   7273 N  N   . ASN C  1  265 ? 4.574   25.271  38.000 1.00 82.39  ? 278 ASN C N   1 
ATOM   7274 C  CA  . ASN C  1  265 ? 3.332   24.915  38.673 1.00 82.58  ? 278 ASN C CA  1 
ATOM   7275 C  C   . ASN C  1  265 ? 2.471   26.161  38.910 1.00 82.76  ? 278 ASN C C   1 
ATOM   7276 O  O   . ASN C  1  265 ? 1.839   26.284  39.955 1.00 78.23  ? 278 ASN C O   1 
ATOM   7277 C  CB  . ASN C  1  265 ? 3.634   24.144  39.954 1.00 79.13  ? 278 ASN C CB  1 
ATOM   7278 C  CG  . ASN C  1  265 ? 2.478   23.291  40.407 1.00 81.22  ? 278 ASN C CG  1 
ATOM   7279 O  OD1 . ASN C  1  265 ? 1.958   22.507  39.613 1.00 88.88  ? 278 ASN C OD1 1 
ATOM   7280 N  ND2 . ASN C  1  265 ? 2.078   23.401  41.665 1.00 81.82  ? 278 ASN C ND2 1 
ATOM   7281 N  N   . GLN C  1  266 ? 2.423   27.066  37.922 1.00 84.41  ? 279 GLN C N   1 
ATOM   7282 C  CA  . GLN C  1  266 ? 1.628   28.280  38.014 1.00 84.49  ? 279 GLN C CA  1 
ATOM   7283 C  C   . GLN C  1  266 ? 0.827   28.516  36.736 1.00 76.92  ? 279 GLN C C   1 
ATOM   7284 O  O   . GLN C  1  266 ? 1.295   28.225  35.644 1.00 78.29  ? 279 GLN C O   1 
ATOM   7285 C  CB  . GLN C  1  266 ? 2.528   29.503  38.149 1.00 96.02  ? 279 GLN C CB  1 
ATOM   7286 C  CG  . GLN C  1  266 ? 3.131   29.717  39.531 1.00 102.36 ? 279 GLN C CG  1 
ATOM   7287 C  CD  . GLN C  1  266 ? 4.133   30.854  39.535 1.00 103.58 ? 279 GLN C CD  1 
ATOM   7288 O  OE1 . GLN C  1  266 ? 4.284   31.596  38.555 1.00 93.34  ? 279 GLN C OE1 1 
ATOM   7289 N  NE2 . GLN C  1  266 ? 4.850   30.993  40.639 1.00 109.10 ? 279 GLN C NE2 1 
ATOM   7290 N  N   . VAL C  1  267 ? -0.349  29.131  36.875 1.00 73.20  ? 280 VAL C N   1 
ATOM   7291 C  CA  . VAL C  1  267 ? -1.182  29.492  35.738 1.00 73.45  ? 280 VAL C CA  1 
ATOM   7292 C  C   . VAL C  1  267 ? -0.676  30.788  35.095 1.00 73.11  ? 280 VAL C C   1 
ATOM   7293 O  O   . VAL C  1  267 ? 0.247   31.417  35.589 1.00 73.45  ? 280 VAL C O   1 
ATOM   7294 C  CB  . VAL C  1  267 ? -2.662  29.590  36.156 1.00 77.28  ? 280 VAL C CB  1 
ATOM   7295 C  CG1 . VAL C  1  267 ? -3.217  28.227  36.562 1.00 77.66  ? 280 VAL C CG1 1 
ATOM   7296 C  CG2 . VAL C  1  267 ? -2.896  30.616  37.263 1.00 81.03  ? 280 VAL C CG2 1 
ATOM   7297 N  N   . ASN C  1  268 ? -1.273  31.139  33.952 1.00 76.56  ? 281 ASN C N   1 
ATOM   7298 C  CA  . ASN C  1  268 ? -0.919  32.298  33.139 1.00 80.69  ? 281 ASN C CA  1 
ATOM   7299 C  C   . ASN C  1  268 ? 0.590   32.525  33.069 1.00 77.32  ? 281 ASN C C   1 
ATOM   7300 O  O   . ASN C  1  268 ? 1.037   33.659  33.139 1.00 83.69  ? 281 ASN C O   1 
ATOM   7301 C  CB  . ASN C  1  268 ? -1.656  33.549  33.602 1.00 83.39  ? 281 ASN C CB  1 
ATOM   7302 C  CG  . ASN C  1  268 ? -3.151  33.398  33.455 1.00 86.89  ? 281 ASN C CG  1 
ATOM   7303 O  OD1 . ASN C  1  268 ? -3.682  33.457  32.341 1.00 91.39  ? 281 ASN C OD1 1 
ATOM   7304 N  ND2 . ASN C  1  268 ? -3.848  33.196  34.558 1.00 87.27  ? 281 ASN C ND2 1 
ATOM   7305 N  N   . ASN C  1  269 ? 1.360   31.461  32.834 1.00 81.22  ? 282 ASN C N   1 
ATOM   7306 C  CA  . ASN C  1  269 ? 2.811   31.524  32.895 1.00 78.84  ? 282 ASN C CA  1 
ATOM   7307 C  C   . ASN C  1  269 ? 3.420   30.682  31.767 1.00 80.94  ? 282 ASN C C   1 
ATOM   7308 O  O   . ASN C  1  269 ? 4.281   29.831  32.003 1.00 81.47  ? 282 ASN C O   1 
ATOM   7309 C  CB  . ASN C  1  269 ? 3.269   31.082  34.281 1.00 74.22  ? 282 ASN C CB  1 
ATOM   7310 C  CG  . ASN C  1  269 ? 4.733   31.359  34.524 1.00 74.15  ? 282 ASN C CG  1 
ATOM   7311 O  OD1 . ASN C  1  269 ? 5.317   32.282  33.940 1.00 71.21  ? 282 ASN C OD1 1 
ATOM   7312 N  ND2 . ASN C  1  269 ? 5.340   30.571  35.393 1.00 72.51  ? 282 ASN C ND2 1 
ATOM   7313 N  N   . TYR C  1  270 ? 2.976   30.929  30.531 1.00 77.68  ? 283 TYR C N   1 
ATOM   7314 C  CA  . TYR C  1  270 ? 3.337   30.072  29.412 1.00 74.93  ? 283 TYR C CA  1 
ATOM   7315 C  C   . TYR C  1  270 ? 4.722   30.459  28.888 1.00 70.70  ? 283 TYR C C   1 
ATOM   7316 O  O   . TYR C  1  270 ? 4.955   31.608  28.537 1.00 64.87  ? 283 TYR C O   1 
ATOM   7317 C  CB  . TYR C  1  270 ? 2.251   30.145  28.333 1.00 78.91  ? 283 TYR C CB  1 
ATOM   7318 C  CG  . TYR C  1  270 ? 2.396   29.132  27.202 1.00 78.90  ? 283 TYR C CG  1 
ATOM   7319 C  CD1 . TYR C  1  270 ? 1.842   27.858  27.294 1.00 79.32  ? 283 TYR C CD1 1 
ATOM   7320 C  CD2 . TYR C  1  270 ? 3.092   29.442  26.038 1.00 76.62  ? 283 TYR C CD2 1 
ATOM   7321 C  CE1 . TYR C  1  270 ? 1.977   26.930  26.272 1.00 74.88  ? 283 TYR C CE1 1 
ATOM   7322 C  CE2 . TYR C  1  270 ? 3.236   28.523  25.011 1.00 77.81  ? 283 TYR C CE2 1 
ATOM   7323 C  CZ  . TYR C  1  270 ? 2.680   27.262  25.128 1.00 73.54  ? 283 TYR C CZ  1 
ATOM   7324 O  OH  . TYR C  1  270 ? 2.821   26.365  24.113 1.00 70.45  ? 283 TYR C OH  1 
ATOM   7325 N  N   . VAL C  1  271 ? 5.620   29.468  28.815 1.00 75.90  ? 284 VAL C N   1 
ATOM   7326 C  CA  . VAL C  1  271 ? 6.984   29.645  28.337 1.00 77.46  ? 284 VAL C CA  1 
ATOM   7327 C  C   . VAL C  1  271 ? 7.188   28.778  27.096 1.00 75.89  ? 284 VAL C C   1 
ATOM   7328 O  O   . VAL C  1  271 ? 6.882   27.591  27.115 1.00 73.65  ? 284 VAL C O   1 
ATOM   7329 C  CB  . VAL C  1  271 ? 8.005   29.242  29.420 1.00 79.66  ? 284 VAL C CB  1 
ATOM   7330 C  CG1 . VAL C  1  271 ? 9.441   29.346  28.914 1.00 77.29  ? 284 VAL C CG1 1 
ATOM   7331 C  CG2 . VAL C  1  271 ? 7.824   30.023  30.716 1.00 81.60  ? 284 VAL C CG2 1 
ATOM   7332 N  N   . GLU C  1  272 ? 7.772   29.372  26.046 1.00 73.90  ? 285 GLU C N   1 
ATOM   7333 C  CA  A GLU C  1  272 ? 8.056   28.666  24.808 0.50 67.49  ? 285 GLU C CA  1 
ATOM   7334 C  CA  B GLU C  1  272 ? 8.083   28.681  24.800 0.50 70.90  ? 285 GLU C CA  1 
ATOM   7335 C  C   . GLU C  1  272 ? 9.150   27.622  25.056 1.00 70.76  ? 285 GLU C C   1 
ATOM   7336 O  O   . GLU C  1  272 ? 10.005  27.803  25.913 1.00 71.31  ? 285 GLU C O   1 
ATOM   7337 C  CB  A GLU C  1  272 ? 8.367   29.691  23.713 0.50 61.37  ? 285 GLU C CB  1 
ATOM   7338 C  CB  B GLU C  1  272 ? 8.609   29.629  23.716 0.50 69.06  ? 285 GLU C CB  1 
ATOM   7339 C  CG  A GLU C  1  272 ? 7.226   30.697  23.514 0.50 55.91  ? 285 GLU C CG  1 
ATOM   7340 C  CG  B GLU C  1  272 ? 9.471   28.946  22.651 0.50 67.63  ? 285 GLU C CG  1 
ATOM   7341 C  CD  A GLU C  1  272 ? 7.364   31.754  22.430 0.50 50.89  ? 285 GLU C CD  1 
ATOM   7342 C  CD  B GLU C  1  272 ? 9.960   29.810  21.499 0.50 66.52  ? 285 GLU C CD  1 
ATOM   7343 O  OE1 A GLU C  1  272 ? 8.374   31.752  21.704 0.50 51.18  ? 285 GLU C OE1 1 
ATOM   7344 O  OE1 B GLU C  1  272 ? 9.457   30.936  21.306 0.50 63.66  ? 285 GLU C OE1 1 
ATOM   7345 O  OE2 A GLU C  1  272 ? 6.439   32.580  22.309 0.50 45.44  ? 285 GLU C OE2 1 
ATOM   7346 O  OE2 B GLU C  1  272 ? 10.874  29.340  20.791 0.50 66.73  ? 285 GLU C OE2 1 
ATOM   7347 N  N   . ASP C  1  273 ? 9.082   26.515  24.301 1.00 71.87  ? 286 ASP C N   1 
ATOM   7348 C  CA  . ASP C  1  273 ? 10.134  25.510  24.271 1.00 68.66  ? 286 ASP C CA  1 
ATOM   7349 C  C   . ASP C  1  273 ? 10.709  25.465  22.860 1.00 71.51  ? 286 ASP C C   1 
ATOM   7350 O  O   . ASP C  1  273 ? 10.061  24.962  21.952 1.00 77.79  ? 286 ASP C O   1 
ATOM   7351 C  CB  . ASP C  1  273 ? 9.647   24.123  24.668 1.00 67.23  ? 286 ASP C CB  1 
ATOM   7352 C  CG  . ASP C  1  273 ? 10.715  23.034  24.619 1.00 71.23  ? 286 ASP C CG  1 
ATOM   7353 O  OD1 . ASP C  1  273 ? 11.845  23.327  24.179 1.00 71.86  ? 286 ASP C OD1 1 
ATOM   7354 O  OD2 . ASP C  1  273 ? 10.436  21.898  25.040 1.00 73.07  ? 286 ASP C OD2 1 
ATOM   7355 N  N   . PRO C  1  274 ? 11.940  25.972  22.621 1.00 79.42  ? 287 PRO C N   1 
ATOM   7356 C  CA  . PRO C  1  274 ? 12.518  25.973  21.271 1.00 75.84  ? 287 PRO C CA  1 
ATOM   7357 C  C   . PRO C  1  274 ? 13.061  24.629  20.775 1.00 68.01  ? 287 PRO C C   1 
ATOM   7358 O  O   . PRO C  1  274 ? 13.387  24.504  19.598 1.00 58.04  ? 287 PRO C O   1 
ATOM   7359 C  CB  . PRO C  1  274 ? 13.621  27.038  21.406 1.00 77.59  ? 287 PRO C CB  1 
ATOM   7360 C  CG  . PRO C  1  274 ? 14.083  26.895  22.841 1.00 81.76  ? 287 PRO C CG  1 
ATOM   7361 C  CD  . PRO C  1  274 ? 12.829  26.571  23.631 1.00 81.55  ? 287 PRO C CD  1 
ATOM   7362 N  N   . ASP C  1  275 ? 13.142  23.626  21.669 1.00 71.30  ? 288 ASP C N   1 
ATOM   7363 C  CA  . ASP C  1  275 ? 13.628  22.283  21.342 1.00 73.24  ? 288 ASP C CA  1 
ATOM   7364 C  C   . ASP C  1  275 ? 12.510  21.323  20.911 1.00 63.89  ? 288 ASP C C   1 
ATOM   7365 O  O   . ASP C  1  275 ? 12.784  20.262  20.363 1.00 56.40  ? 288 ASP C O   1 
ATOM   7366 C  CB  . ASP C  1  275 ? 14.348  21.646  22.521 1.00 76.27  ? 288 ASP C CB  1 
ATOM   7367 C  CG  . ASP C  1  275 ? 15.618  22.353  22.972 1.00 81.10  ? 288 ASP C CG  1 
ATOM   7368 O  OD1 . ASP C  1  275 ? 16.075  23.261  22.248 1.00 75.40  ? 288 ASP C OD1 1 
ATOM   7369 O  OD2 . ASP C  1  275 ? 16.103  22.033  24.069 1.00 86.61  ? 288 ASP C OD2 1 
ATOM   7370 N  N   . SER C  1  276 ? 11.249  21.676  21.171 1.00 62.29  ? 289 SER C N   1 
ATOM   7371 C  CA  . SER C  1  276 ? 10.114  20.841  20.809 1.00 60.37  ? 289 SER C CA  1 
ATOM   7372 C  C   . SER C  1  276 ? 10.010  20.695  19.296 1.00 59.18  ? 289 SER C C   1 
ATOM   7373 O  O   . SER C  1  276 ? 10.431  21.560  18.535 1.00 60.37  ? 289 SER C O   1 
ATOM   7374 C  CB  . SER C  1  276 ? 8.820   21.402  21.360 1.00 62.35  ? 289 SER C CB  1 
ATOM   7375 O  OG  . SER C  1  276 ? 7.682   20.852  20.709 1.00 62.35  ? 289 SER C OG  1 
ATOM   7376 N  N   . ALA C  1  277 ? 9.408   19.583  18.878 1.00 58.80  ? 290 ALA C N   1 
ATOM   7377 C  CA  . ALA C  1  277 ? 8.946   19.422  17.515 1.00 54.82  ? 290 ALA C CA  1 
ATOM   7378 C  C   . ALA C  1  277 ? 7.907   20.488  17.206 1.00 48.85  ? 290 ALA C C   1 
ATOM   7379 O  O   . ALA C  1  277 ? 7.222   20.960  18.104 1.00 47.11  ? 290 ALA C O   1 
ATOM   7380 C  CB  . ALA C  1  277 ? 8.356   18.043  17.340 1.00 53.95  ? 290 ALA C CB  1 
ATOM   7381 N  N   . ASP C  1  278 ? 7.827   20.852  15.925 1.00 52.67  ? 291 ASP C N   1 
ATOM   7382 C  CA  . ASP C  1  278 ? 6.766   21.694  15.393 1.00 59.81  ? 291 ASP C CA  1 
ATOM   7383 C  C   . ASP C  1  278 ? 6.530   21.243  13.953 1.00 55.25  ? 291 ASP C C   1 
ATOM   7384 O  O   . ASP C  1  278 ? 7.038   20.201  13.552 1.00 57.21  ? 291 ASP C O   1 
ATOM   7385 C  CB  . ASP C  1  278 ? 7.082   23.176  15.562 1.00 66.16  ? 291 ASP C CB  1 
ATOM   7386 C  CG  . ASP C  1  278 ? 8.238   23.734  14.734 1.00 72.80  ? 291 ASP C CG  1 
ATOM   7387 O  OD1 . ASP C  1  278 ? 8.618   23.101  13.731 1.00 77.55  ? 291 ASP C OD1 1 
ATOM   7388 O  OD2 . ASP C  1  278 ? 8.763   24.808  15.092 1.00 74.78  ? 291 ASP C OD2 1 
ATOM   7389 N  N   . PHE C  1  279 ? 5.798   22.035  13.169 1.00 50.50  ? 292 PHE C N   1 
ATOM   7390 C  CA  . PHE C  1  279 ? 5.321   21.557  11.883 1.00 55.65  ? 292 PHE C CA  1 
ATOM   7391 C  C   . PHE C  1  279 ? 6.391   21.661  10.794 1.00 60.56  ? 292 PHE C C   1 
ATOM   7392 O  O   . PHE C  1  279 ? 6.229   21.057  9.738  1.00 61.35  ? 292 PHE C O   1 
ATOM   7393 C  CB  . PHE C  1  279 ? 4.014   22.257  11.500 1.00 54.14  ? 292 PHE C CB  1 
ATOM   7394 C  CG  . PHE C  1  279 ? 2.830   21.609  12.197 1.00 55.13  ? 292 PHE C CG  1 
ATOM   7395 C  CD1 . PHE C  1  279 ? 2.330   20.390  11.744 1.00 55.31  ? 292 PHE C CD1 1 
ATOM   7396 C  CD2 . PHE C  1  279 ? 2.266   22.182  13.334 1.00 56.94  ? 292 PHE C CD2 1 
ATOM   7397 C  CE1 . PHE C  1  279 ? 1.273   19.773  12.390 1.00 61.66  ? 292 PHE C CE1 1 
ATOM   7398 C  CE2 . PHE C  1  279 ? 1.203   21.561  13.977 1.00 57.60  ? 292 PHE C CE2 1 
ATOM   7399 C  CZ  . PHE C  1  279 ? 0.708   20.362  13.506 1.00 62.42  ? 292 PHE C CZ  1 
ATOM   7400 N  N   . THR C  1  280 ? 7.483   22.396  11.039 1.00 68.02  ? 293 THR C N   1 
ATOM   7401 C  CA  . THR C  1  280 ? 8.604   22.433  10.106 1.00 66.34  ? 293 THR C CA  1 
ATOM   7402 C  C   . THR C  1  280 ? 9.768   21.604  10.659 1.00 61.08  ? 293 THR C C   1 
ATOM   7403 O  O   . THR C  1  280 ? 10.826  21.566  10.047 1.00 58.38  ? 293 THR C O   1 
ATOM   7404 C  CB  . THR C  1  280 ? 9.022   23.882  9.841  1.00 66.79  ? 293 THR C CB  1 
ATOM   7405 O  OG1 . THR C  1  280 ? 9.471   24.383  11.097 1.00 74.37  ? 293 THR C OG1 1 
ATOM   7406 C  CG2 . THR C  1  280 ? 7.892   24.757  9.322  1.00 63.97  ? 293 THR C CG2 1 
ATOM   7407 N  N   . HIS C  1  281 ? 9.566   20.943  11.813 1.00 56.24  ? 294 HIS C N   1 
ATOM   7408 C  CA  . HIS C  1  281 ? 10.601  20.158  12.468 1.00 54.53  ? 294 HIS C CA  1 
ATOM   7409 C  C   . HIS C  1  281 ? 10.005  18.841  12.983 1.00 49.31  ? 294 HIS C C   1 
ATOM   7410 O  O   . HIS C  1  281 ? 10.136  18.500  14.148 1.00 50.41  ? 294 HIS C O   1 
ATOM   7411 C  CB  . HIS C  1  281 ? 11.311  20.951  13.574 1.00 57.02  ? 294 HIS C CB  1 
ATOM   7412 C  CG  . HIS C  1  281 ? 12.089  22.141  13.118 1.00 66.53  ? 294 HIS C CG  1 
ATOM   7413 N  ND1 . HIS C  1  281 ? 13.421  22.077  12.752 1.00 72.52  ? 294 HIS C ND1 1 
ATOM   7414 C  CD2 . HIS C  1  281 ? 11.725  23.429  13.000 1.00 69.79  ? 294 HIS C CD2 1 
ATOM   7415 C  CE1 . HIS C  1  281 ? 13.835  23.289  12.405 1.00 73.96  ? 294 HIS C CE1 1 
ATOM   7416 N  NE2 . HIS C  1  281 ? 12.821  24.123  12.550 1.00 75.40  ? 294 HIS C NE2 1 
ATOM   7417 N  N   . LEU C  1  282 ? 9.376   18.083  12.089 1.00 46.41  ? 295 LEU C N   1 
ATOM   7418 C  CA  . LEU C  1  282 ? 8.633   16.882  12.442 1.00 49.14  ? 295 LEU C CA  1 
ATOM   7419 C  C   . LEU C  1  282 ? 9.530   15.733  12.899 1.00 49.20  ? 295 LEU C C   1 
ATOM   7420 O  O   . LEU C  1  282 ? 9.104   14.932  13.720 1.00 52.79  ? 295 LEU C O   1 
ATOM   7421 C  CB  . LEU C  1  282 ? 7.755   16.427  11.275 1.00 48.68  ? 295 LEU C CB  1 
ATOM   7422 C  CG  . LEU C  1  282 ? 6.511   17.274  11.016 1.00 46.90  ? 295 LEU C CG  1 
ATOM   7423 C  CD1 . LEU C  1  282 ? 5.837   16.934  9.711  1.00 47.26  ? 295 LEU C CD1 1 
ATOM   7424 C  CD2 . LEU C  1  282 ? 5.579   17.063  12.187 1.00 47.89  ? 295 LEU C CD2 1 
ATOM   7425 N  N   . CYS C  1  283 ? 10.731  15.603  12.340 1.00 48.83  ? 296 CYS C N   1 
ATOM   7426 C  CA  . CYS C  1  283 ? 11.604  14.491  12.683 1.00 54.47  ? 296 CYS C CA  1 
ATOM   7427 C  C   . CYS C  1  283 ? 11.990  14.529  14.161 1.00 48.51  ? 296 CYS C C   1 
ATOM   7428 O  O   . CYS C  1  283 ? 12.352  13.492  14.707 1.00 52.57  ? 296 CYS C O   1 
ATOM   7429 C  CB  . CYS C  1  283 ? 12.849  14.417  11.795 1.00 64.17  ? 296 CYS C CB  1 
ATOM   7430 S  SG  . CYS C  1  283 ? 12.570  13.761  10.117 1.00 78.68  ? 296 CYS C SG  1 
ATOM   7431 N  N   . ARG C  1  284 ? 11.908  15.698  14.809 1.00 44.07  ? 297 ARG C N   1 
ATOM   7432 C  CA  . ARG C  1  284 ? 12.166  15.782  16.240 1.00 46.75  ? 297 ARG C CA  1 
ATOM   7433 C  C   . ARG C  1  284 ? 11.181  14.914  17.022 1.00 41.10  ? 297 ARG C C   1 
ATOM   7434 O  O   . ARG C  1  284 ? 11.531  14.334  18.045 1.00 39.91  ? 297 ARG C O   1 
ATOM   7435 C  CB  . ARG C  1  284 ? 12.072  17.212  16.788 1.00 54.29  ? 297 ARG C CB  1 
ATOM   7436 C  CG  . ARG C  1  284 ? 13.199  18.114  16.314 1.00 61.69  ? 297 ARG C CG  1 
ATOM   7437 C  CD  . ARG C  1  284 ? 13.199  19.432  17.074 1.00 66.97  ? 297 ARG C CD  1 
ATOM   7438 N  NE  . ARG C  1  284 ? 14.035  20.420  16.385 1.00 69.98  ? 297 ARG C NE  1 
ATOM   7439 C  CZ  . ARG C  1  284 ? 14.001  21.730  16.585 1.00 73.37  ? 297 ARG C CZ  1 
ATOM   7440 N  NH1 . ARG C  1  284 ? 13.312  22.236  17.595 1.00 74.43  ? 297 ARG C NH1 1 
ATOM   7441 N  NH2 . ARG C  1  284 ? 14.689  22.518  15.776 1.00 77.33  ? 297 ARG C NH2 1 
ATOM   7442 N  N   . LEU C  1  285 ? 9.938   14.846  16.540 1.00 42.44  ? 298 LEU C N   1 
ATOM   7443 C  CA  . LEU C  1  285 ? 8.910   14.027  17.160 1.00 40.73  ? 298 LEU C CA  1 
ATOM   7444 C  C   . LEU C  1  285 ? 9.367   12.571  17.133 1.00 38.52  ? 298 LEU C C   1 
ATOM   7445 O  O   . LEU C  1  285 ? 9.271   11.888  18.147 1.00 40.18  ? 298 LEU C O   1 
ATOM   7446 C  CB  . LEU C  1  285 ? 7.564   14.236  16.463 1.00 40.13  ? 298 LEU C CB  1 
ATOM   7447 C  CG  . LEU C  1  285 ? 6.336   13.662  17.173 1.00 41.30  ? 298 LEU C CG  1 
ATOM   7448 C  CD1 . LEU C  1  285 ? 5.070   14.317  16.687 1.00 40.07  ? 298 LEU C CD1 1 
ATOM   7449 C  CD2 . LEU C  1  285 ? 6.198   12.150  16.997 1.00 43.67  ? 298 LEU C CD2 1 
ATOM   7450 N  N   . TYR C  1  286 ? 9.896   12.120  15.989 1.00 36.37  ? 299 TYR C N   1 
ATOM   7451 C  CA  . TYR C  1  286 ? 10.392  10.763  15.835 1.00 35.69  ? 299 TYR C CA  1 
ATOM   7452 C  C   . TYR C  1  286 ? 11.465  10.489  16.888 1.00 38.35  ? 299 TYR C C   1 
ATOM   7453 O  O   . TYR C  1  286 ? 11.363  9.511   17.637 1.00 37.03  ? 299 TYR C O   1 
ATOM   7454 C  CB  . TYR C  1  286 ? 10.882  10.519  14.400 1.00 32.54  ? 299 TYR C CB  1 
ATOM   7455 C  CG  . TYR C  1  286 ? 11.530  9.156   14.203 1.00 30.33  ? 299 TYR C CG  1 
ATOM   7456 C  CD1 . TYR C  1  286 ? 10.794  7.985   14.345 1.00 29.39  ? 299 TYR C CD1 1 
ATOM   7457 C  CD2 . TYR C  1  286 ? 12.873  9.035   13.885 1.00 29.08  ? 299 TYR C CD2 1 
ATOM   7458 C  CE1 . TYR C  1  286 ? 11.382  6.739   14.190 1.00 30.50  ? 299 TYR C CE1 1 
ATOM   7459 C  CE2 . TYR C  1  286 ? 13.474  7.795   13.728 1.00 29.77  ? 299 TYR C CE2 1 
ATOM   7460 C  CZ  . TYR C  1  286 ? 12.725  6.639   13.867 1.00 31.49  ? 299 TYR C CZ  1 
ATOM   7461 O  OH  . TYR C  1  286 ? 13.285  5.394   13.723 1.00 33.33  ? 299 TYR C OH  1 
ATOM   7462 N  N   . GLU C  1  287 ? 12.477  11.367  16.952 1.00 42.30  ? 300 GLU C N   1 
ATOM   7463 C  CA  . GLU C  1  287 ? 13.611  11.175  17.848 1.00 45.18  ? 300 GLU C CA  1 
ATOM   7464 C  C   . GLU C  1  287 ? 13.145  11.184  19.305 1.00 40.08  ? 300 GLU C C   1 
ATOM   7465 O  O   . GLU C  1  287 ? 13.533  10.314  20.068 1.00 41.83  ? 300 GLU C O   1 
ATOM   7466 C  CB  . GLU C  1  287 ? 14.687  12.217  17.547 1.00 52.51  ? 300 GLU C CB  1 
ATOM   7467 C  CG  . GLU C  1  287 ? 15.370  12.014  16.196 1.00 63.63  ? 300 GLU C CG  1 
ATOM   7468 C  CD  . GLU C  1  287 ? 15.768  13.258  15.393 1.00 83.22  ? 300 GLU C CD  1 
ATOM   7469 O  OE1 . GLU C  1  287 ? 15.636  14.429  15.840 1.00 86.33  ? 300 GLU C OE1 1 
ATOM   7470 O  OE2 . GLU C  1  287 ? 16.189  13.027  14.236 1.00 93.16  ? 300 GLU C OE2 1 
ATOM   7471 N  N   . PHE C  1  288 ? 12.286  12.138  19.676 1.00 36.71  ? 301 PHE C N   1 
ATOM   7472 C  CA  . PHE C  1  288 ? 11.750  12.226  21.028 1.00 36.22  ? 301 PHE C CA  1 
ATOM   7473 C  C   . PHE C  1  288 ? 11.069  10.917  21.441 1.00 35.96  ? 301 PHE C C   1 
ATOM   7474 O  O   . PHE C  1  288 ? 11.291  10.434  22.542 1.00 39.50  ? 301 PHE C O   1 
ATOM   7475 C  CB  . PHE C  1  288 ? 10.782  13.411  21.092 1.00 38.81  ? 301 PHE C CB  1 
ATOM   7476 C  CG  . PHE C  1  288 ? 10.169  13.615  22.467 1.00 43.27  ? 301 PHE C CG  1 
ATOM   7477 C  CD1 . PHE C  1  288 ? 9.008   12.941  22.835 1.00 46.91  ? 301 PHE C CD1 1 
ATOM   7478 C  CD2 . PHE C  1  288 ? 10.774  14.448  23.398 1.00 47.02  ? 301 PHE C CD2 1 
ATOM   7479 C  CE1 . PHE C  1  288 ? 8.464   13.104  24.101 1.00 48.92  ? 301 PHE C CE1 1 
ATOM   7480 C  CE2 . PHE C  1  288 ? 10.219  14.620  24.661 1.00 49.65  ? 301 PHE C CE2 1 
ATOM   7481 C  CZ  . PHE C  1  288 ? 9.068   13.949  25.011 1.00 49.83  ? 301 PHE C CZ  1 
ATOM   7482 N  N   . VAL C  1  289 ? 10.233  10.341  20.567 1.00 34.76  ? 302 VAL C N   1 
ATOM   7483 C  CA  . VAL C  1  289 ? 9.454   9.161   20.902 1.00 34.00  ? 302 VAL C CA  1 
ATOM   7484 C  C   . VAL C  1  289 ? 10.370  7.948   21.049 1.00 34.14  ? 302 VAL C C   1 
ATOM   7485 O  O   . VAL C  1  289 ? 10.158  7.112   21.933 1.00 37.19  ? 302 VAL C O   1 
ATOM   7486 C  CB  . VAL C  1  289 ? 8.338   8.885   19.871 1.00 37.26  ? 302 VAL C CB  1 
ATOM   7487 C  CG1 . VAL C  1  289 ? 7.714   7.500   20.029 1.00 36.09  ? 302 VAL C CG1 1 
ATOM   7488 C  CG2 . VAL C  1  289 ? 7.242   9.944   19.915 1.00 38.27  ? 302 VAL C CG2 1 
ATOM   7489 N  N   . VAL C  1  290 ? 11.366  7.828   20.165 1.00 33.60  ? 303 VAL C N   1 
ATOM   7490 C  CA  . VAL C  1  290 ? 12.353  6.764   20.287 1.00 36.08  ? 303 VAL C CA  1 
ATOM   7491 C  C   . VAL C  1  290 ? 13.072  6.888   21.634 1.00 36.33  ? 303 VAL C C   1 
ATOM   7492 O  O   . VAL C  1  290 ? 13.279  5.888   22.324 1.00 36.15  ? 303 VAL C O   1 
ATOM   7493 C  CB  . VAL C  1  290 ? 13.339  6.775   19.100 1.00 37.73  ? 303 VAL C CB  1 
ATOM   7494 C  CG1 . VAL C  1  290 ? 14.521  5.843   19.330 1.00 36.25  ? 303 VAL C CG1 1 
ATOM   7495 C  CG2 . VAL C  1  290 ? 12.645  6.403   17.793 1.00 40.18  ? 303 VAL C CG2 1 
ATOM   7496 N  N   . GLY C  1  291 ? 13.427  8.127   22.004 1.00 34.66  ? 304 GLY C N   1 
ATOM   7497 C  CA  . GLY C  1  291 ? 13.935  8.454   23.331 1.00 36.39  ? 304 GLY C CA  1 
ATOM   7498 C  C   . GLY C  1  291 ? 13.037  7.902   24.434 1.00 37.55  ? 304 GLY C C   1 
ATOM   7499 O  O   . GLY C  1  291 ? 13.507  7.193   25.325 1.00 38.05  ? 304 GLY C O   1 
ATOM   7500 N  N   . SER C  1  292 ? 11.732  8.195   24.340 1.00 35.40  ? 305 SER C N   1 
ATOM   7501 C  CA  . SER C  1  292 ? 10.794  7.809   25.384 1.00 33.72  ? 305 SER C CA  1 
ATOM   7502 C  C   . SER C  1  292 ? 10.698  6.290   25.479 1.00 33.85  ? 305 SER C C   1 
ATOM   7503 O  O   . SER C  1  292 ? 10.493  5.754   26.563 1.00 35.31  ? 305 SER C O   1 
ATOM   7504 C  CB  . SER C  1  292 ? 9.435   8.406   25.174 1.00 32.41  ? 305 SER C CB  1 
ATOM   7505 O  OG  . SER C  1  292 ? 9.477   9.806   24.925 1.00 33.09  ? 305 SER C OG  1 
ATOM   7506 N  N   . VAL C  1  293 ? 10.828  5.599   24.343 1.00 31.21  ? 306 VAL C N   1 
ATOM   7507 C  CA  . VAL C  1  293 ? 10.727  4.152   24.350 1.00 31.28  ? 306 VAL C CA  1 
ATOM   7508 C  C   . VAL C  1  293 ? 11.934  3.554   25.077 1.00 34.70  ? 306 VAL C C   1 
ATOM   7509 O  O   . VAL C  1  293 ? 11.800  2.553   25.785 1.00 33.86  ? 306 VAL C O   1 
ATOM   7510 C  CB  . VAL C  1  293 ? 10.559  3.599   22.922 1.00 30.48  ? 306 VAL C CB  1 
ATOM   7511 C  CG1 . VAL C  1  293 ? 10.803  2.094   22.847 1.00 28.56  ? 306 VAL C CG1 1 
ATOM   7512 C  CG2 . VAL C  1  293 ? 9.177   3.929   22.368 1.00 30.73  ? 306 VAL C CG2 1 
ATOM   7513 N  N   . GLN C  1  294 ? 13.108  4.174   24.909 1.00 38.05  ? 307 GLN C N   1 
ATOM   7514 C  CA  . GLN C  1  294 ? 14.313  3.737   25.598 1.00 41.41  ? 307 GLN C CA  1 
ATOM   7515 C  C   . GLN C  1  294 ? 14.137  3.862   27.110 1.00 39.27  ? 307 GLN C C   1 
ATOM   7516 O  O   . GLN C  1  294 ? 14.589  2.980   27.845 1.00 39.52  ? 307 GLN C O   1 
ATOM   7517 C  CB  . GLN C  1  294 ? 15.545  4.493   25.102 1.00 43.77  ? 307 GLN C CB  1 
ATOM   7518 C  CG  . GLN C  1  294 ? 15.939  4.129   23.672 1.00 46.21  ? 307 GLN C CG  1 
ATOM   7519 C  CD  . GLN C  1  294 ? 17.087  4.961   23.124 1.00 44.48  ? 307 GLN C CD  1 
ATOM   7520 O  OE1 . GLN C  1  294 ? 16.943  6.143   22.790 1.00 42.05  ? 307 GLN C OE1 1 
ATOM   7521 N  NE2 . GLN C  1  294 ? 18.255  4.350   23.013 1.00 45.02  ? 307 GLN C NE2 1 
ATOM   7522 N  N   . GLU C  1  295 ? 13.477  4.937   27.575 1.00 42.13  ? 308 GLU C N   1 
ATOM   7523 C  CA  . GLU C  1  295 ? 13.235  5.129   29.001 1.00 43.79  ? 308 GLU C CA  1 
ATOM   7524 C  C   . GLU C  1  295 ? 12.329  4.028   29.547 1.00 41.40  ? 308 GLU C C   1 
ATOM   7525 O  O   . GLU C  1  295 ? 12.584  3.559   30.656 1.00 45.67  ? 308 GLU C O   1 
ATOM   7526 C  CB  . GLU C  1  295 ? 12.645  6.489   29.365 1.00 48.89  ? 308 GLU C CB  1 
ATOM   7527 C  CG  . GLU C  1  295 ? 13.557  7.673   29.047 1.00 58.51  ? 308 GLU C CG  1 
ATOM   7528 C  CD  . GLU C  1  295 ? 12.908  9.054   29.201 1.00 71.39  ? 308 GLU C CD  1 
ATOM   7529 O  OE1 . GLU C  1  295 ? 11.682  9.123   29.455 1.00 76.47  ? 308 GLU C OE1 1 
ATOM   7530 O  OE2 . GLU C  1  295 ? 13.614  10.085  29.064 1.00 77.02  ? 308 GLU C OE2 1 
ATOM   7531 N  N   . LEU C  1  296 ? 11.318  3.598   28.766 1.00 34.63  ? 309 LEU C N   1 
ATOM   7532 C  CA  . LEU C  1  296 ? 10.399  2.549   29.189 1.00 33.84  ? 309 LEU C CA  1 
ATOM   7533 C  C   . LEU C  1  296 ? 11.080  1.178   29.149 1.00 34.42  ? 309 LEU C C   1 
ATOM   7534 O  O   . LEU C  1  296 ? 10.771  0.309   29.969 1.00 34.70  ? 309 LEU C O   1 
ATOM   7535 C  CB  . LEU C  1  296 ? 9.148   2.501   28.315 1.00 36.51  ? 309 LEU C CB  1 
ATOM   7536 C  CG  . LEU C  1  296 ? 8.247   3.738   28.268 1.00 38.99  ? 309 LEU C CG  1 
ATOM   7537 C  CD1 . LEU C  1  296 ? 7.197   3.497   27.212 1.00 40.97  ? 309 LEU C CD1 1 
ATOM   7538 C  CD2 . LEU C  1  296 ? 7.575   4.099   29.572 1.00 39.43  ? 309 LEU C CD2 1 
ATOM   7539 N  N   . TYR C  1  297 ? 11.941  0.963   28.146 1.00 34.41  ? 310 TYR C N   1 
ATOM   7540 C  CA  . TYR C  1  297 ? 12.585  -0.326  27.924 1.00 34.89  ? 310 TYR C CA  1 
ATOM   7541 C  C   . TYR C  1  297 ? 14.102  -0.147  27.882 1.00 35.81  ? 310 TYR C C   1 
ATOM   7542 O  O   . TYR C  1  297 ? 14.713  -0.114  26.815 1.00 37.55  ? 310 TYR C O   1 
ATOM   7543 C  CB  . TYR C  1  297 ? 12.037  -0.922  26.625 1.00 33.90  ? 310 TYR C CB  1 
ATOM   7544 C  CG  . TYR C  1  297 ? 10.550  -1.226  26.672 1.00 32.21  ? 310 TYR C CG  1 
ATOM   7545 C  CD1 . TYR C  1  297 ? 10.076  -2.378  27.274 1.00 32.18  ? 310 TYR C CD1 1 
ATOM   7546 C  CD2 . TYR C  1  297 ? 9.626   -0.381  26.075 1.00 35.83  ? 310 TYR C CD2 1 
ATOM   7547 C  CE1 . TYR C  1  297 ? 8.721   -2.669  27.326 1.00 34.07  ? 310 TYR C CE1 1 
ATOM   7548 C  CE2 . TYR C  1  297 ? 8.266   -0.662  26.095 1.00 35.87  ? 310 TYR C CE2 1 
ATOM   7549 C  CZ  . TYR C  1  297 ? 7.811   -1.804  26.737 1.00 35.27  ? 310 TYR C CZ  1 
ATOM   7550 O  OH  . TYR C  1  297 ? 6.481   -2.108  26.782 1.00 33.32  ? 310 TYR C OH  1 
ATOM   7551 N  N   . PRO C  1  298 ? 14.756  0.035   29.046 1.00 39.62  ? 311 PRO C N   1 
ATOM   7552 C  CA  . PRO C  1  298 ? 16.173  0.393   29.079 1.00 38.36  ? 311 PRO C CA  1 
ATOM   7553 C  C   . PRO C  1  298 ? 17.148  -0.694  28.646 1.00 34.24  ? 311 PRO C C   1 
ATOM   7554 O  O   . PRO C  1  298 ? 18.213  -0.340  28.164 1.00 32.29  ? 311 PRO C O   1 
ATOM   7555 C  CB  . PRO C  1  298 ? 16.399  0.847   30.534 1.00 38.96  ? 311 PRO C CB  1 
ATOM   7556 C  CG  . PRO C  1  298 ? 15.323  0.153   31.315 1.00 40.94  ? 311 PRO C CG  1 
ATOM   7557 C  CD  . PRO C  1  298 ? 14.149  0.001   30.378 1.00 39.34  ? 311 PRO C CD  1 
ATOM   7558 N  N   . ASN C  1  299 ? 16.790  -1.978  28.799 1.00 35.83  ? 312 ASN C N   1 
ATOM   7559 C  CA  . ASN C  1  299 ? 17.712  -3.054  28.455 1.00 33.61  ? 312 ASN C CA  1 
ATOM   7560 C  C   . ASN C  1  299 ? 16.979  -4.376  28.202 1.00 33.19  ? 312 ASN C C   1 
ATOM   7561 O  O   . ASN C  1  299 ? 17.250  -5.387  28.835 1.00 37.86  ? 312 ASN C O   1 
ATOM   7562 C  CB  . ASN C  1  299 ? 18.787  -3.209  29.531 1.00 36.97  ? 312 ASN C CB  1 
ATOM   7563 C  CG  . ASN C  1  299 ? 19.892  -4.163  29.133 1.00 37.26  ? 312 ASN C CG  1 
ATOM   7564 O  OD1 . ASN C  1  299 ? 20.207  -5.087  29.878 1.00 36.18  ? 312 ASN C OD1 1 
ATOM   7565 N  ND2 . ASN C  1  299 ? 20.517  -3.958  27.985 1.00 40.73  ? 312 ASN C ND2 1 
ATOM   7566 N  N   . PRO C  1  300 ? 16.085  -4.456  27.200 1.00 35.47  ? 313 PRO C N   1 
ATOM   7567 C  CA  . PRO C  1  300 ? 15.364  -5.700  26.906 1.00 35.99  ? 313 PRO C CA  1 
ATOM   7568 C  C   . PRO C  1  300 ? 16.225  -6.745  26.200 1.00 39.61  ? 313 PRO C C   1 
ATOM   7569 O  O   . PRO C  1  300 ? 17.154  -6.367  25.483 1.00 39.61  ? 313 PRO C O   1 
ATOM   7570 C  CB  . PRO C  1  300 ? 14.246  -5.147  25.992 1.00 35.47  ? 313 PRO C CB  1 
ATOM   7571 C  CG  . PRO C  1  300 ? 14.943  -4.059  25.207 1.00 35.27  ? 313 PRO C CG  1 
ATOM   7572 C  CD  . PRO C  1  300 ? 15.758  -3.361  26.272 1.00 34.49  ? 313 PRO C CD  1 
ATOM   7573 N  N   . THR C  1  301 ? 15.885  -8.039  26.356 1.00 43.79  ? 314 THR C N   1 
ATOM   7574 C  CA  . THR C  1  301 ? 16.794  -9.092  25.918 1.00 54.53  ? 314 THR C CA  1 
ATOM   7575 C  C   . THR C  1  301 ? 16.121  -10.135 25.021 1.00 57.89  ? 314 THR C C   1 
ATOM   7576 O  O   . THR C  1  301 ? 16.813  -10.736 24.192 1.00 76.91  ? 314 THR C O   1 
ATOM   7577 C  CB  . THR C  1  301 ? 17.499  -9.790  27.088 1.00 59.13  ? 314 THR C CB  1 
ATOM   7578 O  OG1 . THR C  1  301 ? 16.498  -10.274 27.981 1.00 59.47  ? 314 THR C OG1 1 
ATOM   7579 C  CG2 . THR C  1  301 ? 18.474  -8.882  27.823 1.00 62.13  ? 314 THR C CG2 1 
ATOM   7580 N  N   . GLY C  1  302 ? 14.830  -10.439 25.189 1.00 47.55  ? 315 GLY C N   1 
ATOM   7581 C  CA  . GLY C  1  302 ? 14.375  -11.700 24.622 1.00 49.53  ? 315 GLY C CA  1 
ATOM   7582 C  C   . GLY C  1  302 ? 13.416  -11.518 23.448 1.00 52.94  ? 315 GLY C C   1 
ATOM   7583 O  O   . GLY C  1  302 ? 13.728  -10.855 22.468 1.00 47.14  ? 315 GLY C O   1 
ATOM   7584 N  N   . ILE C  1  303 ? 12.245  -12.147 23.582 1.00 54.19  ? 316 ILE C N   1 
ATOM   7585 C  CA  . ILE C  1  303 ? 11.092  -11.904 22.735 1.00 51.65  ? 316 ILE C CA  1 
ATOM   7586 C  C   . ILE C  1  303 ? 10.716  -10.427 22.834 1.00 41.59  ? 316 ILE C C   1 
ATOM   7587 O  O   . ILE C  1  303 ? 10.241  -9.844  21.866 1.00 39.72  ? 316 ILE C O   1 
ATOM   7588 C  CB  . ILE C  1  303 ? 9.944   -12.850 23.146 1.00 63.05  ? 316 ILE C CB  1 
ATOM   7589 C  CG1 . ILE C  1  303 ? 10.353  -14.330 22.976 1.00 82.32  ? 316 ILE C CG1 1 
ATOM   7590 C  CG2 . ILE C  1  303 ? 8.654   -12.548 22.385 1.00 62.02  ? 316 ILE C CG2 1 
ATOM   7591 C  CD1 . ILE C  1  303 ? 9.564   -15.312 23.833 1.00 93.82  ? 316 ILE C CD1 1 
ATOM   7592 N  N   . LEU C  1  304 ? 10.943  -9.807  23.995 1.00 36.89  ? 317 LEU C N   1 
ATOM   7593 C  CA  . LEU C  1  304 ? 10.586  -8.409  24.157 1.00 36.03  ? 317 LEU C CA  1 
ATOM   7594 C  C   . LEU C  1  304 ? 11.493  -7.535  23.284 1.00 36.92  ? 317 LEU C C   1 
ATOM   7595 O  O   . LEU C  1  304 ? 11.018  -6.571  22.681 1.00 39.51  ? 317 LEU C O   1 
ATOM   7596 C  CB  . LEU C  1  304 ? 10.615  -8.012  25.629 1.00 36.37  ? 317 LEU C CB  1 
ATOM   7597 C  CG  . LEU C  1  304 ? 10.456  -6.516  25.917 1.00 36.87  ? 317 LEU C CG  1 
ATOM   7598 C  CD1 . LEU C  1  304 ? 9.098   -6.007  25.459 1.00 36.78  ? 317 LEU C CD1 1 
ATOM   7599 C  CD2 . LEU C  1  304 ? 10.665  -6.216  27.389 1.00 37.52  ? 317 LEU C CD2 1 
ATOM   7600 N  N   . ARG C  1  305 ? 12.796  -7.857  23.224 1.00 35.38  ? 318 ARG C N   1 
ATOM   7601 C  CA  A ARG C  1  305 ? 13.720  -7.120  22.376 0.50 32.42  ? 318 ARG C CA  1 
ATOM   7602 C  CA  B ARG C  1  305 ? 13.742  -7.145  22.373 0.50 35.10  ? 318 ARG C CA  1 
ATOM   7603 C  C   . ARG C  1  305 ? 13.294  -7.263  20.918 1.00 32.48  ? 318 ARG C C   1 
ATOM   7604 O  O   . ARG C  1  305 ? 13.248  -6.292  20.184 1.00 32.44  ? 318 ARG C O   1 
ATOM   7605 C  CB  A ARG C  1  305 ? 15.161  -7.620  22.542 0.50 30.63  ? 318 ARG C CB  1 
ATOM   7606 C  CB  B ARG C  1  305 ? 15.174  -7.686  22.542 0.50 37.25  ? 318 ARG C CB  1 
ATOM   7607 C  CG  A ARG C  1  305 ? 16.199  -6.979  21.636 0.50 28.98  ? 318 ARG C CG  1 
ATOM   7608 C  CG  B ARG C  1  305 ? 16.271  -6.804  21.951 0.50 39.50  ? 318 ARG C CG  1 
ATOM   7609 C  CD  A ARG C  1  305 ? 17.502  -7.752  21.493 0.50 26.47  ? 318 ARG C CD  1 
ATOM   7610 C  CD  B ARG C  1  305 ? 17.686  -7.399  21.882 0.50 41.40  ? 318 ARG C CD  1 
ATOM   7611 N  NE  A ARG C  1  305 ? 18.347  -7.080  20.503 0.50 23.29  ? 318 ARG C NE  1 
ATOM   7612 N  NE  B ARG C  1  305 ? 18.694  -6.364  21.598 0.50 40.81  ? 318 ARG C NE  1 
ATOM   7613 C  CZ  A ARG C  1  305 ? 18.633  -7.585  19.340 0.50 18.55  ? 318 ARG C CZ  1 
ATOM   7614 C  CZ  B ARG C  1  305 ? 19.026  -5.356  22.400 0.50 39.40  ? 318 ARG C CZ  1 
ATOM   7615 N  NH1 A ARG C  1  305 ? 18.190  -8.777  19.059 0.50 17.78  ? 318 ARG C NH1 1 
ATOM   7616 N  NH1 B ARG C  1  305 ? 18.622  -5.300  23.679 0.50 39.34  ? 318 ARG C NH1 1 
ATOM   7617 N  NH2 A ARG C  1  305 ? 19.347  -6.898  18.485 0.50 17.46  ? 318 ARG C NH2 1 
ATOM   7618 N  NH2 B ARG C  1  305 ? 19.786  -4.406  21.892 0.50 34.82  ? 318 ARG C NH2 1 
ATOM   7619 N  N   . ARG C  1  306 ? 12.991  -8.488  20.512 1.00 35.83  ? 319 ARG C N   1 
ATOM   7620 C  CA  . ARG C  1  306 ? 12.629  -8.782  19.136 1.00 41.70  ? 319 ARG C CA  1 
ATOM   7621 C  C   . ARG C  1  306 ? 11.405  -7.963  18.725 1.00 39.07  ? 319 ARG C C   1 
ATOM   7622 O  O   . ARG C  1  306 ? 11.411  -7.342  17.662 1.00 35.13  ? 319 ARG C O   1 
ATOM   7623 C  CB  . ARG C  1  306 ? 12.397  -10.294 19.005 1.00 46.69  ? 319 ARG C CB  1 
ATOM   7624 C  CG  . ARG C  1  306 ? 12.276  -10.795 17.575 1.00 58.29  ? 319 ARG C CG  1 
ATOM   7625 C  CD  . ARG C  1  306 ? 11.700  -12.208 17.497 1.00 67.47  ? 319 ARG C CD  1 
ATOM   7626 N  NE  . ARG C  1  306 ? 10.265  -12.220 17.818 1.00 74.38  ? 319 ARG C NE  1 
ATOM   7627 C  CZ  . ARG C  1  306 ? 9.538   -13.307 18.040 1.00 77.79  ? 319 ARG C CZ  1 
ATOM   7628 N  NH1 . ARG C  1  306 ? 10.053  -14.507 17.843 1.00 81.38  ? 319 ARG C NH1 1 
ATOM   7629 N  NH2 . ARG C  1  306 ? 8.281   -13.190 18.425 1.00 77.56  ? 319 ARG C NH2 1 
ATOM   7630 N  N   . ASN C  1  307 ? 10.384  -7.933  19.595 1.00 33.93  ? 320 ASN C N   1 
ATOM   7631 C  CA  . ASN C  1  307 ? 9.127   -7.282  19.271 1.00 33.25  ? 320 ASN C CA  1 
ATOM   7632 C  C   . ASN C  1  307 ? 9.272   -5.756  19.284 1.00 34.10  ? 320 ASN C C   1 
ATOM   7633 O  O   . ASN C  1  307 ? 8.594   -5.069  18.520 1.00 38.13  ? 320 ASN C O   1 
ATOM   7634 C  CB  . ASN C  1  307 ? 8.002   -7.803  20.153 1.00 33.57  ? 320 ASN C CB  1 
ATOM   7635 C  CG  . ASN C  1  307 ? 7.625   -9.219  19.790 1.00 35.58  ? 320 ASN C CG  1 
ATOM   7636 O  OD1 . ASN C  1  307 ? 8.228   -9.827  18.894 1.00 36.50  ? 320 ASN C OD1 1 
ATOM   7637 N  ND2 . ASN C  1  307 ? 6.622   -9.765  20.458 1.00 38.18  ? 320 ASN C ND2 1 
ATOM   7638 N  N   . LEU C  1  308 ? 10.171  -5.226  20.123 1.00 34.82  ? 321 LEU C N   1 
ATOM   7639 C  CA  . LEU C  1  308 ? 10.493  -3.804  20.117 1.00 34.40  ? 321 LEU C CA  1 
ATOM   7640 C  C   . LEU C  1  308 ? 11.107  -3.401  18.786 1.00 31.54  ? 321 LEU C C   1 
ATOM   7641 O  O   . LEU C  1  308 ? 10.797  -2.346  18.244 1.00 31.66  ? 321 LEU C O   1 
ATOM   7642 C  CB  . LEU C  1  308 ? 11.447  -3.442  21.252 1.00 38.86  ? 321 LEU C CB  1 
ATOM   7643 C  CG  . LEU C  1  308 ? 10.787  -2.968  22.547 1.00 42.95  ? 321 LEU C CG  1 
ATOM   7644 C  CD1 . LEU C  1  308 ? 11.781  -3.012  23.699 1.00 45.81  ? 321 LEU C CD1 1 
ATOM   7645 C  CD2 . LEU C  1  308 ? 10.236  -1.559  22.352 1.00 44.27  ? 321 LEU C CD2 1 
ATOM   7646 N  N   . ILE C  1  309 ? 12.038  -4.215  18.297 1.00 33.20  ? 322 ILE C N   1 
ATOM   7647 C  CA  . ILE C  1  309 ? 12.762  -3.882  17.081 1.00 34.25  ? 322 ILE C CA  1 
ATOM   7648 C  C   . ILE C  1  309 ? 11.777  -3.831  15.923 1.00 33.89  ? 322 ILE C C   1 
ATOM   7649 O  O   . ILE C  1  309 ? 11.853  -2.930  15.095 1.00 32.92  ? 322 ILE C O   1 
ATOM   7650 C  CB  . ILE C  1  309 ? 13.895  -4.889  16.828 1.00 34.06  ? 322 ILE C CB  1 
ATOM   7651 C  CG1 . ILE C  1  309 ? 15.048  -4.625  17.760 1.00 32.25  ? 322 ILE C CG1 1 
ATOM   7652 C  CG2 . ILE C  1  309 ? 14.344  -4.895  15.364 1.00 34.15  ? 322 ILE C CG2 1 
ATOM   7653 C  CD1 . ILE C  1  309 ? 16.007  -5.786  17.866 1.00 32.86  ? 322 ILE C CD1 1 
ATOM   7654 N  N   . LYS C  1  310 ? 10.854  -4.796  15.895 1.00 33.21  ? 323 LYS C N   1 
ATOM   7655 C  CA  . LYS C  1  310 ? 9.872   -4.886  14.828 1.00 34.43  ? 323 LYS C CA  1 
ATOM   7656 C  C   . LYS C  1  310 ? 8.896   -3.718  14.879 1.00 33.32  ? 323 LYS C C   1 
ATOM   7657 O  O   . LYS C  1  310 ? 8.668   -3.078  13.851 1.00 35.65  ? 323 LYS C O   1 
ATOM   7658 C  CB  . LYS C  1  310 ? 9.166   -6.236  14.915 1.00 35.33  ? 323 LYS C CB  1 
ATOM   7659 C  CG  . LYS C  1  310 ? 9.967   -7.372  14.320 1.00 39.74  ? 323 LYS C CG  1 
ATOM   7660 C  CD  . LYS C  1  310 ? 9.342   -8.738  14.547 1.00 46.62  ? 323 LYS C CD  1 
ATOM   7661 C  CE  . LYS C  1  310 ? 10.054  -9.801  13.782 1.00 54.55  ? 323 LYS C CE  1 
ATOM   7662 N  NZ  . LYS C  1  310 ? 9.537   -11.110 14.178 1.00 61.78  ? 323 LYS C NZ  1 
ATOM   7663 N  N   . ASN C  1  311 ? 8.336   -3.443  16.062 1.00 29.15  ? 324 ASN C N   1 
ATOM   7664 C  CA  . ASN C  1  311 ? 7.339   -2.398  16.199 1.00 29.39  ? 324 ASN C CA  1 
ATOM   7665 C  C   . ASN C  1  311 ? 7.967   -1.048  15.870 1.00 29.25  ? 324 ASN C C   1 
ATOM   7666 O  O   . ASN C  1  311 ? 7.316   -0.210  15.261 1.00 33.39  ? 324 ASN C O   1 
ATOM   7667 C  CB  . ASN C  1  311 ? 6.650   -2.450  17.559 1.00 30.90  ? 324 ASN C CB  1 
ATOM   7668 C  CG  . ASN C  1  311 ? 5.524   -3.454  17.597 1.00 31.14  ? 324 ASN C CG  1 
ATOM   7669 O  OD1 . ASN C  1  311 ? 4.426   -3.180  17.113 1.00 32.99  ? 324 ASN C OD1 1 
ATOM   7670 N  ND2 . ASN C  1  311 ? 5.747   -4.612  18.191 1.00 34.40  ? 324 ASN C ND2 1 
ATOM   7671 N  N   . LEU C  1  312 ? 9.234   -0.845  16.236 1.00 31.40  ? 325 LEU C N   1 
ATOM   7672 C  CA  . LEU C  1  312 ? 9.910   0.411   15.926 1.00 33.77  ? 325 LEU C CA  1 
ATOM   7673 C  C   . LEU C  1  312 ? 10.080  0.565   14.414 1.00 30.56  ? 325 LEU C C   1 
ATOM   7674 O  O   . LEU C  1  312 ? 9.927   1.652   13.878 1.00 27.87  ? 325 LEU C O   1 
ATOM   7675 C  CB  . LEU C  1  312 ? 11.262  0.482   16.635 1.00 31.85  ? 325 LEU C CB  1 
ATOM   7676 C  CG  . LEU C  1  312 ? 11.237  0.873   18.110 1.00 31.05  ? 325 LEU C CG  1 
ATOM   7677 C  CD1 . LEU C  1  312 ? 12.565  0.469   18.714 1.00 32.63  ? 325 LEU C CD1 1 
ATOM   7678 C  CD2 . LEU C  1  312 ? 11.003  2.368   18.275 1.00 30.43  ? 325 LEU C CD2 1 
ATOM   7679 N  N   . HIS C  1  313 ? 10.421  -0.533  13.738 1.00 31.81  ? 326 HIS C N   1 
ATOM   7680 C  CA  . HIS C  1  313 ? 10.586  -0.513  12.293 1.00 33.17  ? 326 HIS C CA  1 
ATOM   7681 C  C   . HIS C  1  313 ? 9.227   -0.258  11.634 1.00 32.82  ? 326 HIS C C   1 
ATOM   7682 O  O   . HIS C  1  313 ? 9.119   0.585   10.743 1.00 30.73  ? 326 HIS C O   1 
ATOM   7683 C  CB  . HIS C  1  313 ? 11.293  -1.776  11.791 1.00 33.91  ? 326 HIS C CB  1 
ATOM   7684 C  CG  . HIS C  1  313 ? 11.463  -1.751  10.314 1.00 37.40  ? 326 HIS C CG  1 
ATOM   7685 N  ND1 . HIS C  1  313 ? 12.223  -0.794  9.677  1.00 38.65  ? 326 HIS C ND1 1 
ATOM   7686 C  CD2 . HIS C  1  313 ? 10.888  -2.481  9.353  1.00 38.47  ? 326 HIS C CD2 1 
ATOM   7687 C  CE1 . HIS C  1  313 ? 12.130  -0.980  8.377  1.00 41.65  ? 326 HIS C CE1 1 
ATOM   7688 N  NE2 . HIS C  1  313 ? 11.322  -2.000  8.155  1.00 38.29  ? 326 HIS C NE2 1 
ATOM   7689 N  N   . TYR C  1  314 ? 8.178   -0.955  12.085 1.00 32.41  ? 327 TYR C N   1 
ATOM   7690 C  CA  . TYR C  1  314 ? 6.841   -0.721  11.557 1.00 31.11  ? 327 TYR C CA  1 
ATOM   7691 C  C   . TYR C  1  314 ? 6.466   0.755   11.673 1.00 30.82  ? 327 TYR C C   1 
ATOM   7692 O  O   . TYR C  1  314 ? 5.977   1.339   10.717 1.00 30.54  ? 327 TYR C O   1 
ATOM   7693 C  CB  . TYR C  1  314 ? 5.800   -1.568  12.285 1.00 30.89  ? 327 TYR C CB  1 
ATOM   7694 C  CG  . TYR C  1  314 ? 6.013   -3.071  12.168 1.00 30.26  ? 327 TYR C CG  1 
ATOM   7695 C  CD1 . TYR C  1  314 ? 6.752   -3.632  11.127 1.00 28.34  ? 327 TYR C CD1 1 
ATOM   7696 C  CD2 . TYR C  1  314 ? 5.463   -3.930  13.113 1.00 31.66  ? 327 TYR C CD2 1 
ATOM   7697 C  CE1 . TYR C  1  314 ? 6.944   -5.001  11.035 1.00 27.41  ? 327 TYR C CE1 1 
ATOM   7698 C  CE2 . TYR C  1  314 ? 5.643   -5.303  13.028 1.00 30.43  ? 327 TYR C CE2 1 
ATOM   7699 C  CZ  . TYR C  1  314 ? 6.386   -5.836  11.986 1.00 29.75  ? 327 TYR C CZ  1 
ATOM   7700 O  OH  . TYR C  1  314 ? 6.571   -7.184  11.910 1.00 33.35  ? 327 TYR C OH  1 
ATOM   7701 N  N   . TRP C  1  315 ? 6.705   1.361   12.841 1.00 31.00  ? 328 TRP C N   1 
ATOM   7702 C  CA  . TRP C  1  315 ? 6.369   2.761   13.044 1.00 30.00  ? 328 TRP C CA  1 
ATOM   7703 C  C   . TRP C  1  315 ? 7.123   3.615   12.030 1.00 29.29  ? 328 TRP C C   1 
ATOM   7704 O  O   . TRP C  1  315 ? 6.548   4.490   11.405 1.00 30.37  ? 328 TRP C O   1 
ATOM   7705 C  CB  . TRP C  1  315 ? 6.663   3.196   14.492 1.00 29.64  ? 328 TRP C CB  1 
ATOM   7706 C  CG  . TRP C  1  315 ? 6.098   4.544   14.862 1.00 31.11  ? 328 TRP C CG  1 
ATOM   7707 C  CD1 . TRP C  1  315 ? 4.837   4.997   14.634 1.00 31.90  ? 328 TRP C CD1 1 
ATOM   7708 C  CD2 . TRP C  1  315 ? 6.790   5.639   15.498 1.00 32.62  ? 328 TRP C CD2 1 
ATOM   7709 N  NE1 . TRP C  1  315 ? 4.690   6.284   15.084 1.00 32.05  ? 328 TRP C NE1 1 
ATOM   7710 C  CE2 . TRP C  1  315 ? 5.866   6.705   15.621 1.00 33.00  ? 328 TRP C CE2 1 
ATOM   7711 C  CE3 . TRP C  1  315 ? 8.093   5.825   15.965 1.00 33.15  ? 328 TRP C CE3 1 
ATOM   7712 C  CZ2 . TRP C  1  315 ? 6.190   7.926   16.203 1.00 34.92  ? 328 TRP C CZ2 1 
ATOM   7713 C  CZ3 . TRP C  1  315 ? 8.418   7.033   16.544 1.00 35.75  ? 328 TRP C CZ3 1 
ATOM   7714 C  CH2 . TRP C  1  315 ? 7.484   8.071   16.646 1.00 36.28  ? 328 TRP C CH2 1 
ATOM   7715 N  N   . TRP C  1  316 ? 8.417   3.346   11.864 1.00 32.07  ? 329 TRP C N   1 
ATOM   7716 C  CA  . TRP C  1  316 ? 9.245   4.142   10.978 1.00 31.81  ? 329 TRP C CA  1 
ATOM   7717 C  C   . TRP C  1  316 ? 8.684   4.132   9.552  1.00 28.72  ? 329 TRP C C   1 
ATOM   7718 O  O   . TRP C  1  316 ? 8.729   5.152   8.869  1.00 27.24  ? 329 TRP C O   1 
ATOM   7719 C  CB  . TRP C  1  316 ? 10.718  3.694   11.016 1.00 31.69  ? 329 TRP C CB  1 
ATOM   7720 C  CG  . TRP C  1  316 ? 11.544  4.443   10.003 1.00 31.68  ? 329 TRP C CG  1 
ATOM   7721 C  CD1 . TRP C  1  316 ? 12.089  5.688   10.141 1.00 31.73  ? 329 TRP C CD1 1 
ATOM   7722 C  CD2 . TRP C  1  316 ? 11.821  4.031   8.645  1.00 28.27  ? 329 TRP C CD2 1 
ATOM   7723 N  NE1 . TRP C  1  316 ? 12.707  6.067   8.975  1.00 31.11  ? 329 TRP C NE1 1 
ATOM   7724 C  CE2 . TRP C  1  316 ? 12.554  5.074   8.040  1.00 29.24  ? 329 TRP C CE2 1 
ATOM   7725 C  CE3 . TRP C  1  316 ? 11.520  2.893   7.895  1.00 27.93  ? 329 TRP C CE3 1 
ATOM   7726 C  CZ2 . TRP C  1  316 ? 12.987  5.007   6.720  1.00 29.16  ? 329 TRP C CZ2 1 
ATOM   7727 C  CZ3 . TRP C  1  316 ? 11.941  2.836   6.589  1.00 29.96  ? 329 TRP C CZ3 1 
ATOM   7728 C  CH2 . TRP C  1  316 ? 12.654  3.883   6.007  1.00 29.86  ? 329 TRP C CH2 1 
ATOM   7729 N  N   . THR C  1  317 ? 8.154   2.991   9.089  1.00 30.16  ? 330 THR C N   1 
ATOM   7730 C  CA  . THR C  1  317 ? 7.648   2.915   7.717  1.00 28.21  ? 330 THR C CA  1 
ATOM   7731 C  C   . THR C  1  317 ? 6.559   3.961   7.510  1.00 29.39  ? 330 THR C C   1 
ATOM   7732 O  O   . THR C  1  317 ? 6.453   4.528   6.426  1.00 33.46  ? 330 THR C O   1 
ATOM   7733 C  CB  . THR C  1  317 ? 7.108   1.546   7.314  1.00 26.33  ? 330 THR C CB  1 
ATOM   7734 O  OG1 . THR C  1  317 ? 5.963   1.254   8.100  1.00 29.54  ? 330 THR C OG1 1 
ATOM   7735 C  CG2 . THR C  1  317 ? 8.106   0.423   7.498  1.00 27.30  ? 330 THR C CG2 1 
ATOM   7736 N  N   . GLY C  1  318 ? 5.749   4.204   8.545  1.00 29.87  ? 331 GLY C N   1 
ATOM   7737 C  CA  . GLY C  1  318 ? 4.730   5.240   8.495  1.00 30.78  ? 331 GLY C CA  1 
ATOM   7738 C  C   . GLY C  1  318 ? 5.310   6.644   8.610  1.00 29.92  ? 331 GLY C C   1 
ATOM   7739 O  O   . GLY C  1  318 ? 4.978   7.525   7.820  1.00 30.56  ? 331 GLY C O   1 
ATOM   7740 N  N   . VAL C  1  319 ? 6.176   6.828   9.607  1.00 31.22  ? 332 VAL C N   1 
ATOM   7741 C  CA  . VAL C  1  319 ? 6.768   8.119   9.904  1.00 32.62  ? 332 VAL C CA  1 
ATOM   7742 C  C   . VAL C  1  319 ? 7.497   8.667   8.680  1.00 33.27  ? 332 VAL C C   1 
ATOM   7743 O  O   . VAL C  1  319 ? 7.431   9.859   8.395  1.00 32.39  ? 332 VAL C O   1 
ATOM   7744 C  CB  . VAL C  1  319 ? 7.705   7.982   11.117 1.00 34.95  ? 332 VAL C CB  1 
ATOM   7745 C  CG1 . VAL C  1  319 ? 8.708   9.135   11.210 1.00 34.45  ? 332 VAL C CG1 1 
ATOM   7746 C  CG2 . VAL C  1  319 ? 6.908   7.820   12.412 1.00 37.12  ? 332 VAL C CG2 1 
ATOM   7747 N  N   . ASN C  1  320 ? 8.197   7.783   7.970  1.00 34.78  ? 333 ASN C N   1 
ATOM   7748 C  CA  . ASN C  1  320 ? 9.054   8.187   6.871  1.00 35.32  ? 333 ASN C CA  1 
ATOM   7749 C  C   . ASN C  1  320 ? 8.244   8.894   5.792  1.00 36.38  ? 333 ASN C C   1 
ATOM   7750 O  O   . ASN C  1  320 ? 8.665   9.934   5.281  1.00 37.57  ? 333 ASN C O   1 
ATOM   7751 C  CB  . ASN C  1  320 ? 9.801   6.997   6.280  1.00 36.43  ? 333 ASN C CB  1 
ATOM   7752 C  CG  . ASN C  1  320 ? 10.903  7.445   5.349  1.00 37.80  ? 333 ASN C CG  1 
ATOM   7753 O  OD1 . ASN C  1  320 ? 11.681  8.347   5.699  1.00 42.56  ? 333 ASN C OD1 1 
ATOM   7754 N  ND2 . ASN C  1  320 ? 10.972  6.837   4.173  1.00 35.79  ? 333 ASN C ND2 1 
ATOM   7755 N  N   . VAL C  1  321 ? 7.088   8.305   5.450  1.00 36.04  ? 334 VAL C N   1 
ATOM   7756 C  CA  . VAL C  1  321 ? 6.219   8.893   4.446  1.00 38.07  ? 334 VAL C CA  1 
ATOM   7757 C  C   . VAL C  1  321 ? 5.495   10.099  5.038  1.00 37.83  ? 334 VAL C C   1 
ATOM   7758 O  O   . VAL C  1  321 ? 5.434   11.148  4.406  1.00 41.39  ? 334 VAL C O   1 
ATOM   7759 C  CB  . VAL C  1  321 ? 5.225   7.893   3.827  1.00 37.39  ? 334 VAL C CB  1 
ATOM   7760 C  CG1 . VAL C  1  321 ? 4.279   8.564   2.839  1.00 34.51  ? 334 VAL C CG1 1 
ATOM   7761 C  CG2 . VAL C  1  321 ? 5.954   6.753   3.131  1.00 34.69  ? 334 VAL C CG2 1 
ATOM   7762 N  N   . ALA C  1  322 ? 4.939   9.958   6.238  1.00 36.87  ? 335 ALA C N   1 
ATOM   7763 C  CA  . ALA C  1  322 ? 4.087   11.005  6.788  1.00 38.58  ? 335 ALA C CA  1 
ATOM   7764 C  C   . ALA C  1  322 ? 4.873   12.276  7.110  1.00 38.11  ? 335 ALA C C   1 
ATOM   7765 O  O   . ALA C  1  322 ? 4.337   13.362  6.955  1.00 37.55  ? 335 ALA C O   1 
ATOM   7766 C  CB  . ALA C  1  322 ? 3.366   10.502  8.013  1.00 39.35  ? 335 ALA C CB  1 
ATOM   7767 N  N   . PHE C  1  323 ? 6.127   12.151  7.556  1.00 40.39  ? 336 PHE C N   1 
ATOM   7768 C  CA  . PHE C  1  323 ? 6.907   13.310  7.979  1.00 44.42  ? 336 PHE C CA  1 
ATOM   7769 C  C   . PHE C  1  323 ? 7.857   13.795  6.882  1.00 45.93  ? 336 PHE C C   1 
ATOM   7770 O  O   . PHE C  1  323 ? 8.643   14.716  7.126  1.00 47.64  ? 336 PHE C O   1 
ATOM   7771 C  CB  . PHE C  1  323 ? 7.726   13.003  9.242  1.00 45.41  ? 336 PHE C CB  1 
ATOM   7772 C  CG  . PHE C  1  323 ? 6.922   12.770  10.512 1.00 40.43  ? 336 PHE C CG  1 
ATOM   7773 C  CD1 . PHE C  1  323 ? 5.529   12.781  10.515 1.00 42.65  ? 336 PHE C CD1 1 
ATOM   7774 C  CD2 . PHE C  1  323 ? 7.577   12.509  11.703 1.00 42.19  ? 336 PHE C CD2 1 
ATOM   7775 C  CE1 . PHE C  1  323 ? 4.822   12.547  11.679 1.00 43.82  ? 336 PHE C CE1 1 
ATOM   7776 C  CE2 . PHE C  1  323 ? 6.864   12.266  12.865 1.00 43.86  ? 336 PHE C CE2 1 
ATOM   7777 C  CZ  . PHE C  1  323 ? 5.488   12.278  12.847 1.00 45.50  ? 336 PHE C CZ  1 
ATOM   7778 N  N   . GLY C  1  324 ? 7.810   13.166  5.695  1.00 43.60  ? 337 GLY C N   1 
ATOM   7779 C  CA  . GLY C  1  324 ? 8.558   13.652  4.547  1.00 39.04  ? 337 GLY C CA  1 
ATOM   7780 C  C   . GLY C  1  324 ? 10.040  13.286  4.590  1.00 42.04  ? 337 GLY C C   1 
ATOM   7781 O  O   . GLY C  1  324 ? 10.841  14.006  4.011  1.00 47.19  ? 337 GLY C O   1 
ATOM   7782 N  N   . GLY C  1  325 ? 10.391  12.158  5.239  1.00 44.89  ? 338 GLY C N   1 
ATOM   7783 C  CA  . GLY C  1  325 ? 11.743  11.613  5.241  1.00 42.30  ? 338 GLY C CA  1 
ATOM   7784 C  C   . GLY C  1  325 ? 12.451  11.816  6.583  1.00 41.69  ? 338 GLY C C   1 
ATOM   7785 O  O   . GLY C  1  325 ? 12.733  12.950  6.943  1.00 43.59  ? 338 GLY C O   1 
ATOM   7786 N  N   . CYS C  1  326 ? 12.709  10.722  7.319  1.00 38.88  ? 339 CYS C N   1 
ATOM   7787 C  CA  . CYS C  1  326 ? 13.483  10.741  8.551  1.00 39.29  ? 339 CYS C CA  1 
ATOM   7788 C  C   . CYS C  1  326 ? 14.473  9.581   8.545  1.00 35.99  ? 339 CYS C C   1 
ATOM   7789 O  O   . CYS C  1  326 ? 14.125  8.488   8.117  1.00 33.31  ? 339 CYS C O   1 
ATOM   7790 C  CB  . CYS C  1  326 ? 12.637  10.544  9.816  1.00 45.14  ? 339 CYS C CB  1 
ATOM   7791 S  SG  . CYS C  1  326 ? 11.540  11.927  10.247 1.00 65.06  ? 339 CYS C SG  1 
ATOM   7792 N  N   . ASP C  1  327 ? 15.678  9.804   9.087  1.00 37.66  ? 340 ASP C N   1 
ATOM   7793 C  CA  . ASP C  1  327 ? 16.643  8.732   9.269  1.00 42.40  ? 340 ASP C CA  1 
ATOM   7794 C  C   . ASP C  1  327 ? 16.208  7.802   10.389 1.00 41.64  ? 340 ASP C C   1 
ATOM   7795 O  O   . ASP C  1  327 ? 16.017  8.231   11.524 1.00 43.10  ? 340 ASP C O   1 
ATOM   7796 C  CB  . ASP C  1  327 ? 18.045  9.269   9.507  1.00 48.64  ? 340 ASP C CB  1 
ATOM   7797 C  CG  . ASP C  1  327 ? 18.689  9.890   8.274  1.00 52.62  ? 340 ASP C CG  1 
ATOM   7798 O  OD1 . ASP C  1  327 ? 18.656  9.241   7.221  1.00 52.59  ? 340 ASP C OD1 1 
ATOM   7799 O  OD2 . ASP C  1  327 ? 19.216  11.013  8.376  1.00 60.61  ? 340 ASP C OD2 1 
ATOM   7800 N  N   . GLU C  1  328 ? 16.111  6.517   10.047 1.00 39.70  ? 341 GLU C N   1 
ATOM   7801 C  CA  . GLU C  1  328 ? 15.698  5.497   10.995 1.00 39.88  ? 341 GLU C CA  1 
ATOM   7802 C  C   . GLU C  1  328 ? 16.771  5.322   12.072 1.00 38.82  ? 341 GLU C C   1 
ATOM   7803 O  O   . GLU C  1  328 ? 17.949  5.234   11.765 1.00 38.50  ? 341 GLU C O   1 
ATOM   7804 C  CB  . GLU C  1  328 ? 15.397  4.196   10.248 1.00 40.21  ? 341 GLU C CB  1 
ATOM   7805 C  CG  . GLU C  1  328 ? 14.860  3.084   11.147 1.00 39.90  ? 341 GLU C CG  1 
ATOM   7806 C  CD  . GLU C  1  328 ? 14.381  1.818   10.450 1.00 39.79  ? 341 GLU C CD  1 
ATOM   7807 O  OE1 . GLU C  1  328 ? 14.507  1.704   9.195  1.00 45.14  ? 341 GLU C OE1 1 
ATOM   7808 O  OE2 . GLU C  1  328 ? 13.870  0.942   11.191 1.00 36.11  ? 341 GLU C OE2 1 
ATOM   7809 N  N   . LEU C  1  329 ? 16.330  5.255   13.332 1.00 41.08  ? 342 LEU C N   1 
ATOM   7810 C  CA  . LEU C  1  329 ? 17.167  4.930   14.479 1.00 40.81  ? 342 LEU C CA  1 
ATOM   7811 C  C   . LEU C  1  329 ? 17.017  3.453   14.833 1.00 40.27  ? 342 LEU C C   1 
ATOM   7812 O  O   . LEU C  1  329 ? 15.938  2.883   14.631 1.00 37.98  ? 342 LEU C O   1 
ATOM   7813 C  CB  . LEU C  1  329 ? 16.736  5.806   15.654 1.00 40.88  ? 342 LEU C CB  1 
ATOM   7814 C  CG  . LEU C  1  329 ? 16.920  7.313   15.469 1.00 40.41  ? 342 LEU C CG  1 
ATOM   7815 C  CD1 . LEU C  1  329 ? 16.255  8.073   16.592 1.00 41.08  ? 342 LEU C CD1 1 
ATOM   7816 C  CD2 . LEU C  1  329 ? 18.389  7.629   15.454 1.00 38.57  ? 342 LEU C CD2 1 
ATOM   7817 N  N   . PHE C  1  330 ? 18.087  2.869   15.408 1.00 36.64  ? 343 PHE C N   1 
ATOM   7818 C  CA  . PHE C  1  330 ? 18.103  1.458   15.766 1.00 37.54  ? 343 PHE C CA  1 
ATOM   7819 C  C   . PHE C  1  330 ? 18.593  1.308   17.199 1.00 40.05  ? 343 PHE C C   1 
ATOM   7820 O  O   . PHE C  1  330 ? 19.654  0.747   17.442 1.00 39.03  ? 343 PHE C O   1 
ATOM   7821 C  CB  . PHE C  1  330 ? 18.993  0.654   14.816 1.00 37.31  ? 343 PHE C CB  1 
ATOM   7822 C  CG  . PHE C  1  330 ? 18.608  0.765   13.350 1.00 39.78  ? 343 PHE C CG  1 
ATOM   7823 C  CD1 . PHE C  1  330 ? 17.621  -0.063  12.812 1.00 37.29  ? 343 PHE C CD1 1 
ATOM   7824 C  CD2 . PHE C  1  330 ? 19.203  1.719   12.524 1.00 38.37  ? 343 PHE C CD2 1 
ATOM   7825 C  CE1 . PHE C  1  330 ? 17.268  0.042   11.478 1.00 39.06  ? 343 PHE C CE1 1 
ATOM   7826 C  CE2 . PHE C  1  330 ? 18.838  1.823   11.188 1.00 42.15  ? 343 PHE C CE2 1 
ATOM   7827 C  CZ  . PHE C  1  330 ? 17.873  0.986   10.664 1.00 40.06  ? 343 PHE C CZ  1 
ATOM   7828 N  N   . PRO C  1  331 ? 17.818  1.752   18.207 1.00 44.53  ? 344 PRO C N   1 
ATOM   7829 C  CA  . PRO C  1  331 ? 18.303  1.733   19.587 1.00 42.19  ? 344 PRO C CA  1 
ATOM   7830 C  C   . PRO C  1  331 ? 18.566  0.343   20.168 1.00 37.67  ? 344 PRO C C   1 
ATOM   7831 O  O   . PRO C  1  331 ? 19.210  0.241   21.205 1.00 42.28  ? 344 PRO C O   1 
ATOM   7832 C  CB  . PRO C  1  331 ? 17.168  2.467   20.318 1.00 42.17  ? 344 PRO C CB  1 
ATOM   7833 C  CG  . PRO C  1  331 ? 15.941  2.081   19.523 1.00 43.14  ? 344 PRO C CG  1 
ATOM   7834 C  CD  . PRO C  1  331 ? 16.430  2.236   18.089 1.00 44.11  ? 344 PRO C CD  1 
ATOM   7835 N  N   . TYR C  1  332 ? 18.066  -0.714  19.519 1.00 32.44  ? 345 TYR C N   1 
ATOM   7836 C  CA  . TYR C  1  332 ? 18.283  -2.072  19.989 1.00 31.19  ? 345 TYR C CA  1 
ATOM   7837 C  C   . TYR C  1  332 ? 18.945  -2.902  18.894 1.00 30.48  ? 345 TYR C C   1 
ATOM   7838 O  O   . TYR C  1  332 ? 18.955  -4.133  18.978 1.00 27.96  ? 345 TYR C O   1 
ATOM   7839 C  CB  . TYR C  1  332 ? 16.986  -2.734  20.470 1.00 32.22  ? 345 TYR C CB  1 
ATOM   7840 C  CG  . TYR C  1  332 ? 16.244  -1.895  21.496 1.00 34.35  ? 345 TYR C CG  1 
ATOM   7841 C  CD1 . TYR C  1  332 ? 16.733  -1.729  22.787 1.00 37.25  ? 345 TYR C CD1 1 
ATOM   7842 C  CD2 . TYR C  1  332 ? 15.064  -1.255  21.168 1.00 35.44  ? 345 TYR C CD2 1 
ATOM   7843 C  CE1 . TYR C  1  332 ? 16.066  -0.943  23.718 1.00 42.87  ? 345 TYR C CE1 1 
ATOM   7844 C  CE2 . TYR C  1  332 ? 14.376  -0.482  22.093 1.00 40.62  ? 345 TYR C CE2 1 
ATOM   7845 C  CZ  . TYR C  1  332 ? 14.875  -0.319  23.374 1.00 43.29  ? 345 TYR C CZ  1 
ATOM   7846 O  OH  . TYR C  1  332 ? 14.192  0.461   24.265 1.00 42.49  ? 345 TYR C OH  1 
ATOM   7847 N  N   . GLY C  1  333 ? 19.529  -2.210  17.903 1.00 32.28  ? 346 GLY C N   1 
ATOM   7848 C  CA  . GLY C  1  333 ? 20.194  -2.860  16.783 1.00 35.33  ? 346 GLY C CA  1 
ATOM   7849 C  C   . GLY C  1  333 ? 19.225  -3.591  15.854 1.00 36.33  ? 346 GLY C C   1 
ATOM   7850 O  O   . GLY C  1  333 ? 18.053  -3.252  15.807 1.00 35.50  ? 346 GLY C O   1 
ATOM   7851 N  N   . GLN C  1  334 ? 19.744  -4.604  15.154 1.00 42.53  ? 347 GLN C N   1 
ATOM   7852 C  CA  A GLN C  1  334 ? 19.008  -5.329  14.129 0.50 44.00  ? 347 GLN C CA  1 
ATOM   7853 C  CA  B GLN C  1  334 ? 19.020  -5.337  14.126 0.50 47.55  ? 347 GLN C CA  1 
ATOM   7854 C  C   . GLN C  1  334 ? 18.630  -6.702  14.686 1.00 45.60  ? 347 GLN C C   1 
ATOM   7855 O  O   . GLN C  1  334 ? 19.130  -7.106  15.735 1.00 49.14  ? 347 GLN C O   1 
ATOM   7856 C  CB  A GLN C  1  334 ? 19.852  -5.468  12.859 0.50 43.78  ? 347 GLN C CB  1 
ATOM   7857 C  CB  B GLN C  1  334 ? 19.901  -5.484  12.882 0.50 53.03  ? 347 GLN C CB  1 
ATOM   7858 C  CG  A GLN C  1  334 ? 20.289  -4.167  12.192 0.50 44.30  ? 347 GLN C CG  1 
ATOM   7859 C  CG  B GLN C  1  334 ? 20.333  -4.156  12.264 0.50 59.57  ? 347 GLN C CG  1 
ATOM   7860 C  CD  A GLN C  1  334 ? 19.180  -3.429  11.474 0.50 41.13  ? 347 GLN C CD  1 
ATOM   7861 C  CD  B GLN C  1  334 ? 20.884  -4.288  10.856 0.50 66.28  ? 347 GLN C CD  1 
ATOM   7862 O  OE1 A GLN C  1  334 ? 19.269  -2.218  11.249 0.50 39.80  ? 347 GLN C OE1 1 
ATOM   7863 O  OE1 B GLN C  1  334 ? 21.414  -5.331  10.447 0.50 61.82  ? 347 GLN C OE1 1 
ATOM   7864 N  NE2 A GLN C  1  334 ? 18.132  -4.149  11.100 0.50 39.61  ? 347 GLN C NE2 1 
ATOM   7865 N  NE2 B GLN C  1  334 ? 20.775  -3.207  10.096 0.50 67.51  ? 347 GLN C NE2 1 
ATOM   7866 N  N   . LEU C  1  335 ? 17.747  -7.420  13.981 1.00 47.03  ? 348 LEU C N   1 
ATOM   7867 C  CA  . LEU C  1  335 ? 17.198  -8.672  14.483 1.00 51.59  ? 348 LEU C CA  1 
ATOM   7868 C  C   . LEU C  1  335 ? 18.299  -9.717  14.755 1.00 60.99  ? 348 LEU C C   1 
ATOM   7869 O  O   . LEU C  1  335 ? 18.783  -10.328 13.787 1.00 67.29  ? 348 LEU C O   1 
ATOM   7870 C  CB  . LEU C  1  335 ? 16.130  -9.192  13.529 1.00 50.26  ? 348 LEU C CB  1 
ATOM   7871 C  CG  . LEU C  1  335 ? 14.752  -8.553  13.713 1.00 55.32  ? 348 LEU C CG  1 
ATOM   7872 C  CD1 . LEU C  1  335 ? 13.801  -8.900  12.577 1.00 53.71  ? 348 LEU C CD1 1 
ATOM   7873 C  CD2 . LEU C  1  335 ? 14.191  -8.967  15.076 1.00 53.90  ? 348 LEU C CD2 1 
HETATM 7874 C  C1  . NAG D  2  .   ? 29.128  12.491  34.310 1.00 50.04  ? 1   NAG H C1  1 
HETATM 7875 C  C2  . NAG D  2  .   ? 29.079  13.897  34.913 1.00 55.34  ? 1   NAG H C2  1 
HETATM 7876 C  C3  . NAG D  2  .   ? 28.519  14.897  33.912 1.00 57.48  ? 1   NAG H C3  1 
HETATM 7877 C  C4  . NAG D  2  .   ? 29.199  14.798  32.552 1.00 57.62  ? 1   NAG H C4  1 
HETATM 7878 C  C5  . NAG D  2  .   ? 29.184  13.357  32.048 1.00 56.69  ? 1   NAG H C5  1 
HETATM 7879 C  C6  . NAG D  2  .   ? 29.963  13.150  30.750 1.00 54.35  ? 1   NAG H C6  1 
HETATM 7880 C  C7  . NAG D  2  .   ? 28.879  14.190  37.311 1.00 79.25  ? 1   NAG H C7  1 
HETATM 7881 C  C8  . NAG D  2  .   ? 27.972  14.256  38.501 1.00 71.38  ? 1   NAG H C8  1 
HETATM 7882 N  N2  . NAG D  2  .   ? 28.294  13.948  36.131 1.00 66.21  ? 1   NAG H N2  1 
HETATM 7883 O  O3  . NAG D  2  .   ? 28.703  16.182  34.481 1.00 54.66  ? 1   NAG H O3  1 
HETATM 7884 O  O4  . NAG D  2  .   ? 28.478  15.616  31.615 1.00 58.43  ? 1   NAG H O4  1 
HETATM 7885 O  O5  . NAG D  2  .   ? 29.784  12.505  33.047 1.00 52.68  ? 1   NAG H O5  1 
HETATM 7886 O  O6  . NAG D  2  .   ? 31.353  13.549  30.836 1.00 47.19  ? 1   NAG H O6  1 
HETATM 7887 O  O7  . NAG D  2  .   ? 30.098  14.336  37.414 1.00 86.39  ? 1   NAG H O7  1 
HETATM 7888 C  C1  . NAG D  2  .   ? 29.187  16.546  30.853 1.00 55.55  ? 2   NAG H C1  1 
HETATM 7889 C  C2  . NAG D  2  .   ? 28.417  16.805  29.568 1.00 55.63  ? 2   NAG H C2  1 
HETATM 7890 C  C3  . NAG D  2  .   ? 29.199  17.778  28.689 1.00 60.78  ? 2   NAG H C3  1 
HETATM 7891 C  C4  . NAG D  2  .   ? 29.522  19.057  29.474 1.00 63.24  ? 2   NAG H C4  1 
HETATM 7892 C  C5  . NAG D  2  .   ? 30.221  18.692  30.784 1.00 58.77  ? 2   NAG H C5  1 
HETATM 7893 C  C6  . NAG D  2  .   ? 30.484  19.897  31.666 1.00 58.29  ? 2   NAG H C6  1 
HETATM 7894 C  C7  . NAG D  2  .   ? 26.941  14.929  28.950 1.00 55.74  ? 2   NAG H C7  1 
HETATM 7895 C  C8  . NAG D  2  .   ? 26.810  13.669  28.143 1.00 53.89  ? 2   NAG H C8  1 
HETATM 7896 N  N2  . NAG D  2  .   ? 28.101  15.597  28.831 1.00 56.45  ? 2   NAG H N2  1 
HETATM 7897 O  O3  . NAG D  2  .   ? 28.398  17.999  27.525 1.00 56.21  ? 2   NAG H O3  1 
HETATM 7898 O  O4  . NAG D  2  .   ? 30.401  19.953  28.762 1.00 66.27  ? 2   NAG H O4  1 
HETATM 7899 O  O5  . NAG D  2  .   ? 29.372  17.791  31.525 1.00 53.47  ? 2   NAG H O5  1 
HETATM 7900 O  O6  . NAG D  2  .   ? 29.246  20.501  32.016 1.00 54.64  ? 2   NAG H O6  1 
HETATM 7901 O  O7  . NAG D  2  .   ? 26.039  15.311  29.691 1.00 49.20  ? 2   NAG H O7  1 
HETATM 7902 C  C1  . BMA D  2  .   ? 29.890  20.974  27.953 1.00 72.45  ? 3   BMA H C1  1 
HETATM 7903 C  C2  . BMA D  2  .   ? 31.061  21.906  27.626 1.00 75.16  ? 3   BMA H C2  1 
HETATM 7904 C  C3  . BMA D  2  .   ? 30.683  22.912  26.526 1.00 81.66  ? 3   BMA H C3  1 
HETATM 7905 C  C4  . BMA D  2  .   ? 30.140  22.175  25.305 1.00 86.84  ? 3   BMA H C4  1 
HETATM 7906 C  C5  . BMA D  2  .   ? 28.935  21.311  25.694 1.00 82.27  ? 3   BMA H C5  1 
HETATM 7907 C  C6  . BMA D  2  .   ? 28.437  20.469  24.524 1.00 78.52  ? 3   BMA H C6  1 
HETATM 7908 O  O2  . BMA D  2  .   ? 32.222  21.138  27.275 1.00 65.10  ? 3   BMA H O2  1 
HETATM 7909 O  O3  . BMA D  2  .   ? 31.829  23.703  26.131 1.00 72.74  ? 3   BMA H O3  1 
HETATM 7910 O  O4  . BMA D  2  .   ? 29.754  23.113  24.296 1.00 90.61  ? 3   BMA H O4  1 
HETATM 7911 O  O5  . BMA D  2  .   ? 29.316  20.391  26.775 1.00 70.50  ? 3   BMA H O5  1 
HETATM 7912 O  O6  . BMA D  2  .   ? 27.139  19.923  24.849 1.00 83.06  ? 3   BMA H O6  1 
HETATM 7913 C  C1  . MAN D  2  .   ? 31.963  24.929  26.793 1.00 74.33  ? 4   MAN H C1  1 
HETATM 7914 C  C2  . MAN D  2  .   ? 32.533  25.921  25.775 1.00 70.50  ? 4   MAN H C2  1 
HETATM 7915 C  C3  . MAN D  2  .   ? 33.968  25.479  25.389 1.00 65.98  ? 4   MAN H C3  1 
HETATM 7916 C  C4  . MAN D  2  .   ? 34.855  25.400  26.647 1.00 64.33  ? 4   MAN H C4  1 
HETATM 7917 C  C5  . MAN D  2  .   ? 34.195  24.427  27.677 1.00 64.27  ? 4   MAN H C5  1 
HETATM 7918 C  C6  . MAN D  2  .   ? 34.906  24.374  29.020 1.00 64.13  ? 4   MAN H C6  1 
HETATM 7919 O  O2  . MAN D  2  .   ? 32.406  27.259  26.284 1.00 60.19  ? 4   MAN H O2  1 
HETATM 7920 O  O3  . MAN D  2  .   ? 34.517  26.356  24.401 1.00 65.04  ? 4   MAN H O3  1 
HETATM 7921 O  O4  . MAN D  2  .   ? 36.199  24.973  26.306 1.00 55.53  ? 4   MAN H O4  1 
HETATM 7922 O  O5  . MAN D  2  .   ? 32.809  24.831  27.951 1.00 62.67  ? 4   MAN H O5  1 
HETATM 7923 O  O6  . MAN D  2  .   ? 34.840  25.608  29.744 1.00 54.66  ? 4   MAN H O6  1 
HETATM 7924 C  C1  . MAN D  2  .   ? 26.341  19.475  23.779 1.00 79.03  ? 5   MAN H C1  1 
HETATM 7925 C  C2  . MAN D  2  .   ? 25.021  18.969  24.382 1.00 72.68  ? 5   MAN H C2  1 
HETATM 7926 C  C3  . MAN D  2  .   ? 25.178  17.654  25.197 1.00 71.13  ? 5   MAN H C3  1 
HETATM 7927 C  C4  . MAN D  2  .   ? 25.882  16.597  24.321 1.00 74.44  ? 5   MAN H C4  1 
HETATM 7928 C  C5  . MAN D  2  .   ? 27.242  17.170  23.765 1.00 79.10  ? 5   MAN H C5  1 
HETATM 7929 C  C6  . MAN D  2  .   ? 27.999  16.225  22.828 1.00 78.08  ? 5   MAN H C6  1 
HETATM 7930 O  O2  . MAN D  2  .   ? 24.064  18.800  23.337 1.00 72.44  ? 5   MAN H O2  1 
HETATM 7931 O  O3  . MAN D  2  .   ? 23.907  17.188  25.715 1.00 59.97  ? 5   MAN H O3  1 
HETATM 7932 O  O4  . MAN D  2  .   ? 26.118  15.399  25.083 1.00 73.74  ? 5   MAN H O4  1 
HETATM 7933 O  O5  . MAN D  2  .   ? 27.005  18.442  23.028 1.00 79.12  ? 5   MAN H O5  1 
HETATM 7934 O  O6  . MAN D  2  .   ? 27.277  15.907  21.622 1.00 73.84  ? 5   MAN H O6  1 
HETATM 7935 C  C1  . NAG E  3  .   ? 28.275  -8.970  19.756 1.00 48.34  ? 1   NAG I C1  1 
HETATM 7936 C  C2  . NAG E  3  .   ? 28.914  -9.877  18.707 1.00 51.10  ? 1   NAG I C2  1 
HETATM 7937 C  C3  . NAG E  3  .   ? 28.210  -9.743  17.361 1.00 53.50  ? 1   NAG I C3  1 
HETATM 7938 C  C4  . NAG E  3  .   ? 26.701  -9.874  17.526 1.00 54.95  ? 1   NAG I C4  1 
HETATM 7939 C  C5  . NAG E  3  .   ? 26.209  -8.904  18.601 1.00 51.68  ? 1   NAG I C5  1 
HETATM 7940 C  C6  . NAG E  3  .   ? 24.717  -8.985  18.867 1.00 47.66  ? 1   NAG I C6  1 
HETATM 7941 C  C7  . NAG E  3  .   ? 31.248  -10.519 18.937 1.00 47.19  ? 1   NAG I C7  1 
HETATM 7942 C  C8  . NAG E  3  .   ? 32.679  -10.103 18.757 1.00 48.83  ? 1   NAG I C8  1 
HETATM 7943 N  N2  . NAG E  3  .   ? 30.335  -9.620  18.574 1.00 47.43  ? 1   NAG I N2  1 
HETATM 7944 O  O3  . NAG E  3  .   ? 28.733  -10.744 16.495 1.00 51.52  ? 1   NAG I O3  1 
HETATM 7945 O  O4  . NAG E  3  .   ? 26.065  -9.590  16.280 1.00 58.68  ? 1   NAG I O4  1 
HETATM 7946 O  O5  . NAG E  3  .   ? 26.877  -9.226  19.835 1.00 46.73  ? 1   NAG I O5  1 
HETATM 7947 O  O6  . NAG E  3  .   ? 24.295  -10.316 19.186 1.00 40.88  ? 1   NAG I O6  1 
HETATM 7948 O  O7  . NAG E  3  .   ? 30.931  -11.621 19.386 1.00 39.53  ? 1   NAG I O7  1 
HETATM 7949 C  C1  . NAG E  3  .   ? 25.847  -10.683 15.444 1.00 63.78  ? 2   NAG I C1  1 
HETATM 7950 C  C2  . NAG E  3  .   ? 24.501  -10.568 14.739 1.00 64.33  ? 2   NAG I C2  1 
HETATM 7951 C  C3  . NAG E  3  .   ? 24.354  -11.704 13.738 1.00 71.80  ? 2   NAG I C3  1 
HETATM 7952 C  C4  . NAG E  3  .   ? 25.521  -11.673 12.768 1.00 80.92  ? 2   NAG I C4  1 
HETATM 7953 C  C5  . NAG E  3  .   ? 26.840  -11.763 13.534 1.00 74.73  ? 2   NAG I C5  1 
HETATM 7954 C  C6  . NAG E  3  .   ? 28.055  -11.592 12.660 1.00 67.70  ? 2   NAG I C6  1 
HETATM 7955 C  C7  . NAG E  3  .   ? 22.714  -9.355  15.805 1.00 48.30  ? 2   NAG I C7  1 
HETATM 7956 C  C8  . NAG E  3  .   ? 21.490  -9.380  16.677 1.00 43.57  ? 2   NAG I C8  1 
HETATM 7957 N  N2  . NAG E  3  .   ? 23.329  -10.519 15.591 1.00 55.61  ? 2   NAG I N2  1 
HETATM 7958 O  O3  . NAG E  3  .   ? 23.130  -11.568 13.035 1.00 63.86  ? 2   NAG I O3  1 
HETATM 7959 O  O4  . NAG E  3  .   ? 25.344  -12.760 11.856 1.00 90.46  ? 2   NAG I O4  1 
HETATM 7960 O  O5  . NAG E  3  .   ? 26.912  -10.693 14.496 1.00 70.59  ? 2   NAG I O5  1 
HETATM 7961 O  O6  . NAG E  3  .   ? 29.210  -11.932 13.395 1.00 71.55  ? 2   NAG I O6  1 
HETATM 7962 O  O7  . NAG E  3  .   ? 23.156  -8.319  15.315 1.00 43.87  ? 2   NAG I O7  1 
HETATM 7963 C  C1  . BMA E  3  .   ? 25.631  -12.420 10.536 1.00 98.23  ? 3   BMA I C1  1 
HETATM 7964 C  C2  . BMA E  3  .   ? 25.651  -13.710 9.736  1.00 95.56  ? 3   BMA I C2  1 
HETATM 7965 C  C3  . BMA E  3  .   ? 26.059  -13.378 8.315  1.00 104.11 ? 3   BMA I C3  1 
HETATM 7966 C  C4  . BMA E  3  .   ? 25.142  -12.325 7.709  1.00 101.96 ? 3   BMA I C4  1 
HETATM 7967 C  C5  . BMA E  3  .   ? 25.040  -11.081 8.620  1.00 102.68 ? 3   BMA I C5  1 
HETATM 7968 C  C6  . BMA E  3  .   ? 23.968  -10.096 8.186  1.00 100.35 ? 3   BMA I C6  1 
HETATM 7969 O  O2  . BMA E  3  .   ? 24.403  -14.389 9.848  1.00 71.68  ? 3   BMA I O2  1 
HETATM 7970 O  O3  . BMA E  3  .   ? 26.070  -14.574 7.534  1.00 112.18 ? 3   BMA I O3  1 
HETATM 7971 O  O4  . BMA E  3  .   ? 25.665  -11.942 6.436  1.00 96.47  ? 3   BMA I O4  1 
HETATM 7972 O  O5  . BMA E  3  .   ? 24.700  -11.503 9.961  1.00 108.05 ? 3   BMA I O5  1 
HETATM 7973 O  O6  . BMA E  3  .   ? 22.720  -10.762 7.943  1.00 98.51  ? 3   BMA I O6  1 
HETATM 7974 C  C1  . MAN E  3  .   ? 21.757  -10.091 7.167  1.00 102.01 ? 4   MAN I C1  1 
HETATM 7975 C  C2  . MAN E  3  .   ? 20.402  -10.615 7.632  1.00 101.39 ? 4   MAN I C2  1 
HETATM 7976 C  C3  . MAN E  3  .   ? 20.137  -12.062 7.170  1.00 105.75 ? 4   MAN I C3  1 
HETATM 7977 C  C4  . MAN E  3  .   ? 20.521  -12.318 5.714  1.00 107.61 ? 4   MAN I C4  1 
HETATM 7978 C  C5  . MAN E  3  .   ? 21.908  -11.741 5.399  1.00 124.38 ? 4   MAN I C5  1 
HETATM 7979 C  C6  . MAN E  3  .   ? 22.330  -11.863 3.937  1.00 137.81 ? 4   MAN I C6  1 
HETATM 7980 O  O2  . MAN E  3  .   ? 19.368  -9.712  7.254  1.00 91.46  ? 4   MAN I O2  1 
HETATM 7981 O  O3  . MAN E  3  .   ? 18.757  -12.379 7.364  1.00 107.36 ? 4   MAN I O3  1 
HETATM 7982 O  O4  . MAN E  3  .   ? 20.532  -13.729 5.493  1.00 88.22  ? 4   MAN I O4  1 
HETATM 7983 O  O5  . MAN E  3  .   ? 21.926  -10.329 5.765  1.00 115.02 ? 4   MAN I O5  1 
HETATM 7984 O  O6  . MAN E  3  .   ? 21.247  -11.667 2.982  1.00 159.04 ? 4   MAN I O6  1 
HETATM 7985 C  C1  . MAN E  3  .   ? 18.527  -13.620 7.959  1.00 112.20 ? 5   MAN I C1  1 
HETATM 7986 C  C2  . MAN E  3  .   ? 17.106  -14.006 7.649  1.00 110.58 ? 5   MAN I C2  1 
HETATM 7987 C  C3  . MAN E  3  .   ? 16.127  -13.078 8.355  1.00 112.58 ? 5   MAN I C3  1 
HETATM 7988 C  C4  . MAN E  3  .   ? 16.376  -13.117 9.859  1.00 111.60 ? 5   MAN I C4  1 
HETATM 7989 C  C5  . MAN E  3  .   ? 17.836  -12.729 10.134 1.00 115.07 ? 5   MAN I C5  1 
HETATM 7990 C  C6  . MAN E  3  .   ? 18.225  -12.826 11.598 1.00 104.95 ? 5   MAN I C6  1 
HETATM 7991 O  O2  . MAN E  3  .   ? 16.912  -15.364 8.032  1.00 107.07 ? 5   MAN I O2  1 
HETATM 7992 O  O3  . MAN E  3  .   ? 14.782  -13.455 8.040  1.00 112.00 ? 5   MAN I O3  1 
HETATM 7993 O  O4  . MAN E  3  .   ? 15.508  -12.212 10.536 1.00 90.05  ? 5   MAN I O4  1 
HETATM 7994 O  O5  . MAN E  3  .   ? 18.726  -13.616 9.388  1.00 119.90 ? 5   MAN I O5  1 
HETATM 7995 O  O6  . MAN E  3  .   ? 19.345  -11.983 11.890 1.00 88.27  ? 5   MAN I O6  1 
HETATM 7996 C  C1  . MAN E  3  .   ? 21.491  -12.112 1.667  1.00 156.87 ? 6   MAN I C1  1 
HETATM 7997 C  C2  . MAN E  3  .   ? 22.087  -10.941 0.869  1.00 156.50 ? 6   MAN I C2  1 
HETATM 7998 C  C3  . MAN E  3  .   ? 21.053  -9.887  0.459  1.00 156.38 ? 6   MAN I C3  1 
HETATM 7999 C  C4  . MAN E  3  .   ? 19.772  -10.522 -0.081 1.00 154.60 ? 6   MAN I C4  1 
HETATM 8000 C  C5  . MAN E  3  .   ? 19.249  -11.602 0.883  1.00 143.27 ? 6   MAN I C5  1 
HETATM 8001 C  C6  . MAN E  3  .   ? 18.004  -12.317 0.391  1.00 128.49 ? 6   MAN I C6  1 
HETATM 8002 O  O2  . MAN E  3  .   ? 22.770  -11.434 -0.280 1.00 147.59 ? 6   MAN I O2  1 
HETATM 8003 O  O3  . MAN E  3  .   ? 21.628  -9.025  -0.528 1.00 143.40 ? 6   MAN I O3  1 
HETATM 8004 O  O4  . MAN E  3  .   ? 18.783  -9.510  -0.257 1.00 155.31 ? 6   MAN I O4  1 
HETATM 8005 O  O5  . MAN E  3  .   ? 20.278  -12.605 1.057  1.00 142.72 ? 6   MAN I O5  1 
HETATM 8006 O  O6  . MAN E  3  .   ? 17.115  -12.645 1.481  1.00 112.16 ? 6   MAN I O6  1 
HETATM 8007 C  C1  . MAN E  3  .   ? 27.348  -15.056 7.240  1.00 133.50 ? 7   MAN I C1  1 
HETATM 8008 C  C2  . MAN E  3  .   ? 27.340  -15.423 5.763  1.00 133.88 ? 7   MAN I C2  1 
HETATM 8009 C  C3  . MAN E  3  .   ? 26.664  -16.771 5.474  1.00 130.10 ? 7   MAN I C3  1 
HETATM 8010 C  C4  . MAN E  3  .   ? 26.874  -17.851 6.550  1.00 124.87 ? 7   MAN I C4  1 
HETATM 8011 C  C5  . MAN E  3  .   ? 26.891  -17.316 7.977  1.00 117.82 ? 7   MAN I C5  1 
HETATM 8012 C  C6  . MAN E  3  .   ? 27.417  -18.342 8.954  1.00 105.45 ? 7   MAN I C6  1 
HETATM 8013 O  O2  . MAN E  3  .   ? 28.667  -15.383 5.234  1.00 121.37 ? 7   MAN I O2  1 
HETATM 8014 O  O3  . MAN E  3  .   ? 27.182  -17.230 4.219  1.00 128.86 ? 7   MAN I O3  1 
HETATM 8015 O  O4  . MAN E  3  .   ? 25.810  -18.803 6.506  1.00 111.61 ? 7   MAN I O4  1 
HETATM 8016 O  O5  . MAN E  3  .   ? 27.752  -16.169 8.063  1.00 134.69 ? 7   MAN I O5  1 
HETATM 8017 O  O6  . MAN E  3  .   ? 27.162  -17.953 10.292 1.00 100.43 ? 7   MAN I O6  1 
HETATM 8018 C  C1  . NAG F  2  .   ? 24.943  -11.140 69.299 1.00 56.96  ? 1   NAG Z C1  1 
HETATM 8019 C  C2  . NAG F  2  .   ? 25.753  -10.319 70.308 1.00 62.06  ? 1   NAG Z C2  1 
HETATM 8020 C  C3  . NAG F  2  .   ? 26.255  -11.114 71.511 1.00 67.12  ? 1   NAG Z C3  1 
HETATM 8021 C  C4  . NAG F  2  .   ? 25.187  -12.000 72.120 1.00 67.82  ? 1   NAG Z C4  1 
HETATM 8022 C  C5  . NAG F  2  .   ? 24.538  -12.853 71.027 1.00 69.78  ? 1   NAG Z C5  1 
HETATM 8023 C  C6  . NAG F  2  .   ? 23.374  -13.708 71.534 1.00 65.57  ? 1   NAG Z C6  1 
HETATM 8024 C  C7  . NAG F  2  .   ? 26.870  -8.588  69.076 1.00 70.34  ? 1   NAG Z C7  1 
HETATM 8025 C  C8  . NAG F  2  .   ? 26.222  -7.509  69.899 1.00 62.56  ? 1   NAG Z C8  1 
HETATM 8026 N  N2  . NAG F  2  .   ? 26.915  -9.785  69.641 1.00 67.98  ? 1   NAG Z N2  1 
HETATM 8027 O  O3  . NAG F  2  .   ? 26.703  -10.188 72.482 1.00 60.60  ? 1   NAG Z O3  1 
HETATM 8028 O  O4  . NAG F  2  .   ? 25.879  -12.788 73.113 1.00 70.50  ? 1   NAG Z O4  1 
HETATM 8029 O  O5  . NAG F  2  .   ? 24.024  -12.007 69.968 1.00 58.12  ? 1   NAG Z O5  1 
HETATM 8030 O  O6  . NAG F  2  .   ? 22.267  -12.946 72.065 1.00 57.73  ? 1   NAG Z O6  1 
HETATM 8031 O  O7  . NAG F  2  .   ? 27.315  -8.405  67.945 1.00 78.79  ? 1   NAG Z O7  1 
HETATM 8032 C  C1  . NAG F  2  .   ? 25.266  -12.918 74.363 1.00 68.52  ? 2   NAG Z C1  1 
HETATM 8033 C  C2  . NAG F  2  .   ? 25.672  -14.265 74.941 1.00 68.24  ? 2   NAG Z C2  1 
HETATM 8034 C  C3  . NAG F  2  .   ? 24.986  -14.480 76.286 1.00 73.94  ? 2   NAG Z C3  1 
HETATM 8035 C  C4  . NAG F  2  .   ? 25.251  -13.284 77.208 1.00 72.15  ? 2   NAG Z C4  1 
HETATM 8036 C  C5  . NAG F  2  .   ? 24.863  -11.978 76.515 1.00 65.04  ? 2   NAG Z C5  1 
HETATM 8037 C  C6  . NAG F  2  .   ? 25.134  -10.726 77.350 1.00 63.71  ? 2   NAG Z C6  1 
HETATM 8038 C  C7  . NAG F  2  .   ? 26.451  -15.906 73.279 1.00 73.35  ? 2   NAG Z C7  1 
HETATM 8039 C  C8  . NAG F  2  .   ? 27.860  -15.661 73.729 1.00 76.99  ? 2   NAG Z C8  1 
HETATM 8040 N  N2  . NAG F  2  .   ? 25.469  -15.383 74.037 1.00 73.16  ? 2   NAG Z N2  1 
HETATM 8041 O  O3  . NAG F  2  .   ? 25.509  -15.709 76.800 1.00 66.96  ? 2   NAG Z O3  1 
HETATM 8042 O  O4  . NAG F  2  .   ? 24.492  -13.381 78.426 1.00 79.03  ? 2   NAG Z O4  1 
HETATM 8043 O  O5  . NAG F  2  .   ? 25.623  -11.891 75.292 1.00 62.69  ? 2   NAG Z O5  1 
HETATM 8044 O  O6  . NAG F  2  .   ? 26.471  -10.649 77.847 1.00 63.99  ? 2   NAG Z O6  1 
HETATM 8045 O  O7  . NAG F  2  .   ? 26.226  -16.576 72.274 1.00 58.55  ? 2   NAG Z O7  1 
HETATM 8046 C  C1  . BMA F  2  .   ? 25.156  -13.829 79.567 1.00 79.03  ? 3   BMA Z C1  1 
HETATM 8047 C  C2  . BMA F  2  .   ? 24.299  -13.444 80.771 1.00 76.94  ? 3   BMA Z C2  1 
HETATM 8048 C  C3  . BMA F  2  .   ? 24.893  -14.036 82.039 1.00 83.60  ? 3   BMA Z C3  1 
HETATM 8049 C  C4  . BMA F  2  .   ? 25.144  -15.536 81.930 1.00 88.39  ? 3   BMA Z C4  1 
HETATM 8050 C  C5  . BMA F  2  .   ? 25.955  -15.874 80.660 1.00 85.14  ? 3   BMA Z C5  1 
HETATM 8051 C  C6  . BMA F  2  .   ? 25.978  -17.367 80.389 1.00 85.28  ? 3   BMA Z C6  1 
HETATM 8052 O  O2  . BMA F  2  .   ? 22.935  -13.848 80.608 1.00 64.52  ? 3   BMA Z O2  1 
HETATM 8053 O  O3  . BMA F  2  .   ? 23.977  -13.814 83.112 1.00 82.14  ? 3   BMA Z O3  1 
HETATM 8054 O  O4  . BMA F  2  .   ? 25.842  -15.981 83.115 1.00 76.58  ? 3   BMA Z O4  1 
HETATM 8055 O  O5  . BMA F  2  .   ? 25.355  -15.245 79.481 1.00 74.00  ? 3   BMA Z O5  1 
HETATM 8056 O  O6  . BMA F  2  .   ? 26.598  -17.656 79.112 1.00 88.18  ? 3   BMA Z O6  1 
HETATM 8057 C  C1  . MAN F  2  .   ? 24.514  -12.979 84.091 1.00 88.73  ? 4   MAN Z C1  1 
HETATM 8058 C  C2  . MAN F  2  .   ? 24.019  -13.551 85.418 1.00 84.35  ? 4   MAN Z C2  1 
HETATM 8059 C  C3  . MAN F  2  .   ? 22.463  -13.458 85.444 1.00 79.92  ? 4   MAN Z C3  1 
HETATM 8060 C  C4  . MAN F  2  .   ? 22.002  -11.997 85.232 1.00 75.64  ? 4   MAN Z C4  1 
HETATM 8061 C  C5  . MAN F  2  .   ? 22.650  -11.340 83.958 1.00 77.88  ? 4   MAN Z C5  1 
HETATM 8062 C  C6  . MAN F  2  .   ? 22.541  -9.814  83.916 1.00 73.95  ? 4   MAN Z C6  1 
HETATM 8063 O  O2  . MAN F  2  .   ? 24.732  -12.924 86.495 1.00 62.87  ? 4   MAN Z O2  1 
HETATM 8064 O  O3  . MAN F  2  .   ? 21.948  -14.007 86.669 1.00 78.81  ? 4   MAN Z O3  1 
HETATM 8065 O  O4  . MAN F  2  .   ? 20.570  -11.965 85.114 1.00 61.07  ? 4   MAN Z O4  1 
HETATM 8066 O  O5  . MAN F  2  .   ? 24.100  -11.618 83.891 1.00 83.41  ? 4   MAN Z O5  1 
HETATM 8067 O  O6  . MAN F  2  .   ? 21.382  -9.259  84.595 1.00 66.07  ? 4   MAN Z O6  1 
HETATM 8068 C  C1  . MAN F  2  .   ? 26.858  -19.022 78.854 1.00 88.81  ? 5   MAN Z C1  1 
HETATM 8069 C  C2  . MAN F  2  .   ? 27.927  -19.061 77.742 1.00 84.55  ? 5   MAN Z C2  1 
HETATM 8070 C  C3  . MAN F  2  .   ? 27.352  -18.746 76.319 1.00 88.50  ? 5   MAN Z C3  1 
HETATM 8071 C  C4  . MAN F  2  .   ? 26.117  -19.631 76.035 1.00 85.10  ? 5   MAN Z C4  1 
HETATM 8072 C  C5  . MAN F  2  .   ? 25.059  -19.482 77.178 1.00 87.59  ? 5   MAN Z C5  1 
HETATM 8073 C  C6  . MAN F  2  .   ? 23.800  -20.350 76.989 1.00 82.79  ? 5   MAN Z C6  1 
HETATM 8074 O  O2  . MAN F  2  .   ? 28.598  -20.324 77.746 1.00 73.51  ? 5   MAN Z O2  1 
HETATM 8075 O  O3  . MAN F  2  .   ? 28.353  -18.913 75.289 1.00 72.70  ? 5   MAN Z O3  1 
HETATM 8076 O  O4  . MAN F  2  .   ? 25.504  -19.267 74.787 1.00 83.74  ? 5   MAN Z O4  1 
HETATM 8077 O  O5  . MAN F  2  .   ? 25.682  -19.791 78.503 1.00 76.80  ? 5   MAN Z O5  1 
HETATM 8078 O  O6  . MAN F  2  .   ? 24.053  -21.768 76.873 1.00 76.07  ? 5   MAN Z O6  1 
HETATM 8079 C  C1  . NAG G  4  .   ? 15.304  -30.868 55.389 1.00 51.89  ? 1   NAG a C1  1 
HETATM 8080 C  C2  . NAG G  4  .   ? 14.301  -31.965 55.011 1.00 55.86  ? 1   NAG a C2  1 
HETATM 8081 C  C3  . NAG G  4  .   ? 14.737  -33.403 55.322 1.00 61.10  ? 1   NAG a C3  1 
HETATM 8082 C  C4  . NAG G  4  .   ? 16.115  -33.689 54.758 1.00 57.73  ? 1   NAG a C4  1 
HETATM 8083 C  C5  . NAG G  4  .   ? 17.046  -32.605 55.294 1.00 57.66  ? 1   NAG a C5  1 
HETATM 8084 C  C6  . NAG G  4  .   ? 18.424  -32.707 54.703 1.00 57.94  ? 1   NAG a C6  1 
HETATM 8085 C  C7  . NAG G  4  .   ? 12.115  -30.997 54.923 1.00 58.07  ? 1   NAG a C7  1 
HETATM 8086 C  C8  . NAG G  4  .   ? 10.778  -30.761 55.563 1.00 53.73  ? 1   NAG a C8  1 
HETATM 8087 N  N2  . NAG G  4  .   ? 13.019  -31.690 55.615 1.00 59.64  ? 1   NAG a N2  1 
HETATM 8088 O  O3  . NAG G  4  .   ? 13.777  -34.266 54.727 1.00 67.61  ? 1   NAG a O3  1 
HETATM 8089 O  O4  . NAG G  4  .   ? 16.537  -35.001 55.143 1.00 57.50  ? 1   NAG a O4  1 
HETATM 8090 O  O5  . NAG G  4  .   ? 16.591  -31.277 54.926 1.00 47.29  ? 1   NAG a O5  1 
HETATM 8091 O  O6  . NAG G  4  .   ? 18.403  -32.104 53.411 1.00 51.14  ? 1   NAG a O6  1 
HETATM 8092 O  O7  . NAG G  4  .   ? 12.370  -30.592 53.798 1.00 50.49  ? 1   NAG a O7  1 
HETATM 8093 C  C1  . NAG G  4  .   ? 16.273  -36.093 54.325 1.00 65.73  ? 2   NAG a C1  1 
HETATM 8094 C  C2  . NAG G  4  .   ? 17.310  -37.134 54.699 1.00 66.29  ? 2   NAG a C2  1 
HETATM 8095 C  C3  . NAG G  4  .   ? 16.947  -38.505 54.146 1.00 75.19  ? 2   NAG a C3  1 
HETATM 8096 C  C4  . NAG G  4  .   ? 15.507  -38.853 54.493 1.00 83.14  ? 2   NAG a C4  1 
HETATM 8097 C  C5  . NAG G  4  .   ? 14.571  -37.752 53.989 1.00 79.17  ? 2   NAG a C5  1 
HETATM 8098 C  C6  . NAG G  4  .   ? 13.106  -37.936 54.338 1.00 75.37  ? 2   NAG a C6  1 
HETATM 8099 C  C7  . NAG G  4  .   ? 19.485  -36.088 55.001 1.00 60.20  ? 2   NAG a C7  1 
HETATM 8100 C  C8  . NAG G  4  .   ? 20.755  -35.627 54.352 1.00 58.72  ? 2   NAG a C8  1 
HETATM 8101 N  N2  . NAG G  4  .   ? 18.588  -36.669 54.207 1.00 69.84  ? 2   NAG a N2  1 
HETATM 8102 O  O3  . NAG G  4  .   ? 17.846  -39.457 54.693 1.00 69.31  ? 2   NAG a O3  1 
HETATM 8103 O  O4  . NAG G  4  .   ? 15.202  -40.123 53.901 1.00 93.60  ? 2   NAG a O4  1 
HETATM 8104 O  O5  . NAG G  4  .   ? 14.952  -36.520 54.628 1.00 68.36  ? 2   NAG a O5  1 
HETATM 8105 O  O6  . NAG G  4  .   ? 12.846  -37.498 55.673 1.00 71.75  ? 2   NAG a O6  1 
HETATM 8106 O  O7  . NAG G  4  .   ? 19.282  -35.958 56.201 1.00 54.91  ? 2   NAG a O7  1 
HETATM 8107 C  C1  . BMA G  4  .   ? 14.589  -40.980 54.807 1.00 96.78  ? 3   BMA a C1  1 
HETATM 8108 C  C2  . BMA G  4  .   ? 13.697  -41.913 54.005 1.00 104.80 ? 3   BMA a C2  1 
HETATM 8109 C  C3  . BMA G  4  .   ? 12.949  -42.773 55.001 1.00 118.62 ? 3   BMA a C3  1 
HETATM 8110 C  C4  . BMA G  4  .   ? 13.948  -43.543 55.862 1.00 112.03 ? 3   BMA a C4  1 
HETATM 8111 C  C5  . BMA G  4  .   ? 14.883  -42.561 56.579 1.00 102.66 ? 3   BMA a C5  1 
HETATM 8112 C  C6  . BMA G  4  .   ? 15.979  -43.237 57.381 1.00 99.10  ? 3   BMA a C6  1 
HETATM 8113 O  O2  . BMA G  4  .   ? 14.456  -42.633 53.035 1.00 89.13  ? 3   BMA a O2  1 
HETATM 8114 O  O3  . BMA G  4  .   ? 11.972  -43.586 54.333 1.00 134.46 ? 3   BMA a O3  1 
HETATM 8115 O  O4  . BMA G  4  .   ? 13.272  -44.300 56.866 1.00 109.77 ? 3   BMA a O4  1 
HETATM 8116 O  O5  . BMA G  4  .   ? 15.519  -41.722 55.596 1.00 95.67  ? 3   BMA a O5  1 
HETATM 8117 O  O6  . BMA G  4  .   ? 17.002  -43.786 56.548 1.00 100.28 ? 3   BMA a O6  1 
HETATM 8118 C  C1  . MAN G  4  .   ? 18.118  -44.286 57.237 1.00 99.02  ? 4   MAN a C1  1 
HETATM 8119 C  C2  . MAN G  4  .   ? 19.248  -44.420 56.226 1.00 97.24  ? 4   MAN a C2  1 
HETATM 8120 C  C3  . MAN G  4  .   ? 18.966  -45.519 55.220 1.00 101.75 ? 4   MAN a C3  1 
HETATM 8121 C  C4  . MAN G  4  .   ? 18.632  -46.827 55.919 1.00 111.58 ? 4   MAN a C4  1 
HETATM 8122 C  C5  . MAN G  4  .   ? 17.503  -46.631 56.934 1.00 114.41 ? 4   MAN a C5  1 
HETATM 8123 C  C6  . MAN G  4  .   ? 17.244  -47.851 57.803 1.00 117.21 ? 4   MAN a C6  1 
HETATM 8124 O  O2  . MAN G  4  .   ? 20.470  -44.652 56.916 1.00 94.89  ? 4   MAN a O2  1 
HETATM 8125 O  O3  . MAN G  4  .   ? 20.103  -45.702 54.387 1.00 96.16  ? 4   MAN a O3  1 
HETATM 8126 O  O4  . MAN G  4  .   ? 18.236  -47.781 54.939 1.00 123.61 ? 4   MAN a O4  1 
HETATM 8127 O  O5  . MAN G  4  .   ? 17.849  -45.552 57.846 1.00 107.37 ? 4   MAN a O5  1 
HETATM 8128 O  O6  . MAN G  4  .   ? 16.880  -49.028 57.053 1.00 121.19 ? 4   MAN a O6  1 
HETATM 8129 C  C1  . MAN G  4  .   ? 19.966  -45.345 53.050 1.00 93.11  ? 5   MAN a C1  1 
HETATM 8130 C  C2  . MAN G  4  .   ? 21.034  -46.133 52.346 1.00 97.08  ? 5   MAN a C2  1 
HETATM 8131 C  C3  . MAN G  4  .   ? 22.414  -45.694 52.813 1.00 102.65 ? 5   MAN a C3  1 
HETATM 8132 C  C4  . MAN G  4  .   ? 22.586  -44.203 52.570 1.00 106.80 ? 5   MAN a C4  1 
HETATM 8133 C  C5  . MAN G  4  .   ? 21.452  -43.439 53.272 1.00 106.36 ? 5   MAN a C5  1 
HETATM 8134 C  C6  . MAN G  4  .   ? 21.485  -41.952 52.994 1.00 101.14 ? 5   MAN a C6  1 
HETATM 8135 O  O2  . MAN G  4  .   ? 20.880  -45.958 50.943 1.00 98.58  ? 5   MAN a O2  1 
HETATM 8136 O  O3  . MAN G  4  .   ? 23.433  -46.439 52.145 1.00 106.51 ? 5   MAN a O3  1 
HETATM 8137 O  O4  . MAN G  4  .   ? 23.854  -43.775 53.068 1.00 94.38  ? 5   MAN a O4  1 
HETATM 8138 O  O5  . MAN G  4  .   ? 20.161  -43.940 52.820 1.00 100.47 ? 5   MAN a O5  1 
HETATM 8139 O  O6  . MAN G  4  .   ? 20.475  -41.249 53.714 1.00 95.99  ? 5   MAN a O6  1 
HETATM 8140 C  C1  . MAN G  4  .   ? 12.273  -44.731 53.589 1.00 138.99 ? 6   MAN a C1  1 
HETATM 8141 C  C2  . MAN G  4  .   ? 11.957  -44.409 52.133 1.00 128.47 ? 6   MAN a C2  1 
HETATM 8142 C  C3  . MAN G  4  .   ? 10.471  -44.171 51.939 1.00 126.51 ? 6   MAN a C3  1 
HETATM 8143 C  C4  . MAN G  4  .   ? 9.627   -45.302 52.559 1.00 132.44 ? 6   MAN a C4  1 
HETATM 8144 C  C5  . MAN G  4  .   ? 10.056  -45.587 54.022 1.00 132.69 ? 6   MAN a C5  1 
HETATM 8145 C  C6  . MAN G  4  .   ? 9.394   -46.788 54.674 1.00 120.27 ? 6   MAN a C6  1 
HETATM 8146 O  O2  . MAN G  4  .   ? 12.414  -45.436 51.256 1.00 121.04 ? 6   MAN a O2  1 
HETATM 8147 O  O3  . MAN G  4  .   ? 10.249  -44.026 50.529 1.00 109.72 ? 6   MAN a O3  1 
HETATM 8148 O  O4  . MAN G  4  .   ? 8.250   -44.931 52.548 1.00 123.26 ? 6   MAN a O4  1 
HETATM 8149 O  O5  . MAN G  4  .   ? 11.479  -45.843 54.041 1.00 144.72 ? 6   MAN a O5  1 
HETATM 8150 O  O6  . MAN G  4  .   ? 8.076   -46.490 55.125 1.00 115.84 ? 6   MAN a O6  1 
HETATM 8151 C  C1  . NAG H  5  .   ? -15.442 19.508  32.263 1.00 84.92  ? 1   NAG q C1  1 
HETATM 8152 C  C2  . NAG H  5  .   ? -14.966 19.261  33.694 1.00 81.82  ? 1   NAG q C2  1 
HETATM 8153 C  C3  . NAG H  5  .   ? -15.031 20.571  34.466 1.00 81.49  ? 1   NAG q C3  1 
HETATM 8154 C  C4  . NAG H  5  .   ? -14.251 21.654  33.741 1.00 83.60  ? 1   NAG q C4  1 
HETATM 8155 C  C5  . NAG H  5  .   ? -14.701 21.767  32.285 1.00 84.95  ? 1   NAG q C5  1 
HETATM 8156 C  C6  . NAG H  5  .   ? -13.886 22.752  31.465 1.00 79.24  ? 1   NAG q C6  1 
HETATM 8157 C  C7  . NAG H  5  .   ? -16.962 18.123  34.572 1.00 79.36  ? 1   NAG q C7  1 
HETATM 8158 C  C8  . NAG H  5  .   ? -17.456 16.889  35.267 1.00 79.90  ? 1   NAG q C8  1 
HETATM 8159 N  N2  . NAG H  5  .   ? -15.639 18.216  34.440 1.00 77.40  ? 1   NAG q N2  1 
HETATM 8160 O  O3  . NAG H  5  .   ? -14.503 20.372  35.764 1.00 86.30  ? 1   NAG q O3  1 
HETATM 8161 O  O4  . NAG H  5  .   ? -14.514 22.879  34.414 1.00 86.18  ? 1   NAG q O4  1 
HETATM 8162 O  O5  . NAG H  5  .   ? -14.587 20.477  31.652 1.00 79.57  ? 1   NAG q O5  1 
HETATM 8163 O  O6  . NAG H  5  .   ? -12.477 22.666  31.730 1.00 65.12  ? 1   NAG q O6  1 
HETATM 8164 O  O7  . NAG H  5  .   ? -17.723 18.994  34.155 1.00 83.58  ? 1   NAG q O7  1 
HETATM 8165 C  C1  . NAG H  5  .   ? -13.433 23.553  34.933 1.00 87.44  ? 2   NAG q C1  1 
HETATM 8166 C  C2  . NAG H  5  .   ? -13.464 25.068  34.809 1.00 87.00  ? 2   NAG q C2  1 
HETATM 8167 C  C3  . NAG H  5  .   ? -12.132 25.629  35.298 1.00 91.53  ? 2   NAG q C3  1 
HETATM 8168 C  C4  . NAG H  5  .   ? -11.829 25.084  36.687 1.00 94.97  ? 2   NAG q C4  1 
HETATM 8169 C  C5  . NAG H  5  .   ? -11.694 23.571  36.584 1.00 92.48  ? 2   NAG q C5  1 
HETATM 8170 C  C6  . NAG H  5  .   ? -11.286 22.882  37.875 1.00 81.80  ? 2   NAG q C6  1 
HETATM 8171 C  C7  . NAG H  5  .   ? -14.920 26.145  33.109 1.00 80.66  ? 2   NAG q C7  1 
HETATM 8172 C  C8  . NAG H  5  .   ? -14.817 27.366  32.242 1.00 68.84  ? 2   NAG q C8  1 
HETATM 8173 N  N2  . NAG H  5  .   ? -13.766 25.568  33.478 1.00 83.47  ? 2   NAG q N2  1 
HETATM 8174 O  O3  . NAG H  5  .   ? -12.166 27.050  35.287 1.00 94.28  ? 2   NAG q O3  1 
HETATM 8175 O  O4  . NAG H  5  .   ? -10.625 25.652  37.196 1.00 104.20 ? 2   NAG q O4  1 
HETATM 8176 O  O5  . NAG H  5  .   ? -12.988 23.071  36.190 1.00 95.12  ? 2   NAG q O5  1 
HETATM 8177 O  O6  . NAG H  5  .   ? -12.349 22.807  38.805 1.00 78.71  ? 2   NAG q O6  1 
HETATM 8178 O  O7  . NAG H  5  .   ? -16.011 25.693  33.445 1.00 86.09  ? 2   NAG q O7  1 
HETATM 8179 C  C1  . BMA H  5  .   ? -10.779 26.653  38.152 1.00 128.56 ? 3   BMA q C1  1 
HETATM 8180 C  C2  . BMA H  5  .   ? -9.396  26.812  38.771 1.00 136.71 ? 3   BMA q C2  1 
HETATM 8181 C  C3  . BMA H  5  .   ? -9.231  28.115  39.538 1.00 140.22 ? 3   BMA q C3  1 
HETATM 8182 C  C4  . BMA H  5  .   ? -9.706  29.264  38.664 1.00 134.72 ? 3   BMA q C4  1 
HETATM 8183 C  C5  . BMA H  5  .   ? -11.184 29.029  38.373 1.00 133.12 ? 3   BMA q C5  1 
HETATM 8184 C  C6  . BMA H  5  .   ? -11.904 30.160  37.657 1.00 120.41 ? 3   BMA q C6  1 
HETATM 8185 O  O2  . BMA H  5  .   ? -8.422  26.719  37.736 1.00 137.45 ? 3   BMA q O2  1 
HETATM 8186 O  O3  . BMA H  5  .   ? -7.864  28.294  39.928 1.00 143.57 ? 3   BMA q O3  1 
HETATM 8187 O  O4  . BMA H  5  .   ? -9.493  30.510  39.328 1.00 134.81 ? 3   BMA q O4  1 
HETATM 8188 O  O5  . BMA H  5  .   ? -11.248 27.856  37.536 1.00 137.82 ? 3   BMA q O5  1 
HETATM 8189 O  O6  . BMA H  5  .   ? -11.163 30.681  36.557 1.00 110.65 ? 3   BMA q O6  1 
HETATM 8190 C  C1  . MAN H  5  .   ? -7.491  28.102  41.261 1.00 128.74 ? 4   MAN q C1  1 
HETATM 8191 C  C2  . MAN H  5  .   ? -6.457  29.194  41.546 1.00 120.04 ? 4   MAN q C2  1 
HETATM 8192 C  C3  . MAN H  5  .   ? -5.111  28.871  40.851 1.00 113.16 ? 4   MAN q C3  1 
HETATM 8193 C  C4  . MAN H  5  .   ? -4.623  27.455  41.186 1.00 111.55 ? 4   MAN q C4  1 
HETATM 8194 C  C5  . MAN H  5  .   ? -5.726  26.437  40.830 1.00 111.21 ? 4   MAN q C5  1 
HETATM 8195 C  C6  . MAN H  5  .   ? -5.394  24.975  41.133 1.00 97.19  ? 4   MAN q C6  1 
HETATM 8196 O  O2  . MAN H  5  .   ? -6.369  29.418  42.956 1.00 103.07 ? 4   MAN q O2  1 
HETATM 8197 O  O3  . MAN H  5  .   ? -4.125  29.857  41.191 1.00 101.25 ? 4   MAN q O3  1 
HETATM 8198 O  O4  . MAN H  5  .   ? -3.436  27.153  40.443 1.00 88.84  ? 4   MAN q O4  1 
HETATM 8199 O  O5  . MAN H  5  .   ? -6.956  26.782  41.549 1.00 125.97 ? 4   MAN q O5  1 
HETATM 8200 O  O6  . MAN H  5  .   ? -4.623  24.752  42.315 1.00 81.52  ? 4   MAN q O6  1 
HETATM 8201 C  C1  . NAG I  6  .   ? -17.607 28.229  7.828  1.00 86.65  ? 1   NAG s C1  1 
HETATM 8202 C  C2  . NAG I  6  .   ? -16.979 28.840  6.580  1.00 87.21  ? 1   NAG s C2  1 
HETATM 8203 C  C3  . NAG I  6  .   ? -17.198 30.351  6.558  1.00 94.74  ? 1   NAG s C3  1 
HETATM 8204 C  C4  . NAG I  6  .   ? -18.661 30.700  6.812  1.00 103.41 ? 1   NAG s C4  1 
HETATM 8205 C  C5  . NAG I  6  .   ? -19.133 30.022  8.092  1.00 101.56 ? 1   NAG s C5  1 
HETATM 8206 C  C6  . NAG I  6  .   ? -20.584 30.290  8.432  1.00 106.28 ? 1   NAG s C6  1 
HETATM 8207 C  C7  . NAG I  6  .   ? -14.977 27.776  5.616  1.00 82.59  ? 1   NAG s C7  1 
HETATM 8208 C  C8  . NAG I  6  .   ? -13.606 28.182  5.163  1.00 77.90  ? 1   NAG s C8  1 
HETATM 8209 N  N2  . NAG I  6  .   ? -15.557 28.579  6.508  1.00 86.99  ? 1   NAG s N2  1 
HETATM 8210 O  O3  . NAG I  6  .   ? -16.736 30.854  5.308  1.00 83.37  ? 1   NAG s O3  1 
HETATM 8211 O  O4  . NAG I  6  .   ? -18.830 32.110  6.947  1.00 118.01 ? 1   NAG s O4  1 
HETATM 8212 O  O5  . NAG I  6  .   ? -18.980 28.601  7.913  1.00 93.70  ? 1   NAG s O5  1 
HETATM 8213 O  O6  . NAG I  6  .   ? -21.461 29.368  7.791  1.00 106.86 ? 1   NAG s O6  1 
HETATM 8214 O  O7  . NAG I  6  .   ? -15.529 26.758  5.208  1.00 72.93  ? 1   NAG s O7  1 
HETATM 8215 C  C1  . NAG I  6  .   ? -19.663 32.668  5.978  1.00 136.43 ? 2   NAG s C1  1 
HETATM 8216 C  C2  . NAG I  6  .   ? -20.304 33.952  6.528  1.00 130.46 ? 2   NAG s C2  1 
HETATM 8217 C  C3  . NAG I  6  .   ? -20.356 35.137  5.554  1.00 131.78 ? 2   NAG s C3  1 
HETATM 8218 C  C4  . NAG I  6  .   ? -19.330 35.072  4.426  1.00 141.75 ? 2   NAG s C4  1 
HETATM 8219 C  C5  . NAG I  6  .   ? -19.447 33.682  3.818  1.00 135.79 ? 2   NAG s C5  1 
HETATM 8220 C  C6  . NAG I  6  .   ? -18.730 33.456  2.502  1.00 119.41 ? 2   NAG s C6  1 
HETATM 8221 C  C7  . NAG I  6  .   ? -22.198 33.980  8.144  1.00 114.30 ? 2   NAG s C7  1 
HETATM 8222 C  C8  . NAG I  6  .   ? -23.602 33.515  8.408  1.00 98.26  ? 2   NAG s C8  1 
HETATM 8223 N  N2  . NAG I  6  .   ? -21.661 33.652  6.960  1.00 126.10 ? 2   NAG s N2  1 
HETATM 8224 O  O3  . NAG I  6  .   ? -20.172 36.304  6.341  1.00 125.74 ? 2   NAG s O3  1 
HETATM 8225 O  O4  . NAG I  6  .   ? -19.570 36.091  3.427  1.00 157.43 ? 2   NAG s O4  1 
HETATM 8226 O  O5  . NAG I  6  .   ? -18.853 32.832  4.812  1.00 146.36 ? 2   NAG s O5  1 
HETATM 8227 O  O6  . NAG I  6  .   ? -17.374 33.876  2.546  1.00 108.41 ? 2   NAG s O6  1 
HETATM 8228 O  O7  . NAG I  6  .   ? -21.574 34.628  8.976  1.00 114.36 ? 2   NAG s O7  1 
HETATM 8229 C  C1  . BMA I  6  .   ? -19.815 37.434  3.737  1.00 166.03 ? 3   BMA s C1  1 
HETATM 8230 C  C2  . BMA I  6  .   ? -18.966 38.344  2.854  1.00 155.16 ? 3   BMA s C2  1 
HETATM 8231 C  C3  . BMA I  6  .   ? -19.271 39.804  3.137  1.00 147.26 ? 3   BMA s C3  1 
HETATM 8232 C  C4  . BMA I  6  .   ? -20.767 40.089  3.008  1.00 150.14 ? 3   BMA s C4  1 
HETATM 8233 C  C5  . BMA I  6  .   ? -21.581 39.131  3.893  1.00 154.07 ? 3   BMA s C5  1 
HETATM 8234 C  C6  . BMA I  6  .   ? -23.081 39.222  3.682  1.00 140.96 ? 3   BMA s C6  1 
HETATM 8235 O  O2  . BMA I  6  .   ? -19.158 38.055  1.470  1.00 140.53 ? 3   BMA s O2  1 
HETATM 8236 O  O3  . BMA I  6  .   ? -18.521 40.605  2.228  1.00 128.14 ? 3   BMA s O3  1 
HETATM 8237 O  O4  . BMA I  6  .   ? -21.043 41.441  3.396  1.00 140.05 ? 3   BMA s O4  1 
HETATM 8238 O  O5  . BMA I  6  .   ? -21.214 37.757  3.582  1.00 172.75 ? 3   BMA s O5  1 
HETATM 8239 O  O6  . BMA I  6  .   ? -23.576 40.555  3.774  1.00 127.52 ? 3   BMA s O6  1 
HETATM 8240 C  CHA . HEM J  7  .   ? 40.689  1.311   35.284 1.00 27.79  ? 401 HEM A CHA 1 
HETATM 8241 C  CHB . HEM J  7  .   ? 44.779  0.593   37.772 1.00 27.57  ? 401 HEM A CHB 1 
HETATM 8242 C  CHC . HEM J  7  .   ? 43.881  -4.184  37.774 1.00 31.79  ? 401 HEM A CHC 1 
HETATM 8243 C  CHD . HEM J  7  .   ? 39.812  -3.393  35.266 1.00 28.66  ? 401 HEM A CHD 1 
HETATM 8244 C  C1A . HEM J  7  .   ? 41.861  1.510   35.988 1.00 30.08  ? 401 HEM A C1A 1 
HETATM 8245 C  C2A . HEM J  7  .   ? 42.449  2.785   36.187 1.00 30.51  ? 401 HEM A C2A 1 
HETATM 8246 C  C3A . HEM J  7  .   ? 43.606  2.569   36.880 1.00 29.79  ? 401 HEM A C3A 1 
HETATM 8247 C  C4A . HEM J  7  .   ? 43.743  1.187   37.113 1.00 29.32  ? 401 HEM A C4A 1 
HETATM 8248 C  CMA . HEM J  7  .   ? 44.569  3.638   37.323 1.00 29.16  ? 401 HEM A CMA 1 
HETATM 8249 C  CAA . HEM J  7  .   ? 41.920  4.133   35.724 1.00 33.11  ? 401 HEM A CAA 1 
HETATM 8250 C  CBA . HEM J  7  .   ? 42.421  4.409   34.316 1.00 39.61  ? 401 HEM A CBA 1 
HETATM 8251 C  CGA . HEM J  7  .   ? 42.011  5.757   33.709 1.00 46.48  ? 401 HEM A CGA 1 
HETATM 8252 O  O1A . HEM J  7  .   ? 40.955  6.493   33.914 1.00 45.94  ? 401 HEM A O1A 1 
HETATM 8253 O  O2A . HEM J  7  .   ? 42.872  6.097   32.845 1.00 53.70  ? 401 HEM A O2A 1 
HETATM 8254 C  C1B . HEM J  7  .   ? 44.848  -0.790  37.936 1.00 29.93  ? 401 HEM A C1B 1 
HETATM 8255 C  C2B . HEM J  7  .   ? 45.953  -1.388  38.579 1.00 31.67  ? 401 HEM A C2B 1 
HETATM 8256 C  C3B . HEM J  7  .   ? 45.718  -2.704  38.650 1.00 31.13  ? 401 HEM A C3B 1 
HETATM 8257 C  C4B . HEM J  7  .   ? 44.449  -2.931  37.942 1.00 30.38  ? 401 HEM A C4B 1 
HETATM 8258 C  CMB . HEM J  7  .   ? 47.153  -0.714  39.194 1.00 32.23  ? 401 HEM A CMB 1 
HETATM 8259 C  CAB . HEM J  7  .   ? 46.728  -3.618  39.175 1.00 33.82  ? 401 HEM A CAB 1 
HETATM 8260 C  CBB . HEM J  7  .   ? 46.897  -4.801  38.592 1.00 37.76  ? 401 HEM A CBB 1 
HETATM 8261 C  C1C . HEM J  7  .   ? 42.688  -4.397  37.110 1.00 30.91  ? 401 HEM A C1C 1 
HETATM 8262 C  C2C . HEM J  7  .   ? 42.024  -5.632  36.992 1.00 30.46  ? 401 HEM A C2C 1 
HETATM 8263 C  C3C . HEM J  7  .   ? 40.873  -5.373  36.240 1.00 31.26  ? 401 HEM A C3C 1 
HETATM 8264 C  C4C . HEM J  7  .   ? 40.835  -3.990  35.986 1.00 30.56  ? 401 HEM A C4C 1 
HETATM 8265 C  CMC . HEM J  7  .   ? 42.527  -6.974  37.497 1.00 28.29  ? 401 HEM A CMC 1 
HETATM 8266 C  CAC . HEM J  7  .   ? 39.757  -6.242  35.847 1.00 35.61  ? 401 HEM A CAC 1 
HETATM 8267 C  CBC . HEM J  7  .   ? 39.464  -7.308  36.589 1.00 42.30  ? 401 HEM A CBC 1 
HETATM 8268 C  C1D . HEM J  7  .   ? 39.765  -2.034  35.061 1.00 27.79  ? 401 HEM A C1D 1 
HETATM 8269 C  C2D . HEM J  7  .   ? 38.704  -1.443  34.245 1.00 30.10  ? 401 HEM A C2D 1 
HETATM 8270 C  C3D . HEM J  7  .   ? 38.938  -0.129  34.263 1.00 30.32  ? 401 HEM A C3D 1 
HETATM 8271 C  C4D . HEM J  7  .   ? 40.157  0.055   35.068 1.00 28.26  ? 401 HEM A C4D 1 
HETATM 8272 C  CMD . HEM J  7  .   ? 37.554  -2.125  33.532 1.00 29.39  ? 401 HEM A CMD 1 
HETATM 8273 C  CAD . HEM J  7  .   ? 38.134  0.929   33.547 1.00 33.00  ? 401 HEM A CAD 1 
HETATM 8274 C  CBD . HEM J  7  .   ? 36.997  1.603   34.340 1.00 34.96  ? 401 HEM A CBD 1 
HETATM 8275 C  CGD . HEM J  7  .   ? 36.330  2.646   33.451 1.00 35.69  ? 401 HEM A CGD 1 
HETATM 8276 O  O1D . HEM J  7  .   ? 35.132  2.964   33.657 1.00 35.87  ? 401 HEM A O1D 1 
HETATM 8277 O  O2D . HEM J  7  .   ? 36.970  3.169   32.498 1.00 42.73  ? 401 HEM A O2D 1 
HETATM 8278 N  NA  . HEM J  7  .   ? 42.658  0.545   36.591 1.00 29.87  ? 401 HEM A NA  1 
HETATM 8279 N  NB  . HEM J  7  .   ? 43.983  -1.731  37.568 1.00 29.54  ? 401 HEM A NB  1 
HETATM 8280 N  NC  . HEM J  7  .   ? 41.973  -3.423  36.502 1.00 29.55  ? 401 HEM A NC  1 
HETATM 8281 N  ND  . HEM J  7  .   ? 40.618  -1.111  35.544 1.00 28.93  ? 401 HEM A ND  1 
HETATM 8282 FE FE  . HEM J  7  .   ? 42.189  -1.360  36.613 1.00 29.79  ? 401 HEM A FE  1 
HETATM 8283 C  C1  . GOL K  8  .   ? 40.719  -6.275  56.292 1.00 60.30  ? 402 GOL A C1  1 
HETATM 8284 O  O1  . GOL K  8  .   ? 41.541  -6.755  55.229 1.00 57.92  ? 402 GOL A O1  1 
HETATM 8285 C  C2  . GOL K  8  .   ? 40.870  -4.773  56.457 1.00 58.82  ? 402 GOL A C2  1 
HETATM 8286 O  O2  . GOL K  8  .   ? 40.211  -4.305  57.639 1.00 59.61  ? 402 GOL A O2  1 
HETATM 8287 C  C3  . GOL K  8  .   ? 42.305  -4.301  56.484 1.00 54.81  ? 402 GOL A C3  1 
HETATM 8288 O  O3  . GOL K  8  .   ? 42.331  -2.877  56.400 1.00 56.81  ? 402 GOL A O3  1 
HETATM 8289 C  C1  . GOL L  8  .   ? 37.811  -9.020  57.326 1.00 68.64  ? 403 GOL A C1  1 
HETATM 8290 O  O1  . GOL L  8  .   ? 36.622  -8.795  58.097 1.00 60.06  ? 403 GOL A O1  1 
HETATM 8291 C  C2  . GOL L  8  .   ? 37.511  -9.754  56.029 1.00 69.35  ? 403 GOL A C2  1 
HETATM 8292 O  O2  . GOL L  8  .   ? 38.678  -9.729  55.190 1.00 57.82  ? 403 GOL A O2  1 
HETATM 8293 C  C3  . GOL L  8  .   ? 36.955  -11.159 56.250 1.00 66.06  ? 403 GOL A C3  1 
HETATM 8294 O  O3  . GOL L  8  .   ? 36.748  -11.860 55.019 1.00 59.43  ? 403 GOL A O3  1 
HETATM 8295 C  C01 . C14 M  9  .   ? 50.937  -5.755  25.930 1.00 69.68  ? 404 C14 A C01 1 
HETATM 8296 C  C02 . C14 M  9  .   ? 50.524  -4.356  25.488 1.00 68.92  ? 404 C14 A C02 1 
HETATM 8297 C  C03 . C14 M  9  .   ? 49.875  -3.534  26.591 1.00 64.47  ? 404 C14 A C03 1 
HETATM 8298 C  C04 . C14 M  9  .   ? 50.487  -3.678  27.969 1.00 59.68  ? 404 C14 A C04 1 
HETATM 8299 C  C05 . C14 M  9  .   ? 49.804  -2.856  29.051 1.00 62.98  ? 404 C14 A C05 1 
HETATM 8300 C  C06 . C14 M  9  .   ? 50.423  -1.459  29.317 1.00 69.35  ? 404 C14 A C06 1 
HETATM 8301 C  C07 . C14 M  9  .   ? 49.948  -0.786  30.600 1.00 68.09  ? 404 C14 A C07 1 
HETATM 8302 C  C08 . C14 M  9  .   ? 48.936  -1.648  31.345 1.00 69.75  ? 404 C14 A C08 1 
HETATM 8303 C  C09 . C14 M  9  .   ? 48.129  -0.990  32.434 1.00 68.59  ? 404 C14 A C09 1 
HETATM 8304 C  C10 . C14 M  9  .   ? 46.661  -1.447  32.463 1.00 66.35  ? 404 C14 A C10 1 
HETATM 8305 C  C11 . C14 M  9  .   ? 45.957  -1.034  33.735 1.00 60.53  ? 404 C14 A C11 1 
HETATM 8306 C  C12 . C14 M  9  .   ? 44.912  -1.988  34.216 1.00 52.42  ? 404 C14 A C12 1 
HETATM 8307 C  C13 . C14 M  9  .   ? 43.594  -1.315  34.244 1.00 53.67  ? 404 C14 A C13 1 
HETATM 8308 C  C14 . C14 M  9  .   ? 43.365  -0.425  33.018 1.00 60.70  ? 404 C14 A C14 1 
HETATM 8309 N  N1  . EPE N  10 .   ? 60.757  1.181   19.568 1.00 76.99  ? 405 EPE A N1  1 
HETATM 8310 C  C2  . EPE N  10 .   ? 61.521  -0.004  20.053 1.00 73.49  ? 405 EPE A C2  1 
HETATM 8311 C  C3  . EPE N  10 .   ? 60.643  -1.238  20.093 1.00 69.81  ? 405 EPE A C3  1 
HETATM 8312 N  N4  . EPE N  10 .   ? 59.485  -1.018  20.977 1.00 68.23  ? 405 EPE A N4  1 
HETATM 8313 C  C5  . EPE N  10 .   ? 58.777  0.235   20.584 1.00 68.42  ? 405 EPE A C5  1 
HETATM 8314 C  C6  . EPE N  10 .   ? 59.671  1.455   20.523 1.00 65.37  ? 405 EPE A C6  1 
HETATM 8315 C  C7  . EPE N  10 .   ? 58.590  -2.197  21.021 1.00 67.65  ? 405 EPE A C7  1 
HETATM 8316 C  C8  . EPE N  10 .   ? 57.666  -2.421  19.800 1.00 67.59  ? 405 EPE A C8  1 
HETATM 8317 O  O8  . EPE N  10 .   ? 56.448  -3.087  20.129 1.00 58.53  ? 405 EPE A O8  1 
HETATM 8318 C  C9  . EPE N  10 .   ? 61.611  2.380   19.295 1.00 78.73  ? 405 EPE A C9  1 
HETATM 8319 C  C10 . EPE N  10 .   ? 61.249  3.196   18.035 1.00 71.39  ? 405 EPE A C10 1 
HETATM 8320 S  S   . EPE N  10 .   ? 61.593  4.952   18.243 1.00 73.30  ? 405 EPE A S   1 
HETATM 8321 O  O1S . EPE N  10 .   ? 62.964  5.063   18.706 1.00 65.95  ? 405 EPE A O1S 1 
HETATM 8322 O  O2S . EPE N  10 .   ? 60.589  5.451   19.163 1.00 60.47  ? 405 EPE A O2S 1 
HETATM 8323 O  O3S . EPE N  10 .   ? 61.562  5.564   16.723 1.00 56.00  ? 405 EPE A O3S 1 
HETATM 8324 C  C1  . GOL O  8  .   ? 27.312  -18.970 34.858 1.00 56.21  ? 406 GOL A C1  1 
HETATM 8325 O  O1  . GOL O  8  .   ? 26.872  -17.709 34.353 1.00 52.94  ? 406 GOL A O1  1 
HETATM 8326 C  C2  . GOL O  8  .   ? 26.482  -20.126 34.319 1.00 57.65  ? 406 GOL A C2  1 
HETATM 8327 O  O2  . GOL O  8  .   ? 26.290  -19.977 32.904 1.00 53.09  ? 406 GOL A O2  1 
HETATM 8328 C  C3  . GOL O  8  .   ? 27.101  -21.490 34.594 1.00 59.08  ? 406 GOL A C3  1 
HETATM 8329 O  O3  . GOL O  8  .   ? 26.507  -22.161 35.707 1.00 55.40  ? 406 GOL A O3  1 
HETATM 8330 S  S   . SO4 P  11 .   ? 26.241  8.427   19.388 1.00 70.72  ? 407 SO4 A S   1 
HETATM 8331 O  O1  . SO4 P  11 .   ? 27.536  8.205   18.700 1.00 54.32  ? 407 SO4 A O1  1 
HETATM 8332 O  O2  . SO4 P  11 .   ? 25.123  8.458   18.448 1.00 62.65  ? 407 SO4 A O2  1 
HETATM 8333 O  O3  . SO4 P  11 .   ? 26.003  7.359   20.341 1.00 77.47  ? 407 SO4 A O3  1 
HETATM 8334 O  O4  . SO4 P  11 .   ? 26.262  9.678   20.133 1.00 71.12  ? 407 SO4 A O4  1 
HETATM 8335 S  S   . SO4 Q  11 .   ? 29.094  1.204   50.321 1.00 75.11  ? 408 SO4 A S   1 
HETATM 8336 O  O1  . SO4 Q  11 .   ? 30.225  1.191   49.369 1.00 69.13  ? 408 SO4 A O1  1 
HETATM 8337 O  O2  . SO4 Q  11 .   ? 27.865  1.333   49.568 1.00 79.02  ? 408 SO4 A O2  1 
HETATM 8338 O  O3  . SO4 Q  11 .   ? 29.061  -0.025  51.080 1.00 78.96  ? 408 SO4 A O3  1 
HETATM 8339 O  O4  . SO4 Q  11 .   ? 29.183  2.316   51.268 1.00 74.21  ? 408 SO4 A O4  1 
HETATM 8340 MG MG  . MG  R  12 .   ? 39.254  8.548   33.725 1.00 44.29  ? 409 MG  A MG  1 
HETATM 8341 C  CHA . HEM S  7  .   ? 10.762  -9.481  61.576 1.00 27.61  ? 401 HEM B CHA 1 
HETATM 8342 C  CHB . HEM S  7  .   ? 7.570   -5.989  60.891 1.00 31.20  ? 401 HEM B CHB 1 
HETATM 8343 C  CHC . HEM S  7  .   ? 6.815   -7.620  56.391 1.00 31.27  ? 401 HEM B CHC 1 
HETATM 8344 C  CHD . HEM S  7  .   ? 10.174  -10.967 57.041 1.00 32.86  ? 401 HEM B CHD 1 
HETATM 8345 C  C1A . HEM S  7  .   ? 9.962   -8.396  61.732 1.00 29.72  ? 401 HEM B C1A 1 
HETATM 8346 C  C2A . HEM S  7  .   ? 9.945   -7.630  62.914 1.00 34.04  ? 401 HEM B C2A 1 
HETATM 8347 C  C3A . HEM S  7  .   ? 9.039   -6.649  62.725 1.00 34.06  ? 401 HEM B C3A 1 
HETATM 8348 C  C4A . HEM S  7  .   ? 8.507   -6.803  61.434 1.00 31.30  ? 401 HEM B C4A 1 
HETATM 8349 C  CMA . HEM S  7  .   ? 8.672   -5.597  63.733 1.00 34.51  ? 401 HEM B CMA 1 
HETATM 8350 C  CAA . HEM S  7  .   ? 10.758  -7.841  64.165 1.00 36.45  ? 401 HEM B CAA 1 
HETATM 8351 C  CBA . HEM S  7  .   ? 10.185  -9.010  64.944 1.00 43.36  ? 401 HEM B CBA 1 
HETATM 8352 C  CGA . HEM S  7  .   ? 10.808  -9.172  66.328 1.00 48.37  ? 401 HEM B CGA 1 
HETATM 8353 O  O1A . HEM S  7  .   ? 12.063  -9.290  66.671 1.00 47.77  ? 401 HEM B O1A 1 
HETATM 8354 O  O2A . HEM S  7  .   ? 9.903   -9.258  67.187 1.00 52.77  ? 401 HEM B O2A 1 
HETATM 8355 C  C1B . HEM S  7  .   ? 7.072   -6.178  59.594 1.00 32.84  ? 401 HEM B C1B 1 
HETATM 8356 C  C2B . HEM S  7  .   ? 6.047   -5.335  59.069 1.00 32.03  ? 401 HEM B C2B 1 
HETATM 8357 C  C3B . HEM S  7  .   ? 5.833   -5.726  57.797 1.00 31.45  ? 401 HEM B C3B 1 
HETATM 8358 C  C4B . HEM S  7  .   ? 6.728   -6.906  57.575 1.00 30.86  ? 401 HEM B C4B 1 
HETATM 8359 C  CMB . HEM S  7  .   ? 5.362   -4.154  59.738 1.00 31.89  ? 401 HEM B CMB 1 
HETATM 8360 C  CAB . HEM S  7  .   ? 4.761   -5.125  56.981 1.00 35.28  ? 401 HEM B CAB 1 
HETATM 8361 C  CBB . HEM S  7  .   ? 4.125   -5.862  56.054 1.00 39.92  ? 401 HEM B CBB 1 
HETATM 8362 C  C1C . HEM S  7  .   ? 7.678   -8.658  56.138 1.00 31.41  ? 401 HEM B C1C 1 
HETATM 8363 C  C2C . HEM S  7  .   ? 7.837   -9.344  54.923 1.00 30.69  ? 401 HEM B C2C 1 
HETATM 8364 C  C3C . HEM S  7  .   ? 8.784   -10.327 55.156 1.00 31.15  ? 401 HEM B C3C 1 
HETATM 8365 C  C4C . HEM S  7  .   ? 9.223   -10.170 56.477 1.00 31.12  ? 401 HEM B C4C 1 
HETATM 8366 C  CMC . HEM S  7  .   ? 7.058   -9.101  53.660 1.00 32.60  ? 401 HEM B CMC 1 
HETATM 8367 C  CAC . HEM S  7  .   ? 9.420   -11.271 54.245 1.00 33.69  ? 401 HEM B CAC 1 
HETATM 8368 C  CBC . HEM S  7  .   ? 9.523   -10.931 52.972 1.00 39.78  ? 401 HEM B CBC 1 
HETATM 8369 C  C1D . HEM S  7  .   ? 10.581  -10.811 58.363 1.00 31.85  ? 401 HEM B C1D 1 
HETATM 8370 C  C2D . HEM S  7  .   ? 11.546  -11.727 58.974 1.00 30.80  ? 401 HEM B C2D 1 
HETATM 8371 C  C3D . HEM S  7  .   ? 11.713  -11.322 60.227 1.00 29.28  ? 401 HEM B C3D 1 
HETATM 8372 C  C4D . HEM S  7  .   ? 10.834  -10.161 60.385 1.00 29.11  ? 401 HEM B C4D 1 
HETATM 8373 C  CMD . HEM S  7  .   ? 12.224  -12.900 58.328 1.00 32.79  ? 401 HEM B CMD 1 
HETATM 8374 C  CAD . HEM S  7  .   ? 12.614  -11.970 61.226 1.00 29.65  ? 401 HEM B CAD 1 
HETATM 8375 C  CBD . HEM S  7  .   ? 13.998  -11.342 61.261 1.00 32.98  ? 401 HEM B CBD 1 
HETATM 8376 C  CGD . HEM S  7  .   ? 14.847  -12.003 62.332 1.00 34.35  ? 401 HEM B CGD 1 
HETATM 8377 O  O1D . HEM S  7  .   ? 14.332  -12.366 63.417 1.00 38.10  ? 401 HEM B O1D 1 
HETATM 8378 O  O2D . HEM S  7  .   ? 16.062  -12.160 62.126 1.00 38.03  ? 401 HEM B O2D 1 
HETATM 8379 N  NA  . HEM S  7  .   ? 9.069   -7.869  60.820 1.00 31.22  ? 401 HEM B NA  1 
HETATM 8380 N  NB  . HEM S  7  .   ? 7.432   -7.092  58.683 1.00 32.33  ? 401 HEM B NB  1 
HETATM 8381 N  NC  . HEM S  7  .   ? 8.530   -9.159  57.050 1.00 30.72  ? 401 HEM B NC  1 
HETATM 8382 N  ND  . HEM S  7  .   ? 10.168  -9.886  59.235 1.00 31.86  ? 401 HEM B ND  1 
HETATM 8383 FE FE  . HEM S  7  .   ? 8.900   -8.515  58.949 1.00 31.05  ? 401 HEM B FE  1 
HETATM 8384 N  N1  . EPE T  10 .   ? -11.173 -15.904 71.372 1.00 112.48 ? 402 EPE B N1  1 
HETATM 8385 C  C2  . EPE T  10 .   ? -9.959  -16.643 71.010 1.00 103.38 ? 402 EPE B C2  1 
HETATM 8386 C  C3  . EPE T  10 .   ? -9.853  -16.796 69.514 1.00 103.84 ? 402 EPE B C3  1 
HETATM 8387 N  N4  . EPE T  10 .   ? -10.993 -17.531 68.951 1.00 106.08 ? 402 EPE B N4  1 
HETATM 8388 C  C5  . EPE T  10 .   ? -12.226 -16.818 69.335 1.00 111.32 ? 402 EPE B C5  1 
HETATM 8389 C  C6  . EPE T  10 .   ? -12.329 -16.644 70.834 1.00 114.76 ? 402 EPE B C6  1 
HETATM 8390 C  C7  . EPE T  10 .   ? -10.905 -17.680 67.485 1.00 106.39 ? 402 EPE B C7  1 
HETATM 8391 C  C8  . EPE T  10 .   ? -9.514  -17.620 66.837 1.00 105.60 ? 402 EPE B C8  1 
HETATM 8392 O  O8  . EPE T  10 .   ? -8.864  -18.875 66.705 1.00 92.86  ? 402 EPE B O8  1 
HETATM 8393 C  C9  . EPE T  10 .   ? -11.269 -15.694 72.835 1.00 117.63 ? 402 EPE B C9  1 
HETATM 8394 C  C10 . EPE T  10 .   ? -11.070 -16.971 73.658 1.00 119.04 ? 402 EPE B C10 1 
HETATM 8395 S  S   . EPE T  10 .   ? -11.232 -16.743 75.408 1.00 111.76 ? 402 EPE B S   1 
HETATM 8396 O  O1S . EPE T  10 .   ? -10.310 -15.702 75.775 1.00 97.78  ? 402 EPE B O1S 1 
HETATM 8397 O  O2S . EPE T  10 .   ? -11.141 -18.048 76.005 1.00 90.96  ? 402 EPE B O2S 1 
HETATM 8398 O  O3S . EPE T  10 .   ? -12.690 -16.237 75.536 1.00 110.22 ? 402 EPE B O3S 1 
HETATM 8399 N  N1  . EPE U  10 .   ? 7.468   1.958   43.293 1.00 118.49 ? 403 EPE B N1  1 
HETATM 8400 C  C2  . EPE U  10 .   ? 7.892   1.637   41.923 1.00 119.57 ? 403 EPE B C2  1 
HETATM 8401 C  C3  . EPE U  10 .   ? 7.018   0.558   41.327 1.00 121.10 ? 403 EPE B C3  1 
HETATM 8402 N  N4  . EPE U  10 .   ? 7.044   -0.669  42.147 1.00 120.12 ? 403 EPE B N4  1 
HETATM 8403 C  C5  . EPE U  10 .   ? 6.613   -0.342  43.516 1.00 120.01 ? 403 EPE B C5  1 
HETATM 8404 C  C6  . EPE U  10 .   ? 7.506   0.724   44.101 1.00 124.18 ? 403 EPE B C6  1 
HETATM 8405 C  C7  . EPE U  10 .   ? 6.258   -1.761  41.551 1.00 108.14 ? 403 EPE B C7  1 
HETATM 8406 C  C8  . EPE U  10 .   ? 6.961   -2.484  40.415 1.00 99.69  ? 403 EPE B C8  1 
HETATM 8407 O  O8  . EPE U  10 .   ? 6.259   -3.612  39.941 1.00 94.30  ? 403 EPE B O8  1 
HETATM 8408 C  C9  . EPE U  10 .   ? 8.287   3.039   43.881 1.00 121.89 ? 403 EPE B C9  1 
HETATM 8409 C  C10 . EPE U  10 .   ? 7.899   3.388   45.317 1.00 138.58 ? 403 EPE B C10 1 
HETATM 8410 S  S   . EPE U  10 .   ? 8.812   4.730   46.029 1.00 149.51 ? 403 EPE B S   1 
HETATM 8411 O  O1S . EPE U  10 .   ? 10.152  4.267   46.249 1.00 142.98 ? 403 EPE B O1S 1 
HETATM 8412 O  O2S . EPE U  10 .   ? 8.052   5.185   47.157 1.00 163.79 ? 403 EPE B O2S 1 
HETATM 8413 O  O3S . EPE U  10 .   ? 8.800   5.800   44.914 1.00 156.72 ? 403 EPE B O3S 1 
HETATM 8414 N  N1  . EPE V  10 .   ? 22.246  -28.963 70.488 1.00 80.72  ? 404 EPE B N1  1 
HETATM 8415 C  C2  . EPE V  10 .   ? 21.144  -28.156 71.065 1.00 76.20  ? 404 EPE B C2  1 
HETATM 8416 C  C3  . EPE V  10 .   ? 21.228  -26.728 70.579 1.00 66.73  ? 404 EPE B C3  1 
HETATM 8417 N  N4  . EPE V  10 .   ? 22.544  -26.118 70.893 1.00 60.69  ? 404 EPE B N4  1 
HETATM 8418 C  C5  . EPE V  10 .   ? 23.621  -26.931 70.318 1.00 62.68  ? 404 EPE B C5  1 
HETATM 8419 C  C6  . EPE V  10 .   ? 23.550  -28.345 70.832 1.00 73.25  ? 404 EPE B C6  1 
HETATM 8420 C  C7  . EPE V  10 .   ? 22.601  -24.786 70.280 1.00 71.81  ? 404 EPE B C7  1 
HETATM 8421 C  C8  . EPE V  10 .   ? 23.914  -24.009 70.420 1.00 69.07  ? 404 EPE B C8  1 
HETATM 8422 O  O8  . EPE V  10 .   ? 23.967  -22.891 69.537 1.00 59.82  ? 404 EPE B O8  1 
HETATM 8423 C  C9  . EPE V  10 .   ? 22.183  -30.411 70.863 1.00 77.90  ? 404 EPE B C9  1 
HETATM 8424 C  C10 . EPE V  10 .   ? 22.717  -31.366 69.777 1.00 73.04  ? 404 EPE B C10 1 
HETATM 8425 S  S   . EPE V  10 .   ? 21.929  -32.975 69.873 1.00 83.91  ? 404 EPE B S   1 
HETATM 8426 O  O1S . EPE V  10 .   ? 20.484  -32.774 69.816 1.00 65.99  ? 404 EPE B O1S 1 
HETATM 8427 O  O2S . EPE V  10 .   ? 22.474  -33.601 71.074 1.00 74.81  ? 404 EPE B O2S 1 
HETATM 8428 O  O3S . EPE V  10 .   ? 22.427  -33.619 68.456 1.00 64.84  ? 404 EPE B O3S 1 
HETATM 8429 C  C1  . GOL W  8  .   ? 13.908  8.634   49.450 1.00 51.77  ? 405 GOL B C1  1 
HETATM 8430 O  O1  . GOL W  8  .   ? 12.668  8.689   50.149 1.00 55.71  ? 405 GOL B O1  1 
HETATM 8431 C  C2  . GOL W  8  .   ? 13.685  8.467   47.958 1.00 55.42  ? 405 GOL B C2  1 
HETATM 8432 O  O2  . GOL W  8  .   ? 14.935  8.206   47.297 1.00 55.78  ? 405 GOL B O2  1 
HETATM 8433 C  C3  . GOL W  8  .   ? 12.653  7.394   47.640 1.00 51.43  ? 405 GOL B C3  1 
HETATM 8434 O  O3  . GOL W  8  .   ? 12.588  7.092   46.248 1.00 54.80  ? 405 GOL B O3  1 
HETATM 8435 C  C01 . C14 X  9  .   ? 7.113   -10.926 61.017 1.00 55.30  ? 406 C14 B C01 1 
HETATM 8436 C  C02 . C14 X  9  .   ? 6.334   -9.994  60.145 1.00 49.95  ? 406 C14 B C02 1 
HETATM 8437 C  C03 . C14 X  9  .   ? 5.171   -9.497  60.928 1.00 61.31  ? 406 C14 B C03 1 
HETATM 8438 C  C04 . C14 X  9  .   ? 3.979   -10.439 61.171 1.00 65.56  ? 406 C14 B C04 1 
HETATM 8439 C  C05 . C14 X  9  .   ? 2.826   -9.784  61.988 1.00 70.71  ? 406 C14 B C05 1 
HETATM 8440 C  C06 . C14 X  9  .   ? 1.490   -10.519 62.014 1.00 64.75  ? 406 C14 B C06 1 
HETATM 8441 C  C07 . C14 X  9  .   ? 1.554   -11.910 62.614 1.00 64.24  ? 406 C14 B C07 1 
HETATM 8442 C  C08 . C14 X  9  .   ? 0.285   -12.721 62.484 1.00 62.86  ? 406 C14 B C08 1 
HETATM 8443 C  C09 . C14 X  9  .   ? -0.273  -12.784 61.052 1.00 68.09  ? 406 C14 B C09 1 
HETATM 8444 C  C10 . C14 X  9  .   ? -1.509  -13.632 60.917 1.00 66.96  ? 406 C14 B C10 1 
HETATM 8445 C  C11 . C14 X  9  .   ? -1.358  -15.061 61.406 1.00 60.44  ? 406 C14 B C11 1 
HETATM 8446 C  C12 . C14 X  9  .   ? -2.581  -15.904 61.090 1.00 67.71  ? 406 C14 B C12 1 
HETATM 8447 C  C13 . C14 X  9  .   ? -2.431  -17.410 61.271 1.00 72.15  ? 406 C14 B C13 1 
HETATM 8448 C  C14 . C14 X  9  .   ? -1.641  -17.827 62.516 1.00 70.22  ? 406 C14 B C14 1 
HETATM 8449 S  S   . SO4 Y  11 .   ? 25.134  0.288   52.959 1.00 70.96  ? 407 SO4 B S   1 
HETATM 8450 O  O1  . SO4 Y  11 .   ? 26.025  0.062   51.831 1.00 66.80  ? 407 SO4 B O1  1 
HETATM 8451 O  O2  . SO4 Y  11 .   ? 23.815  -0.357  52.714 1.00 55.61  ? 407 SO4 B O2  1 
HETATM 8452 O  O3  . SO4 Y  11 .   ? 25.727  -0.287  54.173 1.00 72.74  ? 407 SO4 B O3  1 
HETATM 8453 O  O4  . SO4 Y  11 .   ? 25.005  1.742   53.138 1.00 64.92  ? 407 SO4 B O4  1 
HETATM 8454 S  S   . SO4 Z  11 .   ? 16.843  3.137   68.434 1.00 96.38  ? 408 SO4 B S   1 
HETATM 8455 O  O1  . SO4 Z  11 .   ? 17.748  3.280   67.277 1.00 74.08  ? 408 SO4 B O1  1 
HETATM 8456 O  O2  . SO4 Z  11 .   ? 15.628  3.970   68.226 1.00 68.87  ? 408 SO4 B O2  1 
HETATM 8457 O  O3  . SO4 Z  11 .   ? 16.481  1.720   68.617 1.00 88.99  ? 408 SO4 B O3  1 
HETATM 8458 O  O4  . SO4 Z  11 .   ? 17.546  3.573   69.652 1.00 79.41  ? 408 SO4 B O4  1 
HETATM 8459 MG MG  . MG  AA 12 .   ? 13.920  -9.467  68.220 1.00 48.24  ? 409 MG  B MG  1 
HETATM 8460 C  CHA . HEM BA 7  .   ? -8.081  11.856  20.027 1.00 41.68  ? 401 HEM C CHA 1 
HETATM 8461 C  CHB . HEM BA 7  .   ? -5.513  7.831   19.635 1.00 41.12  ? 401 HEM C CHB 1 
HETATM 8462 C  CHC . HEM BA 7  .   ? -7.356  7.183   15.225 1.00 41.09  ? 401 HEM C CHC 1 
HETATM 8463 C  CHD . HEM BA 7  .   ? -10.298 10.911  15.858 1.00 40.80  ? 401 HEM C CHD 1 
HETATM 8464 C  C1A . HEM BA 7  .   ? -7.235  10.812  20.284 1.00 40.37  ? 401 HEM C C1A 1 
HETATM 8465 C  C2A . HEM BA 7  .   ? -6.501  10.673  21.477 1.00 44.63  ? 401 HEM C C2A 1 
HETATM 8466 C  C3A . HEM BA 7  .   ? -5.772  9.540   21.362 1.00 42.80  ? 401 HEM C C3A 1 
HETATM 8467 C  C4A . HEM BA 7  .   ? -6.074  8.980   20.116 1.00 38.52  ? 401 HEM C C4A 1 
HETATM 8468 C  CMA . HEM BA 7  .   ? -4.825  8.976   22.400 1.00 42.37  ? 401 HEM C CMA 1 
HETATM 8469 C  CAA . HEM BA 7  .   ? -6.491  11.606  22.671 1.00 50.77  ? 401 HEM C CAA 1 
HETATM 8470 C  CBA . HEM BA 7  .   ? -5.468  12.742  22.487 1.00 60.02  ? 401 HEM C CBA 1 
HETATM 8471 C  CGA . HEM BA 7  .   ? -5.484  13.793  23.619 1.00 66.40  ? 401 HEM C CGA 1 
HETATM 8472 O  O1A . HEM BA 7  .   ? -4.387  14.366  23.790 1.00 76.42  ? 401 HEM C O1A 1 
HETATM 8473 O  O2A . HEM BA 7  .   ? -6.453  14.146  24.382 1.00 60.26  ? 401 HEM C O2A 1 
HETATM 8474 C  C1B . HEM BA 7  .   ? -5.782  7.342   18.355 1.00 38.81  ? 401 HEM C C1B 1 
HETATM 8475 C  C2B . HEM BA 7  .   ? -5.121  6.188   17.864 1.00 35.19  ? 401 HEM C C2B 1 
HETATM 8476 C  C3B . HEM BA 7  .   ? -5.649  5.969   16.639 1.00 41.18  ? 401 HEM C C3B 1 
HETATM 8477 C  C4B . HEM BA 7  .   ? -6.619  7.069   16.386 1.00 40.00  ? 401 HEM C C4B 1 
HETATM 8478 C  CMB . HEM BA 7  .   ? -4.092  5.310   18.538 1.00 30.58  ? 401 HEM C CMB 1 
HETATM 8479 C  CAB . HEM BA 7  .   ? -5.169  4.912   15.733 1.00 45.05  ? 401 HEM C CAB 1 
HETATM 8480 C  CBB . HEM BA 7  .   ? -5.262  5.079   14.415 1.00 49.64  ? 401 HEM C CBB 1 
HETATM 8481 C  C1C . HEM BA 7  .   ? -8.358  8.105   15.012 1.00 42.53  ? 401 HEM C C1C 1 
HETATM 8482 C  C2C . HEM BA 7  .   ? -9.277  8.072   13.943 1.00 43.61  ? 401 HEM C C2C 1 
HETATM 8483 C  C3C . HEM BA 7  .   ? -10.109 9.170   14.134 1.00 45.67  ? 401 HEM C C3C 1 
HETATM 8484 C  C4C . HEM BA 7  .   ? -9.697  9.810   15.335 1.00 41.46  ? 401 HEM C C4C 1 
HETATM 8485 C  CMC . HEM BA 7  .   ? -9.284  7.051   12.816 1.00 42.18  ? 401 HEM C CMC 1 
HETATM 8486 C  CAC . HEM BA 7  .   ? -11.282 9.599   13.354 1.00 46.83  ? 401 HEM C CAC 1 
HETATM 8487 C  CBC . HEM BA 7  .   ? -11.855 8.770   12.490 1.00 54.24  ? 401 HEM C CBC 1 
HETATM 8488 C  C1D . HEM BA 7  .   ? -9.892  11.474  17.064 1.00 41.66  ? 401 HEM C C1D 1 
HETATM 8489 C  C2D . HEM BA 7  .   ? -10.468 12.752  17.561 1.00 41.15  ? 401 HEM C C2D 1 
HETATM 8490 C  C3D . HEM BA 7  .   ? -9.849  13.016  18.709 1.00 42.94  ? 401 HEM C C3D 1 
HETATM 8491 C  C4D . HEM BA 7  .   ? -8.890  11.904  18.907 1.00 41.86  ? 401 HEM C C4D 1 
HETATM 8492 C  CMD . HEM BA 7  .   ? -11.526 13.638  16.938 1.00 41.73  ? 401 HEM C CMD 1 
HETATM 8493 C  CAD . HEM BA 7  .   ? -10.065 14.246  19.573 1.00 44.62  ? 401 HEM C CAD 1 
HETATM 8494 C  CBD . HEM BA 7  .   ? -11.113 14.099  20.671 1.00 46.35  ? 401 HEM C CBD 1 
HETATM 8495 C  CGD . HEM BA 7  .   ? -11.220 15.407  21.434 1.00 44.92  ? 401 HEM C CGD 1 
HETATM 8496 O  O1D . HEM BA 7  .   ? -12.301 15.654  21.972 1.00 46.50  ? 401 HEM C O1D 1 
HETATM 8497 O  O2D . HEM BA 7  .   ? -10.280 16.241  21.538 1.00 47.72  ? 401 HEM C O2D 1 
HETATM 8498 N  NA  . HEM BA 7  .   ? -6.960  9.762   19.465 1.00 37.42  ? 401 HEM C NA  1 
HETATM 8499 N  NB  . HEM BA 7  .   ? -6.658  7.825   17.468 1.00 37.46  ? 401 HEM C NB  1 
HETATM 8500 N  NC  . HEM BA 7  .   ? -8.632  9.139   15.843 1.00 40.73  ? 401 HEM C NC  1 
HETATM 8501 N  ND  . HEM BA 7  .   ? -8.953  11.010  17.908 1.00 40.34  ? 401 HEM C ND  1 
HETATM 8502 FE FE  . HEM BA 7  .   ? -7.880  9.483   17.749 1.00 35.68  ? 401 HEM C FE  1 
HETATM 8503 C  C1  . GOL CA 8  .   ? -15.953 -8.162  20.817 1.00 69.48  ? 402 GOL C C1  1 
HETATM 8504 O  O1  . GOL CA 8  .   ? -15.555 -9.124  21.799 1.00 63.76  ? 402 GOL C O1  1 
HETATM 8505 C  C2  . GOL CA 8  .   ? -16.624 -8.705  19.552 1.00 75.16  ? 402 GOL C C2  1 
HETATM 8506 O  O2  . GOL CA 8  .   ? -17.851 -9.404  19.820 1.00 71.04  ? 402 GOL C O2  1 
HETATM 8507 C  C3  . GOL CA 8  .   ? -15.716 -9.579  18.704 1.00 75.18  ? 402 GOL C C3  1 
HETATM 8508 O  O3  . GOL CA 8  .   ? -14.695 -8.813  18.063 1.00 76.05  ? 402 GOL C O3  1 
HETATM 8509 C  C   . ACT DA 13 .   ? -4.462  11.488  16.054 1.00 59.42  ? 403 ACT C C   1 
HETATM 8510 O  O   . ACT DA 13 .   ? -3.737  10.599  15.553 1.00 57.24  ? 403 ACT C O   1 
HETATM 8511 O  OXT . ACT DA 13 .   ? -4.179  12.735  16.021 1.00 55.04  ? 403 ACT C OXT 1 
HETATM 8512 C  CH3 . ACT DA 13 .   ? -5.800  11.018  16.676 1.00 51.93  ? 403 ACT C CH3 1 
HETATM 8513 N  N1  . EPE EA 10 .   ? 14.460  18.035  11.424 1.00 72.45  ? 404 EPE C N1  1 
HETATM 8514 C  C2  . EPE EA 10 .   ? 13.183  18.722  11.653 1.00 66.31  ? 404 EPE C C2  1 
HETATM 8515 C  C3  . EPE EA 10 .   ? 12.063  17.962  10.973 1.00 69.14  ? 404 EPE C C3  1 
HETATM 8516 N  N4  . EPE EA 10 .   ? 12.240  17.841  9.505  1.00 67.37  ? 404 EPE C N4  1 
HETATM 8517 C  C5  . EPE EA 10 .   ? 13.514  17.135  9.293  1.00 70.86  ? 404 EPE C C5  1 
HETATM 8518 C  C6  . EPE EA 10 .   ? 14.651  17.890  9.951  1.00 74.76  ? 404 EPE C C6  1 
HETATM 8519 C  C7  . EPE EA 10 .   ? 11.120  17.118  8.862  1.00 69.90  ? 404 EPE C C7  1 
HETATM 8520 C  C8  . EPE EA 10 .   ? 9.688   17.701  9.034  1.00 68.81  ? 404 EPE C C8  1 
HETATM 8521 O  O8  . EPE EA 10 .   ? 9.401   18.971  8.462  1.00 57.36  ? 404 EPE C O8  1 
HETATM 8522 C  C9  . EPE EA 10 .   ? 15.598  18.766  12.054 1.00 73.25  ? 404 EPE C C9  1 
HETATM 8523 C  C10 . EPE EA 10 .   ? 15.487  18.951  13.578 1.00 72.24  ? 404 EPE C C10 1 
HETATM 8524 S  S   . EPE EA 10 .   ? 16.910  19.831  14.207 1.00 77.28  ? 404 EPE C S   1 
HETATM 8525 O  O1S . EPE EA 10 .   ? 16.843  21.152  13.597 1.00 65.60  ? 404 EPE C O1S 1 
HETATM 8526 O  O2S . EPE EA 10 .   ? 18.051  18.982  13.908 1.00 72.01  ? 404 EPE C O2S 1 
HETATM 8527 O  O3S . EPE EA 10 .   ? 16.690  19.846  15.832 1.00 56.90  ? 404 EPE C O3S 1 
HETATM 8528 S  S   . SO4 FA 11 .   ? -7.290  4.376   34.152 1.00 86.15  ? 405 SO4 C S   1 
HETATM 8529 O  O1  . SO4 FA 11 .   ? -6.143  3.537   33.715 1.00 65.16  ? 405 SO4 C O1  1 
HETATM 8530 O  O2  . SO4 FA 11 .   ? -7.297  5.726   33.530 1.00 61.38  ? 405 SO4 C O2  1 
HETATM 8531 O  O3  . SO4 FA 11 .   ? -8.565  3.693   33.843 1.00 79.22  ? 405 SO4 C O3  1 
HETATM 8532 O  O4  . SO4 FA 11 .   ? -7.183  4.542   35.602 1.00 88.01  ? 405 SO4 C O4  1 
HETATM 8533 MG MG  . MG  GA 12 .   ? -7.007  15.084  26.190 1.00 46.42  ? 406 MG  C MG  1 
HETATM 8534 O  O   . HOH HA 14 .   ? 42.966  -9.958  19.087 1.00 36.82  ? 501 HOH A O   1 
HETATM 8535 O  O   . HOH HA 14 .   ? 26.290  -13.410 36.017 1.00 40.65  ? 502 HOH A O   1 
HETATM 8536 O  O   . HOH HA 14 .   ? 39.506  7.539   35.693 1.00 34.93  ? 503 HOH A O   1 
HETATM 8537 O  O   . HOH HA 14 .   ? 46.253  -1.677  26.363 1.00 55.92  ? 504 HOH A O   1 
HETATM 8538 O  O   . HOH HA 14 .   ? 27.429  -10.758 45.655 1.00 49.86  ? 505 HOH A O   1 
HETATM 8539 O  O   . HOH HA 14 .   ? 52.199  -15.477 33.059 1.00 41.68  ? 506 HOH A O   1 
HETATM 8540 O  O   . HOH HA 14 .   ? 25.016  -5.082  44.141 1.00 35.79  ? 507 HOH A O   1 
HETATM 8541 O  O   . HOH HA 14 .   ? 33.751  10.159  37.661 1.00 27.25  ? 508 HOH A O   1 
HETATM 8542 O  O   . HOH HA 14 .   ? 25.141  -9.538  39.046 1.00 38.40  ? 509 HOH A O   1 
HETATM 8543 O  O   . HOH HA 14 .   ? 35.061  -2.184  54.349 1.00 30.02  ? 510 HOH A O   1 
HETATM 8544 O  O   . HOH HA 14 .   ? 55.130  14.838  49.461 1.00 34.94  ? 511 HOH A O   1 
HETATM 8545 O  O   . HOH HA 14 .   ? 30.442  -14.602 49.483 1.00 35.20  ? 512 HOH A O   1 
HETATM 8546 O  O   . HOH HA 14 .   ? 57.695  -2.889  45.901 1.00 35.73  ? 513 HOH A O   1 
HETATM 8547 O  O   . HOH HA 14 .   ? 36.865  9.535   31.454 1.00 33.69  ? 514 HOH A O   1 
HETATM 8548 O  O   . HOH HA 14 .   ? 58.360  0.011   47.641 1.00 29.65  ? 515 HOH A O   1 
HETATM 8549 O  O   . HOH HA 14 .   ? 55.957  7.425   44.111 1.00 34.08  ? 516 HOH A O   1 
HETATM 8550 O  O   . HOH HA 14 .   ? 46.874  -12.325 29.180 1.00 43.22  ? 517 HOH A O   1 
HETATM 8551 O  O   . HOH HA 14 .   ? 28.144  -9.966  51.968 1.00 29.82  ? 518 HOH A O   1 
HETATM 8552 O  O   . HOH HA 14 .   ? 56.393  -5.116  51.657 1.00 47.63  ? 519 HOH A O   1 
HETATM 8553 O  O   . HOH HA 14 .   ? 29.509  -12.602 35.118 1.00 38.40  ? 520 HOH A O   1 
HETATM 8554 O  O   . HOH HA 14 .   ? 37.168  -13.404 26.755 1.00 37.23  ? 521 HOH A O   1 
HETATM 8555 O  O   . HOH HA 14 .   ? 49.625  5.883   47.336 1.00 31.02  ? 522 HOH A O   1 
HETATM 8556 O  O   . HOH HA 14 .   ? 50.620  9.611   38.505 1.00 36.61  ? 523 HOH A O   1 
HETATM 8557 O  O   . HOH HA 14 .   ? 22.487  -4.796  19.367 1.00 34.01  ? 524 HOH A O   1 
HETATM 8558 O  O   . HOH HA 14 .   ? 34.596  -4.043  56.154 1.00 34.79  ? 525 HOH A O   1 
HETATM 8559 O  O   . HOH HA 14 .   ? 33.238  -2.448  16.840 1.00 37.73  ? 526 HOH A O   1 
HETATM 8560 O  O   . HOH HA 14 .   ? 38.593  -17.579 47.106 1.00 38.79  ? 527 HOH A O   1 
HETATM 8561 O  O   . HOH HA 14 .   ? 41.435  10.452  49.944 1.00 40.17  ? 528 HOH A O   1 
HETATM 8562 O  O   . HOH HA 14 .   ? 48.491  8.566   50.342 1.00 36.02  ? 529 HOH A O   1 
HETATM 8563 O  O   . HOH HA 14 .   ? 47.095  7.579   38.360 1.00 28.86  ? 530 HOH A O   1 
HETATM 8564 O  O   . HOH HA 14 .   ? 29.372  -24.375 38.268 1.00 39.33  ? 531 HOH A O   1 
HETATM 8565 O  O   . HOH HA 14 .   ? 52.498  8.417   52.178 1.00 37.84  ? 532 HOH A O   1 
HETATM 8566 O  O   . HOH HA 14 .   ? 45.558  12.239  45.398 1.00 38.27  ? 533 HOH A O   1 
HETATM 8567 O  O   . HOH HA 14 .   ? 40.551  2.033   42.444 1.00 26.10  ? 534 HOH A O   1 
HETATM 8568 O  O   . HOH HA 14 .   ? 36.436  -21.008 46.426 1.00 38.55  ? 535 HOH A O   1 
HETATM 8569 O  O   . HOH HA 14 .   ? 44.197  -7.348  55.387 1.00 43.75  ? 536 HOH A O   1 
HETATM 8570 O  O   . HOH HA 14 .   ? 66.035  -0.401  36.143 1.00 31.86  ? 537 HOH A O   1 
HETATM 8571 O  O   . HOH HA 14 .   ? 46.571  -10.168 48.436 1.00 40.24  ? 538 HOH A O   1 
HETATM 8572 O  O   . HOH HA 14 .   ? 47.793  -10.330 25.605 1.00 41.03  ? 539 HOH A O   1 
HETATM 8573 O  O   . HOH HA 14 .   ? 23.167  -11.555 34.355 1.00 40.77  ? 540 HOH A O   1 
HETATM 8574 O  O   . HOH HA 14 .   ? 46.872  -15.429 36.932 1.00 25.29  ? 541 HOH A O   1 
HETATM 8575 O  O   . HOH HA 14 .   ? 45.866  -25.094 37.177 1.00 42.58  ? 542 HOH A O   1 
HETATM 8576 O  O   . HOH HA 14 .   ? 34.047  12.786  27.835 1.00 43.61  ? 543 HOH A O   1 
HETATM 8577 O  O   . HOH HA 14 .   ? 39.030  -15.069 29.807 1.00 32.06  ? 544 HOH A O   1 
HETATM 8578 O  O   . HOH HA 14 .   ? 31.854  -1.710  49.628 1.00 29.60  ? 545 HOH A O   1 
HETATM 8579 O  O   . HOH HA 14 .   ? 58.125  7.250   48.036 1.00 38.46  ? 546 HOH A O   1 
HETATM 8580 O  O   . HOH HA 14 .   ? 68.507  2.610   38.537 1.00 34.85  ? 547 HOH A O   1 
HETATM 8581 O  O   . HOH HA 14 .   ? 54.466  9.555   44.099 1.00 29.00  ? 548 HOH A O   1 
HETATM 8582 O  O   . HOH HA 14 .   ? 57.286  -5.392  45.685 1.00 27.83  ? 549 HOH A O   1 
HETATM 8583 O  O   . HOH HA 14 .   ? 49.212  -3.902  53.623 1.00 36.06  ? 550 HOH A O   1 
HETATM 8584 O  O   . HOH HA 14 .   ? 66.888  0.019   38.724 1.00 34.07  ? 551 HOH A O   1 
HETATM 8585 O  O   . HOH HA 14 .   ? 40.858  15.925  31.999 1.00 32.06  ? 552 HOH A O   1 
HETATM 8586 O  O   . HOH HA 14 .   ? 44.114  -22.687 32.976 1.00 34.89  ? 553 HOH A O   1 
HETATM 8587 O  O   . HOH HA 14 .   ? 47.703  11.313  27.966 1.00 30.48  ? 554 HOH A O   1 
HETATM 8588 O  O   . HOH HA 14 .   ? 28.943  11.267  27.285 1.00 33.58  ? 555 HOH A O   1 
HETATM 8589 O  O   . HOH HA 14 .   ? 70.879  3.772   48.469 1.00 31.66  ? 556 HOH A O   1 
HETATM 8590 O  O   . HOH HA 14 .   ? 40.520  11.798  33.699 1.00 43.05  ? 557 HOH A O   1 
HETATM 8591 O  O   . HOH HA 14 .   ? 48.792  9.320   29.780 1.00 33.27  ? 558 HOH A O   1 
HETATM 8592 O  O   . HOH HA 14 .   ? 44.424  -12.161 47.989 1.00 26.90  ? 559 HOH A O   1 
HETATM 8593 O  O   . HOH HA 14 .   ? 37.110  -18.616 31.005 1.00 36.35  ? 560 HOH A O   1 
HETATM 8594 O  O   . HOH HA 14 .   ? 51.298  9.469   30.371 1.00 34.15  ? 561 HOH A O   1 
HETATM 8595 O  O   . HOH HA 14 .   ? 49.305  -15.648 35.607 1.00 35.33  ? 562 HOH A O   1 
HETATM 8596 O  O   . HOH HA 14 .   ? 45.215  -3.012  15.691 1.00 36.64  ? 563 HOH A O   1 
HETATM 8597 O  O   . HOH HA 14 .   ? 55.403  -5.908  47.953 1.00 34.23  ? 564 HOH A O   1 
HETATM 8598 O  O   . HOH HA 14 .   ? 20.480  -10.644 22.338 1.00 35.97  ? 565 HOH A O   1 
HETATM 8599 O  O   . HOH HA 14 .   ? 40.110  8.414   48.107 1.00 35.61  ? 566 HOH A O   1 
HETATM 8600 O  O   . HOH HA 14 .   ? 42.602  -13.566 50.398 1.00 36.67  ? 567 HOH A O   1 
HETATM 8601 O  O   . HOH HA 14 .   ? 44.599  -9.819  21.197 1.00 36.55  ? 568 HOH A O   1 
HETATM 8602 O  O   . HOH HA 14 .   ? 34.916  -13.694 56.457 1.00 41.50  ? 569 HOH A O   1 
HETATM 8603 O  O   . HOH HA 14 .   ? 25.007  3.995   14.395 1.00 39.02  ? 570 HOH A O   1 
HETATM 8604 O  O   . HOH HA 14 .   ? 34.038  12.323  30.624 1.00 38.66  ? 571 HOH A O   1 
HETATM 8605 O  O   . HOH HA 14 .   ? 71.266  -3.216  41.144 1.00 45.02  ? 572 HOH A O   1 
HETATM 8606 O  O   . HOH HA 14 .   ? 46.190  -1.842  54.774 1.00 37.43  ? 573 HOH A O   1 
HETATM 8607 O  O   . HOH HA 14 .   ? 29.338  -11.587 49.114 1.00 30.86  ? 574 HOH A O   1 
HETATM 8608 O  O   . HOH HA 14 .   ? 37.039  2.431   60.497 1.00 44.08  ? 575 HOH A O   1 
HETATM 8609 O  O   . HOH HA 14 .   ? 23.995  1.836   43.577 1.00 32.36  ? 576 HOH A O   1 
HETATM 8610 O  O   . HOH HA 14 .   ? 61.583  -5.043  55.729 1.00 39.75  ? 577 HOH A O   1 
HETATM 8611 O  O   . HOH HA 14 .   ? 26.295  9.420   38.949 1.00 35.63  ? 578 HOH A O   1 
HETATM 8612 O  O   . HOH HA 14 .   ? 46.869  -21.446 43.343 1.00 44.10  ? 579 HOH A O   1 
HETATM 8613 O  O   . HOH HA 14 .   ? 55.534  -16.825 43.677 1.00 31.22  ? 580 HOH A O   1 
HETATM 8614 O  O   . HOH HA 14 .   ? 34.729  -3.921  52.248 1.00 38.07  ? 581 HOH A O   1 
HETATM 8615 O  O   . HOH HA 14 .   ? 39.223  -24.757 35.062 1.00 33.86  ? 582 HOH A O   1 
HETATM 8616 O  O   . HOH HA 14 .   ? 22.851  -5.337  39.599 1.00 33.74  ? 583 HOH A O   1 
HETATM 8617 O  O   . HOH HA 14 .   ? 47.750  15.996  38.758 1.00 44.25  ? 584 HOH A O   1 
HETATM 8618 O  O   . HOH HA 14 .   ? 18.283  -5.819  36.309 1.00 40.77  ? 585 HOH A O   1 
HETATM 8619 O  O   . HOH HA 14 .   ? 48.370  -4.354  32.370 1.00 46.00  ? 586 HOH A O   1 
HETATM 8620 O  O   . HOH HA 14 .   ? 31.319  5.888   43.047 1.00 32.64  ? 587 HOH A O   1 
HETATM 8621 O  O   . HOH HA 14 .   ? 27.425  -12.112 32.293 1.00 29.98  ? 588 HOH A O   1 
HETATM 8622 O  O   . HOH HA 14 .   ? 48.319  -15.470 43.425 1.00 33.87  ? 589 HOH A O   1 
HETATM 8623 O  O   . HOH HA 14 .   ? 21.134  -1.926  37.969 1.00 34.89  ? 590 HOH A O   1 
HETATM 8624 O  O   . HOH HA 14 .   ? 66.218  11.006  49.355 1.00 34.51  ? 591 HOH A O   1 
HETATM 8625 O  O   . HOH HA 14 .   ? 20.229  2.306   32.236 1.00 38.28  ? 592 HOH A O   1 
HETATM 8626 O  O   . HOH HA 14 .   ? 33.901  -0.071  41.230 1.00 31.07  ? 593 HOH A O   1 
HETATM 8627 O  O   . HOH HA 14 .   ? 50.943  -22.591 37.114 1.00 45.69  ? 594 HOH A O   1 
HETATM 8628 O  O   . HOH HA 14 .   ? 43.105  12.870  47.208 1.00 33.99  ? 595 HOH A O   1 
HETATM 8629 O  O   . HOH HA 14 .   ? 30.081  4.034   48.074 1.00 43.37  ? 596 HOH A O   1 
HETATM 8630 O  O   . HOH HA 14 .   ? 45.622  -8.826  50.802 1.00 37.83  ? 597 HOH A O   1 
HETATM 8631 O  O   . HOH HA 14 .   ? 48.660  18.068  22.678 1.00 43.82  ? 598 HOH A O   1 
HETATM 8632 O  O   . HOH HA 14 .   ? 73.073  7.895   51.506 1.00 38.04  ? 599 HOH A O   1 
HETATM 8633 O  O   . HOH HA 14 .   ? 28.457  -14.723 37.311 1.00 39.43  ? 600 HOH A O   1 
HETATM 8634 O  O   . HOH HA 14 .   ? 54.561  -2.863  54.075 1.00 38.00  ? 601 HOH A O   1 
HETATM 8635 O  O   . HOH HA 14 .   ? 37.284  6.655   48.940 1.00 39.63  ? 602 HOH A O   1 
HETATM 8636 O  O   . HOH HA 14 .   ? 52.348  -17.229 43.402 1.00 46.39  ? 603 HOH A O   1 
HETATM 8637 O  O   . HOH HA 14 .   ? 40.929  12.728  45.236 1.00 36.76  ? 604 HOH A O   1 
HETATM 8638 O  O   . HOH HA 14 .   ? 64.492  12.962  45.565 1.00 37.43  ? 605 HOH A O   1 
HETATM 8639 O  O   . HOH HA 14 .   ? 67.813  6.406   54.731 1.00 36.66  ? 606 HOH A O   1 
HETATM 8640 O  O   . HOH HA 14 .   ? 45.599  15.175  40.290 1.00 40.75  ? 607 HOH A O   1 
HETATM 8641 O  O   . HOH HA 14 .   ? 27.179  2.076   45.378 1.00 33.96  ? 608 HOH A O   1 
HETATM 8642 O  O   . HOH HA 14 .   ? 29.180  -22.063 27.135 1.00 43.17  ? 609 HOH A O   1 
HETATM 8643 O  O   . HOH HA 14 .   ? 58.818  12.343  31.008 1.00 43.48  ? 610 HOH A O   1 
HETATM 8644 O  O   . HOH HA 14 .   ? 48.974  11.190  51.465 1.00 37.72  ? 611 HOH A O   1 
HETATM 8645 O  O   . HOH HA 14 .   ? 48.823  -10.753 52.949 1.00 36.89  ? 612 HOH A O   1 
HETATM 8646 O  O   . HOH HA 14 .   ? 45.987  -7.668  21.528 1.00 30.31  ? 613 HOH A O   1 
HETATM 8647 O  O   . HOH HA 14 .   ? 42.995  -15.020 48.568 1.00 41.27  ? 614 HOH A O   1 
HETATM 8648 O  O   . HOH HA 14 .   ? 23.041  7.127   26.436 1.00 36.96  ? 615 HOH A O   1 
HETATM 8649 O  O   . HOH HA 14 .   ? 50.143  -19.465 44.636 1.00 34.17  ? 616 HOH A O   1 
HETATM 8650 O  O   . HOH HA 14 .   ? 25.691  -13.562 30.560 1.00 39.76  ? 617 HOH A O   1 
HETATM 8651 O  O   . HOH HA 14 .   ? 66.089  -11.104 27.522 1.00 43.69  ? 618 HOH A O   1 
HETATM 8652 O  O   . HOH HA 14 .   ? 26.030  11.535  37.026 1.00 35.39  ? 619 HOH A O   1 
HETATM 8653 O  O   . HOH HA 14 .   ? 47.770  -4.764  55.309 1.00 44.13  ? 620 HOH A O   1 
HETATM 8654 O  O   . HOH HA 14 .   ? 42.180  30.431  26.590 1.00 39.35  ? 621 HOH A O   1 
HETATM 8655 O  O   . HOH HA 14 .   ? 69.928  6.089   32.269 1.00 42.60  ? 622 HOH A O   1 
HETATM 8656 O  O   . HOH HA 14 .   ? 50.518  -17.200 33.672 1.00 33.96  ? 623 HOH A O   1 
HETATM 8657 O  O   . HOH HA 14 .   ? 46.642  -3.283  29.277 1.00 46.69  ? 624 HOH A O   1 
HETATM 8658 O  O   . HOH HA 14 .   ? 40.486  3.768   60.825 1.00 42.26  ? 625 HOH A O   1 
HETATM 8659 O  O   . HOH HA 14 .   ? 31.929  5.957   12.116 1.00 46.18  ? 626 HOH A O   1 
HETATM 8660 O  O   . HOH HA 14 .   ? 45.374  -5.388  13.903 1.00 39.75  ? 627 HOH A O   1 
HETATM 8661 O  O   . HOH HA 14 .   ? 39.762  -12.715 21.798 1.00 42.44  ? 628 HOH A O   1 
HETATM 8662 O  O   . HOH HA 14 .   ? 44.347  6.543   59.386 1.00 40.15  ? 629 HOH A O   1 
HETATM 8663 O  O   . HOH HA 14 .   ? 50.636  -5.470  30.094 1.00 51.32  ? 630 HOH A O   1 
HETATM 8664 O  O   . HOH HA 14 .   ? 29.495  -8.513  13.724 1.00 52.22  ? 631 HOH A O   1 
HETATM 8665 O  O   . HOH HA 14 .   ? 51.952  -4.622  54.570 1.00 42.99  ? 632 HOH A O   1 
HETATM 8666 O  O   . HOH HA 14 .   ? 34.367  1.110   61.434 1.00 49.14  ? 633 HOH A O   1 
HETATM 8667 O  O   . HOH HA 14 .   ? 27.936  14.228  20.179 1.00 45.44  ? 634 HOH A O   1 
HETATM 8668 O  O   . HOH HA 14 .   ? 21.749  9.214   38.751 1.00 45.62  ? 635 HOH A O   1 
HETATM 8669 O  O   . HOH HA 14 .   ? 31.955  -22.526 48.737 1.00 42.98  ? 636 HOH A O   1 
HETATM 8670 O  O   . HOH HA 14 .   ? 29.883  7.133   46.147 1.00 44.43  ? 637 HOH A O   1 
HETATM 8671 O  O   . HOH HA 14 .   ? 36.759  27.154  30.014 1.00 53.58  ? 638 HOH A O   1 
HETATM 8672 O  O   . HOH HA 14 .   ? 78.468  1.480   47.912 1.00 40.89  ? 639 HOH A O   1 
HETATM 8673 O  O   . HOH HA 14 .   ? 27.086  18.232  32.969 1.00 41.46  ? 640 HOH A O   1 
HETATM 8674 O  O   . HOH HA 14 .   ? 27.359  -17.035 13.315 1.00 46.48  ? 641 HOH A O   1 
HETATM 8675 O  O   . HOH HA 14 .   ? 30.688  29.055  27.851 1.00 51.38  ? 642 HOH A O   1 
HETATM 8676 O  O   . HOH IA 14 .   ? 0.863   -25.255 58.215 1.00 42.93  ? 501 HOH B O   1 
HETATM 8677 O  O   . HOH IA 14 .   ? 13.983  -8.196  66.885 1.00 45.25  ? 502 HOH B O   1 
HETATM 8678 O  O   . HOH IA 14 .   ? 25.314  -8.354  48.772 1.00 38.65  ? 503 HOH B O   1 
HETATM 8679 O  O   . HOH IA 14 .   ? 6.993   -9.570  66.872 1.00 39.87  ? 504 HOH B O   1 
HETATM 8680 O  O   . HOH IA 14 .   ? -3.601  -4.025  45.058 1.00 43.89  ? 505 HOH B O   1 
HETATM 8681 O  O   . HOH IA 14 .   ? -3.389  4.681   57.373 1.00 41.16  ? 506 HOH B O   1 
HETATM 8682 O  O   . HOH IA 14 .   ? 13.899  -7.947  71.916 1.00 35.95  ? 507 HOH B O   1 
HETATM 8683 O  O   . HOH IA 14 .   ? 7.791   -2.736  67.634 1.00 33.63  ? 508 HOH B O   1 
HETATM 8684 O  O   . HOH IA 14 .   ? 28.246  -7.520  54.390 1.00 38.62  ? 509 HOH B O   1 
HETATM 8685 O  O   . HOH IA 14 .   ? 19.511  4.869   50.019 1.00 35.47  ? 510 HOH B O   1 
HETATM 8686 O  O   . HOH IA 14 .   ? 1.101   5.305   66.962 1.00 30.88  ? 511 HOH B O   1 
HETATM 8687 O  O   . HOH IA 14 .   ? -16.550 -9.678  62.953 1.00 40.04  ? 512 HOH B O   1 
HETATM 8688 O  O   . HOH IA 14 .   ? -0.701  -16.887 52.115 1.00 46.33  ? 513 HOH B O   1 
HETATM 8689 O  O   . HOH IA 14 .   ? 12.288  -29.678 63.207 1.00 44.27  ? 514 HOH B O   1 
HETATM 8690 O  O   . HOH IA 14 .   ? 25.390  -0.075  56.746 1.00 39.28  ? 515 HOH B O   1 
HETATM 8691 O  O   . HOH IA 14 .   ? 19.867  -17.801 64.860 1.00 30.93  ? 516 HOH B O   1 
HETATM 8692 O  O   . HOH IA 14 .   ? 23.832  -23.214 51.782 1.00 25.09  ? 517 HOH B O   1 
HETATM 8693 O  O   . HOH IA 14 .   ? 12.507  4.543   68.537 1.00 41.84  ? 518 HOH B O   1 
HETATM 8694 O  O   . HOH IA 14 .   ? 11.626  -8.635  76.772 1.00 39.54  ? 519 HOH B O   1 
HETATM 8695 O  O   . HOH IA 14 .   ? 16.071  -11.246 69.495 1.00 36.10  ? 520 HOH B O   1 
HETATM 8696 O  O   . HOH IA 14 .   ? -12.648 1.903   64.520 1.00 37.31  ? 521 HOH B O   1 
HETATM 8697 O  O   . HOH IA 14 .   ? 9.400   -10.390 73.765 1.00 32.89  ? 522 HOH B O   1 
HETATM 8698 O  O   . HOH IA 14 .   ? 18.818  -14.796 73.143 1.00 31.82  ? 523 HOH B O   1 
HETATM 8699 O  O   . HOH IA 14 .   ? 2.846   5.245   69.070 1.00 38.60  ? 524 HOH B O   1 
HETATM 8700 O  O   . HOH IA 14 .   ? 20.792  -7.133  67.155 1.00 35.04  ? 525 HOH B O   1 
HETATM 8701 O  O   . HOH IA 14 .   ? -2.852  7.301   59.879 1.00 39.31  ? 526 HOH B O   1 
HETATM 8702 O  O   . HOH IA 14 .   ? 29.510  -9.960  59.002 1.00 36.03  ? 527 HOH B O   1 
HETATM 8703 O  O   . HOH IA 14 .   ? 5.525   -13.437 82.627 1.00 40.16  ? 528 HOH B O   1 
HETATM 8704 O  O   . HOH IA 14 .   ? 10.208  -7.255  36.277 1.00 45.09  ? 529 HOH B O   1 
HETATM 8705 O  O   . HOH IA 14 .   ? 6.994   5.699   63.012 1.00 37.07  ? 530 HOH B O   1 
HETATM 8706 O  O   . HOH IA 14 .   ? 5.782   8.387   52.019 1.00 37.63  ? 531 HOH B O   1 
HETATM 8707 O  O   . HOH IA 14 .   ? 8.707   -14.065 47.281 1.00 27.22  ? 532 HOH B O   1 
HETATM 8708 O  O   . HOH IA 14 .   ? 21.386  -0.233  51.463 1.00 36.63  ? 533 HOH B O   1 
HETATM 8709 O  O   . HOH IA 14 .   ? 7.662   -22.800 50.455 1.00 38.60  ? 534 HOH B O   1 
HETATM 8710 O  O   . HOH IA 14 .   ? 0.289   -10.563 47.108 1.00 35.63  ? 535 HOH B O   1 
HETATM 8711 O  O   . HOH IA 14 .   ? 14.615  -7.957  75.625 1.00 32.54  ? 536 HOH B O   1 
HETATM 8712 O  O   . HOH IA 14 .   ? 21.899  -31.868 57.650 1.00 35.29  ? 537 HOH B O   1 
HETATM 8713 O  O   . HOH IA 14 .   ? -12.382 -0.811  64.863 1.00 43.03  ? 538 HOH B O   1 
HETATM 8714 O  O   . HOH IA 14 .   ? 12.879  -3.047  59.463 1.00 32.78  ? 539 HOH B O   1 
HETATM 8715 O  O   . HOH IA 14 .   ? -3.781  3.716   54.941 1.00 40.80  ? 540 HOH B O   1 
HETATM 8716 O  O   . HOH IA 14 .   ? 16.552  -17.495 46.854 1.00 35.19  ? 541 HOH B O   1 
HETATM 8717 O  O   . HOH IA 14 .   ? 15.779  -13.903 34.169 1.00 38.28  ? 542 HOH B O   1 
HETATM 8718 O  O   . HOH IA 14 .   ? 5.942   -19.670 48.047 1.00 39.73  ? 543 HOH B O   1 
HETATM 8719 O  O   . HOH IA 14 .   ? 6.247   11.555  64.584 1.00 41.45  ? 544 HOH B O   1 
HETATM 8720 O  O   . HOH IA 14 .   ? 18.812  2.320   49.004 1.00 34.61  ? 545 HOH B O   1 
HETATM 8721 O  O   . HOH IA 14 .   ? 21.563  -15.260 74.204 1.00 34.89  ? 546 HOH B O   1 
HETATM 8722 O  O   . HOH IA 14 .   ? 5.119   1.531   47.696 1.00 38.68  ? 547 HOH B O   1 
HETATM 8723 O  O   . HOH IA 14 .   ? 27.019  -19.017 66.892 1.00 41.21  ? 548 HOH B O   1 
HETATM 8724 O  O   . HOH IA 14 .   ? 18.346  -20.256 47.908 1.00 30.57  ? 549 HOH B O   1 
HETATM 8725 O  O   . HOH IA 14 .   ? 14.275  -8.946  64.089 1.00 36.76  ? 550 HOH B O   1 
HETATM 8726 O  O   . HOH IA 14 .   ? 6.374   -2.412  70.620 1.00 33.71  ? 551 HOH B O   1 
HETATM 8727 O  O   . HOH IA 14 .   ? 2.494   -8.161  72.707 1.00 39.38  ? 552 HOH B O   1 
HETATM 8728 O  O   . HOH IA 14 .   ? 6.144   -10.962 74.398 1.00 32.46  ? 553 HOH B O   1 
HETATM 8729 O  O   . HOH IA 14 .   ? 20.059  -34.450 60.508 1.00 34.61  ? 554 HOH B O   1 
HETATM 8730 O  O   . HOH IA 14 .   ? 9.866   -11.312 34.975 1.00 43.24  ? 555 HOH B O   1 
HETATM 8731 O  O   . HOH IA 14 .   ? 25.885  -13.275 49.741 1.00 34.52  ? 556 HOH B O   1 
HETATM 8732 O  O   . HOH IA 14 .   ? -2.501  -11.023 47.952 1.00 30.95  ? 557 HOH B O   1 
HETATM 8733 O  O   . HOH IA 14 .   ? 17.178  -33.548 59.550 1.00 37.07  ? 558 HOH B O   1 
HETATM 8734 O  O   . HOH IA 14 .   ? -5.901  15.986  66.156 1.00 51.93  ? 559 HOH B O   1 
HETATM 8735 O  O   . HOH IA 14 .   ? -1.749  4.819   53.630 1.00 47.49  ? 560 HOH B O   1 
HETATM 8736 O  O   . HOH IA 14 .   ? -7.988  -5.530  51.135 1.00 31.94  ? 561 HOH B O   1 
HETATM 8737 O  O   . HOH IA 14 .   ? 19.423  -12.717 71.546 1.00 38.56  ? 562 HOH B O   1 
HETATM 8738 O  O   . HOH IA 14 .   ? 28.996  -14.534 53.886 1.00 39.60  ? 563 HOH B O   1 
HETATM 8739 O  O   . HOH IA 14 .   ? 20.364  -4.589  42.423 1.00 35.51  ? 564 HOH B O   1 
HETATM 8740 O  O   . HOH IA 14 .   ? -6.596  -2.174  45.138 1.00 36.33  ? 565 HOH B O   1 
HETATM 8741 O  O   . HOH IA 14 .   ? 20.197  -9.120  39.130 1.00 40.67  ? 566 HOH B O   1 
HETATM 8742 O  O   . HOH IA 14 .   ? 23.371  -7.457  67.996 1.00 36.50  ? 567 HOH B O   1 
HETATM 8743 O  O   . HOH IA 14 .   ? 12.340  0.522   72.845 1.00 41.21  ? 568 HOH B O   1 
HETATM 8744 O  O   . HOH IA 14 .   ? -5.501  14.444  52.768 1.00 41.28  ? 569 HOH B O   1 
HETATM 8745 O  O   . HOH IA 14 .   ? 6.837   -20.487 44.581 1.00 39.43  ? 570 HOH B O   1 
HETATM 8746 O  O   . HOH IA 14 .   ? 22.533  -4.042  60.406 1.00 31.94  ? 571 HOH B O   1 
HETATM 8747 O  O   . HOH IA 14 .   ? -7.213  18.485  64.653 1.00 47.73  ? 572 HOH B O   1 
HETATM 8748 O  O   . HOH IA 14 .   ? 18.016  -6.475  56.464 1.00 35.86  ? 573 HOH B O   1 
HETATM 8749 O  O   . HOH IA 14 .   ? 0.273   -22.883 59.305 1.00 32.56  ? 574 HOH B O   1 
HETATM 8750 O  O   . HOH IA 14 .   ? -5.326  14.752  71.219 1.00 46.06  ? 575 HOH B O   1 
HETATM 8751 O  O   . HOH IA 14 .   ? 13.978  -18.149 33.977 1.00 42.04  ? 576 HOH B O   1 
HETATM 8752 O  O   . HOH IA 14 .   ? 8.582   -30.886 48.128 1.00 48.09  ? 577 HOH B O   1 
HETATM 8753 O  O   . HOH IA 14 .   ? -2.431  -14.011 38.100 1.00 40.80  ? 578 HOH B O   1 
HETATM 8754 O  O   . HOH IA 14 .   ? 28.192  -15.425 56.659 1.00 43.22  ? 579 HOH B O   1 
HETATM 8755 O  O   . HOH IA 14 .   ? 30.596  -11.112 56.640 1.00 31.40  ? 580 HOH B O   1 
HETATM 8756 O  O   . HOH IA 14 .   ? -9.932  -4.205  74.541 1.00 36.25  ? 581 HOH B O   1 
HETATM 8757 O  O   . HOH IA 14 .   ? -6.920  -18.977 61.517 1.00 39.74  ? 582 HOH B O   1 
HETATM 8758 O  O   . HOH IA 14 .   ? 4.800   -12.949 61.448 1.00 47.52  ? 583 HOH B O   1 
HETATM 8759 O  O   . HOH IA 14 .   ? 26.307  -25.521 69.973 1.00 53.18  ? 584 HOH B O   1 
HETATM 8760 O  O   . HOH IA 14 .   ? -2.308  -3.521  41.080 1.00 44.95  ? 585 HOH B O   1 
HETATM 8761 O  O   . HOH IA 14 .   ? 8.789   -28.353 49.758 1.00 41.55  ? 586 HOH B O   1 
HETATM 8762 O  O   . HOH IA 14 .   ? 18.639  -22.588 46.599 1.00 40.54  ? 587 HOH B O   1 
HETATM 8763 O  O   . HOH IA 14 .   ? 12.723  -12.179 33.733 1.00 44.75  ? 588 HOH B O   1 
HETATM 8764 O  O   . HOH IA 14 .   ? 15.109  5.512   42.650 1.00 47.50  ? 589 HOH B O   1 
HETATM 8765 O  O   . HOH IA 14 .   ? 12.140  -27.633 41.166 1.00 47.33  ? 590 HOH B O   1 
HETATM 8766 O  O   . HOH IA 14 .   ? 3.081   3.258   46.471 1.00 41.35  ? 591 HOH B O   1 
HETATM 8767 O  O   . HOH IA 14 .   ? 28.906  -9.988  66.404 1.00 36.68  ? 592 HOH B O   1 
HETATM 8768 O  O   . HOH IA 14 .   ? 27.348  -17.054 53.920 1.00 41.43  ? 593 HOH B O   1 
HETATM 8769 O  O   . HOH IA 14 .   ? -11.258 15.277  61.838 1.00 46.92  ? 594 HOH B O   1 
HETATM 8770 O  O   . HOH IA 14 .   ? -18.219 -10.609 59.807 1.00 42.82  ? 595 HOH B O   1 
HETATM 8771 O  O   . HOH IA 14 .   ? 14.134  -5.512  33.716 1.00 50.47  ? 596 HOH B O   1 
HETATM 8772 O  O   . HOH IA 14 .   ? 2.508   7.890   46.596 1.00 46.83  ? 597 HOH B O   1 
HETATM 8773 O  O   . HOH IA 14 .   ? 19.173  -32.629 48.652 1.00 41.92  ? 598 HOH B O   1 
HETATM 8774 O  O   . HOH IA 14 .   ? 17.854  1.809   34.246 1.00 41.05  ? 599 HOH B O   1 
HETATM 8775 O  O   . HOH IA 14 .   ? 29.224  -6.596  56.721 1.00 36.55  ? 600 HOH B O   1 
HETATM 8776 O  O   . HOH IA 14 .   ? 2.561   -14.111 61.472 1.00 48.36  ? 601 HOH B O   1 
HETATM 8777 O  O   . HOH IA 14 .   ? 26.241  -6.358  59.521 1.00 37.20  ? 602 HOH B O   1 
HETATM 8778 O  O   . HOH IA 14 .   ? -8.383  -12.566 46.092 1.00 44.16  ? 603 HOH B O   1 
HETATM 8779 O  O   . HOH JA 14 .   ? -10.692 30.170  12.699 1.00 43.74  ? 501 HOH C O   1 
HETATM 8780 O  O   . HOH JA 14 .   ? 1.860   8.073   27.180 1.00 41.30  ? 502 HOH C O   1 
HETATM 8781 O  O   . HOH JA 14 .   ? -5.187  -3.191  4.011  1.00 37.65  ? 503 HOH C O   1 
HETATM 8782 O  O   . HOH JA 14 .   ? -4.409  12.202  4.196  1.00 38.13  ? 504 HOH C O   1 
HETATM 8783 O  O   . HOH JA 14 .   ? 2.618   -5.200  16.292 1.00 39.35  ? 505 HOH C O   1 
HETATM 8784 O  O   . HOH JA 14 .   ? 4.834   -0.210  25.852 1.00 34.38  ? 506 HOH C O   1 
HETATM 8785 O  O   . HOH JA 14 .   ? 1.571   -5.339  13.726 1.00 30.34  ? 507 HOH C O   1 
HETATM 8786 O  O   . HOH JA 14 .   ? -9.614  13.133  23.824 1.00 35.36  ? 508 HOH C O   1 
HETATM 8787 O  O   . HOH JA 14 .   ? -12.804 13.515  3.430  1.00 39.16  ? 509 HOH C O   1 
HETATM 8788 O  O   . HOH JA 14 .   ? 3.801   -6.323  19.644 1.00 33.94  ? 510 HOH C O   1 
HETATM 8789 O  O   . HOH JA 14 .   ? -23.129 1.619   25.885 1.00 36.46  ? 511 HOH C O   1 
HETATM 8790 O  O   . HOH JA 14 .   ? -20.527 -4.063  23.954 1.00 34.13  ? 512 HOH C O   1 
HETATM 8791 O  O   . HOH JA 14 .   ? -1.715  8.299   25.802 1.00 36.16  ? 513 HOH C O   1 
HETATM 8792 O  O   . HOH JA 14 .   ? -23.314 16.563  9.734  1.00 40.47  ? 514 HOH C O   1 
HETATM 8793 O  O   . HOH JA 14 .   ? -4.634  -11.463 27.220 1.00 45.11  ? 515 HOH C O   1 
HETATM 8794 O  O   . HOH JA 14 .   ? 4.161   0.920   28.283 1.00 34.76  ? 516 HOH C O   1 
HETATM 8795 O  O   . HOH JA 14 .   ? 21.907  -7.240  29.764 1.00 28.60  ? 517 HOH C O   1 
HETATM 8796 O  O   . HOH JA 14 .   ? -7.679  4.229   3.950  1.00 27.33  ? 518 HOH C O   1 
HETATM 8797 O  O   . HOH JA 14 .   ? -2.611  -1.234  26.668 1.00 29.74  ? 519 HOH C O   1 
HETATM 8798 O  O   . HOH JA 14 .   ? -7.749  13.472  1.714  1.00 39.42  ? 520 HOH C O   1 
HETATM 8799 O  O   . HOH JA 14 .   ? -3.188  21.214  4.172  1.00 55.04  ? 521 HOH C O   1 
HETATM 8800 O  O   . HOH JA 14 .   ? 14.583  4.023   32.530 1.00 40.32  ? 522 HOH C O   1 
HETATM 8801 O  O   . HOH JA 14 .   ? -7.749  -2.178  5.715  1.00 41.14  ? 523 HOH C O   1 
HETATM 8802 O  O   . HOH JA 14 .   ? -3.053  18.116  32.604 1.00 46.43  ? 524 HOH C O   1 
HETATM 8803 O  O   . HOH JA 14 .   ? 13.813  0.939   14.020 1.00 29.09  ? 525 HOH C O   1 
HETATM 8804 O  O   . HOH JA 14 .   ? 3.042   18.306  25.751 1.00 39.79  ? 526 HOH C O   1 
HETATM 8805 O  O   . HOH JA 14 .   ? -26.753 11.370  13.924 1.00 47.45  ? 527 HOH C O   1 
HETATM 8806 O  O   . HOH JA 14 .   ? 10.717  -2.259  5.337  1.00 38.74  ? 528 HOH C O   1 
HETATM 8807 O  O   . HOH JA 14 .   ? -0.687  -6.735  14.906 1.00 38.07  ? 529 HOH C O   1 
HETATM 8808 O  O   . HOH JA 14 .   ? -12.634 -4.067  10.752 1.00 34.68  ? 530 HOH C O   1 
HETATM 8809 O  O   . HOH JA 14 .   ? -1.753  8.713   33.315 1.00 40.69  ? 531 HOH C O   1 
HETATM 8810 O  O   . HOH JA 14 .   ? -19.434 -8.878  17.274 1.00 40.13  ? 532 HOH C O   1 
HETATM 8811 O  O   . HOH JA 14 .   ? -10.913 2.831   30.609 1.00 41.74  ? 533 HOH C O   1 
HETATM 8812 O  O   . HOH JA 14 .   ? 5.359   -6.572  27.530 1.00 42.37  ? 534 HOH C O   1 
HETATM 8813 O  O   . HOH JA 14 .   ? -5.199  4.385   2.874  1.00 34.74  ? 535 HOH C O   1 
HETATM 8814 O  O   . HOH JA 14 .   ? -22.242 18.072  -2.169 1.00 45.12  ? 536 HOH C O   1 
HETATM 8815 O  O   . HOH JA 14 .   ? -8.674  -4.823  1.713  1.00 46.92  ? 537 HOH C O   1 
HETATM 8816 O  O   . HOH JA 14 .   ? 1.965   -0.186  4.866  1.00 31.99  ? 538 HOH C O   1 
HETATM 8817 O  O   . HOH JA 14 .   ? 20.650  4.357   16.500 1.00 37.95  ? 539 HOH C O   1 
HETATM 8818 O  O   . HOH JA 14 .   ? 19.249  2.654   28.250 1.00 44.08  ? 540 HOH C O   1 
HETATM 8819 O  O   . HOH JA 14 .   ? -7.823  -9.507  19.663 1.00 44.79  ? 541 HOH C O   1 
HETATM 8820 O  O   . HOH JA 14 .   ? -16.430 8.561   21.966 1.00 38.11  ? 542 HOH C O   1 
HETATM 8821 O  O   . HOH JA 14 .   ? -14.941 12.949  1.197  1.00 39.35  ? 543 HOH C O   1 
HETATM 8822 O  O   . HOH JA 14 .   ? 13.754  -8.612  28.794 1.00 43.04  ? 544 HOH C O   1 
HETATM 8823 O  O   . HOH JA 14 .   ? -0.986  12.441  7.947  1.00 40.43  ? 545 HOH C O   1 
HETATM 8824 O  O   . HOH JA 14 .   ? 3.739   3.657   2.170  1.00 23.76  ? 546 HOH C O   1 
HETATM 8825 O  O   . HOH JA 14 .   ? -16.748 6.428   -4.330 1.00 31.56  ? 547 HOH C O   1 
HETATM 8826 O  O   . HOH JA 14 .   ? 7.437   23.983  30.008 1.00 41.71  ? 548 HOH C O   1 
HETATM 8827 O  O   . HOH JA 14 .   ? -2.369  -5.753  3.150  1.00 33.49  ? 549 HOH C O   1 
HETATM 8828 O  O   . HOH JA 14 .   ? 12.026  -11.487 26.873 1.00 45.30  ? 550 HOH C O   1 
HETATM 8829 O  O   . HOH JA 14 .   ? -26.875 2.159   14.375 1.00 38.57  ? 551 HOH C O   1 
HETATM 8830 O  O   . HOH JA 14 .   ? 12.389  -14.578 25.941 1.00 35.16  ? 552 HOH C O   1 
HETATM 8831 O  O   . HOH JA 14 .   ? -23.164 1.605   -0.036 1.00 48.26  ? 553 HOH C O   1 
HETATM 8832 O  O   . HOH JA 14 .   ? -15.641 23.886  -0.741 1.00 40.94  ? 554 HOH C O   1 
HETATM 8833 O  O   . HOH JA 14 .   ? -9.246  -10.193 13.012 1.00 38.55  ? 555 HOH C O   1 
HETATM 8834 O  O   . HOH JA 14 .   ? -15.017 33.181  24.328 1.00 37.69  ? 556 HOH C O   1 
HETATM 8835 O  O   . HOH JA 14 .   ? -16.412 30.462  25.656 1.00 42.60  ? 557 HOH C O   1 
HETATM 8836 O  O   . HOH JA 14 .   ? 1.486   14.603  11.075 1.00 42.29  ? 558 HOH C O   1 
HETATM 8837 O  O   . HOH JA 14 .   ? -26.665 -3.424  4.831  1.00 42.16  ? 559 HOH C O   1 
HETATM 8838 O  O   . HOH JA 14 .   ? 4.597   7.343   31.622 1.00 38.62  ? 560 HOH C O   1 
HETATM 8839 O  O   . HOH JA 14 .   ? -24.182 16.732  7.523  1.00 43.50  ? 561 HOH C O   1 
HETATM 8840 O  O   . HOH JA 14 .   ? 10.749  17.621  27.411 1.00 41.03  ? 562 HOH C O   1 
HETATM 8841 O  O   . HOH JA 14 .   ? -12.197 -4.305  -3.768 1.00 41.44  ? 563 HOH C O   1 
HETATM 8842 O  O   . HOH JA 14 .   ? 0.781   4.397   34.196 1.00 43.25  ? 564 HOH C O   1 
HETATM 8843 O  O   . HOH JA 14 .   ? 13.696  15.482  0.840  1.00 44.08  ? 565 HOH C O   1 
HETATM 8844 O  O   . HOH JA 14 .   ? 13.052  -5.560  11.296 1.00 45.66  ? 566 HOH C O   1 
HETATM 8845 O  O   . HOH JA 14 .   ? -13.784 -4.415  -0.844 1.00 51.05  ? 567 HOH C O   1 
HETATM 8846 O  O   . HOH JA 14 .   ? 20.011  -1.840  33.448 1.00 42.14  ? 568 HOH C O   1 
HETATM 8847 O  O   . HOH JA 14 .   ? 0.824   12.282  14.430 1.00 40.07  ? 569 HOH C O   1 
HETATM 8848 O  O   . HOH JA 14 .   ? 22.483  -13.367 16.716 1.00 43.14  ? 570 HOH C O   1 
HETATM 8849 O  O   . HOH JA 14 .   ? 7.951   -11.791 28.623 1.00 39.80  ? 571 HOH C O   1 
HETATM 8850 O  O   . HOH JA 14 .   ? -15.430 30.610  34.257 1.00 43.40  ? 572 HOH C O   1 
# 
