data_9HE9
# 
_entry.id   9HE9 
# 
_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   9HE9         pdb_00009he9 10.2210/pdb9he9/pdb 
WWPDB D_1292136258 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Source and taxonomy' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            entity_src_gen 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_entity_src_gen.gene_src_common_name' 
2 2 'Structure model' '_entity_src_gen.host_org_common_name' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HE9 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xjulia@iqfr.csic.es 
_pdbx_contact_author.name_first         Julia 
_pdbx_contact_author.name_last          Sanz-Aparicio 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6849-8621 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fernandez-Garcia, A.' 1 0000-0003-2052-6483 
'Sanz-Aparicio, J.'    2 0000-0002-6849-8621 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Characterization of Recombinant Unspecific Peroxygenase from Candolleomyces aberdarensis through Crystallographic and Substrate Selectivity Studies
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202402015 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Menes-Rubio, A.'      1 ? 
primary 'Fernandez-Garcia, A.' 2 ? 
primary 'Monterrey, D.T.'      3 ? 
primary 'de Santos, P.G.'      4 ? 
primary 'Sanchez-Moreno, I.'   5 ? 
primary 'Sanz-Aparicio, J.'    6 ? 
primary 'Alcalde, M.'          7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Heme-thiolate peroxidase' 36630.445 3   1.11.2.1 ? ? ? 
2  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1   ?        ? ? ? 
3  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1235.105  1   ?        ? ? ? 
4  branched    man 
;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   2   ?        ? ? ? 
5  branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1   ?        ? ? ? 
6  branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1   ? ? ? ? 
7  non-polymer syn 'LAURIC ACID' 200.318   2   ?        ? ? ? 
8  non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   3   ?        ? ? ? 
9  non-polymer syn GLYCEROL 92.094    3   ?        ? ? ? 
10 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
11 non-polymer syn 'SULFATE ION' 96.063    5   ?        ? ? ? 
12 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
13 water       nat water 18.015    738 ?        ? ? ? 
# 
_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  'LAURIC ACID'                                         DAO 
8  '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
9  GLYCEROL                                              GOL 
10 'PROTOPORPHYRIN IX CONTAINING FE'                     HEM 
11 'SULFATE ION'                                         SO4 
12 'MAGNESIUM ION'                                       MG  
13 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   GLY n 
1 3   VAL n 
1 4   ASP n 
1 5   PRO n 
1 6   PRO n 
1 7   PRO n 
1 8   PRO n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  PRO n 
1 13  SER n 
1 14  PHE n 
1 15  THR n 
1 16  GLY n 
1 17  THR n 
1 18  LYS n 
1 19  LEU n 
1 20  VAL n 
1 21  ASN n 
1 22  ASP n 
1 23  ALA n 
1 24  ASP n 
1 25  HIS n 
1 26  PRO n 
1 27  TRP n 
1 28  GLN n 
1 29  PRO n 
1 30  LEU n 
1 31  ARG n 
1 32  GLU n 
1 33  GLY n 
1 34  ASP n 
1 35  ILE n 
1 36  ARG n 
1 37  GLY n 
1 38  PRO n 
1 39  CYS n 
1 40  PRO n 
1 41  GLY n 
1 42  LEU n 
1 43  ASN n 
1 44  THR n 
1 45  LEU n 
1 46  ALA n 
1 47  SER n 
1 48  HIS n 
1 49  GLY n 
1 50  TYR n 
1 51  LEU n 
1 52  PRO n 
1 53  ARG n 
1 54  ASP n 
1 55  GLY n 
1 56  VAL n 
1 57  ALA n 
1 58  THR n 
1 59  PRO n 
1 60  ALA n 
1 61  GLN n 
1 62  ILE n 
1 63  ILE n 
1 64  THR n 
1 65  ALA n 
1 66  THR n 
1 67  GLN n 
1 68  GLU n 
1 69  GLY n 
1 70  PHE n 
1 71  ASN n 
1 72  PHE n 
1 73  GLU n 
1 74  ASN n 
1 75  ASN n 
1 76  ALA n 
1 77  ALA n 
1 78  ILE n 
1 79  VAL n 
1 80  ALA n 
1 81  THR n 
1 82  TYR n 
1 83  LEU n 
1 84  GLY n 
1 85  HIS n 
1 86  LEU n 
1 87  LEU n 
1 88  ASN n 
1 89  GLY n 
1 90  ASN n 
1 91  LEU n 
1 92  VAL n 
1 93  THR n 
1 94  ASP n 
1 95  LEU n 
1 96  LEU n 
1 97  SER n 
1 98  ILE n 
1 99  GLY n 
1 100 GLY n 
1 101 ALA n 
1 102 THR n 
1 103 PRO n 
1 104 LYS n 
1 105 THR n 
1 106 GLY n 
1 107 PRO n 
1 108 PRO n 
1 109 PRO n 
1 110 PRO n 
1 111 PRO n 
1 112 PRO n 
1 113 ALA n 
1 114 HIS n 
1 115 ALA n 
1 116 GLY n 
1 117 GLY n 
1 118 LEU n 
1 119 ASN n 
1 120 VAL n 
1 121 HIS n 
1 122 GLY n 
1 123 THR n 
1 124 PHE n 
1 125 GLU n 
1 126 GLY n 
1 127 ASP n 
1 128 ALA n 
1 129 GLY n 
1 130 MET n 
1 131 THR n 
1 132 ARG n 
1 133 ALA n 
1 134 ASP n 
1 135 GLU n 
1 136 PHE n 
1 137 PHE n 
1 138 GLY n 
1 139 ASP n 
1 140 ASN n 
1 141 HIS n 
1 142 SER n 
1 143 PHE n 
1 144 ASN n 
1 145 GLN n 
1 146 THR n 
1 147 LEU n 
1 148 PHE n 
1 149 ASP n 
1 150 LYS n 
1 151 PHE n 
1 152 VAL n 
1 153 ASP n 
1 154 PHE n 
1 155 SER n 
1 156 ASN n 
1 157 ARG n 
1 158 TYR n 
1 159 GLY n 
1 160 GLY n 
1 161 GLY n 
1 162 PHE n 
1 163 TYR n 
1 164 ASN n 
1 165 LEU n 
1 166 THR n 
1 167 VAL n 
1 168 ALA n 
1 169 GLY n 
1 170 GLU n 
1 171 LEU n 
1 172 ARG n 
1 173 TYR n 
1 174 SER n 
1 175 ARG n 
1 176 ILE n 
1 177 GLN n 
1 178 ASP n 
1 179 SER n 
1 180 ILE n 
1 181 ALA n 
1 182 THR n 
1 183 ASN n 
1 184 PRO n 
1 185 GLU n 
1 186 PHE n 
1 187 GLN n 
1 188 PHE n 
1 189 LYS n 
1 190 ASN n 
1 191 VAL n 
1 192 ARG n 
1 193 PHE n 
1 194 ILE n 
1 195 THR n 
1 196 ALA n 
1 197 TYR n 
1 198 GLY n 
1 199 GLU n 
1 200 THR n 
1 201 VAL n 
1 202 PHE n 
1 203 PRO n 
1 204 ILE n 
1 205 ASN n 
1 206 LEU n 
1 207 PHE n 
1 208 VAL n 
1 209 ASP n 
1 210 GLY n 
1 211 ARG n 
1 212 VAL n 
1 213 THR n 
1 214 THR n 
1 215 ASP n 
1 216 ARG n 
1 217 LYS n 
1 218 LEU n 
1 219 SER n 
1 220 MET n 
1 221 GLU n 
1 222 ASP n 
1 223 ALA n 
1 224 ALA n 
1 225 SER n 
1 226 ILE n 
1 227 PHE n 
1 228 ARG n 
1 229 ASP n 
1 230 MET n 
1 231 ARG n 
1 232 PHE n 
1 233 PRO n 
1 234 ASP n 
1 235 ASP n 
1 236 PHE n 
1 237 HIS n 
1 238 ARG n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 PRO n 
1 243 ALA n 
1 244 SER n 
1 245 ASN n 
1 246 GLU n 
1 247 GLY n 
1 248 ALA n 
1 249 ASP n 
1 250 GLN n 
1 251 VAL n 
1 252 LEU n 
1 253 ALA n 
1 254 ALA n 
1 255 HIS n 
1 256 PRO n 
1 257 TRP n 
1 258 VAL n 
1 259 PRO n 
1 260 GLY n 
1 261 GLY n 
1 262 ASN n 
1 263 ALA n 
1 264 ASP n 
1 265 ASN n 
1 266 GLN n 
1 267 VAL n 
1 268 ASN n 
1 269 ASN n 
1 270 TYR n 
1 271 VAL n 
1 272 GLU n 
1 273 ASP n 
1 274 PRO n 
1 275 ASP n 
1 276 SER n 
1 277 ALA n 
1 278 ASP n 
1 279 PHE n 
1 280 THR n 
1 281 HIS n 
1 282 LEU n 
1 283 CYS n 
1 284 ARG n 
1 285 LEU n 
1 286 TYR n 
1 287 GLU n 
1 288 PHE n 
1 289 VAL n 
1 290 VAL n 
1 291 GLY n 
1 292 SER n 
1 293 VAL n 
1 294 GLN n 
1 295 GLU n 
1 296 LEU n 
1 297 TYR n 
1 298 PRO n 
1 299 ASN n 
1 300 PRO n 
1 301 THR n 
1 302 GLY n 
1 303 ILE n 
1 304 LEU n 
1 305 ARG n 
1 306 ARG n 
1 307 ASN n 
1 308 LEU n 
1 309 ILE n 
1 310 LYS n 
1 311 ASN n 
1 312 LEU n 
1 313 HIS n 
1 314 TYR n 
1 315 TRP n 
1 316 TRP n 
1 317 THR n 
1 318 GLY n 
1 319 VAL n 
1 320 ASN n 
1 321 VAL n 
1 322 ALA n 
1 323 PHE n 
1 324 GLY n 
1 325 GLY n 
1 326 CYS n 
1 327 ASP n 
1 328 GLU n 
1 329 LEU n 
1 330 PHE n 
1 331 PRO n 
1 332 TYR n 
1 333 GLY n 
1 334 GLN n 
1 335 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   335 
_entity_src_gen.gene_src_common_name               'basidiomycete fungi' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EST38_g8238 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Candolleomyces aberdarensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2316362 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               yeast 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella phaffii CBS 7435' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     981350 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
6 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1  2 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
2  2 'WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1' WURCS PDB2Glycan 
1.1.0 
3  2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}' LINUCS PDB-CARE   ? 
4  3 'DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
5  3 'WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1' 
WURCS                       PDB2Glycan 1.1.0 
6  3 
;[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}
;
LINUCS                      PDB-CARE   ?     
7  4 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
8  4 '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 
9  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   
?     
10 5 'DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1' WURCS 
PDB2Glycan 1.1.0 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
13 6 DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}' 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 O3 HO3 sing ? 
14 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
15 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
16 5 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
17 5 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
18 5 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
19 6 2 NAG C1 O1 1 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 
ALA 'L-peptide linking'           y ALANINE                                               ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking'           y ARGININE                                              ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking'           y ASPARAGINE                                            ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                                       ? 'C4 H7 N O4'       133.103 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                                  'beta-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
CYS 'L-peptide linking'           y CYSTEINE                                              ? 'C3 H7 N O2 S'     121.158 
DAO non-polymer                   . 'LAURIC ACID'                                         ? 'C12 H24 O2'       200.318 
EPE non-polymer                   . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'   238.305 
GLN 'L-peptide linking'           y GLUTAMINE                                             ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'             y GLYCINE                                               ? 'C2 H5 N O2'       75.067  
GOL non-polymer                   . GLYCEROL                                              'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'         92.094  
HEM non-polymer                   . 'PROTOPORPHYRIN IX CONTAINING FE'                     HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking'           y HISTIDINE                                             ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer                   . WATER                                                 ? 'H2 O'             18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                                            ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking'           y LEUCINE                                               ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking'           y LYSINE                                                ? 'C6 H15 N2 O2 1'   147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                                 'alpha-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
MET 'L-peptide linking'           y METHIONINE                                            ? 'C5 H11 N O2 S'    149.211 
MG  non-polymer                   . 'MAGNESIUM ION'                                       ? 'Mg 2'             24.305  
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose              
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                                         ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking'           y PROLINE                                               ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking'           y SERINE                                                ? 'C3 H7 N O3'       105.093 
SO4 non-polymer                   . 'SULFATE ION'                                         ? 'O4 S -2'          96.063  
THR 'L-peptide linking'           y THREONINE                                             ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking'           y TYROSINE                                              ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking'           y VALINE                                                ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   14  14  GLN GLN A . n 
A 1 2   GLY 2   15  15  GLY GLY A . n 
A 1 3   VAL 3   16  16  VAL VAL A . n 
A 1 4   ASP 4   17  17  ASP ASP A . n 
A 1 5   PRO 5   18  18  PRO PRO A . n 
A 1 6   PRO 6   19  19  PRO PRO A . n 
A 1 7   PRO 7   20  20  PRO PRO A . n 
A 1 8   PRO 8   21  21  PRO PRO A . n 
A 1 9   PRO 9   22  22  PRO PRO A . n 
A 1 10  GLY 10  23  23  GLY GLY A . n 
A 1 11  PRO 11  24  24  PRO PRO A . n 
A 1 12  PRO 12  25  25  PRO PRO A . n 
A 1 13  SER 13  26  26  SER SER A . n 
A 1 14  PHE 14  27  27  PHE PHE A . n 
A 1 15  THR 15  28  28  THR THR A . n 
A 1 16  GLY 16  29  29  GLY GLY A . n 
A 1 17  THR 17  30  30  THR THR A . n 
A 1 18  LYS 18  31  31  LYS LYS A . n 
A 1 19  LEU 19  32  32  LEU LEU A . n 
A 1 20  VAL 20  33  33  VAL VAL A . n 
A 1 21  ASN 21  34  34  ASN ASN A . n 
A 1 22  ASP 22  35  35  ASP ASP A . n 
A 1 23  ALA 23  36  36  ALA ALA A . n 
A 1 24  ASP 24  37  37  ASP ASP A . n 
A 1 25  HIS 25  38  38  HIS HIS A . n 
A 1 26  PRO 26  39  39  PRO PRO A . n 
A 1 27  TRP 27  40  40  TRP TRP A . n 
A 1 28  GLN 28  41  41  GLN GLN A . n 
A 1 29  PRO 29  42  42  PRO PRO A . n 
A 1 30  LEU 30  43  43  LEU LEU A . n 
A 1 31  ARG 31  44  44  ARG ARG A . n 
A 1 32  GLU 32  45  45  GLU GLU A . n 
A 1 33  GLY 33  46  46  GLY GLY A . n 
A 1 34  ASP 34  47  47  ASP ASP A . n 
A 1 35  ILE 35  48  48  ILE ILE A . n 
A 1 36  ARG 36  49  49  ARG ARG A . n 
A 1 37  GLY 37  50  50  GLY GLY A . n 
A 1 38  PRO 38  51  51  PRO PRO A . n 
A 1 39  CYS 39  52  52  CYS CYS A . n 
A 1 40  PRO 40  53  53  PRO PRO A . n 
A 1 41  GLY 41  54  54  GLY GLY A . n 
A 1 42  LEU 42  55  55  LEU LEU A . n 
A 1 43  ASN 43  56  56  ASN ASN A . n 
A 1 44  THR 44  57  57  THR THR A . n 
A 1 45  LEU 45  58  58  LEU LEU A . n 
A 1 46  ALA 46  59  59  ALA ALA A . n 
A 1 47  SER 47  60  60  SER SER A . n 
A 1 48  HIS 48  61  61  HIS HIS A . n 
A 1 49  GLY 49  62  62  GLY GLY A . n 
A 1 50  TYR 50  63  63  TYR TYR A . n 
A 1 51  LEU 51  64  64  LEU LEU A . n 
A 1 52  PRO 52  65  65  PRO PRO A . n 
A 1 53  ARG 53  66  66  ARG ARG A . n 
A 1 54  ASP 54  67  67  ASP ASP A . n 
A 1 55  GLY 55  68  68  GLY GLY A . n 
A 1 56  VAL 56  69  69  VAL VAL A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  THR 58  71  71  THR THR A . n 
A 1 59  PRO 59  72  72  PRO PRO A . n 
A 1 60  ALA 60  73  73  ALA ALA A . n 
A 1 61  GLN 61  74  74  GLN GLN A . n 
A 1 62  ILE 62  75  75  ILE ILE A . n 
A 1 63  ILE 63  76  76  ILE ILE A . n 
A 1 64  THR 64  77  77  THR THR A . n 
A 1 65  ALA 65  78  78  ALA ALA A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  GLN 67  80  80  GLN GLN A . n 
A 1 68  GLU 68  81  81  GLU GLU A . n 
A 1 69  GLY 69  82  82  GLY GLY A . n 
A 1 70  PHE 70  83  83  PHE PHE A . n 
A 1 71  ASN 71  84  84  ASN ASN A . n 
A 1 72  PHE 72  85  85  PHE PHE A . n 
A 1 73  GLU 73  86  86  GLU GLU A . n 
A 1 74  ASN 74  87  87  ASN ASN A . n 
A 1 75  ASN 75  88  88  ASN ASN A . n 
A 1 76  ALA 76  89  89  ALA ALA A . n 
A 1 77  ALA 77  90  90  ALA ALA A . n 
A 1 78  ILE 78  91  91  ILE ILE A . n 
A 1 79  VAL 79  92  92  VAL VAL A . n 
A 1 80  ALA 80  93  93  ALA ALA A . n 
A 1 81  THR 81  94  94  THR THR A . n 
A 1 82  TYR 82  95  95  TYR TYR A . n 
A 1 83  LEU 83  96  96  LEU LEU A . n 
A 1 84  GLY 84  97  97  GLY GLY A . n 
A 1 85  HIS 85  98  98  HIS HIS A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  LEU 87  100 100 LEU LEU A . n 
A 1 88  ASN 88  101 101 ASN ASN A . n 
A 1 89  GLY 89  102 102 GLY GLY A . n 
A 1 90  ASN 90  103 103 ASN ASN A . n 
A 1 91  LEU 91  104 104 LEU LEU A . n 
A 1 92  VAL 92  105 105 VAL VAL A . n 
A 1 93  THR 93  106 106 THR THR A . n 
A 1 94  ASP 94  107 107 ASP ASP A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LEU 96  109 109 LEU LEU A . n 
A 1 97  SER 97  110 110 SER SER A . n 
A 1 98  ILE 98  111 111 ILE ILE A . n 
A 1 99  GLY 99  112 112 GLY GLY A . n 
A 1 100 GLY 100 113 113 GLY GLY A . n 
A 1 101 ALA 101 114 114 ALA ALA A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 PRO 103 116 116 PRO PRO A . n 
A 1 104 LYS 104 117 117 LYS LYS A . n 
A 1 105 THR 105 118 118 THR THR A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 PRO 107 120 120 PRO PRO A . n 
A 1 108 PRO 108 121 121 PRO PRO A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PRO 110 123 123 PRO PRO A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 PRO 112 125 125 PRO PRO A . n 
A 1 113 ALA 113 126 126 ALA ALA A . n 
A 1 114 HIS 114 127 127 HIS HIS A . n 
A 1 115 ALA 115 128 128 ALA ALA A . n 
A 1 116 GLY 116 129 129 GLY GLY A . n 
A 1 117 GLY 117 130 130 GLY GLY A . n 
A 1 118 LEU 118 131 131 LEU LEU A . n 
A 1 119 ASN 119 132 132 ASN ASN A . n 
A 1 120 VAL 120 133 133 VAL VAL A . n 
A 1 121 HIS 121 134 134 HIS HIS A . n 
A 1 122 GLY 122 135 135 GLY GLY A . n 
A 1 123 THR 123 136 136 THR THR A . n 
A 1 124 PHE 124 137 137 PHE PHE A . n 
A 1 125 GLU 125 138 138 GLU GLU A . n 
A 1 126 GLY 126 139 139 GLY GLY A . n 
A 1 127 ASP 127 140 140 ASP ASP A . n 
A 1 128 ALA 128 141 141 ALA ALA A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 MET 130 143 143 MET MET A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 ARG 132 145 145 ARG ARG A . n 
A 1 133 ALA 133 146 146 ALA ALA A . n 
A 1 134 ASP 134 147 147 ASP ASP A . n 
A 1 135 GLU 135 148 148 GLU GLU A . n 
A 1 136 PHE 136 149 149 PHE PHE A . n 
A 1 137 PHE 137 150 150 PHE PHE A . n 
A 1 138 GLY 138 151 151 GLY GLY A . n 
A 1 139 ASP 139 152 152 ASP ASP A . n 
A 1 140 ASN 140 153 153 ASN ASN A . n 
A 1 141 HIS 141 154 154 HIS HIS A . n 
A 1 142 SER 142 155 155 SER SER A . n 
A 1 143 PHE 143 156 156 PHE PHE A . n 
A 1 144 ASN 144 157 157 ASN ASN A . n 
A 1 145 GLN 145 158 158 GLN GLN A . n 
A 1 146 THR 146 159 159 THR THR A . n 
A 1 147 LEU 147 160 160 LEU LEU A . n 
A 1 148 PHE 148 161 161 PHE PHE A . n 
A 1 149 ASP 149 162 162 ASP ASP A . n 
A 1 150 LYS 150 163 163 LYS LYS A . n 
A 1 151 PHE 151 164 164 PHE PHE A . n 
A 1 152 VAL 152 165 165 VAL VAL A . n 
A 1 153 ASP 153 166 166 ASP ASP A . n 
A 1 154 PHE 154 167 167 PHE PHE A . n 
A 1 155 SER 155 168 168 SER SER A . n 
A 1 156 ASN 156 169 169 ASN ASN A . n 
A 1 157 ARG 157 170 170 ARG ARG A . n 
A 1 158 TYR 158 171 171 TYR TYR A . n 
A 1 159 GLY 159 172 172 GLY GLY A . n 
A 1 160 GLY 160 173 173 GLY GLY A . n 
A 1 161 GLY 161 174 174 GLY GLY A . n 
A 1 162 PHE 162 175 175 PHE PHE A . n 
A 1 163 TYR 163 176 176 TYR TYR A . n 
A 1 164 ASN 164 177 177 ASN ASN A . n 
A 1 165 LEU 165 178 178 LEU LEU A . n 
A 1 166 THR 166 179 179 THR THR A . n 
A 1 167 VAL 167 180 180 VAL VAL A . n 
A 1 168 ALA 168 181 181 ALA ALA A . n 
A 1 169 GLY 169 182 182 GLY GLY A . n 
A 1 170 GLU 170 183 183 GLU GLU A . n 
A 1 171 LEU 171 184 184 LEU LEU A . n 
A 1 172 ARG 172 185 185 ARG ARG A . n 
A 1 173 TYR 173 186 186 TYR TYR A . n 
A 1 174 SER 174 187 187 SER SER A . n 
A 1 175 ARG 175 188 188 ARG ARG A . n 
A 1 176 ILE 176 189 189 ILE ILE A . n 
A 1 177 GLN 177 190 190 GLN GLN A . n 
A 1 178 ASP 178 191 191 ASP ASP A . n 
A 1 179 SER 179 192 192 SER SER A . n 
A 1 180 ILE 180 193 193 ILE ILE A . n 
A 1 181 ALA 181 194 194 ALA ALA A . n 
A 1 182 THR 182 195 195 THR THR A . n 
A 1 183 ASN 183 196 196 ASN ASN A . n 
A 1 184 PRO 184 197 197 PRO PRO A . n 
A 1 185 GLU 185 198 198 GLU GLU A . n 
A 1 186 PHE 186 199 199 PHE PHE A . n 
A 1 187 GLN 187 200 200 GLN GLN A . n 
A 1 188 PHE 188 201 201 PHE PHE A . n 
A 1 189 LYS 189 202 202 LYS LYS A . n 
A 1 190 ASN 190 203 203 ASN ASN A . n 
A 1 191 VAL 191 204 204 VAL VAL A . n 
A 1 192 ARG 192 205 205 ARG ARG A . n 
A 1 193 PHE 193 206 206 PHE PHE A . n 
A 1 194 ILE 194 207 207 ILE ILE A . n 
A 1 195 THR 195 208 208 THR THR A . n 
A 1 196 ALA 196 209 209 ALA ALA A . n 
A 1 197 TYR 197 210 210 TYR TYR A . n 
A 1 198 GLY 198 211 211 GLY GLY A . n 
A 1 199 GLU 199 212 212 GLU GLU A . n 
A 1 200 THR 200 213 213 THR THR A . n 
A 1 201 VAL 201 214 214 VAL VAL A . n 
A 1 202 PHE 202 215 215 PHE PHE A . n 
A 1 203 PRO 203 216 216 PRO PRO A . n 
A 1 204 ILE 204 217 217 ILE ILE A . n 
A 1 205 ASN 205 218 218 ASN ASN A . n 
A 1 206 LEU 206 219 219 LEU LEU A . n 
A 1 207 PHE 207 220 220 PHE PHE A . n 
A 1 208 VAL 208 221 221 VAL VAL A . n 
A 1 209 ASP 209 222 222 ASP ASP A . n 
A 1 210 GLY 210 223 223 GLY GLY A . n 
A 1 211 ARG 211 224 224 ARG ARG A . n 
A 1 212 VAL 212 225 225 VAL VAL A . n 
A 1 213 THR 213 226 226 THR THR A . n 
A 1 214 THR 214 227 227 THR THR A . n 
A 1 215 ASP 215 228 228 ASP ASP A . n 
A 1 216 ARG 216 229 229 ARG ARG A . n 
A 1 217 LYS 217 230 230 LYS LYS A . n 
A 1 218 LEU 218 231 231 LEU LEU A . n 
A 1 219 SER 219 232 232 SER SER A . n 
A 1 220 MET 220 233 233 MET MET A . n 
A 1 221 GLU 221 234 234 GLU GLU A . n 
A 1 222 ASP 222 235 235 ASP ASP A . n 
A 1 223 ALA 223 236 236 ALA ALA A . n 
A 1 224 ALA 224 237 237 ALA ALA A . n 
A 1 225 SER 225 238 238 SER SER A . n 
A 1 226 ILE 226 239 239 ILE ILE A . n 
A 1 227 PHE 227 240 240 PHE PHE A . n 
A 1 228 ARG 228 241 241 ARG ARG A . n 
A 1 229 ASP 229 242 242 ASP ASP A . n 
A 1 230 MET 230 243 243 MET MET A . n 
A 1 231 ARG 231 244 244 ARG ARG A . n 
A 1 232 PHE 232 245 245 PHE PHE A . n 
A 1 233 PRO 233 246 246 PRO PRO A . n 
A 1 234 ASP 234 247 247 ASP ASP A . n 
A 1 235 ASP 235 248 248 ASP ASP A . n 
A 1 236 PHE 236 249 249 PHE PHE A . n 
A 1 237 HIS 237 250 250 HIS HIS A . n 
A 1 238 ARG 238 251 251 ARG ARG A . n 
A 1 239 SER 239 252 252 SER SER A . n 
A 1 240 ALA 240 253 253 ALA ALA A . n 
A 1 241 VAL 241 254 254 VAL VAL A . n 
A 1 242 PRO 242 255 255 PRO PRO A . n 
A 1 243 ALA 243 256 256 ALA ALA A . n 
A 1 244 SER 244 257 257 SER SER A . n 
A 1 245 ASN 245 258 258 ASN ASN A . n 
A 1 246 GLU 246 259 259 GLU GLU A . n 
A 1 247 GLY 247 260 260 GLY GLY A . n 
A 1 248 ALA 248 261 261 ALA ALA A . n 
A 1 249 ASP 249 262 262 ASP ASP A . n 
A 1 250 GLN 250 263 263 GLN GLN A . n 
A 1 251 VAL 251 264 264 VAL VAL A . n 
A 1 252 LEU 252 265 265 LEU LEU A . n 
A 1 253 ALA 253 266 266 ALA ALA A . n 
A 1 254 ALA 254 267 267 ALA ALA A . n 
A 1 255 HIS 255 268 268 HIS HIS A . n 
A 1 256 PRO 256 269 269 PRO PRO A . n 
A 1 257 TRP 257 270 270 TRP TRP A . n 
A 1 258 VAL 258 271 271 VAL VAL A . n 
A 1 259 PRO 259 272 272 PRO PRO A . n 
A 1 260 GLY 260 273 273 GLY GLY A . n 
A 1 261 GLY 261 274 274 GLY GLY A . n 
A 1 262 ASN 262 275 275 ASN ASN A . n 
A 1 263 ALA 263 276 276 ALA ALA A . n 
A 1 264 ASP 264 277 277 ASP ASP A . n 
A 1 265 ASN 265 278 278 ASN ASN A . n 
A 1 266 GLN 266 279 279 GLN GLN A . n 
A 1 267 VAL 267 280 280 VAL VAL A . n 
A 1 268 ASN 268 281 281 ASN ASN A . n 
A 1 269 ASN 269 282 282 ASN ASN A . n 
A 1 270 TYR 270 283 283 TYR TYR A . n 
A 1 271 VAL 271 284 284 VAL VAL A . n 
A 1 272 GLU 272 285 285 GLU GLU A . n 
A 1 273 ASP 273 286 286 ASP ASP A . n 
A 1 274 PRO 274 287 287 PRO PRO A . n 
A 1 275 ASP 275 288 288 ASP ASP A . n 
A 1 276 SER 276 289 289 SER SER A . n 
A 1 277 ALA 277 290 290 ALA ALA A . n 
A 1 278 ASP 278 291 291 ASP ASP A . n 
A 1 279 PHE 279 292 292 PHE PHE A . n 
A 1 280 THR 280 293 293 THR THR A . n 
A 1 281 HIS 281 294 294 HIS HIS A . n 
A 1 282 LEU 282 295 295 LEU LEU A . n 
A 1 283 CYS 283 296 296 CYS CYS A . n 
A 1 284 ARG 284 297 297 ARG ARG A . n 
A 1 285 LEU 285 298 298 LEU LEU A . n 
A 1 286 TYR 286 299 299 TYR TYR A . n 
A 1 287 GLU 287 300 300 GLU GLU A . n 
A 1 288 PHE 288 301 301 PHE PHE A . n 
A 1 289 VAL 289 302 302 VAL VAL A . n 
A 1 290 VAL 290 303 303 VAL VAL A . n 
A 1 291 GLY 291 304 304 GLY GLY A . n 
A 1 292 SER 292 305 305 SER SER A . n 
A 1 293 VAL 293 306 306 VAL VAL A . n 
A 1 294 GLN 294 307 307 GLN GLN A . n 
A 1 295 GLU 295 308 308 GLU GLU A . n 
A 1 296 LEU 296 309 309 LEU LEU A . n 
A 1 297 TYR 297 310 310 TYR TYR A . n 
A 1 298 PRO 298 311 311 PRO PRO A . n 
A 1 299 ASN 299 312 312 ASN ASN A . n 
A 1 300 PRO 300 313 313 PRO PRO A . n 
A 1 301 THR 301 314 314 THR THR A . n 
A 1 302 GLY 302 315 315 GLY GLY A . n 
A 1 303 ILE 303 316 316 ILE ILE A . n 
A 1 304 LEU 304 317 317 LEU LEU A . n 
A 1 305 ARG 305 318 318 ARG ARG A . n 
A 1 306 ARG 306 319 319 ARG ARG A . n 
A 1 307 ASN 307 320 320 ASN ASN A . n 
A 1 308 LEU 308 321 321 LEU LEU A . n 
A 1 309 ILE 309 322 322 ILE ILE A . n 
A 1 310 LYS 310 323 323 LYS LYS A . n 
A 1 311 ASN 311 324 324 ASN ASN A . n 
A 1 312 LEU 312 325 325 LEU LEU A . n 
A 1 313 HIS 313 326 326 HIS HIS A . n 
A 1 314 TYR 314 327 327 TYR TYR A . n 
A 1 315 TRP 315 328 328 TRP TRP A . n 
A 1 316 TRP 316 329 329 TRP TRP A . n 
A 1 317 THR 317 330 330 THR THR A . n 
A 1 318 GLY 318 331 331 GLY GLY A . n 
A 1 319 VAL 319 332 332 VAL VAL A . n 
A 1 320 ASN 320 333 333 ASN ASN A . n 
A 1 321 VAL 321 334 334 VAL VAL A . n 
A 1 322 ALA 322 335 335 ALA ALA A . n 
A 1 323 PHE 323 336 336 PHE PHE A . n 
A 1 324 GLY 324 337 337 GLY GLY A . n 
A 1 325 GLY 325 338 338 GLY GLY A . n 
A 1 326 CYS 326 339 339 CYS CYS A . n 
A 1 327 ASP 327 340 340 ASP ASP A . n 
A 1 328 GLU 328 341 341 GLU GLU A . n 
A 1 329 LEU 329 342 342 LEU LEU A . n 
A 1 330 PHE 330 343 343 PHE PHE A . n 
A 1 331 PRO 331 344 344 PRO PRO A . n 
A 1 332 TYR 332 345 345 TYR TYR A . n 
A 1 333 GLY 333 346 346 GLY GLY A . n 
A 1 334 GLN 334 347 347 GLN GLN A . n 
A 1 335 LEU 335 348 348 LEU LEU A . n 
B 1 1   GLN 1   14  14  GLN GLN B . n 
B 1 2   GLY 2   15  15  GLY GLY B . n 
B 1 3   VAL 3   16  16  VAL VAL B . n 
B 1 4   ASP 4   17  17  ASP ASP B . n 
B 1 5   PRO 5   18  18  PRO PRO B . n 
B 1 6   PRO 6   19  19  PRO PRO B . n 
B 1 7   PRO 7   20  20  PRO PRO B . n 
B 1 8   PRO 8   21  21  PRO PRO B . n 
B 1 9   PRO 9   22  22  PRO PRO B . n 
B 1 10  GLY 10  23  23  GLY GLY B . n 
B 1 11  PRO 11  24  24  PRO PRO B . n 
B 1 12  PRO 12  25  25  PRO PRO B . n 
B 1 13  SER 13  26  26  SER SER B . n 
B 1 14  PHE 14  27  27  PHE PHE B . n 
B 1 15  THR 15  28  28  THR THR B . n 
B 1 16  GLY 16  29  29  GLY GLY B . n 
B 1 17  THR 17  30  30  THR THR B . n 
B 1 18  LYS 18  31  31  LYS LYS B . n 
B 1 19  LEU 19  32  32  LEU LEU B . n 
B 1 20  VAL 20  33  33  VAL VAL B . n 
B 1 21  ASN 21  34  34  ASN ASN B . n 
B 1 22  ASP 22  35  35  ASP ASP B . n 
B 1 23  ALA 23  36  36  ALA ALA B . n 
B 1 24  ASP 24  37  37  ASP ASP B . n 
B 1 25  HIS 25  38  38  HIS HIS B . n 
B 1 26  PRO 26  39  39  PRO PRO B . n 
B 1 27  TRP 27  40  40  TRP TRP B . n 
B 1 28  GLN 28  41  41  GLN GLN B . n 
B 1 29  PRO 29  42  42  PRO PRO B . n 
B 1 30  LEU 30  43  43  LEU LEU B . n 
B 1 31  ARG 31  44  44  ARG ARG B . n 
B 1 32  GLU 32  45  45  GLU GLU B . n 
B 1 33  GLY 33  46  46  GLY GLY B . n 
B 1 34  ASP 34  47  47  ASP ASP B . n 
B 1 35  ILE 35  48  48  ILE ILE B . n 
B 1 36  ARG 36  49  49  ARG ARG B . n 
B 1 37  GLY 37  50  50  GLY GLY B . n 
B 1 38  PRO 38  51  51  PRO PRO B . n 
B 1 39  CYS 39  52  52  CYS CYS B . n 
B 1 40  PRO 40  53  53  PRO PRO B . n 
B 1 41  GLY 41  54  54  GLY GLY B . n 
B 1 42  LEU 42  55  55  LEU LEU B . n 
B 1 43  ASN 43  56  56  ASN ASN B . n 
B 1 44  THR 44  57  57  THR THR B . n 
B 1 45  LEU 45  58  58  LEU LEU B . n 
B 1 46  ALA 46  59  59  ALA ALA B . n 
B 1 47  SER 47  60  60  SER SER B . n 
B 1 48  HIS 48  61  61  HIS HIS B . n 
B 1 49  GLY 49  62  62  GLY GLY B . n 
B 1 50  TYR 50  63  63  TYR TYR B . n 
B 1 51  LEU 51  64  64  LEU LEU B . n 
B 1 52  PRO 52  65  65  PRO PRO B . n 
B 1 53  ARG 53  66  66  ARG ARG B . n 
B 1 54  ASP 54  67  67  ASP ASP B . n 
B 1 55  GLY 55  68  68  GLY GLY B . n 
B 1 56  VAL 56  69  69  VAL VAL B . n 
B 1 57  ALA 57  70  70  ALA ALA B . n 
B 1 58  THR 58  71  71  THR THR B . n 
B 1 59  PRO 59  72  72  PRO PRO B . n 
B 1 60  ALA 60  73  73  ALA ALA B . n 
B 1 61  GLN 61  74  74  GLN GLN B . n 
B 1 62  ILE 62  75  75  ILE ILE B . n 
B 1 63  ILE 63  76  76  ILE ILE B . n 
B 1 64  THR 64  77  77  THR THR B . n 
B 1 65  ALA 65  78  78  ALA ALA B . n 
B 1 66  THR 66  79  79  THR THR B . n 
B 1 67  GLN 67  80  80  GLN GLN B . n 
B 1 68  GLU 68  81  81  GLU GLU B . n 
B 1 69  GLY 69  82  82  GLY GLY B . n 
B 1 70  PHE 70  83  83  PHE PHE B . n 
B 1 71  ASN 71  84  84  ASN ASN B . n 
B 1 72  PHE 72  85  85  PHE PHE B . n 
B 1 73  GLU 73  86  86  GLU GLU B . n 
B 1 74  ASN 74  87  87  ASN ASN B . n 
B 1 75  ASN 75  88  88  ASN ASN B . n 
B 1 76  ALA 76  89  89  ALA ALA B . n 
B 1 77  ALA 77  90  90  ALA ALA B . n 
B 1 78  ILE 78  91  91  ILE ILE B . n 
B 1 79  VAL 79  92  92  VAL VAL B . n 
B 1 80  ALA 80  93  93  ALA ALA B . n 
B 1 81  THR 81  94  94  THR THR B . n 
B 1 82  TYR 82  95  95  TYR TYR B . n 
B 1 83  LEU 83  96  96  LEU LEU B . n 
B 1 84  GLY 84  97  97  GLY GLY B . n 
B 1 85  HIS 85  98  98  HIS HIS B . n 
B 1 86  LEU 86  99  99  LEU LEU B . n 
B 1 87  LEU 87  100 100 LEU LEU B . n 
B 1 88  ASN 88  101 101 ASN ASN B . n 
B 1 89  GLY 89  102 102 GLY GLY B . n 
B 1 90  ASN 90  103 103 ASN ASN B . n 
B 1 91  LEU 91  104 104 LEU LEU B . n 
B 1 92  VAL 92  105 105 VAL VAL B . n 
B 1 93  THR 93  106 106 THR THR B . n 
B 1 94  ASP 94  107 107 ASP ASP B . n 
B 1 95  LEU 95  108 108 LEU LEU B . n 
B 1 96  LEU 96  109 109 LEU LEU B . n 
B 1 97  SER 97  110 110 SER SER B . n 
B 1 98  ILE 98  111 111 ILE ILE B . n 
B 1 99  GLY 99  112 112 GLY GLY B . n 
B 1 100 GLY 100 113 113 GLY GLY B . n 
B 1 101 ALA 101 114 114 ALA ALA B . n 
B 1 102 THR 102 115 115 THR THR B . n 
B 1 103 PRO 103 116 116 PRO PRO B . n 
B 1 104 LYS 104 117 117 LYS LYS B . n 
B 1 105 THR 105 118 118 THR THR B . n 
B 1 106 GLY 106 119 119 GLY GLY B . n 
B 1 107 PRO 107 120 120 PRO PRO B . n 
B 1 108 PRO 108 121 121 PRO PRO B . n 
B 1 109 PRO 109 122 122 PRO PRO B . n 
B 1 110 PRO 110 123 123 PRO PRO B . n 
B 1 111 PRO 111 124 124 PRO PRO B . n 
B 1 112 PRO 112 125 125 PRO PRO B . n 
B 1 113 ALA 113 126 126 ALA ALA B . n 
B 1 114 HIS 114 127 127 HIS HIS B . n 
B 1 115 ALA 115 128 128 ALA ALA B . n 
B 1 116 GLY 116 129 129 GLY GLY B . n 
B 1 117 GLY 117 130 130 GLY GLY B . n 
B 1 118 LEU 118 131 131 LEU LEU B . n 
B 1 119 ASN 119 132 132 ASN ASN B . n 
B 1 120 VAL 120 133 133 VAL VAL B . n 
B 1 121 HIS 121 134 134 HIS HIS B . n 
B 1 122 GLY 122 135 135 GLY GLY B . n 
B 1 123 THR 123 136 136 THR THR B . n 
B 1 124 PHE 124 137 137 PHE PHE B . n 
B 1 125 GLU 125 138 138 GLU GLU B . n 
B 1 126 GLY 126 139 139 GLY GLY B . n 
B 1 127 ASP 127 140 140 ASP ASP B . n 
B 1 128 ALA 128 141 141 ALA ALA B . n 
B 1 129 GLY 129 142 142 GLY GLY B . n 
B 1 130 MET 130 143 143 MET MET B . n 
B 1 131 THR 131 144 144 THR THR B . n 
B 1 132 ARG 132 145 145 ARG ARG B . n 
B 1 133 ALA 133 146 146 ALA ALA B . n 
B 1 134 ASP 134 147 147 ASP ASP B . n 
B 1 135 GLU 135 148 148 GLU GLU B . n 
B 1 136 PHE 136 149 149 PHE PHE B . n 
B 1 137 PHE 137 150 150 PHE PHE B . n 
B 1 138 GLY 138 151 151 GLY GLY B . n 
B 1 139 ASP 139 152 152 ASP ASP B . n 
B 1 140 ASN 140 153 153 ASN ASN B . n 
B 1 141 HIS 141 154 154 HIS HIS B . n 
B 1 142 SER 142 155 155 SER SER B . n 
B 1 143 PHE 143 156 156 PHE PHE B . n 
B 1 144 ASN 144 157 157 ASN ASN B . n 
B 1 145 GLN 145 158 158 GLN GLN B . n 
B 1 146 THR 146 159 159 THR THR B . n 
B 1 147 LEU 147 160 160 LEU LEU B . n 
B 1 148 PHE 148 161 161 PHE PHE B . n 
B 1 149 ASP 149 162 162 ASP ASP B . n 
B 1 150 LYS 150 163 163 LYS LYS B . n 
B 1 151 PHE 151 164 164 PHE PHE B . n 
B 1 152 VAL 152 165 165 VAL VAL B . n 
B 1 153 ASP 153 166 166 ASP ASP B . n 
B 1 154 PHE 154 167 167 PHE PHE B . n 
B 1 155 SER 155 168 168 SER SER B . n 
B 1 156 ASN 156 169 169 ASN ASN B . n 
B 1 157 ARG 157 170 170 ARG ARG B . n 
B 1 158 TYR 158 171 171 TYR TYR B . n 
B 1 159 GLY 159 172 172 GLY GLY B . n 
B 1 160 GLY 160 173 173 GLY GLY B . n 
B 1 161 GLY 161 174 174 GLY GLY B . n 
B 1 162 PHE 162 175 175 PHE PHE B . n 
B 1 163 TYR 163 176 176 TYR TYR B . n 
B 1 164 ASN 164 177 177 ASN ASN B . n 
B 1 165 LEU 165 178 178 LEU LEU B . n 
B 1 166 THR 166 179 179 THR THR B . n 
B 1 167 VAL 167 180 180 VAL VAL B . n 
B 1 168 ALA 168 181 181 ALA ALA B . n 
B 1 169 GLY 169 182 182 GLY GLY B . n 
B 1 170 GLU 170 183 183 GLU GLU B . n 
B 1 171 LEU 171 184 184 LEU LEU B . n 
B 1 172 ARG 172 185 185 ARG ARG B . n 
B 1 173 TYR 173 186 186 TYR TYR B . n 
B 1 174 SER 174 187 187 SER SER B . n 
B 1 175 ARG 175 188 188 ARG ARG B . n 
B 1 176 ILE 176 189 189 ILE ILE B . n 
B 1 177 GLN 177 190 190 GLN GLN B . n 
B 1 178 ASP 178 191 191 ASP ASP B . n 
B 1 179 SER 179 192 192 SER SER B . n 
B 1 180 ILE 180 193 193 ILE ILE B . n 
B 1 181 ALA 181 194 194 ALA ALA B . n 
B 1 182 THR 182 195 195 THR THR B . n 
B 1 183 ASN 183 196 196 ASN ASN B . n 
B 1 184 PRO 184 197 197 PRO PRO B . n 
B 1 185 GLU 185 198 198 GLU GLU B . n 
B 1 186 PHE 186 199 199 PHE PHE B . n 
B 1 187 GLN 187 200 200 GLN GLN B . n 
B 1 188 PHE 188 201 201 PHE PHE B . n 
B 1 189 LYS 189 202 202 LYS LYS B . n 
B 1 190 ASN 190 203 203 ASN ASN B . n 
B 1 191 VAL 191 204 204 VAL VAL B . n 
B 1 192 ARG 192 205 205 ARG ARG B . n 
B 1 193 PHE 193 206 206 PHE PHE B . n 
B 1 194 ILE 194 207 207 ILE ILE B . n 
B 1 195 THR 195 208 208 THR THR B . n 
B 1 196 ALA 196 209 209 ALA ALA B . n 
B 1 197 TYR 197 210 210 TYR TYR B . n 
B 1 198 GLY 198 211 211 GLY GLY B . n 
B 1 199 GLU 199 212 212 GLU GLU B . n 
B 1 200 THR 200 213 213 THR THR B . n 
B 1 201 VAL 201 214 214 VAL VAL B . n 
B 1 202 PHE 202 215 215 PHE PHE B . n 
B 1 203 PRO 203 216 216 PRO PRO B . n 
B 1 204 ILE 204 217 217 ILE ILE B . n 
B 1 205 ASN 205 218 218 ASN ASN B . n 
B 1 206 LEU 206 219 219 LEU LEU B . n 
B 1 207 PHE 207 220 220 PHE PHE B . n 
B 1 208 VAL 208 221 221 VAL VAL B . n 
B 1 209 ASP 209 222 222 ASP ASP B . n 
B 1 210 GLY 210 223 223 GLY GLY B . n 
B 1 211 ARG 211 224 224 ARG ARG B . n 
B 1 212 VAL 212 225 225 VAL VAL B . n 
B 1 213 THR 213 226 226 THR THR B . n 
B 1 214 THR 214 227 227 THR THR B . n 
B 1 215 ASP 215 228 228 ASP ASP B . n 
B 1 216 ARG 216 229 229 ARG ARG B . n 
B 1 217 LYS 217 230 230 LYS LYS B . n 
B 1 218 LEU 218 231 231 LEU LEU B . n 
B 1 219 SER 219 232 232 SER SER B . n 
B 1 220 MET 220 233 233 MET MET B . n 
B 1 221 GLU 221 234 234 GLU GLU B . n 
B 1 222 ASP 222 235 235 ASP ASP B . n 
B 1 223 ALA 223 236 236 ALA ALA B . n 
B 1 224 ALA 224 237 237 ALA ALA B . n 
B 1 225 SER 225 238 238 SER SER B . n 
B 1 226 ILE 226 239 239 ILE ILE B . n 
B 1 227 PHE 227 240 240 PHE PHE B . n 
B 1 228 ARG 228 241 241 ARG ARG B . n 
B 1 229 ASP 229 242 242 ASP ASP B . n 
B 1 230 MET 230 243 243 MET MET B . n 
B 1 231 ARG 231 244 244 ARG ARG B . n 
B 1 232 PHE 232 245 245 PHE PHE B . n 
B 1 233 PRO 233 246 246 PRO PRO B . n 
B 1 234 ASP 234 247 247 ASP ASP B . n 
B 1 235 ASP 235 248 248 ASP ASP B . n 
B 1 236 PHE 236 249 249 PHE PHE B . n 
B 1 237 HIS 237 250 250 HIS HIS B . n 
B 1 238 ARG 238 251 251 ARG ARG B . n 
B 1 239 SER 239 252 252 SER SER B . n 
B 1 240 ALA 240 253 253 ALA ALA B . n 
B 1 241 VAL 241 254 254 VAL VAL B . n 
B 1 242 PRO 242 255 255 PRO PRO B . n 
B 1 243 ALA 243 256 256 ALA ALA B . n 
B 1 244 SER 244 257 257 SER SER B . n 
B 1 245 ASN 245 258 258 ASN ASN B . n 
B 1 246 GLU 246 259 259 GLU GLU B . n 
B 1 247 GLY 247 260 260 GLY GLY B . n 
B 1 248 ALA 248 261 261 ALA ALA B . n 
B 1 249 ASP 249 262 262 ASP ASP B . n 
B 1 250 GLN 250 263 263 GLN GLN B . n 
B 1 251 VAL 251 264 264 VAL VAL B . n 
B 1 252 LEU 252 265 265 LEU LEU B . n 
B 1 253 ALA 253 266 266 ALA ALA B . n 
B 1 254 ALA 254 267 267 ALA ALA B . n 
B 1 255 HIS 255 268 268 HIS HIS B . n 
B 1 256 PRO 256 269 269 PRO PRO B . n 
B 1 257 TRP 257 270 270 TRP TRP B . n 
B 1 258 VAL 258 271 271 VAL VAL B . n 
B 1 259 PRO 259 272 272 PRO PRO B . n 
B 1 260 GLY 260 273 273 GLY GLY B . n 
B 1 261 GLY 261 274 274 GLY GLY B . n 
B 1 262 ASN 262 275 275 ASN ASN B . n 
B 1 263 ALA 263 276 276 ALA ALA B . n 
B 1 264 ASP 264 277 277 ASP ASP B . n 
B 1 265 ASN 265 278 278 ASN ASN B . n 
B 1 266 GLN 266 279 279 GLN GLN B . n 
B 1 267 VAL 267 280 280 VAL VAL B . n 
B 1 268 ASN 268 281 281 ASN ASN B . n 
B 1 269 ASN 269 282 282 ASN ASN B . n 
B 1 270 TYR 270 283 283 TYR TYR B . n 
B 1 271 VAL 271 284 284 VAL VAL B . n 
B 1 272 GLU 272 285 285 GLU GLU B . n 
B 1 273 ASP 273 286 286 ASP ASP B . n 
B 1 274 PRO 274 287 287 PRO PRO B . n 
B 1 275 ASP 275 288 288 ASP ASP B . n 
B 1 276 SER 276 289 289 SER SER B . n 
B 1 277 ALA 277 290 290 ALA ALA B . n 
B 1 278 ASP 278 291 291 ASP ASP B . n 
B 1 279 PHE 279 292 292 PHE PHE B . n 
B 1 280 THR 280 293 293 THR THR B . n 
B 1 281 HIS 281 294 294 HIS HIS B . n 
B 1 282 LEU 282 295 295 LEU LEU B . n 
B 1 283 CYS 283 296 296 CYS CYS B . n 
B 1 284 ARG 284 297 297 ARG ARG B . n 
B 1 285 LEU 285 298 298 LEU LEU B . n 
B 1 286 TYR 286 299 299 TYR TYR B . n 
B 1 287 GLU 287 300 300 GLU GLU B . n 
B 1 288 PHE 288 301 301 PHE PHE B . n 
B 1 289 VAL 289 302 302 VAL VAL B . n 
B 1 290 VAL 290 303 303 VAL VAL B . n 
B 1 291 GLY 291 304 304 GLY GLY B . n 
B 1 292 SER 292 305 305 SER SER B . n 
B 1 293 VAL 293 306 306 VAL VAL B . n 
B 1 294 GLN 294 307 307 GLN GLN B . n 
B 1 295 GLU 295 308 308 GLU GLU B . n 
B 1 296 LEU 296 309 309 LEU LEU B . n 
B 1 297 TYR 297 310 310 TYR TYR B . n 
B 1 298 PRO 298 311 311 PRO PRO B . n 
B 1 299 ASN 299 312 312 ASN ASN B . n 
B 1 300 PRO 300 313 313 PRO PRO B . n 
B 1 301 THR 301 314 314 THR THR B . n 
B 1 302 GLY 302 315 315 GLY GLY B . n 
B 1 303 ILE 303 316 316 ILE ILE B . n 
B 1 304 LEU 304 317 317 LEU LEU B . n 
B 1 305 ARG 305 318 318 ARG ARG B . n 
B 1 306 ARG 306 319 319 ARG ARG B . n 
B 1 307 ASN 307 320 320 ASN ASN B . n 
B 1 308 LEU 308 321 321 LEU LEU B . n 
B 1 309 ILE 309 322 322 ILE ILE B . n 
B 1 310 LYS 310 323 323 LYS LYS B . n 
B 1 311 ASN 311 324 324 ASN ASN B . n 
B 1 312 LEU 312 325 325 LEU LEU B . n 
B 1 313 HIS 313 326 326 HIS HIS B . n 
B 1 314 TYR 314 327 327 TYR TYR B . n 
B 1 315 TRP 315 328 328 TRP TRP B . n 
B 1 316 TRP 316 329 329 TRP TRP B . n 
B 1 317 THR 317 330 330 THR THR B . n 
B 1 318 GLY 318 331 331 GLY GLY B . n 
B 1 319 VAL 319 332 332 VAL VAL B . n 
B 1 320 ASN 320 333 333 ASN ASN B . n 
B 1 321 VAL 321 334 334 VAL VAL B . n 
B 1 322 ALA 322 335 335 ALA ALA B . n 
B 1 323 PHE 323 336 336 PHE PHE B . n 
B 1 324 GLY 324 337 337 GLY GLY B . n 
B 1 325 GLY 325 338 338 GLY GLY B . n 
B 1 326 CYS 326 339 339 CYS CYS B . n 
B 1 327 ASP 327 340 340 ASP ASP B . n 
B 1 328 GLU 328 341 341 GLU GLU B . n 
B 1 329 LEU 329 342 342 LEU LEU B . n 
B 1 330 PHE 330 343 343 PHE PHE B . n 
B 1 331 PRO 331 344 344 PRO PRO B . n 
B 1 332 TYR 332 345 345 TYR TYR B . n 
B 1 333 GLY 333 346 346 GLY GLY B . n 
B 1 334 GLN 334 347 347 GLN GLN B . n 
B 1 335 LEU 335 348 348 LEU LEU B . n 
C 1 1   GLN 1   14  14  GLN GLN C . n 
C 1 2   GLY 2   15  15  GLY GLY C . n 
C 1 3   VAL 3   16  16  VAL VAL C . n 
C 1 4   ASP 4   17  17  ASP ASP C . n 
C 1 5   PRO 5   18  18  PRO PRO C . n 
C 1 6   PRO 6   19  19  PRO PRO C . n 
C 1 7   PRO 7   20  20  PRO PRO C . n 
C 1 8   PRO 8   21  21  PRO PRO C . n 
C 1 9   PRO 9   22  22  PRO PRO C . n 
C 1 10  GLY 10  23  23  GLY GLY C . n 
C 1 11  PRO 11  24  24  PRO PRO C . n 
C 1 12  PRO 12  25  25  PRO PRO C . n 
C 1 13  SER 13  26  26  SER SER C . n 
C 1 14  PHE 14  27  27  PHE PHE C . n 
C 1 15  THR 15  28  28  THR THR C . n 
C 1 16  GLY 16  29  29  GLY GLY C . n 
C 1 17  THR 17  30  30  THR THR C . n 
C 1 18  LYS 18  31  31  LYS LYS C . n 
C 1 19  LEU 19  32  32  LEU LEU C . n 
C 1 20  VAL 20  33  33  VAL VAL C . n 
C 1 21  ASN 21  34  34  ASN ASN C . n 
C 1 22  ASP 22  35  35  ASP ASP C . n 
C 1 23  ALA 23  36  36  ALA ALA C . n 
C 1 24  ASP 24  37  37  ASP ASP C . n 
C 1 25  HIS 25  38  38  HIS HIS C . n 
C 1 26  PRO 26  39  39  PRO PRO C . n 
C 1 27  TRP 27  40  40  TRP TRP C . n 
C 1 28  GLN 28  41  41  GLN GLN C . n 
C 1 29  PRO 29  42  42  PRO PRO C . n 
C 1 30  LEU 30  43  43  LEU LEU C . n 
C 1 31  ARG 31  44  44  ARG ARG C . n 
C 1 32  GLU 32  45  45  GLU GLU C . n 
C 1 33  GLY 33  46  46  GLY GLY C . n 
C 1 34  ASP 34  47  47  ASP ASP C . n 
C 1 35  ILE 35  48  48  ILE ILE C . n 
C 1 36  ARG 36  49  49  ARG ARG C . n 
C 1 37  GLY 37  50  50  GLY GLY C . n 
C 1 38  PRO 38  51  51  PRO PRO C . n 
C 1 39  CYS 39  52  52  CYS CYS C . n 
C 1 40  PRO 40  53  53  PRO PRO C . n 
C 1 41  GLY 41  54  54  GLY GLY C . n 
C 1 42  LEU 42  55  55  LEU LEU C . n 
C 1 43  ASN 43  56  56  ASN ASN C . n 
C 1 44  THR 44  57  57  THR THR C . n 
C 1 45  LEU 45  58  58  LEU LEU C . n 
C 1 46  ALA 46  59  59  ALA ALA C . n 
C 1 47  SER 47  60  60  SER SER C . n 
C 1 48  HIS 48  61  61  HIS HIS C . n 
C 1 49  GLY 49  62  62  GLY GLY C . n 
C 1 50  TYR 50  63  63  TYR TYR C . n 
C 1 51  LEU 51  64  64  LEU LEU C . n 
C 1 52  PRO 52  65  65  PRO PRO C . n 
C 1 53  ARG 53  66  66  ARG ARG C . n 
C 1 54  ASP 54  67  67  ASP ASP C . n 
C 1 55  GLY 55  68  68  GLY GLY C . n 
C 1 56  VAL 56  69  69  VAL VAL C . n 
C 1 57  ALA 57  70  70  ALA ALA C . n 
C 1 58  THR 58  71  71  THR THR C . n 
C 1 59  PRO 59  72  72  PRO PRO C . n 
C 1 60  ALA 60  73  73  ALA ALA C . n 
C 1 61  GLN 61  74  74  GLN GLN C . n 
C 1 62  ILE 62  75  75  ILE ILE C . n 
C 1 63  ILE 63  76  76  ILE ILE C . n 
C 1 64  THR 64  77  77  THR THR C . n 
C 1 65  ALA 65  78  78  ALA ALA C . n 
C 1 66  THR 66  79  79  THR THR C . n 
C 1 67  GLN 67  80  80  GLN GLN C . n 
C 1 68  GLU 68  81  81  GLU GLU C . n 
C 1 69  GLY 69  82  82  GLY GLY C . n 
C 1 70  PHE 70  83  83  PHE PHE C . n 
C 1 71  ASN 71  84  84  ASN ASN C . n 
C 1 72  PHE 72  85  85  PHE PHE C . n 
C 1 73  GLU 73  86  86  GLU GLU C . n 
C 1 74  ASN 74  87  87  ASN ASN C . n 
C 1 75  ASN 75  88  88  ASN ASN C . n 
C 1 76  ALA 76  89  89  ALA ALA C . n 
C 1 77  ALA 77  90  90  ALA ALA C . n 
C 1 78  ILE 78  91  91  ILE ILE C . n 
C 1 79  VAL 79  92  92  VAL VAL C . n 
C 1 80  ALA 80  93  93  ALA ALA C . n 
C 1 81  THR 81  94  94  THR THR C . n 
C 1 82  TYR 82  95  95  TYR TYR C . n 
C 1 83  LEU 83  96  96  LEU LEU C . n 
C 1 84  GLY 84  97  97  GLY GLY C . n 
C 1 85  HIS 85  98  98  HIS HIS C . n 
C 1 86  LEU 86  99  99  LEU LEU C . n 
C 1 87  LEU 87  100 100 LEU LEU C . n 
C 1 88  ASN 88  101 101 ASN ASN C . n 
C 1 89  GLY 89  102 102 GLY GLY C . n 
C 1 90  ASN 90  103 103 ASN ASN C . n 
C 1 91  LEU 91  104 104 LEU LEU C . n 
C 1 92  VAL 92  105 105 VAL VAL C . n 
C 1 93  THR 93  106 106 THR THR C . n 
C 1 94  ASP 94  107 107 ASP ASP C . n 
C 1 95  LEU 95  108 108 LEU LEU C . n 
C 1 96  LEU 96  109 109 LEU LEU C . n 
C 1 97  SER 97  110 110 SER SER C . n 
C 1 98  ILE 98  111 111 ILE ILE C . n 
C 1 99  GLY 99  112 112 GLY GLY C . n 
C 1 100 GLY 100 113 113 GLY GLY C . n 
C 1 101 ALA 101 114 114 ALA ALA C . n 
C 1 102 THR 102 115 115 THR THR C . n 
C 1 103 PRO 103 116 116 PRO PRO C . n 
C 1 104 LYS 104 117 117 LYS LYS C . n 
C 1 105 THR 105 118 118 THR THR C . n 
C 1 106 GLY 106 119 119 GLY GLY C . n 
C 1 107 PRO 107 120 120 PRO PRO C . n 
C 1 108 PRO 108 121 121 PRO PRO C . n 
C 1 109 PRO 109 122 122 PRO PRO C . n 
C 1 110 PRO 110 123 123 PRO PRO C . n 
C 1 111 PRO 111 124 124 PRO PRO C . n 
C 1 112 PRO 112 125 125 PRO PRO C . n 
C 1 113 ALA 113 126 126 ALA ALA C . n 
C 1 114 HIS 114 127 127 HIS HIS C . n 
C 1 115 ALA 115 128 128 ALA ALA C . n 
C 1 116 GLY 116 129 129 GLY GLY C . n 
C 1 117 GLY 117 130 130 GLY GLY C . n 
C 1 118 LEU 118 131 131 LEU LEU C . n 
C 1 119 ASN 119 132 132 ASN ASN C . n 
C 1 120 VAL 120 133 133 VAL VAL C . n 
C 1 121 HIS 121 134 134 HIS HIS C . n 
C 1 122 GLY 122 135 135 GLY GLY C . n 
C 1 123 THR 123 136 136 THR THR C . n 
C 1 124 PHE 124 137 137 PHE PHE C . n 
C 1 125 GLU 125 138 138 GLU GLU C . n 
C 1 126 GLY 126 139 139 GLY GLY C . n 
C 1 127 ASP 127 140 140 ASP ASP C . n 
C 1 128 ALA 128 141 141 ALA ALA C . n 
C 1 129 GLY 129 142 142 GLY GLY C . n 
C 1 130 MET 130 143 143 MET MET C . n 
C 1 131 THR 131 144 144 THR THR C . n 
C 1 132 ARG 132 145 145 ARG ARG C . n 
C 1 133 ALA 133 146 146 ALA ALA C . n 
C 1 134 ASP 134 147 147 ASP ASP C . n 
C 1 135 GLU 135 148 148 GLU GLU C . n 
C 1 136 PHE 136 149 149 PHE PHE C . n 
C 1 137 PHE 137 150 150 PHE PHE C . n 
C 1 138 GLY 138 151 151 GLY GLY C . n 
C 1 139 ASP 139 152 152 ASP ASP C . n 
C 1 140 ASN 140 153 153 ASN ASN C . n 
C 1 141 HIS 141 154 154 HIS HIS C . n 
C 1 142 SER 142 155 155 SER SER C . n 
C 1 143 PHE 143 156 156 PHE PHE C . n 
C 1 144 ASN 144 157 157 ASN ASN C . n 
C 1 145 GLN 145 158 158 GLN GLN C . n 
C 1 146 THR 146 159 159 THR THR C . n 
C 1 147 LEU 147 160 160 LEU LEU C . n 
C 1 148 PHE 148 161 161 PHE PHE C . n 
C 1 149 ASP 149 162 162 ASP ASP C . n 
C 1 150 LYS 150 163 163 LYS LYS C . n 
C 1 151 PHE 151 164 164 PHE PHE C . n 
C 1 152 VAL 152 165 165 VAL VAL C . n 
C 1 153 ASP 153 166 166 ASP ASP C . n 
C 1 154 PHE 154 167 167 PHE PHE C . n 
C 1 155 SER 155 168 168 SER SER C . n 
C 1 156 ASN 156 169 169 ASN ASN C . n 
C 1 157 ARG 157 170 170 ARG ARG C . n 
C 1 158 TYR 158 171 171 TYR TYR C . n 
C 1 159 GLY 159 172 172 GLY GLY C . n 
C 1 160 GLY 160 173 173 GLY GLY C . n 
C 1 161 GLY 161 174 174 GLY GLY C . n 
C 1 162 PHE 162 175 175 PHE PHE C . n 
C 1 163 TYR 163 176 176 TYR TYR C . n 
C 1 164 ASN 164 177 177 ASN ASN C . n 
C 1 165 LEU 165 178 178 LEU LEU C . n 
C 1 166 THR 166 179 179 THR THR C . n 
C 1 167 VAL 167 180 180 VAL VAL C . n 
C 1 168 ALA 168 181 181 ALA ALA C . n 
C 1 169 GLY 169 182 182 GLY GLY C . n 
C 1 170 GLU 170 183 183 GLU GLU C . n 
C 1 171 LEU 171 184 184 LEU LEU C . n 
C 1 172 ARG 172 185 185 ARG ARG C . n 
C 1 173 TYR 173 186 186 TYR TYR C . n 
C 1 174 SER 174 187 187 SER SER C . n 
C 1 175 ARG 175 188 188 ARG ARG C . n 
C 1 176 ILE 176 189 189 ILE ILE C . n 
C 1 177 GLN 177 190 190 GLN GLN C . n 
C 1 178 ASP 178 191 191 ASP ASP C . n 
C 1 179 SER 179 192 192 SER SER C . n 
C 1 180 ILE 180 193 193 ILE ILE C . n 
C 1 181 ALA 181 194 194 ALA ALA C . n 
C 1 182 THR 182 195 195 THR THR C . n 
C 1 183 ASN 183 196 196 ASN ASN C . n 
C 1 184 PRO 184 197 197 PRO PRO C . n 
C 1 185 GLU 185 198 198 GLU GLU C . n 
C 1 186 PHE 186 199 199 PHE PHE C . n 
C 1 187 GLN 187 200 200 GLN GLN C . n 
C 1 188 PHE 188 201 201 PHE PHE C . n 
C 1 189 LYS 189 202 202 LYS LYS C . n 
C 1 190 ASN 190 203 203 ASN ASN C . n 
C 1 191 VAL 191 204 204 VAL VAL C . n 
C 1 192 ARG 192 205 205 ARG ARG C . n 
C 1 193 PHE 193 206 206 PHE PHE C . n 
C 1 194 ILE 194 207 207 ILE ILE C . n 
C 1 195 THR 195 208 208 THR THR C . n 
C 1 196 ALA 196 209 209 ALA ALA C . n 
C 1 197 TYR 197 210 210 TYR TYR C . n 
C 1 198 GLY 198 211 211 GLY GLY C . n 
C 1 199 GLU 199 212 212 GLU GLU C . n 
C 1 200 THR 200 213 213 THR THR C . n 
C 1 201 VAL 201 214 214 VAL VAL C . n 
C 1 202 PHE 202 215 215 PHE PHE C . n 
C 1 203 PRO 203 216 216 PRO PRO C . n 
C 1 204 ILE 204 217 217 ILE ILE C . n 
C 1 205 ASN 205 218 218 ASN ASN C . n 
C 1 206 LEU 206 219 219 LEU LEU C . n 
C 1 207 PHE 207 220 220 PHE PHE C . n 
C 1 208 VAL 208 221 221 VAL VAL C . n 
C 1 209 ASP 209 222 222 ASP ASP C . n 
C 1 210 GLY 210 223 223 GLY GLY C . n 
C 1 211 ARG 211 224 224 ARG ARG C . n 
C 1 212 VAL 212 225 225 VAL VAL C . n 
C 1 213 THR 213 226 226 THR THR C . n 
C 1 214 THR 214 227 227 THR THR C . n 
C 1 215 ASP 215 228 228 ASP ASP C . n 
C 1 216 ARG 216 229 229 ARG ARG C . n 
C 1 217 LYS 217 230 230 LYS LYS C . n 
C 1 218 LEU 218 231 231 LEU LEU C . n 
C 1 219 SER 219 232 232 SER SER C . n 
C 1 220 MET 220 233 233 MET MET C . n 
C 1 221 GLU 221 234 234 GLU GLU C . n 
C 1 222 ASP 222 235 235 ASP ASP C . n 
C 1 223 ALA 223 236 236 ALA ALA C . n 
C 1 224 ALA 224 237 237 ALA ALA C . n 
C 1 225 SER 225 238 238 SER SER C . n 
C 1 226 ILE 226 239 239 ILE ILE C . n 
C 1 227 PHE 227 240 240 PHE PHE C . n 
C 1 228 ARG 228 241 241 ARG ARG C . n 
C 1 229 ASP 229 242 242 ASP ASP C . n 
C 1 230 MET 230 243 243 MET MET C . n 
C 1 231 ARG 231 244 244 ARG ARG C . n 
C 1 232 PHE 232 245 245 PHE PHE C . n 
C 1 233 PRO 233 246 246 PRO PRO C . n 
C 1 234 ASP 234 247 247 ASP ASP C . n 
C 1 235 ASP 235 248 248 ASP ASP C . n 
C 1 236 PHE 236 249 249 PHE PHE C . n 
C 1 237 HIS 237 250 250 HIS HIS C . n 
C 1 238 ARG 238 251 251 ARG ARG C . n 
C 1 239 SER 239 252 252 SER SER C . n 
C 1 240 ALA 240 253 253 ALA ALA C . n 
C 1 241 VAL 241 254 254 VAL VAL C . n 
C 1 242 PRO 242 255 255 PRO PRO C . n 
C 1 243 ALA 243 256 256 ALA ALA C . n 
C 1 244 SER 244 257 257 SER SER C . n 
C 1 245 ASN 245 258 258 ASN ASN C . n 
C 1 246 GLU 246 259 259 GLU GLU C . n 
C 1 247 GLY 247 260 260 GLY GLY C . n 
C 1 248 ALA 248 261 261 ALA ALA C . n 
C 1 249 ASP 249 262 262 ASP ASP C . n 
C 1 250 GLN 250 263 263 GLN GLN C . n 
C 1 251 VAL 251 264 264 VAL VAL C . n 
C 1 252 LEU 252 265 265 LEU LEU C . n 
C 1 253 ALA 253 266 266 ALA ALA C . n 
C 1 254 ALA 254 267 267 ALA ALA C . n 
C 1 255 HIS 255 268 268 HIS HIS C . n 
C 1 256 PRO 256 269 269 PRO PRO C . n 
C 1 257 TRP 257 270 270 TRP TRP C . n 
C 1 258 VAL 258 271 271 VAL VAL C . n 
C 1 259 PRO 259 272 272 PRO PRO C . n 
C 1 260 GLY 260 273 273 GLY GLY C . n 
C 1 261 GLY 261 274 274 GLY GLY C . n 
C 1 262 ASN 262 275 275 ASN ASN C . n 
C 1 263 ALA 263 276 276 ALA ALA C . n 
C 1 264 ASP 264 277 277 ASP ASP C . n 
C 1 265 ASN 265 278 278 ASN ASN C . n 
C 1 266 GLN 266 279 279 GLN GLN C . n 
C 1 267 VAL 267 280 280 VAL VAL C . n 
C 1 268 ASN 268 281 281 ASN ASN C . n 
C 1 269 ASN 269 282 282 ASN ASN C . n 
C 1 270 TYR 270 283 283 TYR TYR C . n 
C 1 271 VAL 271 284 284 VAL VAL C . n 
C 1 272 GLU 272 285 285 GLU GLU C . n 
C 1 273 ASP 273 286 286 ASP ASP C . n 
C 1 274 PRO 274 287 287 PRO PRO C . n 
C 1 275 ASP 275 288 288 ASP ASP C . n 
C 1 276 SER 276 289 289 SER SER C . n 
C 1 277 ALA 277 290 290 ALA ALA C . n 
C 1 278 ASP 278 291 291 ASP ASP C . n 
C 1 279 PHE 279 292 292 PHE PHE C . n 
C 1 280 THR 280 293 293 THR THR C . n 
C 1 281 HIS 281 294 294 HIS HIS C . n 
C 1 282 LEU 282 295 295 LEU LEU C . n 
C 1 283 CYS 283 296 296 CYS CYS C . n 
C 1 284 ARG 284 297 297 ARG ARG C . n 
C 1 285 LEU 285 298 298 LEU LEU C . n 
C 1 286 TYR 286 299 299 TYR TYR C . n 
C 1 287 GLU 287 300 300 GLU GLU C . n 
C 1 288 PHE 288 301 301 PHE PHE C . n 
C 1 289 VAL 289 302 302 VAL VAL C . n 
C 1 290 VAL 290 303 303 VAL VAL C . n 
C 1 291 GLY 291 304 304 GLY GLY C . n 
C 1 292 SER 292 305 305 SER SER C . n 
C 1 293 VAL 293 306 306 VAL VAL C . n 
C 1 294 GLN 294 307 307 GLN GLN C . n 
C 1 295 GLU 295 308 308 GLU GLU C . n 
C 1 296 LEU 296 309 309 LEU LEU C . n 
C 1 297 TYR 297 310 310 TYR TYR C . n 
C 1 298 PRO 298 311 311 PRO PRO C . n 
C 1 299 ASN 299 312 312 ASN ASN C . n 
C 1 300 PRO 300 313 313 PRO PRO C . n 
C 1 301 THR 301 314 314 THR THR C . n 
C 1 302 GLY 302 315 315 GLY GLY C . n 
C 1 303 ILE 303 316 316 ILE ILE C . n 
C 1 304 LEU 304 317 317 LEU LEU C . n 
C 1 305 ARG 305 318 318 ARG ARG C . n 
C 1 306 ARG 306 319 319 ARG ARG C . n 
C 1 307 ASN 307 320 320 ASN ASN C . n 
C 1 308 LEU 308 321 321 LEU LEU C . n 
C 1 309 ILE 309 322 322 ILE ILE C . n 
C 1 310 LYS 310 323 323 LYS LYS C . n 
C 1 311 ASN 311 324 324 ASN ASN C . n 
C 1 312 LEU 312 325 325 LEU LEU C . n 
C 1 313 HIS 313 326 326 HIS HIS C . n 
C 1 314 TYR 314 327 327 TYR TYR C . n 
C 1 315 TRP 315 328 328 TRP TRP C . n 
C 1 316 TRP 316 329 329 TRP TRP C . n 
C 1 317 THR 317 330 330 THR THR C . n 
C 1 318 GLY 318 331 331 GLY GLY C . n 
C 1 319 VAL 319 332 332 VAL VAL C . n 
C 1 320 ASN 320 333 333 ASN ASN C . n 
C 1 321 VAL 321 334 334 VAL VAL C . n 
C 1 322 ALA 322 335 335 ALA ALA C . n 
C 1 323 PHE 323 336 336 PHE PHE C . n 
C 1 324 GLY 324 337 337 GLY GLY C . n 
C 1 325 GLY 325 338 338 GLY GLY C . n 
C 1 326 CYS 326 339 339 CYS CYS C . n 
C 1 327 ASP 327 340 340 ASP ASP C . n 
C 1 328 GLU 328 341 341 GLU GLU C . n 
C 1 329 LEU 329 342 342 LEU LEU C . n 
C 1 330 PHE 330 343 343 PHE PHE C . n 
C 1 331 PRO 331 344 344 PRO PRO C . n 
C 1 332 TYR 332 345 345 TYR TYR C . n 
C 1 333 GLY 333 346 346 GLY GLY C . n 
C 1 334 GLN 334 347 347 GLN GLN C . n 
C 1 335 LEU 335 348 348 LEU LEU C . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
D 2 NAG 1 G NAG 1 A NAG 402 n 
D 2 NAG 2 G NAG 2 A NAG 429 n 
D 2 BMA 3 G BMA 3 A BMA 430 n 
D 2 MAN 4 G MAN 4 A MAN 431 n 
D 2 MAN 5 G MAN 5 A MAN 432 n 
E 3 NAG 1 H NAG 1 A NAG 404 n 
E 3 NAG 2 H NAG 2 A NAG 405 n 
E 3 BMA 3 H BMA 3 A BMA 406 n 
E 3 MAN 4 H MAN 4 A MAN 407 n 
E 3 MAN 5 H MAN 5 A MAN 408 n 
E 3 MAN 6 H MAN 6 A MAN 409 n 
E 3 MAN 7 H MAN 7 A MAN 414 n 
F 4 NAG 1 X NAG 1 B NAG 402 n 
F 4 NAG 2 X NAG 2 B NAG 417 n 
F 4 BMA 3 X BMA 3 B BMA 418 n 
F 4 MAN 4 X MAN 4 B MAN 419 n 
G 5 NAG 1 Y NAG 1 B NAG 404 n 
G 5 NAG 2 Y NAG 2 B NAG 405 n 
G 5 BMA 3 Y BMA 3 B BMA 406 n 
G 5 MAN 4 Y MAN 4 B MAN 408 n 
G 5 MAN 5 Y MAN 5 B MAN 409 n 
G 5 MAN 6 Y MAN 6 B MAN 407 n 
H 4 NAG 1 l NAG 1 C NAG 402 n 
H 4 NAG 2 l NAG 2 C NAG 403 n 
H 4 BMA 3 l BMA 3 C BMA 407 n 
H 4 MAN 4 l MAN 4 C MAN 411 n 
I 6 NAG 1 n NAG 1 C NAG 404 n 
I 6 NAG 2 n NAG 2 C NAG 414 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 DAO ? ? DAO ? ? '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  DAO 1   401 424 DAO DAO A . 
K  8  EPE 1   402 425 EPE EPE A . 
L  9  GOL 1   403 426 GOL GOL A . 
M  9  GOL 1   404 427 GOL GOL A . 
N  10 HEM 1   405 428 HEM HEM A . 
O  11 SO4 1   406 1   SO4 SO4 A . 
P  11 SO4 1   407 2   SO4 SO4 A . 
Q  12 MG  1   408 1   MG  MG  A . 
R  7  DAO 1   401 410 DAO DAO B . 
S  8  EPE 1   402 412 EPE EPE B . 
T  9  GOL 1   403 413 GOL GOL B . 
U  10 HEM 1   404 416 HEM HEM B . 
V  11 SO4 1   405 3   SO4 SO4 B . 
W  12 MG  1   406 2   MG  MG  B . 
X  8  EPE 1   401 412 EPE EPE C . 
Y  10 HEM 1   402 413 HEM HEM C . 
Z  11 SO4 1   403 4   SO4 SO4 C . 
AA 11 SO4 1   404 5   SO4 SO4 C . 
BA 12 MG  1   405 3   MG  MG  C . 
CA 13 HOH 1   501 33  HOH HOH A . 
CA 13 HOH 2   502 164 HOH HOH A . 
CA 13 HOH 3   503 306 HOH HOH A . 
CA 13 HOH 4   504 315 HOH HOH A . 
CA 13 HOH 5   505 628 HOH HOH A . 
CA 13 HOH 6   506 46  HOH HOH A . 
CA 13 HOH 7   507 98  HOH HOH A . 
CA 13 HOH 8   508 19  HOH HOH A . 
CA 13 HOH 9   509 258 HOH HOH A . 
CA 13 HOH 10  510 88  HOH HOH A . 
CA 13 HOH 11  511 43  HOH HOH A . 
CA 13 HOH 12  512 368 HOH HOH A . 
CA 13 HOH 13  513 262 HOH HOH A . 
CA 13 HOH 14  514 238 HOH HOH A . 
CA 13 HOH 15  515 351 HOH HOH A . 
CA 13 HOH 16  516 97  HOH HOH A . 
CA 13 HOH 17  517 60  HOH HOH A . 
CA 13 HOH 18  518 282 HOH HOH A . 
CA 13 HOH 19  519 250 HOH HOH A . 
CA 13 HOH 20  520 316 HOH HOH A . 
CA 13 HOH 21  521 293 HOH HOH A . 
CA 13 HOH 22  522 99  HOH HOH A . 
CA 13 HOH 23  523 45  HOH HOH A . 
CA 13 HOH 24  524 359 HOH HOH A . 
CA 13 HOH 25  525 32  HOH HOH A . 
CA 13 HOH 26  526 380 HOH HOH A . 
CA 13 HOH 27  527 11  HOH HOH A . 
CA 13 HOH 28  528 87  HOH HOH A . 
CA 13 HOH 29  529 314 HOH HOH A . 
CA 13 HOH 30  530 65  HOH HOH A . 
CA 13 HOH 31  531 36  HOH HOH A . 
CA 13 HOH 32  532 371 HOH HOH A . 
CA 13 HOH 33  533 622 HOH HOH A . 
CA 13 HOH 34  534 108 HOH HOH A . 
CA 13 HOH 35  535 330 HOH HOH A . 
CA 13 HOH 36  536 459 HOH HOH A . 
CA 13 HOH 37  537 56  HOH HOH A . 
CA 13 HOH 38  538 630 HOH HOH A . 
CA 13 HOH 39  539 454 HOH HOH A . 
CA 13 HOH 40  540 62  HOH HOH A . 
CA 13 HOH 41  541 8   HOH HOH A . 
CA 13 HOH 42  542 253 HOH HOH A . 
CA 13 HOH 43  543 158 HOH HOH A . 
CA 13 HOH 44  544 92  HOH HOH A . 
CA 13 HOH 45  545 233 HOH HOH A . 
CA 13 HOH 46  546 640 HOH HOH A . 
CA 13 HOH 47  547 248 HOH HOH A . 
CA 13 HOH 48  548 296 HOH HOH A . 
CA 13 HOH 49  549 37  HOH HOH A . 
CA 13 HOH 50  550 203 HOH HOH A . 
CA 13 HOH 51  551 71  HOH HOH A . 
CA 13 HOH 52  552 224 HOH HOH A . 
CA 13 HOH 53  553 9   HOH HOH A . 
CA 13 HOH 54  554 649 HOH HOH A . 
CA 13 HOH 55  555 54  HOH HOH A . 
CA 13 HOH 56  556 245 HOH HOH A . 
CA 13 HOH 57  557 475 HOH HOH A . 
CA 13 HOH 58  558 202 HOH HOH A . 
CA 13 HOH 59  559 373 HOH HOH A . 
CA 13 HOH 60  560 122 HOH HOH A . 
CA 13 HOH 61  561 26  HOH HOH A . 
CA 13 HOH 62  562 367 HOH HOH A . 
CA 13 HOH 63  563 410 HOH HOH A . 
CA 13 HOH 64  564 469 HOH HOH A . 
CA 13 HOH 65  565 239 HOH HOH A . 
CA 13 HOH 66  566 350 HOH HOH A . 
CA 13 HOH 67  567 73  HOH HOH A . 
CA 13 HOH 68  568 322 HOH HOH A . 
CA 13 HOH 69  569 29  HOH HOH A . 
CA 13 HOH 70  570 5   HOH HOH A . 
CA 13 HOH 71  571 125 HOH HOH A . 
CA 13 HOH 72  572 103 HOH HOH A . 
CA 13 HOH 73  573 162 HOH HOH A . 
CA 13 HOH 74  574 362 HOH HOH A . 
CA 13 HOH 75  575 1   HOH HOH A . 
CA 13 HOH 76  576 40  HOH HOH A . 
CA 13 HOH 77  577 394 HOH HOH A . 
CA 13 HOH 78  578 615 HOH HOH A . 
CA 13 HOH 79  579 610 HOH HOH A . 
CA 13 HOH 80  580 222 HOH HOH A . 
CA 13 HOH 81  581 219 HOH HOH A . 
CA 13 HOH 82  582 163 HOH HOH A . 
CA 13 HOH 83  583 361 HOH HOH A . 
CA 13 HOH 84  584 113 HOH HOH A . 
CA 13 HOH 85  585 626 HOH HOH A . 
CA 13 HOH 86  586 303 HOH HOH A . 
CA 13 HOH 87  587 3   HOH HOH A . 
CA 13 HOH 88  588 166 HOH HOH A . 
CA 13 HOH 89  589 161 HOH HOH A . 
CA 13 HOH 90  590 650 HOH HOH A . 
CA 13 HOH 91  591 206 HOH HOH A . 
CA 13 HOH 92  592 374 HOH HOH A . 
CA 13 HOH 93  593 130 HOH HOH A . 
CA 13 HOH 94  594 61  HOH HOH A . 
CA 13 HOH 95  595 247 HOH HOH A . 
CA 13 HOH 96  596 84  HOH HOH A . 
CA 13 HOH 97  597 343 HOH HOH A . 
CA 13 HOH 98  598 644 HOH HOH A . 
CA 13 HOH 99  599 17  HOH HOH A . 
CA 13 HOH 100 600 25  HOH HOH A . 
CA 13 HOH 101 601 334 HOH HOH A . 
CA 13 HOH 102 602 34  HOH HOH A . 
CA 13 HOH 103 603 72  HOH HOH A . 
CA 13 HOH 104 604 433 HOH HOH A . 
CA 13 HOH 105 605 80  HOH HOH A . 
CA 13 HOH 106 606 144 HOH HOH A . 
CA 13 HOH 107 607 337 HOH HOH A . 
CA 13 HOH 108 608 94  HOH HOH A . 
CA 13 HOH 109 609 388 HOH HOH A . 
CA 13 HOH 110 610 634 HOH HOH A . 
CA 13 HOH 111 611 731 HOH HOH A . 
CA 13 HOH 112 612 460 HOH HOH A . 
CA 13 HOH 113 613 200 HOH HOH A . 
CA 13 HOH 114 614 246 HOH HOH A . 
CA 13 HOH 115 615 27  HOH HOH A . 
CA 13 HOH 116 616 613 HOH HOH A . 
CA 13 HOH 117 617 85  HOH HOH A . 
CA 13 HOH 118 618 128 HOH HOH A . 
CA 13 HOH 119 619 236 HOH HOH A . 
CA 13 HOH 120 620 623 HOH HOH A . 
CA 13 HOH 121 621 115 HOH HOH A . 
CA 13 HOH 122 622 155 HOH HOH A . 
CA 13 HOH 123 623 142 HOH HOH A . 
CA 13 HOH 124 624 35  HOH HOH A . 
CA 13 HOH 125 625 449 HOH HOH A . 
CA 13 HOH 126 626 414 HOH HOH A . 
CA 13 HOH 127 627 20  HOH HOH A . 
CA 13 HOH 128 628 452 HOH HOH A . 
CA 13 HOH 129 629 135 HOH HOH A . 
CA 13 HOH 130 630 267 HOH HOH A . 
CA 13 HOH 131 631 429 HOH HOH A . 
CA 13 HOH 132 632 430 HOH HOH A . 
CA 13 HOH 133 633 104 HOH HOH A . 
CA 13 HOH 134 634 215 HOH HOH A . 
CA 13 HOH 135 635 252 HOH HOH A . 
CA 13 HOH 136 636 123 HOH HOH A . 
CA 13 HOH 137 637 190 HOH HOH A . 
CA 13 HOH 138 638 189 HOH HOH A . 
CA 13 HOH 139 639 320 HOH HOH A . 
CA 13 HOH 140 640 301 HOH HOH A . 
CA 13 HOH 141 641 336 HOH HOH A . 
CA 13 HOH 142 642 345 HOH HOH A . 
CA 13 HOH 143 643 204 HOH HOH A . 
CA 13 HOH 144 644 526 HOH HOH A . 
CA 13 HOH 145 645 211 HOH HOH A . 
CA 13 HOH 146 646 418 HOH HOH A . 
CA 13 HOH 147 647 416 HOH HOH A . 
CA 13 HOH 148 648 312 HOH HOH A . 
CA 13 HOH 149 649 169 HOH HOH A . 
CA 13 HOH 150 650 321 HOH HOH A . 
CA 13 HOH 151 651 305 HOH HOH A . 
CA 13 HOH 152 652 284 HOH HOH A . 
CA 13 HOH 153 653 331 HOH HOH A . 
CA 13 HOH 154 654 95  HOH HOH A . 
CA 13 HOH 155 655 652 HOH HOH A . 
CA 13 HOH 156 656 256 HOH HOH A . 
CA 13 HOH 157 657 319 HOH HOH A . 
CA 13 HOH 158 658 192 HOH HOH A . 
CA 13 HOH 159 659 197 HOH HOH A . 
CA 13 HOH 160 660 140 HOH HOH A . 
CA 13 HOH 161 661 381 HOH HOH A . 
CA 13 HOH 162 662 13  HOH HOH A . 
CA 13 HOH 163 663 120 HOH HOH A . 
CA 13 HOH 164 664 270 HOH HOH A . 
CA 13 HOH 165 665 313 HOH HOH A . 
CA 13 HOH 166 666 137 HOH HOH A . 
CA 13 HOH 167 667 18  HOH HOH A . 
CA 13 HOH 168 668 100 HOH HOH A . 
CA 13 HOH 169 669 28  HOH HOH A . 
CA 13 HOH 170 670 360 HOH HOH A . 
CA 13 HOH 171 671 283 HOH HOH A . 
CA 13 HOH 172 672 4   HOH HOH A . 
CA 13 HOH 173 673 621 HOH HOH A . 
CA 13 HOH 174 674 216 HOH HOH A . 
CA 13 HOH 175 675 186 HOH HOH A . 
CA 13 HOH 176 676 191 HOH HOH A . 
CA 13 HOH 177 677 458 HOH HOH A . 
CA 13 HOH 178 678 389 HOH HOH A . 
CA 13 HOH 179 679 465 HOH HOH A . 
CA 13 HOH 180 680 195 HOH HOH A . 
CA 13 HOH 181 681 318 HOH HOH A . 
CA 13 HOH 182 682 317 HOH HOH A . 
CA 13 HOH 183 683 57  HOH HOH A . 
CA 13 HOH 184 684 271 HOH HOH A . 
CA 13 HOH 185 685 646 HOH HOH A . 
CA 13 HOH 186 686 339 HOH HOH A . 
CA 13 HOH 187 687 23  HOH HOH A . 
CA 13 HOH 188 688 209 HOH HOH A . 
CA 13 HOH 189 689 648 HOH HOH A . 
CA 13 HOH 190 690 340 HOH HOH A . 
CA 13 HOH 191 691 47  HOH HOH A . 
CA 13 HOH 192 692 117 HOH HOH A . 
CA 13 HOH 193 693 38  HOH HOH A . 
CA 13 HOH 194 694 199 HOH HOH A . 
CA 13 HOH 195 695 229 HOH HOH A . 
CA 13 HOH 196 696 647 HOH HOH A . 
CA 13 HOH 197 697 22  HOH HOH A . 
CA 13 HOH 198 698 357 HOH HOH A . 
CA 13 HOH 199 699 632 HOH HOH A . 
CA 13 HOH 200 700 383 HOH HOH A . 
CA 13 HOH 201 701 379 HOH HOH A . 
CA 13 HOH 202 702 639 HOH HOH A . 
CA 13 HOH 203 703 210 HOH HOH A . 
CA 13 HOH 204 704 412 HOH HOH A . 
CA 13 HOH 205 705 455 HOH HOH A . 
CA 13 HOH 206 706 625 HOH HOH A . 
CA 13 HOH 207 707 472 HOH HOH A . 
CA 13 HOH 208 708 487 HOH HOH A . 
CA 13 HOH 209 709 485 HOH HOH A . 
CA 13 HOH 210 710 456 HOH HOH A . 
CA 13 HOH 211 711 234 HOH HOH A . 
CA 13 HOH 212 712 249 HOH HOH A . 
CA 13 HOH 213 713 110 HOH HOH A . 
CA 13 HOH 214 714 619 HOH HOH A . 
CA 13 HOH 215 715 356 HOH HOH A . 
CA 13 HOH 216 716 272 HOH HOH A . 
CA 13 HOH 217 717 467 HOH HOH A . 
CA 13 HOH 218 718 323 HOH HOH A . 
CA 13 HOH 219 719 642 HOH HOH A . 
CA 13 HOH 220 720 604 HOH HOH A . 
CA 13 HOH 221 721 304 HOH HOH A . 
CA 13 HOH 222 722 369 HOH HOH A . 
CA 13 HOH 223 723 466 HOH HOH A . 
CA 13 HOH 224 724 277 HOH HOH A . 
CA 13 HOH 225 725 299 HOH HOH A . 
CA 13 HOH 226 726 457 HOH HOH A . 
CA 13 HOH 227 727 392 HOH HOH A . 
CA 13 HOH 228 728 370 HOH HOH A . 
CA 13 HOH 229 729 631 HOH HOH A . 
CA 13 HOH 230 730 278 HOH HOH A . 
CA 13 HOH 231 731 274 HOH HOH A . 
CA 13 HOH 232 732 483 HOH HOH A . 
CA 13 HOH 233 733 338 HOH HOH A . 
CA 13 HOH 234 734 607 HOH HOH A . 
CA 13 HOH 235 735 332 HOH HOH A . 
CA 13 HOH 236 736 651 HOH HOH A . 
CA 13 HOH 237 737 342 HOH HOH A . 
CA 13 HOH 238 738 364 HOH HOH A . 
CA 13 HOH 239 739 611 HOH HOH A . 
CA 13 HOH 240 740 354 HOH HOH A . 
CA 13 HOH 241 741 609 HOH HOH A . 
CA 13 HOH 242 742 366 HOH HOH A . 
CA 13 HOH 243 743 486 HOH HOH A . 
CA 13 HOH 244 744 636 HOH HOH A . 
CA 13 HOH 245 745 464 HOH HOH A . 
CA 13 HOH 246 746 419 HOH HOH A . 
CA 13 HOH 247 747 484 HOH HOH A . 
CA 13 HOH 248 748 482 HOH HOH A . 
CA 13 HOH 249 749 653 HOH HOH A . 
CA 13 HOH 250 750 415 HOH HOH A . 
CA 13 HOH 251 751 273 HOH HOH A . 
CA 13 HOH 252 752 620 HOH HOH A . 
CA 13 HOH 253 753 298 HOH HOH A . 
CA 13 HOH 254 754 616 HOH HOH A . 
CA 13 HOH 255 755 450 HOH HOH A . 
CA 13 HOH 256 756 627 HOH HOH A . 
CA 13 HOH 257 757 355 HOH HOH A . 
CA 13 HOH 258 758 453 HOH HOH A . 
CA 13 HOH 259 759 480 HOH HOH A . 
CA 13 HOH 260 760 645 HOH HOH A . 
CA 13 HOH 261 761 603 HOH HOH A . 
CA 13 HOH 262 762 413 HOH HOH A . 
CA 13 HOH 263 763 617 HOH HOH A . 
CA 13 HOH 264 764 608 HOH HOH A . 
CA 13 HOH 265 765 292 HOH HOH A . 
CA 13 HOH 266 766 365 HOH HOH A . 
CA 13 HOH 267 767 606 HOH HOH A . 
CA 13 HOH 268 768 411 HOH HOH A . 
CA 13 HOH 269 769 353 HOH HOH A . 
CA 13 HOH 270 770 624 HOH HOH A . 
CA 13 HOH 271 771 295 HOH HOH A . 
CA 13 HOH 272 772 294 HOH HOH A . 
CA 13 HOH 273 773 420 HOH HOH A . 
CA 13 HOH 274 774 605 HOH HOH A . 
CA 13 HOH 275 775 635 HOH HOH A . 
CA 13 HOH 276 776 638 HOH HOH A . 
CA 13 HOH 277 777 618 HOH HOH A . 
CA 13 HOH 278 778 614 HOH HOH A . 
CA 13 HOH 279 779 376 HOH HOH A . 
CA 13 HOH 280 780 427 HOH HOH A . 
CA 13 HOH 281 781 385 HOH HOH A . 
CA 13 HOH 282 782 302 HOH HOH A . 
CA 13 HOH 283 783 738 HOH HOH A . 
CA 13 HOH 284 784 451 HOH HOH A . 
CA 13 HOH 285 785 280 HOH HOH A . 
CA 13 HOH 286 786 329 HOH HOH A . 
CA 13 HOH 287 787 297 HOH HOH A . 
CA 13 HOH 288 788 654 HOH HOH A . 
CA 13 HOH 289 789 333 HOH HOH A . 
CA 13 HOH 290 790 476 HOH HOH A . 
CA 13 HOH 291 791 395 HOH HOH A . 
CA 13 HOH 292 792 279 HOH HOH A . 
CA 13 HOH 293 793 386 HOH HOH A . 
CA 13 HOH 294 794 643 HOH HOH A . 
CA 13 HOH 295 795 612 HOH HOH A . 
CA 13 HOH 296 796 324 HOH HOH A . 
CA 13 HOH 297 797 633 HOH HOH A . 
CA 13 HOH 298 798 637 HOH HOH A . 
CA 13 HOH 299 799 428 HOH HOH A . 
CA 13 HOH 300 800 377 HOH HOH A . 
CA 13 HOH 301 801 281 HOH HOH A . 
CA 13 HOH 302 802 276 HOH HOH A . 
CA 13 HOH 303 803 300 HOH HOH A . 
CA 13 HOH 304 804 463 HOH HOH A . 
CA 13 HOH 305 805 275 HOH HOH A . 
CA 13 HOH 306 806 375 HOH HOH A . 
CA 13 HOH 307 807 372 HOH HOH A . 
CA 13 HOH 308 808 263 HOH HOH A . 
CA 13 HOH 309 809 461 HOH HOH A . 
CA 13 HOH 310 810 629 HOH HOH A . 
DA 13 HOH 1   501 398 HOH HOH B . 
DA 13 HOH 2   502 675 HOH HOH B . 
DA 13 HOH 3   503 520 HOH HOH B . 
DA 13 HOH 4   504 41  HOH HOH B . 
DA 13 HOH 5   505 514 HOH HOH B . 
DA 13 HOH 6   506 327 HOH HOH B . 
DA 13 HOH 7   507 131 HOH HOH B . 
DA 13 HOH 8   508 109 HOH HOH B . 
DA 13 HOH 9   509 70  HOH HOH B . 
DA 13 HOH 10  510 513 HOH HOH B . 
DA 13 HOH 11  511 133 HOH HOH B . 
DA 13 HOH 12  512 52  HOH HOH B . 
DA 13 HOH 13  513 528 HOH HOH B . 
DA 13 HOH 14  514 307 HOH HOH B . 
DA 13 HOH 15  515 14  HOH HOH B . 
DA 13 HOH 16  516 168 HOH HOH B . 
DA 13 HOH 17  517 67  HOH HOH B . 
DA 13 HOH 18  518 261 HOH HOH B . 
DA 13 HOH 19  519 538 HOH HOH B . 
DA 13 HOH 20  520 143 HOH HOH B . 
DA 13 HOH 21  521 598 HOH HOH B . 
DA 13 HOH 22  522 172 HOH HOH B . 
DA 13 HOH 23  523 477 HOH HOH B . 
DA 13 HOH 24  524 497 HOH HOH B . 
DA 13 HOH 25  525 180 HOH HOH B . 
DA 13 HOH 26  526 393 HOH HOH B . 
DA 13 HOH 27  527 147 HOH HOH B . 
DA 13 HOH 28  528 492 HOH HOH B . 
DA 13 HOH 29  529 491 HOH HOH B . 
DA 13 HOH 30  530 664 HOH HOH B . 
DA 13 HOH 31  531 481 HOH HOH B . 
DA 13 HOH 32  532 12  HOH HOH B . 
DA 13 HOH 33  533 177 HOH HOH B . 
DA 13 HOH 34  534 79  HOH HOH B . 
DA 13 HOH 35  535 86  HOH HOH B . 
DA 13 HOH 36  536 260 HOH HOH B . 
DA 13 HOH 37  537 132 HOH HOH B . 
DA 13 HOH 38  538 170 HOH HOH B . 
DA 13 HOH 39  539 174 HOH HOH B . 
DA 13 HOH 40  540 221 HOH HOH B . 
DA 13 HOH 41  541 535 HOH HOH B . 
DA 13 HOH 42  542 121 HOH HOH B . 
DA 13 HOH 43  543 326 HOH HOH B . 
DA 13 HOH 44  544 81  HOH HOH B . 
DA 13 HOH 45  545 599 HOH HOH B . 
DA 13 HOH 46  546 527 HOH HOH B . 
DA 13 HOH 47  547 139 HOH HOH B . 
DA 13 HOH 48  548 690 HOH HOH B . 
DA 13 HOH 49  549 490 HOH HOH B . 
DA 13 HOH 50  550 101 HOH HOH B . 
DA 13 HOH 51  551 509 HOH HOH B . 
DA 13 HOH 52  552 259 HOH HOH B . 
DA 13 HOH 53  553 671 HOH HOH B . 
DA 13 HOH 54  554 688 HOH HOH B . 
DA 13 HOH 55  555 116 HOH HOH B . 
DA 13 HOH 56  556 501 HOH HOH B . 
DA 13 HOH 57  557 666 HOH HOH B . 
DA 13 HOH 58  558 689 HOH HOH B . 
DA 13 HOH 59  559 146 HOH HOH B . 
DA 13 HOH 60  560 89  HOH HOH B . 
DA 13 HOH 61  561 16  HOH HOH B . 
DA 13 HOH 62  562 512 HOH HOH B . 
DA 13 HOH 63  563 544 HOH HOH B . 
DA 13 HOH 64  564 78  HOH HOH B . 
DA 13 HOH 65  565 600 HOH HOH B . 
DA 13 HOH 66  566 227 HOH HOH B . 
DA 13 HOH 67  567 516 HOH HOH B . 
DA 13 HOH 68  568 58  HOH HOH B . 
DA 13 HOH 69  569 91  HOH HOH B . 
DA 13 HOH 70  570 505 HOH HOH B . 
DA 13 HOH 71  571 114 HOH HOH B . 
DA 13 HOH 72  572 670 HOH HOH B . 
DA 13 HOH 73  573 176 HOH HOH B . 
DA 13 HOH 74  574 64  HOH HOH B . 
DA 13 HOH 75  575 703 HOH HOH B . 
DA 13 HOH 76  576 661 HOH HOH B . 
DA 13 HOH 77  577 119 HOH HOH B . 
DA 13 HOH 78  578 525 HOH HOH B . 
DA 13 HOH 79  579 341 HOH HOH B . 
DA 13 HOH 80  580 223 HOH HOH B . 
DA 13 HOH 81  581 243 HOH HOH B . 
DA 13 HOH 82  582 499 HOH HOH B . 
DA 13 HOH 83  583 470 HOH HOH B . 
DA 13 HOH 84  584 7   HOH HOH B . 
DA 13 HOH 85  585 124 HOH HOH B . 
DA 13 HOH 86  586 529 HOH HOH B . 
DA 13 HOH 87  587 226 HOH HOH B . 
DA 13 HOH 88  588 269 HOH HOH B . 
DA 13 HOH 89  589 290 HOH HOH B . 
DA 13 HOH 90  590 422 HOH HOH B . 
DA 13 HOH 91  591 396 HOH HOH B . 
DA 13 HOH 92  592 506 HOH HOH B . 
DA 13 HOH 93  593 541 HOH HOH B . 
DA 13 HOH 94  594 288 HOH HOH B . 
DA 13 HOH 95  595 184 HOH HOH B . 
DA 13 HOH 96  596 145 HOH HOH B . 
DA 13 HOH 97  597 231 HOH HOH B . 
DA 13 HOH 98  598 539 HOH HOH B . 
DA 13 HOH 99  599 500 HOH HOH B . 
DA 13 HOH 100 600 106 HOH HOH B . 
DA 13 HOH 101 601 676 HOH HOH B . 
DA 13 HOH 102 602 208 HOH HOH B . 
DA 13 HOH 103 603 149 HOH HOH B . 
DA 13 HOH 104 604 39  HOH HOH B . 
DA 13 HOH 105 605 30  HOH HOH B . 
DA 13 HOH 106 606 435 HOH HOH B . 
DA 13 HOH 107 607 205 HOH HOH B . 
DA 13 HOH 108 608 105 HOH HOH B . 
DA 13 HOH 109 609 545 HOH HOH B . 
DA 13 HOH 110 610 400 HOH HOH B . 
DA 13 HOH 111 611 178 HOH HOH B . 
DA 13 HOH 112 612 255 HOH HOH B . 
DA 13 HOH 113 613 55  HOH HOH B . 
DA 13 HOH 114 614 225 HOH HOH B . 
DA 13 HOH 115 615 536 HOH HOH B . 
DA 13 HOH 116 616 524 HOH HOH B . 
DA 13 HOH 117 617 684 HOH HOH B . 
DA 13 HOH 118 618 667 HOH HOH B . 
DA 13 HOH 119 619 181 HOH HOH B . 
DA 13 HOH 120 620 175 HOH HOH B . 
DA 13 HOH 121 621 704 HOH HOH B . 
DA 13 HOH 122 622 417 HOH HOH B . 
DA 13 HOH 123 623 678 HOH HOH B . 
DA 13 HOH 124 624 42  HOH HOH B . 
DA 13 HOH 125 625 532 HOH HOH B . 
DA 13 HOH 126 626 152 HOH HOH B . 
DA 13 HOH 127 627 328 HOH HOH B . 
DA 13 HOH 128 628 522 HOH HOH B . 
DA 13 HOH 129 629 602 HOH HOH B . 
DA 13 HOH 130 630 473 HOH HOH B . 
DA 13 HOH 131 631 107 HOH HOH B . 
DA 13 HOH 132 632 48  HOH HOH B . 
DA 13 HOH 133 633 682 HOH HOH B . 
DA 13 HOH 134 634 504 HOH HOH B . 
DA 13 HOH 135 635 543 HOH HOH B . 
DA 13 HOH 136 636 641 HOH HOH B . 
DA 13 HOH 137 637 691 HOH HOH B . 
DA 13 HOH 138 638 692 HOH HOH B . 
DA 13 HOH 139 639 705 HOH HOH B . 
DA 13 HOH 140 640 434 HOH HOH B . 
DA 13 HOH 141 641 495 HOH HOH B . 
DA 13 HOH 142 642 310 HOH HOH B . 
DA 13 HOH 143 643 502 HOH HOH B . 
DA 13 HOH 144 644 384 HOH HOH B . 
DA 13 HOH 145 645 734 HOH HOH B . 
DA 13 HOH 146 646 519 HOH HOH B . 
DA 13 HOH 147 647 503 HOH HOH B . 
DA 13 HOH 148 648 679 HOH HOH B . 
DA 13 HOH 149 649 534 HOH HOH B . 
DA 13 HOH 150 650 196 HOH HOH B . 
DA 13 HOH 151 651 182 HOH HOH B . 
DA 13 HOH 152 652 74  HOH HOH B . 
DA 13 HOH 153 653 254 HOH HOH B . 
DA 13 HOH 154 654 44  HOH HOH B . 
DA 13 HOH 155 655 407 HOH HOH B . 
DA 13 HOH 156 656 268 HOH HOH B . 
DA 13 HOH 157 657 24  HOH HOH B . 
DA 13 HOH 158 658 220 HOH HOH B . 
DA 13 HOH 159 659 21  HOH HOH B . 
DA 13 HOH 160 660 289 HOH HOH B . 
DA 13 HOH 161 661 736 HOH HOH B . 
DA 13 HOH 162 662 6   HOH HOH B . 
DA 13 HOH 163 663 352 HOH HOH B . 
DA 13 HOH 164 664 488 HOH HOH B . 
DA 13 HOH 165 665 240 HOH HOH B . 
DA 13 HOH 166 666 59  HOH HOH B . 
DA 13 HOH 167 667 391 HOH HOH B . 
DA 13 HOH 168 668 680 HOH HOH B . 
DA 13 HOH 169 669 150 HOH HOH B . 
DA 13 HOH 170 670 496 HOH HOH B . 
DA 13 HOH 171 671 537 HOH HOH B . 
DA 13 HOH 172 672 390 HOH HOH B . 
DA 13 HOH 173 673 687 HOH HOH B . 
DA 13 HOH 174 674 494 HOH HOH B . 
DA 13 HOH 175 675 471 HOH HOH B . 
DA 13 HOH 176 676 479 HOH HOH B . 
DA 13 HOH 177 677 597 HOH HOH B . 
DA 13 HOH 178 678 344 HOH HOH B . 
DA 13 HOH 179 679 695 HOH HOH B . 
DA 13 HOH 180 680 251 HOH HOH B . 
DA 13 HOH 181 681 531 HOH HOH B . 
DA 13 HOH 182 682 402 HOH HOH B . 
DA 13 HOH 183 683 683 HOH HOH B . 
DA 13 HOH 184 684 363 HOH HOH B . 
DA 13 HOH 185 685 663 HOH HOH B . 
DA 13 HOH 186 686 662 HOH HOH B . 
DA 13 HOH 187 687 421 HOH HOH B . 
DA 13 HOH 188 688 699 HOH HOH B . 
DA 13 HOH 189 689 697 HOH HOH B . 
DA 13 HOH 190 690 387 HOH HOH B . 
DA 13 HOH 191 691 257 HOH HOH B . 
DA 13 HOH 192 692 669 HOH HOH B . 
DA 13 HOH 193 693 655 HOH HOH B . 
DA 13 HOH 194 694 214 HOH HOH B . 
DA 13 HOH 195 695 737 HOH HOH B . 
DA 13 HOH 196 696 217 HOH HOH B . 
DA 13 HOH 197 697 735 HOH HOH B . 
DA 13 HOH 198 698 656 HOH HOH B . 
DA 13 HOH 199 699 518 HOH HOH B . 
DA 13 HOH 200 700 701 HOH HOH B . 
DA 13 HOH 201 701 173 HOH HOH B . 
DA 13 HOH 202 702 665 HOH HOH B . 
DA 13 HOH 203 703 715 HOH HOH B . 
DA 13 HOH 204 704 406 HOH HOH B . 
DA 13 HOH 205 705 287 HOH HOH B . 
DA 13 HOH 206 706 489 HOH HOH B . 
DA 13 HOH 207 707 685 HOH HOH B . 
DA 13 HOH 208 708 668 HOH HOH B . 
DA 13 HOH 209 709 700 HOH HOH B . 
DA 13 HOH 210 710 694 HOH HOH B . 
DA 13 HOH 211 711 358 HOH HOH B . 
DA 13 HOH 212 712 517 HOH HOH B . 
DA 13 HOH 213 713 378 HOH HOH B . 
DA 13 HOH 214 714 507 HOH HOH B . 
DA 13 HOH 215 715 542 HOH HOH B . 
DA 13 HOH 216 716 660 HOH HOH B . 
DA 13 HOH 217 717 187 HOH HOH B . 
DA 13 HOH 218 718 291 HOH HOH B . 
DA 13 HOH 219 719 530 HOH HOH B . 
DA 13 HOH 220 720 681 HOH HOH B . 
DA 13 HOH 221 721 401 HOH HOH B . 
DA 13 HOH 222 722 674 HOH HOH B . 
DA 13 HOH 223 723 546 HOH HOH B . 
DA 13 HOH 224 724 508 HOH HOH B . 
DA 13 HOH 225 725 698 HOH HOH B . 
DA 13 HOH 226 726 399 HOH HOH B . 
DA 13 HOH 227 727 521 HOH HOH B . 
DA 13 HOH 228 728 672 HOH HOH B . 
DA 13 HOH 229 729 493 HOH HOH B . 
DA 13 HOH 230 730 601 HOH HOH B . 
DA 13 HOH 231 731 686 HOH HOH B . 
DA 13 HOH 232 732 515 HOH HOH B . 
DA 13 HOH 233 733 397 HOH HOH B . 
DA 13 HOH 234 734 658 HOH HOH B . 
DA 13 HOH 235 735 659 HOH HOH B . 
DA 13 HOH 236 736 405 HOH HOH B . 
DA 13 HOH 237 737 657 HOH HOH B . 
DA 13 HOH 238 738 677 HOH HOH B . 
DA 13 HOH 239 739 673 HOH HOH B . 
DA 13 HOH 240 740 478 HOH HOH B . 
DA 13 HOH 241 741 523 HOH HOH B . 
DA 13 HOH 242 742 286 HOH HOH B . 
DA 13 HOH 243 743 702 HOH HOH B . 
DA 13 HOH 244 744 285 HOH HOH B . 
DA 13 HOH 245 745 693 HOH HOH B . 
DA 13 HOH 246 746 157 HOH HOH B . 
EA 13 HOH 1   501 347 HOH HOH C . 
EA 13 HOH 2   502 576 HOH HOH C . 
EA 13 HOH 3   503 570 HOH HOH C . 
EA 13 HOH 4   504 721 HOH HOH C . 
EA 13 HOH 5   505 241 HOH HOH C . 
EA 13 HOH 6   506 498 HOH HOH C . 
EA 13 HOH 7   507 730 HOH HOH C . 
EA 13 HOH 8   508 739 HOH HOH C . 
EA 13 HOH 9   509 510 HOH HOH C . 
EA 13 HOH 10  510 183 HOH HOH C . 
EA 13 HOH 11  511 574 HOH HOH C . 
EA 13 HOH 12  512 511 HOH HOH C . 
EA 13 HOH 13  513 159 HOH HOH C . 
EA 13 HOH 14  514 228 HOH HOH C . 
EA 13 HOH 15  515 212 HOH HOH C . 
EA 13 HOH 16  516 66  HOH HOH C . 
EA 13 HOH 17  517 112 HOH HOH C . 
EA 13 HOH 18  518 102 HOH HOH C . 
EA 13 HOH 19  519 569 HOH HOH C . 
EA 13 HOH 20  520 438 HOH HOH C . 
EA 13 HOH 21  521 76  HOH HOH C . 
EA 13 HOH 22  522 568 HOH HOH C . 
EA 13 HOH 23  523 244 HOH HOH C . 
EA 13 HOH 24  524 325 HOH HOH C . 
EA 13 HOH 25  525 218 HOH HOH C . 
EA 13 HOH 26  526 575 HOH HOH C . 
EA 13 HOH 27  527 111 HOH HOH C . 
EA 13 HOH 28  528 118 HOH HOH C . 
EA 13 HOH 29  529 431 HOH HOH C . 
EA 13 HOH 30  530 443 HOH HOH C . 
EA 13 HOH 31  531 129 HOH HOH C . 
EA 13 HOH 32  532 10  HOH HOH C . 
EA 13 HOH 33  533 448 HOH HOH C . 
EA 13 HOH 34  534 69  HOH HOH C . 
EA 13 HOH 35  535 63  HOH HOH C . 
EA 13 HOH 36  536 201 HOH HOH C . 
EA 13 HOH 37  537 156 HOH HOH C . 
EA 13 HOH 38  538 136 HOH HOH C . 
EA 13 HOH 39  539 185 HOH HOH C . 
EA 13 HOH 40  540 404 HOH HOH C . 
EA 13 HOH 41  541 436 HOH HOH C . 
EA 13 HOH 42  542 235 HOH HOH C . 
EA 13 HOH 43  543 179 HOH HOH C . 
EA 13 HOH 44  544 552 HOH HOH C . 
EA 13 HOH 45  545 577 HOH HOH C . 
EA 13 HOH 46  546 714 HOH HOH C . 
EA 13 HOH 47  547 591 HOH HOH C . 
EA 13 HOH 48  548 468 HOH HOH C . 
EA 13 HOH 49  549 237 HOH HOH C . 
EA 13 HOH 50  550 49  HOH HOH C . 
EA 13 HOH 51  551 15  HOH HOH C . 
EA 13 HOH 52  552 242 HOH HOH C . 
EA 13 HOH 53  553 740 HOH HOH C . 
EA 13 HOH 54  554 580 HOH HOH C . 
EA 13 HOH 55  555 447 HOH HOH C . 
EA 13 HOH 56  556 2   HOH HOH C . 
EA 13 HOH 57  557 718 HOH HOH C . 
EA 13 HOH 58  558 586 HOH HOH C . 
EA 13 HOH 59  559 587 HOH HOH C . 
EA 13 HOH 60  560 578 HOH HOH C . 
EA 13 HOH 61  561 348 HOH HOH C . 
EA 13 HOH 62  562 308 HOH HOH C . 
EA 13 HOH 63  563 68  HOH HOH C . 
EA 13 HOH 64  564 75  HOH HOH C . 
EA 13 HOH 65  565 31  HOH HOH C . 
EA 13 HOH 66  566 555 HOH HOH C . 
EA 13 HOH 67  567 165 HOH HOH C . 
EA 13 HOH 68  568 409 HOH HOH C . 
EA 13 HOH 69  569 440 HOH HOH C . 
EA 13 HOH 70  570 134 HOH HOH C . 
EA 13 HOH 71  571 733 HOH HOH C . 
EA 13 HOH 72  572 556 HOH HOH C . 
EA 13 HOH 73  573 207 HOH HOH C . 
EA 13 HOH 74  574 566 HOH HOH C . 
EA 13 HOH 75  575 230 HOH HOH C . 
EA 13 HOH 76  576 77  HOH HOH C . 
EA 13 HOH 77  577 426 HOH HOH C . 
EA 13 HOH 78  578 83  HOH HOH C . 
EA 13 HOH 79  579 713 HOH HOH C . 
EA 13 HOH 80  580 382 HOH HOH C . 
EA 13 HOH 81  581 96  HOH HOH C . 
EA 13 HOH 82  582 716 HOH HOH C . 
EA 13 HOH 83  583 709 HOH HOH C . 
EA 13 HOH 84  584 474 HOH HOH C . 
EA 13 HOH 85  585 717 HOH HOH C . 
EA 13 HOH 86  586 53  HOH HOH C . 
EA 13 HOH 87  587 171 HOH HOH C . 
EA 13 HOH 88  588 571 HOH HOH C . 
EA 13 HOH 89  589 153 HOH HOH C . 
EA 13 HOH 90  590 167 HOH HOH C . 
EA 13 HOH 91  591 50  HOH HOH C . 
EA 13 HOH 92  592 151 HOH HOH C . 
EA 13 HOH 93  593 198 HOH HOH C . 
EA 13 HOH 94  594 719 HOH HOH C . 
EA 13 HOH 95  595 729 HOH HOH C . 
EA 13 HOH 96  596 590 HOH HOH C . 
EA 13 HOH 97  597 82  HOH HOH C . 
EA 13 HOH 98  598 722 HOH HOH C . 
EA 13 HOH 99  599 51  HOH HOH C . 
EA 13 HOH 100 600 403 HOH HOH C . 
EA 13 HOH 101 601 93  HOH HOH C . 
EA 13 HOH 102 602 213 HOH HOH C . 
EA 13 HOH 103 603 710 HOH HOH C . 
EA 13 HOH 104 604 127 HOH HOH C . 
EA 13 HOH 105 605 732 HOH HOH C . 
EA 13 HOH 106 606 573 HOH HOH C . 
EA 13 HOH 107 607 564 HOH HOH C . 
EA 13 HOH 108 608 579 HOH HOH C . 
EA 13 HOH 109 609 160 HOH HOH C . 
EA 13 HOH 110 610 725 HOH HOH C . 
EA 13 HOH 111 611 712 HOH HOH C . 
EA 13 HOH 112 612 561 HOH HOH C . 
EA 13 HOH 113 613 148 HOH HOH C . 
EA 13 HOH 114 614 188 HOH HOH C . 
EA 13 HOH 115 615 154 HOH HOH C . 
EA 13 HOH 116 616 138 HOH HOH C . 
EA 13 HOH 117 617 594 HOH HOH C . 
EA 13 HOH 118 618 442 HOH HOH C . 
EA 13 HOH 119 619 193 HOH HOH C . 
EA 13 HOH 120 620 335 HOH HOH C . 
EA 13 HOH 121 621 724 HOH HOH C . 
EA 13 HOH 122 622 711 HOH HOH C . 
EA 13 HOH 123 623 560 HOH HOH C . 
EA 13 HOH 124 624 141 HOH HOH C . 
EA 13 HOH 125 625 551 HOH HOH C . 
EA 13 HOH 126 626 572 HOH HOH C . 
EA 13 HOH 127 627 720 HOH HOH C . 
EA 13 HOH 128 628 581 HOH HOH C . 
EA 13 HOH 129 629 90  HOH HOH C . 
EA 13 HOH 130 630 425 HOH HOH C . 
EA 13 HOH 131 631 232 HOH HOH C . 
EA 13 HOH 132 632 548 HOH HOH C . 
EA 13 HOH 133 633 265 HOH HOH C . 
EA 13 HOH 134 634 446 HOH HOH C . 
EA 13 HOH 135 635 592 HOH HOH C . 
EA 13 HOH 136 636 585 HOH HOH C . 
EA 13 HOH 137 637 432 HOH HOH C . 
EA 13 HOH 138 638 559 HOH HOH C . 
EA 13 HOH 139 639 728 HOH HOH C . 
EA 13 HOH 140 640 723 HOH HOH C . 
EA 13 HOH 141 641 593 HOH HOH C . 
EA 13 HOH 142 642 266 HOH HOH C . 
EA 13 HOH 143 643 589 HOH HOH C . 
EA 13 HOH 144 644 423 HOH HOH C . 
EA 13 HOH 145 645 727 HOH HOH C . 
EA 13 HOH 146 646 309 HOH HOH C . 
EA 13 HOH 147 647 557 HOH HOH C . 
EA 13 HOH 148 648 264 HOH HOH C . 
EA 13 HOH 149 649 445 HOH HOH C . 
EA 13 HOH 150 650 707 HOH HOH C . 
EA 13 HOH 151 651 424 HOH HOH C . 
EA 13 HOH 152 652 582 HOH HOH C . 
EA 13 HOH 153 653 540 HOH HOH C . 
EA 13 HOH 154 654 558 HOH HOH C . 
EA 13 HOH 155 655 553 HOH HOH C . 
EA 13 HOH 156 656 562 HOH HOH C . 
EA 13 HOH 157 657 349 HOH HOH C . 
EA 13 HOH 158 658 547 HOH HOH C . 
EA 13 HOH 159 659 554 HOH HOH C . 
EA 13 HOH 160 660 584 HOH HOH C . 
EA 13 HOH 161 661 563 HOH HOH C . 
EA 13 HOH 162 662 549 HOH HOH C . 
EA 13 HOH 163 663 567 HOH HOH C . 
EA 13 HOH 164 664 437 HOH HOH C . 
EA 13 HOH 165 665 583 HOH HOH C . 
EA 13 HOH 166 666 726 HOH HOH C . 
EA 13 HOH 167 667 706 HOH HOH C . 
EA 13 HOH 168 668 444 HOH HOH C . 
EA 13 HOH 169 669 533 HOH HOH C . 
EA 13 HOH 170 670 708 HOH HOH C . 
EA 13 HOH 171 671 441 HOH HOH C . 
EA 13 HOH 172 672 588 HOH HOH C . 
EA 13 HOH 173 673 596 HOH HOH C . 
EA 13 HOH 174 674 194 HOH HOH C . 
EA 13 HOH 175 675 126 HOH HOH C . 
EA 13 HOH 176 676 346 HOH HOH C . 
EA 13 HOH 177 677 439 HOH HOH C . 
EA 13 HOH 178 678 408 HOH HOH C . 
EA 13 HOH 179 679 550 HOH HOH C . 
EA 13 HOH 180 680 696 HOH HOH C . 
EA 13 HOH 181 681 565 HOH HOH C . 
EA 13 HOH 182 682 595 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                   111.74 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HE9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     271.878 
_cell.length_a_esd                 ? 
_cell.length_b                     75.001 
_cell.length_b_esd                 ? 
_cell.length_c                     105.446 
_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                         9HE9 
_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                   9HE9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             4.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.09 
_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    
;1.9M ammonium sulphate, 100 mM HEPES pH 7.5

Soaking: 10 mM lauric acid 4 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         2021-04-22 
_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                                       9HE9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               48.37 
_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                                     107314 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.76 
_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                                0.141 
_reflns.pdbx_Rpim_I_all                                0.055 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.129 
_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                                    2.15 
_reflns_shell.d_res_low                                     2.19 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5259 
_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                               6.8 
_reflns_shell.pdbx_chi_squared                              0.44 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.686 
_reflns_shell.pdbx_Rpim_I_all                               0.263 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.935 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.632 
_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]                            -1.78 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            1.62 
_refine.aniso_B[2][2]                            2.40 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.45 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               46.423 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_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                                 9HE9 
_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                            2.15 
_refine.ls_d_res_low                             48.37 
_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                     101822 
_refine.ls_number_reflns_R_free                  5489 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.84 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20002 
_refine.ls_R_factor_R_free                       0.22689 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19858 
_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                       0.164 
_refine.pdbx_overall_ESU_R_Free                  0.150 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.221 
_refine.overall_SU_ML                            0.128 
_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                       2.15 
_refine_hist.d_res_low                        48.37 
_refine_hist.number_atoms_solvent             738 
_refine_hist.number_atoms_total               9103 
_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        8337 
_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' ? 0.005  0.012  8809  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7751  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.267  1.845  12150 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.469  1.746  17947 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.269  5.000  1048  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.900  5.000  54    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.468 10.000 1138  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.200  1327  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  10433 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2111  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.726  4.756  4065  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.726  4.756  4065  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.046  8.547  5088  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.046  8.546  5089  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.380  5.431  4744  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.307  5.418  4725  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.160  9.814  7009  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.639  46.75  10069 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.614  46.69  9926  ? 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                       2.150 
_refine_ls_shell.d_res_low                        2.206 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             388 
_refine_ls_shell.number_reflns_R_work             7508 
_refine_ls_shell.percent_reflns_obs               99.87 
_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                  0.282 
_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                  0.302 
# 
_struct.entry_id                     9HE9 
_struct.title                        
'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II) in complex with lauric acid' 
_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        9HE9 
_struct_keywords.text            'Peroxygenase, peroxidase, complex, lauric acid, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 1  ? 
D  N N 2  ? 
E  N N 3  ? 
F  N N 4  ? 
G  N N 5  ? 
H  N N 4  ? 
I  N N 6  ? 
J  N N 7  ? 
K  N N 8  ? 
L  N N 9  ? 
M  N N 9  ? 
N  N N 10 ? 
O  N N 11 ? 
P  N N 11 ? 
Q  N N 12 ? 
R  N N 7  ? 
S  N N 8  ? 
T  N N 9  ? 
U  N N 10 ? 
V  N N 11 ? 
W  N N 12 ? 
X  N N 8  ? 
Y  N N 10 ? 
Z  N N 11 ? 
AA N N 11 ? 
BA N N 12 ? 
CA N N 13 ? 
DA N N 13 ? 
EA N N 13 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A4V1Q376_9AGAR 
_struct_ref.pdbx_db_accession          A0A4V1Q376 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QGVDPPPPPGPPSFTGTKLVNDADHPWQPLREGDIRGPCPGLNTLASHGYLPRDGVATPAQIITATQEGFNFENNAAIVA
TYLGHLLNGNLVTDLLSIGGATPKTGPPPPPPAHAGGLNVHGTFEGDAGMTRADEFFGDNHSFNQTLFDKFVDFSNRYGG
GFYNLTVAGELRYSRIQDSIATNPEFQFKNVRFITAYGETVFPINLFVDGRVTTDRKLSMEDAASIFRDMRFPDDFHRSA
VPASNEGADQVLAAHPWVPGGNADNQVNNYVEDPDSADFTHLCRLYEFVVGSVQELYPNPTGILRRNLIKNLHYWWTGVN
VAFGGCDELFPYGQL
;
_struct_ref.pdbx_align_begin           52 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9HE9 A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HE9 B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HE9 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,CA 
2 1 B,F,G,R,S,T,U,V,W,DA     
3 1 C,H,I,X,Y,Z,AA,BA,EA     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                PISA-monomeric 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 CYS A 39  ? HIS A 48  ? CYS A 52  HIS A 61  1 ? 10 
HELX_P HELX_P2  AA2 THR A 58  ? ASN A 71  ? THR A 71  ASN A 84  1 ? 14 
HELX_P HELX_P3  AA3 GLU A 73  ? GLY A 89  ? GLU A 86  GLY A 102 1 ? 17 
HELX_P HELX_P4  AA4 THR A 102 ? GLY A 106 ? THR A 115 GLY A 119 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 134 ? GLY A 138 ? ASP A 147 GLY A 151 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 144 ? GLY A 159 ? ASN A 157 GLY A 172 1 ? 16 
HELX_P HELX_P7  AA7 ASN A 164 ? ASN A 183 ? ASN A 177 ASN A 196 1 ? 20 
HELX_P HELX_P8  AA8 LYS A 189 ? PHE A 207 ? LYS A 202 PHE A 220 1 ? 19 
HELX_P HELX_P9  AA9 SER A 219 ? ARG A 228 ? SER A 232 ARG A 241 1 ? 10 
HELX_P HELX_P10 AB1 GLY A 247 ? HIS A 255 ? GLY A 260 HIS A 268 1 ? 9  
HELX_P HELX_P11 AB2 LEU A 282 ? TYR A 297 ? LEU A 295 TYR A 310 1 ? 16 
HELX_P HELX_P12 AB3 THR A 301 ? PHE A 323 ? THR A 314 PHE A 336 1 ? 23 
HELX_P HELX_P13 AB4 CYS B 39  ? HIS B 48  ? CYS B 52  HIS B 61  1 ? 10 
HELX_P HELX_P14 AB5 THR B 58  ? ASN B 71  ? THR B 71  ASN B 84  1 ? 14 
HELX_P HELX_P15 AB6 GLU B 73  ? GLY B 89  ? GLU B 86  GLY B 102 1 ? 17 
HELX_P HELX_P16 AB7 THR B 102 ? GLY B 106 ? THR B 115 GLY B 119 5 ? 5  
HELX_P HELX_P17 AB8 ASP B 134 ? GLY B 138 ? ASP B 147 GLY B 151 5 ? 5  
HELX_P HELX_P18 AB9 ASN B 144 ? GLY B 159 ? ASN B 157 GLY B 172 1 ? 16 
HELX_P HELX_P19 AC1 ASN B 164 ? ASN B 183 ? ASN B 177 ASN B 196 1 ? 20 
HELX_P HELX_P20 AC2 LYS B 189 ? PHE B 207 ? LYS B 202 PHE B 220 1 ? 19 
HELX_P HELX_P21 AC3 SER B 219 ? ARG B 228 ? SER B 232 ARG B 241 1 ? 10 
HELX_P HELX_P22 AC4 GLY B 247 ? HIS B 255 ? GLY B 260 HIS B 268 1 ? 9  
HELX_P HELX_P23 AC5 LEU B 282 ? TYR B 297 ? LEU B 295 TYR B 310 1 ? 16 
HELX_P HELX_P24 AC6 THR B 301 ? PHE B 323 ? THR B 314 PHE B 336 1 ? 23 
HELX_P HELX_P25 AC7 CYS C 39  ? HIS C 48  ? CYS C 52  HIS C 61  1 ? 10 
HELX_P HELX_P26 AC8 THR C 58  ? ASN C 71  ? THR C 71  ASN C 84  1 ? 14 
HELX_P HELX_P27 AC9 GLU C 73  ? GLY C 89  ? GLU C 86  GLY C 102 1 ? 17 
HELX_P HELX_P28 AD1 THR C 102 ? GLY C 106 ? THR C 115 GLY C 119 5 ? 5  
HELX_P HELX_P29 AD2 ASP C 134 ? GLY C 138 ? ASP C 147 GLY C 151 5 ? 5  
HELX_P HELX_P30 AD3 ASN C 144 ? GLY C 159 ? ASN C 157 GLY C 172 1 ? 16 
HELX_P HELX_P31 AD4 ASN C 164 ? ASN C 183 ? ASN C 177 ASN C 196 1 ? 20 
HELX_P HELX_P32 AD5 LYS C 189 ? PHE C 207 ? LYS C 202 PHE C 220 1 ? 19 
HELX_P HELX_P33 AD6 SER C 219 ? ARG C 228 ? SER C 232 ARG C 241 1 ? 10 
HELX_P HELX_P34 AD7 GLY C 247 ? HIS C 255 ? GLY C 260 HIS C 268 1 ? 9  
HELX_P HELX_P35 AD8 LEU C 282 ? TYR C 297 ? LEU C 295 TYR C 310 1 ? 16 
HELX_P HELX_P36 AD9 THR C 301 ? PHE C 323 ? THR C 314 PHE C 336 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A  CYS 283 SG  ? ? ? 1_555 A  CYS 326 SG ? ? A CYS 296 A CYS 339 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
disulf2  disulf ?    ? B  CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
disulf3  disulf ?    ? C  CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
covale1  covale one  ? A  ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 G NAG 1   1_555 ? ? ? ? ? ? ? 1.464 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 H NAG 1   1_555 ? ? ? ? ? ? ? 1.424 ? 
N-Glycosylation 
covale3  covale one  ? B  ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 X NAG 1   1_555 ? ? ? ? ? ? ? 1.431 ? 
N-Glycosylation 
covale4  covale one  ? B  ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 Y NAG 1   1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale5  covale one  ? C  ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 l NAG 1   1_555 ? ? ? ? ? ? ? 1.465 ? 
N-Glycosylation 
covale6  covale one  ? C  ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 n NAG 1   1_555 ? ? ? ? ? ? ? 1.448 ? 
N-Glycosylation 
covale7  covale both ? D  NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale8  covale both ? D  NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale9  covale both ? D  BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 4   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale10 covale both ? D  BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 5   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale11 covale both ? E  NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.386 ? ? 
covale12 covale both ? E  NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale13 covale both ? E  BMA .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? H BMA 3   H MAN 4   1_555 ? ? ? ? ? ? ? 1.405 ? ? 
covale14 covale both ? E  BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? H BMA 3   H MAN 7   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale15 covale both ? E  MAN .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? H MAN 4   H MAN 5   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale16 covale both ? E  MAN .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? H MAN 4   H MAN 6   1_555 ? ? ? ? ? ? ? 1.405 ? ? 
covale17 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? X NAG 1   X NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale18 covale both ? F  NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? X NAG 2   X BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale19 covale both ? F  BMA .   O3  ? ? ? 1_555 F  MAN .   C1 ? ? X BMA 3   X MAN 4   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale20 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? Y NAG 1   Y NAG 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale21 covale both ? G  NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? Y NAG 2   Y BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale22 covale both ? G  BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? Y BMA 3   Y MAN 4   1_555 ? ? ? ? ? ? ? 1.407 ? ? 
covale23 covale both ? G  BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? Y BMA 3   Y MAN 6   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale24 covale both ? G  MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? Y MAN 4   Y MAN 5   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale25 covale both ? H  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? l NAG 1   l NAG 2   1_555 ? ? ? ? ? ? ? 1.381 ? ? 
covale26 covale both ? H  NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? l NAG 2   l BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale27 covale both ? H  BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? l BMA 3   l MAN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale28 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? n NAG 1   n NAG 2   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
metalc1  metalc ?    ? A  CYS 39  SG  ? ? ? 1_555 N  HEM .   FE ? ? A CYS 52  A HEM 405 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc2  metalc ?    ? A  GLU 125 OE2 ? ? ? 1_555 Q  MG  .   MG ? ? A GLU 138 A MG  408 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc3  metalc ?    ? A  GLY 126 O   ? ? ? 1_555 Q  MG  .   MG ? ? A GLY 139 A MG  408 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc4  metalc ?    ? N  HEM .   O1A ? ? ? 1_555 Q  MG  .   MG ? ? A HEM 405 A MG  408 1_555 ? ? ? ? ? ? ? 2.136 ? ? 
metalc5  metalc ?    ? Q  MG  .   MG  ? ? ? 1_555 CA HOH .   O  ? ? A MG  408 A HOH 503 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc6  metalc ?    ? Q  MG  .   MG  ? ? ? 1_555 CA HOH .   O  ? ? A MG  408 A HOH 575 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc7  metalc ?    ? Q  MG  .   MG  ? ? ? 1_555 CA HOH .   O  ? ? A MG  408 A HOH 631 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc8  metalc ?    ? B  CYS 39  SG  ? ? ? 1_555 U  HEM .   FE ? ? B CYS 52  B HEM 404 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc9  metalc ?    ? B  GLU 125 OE2 ? ? ? 1_555 W  MG  .   MG ? ? B GLU 138 B MG  406 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc10 metalc ?    ? B  GLY 126 O   ? ? ? 1_555 W  MG  .   MG ? ? B GLY 139 B MG  406 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc11 metalc ?    ? U  HEM .   O2A ? ? ? 1_555 W  MG  .   MG ? ? B HEM 404 B MG  406 1_555 ? ? ? ? ? ? ? 2.821 ? ? 
metalc12 metalc ?    ? W  MG  .   MG  ? ? ? 1_555 DA HOH .   O  ? ? B MG  406 B HOH 501 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc13 metalc ?    ? W  MG  .   MG  ? ? ? 1_555 DA HOH .   O  ? ? B MG  406 B HOH 524 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc14 metalc ?    ? C  CYS 39  SG  ? ? ? 1_555 Y  HEM .   FE ? ? C CYS 52  C HEM 402 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc15 metalc ?    ? C  GLU 125 OE2 ? ? ? 1_555 BA MG  .   MG ? ? C GLU 138 C MG  405 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc16 metalc ?    ? C  GLY 126 O   ? ? ? 1_555 BA MG  .   MG ? ? C GLY 139 C MG  405 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc17 metalc ?    ? Y  HEM .   O2A ? ? ? 1_555 BA MG  .   MG ? ? C HEM 402 C MG  405 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc18 metalc ?    ? BA MG  .   MG  ? ? ? 1_555 EA HOH .   O  ? ? C MG  405 C HOH 506 1_555 ? ? ? ? ? ? ? 1.958 ? ? 
# 
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 ? N  HEM . ? A HEM 405 ? 1_555 NA  ? N  HEM .   ? A HEM 405 ? 1_555 100.9 ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 NB  ? N  HEM .   ? A HEM 405 ? 1_555 92.7  ? 
3  NA  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 NB  ? N  HEM .   ? A HEM 405 ? 1_555 88.6  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 NC  ? N  HEM .   ? A HEM 405 ? 1_555 89.2  ? 
5  NA  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 NC  ? N  HEM .   ? A HEM 405 ? 1_555 168.9 ? 
6  NB  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 NC  ? N  HEM .   ? A HEM 405 ? 1_555 86.3  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 ND  ? N  HEM .   ? A HEM 405 ? 1_555 95.9  ? 
8  NA  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 ND  ? N  HEM .   ? A HEM 405 ? 1_555 92.1  ? 
9  NB  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 ND  ? N  HEM .   ? A HEM 405 ? 1_555 171.1 ? 
10 NC  ? N  HEM .   ? A HEM 405 ? 1_555 FE ? N  HEM . ? A HEM 405 ? 1_555 ND  ? N  HEM .   ? A HEM 405 ? 1_555 91.4  ? 
11 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 81.8  ? 
12 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O1A ? N  HEM .   ? A HEM 405 ? 1_555 97.1  ? 
13 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O1A ? N  HEM .   ? A HEM 405 ? 1_555 94.3  ? 
14 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 503 ? 1_555 164.4 ? 
15 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 503 ? 1_555 87.5  ? 
16 O1A ? N  HEM .   ? A HEM 405 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 503 ? 1_555 72.3  ? 
17 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 575 ? 1_555 91.5  ? 
18 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 575 ? 1_555 172.6 ? 
19 O1A ? N  HEM .   ? A HEM 405 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 575 ? 1_555 83.3  ? 
20 O   ? CA HOH .   ? A HOH 503 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 575 ? 1_555 98.4  ? 
21 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 631 ? 1_555 89.8  ? 
22 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 631 ? 1_555 89.3  ? 
23 O1A ? N  HEM .   ? A HEM 405 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 631 ? 1_555 172.6 ? 
24 O   ? CA HOH .   ? A HOH 503 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 631 ? 1_555 101.5 ? 
25 O   ? CA HOH .   ? A HOH 575 ? 1_555 MG ? Q  MG  . ? A MG  408 ? 1_555 O   ? CA HOH .   ? A HOH 631 ? 1_555 93.9  ? 
26 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NA  ? U  HEM .   ? B HEM 404 ? 1_555 100.1 ? 
27 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NB  ? U  HEM .   ? B HEM 404 ? 1_555 92.2  ? 
28 NA  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NB  ? U  HEM .   ? B HEM 404 ? 1_555 87.7  ? 
29 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NC  ? U  HEM .   ? B HEM 404 ? 1_555 89.8  ? 
30 NA  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NC  ? U  HEM .   ? B HEM 404 ? 1_555 169.5 ? 
31 NB  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 NC  ? U  HEM .   ? B HEM 404 ? 1_555 88.2  ? 
32 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 ND  ? U  HEM .   ? B HEM 404 ? 1_555 96.4  ? 
33 NA  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 ND  ? U  HEM .   ? B HEM 404 ? 1_555 91.3  ? 
34 NB  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 ND  ? U  HEM .   ? B HEM 404 ? 1_555 171.4 ? 
35 NC  ? U  HEM .   ? B HEM 404 ? 1_555 FE ? U  HEM . ? B HEM 404 ? 1_555 ND  ? U  HEM .   ? B HEM 404 ? 1_555 91.3  ? 
36 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 74.4  ? 
37 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O2A ? U  HEM .   ? B HEM 404 ? 1_555 72.7  ? 
38 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O2A ? U  HEM .   ? B HEM 404 ? 1_555 72.6  ? 
39 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 501 ? 1_555 125.1 ? 
40 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 501 ? 1_555 79.9  ? 
41 O2A ? U  HEM .   ? B HEM 404 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 501 ? 1_555 53.5  ? 
42 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 524 ? 1_555 75.0  ? 
43 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 524 ? 1_555 129.7 ? 
44 O2A ? U  HEM .   ? B HEM 404 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 524 ? 1_555 60.6  ? 
45 O   ? DA HOH .   ? B HOH 501 ? 1_555 MG ? W  MG  . ? B MG  406 ? 1_555 O   ? DA HOH .   ? B HOH 524 ? 1_555 86.3  ? 
46 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NA  ? Y  HEM .   ? C HEM 402 ? 1_555 101.4 ? 
47 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NB  ? Y  HEM .   ? C HEM 402 ? 1_555 91.5  ? 
48 NA  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NB  ? Y  HEM .   ? C HEM 402 ? 1_555 88.2  ? 
49 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NC  ? Y  HEM .   ? C HEM 402 ? 1_555 87.3  ? 
50 NA  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NC  ? Y  HEM .   ? C HEM 402 ? 1_555 170.3 ? 
51 NB  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 NC  ? Y  HEM .   ? C HEM 402 ? 1_555 87.3  ? 
52 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 ND  ? Y  HEM .   ? C HEM 402 ? 1_555 94.7  ? 
53 NA  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 ND  ? Y  HEM .   ? C HEM 402 ? 1_555 93.9  ? 
54 NB  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 ND  ? Y  HEM .   ? C HEM 402 ? 1_555 172.8 ? 
55 NC  ? Y  HEM .   ? C HEM 402 ? 1_555 FE ? Y  HEM . ? C HEM 402 ? 1_555 ND  ? Y  HEM .   ? C HEM 402 ? 1_555 89.6  ? 
56 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 69.4  ? 
57 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O2A ? Y  HEM .   ? C HEM 402 ? 1_555 87.3  ? 
58 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O2A ? Y  HEM .   ? C HEM 402 ? 1_555 94.2  ? 
59 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O   ? EA HOH .   ? C HOH 506 ? 1_555 69.0  ? 
60 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O   ? EA HOH .   ? C HOH 506 ? 1_555 136.5 ? 
61 O2A ? Y  HEM .   ? C HEM 402 ? 1_555 MG ? BA MG  . ? C MG  405 ? 1_555 O   ? EA HOH .   ? C HOH 506 ? 1_555 71.7  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG D .   ? ASN A 144 ? NAG G 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG H 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG X 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG Y 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG l 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG n 1   ? 1_555 ASN C 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 283 ? CYS A 326 ? CYS A 296 ? 1_555 CYS A 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 283 ? CYS B 326 ? CYS B 296 ? 1_555 CYS B 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS C 283 ? CYS C 326 ? CYS C 296 ? 1_555 CYS C 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 111 A . ? PRO 124 A PRO 112 A ? PRO 125 A 1 5.18 
2 PRO 111 B . ? PRO 124 B PRO 112 B ? PRO 125 B 1 4.30 
3 PRO 111 C . ? PRO 124 C PRO 112 C ? PRO 125 C 1 4.59 
# 
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                   9HE9 
_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 NH1 A ARG 318 ? B O  A TYR 345 ? ? 2.08 
2 1 NH1 C ARG 318 ? B O  C HOH 501 ? ? 2.14 
3 1 O4  H NAG 1   ? ? O5 H NAG 2   ? ? 2.18 
# 
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 ? ? -140.71 -35.17  
2  1 PHE A 137 ? ? -102.89 -80.57  
3  1 ASN A 203 ? ? 53.73   -123.28 
4  1 SER A 252 ? ? -39.45  140.01  
5  1 SER A 257 ? ? -157.51 -101.07 
6  1 ASN A 282 ? ? -145.37 53.89   
7  1 ASN A 312 ? ? -151.65 64.89   
8  1 HIS B 127 ? ? -140.51 -35.48  
9  1 PHE B 137 ? ? -103.08 -80.53  
10 1 ASN B 203 ? ? 54.06   -123.51 
11 1 SER B 257 ? ? -155.45 -98.79  
12 1 ASN B 282 ? ? -145.02 54.03   
13 1 HIS C 127 ? ? -141.86 -33.95  
14 1 PHE C 137 ? ? -104.13 -81.65  
15 1 ASN C 203 ? ? 52.45   -122.43 
16 1 SER C 257 ? ? -154.08 -100.18 
17 1 ASN C 282 ? ? -144.99 54.63   
18 1 ASN C 312 ? ? -150.56 61.85   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    C 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     675 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   EA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 807 ? 6.09 . 
2 1 O ? B HOH 742 ? 5.95 . 
3 1 O ? B HOH 744 ? 5.99 . 
4 1 O ? B HOH 745 ? 6.35 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BMA C1   C  N R 74  
BMA C2   C  N S 75  
BMA C3   C  N S 76  
BMA C4   C  N S 77  
BMA C5   C  N R 78  
BMA C6   C  N N 79  
BMA O1   O  N N 80  
BMA O2   O  N N 81  
BMA O3   O  N N 82  
BMA O4   O  N N 83  
BMA O5   O  N N 84  
BMA O6   O  N N 85  
BMA H1   H  N N 86  
BMA H2   H  N N 87  
BMA H3   H  N N 88  
BMA H4   H  N N 89  
BMA H5   H  N N 90  
BMA H61  H  N N 91  
BMA H62  H  N N 92  
BMA HO1  H  N N 93  
BMA HO2  H  N N 94  
BMA HO3  H  N N 95  
BMA HO4  H  N N 96  
BMA HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DAO O1   O  N N 112 
DAO O2   O  N N 113 
DAO C1   C  N N 114 
DAO C2   C  N N 115 
DAO C3   C  N N 116 
DAO C4   C  N N 117 
DAO C5   C  N N 118 
DAO C6   C  N N 119 
DAO C7   C  N N 120 
DAO C8   C  N N 121 
DAO C9   C  N N 122 
DAO C10  C  N N 123 
DAO C11  C  N N 124 
DAO C12  C  N N 125 
DAO HO2  H  N N 126 
DAO H21  H  N N 127 
DAO H22  H  N N 128 
DAO H31  H  N N 129 
DAO H32  H  N N 130 
DAO H41  H  N N 131 
DAO H42  H  N N 132 
DAO H51  H  N N 133 
DAO H52  H  N N 134 
DAO H61  H  N N 135 
DAO H62  H  N N 136 
DAO H71  H  N N 137 
DAO H72  H  N N 138 
DAO H81  H  N N 139 
DAO H82  H  N N 140 
DAO H91  H  N N 141 
DAO H92  H  N N 142 
DAO H101 H  N N 143 
DAO H102 H  N N 144 
DAO H111 H  N N 145 
DAO H112 H  N N 146 
DAO H121 H  N N 147 
DAO H122 H  N N 148 
DAO H123 H  N N 149 
EPE N1   N  N N 150 
EPE C2   C  N N 151 
EPE C3   C  N N 152 
EPE N4   N  N N 153 
EPE C5   C  N N 154 
EPE C6   C  N N 155 
EPE C7   C  N N 156 
EPE C8   C  N N 157 
EPE O8   O  N N 158 
EPE C9   C  N N 159 
EPE C10  C  N N 160 
EPE S    S  N N 161 
EPE O1S  O  N N 162 
EPE O2S  O  N N 163 
EPE O3S  O  N N 164 
EPE H21  H  N N 165 
EPE H22  H  N N 166 
EPE H31  H  N N 167 
EPE H32  H  N N 168 
EPE H51  H  N N 169 
EPE H52  H  N N 170 
EPE H61  H  N N 171 
EPE H62  H  N N 172 
EPE H71  H  N N 173 
EPE H72  H  N N 174 
EPE H81  H  N N 175 
EPE H82  H  N N 176 
EPE HO8  H  N N 177 
EPE H91  H  N N 178 
EPE H92  H  N N 179 
EPE H101 H  N N 180 
EPE H102 H  N N 181 
EPE HOS3 H  N N 182 
GLN N    N  N N 183 
GLN CA   C  N S 184 
GLN C    C  N N 185 
GLN O    O  N N 186 
GLN CB   C  N N 187 
GLN CG   C  N N 188 
GLN CD   C  N N 189 
GLN OE1  O  N N 190 
GLN NE2  N  N N 191 
GLN OXT  O  N N 192 
GLN H    H  N N 193 
GLN H2   H  N N 194 
GLN HA   H  N N 195 
GLN HB2  H  N N 196 
GLN HB3  H  N N 197 
GLN HG2  H  N N 198 
GLN HG3  H  N N 199 
GLN HE21 H  N N 200 
GLN HE22 H  N N 201 
GLN HXT  H  N N 202 
GLU N    N  N N 203 
GLU CA   C  N S 204 
GLU C    C  N N 205 
GLU O    O  N N 206 
GLU CB   C  N N 207 
GLU CG   C  N N 208 
GLU CD   C  N N 209 
GLU OE1  O  N N 210 
GLU OE2  O  N N 211 
GLU OXT  O  N N 212 
GLU H    H  N N 213 
GLU H2   H  N N 214 
GLU HA   H  N N 215 
GLU HB2  H  N N 216 
GLU HB3  H  N N 217 
GLU HG2  H  N N 218 
GLU HG3  H  N N 219 
GLU HE2  H  N N 220 
GLU HXT  H  N N 221 
GLY N    N  N N 222 
GLY CA   C  N N 223 
GLY C    C  N N 224 
GLY O    O  N N 225 
GLY OXT  O  N N 226 
GLY H    H  N N 227 
GLY H2   H  N N 228 
GLY HA2  H  N N 229 
GLY HA3  H  N N 230 
GLY HXT  H  N N 231 
GOL C1   C  N N 232 
GOL O1   O  N N 233 
GOL C2   C  N N 234 
GOL O2   O  N N 235 
GOL C3   C  N N 236 
GOL O3   O  N N 237 
GOL H11  H  N N 238 
GOL H12  H  N N 239 
GOL HO1  H  N N 240 
GOL H2   H  N N 241 
GOL HO2  H  N N 242 
GOL H31  H  N N 243 
GOL H32  H  N N 244 
GOL HO3  H  N N 245 
HEM CHA  C  N N 246 
HEM CHB  C  N N 247 
HEM CHC  C  N N 248 
HEM CHD  C  N N 249 
HEM C1A  C  Y N 250 
HEM C2A  C  Y N 251 
HEM C3A  C  Y N 252 
HEM C4A  C  Y N 253 
HEM CMA  C  N N 254 
HEM CAA  C  N N 255 
HEM CBA  C  N N 256 
HEM CGA  C  N N 257 
HEM O1A  O  N N 258 
HEM O2A  O  N N 259 
HEM C1B  C  N N 260 
HEM C2B  C  N N 261 
HEM C3B  C  N N 262 
HEM C4B  C  N N 263 
HEM CMB  C  N N 264 
HEM CAB  C  N N 265 
HEM CBB  C  N N 266 
HEM C1C  C  Y N 267 
HEM C2C  C  Y N 268 
HEM C3C  C  Y N 269 
HEM C4C  C  Y N 270 
HEM CMC  C  N N 271 
HEM CAC  C  N N 272 
HEM CBC  C  N N 273 
HEM C1D  C  N N 274 
HEM C2D  C  N N 275 
HEM C3D  C  N N 276 
HEM C4D  C  N N 277 
HEM CMD  C  N N 278 
HEM CAD  C  N N 279 
HEM CBD  C  N N 280 
HEM CGD  C  N N 281 
HEM O1D  O  N N 282 
HEM O2D  O  N N 283 
HEM NA   N  Y N 284 
HEM NB   N  N N 285 
HEM NC   N  Y N 286 
HEM ND   N  N N 287 
HEM FE   FE N N 288 
HEM HHB  H  N N 289 
HEM HHC  H  N N 290 
HEM HHD  H  N N 291 
HEM HMA  H  N N 292 
HEM HMAA H  N N 293 
HEM HMAB H  N N 294 
HEM HAA  H  N N 295 
HEM HAAA H  N N 296 
HEM HBA  H  N N 297 
HEM HBAA H  N N 298 
HEM HMB  H  N N 299 
HEM HMBA H  N N 300 
HEM HMBB H  N N 301 
HEM HAB  H  N N 302 
HEM HBB  H  N N 303 
HEM HBBA H  N N 304 
HEM HMC  H  N N 305 
HEM HMCA H  N N 306 
HEM HMCB H  N N 307 
HEM HAC  H  N N 308 
HEM HBC  H  N N 309 
HEM HBCA H  N N 310 
HEM HMD  H  N N 311 
HEM HMDA H  N N 312 
HEM HMDB H  N N 313 
HEM HAD  H  N N 314 
HEM HADA H  N N 315 
HEM HBD  H  N N 316 
HEM HBDA H  N N 317 
HEM H2A  H  N N 318 
HEM H2D  H  N N 319 
HEM HHA  H  N N 320 
HIS N    N  N N 321 
HIS CA   C  N S 322 
HIS C    C  N N 323 
HIS O    O  N N 324 
HIS CB   C  N N 325 
HIS CG   C  Y N 326 
HIS ND1  N  Y N 327 
HIS CD2  C  Y N 328 
HIS CE1  C  Y N 329 
HIS NE2  N  Y N 330 
HIS OXT  O  N N 331 
HIS H    H  N N 332 
HIS H2   H  N N 333 
HIS HA   H  N N 334 
HIS HB2  H  N N 335 
HIS HB3  H  N N 336 
HIS HD1  H  N N 337 
HIS HD2  H  N N 338 
HIS HE1  H  N N 339 
HIS HE2  H  N N 340 
HIS HXT  H  N N 341 
HOH O    O  N N 342 
HOH H1   H  N N 343 
HOH H2   H  N N 344 
ILE N    N  N N 345 
ILE CA   C  N S 346 
ILE C    C  N N 347 
ILE O    O  N N 348 
ILE CB   C  N S 349 
ILE CG1  C  N N 350 
ILE CG2  C  N N 351 
ILE CD1  C  N N 352 
ILE OXT  O  N N 353 
ILE H    H  N N 354 
ILE H2   H  N N 355 
ILE HA   H  N N 356 
ILE HB   H  N N 357 
ILE HG12 H  N N 358 
ILE HG13 H  N N 359 
ILE HG21 H  N N 360 
ILE HG22 H  N N 361 
ILE HG23 H  N N 362 
ILE HD11 H  N N 363 
ILE HD12 H  N N 364 
ILE HD13 H  N N 365 
ILE HXT  H  N N 366 
LEU N    N  N N 367 
LEU CA   C  N S 368 
LEU C    C  N N 369 
LEU O    O  N N 370 
LEU CB   C  N N 371 
LEU CG   C  N N 372 
LEU CD1  C  N N 373 
LEU CD2  C  N N 374 
LEU OXT  O  N N 375 
LEU H    H  N N 376 
LEU H2   H  N N 377 
LEU HA   H  N N 378 
LEU HB2  H  N N 379 
LEU HB3  H  N N 380 
LEU HG   H  N N 381 
LEU HD11 H  N N 382 
LEU HD12 H  N N 383 
LEU HD13 H  N N 384 
LEU HD21 H  N N 385 
LEU HD22 H  N N 386 
LEU HD23 H  N N 387 
LEU HXT  H  N N 388 
LYS N    N  N N 389 
LYS CA   C  N S 390 
LYS C    C  N N 391 
LYS O    O  N N 392 
LYS CB   C  N N 393 
LYS CG   C  N N 394 
LYS CD   C  N N 395 
LYS CE   C  N N 396 
LYS NZ   N  N N 397 
LYS OXT  O  N N 398 
LYS H    H  N N 399 
LYS H2   H  N N 400 
LYS HA   H  N N 401 
LYS HB2  H  N N 402 
LYS HB3  H  N N 403 
LYS HG2  H  N N 404 
LYS HG3  H  N N 405 
LYS HD2  H  N N 406 
LYS HD3  H  N N 407 
LYS HE2  H  N N 408 
LYS HE3  H  N N 409 
LYS HZ1  H  N N 410 
LYS HZ2  H  N N 411 
LYS HZ3  H  N N 412 
LYS HXT  H  N N 413 
MAN C1   C  N S 414 
MAN C2   C  N S 415 
MAN C3   C  N S 416 
MAN C4   C  N S 417 
MAN C5   C  N R 418 
MAN C6   C  N N 419 
MAN O1   O  N N 420 
MAN O2   O  N N 421 
MAN O3   O  N N 422 
MAN O4   O  N N 423 
MAN O5   O  N N 424 
MAN O6   O  N N 425 
MAN H1   H  N N 426 
MAN H2   H  N N 427 
MAN H3   H  N N 428 
MAN H4   H  N N 429 
MAN H5   H  N N 430 
MAN H61  H  N N 431 
MAN H62  H  N N 432 
MAN HO1  H  N N 433 
MAN HO2  H  N N 434 
MAN HO3  H  N N 435 
MAN HO4  H  N N 436 
MAN HO6  H  N N 437 
MET N    N  N N 438 
MET CA   C  N S 439 
MET C    C  N N 440 
MET O    O  N N 441 
MET CB   C  N N 442 
MET CG   C  N N 443 
MET SD   S  N N 444 
MET CE   C  N N 445 
MET OXT  O  N N 446 
MET H    H  N N 447 
MET H2   H  N N 448 
MET HA   H  N N 449 
MET HB2  H  N N 450 
MET HB3  H  N N 451 
MET HG2  H  N N 452 
MET HG3  H  N N 453 
MET HE1  H  N N 454 
MET HE2  H  N N 455 
MET HE3  H  N N 456 
MET HXT  H  N N 457 
MG  MG   MG N N 458 
NAG C1   C  N R 459 
NAG C2   C  N R 460 
NAG C3   C  N R 461 
NAG C4   C  N S 462 
NAG C5   C  N R 463 
NAG C6   C  N N 464 
NAG C7   C  N N 465 
NAG C8   C  N N 466 
NAG N2   N  N N 467 
NAG O1   O  N N 468 
NAG O3   O  N N 469 
NAG O4   O  N N 470 
NAG O5   O  N N 471 
NAG O6   O  N N 472 
NAG O7   O  N N 473 
NAG H1   H  N N 474 
NAG H2   H  N N 475 
NAG H3   H  N N 476 
NAG H4   H  N N 477 
NAG H5   H  N N 478 
NAG H61  H  N N 479 
NAG H62  H  N N 480 
NAG H81  H  N N 481 
NAG H82  H  N N 482 
NAG H83  H  N N 483 
NAG HN2  H  N N 484 
NAG HO1  H  N N 485 
NAG HO3  H  N N 486 
NAG HO4  H  N N 487 
NAG HO6  H  N N 488 
PHE N    N  N N 489 
PHE CA   C  N S 490 
PHE C    C  N N 491 
PHE O    O  N N 492 
PHE CB   C  N N 493 
PHE CG   C  Y N 494 
PHE CD1  C  Y N 495 
PHE CD2  C  Y N 496 
PHE CE1  C  Y N 497 
PHE CE2  C  Y N 498 
PHE CZ   C  Y N 499 
PHE OXT  O  N N 500 
PHE H    H  N N 501 
PHE H2   H  N N 502 
PHE HA   H  N N 503 
PHE HB2  H  N N 504 
PHE HB3  H  N N 505 
PHE HD1  H  N N 506 
PHE HD2  H  N N 507 
PHE HE1  H  N N 508 
PHE HE2  H  N N 509 
PHE HZ   H  N N 510 
PHE HXT  H  N N 511 
PRO N    N  N N 512 
PRO CA   C  N S 513 
PRO C    C  N N 514 
PRO O    O  N N 515 
PRO CB   C  N N 516 
PRO CG   C  N N 517 
PRO CD   C  N N 518 
PRO OXT  O  N N 519 
PRO H    H  N N 520 
PRO HA   H  N N 521 
PRO HB2  H  N N 522 
PRO HB3  H  N N 523 
PRO HG2  H  N N 524 
PRO HG3  H  N N 525 
PRO HD2  H  N N 526 
PRO HD3  H  N N 527 
PRO HXT  H  N N 528 
SER N    N  N N 529 
SER CA   C  N S 530 
SER C    C  N N 531 
SER O    O  N N 532 
SER CB   C  N N 533 
SER OG   O  N N 534 
SER OXT  O  N N 535 
SER H    H  N N 536 
SER H2   H  N N 537 
SER HA   H  N N 538 
SER HB2  H  N N 539 
SER HB3  H  N N 540 
SER HG   H  N N 541 
SER HXT  H  N N 542 
SO4 S    S  N N 543 
SO4 O1   O  N N 544 
SO4 O2   O  N N 545 
SO4 O3   O  N N 546 
SO4 O4   O  N N 547 
THR N    N  N N 548 
THR CA   C  N S 549 
THR C    C  N N 550 
THR O    O  N N 551 
THR CB   C  N R 552 
THR OG1  O  N N 553 
THR CG2  C  N N 554 
THR OXT  O  N N 555 
THR H    H  N N 556 
THR H2   H  N N 557 
THR HA   H  N N 558 
THR HB   H  N N 559 
THR HG1  H  N N 560 
THR HG21 H  N N 561 
THR HG22 H  N N 562 
THR HG23 H  N N 563 
THR HXT  H  N N 564 
TRP N    N  N N 565 
TRP CA   C  N S 566 
TRP C    C  N N 567 
TRP O    O  N N 568 
TRP CB   C  N N 569 
TRP CG   C  Y N 570 
TRP CD1  C  Y N 571 
TRP CD2  C  Y N 572 
TRP NE1  N  Y N 573 
TRP CE2  C  Y N 574 
TRP CE3  C  Y N 575 
TRP CZ2  C  Y N 576 
TRP CZ3  C  Y N 577 
TRP CH2  C  Y N 578 
TRP OXT  O  N N 579 
TRP H    H  N N 580 
TRP H2   H  N N 581 
TRP HA   H  N N 582 
TRP HB2  H  N N 583 
TRP HB3  H  N N 584 
TRP HD1  H  N N 585 
TRP HE1  H  N N 586 
TRP HE3  H  N N 587 
TRP HZ2  H  N N 588 
TRP HZ3  H  N N 589 
TRP HH2  H  N N 590 
TRP HXT  H  N N 591 
TYR N    N  N N 592 
TYR CA   C  N S 593 
TYR C    C  N N 594 
TYR O    O  N N 595 
TYR CB   C  N N 596 
TYR CG   C  Y N 597 
TYR CD1  C  Y N 598 
TYR CD2  C  Y N 599 
TYR CE1  C  Y N 600 
TYR CE2  C  Y N 601 
TYR CZ   C  Y N 602 
TYR OH   O  N N 603 
TYR OXT  O  N N 604 
TYR H    H  N N 605 
TYR H2   H  N N 606 
TYR HA   H  N N 607 
TYR HB2  H  N N 608 
TYR HB3  H  N N 609 
TYR HD1  H  N N 610 
TYR HD2  H  N N 611 
TYR HE1  H  N N 612 
TYR HE2  H  N N 613 
TYR HH   H  N N 614 
TYR HXT  H  N N 615 
VAL N    N  N N 616 
VAL CA   C  N S 617 
VAL C    C  N N 618 
VAL O    O  N N 619 
VAL CB   C  N N 620 
VAL CG1  C  N N 621 
VAL CG2  C  N N 622 
VAL OXT  O  N N 623 
VAL H    H  N N 624 
VAL H2   H  N N 625 
VAL HA   H  N N 626 
VAL HB   H  N N 627 
VAL HG11 H  N N 628 
VAL HG12 H  N N 629 
VAL HG13 H  N N 630 
VAL HG21 H  N N 631 
VAL HG22 H  N N 632 
VAL HG23 H  N N 633 
VAL HXT  H  N N 634 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
DAO O1  C1   doub N N 107 
DAO O2  C1   sing N N 108 
DAO O2  HO2  sing N N 109 
DAO C1  C2   sing N N 110 
DAO C2  C3   sing N N 111 
DAO C2  H21  sing N N 112 
DAO C2  H22  sing N N 113 
DAO C3  C4   sing N N 114 
DAO C3  H31  sing N N 115 
DAO C3  H32  sing N N 116 
DAO C4  C5   sing N N 117 
DAO C4  H41  sing N N 118 
DAO C4  H42  sing N N 119 
DAO C5  C6   sing N N 120 
DAO C5  H51  sing N N 121 
DAO C5  H52  sing N N 122 
DAO C6  C7   sing N N 123 
DAO C6  H61  sing N N 124 
DAO C6  H62  sing N N 125 
DAO C7  C8   sing N N 126 
DAO C7  H71  sing N N 127 
DAO C7  H72  sing N N 128 
DAO C8  C9   sing N N 129 
DAO C8  H81  sing N N 130 
DAO C8  H82  sing N N 131 
DAO C9  C10  sing N N 132 
DAO C9  H91  sing N N 133 
DAO C9  H92  sing N N 134 
DAO C10 C11  sing N N 135 
DAO C10 H101 sing N N 136 
DAO C10 H102 sing N N 137 
DAO C11 C12  sing N N 138 
DAO C11 H111 sing N N 139 
DAO C11 H112 sing N N 140 
DAO C12 H121 sing N N 141 
DAO C12 H122 sing N N 142 
DAO C12 H123 sing N N 143 
EPE N1  C2   sing N N 144 
EPE N1  C6   sing N N 145 
EPE N1  C9   sing N N 146 
EPE C2  C3   sing N N 147 
EPE C2  H21  sing N N 148 
EPE C2  H22  sing N N 149 
EPE C3  N4   sing N N 150 
EPE C3  H31  sing N N 151 
EPE C3  H32  sing N N 152 
EPE N4  C5   sing N N 153 
EPE N4  C7   sing N N 154 
EPE C5  C6   sing N N 155 
EPE C5  H51  sing N N 156 
EPE C5  H52  sing N N 157 
EPE C6  H61  sing N N 158 
EPE C6  H62  sing N N 159 
EPE C7  C8   sing N N 160 
EPE C7  H71  sing N N 161 
EPE C7  H72  sing N N 162 
EPE C8  O8   sing N N 163 
EPE C8  H81  sing N N 164 
EPE C8  H82  sing N N 165 
EPE O8  HO8  sing N N 166 
EPE C9  C10  sing N N 167 
EPE C9  H91  sing N N 168 
EPE C9  H92  sing N N 169 
EPE C10 S    sing N N 170 
EPE C10 H101 sing N N 171 
EPE C10 H102 sing N N 172 
EPE S   O1S  doub N N 173 
EPE S   O2S  doub N N 174 
EPE S   O3S  sing N N 175 
EPE O3S HOS3 sing N N 176 
GLN N   CA   sing N N 177 
GLN N   H    sing N N 178 
GLN N   H2   sing N N 179 
GLN CA  C    sing N N 180 
GLN CA  CB   sing N N 181 
GLN CA  HA   sing N N 182 
GLN C   O    doub N N 183 
GLN C   OXT  sing N N 184 
GLN CB  CG   sing N N 185 
GLN CB  HB2  sing N N 186 
GLN CB  HB3  sing N N 187 
GLN CG  CD   sing N N 188 
GLN CG  HG2  sing N N 189 
GLN CG  HG3  sing N N 190 
GLN CD  OE1  doub N N 191 
GLN CD  NE2  sing N N 192 
GLN NE2 HE21 sing N N 193 
GLN NE2 HE22 sing N N 194 
GLN OXT HXT  sing N N 195 
GLU N   CA   sing N N 196 
GLU N   H    sing N N 197 
GLU N   H2   sing N N 198 
GLU CA  C    sing N N 199 
GLU CA  CB   sing N N 200 
GLU CA  HA   sing N N 201 
GLU C   O    doub N N 202 
GLU C   OXT  sing N N 203 
GLU CB  CG   sing N N 204 
GLU CB  HB2  sing N N 205 
GLU CB  HB3  sing N N 206 
GLU CG  CD   sing N N 207 
GLU CG  HG2  sing N N 208 
GLU CG  HG3  sing N N 209 
GLU CD  OE1  doub N N 210 
GLU CD  OE2  sing N N 211 
GLU OE2 HE2  sing N N 212 
GLU OXT HXT  sing N N 213 
GLY N   CA   sing N N 214 
GLY N   H    sing N N 215 
GLY N   H2   sing N N 216 
GLY CA  C    sing N N 217 
GLY CA  HA2  sing N N 218 
GLY CA  HA3  sing N N 219 
GLY C   O    doub N N 220 
GLY C   OXT  sing N N 221 
GLY OXT HXT  sing N N 222 
GOL C1  O1   sing N N 223 
GOL C1  C2   sing N N 224 
GOL C1  H11  sing N N 225 
GOL C1  H12  sing N N 226 
GOL O1  HO1  sing N N 227 
GOL C2  O2   sing N N 228 
GOL C2  C3   sing N N 229 
GOL C2  H2   sing N N 230 
GOL O2  HO2  sing N N 231 
GOL C3  O3   sing N N 232 
GOL C3  H31  sing N N 233 
GOL C3  H32  sing N N 234 
GOL O3  HO3  sing N N 235 
HEM CHA C1A  sing N N 236 
HEM CHA C4D  doub N N 237 
HEM CHA HHA  sing N N 238 
HEM CHB C4A  sing N N 239 
HEM CHB C1B  doub N N 240 
HEM CHB HHB  sing N N 241 
HEM CHC C4B  sing N N 242 
HEM CHC C1C  doub N N 243 
HEM CHC HHC  sing N N 244 
HEM CHD C4C  doub N N 245 
HEM CHD C1D  sing N N 246 
HEM CHD HHD  sing N N 247 
HEM C1A C2A  doub Y N 248 
HEM C1A NA   sing Y N 249 
HEM C2A C3A  sing Y N 250 
HEM C2A CAA  sing N N 251 
HEM C3A C4A  doub Y N 252 
HEM C3A CMA  sing N N 253 
HEM C4A NA   sing Y N 254 
HEM CMA HMA  sing N N 255 
HEM CMA HMAA sing N N 256 
HEM CMA HMAB sing N N 257 
HEM CAA CBA  sing N N 258 
HEM CAA HAA  sing N N 259 
HEM CAA HAAA sing N N 260 
HEM CBA CGA  sing N N 261 
HEM CBA HBA  sing N N 262 
HEM CBA HBAA sing N N 263 
HEM CGA O1A  doub N N 264 
HEM CGA O2A  sing N N 265 
HEM C1B C2B  sing N N 266 
HEM C1B NB   sing N N 267 
HEM C2B C3B  doub N N 268 
HEM C2B CMB  sing N N 269 
HEM C3B C4B  sing N N 270 
HEM C3B CAB  sing N N 271 
HEM C4B NB   doub N N 272 
HEM CMB HMB  sing N N 273 
HEM CMB HMBA sing N N 274 
HEM CMB HMBB sing N N 275 
HEM CAB CBB  doub N N 276 
HEM CAB HAB  sing N N 277 
HEM CBB HBB  sing N N 278 
HEM CBB HBBA sing N N 279 
HEM C1C C2C  sing Y N 280 
HEM C1C NC   sing Y N 281 
HEM C2C C3C  doub Y N 282 
HEM C2C CMC  sing N N 283 
HEM C3C C4C  sing Y N 284 
HEM C3C CAC  sing N N 285 
HEM C4C NC   sing Y N 286 
HEM CMC HMC  sing N N 287 
HEM CMC HMCA sing N N 288 
HEM CMC HMCB sing N N 289 
HEM CAC CBC  doub N N 290 
HEM CAC HAC  sing N N 291 
HEM CBC HBC  sing N N 292 
HEM CBC HBCA sing N N 293 
HEM C1D C2D  sing N N 294 
HEM C1D ND   doub N N 295 
HEM C2D C3D  doub N N 296 
HEM C2D CMD  sing N N 297 
HEM C3D C4D  sing N N 298 
HEM C3D CAD  sing N N 299 
HEM C4D ND   sing N N 300 
HEM CMD HMD  sing N N 301 
HEM CMD HMDA sing N N 302 
HEM CMD HMDB sing N N 303 
HEM CAD CBD  sing N N 304 
HEM CAD HAD  sing N N 305 
HEM CAD HADA sing N N 306 
HEM CBD CGD  sing N N 307 
HEM CBD HBD  sing N N 308 
HEM CBD HBDA sing N N 309 
HEM CGD O1D  doub N N 310 
HEM CGD O2D  sing N N 311 
HEM O2A H2A  sing N N 312 
HEM O2D H2D  sing N N 313 
HEM FE  NA   sing N N 314 
HEM FE  NB   sing N N 315 
HEM FE  NC   sing N N 316 
HEM FE  ND   sing N N 317 
HIS N   CA   sing N N 318 
HIS N   H    sing N N 319 
HIS N   H2   sing N N 320 
HIS CA  C    sing N N 321 
HIS CA  CB   sing N N 322 
HIS CA  HA   sing N N 323 
HIS C   O    doub N N 324 
HIS C   OXT  sing N N 325 
HIS CB  CG   sing N N 326 
HIS CB  HB2  sing N N 327 
HIS CB  HB3  sing N N 328 
HIS CG  ND1  sing Y N 329 
HIS CG  CD2  doub Y N 330 
HIS ND1 CE1  doub Y N 331 
HIS ND1 HD1  sing N N 332 
HIS CD2 NE2  sing Y N 333 
HIS CD2 HD2  sing N N 334 
HIS CE1 NE2  sing Y N 335 
HIS CE1 HE1  sing N N 336 
HIS NE2 HE2  sing N N 337 
HIS OXT HXT  sing N N 338 
HOH O   H1   sing N N 339 
HOH O   H2   sing N N 340 
ILE N   CA   sing N N 341 
ILE N   H    sing N N 342 
ILE N   H2   sing N N 343 
ILE CA  C    sing N N 344 
ILE CA  CB   sing N N 345 
ILE CA  HA   sing N N 346 
ILE C   O    doub N N 347 
ILE C   OXT  sing N N 348 
ILE CB  CG1  sing N N 349 
ILE CB  CG2  sing N N 350 
ILE CB  HB   sing N N 351 
ILE CG1 CD1  sing N N 352 
ILE CG1 HG12 sing N N 353 
ILE CG1 HG13 sing N N 354 
ILE CG2 HG21 sing N N 355 
ILE CG2 HG22 sing N N 356 
ILE CG2 HG23 sing N N 357 
ILE CD1 HD11 sing N N 358 
ILE CD1 HD12 sing N N 359 
ILE CD1 HD13 sing N N 360 
ILE OXT HXT  sing N N 361 
LEU N   CA   sing N N 362 
LEU N   H    sing N N 363 
LEU N   H2   sing N N 364 
LEU CA  C    sing N N 365 
LEU CA  CB   sing N N 366 
LEU CA  HA   sing N N 367 
LEU C   O    doub N N 368 
LEU C   OXT  sing N N 369 
LEU CB  CG   sing N N 370 
LEU CB  HB2  sing N N 371 
LEU CB  HB3  sing N N 372 
LEU CG  CD1  sing N N 373 
LEU CG  CD2  sing N N 374 
LEU CG  HG   sing N N 375 
LEU CD1 HD11 sing N N 376 
LEU CD1 HD12 sing N N 377 
LEU CD1 HD13 sing N N 378 
LEU CD2 HD21 sing N N 379 
LEU CD2 HD22 sing N N 380 
LEU CD2 HD23 sing N N 381 
LEU OXT HXT  sing N N 382 
LYS N   CA   sing N N 383 
LYS N   H    sing N N 384 
LYS N   H2   sing N N 385 
LYS CA  C    sing N N 386 
LYS CA  CB   sing N N 387 
LYS CA  HA   sing N N 388 
LYS C   O    doub N N 389 
LYS C   OXT  sing N N 390 
LYS CB  CG   sing N N 391 
LYS CB  HB2  sing N N 392 
LYS CB  HB3  sing N N 393 
LYS CG  CD   sing N N 394 
LYS CG  HG2  sing N N 395 
LYS CG  HG3  sing N N 396 
LYS CD  CE   sing N N 397 
LYS CD  HD2  sing N N 398 
LYS CD  HD3  sing N N 399 
LYS CE  NZ   sing N N 400 
LYS CE  HE2  sing N N 401 
LYS CE  HE3  sing N N 402 
LYS NZ  HZ1  sing N N 403 
LYS NZ  HZ2  sing N N 404 
LYS NZ  HZ3  sing N N 405 
LYS OXT HXT  sing N N 406 
MAN C1  C2   sing N N 407 
MAN C1  O1   sing N N 408 
MAN C1  O5   sing N N 409 
MAN C1  H1   sing N N 410 
MAN C2  C3   sing N N 411 
MAN C2  O2   sing N N 412 
MAN C2  H2   sing N N 413 
MAN C3  C4   sing N N 414 
MAN C3  O3   sing N N 415 
MAN C3  H3   sing N N 416 
MAN C4  C5   sing N N 417 
MAN C4  O4   sing N N 418 
MAN C4  H4   sing N N 419 
MAN C5  C6   sing N N 420 
MAN C5  O5   sing N N 421 
MAN C5  H5   sing N N 422 
MAN C6  O6   sing N N 423 
MAN C6  H61  sing N N 424 
MAN C6  H62  sing N N 425 
MAN O1  HO1  sing N N 426 
MAN O2  HO2  sing N N 427 
MAN O3  HO3  sing N N 428 
MAN O4  HO4  sing N N 429 
MAN O6  HO6  sing N N 430 
MET N   CA   sing N N 431 
MET N   H    sing N N 432 
MET N   H2   sing N N 433 
MET CA  C    sing N N 434 
MET CA  CB   sing N N 435 
MET CA  HA   sing N N 436 
MET C   O    doub N N 437 
MET C   OXT  sing N N 438 
MET CB  CG   sing N N 439 
MET CB  HB2  sing N N 440 
MET CB  HB3  sing N N 441 
MET CG  SD   sing N N 442 
MET CG  HG2  sing N N 443 
MET CG  HG3  sing N N 444 
MET SD  CE   sing N N 445 
MET CE  HE1  sing N N 446 
MET CE  HE2  sing N N 447 
MET CE  HE3  sing N N 448 
MET OXT HXT  sing N N 449 
NAG C1  C2   sing N N 450 
NAG C1  O1   sing N N 451 
NAG C1  O5   sing N N 452 
NAG C1  H1   sing N N 453 
NAG C2  C3   sing N N 454 
NAG C2  N2   sing N N 455 
NAG C2  H2   sing N N 456 
NAG C3  C4   sing N N 457 
NAG C3  O3   sing N N 458 
NAG C3  H3   sing N N 459 
NAG C4  C5   sing N N 460 
NAG C4  O4   sing N N 461 
NAG C4  H4   sing N N 462 
NAG C5  C6   sing N N 463 
NAG C5  O5   sing N N 464 
NAG C5  H5   sing N N 465 
NAG C6  O6   sing N N 466 
NAG C6  H61  sing N N 467 
NAG C6  H62  sing N N 468 
NAG C7  C8   sing N N 469 
NAG C7  N2   sing N N 470 
NAG C7  O7   doub N N 471 
NAG C8  H81  sing N N 472 
NAG C8  H82  sing N N 473 
NAG C8  H83  sing N N 474 
NAG N2  HN2  sing N N 475 
NAG O1  HO1  sing N N 476 
NAG O3  HO3  sing N N 477 
NAG O4  HO4  sing N N 478 
NAG O6  HO6  sing N N 479 
PHE N   CA   sing N N 480 
PHE N   H    sing N N 481 
PHE N   H2   sing N N 482 
PHE CA  C    sing N N 483 
PHE CA  CB   sing N N 484 
PHE CA  HA   sing N N 485 
PHE C   O    doub N N 486 
PHE C   OXT  sing N N 487 
PHE CB  CG   sing N N 488 
PHE CB  HB2  sing N N 489 
PHE CB  HB3  sing N N 490 
PHE CG  CD1  doub Y N 491 
PHE CG  CD2  sing Y N 492 
PHE CD1 CE1  sing Y N 493 
PHE CD1 HD1  sing N N 494 
PHE CD2 CE2  doub Y N 495 
PHE CD2 HD2  sing N N 496 
PHE CE1 CZ   doub Y N 497 
PHE CE1 HE1  sing N N 498 
PHE CE2 CZ   sing Y N 499 
PHE CE2 HE2  sing N N 500 
PHE CZ  HZ   sing N N 501 
PHE OXT HXT  sing N N 502 
PRO N   CA   sing N N 503 
PRO N   CD   sing N N 504 
PRO N   H    sing N N 505 
PRO CA  C    sing N N 506 
PRO CA  CB   sing N N 507 
PRO CA  HA   sing N N 508 
PRO C   O    doub N N 509 
PRO C   OXT  sing N N 510 
PRO CB  CG   sing N N 511 
PRO CB  HB2  sing N N 512 
PRO CB  HB3  sing N N 513 
PRO CG  CD   sing N N 514 
PRO CG  HG2  sing N N 515 
PRO CG  HG3  sing N N 516 
PRO CD  HD2  sing N N 517 
PRO CD  HD3  sing N N 518 
PRO OXT HXT  sing N N 519 
SER N   CA   sing N N 520 
SER N   H    sing N N 521 
SER N   H2   sing N N 522 
SER CA  C    sing N N 523 
SER CA  CB   sing N N 524 
SER CA  HA   sing N N 525 
SER C   O    doub N N 526 
SER C   OXT  sing N N 527 
SER CB  OG   sing N N 528 
SER CB  HB2  sing N N 529 
SER CB  HB3  sing N N 530 
SER OG  HG   sing N N 531 
SER OXT HXT  sing N N 532 
SO4 S   O1   doub N N 533 
SO4 S   O2   doub N N 534 
SO4 S   O3   sing N N 535 
SO4 S   O4   sing N N 536 
THR N   CA   sing N N 537 
THR N   H    sing N N 538 
THR N   H2   sing N N 539 
THR CA  C    sing N N 540 
THR CA  CB   sing N N 541 
THR CA  HA   sing N N 542 
THR C   O    doub N N 543 
THR C   OXT  sing N N 544 
THR CB  OG1  sing N N 545 
THR CB  CG2  sing N N 546 
THR CB  HB   sing N N 547 
THR OG1 HG1  sing N N 548 
THR CG2 HG21 sing N N 549 
THR CG2 HG22 sing N N 550 
THR CG2 HG23 sing N N 551 
THR OXT HXT  sing N N 552 
TRP N   CA   sing N N 553 
TRP N   H    sing N N 554 
TRP N   H2   sing N N 555 
TRP CA  C    sing N N 556 
TRP CA  CB   sing N N 557 
TRP CA  HA   sing N N 558 
TRP C   O    doub N N 559 
TRP C   OXT  sing N N 560 
TRP CB  CG   sing N N 561 
TRP CB  HB2  sing N N 562 
TRP CB  HB3  sing N N 563 
TRP CG  CD1  doub Y N 564 
TRP CG  CD2  sing Y N 565 
TRP CD1 NE1  sing Y N 566 
TRP CD1 HD1  sing N N 567 
TRP CD2 CE2  doub Y N 568 
TRP CD2 CE3  sing Y N 569 
TRP NE1 CE2  sing Y N 570 
TRP NE1 HE1  sing N N 571 
TRP CE2 CZ2  sing Y N 572 
TRP CE3 CZ3  doub Y N 573 
TRP CE3 HE3  sing N N 574 
TRP CZ2 CH2  doub Y N 575 
TRP CZ2 HZ2  sing N N 576 
TRP CZ3 CH2  sing Y N 577 
TRP CZ3 HZ3  sing N N 578 
TRP CH2 HH2  sing N N 579 
TRP OXT HXT  sing N N 580 
TYR N   CA   sing N N 581 
TYR N   H    sing N N 582 
TYR N   H2   sing N N 583 
TYR CA  C    sing N N 584 
TYR CA  CB   sing N N 585 
TYR CA  HA   sing N N 586 
TYR C   O    doub N N 587 
TYR C   OXT  sing N N 588 
TYR CB  CG   sing N N 589 
TYR CB  HB2  sing N N 590 
TYR CB  HB3  sing N N 591 
TYR CG  CD1  doub Y N 592 
TYR CG  CD2  sing Y N 593 
TYR CD1 CE1  sing Y N 594 
TYR CD1 HD1  sing N N 595 
TYR CD2 CE2  doub Y N 596 
TYR CD2 HD2  sing N N 597 
TYR CE1 CZ   doub Y N 598 
TYR CE1 HE1  sing N N 599 
TYR CE2 CZ   sing Y N 600 
TYR CE2 HE2  sing N N 601 
TYR CZ  OH   sing N N 602 
TYR OH  HH   sing N N 603 
TYR OXT HXT  sing N N 604 
VAL N   CA   sing N N 605 
VAL N   H    sing N N 606 
VAL N   H2   sing N N 607 
VAL CA  C    sing N N 608 
VAL CA  CB   sing N N 609 
VAL CA  HA   sing N N 610 
VAL C   O    doub N N 611 
VAL C   OXT  sing N N 612 
VAL CB  CG1  sing N N 613 
VAL CB  CG2  sing N N 614 
VAL CB  HB   sing N N 615 
VAL CG1 HG11 sing N N 616 
VAL CG1 HG12 sing N N 617 
VAL CG1 HG13 sing N N 618 
VAL CG2 HG21 sing N N 619 
VAL CG2 HG22 sing N N 620 
VAL CG2 HG23 sing N N 621 
VAL OXT HXT  sing N N 622 
# 
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 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
5 MAN 4 n 
5 MAN 5 n 
5 MAN 6 n 
6 NAG 1 n 
6 NAG 2 n 
# 
_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                    9HE9 
_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]   0.003678 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001467 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013333 
_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]   0.010210 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLN A  1  1   ? 60.902  3.730   59.322 1.00 111.36 ? 14  GLN A N   1 
ATOM   2    C  CA  . GLN A  1  1   ? 62.231  3.999   58.700 1.00 112.90 ? 14  GLN A CA  1 
ATOM   3    C  C   . GLN A  1  1   ? 62.272  3.515   57.247 1.00 110.32 ? 14  GLN A C   1 
ATOM   4    O  O   . GLN A  1  1   ? 62.881  4.194   56.425 1.00 111.06 ? 14  GLN A O   1 
ATOM   5    C  CB  . GLN A  1  1   ? 63.401  3.463   59.531 1.00 117.29 ? 14  GLN A CB  1 
ATOM   6    C  CG  . GLN A  1  1   ? 63.395  1.954   59.777 1.00 124.39 ? 14  GLN A CG  1 
ATOM   7    C  CD  . GLN A  1  1   ? 64.432  1.516   60.792 1.00 128.49 ? 14  GLN A CD  1 
ATOM   8    O  OE1 . GLN A  1  1   ? 64.691  2.219   61.774 1.00 126.37 ? 14  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A  1  1   ? 65.049  0.361   60.571 1.00 131.35 ? 14  GLN A NE2 1 
ATOM   10   N  N   . GLY A  1  2   ? 61.640  2.368   56.934 1.00 95.83  ? 15  GLY A N   1 
ATOM   11   C  CA  . GLY A  1  2   ? 61.437  1.940   55.556 1.00 79.61  ? 15  GLY A CA  1 
ATOM   12   C  C   . GLY A  1  2   ? 61.250  0.428   55.420 1.00 66.95  ? 15  GLY A C   1 
ATOM   13   O  O   . GLY A  1  2   ? 61.617  -0.346  56.301 1.00 65.68  ? 15  GLY A O   1 
ATOM   14   N  N   . VAL A  1  3   ? 60.717  0.024   54.265 1.00 58.77  ? 16  VAL A N   1 
ATOM   15   C  CA  . VAL A  1  3   ? 60.494  -1.374  53.927 1.00 54.85  ? 16  VAL A CA  1 
ATOM   16   C  C   . VAL A  1  3   ? 61.461  -1.780  52.817 1.00 52.70  ? 16  VAL A C   1 
ATOM   17   O  O   . VAL A  1  3   ? 61.826  -0.963  51.977 1.00 46.84  ? 16  VAL A O   1 
ATOM   18   C  CB  . VAL A  1  3   ? 59.025  -1.568  53.497 1.00 58.48  ? 16  VAL A CB  1 
ATOM   19   C  CG1 . VAL A  1  3   ? 58.797  -2.861  52.726 1.00 60.79  ? 16  VAL A CG1 1 
ATOM   20   C  CG2 . VAL A  1  3   ? 58.086  -1.493  54.691 1.00 63.11  ? 16  VAL A CG2 1 
ATOM   21   N  N   . ASP A  1  4   ? 61.847  -3.057  52.806 1.00 52.39  ? 17  ASP A N   1 
ATOM   22   C  CA  . ASP A  1  4   ? 62.642  -3.619  51.726 1.00 55.19  ? 17  ASP A CA  1 
ATOM   23   C  C   . ASP A  1  4   ? 61.698  -4.361  50.777 1.00 49.26  ? 17  ASP A C   1 
ATOM   24   O  O   . ASP A  1  4   ? 61.211  -5.432  51.119 1.00 47.97  ? 17  ASP A O   1 
ATOM   25   C  CB  . ASP A  1  4   ? 63.738  -4.506  52.297 1.00 65.20  ? 17  ASP A CB  1 
ATOM   26   C  CG  . ASP A  1  4   ? 64.908  -4.787  51.369 1.00 76.07  ? 17  ASP A CG  1 
ATOM   27   O  OD1 . ASP A  1  4   ? 64.946  -4.195  50.267 1.00 81.39  ? 17  ASP A OD1 1 
ATOM   28   O  OD2 . ASP A  1  4   ? 65.797  -5.557  51.786 1.00 86.34  ? 17  ASP A OD2 1 
ATOM   29   N  N   . PRO A  1  5   ? 61.377  -3.822  49.573 1.00 48.72  ? 18  PRO A N   1 
ATOM   30   C  CA  . PRO A  1  5   ? 60.293  -4.372  48.755 1.00 52.28  ? 18  PRO A CA  1 
ATOM   31   C  C   . PRO A  1  5   ? 60.712  -5.663  48.054 1.00 49.55  ? 18  PRO A C   1 
ATOM   32   O  O   . PRO A  1  5   ? 61.727  -5.695  47.360 1.00 48.84  ? 18  PRO A O   1 
ATOM   33   C  CB  . PRO A  1  5   ? 59.965  -3.251  47.754 1.00 50.84  ? 18  PRO A CB  1 
ATOM   34   C  CG  . PRO A  1  5   ? 61.237  -2.426  47.669 1.00 50.67  ? 18  PRO A CG  1 
ATOM   35   C  CD  . PRO A  1  5   ? 62.060  -2.693  48.917 1.00 47.47  ? 18  PRO A CD  1 
ATOM   36   N  N   . PRO A  1  6   ? 59.937  -6.762  48.197 1.00 48.14  ? 19  PRO A N   1 
ATOM   37   C  CA  . PRO A  1  6   ? 60.295  -8.040  47.589 1.00 49.55  ? 19  PRO A CA  1 
ATOM   38   C  C   . PRO A  1  6   ? 59.972  -8.025  46.097 1.00 49.38  ? 19  PRO A C   1 
ATOM   39   O  O   . PRO A  1  6   ? 59.210  -7.181  45.632 1.00 47.84  ? 19  PRO A O   1 
ATOM   40   C  CB  . PRO A  1  6   ? 59.427  -9.029  48.373 1.00 49.96  ? 19  PRO A CB  1 
ATOM   41   C  CG  . PRO A  1  6   ? 58.170  -8.248  48.660 1.00 51.64  ? 19  PRO A CG  1 
ATOM   42   C  CD  . PRO A  1  6   ? 58.655  -6.824  48.915 1.00 51.02  ? 19  PRO A CD  1 
ATOM   43   N  N   . PRO A  1  7   ? 60.548  -8.952  45.299 1.00 52.80  ? 20  PRO A N   1 
ATOM   44   C  CA  . PRO A  1  7   ? 60.210  -9.054  43.882 1.00 47.96  ? 20  PRO A CA  1 
ATOM   45   C  C   . PRO A  1  7   ? 58.743  -9.461  43.732 1.00 42.87  ? 20  PRO A C   1 
ATOM   46   O  O   . PRO A  1  7   ? 58.139  -9.996  44.652 1.00 39.72  ? 20  PRO A O   1 
ATOM   47   C  CB  . PRO A  1  7   ? 61.188  -10.111 43.342 1.00 53.50  ? 20  PRO A CB  1 
ATOM   48   C  CG  . PRO A  1  7   ? 61.563  -10.926 44.556 1.00 56.70  ? 20  PRO A CG  1 
ATOM   49   C  CD  . PRO A  1  7   ? 61.551  -9.945  45.714 1.00 57.06  ? 20  PRO A CD  1 
ATOM   50   N  N   . PRO A  1  8   ? 58.106  -9.176  42.579 1.00 37.94  ? 21  PRO A N   1 
ATOM   51   C  CA  . PRO A  1  8   ? 56.693  -9.516  42.401 1.00 40.67  ? 21  PRO A CA  1 
ATOM   52   C  C   . PRO A  1  8   ? 56.426  -11.015 42.461 1.00 40.04  ? 21  PRO A C   1 
ATOM   53   O  O   . PRO A  1  8   ? 57.266  -11.816 42.067 1.00 39.87  ? 21  PRO A O   1 
ATOM   54   C  CB  . PRO A  1  8   ? 56.360  -8.946  41.020 1.00 36.75  ? 21  PRO A CB  1 
ATOM   55   C  CG  . PRO A  1  8   ? 57.714  -8.857  40.328 1.00 38.19  ? 21  PRO A CG  1 
ATOM   56   C  CD  . PRO A  1  8   ? 58.700  -8.495  41.413 1.00 37.19  ? 21  PRO A CD  1 
ATOM   57   N  N   . PRO A  1  9   ? 55.228  -11.426 42.919 1.00 38.65  ? 22  PRO A N   1 
ATOM   58   C  CA  . PRO A  1  9   ? 54.781  -12.807 42.780 1.00 38.96  ? 22  PRO A CA  1 
ATOM   59   C  C   . PRO A  1  9   ? 54.795  -13.209 41.311 1.00 37.57  ? 22  PRO A C   1 
ATOM   60   O  O   . PRO A  1  9   ? 54.642  -12.369 40.429 1.00 38.31  ? 22  PRO A O   1 
ATOM   61   C  CB  . PRO A  1  9   ? 53.350  -12.816 43.352 1.00 40.73  ? 22  PRO A CB  1 
ATOM   62   C  CG  . PRO A  1  9   ? 53.258  -11.553 44.183 1.00 41.51  ? 22  PRO A CG  1 
ATOM   63   C  CD  . PRO A  1  9   ? 54.204  -10.567 43.534 1.00 41.87  ? 22  PRO A CD  1 
ATOM   64   N  N   . GLY A  1  10  ? 54.992  -14.507 41.083 1.00 35.70  ? 23  GLY A N   1 
ATOM   65   C  CA  . GLY A  1  10  ? 54.816  -15.114 39.781 1.00 34.72  ? 23  GLY A CA  1 
ATOM   66   C  C   . GLY A  1  10  ? 53.351  -15.477 39.570 1.00 37.40  ? 23  GLY A C   1 
ATOM   67   O  O   . GLY A  1  10  ? 52.497  -15.117 40.385 1.00 34.40  ? 23  GLY A O   1 
ATOM   68   N  N   . PRO A  1  11  ? 53.040  -16.209 38.476 1.00 40.54  ? 24  PRO A N   1 
ATOM   69   C  CA  . PRO A  1  11  ? 51.679  -16.670 38.215 1.00 40.64  ? 24  PRO A CA  1 
ATOM   70   C  C   . PRO A  1  11  ? 51.168  -17.541 39.360 1.00 39.23  ? 24  PRO A C   1 
ATOM   71   O  O   . PRO A  1  11  ? 51.951  -18.142 40.083 1.00 38.61  ? 24  PRO A O   1 
ATOM   72   C  CB  . PRO A  1  11  ? 51.780  -17.473 36.900 1.00 44.44  ? 24  PRO A CB  1 
ATOM   73   C  CG  . PRO A  1  11  ? 53.142  -17.105 36.309 1.00 41.69  ? 24  PRO A CG  1 
ATOM   74   C  CD  . PRO A  1  11  ? 54.010  -16.649 37.458 1.00 41.04  ? 24  PRO A CD  1 
ATOM   75   N  N   . PRO A  1  12  ? 49.838  -17.664 39.552 1.00 38.38  ? 25  PRO A N   1 
ATOM   76   C  CA  . PRO A  1  12  ? 49.310  -18.586 40.555 1.00 41.50  ? 25  PRO A CA  1 
ATOM   77   C  C   . PRO A  1  12  ? 49.576  -20.036 40.141 1.00 43.68  ? 25  PRO A C   1 
ATOM   78   O  O   . PRO A  1  12  ? 49.624  -20.347 38.955 1.00 41.65  ? 25  PRO A O   1 
ATOM   79   C  CB  . PRO A  1  12  ? 47.812  -18.226 40.593 1.00 41.90  ? 25  PRO A CB  1 
ATOM   80   C  CG  . PRO A  1  12  ? 47.521  -17.694 39.203 1.00 41.62  ? 25  PRO A CG  1 
ATOM   81   C  CD  . PRO A  1  12  ? 48.788  -16.979 38.788 1.00 40.16  ? 25  PRO A CD  1 
ATOM   82   N  N   . SER A  1  13  ? 49.745  -20.904 41.146 1.00 45.00  ? 26  SER A N   1 
ATOM   83   C  CA  A SER A  1  13  ? 49.926  -22.336 40.952 0.50 45.16  ? 26  SER A CA  1 
ATOM   84   C  CA  B SER A  1  13  ? 49.931  -22.333 40.945 0.50 45.32  ? 26  SER A CA  1 
ATOM   85   C  C   . SER A  1  13  ? 48.765  -22.923 40.156 1.00 42.11  ? 26  SER A C   1 
ATOM   86   O  O   . SER A  1  13  ? 48.977  -23.733 39.268 1.00 44.80  ? 26  SER A O   1 
ATOM   87   C  CB  A SER A  1  13  ? 50.059  -23.047 42.279 0.50 45.34  ? 26  SER A CB  1 
ATOM   88   C  CB  B SER A  1  13  ? 50.094  -23.041 42.270 0.50 45.76  ? 26  SER A CB  1 
ATOM   89   O  OG  A SER A  1  13  ? 51.126  -22.507 43.041 0.50 47.79  ? 26  SER A OG  1 
ATOM   90   O  OG  B SER A  1  13  ? 50.104  -24.451 42.091 0.50 48.71  ? 26  SER A OG  1 
ATOM   91   N  N   . PHE A  1  14  ? 47.537  -22.528 40.515 1.00 40.16  ? 27  PHE A N   1 
ATOM   92   C  CA  . PHE A  1  14  ? 46.326  -22.970 39.832 1.00 38.61  ? 27  PHE A CA  1 
ATOM   93   C  C   . PHE A  1  14  ? 45.805  -21.819 38.971 1.00 38.11  ? 27  PHE A C   1 
ATOM   94   O  O   . PHE A  1  14  ? 45.592  -20.723 39.488 1.00 37.64  ? 27  PHE A O   1 
ATOM   95   C  CB  . PHE A  1  14  ? 45.284  -23.430 40.861 1.00 36.14  ? 27  PHE A CB  1 
ATOM   96   C  CG  . PHE A  1  14  ? 43.958  -23.862 40.249 1.00 38.35  ? 27  PHE A CG  1 
ATOM   97   C  CD1 . PHE A  1  14  ? 43.854  -25.068 39.553 1.00 37.76  ? 27  PHE A CD1 1 
ATOM   98   C  CD2 . PHE A  1  14  ? 42.822  -23.072 40.371 1.00 36.96  ? 27  PHE A CD2 1 
ATOM   99   C  CE1 . PHE A  1  14  ? 42.658  -25.446 38.966 1.00 38.61  ? 27  PHE A CE1 1 
ATOM   100  C  CE2 . PHE A  1  14  ? 41.618  -23.472 39.795 1.00 40.24  ? 27  PHE A CE2 1 
ATOM   101  C  CZ  . PHE A  1  14  ? 41.542  -24.656 39.096 1.00 37.54  ? 27  PHE A CZ  1 
ATOM   102  N  N   . THR A  1  15  ? 45.592  -22.080 37.670 1.00 37.42  ? 28  THR A N   1 
ATOM   103  C  CA  . THR A  1  15  ? 45.232  -21.048 36.708 1.00 39.04  ? 28  THR A CA  1 
ATOM   104  C  C   . THR A  1  15  ? 43.875  -21.339 36.071 1.00 37.69  ? 28  THR A C   1 
ATOM   105  O  O   . THR A  1  15  ? 43.526  -20.669 35.097 1.00 41.57  ? 28  THR A O   1 
ATOM   106  C  CB  . THR A  1  15  ? 46.285  -20.938 35.608 1.00 43.24  ? 28  THR A CB  1 
ATOM   107  O  OG1 . THR A  1  15  ? 46.191  -22.158 34.873 1.00 44.09  ? 28  THR A OG1 1 
ATOM   108  C  CG2 . THR A  1  15  ? 47.690  -20.742 36.151 1.00 45.85  ? 28  THR A CG2 1 
ATOM   109  N  N   . GLY A  1  16  ? 43.128  -22.322 36.602 1.00 36.31  ? 29  GLY A N   1 
ATOM   110  C  CA  . GLY A  1  16  ? 41.811  -22.647 36.068 1.00 34.37  ? 29  GLY A CA  1 
ATOM   111  C  C   . GLY A  1  16  ? 40.745  -21.747 36.680 1.00 35.89  ? 29  GLY A C   1 
ATOM   112  O  O   . GLY A  1  16  ? 41.063  -20.872 37.486 1.00 33.26  ? 29  GLY A O   1 
ATOM   113  N  N   . THR A  1  17  ? 39.476  -21.979 36.310 1.00 36.17  ? 30  THR A N   1 
ATOM   114  C  CA  . THR A  1  17  ? 38.377  -21.221 36.875 1.00 35.83  ? 30  THR A CA  1 
ATOM   115  C  C   . THR A  1  17  ? 38.149  -21.685 38.309 1.00 39.99  ? 30  THR A C   1 
ATOM   116  O  O   . THR A  1  17  ? 38.480  -22.812 38.672 1.00 39.17  ? 30  THR A O   1 
ATOM   117  C  CB  . THR A  1  17  ? 37.098  -21.374 36.050 1.00 40.12  ? 30  THR A CB  1 
ATOM   118  O  OG1 . THR A  1  17  ? 36.230  -20.384 36.602 1.00 41.78  ? 30  THR A OG1 1 
ATOM   119  C  CG2 . THR A  1  17  ? 36.474  -22.754 36.168 1.00 36.48  ? 30  THR A CG2 1 
ATOM   120  N  N   . LYS A  1  18  ? 37.566  -20.789 39.107 1.00 40.67  ? 31  LYS A N   1 
ATOM   121  C  CA  . LYS A  1  18  ? 37.104  -21.124 40.440 1.00 42.62  ? 31  LYS A CA  1 
ATOM   122  C  C   . LYS A  1  18  ? 36.105  -20.061 40.888 1.00 40.73  ? 31  LYS A C   1 
ATOM   123  O  O   . LYS A  1  18  ? 36.040  -18.970 40.318 1.00 39.52  ? 31  LYS A O   1 
ATOM   124  C  CB  . LYS A  1  18  ? 38.268  -21.253 41.426 1.00 42.71  ? 31  LYS A CB  1 
ATOM   125  C  CG  . LYS A  1  18  ? 39.005  -19.965 41.743 1.00 50.63  ? 31  LYS A CG  1 
ATOM   126  C  CD  . LYS A  1  18  ? 40.259  -20.169 42.590 1.00 56.46  ? 31  LYS A CD  1 
ATOM   127  C  CE  . LYS A  1  18  ? 40.462  -19.041 43.553 1.00 62.78  ? 31  LYS A CE  1 
ATOM   128  N  NZ  . LYS A  1  18  ? 41.831  -18.974 44.071 1.00 67.80  ? 31  LYS A NZ  1 
ATOM   129  N  N   . LEU A  1  19  ? 35.322  -20.409 41.909 1.00 39.77  ? 32  LEU A N   1 
ATOM   130  C  CA  . LEU A  1  19  ? 34.446  -19.458 42.568 1.00 39.75  ? 32  LEU A CA  1 
ATOM   131  C  C   . LEU A  1  19  ? 35.305  -18.446 43.317 1.00 38.91  ? 32  LEU A C   1 
ATOM   132  O  O   . LEU A  1  19  ? 36.092  -18.841 44.174 1.00 38.58  ? 32  LEU A O   1 
ATOM   133  C  CB  . LEU A  1  19  ? 33.524  -20.211 43.523 1.00 42.83  ? 32  LEU A CB  1 
ATOM   134  C  CG  . LEU A  1  19  ? 32.610  -19.335 44.385 1.00 43.27  ? 32  LEU A CG  1 
ATOM   135  C  CD1 . LEU A  1  19  ? 31.628  -18.573 43.527 1.00 41.15  ? 32  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A  1  19  ? 31.859  -20.157 45.435 1.00 43.08  ? 32  LEU A CD2 1 
ATOM   137  N  N   . VAL A  1  20  ? 35.156  -17.154 42.993 1.00 38.93  ? 33  VAL A N   1 
ATOM   138  C  CA  . VAL A  1  20  ? 35.935  -16.134 43.683 1.00 37.39  ? 33  VAL A CA  1 
ATOM   139  C  C   . VAL A  1  20  ? 35.033  -15.336 44.617 1.00 33.78  ? 33  VAL A C   1 
ATOM   140  O  O   . VAL A  1  20  ? 35.521  -14.806 45.609 1.00 32.44  ? 33  VAL A O   1 
ATOM   141  C  CB  . VAL A  1  20  ? 36.744  -15.220 42.741 1.00 38.96  ? 33  VAL A CB  1 
ATOM   142  C  CG1 . VAL A  1  20  ? 37.744  -16.015 41.922 1.00 39.67  ? 33  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A  1  20  ? 35.868  -14.382 41.842 1.00 40.41  ? 33  VAL A CG2 1 
ATOM   144  N  N   . ASN A  1  21  ? 33.731  -15.261 44.309 1.00 32.67  ? 34  ASN A N   1 
ATOM   145  C  CA  . ASN A  1  21  ? 32.758  -14.680 45.218 1.00 35.06  ? 34  ASN A CA  1 
ATOM   146  C  C   . ASN A  1  21  ? 32.279  -15.761 46.183 1.00 38.19  ? 34  ASN A C   1 
ATOM   147  O  O   . ASN A  1  21  ? 31.171  -16.278 46.051 1.00 35.16  ? 34  ASN A O   1 
ATOM   148  C  CB  . ASN A  1  21  ? 31.592  -14.061 44.459 1.00 36.33  ? 34  ASN A CB  1 
ATOM   149  C  CG  . ASN A  1  21  ? 30.640  -13.283 45.342 1.00 37.44  ? 34  ASN A CG  1 
ATOM   150  O  OD1 . ASN A  1  21  ? 30.868  -13.124 46.545 1.00 39.58  ? 34  ASN A OD1 1 
ATOM   151  N  ND2 . ASN A  1  21  ? 29.566  -12.775 44.755 1.00 37.69  ? 34  ASN A ND2 1 
ATOM   152  N  N   . ASP A  1  22  ? 33.130  -16.085 47.158 1.00 37.28  ? 35  ASP A N   1 
ATOM   153  C  CA  . ASP A  1  22  ? 32.919  -17.210 48.055 1.00 38.91  ? 35  ASP A CA  1 
ATOM   154  C  C   . ASP A  1  22  ? 32.754  -16.683 49.477 1.00 39.53  ? 35  ASP A C   1 
ATOM   155  O  O   . ASP A  1  22  ? 32.768  -15.467 49.713 1.00 38.65  ? 35  ASP A O   1 
ATOM   156  C  CB  . ASP A  1  22  ? 34.066  -18.202 47.928 1.00 40.29  ? 35  ASP A CB  1 
ATOM   157  C  CG  . ASP A  1  22  ? 35.455  -17.660 48.229 1.00 40.66  ? 35  ASP A CG  1 
ATOM   158  O  OD1 . ASP A  1  22  ? 35.561  -16.476 48.612 1.00 43.70  ? 35  ASP A OD1 1 
ATOM   159  O  OD2 . ASP A  1  22  ? 36.424  -18.414 48.058 1.00 44.06  ? 35  ASP A OD2 1 
ATOM   160  N  N   . ALA A  1  23  ? 32.621  -17.616 50.418 1.00 40.32  ? 36  ALA A N   1 
ATOM   161  C  CA  . ALA A  1  23  ? 32.222  -17.284 51.775 1.00 42.08  ? 36  ALA A CA  1 
ATOM   162  C  C   . ALA A  1  23  ? 33.318  -16.485 52.469 1.00 39.72  ? 36  ALA A C   1 
ATOM   163  O  O   . ALA A  1  23  ? 33.031  -15.633 53.296 1.00 39.56  ? 36  ALA A O   1 
ATOM   164  C  CB  . ALA A  1  23  ? 31.886  -18.556 52.521 1.00 43.58  ? 36  ALA A CB  1 
ATOM   165  N  N   . ASP A  1  24  ? 34.576  -16.759 52.111 1.00 41.71  ? 37  ASP A N   1 
ATOM   166  C  CA  . ASP A  1  24  ? 35.717  -16.111 52.731 1.00 40.50  ? 37  ASP A CA  1 
ATOM   167  C  C   . ASP A  1  24  ? 35.928  -14.694 52.192 1.00 39.67  ? 37  ASP A C   1 
ATOM   168  O  O   . ASP A  1  24  ? 36.693  -13.945 52.784 1.00 38.26  ? 37  ASP A O   1 
ATOM   169  C  CB  . ASP A  1  24  ? 36.981  -16.927 52.518 1.00 43.93  ? 37  ASP A CB  1 
ATOM   170  C  CG  . ASP A  1  24  ? 38.134  -16.614 53.465 1.00 44.19  ? 37  ASP A CG  1 
ATOM   171  O  OD1 . ASP A  1  24  ? 37.893  -16.600 54.687 1.00 47.65  ? 37  ASP A OD1 1 
ATOM   172  O  OD2 . ASP A  1  24  ? 39.264  -16.401 52.969 1.00 49.38  ? 37  ASP A OD2 1 
ATOM   173  N  N   . HIS A  1  25  ? 35.279  -14.336 51.075 1.00 36.49  ? 38  HIS A N   1 
ATOM   174  C  CA  . HIS A  1  25  ? 35.479  -13.043 50.432 1.00 36.98  ? 38  HIS A CA  1 
ATOM   175  C  C   . HIS A  1  25  ? 34.127  -12.356 50.246 1.00 37.69  ? 38  HIS A C   1 
ATOM   176  O  O   . HIS A  1  25  ? 33.697  -12.108 49.125 1.00 35.67  ? 38  HIS A O   1 
ATOM   177  C  CB  . HIS A  1  25  ? 36.278  -13.209 49.126 1.00 34.62  ? 38  HIS A CB  1 
ATOM   178  C  CG  . HIS A  1  25  ? 37.662  -13.734 49.349 1.00 34.05  ? 38  HIS A CG  1 
ATOM   179  N  ND1 . HIS A  1  25  ? 37.991  -15.068 49.240 1.00 37.41  ? 38  HIS A ND1 1 
ATOM   180  C  CD2 . HIS A  1  25  ? 38.795  -13.110 49.696 1.00 34.74  ? 38  HIS A CD2 1 
ATOM   181  C  CE1 . HIS A  1  25  ? 39.287  -15.227 49.500 1.00 38.00  ? 38  HIS A CE1 1 
ATOM   182  N  NE2 . HIS A  1  25  ? 39.796  -14.050 49.784 1.00 34.98  ? 38  HIS A NE2 1 
ATOM   183  N  N   . PRO A  1  26  ? 33.403  -12.033 51.340 1.00 36.72  ? 39  PRO A N   1 
ATOM   184  C  CA  . PRO A  1  26  ? 32.102  -11.373 51.237 1.00 37.22  ? 39  PRO A CA  1 
ATOM   185  C  C   . PRO A  1  26  ? 32.241  -9.894  50.889 1.00 38.07  ? 39  PRO A C   1 
ATOM   186  O  O   . PRO A  1  26  ? 33.152  -9.216  51.375 1.00 34.27  ? 39  PRO A O   1 
ATOM   187  C  CB  . PRO A  1  26  ? 31.524  -11.563 52.643 1.00 34.84  ? 39  PRO A CB  1 
ATOM   188  C  CG  . PRO A  1  26  ? 32.752  -11.499 53.525 1.00 34.83  ? 39  PRO A CG  1 
ATOM   189  C  CD  . PRO A  1  26  ? 33.796  -12.268 52.740 1.00 36.24  ? 39  PRO A CD  1 
ATOM   190  N  N   . TRP A  1  27  ? 31.314  -9.405  50.066 1.00 33.82  ? 40  TRP A N   1 
ATOM   191  C  CA  . TRP A  1  27  ? 31.166  -7.978  49.877 1.00 33.17  ? 40  TRP A CA  1 
ATOM   192  C  C   . TRP A  1  27  ? 30.808  -7.350  51.216 1.00 32.49  ? 40  TRP A C   1 
ATOM   193  O  O   . TRP A  1  27  ? 30.056  -7.938  51.987 1.00 35.60  ? 40  TRP A O   1 
ATOM   194  C  CB  . TRP A  1  27  ? 30.093  -7.670  48.825 1.00 33.01  ? 40  TRP A CB  1 
ATOM   195  C  CG  . TRP A  1  27  ? 29.937  -6.202  48.530 1.00 33.52  ? 40  TRP A CG  1 
ATOM   196  C  CD1 . TRP A  1  27  ? 30.583  -5.499  47.558 1.00 35.66  ? 40  TRP A CD1 1 
ATOM   197  C  CD2 . TRP A  1  27  ? 29.104  -5.251  49.231 1.00 37.07  ? 40  TRP A CD2 1 
ATOM   198  N  NE1 . TRP A  1  27  ? 30.193  -4.187  47.582 1.00 35.37  ? 40  TRP A NE1 1 
ATOM   199  C  CE2 . TRP A  1  27  ? 29.300  -3.999  48.608 1.00 37.17  ? 40  TRP A CE2 1 
ATOM   200  C  CE3 . TRP A  1  27  ? 28.221  -5.334  50.318 1.00 38.70  ? 40  TRP A CE3 1 
ATOM   201  C  CZ2 . TRP A  1  27  ? 28.637  -2.849  49.036 1.00 37.74  ? 40  TRP A CZ2 1 
ATOM   202  C  CZ3 . TRP A  1  27  ? 27.567  -4.196  50.740 1.00 37.78  ? 40  TRP A CZ3 1 
ATOM   203  C  CH2 . TRP A  1  27  ? 27.774  -2.972  50.104 1.00 40.46  ? 40  TRP A CH2 1 
ATOM   204  N  N   . GLN A  1  28  ? 31.380  -6.173  51.484 1.00 33.74  ? 41  GLN A N   1 
ATOM   205  C  CA  . GLN A  1  28  ? 31.075  -5.407  52.680 1.00 34.80  ? 41  GLN A CA  1 
ATOM   206  C  C   . GLN A  1  28  ? 31.085  -3.924  52.331 1.00 37.36  ? 41  GLN A C   1 
ATOM   207  O  O   . GLN A  1  28  ? 31.876  -3.477  51.499 1.00 36.65  ? 41  GLN A O   1 
ATOM   208  C  CB  . GLN A  1  28  ? 32.066  -5.672  53.814 1.00 37.91  ? 41  GLN A CB  1 
ATOM   209  C  CG  . GLN A  1  28  ? 31.967  -7.085  54.373 1.00 38.56  ? 41  GLN A CG  1 
ATOM   210  C  CD  . GLN A  1  28  ? 33.003  -7.398  55.425 1.00 37.18  ? 41  GLN A CD  1 
ATOM   211  O  OE1 . GLN A  1  28  ? 33.818  -6.552  55.821 1.00 39.73  ? 41  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A  1  28  ? 32.959  -8.638  55.886 1.00 35.25  ? 41  GLN A NE2 1 
ATOM   213  N  N   . PRO A  1  29  ? 30.211  -3.120  52.974 1.00 36.77  ? 42  PRO A N   1 
ATOM   214  C  CA  . PRO A  1  29  ? 30.164  -1.687  52.708 1.00 37.66  ? 42  PRO A CA  1 
ATOM   215  C  C   . PRO A  1  29  ? 31.440  -0.985  53.174 1.00 36.80  ? 42  PRO A C   1 
ATOM   216  O  O   . PRO A  1  29  ? 32.206  -1.514  53.982 1.00 35.68  ? 42  PRO A O   1 
ATOM   217  C  CB  . PRO A  1  29  ? 28.908  -1.204  53.452 1.00 36.97  ? 42  PRO A CB  1 
ATOM   218  C  CG  . PRO A  1  29  ? 28.666  -2.249  54.534 1.00 37.27  ? 42  PRO A CG  1 
ATOM   219  C  CD  . PRO A  1  29  ? 29.266  -3.542  54.022 1.00 38.49  ? 42  PRO A CD  1 
ATOM   220  N  N   . LEU A  1  30  ? 31.649  0.217   52.628 1.00 36.58  ? 43  LEU A N   1 
ATOM   221  C  CA  . LEU A  1  30  ? 32.771  1.058   52.984 1.00 38.23  ? 43  LEU A CA  1 
ATOM   222  C  C   . LEU A  1  30  ? 32.642  1.490   54.440 1.00 41.16  ? 43  LEU A C   1 
ATOM   223  O  O   . LEU A  1  30  ? 31.544  1.773   54.915 1.00 38.40  ? 43  LEU A O   1 
ATOM   224  C  CB  . LEU A  1  30  ? 32.798  2.274   52.060 1.00 42.30  ? 43  LEU A CB  1 
ATOM   225  C  CG  . LEU A  1  30  ? 33.014  2.004   50.568 1.00 42.68  ? 43  LEU A CG  1 
ATOM   226  C  CD1 . LEU A  1  30  ? 33.249  3.343   49.879 1.00 43.56  ? 43  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A  1  30  ? 34.177  1.060   50.279 1.00 41.63  ? 43  LEU A CD2 1 
ATOM   228  N  N   . ARG A  1  31  ? 33.778  1.494   55.139 1.00 39.29  ? 44  ARG A N   1 
ATOM   229  C  CA  . ARG A  1  31  ? 33.901  2.146   56.430 1.00 44.01  ? 44  ARG A CA  1 
ATOM   230  C  C   . ARG A  1  31  ? 34.630  3.477   56.253 1.00 43.42  ? 44  ARG A C   1 
ATOM   231  O  O   . ARG A  1  31  ? 35.230  3.738   55.219 1.00 44.19  ? 44  ARG A O   1 
ATOM   232  C  CB  . ARG A  1  31  ? 34.720  1.286   57.395 1.00 46.34  ? 44  ARG A CB  1 
ATOM   233  C  CG  . ARG A  1  31  ? 34.245  -0.139  57.638 1.00 50.42  ? 44  ARG A CG  1 
ATOM   234  C  CD  . ARG A  1  31  ? 35.398  -0.997  58.147 1.00 57.07  ? 44  ARG A CD  1 
ATOM   235  N  NE  . ARG A  1  31  ? 36.559  -0.898  57.246 1.00 61.22  ? 44  ARG A NE  1 
ATOM   236  C  CZ  . ARG A  1  31  ? 37.716  -1.546  57.321 1.00 60.66  ? 44  ARG A CZ  1 
ATOM   237  N  NH1 . ARG A  1  31  ? 37.876  -2.565  58.149 1.00 70.53  ? 44  ARG A NH1 1 
ATOM   238  N  NH2 . ARG A  1  31  ? 38.698  -1.204  56.513 1.00 51.67  ? 44  ARG A NH2 1 
ATOM   239  N  N   . GLU A  1  32  ? 34.605  4.301   57.300 1.00 46.62  ? 45  GLU A N   1 
ATOM   240  C  CA  . GLU A  1  32  ? 35.353  5.542   57.333 1.00 49.57  ? 45  GLU A CA  1 
ATOM   241  C  C   . GLU A  1  32  ? 36.837  5.251   57.111 1.00 45.74  ? 45  GLU A C   1 
ATOM   242  O  O   . GLU A  1  32  ? 37.422  4.376   57.740 1.00 41.64  ? 45  GLU A O   1 
ATOM   243  C  CB  . GLU A  1  32  ? 35.106  6.217   58.679 1.00 58.08  ? 45  GLU A CB  1 
ATOM   244  C  CG  . GLU A  1  32  ? 35.688  7.621   58.787 1.00 66.85  ? 45  GLU A CG  1 
ATOM   245  C  CD  . GLU A  1  32  ? 35.345  8.275   60.115 1.00 79.65  ? 45  GLU A CD  1 
ATOM   246  O  OE1 . GLU A  1  32  ? 34.153  8.637   60.263 1.00 82.32  ? 45  GLU A OE1 1 
ATOM   247  O  OE2 . GLU A  1  32  ? 36.232  8.383   61.002 1.00 80.50  ? 45  GLU A OE2 1 
ATOM   248  N  N   . GLY A  1  33  ? 37.435  6.008   56.193 1.00 41.76  ? 46  GLY A N   1 
ATOM   249  C  CA  . GLY A  1  33  ? 38.843  5.872   55.869 1.00 42.67  ? 46  GLY A CA  1 
ATOM   250  C  C   . GLY A  1  33  ? 39.097  4.953   54.670 1.00 41.21  ? 46  GLY A C   1 
ATOM   251  O  O   . GLY A  1  33  ? 40.199  4.971   54.122 1.00 43.91  ? 46  GLY A O   1 
ATOM   252  N  N   . ASP A  1  34  ? 38.119  4.118   54.293 1.00 39.40  ? 47  ASP A N   1 
ATOM   253  C  CA  . ASP A  1  34  ? 38.293  3.208   53.165 1.00 40.57  ? 47  ASP A CA  1 
ATOM   254  C  C   . ASP A  1  34  ? 38.391  4.006   51.870 1.00 38.73  ? 47  ASP A C   1 
ATOM   255  O  O   . ASP A  1  34  ? 37.617  4.927   51.652 1.00 43.71  ? 47  ASP A O   1 
ATOM   256  C  CB  . ASP A  1  34  ? 37.197  2.157   53.088 1.00 42.73  ? 47  ASP A CB  1 
ATOM   257  C  CG  . ASP A  1  34  ? 37.227  1.097   54.182 1.00 42.85  ? 47  ASP A CG  1 
ATOM   258  O  OD1 . ASP A  1  34  ? 38.235  1.044   54.925 1.00 41.53  ? 47  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A  1  34  ? 36.232  0.337   54.295 1.00 41.74  ? 47  ASP A OD2 1 
ATOM   260  N  N   . ILE A  1  35  ? 39.356  3.629   51.025 1.00 37.26  ? 48  ILE A N   1 
ATOM   261  C  CA  . ILE A  1  35  ? 39.658  4.327   49.787 1.00 33.57  ? 48  ILE A CA  1 
ATOM   262  C  C   . ILE A  1  35  ? 39.218  3.472   48.602 1.00 32.98  ? 48  ILE A C   1 
ATOM   263  O  O   . ILE A  1  35  ? 39.487  2.274   48.561 1.00 31.10  ? 48  ILE A O   1 
ATOM   264  C  CB  . ILE A  1  35  ? 41.171  4.628   49.717 1.00 34.58  ? 48  ILE A CB  1 
ATOM   265  C  CG1 . ILE A  1  35  ? 41.643  5.512   50.872 1.00 38.29  ? 48  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A  1  35  ? 41.539  5.245   48.374 1.00 35.22  ? 48  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A  1  35  ? 41.019  6.903   50.903 1.00 37.39  ? 48  ILE A CD1 1 
ATOM   268  N  N   . ARG A  1  36  ? 38.565  4.118   47.628 1.00 33.64  ? 49  ARG A N   1 
ATOM   269  C  CA  . ARG A  1  36  ? 38.225  3.515   46.352 1.00 35.91  ? 49  ARG A CA  1 
ATOM   270  C  C   . ARG A  1  36  ? 38.546  4.543   45.278 1.00 35.97  ? 49  ARG A C   1 
ATOM   271  O  O   . ARG A  1  36  ? 38.657  5.728   45.587 1.00 33.78  ? 49  ARG A O   1 
ATOM   272  C  CB  . ARG A  1  36  ? 36.748  3.110   46.333 1.00 36.01  ? 49  ARG A CB  1 
ATOM   273  C  CG  . ARG A  1  36  ? 36.392  2.041   47.361 1.00 33.70  ? 49  ARG A CG  1 
ATOM   274  C  CD  . ARG A  1  36  ? 36.976  0.678   47.019 1.00 32.75  ? 49  ARG A CD  1 
ATOM   275  N  NE  . ARG A  1  36  ? 36.565  -0.350  47.988 1.00 31.64  ? 49  ARG A NE  1 
ATOM   276  C  CZ  . ARG A  1  36  ? 37.062  -0.550  49.196 1.00 31.78  ? 49  ARG A CZ  1 
ATOM   277  N  NH1 . ARG A  1  36  ? 38.085  0.176   49.642 1.00 38.11  ? 49  ARG A NH1 1 
ATOM   278  N  NH2 . ARG A  1  36  ? 36.563  -1.516  49.954 1.00 32.14  ? 49  ARG A NH2 1 
ATOM   279  N  N   . GLY A  1  37  ? 38.716  4.088   44.033 1.00 35.59  ? 50  GLY A N   1 
ATOM   280  C  CA  . GLY A  1  37  ? 39.216  4.961   42.987 1.00 35.48  ? 50  GLY A CA  1 
ATOM   281  C  C   . GLY A  1  37  ? 38.655  4.617   41.613 1.00 34.36  ? 50  GLY A C   1 
ATOM   282  O  O   . GLY A  1  37  ? 37.534  4.129   41.500 1.00 33.20  ? 50  GLY A O   1 
ATOM   283  N  N   . PRO A  1  38  ? 39.425  4.873   40.534 1.00 30.81  ? 51  PRO A N   1 
ATOM   284  C  CA  . PRO A  1  38  ? 38.901  4.760   39.174 1.00 32.09  ? 51  PRO A CA  1 
ATOM   285  C  C   . PRO A  1  38  ? 38.909  3.359   38.575 1.00 31.87  ? 51  PRO A C   1 
ATOM   286  O  O   . PRO A  1  38  ? 38.435  3.185   37.454 1.00 31.19  ? 51  PRO A O   1 
ATOM   287  C  CB  . PRO A  1  38  ? 39.872  5.687   38.431 1.00 30.31  ? 51  PRO A CB  1 
ATOM   288  C  CG  . PRO A  1  38  ? 41.198  5.394   39.095 1.00 31.28  ? 51  PRO A CG  1 
ATOM   289  C  CD  . PRO A  1  38  ? 40.846  5.262   40.569 1.00 32.15  ? 51  PRO A CD  1 
ATOM   290  N  N   . CYS A  1  39  ? 39.473  2.384   39.303 1.00 32.69  ? 52  CYS A N   1 
ATOM   291  C  CA  . CYS A  1  39  ? 39.586  1.022   38.797 1.00 33.03  ? 52  CYS A CA  1 
ATOM   292  C  C   . CYS A  1  39  ? 38.516  0.119   39.404 1.00 32.36  ? 52  CYS A C   1 
ATOM   293  O  O   . CYS A  1  39  ? 38.554  -0.205  40.597 1.00 29.58  ? 52  CYS A O   1 
ATOM   294  C  CB  . CYS A  1  39  ? 40.927  0.372   39.100 1.00 33.00  ? 52  CYS A CB  1 
ATOM   295  S  SG  . CYS A  1  39  ? 41.045  -1.308  38.422 1.00 36.26  ? 52  CYS A SG  1 
ATOM   296  N  N   . PRO A  1  40  ? 37.559  -0.364  38.583 1.00 34.45  ? 53  PRO A N   1 
ATOM   297  C  CA  . PRO A  1  40  ? 36.501  -1.241  39.083 1.00 35.72  ? 53  PRO A CA  1 
ATOM   298  C  C   . PRO A  1  40  ? 37.042  -2.601  39.508 1.00 32.09  ? 53  PRO A C   1 
ATOM   299  O  O   . PRO A  1  40  ? 36.479  -3.232  40.389 1.00 31.48  ? 53  PRO A O   1 
ATOM   300  C  CB  . PRO A  1  40  ? 35.503  -1.324  37.918 1.00 36.53  ? 53  PRO A CB  1 
ATOM   301  C  CG  . PRO A  1  40  ? 36.344  -1.028  36.694 1.00 36.40  ? 53  PRO A CG  1 
ATOM   302  C  CD  . PRO A  1  40  ? 37.424  -0.069  37.151 1.00 36.64  ? 53  PRO A CD  1 
ATOM   303  N  N   . GLY A  1  41  ? 38.170  -3.019  38.916 1.00 35.57  ? 54  GLY A N   1 
ATOM   304  C  CA  . GLY A  1  41  ? 38.784  -4.286  39.285 1.00 32.81  ? 54  GLY A CA  1 
ATOM   305  C  C   . GLY A  1  41  ? 39.304  -4.245  40.719 1.00 33.13  ? 54  GLY A C   1 
ATOM   306  O  O   . GLY A  1  41  ? 38.931  -5.060  41.561 1.00 34.93  ? 54  GLY A O   1 
ATOM   307  N  N   . LEU A  1  42  ? 40.172  -3.273  40.985 1.00 34.52  ? 55  LEU A N   1 
ATOM   308  C  CA  . LEU A  1  42  ? 40.750  -3.098  42.309 1.00 33.96  ? 55  LEU A CA  1 
ATOM   309  C  C   . LEU A  1  42  ? 39.667  -2.756  43.329 1.00 32.40  ? 55  LEU A C   1 
ATOM   310  O  O   . LEU A  1  42  ? 39.689  -3.273  44.441 1.00 32.69  ? 55  LEU A O   1 
ATOM   311  C  CB  . LEU A  1  42  ? 41.831  -2.028  42.239 1.00 34.43  ? 55  LEU A CB  1 
ATOM   312  C  CG  . LEU A  1  42  ? 43.042  -2.363  41.363 1.00 33.86  ? 55  LEU A CG  1 
ATOM   313  C  CD1 . LEU A  1  42  ? 44.074  -1.254  41.425 1.00 33.58  ? 55  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A  1  42  ? 43.681  -3.690  41.760 1.00 35.11  ? 55  LEU A CD2 1 
ATOM   315  N  N   . ASN A  1  43  ? 38.712  -1.907  42.936 1.00 33.68  ? 56  ASN A N   1 
ATOM   316  C  CA  . ASN A  1  43  ? 37.614  -1.540  43.819 1.00 35.40  ? 56  ASN A CA  1 
ATOM   317  C  C   . ASN A  1  43  ? 36.880  -2.780  44.323 1.00 33.89  ? 56  ASN A C   1 
ATOM   318  O  O   . ASN A  1  43  ? 36.629  -2.900  45.528 1.00 32.79  ? 56  ASN A O   1 
ATOM   319  C  CB  . ASN A  1  43  ? 36.622  -0.590  43.164 1.00 33.60  ? 56  ASN A CB  1 
ATOM   320  C  CG  . ASN A  1  43  ? 37.155  0.818   42.988 1.00 35.10  ? 56  ASN A CG  1 
ATOM   321  O  OD1 . ASN A  1  43  ? 38.185  1.209   43.562 1.00 32.12  ? 56  ASN A OD1 1 
ATOM   322  N  ND2 . ASN A  1  43  ? 36.461  1.586   42.165 1.00 33.17  ? 56  ASN A ND2 1 
ATOM   323  N  N   . THR A  1  44  ? 36.555  -3.690  43.401 1.00 31.33  ? 57  THR A N   1 
ATOM   324  C  CA  . THR A  1  44  ? 35.792  -4.884  43.729 1.00 33.12  ? 57  THR A CA  1 
ATOM   325  C  C   . THR A  1  44  ? 36.631  -5.828  44.598 1.00 31.64  ? 57  THR A C   1 
ATOM   326  O  O   . THR A  1  44  ? 36.116  -6.439  45.531 1.00 31.29  ? 57  THR A O   1 
ATOM   327  C  CB  . THR A  1  44  ? 35.333  -5.558  42.439 1.00 32.66  ? 57  THR A CB  1 
ATOM   328  O  OG1 . THR A  1  44  ? 34.512  -4.626  41.729 1.00 34.79  ? 57  THR A OG1 1 
ATOM   329  C  CG2 . THR A  1  44  ? 34.535  -6.821  42.702 1.00 31.80  ? 57  THR A CG2 1 
ATOM   330  N  N   . LEU A  1  45  ? 37.926  -5.954  44.288 1.00 32.63  ? 58  LEU A N   1 
ATOM   331  C  CA  . LEU A  1  45  ? 38.820  -6.788  45.072 1.00 32.18  ? 58  LEU A CA  1 
ATOM   332  C  C   . LEU A  1  45  ? 38.883  -6.280  46.513 1.00 34.45  ? 58  LEU A C   1 
ATOM   333  O  O   . LEU A  1  45  ? 38.874  -7.076  47.455 1.00 33.73  ? 58  LEU A O   1 
ATOM   334  C  CB  . LEU A  1  45  ? 40.196  -6.833  44.411 1.00 32.55  ? 58  LEU A CB  1 
ATOM   335  C  CG  . LEU A  1  45  ? 40.271  -7.573  43.067 1.00 32.87  ? 58  LEU A CG  1 
ATOM   336  C  CD1 . LEU A  1  45  ? 41.593  -7.326  42.322 1.00 31.23  ? 58  LEU A CD1 1 
ATOM   337  C  CD2 . LEU A  1  45  ? 40.077  -9.051  43.272 1.00 33.12  ? 58  LEU A CD2 1 
ATOM   338  N  N   . ALA A  1  46  ? 38.951  -4.957  46.696 1.00 33.23  ? 59  ALA A N   1 
ATOM   339  C  CA  . ALA A  1  46  ? 38.998  -4.389  48.036 1.00 32.30  ? 59  ALA A CA  1 
ATOM   340  C  C   . ALA A  1  46  ? 37.672  -4.615  48.764 1.00 29.52  ? 59  ALA A C   1 
ATOM   341  O  O   . ALA A  1  46  ? 37.666  -4.997  49.931 1.00 33.44  ? 59  ALA A O   1 
ATOM   342  C  CB  . ALA A  1  46  ? 39.344  -2.914  47.974 1.00 29.93  ? 59  ALA A CB  1 
ATOM   343  N  N   . SER A  1  47  ? 36.549  -4.412  48.077 1.00 31.28  ? 60  SER A N   1 
ATOM   344  C  CA  . SER A  1  47  ? 35.249  -4.543  48.727 1.00 32.15  ? 60  SER A CA  1 
ATOM   345  C  C   . SER A  1  47  ? 34.880  -6.000  49.023 1.00 32.64  ? 60  SER A C   1 
ATOM   346  O  O   . SER A  1  47  ? 33.891  -6.236  49.714 1.00 34.03  ? 60  SER A O   1 
ATOM   347  C  CB  . SER A  1  47  ? 34.171  -3.832  47.937 1.00 31.49  ? 60  SER A CB  1 
ATOM   348  O  OG  . SER A  1  47  ? 34.265  -2.423  48.120 1.00 30.73  ? 60  SER A OG  1 
ATOM   349  N  N   . HIS A  1  48  ? 35.650  -6.970  48.496 1.00 34.08  ? 61  HIS A N   1 
ATOM   350  C  CA  . HIS A  1  48  ? 35.455  -8.383  48.797 1.00 31.53  ? 61  HIS A CA  1 
ATOM   351  C  C   . HIS A  1  48  ? 36.591  -8.945  49.653 1.00 33.70  ? 61  HIS A C   1 
ATOM   352  O  O   . HIS A  1  48  ? 36.586  -10.129 49.977 1.00 35.45  ? 61  HIS A O   1 
ATOM   353  C  CB  . HIS A  1  48  ? 35.326  -9.209  47.507 1.00 30.30  ? 61  HIS A CB  1 
ATOM   354  C  CG  . HIS A  1  48  ? 33.961  -9.187  46.916 1.00 29.47  ? 61  HIS A CG  1 
ATOM   355  N  ND1 . HIS A  1  48  ? 33.016  -10.138 47.216 1.00 30.81  ? 61  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A  1  48  ? 33.386  -8.356  46.052 1.00 30.28  ? 61  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A  1  48  ? 31.898  -9.877  46.556 1.00 32.85  ? 61  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A  1  48  ? 32.096  -8.799  45.846 1.00 33.07  ? 61  HIS A NE2 1 
ATOM   359  N  N   . GLY A  1  49  ? 37.588  -8.116  49.982 1.00 34.91  ? 62  GLY A N   1 
ATOM   360  C  CA  . GLY A  1  49  ? 38.648  -8.507  50.896 1.00 31.67  ? 62  GLY A CA  1 
ATOM   361  C  C   . GLY A  1  49  ? 39.776  -9.299  50.230 1.00 31.28  ? 62  GLY A C   1 
ATOM   362  O  O   . GLY A  1  49  ? 40.611  -9.855  50.926 1.00 34.65  ? 62  GLY A O   1 
ATOM   363  N  N   . TYR A  1  50  ? 39.836  -9.333  48.894 1.00 32.96  ? 63  TYR A N   1 
ATOM   364  C  CA  . TYR A  1  50  ? 41.012  -9.842  48.207 1.00 33.26  ? 63  TYR A CA  1 
ATOM   365  C  C   . TYR A  1  50  ? 42.203  -8.902  48.421 1.00 36.94  ? 63  TYR A C   1 
ATOM   366  O  O   . TYR A  1  50  ? 43.346  -9.353  48.508 1.00 37.07  ? 63  TYR A O   1 
ATOM   367  C  CB  . TYR A  1  50  ? 40.741  -10.082 46.721 1.00 33.76  ? 63  TYR A CB  1 
ATOM   368  C  CG  . TYR A  1  50  ? 40.010  -11.391 46.457 1.00 33.15  ? 63  TYR A CG  1 
ATOM   369  C  CD1 . TYR A  1  50  ? 40.699  -12.600 46.390 1.00 35.76  ? 63  TYR A CD1 1 
ATOM   370  C  CD2 . TYR A  1  50  ? 38.630  -11.416 46.293 1.00 34.16  ? 63  TYR A CD2 1 
ATOM   371  C  CE1 . TYR A  1  50  ? 40.040  -13.797 46.159 1.00 31.94  ? 63  TYR A CE1 1 
ATOM   372  C  CE2 . TYR A  1  50  ? 37.957  -12.602 46.058 1.00 31.26  ? 63  TYR A CE2 1 
ATOM   373  C  CZ  . TYR A  1  50  ? 38.662  -13.793 45.994 1.00 33.35  ? 63  TYR A CZ  1 
ATOM   374  O  OH  . TYR A  1  50  ? 37.995  -14.963 45.794 1.00 30.72  ? 63  TYR A OH  1 
ATOM   375  N  N   . LEU A  1  51  ? 41.919  -7.595  48.470 1.00 39.00  ? 64  LEU A N   1 
ATOM   376  C  CA  . LEU A  1  51  ? 42.862  -6.579  48.920 1.00 38.22  ? 64  LEU A CA  1 
ATOM   377  C  C   . LEU A  1  51  ? 42.453  -6.136  50.320 1.00 36.75  ? 64  LEU A C   1 
ATOM   378  O  O   . LEU A  1  51  ? 41.306  -6.330  50.702 1.00 35.88  ? 64  LEU A O   1 
ATOM   379  C  CB  . LEU A  1  51  ? 42.821  -5.373  47.979 1.00 35.53  ? 64  LEU A CB  1 
ATOM   380  C  CG  . LEU A  1  51  ? 43.430  -5.572  46.589 1.00 35.39  ? 64  LEU A CG  1 
ATOM   381  C  CD1 . LEU A  1  51  ? 43.123  -4.359  45.752 1.00 34.94  ? 64  LEU A CD1 1 
ATOM   382  C  CD2 . LEU A  1  51  ? 44.928  -5.801  46.663 1.00 37.63  ? 64  LEU A CD2 1 
ATOM   383  N  N   . PRO A  1  52  ? 43.343  -5.461  51.084 1.00 34.69  ? 65  PRO A N   1 
ATOM   384  C  CA  . PRO A  1  52  ? 42.918  -4.747  52.287 1.00 35.07  ? 65  PRO A CA  1 
ATOM   385  C  C   . PRO A  1  52  ? 41.688  -3.895  51.981 1.00 31.97  ? 65  PRO A C   1 
ATOM   386  O  O   . PRO A  1  52  ? 41.640  -3.196  50.963 1.00 33.96  ? 65  PRO A O   1 
ATOM   387  C  CB  . PRO A  1  52  ? 44.149  -3.905  52.636 1.00 37.41  ? 65  PRO A CB  1 
ATOM   388  C  CG  . PRO A  1  52  ? 45.314  -4.720  52.109 1.00 36.34  ? 65  PRO A CG  1 
ATOM   389  C  CD  . PRO A  1  52  ? 44.778  -5.304  50.808 1.00 36.51  ? 65  PRO A CD  1 
ATOM   390  N  N   . ARG A  1  53  ? 40.684  -3.982  52.853 1.00 30.97  ? 66  ARG A N   1 
ATOM   391  C  CA  . ARG A  1  53  ? 39.398  -3.339  52.622 1.00 33.62  ? 66  ARG A CA  1 
ATOM   392  C  C   . ARG A  1  53  ? 39.507  -1.817  52.629 1.00 34.52  ? 66  ARG A C   1 
ATOM   393  O  O   . ARG A  1  53  ? 38.590  -1.134  52.178 1.00 30.94  ? 66  ARG A O   1 
ATOM   394  C  CB  . ARG A  1  53  ? 38.375  -3.819  53.653 1.00 35.15  ? 66  ARG A CB  1 
ATOM   395  C  CG  . ARG A  1  53  ? 37.995  -5.261  53.361 1.00 37.87  ? 66  ARG A CG  1 
ATOM   396  C  CD  . ARG A  1  53  ? 36.887  -5.768  54.258 1.00 38.49  ? 66  ARG A CD  1 
ATOM   397  N  NE  . ARG A  1  53  ? 36.594  -7.172  53.976 1.00 40.72  ? 66  ARG A NE  1 
ATOM   398  C  CZ  . ARG A  1  53  ? 35.735  -7.639  53.070 1.00 36.88  ? 66  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A  1  53  ? 35.052  -6.822  52.283 1.00 32.50  ? 66  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A  1  53  ? 35.571  -8.949  52.962 1.00 35.23  ? 66  ARG A NH2 1 
ATOM   401  N  N   . ASP A  1  54  ? 40.636  -1.289  53.116 1.00 33.04  ? 67  ASP A N   1 
ATOM   402  C  CA  . ASP A  1  54  ? 40.824  0.149   53.180 1.00 33.57  ? 67  ASP A CA  1 
ATOM   403  C  C   . ASP A  1  54  ? 41.354  0.689   51.857 1.00 32.95  ? 67  ASP A C   1 
ATOM   404  O  O   . ASP A  1  54  ? 41.524  1.894   51.715 1.00 33.59  ? 67  ASP A O   1 
ATOM   405  C  CB  . ASP A  1  54  ? 41.671  0.552   54.370 1.00 36.10  ? 67  ASP A CB  1 
ATOM   406  C  CG  . ASP A  1  54  ? 43.102  0.044   54.373 1.00 38.74  ? 67  ASP A CG  1 
ATOM   407  O  OD1 . ASP A  1  54  ? 43.487  -0.626  53.402 1.00 41.10  ? 67  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A  1  54  ? 43.802  0.293   55.373 1.00 42.78  ? 67  ASP A OD2 1 
ATOM   409  N  N   . GLY A  1  55  ? 41.613  -0.191  50.887 1.00 35.16  ? 68  GLY A N   1 
ATOM   410  C  CA  . GLY A  1  55  ? 42.020  0.243   49.560 1.00 37.24  ? 68  GLY A CA  1 
ATOM   411  C  C   . GLY A  1  55  ? 43.483  0.698   49.505 1.00 34.73  ? 68  GLY A C   1 
ATOM   412  O  O   . GLY A  1  55  ? 43.872  1.394   48.570 1.00 33.19  ? 68  GLY A O   1 
ATOM   413  N  N   . VAL A  1  56  ? 44.291  0.294   50.487 1.00 33.27  ? 69  VAL A N   1 
ATOM   414  C  CA  . VAL A  1  56  ? 45.721  0.587   50.467 1.00 35.69  ? 69  VAL A CA  1 
ATOM   415  C  C   . VAL A  1  56  ? 46.469  -0.736  50.557 1.00 32.78  ? 69  VAL A C   1 
ATOM   416  O  O   . VAL A  1  56  ? 46.191  -1.541  51.436 1.00 33.64  ? 69  VAL A O   1 
ATOM   417  C  CB  . VAL A  1  56  ? 46.129  1.548   51.604 1.00 38.47  ? 69  VAL A CB  1 
ATOM   418  C  CG1 . VAL A  1  56  ? 47.633  1.756   51.679 1.00 38.92  ? 69  VAL A CG1 1 
ATOM   419  C  CG2 . VAL A  1  56  ? 45.428  2.894   51.462 1.00 40.94  ? 69  VAL A CG2 1 
ATOM   420  N  N   . ALA A  1  57  ? 47.408  -0.947  49.638 1.00 31.47  ? 70  ALA A N   1 
ATOM   421  C  CA  . ALA A  1  57  ? 48.025  -2.253  49.492 1.00 34.45  ? 70  ALA A CA  1 
ATOM   422  C  C   . ALA A  1  57  ? 49.451  -2.132  48.965 1.00 33.97  ? 70  ALA A C   1 
ATOM   423  O  O   . ALA A  1  57  ? 49.820  -1.122  48.369 1.00 34.38  ? 70  ALA A O   1 
ATOM   424  C  CB  . ALA A  1  57  ? 47.191  -3.095  48.556 1.00 34.23  ? 70  ALA A CB  1 
ATOM   425  N  N   . THR A  1  58  ? 50.213  -3.211  49.146 1.00 32.87  ? 71  THR A N   1 
ATOM   426  C  CA  . THR A  1  58  ? 51.538  -3.322  48.564 1.00 36.57  ? 71  THR A CA  1 
ATOM   427  C  C   . THR A  1  58  ? 51.379  -3.737  47.107 1.00 35.90  ? 71  THR A C   1 
ATOM   428  O  O   . THR A  1  58  ? 50.343  -4.276  46.716 1.00 33.46  ? 71  THR A O   1 
ATOM   429  C  CB  . THR A  1  58  ? 52.405  -4.320  49.330 1.00 36.29  ? 71  THR A CB  1 
ATOM   430  O  OG1 . THR A  1  58  ? 51.880  -5.614  49.070 1.00 37.72  ? 71  THR A OG1 1 
ATOM   431  C  CG2 . THR A  1  58  ? 52.423  -4.073  50.829 1.00 37.20  ? 71  THR A CG2 1 
ATOM   432  N  N   . PRO A  1  59  ? 52.386  -3.467  46.256 1.00 35.39  ? 72  PRO A N   1 
ATOM   433  C  CA  . PRO A  1  59  ? 52.414  -4.011  44.900 1.00 37.85  ? 72  PRO A CA  1 
ATOM   434  C  C   . PRO A  1  59  ? 52.191  -5.521  44.868 1.00 36.23  ? 72  PRO A C   1 
ATOM   435  O  O   . PRO A  1  59  ? 51.417  -6.009  44.042 1.00 35.99  ? 72  PRO A O   1 
ATOM   436  C  CB  . PRO A  1  59  ? 53.825  -3.615  44.405 1.00 37.80  ? 72  PRO A CB  1 
ATOM   437  C  CG  . PRO A  1  59  ? 54.110  -2.330  45.163 1.00 37.24  ? 72  PRO A CG  1 
ATOM   438  C  CD  . PRO A  1  59  ? 53.515  -2.569  46.532 1.00 35.48  ? 72  PRO A CD  1 
ATOM   439  N  N   . ALA A  1  60  ? 52.880  -6.235  45.772 1.00 35.72  ? 73  ALA A N   1 
ATOM   440  C  CA  . ALA A  1  60  ? 52.772  -7.683  45.858 1.00 36.22  ? 73  ALA A CA  1 
ATOM   441  C  C   . ALA A  1  60  ? 51.325  -8.095  46.115 1.00 35.75  ? 73  ALA A C   1 
ATOM   442  O  O   . ALA A  1  60  ? 50.842  -9.007  45.465 1.00 36.03  ? 73  ALA A O   1 
ATOM   443  C  CB  . ALA A  1  60  ? 53.685  -8.223  46.927 1.00 35.73  ? 73  ALA A CB  1 
ATOM   444  N  N   . GLN A  1  61  ? 50.647  -7.420  47.051 1.00 34.92  ? 74  GLN A N   1 
ATOM   445  C  CA  . GLN A  1  61  ? 49.257  -7.740  47.356 1.00 37.65  ? 74  GLN A CA  1 
ATOM   446  C  C   . GLN A  1  61  ? 48.348  -7.508  46.153 1.00 37.49  ? 74  GLN A C   1 
ATOM   447  O  O   . GLN A  1  61  ? 47.430  -8.287  45.922 1.00 41.64  ? 74  GLN A O   1 
ATOM   448  C  CB  . GLN A  1  61  ? 48.711  -6.937  48.531 1.00 37.73  ? 74  GLN A CB  1 
ATOM   449  C  CG  . GLN A  1  61  ? 49.259  -7.393  49.874 1.00 39.93  ? 74  GLN A CG  1 
ATOM   450  C  CD  . GLN A  1  61  ? 48.934  -6.432  50.994 1.00 42.11  ? 74  GLN A CD  1 
ATOM   451  O  OE1 . GLN A  1  61  ? 48.894  -5.211  50.806 1.00 38.70  ? 74  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A  1  61  ? 48.676  -6.980  52.172 1.00 42.21  ? 74  GLN A NE2 1 
ATOM   453  N  N   . ILE A  1  62  ? 48.600  -6.433  45.400 1.00 37.87  ? 75  ILE A N   1 
ATOM   454  C  CA  . ILE A  1  62  ? 47.772  -6.079  44.258 1.00 37.66  ? 75  ILE A CA  1 
ATOM   455  C  C   . ILE A  1  62  ? 47.907  -7.152  43.177 1.00 36.14  ? 75  ILE A C   1 
ATOM   456  O  O   . ILE A  1  62  ? 46.912  -7.602  42.616 1.00 32.98  ? 75  ILE A O   1 
ATOM   457  C  CB  . ILE A  1  62  ? 48.121  -4.660  43.752 1.00 36.75  ? 75  ILE A CB  1 
ATOM   458  C  CG1 . ILE A  1  62  ? 47.639  -3.624  44.775 1.00 38.42  ? 75  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A  1  62  ? 47.544  -4.393  42.357 1.00 35.15  ? 75  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A  1  62  ? 48.155  -2.216  44.566 1.00 40.40  ? 75  ILE A CD1 1 
ATOM   461  N  N   . ILE A  1  63  ? 49.136  -7.590  42.916 1.00 34.28  ? 76  ILE A N   1 
ATOM   462  C  CA  . ILE A  1  63  ? 49.380  -8.588  41.890 1.00 35.31  ? 76  ILE A CA  1 
ATOM   463  C  C   . ILE A  1  63  ? 48.651  -9.878  42.252 1.00 34.16  ? 76  ILE A C   1 
ATOM   464  O  O   . ILE A  1  63  ? 47.943  -10.434 41.416 1.00 35.61  ? 76  ILE A O   1 
ATOM   465  C  CB  . ILE A  1  63  ? 50.893  -8.811  41.688 1.00 33.36  ? 76  ILE A CB  1 
ATOM   466  C  CG1 . ILE A  1  63  ? 51.522  -7.602  41.008 1.00 34.25  ? 76  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A  1  63  ? 51.140  -10.095 40.905 1.00 32.17  ? 76  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A  1  63  ? 53.025  -7.467  41.196 1.00 39.29  ? 76  ILE A CD1 1 
ATOM   469  N  N   . THR A  1  64  ? 48.821  -10.348 43.491 1.00 32.53  ? 77  THR A N   1 
ATOM   470  C  CA  A THR A  1  64  ? 48.223  -11.606 43.905 0.50 34.63  ? 77  THR A CA  1 
ATOM   471  C  CA  B THR A  1  64  ? 48.221  -11.606 43.908 0.50 35.44  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A  1  64  ? 46.700  -11.472 43.869 1.00 37.80  ? 77  THR A C   1 
ATOM   473  O  O   . THR A  1  64  ? 46.012  -12.377 43.414 1.00 34.83  ? 77  THR A O   1 
ATOM   474  C  CB  A THR A  1  64  ? 48.744  -12.011 45.283 0.50 34.96  ? 77  THR A CB  1 
ATOM   475  C  CB  B THR A  1  64  ? 48.743  -12.074 45.270 0.50 38.09  ? 77  THR A CB  1 
ATOM   476  O  OG1 A THR A  1  64  ? 48.301  -10.956 46.125 0.50 47.57  ? 77  THR A OG1 1 
ATOM   477  O  OG1 B THR A  1  64  ? 47.853  -13.065 45.786 0.50 36.89  ? 77  THR A OG1 1 
ATOM   478  C  CG2 A THR A  1  64  ? 50.255  -12.136 45.337 0.50 30.29  ? 77  THR A CG2 1 
ATOM   479  C  CG2 B THR A  1  64  ? 48.762  -11.021 46.354 0.50 42.79  ? 77  THR A CG2 1 
ATOM   480  N  N   . ALA A  1  65  ? 46.169  -10.319 44.301 1.00 36.47  ? 78  ALA A N   1 
ATOM   481  C  CA  . ALA A  1  65  ? 44.723  -10.123 44.316 1.00 34.26  ? 78  ALA A CA  1 
ATOM   482  C  C   . ALA A  1  65  ? 44.127  -10.145 42.907 1.00 33.24  ? 78  ALA A C   1 
ATOM   483  O  O   . ALA A  1  65  ? 43.061  -10.721 42.719 1.00 35.64  ? 78  ALA A O   1 
ATOM   484  C  CB  . ALA A  1  65  ? 44.351  -8.849  45.036 1.00 35.65  ? 78  ALA A CB  1 
ATOM   485  N  N   . THR A  1  66  ? 44.782  -9.514  41.926 1.00 31.96  ? 79  THR A N   1 
ATOM   486  C  CA  . THR A  1  66  ? 44.267  -9.495  40.561 1.00 32.84  ? 79  THR A CA  1 
ATOM   487  C  C   . THR A  1  66  ? 44.323  -10.904 39.952 1.00 33.56  ? 79  THR A C   1 
ATOM   488  O  O   . THR A  1  66  ? 43.426  -11.296 39.205 1.00 32.76  ? 79  THR A O   1 
ATOM   489  C  CB  . THR A  1  66  ? 45.001  -8.466  39.699 1.00 34.72  ? 79  THR A CB  1 
ATOM   490  O  OG1 . THR A  1  66  ? 46.411  -8.693  39.704 1.00 35.47  ? 79  THR A OG1 1 
ATOM   491  C  CG2 . THR A  1  66  ? 44.772  -7.052  40.197 1.00 36.28  ? 79  THR A CG2 1 
ATOM   492  N  N   . GLN A  1  67  ? 45.351  -11.677 40.309 1.00 33.84  ? 80  GLN A N   1 
ATOM   493  C  CA  . GLN A  1  67  ? 45.463  -13.076 39.905 1.00 35.71  ? 80  GLN A CA  1 
ATOM   494  C  C   . GLN A  1  67  ? 44.387  -13.934 40.573 1.00 34.29  ? 80  GLN A C   1 
ATOM   495  O  O   . GLN A  1  67  ? 43.651  -14.623 39.886 1.00 38.08  ? 80  GLN A O   1 
ATOM   496  C  CB  . GLN A  1  67  ? 46.892  -13.563 40.155 1.00 34.16  ? 80  GLN A CB  1 
ATOM   497  C  CG  . GLN A  1  67  ? 47.896  -12.817 39.282 1.00 34.81  ? 80  GLN A CG  1 
ATOM   498  C  CD  . GLN A  1  67  ? 49.343  -13.236 39.427 1.00 33.97  ? 80  GLN A CD  1 
ATOM   499  O  OE1 . GLN A  1  67  ? 50.169  -12.883 38.581 1.00 35.78  ? 80  GLN A OE1 1 
ATOM   500  N  NE2 . GLN A  1  67  ? 49.679  -13.992 40.464 1.00 34.28  ? 80  GLN A NE2 1 
ATOM   501  N  N   . GLU A  1  68  ? 44.295  -13.896 41.900 1.00 35.97  ? 81  GLU A N   1 
ATOM   502  C  CA  . GLU A  1  68  ? 43.362  -14.740 42.635 1.00 41.31  ? 81  GLU A CA  1 
ATOM   503  C  C   . GLU A  1  68  ? 41.921  -14.427 42.236 1.00 37.36  ? 81  GLU A C   1 
ATOM   504  O  O   . GLU A  1  68  ? 41.129  -15.332 41.990 1.00 38.02  ? 81  GLU A O   1 
ATOM   505  C  CB  . GLU A  1  68  ? 43.492  -14.555 44.150 1.00 43.69  ? 81  GLU A CB  1 
ATOM   506  C  CG  . GLU A  1  68  ? 44.766  -15.166 44.726 1.00 51.17  ? 81  GLU A CG  1 
ATOM   507  C  CD  . GLU A  1  68  ? 44.974  -16.627 44.352 1.00 56.03  ? 81  GLU A CD  1 
ATOM   508  O  OE1 . GLU A  1  68  ? 46.074  -16.993 43.864 1.00 60.87  ? 81  GLU A OE1 1 
ATOM   509  O  OE2 . GLU A  1  68  ? 44.003  -17.388 44.529 1.00 59.62  ? 81  GLU A OE2 1 
ATOM   510  N  N   . GLY A  1  69  ? 41.598  -13.133 42.168 1.00 35.64  ? 82  GLY A N   1 
ATOM   511  C  CA  . GLY A  1  69  ? 40.227  -12.677 42.006 1.00 33.26  ? 82  GLY A CA  1 
ATOM   512  C  C   . GLY A  1  69  ? 39.753  -12.745 40.559 1.00 32.48  ? 82  GLY A C   1 
ATOM   513  O  O   . GLY A  1  69  ? 38.572  -13.023 40.314 1.00 31.71  ? 82  GLY A O   1 
ATOM   514  N  N   . PHE A  1  70  ? 40.646  -12.458 39.597 1.00 33.01  ? 83  PHE A N   1 
ATOM   515  C  CA  . PHE A  1  70  ? 40.210  -12.299 38.214 1.00 35.55  ? 83  PHE A CA  1 
ATOM   516  C  C   . PHE A  1  70  ? 41.009  -13.142 37.224 1.00 36.37  ? 83  PHE A C   1 
ATOM   517  O  O   . PHE A  1  70  ? 40.646  -13.171 36.055 1.00 34.35  ? 83  PHE A O   1 
ATOM   518  C  CB  . PHE A  1  70  ? 40.282  -10.828 37.786 1.00 31.85  ? 83  PHE A CB  1 
ATOM   519  C  CG  . PHE A  1  70  ? 39.179  -9.947  38.344 1.00 33.39  ? 83  PHE A CG  1 
ATOM   520  C  CD1 . PHE A  1  70  ? 37.881  -10.055 37.855 1.00 36.31  ? 83  PHE A CD1 1 
ATOM   521  C  CD2 . PHE A  1  70  ? 39.427  -9.020  39.355 1.00 35.61  ? 83  PHE A CD2 1 
ATOM   522  C  CE1 . PHE A  1  70  ? 36.861  -9.274  38.366 1.00 35.35  ? 83  PHE A CE1 1 
ATOM   523  C  CE2 . PHE A  1  70  ? 38.403  -8.233  39.846 1.00 33.91  ? 83  PHE A CE2 1 
ATOM   524  C  CZ  . PHE A  1  70  ? 37.130  -8.355  39.350 1.00 36.64  ? 83  PHE A CZ  1 
ATOM   525  N  N   . ASN A  1  71  ? 42.097  -13.782 37.678 1.00 39.23  ? 84  ASN A N   1 
ATOM   526  C  CA  . ASN A  1  71  ? 43.029  -14.482 36.802 1.00 37.31  ? 84  ASN A CA  1 
ATOM   527  C  C   . ASN A  1  71  ? 43.672  -13.496 35.829 1.00 37.42  ? 84  ASN A C   1 
ATOM   528  O  O   . ASN A  1  71  ? 43.913  -13.819 34.667 1.00 35.98  ? 84  ASN A O   1 
ATOM   529  C  CB  . ASN A  1  71  ? 42.333  -15.630 36.074 1.00 38.69  ? 84  ASN A CB  1 
ATOM   530  C  CG  . ASN A  1  71  ? 43.195  -16.865 35.932 1.00 40.06  ? 84  ASN A CG  1 
ATOM   531  O  OD1 . ASN A  1  71  ? 44.404  -16.836 36.202 1.00 40.49  ? 84  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A  1  71  ? 42.582  -17.969 35.528 1.00 39.49  ? 84  ASN A ND2 1 
ATOM   533  N  N   . PHE A  1  72  ? 43.938  -12.272 36.299 1.00 36.45  ? 85  PHE A N   1 
ATOM   534  C  CA  . PHE A  1  72  ? 44.701  -11.317 35.515 1.00 34.94  ? 85  PHE A CA  1 
ATOM   535  C  C   . PHE A  1  72  ? 46.075  -11.939 35.275 1.00 34.16  ? 85  PHE A C   1 
ATOM   536  O  O   . PHE A  1  72  ? 46.673  -12.509 36.189 1.00 31.94  ? 85  PHE A O   1 
ATOM   537  C  CB  . PHE A  1  72  ? 44.774  -9.979  36.266 1.00 36.11  ? 85  PHE A CB  1 
ATOM   538  C  CG  . PHE A  1  72  ? 45.100  -8.744  35.434 1.00 37.83  ? 85  PHE A CG  1 
ATOM   539  C  CD1 . PHE A  1  72  ? 44.455  -8.502  34.227 1.00 39.41  ? 85  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A  1  72  ? 46.048  -7.820  35.865 1.00 37.00  ? 85  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A  1  72  ? 44.736  -7.359  33.489 1.00 38.65  ? 85  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A  1  72  ? 46.324  -6.686  35.121 1.00 38.51  ? 85  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A  1  72  ? 45.670  -6.457  33.933 1.00 37.08  ? 85  PHE A CZ  1 
ATOM   544  N  N   . GLU A  1  73  ? 46.549  -11.871 34.031 1.00 36.45  ? 86  GLU A N   1 
ATOM   545  C  CA  . GLU A  1  73  ? 47.796  -12.520 33.670 1.00 35.96  ? 86  GLU A CA  1 
ATOM   546  C  C   . GLU A  1  73  ? 48.961  -11.823 34.382 1.00 37.57  ? 86  GLU A C   1 
ATOM   547  O  O   . GLU A  1  73  ? 48.987  -10.596 34.514 1.00 36.83  ? 86  GLU A O   1 
ATOM   548  C  CB  . GLU A  1  73  ? 47.890  -12.571 32.147 1.00 40.55  ? 86  GLU A CB  1 
ATOM   549  C  CG  . GLU A  1  73  ? 49.071  -13.384 31.626 1.00 41.21  ? 86  GLU A CG  1 
ATOM   550  C  CD  . GLU A  1  73  ? 50.387  -12.631 31.581 1.00 45.03  ? 86  GLU A CD  1 
ATOM   551  O  OE1 . GLU A  1  73  ? 51.443  -13.254 31.887 1.00 45.43  ? 86  GLU A OE1 1 
ATOM   552  O  OE2 . GLU A  1  73  ? 50.349  -11.415 31.267 1.00 43.78  ? 86  GLU A OE2 1 
ATOM   553  N  N   . ASN A  1  74  ? 49.924  -12.642 34.818 1.00 35.94  ? 87  ASN A N   1 
ATOM   554  C  CA  . ASN A  1  74  ? 51.017  -12.236 35.692 1.00 37.42  ? 87  ASN A CA  1 
ATOM   555  C  C   . ASN A  1  74  ? 51.764  -11.013 35.156 1.00 37.48  ? 87  ASN A C   1 
ATOM   556  O  O   . ASN A  1  74  ? 51.979  -10.042 35.882 1.00 35.66  ? 87  ASN A O   1 
ATOM   557  C  CB  . ASN A  1  74  ? 51.969  -13.403 35.929 1.00 35.57  ? 87  ASN A CB  1 
ATOM   558  C  CG  . ASN A  1  74  ? 53.114  -13.058 36.850 1.00 36.81  ? 87  ASN A CG  1 
ATOM   559  O  OD1 . ASN A  1  74  ? 54.279  -13.164 36.450 1.00 40.50  ? 87  ASN A OD1 1 
ATOM   560  N  ND2 . ASN A  1  74  ? 52.813  -12.663 38.078 1.00 35.85  ? 87  ASN A ND2 1 
ATOM   561  N  N   . ASN A  1  75  ? 52.186  -11.060 33.894 1.00 37.89  ? 88  ASN A N   1 
ATOM   562  C  CA  A ASN A  1  75  ? 52.998  -9.984  33.346 0.50 39.14  ? 88  ASN A CA  1 
ATOM   563  C  CA  B ASN A  1  75  ? 52.983  -9.993  33.313 0.50 39.93  ? 88  ASN A CA  1 
ATOM   564  C  C   . ASN A  1  75  ? 52.172  -8.701  33.215 1.00 38.40  ? 88  ASN A C   1 
ATOM   565  O  O   . ASN A  1  75  ? 52.685  -7.609  33.483 1.00 39.89  ? 88  ASN A O   1 
ATOM   566  C  CB  A ASN A  1  75  ? 53.720  -10.403 32.070 0.50 40.99  ? 88  ASN A CB  1 
ATOM   567  C  CB  B ASN A  1  75  ? 53.466  -10.400 31.928 0.50 43.04  ? 88  ASN A CB  1 
ATOM   568  C  CG  A ASN A  1  75  ? 54.964  -11.212 32.374 0.50 41.15  ? 88  ASN A CG  1 
ATOM   569  C  CG  B ASN A  1  75  ? 54.875  -9.952  31.676 0.50 44.72  ? 88  ASN A CG  1 
ATOM   570  O  OD1 A ASN A  1  75  ? 55.043  -12.381 31.984 0.50 42.62  ? 88  ASN A OD1 1 
ATOM   571  O  OD1 B ASN A  1  75  ? 55.789  -10.338 32.415 0.50 48.39  ? 88  ASN A OD1 1 
ATOM   572  N  ND2 A ASN A  1  75  ? 55.926  -10.635 33.089 0.50 39.46  ? 88  ASN A ND2 1 
ATOM   573  N  ND2 B ASN A  1  75  ? 55.059  -9.169  30.626 0.50 46.86  ? 88  ASN A ND2 1 
ATOM   574  N  N   . ALA A  1  76  ? 50.897  -8.827  32.810 1.00 36.40  ? 89  ALA A N   1 
ATOM   575  C  CA  . ALA A  1  76  ? 50.028  -7.668  32.726 1.00 36.33  ? 89  ALA A CA  1 
ATOM   576  C  C   . ALA A  1  76  ? 49.840  -7.035  34.110 1.00 36.34  ? 89  ALA A C   1 
ATOM   577  O  O   . ALA A  1  76  ? 49.803  -5.812  34.237 1.00 37.79  ? 89  ALA A O   1 
ATOM   578  C  CB  . ALA A  1  76  ? 48.715  -8.058  32.096 1.00 39.24  ? 89  ALA A CB  1 
ATOM   579  N  N   . ALA A  1  77  ? 49.740  -7.876  35.142 1.00 33.70  ? 90  ALA A N   1 
ATOM   580  C  CA  . ALA A  1  77  ? 49.614  -7.421  36.519 1.00 34.87  ? 90  ALA A CA  1 
ATOM   581  C  C   . ALA A  1  77  ? 50.871  -6.665  36.960 1.00 36.20  ? 90  ALA A C   1 
ATOM   582  O  O   . ALA A  1  77  ? 50.775  -5.650  37.648 1.00 34.82  ? 90  ALA A O   1 
ATOM   583  C  CB  . ALA A  1  77  ? 49.349  -8.609  37.428 1.00 33.63  ? 90  ALA A CB  1 
ATOM   584  N  N   . ILE A  1  78  ? 52.046  -7.162  36.553 1.00 34.53  ? 91  ILE A N   1 
ATOM   585  C  CA  . ILE A  1  78  ? 53.306  -6.538  36.925 1.00 34.96  ? 91  ILE A CA  1 
ATOM   586  C  C   . ILE A  1  78  ? 53.438  -5.180  36.229 1.00 35.50  ? 91  ILE A C   1 
ATOM   587  O  O   . ILE A  1  78  ? 53.794  -4.184  36.861 1.00 33.57  ? 91  ILE A O   1 
ATOM   588  C  CB  . ILE A  1  78  ? 54.483  -7.494  36.647 1.00 37.13  ? 91  ILE A CB  1 
ATOM   589  C  CG1 . ILE A  1  78  ? 54.459  -8.659  37.654 1.00 38.45  ? 91  ILE A CG1 1 
ATOM   590  C  CG2 . ILE A  1  78  ? 55.830  -6.750  36.676 1.00 39.21  ? 91  ILE A CG2 1 
ATOM   591  C  CD1 . ILE A  1  78  ? 55.409  -9.802  37.327 1.00 38.12  ? 91  ILE A CD1 1 
ATOM   592  N  N   . VAL A  1  79  ? 53.093  -5.126  34.942 1.00 34.82  ? 92  VAL A N   1 
ATOM   593  C  CA  . VAL A  1  79  ? 53.185  -3.880  34.192 1.00 38.03  ? 92  VAL A CA  1 
ATOM   594  C  C   . VAL A  1  79  ? 52.264  -2.819  34.799 1.00 38.33  ? 92  VAL A C   1 
ATOM   595  O  O   . VAL A  1  79  ? 52.688  -1.683  35.022 1.00 39.30  ? 92  VAL A O   1 
ATOM   596  C  CB  . VAL A  1  79  ? 52.892  -4.123  32.700 1.00 42.27  ? 92  VAL A CB  1 
ATOM   597  C  CG1 . VAL A  1  79  ? 52.639  -2.821  31.942 1.00 44.37  ? 92  VAL A CG1 1 
ATOM   598  C  CG2 . VAL A  1  79  ? 54.019  -4.911  32.036 1.00 44.32  ? 92  VAL A CG2 1 
ATOM   599  N  N   . ALA A  1  80  ? 51.001  -3.183  35.069 1.00 36.50  ? 93  ALA A N   1 
ATOM   600  C  CA  . ALA A  1  80  ? 50.045  -2.227  35.606 1.00 33.74  ? 93  ALA A CA  1 
ATOM   601  C  C   . ALA A  1  80  ? 50.429  -1.791  37.020 1.00 34.10  ? 93  ALA A C   1 
ATOM   602  O  O   . ALA A  1  80  ? 50.368  -0.603  37.336 1.00 33.32  ? 93  ALA A O   1 
ATOM   603  C  CB  . ALA A  1  80  ? 48.653  -2.802  35.587 1.00 35.85  ? 93  ALA A CB  1 
ATOM   604  N  N   . THR A  1  81  ? 50.833  -2.745  37.869 1.00 33.88  ? 94  THR A N   1 
ATOM   605  C  CA  . THR A  1  81  ? 50.970  -2.465  39.286 1.00 34.66  ? 94  THR A CA  1 
ATOM   606  C  C   . THR A  1  81  ? 52.160  -1.533  39.539 1.00 36.84  ? 94  THR A C   1 
ATOM   607  O  O   . THR A  1  81  ? 52.038  -0.566  40.290 1.00 36.09  ? 94  THR A O   1 
ATOM   608  C  CB  . THR A  1  81  ? 51.089  -3.765  40.083 1.00 36.59  ? 94  THR A CB  1 
ATOM   609  O  OG1 . THR A  1  81  ? 49.889  -4.515  39.892 1.00 38.43  ? 94  THR A OG1 1 
ATOM   610  C  CG2 . THR A  1  81  ? 51.279  -3.497  41.566 1.00 35.52  ? 94  THR A CG2 1 
ATOM   611  N  N   . TYR A  1  82  ? 53.323  -1.832  38.949 1.00 35.64  ? 95  TYR A N   1 
ATOM   612  C  CA  . TYR A  1  82  ? 54.525  -1.064  39.247 1.00 38.98  ? 95  TYR A CA  1 
ATOM   613  C  C   . TYR A  1  82  ? 54.479  0.286   38.523 1.00 38.42  ? 95  TYR A C   1 
ATOM   614  O  O   . TYR A  1  82  ? 55.089  1.251   38.981 1.00 40.86  ? 95  TYR A O   1 
ATOM   615  C  CB  . TYR A  1  82  ? 55.799  -1.879  38.986 1.00 35.91  ? 95  TYR A CB  1 
ATOM   616  C  CG  . TYR A  1  82  ? 55.969  -3.004  39.999 1.00 37.30  ? 95  TYR A CG  1 
ATOM   617  C  CD1 . TYR A  1  82  ? 56.401  -2.747  41.294 1.00 38.54  ? 95  TYR A CD1 1 
ATOM   618  C  CD2 . TYR A  1  82  ? 55.666  -4.320  39.673 1.00 37.16  ? 95  TYR A CD2 1 
ATOM   619  C  CE1 . TYR A  1  82  ? 56.538  -3.759  42.227 1.00 37.67  ? 95  TYR A CE1 1 
ATOM   620  C  CE2 . TYR A  1  82  ? 55.786  -5.338  40.602 1.00 37.05  ? 95  TYR A CE2 1 
ATOM   621  C  CZ  . TYR A  1  82  ? 56.225  -5.062  41.880 1.00 37.93  ? 95  TYR A CZ  1 
ATOM   622  O  OH  . TYR A  1  82  ? 56.351  -6.068  42.797 1.00 42.19  ? 95  TYR A OH  1 
ATOM   623  N  N   . LEU A  1  83  ? 53.731  0.365   37.420 1.00 38.77  ? 96  LEU A N   1 
ATOM   624  C  CA  . LEU A  1  83  ? 53.457  1.648   36.788 1.00 42.01  ? 96  LEU A CA  1 
ATOM   625  C  C   . LEU A  1  83  ? 52.727  2.540   37.791 1.00 41.24  ? 96  LEU A C   1 
ATOM   626  O  O   . LEU A  1  83  ? 53.173  3.646   38.096 1.00 40.58  ? 96  LEU A O   1 
ATOM   627  C  CB  . LEU A  1  83  ? 52.648  1.459   35.508 1.00 41.02  ? 96  LEU A CB  1 
ATOM   628  C  CG  . LEU A  1  83  ? 52.106  2.738   34.859 1.00 44.90  ? 96  LEU A CG  1 
ATOM   629  C  CD1 . LEU A  1  83  ? 53.216  3.664   34.417 1.00 42.85  ? 96  LEU A CD1 1 
ATOM   630  C  CD2 . LEU A  1  83  ? 51.205  2.399   33.686 1.00 48.12  ? 96  LEU A CD2 1 
ATOM   631  N  N   . GLY A  1  84  ? 51.601  2.030   38.299 1.00 40.54  ? 97  GLY A N   1 
ATOM   632  C  CA  . GLY A  1  84  ? 50.825  2.716   39.316 1.00 41.19  ? 97  GLY A CA  1 
ATOM   633  C  C   . GLY A  1  84  ? 51.674  3.098   40.527 1.00 38.60  ? 97  GLY A C   1 
ATOM   634  O  O   . GLY A  1  84  ? 51.568  4.220   41.017 1.00 40.48  ? 97  GLY A O   1 
ATOM   635  N  N   . HIS A  1  85  ? 52.506  2.164   41.001 1.00 37.21  ? 98  HIS A N   1 
ATOM   636  C  CA  . HIS A  1  85  ? 53.274  2.363   42.222 1.00 38.11  ? 98  HIS A CA  1 
ATOM   637  C  C   . HIS A  1  85  ? 54.378  3.404   42.016 1.00 34.52  ? 98  HIS A C   1 
ATOM   638  O  O   . HIS A  1  85  ? 54.533  4.307   42.836 1.00 37.40  ? 98  HIS A O   1 
ATOM   639  C  CB  . HIS A  1  85  ? 53.860  1.031   42.714 1.00 37.84  ? 98  HIS A CB  1 
ATOM   640  C  CG  . HIS A  1  85  ? 54.494  1.114   44.055 1.00 36.27  ? 98  HIS A CG  1 
ATOM   641  N  ND1 . HIS A  1  85  ? 53.854  1.640   45.155 1.00 35.02  ? 98  HIS A ND1 1 
ATOM   642  C  CD2 . HIS A  1  85  ? 55.705  0.725   44.478 1.00 35.40  ? 98  HIS A CD2 1 
ATOM   643  C  CE1 . HIS A  1  85  ? 54.672  1.570   46.204 1.00 36.65  ? 98  HIS A CE1 1 
ATOM   644  N  NE2 . HIS A  1  85  ? 55.806  1.020   45.817 1.00 34.26  ? 98  HIS A NE2 1 
ATOM   645  N  N   . LEU A  1  86  ? 55.151  3.262   40.934 1.00 35.04  ? 99  LEU A N   1 
ATOM   646  C  CA  . LEU A  1  86  ? 56.246  4.181   40.646 1.00 36.17  ? 99  LEU A CA  1 
ATOM   647  C  C   . LEU A  1  86  ? 55.748  5.629   40.618 1.00 39.78  ? 99  LEU A C   1 
ATOM   648  O  O   . LEU A  1  86  ? 56.387  6.510   41.189 1.00 42.89  ? 99  LEU A O   1 
ATOM   649  C  CB  . LEU A  1  86  ? 56.927  3.823   39.327 1.00 34.67  ? 99  LEU A CB  1 
ATOM   650  C  CG  . LEU A  1  86  ? 57.897  2.641   39.370 1.00 38.18  ? 99  LEU A CG  1 
ATOM   651  C  CD1 . LEU A  1  86  ? 58.222  2.151   37.978 1.00 39.64  ? 99  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A  1  86  ? 59.171  3.029   40.101 1.00 38.04  ? 99  LEU A CD2 1 
ATOM   653  N  N   . LEU A  1  87  ? 54.595  5.855   39.972 1.00 39.38  ? 100 LEU A N   1 
ATOM   654  C  CA  . LEU A  1  87  ? 54.069  7.195   39.752 1.00 37.66  ? 100 LEU A CA  1 
ATOM   655  C  C   . LEU A  1  87  ? 53.258  7.681   40.952 1.00 37.08  ? 100 LEU A C   1 
ATOM   656  O  O   . LEU A  1  87  ? 53.304  8.860   41.272 1.00 38.25  ? 100 LEU A O   1 
ATOM   657  C  CB  . LEU A  1  87  ? 53.213  7.214   38.485 1.00 35.51  ? 100 LEU A CB  1 
ATOM   658  C  CG  . LEU A  1  87  ? 53.934  6.926   37.168 1.00 38.10  ? 100 LEU A CG  1 
ATOM   659  C  CD1 . LEU A  1  87  ? 52.957  6.823   36.030 1.00 39.31  ? 100 LEU A CD1 1 
ATOM   660  C  CD2 . LEU A  1  87  ? 54.963  7.994   36.852 1.00 41.24  ? 100 LEU A CD2 1 
ATOM   661  N  N   . ASN A  1  88  ? 52.503  6.782   41.602 1.00 37.81  ? 101 ASN A N   1 
ATOM   662  C  CA  . ASN A  1  88  ? 51.439  7.194   42.504 1.00 36.86  ? 101 ASN A CA  1 
ATOM   663  C  C   . ASN A  1  88  ? 51.529  6.573   43.893 1.00 37.08  ? 101 ASN A C   1 
ATOM   664  O  O   . ASN A  1  88  ? 50.681  6.879   44.740 1.00 36.35  ? 101 ASN A O   1 
ATOM   665  C  CB  . ASN A  1  88  ? 50.062  6.846   41.963 1.00 35.86  ? 101 ASN A CB  1 
ATOM   666  C  CG  . ASN A  1  88  ? 49.787  7.528   40.645 1.00 37.48  ? 101 ASN A CG  1 
ATOM   667  O  OD1 . ASN A  1  88  ? 50.134  8.703   40.461 1.00 39.19  ? 101 ASN A OD1 1 
ATOM   668  N  ND2 . ASN A  1  88  ? 49.183  6.807   39.713 1.00 38.62  ? 101 ASN A ND2 1 
ATOM   669  N  N   . GLY A  1  89  ? 52.532  5.717   44.124 1.00 36.98  ? 102 GLY A N   1 
ATOM   670  C  CA  . GLY A  1  89  ? 52.667  5.056   45.413 1.00 37.97  ? 102 GLY A CA  1 
ATOM   671  C  C   . GLY A  1  89  ? 53.820  5.624   46.238 1.00 38.86  ? 102 GLY A C   1 
ATOM   672  O  O   . GLY A  1  89  ? 54.609  6.436   45.747 1.00 37.53  ? 102 GLY A O   1 
ATOM   673  N  N   . ASN A  1  90  ? 53.916  5.134   47.481 1.00 38.73  ? 103 ASN A N   1 
ATOM   674  C  CA  . ASN A  1  90  ? 54.979  5.490   48.401 1.00 36.81  ? 103 ASN A CA  1 
ATOM   675  C  C   . ASN A  1  90  ? 56.023  4.375   48.388 1.00 41.38  ? 103 ASN A C   1 
ATOM   676  O  O   . ASN A  1  90  ? 55.811  3.281   48.924 1.00 40.14  ? 103 ASN A O   1 
ATOM   677  C  CB  . ASN A  1  90  ? 54.429  5.729   49.800 1.00 34.22  ? 103 ASN A CB  1 
ATOM   678  C  CG  . ASN A  1  90  ? 55.463  6.280   50.757 1.00 35.43  ? 103 ASN A CG  1 
ATOM   679  O  OD1 . ASN A  1  90  ? 56.606  5.813   50.788 1.00 35.13  ? 103 ASN A OD1 1 
ATOM   680  N  ND2 . ASN A  1  90  ? 55.089  7.287   51.534 1.00 37.99  ? 103 ASN A ND2 1 
ATOM   681  N  N   . LEU A  1  91  ? 57.176  4.685   47.802 1.00 42.94  ? 104 LEU A N   1 
ATOM   682  C  CA  . LEU A  1  91  ? 58.199  3.693   47.527 1.00 42.90  ? 104 LEU A CA  1 
ATOM   683  C  C   . LEU A  1  91  ? 58.906  3.244   48.796 1.00 36.78  ? 104 LEU A C   1 
ATOM   684  O  O   . LEU A  1  91  ? 59.409  2.127   48.847 1.00 38.08  ? 104 LEU A O   1 
ATOM   685  C  CB  . LEU A  1  91  ? 59.141  4.301   46.493 1.00 44.81  ? 104 LEU A CB  1 
ATOM   686  C  CG  . LEU A  1  91  ? 58.474  4.509   45.133 1.00 49.14  ? 104 LEU A CG  1 
ATOM   687  C  CD1 . LEU A  1  91  ? 59.240  5.477   44.302 1.00 50.87  ? 104 LEU A CD1 1 
ATOM   688  C  CD2 . LEU A  1  91  ? 58.354  3.201   44.396 1.00 53.86  ? 104 LEU A CD2 1 
ATOM   689  N  N   . VAL A  1  92  ? 58.898  4.103   49.819 1.00 38.07  ? 105 VAL A N   1 
ATOM   690  C  CA  . VAL A  1  92  ? 59.560  3.828   51.077 1.00 35.54  ? 105 VAL A CA  1 
ATOM   691  C  C   . VAL A  1  92  ? 58.724  2.869   51.916 1.00 36.48  ? 105 VAL A C   1 
ATOM   692  O  O   . VAL A  1  92  ? 59.272  1.933   52.495 1.00 35.73  ? 105 VAL A O   1 
ATOM   693  C  CB  . VAL A  1  92  ? 59.870  5.137   51.827 1.00 40.66  ? 105 VAL A CB  1 
ATOM   694  C  CG1 . VAL A  1  92  ? 60.341  4.876   53.257 1.00 42.02  ? 105 VAL A CG1 1 
ATOM   695  C  CG2 . VAL A  1  92  ? 60.890  5.975   51.063 1.00 38.48  ? 105 VAL A CG2 1 
ATOM   696  N  N   . THR A  1  93  ? 57.406  3.123   52.026 1.00 34.99  ? 106 THR A N   1 
ATOM   697  C  CA  . THR A  1  93  ? 56.544  2.249   52.806 1.00 36.47  ? 106 THR A CA  1 
ATOM   698  C  C   . THR A  1  93  ? 56.032  1.085   51.955 1.00 38.22  ? 106 THR A C   1 
ATOM   699  O  O   . THR A  1  93  ? 55.455  0.154   52.504 1.00 45.40  ? 106 THR A O   1 
ATOM   700  C  CB  . THR A  1  93  ? 55.387  3.030   53.421 1.00 39.54  ? 106 THR A CB  1 
ATOM   701  O  OG1 . THR A  1  93  ? 54.652  3.561   52.324 1.00 38.37  ? 106 THR A OG1 1 
ATOM   702  C  CG2 . THR A  1  93  ? 55.870  4.110   54.373 1.00 39.04  ? 106 THR A CG2 1 
ATOM   703  N  N   . ASP A  1  94  ? 56.207  1.166   50.630 1.00 34.05  ? 107 ASP A N   1 
ATOM   704  C  CA  . ASP A  1  94  ? 55.770  0.138   49.699 1.00 33.88  ? 107 ASP A CA  1 
ATOM   705  C  C   . ASP A  1  94  ? 54.247  0.016   49.715 1.00 34.48  ? 107 ASP A C   1 
ATOM   706  O  O   . ASP A  1  94  ? 53.719  -1.088  49.657 1.00 34.61  ? 107 ASP A O   1 
ATOM   707  C  CB  . ASP A  1  94  ? 56.448  -1.194  49.977 1.00 33.62  ? 107 ASP A CB  1 
ATOM   708  C  CG  . ASP A  1  94  ? 56.415  -2.202  48.838 1.00 36.39  ? 107 ASP A CG  1 
ATOM   709  O  OD1 . ASP A  1  94  ? 56.619  -1.779  47.670 1.00 38.41  ? 107 ASP A OD1 1 
ATOM   710  O  OD2 . ASP A  1  94  ? 56.197  -3.404  49.118 1.00 38.35  ? 107 ASP A OD2 1 
ATOM   711  N  N   . LEU A  1  95  ? 53.549  1.153   49.789 1.00 35.16  ? 108 LEU A N   1 
ATOM   712  C  CA  . LEU A  1  95  ? 52.095  1.176   49.848 1.00 35.48  ? 108 LEU A CA  1 
ATOM   713  C  C   . LEU A  1  95  ? 51.560  2.080   48.737 1.00 36.28  ? 108 LEU A C   1 
ATOM   714  O  O   . LEU A  1  95  ? 52.118  3.135   48.473 1.00 38.27  ? 108 LEU A O   1 
ATOM   715  C  CB  . LEU A  1  95  ? 51.608  1.632   51.222 1.00 32.84  ? 108 LEU A CB  1 
ATOM   716  C  CG  . LEU A  1  95  ? 51.925  0.708   52.399 1.00 36.37  ? 108 LEU A CG  1 
ATOM   717  C  CD1 . LEU A  1  95  ? 51.572  1.421   53.715 1.00 38.97  ? 108 LEU A CD1 1 
ATOM   718  C  CD2 . LEU A  1  95  ? 51.219  -0.636  52.322 1.00 35.72  ? 108 LEU A CD2 1 
ATOM   719  N  N   . LEU A  1  96  ? 50.475  1.628   48.092 1.00 35.24  ? 109 LEU A N   1 
ATOM   720  C  CA  . LEU A  1  96  ? 49.799  2.356   47.041 1.00 34.92  ? 109 LEU A CA  1 
ATOM   721  C  C   . LEU A  1  96  ? 48.317  2.464   47.390 1.00 39.66  ? 109 LEU A C   1 
ATOM   722  O  O   . LEU A  1  96  ? 47.689  1.464   47.726 1.00 39.95  ? 109 LEU A O   1 
ATOM   723  C  CB  . LEU A  1  96  ? 50.016  1.607   45.724 1.00 37.30  ? 109 LEU A CB  1 
ATOM   724  C  CG  . LEU A  1  96  ? 49.163  2.055   44.531 1.00 35.97  ? 109 LEU A CG  1 
ATOM   725  C  CD1 . LEU A  1  96  ? 49.450  3.500   44.179 1.00 36.72  ? 109 LEU A CD1 1 
ATOM   726  C  CD2 . LEU A  1  96  ? 49.378  1.189   43.313 1.00 35.83  ? 109 LEU A CD2 1 
ATOM   727  N  N   . SER A  1  97  ? 47.775  3.685   47.284 1.00 39.66  ? 110 SER A N   1 
ATOM   728  C  CA  . SER A  1  97  ? 46.345  3.934   47.372 1.00 38.32  ? 110 SER A CA  1 
ATOM   729  C  C   . SER A  1  97  ? 45.679  3.652   46.034 1.00 32.72  ? 110 SER A C   1 
ATOM   730  O  O   . SER A  1  97  ? 46.121  4.157   45.012 1.00 32.80  ? 110 SER A O   1 
ATOM   731  C  CB  . SER A  1  97  ? 46.068  5.357   47.797 1.00 38.65  ? 110 SER A CB  1 
ATOM   732  O  OG  . SER A  1  97  ? 44.680  5.655   47.711 1.00 38.41  ? 110 SER A OG  1 
ATOM   733  N  N   . ILE A  1  98  ? 44.569  2.907   46.044 1.00 35.30  ? 111 ILE A N   1 
ATOM   734  C  CA  . ILE A  1  98  ? 43.888  2.613   44.791 1.00 36.16  ? 111 ILE A CA  1 
ATOM   735  C  C   . ILE A  1  98  ? 42.987  3.781   44.395 1.00 38.42  ? 111 ILE A C   1 
ATOM   736  O  O   . ILE A  1  98  ? 42.298  3.714   43.374 1.00 40.24  ? 111 ILE A O   1 
ATOM   737  C  CB  . ILE A  1  98  ? 43.117  1.287   44.843 1.00 35.03  ? 111 ILE A CB  1 
ATOM   738  C  CG1 . ILE A  1  98  ? 41.952  1.318   45.822 1.00 37.49  ? 111 ILE A CG1 1 
ATOM   739  C  CG2 . ILE A  1  98  ? 44.069  0.130   45.114 1.00 35.61  ? 111 ILE A CG2 1 
ATOM   740  C  CD1 . ILE A  1  98  ? 41.061  0.088   45.750 1.00 39.77  ? 111 ILE A CD1 1 
ATOM   741  N  N   . GLY A  1  99  ? 42.979  4.832   45.219 1.00 37.26  ? 112 GLY A N   1 
ATOM   742  C  CA  . GLY A  1  99  ? 42.180  6.018   44.952 1.00 41.49  ? 112 GLY A CA  1 
ATOM   743  C  C   . GLY A  1  99  ? 42.991  7.281   45.196 1.00 41.10  ? 112 GLY A C   1 
ATOM   744  O  O   . GLY A  1  99  ? 44.003  7.476   44.544 1.00 41.82  ? 112 GLY A O   1 
ATOM   745  N  N   . GLY A  1  100 ? 42.532  8.107   46.141 1.00 41.85  ? 113 GLY A N   1 
ATOM   746  C  CA  . GLY A  1  100 ? 43.123  9.407   46.401 1.00 43.55  ? 113 GLY A CA  1 
ATOM   747  C  C   . GLY A  1  100 ? 44.108  9.367   47.564 1.00 44.85  ? 113 GLY A C   1 
ATOM   748  O  O   . GLY A  1  100 ? 44.526  8.298   48.015 1.00 41.16  ? 113 GLY A O   1 
ATOM   749  N  N   . ALA A  1  101 ? 44.464  10.563  48.043 1.00 44.82  ? 114 ALA A N   1 
ATOM   750  C  CA  . ALA A  1  101 ? 45.477  10.718  49.074 1.00 40.83  ? 114 ALA A CA  1 
ATOM   751  C  C   . ALA A  1  101 ? 44.943  10.197  50.402 1.00 36.76  ? 114 ALA A C   1 
ATOM   752  O  O   . ALA A  1  101 ? 43.756  10.289  50.684 1.00 37.04  ? 114 ALA A O   1 
ATOM   753  C  CB  . ALA A  1  101 ? 45.884  12.172  49.183 1.00 43.44  ? 114 ALA A CB  1 
ATOM   754  N  N   . THR A  1  102 ? 45.834  9.627   51.206 1.00 36.14  ? 115 THR A N   1 
ATOM   755  C  CA  . THR A  1  102 ? 45.462  9.089   52.501 1.00 39.11  ? 115 THR A CA  1 
ATOM   756  C  C   . THR A  1  102 ? 46.711  9.026   53.369 1.00 37.96  ? 115 THR A C   1 
ATOM   757  O  O   . THR A  1  102 ? 47.777  8.690   52.865 1.00 37.80  ? 115 THR A O   1 
ATOM   758  C  CB  . THR A  1  102 ? 44.837  7.704   52.338 1.00 40.37  ? 115 THR A CB  1 
ATOM   759  O  OG1 . THR A  1  102 ? 44.586  7.244   53.663 1.00 40.67  ? 115 THR A OG1 1 
ATOM   760  C  CG2 . THR A  1  102 ? 45.761  6.696   51.678 1.00 42.75  ? 115 THR A CG2 1 
ATOM   761  N  N   . PRO A  1  103 ? 46.615  9.322   54.685 1.00 42.08  ? 116 PRO A N   1 
ATOM   762  C  CA  . PRO A  1  103 ? 47.739  9.086   55.601 1.00 46.02  ? 116 PRO A CA  1 
ATOM   763  C  C   . PRO A  1  103 ? 48.147  7.613   55.704 1.00 40.94  ? 116 PRO A C   1 
ATOM   764  O  O   . PRO A  1  103 ? 49.257  7.310   56.131 1.00 40.70  ? 116 PRO A O   1 
ATOM   765  C  CB  . PRO A  1  103 ? 47.222  9.644   56.954 1.00 46.83  ? 116 PRO A CB  1 
ATOM   766  C  CG  . PRO A  1  103 ? 45.704  9.607   56.825 1.00 43.39  ? 116 PRO A CG  1 
ATOM   767  C  CD  . PRO A  1  103 ? 45.427  9.876   55.361 1.00 41.63  ? 116 PRO A CD  1 
ATOM   768  N  N   . LYS A  1  104 ? 47.257  6.704   55.278 1.00 35.14  ? 117 LYS A N   1 
ATOM   769  C  CA  . LYS A  1  104 ? 47.510  5.272   55.342 1.00 37.86  ? 117 LYS A CA  1 
ATOM   770  C  C   . LYS A  1  104 ? 48.711  4.852   54.489 1.00 36.13  ? 117 LYS A C   1 
ATOM   771  O  O   . LYS A  1  104 ? 49.231  3.767   54.708 1.00 39.69  ? 117 LYS A O   1 
ATOM   772  C  CB  . LYS A  1  104 ? 46.276  4.483   54.888 1.00 40.65  ? 117 LYS A CB  1 
ATOM   773  C  CG  . LYS A  1  104 ? 45.108  4.497   55.868 1.00 41.06  ? 117 LYS A CG  1 
ATOM   774  C  CD  . LYS A  1  104 ? 43.781  4.141   55.205 1.00 46.67  ? 117 LYS A CD  1 
ATOM   775  C  CE  . LYS A  1  104 ? 42.662  3.997   56.190 1.00 49.00  ? 117 LYS A CE  1 
ATOM   776  N  NZ  . LYS A  1  104 ? 42.865  2.844   57.071 1.00 53.18  ? 117 LYS A NZ  1 
ATOM   777  N  N   . THR A  1  105 ? 49.161  5.682   53.532 1.00 33.82  ? 118 THR A N   1 
ATOM   778  C  CA  . THR A  1  105 ? 50.332  5.326   52.739 1.00 36.74  ? 118 THR A CA  1 
ATOM   779  C  C   . THR A  1  105 ? 51.613  5.752   53.458 1.00 38.18  ? 118 THR A C   1 
ATOM   780  O  O   . THR A  1  105 ? 52.696  5.416   52.995 1.00 40.30  ? 118 THR A O   1 
ATOM   781  C  CB  . THR A  1  105 ? 50.266  5.893   51.317 1.00 37.72  ? 118 THR A CB  1 
ATOM   782  O  OG1 . THR A  1  105 ? 50.084  7.308   51.342 1.00 35.67  ? 118 THR A OG1 1 
ATOM   783  C  CG2 . THR A  1  105 ? 49.175  5.232   50.499 1.00 36.92  ? 118 THR A CG2 1 
ATOM   784  N  N   . GLY A  1  106 ? 51.481  6.498   54.569 1.00 40.31  ? 119 GLY A N   1 
ATOM   785  C  CA  . GLY A  1  106 ? 52.609  6.818   55.426 1.00 42.33  ? 119 GLY A CA  1 
ATOM   786  C  C   . GLY A  1  106 ? 53.189  8.205   55.145 1.00 42.13  ? 119 GLY A C   1 
ATOM   787  O  O   . GLY A  1  106 ? 52.620  8.988   54.387 1.00 39.69  ? 119 GLY A O   1 
ATOM   788  N  N   . PRO A  1  107 ? 54.348  8.543   55.763 1.00 45.85  ? 120 PRO A N   1 
ATOM   789  C  CA  . PRO A  1  107 ? 54.965  9.859   55.603 1.00 46.00  ? 120 PRO A CA  1 
ATOM   790  C  C   . PRO A  1  107 ? 55.130  10.235  54.134 1.00 45.86  ? 120 PRO A C   1 
ATOM   791  O  O   . PRO A  1  107 ? 55.644  9.458   53.342 1.00 48.65  ? 120 PRO A O   1 
ATOM   792  C  CB  . PRO A  1  107 ? 56.315  9.716   56.322 1.00 47.78  ? 120 PRO A CB  1 
ATOM   793  C  CG  . PRO A  1  107 ? 56.068  8.629   57.337 1.00 48.21  ? 120 PRO A CG  1 
ATOM   794  C  CD  . PRO A  1  107 ? 55.129  7.660   56.645 1.00 46.83  ? 120 PRO A CD  1 
ATOM   795  N  N   . PRO A  1  108 ? 54.683  11.434  53.716 1.00 51.34  ? 121 PRO A N   1 
ATOM   796  C  CA  . PRO A  1  108 ? 54.693  11.808  52.304 1.00 48.24  ? 121 PRO A CA  1 
ATOM   797  C  C   . PRO A  1  108 ? 56.105  11.798  51.728 1.00 46.82  ? 121 PRO A C   1 
ATOM   798  O  O   . PRO A  1  108 ? 57.075  12.043  52.439 1.00 45.33  ? 121 PRO A O   1 
ATOM   799  C  CB  . PRO A  1  108 ? 54.050  13.207  52.285 1.00 53.17  ? 121 PRO A CB  1 
ATOM   800  C  CG  . PRO A  1  108 ? 54.262  13.741  53.702 1.00 61.41  ? 121 PRO A CG  1 
ATOM   801  C  CD  . PRO A  1  108 ? 54.139  12.496  54.577 1.00 57.86  ? 121 PRO A CD  1 
ATOM   802  N  N   . PRO A  1  109 ? 56.269  11.479  50.426 1.00 46.35  ? 122 PRO A N   1 
ATOM   803  C  CA  . PRO A  1  109 ? 57.579  11.557  49.788 1.00 44.34  ? 122 PRO A CA  1 
ATOM   804  C  C   . PRO A  1  109 ? 57.967  13.010  49.529 1.00 44.14  ? 122 PRO A C   1 
ATOM   805  O  O   . PRO A  1  109 ? 57.120  13.896  49.561 1.00 43.60  ? 122 PRO A O   1 
ATOM   806  C  CB  . PRO A  1  109 ? 57.390  10.758  48.497 1.00 42.52  ? 122 PRO A CB  1 
ATOM   807  C  CG  . PRO A  1  109 ? 55.956  10.964  48.159 1.00 47.61  ? 122 PRO A CG  1 
ATOM   808  C  CD  . PRO A  1  109 ? 55.211  11.042  49.499 1.00 45.78  ? 122 PRO A CD  1 
ATOM   809  N  N   . PRO A  1  110 ? 59.260  13.293  49.262 1.00 46.85  ? 123 PRO A N   1 
ATOM   810  C  CA  . PRO A  1  110 ? 59.691  14.628  48.839 1.00 48.01  ? 123 PRO A CA  1 
ATOM   811  C  C   . PRO A  1  110 ? 59.019  15.080  47.545 1.00 45.79  ? 123 PRO A C   1 
ATOM   812  O  O   . PRO A  1  110 ? 59.003  14.342  46.565 1.00 47.64  ? 123 PRO A O   1 
ATOM   813  C  CB  . PRO A  1  110 ? 61.226  14.481  48.656 1.00 47.33  ? 123 PRO A CB  1 
ATOM   814  C  CG  . PRO A  1  110 ? 61.475  12.969  48.559 1.00 47.93  ? 123 PRO A CG  1 
ATOM   815  C  CD  . PRO A  1  110 ? 60.376  12.337  49.388 1.00 47.22  ? 123 PRO A CD  1 
ATOM   816  N  N   . PRO A  1  111 ? 58.434  16.299  47.491 1.00 46.34  ? 124 PRO A N   1 
ATOM   817  C  CA  . PRO A  1  111 ? 57.893  16.837  46.239 1.00 44.87  ? 124 PRO A CA  1 
ATOM   818  C  C   . PRO A  1  111 ? 58.987  16.906  45.179 1.00 42.45  ? 124 PRO A C   1 
ATOM   819  O  O   . PRO A  1  111 ? 60.157  17.058  45.524 1.00 45.80  ? 124 PRO A O   1 
ATOM   820  C  CB  . PRO A  1  111 ? 57.354  18.228  46.628 1.00 46.45  ? 124 PRO A CB  1 
ATOM   821  C  CG  . PRO A  1  111 ? 57.153  18.153  48.119 1.00 49.17  ? 124 PRO A CG  1 
ATOM   822  C  CD  . PRO A  1  111 ? 58.228  17.198  48.638 1.00 50.00  ? 124 PRO A CD  1 
ATOM   823  N  N   . PRO A  1  112 ? 58.678  16.821  43.865 1.00 43.01  ? 125 PRO A N   1 
ATOM   824  C  CA  . PRO A  1  112 ? 57.306  16.770  43.346 1.00 43.88  ? 125 PRO A CA  1 
ATOM   825  C  C   . PRO A  1  112 ? 56.557  15.438  43.397 1.00 42.77  ? 125 PRO A C   1 
ATOM   826  O  O   . PRO A  1  112 ? 55.414  15.377  42.957 1.00 43.47  ? 125 PRO A O   1 
ATOM   827  C  CB  . PRO A  1  112 ? 57.459  17.223  41.871 1.00 45.35  ? 125 PRO A CB  1 
ATOM   828  C  CG  . PRO A  1  112 ? 58.939  17.476  41.660 1.00 46.25  ? 125 PRO A CG  1 
ATOM   829  C  CD  . PRO A  1  112 ? 59.679  16.777  42.792 1.00 45.92  ? 125 PRO A CD  1 
ATOM   830  N  N   . ALA A  1  113 ? 57.182  14.383  43.943 1.00 42.44  ? 126 ALA A N   1 
ATOM   831  C  CA  . ALA A  1  113 ? 56.489  13.122  44.190 1.00 42.33  ? 126 ALA A CA  1 
ATOM   832  C  C   . ALA A  1  113 ? 55.413  13.331  45.251 1.00 41.71  ? 126 ALA A C   1 
ATOM   833  O  O   . ALA A  1  113 ? 55.531  14.224  46.085 1.00 46.01  ? 126 ALA A O   1 
ATOM   834  C  CB  . ALA A  1  113 ? 57.466  12.055  44.618 1.00 41.61  ? 126 ALA A CB  1 
ATOM   835  N  N   . HIS A  1  114 ? 54.384  12.478  45.234 1.00 40.35  ? 127 HIS A N   1 
ATOM   836  C  CA  . HIS A  1  114 ? 53.141  12.759  45.948 1.00 38.61  ? 127 HIS A CA  1 
ATOM   837  C  C   . HIS A  1  114 ? 52.540  11.518  46.622 1.00 38.87  ? 127 HIS A C   1 
ATOM   838  O  O   . HIS A  1  114 ? 51.923  11.652  47.677 1.00 35.43  ? 127 HIS A O   1 
ATOM   839  C  CB  . HIS A  1  114 ? 52.149  13.421  44.991 1.00 38.99  ? 127 HIS A CB  1 
ATOM   840  C  CG  . HIS A  1  114 ? 52.029  12.719  43.679 1.00 40.45  ? 127 HIS A CG  1 
ATOM   841  N  ND1 . HIS A  1  114 ? 51.298  11.564  43.548 1.00 42.31  ? 127 HIS A ND1 1 
ATOM   842  C  CD2 . HIS A  1  114 ? 52.542  12.977  42.468 1.00 40.12  ? 127 HIS A CD2 1 
ATOM   843  C  CE1 . HIS A  1  114 ? 51.350  11.165  42.289 1.00 47.07  ? 127 HIS A CE1 1 
ATOM   844  N  NE2 . HIS A  1  114 ? 52.114  12.003  41.618 1.00 42.87  ? 127 HIS A NE2 1 
ATOM   845  N  N   . ALA A  1  115 ? 52.670  10.331  46.000 1.00 39.95  ? 128 ALA A N   1 
ATOM   846  C  CA  . ALA A  1  115 ? 52.054  9.109   46.504 1.00 37.81  ? 128 ALA A CA  1 
ATOM   847  C  C   . ALA A  1  115 ? 50.559  9.339   46.703 1.00 36.78  ? 128 ALA A C   1 
ATOM   848  O  O   . ALA A  1  115 ? 49.979  8.902   47.694 1.00 36.44  ? 128 ALA A O   1 
ATOM   849  C  CB  . ALA A  1  115 ? 52.704  8.658   47.792 1.00 36.40  ? 128 ALA A CB  1 
ATOM   850  N  N   . GLY A  1  116 ? 49.955  10.028  45.732 1.00 36.04  ? 129 GLY A N   1 
ATOM   851  C  CA  . GLY A  1  116 ? 48.593  10.528  45.820 1.00 38.86  ? 129 GLY A CA  1 
ATOM   852  C  C   . GLY A  1  116 ? 47.574  9.511   45.320 1.00 39.77  ? 129 GLY A C   1 
ATOM   853  O  O   . GLY A  1  116 ? 46.387  9.789   45.387 1.00 42.58  ? 129 GLY A O   1 
ATOM   854  N  N   . GLY A  1  117 ? 48.048  8.363   44.812 1.00 41.53  ? 130 GLY A N   1 
ATOM   855  C  CA  . GLY A  1  117 ? 47.174  7.253   44.475 1.00 37.76  ? 130 GLY A CA  1 
ATOM   856  C  C   . GLY A  1  117 ? 46.749  7.275   43.015 1.00 39.07  ? 130 GLY A C   1 
ATOM   857  O  O   . GLY A  1  117 ? 47.076  8.198   42.271 1.00 35.62  ? 130 GLY A O   1 
ATOM   858  N  N   . LEU A  1  118 ? 45.985  6.246   42.630 1.00 40.19  ? 131 LEU A N   1 
ATOM   859  C  CA  . LEU A  1  118 ? 45.587  6.033   41.249 1.00 40.46  ? 131 LEU A CA  1 
ATOM   860  C  C   . LEU A  1  118 ? 44.685  7.159   40.729 1.00 38.76  ? 131 LEU A C   1 
ATOM   861  O  O   . LEU A  1  118 ? 44.524  7.290   39.517 1.00 35.35  ? 131 LEU A O   1 
ATOM   862  C  CB  . LEU A  1  118 ? 44.899  4.674   41.142 1.00 40.88  ? 131 LEU A CB  1 
ATOM   863  C  CG  . LEU A  1  118 ? 45.767  3.450   41.452 1.00 39.22  ? 131 LEU A CG  1 
ATOM   864  C  CD1 . LEU A  1  118 ? 44.970  2.175   41.186 1.00 41.02  ? 131 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A  1  118 ? 47.077  3.445   40.678 1.00 37.67  ? 131 LEU A CD2 1 
ATOM   866  N  N   . ASN A  1  119 ? 44.115  7.965   41.638 1.00 37.68  ? 132 ASN A N   1 
ATOM   867  C  CA  . ASN A  1  119 ? 43.306  9.115   41.268 1.00 39.62  ? 132 ASN A CA  1 
ATOM   868  C  C   . ASN A  1  119 ? 44.104  10.195  40.540 1.00 38.47  ? 132 ASN A C   1 
ATOM   869  O  O   . ASN A  1  119 ? 43.508  10.983  39.824 1.00 41.16  ? 132 ASN A O   1 
ATOM   870  C  CB  . ASN A  1  119 ? 42.641  9.760   42.478 1.00 40.74  ? 132 ASN A CB  1 
ATOM   871  C  CG  . ASN A  1  119 ? 41.396  9.029   42.922 1.00 42.06  ? 132 ASN A CG  1 
ATOM   872  O  OD1 . ASN A  1  119 ? 41.074  7.948   42.406 1.00 40.37  ? 132 ASN A OD1 1 
ATOM   873  N  ND2 . ASN A  1  119 ? 40.696  9.604   43.887 1.00 43.15  ? 132 ASN A ND2 1 
ATOM   874  N  N   . VAL A  1  120 ? 45.427  10.248  40.720 1.00 37.97  ? 133 VAL A N   1 
ATOM   875  C  CA  . VAL A  1  120 ? 46.224  11.326  40.152 1.00 39.19  ? 133 VAL A CA  1 
ATOM   876  C  C   . VAL A  1  120 ? 46.149  11.305  38.624 1.00 40.00  ? 133 VAL A C   1 
ATOM   877  O  O   . VAL A  1  120 ? 46.459  10.305  37.982 1.00 44.67  ? 133 VAL A O   1 
ATOM   878  C  CB  . VAL A  1  120 ? 47.682  11.283  40.643 1.00 40.24  ? 133 VAL A CB  1 
ATOM   879  C  CG1 . VAL A  1  120 ? 48.567  12.282  39.895 1.00 41.29  ? 133 VAL A CG1 1 
ATOM   880  C  CG2 . VAL A  1  120 ? 47.752  11.527  42.147 1.00 39.37  ? 133 VAL A CG2 1 
ATOM   881  N  N   . HIS A  1  121 ? 45.770  12.455  38.057 1.00 40.46  ? 134 HIS A N   1 
ATOM   882  C  CA  . HIS A  1  121 ? 45.497  12.607  36.636 1.00 43.39  ? 134 HIS A CA  1 
ATOM   883  C  C   . HIS A  1  121 ? 46.762  12.982  35.870 1.00 41.16  ? 134 HIS A C   1 
ATOM   884  O  O   . HIS A  1  121 ? 47.587  13.733  36.372 1.00 41.45  ? 134 HIS A O   1 
ATOM   885  C  CB  . HIS A  1  121 ? 44.448  13.707  36.431 1.00 43.09  ? 134 HIS A CB  1 
ATOM   886  C  CG  . HIS A  1  121 ? 44.195  14.044  35.006 1.00 46.60  ? 134 HIS A CG  1 
ATOM   887  N  ND1 . HIS A  1  121 ? 43.483  13.225  34.156 1.00 48.70  ? 134 HIS A ND1 1 
ATOM   888  C  CD2 . HIS A  1  121 ? 44.583  15.106  34.275 1.00 50.37  ? 134 HIS A CD2 1 
ATOM   889  C  CE1 . HIS A  1  121 ? 43.425  13.793  32.957 1.00 51.96  ? 134 HIS A CE1 1 
ATOM   890  N  NE2 . HIS A  1  121 ? 44.083  14.939  33.009 1.00 48.43  ? 134 HIS A NE2 1 
ATOM   891  N  N   . GLY A  1  122 ? 46.902  12.460  34.646 1.00 44.99  ? 135 GLY A N   1 
ATOM   892  C  CA  . GLY A  1  122 ? 47.748  13.100  33.656 1.00 48.35  ? 135 GLY A CA  1 
ATOM   893  C  C   . GLY A  1  122 ? 48.921  12.245  33.182 1.00 50.49  ? 135 GLY A C   1 
ATOM   894  O  O   . GLY A  1  122 ? 49.430  12.502  32.095 1.00 52.08  ? 135 GLY A O   1 
ATOM   895  N  N   . THR A  1  123 ? 49.376  11.273  33.984 1.00 50.86  ? 136 THR A N   1 
ATOM   896  C  CA  . THR A  1  123 ? 50.454  10.394  33.545 1.00 53.12  ? 136 THR A CA  1 
ATOM   897  C  C   . THR A  1  123 ? 49.962  8.945   33.428 1.00 51.07  ? 136 THR A C   1 
ATOM   898  O  O   . THR A  1  123 ? 50.302  8.287   32.445 1.00 49.54  ? 136 THR A O   1 
ATOM   899  C  CB  . THR A  1  123 ? 51.677  10.529  34.453 1.00 56.36  ? 136 THR A CB  1 
ATOM   900  O  OG1 . THR A  1  123 ? 51.852  11.921  34.714 1.00 53.44  ? 136 THR A OG1 1 
ATOM   901  C  CG2 . THR A  1  123 ? 52.934  9.972   33.805 1.00 55.59  ? 136 THR A CG2 1 
ATOM   902  N  N   . PHE A  1  124 ? 49.195  8.450   34.422 1.00 44.41  ? 137 PHE A N   1 
ATOM   903  C  CA  . PHE A  1  124 ? 48.517  7.160   34.325 1.00 44.62  ? 137 PHE A CA  1 
ATOM   904  C  C   . PHE A  1  124 ? 47.025  7.388   34.031 1.00 44.58  ? 137 PHE A C   1 
ATOM   905  O  O   . PHE A  1  124 ? 46.606  7.271   32.880 1.00 47.68  ? 137 PHE A O   1 
ATOM   906  C  CB  . PHE A  1  124 ? 48.773  6.300   35.568 1.00 42.06  ? 137 PHE A CB  1 
ATOM   907  C  CG  . PHE A  1  124 ? 48.361  4.831   35.499 1.00 42.16  ? 137 PHE A CG  1 
ATOM   908  C  CD1 . PHE A  1  124 ? 47.624  4.314   34.434 1.00 43.73  ? 137 PHE A CD1 1 
ATOM   909  C  CD2 . PHE A  1  124 ? 48.702  3.955   36.527 1.00 43.17  ? 137 PHE A CD2 1 
ATOM   910  C  CE1 . PHE A  1  124 ? 47.258  2.972   34.394 1.00 41.27  ? 137 PHE A CE1 1 
ATOM   911  C  CE2 . PHE A  1  124 ? 48.332  2.611   36.478 1.00 41.75  ? 137 PHE A CE2 1 
ATOM   912  C  CZ  . PHE A  1  124 ? 47.619  2.125   35.412 1.00 41.14  ? 137 PHE A CZ  1 
ATOM   913  N  N   . GLU A  1  125 ? 46.221  7.703   35.055 1.00 41.34  ? 138 GLU A N   1 
ATOM   914  C  CA  . GLU A  1  125 ? 44.794  7.956   34.878 1.00 42.05  ? 138 GLU A CA  1 
ATOM   915  C  C   . GLU A  1  125 ? 44.598  9.038   33.811 1.00 44.22  ? 138 GLU A C   1 
ATOM   916  O  O   . GLU A  1  125 ? 45.290  10.050  33.811 1.00 42.88  ? 138 GLU A O   1 
ATOM   917  C  CB  . GLU A  1  125 ? 44.145  8.387   36.196 1.00 41.50  ? 138 GLU A CB  1 
ATOM   918  C  CG  . GLU A  1  125 ? 42.625  8.545   36.159 1.00 44.93  ? 138 GLU A CG  1 
ATOM   919  C  CD  . GLU A  1  125 ? 42.065  9.719   35.363 1.00 45.44  ? 138 GLU A CD  1 
ATOM   920  O  OE1 . GLU A  1  125 ? 42.689  10.792  35.462 1.00 43.44  ? 138 GLU A OE1 1 
ATOM   921  O  OE2 . GLU A  1  125 ? 41.021  9.585   34.673 1.00 43.03  ? 138 GLU A OE2 1 
ATOM   922  N  N   . GLY A  1  126 ? 43.624  8.832   32.923 1.00 41.18  ? 139 GLY A N   1 
ATOM   923  C  CA  . GLY A  1  126 ? 43.350  9.770   31.843 1.00 41.35  ? 139 GLY A CA  1 
ATOM   924  C  C   . GLY A  1  126 ? 41.906  9.697   31.346 1.00 39.35  ? 139 GLY A C   1 
ATOM   925  O  O   . GLY A  1  126 ? 41.038  9.102   31.990 1.00 37.72  ? 139 GLY A O   1 
ATOM   926  N  N   . ASP A  1  127 ? 41.699  10.273  30.152 1.00 43.73  ? 140 ASP A N   1 
ATOM   927  C  CA  . ASP A  1  127 ? 40.397  10.718  29.684 1.00 39.30  ? 140 ASP A CA  1 
ATOM   928  C  C   . ASP A  1  127 ? 39.708  9.645   28.839 1.00 36.50  ? 140 ASP A C   1 
ATOM   929  O  O   . ASP A  1  127 ? 40.322  8.673   28.416 1.00 38.21  ? 140 ASP A O   1 
ATOM   930  C  CB  . ASP A  1  127 ? 40.548  12.016  28.900 1.00 43.30  ? 140 ASP A CB  1 
ATOM   931  C  CG  . ASP A  1  127 ? 41.132  13.196  29.659 1.00 45.87  ? 140 ASP A CG  1 
ATOM   932  O  OD1 . ASP A  1  127 ? 40.814  13.337  30.860 1.00 42.30  ? 140 ASP A OD1 1 
ATOM   933  O  OD2 . ASP A  1  127 ? 41.890  13.983  29.037 1.00 46.60  ? 140 ASP A OD2 1 
ATOM   934  N  N   . ALA A  1  128 ? 38.417  9.877   28.569 1.00 40.08  ? 141 ALA A N   1 
ATOM   935  C  CA  . ALA A  1  128 ? 37.579  9.048   27.713 1.00 35.98  ? 141 ALA A CA  1 
ATOM   936  C  C   . ALA A  1  128 ? 37.390  7.647   28.290 1.00 34.00  ? 141 ALA A C   1 
ATOM   937  O  O   . ALA A  1  128 ? 37.350  6.675   27.543 1.00 34.05  ? 141 ALA A O   1 
ATOM   938  C  CB  . ALA A  1  128 ? 38.123  9.010   26.294 1.00 38.20  ? 141 ALA A CB  1 
ATOM   939  N  N   . GLY A  1  129 ? 37.230  7.545   29.611 1.00 34.04  ? 142 GLY A N   1 
ATOM   940  C  CA  . GLY A  1  129 ? 36.878  6.282   30.247 1.00 35.41  ? 142 GLY A CA  1 
ATOM   941  C  C   . GLY A  1  129 ? 35.412  5.916   29.994 1.00 36.80  ? 142 GLY A C   1 
ATOM   942  O  O   . GLY A  1  129 ? 34.646  6.729   29.489 1.00 35.06  ? 142 GLY A O   1 
ATOM   943  N  N   . MET A  1  130 ? 35.039  4.684   30.354 1.00 37.86  ? 143 MET A N   1 
ATOM   944  C  CA  . MET A  1  130 ? 33.727  4.142   30.066 1.00 38.52  ? 143 MET A CA  1 
ATOM   945  C  C   . MET A  1  130 ? 32.712  4.585   31.112 1.00 39.83  ? 143 MET A C   1 
ATOM   946  O  O   . MET A  1  130 ? 31.600  4.951   30.740 1.00 39.46  ? 143 MET A O   1 
ATOM   947  C  CB  . MET A  1  130 ? 33.762  2.613   30.031 1.00 42.11  ? 143 MET A CB  1 
ATOM   948  C  CG  . MET A  1  130 ? 34.441  2.052   28.797 1.00 42.44  ? 143 MET A CG  1 
ATOM   949  S  SD  . MET A  1  130 ? 34.625  0.257   28.871 1.00 47.54  ? 143 MET A SD  1 
ATOM   950  C  CE  . MET A  1  130 ? 35.690  0.118   30.310 1.00 46.97  ? 143 MET A CE  1 
ATOM   951  N  N   . THR A  1  131 ? 33.073  4.493   32.403 1.00 38.80  ? 144 THR A N   1 
ATOM   952  C  CA  . THR A  1  131 ? 32.128  4.800   33.469 1.00 37.28  ? 144 THR A CA  1 
ATOM   953  C  C   . THR A  1  131 ? 32.618  5.947   34.346 1.00 37.59  ? 144 THR A C   1 
ATOM   954  O  O   . THR A  1  131 ? 31.920  6.312   35.284 1.00 38.36  ? 144 THR A O   1 
ATOM   955  C  CB  . THR A  1  131 ? 31.823  3.549   34.297 1.00 38.04  ? 144 THR A CB  1 
ATOM   956  O  OG1 . THR A  1  131 ? 32.968  3.215   35.072 1.00 35.87  ? 144 THR A OG1 1 
ATOM   957  C  CG2 . THR A  1  131 ? 31.380  2.390   33.420 1.00 38.81  ? 144 THR A CG2 1 
ATOM   958  N  N   . ARG A  1  132 ? 33.808  6.502   34.060 1.00 39.06  ? 145 ARG A N   1 
ATOM   959  C  CA  . ARG A  1  132 ? 34.316  7.658   34.785 1.00 41.29  ? 145 ARG A CA  1 
ATOM   960  C  C   . ARG A  1  132 ? 34.455  8.845   33.828 1.00 42.26  ? 145 ARG A C   1 
ATOM   961  O  O   . ARG A  1  132 ? 34.801  8.664   32.661 1.00 44.17  ? 145 ARG A O   1 
ATOM   962  C  CB  . ARG A  1  132 ? 35.660  7.338   35.447 1.00 41.02  ? 145 ARG A CB  1 
ATOM   963  C  CG  . ARG A  1  132 ? 35.573  6.759   36.854 1.00 44.69  ? 145 ARG A CG  1 
ATOM   964  C  CD  . ARG A  1  132 ? 34.929  5.378   36.933 1.00 43.59  ? 145 ARG A CD  1 
ATOM   965  N  NE  . ARG A  1  132 ? 34.853  4.926   38.325 1.00 42.69  ? 145 ARG A NE  1 
ATOM   966  C  CZ  . ARG A  1  132 ? 34.130  3.900   38.781 1.00 40.26  ? 145 ARG A CZ  1 
ATOM   967  N  NH1 . ARG A  1  132 ? 34.036  3.716   40.086 1.00 41.87  ? 145 ARG A NH1 1 
ATOM   968  N  NH2 . ARG A  1  132 ? 33.479  3.085   37.961 1.00 38.48  ? 145 ARG A NH2 1 
ATOM   969  N  N   . ALA A  1  133 ? 34.199  10.054  34.348 1.00 38.16  ? 146 ALA A N   1 
ATOM   970  C  CA  . ALA A  1  133 ? 34.277  11.285  33.580 1.00 38.32  ? 146 ALA A CA  1 
ATOM   971  C  C   . ALA A  1  133 ? 35.719  11.794  33.575 1.00 38.95  ? 146 ALA A C   1 
ATOM   972  O  O   . ALA A  1  133 ? 36.496  11.488  34.471 1.00 37.16  ? 146 ALA A O   1 
ATOM   973  N  N   . ASP A  1  134 ? 36.065  12.590  32.559 1.00 40.81  ? 147 ASP A N   1 
ATOM   974  C  CA  . ASP A  1  134 ? 37.372  13.220  32.464 1.00 42.28  ? 147 ASP A CA  1 
ATOM   975  C  C   . ASP A  1  134 ? 37.585  14.153  33.654 1.00 40.36  ? 147 ASP A C   1 
ATOM   976  O  O   . ASP A  1  134 ? 36.643  14.749  34.170 1.00 41.48  ? 147 ASP A O   1 
ATOM   977  C  CB  . ASP A  1  134 ? 37.533  13.983  31.158 1.00 45.09  ? 147 ASP A CB  1 
ATOM   978  C  CG  . ASP A  1  134 ? 37.353  13.170  29.883 1.00 47.42  ? 147 ASP A CG  1 
ATOM   979  O  OD1 . ASP A  1  134 ? 37.011  11.970  29.988 1.00 45.06  ? 147 ASP A OD1 1 
ATOM   980  O  OD2 . ASP A  1  134 ? 37.565  13.740  28.788 1.00 47.00  ? 147 ASP A OD2 1 
ATOM   981  N  N   . GLU A  1  135 ? 38.845  14.271  34.081 1.00 42.20  ? 148 GLU A N   1 
ATOM   982  C  CA  . GLU A  1  135 ? 39.215  15.071  35.241 1.00 43.54  ? 148 GLU A CA  1 
ATOM   983  C  C   . GLU A  1  135 ? 38.817  16.539  35.057 1.00 41.94  ? 148 GLU A C   1 
ATOM   984  O  O   . GLU A  1  135 ? 38.529  17.221  36.034 1.00 42.03  ? 148 GLU A O   1 
ATOM   985  C  CB  . GLU A  1  135 ? 40.718  14.938  35.498 1.00 46.84  ? 148 GLU A CB  1 
ATOM   986  C  CG  . GLU A  1  135 ? 41.203  15.624  36.774 1.00 52.66  ? 148 GLU A CG  1 
ATOM   987  C  CD  . GLU A  1  135 ? 41.668  17.068  36.628 1.00 58.36  ? 148 GLU A CD  1 
ATOM   988  O  OE1 . GLU A  1  135 ? 41.646  17.615  35.500 1.00 60.72  ? 148 GLU A OE1 1 
ATOM   989  O  OE2 . GLU A  1  135 ? 42.072  17.651  37.657 1.00 62.41  ? 148 GLU A OE2 1 
ATOM   990  N  N   . PHE A  1  136 ? 38.817  17.027  33.812 1.00 42.80  ? 149 PHE A N   1 
ATOM   991  C  CA  . PHE A  1  136 ? 38.460  18.405  33.522 1.00 46.20  ? 149 PHE A CA  1 
ATOM   992  C  C   . PHE A  1  136 ? 37.083  18.740  34.084 1.00 46.02  ? 149 PHE A C   1 
ATOM   993  O  O   . PHE A  1  136 ? 36.878  19.874  34.507 1.00 46.53  ? 149 PHE A O   1 
ATOM   994  C  CB  . PHE A  1  136 ? 38.458  18.696  32.019 1.00 52.11  ? 149 PHE A CB  1 
ATOM   995  C  CG  . PHE A  1  136 ? 37.990  20.105  31.679 1.00 56.13  ? 149 PHE A CG  1 
ATOM   996  C  CD1 . PHE A  1  136 ? 38.822  21.196  31.898 1.00 57.80  ? 149 PHE A CD1 1 
ATOM   997  C  CD2 . PHE A  1  136 ? 36.722  20.332  31.152 1.00 59.22  ? 149 PHE A CD2 1 
ATOM   998  C  CE1 . PHE A  1  136 ? 38.395  22.479  31.595 1.00 56.03  ? 149 PHE A CE1 1 
ATOM   999  C  CE2 . PHE A  1  136 ? 36.294  21.616  30.860 1.00 58.79  ? 149 PHE A CE2 1 
ATOM   1000 C  CZ  . PHE A  1  136 ? 37.134  22.686  31.080 1.00 56.22  ? 149 PHE A CZ  1 
ATOM   1001 N  N   . PHE A  1  137 ? 36.159  17.767  34.103 1.00 44.57  ? 150 PHE A N   1 
ATOM   1002 C  CA  . PHE A  1  137 ? 34.791  18.013  34.543 1.00 44.01  ? 150 PHE A CA  1 
ATOM   1003 C  C   . PHE A  1  137 ? 34.666  17.957  36.066 1.00 46.17  ? 150 PHE A C   1 
ATOM   1004 O  O   . PHE A  1  137 ? 33.600  18.251  36.586 1.00 43.62  ? 150 PHE A O   1 
ATOM   1005 C  CB  . PHE A  1  137 ? 33.849  17.017  33.863 1.00 44.51  ? 150 PHE A CB  1 
ATOM   1006 C  CG  . PHE A  1  137 ? 33.910  17.065  32.341 1.00 46.41  ? 150 PHE A CG  1 
ATOM   1007 C  CD1 . PHE A  1  137 ? 33.766  18.271  31.660 1.00 50.17  ? 150 PHE A CD1 1 
ATOM   1008 C  CD2 . PHE A  1  137 ? 34.150  15.919  31.597 1.00 44.47  ? 150 PHE A CD2 1 
ATOM   1009 C  CE1 . PHE A  1  137 ? 33.836  18.323  30.275 1.00 46.56  ? 150 PHE A CE1 1 
ATOM   1010 C  CE2 . PHE A  1  137 ? 34.211  15.973  30.210 1.00 47.20  ? 150 PHE A CE2 1 
ATOM   1011 C  CZ  . PHE A  1  137 ? 34.056  17.177  29.550 1.00 47.77  ? 150 PHE A CZ  1 
ATOM   1012 N  N   . GLY A  1  138 ? 35.739  17.585  36.782 1.00 47.26  ? 151 GLY A N   1 
ATOM   1013 C  CA  . GLY A  1  138 ? 35.808  17.797  38.222 1.00 45.28  ? 151 GLY A CA  1 
ATOM   1014 C  C   . GLY A  1  138 ? 35.836  16.509  39.053 1.00 46.82  ? 151 GLY A C   1 
ATOM   1015 O  O   . GLY A  1  138 ? 35.990  16.592  40.265 1.00 44.43  ? 151 GLY A O   1 
ATOM   1016 N  N   . ASP A  1  139 ? 35.669  15.329  38.433 1.00 44.94  ? 152 ASP A N   1 
ATOM   1017 C  CA  . ASP A  1  139 ? 35.670  14.080  39.188 1.00 44.73  ? 152 ASP A CA  1 
ATOM   1018 C  C   . ASP A  1  139 ? 36.048  12.918  38.275 1.00 42.48  ? 152 ASP A C   1 
ATOM   1019 O  O   . ASP A  1  139 ? 35.223  12.480  37.473 1.00 37.55  ? 152 ASP A O   1 
ATOM   1020 C  CB  . ASP A  1  139 ? 34.326  13.814  39.850 1.00 46.90  ? 152 ASP A CB  1 
ATOM   1021 C  CG  . ASP A  1  139 ? 34.244  12.544  40.690 1.00 52.84  ? 152 ASP A CG  1 
ATOM   1022 O  OD1 . ASP A  1  139 ? 35.198  11.740  40.646 1.00 50.49  ? 152 ASP A OD1 1 
ATOM   1023 O  OD2 . ASP A  1  139 ? 33.228  12.376  41.403 1.00 52.44  ? 152 ASP A OD2 1 
ATOM   1024 N  N   . ASN A  1  140 ? 37.278  12.407  38.441 1.00 39.73  ? 153 ASN A N   1 
ATOM   1025 C  CA  . ASN A  1  140 ? 37.826  11.405  37.538 1.00 42.32  ? 153 ASN A CA  1 
ATOM   1026 C  C   . ASN A  1  140 ? 37.737  9.995   38.137 1.00 42.37  ? 153 ASN A C   1 
ATOM   1027 O  O   . ASN A  1  140 ? 38.247  9.051   37.534 1.00 42.15  ? 153 ASN A O   1 
ATOM   1028 C  CB  . ASN A  1  140 ? 39.271  11.727  37.161 1.00 42.10  ? 153 ASN A CB  1 
ATOM   1029 C  CG  . ASN A  1  140 ? 40.220  11.606  38.327 1.00 41.00  ? 153 ASN A CG  1 
ATOM   1030 O  OD1 . ASN A  1  140 ? 39.790  11.498  39.477 1.00 45.48  ? 153 ASN A OD1 1 
ATOM   1031 N  ND2 . ASN A  1  140 ? 41.514  11.626  38.061 1.00 41.22  ? 153 ASN A ND2 1 
ATOM   1032 N  N   . HIS A  1  141 ? 37.096  9.854   39.307 1.00 39.40  ? 154 HIS A N   1 
ATOM   1033 C  CA  . HIS A  1  141 ? 37.174  8.620   40.083 1.00 42.25  ? 154 HIS A CA  1 
ATOM   1034 C  C   . HIS A  1  141 ? 35.802  7.990   40.361 1.00 41.57  ? 154 HIS A C   1 
ATOM   1035 O  O   . HIS A  1  141 ? 35.699  6.765   40.411 1.00 37.26  ? 154 HIS A O   1 
ATOM   1036 C  CB  . HIS A  1  141 ? 37.967  8.845   41.375 1.00 43.90  ? 154 HIS A CB  1 
ATOM   1037 C  CG  . HIS A  1  141 ? 37.477  9.978   42.205 1.00 48.53  ? 154 HIS A CG  1 
ATOM   1038 N  ND1 . HIS A  1  141 ? 38.033  11.233  42.072 1.00 49.05  ? 154 HIS A ND1 1 
ATOM   1039 C  CD2 . HIS A  1  141 ? 36.492  10.104  43.107 1.00 48.23  ? 154 HIS A CD2 1 
ATOM   1040 C  CE1 . HIS A  1  141 ? 37.414  12.072  42.886 1.00 50.31  ? 154 HIS A CE1 1 
ATOM   1041 N  NE2 . HIS A  1  141 ? 36.485  11.401  43.532 1.00 50.26  ? 154 HIS A NE2 1 
ATOM   1042 N  N   . SER A  1  142 ? 34.758  8.808   40.563 1.00 40.31  ? 155 SER A N   1 
ATOM   1043 C  CA  . SER A  1  142 ? 33.427  8.302   40.873 1.00 41.12  ? 155 SER A CA  1 
ATOM   1044 C  C   . SER A  1  142 ? 32.772  7.666   39.653 1.00 38.03  ? 155 SER A C   1 
ATOM   1045 O  O   . SER A  1  142 ? 32.963  8.112   38.524 1.00 39.00  ? 155 SER A O   1 
ATOM   1046 C  CB  . SER A  1  142 ? 32.529  9.389   41.421 1.00 40.44  ? 155 SER A CB  1 
ATOM   1047 O  OG  . SER A  1  142 ? 33.051  9.923   42.628 1.00 47.15  ? 155 SER A OG  1 
ATOM   1048 N  N   . PHE A  1  143 ? 31.933  6.659   39.909 1.00 38.48  ? 156 PHE A N   1 
ATOM   1049 C  CA  . PHE A  1  143 ? 31.020  6.156   38.893 1.00 40.77  ? 156 PHE A CA  1 
ATOM   1050 C  C   . PHE A  1  143 ? 30.097  7.279   38.410 1.00 39.62  ? 156 PHE A C   1 
ATOM   1051 O  O   . PHE A  1  143 ? 29.644  8.085   39.210 1.00 40.00  ? 156 PHE A O   1 
ATOM   1052 C  CB  . PHE A  1  143 ? 30.230  4.980   39.472 1.00 38.87  ? 156 PHE A CB  1 
ATOM   1053 C  CG  . PHE A  1  143 ? 29.155  4.425   38.551 1.00 35.27  ? 156 PHE A CG  1 
ATOM   1054 C  CD1 . PHE A  1  143 ? 29.460  3.454   37.607 1.00 35.02  ? 156 PHE A CD1 1 
ATOM   1055 C  CD2 . PHE A  1  143 ? 27.846  4.881   38.633 1.00 36.09  ? 156 PHE A CD2 1 
ATOM   1056 C  CE1 . PHE A  1  143 ? 28.475  2.943   36.773 1.00 36.86  ? 156 PHE A CE1 1 
ATOM   1057 C  CE2 . PHE A  1  143 ? 26.865  4.368   37.791 1.00 37.02  ? 156 PHE A CE2 1 
ATOM   1058 C  CZ  . PHE A  1  143 ? 27.181  3.403   36.864 1.00 33.90  ? 156 PHE A CZ  1 
ATOM   1059 N  N   . ASN A  1  144 ? 29.828  7.304   37.099 1.00 38.04  ? 157 ASN A N   1 
ATOM   1060 C  CA  . ASN A  1  144 ? 29.009  8.323   36.459 1.00 40.75  ? 157 ASN A CA  1 
ATOM   1061 C  C   . ASN A  1  144 ? 27.866  7.633   35.719 1.00 36.84  ? 157 ASN A C   1 
ATOM   1062 O  O   . ASN A  1  144 ? 28.103  6.905   34.754 1.00 40.36  ? 157 ASN A O   1 
ATOM   1063 C  CB  . ASN A  1  144 ? 29.886  9.173   35.550 1.00 42.94  ? 157 ASN A CB  1 
ATOM   1064 C  CG  . ASN A  1  144 ? 29.137  10.197  34.722 1.00 46.20  ? 157 ASN A CG  1 
ATOM   1065 O  OD1 . ASN A  1  144 ? 28.115  9.881   34.100 1.00 45.16  ? 157 ASN A OD1 1 
ATOM   1066 N  ND2 . ASN A  1  144 ? 29.659  11.419  34.659 1.00 52.80  ? 157 ASN A ND2 1 
ATOM   1067 N  N   . GLN A  1  145 ? 26.632  7.845   36.189 1.00 36.99  ? 158 GLN A N   1 
ATOM   1068 C  CA  . GLN A  1  145 ? 25.471  7.116   35.688 1.00 38.02  ? 158 GLN A CA  1 
ATOM   1069 C  C   . GLN A  1  145 ? 25.211  7.469   34.221 1.00 37.58  ? 158 GLN A C   1 
ATOM   1070 O  O   . GLN A  1  145 ? 24.848  6.593   33.432 1.00 39.19  ? 158 GLN A O   1 
ATOM   1071 C  CB  . GLN A  1  145 ? 24.256  7.383   36.581 1.00 39.47  ? 158 GLN A CB  1 
ATOM   1072 C  CG  . GLN A  1  145 ? 22.991  6.598   36.221 1.00 39.26  ? 158 GLN A CG  1 
ATOM   1073 C  CD  . GLN A  1  145 ? 23.140  5.092   36.334 1.00 42.26  ? 158 GLN A CD  1 
ATOM   1074 O  OE1 . GLN A  1  145 ? 23.601  4.559   37.349 1.00 44.69  ? 158 GLN A OE1 1 
ATOM   1075 N  NE2 . GLN A  1  145 ? 22.718  4.374   35.303 1.00 42.59  ? 158 GLN A NE2 1 
ATOM   1076 N  N   . THR A  1  146 ? 25.398  8.743   33.855 1.00 36.74  ? 159 THR A N   1 
ATOM   1077 C  CA  . THR A  1  146 ? 25.168  9.188   32.484 1.00 40.34  ? 159 THR A CA  1 
ATOM   1078 C  C   . THR A  1  146 ? 26.063  8.397   31.531 1.00 40.34  ? 159 THR A C   1 
ATOM   1079 O  O   . THR A  1  146 ? 25.608  7.979   30.469 1.00 39.95  ? 159 THR A O   1 
ATOM   1080 C  CB  . THR A  1  146 ? 25.410  10.693  32.345 1.00 43.33  ? 159 THR A CB  1 
ATOM   1081 O  OG1 . THR A  1  146 ? 24.505  11.319  33.245 1.00 43.53  ? 159 THR A OG1 1 
ATOM   1082 C  CG2 . THR A  1  146 ? 25.133  11.218  30.944 1.00 44.97  ? 159 THR A CG2 1 
ATOM   1083 N  N   . LEU A  1  147 ? 27.325  8.177   31.924 1.00 36.64  ? 160 LEU A N   1 
ATOM   1084 C  CA  . LEU A  1  147 ? 28.256  7.442   31.090 1.00 34.63  ? 160 LEU A CA  1 
ATOM   1085 C  C   . LEU A  1  147 ? 27.879  5.966   31.044 1.00 34.49  ? 160 LEU A C   1 
ATOM   1086 O  O   . LEU A  1  147 ? 28.007  5.324   29.997 1.00 36.21  ? 160 LEU A O   1 
ATOM   1087 C  CB  . LEU A  1  147 ? 29.689  7.647   31.576 1.00 36.17  ? 160 LEU A CB  1 
ATOM   1088 C  CG  . LEU A  1  147 ? 30.290  9.019   31.275 1.00 38.18  ? 160 LEU A CG  1 
ATOM   1089 C  CD1 . LEU A  1  147 ? 31.712  9.108   31.794 1.00 40.10  ? 160 LEU A CD1 1 
ATOM   1090 C  CD2 . LEU A  1  147 ? 30.246  9.331   29.788 1.00 35.86  ? 160 LEU A CD2 1 
ATOM   1091 N  N   . PHE A  1  148 ? 27.404  5.431   32.169 1.00 34.89  ? 161 PHE A N   1 
ATOM   1092 C  CA  . PHE A  1  148 ? 26.978  4.041   32.198 1.00 35.79  ? 161 PHE A CA  1 
ATOM   1093 C  C   . PHE A  1  148 ? 25.727  3.870   31.329 1.00 36.34  ? 161 PHE A C   1 
ATOM   1094 O  O   . PHE A  1  148 ? 25.557  2.831   30.692 1.00 38.31  ? 161 PHE A O   1 
ATOM   1095 C  CB  . PHE A  1  148 ? 26.777  3.567   33.641 1.00 34.97  ? 161 PHE A CB  1 
ATOM   1096 C  CG  . PHE A  1  148 ? 26.400  2.097   33.710 1.00 35.86  ? 161 PHE A CG  1 
ATOM   1097 C  CD1 . PHE A  1  148 ? 27.373  1.117   33.566 1.00 38.27  ? 161 PHE A CD1 1 
ATOM   1098 C  CD2 . PHE A  1  148 ? 25.074  1.698   33.869 1.00 36.19  ? 161 PHE A CD2 1 
ATOM   1099 C  CE1 . PHE A  1  148 ? 27.032  -0.226  33.585 1.00 38.14  ? 161 PHE A CE1 1 
ATOM   1100 C  CE2 . PHE A  1  148 ? 24.741  0.357   33.881 1.00 36.74  ? 161 PHE A CE2 1 
ATOM   1101 C  CZ  . PHE A  1  148 ? 25.715  -0.600  33.737 1.00 36.42  ? 161 PHE A CZ  1 
ATOM   1102 N  N   . ASP A  1  149 ? 24.870  4.896   31.277 1.00 38.43  ? 162 ASP A N   1 
ATOM   1103 C  CA  . ASP A  1  149 ? 23.708  4.883   30.390 1.00 41.17  ? 162 ASP A CA  1 
ATOM   1104 C  C   . ASP A  1  149 ? 24.150  4.765   28.927 1.00 40.88  ? 162 ASP A C   1 
ATOM   1105 O  O   . ASP A  1  149 ? 23.506  4.059   28.154 1.00 35.14  ? 162 ASP A O   1 
ATOM   1106 C  CB  . ASP A  1  149 ? 22.828  6.109   30.609 1.00 37.98  ? 162 ASP A CB  1 
ATOM   1107 C  CG  . ASP A  1  149 ? 22.110  6.166   31.948 1.00 42.79  ? 162 ASP A CG  1 
ATOM   1108 O  OD1 . ASP A  1  149 ? 21.892  5.092   32.545 1.00 48.28  ? 162 ASP A OD1 1 
ATOM   1109 O  OD2 . ASP A  1  149 ? 21.796  7.286   32.391 1.00 48.88  ? 162 ASP A OD2 1 
ATOM   1110 N  N   . LYS A  1  150 ? 25.251  5.442   28.562 1.00 41.90  ? 163 LYS A N   1 
ATOM   1111 C  CA  . LYS A  1  150 ? 25.824  5.328   27.225 1.00 42.55  ? 163 LYS A CA  1 
ATOM   1112 C  C   . LYS A  1  150 ? 26.358  3.913   27.004 1.00 41.93  ? 163 LYS A C   1 
ATOM   1113 O  O   . LYS A  1  150 ? 26.176  3.341   25.934 1.00 41.08  ? 163 LYS A O   1 
ATOM   1114 C  CB  . LYS A  1  150 ? 26.925  6.371   26.996 1.00 45.86  ? 163 LYS A CB  1 
ATOM   1115 C  CG  . LYS A  1  150 ? 27.445  6.502   25.563 1.00 44.58  ? 163 LYS A CG  1 
ATOM   1116 C  CD  . LYS A  1  150 ? 28.550  7.535   25.431 1.00 48.80  ? 163 LYS A CD  1 
ATOM   1117 C  CE  . LYS A  1  150 ? 29.164  7.636   24.070 1.00 49.64  ? 163 LYS A CE  1 
ATOM   1118 N  NZ  . LYS A  1  150 ? 28.631  8.779   23.334 1.00 51.30  ? 163 LYS A NZ  1 
ATOM   1119 N  N   . PHE A  1  151 ? 27.008  3.337   28.026 1.00 42.14  ? 164 PHE A N   1 
ATOM   1120 C  CA  . PHE A  1  151 ? 27.470  1.956   27.966 1.00 39.87  ? 164 PHE A CA  1 
ATOM   1121 C  C   . PHE A  1  151 ? 26.294  1.038   27.636 1.00 36.42  ? 164 PHE A C   1 
ATOM   1122 O  O   . PHE A  1  151 ? 26.413  0.149   26.799 1.00 37.12  ? 164 PHE A O   1 
ATOM   1123 C  CB  . PHE A  1  151 ? 28.129  1.600   29.303 1.00 40.13  ? 164 PHE A CB  1 
ATOM   1124 C  CG  . PHE A  1  151 ? 28.746  0.215   29.431 1.00 39.68  ? 164 PHE A CG  1 
ATOM   1125 C  CD1 . PHE A  1  151 ? 27.980  -0.879  29.815 1.00 36.41  ? 164 PHE A CD1 1 
ATOM   1126 C  CD2 . PHE A  1  151 ? 30.114  0.028   29.236 1.00 39.69  ? 164 PHE A CD2 1 
ATOM   1127 C  CE1 . PHE A  1  151 ? 28.561  -2.130  29.957 1.00 37.89  ? 164 PHE A CE1 1 
ATOM   1128 C  CE2 . PHE A  1  151 ? 30.689  -1.226  29.374 1.00 38.07  ? 164 PHE A CE2 1 
ATOM   1129 C  CZ  . PHE A  1  151 ? 29.916  -2.302  29.735 1.00 36.95  ? 164 PHE A CZ  1 
ATOM   1130 N  N   . VAL A  1  152 ? 25.166  1.246   28.318 1.00 39.93  ? 165 VAL A N   1 
ATOM   1131 C  CA  . VAL A  1  152 ? 23.965  0.441   28.109 1.00 38.40  ? 165 VAL A CA  1 
ATOM   1132 C  C   . VAL A  1  152 ? 23.429  0.693   26.699 1.00 37.13  ? 165 VAL A C   1 
ATOM   1133 O  O   . VAL A  1  152 ? 23.106  -0.237  25.969 1.00 32.75  ? 165 VAL A O   1 
ATOM   1134 C  CB  . VAL A  1  152 ? 22.893  0.711   29.186 1.00 38.29  ? 165 VAL A CB  1 
ATOM   1135 C  CG1 . VAL A  1  152 ? 21.591  -0.017  28.896 1.00 42.14  ? 165 VAL A CG1 1 
ATOM   1136 C  CG2 . VAL A  1  152 ? 23.372  0.330   30.580 1.00 38.32  ? 165 VAL A CG2 1 
ATOM   1137 N  N   . ASP A  1  153 ? 23.349  1.963   26.310 1.00 38.57  ? 166 ASP A N   1 
ATOM   1138 C  CA  . ASP A  1  153 ? 22.857  2.317   24.985 1.00 39.81  ? 166 ASP A CA  1 
ATOM   1139 C  C   . ASP A  1  153 ? 23.667  1.586   23.910 1.00 40.79  ? 166 ASP A C   1 
ATOM   1140 O  O   . ASP A  1  153 ? 23.099  0.953   23.023 1.00 38.81  ? 166 ASP A O   1 
ATOM   1141 C  CB  . ASP A  1  153 ? 22.851  3.824   24.799 1.00 42.29  ? 166 ASP A CB  1 
ATOM   1142 C  CG  . ASP A  1  153 ? 22.288  4.314   23.475 1.00 45.10  ? 166 ASP A CG  1 
ATOM   1143 O  OD1 . ASP A  1  153 ? 21.156  3.910   23.138 1.00 43.64  ? 166 ASP A OD1 1 
ATOM   1144 O  OD2 . ASP A  1  153 ? 22.996  5.082   22.794 1.00 44.57  ? 166 ASP A OD2 1 
ATOM   1145 N  N   . PHE A  1  154 ? 25.000  1.666   23.994 1.00 37.58  ? 167 PHE A N   1 
ATOM   1146 C  CA  . PHE A  1  154 ? 25.849  1.096   22.967 1.00 38.58  ? 167 PHE A CA  1 
ATOM   1147 C  C   . PHE A  1  154 ? 25.734  -0.424  22.977 1.00 37.47  ? 167 PHE A C   1 
ATOM   1148 O  O   . PHE A  1  154 ? 25.760  -1.043  21.915 1.00 36.48  ? 167 PHE A O   1 
ATOM   1149 C  CB  . PHE A  1  154 ? 27.296  1.570   23.106 1.00 38.57  ? 167 PHE A CB  1 
ATOM   1150 C  CG  . PHE A  1  154 ? 27.575  2.862   22.351 1.00 40.36  ? 167 PHE A CG  1 
ATOM   1151 C  CD1 . PHE A  1  154 ? 26.870  4.028   22.627 1.00 42.10  ? 167 PHE A CD1 1 
ATOM   1152 C  CD2 . PHE A  1  154 ? 28.527  2.892   21.339 1.00 41.91  ? 167 PHE A CD2 1 
ATOM   1153 C  CE1 . PHE A  1  154 ? 27.137  5.200   21.935 1.00 43.39  ? 167 PHE A CE1 1 
ATOM   1154 C  CE2 . PHE A  1  154 ? 28.783  4.062   20.644 1.00 45.02  ? 167 PHE A CE2 1 
ATOM   1155 C  CZ  . PHE A  1  154 ? 28.083  5.213   20.937 1.00 44.47  ? 167 PHE A CZ  1 
ATOM   1156 N  N   . SER A  1  155 ? 25.598  -1.012  24.171 1.00 35.27  ? 168 SER A N   1 
ATOM   1157 C  CA  . SER A  1  155 ? 25.358  -2.443  24.300 1.00 38.58  ? 168 SER A CA  1 
ATOM   1158 C  C   . SER A  1  155 ? 24.047  -2.841  23.610 1.00 39.57  ? 168 SER A C   1 
ATOM   1159 O  O   . SER A  1  155 ? 23.961  -3.901  23.006 1.00 42.39  ? 168 SER A O   1 
ATOM   1160 C  CB  . SER A  1  155 ? 25.348  -2.862  25.754 1.00 37.01  ? 168 SER A CB  1 
ATOM   1161 O  OG  . SER A  1  155 ? 26.605  -2.618  26.365 1.00 40.36  ? 168 SER A OG  1 
ATOM   1162 N  N   . ASN A  1  156 ? 23.013  -2.003  23.734 1.00 39.82  ? 169 ASN A N   1 
ATOM   1163 C  CA  . ASN A  1  156 ? 21.747  -2.259  23.067 1.00 38.66  ? 169 ASN A CA  1 
ATOM   1164 C  C   . ASN A  1  156 ? 21.913  -2.151  21.555 1.00 40.64  ? 169 ASN A C   1 
ATOM   1165 O  O   . ASN A  1  156 ? 21.384  -2.975  20.823 1.00 38.55  ? 169 ASN A O   1 
ATOM   1166 C  CB  . ASN A  1  156 ? 20.667  -1.289  23.519 1.00 38.67  ? 169 ASN A CB  1 
ATOM   1167 C  CG  . ASN A  1  156 ? 20.218  -1.516  24.941 1.00 37.60  ? 169 ASN A CG  1 
ATOM   1168 O  OD1 . ASN A  1  156 ? 20.312  -2.626  25.476 1.00 40.67  ? 169 ASN A OD1 1 
ATOM   1169 N  ND2 . ASN A  1  156 ? 19.669  -0.476  25.535 1.00 38.90  ? 169 ASN A ND2 1 
ATOM   1170 N  N   . ARG A  1  157 ? 22.645  -1.128  21.091 1.00 41.08  ? 170 ARG A N   1 
ATOM   1171 C  CA  . ARG A  1  157 ? 22.710  -0.820  19.671 1.00 42.56  ? 170 ARG A CA  1 
ATOM   1172 C  C   . ARG A  1  157 ? 23.583  -1.823  18.922 1.00 45.71  ? 170 ARG A C   1 
ATOM   1173 O  O   . ARG A  1  157 ? 23.321  -2.086  17.749 1.00 50.88  ? 170 ARG A O   1 
ATOM   1174 C  CB  . ARG A  1  157 ? 23.207  0.613   19.461 1.00 42.08  ? 170 ARG A CB  1 
ATOM   1175 C  CG  . ARG A  1  157 ? 22.161  1.634   19.879 1.00 43.67  ? 170 ARG A CG  1 
ATOM   1176 C  CD  . ARG A  1  157 ? 22.772  2.990   20.163 1.00 43.91  ? 170 ARG A CD  1 
ATOM   1177 N  NE  . ARG A  1  157 ? 23.567  3.489   19.039 1.00 45.47  ? 170 ARG A NE  1 
ATOM   1178 C  CZ  . ARG A  1  157 ? 24.208  4.640   19.043 1.00 47.20  ? 170 ARG A CZ  1 
ATOM   1179 N  NH1 . ARG A  1  157 ? 24.956  4.971   18.012 1.00 53.30  ? 170 ARG A NH1 1 
ATOM   1180 N  NH2 . ARG A  1  157 ? 24.116  5.458   20.077 1.00 49.36  ? 170 ARG A NH2 1 
ATOM   1181 N  N   . TYR A  1  158 ? 24.606  -2.379  19.590 1.00 46.88  ? 171 TYR A N   1 
ATOM   1182 C  CA  . TYR A  1  158 ? 25.644  -3.129  18.891 1.00 44.60  ? 171 TYR A CA  1 
ATOM   1183 C  C   . TYR A  1  158 ? 25.876  -4.524  19.469 1.00 44.43  ? 171 TYR A C   1 
ATOM   1184 O  O   . TYR A  1  158 ? 26.578  -5.308  18.842 1.00 47.77  ? 171 TYR A O   1 
ATOM   1185 C  CB  . TYR A  1  158 ? 26.967  -2.358  18.903 1.00 43.38  ? 171 TYR A CB  1 
ATOM   1186 C  CG  . TYR A  1  158 ? 26.869  -0.998  18.230 1.00 43.62  ? 171 TYR A CG  1 
ATOM   1187 C  CD1 . TYR A  1  158 ? 26.677  -0.893  16.856 1.00 48.38  ? 171 TYR A CD1 1 
ATOM   1188 C  CD2 . TYR A  1  158 ? 26.948  0.178   18.966 1.00 45.41  ? 171 TYR A CD2 1 
ATOM   1189 C  CE1 . TYR A  1  158 ? 26.550  0.339   16.238 1.00 48.50  ? 171 TYR A CE1 1 
ATOM   1190 C  CE2 . TYR A  1  158 ? 26.843  1.417   18.357 1.00 48.39  ? 171 TYR A CE2 1 
ATOM   1191 C  CZ  . TYR A  1  158 ? 26.640  1.496   16.992 1.00 51.74  ? 171 TYR A CZ  1 
ATOM   1192 O  OH  . TYR A  1  158 ? 26.510  2.713   16.391 1.00 60.00  ? 171 TYR A OH  1 
ATOM   1193 N  N   . GLY A  1  159 ? 25.307  -4.851  20.637 1.00 41.68  ? 172 GLY A N   1 
ATOM   1194 C  CA  . GLY A  1  159 ? 25.637  -6.103  21.300 1.00 39.17  ? 172 GLY A CA  1 
ATOM   1195 C  C   . GLY A  1  159 ? 24.422  -6.907  21.758 1.00 41.43  ? 172 GLY A C   1 
ATOM   1196 O  O   . GLY A  1  159 ? 24.554  -7.808  22.585 1.00 43.56  ? 172 GLY A O   1 
ATOM   1197 N  N   . GLY A  1  160 ? 23.237  -6.605  21.223 1.00 42.46  ? 173 GLY A N   1 
ATOM   1198 C  CA  . GLY A  1  160 ? 22.054  -7.373  21.573 1.00 42.55  ? 173 GLY A CA  1 
ATOM   1199 C  C   . GLY A  1  160 ? 21.619  -7.125  23.019 1.00 44.29  ? 173 GLY A C   1 
ATOM   1200 O  O   . GLY A  1  160 ? 20.889  -7.935  23.588 1.00 40.39  ? 173 GLY A O   1 
ATOM   1201 N  N   . GLY A  1  161 ? 22.062  -6.004  23.604 1.00 41.98  ? 174 GLY A N   1 
ATOM   1202 C  CA  . GLY A  1  161 ? 21.774  -5.687  24.997 1.00 45.72  ? 174 GLY A CA  1 
ATOM   1203 C  C   . GLY A  1  161 ? 22.877  -6.142  25.957 1.00 43.26  ? 174 GLY A C   1 
ATOM   1204 O  O   . GLY A  1  161 ? 22.716  -6.017  27.169 1.00 45.23  ? 174 GLY A O   1 
ATOM   1205 N  N   . PHE A  1  162 ? 23.995  -6.640  25.403 1.00 41.91  ? 175 PHE A N   1 
ATOM   1206 C  CA  . PHE A  1  162 ? 25.144  -7.102  26.169 1.00 39.00  ? 175 PHE A CA  1 
ATOM   1207 C  C   . PHE A  1  162 ? 26.398  -6.389  25.671 1.00 40.26  ? 175 PHE A C   1 
ATOM   1208 O  O   . PHE A  1  162 ? 26.426  -5.897  24.547 1.00 37.02  ? 175 PHE A O   1 
ATOM   1209 C  CB  . PHE A  1  162 ? 25.321  -8.612  25.989 1.00 39.83  ? 175 PHE A CB  1 
ATOM   1210 C  CG  . PHE A  1  162 ? 24.143  -9.457  26.446 1.00 41.39  ? 175 PHE A CG  1 
ATOM   1211 C  CD1 . PHE A  1  162 ? 23.044  -9.683  25.612 1.00 42.38  ? 175 PHE A CD1 1 
ATOM   1212 C  CD2 . PHE A  1  162 ? 24.132  -10.011 27.718 1.00 41.13  ? 175 PHE A CD2 1 
ATOM   1213 C  CE1 . PHE A  1  162 ? 21.973  -10.445 26.049 1.00 41.84  ? 175 PHE A CE1 1 
ATOM   1214 C  CE2 . PHE A  1  162 ? 23.051  -10.769 28.153 1.00 40.56  ? 175 PHE A CE2 1 
ATOM   1215 C  CZ  . PHE A  1  162 ? 21.979  -10.987 27.321 1.00 43.06  ? 175 PHE A CZ  1 
ATOM   1216 N  N   . TYR A  1  163 ? 27.433  -6.326  26.514 1.00 37.72  ? 176 TYR A N   1 
ATOM   1217 C  CA  . TYR A  1  163 ? 28.705  -5.747  26.115 1.00 36.00  ? 176 TYR A CA  1 
ATOM   1218 C  C   . TYR A  1  163 ? 29.576  -6.858  25.546 1.00 36.47  ? 176 TYR A C   1 
ATOM   1219 O  O   . TYR A  1  163 ? 29.876  -7.823  26.245 1.00 41.82  ? 176 TYR A O   1 
ATOM   1220 C  CB  . TYR A  1  163 ? 29.390  -5.052  27.295 1.00 37.69  ? 176 TYR A CB  1 
ATOM   1221 C  CG  . TYR A  1  163 ? 30.653  -4.272  26.963 1.00 37.95  ? 176 TYR A CG  1 
ATOM   1222 C  CD1 . TYR A  1  163 ? 30.591  -2.996  26.428 1.00 38.93  ? 176 TYR A CD1 1 
ATOM   1223 C  CD2 . TYR A  1  163 ? 31.909  -4.798  27.230 1.00 38.42  ? 176 TYR A CD2 1 
ATOM   1224 C  CE1 . TYR A  1  163 ? 31.741  -2.280  26.137 1.00 40.81  ? 176 TYR A CE1 1 
ATOM   1225 C  CE2 . TYR A  1  163 ? 33.065  -4.085  26.965 1.00 39.83  ? 176 TYR A CE2 1 
ATOM   1226 C  CZ  . TYR A  1  163 ? 32.984  -2.825  26.402 1.00 40.12  ? 176 TYR A CZ  1 
ATOM   1227 O  OH  . TYR A  1  163 ? 34.127  -2.126  26.138 1.00 34.99  ? 176 TYR A OH  1 
ATOM   1228 N  N   . ASN A  1  164 ? 29.951  -6.706  24.271 1.00 38.39  ? 177 ASN A N   1 
ATOM   1229 C  CA  . ASN A  1  164 ? 30.860  -7.620  23.601 1.00 42.80  ? 177 ASN A CA  1 
ATOM   1230 C  C   . ASN A  1  164 ? 31.875  -6.794  22.812 1.00 41.88  ? 177 ASN A C   1 
ATOM   1231 O  O   . ASN A  1  164 ? 31.874  -5.565  22.903 1.00 42.68  ? 177 ASN A O   1 
ATOM   1232 C  CB  . ASN A  1  164 ? 30.070  -8.646  22.794 1.00 42.11  ? 177 ASN A CB  1 
ATOM   1233 C  CG  . ASN A  1  164 ? 29.507  -8.108  21.505 1.00 45.61  ? 177 ASN A CG  1 
ATOM   1234 O  OD1 . ASN A  1  164 ? 29.781  -6.973  21.105 1.00 47.06  ? 177 ASN A OD1 1 
ATOM   1235 N  ND2 . ASN A  1  164 ? 28.702  -8.924  20.848 1.00 50.59  ? 177 ASN A ND2 1 
ATOM   1236 N  N   . LEU A  1  165 ? 32.722  -7.469  22.027 1.00 40.97  ? 178 LEU A N   1 
ATOM   1237 C  CA  . LEU A  1  165 ? 33.866  -6.814  21.408 1.00 43.80  ? 178 LEU A CA  1 
ATOM   1238 C  C   . LEU A  1  165 ? 33.417  -5.802  20.353 1.00 40.29  ? 178 LEU A C   1 
ATOM   1239 O  O   . LEU A  1  165 ? 34.058  -4.775  20.176 1.00 39.38  ? 178 LEU A O   1 
ATOM   1240 C  CB  . LEU A  1  165 ? 34.813  -7.867  20.832 1.00 47.11  ? 178 LEU A CB  1 
ATOM   1241 C  CG  . LEU A  1  165 ? 36.210  -7.377  20.452 1.00 49.52  ? 178 LEU A CG  1 
ATOM   1242 C  CD1 . LEU A  1  165 ? 36.984  -6.815  21.623 1.00 52.68  ? 178 LEU A CD1 1 
ATOM   1243 C  CD2 . LEU A  1  165 ? 37.005  -8.522  19.841 1.00 54.24  ? 178 LEU A CD2 1 
ATOM   1244 N  N   . THR A  1  166 ? 32.302  -6.063  19.669 1.00 41.09  ? 179 THR A N   1 
ATOM   1245 C  CA  . THR A  1  166 ? 31.746  -5.097  18.728 1.00 41.33  ? 179 THR A CA  1 
ATOM   1246 C  C   . THR A  1  166 ? 31.395  -3.806  19.464 1.00 40.13  ? 179 THR A C   1 
ATOM   1247 O  O   . THR A  1  166 ? 31.676  -2.711  18.981 1.00 41.16  ? 179 THR A O   1 
ATOM   1248 C  CB  . THR A  1  166 ? 30.512  -5.675  18.030 1.00 42.67  ? 179 THR A CB  1 
ATOM   1249 O  OG1 . THR A  1  166 ? 30.810  -7.001  17.602 1.00 41.63  ? 179 THR A OG1 1 
ATOM   1250 C  CG2 . THR A  1  166 ? 30.069  -4.833  16.850 1.00 43.21  ? 179 THR A CG2 1 
ATOM   1251 N  N   . VAL A  1  167 ? 30.795  -3.941  20.656 1.00 40.25  ? 180 VAL A N   1 
ATOM   1252 C  CA  . VAL A  1  167 ? 30.360  -2.786  21.421 1.00 38.87  ? 180 VAL A CA  1 
ATOM   1253 C  C   . VAL A  1  167 ? 31.581  -1.983  21.863 1.00 39.68  ? 180 VAL A C   1 
ATOM   1254 O  O   . VAL A  1  167 ? 31.568  -0.753  21.823 1.00 42.75  ? 180 VAL A O   1 
ATOM   1255 C  CB  . VAL A  1  167 ? 29.488  -3.174  22.630 1.00 39.77  ? 180 VAL A CB  1 
ATOM   1256 C  CG1 . VAL A  1  167 ? 28.961  -1.939  23.356 1.00 38.16  ? 180 VAL A CG1 1 
ATOM   1257 C  CG2 . VAL A  1  167 ? 28.333  -4.087  22.233 1.00 39.66  ? 180 VAL A CG2 1 
ATOM   1258 N  N   . ALA A  1  168 ? 32.634  -2.694  22.284 1.00 39.87  ? 181 ALA A N   1 
ATOM   1259 C  CA  . ALA A  1  168 ? 33.872  -2.069  22.732 1.00 38.74  ? 181 ALA A CA  1 
ATOM   1260 C  C   . ALA A  1  168 ? 34.430  -1.154  21.643 1.00 39.24  ? 181 ALA A C   1 
ATOM   1261 O  O   . ALA A  1  168 ? 34.787  -0.012  21.914 1.00 41.21  ? 181 ALA A O   1 
ATOM   1262 C  CB  . ALA A  1  168 ? 34.868  -3.136  23.128 1.00 38.66  ? 181 ALA A CB  1 
ATOM   1263 N  N   . GLY A  1  169 ? 34.499  -1.660  20.407 1.00 41.36  ? 182 GLY A N   1 
ATOM   1264 C  CA  . GLY A  1  169 ? 35.000  -0.875  19.288 1.00 41.12  ? 182 GLY A CA  1 
ATOM   1265 C  C   . GLY A  1  169 ? 34.224  0.428   19.104 1.00 39.74  ? 182 GLY A C   1 
ATOM   1266 O  O   . GLY A  1  169 ? 34.819  1.490   18.944 1.00 41.72  ? 182 GLY A O   1 
ATOM   1267 N  N   . GLU A  1  170 ? 32.891  0.336   19.154 1.00 41.17  ? 183 GLU A N   1 
ATOM   1268 C  CA  . GLU A  1  170 ? 32.040  1.493   18.942 1.00 40.02  ? 183 GLU A CA  1 
ATOM   1269 C  C   . GLU A  1  170 ? 32.117  2.461   20.121 1.00 41.45  ? 183 GLU A C   1 
ATOM   1270 O  O   . GLU A  1  170 ? 32.200  3.671   19.916 1.00 44.96  ? 183 GLU A O   1 
ATOM   1271 C  CB  . GLU A  1  170 ? 30.598  1.052   18.676 1.00 45.68  ? 183 GLU A CB  1 
ATOM   1272 C  CG  . GLU A  1  170 ? 30.429  0.284   17.367 1.00 48.46  ? 183 GLU A CG  1 
ATOM   1273 C  CD  . GLU A  1  170 ? 31.015  1.020   16.171 1.00 54.02  ? 183 GLU A CD  1 
ATOM   1274 O  OE1 . GLU A  1  170 ? 30.708  2.219   15.954 1.00 54.43  ? 183 GLU A OE1 1 
ATOM   1275 O  OE2 . GLU A  1  170 ? 31.827  0.373   15.475 1.00 68.28  ? 183 GLU A OE2 1 
ATOM   1276 N  N   . LEU A  1  171 ? 32.097  1.936   21.352 1.00 38.22  ? 184 LEU A N   1 
ATOM   1277 C  CA  . LEU A  1  171 ? 32.017  2.790   22.525 1.00 38.60  ? 184 LEU A CA  1 
ATOM   1278 C  C   . LEU A  1  171 ? 33.318  3.565   22.691 1.00 38.65  ? 184 LEU A C   1 
ATOM   1279 O  O   . LEU A  1  171 ? 33.301  4.741   23.033 1.00 37.43  ? 184 LEU A O   1 
ATOM   1280 C  CB  . LEU A  1  171 ? 31.689  1.967   23.772 1.00 40.13  ? 184 LEU A CB  1 
ATOM   1281 C  CG  . LEU A  1  171 ? 31.584  2.744   25.091 1.00 40.34  ? 184 LEU A CG  1 
ATOM   1282 C  CD1 . LEU A  1  171 ? 30.481  3.786   25.051 1.00 41.57  ? 184 LEU A CD1 1 
ATOM   1283 C  CD2 . LEU A  1  171 ? 31.353  1.773   26.247 1.00 39.54  ? 184 LEU A CD2 1 
ATOM   1284 N  N   . ARG A  1  172 ? 34.450  2.887   22.482 1.00 42.38  ? 185 ARG A N   1 
ATOM   1285 C  CA  . ARG A  1  172 ? 35.754  3.509   22.647 1.00 41.29  ? 185 ARG A CA  1 
ATOM   1286 C  C   . ARG A  1  172 ? 35.859  4.737   21.745 1.00 42.61  ? 185 ARG A C   1 
ATOM   1287 O  O   . ARG A  1  172 ? 36.215  5.817   22.214 1.00 40.00  ? 185 ARG A O   1 
ATOM   1288 C  CB  . ARG A  1  172 ? 36.852  2.464   22.401 1.00 41.89  ? 185 ARG A CB  1 
ATOM   1289 C  CG  . ARG A  1  172 ? 38.280  2.964   22.194 1.00 44.41  ? 185 ARG A CG  1 
ATOM   1290 C  CD  . ARG A  1  172 ? 38.773  3.942   23.233 1.00 51.50  ? 185 ARG A CD  1 
ATOM   1291 N  NE  . ARG A  1  172 ? 38.545  3.460   24.601 1.00 52.95  ? 185 ARG A NE  1 
ATOM   1292 C  CZ  . ARG A  1  172 ? 38.376  4.217   25.663 1.00 54.74  ? 185 ARG A CZ  1 
ATOM   1293 N  NH1 . ARG A  1  172 ? 38.487  5.524   25.551 1.00 62.27  ? 185 ARG A NH1 1 
ATOM   1294 N  NH2 . ARG A  1  172 ? 38.167  3.686   26.857 1.00 59.99  ? 185 ARG A NH2 1 
ATOM   1295 N  N   . TYR A  1  173 ? 35.524  4.577   20.460 1.00 44.69  ? 186 TYR A N   1 
ATOM   1296 C  CA  . TYR A  1  173 ? 35.596  5.677   19.503 1.00 46.24  ? 186 TYR A CA  1 
ATOM   1297 C  C   . TYR A  1  173 ? 34.666  6.818   19.929 1.00 43.73  ? 186 TYR A C   1 
ATOM   1298 O  O   . TYR A  1  173 ? 35.054  7.985   19.927 1.00 44.04  ? 186 TYR A O   1 
ATOM   1299 C  CB  . TYR A  1  173 ? 35.253  5.164   18.100 1.00 45.32  ? 186 TYR A CB  1 
ATOM   1300 C  CG  . TYR A  1  173 ? 35.370  6.220   17.012 1.00 49.36  ? 186 TYR A CG  1 
ATOM   1301 C  CD1 . TYR A  1  173 ? 36.600  6.783   16.695 1.00 52.44  ? 186 TYR A CD1 1 
ATOM   1302 C  CD2 . TYR A  1  173 ? 34.256  6.647   16.297 1.00 50.98  ? 186 TYR A CD2 1 
ATOM   1303 C  CE1 . TYR A  1  173 ? 36.721  7.744   15.706 1.00 50.93  ? 186 TYR A CE1 1 
ATOM   1304 C  CE2 . TYR A  1  173 ? 34.362  7.614   15.310 1.00 53.93  ? 186 TYR A CE2 1 
ATOM   1305 C  CZ  . TYR A  1  173 ? 35.598  8.163   15.016 1.00 53.86  ? 186 TYR A CZ  1 
ATOM   1306 O  OH  . TYR A  1  173 ? 35.725  9.107   14.040 1.00 61.38  ? 186 TYR A OH  1 
ATOM   1307 N  N   . SER A  1  174 ? 33.432  6.469   20.309 1.00 41.65  ? 187 SER A N   1 
ATOM   1308 C  CA  . SER A  1  174 ? 32.431  7.470   20.632 1.00 40.43  ? 187 SER A CA  1 
ATOM   1309 C  C   . SER A  1  174 ? 32.860  8.286   21.848 1.00 40.83  ? 187 SER A C   1 
ATOM   1310 O  O   . SER A  1  174 ? 32.661  9.502   21.879 1.00 42.35  ? 187 SER A O   1 
ATOM   1311 C  CB  . SER A  1  174 ? 31.086  6.837   20.840 1.00 40.49  ? 187 SER A CB  1 
ATOM   1312 O  OG  . SER A  1  174 ? 30.129  7.832   21.160 1.00 45.23  ? 187 SER A OG  1 
ATOM   1313 N  N   . ARG A  1  175 ? 33.456  7.615   22.842 1.00 39.55  ? 188 ARG A N   1 
ATOM   1314 C  CA  . ARG A  1  175 ? 33.914  8.285   24.053 1.00 41.33  ? 188 ARG A CA  1 
ATOM   1315 C  C   . ARG A  1  175 ? 35.079  9.218   23.726 1.00 38.82  ? 188 ARG A C   1 
ATOM   1316 O  O   . ARG A  1  175 ? 35.212  10.274  24.342 1.00 37.51  ? 188 ARG A O   1 
ATOM   1317 C  CB  . ARG A  1  175 ? 34.306  7.293   25.158 1.00 40.17  ? 188 ARG A CB  1 
ATOM   1318 C  CG  . ARG A  1  175 ? 33.130  6.520   25.737 1.00 39.35  ? 188 ARG A CG  1 
ATOM   1319 C  CD  . ARG A  1  175 ? 32.186  7.396   26.541 1.00 40.36  ? 188 ARG A CD  1 
ATOM   1320 N  NE  . ARG A  1  175 ? 32.883  7.960   27.697 1.00 38.12  ? 188 ARG A NE  1 
ATOM   1321 C  CZ  . ARG A  1  175 ? 33.185  9.238   27.911 1.00 41.42  ? 188 ARG A CZ  1 
ATOM   1322 N  NH1 . ARG A  1  175 ? 32.678  10.191  27.151 1.00 44.00  ? 188 ARG A NH1 1 
ATOM   1323 N  NH2 . ARG A  1  175 ? 33.984  9.576   28.912 1.00 41.34  ? 188 ARG A NH2 1 
ATOM   1324 N  N   . ILE A  1  176 ? 35.924  8.832   22.765 1.00 43.26  ? 189 ILE A N   1 
ATOM   1325 C  CA  . ILE A  1  176 ? 36.985  9.721   22.305 1.00 47.11  ? 189 ILE A CA  1 
ATOM   1326 C  C   . ILE A  1  176 ? 36.353  10.986  21.716 1.00 46.74  ? 189 ILE A C   1 
ATOM   1327 O  O   . ILE A  1  176 ? 36.744  12.102  22.068 1.00 48.71  ? 189 ILE A O   1 
ATOM   1328 C  CB  . ILE A  1  176 ? 37.913  9.006   21.305 1.00 46.21  ? 189 ILE A CB  1 
ATOM   1329 C  CG1 . ILE A  1  176 ? 38.767  7.943   22.011 1.00 43.15  ? 189 ILE A CG1 1 
ATOM   1330 C  CG2 . ILE A  1  176 ? 38.781  10.004  20.535 1.00 46.67  ? 189 ILE A CG2 1 
ATOM   1331 C  CD1 . ILE A  1  176 ? 39.442  6.959   21.069 1.00 42.93  ? 189 ILE A CD1 1 
ATOM   1332 N  N   . GLN A  1  177 ? 35.341  10.796  20.860 1.00 45.38  ? 190 GLN A N   1 
ATOM   1333 C  CA  . GLN A  1  177 ? 34.655  11.909  20.220 1.00 47.27  ? 190 GLN A CA  1 
ATOM   1334 C  C   . GLN A  1  177 ? 34.015  12.827  21.259 1.00 44.17  ? 190 GLN A C   1 
ATOM   1335 O  O   . GLN A  1  177 ? 34.057  14.040  21.102 1.00 43.76  ? 190 GLN A O   1 
ATOM   1336 C  CB  . GLN A  1  177 ? 33.630  11.415  19.193 1.00 49.14  ? 190 GLN A CB  1 
ATOM   1337 C  CG  . GLN A  1  177 ? 34.242  10.756  17.958 1.00 52.74  ? 190 GLN A CG  1 
ATOM   1338 C  CD  . GLN A  1  177 ? 35.320  11.592  17.293 1.00 61.10  ? 190 GLN A CD  1 
ATOM   1339 O  OE1 . GLN A  1  177 ? 35.264  12.828  17.259 1.00 64.04  ? 190 GLN A OE1 1 
ATOM   1340 N  NE2 . GLN A  1  177 ? 36.333  10.921  16.765 1.00 60.90  ? 190 GLN A NE2 1 
ATOM   1341 N  N   . ASP A  1  178 ? 33.434  12.260  22.324 1.00 46.05  ? 191 ASP A N   1 
ATOM   1342 C  CA  . ASP A  1  178 ? 32.807  13.058  23.370 1.00 45.59  ? 191 ASP A CA  1 
ATOM   1343 C  C   . ASP A  1  178 ? 33.824  14.010  23.985 1.00 43.54  ? 191 ASP A C   1 
ATOM   1344 O  O   . ASP A  1  178 ? 33.537  15.192  24.175 1.00 45.95  ? 191 ASP A O   1 
ATOM   1345 C  CB  . ASP A  1  178 ? 32.211  12.202  24.478 1.00 48.29  ? 191 ASP A CB  1 
ATOM   1346 C  CG  . ASP A  1  178 ? 31.019  11.335  24.099 1.00 51.21  ? 191 ASP A CG  1 
ATOM   1347 O  OD1 . ASP A  1  178 ? 30.458  11.551  23.003 1.00 52.72  ? 191 ASP A OD1 1 
ATOM   1348 O  OD2 . ASP A  1  178 ? 30.674  10.432  24.897 1.00 51.15  ? 191 ASP A OD2 1 
ATOM   1349 N  N   . SER A  1  179 ? 35.005  13.478  24.321 1.00 44.30  ? 192 SER A N   1 
ATOM   1350 C  CA  . SER A  1  179 ? 36.037  14.262  24.980 1.00 42.25  ? 192 SER A CA  1 
ATOM   1351 C  C   . SER A  1  179 ? 36.589  15.336  24.037 1.00 41.16  ? 192 SER A C   1 
ATOM   1352 O  O   . SER A  1  179 ? 36.878  16.444  24.475 1.00 42.81  ? 192 SER A O   1 
ATOM   1353 C  CB  . SER A  1  179 ? 37.133  13.370  25.533 1.00 43.31  ? 192 SER A CB  1 
ATOM   1354 O  OG  . SER A  1  179 ? 36.690  12.695  26.701 1.00 44.84  ? 192 SER A OG  1 
ATOM   1355 N  N   . ILE A  1  180 ? 36.753  15.010  22.750 1.00 46.11  ? 193 ILE A N   1 
ATOM   1356 C  CA  . ILE A  1  180 ? 37.197  15.997  21.773 1.00 49.13  ? 193 ILE A CA  1 
ATOM   1357 C  C   . ILE A  1  180 ? 36.236  17.185  21.791 1.00 49.42  ? 193 ILE A C   1 
ATOM   1358 O  O   . ILE A  1  180 ? 36.668  18.331  21.880 1.00 48.07  ? 193 ILE A O   1 
ATOM   1359 C  CB  . ILE A  1  180 ? 37.315  15.380  20.364 1.00 49.67  ? 193 ILE A CB  1 
ATOM   1360 C  CG1 . ILE A  1  180 ? 38.498  14.405  20.285 1.00 48.70  ? 193 ILE A CG1 1 
ATOM   1361 C  CG2 . ILE A  1  180 ? 37.421  16.477  19.296 1.00 50.10  ? 193 ILE A CG2 1 
ATOM   1362 C  CD1 . ILE A  1  180 ? 38.504  13.522  19.051 1.00 48.92  ? 193 ILE A CD1 1 
ATOM   1363 N  N   . ALA A  1  181 ? 34.932  16.885  21.740 1.00 49.10  ? 194 ALA A N   1 
ATOM   1364 C  CA  . ALA A  1  181 ? 33.900  17.898  21.594 1.00 50.73  ? 194 ALA A CA  1 
ATOM   1365 C  C   . ALA A  1  181 ? 33.708  18.724  22.868 1.00 52.79  ? 194 ALA A C   1 
ATOM   1366 O  O   . ALA A  1  181 ? 33.295  19.876  22.771 1.00 56.70  ? 194 ALA A O   1 
ATOM   1367 C  CB  . ALA A  1  181 ? 32.603  17.239  21.186 1.00 47.22  ? 194 ALA A CB  1 
ATOM   1368 N  N   . THR A  1  182 ? 33.988  18.157  24.052 1.00 47.39  ? 195 THR A N   1 
ATOM   1369 C  CA  . THR A  1  182 ? 33.531  18.777  25.293 1.00 47.61  ? 195 THR A CA  1 
ATOM   1370 C  C   . THR A  1  182 ? 34.673  19.135  26.244 1.00 47.08  ? 195 THR A C   1 
ATOM   1371 O  O   . THR A  1  182 ? 34.453  19.889  27.189 1.00 46.87  ? 195 THR A O   1 
ATOM   1372 C  CB  . THR A  1  182 ? 32.529  17.854  25.993 1.00 52.09  ? 195 THR A CB  1 
ATOM   1373 O  OG1 . THR A  1  182 ? 33.219  16.649  26.321 1.00 48.23  ? 195 THR A OG1 1 
ATOM   1374 C  CG2 . THR A  1  182 ? 31.311  17.557  25.132 1.00 50.87  ? 195 THR A CG2 1 
ATOM   1375 N  N   . ASN A  1  183 ? 35.873  18.585  26.035 1.00 46.63  ? 196 ASN A N   1 
ATOM   1376 C  CA  . ASN A  1  183 ? 36.941  18.749  27.008 1.00 46.33  ? 196 ASN A CA  1 
ATOM   1377 C  C   . ASN A  1  183 ? 38.118  19.440  26.329 1.00 46.58  ? 196 ASN A C   1 
ATOM   1378 O  O   . ASN A  1  183 ? 38.827  18.824  25.539 1.00 44.87  ? 196 ASN A O   1 
ATOM   1379 C  CB  . ASN A  1  183 ? 37.333  17.412  27.630 1.00 44.75  ? 196 ASN A CB  1 
ATOM   1380 C  CG  . ASN A  1  183 ? 38.485  17.513  28.606 1.00 45.96  ? 196 ASN A CG  1 
ATOM   1381 O  OD1 . ASN A  1  183 ? 38.981  18.608  28.894 1.00 45.45  ? 196 ASN A OD1 1 
ATOM   1382 N  ND2 . ASN A  1  183 ? 38.927  16.382  29.134 1.00 45.39  ? 196 ASN A ND2 1 
ATOM   1383 N  N   . PRO A  1  184 ? 38.371  20.733  26.625 1.00 48.55  ? 197 PRO A N   1 
ATOM   1384 C  CA  . PRO A  1  184 ? 39.467  21.465  25.991 1.00 50.15  ? 197 PRO A CA  1 
ATOM   1385 C  C   . PRO A  1  184 ? 40.863  21.000  26.393 1.00 49.78  ? 197 PRO A C   1 
ATOM   1386 O  O   . PRO A  1  184 ? 41.825  21.305  25.690 1.00 54.72  ? 197 PRO A O   1 
ATOM   1387 C  CB  . PRO A  1  184 ? 39.201  22.920  26.413 1.00 49.65  ? 197 PRO A CB  1 
ATOM   1388 C  CG  . PRO A  1  184 ? 38.493  22.793  27.736 1.00 49.77  ? 197 PRO A CG  1 
ATOM   1389 C  CD  . PRO A  1  184 ? 37.615  21.557  27.574 1.00 50.03  ? 197 PRO A CD  1 
ATOM   1390 N  N   . GLU A  1  185 ? 40.959  20.270  27.517 1.00 51.84  ? 198 GLU A N   1 
ATOM   1391 C  CA  . GLU A  1  185 ? 42.225  19.767  28.032 1.00 47.70  ? 198 GLU A CA  1 
ATOM   1392 C  C   . GLU A  1  185 ? 42.399  18.287  27.698 1.00 46.82  ? 198 GLU A C   1 
ATOM   1393 O  O   . GLU A  1  185 ? 43.302  17.648  28.224 1.00 47.26  ? 198 GLU A O   1 
ATOM   1394 C  CB  . GLU A  1  185 ? 42.311  19.947  29.547 1.00 51.66  ? 198 GLU A CB  1 
ATOM   1395 C  CG  . GLU A  1  185 ? 42.345  21.405  30.000 1.00 54.76  ? 198 GLU A CG  1 
ATOM   1396 C  CD  . GLU A  1  185 ? 42.380  21.589  31.504 1.00 59.51  ? 198 GLU A CD  1 
ATOM   1397 O  OE1 . GLU A  1  185 ? 42.511  20.571  32.211 1.00 59.19  ? 198 GLU A OE1 1 
ATOM   1398 O  OE2 . GLU A  1  185 ? 42.280  22.743  31.972 1.00 66.78  ? 198 GLU A OE2 1 
ATOM   1399 N  N   . PHE A  1  186 ? 41.568  17.760  26.794 1.00 44.52  ? 199 PHE A N   1 
ATOM   1400 C  CA  . PHE A  1  186 ? 41.588  16.349  26.448 1.00 45.20  ? 199 PHE A CA  1 
ATOM   1401 C  C   . PHE A  1  186 ? 42.976  15.921  25.971 1.00 49.37  ? 199 PHE A C   1 
ATOM   1402 O  O   . PHE A  1  186 ? 43.520  16.511  25.042 1.00 48.94  ? 199 PHE A O   1 
ATOM   1403 C  CB  . PHE A  1  186 ? 40.572  16.079  25.339 1.00 45.10  ? 199 PHE A CB  1 
ATOM   1404 C  CG  . PHE A  1  186 ? 40.529  14.644  24.834 1.00 45.48  ? 199 PHE A CG  1 
ATOM   1405 C  CD1 . PHE A  1  186 ? 40.561  13.572  25.720 1.00 47.41  ? 199 PHE A CD1 1 
ATOM   1406 C  CD2 . PHE A  1  186 ? 40.468  14.370  23.474 1.00 44.62  ? 199 PHE A CD2 1 
ATOM   1407 C  CE1 . PHE A  1  186 ? 40.509  12.268  25.254 1.00 44.40  ? 199 PHE A CE1 1 
ATOM   1408 C  CE2 . PHE A  1  186 ? 40.433  13.063  23.014 1.00 44.78  ? 199 PHE A CE2 1 
ATOM   1409 C  CZ  . PHE A  1  186 ? 40.449  12.016  23.907 1.00 43.64  ? 199 PHE A CZ  1 
ATOM   1410 N  N   . GLN A  1  187 ? 43.504  14.861  26.600 1.00 48.66  ? 200 GLN A N   1 
ATOM   1411 C  CA  . GLN A  1  187 ? 44.768  14.243  26.229 1.00 48.07  ? 200 GLN A CA  1 
ATOM   1412 C  C   . GLN A  1  187 ? 44.525  12.752  26.008 1.00 45.75  ? 200 GLN A C   1 
ATOM   1413 O  O   . GLN A  1  187 ? 43.781  12.128  26.756 1.00 52.41  ? 200 GLN A O   1 
ATOM   1414 C  CB  . GLN A  1  187 ? 45.803  14.448  27.330 1.00 47.94  ? 200 GLN A CB  1 
ATOM   1415 C  CG  . GLN A  1  187 ? 46.239  15.897  27.512 1.00 53.10  ? 200 GLN A CG  1 
ATOM   1416 C  CD  . GLN A  1  187 ? 47.154  16.374  26.406 1.00 58.24  ? 200 GLN A CD  1 
ATOM   1417 O  OE1 . GLN A  1  187 ? 48.308  15.943  26.320 1.00 59.66  ? 200 GLN A OE1 1 
ATOM   1418 N  NE2 . GLN A  1  187 ? 46.661  17.259  25.549 1.00 55.84  ? 200 GLN A NE2 1 
ATOM   1419 N  N   . PHE A  1  188 ? 45.155  12.196  24.971 1.00 42.06  ? 201 PHE A N   1 
ATOM   1420 C  CA  . PHE A  1  188 ? 45.015  10.789  24.632 1.00 41.66  ? 201 PHE A CA  1 
ATOM   1421 C  C   . PHE A  1  188 ? 46.330  10.298  24.041 1.00 40.99  ? 201 PHE A C   1 
ATOM   1422 O  O   . PHE A  1  188 ? 46.391  9.876   22.898 1.00 39.62  ? 201 PHE A O   1 
ATOM   1423 C  CB  . PHE A  1  188 ? 43.809  10.639  23.705 1.00 43.82  ? 201 PHE A CB  1 
ATOM   1424 C  CG  . PHE A  1  188 ? 43.175  9.259   23.719 1.00 40.66  ? 201 PHE A CG  1 
ATOM   1425 C  CD1 . PHE A  1  188 ? 42.477  8.819   24.834 1.00 41.81  ? 201 PHE A CD1 1 
ATOM   1426 C  CD2 . PHE A  1  188 ? 43.243  8.427   22.612 1.00 42.27  ? 201 PHE A CD2 1 
ATOM   1427 C  CE1 . PHE A  1  188 ? 41.888  7.568   24.849 1.00 41.68  ? 201 PHE A CE1 1 
ATOM   1428 C  CE2 . PHE A  1  188 ? 42.645  7.177   22.633 1.00 43.44  ? 201 PHE A CE2 1 
ATOM   1429 C  CZ  . PHE A  1  188 ? 41.967  6.756   23.746 1.00 43.52  ? 201 PHE A CZ  1 
ATOM   1430 N  N   . LYS A  1  189 ? 47.364  10.331  24.885 1.00 47.82  ? 202 LYS A N   1 
ATOM   1431 C  CA  . LYS A  1  189 ? 48.754  10.138  24.509 1.00 50.09  ? 202 LYS A CA  1 
ATOM   1432 C  C   . LYS A  1  189 ? 49.411  9.152   25.471 1.00 47.73  ? 202 LYS A C   1 
ATOM   1433 O  O   . LYS A  1  189 ? 48.939  8.957   26.588 1.00 40.44  ? 202 LYS A O   1 
ATOM   1434 C  CB  . LYS A  1  189 ? 49.592  11.396  24.780 1.00 56.73  ? 202 LYS A CB  1 
ATOM   1435 C  CG  . LYS A  1  189 ? 49.404  12.615  23.908 1.00 63.37  ? 202 LYS A CG  1 
ATOM   1436 C  CD  . LYS A  1  189 ? 50.186  13.807  24.450 1.00 64.56  ? 202 LYS A CD  1 
ATOM   1437 C  CE  . LYS A  1  189 ? 50.062  15.017  23.580 1.00 68.66  ? 202 LYS A CE  1 
ATOM   1438 N  NZ  . LYS A  1  189 ? 50.622  16.209  24.225 1.00 75.60  ? 202 LYS A NZ  1 
ATOM   1439 N  N   . ASN A  1  190 ? 50.555  8.601   25.047 1.00 48.57  ? 203 ASN A N   1 
ATOM   1440 C  CA  . ASN A  1  190 ? 51.477  7.910   25.937 1.00 46.71  ? 203 ASN A CA  1 
ATOM   1441 C  C   . ASN A  1  190 ? 50.732  6.819   26.713 1.00 42.83  ? 203 ASN A C   1 
ATOM   1442 O  O   . ASN A  1  190 ? 50.105  5.959   26.109 1.00 44.67  ? 203 ASN A O   1 
ATOM   1443 C  CB  . ASN A  1  190 ? 52.251  8.928   26.765 1.00 48.06  ? 203 ASN A CB  1 
ATOM   1444 C  CG  . ASN A  1  190 ? 53.145  9.784   25.892 1.00 51.05  ? 203 ASN A CG  1 
ATOM   1445 O  OD1 . ASN A  1  190 ? 53.884  9.260   25.047 1.00 48.05  ? 203 ASN A OD1 1 
ATOM   1446 N  ND2 . ASN A  1  190 ? 53.075  11.095  26.062 1.00 47.43  ? 203 ASN A ND2 1 
ATOM   1447 N  N   . VAL A  1  191 ? 50.774  6.863   28.045 1.00 44.04  ? 204 VAL A N   1 
ATOM   1448 C  CA  . VAL A  1  191 ? 50.223  5.782   28.847 1.00 44.55  ? 204 VAL A CA  1 
ATOM   1449 C  C   . VAL A  1  191 ? 48.740  5.624   28.521 1.00 43.58  ? 204 VAL A C   1 
ATOM   1450 O  O   . VAL A  1  191 ? 48.261  4.520   28.288 1.00 41.45  ? 204 VAL A O   1 
ATOM   1451 C  CB  . VAL A  1  191 ? 50.421  6.001   30.360 1.00 46.49  ? 204 VAL A CB  1 
ATOM   1452 C  CG1 . VAL A  1  191 ? 49.714  4.931   31.190 1.00 46.38  ? 204 VAL A CG1 1 
ATOM   1453 C  CG2 . VAL A  1  191 ? 51.899  6.078   30.738 1.00 45.84  ? 204 VAL A CG2 1 
ATOM   1454 N  N   . ARG A  1  192 ? 48.010  6.738   28.512 1.00 42.56  ? 205 ARG A N   1 
ATOM   1455 C  CA  . ARG A  1  192 ? 46.566  6.677   28.386 1.00 41.59  ? 205 ARG A CA  1 
ATOM   1456 C  C   . ARG A  1  192 ? 46.171  6.036   27.062 1.00 39.34  ? 205 ARG A C   1 
ATOM   1457 O  O   . ARG A  1  192 ? 45.187  5.304   27.000 1.00 43.93  ? 205 ARG A O   1 
ATOM   1458 C  CB  . ARG A  1  192 ? 45.929  8.063   28.506 1.00 40.97  ? 205 ARG A CB  1 
ATOM   1459 C  CG  . ARG A  1  192 ? 44.411  8.032   28.414 1.00 41.39  ? 205 ARG A CG  1 
ATOM   1460 C  CD  . ARG A  1  192 ? 43.815  7.002   29.351 1.00 42.46  ? 205 ARG A CD  1 
ATOM   1461 N  NE  . ARG A  1  192 ? 42.355  6.901   29.253 1.00 43.33  ? 205 ARG A NE  1 
ATOM   1462 C  CZ  . ARG A  1  192 ? 41.629  5.897   29.734 1.00 41.36  ? 205 ARG A CZ  1 
ATOM   1463 N  NH1 . ARG A  1  192 ? 42.213  4.820   30.240 1.00 41.63  ? 205 ARG A NH1 1 
ATOM   1464 N  NH2 . ARG A  1  192 ? 40.310  5.975   29.715 1.00 43.04  ? 205 ARG A NH2 1 
ATOM   1465 N  N   . PHE A  1  193 ? 46.925  6.328   25.997 1.00 41.60  ? 206 PHE A N   1 
ATOM   1466 C  CA  . PHE A  1  193 ? 46.573  5.832   24.680 1.00 42.36  ? 206 PHE A CA  1 
ATOM   1467 C  C   . PHE A  1  193 ? 46.614  4.308   24.696 1.00 42.29  ? 206 PHE A C   1 
ATOM   1468 O  O   . PHE A  1  193 ? 45.767  3.654   24.098 1.00 45.32  ? 206 PHE A O   1 
ATOM   1469 C  CB  . PHE A  1  193 ? 47.474  6.393   23.576 1.00 45.80  ? 206 PHE A CB  1 
ATOM   1470 C  CG  . PHE A  1  193 ? 47.144  5.818   22.210 1.00 44.35  ? 206 PHE A CG  1 
ATOM   1471 C  CD1 . PHE A  1  193 ? 46.042  6.264   21.498 1.00 46.31  ? 206 PHE A CD1 1 
ATOM   1472 C  CD2 . PHE A  1  193 ? 47.921  4.812   21.656 1.00 49.00  ? 206 PHE A CD2 1 
ATOM   1473 C  CE1 . PHE A  1  193 ? 45.729  5.721   20.264 1.00 47.16  ? 206 PHE A CE1 1 
ATOM   1474 C  CE2 . PHE A  1  193 ? 47.606  4.276   20.419 1.00 49.94  ? 206 PHE A CE2 1 
ATOM   1475 C  CZ  . PHE A  1  193 ? 46.504  4.725   19.730 1.00 48.99  ? 206 PHE A CZ  1 
ATOM   1476 N  N   . ILE A  1  194 ? 47.588  3.747   25.411 1.00 43.72  ? 207 ILE A N   1 
ATOM   1477 C  CA  . ILE A  1  194 ? 47.757  2.304   25.453 1.00 44.36  ? 207 ILE A CA  1 
ATOM   1478 C  C   . ILE A  1  194 ? 46.711  1.688   26.386 1.00 41.85  ? 207 ILE A C   1 
ATOM   1479 O  O   . ILE A  1  194 ? 46.054  0.721   26.012 1.00 42.10  ? 207 ILE A O   1 
ATOM   1480 C  CB  . ILE A  1  194 ? 49.209  1.955   25.834 1.00 43.95  ? 207 ILE A CB  1 
ATOM   1481 C  CG1 . ILE A  1  194 ? 50.226  2.564   24.840 1.00 44.85  ? 207 ILE A CG1 1 
ATOM   1482 C  CG2 . ILE A  1  194 ? 49.391  0.447   25.971 1.00 44.51  ? 207 ILE A CG2 1 
ATOM   1483 C  CD1 . ILE A  1  194 ? 50.041  2.135   23.389 1.00 44.42  ? 207 ILE A CD1 1 
ATOM   1484 N  N   . THR A  1  195 ? 46.532  2.255   27.588 1.00 40.16  ? 208 THR A N   1 
ATOM   1485 C  CA  . THR A  1  195 ? 45.691  1.632   28.601 1.00 39.99  ? 208 THR A CA  1 
ATOM   1486 C  C   . THR A  1  195 ? 44.217  1.728   28.216 1.00 39.95  ? 208 THR A C   1 
ATOM   1487 O  O   . THR A  1  195 ? 43.413  0.916   28.663 1.00 43.88  ? 208 THR A O   1 
ATOM   1488 C  CB  . THR A  1  195 ? 45.920  2.247   29.984 1.00 40.14  ? 208 THR A CB  1 
ATOM   1489 O  OG1 . THR A  1  195 ? 45.604  3.634   29.907 1.00 43.76  ? 208 THR A OG1 1 
ATOM   1490 C  CG2 . THR A  1  195 ? 47.333  2.048   30.489 1.00 39.42  ? 208 THR A CG2 1 
ATOM   1491 N  N   . ALA A  1  196 ? 43.861  2.719   27.393 1.00 41.87  ? 209 ALA A N   1 
ATOM   1492 C  CA  . ALA A  1  196 ? 42.466  2.975   27.073 1.00 45.43  ? 209 ALA A CA  1 
ATOM   1493 C  C   . ALA A  1  196 ? 41.879  1.858   26.211 1.00 48.63  ? 209 ALA A C   1 
ATOM   1494 O  O   . ALA A  1  196 ? 40.672  1.663   26.220 1.00 49.51  ? 209 ALA A O   1 
ATOM   1495 C  CB  . ALA A  1  196 ? 42.332  4.314   26.394 1.00 45.62  ? 209 ALA A CB  1 
ATOM   1496 N  N   . TYR A  1  197 ? 42.725  1.139   25.455 1.00 43.45  ? 210 TYR A N   1 
ATOM   1497 C  CA  . TYR A  1  197 ? 42.236  0.065   24.602 1.00 41.99  ? 210 TYR A CA  1 
ATOM   1498 C  C   . TYR A  1  197 ? 42.106  -1.216  25.428 1.00 41.10  ? 210 TYR A C   1 
ATOM   1499 O  O   . TYR A  1  197 ? 41.088  -1.902  25.352 1.00 40.57  ? 210 TYR A O   1 
ATOM   1500 C  CB  . TYR A  1  197 ? 43.093  0.013   23.330 1.00 41.99  ? 210 TYR A CB  1 
ATOM   1501 C  CG  . TYR A  1  197 ? 42.703  1.148   22.387 1.00 43.13  ? 210 TYR A CG  1 
ATOM   1502 C  CD1 . TYR A  1  197 ? 41.623  1.021   21.521 1.00 42.84  ? 210 TYR A CD1 1 
ATOM   1503 C  CD2 . TYR A  1  197 ? 43.346  2.380   22.435 1.00 45.30  ? 210 TYR A CD2 1 
ATOM   1504 C  CE1 . TYR A  1  197 ? 41.227  2.061   20.696 1.00 44.34  ? 210 TYR A CE1 1 
ATOM   1505 C  CE2 . TYR A  1  197 ? 42.963  3.434   21.620 1.00 46.18  ? 210 TYR A CE2 1 
ATOM   1506 C  CZ  . TYR A  1  197 ? 41.894  3.274   20.754 1.00 46.93  ? 210 TYR A CZ  1 
ATOM   1507 O  OH  . TYR A  1  197 ? 41.524  4.309   19.952 1.00 44.81  ? 210 TYR A OH  1 
ATOM   1508 N  N   . GLY A  1  198 ? 43.114  -1.512  26.250 1.00 40.93  ? 211 GLY A N   1 
ATOM   1509 C  CA  . GLY A  1  198 ? 43.054  -2.655  27.154 1.00 42.71  ? 211 GLY A CA  1 
ATOM   1510 C  C   . GLY A  1  198 ? 41.820  -2.622  28.062 1.00 40.78  ? 211 GLY A C   1 
ATOM   1511 O  O   . GLY A  1  198 ? 41.135  -3.631  28.215 1.00 38.99  ? 211 GLY A O   1 
ATOM   1512 N  N   . GLU A  1  199 ? 41.516  -1.443  28.620 1.00 38.84  ? 212 GLU A N   1 
ATOM   1513 C  CA  A GLU A  1  199 ? 40.460  -1.335  29.611 0.50 40.13  ? 212 GLU A CA  1 
ATOM   1514 C  CA  B GLU A  1  199 ? 40.455  -1.299  29.604 0.50 39.87  ? 212 GLU A CA  1 
ATOM   1515 C  C   . GLU A  1  199 ? 39.102  -1.655  28.981 1.00 41.02  ? 212 GLU A C   1 
ATOM   1516 O  O   . GLU A  1  199 ? 38.194  -2.087  29.686 1.00 39.91  ? 212 GLU A O   1 
ATOM   1517 C  CB  A GLU A  1  199 ? 40.532  0.017   30.320 0.50 39.79  ? 212 GLU A CB  1 
ATOM   1518 C  CB  B GLU A  1  199 ? 40.443  0.115   30.206 0.50 39.22  ? 212 GLU A CB  1 
ATOM   1519 C  CG  A GLU A  1  199 ? 41.700  0.107   31.300 0.50 40.26  ? 212 GLU A CG  1 
ATOM   1520 C  CG  B GLU A  1  199 ? 39.572  1.133   29.462 0.50 38.95  ? 212 GLU A CG  1 
ATOM   1521 C  CD  A GLU A  1  199 ? 42.076  1.526   31.685 0.50 38.38  ? 212 GLU A CD  1 
ATOM   1522 C  CD  B GLU A  1  199 ? 39.555  2.544   30.044 0.50 36.75  ? 212 GLU A CD  1 
ATOM   1523 O  OE1 A GLU A  1  199 ? 41.287  2.451   31.396 0.50 34.63  ? 212 GLU A OE1 1 
ATOM   1524 O  OE1 B GLU A  1  199 ? 40.095  2.771   31.140 0.50 39.06  ? 212 GLU A OE1 1 
ATOM   1525 O  OE2 A GLU A  1  199 ? 43.175  1.702   32.244 0.50 35.61  ? 212 GLU A OE2 1 
ATOM   1526 O  OE2 B GLU A  1  199 ? 39.045  3.456   29.385 0.50 35.21  ? 212 GLU A OE2 1 
ATOM   1527 N  N   . THR A  1  200 ? 38.962  -1.479  27.652 1.00 40.38  ? 213 THR A N   1 
ATOM   1528 C  CA  . THR A  1  200 ? 37.670  -1.700  27.006 1.00 38.34  ? 213 THR A CA  1 
ATOM   1529 C  C   . THR A  1  200 ? 37.398  -3.186  26.801 1.00 33.77  ? 213 THR A C   1 
ATOM   1530 O  O   . THR A  1  200 ? 36.244  -3.548  26.589 1.00 32.80  ? 213 THR A O   1 
ATOM   1531 C  CB  . THR A  1  200 ? 37.541  -0.974  25.667 1.00 41.36  ? 213 THR A CB  1 
ATOM   1532 O  OG1 . THR A  1  200 ? 38.389  -1.614  24.725 1.00 45.10  ? 213 THR A OG1 1 
ATOM   1533 C  CG2 . THR A  1  200 ? 37.919  0.487   25.758 1.00 44.07  ? 213 THR A CG2 1 
ATOM   1534 N  N   . VAL A  1  201 ? 38.428  -4.041  26.850 1.00 32.43  ? 214 VAL A N   1 
ATOM   1535 C  CA  . VAL A  1  201 ? 38.219  -5.478  26.692 1.00 34.97  ? 214 VAL A CA  1 
ATOM   1536 C  C   . VAL A  1  201 ? 38.261  -6.206  28.038 1.00 35.12  ? 214 VAL A C   1 
ATOM   1537 O  O   . VAL A  1  201 ? 37.835  -7.361  28.117 1.00 36.03  ? 214 VAL A O   1 
ATOM   1538 C  CB  . VAL A  1  201 ? 39.194  -6.126  25.690 1.00 36.19  ? 214 VAL A CB  1 
ATOM   1539 C  CG1 . VAL A  1  201 ? 38.995  -5.568  24.292 1.00 36.71  ? 214 VAL A CG1 1 
ATOM   1540 C  CG2 . VAL A  1  201 ? 40.658  -5.982  26.102 1.00 34.78  ? 214 VAL A CG2 1 
ATOM   1541 N  N   . PHE A  1  202 ? 38.747  -5.549  29.099 1.00 36.64  ? 215 PHE A N   1 
ATOM   1542 C  CA  . PHE A  1  202 ? 38.831  -6.213  30.394 1.00 35.45  ? 215 PHE A CA  1 
ATOM   1543 C  C   . PHE A  1  202 ? 37.448  -6.701  30.828 1.00 34.93  ? 215 PHE A C   1 
ATOM   1544 O  O   . PHE A  1  202 ? 37.327  -7.792  31.374 1.00 37.24  ? 215 PHE A O   1 
ATOM   1545 C  CB  . PHE A  1  202 ? 39.468  -5.341  31.480 1.00 35.92  ? 215 PHE A CB  1 
ATOM   1546 C  CG  . PHE A  1  202 ? 40.959  -5.062  31.337 1.00 35.08  ? 215 PHE A CG  1 
ATOM   1547 C  CD1 . PHE A  1  202 ? 41.764  -5.798  30.473 1.00 36.88  ? 215 PHE A CD1 1 
ATOM   1548 C  CD2 . PHE A  1  202 ? 41.559  -4.068  32.104 1.00 38.74  ? 215 PHE A CD2 1 
ATOM   1549 C  CE1 . PHE A  1  202 ? 43.126  -5.531  30.370 1.00 38.75  ? 215 PHE A CE1 1 
ATOM   1550 C  CE2 . PHE A  1  202 ? 42.914  -3.801  31.994 1.00 41.52  ? 215 PHE A CE2 1 
ATOM   1551 C  CZ  . PHE A  1  202 ? 43.698  -4.543  31.138 1.00 39.31  ? 215 PHE A CZ  1 
ATOM   1552 N  N   . PRO A  1  203 ? 36.353  -5.941  30.612 1.00 36.40  ? 216 PRO A N   1 
ATOM   1553 C  CA  . PRO A  1  203 ? 35.016  -6.426  30.968 1.00 39.32  ? 216 PRO A CA  1 
ATOM   1554 C  C   . PRO A  1  203 ? 34.646  -7.740  30.282 1.00 43.11  ? 216 PRO A C   1 
ATOM   1555 O  O   . PRO A  1  203 ? 33.969  -8.575  30.877 1.00 46.02  ? 216 PRO A O   1 
ATOM   1556 C  CB  . PRO A  1  203 ? 34.101  -5.273  30.540 1.00 38.10  ? 216 PRO A CB  1 
ATOM   1557 C  CG  . PRO A  1  203 ? 35.004  -4.062  30.578 1.00 39.09  ? 216 PRO A CG  1 
ATOM   1558 C  CD  . PRO A  1  203 ? 36.337  -4.570  30.070 1.00 36.15  ? 216 PRO A CD  1 
ATOM   1559 N  N   . ILE A  1  204 ? 35.086  -7.914  29.029 1.00 42.31  ? 217 ILE A N   1 
ATOM   1560 C  CA  . ILE A  1  204 ? 34.794  -9.119  28.265 1.00 40.48  ? 217 ILE A CA  1 
ATOM   1561 C  C   . ILE A  1  204 ? 35.637  -10.277 28.788 1.00 39.95  ? 217 ILE A C   1 
ATOM   1562 O  O   . ILE A  1  204 ? 35.114  -11.365 28.998 1.00 42.77  ? 217 ILE A O   1 
ATOM   1563 C  CB  . ILE A  1  204 ? 35.043  -8.882  26.760 1.00 42.79  ? 217 ILE A CB  1 
ATOM   1564 C  CG1 . ILE A  1  204 ? 34.150  -7.779  26.215 1.00 44.26  ? 217 ILE A CG1 1 
ATOM   1565 C  CG2 . ILE A  1  204 ? 34.894  -10.179 25.958 1.00 43.39  ? 217 ILE A CG2 1 
ATOM   1566 C  CD1 . ILE A  1  204 ? 34.638  -7.158  24.922 1.00 45.11  ? 217 ILE A CD1 1 
ATOM   1567 N  N   . ASN A  1  205 ? 36.946  -10.048 28.971 1.00 37.75  ? 218 ASN A N   1 
ATOM   1568 C  CA  . ASN A  1  205 ? 37.864  -11.131 29.279 1.00 37.69  ? 218 ASN A CA  1 
ATOM   1569 C  C   . ASN A  1  205 ? 37.854  -11.489 30.762 1.00 38.76  ? 218 ASN A C   1 
ATOM   1570 O  O   . ASN A  1  205 ? 38.169  -12.626 31.094 1.00 41.63  ? 218 ASN A O   1 
ATOM   1571 C  CB  . ASN A  1  205 ? 39.290  -10.818 28.837 1.00 38.49  ? 218 ASN A CB  1 
ATOM   1572 C  CG  . ASN A  1  205 ? 39.372  -10.484 27.366 1.00 39.76  ? 218 ASN A CG  1 
ATOM   1573 O  OD1 . ASN A  1  205 ? 38.563  -10.971 26.572 1.00 43.69  ? 218 ASN A OD1 1 
ATOM   1574 N  ND2 . ASN A  1  205 ? 40.293  -9.615  26.988 1.00 42.48  ? 218 ASN A ND2 1 
ATOM   1575 N  N   . LEU A  1  206 ? 37.530  -10.527 31.644 1.00 35.47  ? 219 LEU A N   1 
ATOM   1576 C  CA  . LEU A  1  206 ? 37.691  -10.729 33.077 1.00 35.15  ? 219 LEU A CA  1 
ATOM   1577 C  C   . LEU A  1  206 ? 36.378  -10.603 33.859 1.00 36.57  ? 219 LEU A C   1 
ATOM   1578 O  O   . LEU A  1  206 ? 36.262  -11.207 34.923 1.00 38.18  ? 219 LEU A O   1 
ATOM   1579 C  CB  . LEU A  1  206 ? 38.754  -9.766  33.593 1.00 36.28  ? 219 LEU A CB  1 
ATOM   1580 C  CG  . LEU A  1  206 ? 40.140  -9.917  32.955 1.00 35.54  ? 219 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A  1  206 ? 41.028  -8.736  33.291 1.00 35.11  ? 219 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A  1  206 ? 40.818  -11.219 33.371 1.00 35.81  ? 219 LEU A CD2 1 
ATOM   1583 N  N   . PHE A  1  207 ? 35.406  -9.815  33.381 1.00 37.60  ? 220 PHE A N   1 
ATOM   1584 C  CA  . PHE A  1  207 ? 34.169  -9.624  34.134 1.00 37.78  ? 220 PHE A CA  1 
ATOM   1585 C  C   . PHE A  1  207 ? 33.109  -10.632 33.703 1.00 36.99  ? 220 PHE A C   1 
ATOM   1586 O  O   . PHE A  1  207 ? 32.135  -10.841 34.415 1.00 39.28  ? 220 PHE A O   1 
ATOM   1587 C  CB  . PHE A  1  207 ? 33.563  -8.225  34.017 1.00 35.99  ? 220 PHE A CB  1 
ATOM   1588 C  CG  . PHE A  1  207 ? 34.383  -7.091  34.607 1.00 35.84  ? 220 PHE A CG  1 
ATOM   1589 C  CD1 . PHE A  1  207 ? 35.458  -7.333  35.452 1.00 37.32  ? 220 PHE A CD1 1 
ATOM   1590 C  CD2 . PHE A  1  207 ? 34.052  -5.771  34.328 1.00 35.85  ? 220 PHE A CD2 1 
ATOM   1591 C  CE1 . PHE A  1  207 ? 36.202  -6.291  35.971 1.00 37.52  ? 220 PHE A CE1 1 
ATOM   1592 C  CE2 . PHE A  1  207 ? 34.802  -4.735  34.850 1.00 34.41  ? 220 PHE A CE2 1 
ATOM   1593 C  CZ  . PHE A  1  207 ? 35.870  -4.999  35.667 1.00 37.82  ? 220 PHE A CZ  1 
ATOM   1594 N  N   . VAL A  1  208 ? 33.293  -11.239 32.529 1.00 39.14  ? 221 VAL A N   1 
ATOM   1595 C  CA  . VAL A  1  208 ? 32.446  -12.337 32.100 1.00 40.12  ? 221 VAL A CA  1 
ATOM   1596 C  C   . VAL A  1  208 ? 32.872  -13.592 32.853 1.00 38.65  ? 221 VAL A C   1 
ATOM   1597 O  O   . VAL A  1  208 ? 34.060  -13.876 33.001 1.00 39.59  ? 221 VAL A O   1 
ATOM   1598 C  CB  . VAL A  1  208 ? 32.484  -12.562 30.577 1.00 42.14  ? 221 VAL A CB  1 
ATOM   1599 C  CG1 . VAL A  1  208 ? 31.682  -13.792 30.160 1.00 44.31  ? 221 VAL A CG1 1 
ATOM   1600 C  CG2 . VAL A  1  208 ? 31.988  -11.328 29.833 1.00 42.11  ? 221 VAL A CG2 1 
ATOM   1601 N  N   . ASP A  1  209 ? 31.869  -14.346 33.310 1.00 39.71  ? 222 ASP A N   1 
ATOM   1602 C  CA  . ASP A  1  209 ? 32.093  -15.524 34.123 1.00 39.96  ? 222 ASP A CA  1 
ATOM   1603 C  C   . ASP A  1  209 ? 32.919  -16.530 33.329 1.00 41.61  ? 222 ASP A C   1 
ATOM   1604 O  O   . ASP A  1  209 ? 32.661  -16.749 32.142 1.00 38.20  ? 222 ASP A O   1 
ATOM   1605 C  CB  . ASP A  1  209 ? 30.773  -16.130 34.564 1.00 41.96  ? 222 ASP A CB  1 
ATOM   1606 C  CG  . ASP A  1  209 ? 30.902  -17.248 35.585 1.00 40.49  ? 222 ASP A CG  1 
ATOM   1607 O  OD1 . ASP A  1  209 ? 31.291  -18.355 35.180 1.00 42.53  ? 222 ASP A OD1 1 
ATOM   1608 O  OD2 . ASP A  1  209 ? 30.654  -16.987 36.779 1.00 41.85  ? 222 ASP A OD2 1 
ATOM   1609 N  N   . GLY A  1  210 ? 33.880  -17.166 34.011 1.00 42.93  ? 223 GLY A N   1 
ATOM   1610 C  CA  . GLY A  1  210 ? 34.850  -18.033 33.362 1.00 42.68  ? 223 GLY A CA  1 
ATOM   1611 C  C   . GLY A  1  210 ? 34.249  -19.351 32.872 1.00 44.80  ? 223 GLY A C   1 
ATOM   1612 O  O   . GLY A  1  210 ? 34.902  -20.069 32.128 1.00 49.64  ? 223 GLY A O   1 
ATOM   1613 N  N   . ARG A  1  211 ? 33.018  -19.674 33.290 1.00 46.58  ? 224 ARG A N   1 
ATOM   1614 C  CA  . ARG A  1  211 ? 32.335  -20.871 32.816 1.00 46.63  ? 224 ARG A CA  1 
ATOM   1615 C  C   . ARG A  1  211 ? 31.703  -20.631 31.445 1.00 48.39  ? 224 ARG A C   1 
ATOM   1616 O  O   . ARG A  1  211 ? 31.282  -21.589 30.807 1.00 47.95  ? 224 ARG A O   1 
ATOM   1617 C  CB  . ARG A  1  211 ? 31.261  -21.339 33.800 1.00 47.39  ? 224 ARG A CB  1 
ATOM   1618 C  CG  . ARG A  1  211 ? 31.856  -21.895 35.088 1.00 48.49  ? 224 ARG A CG  1 
ATOM   1619 C  CD  . ARG A  1  211 ? 30.830  -22.003 36.197 1.00 49.43  ? 224 ARG A CD  1 
ATOM   1620 N  NE  . ARG A  1  211 ? 30.324  -20.679 36.582 1.00 49.55  ? 224 ARG A NE  1 
ATOM   1621 C  CZ  . ARG A  1  211 ? 29.463  -20.437 37.566 1.00 53.06  ? 224 ARG A CZ  1 
ATOM   1622 N  NH1 . ARG A  1  211 ? 28.966  -21.431 38.286 1.00 51.90  ? 224 ARG A NH1 1 
ATOM   1623 N  NH2 . ARG A  1  211 ? 29.100  -19.196 37.837 1.00 48.30  ? 224 ARG A NH2 1 
ATOM   1624 N  N   . VAL A  1  212 ? 31.647  -19.367 31.001 1.00 48.68  ? 225 VAL A N   1 
ATOM   1625 C  CA  . VAL A  1  212 ? 31.205  -19.037 29.656 1.00 50.80  ? 225 VAL A CA  1 
ATOM   1626 C  C   . VAL A  1  212 ? 32.397  -19.163 28.703 1.00 54.64  ? 225 VAL A C   1 
ATOM   1627 O  O   . VAL A  1  212 ? 33.312  -18.339 28.752 1.00 46.04  ? 225 VAL A O   1 
ATOM   1628 C  CB  . VAL A  1  212 ? 30.584  -17.626 29.604 1.00 49.06  ? 225 VAL A CB  1 
ATOM   1629 C  CG1 . VAL A  1  212 ? 30.134  -17.246 28.197 1.00 49.56  ? 225 VAL A CG1 1 
ATOM   1630 C  CG2 . VAL A  1  212 ? 29.417  -17.497 30.571 1.00 50.98  ? 225 VAL A CG2 1 
ATOM   1631 N  N   . THR A  1  213 ? 32.335  -20.164 27.810 1.00 63.70  ? 226 THR A N   1 
ATOM   1632 C  CA  . THR A  1  213 ? 33.447  -20.541 26.944 1.00 73.74  ? 226 THR A CA  1 
ATOM   1633 C  C   . THR A  1  213 ? 33.331  -19.865 25.572 1.00 75.74  ? 226 THR A C   1 
ATOM   1634 O  O   . THR A  1  213 ? 34.340  -19.488 24.984 1.00 73.25  ? 226 THR A O   1 
ATOM   1635 C  CB  . THR A  1  213 ? 33.472  -22.067 26.804 1.00 71.78  ? 226 THR A CB  1 
ATOM   1636 O  OG1 . THR A  1  213 ? 32.201  -22.461 26.298 1.00 71.91  ? 226 THR A OG1 1 
ATOM   1637 C  CG2 . THR A  1  213 ? 33.659  -22.794 28.123 1.00 73.88  ? 226 THR A CG2 1 
ATOM   1638 N  N   . THR A  1  214 ? 32.100  -19.718 25.071 1.00 75.48  ? 227 THR A N   1 
ATOM   1639 C  CA  . THR A  1  214 ? 31.835  -19.202 23.738 1.00 81.17  ? 227 THR A CA  1 
ATOM   1640 C  C   . THR A  1  214 ? 30.919  -17.984 23.852 1.00 75.88  ? 227 THR A C   1 
ATOM   1641 O  O   . THR A  1  214 ? 30.081  -17.915 24.750 1.00 71.87  ? 227 THR A O   1 
ATOM   1642 C  CB  . THR A  1  214 ? 31.201  -20.320 22.900 1.00 82.48  ? 227 THR A CB  1 
ATOM   1643 O  OG1 . THR A  1  214 ? 30.988  -19.773 21.604 1.00 89.44  ? 227 THR A OG1 1 
ATOM   1644 C  CG2 . THR A  1  214 ? 29.889  -20.831 23.473 1.00 82.68  ? 227 THR A CG2 1 
ATOM   1645 N  N   . ASP A  1  215 ? 31.062  -17.030 22.917 1.00 74.85  ? 228 ASP A N   1 
ATOM   1646 C  CA  . ASP A  1  215 ? 30.150  -15.900 22.811 1.00 75.21  ? 228 ASP A CA  1 
ATOM   1647 C  C   . ASP A  1  215 ? 30.214  -15.106 24.111 1.00 61.87  ? 228 ASP A C   1 
ATOM   1648 O  O   . ASP A  1  215 ? 29.198  -14.856 24.750 1.00 55.88  ? 228 ASP A O   1 
ATOM   1649 C  CB  . ASP A  1  215 ? 28.738  -16.355 22.451 1.00 83.43  ? 228 ASP A CB  1 
ATOM   1650 C  CG  . ASP A  1  215 ? 27.712  -15.247 22.227 1.00 92.66  ? 228 ASP A CG  1 
ATOM   1651 O  OD1 . ASP A  1  215 ? 28.123  -14.155 21.772 1.00 93.10  ? 228 ASP A OD1 1 
ATOM   1652 O  OD2 . ASP A  1  215 ? 26.504  -15.483 22.490 1.00 96.11  ? 228 ASP A OD2 1 
ATOM   1653 N  N   . ARG A  1  216 ? 31.431  -14.716 24.499 1.00 52.88  ? 229 ARG A N   1 
ATOM   1654 C  CA  . ARG A  1  216 ? 31.642  -14.044 25.767 1.00 53.23  ? 229 ARG A CA  1 
ATOM   1655 C  C   . ARG A  1  216 ? 31.044  -12.643 25.667 1.00 46.00  ? 229 ARG A C   1 
ATOM   1656 O  O   . ARG A  1  216 ? 31.386  -11.878 24.776 1.00 45.30  ? 229 ARG A O   1 
ATOM   1657 C  CB  . ARG A  1  216 ? 33.123  -14.117 26.163 1.00 56.31  ? 229 ARG A CB  1 
ATOM   1658 C  CG  . ARG A  1  216 ? 33.526  -15.507 26.650 1.00 59.38  ? 229 ARG A CG  1 
ATOM   1659 C  CD  . ARG A  1  216 ? 35.012  -15.631 26.960 1.00 63.13  ? 229 ARG A CD  1 
ATOM   1660 N  NE  . ARG A  1  216 ? 35.423  -14.793 28.095 1.00 69.27  ? 229 ARG A NE  1 
ATOM   1661 C  CZ  . ARG A  1  216 ? 35.222  -15.043 29.394 1.00 68.26  ? 229 ARG A CZ  1 
ATOM   1662 N  NH1 . ARG A  1  216 ? 34.661  -16.177 29.792 1.00 64.51  ? 229 ARG A NH1 1 
ATOM   1663 N  NH2 . ARG A  1  216 ? 35.610  -14.150 30.297 1.00 68.83  ? 229 ARG A NH2 1 
ATOM   1664 N  N   . LYS A  1  217 ? 30.114  -12.344 26.575 1.00 42.29  ? 230 LYS A N   1 
ATOM   1665 C  CA  . LYS A  1  217 ? 29.410  -11.077 26.582 1.00 42.18  ? 230 LYS A CA  1 
ATOM   1666 C  C   . LYS A  1  217 ? 28.975  -10.783 28.016 1.00 38.49  ? 230 LYS A C   1 
ATOM   1667 O  O   . LYS A  1  217 ? 28.633  -11.697 28.761 1.00 36.70  ? 230 LYS A O   1 
ATOM   1668 C  CB  . LYS A  1  217 ? 28.211  -11.156 25.629 1.00 43.48  ? 230 LYS A CB  1 
ATOM   1669 C  CG  . LYS A  1  217 ? 27.109  -12.099 26.096 1.00 44.21  ? 230 LYS A CG  1 
ATOM   1670 C  CD  . LYS A  1  217 ? 26.002  -12.388 25.090 1.00 45.00  ? 230 LYS A CD  1 
ATOM   1671 C  CE  . LYS A  1  217 ? 24.895  -13.201 25.690 1.00 45.77  ? 230 LYS A CE  1 
ATOM   1672 N  NZ  . LYS A  1  217 ? 23.782  -13.408 24.753 1.00 48.43  ? 230 LYS A NZ  1 
ATOM   1673 N  N   . LEU A  1  218 ? 28.980  -9.497  28.383 1.00 38.88  ? 231 LEU A N   1 
ATOM   1674 C  CA  . LEU A  1  218 ? 28.699  -9.096  29.749 1.00 36.43  ? 231 LEU A CA  1 
ATOM   1675 C  C   . LEU A  1  218 ? 27.300  -8.497  29.838 1.00 37.41  ? 231 LEU A C   1 
ATOM   1676 O  O   . LEU A  1  218 ? 26.973  -7.584  29.081 1.00 38.02  ? 231 LEU A O   1 
ATOM   1677 C  CB  . LEU A  1  218 ? 29.754  -8.081  30.164 1.00 36.01  ? 231 LEU A CB  1 
ATOM   1678 C  CG  . LEU A  1  218 ? 29.681  -7.604  31.617 1.00 35.25  ? 231 LEU A CG  1 
ATOM   1679 C  CD1 . LEU A  1  218 ? 30.036  -8.738  32.565 1.00 36.92  ? 231 LEU A CD1 1 
ATOM   1680 C  CD2 . LEU A  1  218 ? 30.588  -6.408  31.825 1.00 36.23  ? 231 LEU A CD2 1 
ATOM   1681 N  N   . SER A  1  219 ? 26.507  -8.971  30.807 1.00 36.77  ? 232 SER A N   1 
ATOM   1682 C  CA  . SER A  1  219 ? 25.179  -8.413  31.033 1.00 40.59  ? 232 SER A CA  1 
ATOM   1683 C  C   . SER A  1  219 ? 25.302  -7.048  31.708 1.00 38.30  ? 232 SER A C   1 
ATOM   1684 O  O   . SER A  1  219 ? 26.310  -6.747  32.339 1.00 38.57  ? 232 SER A O   1 
ATOM   1685 C  CB  . SER A  1  219 ? 24.323  -9.346  31.845 1.00 39.45  ? 232 SER A CB  1 
ATOM   1686 O  OG  . SER A  1  219 ? 24.788  -9.407  33.184 1.00 39.84  ? 232 SER A OG  1 
ATOM   1687 N  N   . MET A  1  220 ? 24.269  -6.221  31.569 1.00 39.65  ? 233 MET A N   1 
ATOM   1688 C  CA  . MET A  1  220 ? 24.289  -4.890  32.155 1.00 39.07  ? 233 MET A CA  1 
ATOM   1689 C  C   . MET A  1  220 ? 24.157  -4.986  33.673 1.00 40.83  ? 233 MET A C   1 
ATOM   1690 O  O   . MET A  1  220 ? 24.716  -4.158  34.390 1.00 36.84  ? 233 MET A O   1 
ATOM   1691 C  CB  . MET A  1  220 ? 23.176  -4.021  31.568 1.00 37.19  ? 233 MET A CB  1 
ATOM   1692 C  CG  . MET A  1  220 ? 23.332  -3.731  30.087 1.00 35.97  ? 233 MET A CG  1 
ATOM   1693 S  SD  . MET A  1  220 ? 24.910  -2.964  29.652 1.00 38.51  ? 233 MET A SD  1 
ATOM   1694 C  CE  . MET A  1  220 ? 25.806  -4.376  29.001 1.00 41.37  ? 233 MET A CE  1 
ATOM   1695 N  N   . GLU A  1  221 ? 23.446  -6.015  34.158 1.00 41.63  ? 234 GLU A N   1 
ATOM   1696 C  CA  . GLU A  1  221 ? 23.353  -6.277  35.588 1.00 41.07  ? 234 GLU A CA  1 
ATOM   1697 C  C   . GLU A  1  221 ? 24.747  -6.537  36.166 1.00 38.40  ? 234 GLU A C   1 
ATOM   1698 O  O   . GLU A  1  221 ? 25.108  -5.989  37.204 1.00 37.57  ? 234 GLU A O   1 
ATOM   1699 C  CB  . GLU A  1  221 ? 22.435  -7.463  35.883 1.00 41.57  ? 234 GLU A CB  1 
ATOM   1700 C  CG  . GLU A  1  221 ? 20.979  -7.214  35.489 1.00 47.51  ? 234 GLU A CG  1 
ATOM   1701 C  CD  . GLU A  1  221 ? 20.606  -7.445  34.022 1.00 53.42  ? 234 GLU A CD  1 
ATOM   1702 O  OE1 . GLU A  1  221 ? 21.442  -7.734  33.117 1.00 51.66  ? 234 GLU A OE1 1 
ATOM   1703 O  OE2 . GLU A  1  221 ? 19.374  -7.381  33.795 1.00 61.80  ? 234 GLU A OE2 1 
ATOM   1704 N  N   . ASP A  1  222 ? 25.522  -7.405  35.509 1.00 38.44  ? 235 ASP A N   1 
ATOM   1705 C  CA  . ASP A  1  222 ? 26.856  -7.748  35.988 1.00 38.60  ? 235 ASP A CA  1 
ATOM   1706 C  C   . ASP A  1  222 ? 27.771  -6.530  35.890 1.00 38.12  ? 235 ASP A C   1 
ATOM   1707 O  O   . ASP A  1  222 ? 28.566  -6.273  36.792 1.00 39.34  ? 235 ASP A O   1 
ATOM   1708 C  CB  . ASP A  1  222 ? 27.395  -8.978  35.275 1.00 41.72  ? 235 ASP A CB  1 
ATOM   1709 C  CG  . ASP A  1  222 ? 26.751  -10.303 35.669 1.00 40.89  ? 235 ASP A CG  1 
ATOM   1710 O  OD1 . ASP A  1  222 ? 25.936  -10.307 36.621 1.00 42.29  ? 235 ASP A OD1 1 
ATOM   1711 O  OD2 . ASP A  1  222 ? 27.063  -11.321 35.017 1.00 42.55  ? 235 ASP A OD2 1 
ATOM   1712 N  N   . ALA A  1  223 ? 27.643  -5.768  34.794 1.00 36.13  ? 236 ALA A N   1 
ATOM   1713 C  CA  . ALA A  1  223 ? 28.427  -4.561  34.609 1.00 36.83  ? 236 ALA A CA  1 
ATOM   1714 C  C   . ALA A  1  223 ? 28.161  -3.567  35.738 1.00 35.42  ? 236 ALA A C   1 
ATOM   1715 O  O   . ALA A  1  223 ? 29.106  -3.051  36.337 1.00 33.87  ? 236 ALA A O   1 
ATOM   1716 C  CB  . ALA A  1  223 ? 28.143  -3.949  33.263 1.00 37.17  ? 236 ALA A CB  1 
ATOM   1717 N  N   . ALA A  1  224 ? 26.881  -3.310  36.035 1.00 32.34  ? 237 ALA A N   1 
ATOM   1718 C  CA  . ALA A  1  224 ? 26.505  -2.342  37.058 1.00 33.95  ? 237 ALA A CA  1 
ATOM   1719 C  C   . ALA A  1  224 ? 27.032  -2.798  38.415 1.00 33.07  ? 237 ALA A C   1 
ATOM   1720 O  O   . ALA A  1  224 ? 27.561  -1.993  39.173 1.00 35.35  ? 237 ALA A O   1 
ATOM   1721 C  CB  . ALA A  1  224 ? 25.001  -2.156  37.097 1.00 35.12  ? 237 ALA A CB  1 
ATOM   1722 N  N   . SER A  1  225 ? 26.913  -4.097  38.692 1.00 31.51  ? 238 SER A N   1 
ATOM   1723 C  CA  . SER A  1  225 ? 27.367  -4.657  39.953 1.00 34.10  ? 238 SER A CA  1 
ATOM   1724 C  C   . SER A  1  225 ? 28.849  -4.340  40.184 1.00 34.33  ? 238 SER A C   1 
ATOM   1725 O  O   . SER A  1  225 ? 29.221  -3.933  41.279 1.00 35.49  ? 238 SER A O   1 
ATOM   1726 C  CB  . SER A  1  225 ? 27.099  -6.148  40.009 1.00 34.72  ? 238 SER A CB  1 
ATOM   1727 O  OG  . SER A  1  225 ? 27.471  -6.668  41.279 1.00 40.29  ? 238 SER A OG  1 
ATOM   1728 N  N   . ILE A  1  226 ? 29.692  -4.514  39.157 1.00 32.97  ? 239 ILE A N   1 
ATOM   1729 C  CA  . ILE A  1  226 ? 31.133  -4.323  39.314 1.00 32.02  ? 239 ILE A CA  1 
ATOM   1730 C  C   . ILE A  1  226 ? 31.492  -2.838  39.210 1.00 32.04  ? 239 ILE A C   1 
ATOM   1731 O  O   . ILE A  1  226 ? 32.130  -2.306  40.110 1.00 34.24  ? 239 ILE A O   1 
ATOM   1732 C  CB  . ILE A  1  226 ? 31.901  -5.179  38.293 1.00 30.59  ? 239 ILE A CB  1 
ATOM   1733 C  CG1 . ILE A  1  226 ? 31.733  -6.662  38.595 1.00 34.51  ? 239 ILE A CG1 1 
ATOM   1734 C  CG2 . ILE A  1  226 ? 33.380  -4.803  38.234 1.00 29.20  ? 239 ILE A CG2 1 
ATOM   1735 C  CD1 . ILE A  1  226 ? 32.089  -7.577  37.432 1.00 36.65  ? 239 ILE A CD1 1 
ATOM   1736 N  N   . PHE A  1  227 ? 31.062  -2.175  38.126 1.00 31.72  ? 240 PHE A N   1 
ATOM   1737 C  CA  . PHE A  1  227 ? 31.427  -0.791  37.839 1.00 32.73  ? 240 PHE A CA  1 
ATOM   1738 C  C   . PHE A  1  227 ? 30.866  0.177   38.885 1.00 32.53  ? 240 PHE A C   1 
ATOM   1739 O  O   . PHE A  1  227 ? 31.544  1.136   39.247 1.00 32.51  ? 240 PHE A O   1 
ATOM   1740 C  CB  . PHE A  1  227 ? 30.950  -0.319  36.458 1.00 32.79  ? 240 PHE A CB  1 
ATOM   1741 C  CG  . PHE A  1  227 ? 31.749  -0.812  35.260 1.00 34.56  ? 240 PHE A CG  1 
ATOM   1742 C  CD1 . PHE A  1  227 ? 32.988  -0.261  34.952 1.00 35.62  ? 240 PHE A CD1 1 
ATOM   1743 C  CD2 . PHE A  1  227 ? 31.250  -1.793  34.412 1.00 38.35  ? 240 PHE A CD2 1 
ATOM   1744 C  CE1 . PHE A  1  227 ? 33.703  -0.689  33.846 1.00 35.63  ? 240 PHE A CE1 1 
ATOM   1745 C  CE2 . PHE A  1  227 ? 31.971  -2.216  33.304 1.00 38.41  ? 240 PHE A CE2 1 
ATOM   1746 C  CZ  . PHE A  1  227 ? 33.199  -1.671  33.032 1.00 36.67  ? 240 PHE A CZ  1 
ATOM   1747 N  N   . ARG A  1  228 ? 29.615  -0.029  39.322 1.00 33.14  ? 241 ARG A N   1 
ATOM   1748 C  CA  . ARG A  1  228 ? 28.971  0.885   40.255 1.00 32.30  ? 241 ARG A CA  1 
ATOM   1749 C  C   . ARG A  1  228 ? 29.144  0.401   41.696 1.00 32.21  ? 241 ARG A C   1 
ATOM   1750 O  O   . ARG A  1  228 ? 29.596  1.163   42.539 1.00 35.16  ? 241 ARG A O   1 
ATOM   1751 C  CB  . ARG A  1  228 ? 27.485  1.095   39.943 1.00 34.64  ? 241 ARG A CB  1 
ATOM   1752 C  CG  . ARG A  1  228 ? 26.808  2.101   40.868 1.00 36.13  ? 241 ARG A CG  1 
ATOM   1753 C  CD  . ARG A  1  228 ? 25.405  2.519   40.461 1.00 37.51  ? 241 ARG A CD  1 
ATOM   1754 N  NE  . ARG A  1  228 ? 24.468  1.396   40.402 1.00 39.67  ? 241 ARG A NE  1 
ATOM   1755 C  CZ  . ARG A  1  228 ? 23.779  0.956   39.359 1.00 41.22  ? 241 ARG A CZ  1 
ATOM   1756 N  NH1 . ARG A  1  228 ? 23.790  1.599   38.199 1.00 44.01  ? 241 ARG A NH1 1 
ATOM   1757 N  NH2 . ARG A  1  228 ? 23.062  -0.144  39.496 1.00 41.07  ? 241 ARG A NH2 1 
ATOM   1758 N  N   . ASP A  1  229 ? 28.795  -0.861  41.981 1.00 31.69  ? 242 ASP A N   1 
ATOM   1759 C  CA  . ASP A  1  229 ? 28.659  -1.317  43.358 1.00 33.00  ? 242 ASP A CA  1 
ATOM   1760 C  C   . ASP A  1  229 ? 29.932  -1.982  43.877 1.00 31.77  ? 242 ASP A C   1 
ATOM   1761 O  O   . ASP A  1  229 ? 30.025  -2.268  45.071 1.00 34.76  ? 242 ASP A O   1 
ATOM   1762 C  CB  . ASP A  1  229 ? 27.449  -2.223  43.521 1.00 33.87  ? 242 ASP A CB  1 
ATOM   1763 C  CG  . ASP A  1  229 ? 26.099  -1.565  43.273 1.00 36.14  ? 242 ASP A CG  1 
ATOM   1764 O  OD1 . ASP A  1  229 ? 26.010  -0.318  43.367 1.00 38.50  ? 242 ASP A OD1 1 
ATOM   1765 O  OD2 . ASP A  1  229 ? 25.155  -2.309  42.956 1.00 37.77  ? 242 ASP A OD2 1 
ATOM   1766 N  N   . MET A  1  230 ? 30.911  -2.226  43.008 1.00 32.58  ? 243 MET A N   1 
ATOM   1767 C  CA  . MET A  1  230 ? 32.156  -2.860  43.423 1.00 34.87  ? 243 MET A CA  1 
ATOM   1768 C  C   . MET A  1  230 ? 31.884  -4.257  43.983 1.00 34.54  ? 243 MET A C   1 
ATOM   1769 O  O   . MET A  1  230 ? 32.494  -4.656  44.974 1.00 35.47  ? 243 MET A O   1 
ATOM   1770 C  CB  . MET A  1  230 ? 32.872  -2.031  44.498 1.00 35.36  ? 243 MET A CB  1 
ATOM   1771 C  CG  . MET A  1  230 ? 33.061  -0.582  44.119 1.00 38.89  ? 243 MET A CG  1 
ATOM   1772 S  SD  . MET A  1  230 ? 33.869  0.371   45.418 1.00 39.19  ? 243 MET A SD  1 
ATOM   1773 C  CE  . MET A  1  230 ? 32.491  0.695   46.524 1.00 43.19  ? 243 MET A CE  1 
ATOM   1774 N  N   . ARG A  1  231 ? 30.967  -4.990  43.338 1.00 33.79  ? 244 ARG A N   1 
ATOM   1775 C  CA  A ARG A  1  231 ? 30.501  -6.274  43.835 0.50 34.67  ? 244 ARG A CA  1 
ATOM   1776 C  CA  B ARG A  1  231 ? 30.506  -6.275  43.834 0.50 33.03  ? 244 ARG A CA  1 
ATOM   1777 C  C   . ARG A  1  231 ? 30.579  -7.307  42.711 1.00 33.52  ? 244 ARG A C   1 
ATOM   1778 O  O   . ARG A  1  231 ? 30.123  -7.062  41.598 1.00 31.47  ? 244 ARG A O   1 
ATOM   1779 C  CB  A ARG A  1  231 ? 29.070  -6.124  44.363 0.50 37.40  ? 244 ARG A CB  1 
ATOM   1780 C  CB  B ARG A  1  231 ? 29.077  -6.117  44.357 0.50 33.15  ? 244 ARG A CB  1 
ATOM   1781 C  CG  A ARG A  1  231 ? 28.507  -7.368  45.042 0.50 41.46  ? 244 ARG A CG  1 
ATOM   1782 C  CG  B ARG A  1  231 ? 28.481  -7.340  45.040 0.50 34.12  ? 244 ARG A CG  1 
ATOM   1783 C  CD  A ARG A  1  231 ? 27.019  -7.355  45.384 0.50 44.11  ? 244 ARG A CD  1 
ATOM   1784 C  CD  B ARG A  1  231 ? 27.044  -7.061  45.509 0.50 33.29  ? 244 ARG A CD  1 
ATOM   1785 N  NE  A ARG A  1  231 ? 26.183  -7.125  44.201 0.50 51.93  ? 244 ARG A NE  1 
ATOM   1786 N  NE  B ARG A  1  231 ? 26.143  -6.812  44.377 0.50 36.14  ? 244 ARG A NE  1 
ATOM   1787 C  CZ  A ARG A  1  231 ? 25.668  -8.074  43.418 0.50 52.86  ? 244 ARG A CZ  1 
ATOM   1788 C  CZ  B ARG A  1  231 ? 25.533  -5.668  44.044 0.50 33.80  ? 244 ARG A CZ  1 
ATOM   1789 N  NH1 A ARG A  1  231 ? 25.934  -9.346  43.645 0.50 55.25  ? 244 ARG A NH1 1 
ATOM   1790 N  NH1 B ARG A  1  231 ? 25.558  -4.622  44.844 0.50 34.87  ? 244 ARG A NH1 1 
ATOM   1791 N  NH2 A ARG A  1  231 ? 24.905  -7.739  42.394 0.50 50.18  ? 244 ARG A NH2 1 
ATOM   1792 N  NH2 B ARG A  1  231 ? 24.865  -5.578  42.912 0.50 31.58  ? 244 ARG A NH2 1 
ATOM   1793 N  N   . PHE A  1  232 ? 31.155  -8.471  43.014 1.00 34.03  ? 245 PHE A N   1 
ATOM   1794 C  CA  . PHE A  1  232 ? 31.130  -9.592  42.092 1.00 33.35  ? 245 PHE A CA  1 
ATOM   1795 C  C   . PHE A  1  232 ? 29.683  -10.011 41.863 1.00 37.13  ? 245 PHE A C   1 
ATOM   1796 O  O   . PHE A  1  232 ? 28.870  -9.975  42.784 1.00 35.75  ? 245 PHE A O   1 
ATOM   1797 C  CB  . PHE A  1  232 ? 31.884  -10.802 42.625 1.00 32.34  ? 245 PHE A CB  1 
ATOM   1798 C  CG  . PHE A  1  232 ? 33.400  -10.691 42.621 1.00 34.17  ? 245 PHE A CG  1 
ATOM   1799 C  CD1 . PHE A  1  232 ? 34.096  -10.622 41.421 1.00 35.88  ? 245 PHE A CD1 1 
ATOM   1800 C  CD2 . PHE A  1  232 ? 34.126  -10.748 43.806 1.00 37.74  ? 245 PHE A CD2 1 
ATOM   1801 C  CE1 . PHE A  1  232 ? 35.483  -10.567 41.400 1.00 36.20  ? 245 PHE A CE1 1 
ATOM   1802 C  CE2 . PHE A  1  232 ? 35.520  -10.697 43.782 1.00 36.24  ? 245 PHE A CE2 1 
ATOM   1803 C  CZ  . PHE A  1  232 ? 36.191  -10.608 42.584 1.00 38.20  ? 245 PHE A CZ  1 
ATOM   1804 N  N   . PRO A  1  233 ? 29.311  -10.427 40.635 1.00 36.81  ? 246 PRO A N   1 
ATOM   1805 C  CA  . PRO A  1  233 ? 28.042  -11.122 40.430 1.00 37.65  ? 246 PRO A CA  1 
ATOM   1806 C  C   . PRO A  1  233 ? 27.968  -12.310 41.386 1.00 37.23  ? 246 PRO A C   1 
ATOM   1807 O  O   . PRO A  1  233 ? 28.997  -12.857 41.776 1.00 33.68  ? 246 PRO A O   1 
ATOM   1808 C  CB  . PRO A  1  233 ? 28.092  -11.558 38.946 1.00 38.07  ? 246 PRO A CB  1 
ATOM   1809 C  CG  . PRO A  1  233 ? 29.077  -10.602 38.302 1.00 37.25  ? 246 PRO A CG  1 
ATOM   1810 C  CD  . PRO A  1  233 ? 30.085  -10.257 39.396 1.00 37.25  ? 246 PRO A CD  1 
ATOM   1811 N  N   . ASP A  1  234 ? 26.746  -12.687 41.775 1.00 35.04  ? 247 ASP A N   1 
ATOM   1812 C  CA  . ASP A  1  234 ? 26.530  -13.877 42.583 1.00 36.72  ? 247 ASP A CA  1 
ATOM   1813 C  C   . ASP A  1  234 ? 27.205  -15.067 41.912 1.00 38.55  ? 247 ASP A C   1 
ATOM   1814 O  O   . ASP A  1  234 ? 27.086  -15.227 40.704 1.00 36.14  ? 247 ASP A O   1 
ATOM   1815 C  CB  . ASP A  1  234 ? 25.044  -14.168 42.770 1.00 36.29  ? 247 ASP A CB  1 
ATOM   1816 C  CG  . ASP A  1  234 ? 24.273  -13.191 43.649 1.00 36.70  ? 247 ASP A CG  1 
ATOM   1817 O  OD1 . ASP A  1  234 ? 24.889  -12.228 44.179 1.00 37.26  ? 247 ASP A OD1 1 
ATOM   1818 O  OD2 . ASP A  1  234 ? 23.050  -13.391 43.790 1.00 40.04  ? 247 ASP A OD2 1 
ATOM   1819 N  N   . ASP A  1  235 ? 27.905  -15.888 42.711 1.00 39.86  ? 248 ASP A N   1 
ATOM   1820 C  CA  . ASP A  1  235 ? 28.483  -17.143 42.250 1.00 41.96  ? 248 ASP A CA  1 
ATOM   1821 C  C   . ASP A  1  235 ? 29.522  -16.901 41.147 1.00 41.01  ? 248 ASP A C   1 
ATOM   1822 O  O   . ASP A  1  235 ? 29.718  -17.748 40.275 1.00 39.95  ? 248 ASP A O   1 
ATOM   1823 C  CB  . ASP A  1  235 ? 27.394  -18.109 41.796 1.00 43.84  ? 248 ASP A CB  1 
ATOM   1824 C  CG  . ASP A  1  235 ? 27.878  -19.523 41.504 1.00 45.60  ? 248 ASP A CG  1 
ATOM   1825 O  OD1 . ASP A  1  235 ? 28.576  -20.092 42.369 1.00 49.97  ? 248 ASP A OD1 1 
ATOM   1826 O  OD2 . ASP A  1  235 ? 27.577  -20.031 40.406 1.00 47.59  ? 248 ASP A OD2 1 
ATOM   1827 N  N   . PHE A  1  236 ? 30.205  -15.755 41.191 1.00 38.34  ? 249 PHE A N   1 
ATOM   1828 C  CA  . PHE A  1  236 ? 31.092  -15.363 40.111 1.00 38.18  ? 249 PHE A CA  1 
ATOM   1829 C  C   . PHE A  1  236 ? 32.292  -16.296 40.054 1.00 35.75  ? 249 PHE A C   1 
ATOM   1830 O  O   . PHE A  1  236 ? 32.961  -16.493 41.058 1.00 34.80  ? 249 PHE A O   1 
ATOM   1831 C  CB  . PHE A  1  236 ? 31.607  -13.930 40.253 1.00 39.62  ? 249 PHE A CB  1 
ATOM   1832 C  CG  . PHE A  1  236 ? 32.495  -13.498 39.097 1.00 39.04  ? 249 PHE A CG  1 
ATOM   1833 C  CD1 . PHE A  1  236 ? 31.958  -13.278 37.835 1.00 38.53  ? 249 PHE A CD1 1 
ATOM   1834 C  CD2 . PHE A  1  236 ? 33.862  -13.320 39.281 1.00 39.43  ? 249 PHE A CD2 1 
ATOM   1835 C  CE1 . PHE A  1  236 ? 32.773  -12.896 36.782 1.00 39.31  ? 249 PHE A CE1 1 
ATOM   1836 C  CE2 . PHE A  1  236 ? 34.672  -12.929 38.228 1.00 37.43  ? 249 PHE A CE2 1 
ATOM   1837 C  CZ  . PHE A  1  236 ? 34.124  -12.702 36.992 1.00 38.95  ? 249 PHE A CZ  1 
ATOM   1838 N  N   . HIS A  1  237 ? 32.550  -16.837 38.858 1.00 37.27  ? 250 HIS A N   1 
ATOM   1839 C  CA  . HIS A  1  237 ? 33.736  -17.637 38.588 1.00 38.63  ? 250 HIS A CA  1 
ATOM   1840 C  C   . HIS A  1  237 ? 34.668  -16.843 37.679 1.00 36.89  ? 250 HIS A C   1 
ATOM   1841 O  O   . HIS A  1  237 ? 34.255  -16.352 36.634 1.00 37.13  ? 250 HIS A O   1 
ATOM   1842 C  CB  . HIS A  1  237 ? 33.371  -18.993 37.967 1.00 38.83  ? 250 HIS A CB  1 
ATOM   1843 C  CG  . HIS A  1  237 ? 32.804  -19.984 38.925 1.00 41.83  ? 250 HIS A CG  1 
ATOM   1844 N  ND1 . HIS A  1  237 ? 31.718  -19.722 39.730 1.00 45.35  ? 250 HIS A ND1 1 
ATOM   1845 C  CD2 . HIS A  1  237 ? 33.166  -21.256 39.188 1.00 43.00  ? 250 HIS A CD2 1 
ATOM   1846 C  CE1 . HIS A  1  237 ? 31.455  -20.799 40.470 1.00 46.66  ? 250 HIS A CE1 1 
ATOM   1847 N  NE2 . HIS A  1  237 ? 32.324  -21.744 40.156 1.00 43.53  ? 250 HIS A NE2 1 
ATOM   1848 N  N   . ARG A  1  238 ? 35.945  -16.760 38.068 1.00 35.33  ? 251 ARG A N   1 
ATOM   1849 C  CA  . ARG A  1  238 ? 36.933  -16.022 37.300 1.00 35.77  ? 251 ARG A CA  1 
ATOM   1850 C  C   . ARG A  1  238 ? 37.193  -16.720 35.966 1.00 37.62  ? 251 ARG A C   1 
ATOM   1851 O  O   . ARG A  1  238 ? 36.887  -17.895 35.808 1.00 36.97  ? 251 ARG A O   1 
ATOM   1852 C  CB  . ARG A  1  238 ? 38.253  -15.907 38.067 1.00 37.01  ? 251 ARG A CB  1 
ATOM   1853 C  CG  . ARG A  1  238 ? 38.949  -17.241 38.301 1.00 37.97  ? 251 ARG A CG  1 
ATOM   1854 C  CD  . ARG A  1  238 ? 40.243  -17.092 39.072 1.00 37.74  ? 251 ARG A CD  1 
ATOM   1855 N  NE  . ARG A  1  238 ? 41.106  -18.260 38.900 1.00 38.29  ? 251 ARG A NE  1 
ATOM   1856 C  CZ  . ARG A  1  238 ? 42.264  -18.473 39.522 1.00 39.14  ? 251 ARG A CZ  1 
ATOM   1857 N  NH1 . ARG A  1  238 ? 42.738  -17.585 40.382 1.00 41.88  ? 251 ARG A NH1 1 
ATOM   1858 N  NH2 . ARG A  1  238 ? 42.933  -19.596 39.293 1.00 38.22  ? 251 ARG A NH2 1 
ATOM   1859 N  N   . SER A  1  239 ? 37.784  -15.970 35.026 1.00 37.39  ? 252 SER A N   1 
ATOM   1860 C  CA  . SER A  1  239 ? 38.310  -16.492 33.776 1.00 37.56  ? 252 SER A CA  1 
ATOM   1861 C  C   . SER A  1  239 ? 38.996  -17.841 33.990 1.00 38.83  ? 252 SER A C   1 
ATOM   1862 O  O   . SER A  1  239 ? 39.717  -18.023 34.969 1.00 37.00  ? 252 SER A O   1 
ATOM   1863 C  CB  . SER A  1  239 ? 39.280  -15.512 33.175 1.00 36.24  ? 252 SER A CB  1 
ATOM   1864 O  OG  . SER A  1  239 ? 39.854  -16.029 31.988 1.00 37.70  ? 252 SER A OG  1 
ATOM   1865 N  N   . ALA A  1  240 ? 38.783  -18.757 33.039 1.00 40.61  ? 253 ALA A N   1 
ATOM   1866 C  CA  . ALA A  1  240 ? 39.310  -20.113 33.101 1.00 42.00  ? 253 ALA A CA  1 
ATOM   1867 C  C   . ALA A  1  240 ? 40.786  -20.143 32.716 1.00 40.14  ? 253 ALA A C   1 
ATOM   1868 O  O   . ALA A  1  240 ? 41.443  -21.160 32.905 1.00 42.10  ? 253 ALA A O   1 
ATOM   1869 C  CB  . ALA A  1  240 ? 38.504  -21.022 32.191 1.00 42.92  ? 253 ALA A CB  1 
ATOM   1870 N  N   . VAL A  1  241 ? 41.294  -19.035 32.159 1.00 41.82  ? 254 VAL A N   1 
ATOM   1871 C  CA  . VAL A  1  241 ? 42.706  -18.897 31.836 1.00 40.49  ? 254 VAL A CA  1 
ATOM   1872 C  C   . VAL A  1  241 ? 43.181  -17.516 32.275 1.00 40.17  ? 254 VAL A C   1 
ATOM   1873 O  O   . VAL A  1  241 ? 42.397  -16.569 32.309 1.00 38.43  ? 254 VAL A O   1 
ATOM   1874 C  CB  . VAL A  1  241 ? 42.985  -19.087 30.334 1.00 46.20  ? 254 VAL A CB  1 
ATOM   1875 C  CG1 . VAL A  1  241 ? 42.653  -20.501 29.861 1.00 47.94  ? 254 VAL A CG1 1 
ATOM   1876 C  CG2 . VAL A  1  241 ? 42.238  -18.064 29.484 1.00 47.49  ? 254 VAL A CG2 1 
ATOM   1877 N  N   . PRO A  1  242 ? 44.488  -17.350 32.574 1.00 37.80  ? 255 PRO A N   1 
ATOM   1878 C  CA  . PRO A  1  242 ? 45.075  -16.022 32.733 1.00 37.81  ? 255 PRO A CA  1 
ATOM   1879 C  C   . PRO A  1  242 ? 44.731  -15.191 31.505 1.00 38.49  ? 255 PRO A C   1 
ATOM   1880 O  O   . PRO A  1  242 ? 44.829  -15.685 30.384 1.00 37.76  ? 255 PRO A O   1 
ATOM   1881 C  CB  . PRO A  1  242 ? 46.581  -16.302 32.861 1.00 37.96  ? 255 PRO A CB  1 
ATOM   1882 C  CG  . PRO A  1  242 ? 46.637  -17.715 33.415 1.00 38.38  ? 255 PRO A CG  1 
ATOM   1883 C  CD  . PRO A  1  242 ? 45.474  -18.427 32.748 1.00 39.11  ? 255 PRO A CD  1 
ATOM   1884 N  N   . ALA A  1  243 ? 44.307  -13.944 31.723 1.00 36.35  ? 256 ALA A N   1 
ATOM   1885 C  CA  . ALA A  1  243 ? 43.911  -13.091 30.617 1.00 36.80  ? 256 ALA A CA  1 
ATOM   1886 C  C   . ALA A  1  243 ? 44.130  -11.630 30.979 1.00 37.89  ? 256 ALA A C   1 
ATOM   1887 O  O   . ALA A  1  243 ? 44.355  -11.283 32.140 1.00 34.90  ? 256 ALA A O   1 
ATOM   1888 C  CB  . ALA A  1  243 ? 42.466  -13.346 30.242 1.00 39.93  ? 256 ALA A CB  1 
ATOM   1889 N  N   . SER A  1  244 ? 44.072  -10.791 29.939 1.00 36.00  ? 257 SER A N   1 
ATOM   1890 C  CA  . SER A  1  244 ? 44.282  -9.364  30.068 1.00 34.11  ? 257 SER A CA  1 
ATOM   1891 C  C   . SER A  1  244 ? 43.615  -8.678  28.884 1.00 34.33  ? 257 SER A C   1 
ATOM   1892 O  O   . SER A  1  244 ? 42.389  -8.551  28.862 1.00 35.44  ? 257 SER A O   1 
ATOM   1893 C  CB  . SER A  1  244 ? 45.758  -9.033  30.206 1.00 35.46  ? 257 SER A CB  1 
ATOM   1894 O  OG  . SER A  1  244 ? 46.528  -9.563  29.130 1.00 35.72  ? 257 SER A OG  1 
ATOM   1895 N  N   . ASN A  1  245 ? 44.407  -8.292  27.881 1.00 35.71  ? 258 ASN A N   1 
ATOM   1896 C  CA  . ASN A  1  245 ? 43.962  -7.353  26.860 1.00 37.33  ? 258 ASN A CA  1 
ATOM   1897 C  C   . ASN A  1  245 ? 43.675  -8.042  25.525 1.00 37.62  ? 258 ASN A C   1 
ATOM   1898 O  O   . ASN A  1  245 ? 43.777  -7.403  24.484 1.00 39.03  ? 258 ASN A O   1 
ATOM   1899 C  CB  . ASN A  1  245 ? 44.986  -6.241  26.657 1.00 40.86  ? 258 ASN A CB  1 
ATOM   1900 C  CG  . ASN A  1  245 ? 46.305  -6.762  26.128 1.00 45.02  ? 258 ASN A CG  1 
ATOM   1901 O  OD1 . ASN A  1  245 ? 46.589  -7.959  26.229 1.00 45.80  ? 258 ASN A OD1 1 
ATOM   1902 N  ND2 . ASN A  1  245 ? 47.120  -5.896  25.549 1.00 53.63  ? 258 ASN A ND2 1 
ATOM   1903 N  N   . GLU A  1  246 ? 43.289  -9.323  25.548 1.00 38.73  ? 259 GLU A N   1 
ATOM   1904 C  CA  . GLU A  1  246 ? 42.982  -10.032 24.314 1.00 40.31  ? 259 GLU A CA  1 
ATOM   1905 C  C   . GLU A  1  246 ? 41.848  -9.298  23.604 1.00 42.38  ? 259 GLU A C   1 
ATOM   1906 O  O   . GLU A  1  246 ? 40.814  -9.021  24.207 1.00 39.80  ? 259 GLU A O   1 
ATOM   1907 C  CB  . GLU A  1  246 ? 42.587  -11.493 24.552 1.00 41.22  ? 259 GLU A CB  1 
ATOM   1908 C  CG  . GLU A  1  246 ? 43.745  -12.373 25.023 1.00 47.47  ? 259 GLU A CG  1 
ATOM   1909 C  CD  . GLU A  1  246 ? 44.116  -12.248 26.494 1.00 46.98  ? 259 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A  1  246 ? 43.463  -11.453 27.191 1.00 45.40  ? 259 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A  1  246 ? 45.036  -12.951 26.959 1.00 54.58  ? 259 GLU A OE2 1 
ATOM   1912 N  N   . GLY A  1  247 ? 42.067  -8.967  22.324 1.00 43.28  ? 260 GLY A N   1 
ATOM   1913 C  CA  . GLY A  1  247 ? 41.042  -8.356  21.488 1.00 41.58  ? 260 GLY A CA  1 
ATOM   1914 C  C   . GLY A  1  247 ? 41.178  -6.839  21.381 1.00 43.67  ? 260 GLY A C   1 
ATOM   1915 O  O   . GLY A  1  247 ? 40.442  -6.219  20.623 1.00 47.15  ? 260 GLY A O   1 
ATOM   1916 N  N   . ALA A  1  248 ? 42.119  -6.238  22.122 1.00 43.29  ? 261 ALA A N   1 
ATOM   1917 C  CA  . ALA A  1  248 ? 42.282  -4.789  22.136 1.00 46.56  ? 261 ALA A CA  1 
ATOM   1918 C  C   . ALA A  1  248 ? 42.696  -4.262  20.759 1.00 46.39  ? 261 ALA A C   1 
ATOM   1919 O  O   . ALA A  1  248 ? 42.325  -3.155  20.373 1.00 44.65  ? 261 ALA A O   1 
ATOM   1920 C  CB  . ALA A  1  248 ? 43.290  -4.393  23.201 1.00 47.80  ? 261 ALA A CB  1 
ATOM   1921 N  N   . ASP A  1  249 ? 43.486  -5.062  20.037 1.00 48.98  ? 262 ASP A N   1 
ATOM   1922 C  CA  . ASP A  1  249 ? 43.860  -4.799  18.652 1.00 52.41  ? 262 ASP A CA  1 
ATOM   1923 C  C   . ASP A  1  249 ? 42.626  -4.565  17.770 1.00 48.52  ? 262 ASP A C   1 
ATOM   1924 O  O   . ASP A  1  249 ? 42.632  -3.673  16.925 1.00 52.42  ? 262 ASP A O   1 
ATOM   1925 C  CB  . ASP A  1  249 ? 44.748  -5.915  18.113 1.00 55.03  ? 262 ASP A CB  1 
ATOM   1926 C  CG  . ASP A  1  249 ? 44.241  -7.342  18.315 1.00 62.77  ? 262 ASP A CG  1 
ATOM   1927 O  OD1 . ASP A  1  249 ? 43.157  -7.521  18.925 1.00 58.29  ? 262 ASP A OD1 1 
ATOM   1928 O  OD2 . ASP A  1  249 ? 44.937  -8.280  17.864 1.00 70.73  ? 262 ASP A OD2 1 
ATOM   1929 N  N   . GLN A  1  250 ? 41.577  -5.370  17.956 1.00 46.62  ? 263 GLN A N   1 
ATOM   1930 C  CA  . GLN A  1  250 ? 40.381  -5.296  17.124 1.00 46.72  ? 263 GLN A CA  1 
ATOM   1931 C  C   . GLN A  1  250 ? 39.554  -4.054  17.451 1.00 46.78  ? 263 GLN A C   1 
ATOM   1932 O  O   . GLN A  1  250 ? 38.839  -3.556  16.585 1.00 53.32  ? 263 GLN A O   1 
ATOM   1933 C  CB  . GLN A  1  250 ? 39.476  -6.513  17.299 1.00 45.39  ? 263 GLN A CB  1 
ATOM   1934 C  CG  . GLN A  1  250 ? 40.087  -7.816  16.800 1.00 50.96  ? 263 GLN A CG  1 
ATOM   1935 C  CD  . GLN A  1  250 ? 39.220  -9.023  17.089 1.00 53.73  ? 263 GLN A CD  1 
ATOM   1936 O  OE1 . GLN A  1  250 ? 38.059  -9.079  16.674 1.00 54.80  ? 263 GLN A OE1 1 
ATOM   1937 N  NE2 . GLN A  1  250 ? 39.763  -9.999  17.808 1.00 52.08  ? 263 GLN A NE2 1 
ATOM   1938 N  N   . VAL A  1  251 ? 39.635  -3.585  18.704 1.00 45.64  ? 264 VAL A N   1 
ATOM   1939 C  CA  . VAL A  1  251 ? 38.948  -2.377  19.133 1.00 43.24  ? 264 VAL A CA  1 
ATOM   1940 C  C   . VAL A  1  251 ? 39.541  -1.178  18.398 1.00 42.86  ? 264 VAL A C   1 
ATOM   1941 O  O   . VAL A  1  251 ? 38.806  -0.312  17.923 1.00 42.59  ? 264 VAL A O   1 
ATOM   1942 C  CB  . VAL A  1  251 ? 39.032  -2.185  20.662 1.00 44.84  ? 264 VAL A CB  1 
ATOM   1943 C  CG1 . VAL A  1  251 ? 38.525  -0.820  21.114 1.00 42.89  ? 264 VAL A CG1 1 
ATOM   1944 C  CG2 . VAL A  1  251 ? 38.297  -3.286  21.412 1.00 46.74  ? 264 VAL A CG2 1 
ATOM   1945 N  N   . LEU A  1  252 ? 40.878  -1.123  18.344 1.00 42.33  ? 265 LEU A N   1 
ATOM   1946 C  CA  . LEU A  1  252 ? 41.580  -0.094  17.604 1.00 45.69  ? 265 LEU A CA  1 
ATOM   1947 C  C   . LEU A  1  252 ? 41.243  -0.204  16.118 1.00 45.51  ? 265 LEU A C   1 
ATOM   1948 O  O   . LEU A  1  252 ? 40.962  0.812   15.488 1.00 49.83  ? 265 LEU A O   1 
ATOM   1949 C  CB  . LEU A  1  252 ? 43.085  -0.196  17.841 1.00 50.65  ? 265 LEU A CB  1 
ATOM   1950 C  CG  . LEU A  1  252 ? 43.929  0.928   17.227 1.00 52.07  ? 265 LEU A CG  1 
ATOM   1951 C  CD1 . LEU A  1  252 ? 43.628  2.277   17.885 1.00 51.13  ? 265 LEU A CD1 1 
ATOM   1952 C  CD2 . LEU A  1  252 ? 45.415  0.598   17.346 1.00 52.79  ? 265 LEU A CD2 1 
ATOM   1953 N  N   . ALA A  1  253 ? 41.255  -1.430  15.575 1.00 43.71  ? 266 ALA A N   1 
ATOM   1954 C  CA  . ALA A  1  253 ? 41.045  -1.650  14.150 1.00 45.58  ? 266 ALA A CA  1 
ATOM   1955 C  C   . ALA A  1  253 ? 39.661  -1.171  13.705 1.00 50.21  ? 266 ALA A C   1 
ATOM   1956 O  O   . ALA A  1  253 ? 39.512  -0.691  12.583 1.00 51.31  ? 266 ALA A O   1 
ATOM   1957 C  CB  . ALA A  1  253 ? 41.255  -3.110  13.805 1.00 47.16  ? 266 ALA A CB  1 
ATOM   1958 N  N   . ALA A  1  254 ? 38.655  -1.281  14.583 1.00 52.32  ? 267 ALA A N   1 
ATOM   1959 C  CA  . ALA A  1  254 ? 37.297  -0.862  14.257 1.00 51.73  ? 267 ALA A CA  1 
ATOM   1960 C  C   . ALA A  1  254 ? 37.222  0.645   13.988 1.00 51.35  ? 267 ALA A C   1 
ATOM   1961 O  O   . ALA A  1  254 ? 36.386  1.084   13.206 1.00 51.24  ? 267 ALA A O   1 
ATOM   1962 C  CB  . ALA A  1  254 ? 36.350  -1.266  15.367 1.00 50.85  ? 267 ALA A CB  1 
ATOM   1963 N  N   . HIS A  1  255 ? 38.068  1.436   14.659 1.00 50.36  ? 268 HIS A N   1 
ATOM   1964 C  CA  . HIS A  1  255 ? 38.110  2.873   14.441 1.00 51.17  ? 268 HIS A CA  1 
ATOM   1965 C  C   . HIS A  1  255 ? 39.538  3.368   14.639 1.00 49.63  ? 268 HIS A C   1 
ATOM   1966 O  O   . HIS A  1  255 ? 39.872  3.906   15.692 1.00 53.94  ? 268 HIS A O   1 
ATOM   1967 C  CB  . HIS A  1  255 ? 37.128  3.619   15.352 1.00 52.89  ? 268 HIS A CB  1 
ATOM   1968 C  CG  . HIS A  1  255 ? 35.694  3.441   14.981 1.00 53.51  ? 268 HIS A CG  1 
ATOM   1969 N  ND1 . HIS A  1  255 ? 35.118  4.149   13.950 1.00 59.19  ? 268 HIS A ND1 1 
ATOM   1970 C  CD2 . HIS A  1  255 ? 34.722  2.665   15.487 1.00 55.62  ? 268 HIS A CD2 1 
ATOM   1971 C  CE1 . HIS A  1  255 ? 33.842  3.803   13.845 1.00 57.27  ? 268 HIS A CE1 1 
ATOM   1972 N  NE2 . HIS A  1  255 ? 33.577  2.909   14.775 1.00 54.97  ? 268 HIS A NE2 1 
ATOM   1973 N  N   . PRO A  1  256 ? 40.424  3.180   13.634 1.00 49.82  ? 269 PRO A N   1 
ATOM   1974 C  CA  . PRO A  1  256 ? 41.827  3.579   13.759 1.00 50.35  ? 269 PRO A CA  1 
ATOM   1975 C  C   . PRO A  1  256 ? 41.956  4.987   14.324 1.00 47.74  ? 269 PRO A C   1 
ATOM   1976 O  O   . PRO A  1  256 ? 41.220  5.894   13.940 1.00 44.95  ? 269 PRO A O   1 
ATOM   1977 C  CB  . PRO A  1  256 ? 42.346  3.473   12.318 1.00 54.40  ? 269 PRO A CB  1 
ATOM   1978 C  CG  . PRO A  1  256 ? 41.511  2.357   11.724 1.00 54.18  ? 269 PRO A CG  1 
ATOM   1979 C  CD  . PRO A  1  256 ? 40.127  2.539   12.343 1.00 50.48  ? 269 PRO A CD  1 
ATOM   1980 N  N   . TRP A  1  257 ? 42.884  5.145   15.265 1.00 46.23  ? 270 TRP A N   1 
ATOM   1981 C  CA  . TRP A  1  257 ? 43.041  6.402   15.970 1.00 45.43  ? 270 TRP A CA  1 
ATOM   1982 C  C   . TRP A  1  257 ? 44.510  6.607   16.342 1.00 46.40  ? 270 TRP A C   1 
ATOM   1983 O  O   . TRP A  1  257 ? 45.241  5.648   16.577 1.00 49.23  ? 270 TRP A O   1 
ATOM   1984 C  CB  . TRP A  1  257 ? 42.123  6.430   17.200 1.00 45.27  ? 270 TRP A CB  1 
ATOM   1985 C  CG  . TRP A  1  257 ? 42.023  7.807   17.794 1.00 42.17  ? 270 TRP A CG  1 
ATOM   1986 C  CD1 . TRP A  1  257 ? 42.655  8.277   18.902 1.00 42.41  ? 270 TRP A CD1 1 
ATOM   1987 C  CD2 . TRP A  1  257 ? 41.289  8.919   17.243 1.00 43.91  ? 270 TRP A CD2 1 
ATOM   1988 N  NE1 . TRP A  1  257 ? 42.358  9.598   19.095 1.00 44.09  ? 270 TRP A NE1 1 
ATOM   1989 C  CE2 . TRP A  1  257 ? 41.531  10.022  18.092 1.00 43.46  ? 270 TRP A CE2 1 
ATOM   1990 C  CE3 . TRP A  1  257 ? 40.460  9.085   16.126 1.00 46.60  ? 270 TRP A CE3 1 
ATOM   1991 C  CZ2 . TRP A  1  257 ? 40.974  11.274  17.857 1.00 47.80  ? 270 TRP A CZ2 1 
ATOM   1992 C  CZ3 . TRP A  1  257 ? 39.910  10.328  15.894 1.00 47.72  ? 270 TRP A CZ3 1 
ATOM   1993 C  CH2 . TRP A  1  257 ? 40.172  11.407  16.743 1.00 48.31  ? 270 TRP A CH2 1 
ATOM   1994 N  N   . VAL A  1  258 ? 44.922  7.871   16.383 1.00 47.30  ? 271 VAL A N   1 
ATOM   1995 C  CA  . VAL A  1  258 ? 46.310  8.233   16.591 1.00 52.12  ? 271 VAL A CA  1 
ATOM   1996 C  C   . VAL A  1  258 ? 46.413  9.003   17.904 1.00 47.47  ? 271 VAL A C   1 
ATOM   1997 O  O   . VAL A  1  258 ? 45.547  9.819   18.209 1.00 47.71  ? 271 VAL A O   1 
ATOM   1998 C  CB  . VAL A  1  258 ? 46.823  9.059   15.393 1.00 56.02  ? 271 VAL A CB  1 
ATOM   1999 C  CG1 . VAL A  1  258 ? 48.221  9.615   15.627 1.00 60.69  ? 271 VAL A CG1 1 
ATOM   2000 C  CG2 . VAL A  1  258 ? 46.808  8.243   14.109 1.00 58.19  ? 271 VAL A CG2 1 
ATOM   2001 N  N   . PRO A  1  259 ? 47.458  8.761   18.723 1.00 46.18  ? 272 PRO A N   1 
ATOM   2002 C  CA  . PRO A  1  259 ? 47.644  9.512   19.960 1.00 49.11  ? 272 PRO A CA  1 
ATOM   2003 C  C   . PRO A  1  259 ? 47.768  11.007  19.683 1.00 49.93  ? 272 PRO A C   1 
ATOM   2004 O  O   . PRO A  1  259 ? 48.293  11.413  18.650 1.00 52.87  ? 272 PRO A O   1 
ATOM   2005 C  CB  . PRO A  1  259 ? 48.925  8.911   20.582 1.00 48.02  ? 272 PRO A CB  1 
ATOM   2006 C  CG  . PRO A  1  259 ? 49.620  8.236   19.421 1.00 47.42  ? 272 PRO A CG  1 
ATOM   2007 C  CD  . PRO A  1  259 ? 48.490  7.729   18.536 1.00 47.93  ? 272 PRO A CD  1 
ATOM   2008 N  N   . GLY A  1  260 ? 47.291  11.809  20.637 1.00 50.31  ? 273 GLY A N   1 
ATOM   2009 C  CA  . GLY A  1  260 ? 47.296  13.252  20.522 1.00 50.94  ? 273 GLY A CA  1 
ATOM   2010 C  C   . GLY A  1  260 ? 46.446  13.885  21.616 1.00 54.65  ? 273 GLY A C   1 
ATOM   2011 O  O   . GLY A  1  260 ? 46.320  13.327  22.703 1.00 52.68  ? 273 GLY A O   1 
ATOM   2012 N  N   . GLY A  1  261 ? 45.865  15.048  21.303 1.00 56.06  ? 274 GLY A N   1 
ATOM   2013 C  CA  . GLY A  1  261 ? 45.052  15.793  22.248 1.00 60.33  ? 274 GLY A CA  1 
ATOM   2014 C  C   . GLY A  1  261 ? 44.505  17.076  21.627 1.00 58.78  ? 274 GLY A C   1 
ATOM   2015 O  O   . GLY A  1  261 ? 44.952  17.497  20.565 1.00 59.64  ? 274 GLY A O   1 
ATOM   2016 N  N   . ASN A  1  262 ? 43.511  17.674  22.293 1.00 56.71  ? 275 ASN A N   1 
ATOM   2017 C  CA  . ASN A  1  262 ? 43.041  19.009  21.958 1.00 56.22  ? 275 ASN A CA  1 
ATOM   2018 C  C   . ASN A  1  262 ? 44.146  20.015  22.271 1.00 56.47  ? 275 ASN A C   1 
ATOM   2019 O  O   . ASN A  1  262 ? 44.638  20.048  23.392 1.00 52.02  ? 275 ASN A O   1 
ATOM   2020 C  CB  . ASN A  1  262 ? 41.783  19.380  22.735 1.00 52.61  ? 275 ASN A CB  1 
ATOM   2021 C  CG  . ASN A  1  262 ? 40.507  18.889  22.094 1.00 53.38  ? 275 ASN A CG  1 
ATOM   2022 O  OD1 . ASN A  1  262 ? 40.471  18.608  20.891 1.00 54.77  ? 275 ASN A OD1 1 
ATOM   2023 N  ND2 . ASN A  1  262 ? 39.436  18.807  22.872 1.00 54.64  ? 275 ASN A ND2 1 
ATOM   2024 N  N   . ALA A  1  263 ? 44.518  20.837  21.280 1.00 60.19  ? 276 ALA A N   1 
ATOM   2025 C  CA  . ALA A  1  263 ? 45.572  21.825  21.463 1.00 63.71  ? 276 ALA A CA  1 
ATOM   2026 C  C   . ALA A  1  263 ? 44.981  23.183  21.843 1.00 61.97  ? 276 ALA A C   1 
ATOM   2027 O  O   . ALA A  1  263 ? 43.828  23.485  21.523 1.00 59.87  ? 276 ALA A O   1 
ATOM   2028 C  CB  . ALA A  1  263 ? 46.410  21.925  20.209 1.00 66.43  ? 276 ALA A CB  1 
ATOM   2029 N  N   . ASP A  1  264 ? 45.787  23.965  22.577 1.00 69.87  ? 277 ASP A N   1 
ATOM   2030 C  CA  . ASP A  1  264 ? 45.539  25.375  22.841 1.00 73.14  ? 277 ASP A CA  1 
ATOM   2031 C  C   . ASP A  1  264 ? 44.198  25.585  23.536 1.00 70.61  ? 277 ASP A C   1 
ATOM   2032 O  O   . ASP A  1  264 ? 43.480  26.530  23.213 1.00 70.19  ? 277 ASP A O   1 
ATOM   2033 C  CB  . ASP A  1  264 ? 45.654  26.200  21.569 1.00 82.58  ? 277 ASP A CB  1 
ATOM   2034 C  CG  . ASP A  1  264 ? 47.010  26.111  20.878 1.00 96.29  ? 277 ASP A CG  1 
ATOM   2035 O  OD1 . ASP A  1  264 ? 48.029  26.386  21.556 1.00 101.97 ? 277 ASP A OD1 1 
ATOM   2036 O  OD2 . ASP A  1  264 ? 47.040  25.770  19.669 1.00 103.16 ? 277 ASP A OD2 1 
ATOM   2037 N  N   . ASN A  1  265 ? 43.885  24.698  24.489 1.00 64.96  ? 278 ASN A N   1 
ATOM   2038 C  CA  . ASN A  1  265 ? 42.764  24.873  25.398 1.00 61.98  ? 278 ASN A CA  1 
ATOM   2039 C  C   . ASN A  1  265 ? 41.468  25.117  24.622 1.00 57.33  ? 278 ASN A C   1 
ATOM   2040 O  O   . ASN A  1  265 ? 40.629  25.896  25.059 1.00 54.64  ? 278 ASN A O   1 
ATOM   2041 C  CB  . ASN A  1  265 ? 43.066  25.982  26.402 1.00 67.78  ? 278 ASN A CB  1 
ATOM   2042 C  CG  . ASN A  1  265 ? 42.326  25.802  27.707 1.00 77.14  ? 278 ASN A CG  1 
ATOM   2043 O  OD1 . ASN A  1  265 ? 41.956  24.679  28.080 1.00 84.99  ? 278 ASN A OD1 1 
ATOM   2044 N  ND2 . ASN A  1  265 ? 42.130  26.892  28.433 1.00 84.44  ? 278 ASN A ND2 1 
ATOM   2045 N  N   . GLN A  1  266 ? 41.300  24.415  23.494 1.00 57.15  ? 279 GLN A N   1 
ATOM   2046 C  CA  . GLN A  1  266 ? 40.125  24.546  22.651 1.00 63.87  ? 279 GLN A CA  1 
ATOM   2047 C  C   . GLN A  1  266 ? 39.540  23.168  22.364 1.00 59.38  ? 279 GLN A C   1 
ATOM   2048 O  O   . GLN A  1  266 ? 40.284  22.226  22.123 1.00 54.65  ? 279 GLN A O   1 
ATOM   2049 C  CB  . GLN A  1  266 ? 40.471  25.196  21.310 1.00 73.95  ? 279 GLN A CB  1 
ATOM   2050 C  CG  . GLN A  1  266 ? 40.647  26.708  21.403 1.00 80.18  ? 279 GLN A CG  1 
ATOM   2051 C  CD  . GLN A  1  266 ? 41.070  27.348  20.101 1.00 87.53  ? 279 GLN A CD  1 
ATOM   2052 O  OE1 . GLN A  1  266 ? 41.259  26.691  19.070 1.00 83.46  ? 279 GLN A OE1 1 
ATOM   2053 N  NE2 . GLN A  1  266 ? 41.212  28.662  20.141 1.00 94.41  ? 279 GLN A NE2 1 
ATOM   2054 N  N   . VAL A  1  267 ? 38.206  23.084  22.347 1.00 53.01  ? 280 VAL A N   1 
ATOM   2055 C  CA  . VAL A  1  267 ? 37.516  21.866  21.956 1.00 55.65  ? 280 VAL A CA  1 
ATOM   2056 C  C   . VAL A  1  267 ? 37.623  21.690  20.440 1.00 59.65  ? 280 VAL A C   1 
ATOM   2057 O  O   . VAL A  1  267 ? 38.047  22.598  19.731 1.00 66.34  ? 280 VAL A O   1 
ATOM   2058 C  CB  . VAL A  1  267 ? 36.047  21.850  22.422 1.00 57.83  ? 280 VAL A CB  1 
ATOM   2059 C  CG1 . VAL A  1  267 ? 35.935  21.817  23.938 1.00 56.29  ? 280 VAL A CG1 1 
ATOM   2060 C  CG2 . VAL A  1  267 ? 35.240  23.018  21.865 1.00 61.38  ? 280 VAL A CG2 1 
ATOM   2061 N  N   . ASN A  1  268 ? 37.244  20.498  19.963 1.00 57.77  ? 281 ASN A N   1 
ATOM   2062 C  CA  . ASN A  1  268 ? 37.248  20.155  18.549 1.00 60.30  ? 281 ASN A CA  1 
ATOM   2063 C  C   . ASN A  1  268 ? 38.544  20.611  17.881 1.00 60.36  ? 281 ASN A C   1 
ATOM   2064 O  O   . ASN A  1  268 ? 38.509  21.197  16.806 1.00 58.52  ? 281 ASN A O   1 
ATOM   2065 C  CB  . ASN A  1  268 ? 36.022  20.725  17.843 1.00 61.50  ? 281 ASN A CB  1 
ATOM   2066 C  CG  . ASN A  1  268 ? 34.742  20.102  18.345 1.00 62.59  ? 281 ASN A CG  1 
ATOM   2067 O  OD1 . ASN A  1  268 ? 34.493  18.912  18.119 1.00 68.08  ? 281 ASN A OD1 1 
ATOM   2068 N  ND2 . ASN A  1  268 ? 33.914  20.885  19.017 1.00 61.88  ? 281 ASN A ND2 1 
ATOM   2069 N  N   . ASN A  1  269 ? 39.684  20.304  18.507 1.00 61.71  ? 282 ASN A N   1 
ATOM   2070 C  CA  . ASN A  1  269 ? 40.972  20.787  18.037 1.00 56.79  ? 282 ASN A CA  1 
ATOM   2071 C  C   . ASN A  1  269 ? 42.041  19.724  18.295 1.00 54.69  ? 282 ASN A C   1 
ATOM   2072 O  O   . ASN A  1  269 ? 43.071  20.009  18.906 1.00 50.75  ? 282 ASN A O   1 
ATOM   2073 C  CB  . ASN A  1  269 ? 41.302  22.133  18.681 1.00 57.21  ? 282 ASN A CB  1 
ATOM   2074 C  CG  . ASN A  1  269 ? 42.457  22.827  17.992 1.00 55.26  ? 282 ASN A CG  1 
ATOM   2075 O  OD1 . ASN A  1  269 ? 42.640  22.668  16.781 1.00 54.42  ? 282 ASN A OD1 1 
ATOM   2076 N  ND2 . ASN A  1  269 ? 43.258  23.578  18.736 1.00 56.40  ? 282 ASN A ND2 1 
ATOM   2077 N  N   . TYR A  1  270 ? 41.793  18.502  17.808 1.00 55.72  ? 283 TYR A N   1 
ATOM   2078 C  CA  . TYR A  1  270 ? 42.649  17.366  18.116 1.00 57.84  ? 283 TYR A CA  1 
ATOM   2079 C  C   . TYR A  1  270 ? 43.846  17.358  17.167 1.00 54.02  ? 283 TYR A C   1 
ATOM   2080 O  O   . TYR A  1  270 ? 43.672  17.259  15.957 1.00 52.37  ? 283 TYR A O   1 
ATOM   2081 C  CB  . TYR A  1  270 ? 41.852  16.058  18.032 1.00 55.54  ? 283 TYR A CB  1 
ATOM   2082 C  CG  . TYR A  1  270 ? 42.572  14.824  18.563 1.00 54.00  ? 283 TYR A CG  1 
ATOM   2083 C  CD1 . TYR A  1  270 ? 42.576  14.523  19.920 1.00 54.88  ? 283 TYR A CD1 1 
ATOM   2084 C  CD2 . TYR A  1  270 ? 43.238  13.948  17.710 1.00 55.75  ? 283 TYR A CD2 1 
ATOM   2085 C  CE1 . TYR A  1  270 ? 43.226  13.399  20.411 1.00 53.03  ? 283 TYR A CE1 1 
ATOM   2086 C  CE2 . TYR A  1  270 ? 43.895  12.824  18.190 1.00 53.30  ? 283 TYR A CE2 1 
ATOM   2087 C  CZ  . TYR A  1  270 ? 43.876  12.542  19.545 1.00 51.69  ? 283 TYR A CZ  1 
ATOM   2088 O  OH  . TYR A  1  270 ? 44.506  11.435  20.033 1.00 50.63  ? 283 TYR A OH  1 
ATOM   2089 N  N   . VAL A  1  271 ? 45.051  17.436  17.744 1.00 55.04  ? 284 VAL A N   1 
ATOM   2090 C  CA  . VAL A  1  271 ? 46.308  17.400  17.013 1.00 54.35  ? 284 VAL A CA  1 
ATOM   2091 C  C   . VAL A  1  271 ? 47.048  16.115  17.376 1.00 53.64  ? 284 VAL A C   1 
ATOM   2092 O  O   . VAL A  1  271 ? 47.206  15.815  18.557 1.00 50.57  ? 284 VAL A O   1 
ATOM   2093 C  CB  . VAL A  1  271 ? 47.169  18.631  17.363 1.00 56.10  ? 284 VAL A CB  1 
ATOM   2094 C  CG1 . VAL A  1  271 ? 48.521  18.618  16.658 1.00 56.37  ? 284 VAL A CG1 1 
ATOM   2095 C  CG2 . VAL A  1  271 ? 46.439  19.940  17.082 1.00 58.70  ? 284 VAL A CG2 1 
ATOM   2096 N  N   . GLU A  1  272 ? 47.549  15.410  16.358 1.00 54.21  ? 285 GLU A N   1 
ATOM   2097 C  CA  A GLU A  1  272 ? 48.316  14.194  16.563 0.50 53.50  ? 285 GLU A CA  1 
ATOM   2098 C  CA  B GLU A  1  272 ? 48.325  14.195  16.549 0.50 55.81  ? 285 GLU A CA  1 
ATOM   2099 C  C   . GLU A  1  272 ? 49.647  14.532  17.238 1.00 56.24  ? 285 GLU A C   1 
ATOM   2100 O  O   . GLU A  1  272 ? 50.218  15.600  17.015 1.00 59.93  ? 285 GLU A O   1 
ATOM   2101 C  CB  A GLU A  1  272 ? 48.477  13.479  15.220 0.50 52.75  ? 285 GLU A CB  1 
ATOM   2102 C  CB  B GLU A  1  272 ? 48.585  13.469  15.222 0.50 58.55  ? 285 GLU A CB  1 
ATOM   2103 C  CG  A GLU A  1  272 ? 47.138  13.085  14.596 0.50 51.90  ? 285 GLU A CG  1 
ATOM   2104 C  CG  B GLU A  1  272 ? 49.814  12.558  15.273 0.50 60.92  ? 285 GLU A CG  1 
ATOM   2105 C  CD  A GLU A  1  272 ? 47.174  12.632  13.146 0.50 48.56  ? 285 GLU A CD  1 
ATOM   2106 C  CD  B GLU A  1  272 ? 50.137  11.733  14.041 0.50 61.41  ? 285 GLU A CD  1 
ATOM   2107 O  OE1 A GLU A  1  272 ? 48.267  12.499  12.570 0.50 49.10  ? 285 GLU A OE1 1 
ATOM   2108 O  OE1 B GLU A  1  272 ? 49.406  11.828  13.033 0.50 60.35  ? 285 GLU A OE1 1 
ATOM   2109 O  OE2 A GLU A  1  272 ? 46.084  12.401  12.595 0.50 48.96  ? 285 GLU A OE2 1 
ATOM   2110 O  OE2 B GLU A  1  272 ? 51.130  10.975  14.107 0.50 63.79  ? 285 GLU A OE2 1 
ATOM   2111 N  N   . ASP A  1  273 ? 50.123  13.606  18.087 1.00 58.40  ? 286 ASP A N   1 
ATOM   2112 C  CA  . ASP A  1  273 ? 51.454  13.670  18.668 1.00 58.28  ? 286 ASP A CA  1 
ATOM   2113 C  C   . ASP A  1  273 ? 52.283  12.521  18.101 1.00 58.91  ? 286 ASP A C   1 
ATOM   2114 O  O   . ASP A  1  273 ? 52.111  11.374  18.509 1.00 52.69  ? 286 ASP A O   1 
ATOM   2115 C  CB  . ASP A  1  273 ? 51.428  13.616  20.186 1.00 60.21  ? 286 ASP A CB  1 
ATOM   2116 C  CG  . ASP A  1  273 ? 52.796  13.663  20.855 1.00 65.18  ? 286 ASP A CG  1 
ATOM   2117 O  OD1 . ASP A  1  273 ? 53.808  13.718  20.131 1.00 65.05  ? 286 ASP A OD1 1 
ATOM   2118 O  OD2 . ASP A  1  273 ? 52.844  13.633  22.103 1.00 66.06  ? 286 ASP A OD2 1 
ATOM   2119 N  N   . PRO A  1  274 ? 53.221  12.792  17.162 1.00 59.80  ? 287 PRO A N   1 
ATOM   2120 C  CA  . PRO A  1  274 ? 54.005  11.728  16.533 1.00 58.86  ? 287 PRO A CA  1 
ATOM   2121 C  C   . PRO A  1  274 ? 55.068  11.093  17.428 1.00 54.75  ? 287 PRO A C   1 
ATOM   2122 O  O   . PRO A  1  274 ? 55.582  10.032  17.086 1.00 52.93  ? 287 PRO A O   1 
ATOM   2123 C  CB  . PRO A  1  274 ? 54.629  12.448  15.321 1.00 61.52  ? 287 PRO A CB  1 
ATOM   2124 C  CG  . PRO A  1  274 ? 54.793  13.872  15.789 1.00 61.54  ? 287 PRO A CG  1 
ATOM   2125 C  CD  . PRO A  1  274 ? 53.586  14.133  16.674 1.00 62.08  ? 287 PRO A CD  1 
ATOM   2126 N  N   . ASP A  1  275 ? 55.383  11.740  18.560 1.00 51.97  ? 288 ASP A N   1 
ATOM   2127 C  CA  . ASP A  1  275 ? 56.384  11.251  19.500 1.00 55.42  ? 288 ASP A CA  1 
ATOM   2128 C  C   . ASP A  1  275 ? 55.792  10.257  20.503 1.00 51.88  ? 288 ASP A C   1 
ATOM   2129 O  O   . ASP A  1  275 ? 56.541  9.543   21.156 1.00 50.97  ? 288 ASP A O   1 
ATOM   2130 C  CB  . ASP A  1  275 ? 57.040  12.396  20.262 1.00 60.51  ? 288 ASP A CB  1 
ATOM   2131 C  CG  . ASP A  1  275 ? 57.904  13.336  19.434 1.00 66.43  ? 288 ASP A CG  1 
ATOM   2132 O  OD1 . ASP A  1  275 ? 58.133  13.025  18.241 1.00 60.35  ? 288 ASP A OD1 1 
ATOM   2133 O  OD2 . ASP A  1  275 ? 58.320  14.374  19.992 1.00 69.34  ? 288 ASP A OD2 1 
ATOM   2134 N  N   . SER A  1  276 ? 54.461  10.227  20.638 1.00 49.59  ? 289 SER A N   1 
ATOM   2135 C  CA  . SER A  1  276 ? 53.791  9.404   21.631 1.00 46.44  ? 289 SER A CA  1 
ATOM   2136 C  C   . SER A  1  276 ? 54.048  7.924   21.367 1.00 43.32  ? 289 SER A C   1 
ATOM   2137 O  O   . SER A  1  276 ? 54.249  7.508   20.234 1.00 44.10  ? 289 SER A O   1 
ATOM   2138 C  CB  . SER A  1  276 ? 52.300  9.687   21.647 1.00 48.44  ? 289 SER A CB  1 
ATOM   2139 O  OG  . SER A  1  276 ? 51.596  8.708   22.400 1.00 46.57  ? 289 SER A OG  1 
ATOM   2140 N  N   . ALA A  1  277 ? 53.999  7.122   22.428 1.00 43.79  ? 290 ALA A N   1 
ATOM   2141 C  CA  . ALA A  1  277 ? 53.892  5.682   22.272 1.00 41.31  ? 290 ALA A CA  1 
ATOM   2142 C  C   . ALA A  1  277 ? 52.622  5.348   21.496 1.00 42.14  ? 290 ALA A C   1 
ATOM   2143 O  O   . ALA A  1  277 ? 51.656  6.106   21.513 1.00 43.65  ? 290 ALA A O   1 
ATOM   2144 C  CB  . ALA A  1  277 ? 53.887  5.009   23.627 1.00 42.53  ? 290 ALA A CB  1 
ATOM   2145 N  N   . ASP A  1  278 ? 52.657  4.216   20.793 1.00 44.38  ? 291 ASP A N   1 
ATOM   2146 C  CA  . ASP A  1  278 ? 51.479  3.612   20.192 1.00 46.11  ? 291 ASP A CA  1 
ATOM   2147 C  C   . ASP A  1  278 ? 51.723  2.107   20.178 1.00 44.25  ? 291 ASP A C   1 
ATOM   2148 O  O   . ASP A  1  278 ? 52.710  1.656   20.760 1.00 44.95  ? 291 ASP A O   1 
ATOM   2149 C  CB  . ASP A  1  278 ? 51.145  4.259   18.858 1.00 50.20  ? 291 ASP A CB  1 
ATOM   2150 C  CG  . ASP A  1  278 ? 52.157  4.052   17.743 1.00 53.02  ? 291 ASP A CG  1 
ATOM   2151 O  OD1 . ASP A  1  278 ? 52.943  3.091   17.831 1.00 51.67  ? 291 ASP A OD1 1 
ATOM   2152 O  OD2 . ASP A  1  278 ? 52.157  4.883   16.810 1.00 57.09  ? 291 ASP A OD2 1 
ATOM   2153 N  N   . PHE A  1  279 ? 50.861  1.344   19.504 1.00 43.03  ? 292 PHE A N   1 
ATOM   2154 C  CA  . PHE A  1  279 ? 50.882  -0.108  19.639 1.00 45.96  ? 292 PHE A CA  1 
ATOM   2155 C  C   . PHE A  1  279 ? 52.014  -0.746  18.833 1.00 49.32  ? 292 PHE A C   1 
ATOM   2156 O  O   . PHE A  1  279 ? 52.317  -1.917  19.052 1.00 50.30  ? 292 PHE A O   1 
ATOM   2157 C  CB  . PHE A  1  279 ? 49.506  -0.684  19.292 1.00 47.64  ? 292 PHE A CB  1 
ATOM   2158 C  CG  . PHE A  1  279 ? 48.520  -0.471  20.433 1.00 49.24  ? 292 PHE A CG  1 
ATOM   2159 C  CD1 . PHE A  1  279 ? 48.528  -1.311  21.544 1.00 51.42  ? 292 PHE A CD1 1 
ATOM   2160 C  CD2 . PHE A  1  279 ? 47.621  0.586   20.417 1.00 47.18  ? 292 PHE A CD2 1 
ATOM   2161 C  CE1 . PHE A  1  279 ? 47.648  -1.106  22.599 1.00 51.39  ? 292 PHE A CE1 1 
ATOM   2162 C  CE2 . PHE A  1  279 ? 46.734  0.780   21.468 1.00 49.85  ? 292 PHE A CE2 1 
ATOM   2163 C  CZ  . PHE A  1  279 ? 46.747  -0.066  22.554 1.00 50.62  ? 292 PHE A CZ  1 
ATOM   2164 N  N   . THR A  1  280 ? 52.653  0.008   17.929 1.00 48.66  ? 293 THR A N   1 
ATOM   2165 C  CA  . THR A  1  280 ? 53.841  -0.490  17.252 1.00 52.03  ? 293 THR A CA  1 
ATOM   2166 C  C   . THR A  1  280 ? 55.091  0.213   17.784 1.00 52.06  ? 293 THR A C   1 
ATOM   2167 O  O   . THR A  1  280 ? 56.173  0.008   17.242 1.00 48.83  ? 293 THR A O   1 
ATOM   2168 C  CB  . THR A  1  280 ? 53.694  -0.314  15.736 1.00 53.75  ? 293 THR A CB  1 
ATOM   2169 O  OG1 . THR A  1  280 ? 53.565  1.082   15.472 1.00 50.55  ? 293 THR A OG1 1 
ATOM   2170 C  CG2 . THR A  1  280 ? 52.496  -1.058  15.174 1.00 55.38  ? 293 THR A CG2 1 
ATOM   2171 N  N   . HIS A  1  281 ? 54.939  1.035   18.834 1.00 50.21  ? 294 HIS A N   1 
ATOM   2172 C  CA  . HIS A  1  281 ? 56.059  1.742   19.444 1.00 50.41  ? 294 HIS A CA  1 
ATOM   2173 C  C   . HIS A  1  281 ? 55.936  1.713   20.971 1.00 47.85  ? 294 HIS A C   1 
ATOM   2174 O  O   . HIS A  1  281 ? 55.980  2.751   21.628 1.00 48.97  ? 294 HIS A O   1 
ATOM   2175 C  CB  . HIS A  1  281 ? 56.143  3.185   18.923 1.00 55.60  ? 294 HIS A CB  1 
ATOM   2176 C  CG  . HIS A  1  281 ? 56.400  3.327   17.457 1.00 64.25  ? 294 HIS A CG  1 
ATOM   2177 N  ND1 . HIS A  1  281 ? 57.669  3.484   16.941 1.00 74.58  ? 294 HIS A ND1 1 
ATOM   2178 C  CD2 . HIS A  1  281 ? 55.577  3.351   16.401 1.00 64.17  ? 294 HIS A CD2 1 
ATOM   2179 C  CE1 . HIS A  1  281 ? 57.602  3.600   15.623 1.00 74.63  ? 294 HIS A CE1 1 
ATOM   2180 N  NE2 . HIS A  1  281 ? 56.338  3.513   15.273 1.00 70.66  ? 294 HIS A NE2 1 
ATOM   2181 N  N   . LEU A  1  282 ? 55.809  0.511   21.541 1.00 45.54  ? 295 LEU A N   1 
ATOM   2182 C  CA  . LEU A  1  282 ? 55.480  0.351   22.952 1.00 47.39  ? 295 LEU A CA  1 
ATOM   2183 C  C   . LEU A  1  282 ? 56.611  0.811   23.873 1.00 49.93  ? 295 LEU A C   1 
ATOM   2184 O  O   . LEU A  1  282 ? 56.330  1.330   24.953 1.00 45.46  ? 295 LEU A O   1 
ATOM   2185 C  CB  . LEU A  1  282 ? 55.094  -1.100  23.229 1.00 47.72  ? 295 LEU A CB  1 
ATOM   2186 C  CG  . LEU A  1  282 ? 53.749  -1.544  22.649 1.00 49.29  ? 295 LEU A CG  1 
ATOM   2187 C  CD1 . LEU A  1  282 ? 53.534  -3.045  22.694 1.00 53.21  ? 295 LEU A CD1 1 
ATOM   2188 C  CD2 . LEU A  1  282 ? 52.614  -0.825  23.353 1.00 47.75  ? 295 LEU A CD2 1 
ATOM   2189 N  N   . CYS A  1  283 ? 57.881  0.614   23.482 1.00 49.47  ? 296 CYS A N   1 
ATOM   2190 C  CA  . CYS A  1  283 ? 58.997  0.920   24.369 1.00 48.53  ? 296 CYS A CA  1 
ATOM   2191 C  C   . CYS A  1  283 ? 59.067  2.411   24.694 1.00 45.25  ? 296 CYS A C   1 
ATOM   2192 O  O   . CYS A  1  283 ? 59.647  2.798   25.711 1.00 48.12  ? 296 CYS A O   1 
ATOM   2193 C  CB  . CYS A  1  283 ? 60.344  0.465   23.806 1.00 54.17  ? 296 CYS A CB  1 
ATOM   2194 S  SG  . CYS A  1  283 ? 60.601  -1.331  23.821 1.00 64.50  ? 296 CYS A SG  1 
ATOM   2195 N  N   . ARG A  1  284 ? 58.497  3.251   23.822 1.00 46.29  ? 297 ARG A N   1 
ATOM   2196 C  CA  . ARG A  1  284 ? 58.396  4.674   24.108 1.00 49.53  ? 297 ARG A CA  1 
ATOM   2197 C  C   . ARG A  1  284 ? 57.656  4.900   25.423 1.00 46.43  ? 297 ARG A C   1 
ATOM   2198 O  O   . ARG A  1  284 ? 57.953  5.849   26.142 1.00 48.64  ? 297 ARG A O   1 
ATOM   2199 C  CB  . ARG A  1  284 ? 57.626  5.437   23.027 1.00 52.58  ? 297 ARG A CB  1 
ATOM   2200 C  CG  . ARG A  1  284 ? 58.367  5.513   21.703 1.00 53.87  ? 297 ARG A CG  1 
ATOM   2201 C  CD  . ARG A  1  284 ? 57.613  6.346   20.697 1.00 55.74  ? 297 ARG A CD  1 
ATOM   2202 N  NE  . ARG A  1  284 ? 58.297  6.388   19.403 1.00 56.70  ? 297 ARG A NE  1 
ATOM   2203 C  CZ  . ARG A  1  284 ? 57.803  6.942   18.312 1.00 59.81  ? 297 ARG A CZ  1 
ATOM   2204 N  NH1 . ARG A  1  284 ? 56.609  7.506   18.332 1.00 57.45  ? 297 ARG A NH1 1 
ATOM   2205 N  NH2 . ARG A  1  284 ? 58.494  6.914   17.190 1.00 64.52  ? 297 ARG A NH2 1 
ATOM   2206 N  N   . LEU A  1  285 ? 56.673  4.041   25.708 1.00 46.01  ? 298 LEU A N   1 
ATOM   2207 C  CA  . LEU A  1  285 ? 55.915  4.139   26.942 1.00 47.82  ? 298 LEU A CA  1 
ATOM   2208 C  C   . LEU A  1  285 ? 56.856  3.886   28.116 1.00 42.69  ? 298 LEU A C   1 
ATOM   2209 O  O   . LEU A  1  285 ? 56.824  4.630   29.087 1.00 41.61  ? 298 LEU A O   1 
ATOM   2210 C  CB  . LEU A  1  285 ? 54.718  3.189   26.922 1.00 49.01  ? 298 LEU A CB  1 
ATOM   2211 C  CG  . LEU A  1  285 ? 53.750  3.291   28.109 1.00 51.14  ? 298 LEU A CG  1 
ATOM   2212 C  CD1 . LEU A  1  285 ? 52.363  2.843   27.684 1.00 51.83  ? 298 LEU A CD1 1 
ATOM   2213 C  CD2 . LEU A  1  285 ? 54.213  2.458   29.299 1.00 52.70  ? 298 LEU A CD2 1 
ATOM   2214 N  N   . TYR A  1  286 ? 57.709  2.863   28.006 1.00 45.64  ? 299 TYR A N   1 
ATOM   2215 C  CA  . TYR A  1  286 ? 58.691  2.564   29.045 1.00 45.31  ? 299 TYR A CA  1 
ATOM   2216 C  C   . TYR A  1  286 ? 59.553  3.800   29.300 1.00 43.94  ? 299 TYR A C   1 
ATOM   2217 O  O   . TYR A  1  286 ? 59.704  4.236   30.448 1.00 43.12  ? 299 TYR A O   1 
ATOM   2218 C  CB  . TYR A  1  286 ? 59.550  1.347   28.674 1.00 43.28  ? 299 TYR A CB  1 
ATOM   2219 C  CG  . TYR A  1  286 ? 60.703  1.077   29.631 1.00 40.70  ? 299 TYR A CG  1 
ATOM   2220 C  CD1 . TYR A  1  286 ? 60.468  0.739   30.960 1.00 41.32  ? 299 TYR A CD1 1 
ATOM   2221 C  CD2 . TYR A  1  286 ? 62.024  1.188   29.213 1.00 39.88  ? 299 TYR A CD2 1 
ATOM   2222 C  CE1 . TYR A  1  286 ? 61.509  0.497   31.843 1.00 38.91  ? 299 TYR A CE1 1 
ATOM   2223 C  CE2 . TYR A  1  286 ? 63.077  0.967   30.091 1.00 42.18  ? 299 TYR A CE2 1 
ATOM   2224 C  CZ  . TYR A  1  286 ? 62.821  0.628   31.408 1.00 41.02  ? 299 TYR A CZ  1 
ATOM   2225 O  OH  . TYR A  1  286 ? 63.865  0.416   32.260 1.00 38.68  ? 299 TYR A OH  1 
ATOM   2226 N  N   . GLU A  1  287 ? 60.082  4.382   28.218 1.00 45.64  ? 300 GLU A N   1 
ATOM   2227 C  CA  . GLU A  1  287 ? 61.023  5.489   28.320 1.00 51.84  ? 300 GLU A CA  1 
ATOM   2228 C  C   . GLU A  1  287 ? 60.325  6.727   28.885 1.00 46.53  ? 300 GLU A C   1 
ATOM   2229 O  O   . GLU A  1  287 ? 60.883  7.423   29.732 1.00 43.62  ? 300 GLU A O   1 
ATOM   2230 C  CB  . GLU A  1  287 ? 61.666  5.769   26.961 1.00 54.29  ? 300 GLU A CB  1 
ATOM   2231 C  CG  . GLU A  1  287 ? 62.536  4.616   26.464 1.00 60.32  ? 300 GLU A CG  1 
ATOM   2232 C  CD  . GLU A  1  287 ? 63.045  4.761   25.036 1.00 71.78  ? 300 GLU A CD  1 
ATOM   2233 O  OE1 . GLU A  1  287 ? 62.197  4.943   24.132 1.00 67.10  ? 300 GLU A OE1 1 
ATOM   2234 O  OE2 . GLU A  1  287 ? 64.280  4.681   24.813 1.00 83.26  ? 300 GLU A OE2 1 
ATOM   2235 N  N   . PHE A  1  288 ? 59.098  6.983   28.419 1.00 45.14  ? 301 PHE A N   1 
ATOM   2236 C  CA  . PHE A  1  288 ? 58.329  8.121   28.889 1.00 43.71  ? 301 PHE A CA  1 
ATOM   2237 C  C   . PHE A  1  288 ? 58.155  8.018   30.399 1.00 40.50  ? 301 PHE A C   1 
ATOM   2238 O  O   . PHE A  1  288 ? 58.427  8.967   31.125 1.00 41.51  ? 301 PHE A O   1 
ATOM   2239 C  CB  . PHE A  1  288 ? 56.976  8.203   28.175 1.00 48.77  ? 301 PHE A CB  1 
ATOM   2240 C  CG  . PHE A  1  288 ? 56.168  9.432   28.574 1.00 51.70  ? 301 PHE A CG  1 
ATOM   2241 C  CD1 . PHE A  1  288 ? 56.333  10.646  27.906 1.00 51.31  ? 301 PHE A CD1 1 
ATOM   2242 C  CD2 . PHE A  1  288 ? 55.264  9.377   29.629 1.00 53.31  ? 301 PHE A CD2 1 
ATOM   2243 C  CE1 . PHE A  1  288 ? 55.600  11.763  28.274 1.00 52.98  ? 301 PHE A CE1 1 
ATOM   2244 C  CE2 . PHE A  1  288 ? 54.538  10.501  29.996 1.00 53.72  ? 301 PHE A CE2 1 
ATOM   2245 C  CZ  . PHE A  1  288 ? 54.706  11.689  29.318 1.00 54.09  ? 301 PHE A CZ  1 
ATOM   2246 N  N   . VAL A  1  289 ? 57.733  6.843   30.876 1.00 39.55  ? 302 VAL A N   1 
ATOM   2247 C  CA  . VAL A  1  289 ? 57.444  6.670   32.292 1.00 36.54  ? 302 VAL A CA  1 
ATOM   2248 C  C   . VAL A  1  289 ? 58.724  6.815   33.118 1.00 35.80  ? 302 VAL A C   1 
ATOM   2249 O  O   . VAL A  1  289 ? 58.706  7.391   34.204 1.00 35.28  ? 302 VAL A O   1 
ATOM   2250 C  CB  . VAL A  1  289 ? 56.739  5.328   32.579 1.00 37.04  ? 302 VAL A CB  1 
ATOM   2251 C  CG1 . VAL A  1  289 ? 56.693  5.030   34.076 1.00 37.84  ? 302 VAL A CG1 1 
ATOM   2252 C  CG2 . VAL A  1  289 ? 55.334  5.290   31.985 1.00 37.19  ? 302 VAL A CG2 1 
ATOM   2253 N  N   . VAL A  1  290 ? 59.840  6.273   32.632 1.00 37.91  ? 303 VAL A N   1 
ATOM   2254 C  CA  . VAL A  1  290 ? 61.082  6.412   33.377 1.00 35.62  ? 303 VAL A CA  1 
ATOM   2255 C  C   . VAL A  1  290 ? 61.422  7.898   33.494 1.00 35.44  ? 303 VAL A C   1 
ATOM   2256 O  O   . VAL A  1  290 ? 61.820  8.366   34.553 1.00 36.92  ? 303 VAL A O   1 
ATOM   2257 C  CB  . VAL A  1  290 ? 62.221  5.589   32.760 1.00 35.33  ? 303 VAL A CB  1 
ATOM   2258 C  CG1 . VAL A  1  290 ? 63.579  5.933   33.371 1.00 39.11  ? 303 VAL A CG1 1 
ATOM   2259 C  CG2 . VAL A  1  290 ? 61.943  4.101   32.911 1.00 36.61  ? 303 VAL A CG2 1 
ATOM   2260 N  N   . GLY A  1  291 ? 61.216  8.646   32.409 1.00 38.33  ? 304 GLY A N   1 
ATOM   2261 C  CA  . GLY A  1  291 ? 61.367  10.094  32.420 1.00 39.28  ? 304 GLY A CA  1 
ATOM   2262 C  C   . GLY A  1  291 ? 60.476  10.755  33.469 1.00 40.78  ? 304 GLY A C   1 
ATOM   2263 O  O   . GLY A  1  291 ? 60.929  11.622  34.216 1.00 39.84  ? 304 GLY A O   1 
ATOM   2264 N  N   . SER A  1  292 ? 59.201  10.332  33.526 1.00 40.28  ? 305 SER A N   1 
ATOM   2265 C  CA  . SER A  1  292 ? 58.271  10.894  34.488 1.00 39.53  ? 305 SER A CA  1 
ATOM   2266 C  C   . SER A  1  292 ? 58.757  10.622  35.907 1.00 37.21  ? 305 SER A C   1 
ATOM   2267 O  O   . SER A  1  292 ? 58.669  11.487  36.768 1.00 38.10  ? 305 SER A O   1 
ATOM   2268 C  CB  . SER A  1  292 ? 56.873  10.385  34.274 1.00 39.06  ? 305 SER A CB  1 
ATOM   2269 O  OG  . SER A  1  292 ? 56.462  10.574  32.927 1.00 41.50  ? 305 SER A OG  1 
ATOM   2270 N  N   . VAL A  1  293 ? 59.262  9.416   36.155 1.00 39.28  ? 306 VAL A N   1 
ATOM   2271 C  CA  . VAL A  1  293 ? 59.768  9.055   37.472 1.00 41.21  ? 306 VAL A CA  1 
ATOM   2272 C  C   . VAL A  1  293 ? 60.937  9.969   37.852 1.00 39.28  ? 306 VAL A C   1 
ATOM   2273 O  O   . VAL A  1  293 ? 61.031  10.376  39.004 1.00 39.46  ? 306 VAL A O   1 
ATOM   2274 C  CB  . VAL A  1  293 ? 60.172  7.567   37.564 1.00 42.20  ? 306 VAL A CB  1 
ATOM   2275 C  CG1 . VAL A  1  293 ? 60.946  7.252   38.849 1.00 40.16  ? 306 VAL A CG1 1 
ATOM   2276 C  CG2 . VAL A  1  293 ? 58.959  6.655   37.420 1.00 42.42  ? 306 VAL A CG2 1 
ATOM   2277 N  N   . GLN A  1  294 ? 61.811  10.300  36.897 1.00 41.31  ? 307 GLN A N   1 
ATOM   2278 C  CA  . GLN A  1  294 ? 62.949  11.168  37.180 1.00 45.33  ? 307 GLN A CA  1 
ATOM   2279 C  C   . GLN A  1  294 ? 62.472  12.567  37.572 1.00 45.45  ? 307 GLN A C   1 
ATOM   2280 O  O   . GLN A  1  294 ? 63.093  13.210  38.418 1.00 44.62  ? 307 GLN A O   1 
ATOM   2281 C  CB  . GLN A  1  294 ? 63.904  11.265  35.993 1.00 44.94  ? 307 GLN A CB  1 
ATOM   2282 C  CG  . GLN A  1  294 ? 64.638  9.960   35.703 1.00 49.58  ? 307 GLN A CG  1 
ATOM   2283 C  CD  . GLN A  1  294 ? 65.504  10.022  34.466 1.00 48.43  ? 307 GLN A CD  1 
ATOM   2284 O  OE1 . GLN A  1  294 ? 65.054  9.733   33.352 1.00 48.55  ? 307 GLN A OE1 1 
ATOM   2285 N  NE2 . GLN A  1  294 ? 66.770  10.371  34.660 1.00 45.50  ? 307 GLN A NE2 1 
ATOM   2286 N  N   . GLU A  1  295 ? 61.374  13.025  36.952 1.00 43.60  ? 308 GLU A N   1 
ATOM   2287 C  CA  . GLU A  1  295 ? 60.780  14.307  37.303 1.00 47.14  ? 308 GLU A CA  1 
ATOM   2288 C  C   . GLU A  1  295 ? 60.215  14.263  38.721 1.00 44.04  ? 308 GLU A C   1 
ATOM   2289 O  O   . GLU A  1  295 ? 60.317  15.245  39.444 1.00 40.69  ? 308 GLU A O   1 
ATOM   2290 C  CB  . GLU A  1  295 ? 59.660  14.734  36.354 1.00 49.61  ? 308 GLU A CB  1 
ATOM   2291 C  CG  . GLU A  1  295 ? 60.146  15.161  34.974 1.00 56.12  ? 308 GLU A CG  1 
ATOM   2292 C  CD  . GLU A  1  295 ? 59.046  15.252  33.926 1.00 66.61  ? 308 GLU A CD  1 
ATOM   2293 O  OE1 . GLU A  1  295 ? 57.854  14.959  34.212 1.00 72.67  ? 308 GLU A OE1 1 
ATOM   2294 O  OE2 . GLU A  1  295 ? 59.408  15.609  32.787 1.00 71.68  ? 308 GLU A OE2 1 
ATOM   2295 N  N   . LEU A  1  296 ? 59.616  13.129  39.111 1.00 43.57  ? 309 LEU A N   1 
ATOM   2296 C  CA  . LEU A  1  296 ? 59.052  12.983  40.446 1.00 41.19  ? 309 LEU A CA  1 
ATOM   2297 C  C   . LEU A  1  296 ? 60.167  12.869  41.477 1.00 38.60  ? 309 LEU A C   1 
ATOM   2298 O  O   . LEU A  1  296 ? 59.998  13.309  42.612 1.00 39.21  ? 309 LEU A O   1 
ATOM   2299 C  CB  . LEU A  1  296 ? 58.111  11.780  40.541 1.00 41.69  ? 309 LEU A CB  1 
ATOM   2300 C  CG  . LEU A  1  296 ? 56.788  11.902  39.772 1.00 42.76  ? 309 LEU A CG  1 
ATOM   2301 C  CD1 . LEU A  1  296 ? 56.007  10.610  39.917 1.00 45.40  ? 309 LEU A CD1 1 
ATOM   2302 C  CD2 . LEU A  1  296 ? 55.911  13.073  40.188 1.00 40.11  ? 309 LEU A CD2 1 
ATOM   2303 N  N   . TYR A  1  297 ? 61.285  12.246  41.086 1.00 37.09  ? 310 TYR A N   1 
ATOM   2304 C  CA  . TYR A  1  297 ? 62.370  11.929  42.008 1.00 40.31  ? 310 TYR A CA  1 
ATOM   2305 C  C   . TYR A  1  297 ? 63.694  12.385  41.394 1.00 42.43  ? 310 TYR A C   1 
ATOM   2306 O  O   . TYR A  1  297 ? 64.459  11.574  40.875 1.00 40.73  ? 310 TYR A O   1 
ATOM   2307 C  CB  . TYR A  1  297 ? 62.369  10.429  42.327 1.00 39.71  ? 310 TYR A CB  1 
ATOM   2308 C  CG  . TYR A  1  297 ? 61.127  9.938   43.057 1.00 38.15  ? 310 TYR A CG  1 
ATOM   2309 C  CD1 . TYR A  1  297 ? 60.990  10.109  44.432 1.00 40.82  ? 310 TYR A CD1 1 
ATOM   2310 C  CD2 . TYR A  1  297 ? 60.102  9.284   42.380 1.00 38.48  ? 310 TYR A CD2 1 
ATOM   2311 C  CE1 . TYR A  1  297 ? 59.867  9.656   45.103 1.00 40.14  ? 310 TYR A CE1 1 
ATOM   2312 C  CE2 . TYR A  1  297 ? 58.977  8.820   43.047 1.00 39.48  ? 310 TYR A CE2 1 
ATOM   2313 C  CZ  . TYR A  1  297 ? 58.862  9.004   44.414 1.00 37.21  ? 310 TYR A CZ  1 
ATOM   2314 O  OH  . TYR A  1  297 ? 57.760  8.582   45.099 1.00 40.49  ? 310 TYR A OH  1 
ATOM   2315 N  N   . PRO A  1  298 ? 63.981  13.706  41.391 1.00 44.12  ? 311 PRO A N   1 
ATOM   2316 C  CA  . PRO A  1  298 ? 65.173  14.226  40.727 1.00 44.18  ? 311 PRO A CA  1 
ATOM   2317 C  C   . PRO A  1  298 ? 66.514  13.862  41.366 1.00 40.28  ? 311 PRO A C   1 
ATOM   2318 O  O   . PRO A  1  298 ? 67.490  13.763  40.639 1.00 38.53  ? 311 PRO A O   1 
ATOM   2319 C  CB  . PRO A  1  298 ? 64.914  15.748  40.701 1.00 48.40  ? 311 PRO A CB  1 
ATOM   2320 C  CG  . PRO A  1  298 ? 64.032  16.000  41.902 1.00 53.83  ? 311 PRO A CG  1 
ATOM   2321 C  CD  . PRO A  1  298 ? 63.148  14.770  41.970 1.00 48.44  ? 311 PRO A CD  1 
ATOM   2322 N  N   . ASN A  1  299 ? 66.578  13.686  42.693 1.00 41.95  ? 312 ASN A N   1 
ATOM   2323 C  CA  . ASN A  1  299 ? 67.854  13.378  43.341 1.00 40.98  ? 312 ASN A CA  1 
ATOM   2324 C  C   . ASN A  1  299 ? 67.643  12.567  44.614 1.00 38.37  ? 312 ASN A C   1 
ATOM   2325 O  O   . ASN A  1  299 ? 67.989  13.025  45.702 1.00 39.29  ? 312 ASN A O   1 
ATOM   2326 C  CB  . ASN A  1  299 ? 68.667  14.639  43.633 1.00 39.86  ? 312 ASN A CB  1 
ATOM   2327 C  CG  . ASN A  1  299 ? 70.062  14.357  44.151 1.00 37.40  ? 312 ASN A CG  1 
ATOM   2328 O  OD1 . ASN A  1  299 ? 70.826  13.575  43.564 1.00 37.12  ? 312 ASN A OD1 1 
ATOM   2329 N  ND2 . ASN A  1  299 ? 70.412  14.965  45.271 1.00 36.97  ? 312 ASN A ND2 1 
ATOM   2330 N  N   . PRO A  1  300 ? 67.124  11.319  44.521 1.00 39.88  ? 313 PRO A N   1 
ATOM   2331 C  CA  . PRO A  1  300 ? 66.931  10.476  45.706 1.00 41.98  ? 313 PRO A CA  1 
ATOM   2332 C  C   . PRO A  1  300 ? 68.221  9.874   46.258 1.00 38.32  ? 313 PRO A C   1 
ATOM   2333 O  O   . PRO A  1  300 ? 69.151  9.642   45.500 1.00 43.44  ? 313 PRO A O   1 
ATOM   2334 C  CB  . PRO A  1  300 ? 65.978  9.405   45.169 1.00 40.59  ? 313 PRO A CB  1 
ATOM   2335 C  CG  . PRO A  1  300 ? 66.413  9.234   43.744 1.00 41.15  ? 313 PRO A CG  1 
ATOM   2336 C  CD  . PRO A  1  300 ? 66.701  10.657  43.278 1.00 41.40  ? 313 PRO A CD  1 
ATOM   2337 N  N   . THR A  1  301 ? 68.247  9.628   47.575 1.00 38.30  ? 314 THR A N   1 
ATOM   2338 C  CA  . THR A  1  301 ? 69.336  8.942   48.257 1.00 44.39  ? 314 THR A CA  1 
ATOM   2339 C  C   . THR A  1  301 ? 68.737  7.963   49.267 1.00 42.54  ? 314 THR A C   1 
ATOM   2340 O  O   . THR A  1  301 ? 67.527  7.979   49.490 1.00 43.09  ? 314 THR A O   1 
ATOM   2341 C  CB  . THR A  1  301 ? 70.256  9.958   48.942 1.00 48.09  ? 314 THR A CB  1 
ATOM   2342 O  OG1 . THR A  1  301 ? 69.453  10.754  49.802 1.00 49.88  ? 314 THR A OG1 1 
ATOM   2343 C  CG2 . THR A  1  301 ? 70.918  10.920  47.972 1.00 51.11  ? 314 THR A CG2 1 
ATOM   2344 N  N   . GLY A  1  302 ? 69.586  7.106   49.865 1.00 43.55  ? 315 GLY A N   1 
ATOM   2345 C  CA  . GLY A  1  302 ? 69.167  6.216   50.943 1.00 43.75  ? 315 GLY A CA  1 
ATOM   2346 C  C   . GLY A  1  302 ? 68.120  5.187   50.504 1.00 41.81  ? 315 GLY A C   1 
ATOM   2347 O  O   . GLY A  1  302 ? 68.193  4.658   49.399 1.00 43.83  ? 315 GLY A O   1 
ATOM   2348 N  N   . ILE A  1  303 ? 67.155  4.903   51.388 1.00 45.39  ? 316 ILE A N   1 
ATOM   2349 C  CA  . ILE A  1  303 ? 66.155  3.867   51.161 1.00 50.91  ? 316 ILE A CA  1 
ATOM   2350 C  C   . ILE A  1  303 ? 65.318  4.227   49.934 1.00 45.04  ? 316 ILE A C   1 
ATOM   2351 O  O   . ILE A  1  303 ? 64.976  3.350   49.140 1.00 44.49  ? 316 ILE A O   1 
ATOM   2352 C  CB  . ILE A  1  303 ? 65.306  3.615   52.427 1.00 58.45  ? 316 ILE A CB  1 
ATOM   2353 C  CG1 . ILE A  1  303 ? 66.217  3.172   53.587 1.00 72.67  ? 316 ILE A CG1 1 
ATOM   2354 C  CG2 . ILE A  1  303 ? 64.197  2.584   52.183 1.00 64.24  ? 316 ILE A CG2 1 
ATOM   2355 C  CD1 . ILE A  1  303 ? 65.511  2.812   54.889 1.00 81.90  ? 316 ILE A CD1 1 
ATOM   2356 N  N   . LEU A  1  304 ? 65.014  5.517   49.767 1.00 41.04  ? 317 LEU A N   1 
ATOM   2357 C  CA  . LEU A  1  304 ? 64.191  5.955   48.650 1.00 38.51  ? 317 LEU A CA  1 
ATOM   2358 C  C   . LEU A  1  304 ? 64.875  5.613   47.326 1.00 38.66  ? 317 LEU A C   1 
ATOM   2359 O  O   . LEU A  1  304 ? 64.234  5.092   46.413 1.00 38.04  ? 317 LEU A O   1 
ATOM   2360 C  CB  . LEU A  1  304 ? 63.878  7.445   48.769 1.00 39.79  ? 317 LEU A CB  1 
ATOM   2361 C  CG  . LEU A  1  304 ? 63.099  8.055   47.602 1.00 39.97  ? 317 LEU A CG  1 
ATOM   2362 C  CD1 . LEU A  1  304 ? 61.752  7.339   47.376 1.00 41.45  ? 317 LEU A CD1 1 
ATOM   2363 C  CD2 . LEU A  1  304 ? 62.887  9.548   47.820 1.00 40.46  ? 317 LEU A CD2 1 
ATOM   2364 N  N   . ARG A  1  305 ? 66.177  5.913   47.223 1.00 38.33  ? 318 ARG A N   1 
ATOM   2365 C  CA  A ARG A  1  305 ? 66.942  5.597   46.028 0.50 36.58  ? 318 ARG A CA  1 
ATOM   2366 C  CA  B ARG A  1  305 ? 66.941  5.596   46.028 0.50 39.89  ? 318 ARG A CA  1 
ATOM   2367 C  C   . ARG A  1  305 ? 66.910  4.089   45.794 1.00 37.15  ? 318 ARG A C   1 
ATOM   2368 O  O   . ARG A  1  305 ? 66.642  3.644   44.685 1.00 36.94  ? 318 ARG A O   1 
ATOM   2369 C  CB  A ARG A  1  305 ? 68.396  6.069   46.144 0.50 33.94  ? 318 ARG A CB  1 
ATOM   2370 C  CB  B ARG A  1  305 ? 68.395  6.067   46.143 0.50 41.96  ? 318 ARG A CB  1 
ATOM   2371 C  CG  A ARG A  1  305 ? 69.290  5.673   44.980 0.50 31.04  ? 318 ARG A CG  1 
ATOM   2372 C  CG  B ARG A  1  305 ? 69.284  5.686   44.970 0.50 43.29  ? 318 ARG A CG  1 
ATOM   2373 C  CD  A ARG A  1  305 ? 70.732  6.074   45.223 0.50 30.23  ? 318 ARG A CD  1 
ATOM   2374 C  CD  B ARG A  1  305 ? 70.735  5.996   45.283 0.50 47.09  ? 318 ARG A CD  1 
ATOM   2375 N  NE  A ARG A  1  305 ? 71.573  5.440   44.208 0.50 27.93  ? 318 ARG A NE  1 
ATOM   2376 N  NE  B ARG A  1  305 ? 71.628  5.553   44.208 0.50 49.94  ? 318 ARG A NE  1 
ATOM   2377 C  CZ  A ARG A  1  305 ? 72.085  4.233   44.317 0.50 25.79  ? 318 ARG A CZ  1 
ATOM   2378 C  CZ  B ARG A  1  305 ? 71.828  6.165   43.036 0.50 53.13  ? 318 ARG A CZ  1 
ATOM   2379 N  NH1 A ARG A  1  305 ? 72.024  3.604   45.470 0.50 23.91  ? 318 ARG A NH1 1 
ATOM   2380 N  NH1 B ARG A  1  305 ? 72.715  5.665   42.201 0.50 60.26  ? 318 ARG A NH1 1 
ATOM   2381 N  NH2 A ARG A  1  305 ? 72.674  3.681   43.275 0.50 25.18  ? 318 ARG A NH2 1 
ATOM   2382 N  NH2 B ARG A  1  305 ? 71.205  7.277   42.692 0.50 47.86  ? 318 ARG A NH2 1 
ATOM   2383 N  N   . ARG A  1  306 ? 67.212  3.325   46.849 1.00 38.86  ? 319 ARG A N   1 
ATOM   2384 C  CA  . ARG A  1  306 ? 67.250  1.871   46.783 1.00 42.65  ? 319 ARG A CA  1 
ATOM   2385 C  C   . ARG A  1  306 ? 65.903  1.332   46.298 1.00 38.56  ? 319 ARG A C   1 
ATOM   2386 O  O   . ARG A  1  306 ? 65.847  0.511   45.388 1.00 37.52  ? 319 ARG A O   1 
ATOM   2387 C  CB  . ARG A  1  306 ? 67.621  1.308   48.161 1.00 47.62  ? 319 ARG A CB  1 
ATOM   2388 C  CG  . ARG A  1  306 ? 67.931  -0.185  48.188 1.00 59.56  ? 319 ARG A CG  1 
ATOM   2389 C  CD  . ARG A  1  306 ? 67.946  -0.775  49.593 1.00 66.60  ? 319 ARG A CD  1 
ATOM   2390 N  NE  . ARG A  1  306 ? 66.598  -0.816  50.177 1.00 72.94  ? 319 ARG A NE  1 
ATOM   2391 C  CZ  . ARG A  1  306 ? 66.307  -1.207  51.420 1.00 78.14  ? 319 ARG A CZ  1 
ATOM   2392 N  NH1 . ARG A  1  306 ? 67.261  -1.673  52.216 1.00 81.41  ? 319 ARG A NH1 1 
ATOM   2393 N  NH2 . ARG A  1  306 ? 65.058  -1.150  51.861 1.00 76.35  ? 319 ARG A NH2 1 
ATOM   2394 N  N   . ASN A  1  307 ? 64.809  1.798   46.903 1.00 36.83  ? 320 ASN A N   1 
ATOM   2395 C  CA  . ASN A  1  307 ? 63.499  1.250   46.582 1.00 38.07  ? 320 ASN A CA  1 
ATOM   2396 C  C   . ASN A  1  307 ? 63.069  1.652   45.176 1.00 36.51  ? 320 ASN A C   1 
ATOM   2397 O  O   . ASN A  1  307 ? 62.378  0.890   44.506 1.00 39.84  ? 320 ASN A O   1 
ATOM   2398 C  CB  . ASN A  1  307 ? 62.476  1.603   47.645 1.00 36.41  ? 320 ASN A CB  1 
ATOM   2399 C  CG  . ASN A  1  307 ? 62.718  0.810   48.905 1.00 38.12  ? 320 ASN A CG  1 
ATOM   2400 O  OD1 . ASN A  1  307 ? 63.745  0.136   49.026 1.00 37.75  ? 320 ASN A OD1 1 
ATOM   2401 N  ND2 . ASN A  1  307 ? 61.792  0.881   49.847 1.00 39.80  ? 320 ASN A ND2 1 
ATOM   2402 N  N   . LEU A  1  308 ? 63.513  2.828   44.717 1.00 36.33  ? 321 LEU A N   1 
ATOM   2403 C  CA  . LEU A  1  308 ? 63.236  3.250   43.353 1.00 38.88  ? 321 LEU A CA  1 
ATOM   2404 C  C   . LEU A  1  308 ? 63.912  2.308   42.365 1.00 38.29  ? 321 LEU A C   1 
ATOM   2405 O  O   . LEU A  1  308 ? 63.318  1.933   41.355 1.00 35.40  ? 321 LEU A O   1 
ATOM   2406 C  CB  . LEU A  1  308 ? 63.716  4.679   43.112 1.00 40.94  ? 321 LEU A CB  1 
ATOM   2407 C  CG  . LEU A  1  308 ? 62.693  5.783   43.356 1.00 46.65  ? 321 LEU A CG  1 
ATOM   2408 C  CD1 . LEU A  1  308 ? 63.416  7.106   43.453 1.00 47.53  ? 321 LEU A CD1 1 
ATOM   2409 C  CD2 . LEU A  1  308 ? 61.675  5.803   42.223 1.00 48.46  ? 321 LEU A CD2 1 
ATOM   2410 N  N   . ILE A  1  309 ? 65.187  2.005   42.634 1.00 34.76  ? 322 ILE A N   1 
ATOM   2411 C  CA  . ILE A  1  309 ? 65.971  1.166   41.750 1.00 35.98  ? 322 ILE A CA  1 
ATOM   2412 C  C   . ILE A  1  309 ? 65.310  -0.205  41.647 1.00 34.99  ? 322 ILE A C   1 
ATOM   2413 O  O   . ILE A  1  309 ? 65.198  -0.762  40.559 1.00 38.06  ? 322 ILE A O   1 
ATOM   2414 C  CB  . ILE A  1  309 ? 67.430  1.079   42.245 1.00 33.87  ? 322 ILE A CB  1 
ATOM   2415 C  CG1 . ILE A  1  309 ? 68.163  2.413   42.016 1.00 36.19  ? 322 ILE A CG1 1 
ATOM   2416 C  CG2 . ILE A  1  309 ? 68.152  -0.109  41.605 1.00 34.32  ? 322 ILE A CG2 1 
ATOM   2417 C  CD1 . ILE A  1  309 ? 69.505  2.521   42.724 1.00 37.86  ? 322 ILE A CD1 1 
ATOM   2418 N  N   . LYS A  1  310 ? 64.894  -0.752  42.788 1.00 35.55  ? 323 LYS A N   1 
ATOM   2419 C  CA  . LYS A  1  310 ? 64.271  -2.068  42.809 1.00 41.14  ? 323 LYS A CA  1 
ATOM   2420 C  C   . LYS A  1  310 ? 62.950  -2.063  42.041 1.00 38.75  ? 323 LYS A C   1 
ATOM   2421 O  O   . LYS A  1  310 ? 62.706  -2.939  41.207 1.00 38.23  ? 323 LYS A O   1 
ATOM   2422 C  CB  . LYS A  1  310 ? 64.069  -2.520  44.255 1.00 42.92  ? 323 LYS A CB  1 
ATOM   2423 C  CG  . LYS A  1  310 ? 65.352  -2.931  44.928 1.00 42.23  ? 323 LYS A CG  1 
ATOM   2424 C  CD  . LYS A  1  310 ? 65.181  -3.378  46.372 1.00 47.21  ? 323 LYS A CD  1 
ATOM   2425 C  CE  . LYS A  1  310 ? 66.418  -4.102  46.838 1.00 51.54  ? 323 LYS A CE  1 
ATOM   2426 N  NZ  . LYS A  1  310 ? 66.366  -4.333  48.281 1.00 57.87  ? 323 LYS A NZ  1 
ATOM   2427 N  N   . ASN A  1  311 ? 62.111  -1.062  42.310 1.00 38.44  ? 324 ASN A N   1 
ATOM   2428 C  CA  . ASN A  1  311 ? 60.791  -1.015  41.700 1.00 38.33  ? 324 ASN A CA  1 
ATOM   2429 C  C   . ASN A  1  311 ? 60.903  -0.809  40.190 1.00 39.61  ? 324 ASN A C   1 
ATOM   2430 O  O   . ASN A  1  311 ? 60.092  -1.336  39.434 1.00 38.71  ? 324 ASN A O   1 
ATOM   2431 C  CB  . ASN A  1  311 ? 59.918  0.046   42.353 1.00 37.36  ? 324 ASN A CB  1 
ATOM   2432 C  CG  . ASN A  1  311 ? 59.277  -0.470  43.613 1.00 38.88  ? 324 ASN A CG  1 
ATOM   2433 O  OD1 . ASN A  1  311 ? 58.245  -1.146  43.540 1.00 37.79  ? 324 ASN A OD1 1 
ATOM   2434 N  ND2 . ASN A  1  311 ? 59.848  -0.147  44.765 1.00 40.84  ? 324 ASN A ND2 1 
ATOM   2435 N  N   . LEU A  1  312 ? 61.913  -0.041  39.759 1.00 41.60  ? 325 LEU A N   1 
ATOM   2436 C  CA  . LEU A  1  312 ? 62.121  0.209   38.344 1.00 41.72  ? 325 LEU A CA  1 
ATOM   2437 C  C   . LEU A  1  312 ? 62.518  -1.098  37.664 1.00 41.10  ? 325 LEU A C   1 
ATOM   2438 O  O   . LEU A  1  312 ? 62.065  -1.371  36.558 1.00 38.15  ? 325 LEU A O   1 
ATOM   2439 C  CB  . LEU A  1  312 ? 63.183  1.289   38.127 1.00 44.59  ? 325 LEU A CB  1 
ATOM   2440 C  CG  . LEU A  1  312 ? 62.717  2.736   38.296 1.00 44.65  ? 325 LEU A CG  1 
ATOM   2441 C  CD1 . LEU A  1  312 ? 63.910  3.662   38.519 1.00 44.76  ? 325 LEU A CD1 1 
ATOM   2442 C  CD2 . LEU A  1  312 ? 61.899  3.173   37.086 1.00 41.72  ? 325 LEU A CD2 1 
ATOM   2443 N  N   . HIS A  1  313 ? 63.376  -1.882  38.327 1.00 42.32  ? 326 HIS A N   1 
ATOM   2444 C  CA  . HIS A  1  313 ? 63.788  -3.175  37.806 1.00 45.65  ? 326 HIS A CA  1 
ATOM   2445 C  C   . HIS A  1  313 ? 62.588  -4.117  37.748 1.00 41.92  ? 326 HIS A C   1 
ATOM   2446 O  O   . HIS A  1  313 ? 62.364  -4.750  36.726 1.00 43.82  ? 326 HIS A O   1 
ATOM   2447 C  CB  . HIS A  1  313 ? 64.966  -3.760  38.599 1.00 46.44  ? 326 HIS A CB  1 
ATOM   2448 C  CG  . HIS A  1  313 ? 65.399  -5.063  38.026 1.00 49.72  ? 326 HIS A CG  1 
ATOM   2449 N  ND1 . HIS A  1  313 ? 65.945  -5.134  36.762 1.00 49.26  ? 326 HIS A ND1 1 
ATOM   2450 C  CD2 . HIS A  1  313 ? 65.292  -6.326  38.463 1.00 48.56  ? 326 HIS A CD2 1 
ATOM   2451 C  CE1 . HIS A  1  313 ? 66.212  -6.401  36.481 1.00 50.16  ? 326 HIS A CE1 1 
ATOM   2452 N  NE2 . HIS A  1  313 ? 65.806  -7.144  37.491 1.00 49.92  ? 326 HIS A NE2 1 
ATOM   2453 N  N   . TYR A  1  314 ? 61.809  -4.185  38.832 1.00 45.67  ? 327 TYR A N   1 
ATOM   2454 C  CA  . TYR A  1  314 ? 60.615  -5.025  38.866 1.00 43.45  ? 327 TYR A CA  1 
ATOM   2455 C  C   . TYR A  1  314 ? 59.714  -4.698  37.679 1.00 44.75  ? 327 TYR A C   1 
ATOM   2456 O  O   . TYR A  1  314 ? 59.250  -5.599  36.981 1.00 40.99  ? 327 TYR A O   1 
ATOM   2457 C  CB  . TYR A  1  314 ? 59.804  -4.868  40.157 1.00 42.15  ? 327 TYR A CB  1 
ATOM   2458 C  CG  . TYR A  1  314 ? 60.546  -5.265  41.426 1.00 44.04  ? 327 TYR A CG  1 
ATOM   2459 C  CD1 . TYR A  1  314 ? 61.616  -6.153  41.391 1.00 44.85  ? 327 TYR A CD1 1 
ATOM   2460 C  CD2 . TYR A  1  314 ? 60.175  -4.747  42.665 1.00 44.59  ? 327 TYR A CD2 1 
ATOM   2461 C  CE1 . TYR A  1  314 ? 62.303  -6.504  42.545 1.00 44.03  ? 327 TYR A CE1 1 
ATOM   2462 C  CE2 . TYR A  1  314 ? 60.836  -5.109  43.826 1.00 44.93  ? 327 TYR A CE2 1 
ATOM   2463 C  CZ  . TYR A  1  314 ? 61.909  -5.981  43.764 1.00 45.78  ? 327 TYR A CZ  1 
ATOM   2464 O  OH  . TYR A  1  314 ? 62.558  -6.315  44.916 1.00 43.57  ? 327 TYR A OH  1 
ATOM   2465 N  N   . TRP A  1  315 ? 59.465  -3.404  37.458 1.00 42.29  ? 328 TRP A N   1 
ATOM   2466 C  CA  . TRP A  1  315 ? 58.579  -3.000  36.383 1.00 41.48  ? 328 TRP A CA  1 
ATOM   2467 C  C   . TRP A  1  315 ? 59.158  -3.444  35.042 1.00 41.62  ? 328 TRP A C   1 
ATOM   2468 O  O   . TRP A  1  315 ? 58.444  -4.019  34.219 1.00 39.08  ? 328 TRP A O   1 
ATOM   2469 C  CB  . TRP A  1  315 ? 58.343  -1.487  36.411 1.00 40.14  ? 328 TRP A CB  1 
ATOM   2470 C  CG  . TRP A  1  315 ? 57.255  -1.038  35.477 1.00 37.58  ? 328 TRP A CG  1 
ATOM   2471 C  CD1 . TRP A  1  315 ? 55.996  -1.561  35.347 1.00 37.16  ? 328 TRP A CD1 1 
ATOM   2472 C  CD2 . TRP A  1  315 ? 57.359  0.026   34.509 1.00 37.18  ? 328 TRP A CD2 1 
ATOM   2473 N  NE1 . TRP A  1  315 ? 55.308  -0.881  34.379 1.00 36.97  ? 328 TRP A NE1 1 
ATOM   2474 C  CE2 . TRP A  1  315 ? 56.117  0.094   33.848 1.00 35.88  ? 328 TRP A CE2 1 
ATOM   2475 C  CE3 . TRP A  1  315 ? 58.374  0.916   34.145 1.00 36.87  ? 328 TRP A CE3 1 
ATOM   2476 C  CZ2 . TRP A  1  315 ? 55.869  1.028   32.847 1.00 38.04  ? 328 TRP A CZ2 1 
ATOM   2477 C  CZ3 . TRP A  1  315 ? 58.128  1.833   33.150 1.00 38.56  ? 328 TRP A CZ3 1 
ATOM   2478 C  CH2 . TRP A  1  315 ? 56.897  1.874   32.500 1.00 38.54  ? 328 TRP A CH2 1 
ATOM   2479 N  N   . TRP A  1  316 ? 60.460  -3.205  34.848 1.00 39.90  ? 329 TRP A N   1 
ATOM   2480 C  CA  . TRP A  1  316 ? 61.124  -3.575  33.608 1.00 41.16  ? 329 TRP A CA  1 
ATOM   2481 C  C   . TRP A  1  316 ? 60.949  -5.065  33.311 1.00 41.16  ? 329 TRP A C   1 
ATOM   2482 O  O   . TRP A  1  316 ? 60.813  -5.417  32.144 1.00 40.84  ? 329 TRP A O   1 
ATOM   2483 C  CB  . TRP A  1  316 ? 62.615  -3.196  33.627 1.00 44.79  ? 329 TRP A CB  1 
ATOM   2484 C  CG  . TRP A  1  316 ? 63.336  -3.724  32.414 1.00 47.61  ? 329 TRP A CG  1 
ATOM   2485 C  CD1 . TRP A  1  316 ? 63.397  -3.159  31.174 1.00 51.31  ? 329 TRP A CD1 1 
ATOM   2486 C  CD2 . TRP A  1  316 ? 64.029  -4.982  32.312 1.00 47.25  ? 329 TRP A CD2 1 
ATOM   2487 N  NE1 . TRP A  1  316 ? 64.101  -3.963  30.314 1.00 48.88  ? 329 TRP A NE1 1 
ATOM   2488 C  CE2 . TRP A  1  316 ? 64.504  -5.083  30.988 1.00 48.98  ? 329 TRP A CE2 1 
ATOM   2489 C  CE3 . TRP A  1  316 ? 64.310  -6.015  33.213 1.00 51.02  ? 329 TRP A CE3 1 
ATOM   2490 C  CZ2 . TRP A  1  316 ? 65.237  -6.181  30.547 1.00 49.48  ? 329 TRP A CZ2 1 
ATOM   2491 C  CZ3 . TRP A  1  316 ? 65.034  -7.103  32.774 1.00 50.67  ? 329 TRP A CZ3 1 
ATOM   2492 C  CH2 . TRP A  1  316 ? 65.483  -7.185  31.457 1.00 49.44  ? 329 TRP A CH2 1 
ATOM   2493 N  N   . THR A  1  317 ? 60.963  -5.933  34.338 1.00 44.84  ? 330 THR A N   1 
ATOM   2494 C  CA  . THR A  1  317 ? 60.887  -7.369  34.094 1.00 47.57  ? 330 THR A CA  1 
ATOM   2495 C  C   . THR A  1  317 ? 59.566  -7.686  33.407 1.00 44.87  ? 330 THR A C   1 
ATOM   2496 O  O   . THR A  1  317 ? 59.510  -8.563  32.554 1.00 51.67  ? 330 THR A O   1 
ATOM   2497 C  CB  . THR A  1  317 ? 61.048  -8.227  35.352 1.00 45.61  ? 330 THR A CB  1 
ATOM   2498 O  OG1 . THR A  1  317 ? 59.945  -8.002  36.222 1.00 46.04  ? 330 THR A OG1 1 
ATOM   2499 C  CG2 . THR A  1  317 ? 62.352  -7.972  36.080 1.00 46.75  ? 330 THR A CG2 1 
ATOM   2500 N  N   . GLY A  1  318 ? 58.503  -6.977  33.787 1.00 43.97  ? 331 GLY A N   1 
ATOM   2501 C  CA  . GLY A  1  318 ? 57.217  -7.147  33.136 1.00 41.27  ? 331 GLY A CA  1 
ATOM   2502 C  C   . GLY A  1  318 ? 57.194  -6.498  31.754 1.00 40.56  ? 331 GLY A C   1 
ATOM   2503 O  O   . GLY A  1  318 ? 56.698  -7.078  30.791 1.00 38.10  ? 331 GLY A O   1 
ATOM   2504 N  N   . VAL A  1  319 ? 57.720  -5.276  31.667 1.00 43.96  ? 332 VAL A N   1 
ATOM   2505 C  CA  . VAL A  1  319 ? 57.696  -4.510  30.431 1.00 43.64  ? 332 VAL A CA  1 
ATOM   2506 C  C   . VAL A  1  319 ? 58.465  -5.262  29.348 1.00 44.44  ? 332 VAL A C   1 
ATOM   2507 O  O   . VAL A  1  319 ? 58.030  -5.326  28.197 1.00 43.99  ? 332 VAL A O   1 
ATOM   2508 C  CB  . VAL A  1  319 ? 58.294  -3.114  30.690 1.00 47.31  ? 332 VAL A CB  1 
ATOM   2509 C  CG1 . VAL A  1  319 ? 58.697  -2.400  29.409 1.00 46.98  ? 332 VAL A CG1 1 
ATOM   2510 C  CG2 . VAL A  1  319 ? 57.331  -2.259  31.495 1.00 49.36  ? 332 VAL A CG2 1 
ATOM   2511 N  N   . ASN A  1  320 ? 59.621  -5.821  29.724 1.00 45.22  ? 333 ASN A N   1 
ATOM   2512 C  CA  . ASN A  1  320 ? 60.502  -6.465  28.765 1.00 44.94  ? 333 ASN A CA  1 
ATOM   2513 C  C   . ASN A  1  320 ? 59.752  -7.560  28.017 1.00 45.40  ? 333 ASN A C   1 
ATOM   2514 O  O   . ASN A  1  320 ? 59.908  -7.686  26.811 1.00 44.26  ? 333 ASN A O   1 
ATOM   2515 C  CB  . ASN A  1  320 ? 61.751  -7.026  29.431 1.00 47.24  ? 333 ASN A CB  1 
ATOM   2516 C  CG  . ASN A  1  320 ? 62.798  -7.409  28.418 1.00 47.09  ? 333 ASN A CG  1 
ATOM   2517 O  OD1 . ASN A  1  320 ? 63.146  -6.593  27.561 1.00 46.56  ? 333 ASN A OD1 1 
ATOM   2518 N  ND2 . ASN A  1  320 ? 63.289  -8.634  28.483 1.00 46.86  ? 333 ASN A ND2 1 
ATOM   2519 N  N   . VAL A  1  321 ? 58.927  -8.330  28.738 1.00 44.97  ? 334 VAL A N   1 
ATOM   2520 C  CA  . VAL A  1  321 ? 58.154  -9.404  28.139 1.00 46.18  ? 334 VAL A CA  1 
ATOM   2521 C  C   . VAL A  1  321 ? 56.946  -8.817  27.412 1.00 47.30  ? 334 VAL A C   1 
ATOM   2522 O  O   . VAL A  1  321 ? 56.732  -9.121  26.250 1.00 48.21  ? 334 VAL A O   1 
ATOM   2523 C  CB  . VAL A  1  321 ? 57.754  -10.447 29.203 1.00 48.44  ? 334 VAL A CB  1 
ATOM   2524 C  CG1 . VAL A  1  321 ? 56.802  -11.515 28.668 1.00 49.86  ? 334 VAL A CG1 1 
ATOM   2525 C  CG2 . VAL A  1  321 ? 58.978  -11.080 29.861 1.00 49.37  ? 334 VAL A CG2 1 
ATOM   2526 N  N   . ALA A  1  322 ? 56.164  -7.960  28.078 1.00 48.02  ? 335 ALA A N   1 
ATOM   2527 C  CA  . ALA A  1  322 ? 54.891  -7.520  27.530 1.00 49.36  ? 335 ALA A CA  1 
ATOM   2528 C  C   . ALA A  1  322 ? 55.094  -6.711  26.248 1.00 51.50  ? 335 ALA A C   1 
ATOM   2529 O  O   . ALA A  1  322 ? 54.231  -6.722  25.376 1.00 49.37  ? 335 ALA A O   1 
ATOM   2530 C  CB  . ALA A  1  322 ? 54.123  -6.713  28.569 1.00 52.47  ? 335 ALA A CB  1 
ATOM   2531 N  N   . PHE A  1  323 ? 56.213  -5.979  26.150 1.00 50.69  ? 336 PHE A N   1 
ATOM   2532 C  CA  . PHE A  1  323 ? 56.434  -5.080  25.029 1.00 51.64  ? 336 PHE A CA  1 
ATOM   2533 C  C   . PHE A  1  323 ? 57.350  -5.721  23.989 1.00 52.78  ? 336 PHE A C   1 
ATOM   2534 O  O   . PHE A  1  323 ? 57.637  -5.103  22.972 1.00 53.50  ? 336 PHE A O   1 
ATOM   2535 C  CB  . PHE A  1  323 ? 57.001  -3.732  25.489 1.00 49.87  ? 336 PHE A CB  1 
ATOM   2536 C  CG  . PHE A  1  323 ? 56.075  -2.856  26.328 1.00 48.55  ? 336 PHE A CG  1 
ATOM   2537 C  CD1 . PHE A  1  323 ? 54.735  -3.190  26.518 1.00 53.06  ? 336 PHE A CD1 1 
ATOM   2538 C  CD2 . PHE A  1  323 ? 56.528  -1.660  26.867 1.00 47.74  ? 336 PHE A CD2 1 
ATOM   2539 C  CE1 . PHE A  1  323 ? 53.896  -2.375  27.263 1.00 50.46  ? 336 PHE A CE1 1 
ATOM   2540 C  CE2 . PHE A  1  323 ? 55.689  -0.856  27.620 1.00 48.46  ? 336 PHE A CE2 1 
ATOM   2541 C  CZ  . PHE A  1  323 ? 54.374  -1.213  27.816 1.00 51.03  ? 336 PHE A CZ  1 
ATOM   2542 N  N   . GLY A  1  324 ? 57.794  -6.958  24.233 1.00 53.54  ? 337 GLY A N   1 
ATOM   2543 C  CA  . GLY A  1  324 ? 58.627  -7.679  23.283 1.00 54.95  ? 337 GLY A CA  1 
ATOM   2544 C  C   . GLY A  1  324 ? 60.064  -7.156  23.230 1.00 53.43  ? 337 GLY A C   1 
ATOM   2545 O  O   . GLY A  1  324 ? 60.716  -7.278  22.200 1.00 57.28  ? 337 GLY A O   1 
ATOM   2546 N  N   . GLY A  1  325 ? 60.560  -6.600  24.342 1.00 53.24  ? 338 GLY A N   1 
ATOM   2547 C  CA  . GLY A  1  325 ? 61.977  -6.287  24.492 1.00 48.69  ? 338 GLY A CA  1 
ATOM   2548 C  C   . GLY A  1  325 ? 62.228  -4.780  24.498 1.00 50.88  ? 338 GLY A C   1 
ATOM   2549 O  O   . GLY A  1  325 ? 62.016  -4.119  23.489 1.00 50.10  ? 338 GLY A O   1 
ATOM   2550 N  N   . CYS A  1  326 ? 62.658  -4.243  25.652 1.00 51.88  ? 339 CYS A N   1 
ATOM   2551 C  CA  . CYS A  1  326 ? 63.089  -2.855  25.764 1.00 49.26  ? 339 CYS A CA  1 
ATOM   2552 C  C   . CYS A  1  326 ? 64.395  -2.809  26.552 1.00 48.20  ? 339 CYS A C   1 
ATOM   2553 O  O   . CYS A  1  326 ? 64.558  -3.548  27.521 1.00 45.46  ? 339 CYS A O   1 
ATOM   2554 C  CB  . CYS A  1  326 ? 62.079  -1.988  26.509 1.00 53.94  ? 339 CYS A CB  1 
ATOM   2555 S  SG  . CYS A  1  326 ? 60.405  -1.978  25.806 1.00 63.22  ? 339 CYS A SG  1 
ATOM   2556 N  N   . ASP A  1  327 ? 65.316  -1.929  26.145 1.00 48.65  ? 340 ASP A N   1 
ATOM   2557 C  CA  . ASP A  1  327 ? 66.570  -1.760  26.862 1.00 50.87  ? 340 ASP A CA  1 
ATOM   2558 C  C   . ASP A  1  327 ? 66.286  -1.121  28.217 1.00 49.97  ? 340 ASP A C   1 
ATOM   2559 O  O   . ASP A  1  327 ? 65.660  -0.061  28.293 1.00 48.30  ? 340 ASP A O   1 
ATOM   2560 C  CB  . ASP A  1  327 ? 67.567  -0.933  26.066 1.00 55.61  ? 340 ASP A CB  1 
ATOM   2561 C  CG  . ASP A  1  327 ? 68.010  -1.532  24.737 1.00 61.72  ? 340 ASP A CG  1 
ATOM   2562 O  OD1 . ASP A  1  327 ? 67.794  -2.747  24.535 1.00 60.87  ? 340 ASP A OD1 1 
ATOM   2563 O  OD2 . ASP A  1  327 ? 68.537  -0.769  23.899 1.00 69.45  ? 340 ASP A OD2 1 
ATOM   2564 N  N   . GLU A  1  328 ? 66.764  -1.779  29.279 1.00 48.01  ? 341 GLU A N   1 
ATOM   2565 C  CA  . GLU A  1  328 ? 66.528  -1.312  30.631 1.00 49.76  ? 341 GLU A CA  1 
ATOM   2566 C  C   . GLU A  1  328 ? 67.295  -0.010  30.847 1.00 51.24  ? 341 GLU A C   1 
ATOM   2567 O  O   . GLU A  1  328 ? 68.460  0.096   30.466 1.00 53.39  ? 341 GLU A O   1 
ATOM   2568 C  CB  . GLU A  1  328 ? 66.942  -2.366  31.658 1.00 46.94  ? 341 GLU A CB  1 
ATOM   2569 C  CG  . GLU A  1  328 ? 66.542  -1.998  33.084 1.00 46.51  ? 341 GLU A CG  1 
ATOM   2570 C  CD  . GLU A  1  328 ? 66.699  -3.102  34.108 1.00 47.86  ? 341 GLU A CD  1 
ATOM   2571 O  OE1 . GLU A  1  328 ? 67.213  -4.169  33.718 1.00 51.55  ? 341 GLU A OE1 1 
ATOM   2572 O  OE2 . GLU A  1  328 ? 66.309  -2.900  35.283 1.00 45.32  ? 341 GLU A OE2 1 
ATOM   2573 N  N   . LEU A  1  329 ? 66.624  0.971   31.466 1.00 49.41  ? 342 LEU A N   1 
ATOM   2574 C  CA  . LEU A  1  329 ? 67.266  2.219   31.843 1.00 48.28  ? 342 LEU A CA  1 
ATOM   2575 C  C   . LEU A  1  329 ? 67.619  2.170   33.325 1.00 47.81  ? 342 LEU A C   1 
ATOM   2576 O  O   . LEU A  1  329 ? 66.900  1.550   34.111 1.00 46.70  ? 342 LEU A O   1 
ATOM   2577 C  CB  . LEU A  1  329 ? 66.352  3.395   31.510 1.00 47.71  ? 342 LEU A CB  1 
ATOM   2578 C  CG  . LEU A  1  329 ? 66.000  3.563   30.027 1.00 48.86  ? 342 LEU A CG  1 
ATOM   2579 C  CD1 . LEU A  1  329 ? 64.873  4.562   29.842 1.00 47.10  ? 342 LEU A CD1 1 
ATOM   2580 C  CD2 . LEU A  1  329 ? 67.229  3.984   29.225 1.00 48.85  ? 342 LEU A CD2 1 
ATOM   2581 N  N   . PHE A  1  330 ? 68.719  2.851   33.685 1.00 48.61  ? 343 PHE A N   1 
ATOM   2582 C  CA  . PHE A  1  330 ? 69.222  2.875   35.049 1.00 48.04  ? 343 PHE A CA  1 
ATOM   2583 C  C   . PHE A  1  330 ? 69.458  4.314   35.492 1.00 48.55  ? 343 PHE A C   1 
ATOM   2584 O  O   . PHE A  1  330 ? 70.598  4.720   35.719 1.00 48.40  ? 343 PHE A O   1 
ATOM   2585 C  CB  . PHE A  1  330 ? 70.516  2.063   35.133 1.00 50.78  ? 343 PHE A CB  1 
ATOM   2586 C  CG  . PHE A  1  330 ? 70.335  0.605   34.739 1.00 53.35  ? 343 PHE A CG  1 
ATOM   2587 C  CD1 . PHE A  1  330 ? 69.735  -0.306  35.606 1.00 57.61  ? 343 PHE A CD1 1 
ATOM   2588 C  CD2 . PHE A  1  330 ? 70.765  0.153   33.499 1.00 52.95  ? 343 PHE A CD2 1 
ATOM   2589 C  CE1 . PHE A  1  330 ? 69.552  -1.631  35.230 1.00 58.44  ? 343 PHE A CE1 1 
ATOM   2590 C  CE2 . PHE A  1  330 ? 70.593  -1.175  33.133 1.00 57.48  ? 343 PHE A CE2 1 
ATOM   2591 C  CZ  . PHE A  1  330 ? 70.013  -2.067  34.007 1.00 56.42  ? 343 PHE A CZ  1 
ATOM   2592 N  N   . PRO A  1  331 ? 68.390  5.122   35.661 1.00 43.89  ? 344 PRO A N   1 
ATOM   2593 C  CA  . PRO A  1  331 ? 68.544  6.540   35.984 1.00 43.28  ? 344 PRO A CA  1 
ATOM   2594 C  C   . PRO A  1  331 ? 69.229  6.812   37.316 1.00 41.07  ? 344 PRO A C   1 
ATOM   2595 O  O   . PRO A  1  331 ? 69.750  7.906   37.511 1.00 44.92  ? 344 PRO A O   1 
ATOM   2596 C  CB  . PRO A  1  331 ? 67.085  7.052   35.977 1.00 44.11  ? 344 PRO A CB  1 
ATOM   2597 C  CG  . PRO A  1  331 ? 66.255  5.825   36.283 1.00 42.42  ? 344 PRO A CG  1 
ATOM   2598 C  CD  . PRO A  1  331 ? 66.977  4.725   35.545 1.00 44.13  ? 344 PRO A CD  1 
ATOM   2599 N  N   . TYR A  1  332 ? 69.223  5.826   38.226 1.00 40.06  ? 345 TYR A N   1 
ATOM   2600 C  CA  . TYR A  1  332 ? 69.864  5.994   39.520 1.00 42.76  ? 345 TYR A CA  1 
ATOM   2601 C  C   . TYR A  1  332 ? 71.019  5.010   39.685 1.00 40.00  ? 345 TYR A C   1 
ATOM   2602 O  O   . TYR A  1  332 ? 71.468  4.782   40.792 1.00 37.33  ? 345 TYR A O   1 
ATOM   2603 C  CB  . TYR A  1  332 ? 68.830  5.850   40.638 1.00 43.40  ? 345 TYR A CB  1 
ATOM   2604 C  CG  . TYR A  1  332 ? 67.620  6.741   40.407 1.00 43.67  ? 345 TYR A CG  1 
ATOM   2605 C  CD1 . TYR A  1  332 ? 67.732  8.131   40.426 1.00 43.06  ? 345 TYR A CD1 1 
ATOM   2606 C  CD2 . TYR A  1  332 ? 66.378  6.194   40.111 1.00 44.52  ? 345 TYR A CD2 1 
ATOM   2607 C  CE1 . TYR A  1  332 ? 66.639  8.945   40.183 1.00 44.08  ? 345 TYR A CE1 1 
ATOM   2608 C  CE2 . TYR A  1  332 ? 65.274  6.997   39.874 1.00 45.31  ? 345 TYR A CE2 1 
ATOM   2609 C  CZ  . TYR A  1  332 ? 65.405  8.375   39.903 1.00 47.32  ? 345 TYR A CZ  1 
ATOM   2610 O  OH  . TYR A  1  332 ? 64.304  9.146   39.659 1.00 45.61  ? 345 TYR A OH  1 
ATOM   2611 N  N   . GLY A  1  333 ? 71.504  4.442   38.577 1.00 44.51  ? 346 GLY A N   1 
ATOM   2612 C  CA  . GLY A  1  333 ? 72.549  3.431   38.636 1.00 49.31  ? 346 GLY A CA  1 
ATOM   2613 C  C   . GLY A  1  333 ? 72.007  2.108   39.172 1.00 50.06  ? 346 GLY A C   1 
ATOM   2614 O  O   . GLY A  1  333 ? 70.826  1.801   38.962 1.00 46.37  ? 346 GLY A O   1 
ATOM   2615 N  N   . GLN A  1  334 ? 72.877  1.377   39.895 1.00 50.03  ? 347 GLN A N   1 
ATOM   2616 C  CA  A GLN A  1  334 ? 72.554  0.073   40.450 0.50 53.20  ? 347 GLN A CA  1 
ATOM   2617 C  CA  B GLN A  1  334 ? 72.553  0.070   40.448 0.50 53.24  ? 347 GLN A CA  1 
ATOM   2618 C  C   . GLN A  1  334 ? 72.729  0.097   41.965 1.00 51.75  ? 347 GLN A C   1 
ATOM   2619 O  O   . GLN A  1  334 ? 73.262  1.052   42.515 1.00 50.68  ? 347 GLN A O   1 
ATOM   2620 C  CB  A GLN A  1  334 ? 73.432  -0.995  39.796 0.50 57.88  ? 347 GLN A CB  1 
ATOM   2621 C  CB  B GLN A  1  334 ? 73.402  -1.027  39.794 0.50 58.05  ? 347 GLN A CB  1 
ATOM   2622 C  CG  A GLN A  1  334 ? 72.976  -1.362  38.386 0.50 59.51  ? 347 GLN A CG  1 
ATOM   2623 C  CG  B GLN A  1  334 ? 73.141  -1.186  38.297 0.50 59.51  ? 347 GLN A CG  1 
ATOM   2624 C  CD  A GLN A  1  334 ? 73.594  -0.505  37.304 0.50 58.64  ? 347 GLN A CD  1 
ATOM   2625 C  CD  B GLN A  1  334 ? 73.045  -2.619  37.811 0.50 58.65  ? 347 GLN A CD  1 
ATOM   2626 O  OE1 A GLN A  1  334 ? 74.394  0.399   37.575 0.50 60.47  ? 347 GLN A OE1 1 
ATOM   2627 O  OE1 B GLN A  1  334 ? 73.164  -3.583  38.577 0.50 58.71  ? 347 GLN A OE1 1 
ATOM   2628 N  NE2 A GLN A  1  334 ? 73.225  -0.782  36.064 0.50 56.02  ? 347 GLN A NE2 1 
ATOM   2629 N  NE2 B GLN A  1  334 ? 72.804  -2.769  36.518 0.50 59.48  ? 347 GLN A NE2 1 
ATOM   2630 N  N   . LEU A  1  335 ? 72.267  -0.967  42.635 1.00 53.72  ? 348 LEU A N   1 
ATOM   2631 C  CA  . LEU A  1  335 ? 72.356  -1.095  44.086 1.00 54.64  ? 348 LEU A CA  1 
ATOM   2632 C  C   . LEU A  1  335 ? 73.832  -1.204  44.512 1.00 55.75  ? 348 LEU A C   1 
ATOM   2633 O  O   . LEU A  1  335 ? 74.565  -1.870  43.753 1.00 57.98  ? 348 LEU A O   1 
ATOM   2634 C  CB  . LEU A  1  335 ? 71.577  -2.320  44.559 1.00 51.85  ? 348 LEU A CB  1 
ATOM   2635 C  CG  . LEU A  1  335 ? 70.063  -2.307  44.314 1.00 55.30  ? 348 LEU A CG  1 
ATOM   2636 C  CD1 . LEU A  1  335 ? 69.420  -3.625  44.712 1.00 55.87  ? 348 LEU A CD1 1 
ATOM   2637 C  CD2 . LEU A  1  335 ? 69.431  -1.164  45.074 1.00 54.64  ? 348 LEU A CD2 1 
ATOM   2638 N  N   . GLN B  1  1   ? -0.363  19.176  56.789 1.00 141.80 ? 14  GLN B N   1 
ATOM   2639 C  CA  . GLN B  1  1   ? 0.001   18.572  58.101 1.00 141.62 ? 14  GLN B CA  1 
ATOM   2640 C  C   . GLN B  1  1   ? -0.730  17.241  58.279 1.00 131.99 ? 14  GLN B C   1 
ATOM   2641 O  O   . GLN B  1  1   ? -0.095  16.190  58.383 1.00 127.27 ? 14  GLN B O   1 
ATOM   2642 C  CB  . GLN B  1  1   ? -0.351  19.505  59.263 1.00 145.59 ? 14  GLN B CB  1 
ATOM   2643 C  CG  . GLN B  1  1   ? 0.439   20.808  59.294 1.00 141.96 ? 14  GLN B CG  1 
ATOM   2644 C  CD  . GLN B  1  1   ? -0.067  21.799  60.321 1.00 140.06 ? 14  GLN B CD  1 
ATOM   2645 O  OE1 . GLN B  1  1   ? -1.046  21.567  61.043 1.00 134.65 ? 14  GLN B OE1 1 
ATOM   2646 N  NE2 . GLN B  1  1   ? 0.610   22.934  60.390 1.00 140.11 ? 14  GLN B NE2 1 
ATOM   2647 N  N   . GLY B  1  2   ? -2.072  17.305  58.293 1.00 115.71 ? 15  GLY B N   1 
ATOM   2648 C  CA  . GLY B  1  2   ? -2.918  16.146  58.546 1.00 97.85  ? 15  GLY B CA  1 
ATOM   2649 C  C   . GLY B  1  2   ? -3.419  15.522  57.246 1.00 83.30  ? 15  GLY B C   1 
ATOM   2650 O  O   . GLY B  1  2   ? -3.883  16.228  56.356 1.00 75.60  ? 15  GLY B O   1 
ATOM   2651 N  N   . VAL B  1  3   ? -3.326  14.190  57.158 1.00 76.14  ? 16  VAL B N   1 
ATOM   2652 C  CA  . VAL B  1  3   ? -3.615  13.454  55.939 1.00 72.18  ? 16  VAL B CA  1 
ATOM   2653 C  C   . VAL B  1  3   ? -4.878  12.626  56.152 1.00 63.68  ? 16  VAL B C   1 
ATOM   2654 O  O   . VAL B  1  3   ? -5.186  12.215  57.269 1.00 61.73  ? 16  VAL B O   1 
ATOM   2655 C  CB  . VAL B  1  3   ? -2.399  12.575  55.576 1.00 76.86  ? 16  VAL B CB  1 
ATOM   2656 C  CG1 . VAL B  1  3   ? -2.743  11.420  54.638 1.00 76.96  ? 16  VAL B CG1 1 
ATOM   2657 C  CG2 . VAL B  1  3   ? -1.257  13.411  55.011 1.00 77.53  ? 16  VAL B CG2 1 
ATOM   2658 N  N   . ASP B  1  4   ? -5.594  12.386  55.051 1.00 64.22  ? 17  ASP B N   1 
ATOM   2659 C  CA  . ASP B  1  4   ? -6.758  11.524  55.055 1.00 68.44  ? 17  ASP B CA  1 
ATOM   2660 C  C   . ASP B  1  4   ? -6.329  10.142  54.555 1.00 65.65  ? 17  ASP B C   1 
ATOM   2661 O  O   . ASP B  1  4   ? -6.097  9.973   53.360 1.00 58.97  ? 17  ASP B O   1 
ATOM   2662 C  CB  . ASP B  1  4   ? -7.868  12.160  54.233 1.00 77.21  ? 17  ASP B CB  1 
ATOM   2663 C  CG  . ASP B  1  4   ? -9.263  11.616  54.494 1.00 86.59  ? 17  ASP B CG  1 
ATOM   2664 O  OD1 . ASP B  1  4   ? -9.417  10.880  55.482 1.00 101.50 ? 17  ASP B OD1 1 
ATOM   2665 O  OD2 . ASP B  1  4   ? -10.170 11.891  53.687 1.00 94.42  ? 17  ASP B OD2 1 
ATOM   2666 N  N   . PRO B  1  5   ? -6.202  9.113   55.432 1.00 62.13  ? 18  PRO B N   1 
ATOM   2667 C  CA  . PRO B  1  5   ? -5.545  7.860   55.063 1.00 58.71  ? 18  PRO B CA  1 
ATOM   2668 C  C   . PRO B  1  5   ? -6.437  6.990   54.182 1.00 55.32  ? 18  PRO B C   1 
ATOM   2669 O  O   . PRO B  1  5   ? -7.570  6.690   54.548 1.00 56.93  ? 18  PRO B O   1 
ATOM   2670 C  CB  . PRO B  1  5   ? -5.228  7.207   56.423 1.00 58.18  ? 18  PRO B CB  1 
ATOM   2671 C  CG  . PRO B  1  5   ? -6.350  7.676   57.324 1.00 59.68  ? 18  PRO B CG  1 
ATOM   2672 C  CD  . PRO B  1  5   ? -6.709  9.073   56.808 1.00 62.34  ? 18  PRO B CD  1 
ATOM   2673 N  N   . PRO B  1  6   ? -5.949  6.549   53.004 1.00 55.09  ? 19  PRO B N   1 
ATOM   2674 C  CA  . PRO B  1  6   ? -6.768  5.766   52.082 1.00 54.91  ? 19  PRO B CA  1 
ATOM   2675 C  C   . PRO B  1  6   ? -6.882  4.324   52.564 1.00 55.80  ? 19  PRO B C   1 
ATOM   2676 O  O   . PRO B  1  6   ? -6.070  3.873   53.363 1.00 53.07  ? 19  PRO B O   1 
ATOM   2677 C  CB  . PRO B  1  6   ? -5.989  5.881   50.763 1.00 56.42  ? 19  PRO B CB  1 
ATOM   2678 C  CG  . PRO B  1  6   ? -4.536  5.961   51.213 1.00 58.05  ? 19  PRO B CG  1 
ATOM   2679 C  CD  . PRO B  1  6   ? -4.577  6.750   52.512 1.00 57.96  ? 19  PRO B CD  1 
ATOM   2680 N  N   . PRO B  1  7   ? -7.899  3.565   52.101 1.00 58.15  ? 20  PRO B N   1 
ATOM   2681 C  CA  . PRO B  1  7   ? -8.027  2.153   52.459 1.00 57.34  ? 20  PRO B CA  1 
ATOM   2682 C  C   . PRO B  1  7   ? -6.845  1.375   51.889 1.00 53.67  ? 20  PRO B C   1 
ATOM   2683 O  O   . PRO B  1  7   ? -6.192  1.829   50.954 1.00 51.47  ? 20  PRO B O   1 
ATOM   2684 C  CB  . PRO B  1  7   ? -9.381  1.748   51.841 1.00 59.31  ? 20  PRO B CB  1 
ATOM   2685 C  CG  . PRO B  1  7   ? -9.576  2.732   50.690 1.00 63.53  ? 20  PRO B CG  1 
ATOM   2686 C  CD  . PRO B  1  7   ? -8.966  4.032   51.199 1.00 63.27  ? 20  PRO B CD  1 
ATOM   2687 N  N   . PRO B  1  8   ? -6.505  0.196   52.445 1.00 51.46  ? 21  PRO B N   1 
ATOM   2688 C  CA  . PRO B  1  8   ? -5.369  -0.573  51.940 1.00 52.07  ? 21  PRO B CA  1 
ATOM   2689 C  C   . PRO B  1  8   ? -5.581  -1.034  50.503 1.00 47.87  ? 21  PRO B C   1 
ATOM   2690 O  O   . PRO B  1  8   ? -6.705  -1.299  50.085 1.00 47.70  ? 21  PRO B O   1 
ATOM   2691 C  CB  . PRO B  1  8   ? -5.250  -1.757  52.901 1.00 52.24  ? 21  PRO B CB  1 
ATOM   2692 C  CG  . PRO B  1  8   ? -6.638  -1.879  53.492 1.00 54.24  ? 21  PRO B CG  1 
ATOM   2693 C  CD  . PRO B  1  8   ? -7.160  -0.448  53.588 1.00 52.48  ? 21  PRO B CD  1 
ATOM   2694 N  N   . PRO B  1  9   ? -4.494  -1.148  49.711 1.00 44.20  ? 22  PRO B N   1 
ATOM   2695 C  CA  . PRO B  1  9   ? -4.560  -1.794  48.405 1.00 42.32  ? 22  PRO B CA  1 
ATOM   2696 C  C   . PRO B  1  9   ? -5.080  -3.213  48.584 1.00 44.05  ? 22  PRO B C   1 
ATOM   2697 O  O   . PRO B  1  9   ? -4.876  -3.823  49.637 1.00 45.87  ? 22  PRO B O   1 
ATOM   2698 C  CB  . PRO B  1  9   ? -3.107  -1.777  47.900 1.00 40.78  ? 22  PRO B CB  1 
ATOM   2699 C  CG  . PRO B  1  9   ? -2.461  -0.657  48.683 1.00 41.61  ? 22  PRO B CG  1 
ATOM   2700 C  CD  . PRO B  1  9   ? -3.153  -0.643  50.031 1.00 41.43  ? 22  PRO B CD  1 
ATOM   2701 N  N   . GLY B  1  10  ? -5.742  -3.717  47.539 1.00 43.89  ? 23  GLY B N   1 
ATOM   2702 C  CA  . GLY B  1  10  ? -6.073  -5.125  47.440 1.00 46.02  ? 23  GLY B CA  1 
ATOM   2703 C  C   . GLY B  1  10  ? -4.892  -5.898  46.862 1.00 47.37  ? 23  GLY B C   1 
ATOM   2704 O  O   . GLY B  1  10  ? -3.801  -5.346  46.706 1.00 43.21  ? 23  GLY B O   1 
ATOM   2705 N  N   . PRO B  1  11  ? -5.085  -7.191  46.519 1.00 49.67  ? 24  PRO B N   1 
ATOM   2706 C  CA  . PRO B  1  11  ? -4.032  -7.988  45.888 1.00 48.93  ? 24  PRO B CA  1 
ATOM   2707 C  C   . PRO B  1  11  ? -3.570  -7.341  44.580 1.00 49.93  ? 24  PRO B C   1 
ATOM   2708 O  O   . PRO B  1  11  ? -4.314  -6.593  43.954 1.00 46.76  ? 24  PRO B O   1 
ATOM   2709 C  CB  . PRO B  1  11  ? -4.673  -9.365  45.638 1.00 51.14  ? 24  PRO B CB  1 
ATOM   2710 C  CG  . PRO B  1  11  ? -5.917  -9.383  46.520 1.00 52.39  ? 24  PRO B CG  1 
ATOM   2711 C  CD  . PRO B  1  11  ? -6.343  -7.933  46.695 1.00 49.18  ? 24  PRO B CD  1 
ATOM   2712 N  N   . PRO B  1  12  ? -2.334  -7.612  44.110 1.00 50.80  ? 25  PRO B N   1 
ATOM   2713 C  CA  . PRO B  1  12  ? -1.900  -7.094  42.815 1.00 52.78  ? 25  PRO B CA  1 
ATOM   2714 C  C   . PRO B  1  12  ? -2.674  -7.786  41.695 1.00 54.20  ? 25  PRO B C   1 
ATOM   2715 O  O   . PRO B  1  12  ? -3.090  -8.936  41.851 1.00 47.99  ? 25  PRO B O   1 
ATOM   2716 C  CB  . PRO B  1  12  ? -0.394  -7.417  42.803 1.00 52.84  ? 25  PRO B CB  1 
ATOM   2717 C  CG  . PRO B  1  12  ? -0.257  -8.617  43.711 1.00 47.82  ? 25  PRO B CG  1 
ATOM   2718 C  CD  . PRO B  1  12  ? -1.332  -8.469  44.765 1.00 48.87  ? 25  PRO B CD  1 
ATOM   2719 N  N   . SER B  1  13  ? -2.860  -7.066  40.578 1.00 57.72  ? 26  SER B N   1 
ATOM   2720 C  CA  A SER B  1  13  ? -3.554  -7.586  39.408 0.50 58.50  ? 26  SER B CA  1 
ATOM   2721 C  CA  B SER B  1  13  ? -3.552  -7.583  39.405 0.50 57.80  ? 26  SER B CA  1 
ATOM   2722 C  C   . SER B  1  13  ? -2.886  -8.865  38.908 1.00 57.73  ? 26  SER B C   1 
ATOM   2723 O  O   . SER B  1  13  ? -3.570  -9.833  38.585 1.00 58.63  ? 26  SER B O   1 
ATOM   2724 C  CB  A SER B  1  13  ? -3.613  -6.558  38.308 0.50 60.25  ? 26  SER B CB  1 
ATOM   2725 C  CB  B SER B  1  13  ? -3.601  -6.541  38.308 0.50 58.67  ? 26  SER B CB  1 
ATOM   2726 O  OG  A SER B  1  13  ? -4.258  -5.374  38.754 0.50 61.37  ? 26  SER B OG  1 
ATOM   2727 O  OG  B SER B  1  13  ? -4.271  -7.028  37.153 0.50 57.89  ? 26  SER B OG  1 
ATOM   2728 N  N   . PHE B  1  14  ? -1.545  -8.849  38.833 1.00 52.35  ? 27  PHE B N   1 
ATOM   2729 C  CA  . PHE B  1  14  ? -0.765  -10.009 38.421 1.00 53.34  ? 27  PHE B CA  1 
ATOM   2730 C  C   . PHE B  1  14  ? -0.108  -10.626 39.657 1.00 46.03  ? 27  PHE B C   1 
ATOM   2731 O  O   . PHE B  1  14  ? 0.567   -9.919  40.400 1.00 43.57  ? 27  PHE B O   1 
ATOM   2732 C  CB  . PHE B  1  14  ? 0.263   -9.588  37.362 1.00 52.91  ? 27  PHE B CB  1 
ATOM   2733 C  CG  . PHE B  1  14  ? 1.203   -10.704 36.922 1.00 53.07  ? 27  PHE B CG  1 
ATOM   2734 C  CD1 . PHE B  1  14  ? 0.748   -11.720 36.085 1.00 53.38  ? 27  PHE B CD1 1 
ATOM   2735 C  CD2 . PHE B  1  14  ? 2.535   -10.737 37.334 1.00 54.00  ? 27  PHE B CD2 1 
ATOM   2736 C  CE1 . PHE B  1  14  ? 1.593   -12.745 35.686 1.00 53.25  ? 27  PHE B CE1 1 
ATOM   2737 C  CE2 . PHE B  1  14  ? 3.377   -11.767 36.930 1.00 50.86  ? 27  PHE B CE2 1 
ATOM   2738 C  CZ  . PHE B  1  14  ? 2.906   -12.764 36.104 1.00 50.53  ? 27  PHE B CZ  1 
ATOM   2739 N  N   . THR B  1  15  ? -0.309  -11.938 39.863 1.00 46.90  ? 28  THR B N   1 
ATOM   2740 C  CA  . THR B  1  15  ? 0.138   -12.620 41.071 1.00 50.06  ? 28  THR B CA  1 
ATOM   2741 C  C   . THR B  1  15  ? 1.130   -13.737 40.743 1.00 51.77  ? 28  THR B C   1 
ATOM   2742 O  O   . THR B  1  15  ? 1.429   -14.547 41.623 1.00 49.78  ? 28  THR B O   1 
ATOM   2743 C  CB  . THR B  1  15  ? -1.048  -13.202 41.841 1.00 48.68  ? 28  THR B CB  1 
ATOM   2744 O  OG1 . THR B  1  15  ? -1.538  -14.261 41.033 1.00 47.15  ? 28  THR B OG1 1 
ATOM   2745 C  CG2 . THR B  1  15  ? -2.164  -12.208 42.090 1.00 52.13  ? 28  THR B CG2 1 
ATOM   2746 N  N   . GLY B  1  16  ? 1.617   -13.797 39.492 1.00 50.28  ? 29  GLY B N   1 
ATOM   2747 C  CA  . GLY B  1  16  ? 2.590   -14.809 39.103 1.00 51.91  ? 29  GLY B CA  1 
ATOM   2748 C  C   . GLY B  1  16  ? 4.010   -14.359 39.437 1.00 52.13  ? 29  GLY B C   1 
ATOM   2749 O  O   . GLY B  1  16  ? 4.193   -13.283 40.000 1.00 48.33  ? 29  GLY B O   1 
ATOM   2750 N  N   . THR B  1  17  ? 5.011   -15.183 39.084 1.00 50.28  ? 30  THR B N   1 
ATOM   2751 C  CA  . THR B  1  17  ? 6.399   -14.825 39.327 1.00 46.59  ? 30  THR B CA  1 
ATOM   2752 C  C   . THR B  1  17  ? 6.807   -13.752 38.329 1.00 45.26  ? 30  THR B C   1 
ATOM   2753 O  O   . THR B  1  17  ? 6.223   -13.624 37.260 1.00 46.74  ? 30  THR B O   1 
ATOM   2754 C  CB  . THR B  1  17  ? 7.328   -16.033 39.229 1.00 50.63  ? 30  THR B CB  1 
ATOM   2755 O  OG1 . THR B  1  17  ? 8.576   -15.550 39.723 1.00 47.29  ? 30  THR B OG1 1 
ATOM   2756 C  CG2 . THR B  1  17  ? 7.487   -16.547 37.810 1.00 51.70  ? 30  THR B CG2 1 
ATOM   2757 N  N   . LYS B  1  18  ? 7.824   -12.984 38.709 1.00 46.48  ? 31  LYS B N   1 
ATOM   2758 C  CA  . LYS B  1  18  ? 8.457   -12.030 37.815 1.00 46.86  ? 31  LYS B CA  1 
ATOM   2759 C  C   . LYS B  1  18  ? 9.809   -11.645 38.406 1.00 44.81  ? 31  LYS B C   1 
ATOM   2760 O  O   . LYS B  1  18  ? 10.059  -11.858 39.599 1.00 44.63  ? 31  LYS B O   1 
ATOM   2761 C  CB  . LYS B  1  18  ? 7.588   -10.787 37.587 1.00 48.76  ? 31  LYS B CB  1 
ATOM   2762 C  CG  . LYS B  1  18  ? 7.379   -9.901  38.803 1.00 52.89  ? 31  LYS B CG  1 
ATOM   2763 C  CD  . LYS B  1  18  ? 6.612   -8.621  38.510 1.00 58.99  ? 31  LYS B CD  1 
ATOM   2764 C  CE  . LYS B  1  18  ? 7.100   -7.480  39.337 1.00 66.36  ? 31  LYS B CE  1 
ATOM   2765 N  NZ  . LYS B  1  18  ? 6.074   -6.445  39.499 1.00 71.10  ? 31  LYS B NZ  1 
ATOM   2766 N  N   . LEU B  1  19  ? 10.662  -11.081 37.550 1.00 44.56  ? 32  LEU B N   1 
ATOM   2767 C  CA  . LEU B  1  19  ? 11.920  -10.507 37.987 1.00 46.10  ? 32  LEU B CA  1 
ATOM   2768 C  C   . LEU B  1  19  ? 11.625  -9.255  38.809 1.00 43.35  ? 32  LEU B C   1 
ATOM   2769 O  O   . LEU B  1  19  ? 10.997  -8.331  38.303 1.00 43.40  ? 32  LEU B O   1 
ATOM   2770 C  CB  . LEU B  1  19  ? 12.775  -10.174 36.766 1.00 45.61  ? 32  LEU B CB  1 
ATOM   2771 C  CG  . LEU B  1  19  ? 14.087  -9.440  37.064 1.00 47.91  ? 32  LEU B CG  1 
ATOM   2772 C  CD1 . LEU B  1  19  ? 15.025  -10.317 37.851 1.00 45.28  ? 32  LEU B CD1 1 
ATOM   2773 C  CD2 . LEU B  1  19  ? 14.750  -8.958  35.779 1.00 51.66  ? 32  LEU B CD2 1 
ATOM   2774 N  N   . VAL B  1  20  ? 12.083  -9.221  40.071 1.00 40.73  ? 33  VAL B N   1 
ATOM   2775 C  CA  . VAL B  1  20  ? 11.858  -8.050  40.902 1.00 38.23  ? 33  VAL B CA  1 
ATOM   2776 C  C   . VAL B  1  20  ? 13.154  -7.267  41.081 1.00 39.34  ? 33  VAL B C   1 
ATOM   2777 O  O   . VAL B  1  20  ? 13.101  -6.062  41.325 1.00 37.09  ? 33  VAL B O   1 
ATOM   2778 C  CB  . VAL B  1  20  ? 11.200  -8.380  42.252 1.00 42.44  ? 33  VAL B CB  1 
ATOM   2779 C  CG1 . VAL B  1  20  ? 9.829   -9.023  42.046 1.00 43.10  ? 33  VAL B CG1 1 
ATOM   2780 C  CG2 . VAL B  1  20  ? 12.078  -9.240  43.148 1.00 43.09  ? 33  VAL B CG2 1 
ATOM   2781 N  N   . ASN B  1  21  ? 14.304  -7.949  40.952 1.00 39.14  ? 34  ASN B N   1 
ATOM   2782 C  CA  . ASN B  1  21  ? 15.597  -7.283  40.963 1.00 41.01  ? 34  ASN B CA  1 
ATOM   2783 C  C   . ASN B  1  21  ? 15.919  -6.842  39.535 1.00 44.92  ? 34  ASN B C   1 
ATOM   2784 O  O   . ASN B  1  21  ? 16.747  -7.458  38.867 1.00 44.65  ? 34  ASN B O   1 
ATOM   2785 C  CB  . ASN B  1  21  ? 16.671  -8.193  41.546 1.00 40.10  ? 34  ASN B CB  1 
ATOM   2786 C  CG  . ASN B  1  21  ? 18.006  -7.508  41.730 1.00 38.64  ? 34  ASN B CG  1 
ATOM   2787 O  OD1 . ASN B  1  21  ? 18.146  -6.303  41.507 1.00 37.19  ? 34  ASN B OD1 1 
ATOM   2788 N  ND2 . ASN B  1  21  ? 19.004  -8.262  42.159 1.00 41.26  ? 34  ASN B ND2 1 
ATOM   2789 N  N   . ASP B  1  22  ? 15.255  -5.771  39.085 1.00 43.17  ? 35  ASP B N   1 
ATOM   2790 C  CA  . ASP B  1  22  ? 15.248  -5.375  37.684 1.00 45.45  ? 35  ASP B CA  1 
ATOM   2791 C  C   . ASP B  1  22  ? 15.870  -3.991  37.558 1.00 46.72  ? 35  ASP B C   1 
ATOM   2792 O  O   . ASP B  1  22  ? 16.308  -3.411  38.553 1.00 41.00  ? 35  ASP B O   1 
ATOM   2793 C  CB  . ASP B  1  22  ? 13.836  -5.443  37.107 1.00 48.00  ? 35  ASP B CB  1 
ATOM   2794 C  CG  . ASP B  1  22  ? 12.799  -4.546  37.773 1.00 47.42  ? 35  ASP B CG  1 
ATOM   2795 O  OD1 . ASP B  1  22  ? 13.171  -3.821  38.726 1.00 42.23  ? 35  ASP B OD1 1 
ATOM   2796 O  OD2 . ASP B  1  22  ? 11.631  -4.554  37.313 1.00 49.20  ? 35  ASP B OD2 1 
ATOM   2797 N  N   . ALA B  1  23  ? 15.866  -3.457  36.328 1.00 52.02  ? 36  ALA B N   1 
ATOM   2798 C  CA  . ALA B  1  23  ? 16.608  -2.248  36.009 1.00 53.91  ? 36  ALA B CA  1 
ATOM   2799 C  C   . ALA B  1  23  ? 16.041  -1.051  36.770 1.00 47.44  ? 36  ALA B C   1 
ATOM   2800 O  O   . ALA B  1  23  ? 16.779  -0.159  37.182 1.00 44.92  ? 36  ALA B O   1 
ATOM   2801 C  CB  . ALA B  1  23  ? 16.577  -2.016  34.510 1.00 58.40  ? 36  ALA B CB  1 
ATOM   2802 N  N   . ASP B  1  24  ? 14.717  -1.054  36.960 1.00 46.73  ? 37  ASP B N   1 
ATOM   2803 C  CA  . ASP B  1  24  ? 14.047  0.062   37.593 1.00 47.40  ? 37  ASP B CA  1 
ATOM   2804 C  C   . ASP B  1  24  ? 14.209  0.052   39.111 1.00 45.02  ? 37  ASP B C   1 
ATOM   2805 O  O   . ASP B  1  24  ? 13.907  1.057   39.744 1.00 47.15  ? 37  ASP B O   1 
ATOM   2806 C  CB  . ASP B  1  24  ? 12.574  0.103   37.226 1.00 53.78  ? 37  ASP B CB  1 
ATOM   2807 C  CG  . ASP B  1  24  ? 11.965  1.491   37.315 1.00 52.18  ? 37  ASP B CG  1 
ATOM   2808 O  OD1 . ASP B  1  24  ? 12.603  2.441   36.802 1.00 55.47  ? 37  ASP B OD1 1 
ATOM   2809 O  OD2 . ASP B  1  24  ? 10.863  1.595   37.881 1.00 62.77  ? 37  ASP B OD2 1 
ATOM   2810 N  N   . HIS B  1  25  ? 14.666  -1.074  39.686 1.00 42.76  ? 38  HIS B N   1 
ATOM   2811 C  CA  . HIS B  1  25  ? 14.768  -1.228  41.130 1.00 39.64  ? 38  HIS B CA  1 
ATOM   2812 C  C   . HIS B  1  25  ? 16.184  -1.662  41.513 1.00 41.90  ? 38  HIS B C   1 
ATOM   2813 O  O   . HIS B  1  25  ? 16.391  -2.751  42.054 1.00 41.37  ? 38  HIS B O   1 
ATOM   2814 C  CB  . HIS B  1  25  ? 13.678  -2.181  41.628 1.00 36.63  ? 38  HIS B CB  1 
ATOM   2815 C  CG  . HIS B  1  25  ? 12.291  -1.669  41.390 1.00 38.58  ? 38  HIS B CG  1 
ATOM   2816 N  ND1 . HIS B  1  25  ? 11.530  -2.048  40.298 1.00 39.84  ? 38  HIS B ND1 1 
ATOM   2817 C  CD2 . HIS B  1  25  ? 11.532  -0.815  42.095 1.00 40.37  ? 38  HIS B CD2 1 
ATOM   2818 C  CE1 . HIS B  1  25  ? 10.348  -1.437  40.354 1.00 42.56  ? 38  HIS B CE1 1 
ATOM   2819 N  NE2 . HIS B  1  25  ? 10.323  -0.676  41.436 1.00 38.78  ? 38  HIS B NE2 1 
ATOM   2820 N  N   . PRO B  1  26  ? 17.208  -0.823  41.246 1.00 43.73  ? 39  PRO B N   1 
ATOM   2821 C  CA  . PRO B  1  26  ? 18.589  -1.159  41.607 1.00 43.79  ? 39  PRO B CA  1 
ATOM   2822 C  C   . PRO B  1  26  ? 18.858  -1.027  43.100 1.00 42.72  ? 39  PRO B C   1 
ATOM   2823 O  O   . PRO B  1  26  ? 18.372  -0.100  43.737 1.00 40.02  ? 39  PRO B O   1 
ATOM   2824 C  CB  . PRO B  1  26  ? 19.384  -0.124  40.803 1.00 45.04  ? 39  PRO B CB  1 
ATOM   2825 C  CG  . PRO B  1  26  ? 18.492  1.093   40.820 1.00 44.14  ? 39  PRO B CG  1 
ATOM   2826 C  CD  . PRO B  1  26  ? 17.101  0.501   40.612 1.00 43.15  ? 39  PRO B CD  1 
ATOM   2827 N  N   . TRP B  1  27  ? 19.668  -1.941  43.639 1.00 44.54  ? 40  TRP B N   1 
ATOM   2828 C  CA  . TRP B  1  27  ? 20.219  -1.755  44.971 1.00 39.86  ? 40  TRP B CA  1 
ATOM   2829 C  C   . TRP B  1  27  ? 21.062  -0.486  44.974 1.00 37.47  ? 40  TRP B C   1 
ATOM   2830 O  O   . TRP B  1  27  ? 21.748  -0.207  43.993 1.00 38.30  ? 40  TRP B O   1 
ATOM   2831 C  CB  . TRP B  1  27  ? 21.050  -2.966  45.408 1.00 37.59  ? 40  TRP B CB  1 
ATOM   2832 C  CG  . TRP B  1  27  ? 21.603  -2.860  46.803 1.00 36.81  ? 40  TRP B CG  1 
ATOM   2833 C  CD1 . TRP B  1  27  ? 21.028  -3.317  47.954 1.00 37.31  ? 40  TRP B CD1 1 
ATOM   2834 C  CD2 . TRP B  1  27  ? 22.861  -2.263  47.191 1.00 36.89  ? 40  TRP B CD2 1 
ATOM   2835 N  NE1 . TRP B  1  27  ? 21.850  -3.064  49.025 1.00 37.22  ? 40  TRP B NE1 1 
ATOM   2836 C  CE2 . TRP B  1  27  ? 22.975  -2.412  48.590 1.00 34.66  ? 40  TRP B CE2 1 
ATOM   2837 C  CE3 . TRP B  1  27  ? 23.892  -1.613  46.498 1.00 39.13  ? 40  TRP B CE3 1 
ATOM   2838 C  CZ2 . TRP B  1  27  ? 24.072  -1.922  49.297 1.00 35.49  ? 40  TRP B CZ2 1 
ATOM   2839 C  CZ3 . TRP B  1  27  ? 24.982  -1.142  47.199 1.00 34.83  ? 40  TRP B CZ3 1 
ATOM   2840 C  CH2 . TRP B  1  27  ? 25.065  -1.293  48.579 1.00 35.93  ? 40  TRP B CH2 1 
ATOM   2841 N  N   . GLN B  1  28  ? 20.979  0.269   46.076 1.00 36.42  ? 41  GLN B N   1 
ATOM   2842 C  CA  . GLN B  1  28  ? 21.794  1.453   46.275 1.00 38.64  ? 41  GLN B CA  1 
ATOM   2843 C  C   . GLN B  1  28  ? 22.193  1.535   47.740 1.00 38.04  ? 41  GLN B C   1 
ATOM   2844 O  O   . GLN B  1  28  ? 21.418  1.174   48.621 1.00 39.84  ? 41  GLN B O   1 
ATOM   2845 C  CB  . GLN B  1  28  ? 21.091  2.737   45.839 1.00 41.63  ? 41  GLN B CB  1 
ATOM   2846 C  CG  . GLN B  1  28  ? 20.867  2.824   44.332 1.00 43.11  ? 41  GLN B CG  1 
ATOM   2847 C  CD  . GLN B  1  28  ? 20.052  4.034   43.917 1.00 47.07  ? 41  GLN B CD  1 
ATOM   2848 O  OE1 . GLN B  1  28  ? 19.693  4.895   44.729 1.00 48.37  ? 41  GLN B OE1 1 
ATOM   2849 N  NE2 . GLN B  1  28  ? 19.744  4.112   42.634 1.00 46.79  ? 41  GLN B NE2 1 
ATOM   2850 N  N   . PRO B  1  29  ? 23.406  2.037   48.042 1.00 37.58  ? 42  PRO B N   1 
ATOM   2851 C  CA  . PRO B  1  29  ? 23.839  2.192   49.428 1.00 41.03  ? 42  PRO B CA  1 
ATOM   2852 C  C   . PRO B  1  29  ? 23.023  3.263   50.157 1.00 40.63  ? 42  PRO B C   1 
ATOM   2853 O  O   . PRO B  1  29  ? 22.346  4.080   49.549 1.00 40.46  ? 42  PRO B O   1 
ATOM   2854 C  CB  . PRO B  1  29  ? 25.332  2.554   49.343 1.00 41.01  ? 42  PRO B CB  1 
ATOM   2855 C  CG  . PRO B  1  29  ? 25.539  3.026   47.929 1.00 40.69  ? 42  PRO B CG  1 
ATOM   2856 C  CD  . PRO B  1  29  ? 24.390  2.535   47.070 1.00 39.45  ? 42  PRO B CD  1 
ATOM   2857 N  N   . LEU B  1  30  ? 23.094  3.223   51.484 1.00 44.04  ? 43  LEU B N   1 
ATOM   2858 C  CA  . LEU B  1  30  ? 22.408  4.167   52.344 1.00 48.53  ? 43  LEU B CA  1 
ATOM   2859 C  C   . LEU B  1  30  ? 23.017  5.550   52.149 1.00 48.69  ? 43  LEU B C   1 
ATOM   2860 O  O   . LEU B  1  30  ? 24.231  5.686   52.001 1.00 49.00  ? 43  LEU B O   1 
ATOM   2861 C  CB  . LEU B  1  30  ? 22.529  3.703   53.796 1.00 49.74  ? 43  LEU B CB  1 
ATOM   2862 C  CG  . LEU B  1  30  ? 21.919  2.331   54.111 1.00 51.01  ? 43  LEU B CG  1 
ATOM   2863 C  CD1 . LEU B  1  30  ? 22.056  2.028   55.589 1.00 49.90  ? 43  LEU B CD1 1 
ATOM   2864 C  CD2 . LEU B  1  30  ? 20.458  2.219   53.662 1.00 52.18  ? 43  LEU B CD2 1 
ATOM   2865 N  N   . ARG B  1  31  ? 22.147  6.561   52.128 1.00 49.02  ? 44  ARG B N   1 
ATOM   2866 C  CA  . ARG B  1  31  ? 22.550  7.950   52.269 1.00 51.58  ? 44  ARG B CA  1 
ATOM   2867 C  C   . ARG B  1  31  ? 22.276  8.416   53.698 1.00 52.11  ? 44  ARG B C   1 
ATOM   2868 O  O   . ARG B  1  31  ? 21.572  7.752   54.456 1.00 49.95  ? 44  ARG B O   1 
ATOM   2869 C  CB  . ARG B  1  31  ? 21.747  8.850   51.328 1.00 52.93  ? 44  ARG B CB  1 
ATOM   2870 C  CG  . ARG B  1  31  ? 21.798  8.507   49.846 1.00 56.45  ? 44  ARG B CG  1 
ATOM   2871 C  CD  . ARG B  1  31  ? 20.578  9.072   49.119 1.00 64.76  ? 44  ARG B CD  1 
ATOM   2872 N  NE  . ARG B  1  31  ? 19.333  8.669   49.793 1.00 71.69  ? 44  ARG B NE  1 
ATOM   2873 C  CZ  . ARG B  1  31  ? 18.080  8.864   49.397 1.00 73.27  ? 44  ARG B CZ  1 
ATOM   2874 N  NH1 . ARG B  1  31  ? 17.812  9.243   48.156 1.00 83.47  ? 44  ARG B NH1 1 
ATOM   2875 N  NH2 . ARG B  1  31  ? 17.090  8.601   50.234 1.00 64.95  ? 44  ARG B NH2 1 
ATOM   2876 N  N   . GLU B  1  32  ? 22.816  9.587   54.039 1.00 57.55  ? 45  GLU B N   1 
ATOM   2877 C  CA  . GLU B  1  32  ? 22.570  10.204  55.333 1.00 59.57  ? 45  GLU B CA  1 
ATOM   2878 C  C   . GLU B  1  32  ? 21.065  10.400  55.520 1.00 56.21  ? 45  GLU B C   1 
ATOM   2879 O  O   . GLU B  1  32  ? 20.377  10.912  54.635 1.00 50.84  ? 45  GLU B O   1 
ATOM   2880 C  CB  . GLU B  1  32  ? 23.292  11.545  55.426 1.00 67.61  ? 45  GLU B CB  1 
ATOM   2881 C  CG  . GLU B  1  32  ? 23.747  11.886  56.841 1.00 76.27  ? 45  GLU B CG  1 
ATOM   2882 C  CD  . GLU B  1  32  ? 24.254  13.311  57.033 1.00 91.34  ? 45  GLU B CD  1 
ATOM   2883 O  OE1 . GLU B  1  32  ? 24.987  13.869  56.173 1.00 90.40  ? 45  GLU B OE1 1 
ATOM   2884 O  OE2 . GLU B  1  32  ? 23.924  13.869  58.103 1.00 102.36 ? 45  GLU B OE2 1 
ATOM   2885 N  N   . GLY B  1  33  ? 20.560  9.961   56.675 1.00 54.05  ? 46  GLY B N   1 
ATOM   2886 C  CA  . GLY B  1  33  ? 19.149  10.104  57.002 1.00 57.01  ? 46  GLY B CA  1 
ATOM   2887 C  C   . GLY B  1  33  ? 18.313  8.873   56.646 1.00 51.39  ? 46  GLY B C   1 
ATOM   2888 O  O   . GLY B  1  33  ? 17.189  8.759   57.119 1.00 58.12  ? 46  GLY B O   1 
ATOM   2889 N  N   . ASP B  1  34  ? 18.831  7.977   55.794 1.00 49.08  ? 47  ASP B N   1 
ATOM   2890 C  CA  . ASP B  1  34  ? 18.102  6.771   55.424 1.00 46.43  ? 47  ASP B CA  1 
ATOM   2891 C  C   . ASP B  1  34  ? 17.974  5.852   56.640 1.00 43.89  ? 47  ASP B C   1 
ATOM   2892 O  O   . ASP B  1  34  ? 18.928  5.666   57.382 1.00 41.41  ? 47  ASP B O   1 
ATOM   2893 C  CB  . ASP B  1  34  ? 18.749  6.047   54.253 1.00 49.40  ? 47  ASP B CB  1 
ATOM   2894 C  CG  . ASP B  1  34  ? 18.636  6.741   52.900 1.00 49.27  ? 47  ASP B CG  1 
ATOM   2895 O  OD1 . ASP B  1  34  ? 17.872  7.718   52.789 1.00 50.24  ? 47  ASP B OD1 1 
ATOM   2896 O  OD2 . ASP B  1  34  ? 19.322  6.294   51.956 1.00 49.87  ? 47  ASP B OD2 1 
ATOM   2897 N  N   . ILE B  1  35  ? 16.771  5.300   56.835 1.00 40.58  ? 48  ILE B N   1 
ATOM   2898 C  CA  . ILE B  1  35  ? 16.432  4.488   57.992 1.00 40.76  ? 48  ILE B CA  1 
ATOM   2899 C  C   . ILE B  1  35  ? 16.277  3.032   57.551 1.00 37.60  ? 48  ILE B C   1 
ATOM   2900 O  O   . ILE B  1  35  ? 15.621  2.742   56.552 1.00 40.63  ? 48  ILE B O   1 
ATOM   2901 C  CB  . ILE B  1  35  ? 15.132  5.011   58.643 1.00 47.75  ? 48  ILE B CB  1 
ATOM   2902 C  CG1 . ILE B  1  35  ? 15.262  6.468   59.112 1.00 50.08  ? 48  ILE B CG1 1 
ATOM   2903 C  CG2 . ILE B  1  35  ? 14.679  4.104   59.787 1.00 48.39  ? 48  ILE B CG2 1 
ATOM   2904 C  CD1 . ILE B  1  35  ? 16.293  6.684   60.209 1.00 49.59  ? 48  ILE B CD1 1 
ATOM   2905 N  N   . ARG B  1  36  ? 16.851  2.118   58.337 1.00 39.51  ? 49  ARG B N   1 
ATOM   2906 C  CA  . ARG B  1  36  ? 16.640  0.688   58.195 1.00 40.31  ? 49  ARG B CA  1 
ATOM   2907 C  C   . ARG B  1  36  ? 16.418  0.128   59.595 1.00 42.67  ? 49  ARG B C   1 
ATOM   2908 O  O   . ARG B  1  36  ? 16.787  0.783   60.568 1.00 41.05  ? 49  ARG B O   1 
ATOM   2909 C  CB  . ARG B  1  36  ? 17.855  0.054   57.506 1.00 39.50  ? 49  ARG B CB  1 
ATOM   2910 C  CG  . ARG B  1  36  ? 18.088  0.541   56.082 1.00 38.31  ? 49  ARG B CG  1 
ATOM   2911 C  CD  . ARG B  1  36  ? 17.032  0.056   55.118 1.00 37.06  ? 49  ARG B CD  1 
ATOM   2912 N  NE  . ARG B  1  36  ? 17.296  0.484   53.739 1.00 36.22  ? 49  ARG B NE  1 
ATOM   2913 C  CZ  . ARG B  1  36  ? 17.045  1.684   53.227 1.00 38.82  ? 49  ARG B CZ  1 
ATOM   2914 N  NH1 . ARG B  1  36  ? 16.462  2.632   53.946 1.00 41.09  ? 49  ARG B NH1 1 
ATOM   2915 N  NH2 . ARG B  1  36  ? 17.361  1.927   51.970 1.00 40.20  ? 49  ARG B NH2 1 
ATOM   2916 N  N   . GLY B  1  37  ? 15.820  -1.070  59.689 1.00 40.17  ? 50  GLY B N   1 
ATOM   2917 C  CA  . GLY B  1  37  ? 15.423  -1.593  60.982 1.00 41.59  ? 50  GLY B CA  1 
ATOM   2918 C  C   . GLY B  1  37  ? 15.511  -3.113  61.062 1.00 40.41  ? 50  GLY B C   1 
ATOM   2919 O  O   . GLY B  1  37  ? 16.345  -3.739  60.406 1.00 36.67  ? 50  GLY B O   1 
ATOM   2920 N  N   . PRO B  1  38  ? 14.636  -3.749  61.875 1.00 38.27  ? 51  PRO B N   1 
ATOM   2921 C  CA  . PRO B  1  38  ? 14.747  -5.179  62.174 1.00 36.81  ? 51  PRO B CA  1 
ATOM   2922 C  C   . PRO B  1  38  ? 14.159  -6.123  61.126 1.00 36.25  ? 51  PRO B C   1 
ATOM   2923 O  O   . PRO B  1  38  ? 14.256  -7.334  61.279 1.00 36.52  ? 51  PRO B O   1 
ATOM   2924 C  CB  . PRO B  1  38  ? 13.952  -5.242  63.472 1.00 35.52  ? 51  PRO B CB  1 
ATOM   2925 C  CG  . PRO B  1  38  ? 12.810  -4.294  63.242 1.00 39.76  ? 51  PRO B CG  1 
ATOM   2926 C  CD  . PRO B  1  38  ? 13.461  -3.133  62.509 1.00 40.44  ? 51  PRO B CD  1 
ATOM   2927 N  N   . CYS B  1  39  ? 13.529  -5.562  60.085 1.00 31.98  ? 52  CYS B N   1 
ATOM   2928 C  CA  . CYS B  1  39  ? 12.872  -6.368  59.070 1.00 37.22  ? 52  CYS B CA  1 
ATOM   2929 C  C   . CYS B  1  39  ? 13.703  -6.438  57.791 1.00 34.98  ? 52  CYS B C   1 
ATOM   2930 O  O   . CYS B  1  39  ? 13.822  -5.450  57.057 1.00 31.36  ? 52  CYS B O   1 
ATOM   2931 C  CB  . CYS B  1  39  ? 11.499  -5.838  58.677 1.00 33.76  ? 52  CYS B CB  1 
ATOM   2932 S  SG  . CYS B  1  39  ? 10.720  -6.916  57.456 1.00 41.59  ? 52  CYS B SG  1 
ATOM   2933 N  N   . PRO B  1  40  ? 14.248  -7.627  57.454 1.00 36.81  ? 53  PRO B N   1 
ATOM   2934 C  CA  . PRO B  1  40  ? 15.030  -7.786  56.228 1.00 36.97  ? 53  PRO B CA  1 
ATOM   2935 C  C   . PRO B  1  40  ? 14.182  -7.613  54.971 1.00 35.34  ? 53  PRO B C   1 
ATOM   2936 O  O   . PRO B  1  40  ? 14.691  -7.182  53.942 1.00 35.01  ? 53  PRO B O   1 
ATOM   2937 C  CB  . PRO B  1  40  ? 15.631  -9.194  56.368 1.00 37.75  ? 53  PRO B CB  1 
ATOM   2938 C  CG  . PRO B  1  40  ? 14.680  -9.924  57.285 1.00 38.45  ? 53  PRO B CG  1 
ATOM   2939 C  CD  . PRO B  1  40  ? 14.132  -8.872  58.225 1.00 36.53  ? 53  PRO B CD  1 
ATOM   2940 N  N   . GLY B  1  41  ? 12.876  -7.909  55.071 1.00 35.52  ? 54  GLY B N   1 
ATOM   2941 C  CA  . GLY B  1  41  ? 11.982  -7.742  53.935 1.00 33.02  ? 54  GLY B CA  1 
ATOM   2942 C  C   . GLY B  1  41  ? 11.835  -6.268  53.551 1.00 34.94  ? 54  GLY B C   1 
ATOM   2943 O  O   . GLY B  1  41  ? 12.108  -5.871  52.414 1.00 33.95  ? 54  GLY B O   1 
ATOM   2944 N  N   . LEU B  1  42  ? 11.421  -5.458  54.531 1.00 34.67  ? 55  LEU B N   1 
ATOM   2945 C  CA  . LEU B  1  42  ? 11.237  -4.035  54.318 1.00 34.40  ? 55  LEU B CA  1 
ATOM   2946 C  C   . LEU B  1  42  ? 12.578  -3.377  53.992 1.00 36.42  ? 55  LEU B C   1 
ATOM   2947 O  O   . LEU B  1  42  ? 12.640  -2.515  53.120 1.00 37.86  ? 55  LEU B O   1 
ATOM   2948 C  CB  . LEU B  1  42  ? 10.593  -3.417  55.557 1.00 33.25  ? 55  LEU B CB  1 
ATOM   2949 C  CG  . LEU B  1  42  ? 9.186   -3.920  55.901 1.00 36.47  ? 55  LEU B CG  1 
ATOM   2950 C  CD1 . LEU B  1  42  ? 8.707   -3.198  57.141 1.00 39.01  ? 55  LEU B CD1 1 
ATOM   2951 C  CD2 . LEU B  1  42  ? 8.187   -3.772  54.769 1.00 33.91  ? 55  LEU B CD2 1 
ATOM   2952 N  N   . ASN B  1  43  ? 13.642  -3.781  54.696 1.00 37.04  ? 56  ASN B N   1 
ATOM   2953 C  CA  . ASN B  1  43  ? 14.964  -3.227  54.456 1.00 36.55  ? 56  ASN B CA  1 
ATOM   2954 C  C   . ASN B  1  43  ? 15.358  -3.392  52.988 1.00 35.65  ? 56  ASN B C   1 
ATOM   2955 O  O   . ASN B  1  43  ? 15.827  -2.434  52.379 1.00 35.61  ? 56  ASN B O   1 
ATOM   2956 C  CB  . ASN B  1  43  ? 16.036  -3.866  55.328 1.00 35.58  ? 56  ASN B CB  1 
ATOM   2957 C  CG  . ASN B  1  43  ? 15.967  -3.457  56.779 1.00 37.19  ? 56  ASN B CG  1 
ATOM   2958 O  OD1 . ASN B  1  43  ? 15.301  -2.482  57.146 1.00 38.10  ? 56  ASN B OD1 1 
ATOM   2959 N  ND2 . ASN B  1  43  ? 16.647  -4.207  57.629 1.00 36.70  ? 56  ASN B ND2 1 
ATOM   2960 N  N   . THR B  1  44  ? 15.155  -4.595  52.433 1.00 35.25  ? 57  THR B N   1 
ATOM   2961 C  CA  . THR B  1  44  ? 15.559  -4.888  51.064 1.00 34.56  ? 57  THR B CA  1 
ATOM   2962 C  C   . THR B  1  44  ? 14.685  -4.108  50.078 1.00 34.96  ? 57  THR B C   1 
ATOM   2963 O  O   . THR B  1  44  ? 15.174  -3.621  49.062 1.00 33.39  ? 57  THR B O   1 
ATOM   2964 C  CB  . THR B  1  44  ? 15.469  -6.396  50.825 1.00 34.88  ? 57  THR B CB  1 
ATOM   2965 O  OG1 . THR B  1  44  ? 16.354  -7.044  51.734 1.00 35.67  ? 57  THR B OG1 1 
ATOM   2966 C  CG2 . THR B  1  44  ? 15.869  -6.776  49.413 1.00 35.23  ? 57  THR B CG2 1 
ATOM   2967 N  N   . LEU B  1  45  ? 13.379  -4.003  50.367 1.00 35.43  ? 58  LEU B N   1 
ATOM   2968 C  CA  . LEU B  1  45  ? 12.478  -3.248  49.516 1.00 34.86  ? 58  LEU B CA  1 
ATOM   2969 C  C   . LEU B  1  45  ? 12.901  -1.779  49.459 1.00 37.58  ? 58  LEU B C   1 
ATOM   2970 O  O   . LEU B  1  45  ? 12.880  -1.163  48.392 1.00 37.84  ? 58  LEU B O   1 
ATOM   2971 C  CB  . LEU B  1  45  ? 11.045  -3.431  50.017 1.00 38.60  ? 58  LEU B CB  1 
ATOM   2972 C  CG  . LEU B  1  45  ? 10.457  -4.834  49.834 1.00 37.68  ? 58  LEU B CG  1 
ATOM   2973 C  CD1 . LEU B  1  45  ? 9.148   -5.002  50.595 1.00 40.83  ? 58  LEU B CD1 1 
ATOM   2974 C  CD2 . LEU B  1  45  ? 10.234  -5.133  48.359 1.00 37.54  ? 58  LEU B CD2 1 
ATOM   2975 N  N   . ALA B  1  46  ? 13.304  -1.219  50.601 1.00 38.26  ? 59  ALA B N   1 
ATOM   2976 C  CA  . ALA B  1  46  ? 13.750  0.166   50.636 1.00 40.40  ? 59  ALA B CA  1 
ATOM   2977 C  C   . ALA B  1  46  ? 15.066  0.331   49.869 1.00 41.26  ? 59  ALA B C   1 
ATOM   2978 O  O   . ALA B  1  46  ? 15.224  1.271   49.094 1.00 40.69  ? 59  ALA B O   1 
ATOM   2979 C  CB  . ALA B  1  46  ? 13.891  0.644   52.073 1.00 38.94  ? 59  ALA B CB  1 
ATOM   2980 N  N   . SER B  1  47  ? 16.004  -0.599  50.055 1.00 39.78  ? 60  SER B N   1 
ATOM   2981 C  CA  . SER B  1  47  ? 17.311  -0.477  49.415 1.00 39.61  ? 60  SER B CA  1 
ATOM   2982 C  C   . SER B  1  47  ? 17.253  -0.746  47.905 1.00 40.58  ? 60  SER B C   1 
ATOM   2983 O  O   . SER B  1  47  ? 18.250  -0.522  47.225 1.00 34.62  ? 60  SER B O   1 
ATOM   2984 C  CB  . SER B  1  47  ? 18.334  -1.345  50.103 1.00 37.27  ? 60  SER B CB  1 
ATOM   2985 O  OG  . SER B  1  47  ? 18.748  -0.741  51.320 1.00 33.52  ? 60  SER B OG  1 
ATOM   2986 N  N   . HIS B  1  48  ? 16.111  -1.241  47.391 1.00 38.78  ? 61  HIS B N   1 
ATOM   2987 C  CA  . HIS B  1  48  ? 15.921  -1.432  45.959 1.00 42.03  ? 61  HIS B CA  1 
ATOM   2988 C  C   . HIS B  1  48  ? 14.898  -0.444  45.386 1.00 42.40  ? 61  HIS B C   1 
ATOM   2989 O  O   . HIS B  1  48  ? 14.599  -0.487  44.199 1.00 37.64  ? 61  HIS B O   1 
ATOM   2990 C  CB  . HIS B  1  48  ? 15.475  -2.867  45.650 1.00 41.13  ? 61  HIS B CB  1 
ATOM   2991 C  CG  . HIS B  1  48  ? 16.597  -3.840  45.580 1.00 41.01  ? 61  HIS B CG  1 
ATOM   2992 N  ND1 . HIS B  1  48  ? 17.214  -4.149  44.391 1.00 40.36  ? 61  HIS B ND1 1 
ATOM   2993 C  CD2 . HIS B  1  48  ? 17.218  -4.564  46.529 1.00 39.17  ? 61  HIS B CD2 1 
ATOM   2994 C  CE1 . HIS B  1  48  ? 18.176  -5.033  44.632 1.00 42.57  ? 61  HIS B CE1 1 
ATOM   2995 N  NE2 . HIS B  1  48  ? 18.197  -5.292  45.922 1.00 36.72  ? 61  HIS B NE2 1 
ATOM   2996 N  N   . GLY B  1  49  ? 14.332  0.420   46.235 1.00 42.39  ? 62  GLY B N   1 
ATOM   2997 C  CA  . GLY B  1  49  ? 13.455  1.482   45.775 1.00 41.45  ? 62  GLY B CA  1 
ATOM   2998 C  C   . GLY B  1  49  ? 12.006  1.035   45.568 1.00 41.73  ? 62  GLY B C   1 
ATOM   2999 O  O   . GLY B  1  49  ? 11.225  1.786   44.991 1.00 43.07  ? 62  GLY B O   1 
ATOM   3000 N  N   . TYR B  1  50  ? 11.634  -0.164  46.044 1.00 38.27  ? 63  TYR B N   1 
ATOM   3001 C  CA  . TYR B  1  50  ? 10.230  -0.547  46.080 1.00 42.61  ? 63  TYR B CA  1 
ATOM   3002 C  C   . TYR B  1  50  ? 9.482   0.311   47.100 1.00 42.72  ? 63  TYR B C   1 
ATOM   3003 O  O   . TYR B  1  50  ? 8.311   0.620   46.901 1.00 45.21  ? 63  TYR B O   1 
ATOM   3004 C  CB  . TYR B  1  50  ? 10.059  -2.043  46.356 1.00 40.96  ? 63  TYR B CB  1 
ATOM   3005 C  CG  . TYR B  1  50  ? 10.255  -2.883  45.101 1.00 40.41  ? 63  TYR B CG  1 
ATOM   3006 C  CD1 . TYR B  1  50  ? 9.219   -3.063  44.190 1.00 41.66  ? 63  TYR B CD1 1 
ATOM   3007 C  CD2 . TYR B  1  50  ? 11.481  -3.478  44.821 1.00 37.66  ? 63  TYR B CD2 1 
ATOM   3008 C  CE1 . TYR B  1  50  ? 9.392   -3.817  43.039 1.00 44.40  ? 63  TYR B CE1 1 
ATOM   3009 C  CE2 . TYR B  1  50  ? 11.667  -4.233  43.676 1.00 37.98  ? 63  TYR B CE2 1 
ATOM   3010 C  CZ  . TYR B  1  50  ? 10.621  -4.402  42.782 1.00 42.84  ? 63  TYR B CZ  1 
ATOM   3011 O  OH  . TYR B  1  50  ? 10.798  -5.142  41.650 1.00 42.04  ? 63  TYR B OH  1 
ATOM   3012 N  N   . LEU B  1  51  ? 10.167  0.640   48.202 1.00 42.61  ? 64  LEU B N   1 
ATOM   3013 C  CA  . LEU B  1  51  ? 9.732   1.641   49.162 1.00 44.88  ? 64  LEU B CA  1 
ATOM   3014 C  C   . LEU B  1  51  ? 10.589  2.883   48.969 1.00 47.35  ? 64  LEU B C   1 
ATOM   3015 O  O   . LEU B  1  51  ? 11.678  2.790   48.404 1.00 47.61  ? 64  LEU B O   1 
ATOM   3016 C  CB  . LEU B  1  51  ? 9.925   1.115   50.585 1.00 45.55  ? 64  LEU B CB  1 
ATOM   3017 C  CG  . LEU B  1  51  ? 8.980   0.002   51.038 1.00 46.46  ? 64  LEU B CG  1 
ATOM   3018 C  CD1 . LEU B  1  51  ? 9.428   -0.580  52.359 1.00 47.59  ? 64  LEU B CD1 1 
ATOM   3019 C  CD2 . LEU B  1  51  ? 7.569   0.539   51.138 1.00 49.58  ? 64  LEU B CD2 1 
ATOM   3020 N  N   . PRO B  1  52  ? 10.184  4.056   49.506 1.00 43.31  ? 65  PRO B N   1 
ATOM   3021 C  CA  . PRO B  1  52  ? 11.095  5.193   49.613 1.00 43.50  ? 65  PRO B CA  1 
ATOM   3022 C  C   . PRO B  1  52  ? 12.420  4.735   50.217 1.00 43.76  ? 65  PRO B C   1 
ATOM   3023 O  O   . PRO B  1  52  ? 12.441  4.013   51.211 1.00 42.58  ? 65  PRO B O   1 
ATOM   3024 C  CB  . PRO B  1  52  ? 10.339  6.175   50.505 1.00 44.64  ? 65  PRO B CB  1 
ATOM   3025 C  CG  . PRO B  1  52  ? 8.879   5.846   50.257 1.00 43.75  ? 65  PRO B CG  1 
ATOM   3026 C  CD  . PRO B  1  52  ? 8.849   4.342   50.051 1.00 44.48  ? 65  PRO B CD  1 
ATOM   3027 N  N   . ARG B  1  53  ? 13.524  5.145   49.589 1.00 41.55  ? 66  ARG B N   1 
ATOM   3028 C  CA  . ARG B  1  53  ? 14.854  4.718   49.988 1.00 42.14  ? 66  ARG B CA  1 
ATOM   3029 C  C   . ARG B  1  53  ? 15.237  5.223   51.371 1.00 41.80  ? 66  ARG B C   1 
ATOM   3030 O  O   . ARG B  1  53  ? 16.191  4.713   51.960 1.00 43.27  ? 66  ARG B O   1 
ATOM   3031 C  CB  . ARG B  1  53  ? 15.890  5.156   48.951 1.00 47.57  ? 66  ARG B CB  1 
ATOM   3032 C  CG  . ARG B  1  53  ? 15.663  4.449   47.624 1.00 47.15  ? 66  ARG B CG  1 
ATOM   3033 C  CD  . ARG B  1  53  ? 16.807  4.666   46.668 1.00 47.48  ? 66  ARG B CD  1 
ATOM   3034 N  NE  . ARG B  1  53  ? 16.506  3.937   45.431 1.00 45.52  ? 66  ARG B NE  1 
ATOM   3035 C  CZ  . ARG B  1  53  ? 16.918  2.713   45.131 1.00 40.63  ? 66  ARG B CZ  1 
ATOM   3036 N  NH1 . ARG B  1  53  ? 17.628  1.997   45.990 1.00 37.90  ? 66  ARG B NH1 1 
ATOM   3037 N  NH2 . ARG B  1  53  ? 16.604  2.204   43.959 1.00 39.19  ? 66  ARG B NH2 1 
ATOM   3038 N  N   . ASP B  1  54  ? 14.485  6.189   51.911 1.00 44.10  ? 67  ASP B N   1 
ATOM   3039 C  CA  . ASP B  1  54  ? 14.797  6.715   53.233 1.00 41.81  ? 67  ASP B CA  1 
ATOM   3040 C  C   . ASP B  1  54  ? 14.169  5.850   54.325 1.00 42.19  ? 67  ASP B C   1 
ATOM   3041 O  O   . ASP B  1  54  ? 14.377  6.116   55.504 1.00 38.32  ? 67  ASP B O   1 
ATOM   3042 C  CB  . ASP B  1  54  ? 14.437  8.184   53.371 1.00 43.52  ? 67  ASP B CB  1 
ATOM   3043 C  CG  . ASP B  1  54  ? 12.961  8.517   53.246 1.00 44.74  ? 67  ASP B CG  1 
ATOM   3044 O  OD1 . ASP B  1  54  ? 12.163  7.577   53.053 1.00 43.19  ? 67  ASP B OD1 1 
ATOM   3045 O  OD2 . ASP B  1  54  ? 12.626  9.712   53.346 1.00 50.93  ? 67  ASP B OD2 1 
ATOM   3046 N  N   . GLY B  1  55  ? 13.407  4.815   53.939 1.00 40.67  ? 68  GLY B N   1 
ATOM   3047 C  CA  . GLY B  1  55  ? 12.868  3.869   54.905 1.00 42.52  ? 68  GLY B CA  1 
ATOM   3048 C  C   . GLY B  1  55  ? 11.683  4.434   55.691 1.00 44.02  ? 68  GLY B C   1 
ATOM   3049 O  O   . GLY B  1  55  ? 11.360  3.927   56.767 1.00 40.18  ? 68  GLY B O   1 
ATOM   3050 N  N   . VAL B  1  56  ? 11.032  5.469   55.144 1.00 44.67  ? 69  VAL B N   1 
ATOM   3051 C  CA  . VAL B  1  56  ? 9.814   6.010   55.725 1.00 43.97  ? 69  VAL B CA  1 
ATOM   3052 C  C   . VAL B  1  56  ? 8.736   5.966   54.652 1.00 43.65  ? 69  VAL B C   1 
ATOM   3053 O  O   . VAL B  1  56  ? 8.939   6.449   53.546 1.00 50.77  ? 69  VAL B O   1 
ATOM   3054 C  CB  . VAL B  1  56  ? 10.015  7.433   56.274 1.00 47.73  ? 69  VAL B CB  1 
ATOM   3055 C  CG1 . VAL B  1  56  ? 8.707   8.068   56.731 1.00 48.71  ? 69  VAL B CG1 1 
ATOM   3056 C  CG2 . VAL B  1  56  ? 11.035  7.445   57.403 1.00 46.96  ? 69  VAL B CG2 1 
ATOM   3057 N  N   . ALA B  1  57  ? 7.576   5.404   54.997 1.00 41.78  ? 70  ALA B N   1 
ATOM   3058 C  CA  . ALA B  1  57  ? 6.565   5.101   54.000 1.00 44.37  ? 70  ALA B CA  1 
ATOM   3059 C  C   . ALA B  1  57  ? 5.169   5.125   54.615 1.00 43.77  ? 70  ALA B C   1 
ATOM   3060 O  O   . ALA B  1  57  ? 5.019   4.992   55.831 1.00 46.52  ? 70  ALA B O   1 
ATOM   3061 C  CB  . ALA B  1  57  ? 6.855   3.742   53.405 1.00 45.65  ? 70  ALA B CB  1 
ATOM   3062 N  N   . THR B  1  58  ? 4.161   5.247   53.745 1.00 42.97  ? 71  THR B N   1 
ATOM   3063 C  CA  . THR B  1  58  ? 2.774   5.111   54.153 1.00 42.34  ? 71  THR B CA  1 
ATOM   3064 C  C   . THR B  1  58  ? 2.456   3.624   54.271 1.00 43.36  ? 71  THR B C   1 
ATOM   3065 O  O   . THR B  1  58  ? 3.141   2.785   53.684 1.00 42.83  ? 71  THR B O   1 
ATOM   3066 C  CB  . THR B  1  58  ? 1.822   5.796   53.169 1.00 41.41  ? 71  THR B CB  1 
ATOM   3067 O  OG1 . THR B  1  58  ? 1.838   5.029   51.971 1.00 46.19  ? 71  THR B OG1 1 
ATOM   3068 C  CG2 . THR B  1  58  ? 2.196   7.232   52.866 1.00 44.45  ? 71  THR B CG2 1 
ATOM   3069 N  N   . PRO B  1  59  ? 1.406   3.259   55.036 1.00 42.11  ? 72  PRO B N   1 
ATOM   3070 C  CA  . PRO B  1  59  ? 0.906   1.886   55.041 1.00 40.92  ? 72  PRO B CA  1 
ATOM   3071 C  C   . PRO B  1  59  ? 0.618   1.364   53.637 1.00 42.95  ? 72  PRO B C   1 
ATOM   3072 O  O   . PRO B  1  59  ? 0.956   0.229   53.324 1.00 39.61  ? 72  PRO B O   1 
ATOM   3073 C  CB  . PRO B  1  59  ? -0.366  1.981   55.898 1.00 43.20  ? 72  PRO B CB  1 
ATOM   3074 C  CG  . PRO B  1  59  ? -0.088  3.152   56.819 1.00 41.83  ? 72  PRO B CG  1 
ATOM   3075 C  CD  . PRO B  1  59  ? 0.681   4.137   55.967 1.00 41.95  ? 72  PRO B CD  1 
ATOM   3076 N  N   . ALA B  1  60  ? -0.014  2.204   52.806 1.00 43.74  ? 73  ALA B N   1 
ATOM   3077 C  CA  . ALA B  1  60  ? -0.382  1.836   51.450 1.00 42.93  ? 73  ALA B CA  1 
ATOM   3078 C  C   . ALA B  1  60  ? 0.865   1.484   50.652 1.00 41.30  ? 73  ALA B C   1 
ATOM   3079 O  O   . ALA B  1  60  ? 0.853   0.481   49.948 1.00 42.32  ? 73  ALA B O   1 
ATOM   3080 C  CB  . ALA B  1  60  ? -1.149  2.945   50.779 1.00 43.38  ? 73  ALA B CB  1 
ATOM   3081 N  N   . GLN B  1  61  ? 1.927   2.288   50.783 1.00 43.43  ? 74  GLN B N   1 
ATOM   3082 C  CA  . GLN B  1  61  ? 3.177   2.023   50.078 1.00 44.40  ? 74  GLN B CA  1 
ATOM   3083 C  C   . GLN B  1  61  ? 3.780   0.693   50.516 1.00 43.72  ? 74  GLN B C   1 
ATOM   3084 O  O   . GLN B  1  61  ? 4.304   -0.044  49.685 1.00 44.71  ? 74  GLN B O   1 
ATOM   3085 C  CB  . GLN B  1  61  ? 4.218   3.122   50.285 1.00 46.12  ? 74  GLN B CB  1 
ATOM   3086 C  CG  . GLN B  1  61  ? 3.873   4.398   49.531 1.00 50.07  ? 74  GLN B CG  1 
ATOM   3087 C  CD  . GLN B  1  61  ? 4.756   5.566   49.892 1.00 52.54  ? 74  GLN B CD  1 
ATOM   3088 O  OE1 . GLN B  1  61  ? 5.114   5.768   51.056 1.00 54.11  ? 74  GLN B OE1 1 
ATOM   3089 N  NE2 . GLN B  1  61  ? 5.131   6.337   48.882 1.00 55.98  ? 74  GLN B NE2 1 
ATOM   3090 N  N   . ILE B  1  62  ? 3.724   0.407   51.823 1.00 46.40  ? 75  ILE B N   1 
ATOM   3091 C  CA  . ILE B  1  62  ? 4.325   -0.796  52.378 1.00 42.24  ? 75  ILE B CA  1 
ATOM   3092 C  C   . ILE B  1  62  ? 3.605   -2.023  51.827 1.00 42.36  ? 75  ILE B C   1 
ATOM   3093 O  O   . ILE B  1  62  ? 4.245   -2.984  51.402 1.00 41.44  ? 75  ILE B O   1 
ATOM   3094 C  CB  . ILE B  1  62  ? 4.341   -0.736  53.918 1.00 42.92  ? 75  ILE B CB  1 
ATOM   3095 C  CG1 . ILE B  1  62  ? 5.334   0.327   54.393 1.00 41.79  ? 75  ILE B CG1 1 
ATOM   3096 C  CG2 . ILE B  1  62  ? 4.661   -2.105  54.532 1.00 44.28  ? 75  ILE B CG2 1 
ATOM   3097 C  CD1 . ILE B  1  62  ? 5.230   0.695   55.860 1.00 40.57  ? 75  ILE B CD1 1 
ATOM   3098 N  N   . ILE B  1  63  ? 2.271   -1.977  51.800 1.00 38.61  ? 76  ILE B N   1 
ATOM   3099 C  CA  . ILE B  1  63  ? 1.495   -3.110  51.339 1.00 37.81  ? 76  ILE B CA  1 
ATOM   3100 C  C   . ILE B  1  63  ? 1.820   -3.395  49.876 1.00 39.80  ? 76  ILE B C   1 
ATOM   3101 O  O   . ILE B  1  63  ? 2.106   -4.538  49.521 1.00 44.85  ? 76  ILE B O   1 
ATOM   3102 C  CB  . ILE B  1  63  ? -0.007  -2.876  51.565 1.00 40.43  ? 76  ILE B CB  1 
ATOM   3103 C  CG1 . ILE B  1  63  ? -0.344  -2.928  53.055 1.00 43.72  ? 76  ILE B CG1 1 
ATOM   3104 C  CG2 . ILE B  1  63  ? -0.831  -3.885  50.765 1.00 38.07  ? 76  ILE B CG2 1 
ATOM   3105 C  CD1 . ILE B  1  63  ? -1.675  -2.299  53.424 1.00 46.49  ? 76  ILE B CD1 1 
ATOM   3106 N  N   . THR B  1  64  ? 1.793   -2.362  49.030 1.00 40.78  ? 77  THR B N   1 
ATOM   3107 C  CA  A THR B  1  64  ? 2.035   -2.543  47.606 0.50 41.92  ? 77  THR B CA  1 
ATOM   3108 C  CA  B THR B  1  64  ? 2.029   -2.559  47.610 0.50 42.49  ? 77  THR B CA  1 
ATOM   3109 C  C   . THR B  1  64  ? 3.468   -3.039  47.396 1.00 41.46  ? 77  THR B C   1 
ATOM   3110 O  O   . THR B  1  64  ? 3.703   -3.932  46.588 1.00 41.47  ? 77  THR B O   1 
ATOM   3111 C  CB  A THR B  1  64  ? 1.759   -1.250  46.838 0.50 41.89  ? 77  THR B CB  1 
ATOM   3112 C  CB  B THR B  1  64  ? 1.675   -1.302  46.814 0.50 44.11  ? 77  THR B CB  1 
ATOM   3113 O  OG1 A THR B  1  64  ? 2.695   -0.336  47.398 0.50 52.73  ? 77  THR B OG1 1 
ATOM   3114 O  OG1 B THR B  1  64  ? 2.065   -1.553  45.467 0.50 43.15  ? 77  THR B OG1 1 
ATOM   3115 C  CG2 A THR B  1  64  ? 0.352   -0.723  47.028 0.50 38.50  ? 77  THR B CG2 1 
ATOM   3116 C  CG2 B THR B  1  64  ? 2.424   -0.060  47.247 0.50 49.45  ? 77  THR B CG2 1 
ATOM   3117 N  N   . ALA B  1  65  ? 4.426   -2.492  48.158 1.00 40.97  ? 78  ALA B N   1 
ATOM   3118 C  CA  . ALA B  1  65  ? 5.826   -2.887  48.017 1.00 40.05  ? 78  ALA B CA  1 
ATOM   3119 C  C   . ALA B  1  65  ? 6.050   -4.357  48.376 1.00 40.39  ? 78  ALA B C   1 
ATOM   3120 O  O   . ALA B  1  65  ? 6.809   -5.036  47.693 1.00 41.18  ? 78  ALA B O   1 
ATOM   3121 C  CB  . ALA B  1  65  ? 6.732   -2.008  48.850 1.00 38.90  ? 78  ALA B CB  1 
ATOM   3122 N  N   . THR B  1  66  ? 5.414   -4.852  49.445 1.00 39.18  ? 79  THR B N   1 
ATOM   3123 C  CA  . THR B  1  66  ? 5.597   -6.241  49.854 1.00 36.80  ? 79  THR B CA  1 
ATOM   3124 C  C   . THR B  1  66  ? 4.964   -7.180  48.824 1.00 39.71  ? 79  THR B C   1 
ATOM   3125 O  O   . THR B  1  66  ? 5.487   -8.266  48.566 1.00 38.49  ? 79  THR B O   1 
ATOM   3126 C  CB  . THR B  1  66  ? 5.055   -6.479  51.267 1.00 39.06  ? 79  THR B CB  1 
ATOM   3127 O  OG1 . THR B  1  66  ? 3.687   -6.092  51.361 1.00 37.19  ? 79  THR B OG1 1 
ATOM   3128 C  CG2 . THR B  1  66  ? 5.839   -5.701  52.313 1.00 39.92  ? 79  THR B CG2 1 
ATOM   3129 N  N   . GLN B  1  67  ? 3.857   -6.743  48.212 1.00 41.16  ? 80  GLN B N   1 
ATOM   3130 C  CA  . GLN B  1  67  ? 3.201   -7.489  47.150 1.00 40.63  ? 80  GLN B CA  1 
ATOM   3131 C  C   . GLN B  1  67  ? 4.065   -7.486  45.890 1.00 42.49  ? 80  GLN B C   1 
ATOM   3132 O  O   . GLN B  1  67  ? 4.355   -8.549  45.356 1.00 43.97  ? 80  GLN B O   1 
ATOM   3133 C  CB  . GLN B  1  67  ? 1.788   -6.937  46.944 1.00 42.58  ? 80  GLN B CB  1 
ATOM   3134 C  CG  . GLN B  1  67  ? 0.914   -7.155  48.173 1.00 43.10  ? 80  GLN B CG  1 
ATOM   3135 C  CD  . GLN B  1  67  ? -0.520  -6.683  48.060 1.00 45.14  ? 80  GLN B CD  1 
ATOM   3136 O  OE1 . GLN B  1  67  ? -1.357  -7.087  48.872 1.00 41.81  ? 80  GLN B OE1 1 
ATOM   3137 N  NE2 . GLN B  1  67  ? -0.835  -5.845  47.076 1.00 43.48  ? 80  GLN B NE2 1 
ATOM   3138 N  N   . GLU B  1  68  ? 4.463   -6.304  45.407 1.00 46.24  ? 81  GLU B N   1 
ATOM   3139 C  CA  . GLU B  1  68  ? 5.241   -6.193  44.182 1.00 48.19  ? 81  GLU B CA  1 
ATOM   3140 C  C   . GLU B  1  68  ? 6.565   -6.942  44.304 1.00 45.06  ? 81  GLU B C   1 
ATOM   3141 O  O   . GLU B  1  68  ? 6.937   -7.685  43.404 1.00 45.57  ? 81  GLU B O   1 
ATOM   3142 C  CB  . GLU B  1  68  ? 5.534   -4.735  43.821 1.00 51.93  ? 81  GLU B CB  1 
ATOM   3143 C  CG  . GLU B  1  68  ? 4.304   -4.004  43.289 1.00 56.86  ? 81  GLU B CG  1 
ATOM   3144 C  CD  . GLU B  1  68  ? 3.691   -4.711  42.090 1.00 65.07  ? 81  GLU B CD  1 
ATOM   3145 O  OE1 . GLU B  1  68  ? 2.460   -4.947  42.073 1.00 63.12  ? 81  GLU B OE1 1 
ATOM   3146 O  OE2 . GLU B  1  68  ? 4.475   -5.061  41.174 1.00 66.71  ? 81  GLU B OE2 1 
ATOM   3147 N  N   . GLY B  1  69  ? 7.261   -6.732  45.420 1.00 39.17  ? 82  GLY B N   1 
ATOM   3148 C  CA  . GLY B  1  69  ? 8.629   -7.199  45.581 1.00 39.23  ? 82  GLY B CA  1 
ATOM   3149 C  C   . GLY B  1  69  ? 8.721   -8.681  45.953 1.00 40.68  ? 82  GLY B C   1 
ATOM   3150 O  O   . GLY B  1  69  ? 9.648   -9.358  45.510 1.00 38.20  ? 82  GLY B O   1 
ATOM   3151 N  N   . PHE B  1  70  ? 7.774   -9.184  46.764 1.00 37.42  ? 83  PHE B N   1 
ATOM   3152 C  CA  . PHE B  1  70  ? 7.908   -10.524 47.314 1.00 37.55  ? 83  PHE B CA  1 
ATOM   3153 C  C   . PHE B  1  70  ? 6.657   -11.379 47.122 1.00 37.33  ? 83  PHE B C   1 
ATOM   3154 O  O   . PHE B  1  70  ? 6.678   -12.560 47.467 1.00 40.24  ? 83  PHE B O   1 
ATOM   3155 C  CB  . PHE B  1  70  ? 8.229   -10.464 48.809 1.00 37.19  ? 83  PHE B CB  1 
ATOM   3156 C  CG  . PHE B  1  70  ? 9.663   -10.086 49.152 1.00 36.62  ? 83  PHE B CG  1 
ATOM   3157 C  CD1 . PHE B  1  70  ? 10.709  -10.970 48.930 1.00 38.62  ? 83  PHE B CD1 1 
ATOM   3158 C  CD2 . PHE B  1  70  ? 9.957   -8.856  49.719 1.00 37.37  ? 83  PHE B CD2 1 
ATOM   3159 C  CE1 . PHE B  1  70  ? 12.013  -10.638 49.272 1.00 37.68  ? 83  PHE B CE1 1 
ATOM   3160 C  CE2 . PHE B  1  70  ? 11.261  -8.518  50.050 1.00 39.32  ? 83  PHE B CE2 1 
ATOM   3161 C  CZ  . PHE B  1  70  ? 12.286  -9.410  49.830 1.00 40.83  ? 83  PHE B CZ  1 
ATOM   3162 N  N   . ASN B  1  71  ? 5.569   -10.795 46.609 1.00 36.99  ? 84  ASN B N   1 
ATOM   3163 C  CA  . ASN B  1  71  ? 4.284   -11.473 46.496 1.00 38.29  ? 84  ASN B CA  1 
ATOM   3164 C  C   . ASN B  1  71  ? 3.767   -11.848 47.882 1.00 37.69  ? 84  ASN B C   1 
ATOM   3165 O  O   . ASN B  1  71  ? 3.194   -12.916 48.069 1.00 34.90  ? 84  ASN B O   1 
ATOM   3166 C  CB  . ASN B  1  71  ? 4.372   -12.677 45.566 1.00 39.67  ? 84  ASN B CB  1 
ATOM   3167 C  CG  . ASN B  1  71  ? 3.152   -12.837 44.688 1.00 41.63  ? 84  ASN B CG  1 
ATOM   3168 O  OD1 . ASN B  1  71  ? 2.125   -12.179 44.897 1.00 39.96  ? 84  ASN B OD1 1 
ATOM   3169 N  ND2 . ASN B  1  71  ? 3.256   -13.705 43.689 1.00 42.47  ? 84  ASN B ND2 1 
ATOM   3170 N  N   . PHE B  1  72  ? 4.003   -10.978 48.868 1.00 39.02  ? 85  PHE B N   1 
ATOM   3171 C  CA  . PHE B  1  72  ? 3.438   -11.166 50.190 1.00 38.35  ? 85  PHE B CA  1 
ATOM   3172 C  C   . PHE B  1  72  ? 1.920   -11.114 50.026 1.00 39.42  ? 85  PHE B C   1 
ATOM   3173 O  O   . PHE B  1  72  ? 1.391   -10.255 49.312 1.00 38.69  ? 85  PHE B O   1 
ATOM   3174 C  CB  . PHE B  1  72  ? 3.968   -10.080 51.132 1.00 39.15  ? 85  PHE B CB  1 
ATOM   3175 C  CG  . PHE B  1  72  ? 3.896   -10.374 52.626 1.00 39.31  ? 85  PHE B CG  1 
ATOM   3176 C  CD1 . PHE B  1  72  ? 4.245   -11.617 53.148 1.00 39.90  ? 85  PHE B CD1 1 
ATOM   3177 C  CD2 . PHE B  1  72  ? 3.474   -9.393  53.511 1.00 40.45  ? 85  PHE B CD2 1 
ATOM   3178 C  CE1 . PHE B  1  72  ? 4.181   -11.862 54.515 1.00 41.73  ? 85  PHE B CE1 1 
ATOM   3179 C  CE2 . PHE B  1  72  ? 3.417   -9.637  54.876 1.00 41.38  ? 85  PHE B CE2 1 
ATOM   3180 C  CZ  . PHE B  1  72  ? 3.785   -10.867 55.378 1.00 39.21  ? 85  PHE B CZ  1 
ATOM   3181 N  N   . GLU B  1  73  ? 1.227   -12.072 50.635 1.00 37.53  ? 86  GLU B N   1 
ATOM   3182 C  CA  . GLU B  1  73  ? -0.212  -12.177 50.477 1.00 41.33  ? 86  GLU B CA  1 
ATOM   3183 C  C   . GLU B  1  73  ? -0.886  -10.954 51.104 1.00 38.46  ? 86  GLU B C   1 
ATOM   3184 O  O   . GLU B  1  73  ? -0.473  -10.464 52.151 1.00 40.87  ? 86  GLU B O   1 
ATOM   3185 C  CB  . GLU B  1  73  ? -0.666  -13.526 51.031 1.00 42.74  ? 86  GLU B CB  1 
ATOM   3186 C  CG  . GLU B  1  73  ? -2.135  -13.846 50.769 1.00 45.80  ? 86  GLU B CG  1 
ATOM   3187 C  CD  . GLU B  1  73  ? -3.099  -13.222 51.761 1.00 50.80  ? 86  GLU B CD  1 
ATOM   3188 O  OE1 . GLU B  1  73  ? -4.189  -12.776 51.331 1.00 58.93  ? 86  GLU B OE1 1 
ATOM   3189 O  OE2 . GLU B  1  73  ? -2.751  -13.164 52.957 1.00 53.81  ? 86  GLU B OE2 1 
ATOM   3190 N  N   . ASN B  1  74  ? -1.936  -10.483 50.434 1.00 41.08  ? 87  ASN B N   1 
ATOM   3191 C  CA  . ASN B  1  74  ? -2.588  -9.207  50.706 1.00 42.16  ? 87  ASN B CA  1 
ATOM   3192 C  C   . ASN B  1  74  ? -3.006  -9.081  52.172 1.00 41.49  ? 87  ASN B C   1 
ATOM   3193 O  O   . ASN B  1  74  ? -2.707  -8.077  52.817 1.00 43.48  ? 87  ASN B O   1 
ATOM   3194 C  CB  . ASN B  1  74  ? -3.766  -9.027  49.751 1.00 45.92  ? 87  ASN B CB  1 
ATOM   3195 C  CG  . ASN B  1  74  ? -4.523  -7.745  49.984 1.00 46.36  ? 87  ASN B CG  1 
ATOM   3196 O  OD1 . ASN B  1  74  ? -5.723  -7.789  50.279 1.00 48.49  ? 87  ASN B OD1 1 
ATOM   3197 N  ND2 . ASN B  1  74  ? -3.851  -6.612  49.837 1.00 44.88  ? 87  ASN B ND2 1 
ATOM   3198 N  N   . ASN B  1  75  ? -3.702  -10.088 52.700 1.00 39.31  ? 88  ASN B N   1 
ATOM   3199 C  CA  . ASN B  1  75  ? -4.207  -10.004 54.063 1.00 43.44  ? 88  ASN B CA  1 
ATOM   3200 C  C   . ASN B  1  75  ? -3.055  -10.037 55.071 1.00 44.87  ? 88  ASN B C   1 
ATOM   3201 O  O   . ASN B  1  75  ? -3.098  -9.326  56.073 1.00 39.99  ? 88  ASN B O   1 
ATOM   3202 C  CB  . ASN B  1  75  ? -5.285  -11.048 54.341 1.00 45.42  ? 88  ASN B CB  1 
ATOM   3203 C  CG  . ASN B  1  75  ? -6.631  -10.641 53.775 1.00 46.96  ? 88  ASN B CG  1 
ATOM   3204 O  OD1 . ASN B  1  75  ? -7.075  -9.497  53.945 1.00 42.51  ? 88  ASN B OD1 1 
ATOM   3205 N  ND2 . ASN B  1  75  ? -7.285  -11.556 53.081 1.00 48.03  ? 88  ASN B ND2 1 
ATOM   3206 N  N   . ALA B  1  76  ? -2.024  -10.850 54.808 1.00 42.32  ? 89  ALA B N   1 
ATOM   3207 C  CA  . ALA B  1  76  ? -0.861  -10.890 55.683 1.00 41.30  ? 89  ALA B CA  1 
ATOM   3208 C  C   . ALA B  1  76  ? -0.164  -9.531  55.700 1.00 37.53  ? 89  ALA B C   1 
ATOM   3209 O  O   . ALA B  1  76  ? 0.284   -9.083  56.750 1.00 42.48  ? 89  ALA B O   1 
ATOM   3210 C  CB  . ALA B  1  76  ? 0.074   -11.990 55.265 1.00 40.82  ? 89  ALA B CB  1 
ATOM   3211 N  N   . ALA B  1  77  ? -0.110  -8.873  54.537 1.00 37.29  ? 90  ALA B N   1 
ATOM   3212 C  CA  . ALA B  1  77  ? 0.460   -7.541  54.416 1.00 35.03  ? 90  ALA B CA  1 
ATOM   3213 C  C   . ALA B  1  77  ? -0.345  -6.523  55.228 1.00 36.18  ? 90  ALA B C   1 
ATOM   3214 O  O   . ALA B  1  77  ? 0.230   -5.652  55.877 1.00 38.64  ? 90  ALA B O   1 
ATOM   3215 C  CB  . ALA B  1  77  ? 0.534   -7.162  52.953 1.00 36.24  ? 90  ALA B CB  1 
ATOM   3216 N  N   . ILE B  1  78  ? -1.680  -6.643  55.195 1.00 39.50  ? 91  ILE B N   1 
ATOM   3217 C  CA  . ILE B  1  78  ? -2.553  -5.720  55.905 1.00 38.99  ? 91  ILE B CA  1 
ATOM   3218 C  C   . ILE B  1  78  ? -2.394  -5.920  57.414 1.00 36.68  ? 91  ILE B C   1 
ATOM   3219 O  O   . ILE B  1  78  ? -2.255  -4.952  58.161 1.00 40.34  ? 91  ILE B O   1 
ATOM   3220 C  CB  . ILE B  1  78  ? -4.012  -5.874  55.418 1.00 42.08  ? 91  ILE B CB  1 
ATOM   3221 C  CG1 . ILE B  1  78  ? -4.170  -5.319  54.000 1.00 42.70  ? 91  ILE B CG1 1 
ATOM   3222 C  CG2 . ILE B  1  78  ? -4.989  -5.206  56.384 1.00 41.04  ? 91  ILE B CG2 1 
ATOM   3223 C  CD1 . ILE B  1  78  ? -5.462  -5.692  53.291 1.00 41.29  ? 91  ILE B CD1 1 
ATOM   3224 N  N   . VAL B  1  79  ? -2.366  -7.176  57.860 1.00 34.57  ? 92  VAL B N   1 
ATOM   3225 C  CA  . VAL B  1  79  ? -2.209  -7.481  59.274 1.00 36.07  ? 92  VAL B CA  1 
ATOM   3226 C  C   . VAL B  1  79  ? -0.880  -6.932  59.798 1.00 37.87  ? 92  VAL B C   1 
ATOM   3227 O  O   . VAL B  1  79  ? -0.846  -6.285  60.844 1.00 40.00  ? 92  VAL B O   1 
ATOM   3228 C  CB  . VAL B  1  79  ? -2.329  -8.997  59.532 1.00 37.63  ? 92  VAL B CB  1 
ATOM   3229 C  CG1 . VAL B  1  79  ? -1.854  -9.392  60.928 1.00 38.95  ? 92  VAL B CG1 1 
ATOM   3230 C  CG2 . VAL B  1  79  ? -3.747  -9.478  59.291 1.00 39.69  ? 92  VAL B CG2 1 
ATOM   3231 N  N   . ALA B  1  80  ? 0.218   -7.196  59.086 1.00 35.31  ? 93  ALA B N   1 
ATOM   3232 C  CA  . ALA B  1  80  ? 1.530   -6.764  59.551 1.00 36.71  ? 93  ALA B CA  1 
ATOM   3233 C  C   . ALA B  1  80  ? 1.642   -5.242  59.508 1.00 37.11  ? 93  ALA B C   1 
ATOM   3234 O  O   . ALA B  1  80  ? 2.144   -4.639  60.458 1.00 37.61  ? 93  ALA B O   1 
ATOM   3235 C  CB  . ALA B  1  80  ? 2.623   -7.412  58.729 1.00 37.12  ? 93  ALA B CB  1 
ATOM   3236 N  N   . THR B  1  81  ? 1.163   -4.618  58.421 1.00 36.39  ? 94  THR B N   1 
ATOM   3237 C  CA  . THR B  1  81  ? 1.451   -3.209  58.191 1.00 36.81  ? 94  THR B CA  1 
ATOM   3238 C  C   . THR B  1  81  ? 0.713   -2.336  59.205 1.00 40.45  ? 94  THR B C   1 
ATOM   3239 O  O   . THR B  1  81  ? 1.314   -1.433  59.784 1.00 41.53  ? 94  THR B O   1 
ATOM   3240 C  CB  . THR B  1  81  ? 1.102   -2.812  56.758 1.00 38.51  ? 94  THR B CB  1 
ATOM   3241 O  OG1 . THR B  1  81  ? 1.910   -3.574  55.872 1.00 42.12  ? 94  THR B OG1 1 
ATOM   3242 C  CG2 . THR B  1  81  ? 1.361   -1.340  56.492 1.00 37.85  ? 94  THR B CG2 1 
ATOM   3243 N  N   . TYR B  1  82  ? -0.594  -2.573  59.403 1.00 42.21  ? 95  TYR B N   1 
ATOM   3244 C  CA  . TYR B  1  82  ? -1.381  -1.688  60.253 1.00 42.24  ? 95  TYR B CA  1 
ATOM   3245 C  C   . TYR B  1  82  ? -1.087  -1.983  61.724 1.00 42.81  ? 95  TYR B C   1 
ATOM   3246 O  O   . TYR B  1  82  ? -1.237  -1.101  62.568 1.00 41.88  ? 95  TYR B O   1 
ATOM   3247 C  CB  . TYR B  1  82  ? -2.871  -1.720  59.895 1.00 41.60  ? 95  TYR B CB  1 
ATOM   3248 C  CG  . TYR B  1  82  ? -3.159  -1.080  58.547 1.00 39.39  ? 95  TYR B CG  1 
ATOM   3249 C  CD1 . TYR B  1  82  ? -3.181  0.300   58.399 1.00 41.27  ? 95  TYR B CD1 1 
ATOM   3250 C  CD2 . TYR B  1  82  ? -3.386  -1.852  57.419 1.00 38.51  ? 95  TYR B CD2 1 
ATOM   3251 C  CE1 . TYR B  1  82  ? -3.414  0.892   57.166 1.00 42.91  ? 95  TYR B CE1 1 
ATOM   3252 C  CE2 . TYR B  1  82  ? -3.622  -1.274  56.182 1.00 39.99  ? 95  TYR B CE2 1 
ATOM   3253 C  CZ  . TYR B  1  82  ? -3.629  0.104   56.049 1.00 43.17  ? 95  TYR B CZ  1 
ATOM   3254 O  OH  . TYR B  1  82  ? -3.868  0.678   54.827 1.00 45.97  ? 95  TYR B OH  1 
ATOM   3255 N  N   . LEU B  1  83  ? -0.635  -3.202  62.037 1.00 42.88  ? 96  LEU B N   1 
ATOM   3256 C  CA  . LEU B  1  83  ? -0.128  -3.490  63.373 1.00 43.46  ? 96  LEU B CA  1 
ATOM   3257 C  C   . LEU B  1  83  ? 1.060   -2.573  63.656 1.00 44.18  ? 96  LEU B C   1 
ATOM   3258 O  O   . LEU B  1  83  ? 1.074   -1.835  64.647 1.00 40.16  ? 96  LEU B O   1 
ATOM   3259 C  CB  . LEU B  1  83  ? 0.257   -4.962  63.486 1.00 44.97  ? 96  LEU B CB  1 
ATOM   3260 C  CG  . LEU B  1  83  ? 0.999   -5.377  64.759 1.00 46.57  ? 96  LEU B CG  1 
ATOM   3261 C  CD1 . LEU B  1  83  ? 0.173   -5.132  66.011 1.00 46.79  ? 96  LEU B CD1 1 
ATOM   3262 C  CD2 . LEU B  1  83  ? 1.414   -6.839  64.652 1.00 45.66  ? 96  LEU B CD2 1 
ATOM   3263 N  N   . GLY B  1  84  ? 2.049   -2.622  62.759 1.00 39.45  ? 97  GLY B N   1 
ATOM   3264 C  CA  . GLY B  1  84  ? 3.215   -1.764  62.853 1.00 40.58  ? 97  GLY B CA  1 
ATOM   3265 C  C   . GLY B  1  84  ? 2.833   -0.283  62.938 1.00 41.94  ? 97  GLY B C   1 
ATOM   3266 O  O   . GLY B  1  84  ? 3.388   0.451   63.756 1.00 40.40  ? 97  GLY B O   1 
ATOM   3267 N  N   . HIS B  1  85  ? 1.881   0.143   62.094 1.00 39.96  ? 98  HIS B N   1 
ATOM   3268 C  CA  . HIS B  1  85  ? 1.522   1.550   61.988 1.00 42.57  ? 98  HIS B CA  1 
ATOM   3269 C  C   . HIS B  1  85  ? 0.774   2.021   63.238 1.00 43.97  ? 98  HIS B C   1 
ATOM   3270 O  O   . HIS B  1  85  ? 1.094   3.074   63.789 1.00 39.36  ? 98  HIS B O   1 
ATOM   3271 C  CB  . HIS B  1  85  ? 0.698   1.794   60.724 1.00 40.98  ? 98  HIS B CB  1 
ATOM   3272 C  CG  . HIS B  1  85  ? 0.420   3.225   60.441 1.00 40.34  ? 98  HIS B CG  1 
ATOM   3273 N  ND1 . HIS B  1  85  ? 1.424   4.162   60.361 1.00 42.81  ? 98  HIS B ND1 1 
ATOM   3274 C  CD2 . HIS B  1  85  ? -0.733  3.877   60.184 1.00 43.50  ? 98  HIS B CD2 1 
ATOM   3275 C  CE1 . HIS B  1  85  ? 0.894   5.346   60.084 1.00 43.35  ? 98  HIS B CE1 1 
ATOM   3276 N  NE2 . HIS B  1  85  ? -0.415  5.198   59.970 1.00 44.51  ? 98  HIS B NE2 1 
ATOM   3277 N  N   . LEU B  1  86  ? -0.228  1.249   63.680 1.00 44.67  ? 99  LEU B N   1 
ATOM   3278 C  CA  . LEU B  1  86  ? -1.026  1.618   64.845 1.00 45.31  ? 99  LEU B CA  1 
ATOM   3279 C  C   . LEU B  1  86  ? -0.130  1.852   66.060 1.00 44.91  ? 99  LEU B C   1 
ATOM   3280 O  O   . LEU B  1  86  ? -0.311  2.839   66.776 1.00 46.18  ? 99  LEU B O   1 
ATOM   3281 C  CB  . LEU B  1  86  ? -2.078  0.551   65.139 1.00 43.83  ? 99  LEU B CB  1 
ATOM   3282 C  CG  . LEU B  1  86  ? -3.312  0.568   64.228 1.00 41.04  ? 99  LEU B CG  1 
ATOM   3283 C  CD1 . LEU B  1  86  ? -4.089  -0.719  64.312 1.00 41.45  ? 99  LEU B CD1 1 
ATOM   3284 C  CD2 . LEU B  1  86  ? -4.210  1.738   64.564 1.00 44.28  ? 99  LEU B CD2 1 
ATOM   3285 N  N   . LEU B  1  87  ? 0.844   0.956   66.258 1.00 44.03  ? 100 LEU B N   1 
ATOM   3286 C  CA  . LEU B  1  87  ? 1.681   0.960   67.447 1.00 45.26  ? 100 LEU B CA  1 
ATOM   3287 C  C   . LEU B  1  87  ? 2.863   1.914   67.290 1.00 44.13  ? 100 LEU B C   1 
ATOM   3288 O  O   . LEU B  1  87  ? 3.259   2.540   68.274 1.00 42.47  ? 100 LEU B O   1 
ATOM   3289 C  CB  . LEU B  1  87  ? 2.179   -0.455  67.739 1.00 47.27  ? 100 LEU B CB  1 
ATOM   3290 C  CG  . LEU B  1  87  ? 1.120   -1.501  68.097 1.00 46.00  ? 100 LEU B CG  1 
ATOM   3291 C  CD1 . LEU B  1  87  ? 1.793   -2.859  68.246 1.00 47.58  ? 100 LEU B CD1 1 
ATOM   3292 C  CD2 . LEU B  1  87  ? 0.362   -1.170  69.367 1.00 44.56  ? 100 LEU B CD2 1 
ATOM   3293 N  N   . ASN B  1  88  ? 3.431   2.010   66.074 1.00 41.88  ? 101 ASN B N   1 
ATOM   3294 C  CA  . ASN B  1  88  ? 4.744   2.609   65.906 1.00 41.84  ? 101 ASN B CA  1 
ATOM   3295 C  C   . ASN B  1  88  ? 4.784   3.708   64.853 1.00 44.90  ? 101 ASN B C   1 
ATOM   3296 O  O   . ASN B  1  88  ? 5.851   4.281   64.627 1.00 45.55  ? 101 ASN B O   1 
ATOM   3297 C  CB  . ASN B  1  88  ? 5.787   1.579   65.492 1.00 43.11  ? 101 ASN B CB  1 
ATOM   3298 C  CG  . ASN B  1  88  ? 5.949   0.492   66.522 1.00 43.66  ? 101 ASN B CG  1 
ATOM   3299 O  OD1 . ASN B  1  88  ? 5.941   0.771   67.728 1.00 46.36  ? 101 ASN B OD1 1 
ATOM   3300 N  ND2 . ASN B  1  88  ? 6.063   -0.748  66.074 1.00 46.43  ? 101 ASN B ND2 1 
ATOM   3301 N  N   . GLY B  1  89  ? 3.654   3.993   64.200 1.00 42.96  ? 102 GLY B N   1 
ATOM   3302 C  CA  . GLY B  1  89  ? 3.621   4.996   63.144 1.00 45.62  ? 102 GLY B CA  1 
ATOM   3303 C  C   . GLY B  1  89  ? 2.921   6.279   63.588 1.00 47.02  ? 102 GLY B C   1 
ATOM   3304 O  O   . GLY B  1  89  ? 2.343   6.346   64.677 1.00 47.90  ? 102 GLY B O   1 
ATOM   3305 N  N   . ASN B  1  90  ? 2.977   7.285   62.709 1.00 48.03  ? 103 ASN B N   1 
ATOM   3306 C  CA  . ASN B  1  90  ? 2.323   8.563   62.917 1.00 47.53  ? 103 ASN B CA  1 
ATOM   3307 C  C   . ASN B  1  90  ? 1.003   8.563   62.154 1.00 46.59  ? 103 ASN B C   1 
ATOM   3308 O  O   . ASN B  1  90  ? 0.984   8.664   60.930 1.00 43.95  ? 103 ASN B O   1 
ATOM   3309 C  CB  . ASN B  1  90  ? 3.227   9.714   62.495 1.00 49.71  ? 103 ASN B CB  1 
ATOM   3310 C  CG  . ASN B  1  90  ? 2.674   11.060  62.894 1.00 49.42  ? 103 ASN B CG  1 
ATOM   3311 O  OD1 . ASN B  1  90  ? 1.473   11.314  62.730 1.00 49.62  ? 103 ASN B OD1 1 
ATOM   3312 N  ND2 . ASN B  1  90  ? 3.529   11.930  63.415 1.00 49.99  ? 103 ASN B ND2 1 
ATOM   3313 N  N   . LEU B  1  91  ? -0.103  8.494   62.898 1.00 48.17  ? 104 LEU B N   1 
ATOM   3314 C  CA  . LEU B  1  91  ? -1.415  8.287   62.307 1.00 50.87  ? 104 LEU B CA  1 
ATOM   3315 C  C   . LEU B  1  91  ? -1.920  9.557   61.630 1.00 48.35  ? 104 LEU B C   1 
ATOM   3316 O  O   . LEU B  1  91  ? -2.718  9.466   60.705 1.00 49.84  ? 104 LEU B O   1 
ATOM   3317 C  CB  . LEU B  1  91  ? -2.340  7.783   63.404 1.00 53.64  ? 104 LEU B CB  1 
ATOM   3318 C  CG  . LEU B  1  91  ? -1.935  6.415   63.961 1.00 60.97  ? 104 LEU B CG  1 
ATOM   3319 C  CD1 . LEU B  1  91  ? -2.421  6.177   65.368 1.00 66.76  ? 104 LEU B CD1 1 
ATOM   3320 C  CD2 . LEU B  1  91  ? -2.462  5.358   63.020 1.00 65.94  ? 104 LEU B CD2 1 
ATOM   3321 N  N   . VAL B  1  92  ? -1.403  10.718  62.041 1.00 51.33  ? 105 VAL B N   1 
ATOM   3322 C  CA  . VAL B  1  92  ? -1.802  11.997  61.474 1.00 49.44  ? 105 VAL B CA  1 
ATOM   3323 C  C   . VAL B  1  92  ? -1.135  12.208  60.117 1.00 51.32  ? 105 VAL B C   1 
ATOM   3324 O  O   . VAL B  1  92  ? -1.812  12.619  59.173 1.00 50.26  ? 105 VAL B O   1 
ATOM   3325 C  CB  . VAL B  1  92  ? -1.470  13.158  62.432 1.00 51.51  ? 105 VAL B CB  1 
ATOM   3326 C  CG1 . VAL B  1  92  ? -1.692  14.519  61.787 1.00 51.35  ? 105 VAL B CG1 1 
ATOM   3327 C  CG2 . VAL B  1  92  ? -2.238  13.053  63.736 1.00 54.74  ? 105 VAL B CG2 1 
ATOM   3328 N  N   . THR B  1  93  ? 0.181   11.951  60.020 1.00 50.56  ? 106 THR B N   1 
ATOM   3329 C  CA  . THR B  1  93  ? 0.884   12.132  58.755 1.00 53.39  ? 106 THR B CA  1 
ATOM   3330 C  C   . THR B  1  93  ? 0.802   10.865  57.904 1.00 52.10  ? 106 THR B C   1 
ATOM   3331 O  O   . THR B  1  93  ? 1.138   10.909  56.725 1.00 54.81  ? 106 THR B O   1 
ATOM   3332 C  CB  . THR B  1  93  ? 2.341   12.525  58.984 1.00 56.48  ? 106 THR B CB  1 
ATOM   3333 O  OG1 . THR B  1  93  ? 2.938   11.442  59.690 1.00 55.30  ? 106 THR B OG1 1 
ATOM   3334 C  CG2 . THR B  1  93  ? 2.478   13.819  59.764 1.00 55.52  ? 106 THR B CG2 1 
ATOM   3335 N  N   . ASP B  1  94  ? 0.376   9.747   58.507 1.00 45.54  ? 107 ASP B N   1 
ATOM   3336 C  CA  . ASP B  1  94  ? 0.222   8.479   57.813 1.00 47.59  ? 107 ASP B CA  1 
ATOM   3337 C  C   . ASP B  1  94  ? 1.585   7.965   57.350 1.00 45.23  ? 107 ASP B C   1 
ATOM   3338 O  O   . ASP B  1  94  ? 1.697   7.429   56.259 1.00 46.71  ? 107 ASP B O   1 
ATOM   3339 C  CB  . ASP B  1  94  ? -0.787  8.585   56.680 1.00 44.39  ? 107 ASP B CB  1 
ATOM   3340 C  CG  . ASP B  1  94  ? -1.333  7.265   56.157 1.00 47.03  ? 107 ASP B CG  1 
ATOM   3341 O  OD1 . ASP B  1  94  ? -1.665  6.397   56.992 1.00 48.54  ? 107 ASP B OD1 1 
ATOM   3342 O  OD2 . ASP B  1  94  ? -1.440  7.123   54.916 1.00 45.85  ? 107 ASP B OD2 1 
ATOM   3343 N  N   . LEU B  1  95  ? 2.607   8.114   58.196 1.00 45.36  ? 108 LEU B N   1 
ATOM   3344 C  CA  . LEU B  1  95  ? 3.962   7.697   57.867 1.00 46.57  ? 108 LEU B CA  1 
ATOM   3345 C  C   . LEU B  1  95  ? 4.497   6.794   58.977 1.00 46.51  ? 108 LEU B C   1 
ATOM   3346 O  O   . LEU B  1  95  ? 4.267   7.042   60.161 1.00 43.60  ? 108 LEU B O   1 
ATOM   3347 C  CB  . LEU B  1  95  ? 4.874   8.909   57.658 1.00 48.64  ? 108 LEU B CB  1 
ATOM   3348 C  CG  . LEU B  1  95  ? 4.552   9.828   56.477 1.00 50.10  ? 108 LEU B CG  1 
ATOM   3349 C  CD1 . LEU B  1  95  ? 5.428   11.071  56.583 1.00 53.07  ? 108 LEU B CD1 1 
ATOM   3350 C  CD2 . LEU B  1  95  ? 4.765   9.149   55.141 1.00 51.74  ? 108 LEU B CD2 1 
ATOM   3351 N  N   . LEU B  1  96  ? 5.212   5.737   58.564 1.00 43.95  ? 109 LEU B N   1 
ATOM   3352 C  CA  . LEU B  1  96  ? 5.832   4.783   59.468 1.00 42.55  ? 109 LEU B CA  1 
ATOM   3353 C  C   . LEU B  1  96  ? 7.308   4.646   59.112 1.00 40.20  ? 109 LEU B C   1 
ATOM   3354 O  O   . LEU B  1  96  ? 7.642   4.454   57.947 1.00 44.27  ? 109 LEU B O   1 
ATOM   3355 C  CB  . LEU B  1  96  ? 5.090   3.452   59.331 1.00 42.22  ? 109 LEU B CB  1 
ATOM   3356 C  CG  . LEU B  1  96  ? 5.729   2.235   60.006 1.00 40.43  ? 109 LEU B CG  1 
ATOM   3357 C  CD1 . LEU B  1  96  ? 5.845   2.429   61.502 1.00 39.58  ? 109 LEU B CD1 1 
ATOM   3358 C  CD2 . LEU B  1  96  ? 4.926   0.984   59.670 1.00 40.77  ? 109 LEU B CD2 1 
ATOM   3359 N  N   . SER B  1  97  ? 8.169   4.719   60.132 1.00 43.26  ? 110 SER B N   1 
ATOM   3360 C  CA  . SER B  1  97  ? 9.584   4.401   60.017 1.00 41.76  ? 110 SER B CA  1 
ATOM   3361 C  C   . SER B  1  97  ? 9.785   2.894   60.123 1.00 41.70  ? 110 SER B C   1 
ATOM   3362 O  O   . SER B  1  97  ? 9.296   2.268   61.062 1.00 42.30  ? 110 SER B O   1 
ATOM   3363 C  CB  . SER B  1  97  ? 10.382  5.090   61.088 1.00 41.04  ? 110 SER B CB  1 
ATOM   3364 O  OG  . SER B  1  97  ? 11.735  4.651   61.089 1.00 42.38  ? 110 SER B OG  1 
ATOM   3365 N  N   . ILE B  1  98  ? 10.563  2.314   59.203 1.00 39.97  ? 111 ILE B N   1 
ATOM   3366 C  CA  . ILE B  1  98  ? 10.801  0.882   59.254 1.00 40.24  ? 111 ILE B CA  1 
ATOM   3367 C  C   . ILE B  1  98  ? 11.915  0.574   60.254 1.00 38.82  ? 111 ILE B C   1 
ATOM   3368 O  O   . ILE B  1  98  ? 12.277  -0.585  60.430 1.00 40.22  ? 111 ILE B O   1 
ATOM   3369 C  CB  . ILE B  1  98  ? 11.105  0.297   57.862 1.00 40.37  ? 111 ILE B CB  1 
ATOM   3370 C  CG1 . ILE B  1  98  ? 12.437  0.782   57.282 1.00 37.92  ? 111 ILE B CG1 1 
ATOM   3371 C  CG2 . ILE B  1  98  ? 9.943   0.549   56.912 1.00 39.86  ? 111 ILE B CG2 1 
ATOM   3372 C  CD1 . ILE B  1  98  ? 12.824  0.076   55.997 1.00 39.63  ? 111 ILE B CD1 1 
ATOM   3373 N  N   . GLY B  1  99  ? 12.452  1.614   60.896 1.00 39.99  ? 112 GLY B N   1 
ATOM   3374 C  CA  . GLY B  1  99  ? 13.501  1.460   61.892 1.00 44.25  ? 112 GLY B CA  1 
ATOM   3375 C  C   . GLY B  1  99  ? 13.195  2.299   63.129 1.00 46.07  ? 112 GLY B C   1 
ATOM   3376 O  O   . GLY B  1  99  ? 12.162  2.103   63.773 1.00 46.66  ? 112 GLY B O   1 
ATOM   3377 N  N   . GLY B  1  100 ? 14.092  3.242   63.436 1.00 46.17  ? 113 GLY B N   1 
ATOM   3378 C  CA  . GLY B  1  100 ? 14.004  4.034   64.650 1.00 46.69  ? 113 GLY B CA  1 
ATOM   3379 C  C   . GLY B  1  100 ? 13.331  5.383   64.415 1.00 45.87  ? 113 GLY B C   1 
ATOM   3380 O  O   . GLY B  1  100 ? 12.704  5.615   63.382 1.00 42.92  ? 113 GLY B O   1 
ATOM   3381 N  N   . ALA B  1  101 ? 13.472  6.271   65.405 1.00 49.77  ? 114 ALA B N   1 
ATOM   3382 C  CA  . ALA B  1  101 ? 12.811  7.565   65.382 1.00 50.70  ? 114 ALA B CA  1 
ATOM   3383 C  C   . ALA B  1  101 ? 13.463  8.452   64.327 1.00 53.15  ? 114 ALA B C   1 
ATOM   3384 O  O   . ALA B  1  101 ? 14.666  8.363   64.102 1.00 54.28  ? 114 ALA B O   1 
ATOM   3385 C  CB  . ALA B  1  101 ? 12.872  8.200   66.756 1.00 51.92  ? 114 ALA B CB  1 
ATOM   3386 N  N   . THR B  1  102 ? 12.657  9.298   63.686 1.00 51.13  ? 115 THR B N   1 
ATOM   3387 C  CA  . THR B  1  102 ? 13.162  10.183  62.655 1.00 51.70  ? 115 THR B CA  1 
ATOM   3388 C  C   . THR B  1  102 ? 12.202  11.356  62.516 1.00 52.44  ? 115 THR B C   1 
ATOM   3389 O  O   . THR B  1  102 ? 10.996  11.161  62.602 1.00 53.64  ? 115 THR B O   1 
ATOM   3390 C  CB  . THR B  1  102 ? 13.298  9.423   61.333 1.00 51.68  ? 115 THR B CB  1 
ATOM   3391 O  OG1 . THR B  1  102 ? 13.689  10.384  60.356 1.00 49.41  ? 115 THR B OG1 1 
ATOM   3392 C  CG2 . THR B  1  102 ? 11.986  8.847   60.826 1.00 53.35  ? 115 THR B CG2 1 
ATOM   3393 N  N   . PRO B  1  103 ? 12.700  12.589  62.263 1.00 56.23  ? 116 PRO B N   1 
ATOM   3394 C  CA  . PRO B  1  103 ? 11.827  13.716  61.929 1.00 54.14  ? 116 PRO B CA  1 
ATOM   3395 C  C   . PRO B  1  103 ? 11.023  13.506  60.646 1.00 52.75  ? 116 PRO B C   1 
ATOM   3396 O  O   . PRO B  1  103 ? 10.004  14.164  60.442 1.00 55.89  ? 116 PRO B O   1 
ATOM   3397 C  CB  . PRO B  1  103 ? 12.799  14.913  61.823 1.00 58.10  ? 116 PRO B CB  1 
ATOM   3398 C  CG  . PRO B  1  103 ? 14.150  14.285  61.564 1.00 57.93  ? 116 PRO B CG  1 
ATOM   3399 C  CD  . PRO B  1  103 ? 14.123  12.966  62.310 1.00 57.04  ? 116 PRO B CD  1 
ATOM   3400 N  N   . LYS B  1  104 ? 11.462  12.564  59.801 1.00 49.84  ? 117 LYS B N   1 
ATOM   3401 C  CA  . LYS B  1  104 ? 10.794  12.276  58.538 1.00 48.52  ? 117 LYS B CA  1 
ATOM   3402 C  C   . LYS B  1  104 ? 9.352   11.793  58.727 1.00 49.39  ? 117 LYS B C   1 
ATOM   3403 O  O   . LYS B  1  104 ? 8.585   11.851  57.774 1.00 48.37  ? 117 LYS B O   1 
ATOM   3404 C  CB  . LYS B  1  104 ? 11.589  11.246  57.728 1.00 53.90  ? 117 LYS B CB  1 
ATOM   3405 C  CG  . LYS B  1  104 ? 12.880  11.779  57.110 1.00 57.26  ? 117 LYS B CG  1 
ATOM   3406 C  CD  . LYS B  1  104 ? 13.928  10.711  56.820 1.00 62.04  ? 117 LYS B CD  1 
ATOM   3407 C  CE  . LYS B  1  104 ? 15.111  11.231  56.051 1.00 61.31  ? 117 LYS B CE  1 
ATOM   3408 N  NZ  . LYS B  1  104 ? 14.750  11.665  54.698 1.00 63.53  ? 117 LYS B NZ  1 
ATOM   3409 N  N   . THR B  1  105 ? 8.971   11.313  59.922 1.00 49.63  ? 118 THR B N   1 
ATOM   3410 C  CA  . THR B  1  105 ? 7.592   10.889  60.145 1.00 51.67  ? 118 THR B CA  1 
ATOM   3411 C  C   . THR B  1  105 ? 6.720   12.080  60.552 1.00 57.56  ? 118 THR B C   1 
ATOM   3412 O  O   . THR B  1  105 ? 5.499   11.935  60.653 1.00 55.62  ? 118 THR B O   1 
ATOM   3413 C  CB  . THR B  1  105 ? 7.482   9.749   61.163 1.00 46.10  ? 118 THR B CB  1 
ATOM   3414 O  OG1 . THR B  1  105 ? 8.104   10.090  62.397 1.00 43.47  ? 118 THR B OG1 1 
ATOM   3415 C  CG2 . THR B  1  105 ? 8.116   8.472   60.654 1.00 45.35  ? 118 THR B CG2 1 
ATOM   3416 N  N   . GLY B  1  106 ? 7.350   13.236  60.815 1.00 64.37  ? 119 GLY B N   1 
ATOM   3417 C  CA  . GLY B  1  106 ? 6.627   14.480  61.035 1.00 63.18  ? 119 GLY B CA  1 
ATOM   3418 C  C   . GLY B  1  106 ? 6.462   14.807  62.518 1.00 63.13  ? 119 GLY B C   1 
ATOM   3419 O  O   . GLY B  1  106 ? 7.052   14.148  63.373 1.00 55.79  ? 119 GLY B O   1 
ATOM   3420 N  N   . PRO B  1  107 ? 5.645   15.834  62.856 1.00 68.39  ? 120 PRO B N   1 
ATOM   3421 C  CA  . PRO B  1  107 ? 5.451   16.254  64.245 1.00 66.76  ? 120 PRO B CA  1 
ATOM   3422 C  C   . PRO B  1  107 ? 5.086   15.083  65.153 1.00 60.99  ? 120 PRO B C   1 
ATOM   3423 O  O   . PRO B  1  107 ? 4.162   14.338  64.858 1.00 59.35  ? 120 PRO B O   1 
ATOM   3424 C  CB  . PRO B  1  107 ? 4.315   17.289  64.162 1.00 67.81  ? 120 PRO B CB  1 
ATOM   3425 C  CG  . PRO B  1  107 ? 4.364   17.804  62.736 1.00 69.04  ? 120 PRO B CG  1 
ATOM   3426 C  CD  . PRO B  1  107 ? 4.863   16.640  61.904 1.00 67.89  ? 120 PRO B CD  1 
ATOM   3427 N  N   . PRO B  1  108 ? 5.797   14.875  66.279 1.00 61.83  ? 121 PRO B N   1 
ATOM   3428 C  CA  . PRO B  1  108 ? 5.539   13.711  67.127 1.00 63.92  ? 121 PRO B CA  1 
ATOM   3429 C  C   . PRO B  1  108 ? 4.122   13.741  67.695 1.00 67.46  ? 121 PRO B C   1 
ATOM   3430 O  O   . PRO B  1  108 ? 3.561   14.811  67.899 1.00 69.05  ? 121 PRO B O   1 
ATOM   3431 C  CB  . PRO B  1  108 ? 6.617   13.767  68.221 1.00 63.79  ? 121 PRO B CB  1 
ATOM   3432 C  CG  . PRO B  1  108 ? 7.202   15.158  68.133 1.00 65.58  ? 121 PRO B CG  1 
ATOM   3433 C  CD  . PRO B  1  108 ? 6.879   15.738  66.775 1.00 63.23  ? 121 PRO B CD  1 
ATOM   3434 N  N   . PRO B  1  109 ? 3.480   12.572  67.932 1.00 65.79  ? 122 PRO B N   1 
ATOM   3435 C  CA  . PRO B  1  109 ? 2.143   12.540  68.523 1.00 66.80  ? 122 PRO B CA  1 
ATOM   3436 C  C   . PRO B  1  109 ? 2.212   12.830  70.020 1.00 64.76  ? 122 PRO B C   1 
ATOM   3437 O  O   . PRO B  1  109 ? 3.286   12.772  70.614 1.00 62.66  ? 122 PRO B O   1 
ATOM   3438 C  CB  . PRO B  1  109 ? 1.673   11.106  68.224 1.00 66.11  ? 122 PRO B CB  1 
ATOM   3439 C  CG  . PRO B  1  109 ? 2.963   10.287  68.221 1.00 66.34  ? 122 PRO B CG  1 
ATOM   3440 C  CD  . PRO B  1  109 ? 4.018   11.225  67.667 1.00 65.92  ? 122 PRO B CD  1 
ATOM   3441 N  N   . PRO B  1  110 ? 1.074   13.154  70.675 1.00 63.85  ? 123 PRO B N   1 
ATOM   3442 C  CA  . PRO B  1  110 ? 1.050   13.330  72.129 1.00 60.06  ? 123 PRO B CA  1 
ATOM   3443 C  C   . PRO B  1  110 ? 1.443   12.056  72.881 1.00 58.50  ? 123 PRO B C   1 
ATOM   3444 O  O   . PRO B  1  110 ? 0.962   10.966  72.571 1.00 59.03  ? 123 PRO B O   1 
ATOM   3445 C  CB  . PRO B  1  110 ? -0.389  13.789  72.438 1.00 63.82  ? 123 PRO B CB  1 
ATOM   3446 C  CG  . PRO B  1  110 ? -1.194  13.404  71.219 1.00 67.19  ? 123 PRO B CG  1 
ATOM   3447 C  CD  . PRO B  1  110 ? -0.228  13.413  70.042 1.00 66.71  ? 123 PRO B CD  1 
ATOM   3448 N  N   . PRO B  1  111 ? 2.364   12.145  73.869 1.00 58.02  ? 124 PRO B N   1 
ATOM   3449 C  CA  . PRO B  1  111 ? 2.702   11.006  74.726 1.00 58.59  ? 124 PRO B CA  1 
ATOM   3450 C  C   . PRO B  1  111 ? 1.454   10.424  75.385 1.00 57.61  ? 124 PRO B C   1 
ATOM   3451 O  O   . PRO B  1  111 ? 0.495   11.151  75.613 1.00 57.79  ? 124 PRO B O   1 
ATOM   3452 C  CB  . PRO B  1  111 ? 3.672   11.603  75.776 1.00 60.04  ? 124 PRO B CB  1 
ATOM   3453 C  CG  . PRO B  1  111 ? 4.250   12.821  75.101 1.00 59.91  ? 124 PRO B CG  1 
ATOM   3454 C  CD  . PRO B  1  111 ? 3.158   13.342  74.187 1.00 58.76  ? 124 PRO B CD  1 
ATOM   3455 N  N   . PRO B  1  112 ? 1.413   9.112   75.725 1.00 56.41  ? 125 PRO B N   1 
ATOM   3456 C  CA  . PRO B  1  112 ? 2.562   8.209   75.575 1.00 56.90  ? 125 PRO B CA  1 
ATOM   3457 C  C   . PRO B  1  112 ? 2.800   7.591   74.191 1.00 58.45  ? 125 PRO B C   1 
ATOM   3458 O  O   . PRO B  1  112 ? 3.676   6.738   74.038 1.00 62.86  ? 125 PRO B O   1 
ATOM   3459 C  CB  . PRO B  1  112 ? 2.294   7.131   76.636 1.00 58.17  ? 125 PRO B CB  1 
ATOM   3460 C  CG  . PRO B  1  112 ? 0.798   7.208   76.930 1.00 57.58  ? 125 PRO B CG  1 
ATOM   3461 C  CD  . PRO B  1  112 ? 0.231   8.454   76.300 1.00 57.84  ? 125 PRO B CD  1 
ATOM   3462 N  N   . ALA B  1  113 ? 2.032   8.015   73.182 1.00 59.32  ? 126 ALA B N   1 
ATOM   3463 C  CA  . ALA B  1  113 ? 2.296   7.622   71.805 1.00 59.46  ? 126 ALA B CA  1 
ATOM   3464 C  C   . ALA B  1  113 ? 3.610   8.242   71.344 1.00 57.26  ? 126 ALA B C   1 
ATOM   3465 O  O   . ALA B  1  113 ? 3.997   9.293   71.862 1.00 56.06  ? 126 ALA B O   1 
ATOM   3466 C  CB  . ALA B  1  113 ? 1.157   8.031   70.911 1.00 56.89  ? 126 ALA B CB  1 
ATOM   3467 N  N   . HIS B  1  114 ? 4.254   7.608   70.349 1.00 55.66  ? 127 HIS B N   1 
ATOM   3468 C  CA  . HIS B  1  114 ? 5.649   7.900   70.049 1.00 52.62  ? 127 HIS B CA  1 
ATOM   3469 C  C   . HIS B  1  114 ? 5.967   7.933   68.551 1.00 48.62  ? 127 HIS B C   1 
ATOM   3470 O  O   . HIS B  1  114 ? 6.815   8.718   68.140 1.00 47.64  ? 127 HIS B O   1 
ATOM   3471 C  CB  . HIS B  1  114 ? 6.542   6.904   70.790 1.00 51.90  ? 127 HIS B CB  1 
ATOM   3472 C  CG  . HIS B  1  114 ? 6.133   5.484   70.615 1.00 52.34  ? 127 HIS B CG  1 
ATOM   3473 N  ND1 . HIS B  1  114 ? 6.417   4.785   69.464 1.00 52.85  ? 127 HIS B ND1 1 
ATOM   3474 C  CD2 . HIS B  1  114 ? 5.479   4.634   71.409 1.00 51.66  ? 127 HIS B CD2 1 
ATOM   3475 C  CE1 . HIS B  1  114 ? 5.979   3.541   69.576 1.00 50.31  ? 127 HIS B CE1 1 
ATOM   3476 N  NE2 . HIS B  1  114 ? 5.411   3.421   70.751 1.00 48.66  ? 127 HIS B NE2 1 
ATOM   3477 N  N   . ALA B  1  115 ? 5.326   7.077   67.743 1.00 46.87  ? 128 ALA B N   1 
ATOM   3478 C  CA  . ALA B  1  115 ? 5.636   6.965   66.322 1.00 42.09  ? 128 ALA B CA  1 
ATOM   3479 C  C   . ALA B  1  115 ? 7.135   6.730   66.129 1.00 40.43  ? 128 ALA B C   1 
ATOM   3480 O  O   . ALA B  1  115 ? 7.750   7.310   65.237 1.00 40.56  ? 128 ALA B O   1 
ATOM   3481 C  CB  . ALA B  1  115 ? 5.173   8.194   65.586 1.00 43.55  ? 128 ALA B CB  1 
ATOM   3482 N  N   . GLY B  1  116 ? 7.688   5.847   66.967 1.00 39.81  ? 129 GLY B N   1 
ATOM   3483 C  CA  . GLY B  1  116 ? 9.124   5.649   67.081 1.00 41.97  ? 129 GLY B CA  1 
ATOM   3484 C  C   . GLY B  1  116 ? 9.653   4.578   66.122 1.00 41.15  ? 129 GLY B C   1 
ATOM   3485 O  O   . GLY B  1  116 ? 10.850  4.318   66.102 1.00 45.23  ? 129 GLY B O   1 
ATOM   3486 N  N   . GLY B  1  117 ? 8.757   3.944   65.352 1.00 39.85  ? 130 GLY B N   1 
ATOM   3487 C  CA  . GLY B  1  117 ? 9.141   3.032   64.288 1.00 40.47  ? 130 GLY B CA  1 
ATOM   3488 C  C   . GLY B  1  117 ? 9.211   1.582   64.758 1.00 41.02  ? 130 GLY B C   1 
ATOM   3489 O  O   . GLY B  1  117 ? 9.028   1.288   65.936 1.00 40.99  ? 130 GLY B O   1 
ATOM   3490 N  N   . LEU B  1  118 ? 9.513   0.682   63.812 1.00 41.78  ? 131 LEU B N   1 
ATOM   3491 C  CA  . LEU B  1  118 ? 9.500   -0.754  64.051 1.00 42.32  ? 131 LEU B CA  1 
ATOM   3492 C  C   . LEU B  1  118 ? 10.564  -1.182  65.063 1.00 43.81  ? 131 LEU B C   1 
ATOM   3493 O  O   . LEU B  1  118 ? 10.497  -2.293  65.580 1.00 42.79  ? 131 LEU B O   1 
ATOM   3494 C  CB  . LEU B  1  118 ? 9.687   -1.471  62.713 1.00 42.73  ? 131 LEU B CB  1 
ATOM   3495 C  CG  . LEU B  1  118 ? 8.576   -1.264  61.680 1.00 45.70  ? 131 LEU B CG  1 
ATOM   3496 C  CD1 . LEU B  1  118 ? 8.832   -2.118  60.463 1.00 45.91  ? 131 LEU B CD1 1 
ATOM   3497 C  CD2 . LEU B  1  118 ? 7.200   -1.569  62.254 1.00 46.34  ? 131 LEU B CD2 1 
ATOM   3498 N  N   . ASN B  1  119 ? 11.552  -0.317  65.329 1.00 43.87  ? 132 ASN B N   1 
ATOM   3499 C  CA  . ASN B  1  119 ? 12.578  -0.590  66.321 1.00 44.84  ? 132 ASN B CA  1 
ATOM   3500 C  C   . ASN B  1  119 ? 12.009  -0.653  67.741 1.00 47.24  ? 132 ASN B C   1 
ATOM   3501 O  O   . ASN B  1  119 ? 12.638  -1.260  68.603 1.00 41.79  ? 132 ASN B O   1 
ATOM   3502 C  CB  . ASN B  1  119 ? 13.694  0.446   66.299 1.00 46.01  ? 132 ASN B CB  1 
ATOM   3503 C  CG  . ASN B  1  119 ? 14.691  0.224   65.186 1.00 48.91  ? 132 ASN B CG  1 
ATOM   3504 O  OD1 . ASN B  1  119 ? 14.505  -0.647  64.327 1.00 48.45  ? 132 ASN B OD1 1 
ATOM   3505 N  ND2 . ASN B  1  119 ? 15.753  1.015   65.172 1.00 48.40  ? 132 ASN B ND2 1 
ATOM   3506 N  N   . VAL B  1  120 ? 10.844  -0.039  68.000 1.00 46.08  ? 133 VAL B N   1 
ATOM   3507 C  CA  . VAL B  1  120 ? 10.298  0.005   69.353 1.00 50.65  ? 133 VAL B CA  1 
ATOM   3508 C  C   . VAL B  1  120 ? 10.001  -1.410  69.856 1.00 49.02  ? 133 VAL B C   1 
ATOM   3509 O  O   . VAL B  1  120 ? 9.251   -2.163  69.233 1.00 46.63  ? 133 VAL B O   1 
ATOM   3510 C  CB  . VAL B  1  120 ? 9.044   0.899   69.454 1.00 51.62  ? 133 VAL B CB  1 
ATOM   3511 C  CG1 . VAL B  1  120 ? 8.365   0.783   70.819 1.00 49.98  ? 133 VAL B CG1 1 
ATOM   3512 C  CG2 . VAL B  1  120 ? 9.370   2.357   69.140 1.00 50.62  ? 133 VAL B CG2 1 
ATOM   3513 N  N   . HIS B  1  121 ? 10.578  -1.737  71.021 1.00 47.97  ? 134 HIS B N   1 
ATOM   3514 C  CA  . HIS B  1  121 ? 10.530  -3.077  71.588 1.00 48.28  ? 134 HIS B CA  1 
ATOM   3515 C  C   . HIS B  1  121 ? 9.305   -3.249  72.484 1.00 47.49  ? 134 HIS B C   1 
ATOM   3516 O  O   . HIS B  1  121 ? 8.906   -2.321  73.174 1.00 43.43  ? 134 HIS B O   1 
ATOM   3517 C  CB  . HIS B  1  121 ? 11.796  -3.329  72.411 1.00 45.85  ? 134 HIS B CB  1 
ATOM   3518 C  CG  . HIS B  1  121 ? 11.790  -4.610  73.166 1.00 47.59  ? 134 HIS B CG  1 
ATOM   3519 N  ND1 . HIS B  1  121 ? 11.973  -5.836  72.565 1.00 46.42  ? 134 HIS B ND1 1 
ATOM   3520 C  CD2 . HIS B  1  121 ? 11.603  -4.859  74.470 1.00 48.51  ? 134 HIS B CD2 1 
ATOM   3521 C  CE1 . HIS B  1  121 ? 11.914  -6.789  73.490 1.00 51.64  ? 134 HIS B CE1 1 
ATOM   3522 N  NE2 . HIS B  1  121 ? 11.690  -6.216  74.656 1.00 48.77  ? 134 HIS B NE2 1 
ATOM   3523 N  N   . GLY B  1  122 ? 8.714   -4.446  72.476 1.00 49.62  ? 135 GLY B N   1 
ATOM   3524 C  CA  . GLY B  1  122 ? 7.911   -4.884  73.606 1.00 52.04  ? 135 GLY B CA  1 
ATOM   3525 C  C   . GLY B  1  122 ? 6.459   -5.195  73.252 1.00 51.85  ? 135 GLY B C   1 
ATOM   3526 O  O   . GLY B  1  122 ? 5.823   -5.961  73.977 1.00 56.35  ? 135 GLY B O   1 
ATOM   3527 N  N   . THR B  1  123 ? 5.920   -4.593  72.183 1.00 53.72  ? 136 THR B N   1 
ATOM   3528 C  CA  . THR B  1  123 ? 4.547   -4.894  71.787 1.00 56.87  ? 136 THR B CA  1 
ATOM   3529 C  C   . THR B  1  123 ? 4.511   -5.558  70.406 1.00 55.82  ? 136 THR B C   1 
ATOM   3530 O  O   . THR B  1  123 ? 3.765   -6.522  70.240 1.00 54.27  ? 136 THR B O   1 
ATOM   3531 C  CB  . THR B  1  123 ? 3.657   -3.651  71.862 1.00 59.83  ? 136 THR B CB  1 
ATOM   3532 O  OG1 . THR B  1  123 ? 4.009   -2.966  73.060 1.00 61.95  ? 136 THR B OG1 1 
ATOM   3533 C  CG2 . THR B  1  123 ? 2.179   -4.003  71.908 1.00 59.03  ? 136 THR B CG2 1 
ATOM   3534 N  N   . PHE B  1  124 ? 5.295   -5.052  69.434 1.00 51.15  ? 137 PHE B N   1 
ATOM   3535 C  CA  . PHE B  1  124 ? 5.504   -5.740  68.161 1.00 49.46  ? 137 PHE B CA  1 
ATOM   3536 C  C   . PHE B  1  124 ? 6.886   -6.410  68.166 1.00 47.68  ? 137 PHE B C   1 
ATOM   3537 O  O   . PHE B  1  124 ? 6.967   -7.617  68.393 1.00 52.37  ? 137 PHE B O   1 
ATOM   3538 C  CB  . PHE B  1  124 ? 5.284   -4.805  66.966 1.00 43.59  ? 137 PHE B CB  1 
ATOM   3539 C  CG  . PHE B  1  124 ? 5.205   -5.444  65.581 1.00 42.36  ? 137 PHE B CG  1 
ATOM   3540 C  CD1 . PHE B  1  124 ? 5.471   -6.796  65.368 1.00 44.55  ? 137 PHE B CD1 1 
ATOM   3541 C  CD2 . PHE B  1  124 ? 4.893   -4.665  64.470 1.00 43.19  ? 137 PHE B CD2 1 
ATOM   3542 C  CE1 . PHE B  1  124 ? 5.397   -7.349  64.092 1.00 45.72  ? 137 PHE B CE1 1 
ATOM   3543 C  CE2 . PHE B  1  124 ? 4.803   -5.224  63.203 1.00 43.10  ? 137 PHE B CE2 1 
ATOM   3544 C  CZ  . PHE B  1  124 ? 5.061   -6.562  63.013 1.00 43.67  ? 137 PHE B CZ  1 
ATOM   3545 N  N   . GLU B  1  125 ? 7.963   -5.649  67.901 1.00 48.15  ? 138 GLU B N   1 
ATOM   3546 C  CA  . GLU B  1  125 ? 9.312   -6.209  67.868 1.00 45.06  ? 138 GLU B CA  1 
ATOM   3547 C  C   . GLU B  1  125 ? 9.595   -6.937  69.185 1.00 42.84  ? 138 GLU B C   1 
ATOM   3548 O  O   . GLU B  1  125 ? 9.279   -6.414  70.249 1.00 45.02  ? 138 GLU B O   1 
ATOM   3549 C  CB  . GLU B  1  125 ? 10.360  -5.117  67.640 1.00 47.74  ? 138 GLU B CB  1 
ATOM   3550 C  CG  . GLU B  1  125 ? 11.790  -5.630  67.439 1.00 47.91  ? 138 GLU B CG  1 
ATOM   3551 C  CD  . GLU B  1  125 ? 12.501  -6.204  68.658 1.00 51.15  ? 138 GLU B CD  1 
ATOM   3552 O  OE1 . GLU B  1  125 ? 12.298  -5.596  69.730 1.00 50.47  ? 138 GLU B OE1 1 
ATOM   3553 O  OE2 . GLU B  1  125 ? 13.245  -7.215  68.549 1.00 54.03  ? 138 GLU B OE2 1 
ATOM   3554 N  N   . GLY B  1  126 ? 10.203  -8.127  69.104 1.00 41.14  ? 139 GLY B N   1 
ATOM   3555 C  CA  . GLY B  1  126 ? 10.480  -8.938  70.279 1.00 42.99  ? 139 GLY B CA  1 
ATOM   3556 C  C   . GLY B  1  126 ? 11.685  -9.872  70.106 1.00 45.42  ? 139 GLY B C   1 
ATOM   3557 O  O   . GLY B  1  126 ? 12.470  -9.739  69.169 1.00 48.12  ? 139 GLY B O   1 
ATOM   3558 N  N   . ASP B  1  127 ? 11.767  -10.858 71.008 1.00 43.64  ? 140 ASP B N   1 
ATOM   3559 C  CA  . ASP B  1  127 ? 12.987  -11.596 71.297 1.00 46.05  ? 140 ASP B CA  1 
ATOM   3560 C  C   . ASP B  1  127 ? 13.087  -12.891 70.479 1.00 41.94  ? 140 ASP B C   1 
ATOM   3561 O  O   . ASP B  1  127 ? 12.126  -13.331 69.861 1.00 38.21  ? 140 ASP B O   1 
ATOM   3562 C  CB  . ASP B  1  127 ? 13.078  -11.891 72.790 1.00 42.69  ? 140 ASP B CB  1 
ATOM   3563 C  CG  . ASP B  1  127 ? 13.089  -10.678 73.711 1.00 42.32  ? 140 ASP B CG  1 
ATOM   3564 O  OD1 . ASP B  1  127 ? 13.707  -9.651  73.339 1.00 41.93  ? 140 ASP B OD1 1 
ATOM   3565 O  OD2 . ASP B  1  127 ? 12.494  -10.773 74.809 1.00 43.57  ? 140 ASP B OD2 1 
ATOM   3566 N  N   . ALA B  1  128 ? 14.276  -13.499 70.518 1.00 41.51  ? 141 ALA B N   1 
ATOM   3567 C  CA  . ALA B  1  128 ? 14.583  -14.785 69.902 1.00 42.64  ? 141 ALA B CA  1 
ATOM   3568 C  C   . ALA B  1  128 ? 14.447  -14.732 68.379 1.00 41.32  ? 141 ALA B C   1 
ATOM   3569 O  O   . ALA B  1  128 ? 13.991  -15.684 67.753 1.00 45.09  ? 141 ALA B O   1 
ATOM   3570 C  CB  . ALA B  1  128 ? 13.738  -15.890 70.504 1.00 41.60  ? 141 ALA B CB  1 
ATOM   3571 N  N   . GLY B  1  129 ? 14.890  -13.628 67.777 1.00 43.47  ? 142 GLY B N   1 
ATOM   3572 C  CA  . GLY B  1  129 ? 14.951  -13.512 66.328 1.00 42.29  ? 142 GLY B CA  1 
ATOM   3573 C  C   . GLY B  1  129 ? 16.135  -14.298 65.774 1.00 43.68  ? 142 GLY B C   1 
ATOM   3574 O  O   . GLY B  1  129 ? 16.983  -14.757 66.538 1.00 39.75  ? 142 GLY B O   1 
ATOM   3575 N  N   . MET B  1  130 ? 16.174  -14.440 64.439 1.00 40.53  ? 143 MET B N   1 
ATOM   3576 C  CA  . MET B  1  130 ? 17.141  -15.296 63.776 1.00 40.20  ? 143 MET B CA  1 
ATOM   3577 C  C   . MET B  1  130 ? 18.469  -14.573 63.581 1.00 41.39  ? 143 MET B C   1 
ATOM   3578 O  O   . MET B  1  130 ? 19.520  -15.151 63.850 1.00 44.09  ? 143 MET B O   1 
ATOM   3579 C  CB  . MET B  1  130 ? 16.622  -15.767 62.419 1.00 41.10  ? 143 MET B CB  1 
ATOM   3580 C  CG  . MET B  1  130 ? 15.498  -16.782 62.515 1.00 44.87  ? 143 MET B CG  1 
ATOM   3581 S  SD  . MET B  1  130 ? 14.782  -17.182 60.908 1.00 43.13  ? 143 MET B SD  1 
ATOM   3582 C  CE  . MET B  1  130 ? 14.133  -15.563 60.476 1.00 42.60  ? 143 MET B CE  1 
ATOM   3583 N  N   . THR B  1  131 ? 18.417  -13.329 63.082 1.00 41.39  ? 144 THR B N   1 
ATOM   3584 C  CA  . THR B  1  131 ? 19.627  -12.591 62.769 1.00 37.83  ? 144 THR B CA  1 
ATOM   3585 C  C   . THR B  1  131 ? 19.726  -11.300 63.583 1.00 40.65  ? 144 THR B C   1 
ATOM   3586 O  O   . THR B  1  131 ? 20.708  -10.576 63.427 1.00 37.53  ? 144 THR B O   1 
ATOM   3587 C  CB  . THR B  1  131 ? 19.719  -12.323 61.267 1.00 36.92  ? 144 THR B CB  1 
ATOM   3588 O  OG1 . THR B  1  131 ? 18.797  -11.304 60.908 1.00 37.24  ? 144 THR B OG1 1 
ATOM   3589 C  CG2 . THR B  1  131 ? 19.508  -13.584 60.443 1.00 34.95  ? 144 THR B CG2 1 
ATOM   3590 N  N   . ARG B  1  132 ? 18.739  -11.017 64.447 1.00 40.69  ? 145 ARG B N   1 
ATOM   3591 C  CA  . ARG B  1  132 ? 18.808  -9.864  65.338 1.00 43.48  ? 145 ARG B CA  1 
ATOM   3592 C  C   . ARG B  1  132 ? 18.826  -10.321 66.796 1.00 42.34  ? 145 ARG B C   1 
ATOM   3593 O  O   . ARG B  1  132 ? 18.172  -11.297 67.141 1.00 41.22  ? 145 ARG B O   1 
ATOM   3594 C  CB  . ARG B  1  132 ? 17.644  -8.899  65.096 1.00 45.38  ? 145 ARG B CB  1 
ATOM   3595 C  CG  . ARG B  1  132 ? 17.881  -7.833  64.037 1.00 45.46  ? 145 ARG B CG  1 
ATOM   3596 C  CD  . ARG B  1  132 ? 18.045  -8.374  62.623 1.00 45.47  ? 145 ARG B CD  1 
ATOM   3597 N  NE  . ARG B  1  132 ? 18.301  -7.277  61.685 1.00 44.16  ? 145 ARG B NE  1 
ATOM   3598 C  CZ  . ARG B  1  132 ? 18.743  -7.425  60.438 1.00 45.04  ? 145 ARG B CZ  1 
ATOM   3599 N  NH1 . ARG B  1  132 ? 18.879  -8.639  59.910 1.00 42.65  ? 145 ARG B NH1 1 
ATOM   3600 N  NH2 . ARG B  1  132 ? 19.049  -6.357  59.720 1.00 42.99  ? 145 ARG B NH2 1 
ATOM   3601 N  N   . ALA B  1  133 ? 19.586  -9.598  67.634 1.00 44.58  ? 146 ALA B N   1 
ATOM   3602 C  CA  . ALA B  1  133 ? 19.743  -9.927  69.045 1.00 44.35  ? 146 ALA B CA  1 
ATOM   3603 C  C   . ALA B  1  133 ? 18.597  -9.297  69.839 1.00 42.71  ? 146 ALA B C   1 
ATOM   3604 O  O   . ALA B  1  133 ? 18.030  -8.294  69.413 1.00 36.43  ? 146 ALA B O   1 
ATOM   3605 N  N   . ASP B  1  134 ? 18.280  -9.885  71.000 1.00 43.85  ? 147 ASP B N   1 
ATOM   3606 C  CA  . ASP B  1  134 ? 17.233  -9.372  71.875 1.00 46.65  ? 147 ASP B CA  1 
ATOM   3607 C  C   . ASP B  1  134 ? 17.598  -7.964  72.334 1.00 45.42  ? 147 ASP B C   1 
ATOM   3608 O  O   . ASP B  1  134 ? 18.776  -7.650  72.514 1.00 43.84  ? 147 ASP B O   1 
ATOM   3609 C  CB  . ASP B  1  134 ? 17.009  -10.272 73.083 1.00 45.09  ? 147 ASP B CB  1 
ATOM   3610 C  CG  . ASP B  1  134 ? 16.611  -11.705 72.769 1.00 47.54  ? 147 ASP B CG  1 
ATOM   3611 O  OD1 . ASP B  1  134 ? 16.558  -12.052 71.564 1.00 47.59  ? 147 ASP B OD1 1 
ATOM   3612 O  OD2 . ASP B  1  134 ? 16.350  -12.463 73.733 1.00 46.45  ? 147 ASP B OD2 1 
ATOM   3613 N  N   . GLU B  1  135 ? 16.567  -7.131  72.528 1.00 44.60  ? 148 GLU B N   1 
ATOM   3614 C  CA  . GLU B  1  135 ? 16.743  -5.741  72.922 1.00 49.87  ? 148 GLU B CA  1 
ATOM   3615 C  C   . GLU B  1  135 ? 17.521  -5.611  74.235 1.00 48.99  ? 148 GLU B C   1 
ATOM   3616 O  O   . GLU B  1  135 ? 18.225  -4.624  74.420 1.00 46.63  ? 148 GLU B O   1 
ATOM   3617 C  CB  . GLU B  1  135 ? 15.379  -5.062  73.028 1.00 53.43  ? 148 GLU B CB  1 
ATOM   3618 C  CG  . GLU B  1  135 ? 15.451  -3.555  73.276 1.00 56.41  ? 148 GLU B CG  1 
ATOM   3619 C  CD  . GLU B  1  135 ? 15.430  -3.116  74.732 1.00 61.00  ? 148 GLU B CD  1 
ATOM   3620 O  OE1 . GLU B  1  135 ? 15.370  -3.965  75.647 1.00 60.09  ? 148 GLU B OE1 1 
ATOM   3621 O  OE2 . GLU B  1  135 ? 15.463  -1.886  74.943 1.00 66.18  ? 148 GLU B OE2 1 
ATOM   3622 N  N   . PHE B  1  136 ? 17.385  -6.591  75.141 1.00 50.24  ? 149 PHE B N   1 
ATOM   3623 C  CA  . PHE B  1  136 ? 18.074  -6.561  76.421 1.00 55.22  ? 149 PHE B CA  1 
ATOM   3624 C  C   . PHE B  1  136 ? 19.579  -6.372  76.223 1.00 54.21  ? 149 PHE B C   1 
ATOM   3625 O  O   . PHE B  1  136 ? 20.217  -5.730  77.048 1.00 56.65  ? 149 PHE B O   1 
ATOM   3626 C  CB  . PHE B  1  136 ? 17.827  -7.838  77.232 1.00 58.04  ? 149 PHE B CB  1 
ATOM   3627 C  CG  . PHE B  1  136 ? 18.640  -7.897  78.521 1.00 62.34  ? 149 PHE B CG  1 
ATOM   3628 C  CD1 . PHE B  1  136 ? 18.278  -7.121  79.615 1.00 64.36  ? 149 PHE B CD1 1 
ATOM   3629 C  CD2 . PHE B  1  136 ? 19.763  -8.712  78.633 1.00 61.24  ? 149 PHE B CD2 1 
ATOM   3630 C  CE1 . PHE B  1  136 ? 19.009  -7.165  80.792 1.00 64.54  ? 149 PHE B CE1 1 
ATOM   3631 C  CE2 . PHE B  1  136 ? 20.500  -8.744  79.809 1.00 63.72  ? 149 PHE B CE2 1 
ATOM   3632 C  CZ  . PHE B  1  136 ? 20.119  -7.977  80.887 1.00 62.28  ? 149 PHE B CZ  1 
ATOM   3633 N  N   . PHE B  1  137 ? 20.143  -6.942  75.147 1.00 50.55  ? 150 PHE B N   1 
ATOM   3634 C  CA  . PHE B  1  137 ? 21.580  -6.918  74.923 1.00 50.63  ? 150 PHE B CA  1 
ATOM   3635 C  C   . PHE B  1  137 ? 22.019  -5.607  74.266 1.00 46.87  ? 150 PHE B C   1 
ATOM   3636 O  O   . PHE B  1  137 ? 23.215  -5.400  74.098 1.00 44.94  ? 150 PHE B O   1 
ATOM   3637 C  CB  . PHE B  1  137 ? 21.981  -8.142  74.094 1.00 50.55  ? 150 PHE B CB  1 
ATOM   3638 C  CG  . PHE B  1  137 ? 21.609  -9.469  74.738 1.00 51.18  ? 150 PHE B CG  1 
ATOM   3639 C  CD1 . PHE B  1  137 ? 22.063  -9.786  76.012 1.00 56.61  ? 150 PHE B CD1 1 
ATOM   3640 C  CD2 . PHE B  1  137 ? 20.793  -10.390 74.085 1.00 52.22  ? 150 PHE B CD2 1 
ATOM   3641 C  CE1 . PHE B  1  137 ? 21.725  -11.003 76.605 1.00 57.53  ? 150 PHE B CE1 1 
ATOM   3642 C  CE2 . PHE B  1  137 ? 20.441  -11.586 74.689 1.00 52.92  ? 150 PHE B CE2 1 
ATOM   3643 C  CZ  . PHE B  1  137 ? 20.912  -11.897 75.939 1.00 54.79  ? 150 PHE B CZ  1 
ATOM   3644 N  N   . GLY B  1  138 ? 21.076  -4.737  73.870 1.00 44.60  ? 151 GLY B N   1 
ATOM   3645 C  CA  . GLY B  1  138 ? 21.416  -3.353  73.564 1.00 46.19  ? 151 GLY B CA  1 
ATOM   3646 C  C   . GLY B  1  138 ? 21.176  -2.937  72.110 1.00 49.85  ? 151 GLY B C   1 
ATOM   3647 O  O   . GLY B  1  138 ? 21.295  -1.756  71.796 1.00 49.09  ? 151 GLY B O   1 
ATOM   3648 N  N   . ASP B  1  139 ? 20.835  -3.875  71.218 1.00 48.80  ? 152 ASP B N   1 
ATOM   3649 C  CA  . ASP B  1  139 ? 20.615  -3.539  69.815 1.00 49.56  ? 152 ASP B CA  1 
ATOM   3650 C  C   . ASP B  1  139 ? 19.723  -4.595  69.166 1.00 45.61  ? 152 ASP B C   1 
ATOM   3651 O  O   . ASP B  1  139 ? 20.177  -5.710  68.890 1.00 45.76  ? 152 ASP B O   1 
ATOM   3652 C  CB  . ASP B  1  139 ? 21.926  -3.410  69.051 1.00 52.41  ? 152 ASP B CB  1 
ATOM   3653 C  CG  . ASP B  1  139 ? 21.813  -3.090  67.567 1.00 52.07  ? 152 ASP B CG  1 
ATOM   3654 O  OD1 . ASP B  1  139 ? 20.685  -3.080  67.046 1.00 52.22  ? 152 ASP B OD1 1 
ATOM   3655 O  OD2 . ASP B  1  139 ? 22.857  -2.843  66.939 1.00 53.20  ? 152 ASP B OD2 1 
ATOM   3656 N  N   . ASN B  1  140 ? 18.468  -4.206  68.898 1.00 40.30  ? 153 ASN B N   1 
ATOM   3657 C  CA  . ASN B  1  140 ? 17.444  -5.136  68.459 1.00 43.34  ? 153 ASN B CA  1 
ATOM   3658 C  C   . ASN B  1  140 ? 17.224  -5.040  66.946 1.00 43.60  ? 153 ASN B C   1 
ATOM   3659 O  O   . ASN B  1  140 ? 16.311  -5.689  66.436 1.00 43.80  ? 153 ASN B O   1 
ATOM   3660 C  CB  . ASN B  1  140 ? 16.129  -4.910  69.201 1.00 42.52  ? 153 ASN B CB  1 
ATOM   3661 C  CG  . ASN B  1  140 ? 15.483  -3.586  68.857 1.00 43.01  ? 153 ASN B CG  1 
ATOM   3662 O  OD1 . ASN B  1  140 ? 16.111  -2.717  68.243 1.00 44.71  ? 153 ASN B OD1 1 
ATOM   3663 N  ND2 . ASN B  1  140 ? 14.238  -3.402  69.267 1.00 42.54  ? 153 ASN B ND2 1 
ATOM   3664 N  N   . HIS B  1  141 ? 18.048  -4.246  66.242 1.00 43.40  ? 154 HIS B N   1 
ATOM   3665 C  CA  . HIS B  1  141 ? 17.770  -3.878  64.857 1.00 47.16  ? 154 HIS B CA  1 
ATOM   3666 C  C   . HIS B  1  141 ? 18.905  -4.266  63.897 1.00 44.03  ? 154 HIS B C   1 
ATOM   3667 O  O   . HIS B  1  141 ? 18.630  -4.611  62.749 1.00 42.30  ? 154 HIS B O   1 
ATOM   3668 C  CB  . HIS B  1  141 ? 17.396  -2.392  64.755 1.00 47.44  ? 154 HIS B CB  1 
ATOM   3669 C  CG  . HIS B  1  141 ? 18.406  -1.477  65.345 1.00 52.89  ? 154 HIS B CG  1 
ATOM   3670 N  ND1 . HIS B  1  141 ? 18.285  -1.047  66.648 1.00 56.49  ? 154 HIS B ND1 1 
ATOM   3671 C  CD2 . HIS B  1  141 ? 19.556  -0.953  64.883 1.00 55.62  ? 154 HIS B CD2 1 
ATOM   3672 C  CE1 . HIS B  1  141 ? 19.306  -0.248  66.935 1.00 59.10  ? 154 HIS B CE1 1 
ATOM   3673 N  NE2 . HIS B  1  141 ? 20.088  -0.180  65.878 1.00 56.48  ? 154 HIS B NE2 1 
ATOM   3674 N  N   . SER B  1  142 ? 20.169  -4.192  64.343 1.00 45.05  ? 155 SER B N   1 
ATOM   3675 C  CA  . SER B  1  142 ? 21.311  -4.506  63.495 1.00 42.64  ? 155 SER B CA  1 
ATOM   3676 C  C   . SER B  1  142 ? 21.414  -6.005  63.216 1.00 41.69  ? 155 SER B C   1 
ATOM   3677 O  O   . SER B  1  142 ? 21.115  -6.831  64.077 1.00 39.37  ? 155 SER B O   1 
ATOM   3678 C  CB  . SER B  1  142 ? 22.601  -4.021  64.111 1.00 44.06  ? 155 SER B CB  1 
ATOM   3679 O  OG  . SER B  1  142 ? 22.605  -2.606  64.241 1.00 47.58  ? 155 SER B OG  1 
ATOM   3680 N  N   . PHE B  1  143 ? 21.920  -6.340  62.026 1.00 40.64  ? 156 PHE B N   1 
ATOM   3681 C  CA  . PHE B  1  143 ? 22.347  -7.695  61.727 1.00 39.71  ? 156 PHE B CA  1 
ATOM   3682 C  C   . PHE B  1  143 ? 23.444  -8.107  62.705 1.00 39.04  ? 156 PHE B C   1 
ATOM   3683 O  O   . PHE B  1  143 ? 24.318  -7.311  63.030 1.00 38.10  ? 156 PHE B O   1 
ATOM   3684 C  CB  . PHE B  1  143 ? 22.838  -7.773  60.281 1.00 36.59  ? 156 PHE B CB  1 
ATOM   3685 C  CG  . PHE B  1  143 ? 23.423  -9.118  59.880 1.00 34.99  ? 156 PHE B CG  1 
ATOM   3686 C  CD1 . PHE B  1  143 ? 22.612  -10.143 59.411 1.00 33.16  ? 156 PHE B CD1 1 
ATOM   3687 C  CD2 . PHE B  1  143 ? 24.790  -9.350  59.966 1.00 37.45  ? 156 PHE B CD2 1 
ATOM   3688 C  CE1 . PHE B  1  143 ? 23.153  -11.363 59.035 1.00 34.93  ? 156 PHE B CE1 1 
ATOM   3689 C  CE2 . PHE B  1  143 ? 25.323  -10.570 59.588 1.00 34.55  ? 156 PHE B CE2 1 
ATOM   3690 C  CZ  . PHE B  1  143 ? 24.512  -11.570 59.116 1.00 34.82  ? 156 PHE B CZ  1 
ATOM   3691 N  N   . ASN B  1  144 ? 23.385  -9.367  63.148 1.00 42.15  ? 157 ASN B N   1 
ATOM   3692 C  CA  . ASN B  1  144 ? 24.305  -9.915  64.126 1.00 42.60  ? 157 ASN B CA  1 
ATOM   3693 C  C   . ASN B  1  144 ? 24.940  -11.167 63.530 1.00 42.20  ? 157 ASN B C   1 
ATOM   3694 O  O   . ASN B  1  144 ? 24.255  -12.166 63.297 1.00 35.38  ? 157 ASN B O   1 
ATOM   3695 C  CB  . ASN B  1  144 ? 23.555  -10.183 65.422 1.00 43.37  ? 157 ASN B CB  1 
ATOM   3696 C  CG  . ASN B  1  144 ? 24.383  -10.848 66.492 1.00 47.98  ? 157 ASN B CG  1 
ATOM   3697 O  OD1 . ASN B  1  144 ? 25.051  -11.856 66.231 1.00 43.66  ? 157 ASN B OD1 1 
ATOM   3698 N  ND2 . ASN B  1  144 ? 24.353  -10.267 67.687 1.00 54.31  ? 157 ASN B ND2 1 
ATOM   3699 N  N   . GLN B  1  145 ? 26.257  -11.090 63.283 1.00 39.27  ? 158 GLN B N   1 
ATOM   3700 C  CA  . GLN B  1  145 ? 26.975  -12.127 62.560 1.00 38.70  ? 158 GLN B CA  1 
ATOM   3701 C  C   . GLN B  1  145 ? 26.983  -13.422 63.372 1.00 36.36  ? 158 GLN B C   1 
ATOM   3702 O  O   . GLN B  1  145 ? 26.863  -14.504 62.804 1.00 37.07  ? 158 GLN B O   1 
ATOM   3703 C  CB  . GLN B  1  145 ? 28.388  -11.636 62.215 1.00 40.64  ? 158 GLN B CB  1 
ATOM   3704 C  CG  . GLN B  1  145 ? 29.218  -12.588 61.355 1.00 40.35  ? 158 GLN B CG  1 
ATOM   3705 C  CD  . GLN B  1  145 ? 28.627  -12.881 59.988 1.00 42.39  ? 158 GLN B CD  1 
ATOM   3706 O  OE1 . GLN B  1  145 ? 28.253  -11.982 59.227 1.00 42.73  ? 158 GLN B OE1 1 
ATOM   3707 N  NE2 . GLN B  1  145 ? 28.571  -14.156 59.634 1.00 43.79  ? 158 GLN B NE2 1 
ATOM   3708 N  N   . THR B  1  146 ? 27.136  -13.311 64.698 1.00 39.09  ? 159 THR B N   1 
ATOM   3709 C  CA  . THR B  1  146 ? 27.183  -14.476 65.574 1.00 39.90  ? 159 THR B CA  1 
ATOM   3710 C  C   . THR B  1  146 ? 25.891  -15.277 65.422 1.00 38.47  ? 159 THR B C   1 
ATOM   3711 O  O   . THR B  1  146 ? 25.928  -16.500 65.342 1.00 40.78  ? 159 THR B O   1 
ATOM   3712 C  CB  . THR B  1  146 ? 27.404  -14.043 67.025 1.00 45.93  ? 159 THR B CB  1 
ATOM   3713 O  OG1 . THR B  1  146 ? 28.628  -13.317 67.049 1.00 51.98  ? 159 THR B OG1 1 
ATOM   3714 C  CG2 . THR B  1  146 ? 27.529  -15.210 67.989 1.00 48.22  ? 159 THR B CG2 1 
ATOM   3715 N  N   . LEU B  1  147 ? 24.749  -14.580 65.352 1.00 35.71  ? 160 LEU B N   1 
ATOM   3716 C  CA  . LEU B  1  147 ? 23.472  -15.251 65.206 1.00 36.87  ? 160 LEU B CA  1 
ATOM   3717 C  C   . LEU B  1  147 ? 23.332  -15.845 63.806 1.00 36.34  ? 160 LEU B C   1 
ATOM   3718 O  O   . LEU B  1  147 ? 22.759  -16.920 63.644 1.00 34.24  ? 160 LEU B O   1 
ATOM   3719 C  CB  . LEU B  1  147 ? 22.346  -14.276 65.536 1.00 37.99  ? 160 LEU B CB  1 
ATOM   3720 C  CG  . LEU B  1  147 ? 22.163  -13.940 67.018 1.00 39.31  ? 160 LEU B CG  1 
ATOM   3721 C  CD1 . LEU B  1  147 ? 20.992  -12.977 67.185 1.00 42.18  ? 160 LEU B CD1 1 
ATOM   3722 C  CD2 . LEU B  1  147 ? 21.956  -15.198 67.844 1.00 39.18  ? 160 LEU B CD2 1 
ATOM   3723 N  N   . PHE B  1  148 ? 23.859  -15.147 62.794 1.00 37.22  ? 161 PHE B N   1 
ATOM   3724 C  CA  . PHE B  1  148 ? 23.813  -15.660 61.434 1.00 37.66  ? 161 PHE B CA  1 
ATOM   3725 C  C   . PHE B  1  148 ? 24.688  -16.912 61.339 1.00 39.52  ? 161 PHE B C   1 
ATOM   3726 O  O   . PHE B  1  148 ? 24.355  -17.839 60.602 1.00 37.48  ? 161 PHE B O   1 
ATOM   3727 C  CB  . PHE B  1  148 ? 24.200  -14.567 60.428 1.00 36.20  ? 161 PHE B CB  1 
ATOM   3728 C  CG  . PHE B  1  148 ? 24.105  -15.048 58.988 1.00 35.65  ? 161 PHE B CG  1 
ATOM   3729 C  CD1 . PHE B  1  148 ? 22.867  -15.144 58.357 1.00 36.40  ? 161 PHE B CD1 1 
ATOM   3730 C  CD2 . PHE B  1  148 ? 25.233  -15.459 58.292 1.00 35.58  ? 161 PHE B CD2 1 
ATOM   3731 C  CE1 . PHE B  1  148 ? 22.768  -15.620 57.058 1.00 36.54  ? 161 PHE B CE1 1 
ATOM   3732 C  CE2 . PHE B  1  148 ? 25.130  -15.932 56.987 1.00 39.32  ? 161 PHE B CE2 1 
ATOM   3733 C  CZ  . PHE B  1  148 ? 23.896  -16.009 56.373 1.00 37.32  ? 161 PHE B CZ  1 
ATOM   3734 N  N   . ASP B  1  149 ? 25.797  -16.942 62.099 1.00 37.83  ? 162 ASP B N   1 
ATOM   3735 C  CA  . ASP B  1  149 ? 26.649  -18.122 62.166 1.00 41.20  ? 162 ASP B CA  1 
ATOM   3736 C  C   . ASP B  1  149 ? 25.859  -19.324 62.694 1.00 40.64  ? 162 ASP B C   1 
ATOM   3737 O  O   . ASP B  1  149 ? 26.041  -20.444 62.215 1.00 41.90  ? 162 ASP B O   1 
ATOM   3738 C  CB  . ASP B  1  149 ? 27.908  -17.851 62.978 1.00 43.77  ? 162 ASP B CB  1 
ATOM   3739 C  CG  . ASP B  1  149 ? 28.890  -16.859 62.361 1.00 49.47  ? 162 ASP B CG  1 
ATOM   3740 O  OD1 . ASP B  1  149 ? 28.864  -16.693 61.122 1.00 48.81  ? 162 ASP B OD1 1 
ATOM   3741 O  OD2 . ASP B  1  149 ? 29.653  -16.226 63.128 1.00 50.46  ? 162 ASP B OD2 1 
ATOM   3742 N  N   . LYS B  1  150 ? 24.982  -19.092 63.678 1.00 38.35  ? 163 LYS B N   1 
ATOM   3743 C  CA  . LYS B  1  150 ? 24.102  -20.133 64.198 1.00 40.93  ? 163 LYS B CA  1 
ATOM   3744 C  C   . LYS B  1  150 ? 23.113  -20.581 63.122 1.00 39.00  ? 163 LYS B C   1 
ATOM   3745 O  O   . LYS B  1  150 ? 22.868  -21.776 62.959 1.00 39.20  ? 163 LYS B O   1 
ATOM   3746 C  CB  . LYS B  1  150 ? 23.366  -19.663 65.460 1.00 44.54  ? 163 LYS B CB  1 
ATOM   3747 C  CG  . LYS B  1  150 ? 22.636  -20.747 66.238 1.00 49.02  ? 163 LYS B CG  1 
ATOM   3748 C  CD  . LYS B  1  150 ? 21.880  -20.196 67.440 1.00 51.69  ? 163 LYS B CD  1 
ATOM   3749 C  CE  . LYS B  1  150 ? 21.028  -21.200 68.158 1.00 52.84  ? 163 LYS B CE  1 
ATOM   3750 N  NZ  . LYS B  1  150 ? 21.710  -21.712 69.345 1.00 55.33  ? 163 LYS B NZ  1 
ATOM   3751 N  N   . PHE B  1  151 ? 22.562  -19.618 62.369 1.00 39.92  ? 164 PHE B N   1 
ATOM   3752 C  CA  . PHE B  1  151 ? 21.686  -19.927 61.245 1.00 38.28  ? 164 PHE B CA  1 
ATOM   3753 C  C   . PHE B  1  151 ? 22.398  -20.875 60.274 1.00 36.91  ? 164 PHE B C   1 
ATOM   3754 O  O   . PHE B  1  151 ? 21.812  -21.850 59.808 1.00 36.78  ? 164 PHE B O   1 
ATOM   3755 C  CB  . PHE B  1  151 ? 21.285  -18.604 60.583 1.00 37.72  ? 164 PHE B CB  1 
ATOM   3756 C  CG  . PHE B  1  151 ? 20.320  -18.675 59.408 1.00 37.92  ? 164 PHE B CG  1 
ATOM   3757 C  CD1 . PHE B  1  151 ? 20.775  -18.886 58.108 1.00 36.34  ? 164 PHE B CD1 1 
ATOM   3758 C  CD2 . PHE B  1  151 ? 18.964  -18.448 59.601 1.00 36.57  ? 164 PHE B CD2 1 
ATOM   3759 C  CE1 . PHE B  1  151 ? 19.889  -18.907 57.045 1.00 38.36  ? 164 PHE B CE1 1 
ATOM   3760 C  CE2 . PHE B  1  151 ? 18.078  -18.477 58.537 1.00 34.62  ? 164 PHE B CE2 1 
ATOM   3761 C  CZ  . PHE B  1  151 ? 18.537  -18.711 57.262 1.00 35.74  ? 164 PHE B CZ  1 
ATOM   3762 N  N   . VAL B  1  152 ? 23.662  -20.569 59.959 1.00 36.74  ? 165 VAL B N   1 
ATOM   3763 C  CA  . VAL B  1  152 ? 24.460  -21.384 59.052 1.00 36.67  ? 165 VAL B CA  1 
ATOM   3764 C  C   . VAL B  1  152 ? 24.704  -22.754 59.689 1.00 34.91  ? 165 VAL B C   1 
ATOM   3765 O  O   . VAL B  1  152 ? 24.558  -23.785 59.043 1.00 35.28  ? 165 VAL B O   1 
ATOM   3766 C  CB  . VAL B  1  152 ? 25.784  -20.679 58.683 1.00 37.01  ? 165 VAL B CB  1 
ATOM   3767 C  CG1 . VAL B  1  152 ? 26.751  -21.590 57.920 1.00 35.92  ? 165 VAL B CG1 1 
ATOM   3768 C  CG2 . VAL B  1  152 ? 25.535  -19.384 57.909 1.00 38.56  ? 165 VAL B CG2 1 
ATOM   3769 N  N   . ASP B  1  153 ? 25.084  -22.771 60.965 1.00 40.22  ? 166 ASP B N   1 
ATOM   3770 C  CA  . ASP B  1  153 ? 25.362  -24.029 61.643 1.00 41.11  ? 166 ASP B CA  1 
ATOM   3771 C  C   . ASP B  1  153 ? 24.135  -24.947 61.568 1.00 40.13  ? 166 ASP B C   1 
ATOM   3772 O  O   . ASP B  1  153 ? 24.246  -26.115 61.198 1.00 39.55  ? 166 ASP B O   1 
ATOM   3773 C  CB  . ASP B  1  153 ? 25.841  -23.782 63.061 1.00 42.17  ? 166 ASP B CB  1 
ATOM   3774 C  CG  . ASP B  1  153 ? 26.212  -25.033 63.841 1.00 45.55  ? 166 ASP B CG  1 
ATOM   3775 O  OD1 . ASP B  1  153 ? 27.022  -25.833 63.313 1.00 47.06  ? 166 ASP B OD1 1 
ATOM   3776 O  OD2 . ASP B  1  153 ? 25.653  -25.205 64.949 1.00 45.33  ? 166 ASP B OD2 1 
ATOM   3777 N  N   . PHE B  1  154 ? 22.959  -24.407 61.903 1.00 37.96  ? 167 PHE B N   1 
ATOM   3778 C  CA  . PHE B  1  154 ? 21.747  -25.214 61.938 1.00 37.76  ? 167 PHE B CA  1 
ATOM   3779 C  C   . PHE B  1  154 ? 21.389  -25.691 60.536 1.00 37.60  ? 167 PHE B C   1 
ATOM   3780 O  O   . PHE B  1  154 ? 20.922  -26.814 60.375 1.00 40.36  ? 167 PHE B O   1 
ATOM   3781 C  CB  . PHE B  1  154 ? 20.615  -24.444 62.622 1.00 37.75  ? 167 PHE B CB  1 
ATOM   3782 C  CG  . PHE B  1  154 ? 20.584  -24.668 64.127 1.00 41.73  ? 167 PHE B CG  1 
ATOM   3783 C  CD1 . PHE B  1  154 ? 21.656  -24.282 64.932 1.00 44.12  ? 167 PHE B CD1 1 
ATOM   3784 C  CD2 . PHE B  1  154 ? 19.486  -25.269 64.731 1.00 45.16  ? 167 PHE B CD2 1 
ATOM   3785 C  CE1 . PHE B  1  154 ? 21.621  -24.482 66.300 1.00 43.96  ? 167 PHE B CE1 1 
ATOM   3786 C  CE2 . PHE B  1  154 ? 19.457  -25.469 66.103 1.00 45.94  ? 167 PHE B CE2 1 
ATOM   3787 C  CZ  . PHE B  1  154 ? 20.526  -25.079 66.882 1.00 44.74  ? 167 PHE B CZ  1 
ATOM   3788 N  N   . SER B  1  155 ? 21.610  -24.828 59.532 1.00 38.72  ? 168 SER B N   1 
ATOM   3789 C  CA  . SER B  1  155 ? 21.419  -25.195 58.139 1.00 38.93  ? 168 SER B CA  1 
ATOM   3790 C  C   . SER B  1  155 ? 22.333  -26.359 57.754 1.00 40.95  ? 168 SER B C   1 
ATOM   3791 O  O   . SER B  1  155 ? 21.926  -27.238 56.994 1.00 43.46  ? 168 SER B O   1 
ATOM   3792 C  CB  . SER B  1  155 ? 21.633  -24.002 57.227 1.00 41.95  ? 168 SER B CB  1 
ATOM   3793 O  OG  . SER B  1  155 ? 20.703  -22.963 57.496 1.00 43.40  ? 168 SER B OG  1 
ATOM   3794 N  N   . ASN B  1  156 ? 23.586  -26.338 58.233 1.00 39.01  ? 169 ASN B N   1 
ATOM   3795 C  CA  . ASN B  1  156 ? 24.513  -27.428 57.976 1.00 40.63  ? 169 ASN B CA  1 
ATOM   3796 C  C   . ASN B  1  156 ? 24.033  -28.714 58.658 1.00 41.18  ? 169 ASN B C   1 
ATOM   3797 O  O   . ASN B  1  156 ? 24.098  -29.787 58.062 1.00 39.58  ? 169 ASN B O   1 
ATOM   3798 C  CB  . ASN B  1  156 ? 25.923  -27.130 58.487 1.00 43.19  ? 169 ASN B CB  1 
ATOM   3799 C  CG  . ASN B  1  156 ? 26.629  -26.048 57.716 1.00 44.00  ? 169 ASN B CG  1 
ATOM   3800 O  OD1 . ASN B  1  156 ? 26.352  -25.826 56.531 1.00 44.08  ? 169 ASN B OD1 1 
ATOM   3801 N  ND2 . ASN B  1  156 ? 27.572  -25.395 58.374 1.00 48.57  ? 169 ASN B ND2 1 
ATOM   3802 N  N   . ARG B  1  157 ? 23.571  -28.603 59.914 1.00 41.64  ? 170 ARG B N   1 
ATOM   3803 C  CA  . ARG B  1  157 ? 23.270  -29.774 60.717 1.00 44.03  ? 170 ARG B CA  1 
ATOM   3804 C  C   . ARG B  1  157 ? 21.975  -30.451 60.272 1.00 46.77  ? 170 ARG B C   1 
ATOM   3805 O  O   . ARG B  1  157 ? 21.856  -31.666 60.419 1.00 48.30  ? 170 ARG B O   1 
ATOM   3806 C  CB  . ARG B  1  157 ? 23.205  -29.391 62.195 1.00 44.94  ? 170 ARG B CB  1 
ATOM   3807 C  CG  . ARG B  1  157 ? 24.584  -29.094 62.753 1.00 48.58  ? 170 ARG B CG  1 
ATOM   3808 C  CD  . ARG B  1  157 ? 24.544  -28.244 64.006 1.00 51.35  ? 170 ARG B CD  1 
ATOM   3809 N  NE  . ARG B  1  157 ? 23.639  -28.796 65.019 1.00 52.93  ? 170 ARG B NE  1 
ATOM   3810 C  CZ  . ARG B  1  157 ? 23.406  -28.225 66.192 1.00 52.24  ? 170 ARG B CZ  1 
ATOM   3811 N  NH1 . ARG B  1  157 ? 22.555  -28.776 67.037 1.00 55.93  ? 170 ARG B NH1 1 
ATOM   3812 N  NH2 . ARG B  1  157 ? 24.023  -27.105 66.525 1.00 50.90  ? 170 ARG B NH2 1 
ATOM   3813 N  N   . TYR B  1  158 ? 21.018  -29.679 59.739 1.00 46.39  ? 171 TYR B N   1 
ATOM   3814 C  CA  . TYR B  1  158 ? 19.663  -30.183 59.544 1.00 44.00  ? 171 TYR B CA  1 
ATOM   3815 C  C   . TYR B  1  158 ? 19.137  -29.986 58.123 1.00 45.11  ? 171 TYR B C   1 
ATOM   3816 O  O   . TYR B  1  158 ? 18.087  -30.538 57.796 1.00 49.46  ? 171 TYR B O   1 
ATOM   3817 C  CB  . TYR B  1  158 ? 18.696  -29.501 60.514 1.00 42.21  ? 171 TYR B CB  1 
ATOM   3818 C  CG  . TYR B  1  158 ? 19.036  -29.754 61.970 1.00 41.43  ? 171 TYR B CG  1 
ATOM   3819 C  CD1 . TYR B  1  158 ? 18.894  -31.024 62.530 1.00 44.55  ? 171 TYR B CD1 1 
ATOM   3820 C  CD2 . TYR B  1  158 ? 19.504  -28.729 62.783 1.00 39.23  ? 171 TYR B CD2 1 
ATOM   3821 C  CE1 . TYR B  1  158 ? 19.217  -31.265 63.858 1.00 43.67  ? 171 TYR B CE1 1 
ATOM   3822 C  CE2 . TYR B  1  158 ? 19.825  -28.957 64.109 1.00 42.18  ? 171 TYR B CE2 1 
ATOM   3823 C  CZ  . TYR B  1  158 ? 19.686  -30.226 64.648 1.00 45.62  ? 171 TYR B CZ  1 
ATOM   3824 O  OH  . TYR B  1  158 ? 20.025  -30.404 65.959 1.00 43.76  ? 171 TYR B OH  1 
ATOM   3825 N  N   . GLY B  1  159 ? 19.829  -29.200 57.284 1.00 46.27  ? 172 GLY B N   1 
ATOM   3826 C  CA  . GLY B  1  159 ? 19.288  -28.853 55.980 1.00 45.30  ? 172 GLY B CA  1 
ATOM   3827 C  C   . GLY B  1  159 ? 20.270  -29.060 54.830 1.00 45.88  ? 172 GLY B C   1 
ATOM   3828 O  O   . GLY B  1  159 ? 20.061  -28.529 53.742 1.00 42.40  ? 172 GLY B O   1 
ATOM   3829 N  N   . GLY B  1  160 ? 21.333  -29.840 55.056 1.00 47.61  ? 173 GLY B N   1 
ATOM   3830 C  CA  . GLY B  1  160 ? 22.282  -30.129 53.994 1.00 46.04  ? 173 GLY B CA  1 
ATOM   3831 C  C   . GLY B  1  160 ? 23.078  -28.896 53.575 1.00 43.30  ? 173 GLY B C   1 
ATOM   3832 O  O   . GLY B  1  160 ? 23.608  -28.858 52.469 1.00 44.51  ? 173 GLY B O   1 
ATOM   3833 N  N   . GLY B  1  161 ? 23.149  -27.891 54.459 1.00 41.57  ? 174 GLY B N   1 
ATOM   3834 C  CA  . GLY B  1  161 ? 23.836  -26.643 54.166 1.00 41.91  ? 174 GLY B CA  1 
ATOM   3835 C  C   . GLY B  1  161 ? 22.896  -25.553 53.636 1.00 42.04  ? 174 GLY B C   1 
ATOM   3836 O  O   . GLY B  1  161 ? 23.355  -24.471 53.267 1.00 39.12  ? 174 GLY B O   1 
ATOM   3837 N  N   . PHE B  1  162 ? 21.585  -25.834 53.639 1.00 41.70  ? 175 PHE B N   1 
ATOM   3838 C  CA  . PHE B  1  162 ? 20.560  -24.904 53.190 1.00 41.52  ? 175 PHE B CA  1 
ATOM   3839 C  C   . PHE B  1  162 ? 19.524  -24.732 54.298 1.00 42.55  ? 175 PHE B C   1 
ATOM   3840 O  O   . PHE B  1  162 ? 19.389  -25.599 55.159 1.00 43.74  ? 175 PHE B O   1 
ATOM   3841 C  CB  . PHE B  1  162 ? 19.868  -25.442 51.933 1.00 42.47  ? 175 PHE B CB  1 
ATOM   3842 C  CG  . PHE B  1  162 ? 20.775  -25.590 50.722 1.00 42.22  ? 175 PHE B CG  1 
ATOM   3843 C  CD1 . PHE B  1  162 ? 20.937  -24.532 49.831 1.00 43.84  ? 175 PHE B CD1 1 
ATOM   3844 C  CD2 . PHE B  1  162 ? 21.457  -26.777 50.473 1.00 43.37  ? 175 PHE B CD2 1 
ATOM   3845 C  CE1 . PHE B  1  162 ? 21.775  -24.657 48.729 1.00 44.29  ? 175 PHE B CE1 1 
ATOM   3846 C  CE2 . PHE B  1  162 ? 22.285  -26.899 49.366 1.00 43.75  ? 175 PHE B CE2 1 
ATOM   3847 C  CZ  . PHE B  1  162 ? 22.439  -25.841 48.493 1.00 44.03  ? 175 PHE B CZ  1 
ATOM   3848 N  N   . TYR B  1  163 ? 18.794  -23.611 54.266 1.00 38.77  ? 176 TYR B N   1 
ATOM   3849 C  CA  . TYR B  1  163 ? 17.724  -23.376 55.218 1.00 38.01  ? 176 TYR B CA  1 
ATOM   3850 C  C   . TYR B  1  163 ? 16.431  -23.908 54.611 1.00 36.73  ? 176 TYR B C   1 
ATOM   3851 O  O   . TYR B  1  163 ? 16.030  -23.464 53.548 1.00 37.97  ? 176 TYR B O   1 
ATOM   3852 C  CB  . TYR B  1  163 ? 17.598  -21.889 55.564 1.00 38.11  ? 176 TYR B CB  1 
ATOM   3853 C  CG  . TYR B  1  163 ? 16.604  -21.538 56.661 1.00 38.66  ? 176 TYR B CG  1 
ATOM   3854 C  CD1 . TYR B  1  163 ? 16.939  -21.679 58.002 1.00 41.90  ? 176 TYR B CD1 1 
ATOM   3855 C  CD2 . TYR B  1  163 ? 15.346  -21.037 56.357 1.00 41.12  ? 176 TYR B CD2 1 
ATOM   3856 C  CE1 . TYR B  1  163 ? 16.045  -21.351 59.006 1.00 41.27  ? 176 TYR B CE1 1 
ATOM   3857 C  CE2 . TYR B  1  163 ? 14.446  -20.691 57.355 1.00 41.61  ? 176 TYR B CE2 1 
ATOM   3858 C  CZ  . TYR B  1  163 ? 14.795  -20.849 58.684 1.00 42.23  ? 176 TYR B CZ  1 
ATOM   3859 O  OH  . TYR B  1  163 ? 13.898  -20.510 59.659 1.00 38.13  ? 176 TYR B OH  1 
ATOM   3860 N  N   . ASN B  1  164 ? 15.824  -24.881 55.294 1.00 39.67  ? 177 ASN B N   1 
ATOM   3861 C  CA  . ASN B  1  164 ? 14.553  -25.456 54.893 1.00 41.98  ? 177 ASN B CA  1 
ATOM   3862 C  C   . ASN B  1  164 ? 13.696  -25.601 56.147 1.00 40.71  ? 177 ASN B C   1 
ATOM   3863 O  O   . ASN B  1  164 ? 14.116  -25.186 57.229 1.00 38.97  ? 177 ASN B O   1 
ATOM   3864 C  CB  . ASN B  1  164 ? 14.770  -26.734 54.085 1.00 43.96  ? 177 ASN B CB  1 
ATOM   3865 C  CG  . ASN B  1  164 ? 15.154  -27.932 54.921 1.00 43.28  ? 177 ASN B CG  1 
ATOM   3866 O  OD1 . ASN B  1  164 ? 15.156  -27.888 56.158 1.00 40.98  ? 177 ASN B OD1 1 
ATOM   3867 N  ND2 . ASN B  1  164 ? 15.487  -29.017 54.241 1.00 48.51  ? 177 ASN B ND2 1 
ATOM   3868 N  N   . LEU B  1  165 ? 12.513  -26.210 55.998 1.00 39.96  ? 178 LEU B N   1 
ATOM   3869 C  CA  . LEU B  1  165 ? 11.520  -26.199 57.061 1.00 42.23  ? 178 LEU B CA  1 
ATOM   3870 C  C   . LEU B  1  165 ? 11.994  -27.009 58.269 1.00 39.78  ? 178 LEU B C   1 
ATOM   3871 O  O   . LEU B  1  165 ? 11.691  -26.657 59.403 1.00 37.99  ? 178 LEU B O   1 
ATOM   3872 C  CB  . LEU B  1  165 ? 10.183  -26.698 56.509 1.00 46.51  ? 178 LEU B CB  1 
ATOM   3873 C  CG  . LEU B  1  165 ? 8.964   -26.462 57.403 1.00 51.19  ? 178 LEU B CG  1 
ATOM   3874 C  CD1 . LEU B  1  165 ? 8.677   -24.985 57.611 1.00 53.68  ? 178 LEU B CD1 1 
ATOM   3875 C  CD2 . LEU B  1  165 ? 7.746   -27.141 56.797 1.00 54.57  ? 178 LEU B CD2 1 
ATOM   3876 N  N   . THR B  1  166 ? 12.762  -28.082 58.038 1.00 44.03  ? 179 THR B N   1 
ATOM   3877 C  CA  . THR B  1  166 ? 13.357  -28.839 59.137 1.00 43.65  ? 179 THR B CA  1 
ATOM   3878 C  C   . THR B  1  166 ? 14.266  -27.931 59.967 1.00 43.18  ? 179 THR B C   1 
ATOM   3879 O  O   . THR B  1  166 ? 14.235  -27.961 61.196 1.00 44.25  ? 179 THR B O   1 
ATOM   3880 C  CB  . THR B  1  166 ? 14.122  -30.045 58.590 1.00 43.48  ? 179 THR B CB  1 
ATOM   3881 O  OG1 . THR B  1  166 ? 13.262  -30.697 57.653 1.00 44.65  ? 179 THR B OG1 1 
ATOM   3882 C  CG2 . THR B  1  166 ? 14.533  -31.018 59.683 1.00 43.79  ? 179 THR B CG2 1 
ATOM   3883 N  N   . VAL B  1  167 ? 15.069  -27.106 59.287 1.00 43.46  ? 180 VAL B N   1 
ATOM   3884 C  CA  . VAL B  1  167 ? 16.028  -26.238 59.963 1.00 42.36  ? 180 VAL B CA  1 
ATOM   3885 C  C   . VAL B  1  167 ? 15.274  -25.194 60.786 1.00 40.07  ? 180 VAL B C   1 
ATOM   3886 O  O   . VAL B  1  167 ? 15.674  -24.873 61.906 1.00 37.81  ? 180 VAL B O   1 
ATOM   3887 C  CB  . VAL B  1  167 ? 16.994  -25.549 58.977 1.00 41.31  ? 180 VAL B CB  1 
ATOM   3888 C  CG1 . VAL B  1  167 ? 18.041  -24.711 59.698 1.00 42.41  ? 180 VAL B CG1 1 
ATOM   3889 C  CG2 . VAL B  1  167 ? 17.668  -26.555 58.049 1.00 44.10  ? 180 VAL B CG2 1 
ATOM   3890 N  N   . ALA B  1  168 ? 14.185  -24.660 60.211 1.00 42.45  ? 181 ALA B N   1 
ATOM   3891 C  CA  . ALA B  1  168 ? 13.363  -23.657 60.871 1.00 40.77  ? 181 ALA B CA  1 
ATOM   3892 C  C   . ALA B  1  168 ? 12.872  -24.180 62.218 1.00 39.51  ? 181 ALA B C   1 
ATOM   3893 O  O   . ALA B  1  168 ? 12.967  -23.481 63.222 1.00 38.41  ? 181 ALA B O   1 
ATOM   3894 C  CB  . ALA B  1  168 ? 12.209  -23.268 59.970 1.00 39.83  ? 181 ALA B CB  1 
ATOM   3895 N  N   . GLY B  1  169 ? 12.355  -25.415 62.230 1.00 41.68  ? 182 GLY B N   1 
ATOM   3896 C  CA  . GLY B  1  169 ? 11.878  -26.032 63.457 1.00 43.18  ? 182 GLY B CA  1 
ATOM   3897 C  C   . GLY B  1  169 ? 12.954  -26.071 64.540 1.00 42.82  ? 182 GLY B C   1 
ATOM   3898 O  O   . GLY B  1  169 ? 12.703  -25.718 65.689 1.00 44.50  ? 182 GLY B O   1 
ATOM   3899 N  N   . GLU B  1  170 ? 14.164  -26.486 64.155 1.00 44.17  ? 183 GLU B N   1 
ATOM   3900 C  CA  . GLU B  1  170 ? 15.254  -26.641 65.107 1.00 44.76  ? 183 GLU B CA  1 
ATOM   3901 C  C   . GLU B  1  170 ? 15.765  -25.272 65.564 1.00 44.51  ? 183 GLU B C   1 
ATOM   3902 O  O   . GLU B  1  170 ? 16.015  -25.075 66.748 1.00 40.66  ? 183 GLU B O   1 
ATOM   3903 C  CB  . GLU B  1  170 ? 16.369  -27.494 64.499 1.00 49.23  ? 183 GLU B CB  1 
ATOM   3904 C  CG  . GLU B  1  170 ? 15.953  -28.934 64.197 1.00 51.05  ? 183 GLU B CG  1 
ATOM   3905 C  CD  . GLU B  1  170 ? 15.300  -29.647 65.363 1.00 55.57  ? 183 GLU B CD  1 
ATOM   3906 O  OE1 . GLU B  1  170 ? 15.918  -29.674 66.438 1.00 50.79  ? 183 GLU B OE1 1 
ATOM   3907 O  OE2 . GLU B  1  170 ? 14.155  -30.124 65.209 1.00 67.32  ? 183 GLU B OE2 1 
ATOM   3908 N  N   . LEU B  1  171 ? 15.919  -24.324 64.628 1.00 44.33  ? 184 LEU B N   1 
ATOM   3909 C  CA  . LEU B  1  171 ? 16.542  -23.051 64.951 1.00 43.06  ? 184 LEU B CA  1 
ATOM   3910 C  C   . LEU B  1  171 ? 15.631  -22.238 65.865 1.00 41.60  ? 184 LEU B C   1 
ATOM   3911 O  O   . LEU B  1  171 ? 16.106  -21.596 66.798 1.00 40.82  ? 184 LEU B O   1 
ATOM   3912 C  CB  . LEU B  1  171 ? 16.880  -22.278 63.673 1.00 45.39  ? 184 LEU B CB  1 
ATOM   3913 C  CG  . LEU B  1  171 ? 17.526  -20.899 63.872 1.00 45.36  ? 184 LEU B CG  1 
ATOM   3914 C  CD1 . LEU B  1  171 ? 18.881  -21.000 64.567 1.00 44.39  ? 184 LEU B CD1 1 
ATOM   3915 C  CD2 . LEU B  1  171 ? 17.645  -20.169 62.544 1.00 43.88  ? 184 LEU B CD2 1 
ATOM   3916 N  N   . ARG B  1  172 ? 14.325  -22.250 65.577 1.00 42.02  ? 185 ARG B N   1 
ATOM   3917 C  CA  . ARG B  1  172 ? 13.357  -21.470 66.336 1.00 43.78  ? 185 ARG B CA  1 
ATOM   3918 C  C   . ARG B  1  172 ? 13.440  -21.866 67.809 1.00 46.77  ? 185 ARG B C   1 
ATOM   3919 O  O   . ARG B  1  172 ? 13.545  -21.007 68.686 1.00 42.30  ? 185 ARG B O   1 
ATOM   3920 C  CB  . ARG B  1  172 ? 11.966  -21.674 65.716 1.00 46.40  ? 185 ARG B CB  1 
ATOM   3921 C  CG  . ARG B  1  172 ? 10.740  -21.372 66.566 1.00 48.91  ? 185 ARG B CG  1 
ATOM   3922 C  CD  . ARG B  1  172 ? 10.725  -19.998 67.221 1.00 48.64  ? 185 ARG B CD  1 
ATOM   3923 N  NE  . ARG B  1  172 ? 11.075  -18.909 66.304 1.00 49.76  ? 185 ARG B NE  1 
ATOM   3924 C  CZ  . ARG B  1  172 ? 11.954  -17.944 66.541 1.00 46.37  ? 185 ARG B CZ  1 
ATOM   3925 N  NH1 . ARG B  1  172 ? 12.654  -17.927 67.668 1.00 46.59  ? 185 ARG B NH1 1 
ATOM   3926 N  NH2 . ARG B  1  172 ? 12.141  -17.001 65.635 1.00 48.35  ? 185 ARG B NH2 1 
ATOM   3927 N  N   . TYR B  1  173 ? 13.388  -23.178 68.068 1.00 47.25  ? 186 TYR B N   1 
ATOM   3928 C  CA  . TYR B  1  173 ? 13.431  -23.692 69.428 1.00 48.27  ? 186 TYR B CA  1 
ATOM   3929 C  C   . TYR B  1  173 ? 14.751  -23.317 70.100 1.00 47.03  ? 186 TYR B C   1 
ATOM   3930 O  O   . TYR B  1  173 ? 14.764  -22.869 71.244 1.00 47.30  ? 186 TYR B O   1 
ATOM   3931 C  CB  . TYR B  1  173 ? 13.206  -25.208 69.381 1.00 51.62  ? 186 TYR B CB  1 
ATOM   3932 C  CG  . TYR B  1  173 ? 13.194  -25.868 70.749 1.00 56.66  ? 186 TYR B CG  1 
ATOM   3933 C  CD1 . TYR B  1  173 ? 12.171  -25.594 71.644 1.00 63.54  ? 186 TYR B CD1 1 
ATOM   3934 C  CD2 . TYR B  1  173 ? 14.185  -26.759 71.145 1.00 60.42  ? 186 TYR B CD2 1 
ATOM   3935 C  CE1 . TYR B  1  173 ? 12.136  -26.177 72.901 1.00 63.35  ? 186 TYR B CE1 1 
ATOM   3936 C  CE2 . TYR B  1  173 ? 14.167  -27.342 72.401 1.00 62.78  ? 186 TYR B CE2 1 
ATOM   3937 C  CZ  . TYR B  1  173 ? 13.135  -27.055 73.278 1.00 62.69  ? 186 TYR B CZ  1 
ATOM   3938 O  OH  . TYR B  1  173 ? 13.079  -27.635 74.509 1.00 65.84  ? 186 TYR B OH  1 
ATOM   3939 N  N   . SER B  1  174 ? 15.867  -23.503 69.389 1.00 43.39  ? 187 SER B N   1 
ATOM   3940 C  CA  . SER B  1  174 ? 17.181  -23.268 69.972 1.00 43.05  ? 187 SER B CA  1 
ATOM   3941 C  C   . SER B  1  174 ? 17.352  -21.799 70.353 1.00 46.70  ? 187 SER B C   1 
ATOM   3942 O  O   . SER B  1  174 ? 17.927  -21.497 71.405 1.00 42.14  ? 187 SER B O   1 
ATOM   3943 C  CB  . SER B  1  174 ? 18.269  -23.716 69.041 1.00 45.02  ? 187 SER B CB  1 
ATOM   3944 O  OG  . SER B  1  174 ? 19.542  -23.474 69.624 1.00 46.23  ? 187 SER B OG  1 
ATOM   3945 N  N   . ARG B  1  175 ? 16.823  -20.897 69.507 1.00 46.43  ? 188 ARG B N   1 
ATOM   3946 C  CA  . ARG B  1  175 ? 16.892  -19.466 69.768 1.00 45.47  ? 188 ARG B CA  1 
ATOM   3947 C  C   . ARG B  1  175 ? 16.050  -19.111 70.990 1.00 44.22  ? 188 ARG B C   1 
ATOM   3948 O  O   . ARG B  1  175 ? 16.406  -18.205 71.743 1.00 40.92  ? 188 ARG B O   1 
ATOM   3949 C  CB  . ARG B  1  175 ? 16.476  -18.624 68.552 1.00 41.55  ? 188 ARG B CB  1 
ATOM   3950 C  CG  . ARG B  1  175 ? 17.449  -18.710 67.380 1.00 40.27  ? 188 ARG B CG  1 
ATOM   3951 C  CD  . ARG B  1  175 ? 18.781  -18.036 67.683 1.00 40.43  ? 188 ARG B CD  1 
ATOM   3952 N  NE  . ARG B  1  175 ? 18.580  -16.606 67.916 1.00 40.72  ? 188 ARG B NE  1 
ATOM   3953 C  CZ  . ARG B  1  175 ? 18.755  -15.950 69.057 1.00 41.85  ? 188 ARG B CZ  1 
ATOM   3954 N  NH1 . ARG B  1  175 ? 19.344  -16.527 70.092 1.00 43.15  ? 188 ARG B NH1 1 
ATOM   3955 N  NH2 . ARG B  1  175 ? 18.363  -14.687 69.153 1.00 39.96  ? 188 ARG B NH2 1 
ATOM   3956 N  N   . ILE B  1  176 ? 14.926  -19.810 71.180 1.00 45.09  ? 189 ILE B N   1 
ATOM   3957 C  CA  . ILE B  1  176 ? 14.122  -19.612 72.377 1.00 48.55  ? 189 ILE B CA  1 
ATOM   3958 C  C   . ILE B  1  176 ? 14.959  -20.003 73.597 1.00 47.95  ? 189 ILE B C   1 
ATOM   3959 O  O   . ILE B  1  176 ? 15.032  -19.253 74.569 1.00 44.48  ? 189 ILE B O   1 
ATOM   3960 C  CB  . ILE B  1  176 ? 12.795  -20.394 72.303 1.00 47.25  ? 189 ILE B CB  1 
ATOM   3961 C  CG1 . ILE B  1  176 ? 11.844  -19.786 71.274 1.00 47.35  ? 189 ILE B CG1 1 
ATOM   3962 C  CG2 . ILE B  1  176 ? 12.133  -20.490 73.682 1.00 48.79  ? 189 ILE B CG2 1 
ATOM   3963 C  CD1 . ILE B  1  176 ? 10.690  -20.696 70.884 1.00 47.86  ? 189 ILE B CD1 1 
ATOM   3964 N  N   . GLN B  1  177 ? 15.608  -21.169 73.525 1.00 47.30  ? 190 GLN B N   1 
ATOM   3965 C  CA  . GLN B  1  177 ? 16.436  -21.658 74.619 1.00 51.87  ? 190 GLN B CA  1 
ATOM   3966 C  C   . GLN B  1  177 ? 17.566  -20.671 74.935 1.00 49.33  ? 190 GLN B C   1 
ATOM   3967 O  O   . GLN B  1  177 ? 17.861  -20.453 76.106 1.00 48.05  ? 190 GLN B O   1 
ATOM   3968 C  CB  . GLN B  1  177 ? 16.974  -23.058 74.319 1.00 55.38  ? 190 GLN B CB  1 
ATOM   3969 C  CG  . GLN B  1  177 ? 15.914  -24.154 74.303 1.00 60.32  ? 190 GLN B CG  1 
ATOM   3970 C  CD  . GLN B  1  177 ? 15.038  -24.170 75.542 1.00 73.51  ? 190 GLN B CD  1 
ATOM   3971 O  OE1 . GLN B  1  177 ? 15.467  -23.864 76.661 1.00 77.87  ? 190 GLN B OE1 1 
ATOM   3972 N  NE2 . GLN B  1  177 ? 13.772  -24.514 75.355 1.00 80.13  ? 190 GLN B NE2 1 
ATOM   3973 N  N   . ASP B  1  178 ? 18.178  -20.062 73.907 1.00 50.97  ? 191 ASP B N   1 
ATOM   3974 C  CA  . ASP B  1  178 ? 19.248  -19.092 74.113 1.00 50.79  ? 191 ASP B CA  1 
ATOM   3975 C  C   . ASP B  1  178 ? 18.756  -17.929 74.969 1.00 50.80  ? 191 ASP B C   1 
ATOM   3976 O  O   . ASP B  1  178 ? 19.433  -17.513 75.909 1.00 48.99  ? 191 ASP B O   1 
ATOM   3977 C  CB  . ASP B  1  178 ? 19.783  -18.524 72.804 1.00 52.00  ? 191 ASP B CB  1 
ATOM   3978 C  CG  . ASP B  1  178 ? 20.521  -19.495 71.895 1.00 54.12  ? 191 ASP B CG  1 
ATOM   3979 O  OD1 . ASP B  1  178 ? 20.864  -20.598 72.373 1.00 53.84  ? 191 ASP B OD1 1 
ATOM   3980 O  OD2 . ASP B  1  178 ? 20.730  -19.146 70.708 1.00 50.87  ? 191 ASP B OD2 1 
ATOM   3981 N  N   . SER B  1  179 ? 17.580  -17.396 74.618 1.00 48.55  ? 192 SER B N   1 
ATOM   3982 C  CA  . SER B  1  179 ? 17.026  -16.239 75.302 1.00 47.47  ? 192 SER B CA  1 
ATOM   3983 C  C   . SER B  1  179 ? 16.625  -16.601 76.733 1.00 49.63  ? 192 SER B C   1 
ATOM   3984 O  O   . SER B  1  179 ? 16.812  -15.794 77.635 1.00 46.71  ? 192 SER B O   1 
ATOM   3985 C  CB  . SER B  1  179 ? 15.875  -15.634 74.523 1.00 48.64  ? 192 SER B CB  1 
ATOM   3986 O  OG  . SER B  1  179 ? 16.344  -14.922 73.382 1.00 46.30  ? 192 SER B OG  1 
ATOM   3987 N  N   . ILE B  1  180 ? 16.074  -17.803 76.948 1.00 50.66  ? 193 ILE B N   1 
ATOM   3988 C  CA  . ILE B  1  180 ? 15.743  -18.250 78.295 1.00 51.75  ? 193 ILE B CA  1 
ATOM   3989 C  C   . ILE B  1  180 ? 17.008  -18.215 79.155 1.00 51.28  ? 193 ILE B C   1 
ATOM   3990 O  O   . ILE B  1  180 ? 16.999  -17.668 80.254 1.00 46.95  ? 193 ILE B O   1 
ATOM   3991 C  CB  . ILE B  1  180 ? 15.099  -19.649 78.282 1.00 54.14  ? 193 ILE B CB  1 
ATOM   3992 C  CG1 . ILE B  1  180 ? 13.695  -19.620 77.682 1.00 55.02  ? 193 ILE B CG1 1 
ATOM   3993 C  CG2 . ILE B  1  180 ? 15.083  -20.259 79.685 1.00 55.07  ? 193 ILE B CG2 1 
ATOM   3994 C  CD1 . ILE B  1  180 ? 13.131  -20.992 77.345 1.00 56.17  ? 193 ILE B CD1 1 
ATOM   3995 N  N   . ALA B  1  181 ? 18.099  -18.774 78.624 1.00 50.96  ? 194 ALA B N   1 
ATOM   3996 C  CA  . ALA B  1  181 ? 19.334  -18.956 79.372 1.00 51.85  ? 194 ALA B CA  1 
ATOM   3997 C  C   . ALA B  1  181 ? 20.069  -17.640 79.617 1.00 52.19  ? 194 ALA B C   1 
ATOM   3998 O  O   . ALA B  1  181 ? 20.786  -17.540 80.604 1.00 57.18  ? 194 ALA B O   1 
ATOM   3999 C  CB  . ALA B  1  181 ? 20.232  -19.933 78.646 1.00 53.87  ? 194 ALA B CB  1 
ATOM   4000 N  N   . THR B  1  182 ? 19.906  -16.635 78.741 1.00 51.48  ? 195 THR B N   1 
ATOM   4001 C  CA  . THR B  1  182 ? 20.815  -15.495 78.750 1.00 50.84  ? 195 THR B CA  1 
ATOM   4002 C  C   . THR B  1  182 ? 20.099  -14.165 78.967 1.00 51.07  ? 195 THR B C   1 
ATOM   4003 O  O   . THR B  1  182 ? 20.759  -13.166 79.256 1.00 49.81  ? 195 THR B O   1 
ATOM   4004 C  CB  . THR B  1  182 ? 21.619  -15.449 77.447 1.00 55.62  ? 195 THR B CB  1 
ATOM   4005 O  OG1 . THR B  1  182 ? 20.683  -15.267 76.382 1.00 54.48  ? 195 THR B OG1 1 
ATOM   4006 C  CG2 . THR B  1  182 ? 22.456  -16.700 77.246 1.00 54.72  ? 195 THR B CG2 1 
ATOM   4007 N  N   . ASN B  1  183 ? 18.774  -14.117 78.780 1.00 49.77  ? 196 ASN B N   1 
ATOM   4008 C  CA  . ASN B  1  183 ? 18.071  -12.847 78.791 1.00 49.62  ? 196 ASN B CA  1 
ATOM   4009 C  C   . ASN B  1  183 ? 17.046  -12.881 79.918 1.00 54.33  ? 196 ASN B C   1 
ATOM   4010 O  O   . ASN B  1  183 ? 16.012  -13.536 79.805 1.00 49.87  ? 196 ASN B O   1 
ATOM   4011 C  CB  . ASN B  1  183 ? 17.448  -12.535 77.434 1.00 53.98  ? 196 ASN B CB  1 
ATOM   4012 C  CG  . ASN B  1  183 ? 16.634  -11.258 77.424 1.00 50.23  ? 196 ASN B CG  1 
ATOM   4013 O  OD1 . ASN B  1  183 ? 16.581  -10.521 78.414 1.00 48.91  ? 196 ASN B OD1 1 
ATOM   4014 N  ND2 . ASN B  1  183 ? 15.998  -10.961 76.303 1.00 51.52  ? 196 ASN B ND2 1 
ATOM   4015 N  N   . PRO B  1  184 ? 17.301  -12.165 81.036 1.00 56.87  ? 197 PRO B N   1 
ATOM   4016 C  CA  . PRO B  1  184 ? 16.377  -12.179 82.170 1.00 59.60  ? 197 PRO B CA  1 
ATOM   4017 C  C   . PRO B  1  184 ? 15.041  -11.482 81.909 1.00 56.99  ? 197 PRO B C   1 
ATOM   4018 O  O   . PRO B  1  184 ? 14.090  -11.725 82.642 1.00 53.45  ? 197 PRO B O   1 
ATOM   4019 C  CB  . PRO B  1  184 ? 17.211  -11.478 83.254 1.00 58.37  ? 197 PRO B CB  1 
ATOM   4020 C  CG  . PRO B  1  184 ? 18.111  -10.529 82.493 1.00 58.81  ? 197 PRO B CG  1 
ATOM   4021 C  CD  . PRO B  1  184 ? 18.475  -11.303 81.255 1.00 55.21  ? 197 PRO B CD  1 
ATOM   4022 N  N   . GLU B  1  185 ? 14.981  -10.641 80.860 1.00 57.33  ? 198 GLU B N   1 
ATOM   4023 C  CA  . GLU B  1  185 ? 13.773  -9.908  80.498 1.00 57.72  ? 198 GLU B CA  1 
ATOM   4024 C  C   . GLU B  1  185 ? 13.060  -10.570 79.315 1.00 49.36  ? 198 GLU B C   1 
ATOM   4025 O  O   . GLU B  1  185 ? 12.167  -9.976  78.720 1.00 52.13  ? 198 GLU B O   1 
ATOM   4026 C  CB  . GLU B  1  185 ? 14.105  -8.464  80.119 1.00 58.13  ? 198 GLU B CB  1 
ATOM   4027 C  CG  . GLU B  1  185 ? 14.688  -7.629  81.254 1.00 60.01  ? 198 GLU B CG  1 
ATOM   4028 C  CD  . GLU B  1  185 ? 15.037  -6.203  80.855 1.00 63.31  ? 198 GLU B CD  1 
ATOM   4029 O  OE1 . GLU B  1  185 ? 14.755  -5.828  79.698 1.00 62.71  ? 198 GLU B OE1 1 
ATOM   4030 O  OE2 . GLU B  1  185 ? 15.596  -5.461  81.691 1.00 63.54  ? 198 GLU B OE2 1 
ATOM   4031 N  N   . PHE B  1  186 ? 13.439  -11.812 78.995 1.00 44.45  ? 199 PHE B N   1 
ATOM   4032 C  CA  . PHE B  1  186 ? 12.905  -12.516 77.843 1.00 43.88  ? 199 PHE B CA  1 
ATOM   4033 C  C   . PHE B  1  186 ? 11.382  -12.615 77.921 1.00 47.07  ? 199 PHE B C   1 
ATOM   4034 O  O   . PHE B  1  186 ? 10.842  -13.106 78.910 1.00 49.29  ? 199 PHE B O   1 
ATOM   4035 C  CB  . PHE B  1  186 ? 13.487  -13.927 77.790 1.00 40.23  ? 199 PHE B CB  1 
ATOM   4036 C  CG  . PHE B  1  186 ? 12.963  -14.803 76.661 1.00 42.43  ? 199 PHE B CG  1 
ATOM   4037 C  CD1 . PHE B  1  186 ? 12.819  -14.303 75.371 1.00 39.81  ? 199 PHE B CD1 1 
ATOM   4038 C  CD2 . PHE B  1  186 ? 12.620  -16.129 76.894 1.00 42.56  ? 199 PHE B CD2 1 
ATOM   4039 C  CE1 . PHE B  1  186 ? 12.359  -15.112 74.347 1.00 41.04  ? 199 PHE B CE1 1 
ATOM   4040 C  CE2 . PHE B  1  186 ? 12.148  -16.930 75.865 1.00 43.65  ? 199 PHE B CE2 1 
ATOM   4041 C  CZ  . PHE B  1  186 ? 12.033  -16.423 74.592 1.00 40.67  ? 199 PHE B CZ  1 
ATOM   4042 N  N   . GLN B  1  187 ? 10.714  -12.177 76.844 1.00 49.25  ? 200 GLN B N   1 
ATOM   4043 C  CA  . GLN B  1  187 ? 9.272   -12.305 76.689 1.00 47.10  ? 200 GLN B CA  1 
ATOM   4044 C  C   . GLN B  1  187 ? 8.982   -13.008 75.367 1.00 48.58  ? 200 GLN B C   1 
ATOM   4045 O  O   . GLN B  1  187 ? 9.645   -12.747 74.366 1.00 47.17  ? 200 GLN B O   1 
ATOM   4046 C  CB  . GLN B  1  187 ? 8.623   -10.922 76.696 1.00 49.31  ? 200 GLN B CB  1 
ATOM   4047 C  CG  . GLN B  1  187 ? 8.692   -10.200 78.039 1.00 54.11  ? 200 GLN B CG  1 
ATOM   4048 C  CD  . GLN B  1  187 ? 7.748   -10.799 79.060 1.00 58.82  ? 200 GLN B CD  1 
ATOM   4049 O  OE1 . GLN B  1  187 ? 6.522   -10.729 78.921 1.00 62.51  ? 200 GLN B OE1 1 
ATOM   4050 N  NE2 . GLN B  1  187 ? 8.311   -11.421 80.083 1.00 60.31  ? 200 GLN B NE2 1 
ATOM   4051 N  N   . PHE B  1  188 ? 7.995   -13.910 75.383 1.00 44.96  ? 201 PHE B N   1 
ATOM   4052 C  CA  . PHE B  1  188 ? 7.599   -14.651 74.201 1.00 43.73  ? 201 PHE B CA  1 
ATOM   4053 C  C   . PHE B  1  188 ? 6.090   -14.881 74.248 1.00 42.86  ? 201 PHE B C   1 
ATOM   4054 O  O   . PHE B  1  188 ? 5.633   -16.015 74.297 1.00 40.68  ? 201 PHE B O   1 
ATOM   4055 C  CB  . PHE B  1  188 ? 8.451   -15.920 74.158 1.00 45.03  ? 201 PHE B CB  1 
ATOM   4056 C  CG  . PHE B  1  188 ? 8.606   -16.512 72.767 1.00 45.40  ? 201 PHE B CG  1 
ATOM   4057 C  CD1 . PHE B  1  188 ? 9.366   -15.854 71.807 1.00 47.29  ? 201 PHE B CD1 1 
ATOM   4058 C  CD2 . PHE B  1  188 ? 8.016   -17.721 72.428 1.00 43.57  ? 201 PHE B CD2 1 
ATOM   4059 C  CE1 . PHE B  1  188 ? 9.505   -16.376 70.540 1.00 44.81  ? 201 PHE B CE1 1 
ATOM   4060 C  CE2 . PHE B  1  188 ? 8.172   -18.243 71.159 1.00 45.23  ? 201 PHE B CE2 1 
ATOM   4061 C  CZ  . PHE B  1  188 ? 8.910   -17.568 70.219 1.00 43.92  ? 201 PHE B CZ  1 
ATOM   4062 N  N   . LYS B  1  189 ? 5.350   -13.772 74.196 1.00 45.21  ? 202 LYS B N   1 
ATOM   4063 C  CA  . LYS B  1  189 ? 3.920   -13.721 74.458 1.00 50.84  ? 202 LYS B CA  1 
ATOM   4064 C  C   . LYS B  1  189 ? 3.226   -12.913 73.367 1.00 48.11  ? 202 LYS B C   1 
ATOM   4065 O  O   . LYS B  1  189 ? 3.857   -12.100 72.696 1.00 47.07  ? 202 LYS B O   1 
ATOM   4066 C  CB  . LYS B  1  189 ? 3.586   -12.860 75.684 1.00 51.83  ? 202 LYS B CB  1 
ATOM   4067 C  CG  . LYS B  1  189 ? 3.904   -13.378 77.057 1.00 57.48  ? 202 LYS B CG  1 
ATOM   4068 C  CD  . LYS B  1  189 ? 3.657   -12.309 78.117 1.00 59.43  ? 202 LYS B CD  1 
ATOM   4069 C  CE  . LYS B  1  189 ? 3.919   -12.805 79.502 1.00 65.46  ? 202 LYS B CE  1 
ATOM   4070 N  NZ  . LYS B  1  189 ? 3.977   -11.713 80.476 1.00 70.21  ? 202 LYS B NZ  1 
ATOM   4071 N  N   . ASN B  1  190 ? 1.904   -13.089 73.260 1.00 49.24  ? 203 ASN B N   1 
ATOM   4072 C  CA  . ASN B  1  190 ? 1.046   -12.182 72.514 1.00 46.06  ? 203 ASN B CA  1 
ATOM   4073 C  C   . ASN B  1  190 ? 1.578   -12.028 71.091 1.00 43.40  ? 203 ASN B C   1 
ATOM   4074 O  O   . ASN B  1  190 ? 1.733   -13.020 70.385 1.00 45.53  ? 203 ASN B O   1 
ATOM   4075 C  CB  . ASN B  1  190 ? 0.837   -10.890 73.303 1.00 49.66  ? 203 ASN B CB  1 
ATOM   4076 C  CG  . ASN B  1  190 ? 0.078   -11.152 74.586 1.00 50.99  ? 203 ASN B CG  1 
ATOM   4077 O  OD1 . ASN B  1  190 ? -0.970  -11.815 74.564 1.00 44.35  ? 203 ASN B OD1 1 
ATOM   4078 N  ND2 . ASN B  1  190 ? 0.591   -10.648 75.699 1.00 47.89  ? 203 ASN B ND2 1 
ATOM   4079 N  N   . VAL B  1  191 ? 1.858   -10.790 70.666 1.00 42.18  ? 204 VAL B N   1 
ATOM   4080 C  CA  . VAL B  1  191 ? 2.225   -10.540 69.284 1.00 41.77  ? 204 VAL B CA  1 
ATOM   4081 C  C   . VAL B  1  191 ? 3.458   -11.371 68.937 1.00 42.87  ? 204 VAL B C   1 
ATOM   4082 O  O   . VAL B  1  191 ? 3.490   -12.056 67.916 1.00 46.77  ? 204 VAL B O   1 
ATOM   4083 C  CB  . VAL B  1  191 ? 2.476   -9.050  68.994 1.00 42.85  ? 204 VAL B CB  1 
ATOM   4084 C  CG1 . VAL B  1  191 ? 2.972   -8.826  67.568 1.00 41.39  ? 204 VAL B CG1 1 
ATOM   4085 C  CG2 . VAL B  1  191 ? 1.237   -8.205  69.259 1.00 43.48  ? 204 VAL B CG2 1 
ATOM   4086 N  N   . ARG B  1  192 ? 4.477   -11.307 69.795 1.00 41.66  ? 205 ARG B N   1 
ATOM   4087 C  CA  . ARG B  1  192 ? 5.752   -11.916 69.475 1.00 40.47  ? 205 ARG B CA  1 
ATOM   4088 C  C   . ARG B  1  192 ? 5.604   -13.423 69.286 1.00 42.11  ? 205 ARG B C   1 
ATOM   4089 O  O   . ARG B  1  192 ? 6.266   -14.005 68.432 1.00 38.67  ? 205 ARG B O   1 
ATOM   4090 C  CB  . ARG B  1  192 ? 6.804   -11.635 70.551 1.00 42.63  ? 205 ARG B CB  1 
ATOM   4091 C  CG  . ARG B  1  192 ? 8.171   -12.206 70.204 1.00 44.77  ? 205 ARG B CG  1 
ATOM   4092 C  CD  . ARG B  1  192 ? 8.606   -11.822 68.800 1.00 43.48  ? 205 ARG B CD  1 
ATOM   4093 N  NE  . ARG B  1  192 ? 9.899   -12.392 68.418 1.00 46.70  ? 205 ARG B NE  1 
ATOM   4094 C  CZ  . ARG B  1  192 ? 10.373  -12.466 67.169 1.00 50.80  ? 205 ARG B CZ  1 
ATOM   4095 N  NH1 . ARG B  1  192 ? 9.617   -12.138 66.134 1.00 47.90  ? 205 ARG B NH1 1 
ATOM   4096 N  NH2 . ARG B  1  192 ? 11.608  -12.894 66.962 1.00 49.09  ? 205 ARG B NH2 1 
ATOM   4097 N  N   . PHE B  1  193 ? 4.747   -14.058 70.089 1.00 44.49  ? 206 PHE B N   1 
ATOM   4098 C  CA  . PHE B  1  193 ? 4.611   -15.502 70.038 1.00 44.04  ? 206 PHE B CA  1 
ATOM   4099 C  C   . PHE B  1  193 ? 4.104   -15.901 68.657 1.00 44.81  ? 206 PHE B C   1 
ATOM   4100 O  O   . PHE B  1  193 ? 4.534   -16.905 68.098 1.00 47.46  ? 206 PHE B O   1 
ATOM   4101 C  CB  . PHE B  1  193 ? 3.693   -16.051 71.132 1.00 44.85  ? 206 PHE B CB  1 
ATOM   4102 C  CG  . PHE B  1  193 ? 3.515   -17.560 71.031 1.00 44.35  ? 206 PHE B CG  1 
ATOM   4103 C  CD1 . PHE B  1  193 ? 4.510   -18.422 71.471 1.00 46.11  ? 206 PHE B CD1 1 
ATOM   4104 C  CD2 . PHE B  1  193 ? 2.365   -18.111 70.480 1.00 46.10  ? 206 PHE B CD2 1 
ATOM   4105 C  CE1 . PHE B  1  193 ? 4.351   -19.797 71.372 1.00 48.00  ? 206 PHE B CE1 1 
ATOM   4106 C  CE2 . PHE B  1  193 ? 2.207   -19.483 70.383 1.00 46.55  ? 206 PHE B CE2 1 
ATOM   4107 C  CZ  . PHE B  1  193 ? 3.204   -20.323 70.827 1.00 46.51  ? 206 PHE B CZ  1 
ATOM   4108 N  N   . ILE B  1  194 ? 3.203   -15.094 68.099 1.00 45.00  ? 207 ILE B N   1 
ATOM   4109 C  CA  . ILE B  1  194 ? 2.617   -15.411 66.810 1.00 45.26  ? 207 ILE B CA  1 
ATOM   4110 C  C   . ILE B  1  194 ? 3.605   -15.068 65.693 1.00 43.79  ? 207 ILE B C   1 
ATOM   4111 O  O   . ILE B  1  194 ? 3.829   -15.893 64.810 1.00 43.51  ? 207 ILE B O   1 
ATOM   4112 C  CB  . ILE B  1  194 ? 1.252   -14.716 66.648 1.00 47.60  ? 207 ILE B CB  1 
ATOM   4113 C  CG1 . ILE B  1  194 ? 0.273   -15.094 67.770 1.00 49.96  ? 207 ILE B CG1 1 
ATOM   4114 C  CG2 . ILE B  1  194 ? 0.663   -15.009 65.268 1.00 49.82  ? 207 ILE B CG2 1 
ATOM   4115 C  CD1 . ILE B  1  194 ? -0.013  -16.589 67.877 1.00 48.42  ? 207 ILE B CD1 1 
ATOM   4116 N  N   . THR B  1  195 ? 4.217   -13.879 65.746 1.00 42.72  ? 208 THR B N   1 
ATOM   4117 C  CA  . THR B  1  195 ? 5.042   -13.405 64.640 1.00 46.68  ? 208 THR B CA  1 
ATOM   4118 C  C   . THR B  1  195 ? 6.343   -14.204 64.553 1.00 44.09  ? 208 THR B C   1 
ATOM   4119 O  O   . THR B  1  195 ? 6.931   -14.298 63.483 1.00 45.11  ? 208 THR B O   1 
ATOM   4120 C  CB  . THR B  1  195 ? 5.336   -11.910 64.749 1.00 45.59  ? 208 THR B CB  1 
ATOM   4121 O  OG1 . THR B  1  195 ? 6.042   -11.693 65.963 1.00 49.15  ? 208 THR B OG1 1 
ATOM   4122 C  CG2 . THR B  1  195 ? 4.080   -11.059 64.689 1.00 47.06  ? 208 THR B CG2 1 
ATOM   4123 N  N   . ALA B  1  196 ? 6.784   -14.788 65.670 1.00 44.66  ? 209 ALA B N   1 
ATOM   4124 C  CA  . ALA B  1  196 ? 8.075   -15.454 65.711 1.00 47.12  ? 209 ALA B CA  1 
ATOM   4125 C  C   . ALA B  1  196 ? 8.053   -16.745 64.895 1.00 49.16  ? 209 ALA B C   1 
ATOM   4126 O  O   . ALA B  1  196 ? 9.108   -17.183 64.457 1.00 49.23  ? 209 ALA B O   1 
ATOM   4127 C  CB  . ALA B  1  196 ? 8.493   -15.723 67.135 1.00 47.20  ? 209 ALA B CB  1 
ATOM   4128 N  N   . TYR B  1  197 ? 6.881   -17.363 64.712 1.00 42.57  ? 210 TYR B N   1 
ATOM   4129 C  CA  . TYR B  1  197 ? 6.800   -18.594 63.943 1.00 43.03  ? 210 TYR B CA  1 
ATOM   4130 C  C   . TYR B  1  197 ? 6.693   -18.247 62.458 1.00 44.74  ? 210 TYR B C   1 
ATOM   4131 O  O   . TYR B  1  197 ? 7.385   -18.850 61.640 1.00 46.30  ? 210 TYR B O   1 
ATOM   4132 C  CB  . TYR B  1  197 ? 5.702   -19.493 64.527 1.00 42.41  ? 210 TYR B CB  1 
ATOM   4133 C  CG  . TYR B  1  197 ? 6.187   -20.146 65.813 1.00 43.51  ? 210 TYR B CG  1 
ATOM   4134 C  CD1 . TYR B  1  197 ? 6.920   -21.324 65.782 1.00 43.28  ? 210 TYR B CD1 1 
ATOM   4135 C  CD2 . TYR B  1  197 ? 5.991   -19.545 67.047 1.00 41.73  ? 210 TYR B CD2 1 
ATOM   4136 C  CE1 . TYR B  1  197 ? 7.408   -21.906 66.941 1.00 41.48  ? 210 TYR B CE1 1 
ATOM   4137 C  CE2 . TYR B  1  197 ? 6.477   -20.113 68.212 1.00 42.65  ? 210 TYR B CE2 1 
ATOM   4138 C  CZ  . TYR B  1  197 ? 7.186   -21.297 68.159 1.00 42.86  ? 210 TYR B CZ  1 
ATOM   4139 O  OH  . TYR B  1  197 ? 7.665   -21.834 69.318 1.00 45.65  ? 210 TYR B OH  1 
ATOM   4140 N  N   . GLY B  1  198 ? 5.855   -17.262 62.114 1.00 42.60  ? 211 GLY B N   1 
ATOM   4141 C  CA  . GLY B  1  198 ? 5.747   -16.787 60.742 1.00 41.07  ? 211 GLY B CA  1 
ATOM   4142 C  C   . GLY B  1  198 ? 7.101   -16.373 60.163 1.00 40.01  ? 211 GLY B C   1 
ATOM   4143 O  O   . GLY B  1  198 ? 7.446   -16.753 59.048 1.00 40.99  ? 211 GLY B O   1 
ATOM   4144 N  N   . GLU B  1  199 ? 7.889   -15.637 60.952 1.00 41.16  ? 212 GLU B N   1 
ATOM   4145 C  CA  A GLU B  1  199 ? 9.130   -15.065 60.457 0.50 42.20  ? 212 GLU B CA  1 
ATOM   4146 C  CA  B GLU B  1  199 ? 9.142   -15.063 60.487 0.50 41.48  ? 212 GLU B CA  1 
ATOM   4147 C  C   . GLU B  1  199 ? 10.125  -16.172 60.105 1.00 43.20  ? 212 GLU B C   1 
ATOM   4148 O  O   . GLU B  1  199 ? 10.992  -15.958 59.266 1.00 44.84  ? 212 GLU B O   1 
ATOM   4149 C  CB  A GLU B  1  199 ? 9.661   -13.999 61.417 0.50 43.01  ? 212 GLU B CB  1 
ATOM   4150 C  CB  B GLU B  1  199 ? 9.736   -14.093 61.520 0.50 41.12  ? 212 GLU B CB  1 
ATOM   4151 C  CG  A GLU B  1  199 ? 8.826   -12.718 61.392 0.50 42.40  ? 212 GLU B CG  1 
ATOM   4152 C  CG  B GLU B  1  199 ? 10.468  -14.744 62.697 0.50 39.78  ? 212 GLU B CG  1 
ATOM   4153 C  CD  A GLU B  1  199 ? 9.024   -11.825 62.603 0.50 41.88  ? 212 GLU B CD  1 
ATOM   4154 C  CD  B GLU B  1  199 ? 11.152  -13.772 63.664 0.50 37.81  ? 212 GLU B CD  1 
ATOM   4155 O  OE1 A GLU B  1  199 ? 9.987   -12.050 63.363 0.50 40.66  ? 212 GLU B OE1 1 
ATOM   4156 O  OE1 B GLU B  1  199 ? 10.833  -12.568 63.628 0.50 38.39  ? 212 GLU B OE1 1 
ATOM   4157 O  OE2 A GLU B  1  199 ? 8.193   -10.922 62.802 0.50 44.26  ? 212 GLU B OE2 1 
ATOM   4158 O  OE2 B GLU B  1  199 ? 12.027  -14.187 64.442 0.50 29.25  ? 212 GLU B OE2 1 
ATOM   4159 N  N   . THR B  1  200 ? 10.004  -17.359 60.723 1.00 41.77  ? 213 THR B N   1 
ATOM   4160 C  CA  . THR B  1  200 ? 10.965  -18.428 60.478 1.00 44.30  ? 213 THR B CA  1 
ATOM   4161 C  C   . THR B  1  200 ? 10.701  -19.126 59.145 1.00 40.33  ? 213 THR B C   1 
ATOM   4162 O  O   . THR B  1  200 ? 11.602  -19.800 58.640 1.00 36.34  ? 213 THR B O   1 
ATOM   4163 C  CB  . THR B  1  200 ? 11.005  -19.465 61.601 1.00 52.33  ? 213 THR B CB  1 
ATOM   4164 O  OG1 . THR B  1  200 ? 9.810   -20.237 61.532 1.00 56.83  ? 213 THR B OG1 1 
ATOM   4165 C  CG2 . THR B  1  200 ? 11.171  -18.834 62.969 1.00 52.80  ? 213 THR B CG2 1 
ATOM   4166 N  N   . VAL B  1  201 ? 9.490   -18.987 58.583 1.00 36.81  ? 214 VAL B N   1 
ATOM   4167 C  CA  . VAL B  1  201 ? 9.186   -19.609 57.299 1.00 35.42  ? 214 VAL B CA  1 
ATOM   4168 C  C   . VAL B  1  201 ? 9.224   -18.582 56.163 1.00 36.65  ? 214 VAL B C   1 
ATOM   4169 O  O   . VAL B  1  201 ? 9.259   -18.967 54.994 1.00 37.80  ? 214 VAL B O   1 
ATOM   4170 C  CB  . VAL B  1  201 ? 7.844   -20.373 57.297 1.00 36.77  ? 214 VAL B CB  1 
ATOM   4171 C  CG1 . VAL B  1  201 ? 7.884   -21.556 58.254 1.00 37.06  ? 214 VAL B CG1 1 
ATOM   4172 C  CG2 . VAL B  1  201 ? 6.639   -19.483 57.594 1.00 37.05  ? 214 VAL B CG2 1 
ATOM   4173 N  N   . PHE B  1  202 ? 9.241   -17.281 56.478 1.00 36.23  ? 215 PHE B N   1 
ATOM   4174 C  CA  . PHE B  1  202 ? 9.261   -16.267 55.431 1.00 37.76  ? 215 PHE B CA  1 
ATOM   4175 C  C   . PHE B  1  202 ? 10.471  -16.480 54.522 1.00 37.55  ? 215 PHE B C   1 
ATOM   4176 O  O   . PHE B  1  202 ? 10.353  -16.351 53.308 1.00 40.82  ? 215 PHE B O   1 
ATOM   4177 C  CB  . PHE B  1  202 ? 9.207   -14.832 55.967 1.00 35.73  ? 215 PHE B CB  1 
ATOM   4178 C  CG  . PHE B  1  202 ? 7.881   -14.396 56.587 1.00 38.21  ? 215 PHE B CG  1 
ATOM   4179 C  CD1 . PHE B  1  202 ? 6.705   -15.123 56.411 1.00 39.79  ? 215 PHE B CD1 1 
ATOM   4180 C  CD2 . PHE B  1  202 ? 7.811   -13.223 57.331 1.00 40.73  ? 215 PHE B CD2 1 
ATOM   4181 C  CE1 . PHE B  1  202 ? 5.507   -14.692 56.973 1.00 40.37  ? 215 PHE B CE1 1 
ATOM   4182 C  CE2 . PHE B  1  202 ? 6.614   -12.799 57.890 1.00 43.17  ? 215 PHE B CE2 1 
ATOM   4183 C  CZ  . PHE B  1  202 ? 5.462   -13.531 57.706 1.00 39.76  ? 215 PHE B CZ  1 
ATOM   4184 N  N   . PRO B  1  203 ? 11.666  -16.819 55.051 1.00 36.85  ? 216 PRO B N   1 
ATOM   4185 C  CA  . PRO B  1  203 ? 12.823  -17.091 54.197 1.00 38.09  ? 216 PRO B CA  1 
ATOM   4186 C  C   . PRO B  1  203 ? 12.581  -18.201 53.176 1.00 39.25  ? 216 PRO B C   1 
ATOM   4187 O  O   . PRO B  1  203 ? 13.080  -18.125 52.057 1.00 45.32  ? 216 PRO B O   1 
ATOM   4188 C  CB  . PRO B  1  203 ? 13.927  -17.468 55.203 1.00 37.35  ? 216 PRO B CB  1 
ATOM   4189 C  CG  . PRO B  1  203 ? 13.508  -16.811 56.489 1.00 37.59  ? 216 PRO B CG  1 
ATOM   4190 C  CD  . PRO B  1  203 ? 11.993  -16.916 56.479 1.00 37.97  ? 216 PRO B CD  1 
ATOM   4191 N  N   . ILE B  1  204 ? 11.827  -19.232 53.576 1.00 36.58  ? 217 ILE B N   1 
ATOM   4192 C  CA  . ILE B  1  204 ? 11.536  -20.357 52.700 1.00 37.87  ? 217 ILE B CA  1 
ATOM   4193 C  C   . ILE B  1  204 ? 10.517  -19.937 51.642 1.00 37.49  ? 217 ILE B C   1 
ATOM   4194 O  O   . ILE B  1  204 ? 10.710  -20.218 50.466 1.00 39.80  ? 217 ILE B O   1 
ATOM   4195 C  CB  . ILE B  1  204 ? 11.039  -21.564 53.516 1.00 39.81  ? 217 ILE B CB  1 
ATOM   4196 C  CG1 . ILE B  1  204 ? 12.101  -22.032 54.512 1.00 39.36  ? 217 ILE B CG1 1 
ATOM   4197 C  CG2 . ILE B  1  204 ? 10.577  -22.704 52.606 1.00 39.17  ? 217 ILE B CG2 1 
ATOM   4198 C  CD1 . ILE B  1  204 ? 11.559  -22.874 55.650 1.00 41.72  ? 217 ILE B CD1 1 
ATOM   4199 N  N   . ASN B  1  205 ? 9.433   -19.280 52.064 1.00 36.37  ? 218 ASN B N   1 
ATOM   4200 C  CA  . ASN B  1  205 ? 8.312   -19.022 51.171 1.00 38.79  ? 218 ASN B CA  1 
ATOM   4201 C  C   . ASN B  1  205 ? 8.553   -17.795 50.292 1.00 39.96  ? 218 ASN B C   1 
ATOM   4202 O  O   . ASN B  1  205 ? 7.968   -17.713 49.208 1.00 42.63  ? 218 ASN B O   1 
ATOM   4203 C  CB  . ASN B  1  205 ? 6.996   -18.861 51.924 1.00 38.87  ? 218 ASN B CB  1 
ATOM   4204 C  CG  . ASN B  1  205 ? 6.693   -20.056 52.800 1.00 39.90  ? 218 ASN B CG  1 
ATOM   4205 O  OD1 . ASN B  1  205 ? 7.097   -21.175 52.485 1.00 42.50  ? 218 ASN B OD1 1 
ATOM   4206 N  ND2 . ASN B  1  205 ? 6.021   -19.843 53.918 1.00 46.52  ? 218 ASN B ND2 1 
ATOM   4207 N  N   . LEU B  1  206 ? 9.378   -16.841 50.763 1.00 37.01  ? 219 LEU B N   1 
ATOM   4208 C  CA  . LEU B  1  206 ? 9.492   -15.548 50.106 1.00 37.27  ? 219 LEU B CA  1 
ATOM   4209 C  C   . LEU B  1  206 ? 10.918  -15.224 49.656 1.00 36.52  ? 219 LEU B C   1 
ATOM   4210 O  O   . LEU B  1  206 ? 11.077  -14.470 48.699 1.00 35.46  ? 219 LEU B O   1 
ATOM   4211 C  CB  . LEU B  1  206 ? 8.929   -14.480 51.040 1.00 37.68  ? 219 LEU B CB  1 
ATOM   4212 C  CG  . LEU B  1  206 ? 7.450   -14.646 51.412 1.00 40.42  ? 219 LEU B CG  1 
ATOM   4213 C  CD1 . LEU B  1  206 ? 7.071   -13.717 52.551 1.00 43.41  ? 219 LEU B CD1 1 
ATOM   4214 C  CD2 . LEU B  1  206 ? 6.539   -14.404 50.222 1.00 41.68  ? 219 LEU B CD2 1 
ATOM   4215 N  N   . PHE B  1  207 ? 11.953  -15.747 50.336 1.00 37.67  ? 220 PHE B N   1 
ATOM   4216 C  CA  . PHE B  1  207 ? 13.321  -15.409 49.970 1.00 39.54  ? 220 PHE B CA  1 
ATOM   4217 C  C   . PHE B  1  207 ? 13.884  -16.421 48.978 1.00 42.82  ? 220 PHE B C   1 
ATOM   4218 O  O   . PHE B  1  207 ? 14.883  -16.137 48.313 1.00 44.95  ? 220 PHE B O   1 
ATOM   4219 C  CB  . PHE B  1  207 ? 14.286  -15.325 51.151 1.00 41.52  ? 220 PHE B CB  1 
ATOM   4220 C  CG  . PHE B  1  207 ? 14.023  -14.202 52.142 1.00 42.98  ? 220 PHE B CG  1 
ATOM   4221 C  CD1 . PHE B  1  207 ? 13.168  -13.148 51.836 1.00 42.42  ? 220 PHE B CD1 1 
ATOM   4222 C  CD2 . PHE B  1  207 ? 14.677  -14.185 53.366 1.00 41.45  ? 220 PHE B CD2 1 
ATOM   4223 C  CE1 . PHE B  1  207 ? 12.960  -12.128 52.745 1.00 43.10  ? 220 PHE B CE1 1 
ATOM   4224 C  CE2 . PHE B  1  207 ? 14.461  -13.163 54.267 1.00 41.25  ? 220 PHE B CE2 1 
ATOM   4225 C  CZ  . PHE B  1  207 ? 13.603  -12.140 53.956 1.00 41.90  ? 220 PHE B CZ  1 
ATOM   4226 N  N   . VAL B  1  208 ? 13.261  -17.602 48.904 1.00 41.18  ? 221 VAL B N   1 
ATOM   4227 C  CA  . VAL B  1  208 ? 13.599  -18.574 47.879 1.00 41.20  ? 221 VAL B CA  1 
ATOM   4228 C  C   . VAL B  1  208 ? 12.981  -18.110 46.567 1.00 39.78  ? 221 VAL B C   1 
ATOM   4229 O  O   . VAL B  1  208 ? 11.831  -17.678 46.525 1.00 42.54  ? 221 VAL B O   1 
ATOM   4230 C  CB  . VAL B  1  208 ? 13.134  -19.998 48.245 1.00 40.09  ? 221 VAL B CB  1 
ATOM   4231 C  CG1 . VAL B  1  208 ? 13.382  -20.987 47.114 1.00 41.27  ? 221 VAL B CG1 1 
ATOM   4232 C  CG2 . VAL B  1  208 ? 13.797  -20.490 49.525 1.00 40.08  ? 221 VAL B CG2 1 
ATOM   4233 N  N   . ASP B  1  209 ? 13.757  -18.230 45.491 1.00 37.88  ? 222 ASP B N   1 
ATOM   4234 C  CA  . ASP B  1  209 ? 13.345  -17.749 44.185 1.00 37.61  ? 222 ASP B CA  1 
ATOM   4235 C  C   . ASP B  1  209 ? 12.067  -18.469 43.758 1.00 38.86  ? 222 ASP B C   1 
ATOM   4236 O  O   . ASP B  1  209 ? 11.947  -19.674 43.943 1.00 37.09  ? 222 ASP B O   1 
ATOM   4237 C  CB  . ASP B  1  209 ? 14.458  -17.947 43.175 1.00 37.34  ? 222 ASP B CB  1 
ATOM   4238 C  CG  . ASP B  1  209 ? 14.214  -17.325 41.816 1.00 38.15  ? 222 ASP B CG  1 
ATOM   4239 O  OD1 . ASP B  1  209 ? 13.411  -17.900 41.053 1.00 40.42  ? 222 ASP B OD1 1 
ATOM   4240 O  OD2 . ASP B  1  209 ? 14.801  -16.258 41.552 1.00 40.75  ? 222 ASP B OD2 1 
ATOM   4241 N  N   . GLY B  1  210 ? 11.138  -17.722 43.147 1.00 41.60  ? 223 GLY B N   1 
ATOM   4242 C  CA  . GLY B  1  210 ? 9.817   -18.241 42.823 1.00 44.28  ? 223 GLY B CA  1 
ATOM   4243 C  C   . GLY B  1  210 ? 9.827   -19.258 41.681 1.00 50.21  ? 223 GLY B C   1 
ATOM   4244 O  O   . GLY B  1  210 ? 8.828   -19.945 41.468 1.00 51.21  ? 223 GLY B O   1 
ATOM   4245 N  N   . ARG B  1  211 ? 10.947  -19.361 40.949 1.00 47.83  ? 224 ARG B N   1 
ATOM   4246 C  CA  . ARG B  1  211 ? 11.074  -20.359 39.896 1.00 48.23  ? 224 ARG B CA  1 
ATOM   4247 C  C   . ARG B  1  211 ? 11.461  -21.716 40.471 1.00 47.43  ? 224 ARG B C   1 
ATOM   4248 O  O   . ARG B  1  211 ? 11.446  -22.705 39.747 1.00 49.67  ? 224 ARG B O   1 
ATOM   4249 C  CB  . ARG B  1  211 ? 12.101  -19.953 38.837 1.00 45.93  ? 224 ARG B CB  1 
ATOM   4250 C  CG  . ARG B  1  211 ? 11.694  -18.740 38.019 1.00 45.31  ? 224 ARG B CG  1 
ATOM   4251 C  CD  . ARG B  1  211 ? 12.897  -18.184 37.282 1.00 48.52  ? 224 ARG B CD  1 
ATOM   4252 N  NE  . ARG B  1  211 ? 13.880  -17.618 38.216 1.00 50.86  ? 224 ARG B NE  1 
ATOM   4253 C  CZ  . ARG B  1  211 ? 14.974  -16.949 37.882 1.00 52.22  ? 224 ARG B CZ  1 
ATOM   4254 N  NH1 . ARG B  1  211 ? 15.284  -16.758 36.610 1.00 51.43  ? 224 ARG B NH1 1 
ATOM   4255 N  NH2 . ARG B  1  211 ? 15.760  -16.464 38.826 1.00 53.01  ? 224 ARG B NH2 1 
ATOM   4256 N  N   . VAL B  1  212 ? 11.803  -21.772 41.763 1.00 47.91  ? 225 VAL B N   1 
ATOM   4257 C  CA  . VAL B  1  212 ? 11.994  -23.037 42.456 1.00 52.13  ? 225 VAL B CA  1 
ATOM   4258 C  C   . VAL B  1  212 ? 10.636  -23.540 42.946 1.00 57.65  ? 225 VAL B C   1 
ATOM   4259 O  O   . VAL B  1  212 ? 10.066  -22.976 43.871 1.00 56.13  ? 225 VAL B O   1 
ATOM   4260 C  CB  . VAL B  1  212 ? 12.994  -22.889 43.617 1.00 54.01  ? 225 VAL B CB  1 
ATOM   4261 C  CG1 . VAL B  1  212 ? 13.215  -24.208 44.338 1.00 56.36  ? 225 VAL B CG1 1 
ATOM   4262 C  CG2 . VAL B  1  212 ? 14.331  -22.319 43.156 1.00 54.88  ? 225 VAL B CG2 1 
ATOM   4263 N  N   . THR B  1  213 ? 10.130  -24.622 42.340 1.00 61.86  ? 226 THR B N   1 
ATOM   4264 C  CA  . THR B  1  213 ? 8.813   -25.163 42.667 1.00 69.50  ? 226 THR B CA  1 
ATOM   4265 C  C   . THR B  1  213 ? 8.944   -26.341 43.633 1.00 72.84  ? 226 THR B C   1 
ATOM   4266 O  O   . THR B  1  213 ? 8.083   -26.540 44.489 1.00 74.90  ? 226 THR B O   1 
ATOM   4267 C  CB  . THR B  1  213 ? 8.088   -25.576 41.384 1.00 70.79  ? 226 THR B CB  1 
ATOM   4268 O  OG1 . THR B  1  213 ? 8.942   -26.510 40.728 1.00 72.99  ? 226 THR B OG1 1 
ATOM   4269 C  CG2 . THR B  1  213 ? 7.816   -24.400 40.463 1.00 68.79  ? 226 THR B CG2 1 
ATOM   4270 N  N   . THR B  1  214 ? 10.030  -27.109 43.491 1.00 76.79  ? 227 THR B N   1 
ATOM   4271 C  CA  . THR B  1  214 ? 10.244  -28.305 44.289 1.00 85.38  ? 227 THR B CA  1 
ATOM   4272 C  C   . THR B  1  214 ? 11.435  -28.110 45.233 1.00 80.34  ? 227 THR B C   1 
ATOM   4273 O  O   . THR B  1  214 ? 12.424  -27.475 44.876 1.00 78.99  ? 227 THR B O   1 
ATOM   4274 C  CB  . THR B  1  214 ? 10.435  -29.487 43.340 1.00 90.36  ? 227 THR B CB  1 
ATOM   4275 O  OG1 . THR B  1  214 ? 10.505  -30.626 44.195 1.00 92.58  ? 227 THR B OG1 1 
ATOM   4276 C  CG2 . THR B  1  214 ? 11.679  -29.379 42.472 1.00 90.10  ? 227 THR B CG2 1 
ATOM   4277 N  N   . ASP B  1  215 ? 11.313  -28.662 46.444 1.00 73.67  ? 228 ASP B N   1 
ATOM   4278 C  CA  . ASP B  1  215 ? 12.419  -28.726 47.385 1.00 77.59  ? 228 ASP B CA  1 
ATOM   4279 C  C   . ASP B  1  215 ? 12.904  -27.313 47.706 1.00 64.91  ? 228 ASP B C   1 
ATOM   4280 O  O   . ASP B  1  215 ? 14.077  -26.999 47.528 1.00 62.57  ? 228 ASP B O   1 
ATOM   4281 C  CB  . ASP B  1  215 ? 13.533  -29.616 46.843 1.00 90.82  ? 228 ASP B CB  1 
ATOM   4282 C  CG  . ASP B  1  215 ? 14.702  -29.888 47.784 1.00 109.74 ? 228 ASP B CG  1 
ATOM   4283 O  OD1 . ASP B  1  215 ? 14.501  -29.832 49.021 1.00 118.24 ? 228 ASP B OD1 1 
ATOM   4284 O  OD2 . ASP B  1  215 ? 15.817  -30.131 47.267 1.00 113.29 ? 228 ASP B OD2 1 
ATOM   4285 N  N   . ARG B  1  216 ? 11.989  -26.463 48.177 1.00 56.72  ? 229 ARG B N   1 
ATOM   4286 C  CA  . ARG B  1  216 ? 12.303  -25.065 48.423 1.00 51.29  ? 229 ARG B CA  1 
ATOM   4287 C  C   . ARG B  1  216 ? 13.263  -24.963 49.608 1.00 47.58  ? 229 ARG B C   1 
ATOM   4288 O  O   . ARG B  1  216 ? 12.986  -25.459 50.693 1.00 53.40  ? 229 ARG B O   1 
ATOM   4289 C  CB  . ARG B  1  216 ? 11.022  -24.233 48.565 1.00 50.26  ? 229 ARG B CB  1 
ATOM   4290 C  CG  . ARG B  1  216 ? 10.313  -24.033 47.232 1.00 57.16  ? 229 ARG B CG  1 
ATOM   4291 C  CD  . ARG B  1  216 ? 8.977   -23.313 47.354 1.00 60.69  ? 229 ARG B CD  1 
ATOM   4292 N  NE  . ARG B  1  216 ? 9.128   -21.921 47.798 1.00 65.72  ? 229 ARG B NE  1 
ATOM   4293 C  CZ  . ARG B  1  216 ? 9.545   -20.887 47.054 1.00 74.12  ? 229 ARG B CZ  1 
ATOM   4294 N  NH1 . ARG B  1  216 ? 9.787   -21.017 45.761 1.00 71.75  ? 229 ARG B NH1 1 
ATOM   4295 N  NH2 . ARG B  1  216 ? 9.695   -19.690 47.597 1.00 74.01  ? 229 ARG B NH2 1 
ATOM   4296 N  N   . LYS B  1  217 ? 14.417  -24.340 49.368 1.00 46.11  ? 230 LYS B N   1 
ATOM   4297 C  CA  . LYS B  1  217 ? 15.469  -24.219 50.365 1.00 43.79  ? 230 LYS B CA  1 
ATOM   4298 C  C   . LYS B  1  217 ? 16.299  -22.986 50.027 1.00 40.90  ? 230 LYS B C   1 
ATOM   4299 O  O   . LYS B  1  217 ? 16.500  -22.672 48.855 1.00 40.46  ? 230 LYS B O   1 
ATOM   4300 C  CB  . LYS B  1  217 ? 16.326  -25.490 50.367 1.00 45.62  ? 230 LYS B CB  1 
ATOM   4301 C  CG  . LYS B  1  217 ? 17.144  -25.702 49.102 1.00 46.55  ? 230 LYS B CG  1 
ATOM   4302 C  CD  . LYS B  1  217 ? 17.839  -27.051 48.980 1.00 52.85  ? 230 LYS B CD  1 
ATOM   4303 C  CE  . LYS B  1  217 ? 18.719  -27.080 47.756 1.00 58.20  ? 230 LYS B CE  1 
ATOM   4304 N  NZ  . LYS B  1  217 ? 19.482  -28.319 47.586 1.00 60.77  ? 230 LYS B NZ  1 
ATOM   4305 N  N   . LEU B  1  218 ? 16.790  -22.296 51.062 1.00 39.70  ? 231 LEU B N   1 
ATOM   4306 C  CA  . LEU B  1  218 ? 17.492  -21.038 50.878 1.00 35.26  ? 231 LEU B CA  1 
ATOM   4307 C  C   . LEU B  1  218 ? 18.993  -21.248 51.075 1.00 34.66  ? 231 LEU B C   1 
ATOM   4308 O  O   . LEU B  1  218 ? 19.411  -21.799 52.084 1.00 36.29  ? 231 LEU B O   1 
ATOM   4309 C  CB  . LEU B  1  218 ? 16.932  -20.031 51.877 1.00 32.54  ? 231 LEU B CB  1 
ATOM   4310 C  CG  . LEU B  1  218 ? 17.483  -18.610 51.744 1.00 35.62  ? 231 LEU B CG  1 
ATOM   4311 C  CD1 . LEU B  1  218 ? 17.034  -17.950 50.453 1.00 35.93  ? 231 LEU B CD1 1 
ATOM   4312 C  CD2 . LEU B  1  218 ? 17.085  -17.757 52.934 1.00 34.82  ? 231 LEU B CD2 1 
ATOM   4313 N  N   . SER B  1  219 ? 19.799  -20.773 50.120 1.00 33.58  ? 232 SER B N   1 
ATOM   4314 C  CA  . SER B  1  219 ? 21.250  -20.840 50.236 1.00 35.69  ? 232 SER B CA  1 
ATOM   4315 C  C   . SER B  1  219 ? 21.727  -19.795 51.240 1.00 38.59  ? 232 SER B C   1 
ATOM   4316 O  O   . SER B  1  219 ? 21.045  -18.807 51.503 1.00 40.61  ? 232 SER B O   1 
ATOM   4317 C  CB  . SER B  1  219 ? 21.914  -20.644 48.907 1.00 37.37  ? 232 SER B CB  1 
ATOM   4318 O  OG  . SER B  1  219 ? 21.732  -19.306 48.451 1.00 37.40  ? 232 SER B OG  1 
ATOM   4319 N  N   . MET B  1  220 ? 22.912  -20.023 51.805 1.00 38.50  ? 233 MET B N   1 
ATOM   4320 C  CA  . MET B  1  220 ? 23.465  -19.115 52.792 1.00 38.33  ? 233 MET B CA  1 
ATOM   4321 C  C   . MET B  1  220 ? 23.905  -17.814 52.116 1.00 37.06  ? 233 MET B C   1 
ATOM   4322 O  O   . MET B  1  220 ? 23.816  -16.746 52.717 1.00 37.22  ? 233 MET B O   1 
ATOM   4323 C  CB  . MET B  1  220 ? 24.620  -19.772 53.548 1.00 36.42  ? 233 MET B CB  1 
ATOM   4324 C  CG  . MET B  1  220 ? 24.215  -20.971 54.391 1.00 36.73  ? 233 MET B CG  1 
ATOM   4325 S  SD  . MET B  1  220 ? 22.903  -20.633 55.584 1.00 39.52  ? 233 MET B SD  1 
ATOM   4326 C  CE  . MET B  1  220 ? 21.483  -21.341 54.752 1.00 37.51  ? 233 MET B CE  1 
ATOM   4327 N  N   . GLU B  1  221 ? 24.336  -17.906 50.855 1.00 37.33  ? 234 GLU B N   1 
ATOM   4328 C  CA  . GLU B  1  221 ? 24.655  -16.731 50.054 1.00 39.84  ? 234 GLU B CA  1 
ATOM   4329 C  C   . GLU B  1  221 ? 23.424  -15.823 49.926 1.00 35.94  ? 234 GLU B C   1 
ATOM   4330 O  O   . GLU B  1  221 ? 23.510  -14.613 50.124 1.00 32.48  ? 234 GLU B O   1 
ATOM   4331 C  CB  . GLU B  1  221 ? 25.149  -17.116 48.656 1.00 42.16  ? 234 GLU B CB  1 
ATOM   4332 C  CG  . GLU B  1  221 ? 26.443  -17.931 48.632 1.00 45.92  ? 234 GLU B CG  1 
ATOM   4333 C  CD  . GLU B  1  221 ? 26.384  -19.405 49.038 1.00 51.46  ? 234 GLU B CD  1 
ATOM   4334 O  OE1 . GLU B  1  221 ? 25.287  -20.009 49.158 1.00 47.08  ? 234 GLU B OE1 1 
ATOM   4335 O  OE2 . GLU B  1  221 ? 27.478  -19.947 49.286 1.00 57.02  ? 234 GLU B OE2 1 
ATOM   4336 N  N   . ASP B  1  222 ? 22.277  -16.406 49.570 1.00 37.85  ? 235 ASP B N   1 
ATOM   4337 C  CA  . ASP B  1  222 ? 21.055  -15.637 49.374 1.00 35.66  ? 235 ASP B CA  1 
ATOM   4338 C  C   . ASP B  1  222 ? 20.584  -15.066 50.706 1.00 36.27  ? 235 ASP B C   1 
ATOM   4339 O  O   . ASP B  1  222 ? 20.174  -13.905 50.769 1.00 34.39  ? 235 ASP B O   1 
ATOM   4340 C  CB  . ASP B  1  222 ? 19.993  -16.452 48.657 1.00 38.41  ? 235 ASP B CB  1 
ATOM   4341 C  CG  . ASP B  1  222 ? 20.225  -16.682 47.170 1.00 41.91  ? 235 ASP B CG  1 
ATOM   4342 O  OD1 . ASP B  1  222 ? 21.208  -16.115 46.636 1.00 39.15  ? 235 ASP B OD1 1 
ATOM   4343 O  OD2 . ASP B  1  222 ? 19.419  -17.441 46.570 1.00 43.23  ? 235 ASP B OD2 1 
ATOM   4344 N  N   . ALA B  1  223 ? 20.685  -15.872 51.771 1.00 35.40  ? 236 ALA B N   1 
ATOM   4345 C  CA  . ALA B  1  223 ? 20.312  -15.426 53.100 1.00 36.08  ? 236 ALA B CA  1 
ATOM   4346 C  C   . ALA B  1  223 ? 21.144  -14.210 53.514 1.00 36.21  ? 236 ALA B C   1 
ATOM   4347 O  O   . ALA B  1  223 ? 20.589  -13.215 53.972 1.00 35.97  ? 236 ALA B O   1 
ATOM   4348 C  CB  . ALA B  1  223 ? 20.464  -16.569 54.077 1.00 39.93  ? 236 ALA B CB  1 
ATOM   4349 N  N   . ALA B  1  224 ? 22.473  -14.290 53.351 1.00 35.83  ? 237 ALA B N   1 
ATOM   4350 C  CA  . ALA B  1  224 ? 23.359  -13.219 53.771 1.00 34.26  ? 237 ALA B CA  1 
ATOM   4351 C  C   . ALA B  1  224 ? 23.055  -11.952 52.974 1.00 34.33  ? 237 ALA B C   1 
ATOM   4352 O  O   . ALA B  1  224 ? 23.003  -10.856 53.537 1.00 34.99  ? 237 ALA B O   1 
ATOM   4353 C  CB  . ALA B  1  224 ? 24.816  -13.623 53.612 1.00 33.78  ? 237 ALA B CB  1 
ATOM   4354 N  N   . SER B  1  225 ? 22.831  -12.113 51.667 1.00 32.53  ? 238 SER B N   1 
ATOM   4355 C  CA  . SER B  1  225 ? 22.520  -10.989 50.797 1.00 36.06  ? 238 SER B CA  1 
ATOM   4356 C  C   . SER B  1  225 ? 21.320  -10.194 51.331 1.00 38.46  ? 238 SER B C   1 
ATOM   4357 O  O   . SER B  1  225 ? 21.359  -8.964  51.372 1.00 38.10  ? 238 SER B O   1 
ATOM   4358 C  CB  . SER B  1  225 ? 22.294  -11.448 49.365 1.00 36.82  ? 238 SER B CB  1 
ATOM   4359 O  OG  . SER B  1  225 ? 22.071  -10.336 48.505 1.00 39.43  ? 238 SER B OG  1 
ATOM   4360 N  N   . ILE B  1  226 ? 20.260  -10.893 51.752 1.00 35.73  ? 239 ILE B N   1 
ATOM   4361 C  CA  . ILE B  1  226 ? 19.027  -10.237 52.170 1.00 37.70  ? 239 ILE B CA  1 
ATOM   4362 C  C   . ILE B  1  226 ? 19.140  -9.782  53.628 1.00 36.39  ? 239 ILE B C   1 
ATOM   4363 O  O   . ILE B  1  226 ? 18.909  -8.609  53.920 1.00 34.12  ? 239 ILE B O   1 
ATOM   4364 C  CB  . ILE B  1  226 ? 17.815  -11.159 51.948 1.00 36.99  ? 239 ILE B CB  1 
ATOM   4365 C  CG1 . ILE B  1  226 ? 17.581  -11.393 50.461 1.00 39.47  ? 239 ILE B CG1 1 
ATOM   4366 C  CG2 . ILE B  1  226 ? 16.564  -10.618 52.644 1.00 40.63  ? 239 ILE B CG2 1 
ATOM   4367 C  CD1 . ILE B  1  226 ? 16.659  -12.561 50.146 1.00 41.26  ? 239 ILE B CD1 1 
ATOM   4368 N  N   . PHE B  1  227 ? 19.500  -10.708 54.535 1.00 34.07  ? 240 PHE B N   1 
ATOM   4369 C  CA  . PHE B  1  227 ? 19.525  -10.434 55.963 1.00 34.48  ? 240 PHE B CA  1 
ATOM   4370 C  C   . PHE B  1  227 ? 20.591  -9.392  56.320 1.00 36.71  ? 240 PHE B C   1 
ATOM   4371 O  O   . PHE B  1  227 ? 20.354  -8.570  57.205 1.00 36.15  ? 240 PHE B O   1 
ATOM   4372 C  CB  . PHE B  1  227 ? 19.767  -11.687 56.808 1.00 36.90  ? 240 PHE B CB  1 
ATOM   4373 C  CG  . PHE B  1  227 ? 18.602  -12.655 56.962 1.00 37.17  ? 240 PHE B CG  1 
ATOM   4374 C  CD1 . PHE B  1  227 ? 17.564  -12.387 57.840 1.00 39.07  ? 240 PHE B CD1 1 
ATOM   4375 C  CD2 . PHE B  1  227 ? 18.591  -13.876 56.305 1.00 39.44  ? 240 PHE B CD2 1 
ATOM   4376 C  CE1 . PHE B  1  227 ? 16.513  -13.284 58.000 1.00 39.19  ? 240 PHE B CE1 1 
ATOM   4377 C  CE2 . PHE B  1  227 ? 17.544  -14.770 56.467 1.00 41.20  ? 240 PHE B CE2 1 
ATOM   4378 C  CZ  . PHE B  1  227 ? 16.506  -14.471 57.314 1.00 39.85  ? 240 PHE B CZ  1 
ATOM   4379 N  N   . ARG B  1  228 ? 21.779  -9.461  55.693 1.00 34.40  ? 241 ARG B N   1 
ATOM   4380 C  CA  . ARG B  1  228 ? 22.883  -8.576  56.047 1.00 31.54  ? 241 ARG B CA  1 
ATOM   4381 C  C   . ARG B  1  228 ? 22.901  -7.359  55.123 1.00 32.78  ? 241 ARG B C   1 
ATOM   4382 O  O   . ARG B  1  228 ? 22.928  -6.233  55.602 1.00 34.29  ? 241 ARG B O   1 
ATOM   4383 C  CB  . ARG B  1  228 ? 24.244  -9.281  56.016 1.00 32.52  ? 241 ARG B CB  1 
ATOM   4384 C  CG  . ARG B  1  228 ? 25.404  -8.384  56.438 1.00 33.95  ? 241 ARG B CG  1 
ATOM   4385 C  CD  . ARG B  1  228 ? 26.746  -9.097  56.651 1.00 35.30  ? 241 ARG B CD  1 
ATOM   4386 N  NE  . ARG B  1  228 ? 27.251  -9.771  55.452 1.00 35.76  ? 241 ARG B NE  1 
ATOM   4387 C  CZ  . ARG B  1  228 ? 27.485  -11.071 55.283 1.00 36.96  ? 241 ARG B CZ  1 
ATOM   4388 N  NH1 . ARG B  1  228 ? 27.394  -11.928 56.284 1.00 40.67  ? 241 ARG B NH1 1 
ATOM   4389 N  NH2 . ARG B  1  228 ? 27.846  -11.523 54.091 1.00 38.35  ? 241 ARG B NH2 1 
ATOM   4390 N  N   . ASP B  1  229 ? 22.881  -7.578  53.800 1.00 33.22  ? 242 ASP B N   1 
ATOM   4391 C  CA  . ASP B  1  229 ? 23.175  -6.512  52.853 1.00 32.99  ? 242 ASP B CA  1 
ATOM   4392 C  C   . ASP B  1  229 ? 21.910  -5.822  52.343 1.00 33.65  ? 242 ASP B C   1 
ATOM   4393 O  O   . ASP B  1  229 ? 22.010  -4.799  51.669 1.00 33.86  ? 242 ASP B O   1 
ATOM   4394 C  CB  . ASP B  1  229 ? 24.043  -7.017  51.711 1.00 35.56  ? 242 ASP B CB  1 
ATOM   4395 C  CG  . ASP B  1  229 ? 25.433  -7.497  52.107 1.00 36.78  ? 242 ASP B CG  1 
ATOM   4396 O  OD1 . ASP B  1  229 ? 25.932  -7.068  53.174 1.00 34.61  ? 242 ASP B OD1 1 
ATOM   4397 O  OD2 . ASP B  1  229 ? 25.972  -8.355  51.383 1.00 38.38  ? 242 ASP B OD2 1 
ATOM   4398 N  N   . MET B  1  230 ? 20.728  -6.363  52.661 1.00 34.99  ? 243 MET B N   1 
ATOM   4399 C  CA  A MET B  1  230 ? 19.471  -5.773  52.216 0.50 35.23  ? 243 MET B CA  1 
ATOM   4400 C  CA  B MET B  1  230 ? 19.469  -5.779  52.212 0.50 36.52  ? 243 MET B CA  1 
ATOM   4401 C  C   . MET B  1  230 ? 19.413  -5.752  50.688 1.00 34.53  ? 243 MET B C   1 
ATOM   4402 O  O   . MET B  1  230 ? 18.962  -4.775  50.097 1.00 37.84  ? 243 MET B O   1 
ATOM   4403 C  CB  A MET B  1  230 ? 19.315  -4.332  52.725 0.50 34.25  ? 243 MET B CB  1 
ATOM   4404 C  CB  B MET B  1  230 ? 19.308  -4.345  52.728 0.50 37.38  ? 243 MET B CB  1 
ATOM   4405 C  CG  A MET B  1  230 ? 19.587  -4.142  54.211 0.50 34.16  ? 243 MET B CG  1 
ATOM   4406 C  CG  B MET B  1  230 ? 19.453  -4.238  54.226 0.50 39.16  ? 243 MET B CG  1 
ATOM   4407 S  SD  A MET B  1  230 ? 19.696  -2.402  54.674 0.50 32.26  ? 243 MET B SD  1 
ATOM   4408 S  SD  B MET B  1  230 ? 19.186  -2.556  54.809 0.50 39.42  ? 243 MET B SD  1 
ATOM   4409 C  CE  A MET B  1  230 ? 20.153  -2.656  56.397 0.50 34.95  ? 243 MET B CE  1 
ATOM   4410 C  CE  B MET B  1  230 ? 20.807  -1.853  54.480 0.50 37.80  ? 243 MET B CE  1 
ATOM   4411 N  N   . ARG B  1  231 ? 19.859  -6.849  50.059 1.00 38.43  ? 244 ARG B N   1 
ATOM   4412 C  CA  A ARG B  1  231 ? 19.999  -6.916  48.612 0.50 35.97  ? 244 ARG B CA  1 
ATOM   4413 C  CA  B ARG B  1  231 ? 19.996  -6.916  48.613 0.50 36.23  ? 244 ARG B CA  1 
ATOM   4414 C  C   . ARG B  1  231 ? 19.345  -8.197  48.104 1.00 34.28  ? 244 ARG B C   1 
ATOM   4415 O  O   . ARG B  1  231 ? 19.593  -9.280  48.634 1.00 33.81  ? 244 ARG B O   1 
ATOM   4416 C  CB  A ARG B  1  231 ? 21.489  -6.871  48.241 0.50 37.37  ? 244 ARG B CB  1 
ATOM   4417 C  CB  B ARG B  1  231 ? 21.490  -6.875  48.266 0.50 37.97  ? 244 ARG B CB  1 
ATOM   4418 C  CG  A ARG B  1  231 ? 21.783  -6.797  46.745 0.50 38.13  ? 244 ARG B CG  1 
ATOM   4419 C  CG  B ARG B  1  231 ? 21.847  -6.814  46.787 0.50 39.29  ? 244 ARG B CG  1 
ATOM   4420 C  CD  A ARG B  1  231 ? 23.273  -6.861  46.401 0.50 38.71  ? 244 ARG B CD  1 
ATOM   4421 C  CD  B ARG B  1  231 ? 23.381  -6.818  46.627 0.50 40.12  ? 244 ARG B CD  1 
ATOM   4422 N  NE  A ARG B  1  231 ? 23.813  -8.216  46.566 0.50 40.18  ? 244 ARG B NE  1 
ATOM   4423 N  NE  B ARG B  1  231 ? 24.019  -8.066  47.072 0.50 42.46  ? 244 ARG B NE  1 
ATOM   4424 C  CZ  A ARG B  1  231 ? 23.602  -9.246  45.747 0.50 39.91  ? 244 ARG B CZ  1 
ATOM   4425 C  CZ  B ARG B  1  231 ? 24.905  -8.229  48.065 0.50 42.18  ? 244 ARG B CZ  1 
ATOM   4426 N  NH1 A ARG B  1  231 ? 23.064  -9.047  44.554 0.50 40.52  ? 244 ARG B NH1 1 
ATOM   4427 N  NH1 B ARG B  1  231 ? 25.380  -7.199  48.746 0.50 44.78  ? 244 ARG B NH1 1 
ATOM   4428 N  NH2 A ARG B  1  231 ? 23.935  -10.471 46.131 0.50 37.02  ? 244 ARG B NH2 1 
ATOM   4429 N  NH2 B ARG B  1  231 ? 25.323  -9.441  48.373 0.50 41.34  ? 244 ARG B NH2 1 
ATOM   4430 N  N   . PHE B  1  232 ? 18.511  -8.062  47.068 1.00 34.60  ? 245 PHE B N   1 
ATOM   4431 C  CA  . PHE B  1  232 ? 17.961  -9.219  46.387 1.00 38.39  ? 245 PHE B CA  1 
ATOM   4432 C  C   . PHE B  1  232 ? 19.101  -10.018 45.765 1.00 37.87  ? 245 PHE B C   1 
ATOM   4433 O  O   . PHE B  1  232 ? 20.061  -9.433  45.275 1.00 37.62  ? 245 PHE B O   1 
ATOM   4434 C  CB  . PHE B  1  232 ? 17.009  -8.826  45.262 1.00 39.60  ? 245 PHE B CB  1 
ATOM   4435 C  CG  . PHE B  1  232 ? 15.651  -8.312  45.707 1.00 38.48  ? 245 PHE B CG  1 
ATOM   4436 C  CD1 . PHE B  1  232 ? 14.758  -9.153  46.353 1.00 39.43  ? 245 PHE B CD1 1 
ATOM   4437 C  CD2 . PHE B  1  232 ? 15.233  -7.026  45.382 1.00 40.07  ? 245 PHE B CD2 1 
ATOM   4438 C  CE1 . PHE B  1  232 ? 13.492  -8.701  46.707 1.00 41.19  ? 245 PHE B CE1 1 
ATOM   4439 C  CE2 . PHE B  1  232 ? 13.960  -6.579  45.728 1.00 40.61  ? 245 PHE B CE2 1 
ATOM   4440 C  CZ  . PHE B  1  232 ? 13.098  -7.415  46.402 1.00 40.89  ? 245 PHE B CZ  1 
ATOM   4441 N  N   . PRO B  1  233 ? 19.033  -11.367 45.757 1.00 37.60  ? 246 PRO B N   1 
ATOM   4442 C  CA  . PRO B  1  233 ? 19.937  -12.159 44.930 1.00 35.97  ? 246 PRO B CA  1 
ATOM   4443 C  C   . PRO B  1  233 ? 19.854  -11.665 43.488 1.00 36.69  ? 246 PRO B C   1 
ATOM   4444 O  O   . PRO B  1  233 ? 18.825  -11.139 43.073 1.00 39.52  ? 246 PRO B O   1 
ATOM   4445 C  CB  . PRO B  1  233 ? 19.451  -13.614 45.103 1.00 36.34  ? 246 PRO B CB  1 
ATOM   4446 C  CG  . PRO B  1  233 ? 18.657  -13.605 46.398 1.00 37.12  ? 246 PRO B CG  1 
ATOM   4447 C  CD  . PRO B  1  233 ? 18.093  -12.190 46.535 1.00 36.95  ? 246 PRO B CD  1 
ATOM   4448 N  N   . ASP B  1  234 ? 20.959  -11.808 42.745 1.00 38.53  ? 247 ASP B N   1 
ATOM   4449 C  CA  . ASP B  1  234 ? 20.973  -11.522 41.318 1.00 41.40  ? 247 ASP B CA  1 
ATOM   4450 C  C   . ASP B  1  234 ? 19.807  -12.258 40.646 1.00 41.53  ? 247 ASP B C   1 
ATOM   4451 O  O   . ASP B  1  234 ? 19.561  -13.428 40.939 1.00 39.57  ? 247 ASP B O   1 
ATOM   4452 C  CB  . ASP B  1  234 ? 22.289  -11.927 40.669 1.00 40.42  ? 247 ASP B CB  1 
ATOM   4453 C  CG  . ASP B  1  234 ? 23.532  -11.126 41.063 1.00 41.76  ? 247 ASP B CG  1 
ATOM   4454 O  OD1 . ASP B  1  234 ? 23.440  -10.234 41.939 1.00 38.00  ? 247 ASP B OD1 1 
ATOM   4455 O  OD2 . ASP B  1  234 ? 24.613  -11.387 40.484 1.00 40.61  ? 247 ASP B OD2 1 
ATOM   4456 N  N   . ASP B  1  235 ? 19.097  -11.552 39.756 1.00 38.75  ? 248 ASP B N   1 
ATOM   4457 C  CA  . ASP B  1  235 ? 18.053  -12.132 38.924 1.00 44.49  ? 248 ASP B CA  1 
ATOM   4458 C  C   . ASP B  1  235 ? 16.906  -12.694 39.773 1.00 42.94  ? 248 ASP B C   1 
ATOM   4459 O  O   . ASP B  1  235 ? 16.242  -13.646 39.364 1.00 44.01  ? 248 ASP B O   1 
ATOM   4460 C  CB  . ASP B  1  235 ? 18.631  -13.177 37.975 1.00 43.94  ? 248 ASP B CB  1 
ATOM   4461 C  CG  . ASP B  1  235 ? 17.656  -13.673 36.913 1.00 44.39  ? 248 ASP B CG  1 
ATOM   4462 O  OD1 . ASP B  1  235 ? 17.049  -12.824 36.240 1.00 43.84  ? 248 ASP B OD1 1 
ATOM   4463 O  OD2 . ASP B  1  235 ? 17.493  -14.902 36.790 1.00 47.24  ? 248 ASP B OD2 1 
ATOM   4464 N  N   . PHE B  1  236 ? 16.649  -12.091 40.938 1.00 39.08  ? 249 PHE B N   1 
ATOM   4465 C  CA  . PHE B  1  236 ? 15.708  -12.665 41.883 1.00 38.56  ? 249 PHE B CA  1 
ATOM   4466 C  C   . PHE B  1  236 ? 14.292  -12.582 41.318 1.00 38.37  ? 249 PHE B C   1 
ATOM   4467 O  O   . PHE B  1  236 ? 13.850  -11.510 40.912 1.00 36.67  ? 249 PHE B O   1 
ATOM   4468 C  CB  . PHE B  1  236 ? 15.731  -11.968 43.245 1.00 38.41  ? 249 PHE B CB  1 
ATOM   4469 C  CG  . PHE B  1  236 ? 14.764  -12.583 44.246 1.00 38.33  ? 249 PHE B CG  1 
ATOM   4470 C  CD1 . PHE B  1  236 ? 15.023  -13.827 44.802 1.00 38.78  ? 249 PHE B CD1 1 
ATOM   4471 C  CD2 . PHE B  1  236 ? 13.607  -11.914 44.635 1.00 44.28  ? 249 PHE B CD2 1 
ATOM   4472 C  CE1 . PHE B  1  236 ? 14.151  -14.385 45.724 1.00 40.74  ? 249 PHE B CE1 1 
ATOM   4473 C  CE2 . PHE B  1  236 ? 12.729  -12.482 45.552 1.00 41.62  ? 249 PHE B CE2 1 
ATOM   4474 C  CZ  . PHE B  1  236 ? 13.018  -13.711 46.101 1.00 42.29  ? 249 PHE B CZ  1 
ATOM   4475 N  N   . HIS B  1  237 ? 13.601  -13.727 41.318 1.00 36.83  ? 250 HIS B N   1 
ATOM   4476 C  CA  . HIS B  1  237 ? 12.196  -13.794 40.952 1.00 39.76  ? 250 HIS B CA  1 
ATOM   4477 C  C   . HIS B  1  237 ? 11.370  -14.077 42.204 1.00 41.29  ? 250 HIS B C   1 
ATOM   4478 O  O   . HIS B  1  237 ? 11.650  -15.024 42.943 1.00 37.57  ? 250 HIS B O   1 
ATOM   4479 C  CB  . HIS B  1  237 ? 11.952  -14.868 39.884 1.00 43.50  ? 250 HIS B CB  1 
ATOM   4480 C  CG  . HIS B  1  237 ? 12.382  -14.481 38.505 1.00 44.99  ? 250 HIS B CG  1 
ATOM   4481 N  ND1 . HIS B  1  237 ? 13.653  -14.040 38.209 1.00 46.89  ? 250 HIS B ND1 1 
ATOM   4482 C  CD2 . HIS B  1  237 ? 11.710  -14.501 37.342 1.00 45.21  ? 250 HIS B CD2 1 
ATOM   4483 C  CE1 . HIS B  1  237 ? 13.726  -13.780 36.907 1.00 46.21  ? 250 HIS B CE1 1 
ATOM   4484 N  NE2 . HIS B  1  237 ? 12.550  -14.052 36.365 1.00 45.65  ? 250 HIS B NE2 1 
ATOM   4485 N  N   . ARG B  1  238 ? 10.325  -13.267 42.411 1.00 43.29  ? 251 ARG B N   1 
ATOM   4486 C  CA  . ARG B  1  238 ? 9.454   -13.425 43.562 1.00 45.09  ? 251 ARG B CA  1 
ATOM   4487 C  C   . ARG B  1  238 ? 8.676   -14.735 43.475 1.00 44.13  ? 251 ARG B C   1 
ATOM   4488 O  O   . ARG B  1  238 ? 8.565   -15.324 42.408 1.00 41.06  ? 251 ARG B O   1 
ATOM   4489 C  CB  . ARG B  1  238 ? 8.452   -12.273 43.661 1.00 44.52  ? 251 ARG B CB  1 
ATOM   4490 C  CG  . ARG B  1  238 ? 7.448   -12.214 42.524 1.00 44.36  ? 251 ARG B CG  1 
ATOM   4491 C  CD  . ARG B  1  238 ? 6.502   -11.049 42.678 1.00 46.50  ? 251 ARG B CD  1 
ATOM   4492 N  NE  . ARG B  1  238 ? 5.300   -11.249 41.863 1.00 46.57  ? 251 ARG B NE  1 
ATOM   4493 C  CZ  . ARG B  1  238 ? 4.329   -10.371 41.676 1.00 48.95  ? 251 ARG B CZ  1 
ATOM   4494 N  NH1 . ARG B  1  238 ? 4.357   -9.199  42.279 1.00 52.23  ? 251 ARG B NH1 1 
ATOM   4495 N  NH2 . ARG B  1  238 ? 3.326   -10.666 40.879 1.00 54.33  ? 251 ARG B NH2 1 
ATOM   4496 N  N   . SER B  1  239 ? 8.136   -15.159 44.625 1.00 43.70  ? 252 SER B N   1 
ATOM   4497 C  CA  . SER B  1  239 ? 7.216   -16.276 44.725 1.00 44.46  ? 252 SER B CA  1 
ATOM   4498 C  C   . SER B  1  239 ? 6.206   -16.250 43.581 1.00 43.83  ? 252 SER B C   1 
ATOM   4499 O  O   . SER B  1  239 ? 5.718   -15.188 43.211 1.00 38.33  ? 252 SER B O   1 
ATOM   4500 C  CB  . SER B  1  239 ? 6.506   -16.262 46.056 1.00 44.24  ? 252 SER B CB  1 
ATOM   4501 O  OG  . SER B  1  239 ? 5.557   -17.313 46.128 1.00 40.73  ? 252 SER B OG  1 
ATOM   4502 N  N   . ALA B  1  240 ? 5.889   -17.443 43.056 1.00 42.92  ? 253 ALA B N   1 
ATOM   4503 C  CA  . ALA B  1  240 ? 4.997   -17.600 41.919 1.00 44.62  ? 253 ALA B CA  1 
ATOM   4504 C  C   . ALA B  1  240 ? 3.535   -17.458 42.348 1.00 45.70  ? 253 ALA B C   1 
ATOM   4505 O  O   . ALA B  1  240 ? 2.657   -17.367 41.494 1.00 46.10  ? 253 ALA B O   1 
ATOM   4506 C  CB  . ALA B  1  240 ? 5.245   -18.942 41.264 1.00 47.56  ? 253 ALA B CB  1 
ATOM   4507 N  N   . VAL B  1  241 ? 3.287   -17.469 43.667 1.00 44.91  ? 254 VAL B N   1 
ATOM   4508 C  CA  . VAL B  1  241 ? 1.965   -17.240 44.222 1.00 47.24  ? 254 VAL B CA  1 
ATOM   4509 C  C   . VAL B  1  241 ? 2.085   -16.312 45.424 1.00 46.50  ? 254 VAL B C   1 
ATOM   4510 O  O   . VAL B  1  241 ? 3.116   -16.294 46.097 1.00 45.43  ? 254 VAL B O   1 
ATOM   4511 C  CB  . VAL B  1  241 ? 1.283   -18.554 44.655 1.00 50.57  ? 254 VAL B CB  1 
ATOM   4512 C  CG1 . VAL B  1  241 ? 0.983   -19.464 43.467 1.00 49.82  ? 254 VAL B CG1 1 
ATOM   4513 C  CG2 . VAL B  1  241 ? 2.094   -19.298 45.711 1.00 49.71  ? 254 VAL B CG2 1 
ATOM   4514 N  N   . PRO B  1  242 ? 1.010   -15.562 45.765 1.00 45.20  ? 255 PRO B N   1 
ATOM   4515 C  CA  . PRO B  1  242 ? 0.941   -14.855 47.043 1.00 42.76  ? 255 PRO B CA  1 
ATOM   4516 C  C   . PRO B  1  242 ? 1.227   -15.851 48.160 1.00 42.96  ? 255 PRO B C   1 
ATOM   4517 O  O   . PRO B  1  242 ? 0.714   -16.969 48.134 1.00 43.59  ? 255 PRO B O   1 
ATOM   4518 C  CB  . PRO B  1  242 ? -0.493  -14.307 47.087 1.00 44.81  ? 255 PRO B CB  1 
ATOM   4519 C  CG  . PRO B  1  242 ? -0.887  -14.195 45.631 1.00 42.62  ? 255 PRO B CG  1 
ATOM   4520 C  CD  . PRO B  1  242 ? -0.203  -15.372 44.951 1.00 44.67  ? 255 PRO B CD  1 
ATOM   4521 N  N   . ALA B  1  243 ? 2.070   -15.455 49.121 1.00 41.09  ? 256 ALA B N   1 
ATOM   4522 C  CA  . ALA B  1  243 ? 2.437   -16.345 50.208 1.00 40.59  ? 256 ALA B CA  1 
ATOM   4523 C  C   . ALA B  1  243 ? 2.784   -15.543 51.458 1.00 39.24  ? 256 ALA B C   1 
ATOM   4524 O  O   . ALA B  1  243 ? 2.987   -14.332 51.394 1.00 42.17  ? 256 ALA B O   1 
ATOM   4525 C  CB  . ALA B  1  243 ? 3.595   -17.219 49.784 1.00 42.21  ? 256 ALA B CB  1 
ATOM   4526 N  N   . SER B  1  244 ? 2.831   -16.254 52.587 1.00 39.44  ? 257 SER B N   1 
ATOM   4527 C  CA  . SER B  1  244 ? 3.164   -15.676 53.874 1.00 40.58  ? 257 SER B CA  1 
ATOM   4528 C  C   . SER B  1  244 ? 3.716   -16.769 54.782 1.00 41.59  ? 257 SER B C   1 
ATOM   4529 O  O   . SER B  1  244 ? 4.878   -17.146 54.632 1.00 41.67  ? 257 SER B O   1 
ATOM   4530 C  CB  . SER B  1  244 ? 1.976   -14.966 54.478 1.00 40.51  ? 257 SER B CB  1 
ATOM   4531 O  OG  . SER B  1  244 ? 0.847   -15.823 54.565 1.00 42.58  ? 257 SER B OG  1 
ATOM   4532 N  N   . ASN B  1  245 ? 2.868   -17.316 55.666 1.00 40.06  ? 258 ASN B N   1 
ATOM   4533 C  CA  . ASN B  1  245 ? 3.337   -18.107 56.793 1.00 41.19  ? 258 ASN B CA  1 
ATOM   4534 C  C   . ASN B  1  245 ? 3.053   -19.594 56.600 1.00 40.79  ? 258 ASN B C   1 
ATOM   4535 O  O   . ASN B  1  245 ? 2.929   -20.316 57.589 1.00 42.65  ? 258 ASN B O   1 
ATOM   4536 C  CB  . ASN B  1  245 ? 2.725   -17.624 58.106 1.00 41.69  ? 258 ASN B CB  1 
ATOM   4537 C  CG  . ASN B  1  245 ? 1.227   -17.802 58.143 1.00 47.03  ? 258 ASN B CG  1 
ATOM   4538 O  OD1 . ASN B  1  245 ? 0.589   -17.957 57.098 1.00 48.22  ? 258 ASN B OD1 1 
ATOM   4539 N  ND2 . ASN B  1  245 ? 0.648   -17.788 59.335 1.00 54.98  ? 258 ASN B ND2 1 
ATOM   4540 N  N   . GLU B  1  246 ? 2.990   -20.060 55.345 1.00 41.47  ? 259 GLU B N   1 
ATOM   4541 C  CA  . GLU B  1  246 ? 2.773   -21.474 55.086 1.00 44.56  ? 259 GLU B CA  1 
ATOM   4542 C  C   . GLU B  1  246 ? 3.871   -22.283 55.775 1.00 45.51  ? 259 GLU B C   1 
ATOM   4543 O  O   . GLU B  1  246 ? 5.059   -21.996 55.589 1.00 45.92  ? 259 GLU B O   1 
ATOM   4544 C  CB  . GLU B  1  246 ? 2.748   -21.805 53.591 1.00 46.74  ? 259 GLU B CB  1 
ATOM   4545 C  CG  . GLU B  1  246 ? 1.526   -21.252 52.855 1.00 48.64  ? 259 GLU B CG  1 
ATOM   4546 C  CD  . GLU B  1  246 ? 1.594   -19.779 52.494 1.00 49.66  ? 259 GLU B CD  1 
ATOM   4547 O  OE1 . GLU B  1  246 ? 2.613   -19.123 52.829 1.00 45.36  ? 259 GLU B OE1 1 
ATOM   4548 O  OE2 . GLU B  1  246 ? 0.620   -19.283 51.883 1.00 51.75  ? 259 GLU B OE2 1 
ATOM   4549 N  N   . GLY B  1  247 ? 3.457   -23.264 56.601 1.00 41.38  ? 260 GLY B N   1 
ATOM   4550 C  CA  . GLY B  1  247 ? 4.387   -24.191 57.230 1.00 41.02  ? 260 GLY B CA  1 
ATOM   4551 C  C   . GLY B  1  247 ? 4.759   -23.807 58.662 1.00 40.96  ? 260 GLY B C   1 
ATOM   4552 O  O   . GLY B  1  247 ? 5.467   -24.558 59.331 1.00 44.74  ? 260 GLY B O   1 
ATOM   4553 N  N   . ALA B  1  248 ? 4.276   -22.655 59.146 1.00 38.82  ? 261 ALA B N   1 
ATOM   4554 C  CA  . ALA B  1  248 ? 4.607   -22.187 60.487 1.00 42.91  ? 261 ALA B CA  1 
ATOM   4555 C  C   . ALA B  1  248 ? 4.080   -23.147 61.560 1.00 45.76  ? 261 ALA B C   1 
ATOM   4556 O  O   . ALA B  1  248 ? 4.697   -23.302 62.616 1.00 45.15  ? 261 ALA B O   1 
ATOM   4557 C  CB  . ALA B  1  248 ? 4.071   -20.785 60.688 1.00 40.92  ? 261 ALA B CB  1 
ATOM   4558 N  N   . ASP B  1  249 ? 2.924   -23.767 61.283 1.00 48.14  ? 262 ASP B N   1 
ATOM   4559 C  CA  . ASP B  1  249 ? 2.346   -24.808 62.124 1.00 53.25  ? 262 ASP B CA  1 
ATOM   4560 C  C   . ASP B  1  249 ? 3.346   -25.945 62.372 1.00 53.09  ? 262 ASP B C   1 
ATOM   4561 O  O   . ASP B  1  249 ? 3.426   -26.459 63.484 1.00 54.87  ? 262 ASP B O   1 
ATOM   4562 C  CB  . ASP B  1  249 ? 1.040   -25.327 61.530 1.00 55.85  ? 262 ASP B CB  1 
ATOM   4563 C  CG  . ASP B  1  249 ? 1.080   -25.735 60.057 1.00 63.87  ? 262 ASP B CG  1 
ATOM   4564 O  OD1 . ASP B  1  249 ? 2.151   -25.574 59.409 1.00 61.66  ? 262 ASP B OD1 1 
ATOM   4565 O  OD2 . ASP B  1  249 ? 0.031   -26.196 59.552 1.00 64.36  ? 262 ASP B OD2 1 
ATOM   4566 N  N   . GLN B  1  250 ? 4.090   -26.354 61.336 1.00 46.84  ? 263 GLN B N   1 
ATOM   4567 C  CA  . GLN B  1  250 ? 5.008   -27.478 61.443 1.00 52.27  ? 263 GLN B CA  1 
ATOM   4568 C  C   . GLN B  1  250 ? 6.251   -27.112 62.253 1.00 49.07  ? 263 GLN B C   1 
ATOM   4569 O  O   . GLN B  1  250 ? 6.868   -27.989 62.859 1.00 48.72  ? 263 GLN B O   1 
ATOM   4570 C  CB  . GLN B  1  250 ? 5.486   -27.961 60.076 1.00 53.82  ? 263 GLN B CB  1 
ATOM   4571 C  CG  . GLN B  1  250 ? 4.393   -28.573 59.208 1.00 55.93  ? 263 GLN B CG  1 
ATOM   4572 C  CD  . GLN B  1  250 ? 4.923   -29.028 57.864 1.00 55.93  ? 263 GLN B CD  1 
ATOM   4573 O  OE1 . GLN B  1  250 ? 5.900   -29.779 57.792 1.00 59.71  ? 263 GLN B OE1 1 
ATOM   4574 N  NE2 . GLN B  1  250 ? 4.316   -28.551 56.787 1.00 53.69  ? 263 GLN B NE2 1 
ATOM   4575 N  N   . VAL B  1  251 ? 6.625   -25.826 62.231 1.00 45.96  ? 264 VAL B N   1 
ATOM   4576 C  CA  . VAL B  1  251 ? 7.751   -25.329 63.008 1.00 44.53  ? 264 VAL B CA  1 
ATOM   4577 C  C   . VAL B  1  251 ? 7.419   -25.447 64.493 1.00 46.67  ? 264 VAL B C   1 
ATOM   4578 O  O   . VAL B  1  251 ? 8.258   -25.868 65.286 1.00 47.85  ? 264 VAL B O   1 
ATOM   4579 C  CB  . VAL B  1  251 ? 8.092   -23.876 62.613 1.00 44.27  ? 264 VAL B CB  1 
ATOM   4580 C  CG1 . VAL B  1  251 ? 9.076   -23.218 63.568 1.00 43.53  ? 264 VAL B CG1 1 
ATOM   4581 C  CG2 . VAL B  1  251 ? 8.611   -23.781 61.181 1.00 43.89  ? 264 VAL B CG2 1 
ATOM   4582 N  N   . LEU B  1  252 ? 6.194   -25.048 64.861 1.00 50.41  ? 265 LEU B N   1 
ATOM   4583 C  CA  . LEU B  1  252 ? 5.706   -25.191 66.224 1.00 52.55  ? 265 LEU B CA  1 
ATOM   4584 C  C   . LEU B  1  252 ? 5.629   -26.671 66.597 1.00 49.52  ? 265 LEU B C   1 
ATOM   4585 O  O   . LEU B  1  252 ? 6.055   -27.043 67.684 1.00 52.95  ? 265 LEU B O   1 
ATOM   4586 C  CB  . LEU B  1  252 ? 4.345   -24.511 66.376 1.00 55.33  ? 265 LEU B CB  1 
ATOM   4587 C  CG  . LEU B  1  252 ? 3.776   -24.462 67.796 1.00 57.59  ? 265 LEU B CG  1 
ATOM   4588 C  CD1 . LEU B  1  252 ? 4.624   -23.602 68.712 1.00 56.03  ? 265 LEU B CD1 1 
ATOM   4589 C  CD2 . LEU B  1  252 ? 2.343   -23.950 67.774 1.00 58.45  ? 265 LEU B CD2 1 
ATOM   4590 N  N   . ALA B  1  253 ? 5.094   -27.504 65.691 1.00 49.43  ? 266 ALA B N   1 
ATOM   4591 C  CA  . ALA B  1  253 ? 4.882   -28.921 65.962 1.00 49.97  ? 266 ALA B CA  1 
ATOM   4592 C  C   . ALA B  1  253 ? 6.203   -29.639 66.259 1.00 54.19  ? 266 ALA B C   1 
ATOM   4593 O  O   . ALA B  1  253 ? 6.226   -30.564 67.068 1.00 56.26  ? 266 ALA B O   1 
ATOM   4594 C  CB  . ALA B  1  253 ? 4.150   -29.574 64.810 1.00 47.04  ? 266 ALA B CB  1 
ATOM   4595 N  N   . ALA B  1  254 ? 7.301   -29.207 65.623 1.00 55.18  ? 267 ALA B N   1 
ATOM   4596 C  CA  . ALA B  1  254 ? 8.605   -29.826 65.829 1.00 54.92  ? 267 ALA B CA  1 
ATOM   4597 C  C   . ALA B  1  254 ? 9.080   -29.681 67.277 1.00 55.53  ? 267 ALA B C   1 
ATOM   4598 O  O   . ALA B  1  254 ? 9.800   -30.540 67.785 1.00 52.60  ? 267 ALA B O   1 
ATOM   4599 C  CB  . ALA B  1  254 ? 9.612   -29.237 64.864 1.00 53.50  ? 267 ALA B CB  1 
ATOM   4600 N  N   . HIS B  1  255 ? 8.710   -28.571 67.930 1.00 54.47  ? 268 HIS B N   1 
ATOM   4601 C  CA  . HIS B  1  255 ? 9.066   -28.343 69.322 1.00 53.83  ? 268 HIS B CA  1 
ATOM   4602 C  C   . HIS B  1  255 ? 7.947   -27.557 69.995 1.00 57.34  ? 268 HIS B C   1 
ATOM   4603 O  O   . HIS B  1  255 ? 8.055   -26.342 70.166 1.00 54.77  ? 268 HIS B O   1 
ATOM   4604 C  CB  . HIS B  1  255 ? 10.410  -27.617 69.444 1.00 57.99  ? 268 HIS B CB  1 
ATOM   4605 C  CG  . HIS B  1  255 ? 11.594  -28.454 69.096 1.00 63.55  ? 268 HIS B CG  1 
ATOM   4606 N  ND1 . HIS B  1  255 ? 12.117  -29.368 69.984 1.00 64.98  ? 268 HIS B ND1 1 
ATOM   4607 C  CD2 . HIS B  1  255 ? 12.347  -28.533 67.991 1.00 65.00  ? 268 HIS B CD2 1 
ATOM   4608 C  CE1 . HIS B  1  255 ? 13.150  -29.978 69.423 1.00 67.71  ? 268 HIS B CE1 1 
ATOM   4609 N  NE2 . HIS B  1  255 ? 13.308  -29.487 68.211 1.00 68.91  ? 268 HIS B NE2 1 
ATOM   4610 N  N   . PRO B  1  256 ? 6.836   -28.232 70.381 1.00 54.50  ? 269 PRO B N   1 
ATOM   4611 C  CA  . PRO B  1  256 ? 5.704   -27.567 71.022 1.00 54.79  ? 269 PRO B CA  1 
ATOM   4612 C  C   . PRO B  1  256 ? 6.170   -26.605 72.107 1.00 53.79  ? 269 PRO B C   1 
ATOM   4613 O  O   . PRO B  1  256 ? 7.059   -26.922 72.897 1.00 53.57  ? 269 PRO B O   1 
ATOM   4614 C  CB  . PRO B  1  256 ? 4.900   -28.746 71.593 1.00 56.45  ? 269 PRO B CB  1 
ATOM   4615 C  CG  . PRO B  1  256 ? 5.157   -29.854 70.593 1.00 56.73  ? 269 PRO B CG  1 
ATOM   4616 C  CD  . PRO B  1  256 ? 6.614   -29.676 70.212 1.00 53.31  ? 269 PRO B CD  1 
ATOM   4617 N  N   . TRP B  1  257 ? 5.561   -25.421 72.119 1.00 52.45  ? 270 TRP B N   1 
ATOM   4618 C  CA  . TRP B  1  257 ? 5.994   -24.365 73.012 1.00 52.48  ? 270 TRP B CA  1 
ATOM   4619 C  C   . TRP B  1  257 ? 4.801   -23.480 73.361 1.00 53.40  ? 270 TRP B C   1 
ATOM   4620 O  O   . TRP B  1  257 ? 3.894   -23.293 72.555 1.00 52.42  ? 270 TRP B O   1 
ATOM   4621 C  CB  . TRP B  1  257 ? 7.143   -23.560 72.383 1.00 48.99  ? 270 TRP B CB  1 
ATOM   4622 C  CG  . TRP B  1  257 ? 7.805   -22.647 73.374 1.00 47.30  ? 270 TRP B CG  1 
ATOM   4623 C  CD1 . TRP B  1  257 ? 7.629   -21.302 73.510 1.00 47.39  ? 270 TRP B CD1 1 
ATOM   4624 C  CD2 . TRP B  1  257 ? 8.697   -23.048 74.431 1.00 47.90  ? 270 TRP B CD2 1 
ATOM   4625 N  NE1 . TRP B  1  257 ? 8.373   -20.830 74.558 1.00 49.97  ? 270 TRP B NE1 1 
ATOM   4626 C  CE2 . TRP B  1  257 ? 9.034   -21.876 75.143 1.00 49.62  ? 270 TRP B CE2 1 
ATOM   4627 C  CE3 . TRP B  1  257 ? 9.239   -24.272 74.838 1.00 50.93  ? 270 TRP B CE3 1 
ATOM   4628 C  CZ2 . TRP B  1  257 ? 9.887   -21.896 76.243 1.00 51.38  ? 270 TRP B CZ2 1 
ATOM   4629 C  CZ3 . TRP B  1  257 ? 10.083  -24.290 75.928 1.00 52.46  ? 270 TRP B CZ3 1 
ATOM   4630 C  CH2 . TRP B  1  257 ? 10.396  -23.118 76.622 1.00 53.01  ? 270 TRP B CH2 1 
ATOM   4631 N  N   . VAL B  1  258 ? 4.829   -22.940 74.581 1.00 55.47  ? 271 VAL B N   1 
ATOM   4632 C  CA  . VAL B  1  258 ? 3.708   -22.190 75.115 1.00 59.41  ? 271 VAL B CA  1 
ATOM   4633 C  C   . VAL B  1  258 ? 4.167   -20.757 75.351 1.00 50.39  ? 271 VAL B C   1 
ATOM   4634 O  O   . VAL B  1  258 ? 5.291   -20.533 75.793 1.00 49.77  ? 271 VAL B O   1 
ATOM   4635 C  CB  . VAL B  1  258 ? 3.187   -22.853 76.407 1.00 64.57  ? 271 VAL B CB  1 
ATOM   4636 C  CG1 . VAL B  1  258 ? 2.111   -22.024 77.083 1.00 70.15  ? 271 VAL B CG1 1 
ATOM   4637 C  CG2 . VAL B  1  258 ? 2.662   -24.260 76.149 1.00 68.22  ? 271 VAL B CG2 1 
ATOM   4638 N  N   . PRO B  1  259 ? 3.325   -19.745 75.042 1.00 49.27  ? 272 PRO B N   1 
ATOM   4639 C  CA  . PRO B  1  259 ? 3.678   -18.353 75.309 1.00 51.67  ? 272 PRO B CA  1 
ATOM   4640 C  C   . PRO B  1  259 ? 3.963   -18.127 76.788 1.00 50.55  ? 272 PRO B C   1 
ATOM   4641 O  O   . PRO B  1  259 ? 3.373   -18.771 77.642 1.00 50.84  ? 272 PRO B O   1 
ATOM   4642 C  CB  . PRO B  1  259 ? 2.459   -17.550 74.814 1.00 50.43  ? 272 PRO B CB  1 
ATOM   4643 C  CG  . PRO B  1  259 ? 1.342   -18.568 74.757 1.00 50.31  ? 272 PRO B CG  1 
ATOM   4644 C  CD  . PRO B  1  259 ? 2.012   -19.871 74.387 1.00 49.22  ? 272 PRO B CD  1 
ATOM   4645 N  N   . GLY B  1  260 ? 4.881   -17.203 77.065 1.00 51.47  ? 273 GLY B N   1 
ATOM   4646 C  CA  . GLY B  1  260 ? 5.301   -16.906 78.419 1.00 50.72  ? 273 GLY B CA  1 
ATOM   4647 C  C   . GLY B  1  260 ? 6.532   -16.009 78.412 1.00 54.89  ? 273 GLY B C   1 
ATOM   4648 O  O   . GLY B  1  260 ? 6.720   -15.228 77.482 1.00 54.44  ? 273 GLY B O   1 
ATOM   4649 N  N   . GLY B  1  261 ? 7.355   -16.139 79.459 1.00 54.55  ? 274 GLY B N   1 
ATOM   4650 C  CA  . GLY B  1  261 ? 8.550   -15.330 79.618 1.00 53.62  ? 274 GLY B CA  1 
ATOM   4651 C  C   . GLY B  1  261 ? 9.314   -15.698 80.889 1.00 56.44  ? 274 GLY B C   1 
ATOM   4652 O  O   . GLY B  1  261 ? 8.788   -16.387 81.757 1.00 59.68  ? 274 GLY B O   1 
ATOM   4653 N  N   . ASN B  1  262 ? 10.572  -15.255 80.965 1.00 54.03  ? 275 ASN B N   1 
ATOM   4654 C  CA  . ASN B  1  262 ? 11.353  -15.334 82.187 1.00 55.60  ? 275 ASN B CA  1 
ATOM   4655 C  C   . ASN B  1  262 ? 10.742  -14.394 83.221 1.00 57.96  ? 275 ASN B C   1 
ATOM   4656 O  O   . ASN B  1  262 ? 10.570  -13.212 82.943 1.00 54.57  ? 275 ASN B O   1 
ATOM   4657 C  CB  . ASN B  1  262 ? 12.813  -14.943 81.962 1.00 54.05  ? 275 ASN B CB  1 
ATOM   4658 C  CG  . ASN B  1  262 ? 13.676  -16.083 81.479 1.00 54.10  ? 275 ASN B CG  1 
ATOM   4659 O  OD1 . ASN B  1  262 ? 13.332  -17.257 81.654 1.00 53.06  ? 275 ASN B OD1 1 
ATOM   4660 N  ND2 . ASN B  1  262 ? 14.826  -15.756 80.908 1.00 59.46  ? 275 ASN B ND2 1 
ATOM   4661 N  N   . ALA B  1  263 ? 10.446  -14.917 84.418 1.00 65.53  ? 276 ALA B N   1 
ATOM   4662 C  CA  . ALA B  1  263 ? 9.854   -14.108 85.475 1.00 69.43  ? 276 ALA B CA  1 
ATOM   4663 C  C   . ALA B  1  263 ? 10.932  -13.558 86.410 1.00 67.38  ? 276 ALA B C   1 
ATOM   4664 O  O   . ALA B  1  263 ? 11.997  -14.146 86.554 1.00 67.95  ? 276 ALA B O   1 
ATOM   4665 C  CB  . ALA B  1  263 ? 8.822   -14.922 86.232 1.00 70.60  ? 276 ALA B CB  1 
ATOM   4666 N  N   . ASP B  1  264 ? 10.616  -12.418 87.037 1.00 75.07  ? 277 ASP B N   1 
ATOM   4667 C  CA  . ASP B  1  264 ? 11.351  -11.868 88.169 1.00 80.65  ? 277 ASP B CA  1 
ATOM   4668 C  C   . ASP B  1  264 ? 12.813  -11.606 87.806 1.00 79.47  ? 277 ASP B C   1 
ATOM   4669 O  O   . ASP B  1  264 ? 13.697  -11.851 88.620 1.00 76.64  ? 277 ASP B O   1 
ATOM   4670 C  CB  . ASP B  1  264 ? 11.254  -12.752 89.407 1.00 86.18  ? 277 ASP B CB  1 
ATOM   4671 C  CG  . ASP B  1  264 ? 9.851   -13.146 89.848 1.00 88.81  ? 277 ASP B CG  1 
ATOM   4672 O  OD1 . ASP B  1  264 ? 8.994   -12.250 89.999 1.00 84.11  ? 277 ASP B OD1 1 
ATOM   4673 O  OD2 . ASP B  1  264 ? 9.624   -14.356 90.027 1.00 95.53  ? 277 ASP B OD2 1 
ATOM   4674 N  N   . ASN B  1  265 ? 13.049  -11.099 86.591 1.00 71.50  ? 278 ASN B N   1 
ATOM   4675 C  CA  . ASN B  1  265 ? 14.359  -10.632 86.160 1.00 69.83  ? 278 ASN B CA  1 
ATOM   4676 C  C   . ASN B  1  265 ? 15.429  -11.703 86.391 1.00 63.80  ? 278 ASN B C   1 
ATOM   4677 O  O   . ASN B  1  265 ? 16.558  -11.390 86.757 1.00 65.46  ? 278 ASN B O   1 
ATOM   4678 C  CB  . ASN B  1  265 ? 14.731  -9.312  86.829 1.00 72.27  ? 278 ASN B CB  1 
ATOM   4679 C  CG  . ASN B  1  265 ? 15.631  -8.462  85.959 1.00 80.90  ? 278 ASN B CG  1 
ATOM   4680 O  OD1 . ASN B  1  265 ? 15.568  -8.540  84.729 1.00 84.09  ? 278 ASN B OD1 1 
ATOM   4681 N  ND2 . ASN B  1  265 ? 16.432  -7.595  86.564 1.00 85.25  ? 278 ASN B ND2 1 
ATOM   4682 N  N   . GLN B  1  266 ? 15.075  -12.968 86.137 1.00 62.16  ? 279 GLN B N   1 
ATOM   4683 C  CA  . GLN B  1  266 ? 15.972  -14.094 86.326 1.00 66.33  ? 279 GLN B CA  1 
ATOM   4684 C  C   . GLN B  1  266 ? 15.999  -14.944 85.062 1.00 63.24  ? 279 GLN B C   1 
ATOM   4685 O  O   . GLN B  1  266 ? 14.966  -15.177 84.442 1.00 64.29  ? 279 GLN B O   1 
ATOM   4686 C  CB  . GLN B  1  266 ? 15.475  -15.001 87.450 1.00 74.31  ? 279 GLN B CB  1 
ATOM   4687 C  CG  . GLN B  1  266 ? 15.664  -14.441 88.853 1.00 81.17  ? 279 GLN B CG  1 
ATOM   4688 C  CD  . GLN B  1  266 ? 15.126  -15.372 89.917 1.00 87.52  ? 279 GLN B CD  1 
ATOM   4689 O  OE1 . GLN B  1  266 ? 14.213  -16.173 89.683 1.00 89.23  ? 279 GLN B OE1 1 
ATOM   4690 N  NE2 . GLN B  1  266 ? 15.692  -15.271 91.110 1.00 94.22  ? 279 GLN B NE2 1 
ATOM   4691 N  N   . VAL B  1  267 ? 17.193  -15.436 84.716 1.00 59.96  ? 280 VAL B N   1 
ATOM   4692 C  CA  . VAL B  1  267 ? 17.356  -16.356 83.604 1.00 55.99  ? 280 VAL B CA  1 
ATOM   4693 C  C   . VAL B  1  267 ? 16.834  -17.730 84.015 1.00 56.84  ? 280 VAL B C   1 
ATOM   4694 O  O   . VAL B  1  267 ? 16.549  -17.970 85.183 1.00 61.82  ? 280 VAL B O   1 
ATOM   4695 C  CB  . VAL B  1  267 ? 18.820  -16.413 83.120 1.00 55.90  ? 280 VAL B CB  1 
ATOM   4696 C  CG1 . VAL B  1  267 ? 19.269  -15.074 82.523 1.00 54.23  ? 280 VAL B CG1 1 
ATOM   4697 C  CG2 . VAL B  1  267 ? 19.782  -16.883 84.209 1.00 56.64  ? 280 VAL B CG2 1 
ATOM   4698 N  N   . ASN B  1  268 ? 16.689  -18.617 83.027 1.00 58.73  ? 281 ASN B N   1 
ATOM   4699 C  CA  . ASN B  1  268 ? 16.231  -19.986 83.229 1.00 61.15  ? 281 ASN B CA  1 
ATOM   4700 C  C   . ASN B  1  268 ? 15.026  -20.024 84.168 1.00 63.32  ? 281 ASN B C   1 
ATOM   4701 O  O   . ASN B  1  268 ? 14.987  -20.837 85.087 1.00 58.88  ? 281 ASN B O   1 
ATOM   4702 C  CB  . ASN B  1  268 ? 17.360  -20.881 83.725 1.00 60.88  ? 281 ASN B CB  1 
ATOM   4703 C  CG  . ASN B  1  268 ? 18.460  -21.024 82.698 1.00 62.34  ? 281 ASN B CG  1 
ATOM   4704 O  OD1 . ASN B  1  268 ? 18.256  -21.639 81.643 1.00 63.44  ? 281 ASN B OD1 1 
ATOM   4705 N  ND2 . ASN B  1  268 ? 19.629  -20.470 82.981 1.00 60.27  ? 281 ASN B ND2 1 
ATOM   4706 N  N   . ASN B  1  269 ? 14.033  -19.166 83.908 1.00 63.40  ? 282 ASN B N   1 
ATOM   4707 C  CA  . ASN B  1  269 ? 12.891  -19.026 84.795 1.00 62.17  ? 282 ASN B CA  1 
ATOM   4708 C  C   . ASN B  1  269 ? 11.630  -18.745 83.976 1.00 61.81  ? 282 ASN B C   1 
ATOM   4709 O  O   . ASN B  1  269 ? 10.918  -17.774 84.231 1.00 62.14  ? 282 ASN B O   1 
ATOM   4710 C  CB  . ASN B  1  269 ? 13.167  -17.942 85.833 1.00 61.85  ? 282 ASN B CB  1 
ATOM   4711 C  CG  . ASN B  1  269 ? 12.174  -17.966 86.973 1.00 58.68  ? 282 ASN B CG  1 
ATOM   4712 O  OD1 . ASN B  1  269 ? 11.662  -19.032 87.330 1.00 58.08  ? 282 ASN B OD1 1 
ATOM   4713 N  ND2 . ASN B  1  269 ? 11.901  -16.811 87.560 1.00 54.15  ? 282 ASN B ND2 1 
ATOM   4714 N  N   . TYR B  1  270 ? 11.353  -19.617 82.998 1.00 64.25  ? 283 TYR B N   1 
ATOM   4715 C  CA  . TYR B  1  270 ? 10.280  -19.387 82.042 1.00 63.51  ? 283 TYR B CA  1 
ATOM   4716 C  C   . TYR B  1  270 ? 8.953   -19.845 82.645 1.00 63.90  ? 283 TYR B C   1 
ATOM   4717 O  O   . TYR B  1  270 ? 8.796   -21.016 82.976 1.00 58.18  ? 283 TYR B O   1 
ATOM   4718 C  CB  . TYR B  1  270 ? 10.573  -20.115 80.725 1.00 60.04  ? 283 TYR B CB  1 
ATOM   4719 C  CG  . TYR B  1  270 ? 9.660   -19.744 79.563 1.00 57.91  ? 283 TYR B CG  1 
ATOM   4720 C  CD1 . TYR B  1  270 ? 9.893   -18.606 78.793 1.00 58.61  ? 283 TYR B CD1 1 
ATOM   4721 C  CD2 . TYR B  1  270 ? 8.573   -20.542 79.222 1.00 56.18  ? 283 TYR B CD2 1 
ATOM   4722 C  CE1 . TYR B  1  270 ? 9.068   -18.275 77.728 1.00 58.22  ? 283 TYR B CE1 1 
ATOM   4723 C  CE2 . TYR B  1  270 ? 7.748   -20.226 78.154 1.00 57.25  ? 283 TYR B CE2 1 
ATOM   4724 C  CZ  . TYR B  1  270 ? 7.998   -19.091 77.403 1.00 58.41  ? 283 TYR B CZ  1 
ATOM   4725 O  OH  . TYR B  1  270 ? 7.185   -18.768 76.356 1.00 53.68  ? 283 TYR B OH  1 
ATOM   4726 N  N   . VAL B  1  271 ? 8.004   -18.905 82.751 1.00 64.32  ? 284 VAL B N   1 
ATOM   4727 C  CA  . VAL B  1  271 ? 6.660   -19.160 83.248 1.00 60.06  ? 284 VAL B CA  1 
ATOM   4728 C  C   . VAL B  1  271 ? 5.672   -18.978 82.101 1.00 57.25  ? 284 VAL B C   1 
ATOM   4729 O  O   . VAL B  1  271 ? 5.699   -17.954 81.426 1.00 56.34  ? 284 VAL B O   1 
ATOM   4730 C  CB  . VAL B  1  271 ? 6.319   -18.188 84.396 1.00 63.30  ? 284 VAL B CB  1 
ATOM   4731 C  CG1 . VAL B  1  271 ? 4.908   -18.396 84.935 1.00 65.09  ? 284 VAL B CG1 1 
ATOM   4732 C  CG2 . VAL B  1  271 ? 7.345   -18.244 85.522 1.00 67.12  ? 284 VAL B CG2 1 
ATOM   4733 N  N   . GLU B  1  272 ? 4.766   -19.947 81.939 1.00 57.62  ? 285 GLU B N   1 
ATOM   4734 C  CA  A GLU B  1  272 ? 3.735   -19.877 80.916 0.50 56.14  ? 285 GLU B CA  1 
ATOM   4735 C  CA  B GLU B  1  272 ? 3.729   -19.883 80.920 0.50 57.97  ? 285 GLU B CA  1 
ATOM   4736 C  C   . GLU B  1  272 ? 2.744   -18.765 81.262 1.00 58.07  ? 285 GLU B C   1 
ATOM   4737 O  O   . GLU B  1  272 ? 2.473   -18.510 82.431 1.00 59.64  ? 285 GLU B O   1 
ATOM   4738 C  CB  A GLU B  1  272 ? 3.081   -21.252 80.766 0.50 54.71  ? 285 GLU B CB  1 
ATOM   4739 C  CB  B GLU B  1  272 ? 3.012   -21.230 80.777 0.50 59.02  ? 285 GLU B CB  1 
ATOM   4740 C  CG  A GLU B  1  272 ? 4.076   -22.336 80.357 0.50 52.44  ? 285 GLU B CG  1 
ATOM   4741 C  CG  B GLU B  1  272 ? 1.625   -21.104 80.148 0.50 59.65  ? 285 GLU B CG  1 
ATOM   4742 C  CD  A GLU B  1  272 ? 3.620   -23.762 80.594 0.50 50.79  ? 285 GLU B CD  1 
ATOM   4743 C  CD  B GLU B  1  272 ? 0.894   -22.402 79.863 0.50 58.21  ? 285 GLU B CD  1 
ATOM   4744 O  OE1 A GLU B  1  272 ? 2.526   -23.945 81.160 0.50 56.13  ? 285 GLU B OE1 1 
ATOM   4745 O  OE1 B GLU B  1  272 ? 1.444   -23.485 80.154 0.50 56.70  ? 285 GLU B OE1 1 
ATOM   4746 O  OE2 A GLU B  1  272 ? 4.357   -24.691 80.212 0.50 46.68  ? 285 GLU B OE2 1 
ATOM   4747 O  OE2 B GLU B  1  272 ? -0.231  -22.312 79.325 0.50 57.54  ? 285 GLU B OE2 1 
ATOM   4748 N  N   . ASP B  1  273 ? 2.221   -18.094 80.222 1.00 61.79  ? 286 ASP B N   1 
ATOM   4749 C  CA  . ASP B  1  273 ? 1.134   -17.136 80.357 1.00 62.42  ? 286 ASP B CA  1 
ATOM   4750 C  C   . ASP B  1  273 ? -0.101  -17.695 79.653 1.00 60.61  ? 286 ASP B C   1 
ATOM   4751 O  O   . ASP B  1  273 ? -0.183  -17.674 78.429 1.00 58.48  ? 286 ASP B O   1 
ATOM   4752 C  CB  . ASP B  1  273 ? 1.494   -15.763 79.811 1.00 60.31  ? 286 ASP B CB  1 
ATOM   4753 C  CG  . ASP B  1  273 ? 0.373   -14.730 79.839 1.00 61.94  ? 286 ASP B CG  1 
ATOM   4754 O  OD1 . ASP B  1  273 ? -0.716  -15.055 80.347 1.00 66.76  ? 286 ASP B OD1 1 
ATOM   4755 O  OD2 . ASP B  1  273 ? 0.598   -13.609 79.345 1.00 64.17  ? 286 ASP B OD2 1 
ATOM   4756 N  N   . PRO B  1  274 ? -1.109  -18.199 80.398 1.00 62.89  ? 287 PRO B N   1 
ATOM   4757 C  CA  . PRO B  1  274 ? -2.283  -18.819 79.774 1.00 60.36  ? 287 PRO B CA  1 
ATOM   4758 C  C   . PRO B  1  274 ? -3.265  -17.848 79.118 1.00 55.60  ? 287 PRO B C   1 
ATOM   4759 O  O   . PRO B  1  274 ? -4.132  -18.282 78.364 1.00 58.45  ? 287 PRO B O   1 
ATOM   4760 C  CB  . PRO B  1  274 ? -2.917  -19.567 80.960 1.00 64.56  ? 287 PRO B CB  1 
ATOM   4761 C  CG  . PRO B  1  274 ? -2.574  -18.710 82.157 1.00 62.71  ? 287 PRO B CG  1 
ATOM   4762 C  CD  . PRO B  1  274 ? -1.176  -18.181 81.870 1.00 62.13  ? 287 PRO B CD  1 
ATOM   4763 N  N   . ASP B  1  275 ? -3.121  -16.545 79.405 1.00 53.03  ? 288 ASP B N   1 
ATOM   4764 C  CA  . ASP B  1  275 ? -3.984  -15.510 78.847 1.00 57.14  ? 288 ASP B CA  1 
ATOM   4765 C  C   . ASP B  1  275 ? -3.503  -15.036 77.469 1.00 56.18  ? 288 ASP B C   1 
ATOM   4766 O  O   . ASP B  1  275 ? -4.253  -14.384 76.745 1.00 50.74  ? 288 ASP B O   1 
ATOM   4767 C  CB  . ASP B  1  275 ? -4.084  -14.310 79.778 1.00 62.47  ? 288 ASP B CB  1 
ATOM   4768 C  CG  . ASP B  1  275 ? -4.846  -14.536 81.077 1.00 68.54  ? 288 ASP B CG  1 
ATOM   4769 O  OD1 . ASP B  1  275 ? -5.246  -15.689 81.355 1.00 64.56  ? 288 ASP B OD1 1 
ATOM   4770 O  OD2 . ASP B  1  275 ? -5.056  -13.536 81.798 1.00 76.31  ? 288 ASP B OD2 1 
ATOM   4771 N  N   . SER B  1  276 ? -2.248  -15.342 77.116 1.00 55.65  ? 289 SER B N   1 
ATOM   4772 C  CA  . SER B  1  276 ? -1.649  -14.894 75.867 1.00 52.09  ? 289 SER B CA  1 
ATOM   4773 C  C   . SER B  1  276 ? -2.395  -15.475 74.672 1.00 48.38  ? 289 SER B C   1 
ATOM   4774 O  O   . SER B  1  276 ? -2.969  -16.563 74.754 1.00 49.32  ? 289 SER B O   1 
ATOM   4775 C  CB  . SER B  1  276 ? -0.183  -15.277 75.813 1.00 54.62  ? 289 SER B CB  1 
ATOM   4776 O  OG  . SER B  1  276 ? 0.346   -15.110 74.506 1.00 56.10  ? 289 SER B OG  1 
ATOM   4777 N  N   . ALA B  1  277 ? -2.344  -14.758 73.546 1.00 46.81  ? 290 ALA B N   1 
ATOM   4778 C  CA  . ALA B  1  277 ? -2.709  -15.350 72.267 1.00 43.94  ? 290 ALA B CA  1 
ATOM   4779 C  C   . ALA B  1  277 ? -1.840  -16.578 71.998 1.00 45.50  ? 290 ALA B C   1 
ATOM   4780 O  O   . ALA B  1  277 ? -0.712  -16.666 72.483 1.00 43.27  ? 290 ALA B O   1 
ATOM   4781 C  CB  . ALA B  1  277 ? -2.556  -14.330 71.151 1.00 44.13  ? 290 ALA B CB  1 
ATOM   4782 N  N   . ASP B  1  278 ? -2.394  -17.516 71.225 1.00 48.52  ? 291 ASP B N   1 
ATOM   4783 C  CA  . ASP B  1  278 ? -1.642  -18.606 70.631 1.00 49.90  ? 291 ASP B CA  1 
ATOM   4784 C  C   . ASP B  1  278 ? -2.332  -18.955 69.313 1.00 47.72  ? 291 ASP B C   1 
ATOM   4785 O  O   . ASP B  1  278 ? -3.215  -18.221 68.881 1.00 46.80  ? 291 ASP B O   1 
ATOM   4786 C  CB  . ASP B  1  278 ? -1.459  -19.743 71.624 1.00 52.43  ? 291 ASP B CB  1 
ATOM   4787 C  CG  . ASP B  1  278 ? -2.725  -20.481 72.027 1.00 55.28  ? 291 ASP B CG  1 
ATOM   4788 O  OD1 . ASP B  1  278 ? -3.735  -20.369 71.294 1.00 49.46  ? 291 ASP B OD1 1 
ATOM   4789 O  OD2 . ASP B  1  278 ? -2.690  -21.152 73.079 1.00 55.30  ? 291 ASP B OD2 1 
ATOM   4790 N  N   . PHE B  1  279 ? -1.948  -20.070 68.680 1.00 47.48  ? 292 PHE B N   1 
ATOM   4791 C  CA  . PHE B  1  279 ? -2.373  -20.338 67.312 1.00 48.44  ? 292 PHE B CA  1 
ATOM   4792 C  C   . PHE B  1  279 ? -3.801  -20.871 67.251 1.00 51.75  ? 292 PHE B C   1 
ATOM   4793 O  O   . PHE B  1  279 ? -4.379  -20.907 66.170 1.00 53.42  ? 292 PHE B O   1 
ATOM   4794 C  CB  . PHE B  1  279 ? -1.375  -21.255 66.604 1.00 46.98  ? 292 PHE B CB  1 
ATOM   4795 C  CG  . PHE B  1  279 ? -0.126  -20.485 66.205 1.00 50.32  ? 292 PHE B CG  1 
ATOM   4796 C  CD1 . PHE B  1  279 ? -0.123  -19.703 65.054 1.00 53.01  ? 292 PHE B CD1 1 
ATOM   4797 C  CD2 . PHE B  1  279 ? 1.020   -20.503 66.998 1.00 51.41  ? 292 PHE B CD2 1 
ATOM   4798 C  CE1 . PHE B  1  279 ? 1.008   -18.990 64.687 1.00 56.31  ? 292 PHE B CE1 1 
ATOM   4799 C  CE2 . PHE B  1  279 ? 2.143   -19.781 66.630 1.00 53.41  ? 292 PHE B CE2 1 
ATOM   4800 C  CZ  . PHE B  1  279 ? 2.134   -19.026 65.476 1.00 53.18  ? 292 PHE B CZ  1 
ATOM   4801 N  N   . THR B  1  280 ? -4.384  -21.250 68.395 1.00 57.51  ? 293 THR B N   1 
ATOM   4802 C  CA  . THR B  1  280 ? -5.795  -21.608 68.434 1.00 58.96  ? 293 THR B CA  1 
ATOM   4803 C  C   . THR B  1  280 ? -6.598  -20.507 69.131 1.00 61.53  ? 293 THR B C   1 
ATOM   4804 O  O   . THR B  1  280 ? -7.795  -20.679 69.357 1.00 62.68  ? 293 THR B O   1 
ATOM   4805 C  CB  . THR B  1  280 ? -5.975  -22.967 69.110 1.00 56.79  ? 293 THR B CB  1 
ATOM   4806 O  OG1 . THR B  1  280 ? -5.512  -22.842 70.450 1.00 56.79  ? 293 THR B OG1 1 
ATOM   4807 C  CG2 . THR B  1  280 ? -5.184  -24.071 68.430 1.00 56.19  ? 293 THR B CG2 1 
ATOM   4808 N  N   . HIS B  1  281 ? -5.947  -19.380 69.454 1.00 56.45  ? 294 HIS B N   1 
ATOM   4809 C  CA  . HIS B  1  281 ? -6.606  -18.247 70.092 1.00 56.69  ? 294 HIS B CA  1 
ATOM   4810 C  C   . HIS B  1  281 ? -6.106  -16.938 69.470 1.00 53.19  ? 294 HIS B C   1 
ATOM   4811 O  O   . HIS B  1  281 ? -5.662  -16.044 70.183 1.00 53.53  ? 294 HIS B O   1 
ATOM   4812 C  CB  . HIS B  1  281 ? -6.380  -18.270 71.613 1.00 58.67  ? 294 HIS B CB  1 
ATOM   4813 C  CG  . HIS B  1  281 ? -6.932  -19.462 72.333 1.00 64.55  ? 294 HIS B CG  1 
ATOM   4814 N  ND1 . HIS B  1  281 ? -8.182  -19.467 72.914 1.00 68.27  ? 294 HIS B ND1 1 
ATOM   4815 C  CD2 . HIS B  1  281 ? -6.413  -20.672 72.582 1.00 65.13  ? 294 HIS B CD2 1 
ATOM   4816 C  CE1 . HIS B  1  281 ? -8.397  -20.642 73.486 1.00 67.51  ? 294 HIS B CE1 1 
ATOM   4817 N  NE2 . HIS B  1  281 ? -7.335  -21.386 73.300 1.00 67.67  ? 294 HIS B NE2 1 
ATOM   4818 N  N   . LEU B  1  282 ? -6.198  -16.816 68.140 1.00 51.52  ? 295 LEU B N   1 
ATOM   4819 C  CA  . LEU B  1  282 ? -5.600  -15.701 67.414 1.00 50.69  ? 295 LEU B CA  1 
ATOM   4820 C  C   . LEU B  1  282 ? -6.263  -14.359 67.729 1.00 50.22  ? 295 LEU B C   1 
ATOM   4821 O  O   . LEU B  1  282 ? -5.578  -13.335 67.769 1.00 48.50  ? 295 LEU B O   1 
ATOM   4822 C  CB  . LEU B  1  282 ? -5.619  -15.969 65.909 1.00 47.73  ? 295 LEU B CB  1 
ATOM   4823 C  CG  . LEU B  1  282 ? -4.673  -17.066 65.410 1.00 49.47  ? 295 LEU B CG  1 
ATOM   4824 C  CD1 . LEU B  1  282 ? -4.939  -17.353 63.934 1.00 49.84  ? 295 LEU B CD1 1 
ATOM   4825 C  CD2 . LEU B  1  282 ? -3.227  -16.643 65.633 1.00 48.60  ? 295 LEU B CD2 1 
ATOM   4826 N  N   . CYS B  1  283 ? -7.585  -14.341 67.939 1.00 50.35  ? 296 CYS B N   1 
ATOM   4827 C  CA  . CYS B  1  283 ? -8.284  -13.073 68.121 1.00 50.84  ? 296 CYS B CA  1 
ATOM   4828 C  C   . CYS B  1  283 ? -7.861  -12.397 69.423 1.00 48.91  ? 296 CYS B C   1 
ATOM   4829 O  O   . CYS B  1  283 ? -8.032  -11.193 69.553 1.00 48.82  ? 296 CYS B O   1 
ATOM   4830 C  CB  . CYS B  1  283 ? -9.809  -13.150 68.111 1.00 56.06  ? 296 CYS B CB  1 
ATOM   4831 S  SG  . CYS B  1  283 ? -10.536 -13.746 66.556 1.00 61.85  ? 296 CYS B SG  1 
ATOM   4832 N  N   . ARG B  1  284 ? -7.288  -13.141 70.372 1.00 47.93  ? 297 ARG B N   1 
ATOM   4833 C  CA  . ARG B  1  284 ? -6.710  -12.521 71.555 1.00 51.30  ? 297 ARG B CA  1 
ATOM   4834 C  C   . ARG B  1  284 ? -5.636  -11.514 71.160 1.00 49.04  ? 297 ARG B C   1 
ATOM   4835 O  O   . ARG B  1  284 ? -5.461  -10.504 71.840 1.00 48.25  ? 297 ARG B O   1 
ATOM   4836 C  CB  . ARG B  1  284 ? -6.044  -13.528 72.493 1.00 51.77  ? 297 ARG B CB  1 
ATOM   4837 C  CG  . ARG B  1  284 ? -7.031  -14.458 73.177 1.00 57.79  ? 297 ARG B CG  1 
ATOM   4838 C  CD  . ARG B  1  284 ? -6.319  -15.343 74.178 1.00 60.87  ? 297 ARG B CD  1 
ATOM   4839 N  NE  . ARG B  1  284 ? -7.249  -16.264 74.837 1.00 61.13  ? 297 ARG B NE  1 
ATOM   4840 C  CZ  . ARG B  1  284 ? -6.893  -17.261 75.627 1.00 64.52  ? 297 ARG B CZ  1 
ATOM   4841 N  NH1 . ARG B  1  284 ? -5.616  -17.479 75.886 1.00 65.01  ? 297 ARG B NH1 1 
ATOM   4842 N  NH2 . ARG B  1  284 ? -7.817  -18.050 76.145 1.00 67.83  ? 297 ARG B NH2 1 
ATOM   4843 N  N   . LEU B  1  285 ? -4.909  -11.813 70.078 1.00 47.18  ? 298 LEU B N   1 
ATOM   4844 C  CA  . LEU B  1  285 ? -3.887  -10.903 69.586 1.00 49.60  ? 298 LEU B CA  1 
ATOM   4845 C  C   . LEU B  1  285 ? -4.561  -9.602  69.144 1.00 43.12  ? 298 LEU B C   1 
ATOM   4846 O  O   . LEU B  1  285 ? -4.095  -8.515  69.478 1.00 47.14  ? 298 LEU B O   1 
ATOM   4847 C  CB  . LEU B  1  285 ? -3.069  -11.556 68.470 1.00 49.37  ? 298 LEU B CB  1 
ATOM   4848 C  CG  . LEU B  1  285 ? -1.868  -10.757 67.951 1.00 49.84  ? 298 LEU B CG  1 
ATOM   4849 C  CD1 . LEU B  1  285 ? -0.846  -11.708 67.375 1.00 50.84  ? 298 LEU B CD1 1 
ATOM   4850 C  CD2 . LEU B  1  285 ? -2.256  -9.739  66.893 1.00 54.70  ? 298 LEU B CD2 1 
ATOM   4851 N  N   . TYR B  1  286 ? -5.679  -9.724  68.422 1.00 43.89  ? 299 TYR B N   1 
ATOM   4852 C  CA  . TYR B  1  286 ? -6.438  -8.562  67.978 1.00 42.89  ? 299 TYR B CA  1 
ATOM   4853 C  C   . TYR B  1  286 ? -6.838  -7.713  69.187 1.00 43.63  ? 299 TYR B C   1 
ATOM   4854 O  O   . TYR B  1  286 ? -6.580  -6.516  69.212 1.00 43.42  ? 299 TYR B O   1 
ATOM   4855 C  CB  . TYR B  1  286 ? -7.631  -9.012  67.130 1.00 41.25  ? 299 TYR B CB  1 
ATOM   4856 C  CG  . TYR B  1  286 ? -8.589  -7.890  66.775 1.00 40.42  ? 299 TYR B CG  1 
ATOM   4857 C  CD1 . TYR B  1  286 ? -8.179  -6.839  65.974 1.00 40.44  ? 299 TYR B CD1 1 
ATOM   4858 C  CD2 . TYR B  1  286 ? -9.893  -7.874  67.255 1.00 42.92  ? 299 TYR B CD2 1 
ATOM   4859 C  CE1 . TYR B  1  286 ? -9.031  -5.798  65.651 1.00 42.73  ? 299 TYR B CE1 1 
ATOM   4860 C  CE2 . TYR B  1  286 ? -10.770 -6.856  66.908 1.00 42.02  ? 299 TYR B CE2 1 
ATOM   4861 C  CZ  . TYR B  1  286 ? -10.338 -5.815  66.109 1.00 41.93  ? 299 TYR B CZ  1 
ATOM   4862 O  OH  . TYR B  1  286 ? -11.186 -4.802  65.790 1.00 42.31  ? 299 TYR B OH  1 
ATOM   4863 N  N   . GLU B  1  287 ? -7.406  -8.356  70.208 1.00 44.33  ? 300 GLU B N   1 
ATOM   4864 C  CA  . GLU B  1  287 ? -7.925  -7.666  71.382 1.00 48.31  ? 300 GLU B CA  1 
ATOM   4865 C  C   . GLU B  1  287 ? -6.784  -7.032  72.179 1.00 47.10  ? 300 GLU B C   1 
ATOM   4866 O  O   . GLU B  1  287 ? -6.898  -5.897  72.649 1.00 47.27  ? 300 GLU B O   1 
ATOM   4867 C  CB  . GLU B  1  287 ? -8.737  -8.631  72.249 1.00 49.80  ? 300 GLU B CB  1 
ATOM   4868 C  CG  . GLU B  1  287 ? -9.991  -9.155  71.557 1.00 57.73  ? 300 GLU B CG  1 
ATOM   4869 C  CD  . GLU B  1  287 ? -10.589 -10.445 72.087 1.00 69.75  ? 300 GLU B CD  1 
ATOM   4870 O  OE1 . GLU B  1  287 ? -9.923  -11.248 72.777 1.00 76.64  ? 300 GLU B OE1 1 
ATOM   4871 O  OE2 . GLU B  1  287 ? -11.783 -10.630 71.787 1.00 78.50  ? 300 GLU B OE2 1 
ATOM   4872 N  N   . PHE B  1  288 ? -5.682  -7.771  72.331 1.00 46.38  ? 301 PHE B N   1 
ATOM   4873 C  CA  . PHE B  1  288 ? -4.529  -7.261  73.058 1.00 43.61  ? 301 PHE B CA  1 
ATOM   4874 C  C   . PHE B  1  288 ? -4.057  -5.963  72.409 1.00 41.59  ? 301 PHE B C   1 
ATOM   4875 O  O   . PHE B  1  288 ? -3.874  -4.949  73.084 1.00 39.95  ? 301 PHE B O   1 
ATOM   4876 C  CB  . PHE B  1  288 ? -3.409  -8.304  73.098 1.00 49.19  ? 301 PHE B CB  1 
ATOM   4877 C  CG  . PHE B  1  288 ? -2.202  -7.862  73.913 1.00 52.77  ? 301 PHE B CG  1 
ATOM   4878 C  CD1 . PHE B  1  288 ? -2.149  -8.086  75.289 1.00 51.02  ? 301 PHE B CD1 1 
ATOM   4879 C  CD2 . PHE B  1  288 ? -1.142  -7.190  73.309 1.00 49.86  ? 301 PHE B CD2 1 
ATOM   4880 C  CE1 . PHE B  1  288 ? -1.049  -7.678  76.031 1.00 53.25  ? 301 PHE B CE1 1 
ATOM   4881 C  CE2 . PHE B  1  288 ? -0.052  -6.773  74.064 1.00 52.47  ? 301 PHE B CE2 1 
ATOM   4882 C  CZ  . PHE B  1  288 ? -0.003  -7.021  75.417 1.00 51.04  ? 301 PHE B CZ  1 
ATOM   4883 N  N   . VAL B  1  289 ? -3.904  -5.990  71.078 1.00 42.41  ? 302 VAL B N   1 
ATOM   4884 C  CA  . VAL B  1  289 ? -3.368  -4.840  70.371 1.00 42.34  ? 302 VAL B CA  1 
ATOM   4885 C  C   . VAL B  1  289 ? -4.334  -3.663  70.460 1.00 40.17  ? 302 VAL B C   1 
ATOM   4886 O  O   . VAL B  1  289 ? -3.899  -2.523  70.592 1.00 37.88  ? 302 VAL B O   1 
ATOM   4887 C  CB  . VAL B  1  289 ? -3.012  -5.169  68.910 1.00 44.24  ? 302 VAL B CB  1 
ATOM   4888 C  CG1 . VAL B  1  289 ? -2.731  -3.914  68.098 1.00 43.26  ? 302 VAL B CG1 1 
ATOM   4889 C  CG2 . VAL B  1  289 ? -1.825  -6.118  68.846 1.00 43.96  ? 302 VAL B CG2 1 
ATOM   4890 N  N   . VAL B  1  290 ? -5.641  -3.918  70.368 1.00 42.09  ? 303 VAL B N   1 
ATOM   4891 C  CA  . VAL B  1  290 ? -6.602  -2.831  70.481 1.00 41.61  ? 303 VAL B CA  1 
ATOM   4892 C  C   . VAL B  1  290 ? -6.428  -2.165  71.848 1.00 41.95  ? 303 VAL B C   1 
ATOM   4893 O  O   . VAL B  1  290 ? -6.396  -0.930  71.946 1.00 42.40  ? 303 VAL B O   1 
ATOM   4894 C  CB  . VAL B  1  290 ? -8.041  -3.324  70.234 1.00 44.85  ? 303 VAL B CB  1 
ATOM   4895 C  CG1 . VAL B  1  290 ? -9.083  -2.293  70.643 1.00 43.73  ? 303 VAL B CG1 1 
ATOM   4896 C  CG2 . VAL B  1  290 ? -8.255  -3.759  68.780 1.00 41.75  ? 303 VAL B CG2 1 
ATOM   4897 N  N   . GLY B  1  291 ? -6.252  -2.991  72.891 1.00 42.80  ? 304 GLY B N   1 
ATOM   4898 C  CA  . GLY B  1  291 ? -5.961  -2.487  74.222 1.00 47.47  ? 304 GLY B CA  1 
ATOM   4899 C  C   . GLY B  1  291 ? -4.687  -1.637  74.254 1.00 50.71  ? 304 GLY B C   1 
ATOM   4900 O  O   . GLY B  1  291 ? -4.670  -0.560  74.853 1.00 47.41  ? 304 GLY B O   1 
ATOM   4901 N  N   . SER B  1  292 ? -3.620  -2.127  73.604 1.00 46.86  ? 305 SER B N   1 
ATOM   4902 C  CA  . SER B  1  292 ? -2.358  -1.404  73.577 1.00 42.31  ? 305 SER B CA  1 
ATOM   4903 C  C   . SER B  1  292 ? -2.537  -0.049  72.902 1.00 42.34  ? 305 SER B C   1 
ATOM   4904 O  O   . SER B  1  292 ? -1.971  0.943   73.359 1.00 44.11  ? 305 SER B O   1 
ATOM   4905 C  CB  . SER B  1  292 ? -1.273  -2.207  72.897 1.00 43.55  ? 305 SER B CB  1 
ATOM   4906 O  OG  . SER B  1  292 ? -1.136  -3.482  73.509 1.00 44.91  ? 305 SER B OG  1 
ATOM   4907 N  N   . VAL B  1  293 ? -3.324  -0.010  71.818 1.00 42.43  ? 306 VAL B N   1 
ATOM   4908 C  CA  . VAL B  1  293 ? -3.562  1.237   71.104 1.00 46.73  ? 306 VAL B CA  1 
ATOM   4909 C  C   . VAL B  1  293 ? -4.232  2.248   72.042 1.00 49.70  ? 306 VAL B C   1 
ATOM   4910 O  O   . VAL B  1  293 ? -3.901  3.437   72.028 1.00 50.04  ? 306 VAL B O   1 
ATOM   4911 C  CB  . VAL B  1  293 ? -4.392  1.040   69.820 1.00 45.46  ? 306 VAL B CB  1 
ATOM   4912 C  CG1 . VAL B  1  293 ? -4.819  2.363   69.207 1.00 47.42  ? 306 VAL B CG1 1 
ATOM   4913 C  CG2 . VAL B  1  293 ? -3.669  0.209   68.772 1.00 49.24  ? 306 VAL B CG2 1 
ATOM   4914 N  N   . GLN B  1  294 ? -5.181  1.776   72.860 1.00 51.08  ? 307 GLN B N   1 
ATOM   4915 C  CA  . GLN B  1  294 ? -5.900  2.656   73.769 1.00 52.15  ? 307 GLN B CA  1 
ATOM   4916 C  C   . GLN B  1  294 ? -4.950  3.222   74.820 1.00 53.79  ? 307 GLN B C   1 
ATOM   4917 O  O   . GLN B  1  294 ? -5.122  4.357   75.235 1.00 56.60  ? 307 GLN B O   1 
ATOM   4918 C  CB  . GLN B  1  294 ? -7.058  1.938   74.451 1.00 53.28  ? 307 GLN B CB  1 
ATOM   4919 C  CG  . GLN B  1  294 ? -8.140  1.489   73.481 1.00 57.13  ? 307 GLN B CG  1 
ATOM   4920 C  CD  . GLN B  1  294 ? -9.255  0.753   74.176 1.00 59.13  ? 307 GLN B CD  1 
ATOM   4921 O  OE1 . GLN B  1  294 ? -9.250  -0.481  74.260 1.00 62.07  ? 307 GLN B OE1 1 
ATOM   4922 N  NE2 . GLN B  1  294 ? -10.185 1.534   74.705 1.00 57.36  ? 307 GLN B NE2 1 
ATOM   4923 N  N   . GLU B  1  295 ? -3.958  2.430   75.246 1.00 53.98  ? 308 GLU B N   1 
ATOM   4924 C  CA  . GLU B  1  295 ? -2.946  2.903   76.180 1.00 55.47  ? 308 GLU B CA  1 
ATOM   4925 C  C   . GLU B  1  295 ? -2.086  3.988   75.534 1.00 56.72  ? 308 GLU B C   1 
ATOM   4926 O  O   . GLU B  1  295 ? -1.708  4.942   76.206 1.00 56.66  ? 308 GLU B O   1 
ATOM   4927 C  CB  . GLU B  1  295 ? -2.034  1.789   76.690 1.00 59.08  ? 308 GLU B CB  1 
ATOM   4928 C  CG  . GLU B  1  295 ? -2.719  0.848   77.676 1.00 65.19  ? 308 GLU B CG  1 
ATOM   4929 C  CD  . GLU B  1  295 ? -1.909  -0.379  78.059 1.00 72.20  ? 308 GLU B CD  1 
ATOM   4930 O  OE1 . GLU B  1  295 ? -0.808  -0.613  77.511 1.00 79.53  ? 308 GLU B OE1 1 
ATOM   4931 O  OE2 . GLU B  1  295 ? -2.408  -1.117  78.927 1.00 76.18  ? 308 GLU B OE2 1 
ATOM   4932 N  N   . LEU B  1  296 ? -1.767  3.837   74.241 1.00 57.52  ? 309 LEU B N   1 
ATOM   4933 C  CA  . LEU B  1  296 ? -0.973  4.833   73.535 1.00 55.19  ? 309 LEU B CA  1 
ATOM   4934 C  C   . LEU B  1  296 ? -1.786  6.106   73.308 1.00 50.62  ? 309 LEU B C   1 
ATOM   4935 O  O   . LEU B  1  296 ? -1.228  7.205   73.305 1.00 50.68  ? 309 LEU B O   1 
ATOM   4936 C  CB  . LEU B  1  296 ? -0.442  4.283   72.211 1.00 56.89  ? 309 LEU B CB  1 
ATOM   4937 C  CG  . LEU B  1  296 ? 0.627   3.189   72.313 1.00 56.92  ? 309 LEU B CG  1 
ATOM   4938 C  CD1 . LEU B  1  296 ? 0.904   2.572   70.955 1.00 59.41  ? 309 LEU B CD1 1 
ATOM   4939 C  CD2 . LEU B  1  296 ? 1.907   3.742   72.918 1.00 55.39  ? 309 LEU B CD2 1 
ATOM   4940 N  N   . TYR B  1  297 ? -3.095  5.942   73.087 1.00 48.86  ? 310 TYR B N   1 
ATOM   4941 C  CA  . TYR B  1  297 ? -3.960  7.044   72.699 1.00 53.24  ? 310 TYR B CA  1 
ATOM   4942 C  C   . TYR B  1  297 ? -5.215  7.019   73.571 1.00 59.19  ? 310 TYR B C   1 
ATOM   4943 O  O   . TYR B  1  297 ? -6.272  6.585   73.118 1.00 52.96  ? 310 TYR B O   1 
ATOM   4944 C  CB  . TYR B  1  297 ? -4.318  6.924   71.212 1.00 55.32  ? 310 TYR B CB  1 
ATOM   4945 C  CG  . TYR B  1  297 ? -3.146  7.029   70.250 1.00 53.48  ? 310 TYR B CG  1 
ATOM   4946 C  CD1 . TYR B  1  297 ? -2.654  8.267   69.880 1.00 52.14  ? 310 TYR B CD1 1 
ATOM   4947 C  CD2 . TYR B  1  297 ? -2.555  5.901   69.688 1.00 53.32  ? 310 TYR B CD2 1 
ATOM   4948 C  CE1 . TYR B  1  297 ? -1.592  8.386   68.996 1.00 51.49  ? 310 TYR B CE1 1 
ATOM   4949 C  CE2 . TYR B  1  297 ? -1.483  6.007   68.810 1.00 51.79  ? 310 TYR B CE2 1 
ATOM   4950 C  CZ  . TYR B  1  297 ? -1.006  7.256   68.455 1.00 50.48  ? 310 TYR B CZ  1 
ATOM   4951 O  OH  . TYR B  1  297 ? 0.042   7.410   67.598 1.00 47.55  ? 310 TYR B OH  1 
ATOM   4952 N  N   . PRO B  1  298 ? -5.137  7.435   74.858 1.00 59.30  ? 311 PRO B N   1 
ATOM   4953 C  CA  . PRO B  1  298 ? -6.287  7.326   75.765 1.00 58.39  ? 311 PRO B CA  1 
ATOM   4954 C  C   . PRO B  1  298 ? -7.477  8.230   75.448 1.00 54.88  ? 311 PRO B C   1 
ATOM   4955 O  O   . PRO B  1  298 ? -8.616  7.800   75.604 1.00 58.93  ? 311 PRO B O   1 
ATOM   4956 C  CB  . PRO B  1  298 ? -5.713  7.608   77.153 1.00 60.85  ? 311 PRO B CB  1 
ATOM   4957 C  CG  . PRO B  1  298 ? -4.461  8.408   76.876 1.00 64.74  ? 311 PRO B CG  1 
ATOM   4958 C  CD  . PRO B  1  298 ? -3.932  7.962   75.515 1.00 61.64  ? 311 PRO B CD  1 
ATOM   4959 N  N   . ASN B  1  299 ? -7.222  9.438   74.925 1.00 55.00  ? 312 ASN B N   1 
ATOM   4960 C  CA  . ASN B  1  299 ? -8.287  10.395  74.666 1.00 57.84  ? 312 ASN B CA  1 
ATOM   4961 C  C   . ASN B  1  299 ? -7.947  11.253  73.447 1.00 58.64  ? 312 ASN B C   1 
ATOM   4962 O  O   . ASN B  1  299 ? -7.787  12.469  73.561 1.00 62.98  ? 312 ASN B O   1 
ATOM   4963 C  CB  . ASN B  1  299 ? -8.558  11.310  75.859 1.00 61.95  ? 312 ASN B CB  1 
ATOM   4964 C  CG  . ASN B  1  299 ? -8.791  10.588  77.167 1.00 68.72  ? 312 ASN B CG  1 
ATOM   4965 O  OD1 . ASN B  1  299 ? -9.724  9.784   77.279 1.00 67.54  ? 312 ASN B OD1 1 
ATOM   4966 N  ND2 . ASN B  1  299 ? -7.989  10.887  78.180 1.00 75.23  ? 312 ASN B ND2 1 
ATOM   4967 N  N   . PRO B  1  300 ? -7.878  10.661  72.229 1.00 55.90  ? 313 PRO B N   1 
ATOM   4968 C  CA  . PRO B  1  300 ? -7.604  11.434  71.019 1.00 55.40  ? 313 PRO B CA  1 
ATOM   4969 C  C   . PRO B  1  300 ? -8.797  12.259  70.546 1.00 57.06  ? 313 PRO B C   1 
ATOM   4970 O  O   . PRO B  1  300 ? -9.948  11.907  70.815 1.00 57.63  ? 313 PRO B O   1 
ATOM   4971 C  CB  . PRO B  1  300 ? -7.245  10.315  70.032 1.00 56.64  ? 313 PRO B CB  1 
ATOM   4972 C  CG  . PRO B  1  300 ? -8.147  9.172   70.437 1.00 53.46  ? 313 PRO B CG  1 
ATOM   4973 C  CD  . PRO B  1  300 ? -8.075  9.227   71.951 1.00 53.58  ? 313 PRO B CD  1 
ATOM   4974 N  N   . THR B  1  301 ? -8.493  13.345  69.824 1.00 58.82  ? 314 THR B N   1 
ATOM   4975 C  CA  . THR B  1  301 ? -9.495  14.213  69.227 1.00 61.08  ? 314 THR B CA  1 
ATOM   4976 C  C   . THR B  1  301 ? -9.039  14.567  67.816 1.00 58.45  ? 314 THR B C   1 
ATOM   4977 O  O   . THR B  1  301 ? -7.902  14.306  67.457 1.00 58.79  ? 314 THR B O   1 
ATOM   4978 C  CB  . THR B  1  301 ? -9.673  15.467  70.094 1.00 64.57  ? 314 THR B CB  1 
ATOM   4979 O  OG1 . THR B  1  301 ? -8.400  16.094  70.234 1.00 67.28  ? 314 THR B OG1 1 
ATOM   4980 C  CG2 . THR B  1  301 ? -10.172 15.164  71.497 1.00 63.96  ? 314 THR B CG2 1 
ATOM   4981 N  N   . GLY B  1  302 ? -9.930  15.176  67.032 1.00 57.27  ? 315 GLY B N   1 
ATOM   4982 C  CA  . GLY B  1  302 ? -9.581  15.731  65.732 1.00 61.64  ? 315 GLY B CA  1 
ATOM   4983 C  C   . GLY B  1  302 ? -9.160  14.659  64.722 1.00 64.75  ? 315 GLY B C   1 
ATOM   4984 O  O   . GLY B  1  302 ? -9.710  13.547  64.695 1.00 60.00  ? 315 GLY B O   1 
ATOM   4985 N  N   . ILE B  1  303 ? -8.157  15.013  63.904 1.00 69.62  ? 316 ILE B N   1 
ATOM   4986 C  CA  . ILE B  1  303 ? -7.698  14.158  62.818 1.00 67.85  ? 316 ILE B CA  1 
ATOM   4987 C  C   . ILE B  1  303 ? -7.145  12.862  63.410 1.00 57.45  ? 316 ILE B C   1 
ATOM   4988 O  O   . ILE B  1  303 ? -7.357  11.790  62.861 1.00 55.58  ? 316 ILE B O   1 
ATOM   4989 C  CB  . ILE B  1  303 ? -6.655  14.848  61.916 1.00 77.74  ? 316 ILE B CB  1 
ATOM   4990 C  CG1 . ILE B  1  303 ? -7.023  16.284  61.535 1.00 95.52  ? 316 ILE B CG1 1 
ATOM   4991 C  CG2 . ILE B  1  303 ? -6.432  14.004  60.667 1.00 77.26  ? 316 ILE B CG2 1 
ATOM   4992 C  CD1 . ILE B  1  303 ? -5.979  16.989  60.682 1.00 101.78 ? 316 ILE B CD1 1 
ATOM   4993 N  N   . LEU B  1  304 ? -6.454  12.961  64.544 1.00 52.59  ? 317 LEU B N   1 
ATOM   4994 C  CA  . LEU B  1  304 ? -5.854  11.802  65.185 1.00 54.50  ? 317 LEU B CA  1 
ATOM   4995 C  C   . LEU B  1  304 ? -6.924  10.771  65.546 1.00 55.91  ? 317 LEU B C   1 
ATOM   4996 O  O   . LEU B  1  304 ? -6.740  9.587   65.281 1.00 54.05  ? 317 LEU B O   1 
ATOM   4997 C  CB  . LEU B  1  304 ? -5.055  12.244  66.412 1.00 51.42  ? 317 LEU B CB  1 
ATOM   4998 C  CG  . LEU B  1  304 ? -4.431  11.125  67.249 1.00 55.89  ? 317 LEU B CG  1 
ATOM   4999 C  CD1 . LEU B  1  304 ? -3.486  10.291  66.402 1.00 55.27  ? 317 LEU B CD1 1 
ATOM   5000 C  CD2 . LEU B  1  304 ? -3.733  11.726  68.456 1.00 54.13  ? 317 LEU B CD2 1 
ATOM   5001 N  N   . ARG B  1  305 ? -8.031  11.223  66.152 1.00 56.17  ? 318 ARG B N   1 
ATOM   5002 C  CA  A ARG B  1  305 ? -9.137  10.346  66.504 0.50 54.26  ? 318 ARG B CA  1 
ATOM   5003 C  CA  B ARG B  1  305 ? -9.125  10.332  66.504 0.50 52.22  ? 318 ARG B CA  1 
ATOM   5004 C  C   . ARG B  1  305 ? -9.665  9.677   65.235 1.00 51.52  ? 318 ARG B C   1 
ATOM   5005 O  O   . ARG B  1  305 ? -9.848  8.453   65.184 1.00 49.22  ? 318 ARG B O   1 
ATOM   5006 C  CB  A ARG B  1  305 ? -10.264 11.116  67.217 0.50 55.41  ? 318 ARG B CB  1 
ATOM   5007 C  CB  B ARG B  1  305 ? -10.247 11.057  67.263 0.50 50.47  ? 318 ARG B CB  1 
ATOM   5008 C  CG  A ARG B  1  305 ? -11.480 10.227  67.515 0.50 56.12  ? 318 ARG B CG  1 
ATOM   5009 C  CG  B ARG B  1  305 ? -11.464 10.165  67.506 0.50 48.69  ? 318 ARG B CG  1 
ATOM   5010 C  CD  A ARG B  1  305 ? -12.830 10.951  67.706 0.50 56.82  ? 318 ARG B CD  1 
ATOM   5011 C  CD  B ARG B  1  305 ? -12.517 10.677  68.484 0.50 46.62  ? 318 ARG B CD  1 
ATOM   5012 N  NE  A ARG B  1  305 ? -14.001 10.080  67.920 0.50 54.92  ? 318 ARG B NE  1 
ATOM   5013 N  NE  B ARG B  1  305 ? -12.077 10.519  69.872 0.50 44.53  ? 318 ARG B NE  1 
ATOM   5014 C  CZ  A ARG B  1  305 ? -15.031 9.964   67.066 0.50 50.67  ? 318 ARG B CZ  1 
ATOM   5015 C  CZ  B ARG B  1  305 ? -12.590 9.674   70.748 0.50 40.75  ? 318 ARG B CZ  1 
ATOM   5016 N  NH1 A ARG B  1  305 ? -15.063 10.671  65.947 0.50 51.42  ? 318 ARG B NH1 1 
ATOM   5017 N  NH1 B ARG B  1  305 ? -11.998 9.525   71.913 0.50 42.45  ? 318 ARG B NH1 1 
ATOM   5018 N  NH2 A ARG B  1  305 ? -16.042 9.158   67.344 0.50 45.85  ? 318 ARG B NH2 1 
ATOM   5019 N  NH2 B ARG B  1  305 ? -13.647 8.946   70.452 0.50 39.55  ? 318 ARG B NH2 1 
ATOM   5020 N  N   . ARG B  1  306 ? -9.928  10.510  64.224 1.00 49.37  ? 319 ARG B N   1 
ATOM   5021 C  CA  . ARG B  1  306 ? -10.479 10.048  62.962 1.00 54.86  ? 319 ARG B CA  1 
ATOM   5022 C  C   . ARG B  1  306 ? -9.555  9.005   62.325 1.00 51.21  ? 319 ARG B C   1 
ATOM   5023 O  O   . ARG B  1  306 ? -9.999  7.937   61.907 1.00 46.34  ? 319 ARG B O   1 
ATOM   5024 C  CB  . ARG B  1  306 ? -10.691 11.268  62.062 1.00 65.05  ? 319 ARG B CB  1 
ATOM   5025 C  CG  . ARG B  1  306 ? -11.613 11.030  60.877 1.00 81.64  ? 319 ARG B CG  1 
ATOM   5026 C  CD  . ARG B  1  306 ? -11.645 12.249  59.945 1.00 94.20  ? 319 ARG B CD  1 
ATOM   5027 N  NE  . ARG B  1  306 ? -10.369 12.394  59.231 1.00 108.89 ? 319 ARG B NE  1 
ATOM   5028 C  CZ  . ARG B  1  306 ? -10.039 13.358  58.379 1.00 117.58 ? 319 ARG B CZ  1 
ATOM   5029 N  NH1 . ARG B  1  306 ? -10.886 14.346  58.137 1.00 120.22 ? 319 ARG B NH1 1 
ATOM   5030 N  NH2 . ARG B  1  306 ? -8.856  13.327  57.779 1.00 118.75 ? 319 ARG B NH2 1 
ATOM   5031 N  N   . ASN B  1  307 ? -8.255  9.306   62.264 1.00 48.93  ? 320 ASN B N   1 
ATOM   5032 C  CA  . ASN B  1  307 ? -7.310  8.426   61.593 1.00 48.64  ? 320 ASN B CA  1 
ATOM   5033 C  C   . ASN B  1  307 ? -7.124  7.135   62.380 1.00 50.09  ? 320 ASN B C   1 
ATOM   5034 O  O   . ASN B  1  307 ? -6.888  6.096   61.774 1.00 51.95  ? 320 ASN B O   1 
ATOM   5035 C  CB  . ASN B  1  307 ? -5.994  9.131   61.290 1.00 47.41  ? 320 ASN B CB  1 
ATOM   5036 C  CG  . ASN B  1  307 ? -6.167  10.112  60.156 1.00 50.08  ? 320 ASN B CG  1 
ATOM   5037 O  OD1 . ASN B  1  307 ? -7.302  10.351  59.723 1.00 50.10  ? 320 ASN B OD1 1 
ATOM   5038 N  ND2 . ASN B  1  307 ? -5.071  10.674  59.659 1.00 50.87  ? 320 ASN B ND2 1 
ATOM   5039 N  N   . LEU B  1  308 ? -7.255  7.193   63.711 1.00 50.30  ? 321 LEU B N   1 
ATOM   5040 C  CA  . LEU B  1  308 ? -7.190  5.991   64.526 1.00 49.78  ? 321 LEU B CA  1 
ATOM   5041 C  C   . LEU B  1  308 ? -8.339  5.054   64.165 1.00 49.19  ? 321 LEU B C   1 
ATOM   5042 O  O   . LEU B  1  308 ? -8.152  3.842   64.032 1.00 45.26  ? 321 LEU B O   1 
ATOM   5043 C  CB  . LEU B  1  308 ? -7.235  6.331   66.012 1.00 51.81  ? 321 LEU B CB  1 
ATOM   5044 C  CG  . LEU B  1  308 ? -5.888  6.556   66.698 1.00 53.12  ? 321 LEU B CG  1 
ATOM   5045 C  CD1 . LEU B  1  308 ? -6.085  7.244   68.033 1.00 52.95  ? 321 LEU B CD1 1 
ATOM   5046 C  CD2 . LEU B  1  308 ? -5.168  5.242   66.897 1.00 53.63  ? 321 LEU B CD2 1 
ATOM   5047 N  N   . ILE B  1  309 ? -9.542  5.629   64.057 1.00 47.19  ? 322 ILE B N   1 
ATOM   5048 C  CA  . ILE B  1  309 ? -10.726 4.845   63.781 1.00 44.95  ? 322 ILE B CA  1 
ATOM   5049 C  C   . ILE B  1  309 ? -10.578 4.158   62.423 1.00 46.59  ? 322 ILE B C   1 
ATOM   5050 O  O   . ILE B  1  309 ? -10.895 2.975   62.262 1.00 49.90  ? 322 ILE B O   1 
ATOM   5051 C  CB  . ILE B  1  309 ? -11.984 5.730   63.860 1.00 46.74  ? 322 ILE B CB  1 
ATOM   5052 C  CG1 . ILE B  1  309 ? -12.274 6.147   65.307 1.00 48.30  ? 322 ILE B CG1 1 
ATOM   5053 C  CG2 . ILE B  1  309 ? -13.173 4.999   63.235 1.00 43.40  ? 322 ILE B CG2 1 
ATOM   5054 C  CD1 . ILE B  1  309 ? -13.228 7.318   65.448 1.00 50.93  ? 322 ILE B CD1 1 
ATOM   5055 N  N   . LYS B  1  310 ? -10.119 4.914   61.431 1.00 45.16  ? 323 LYS B N   1 
ATOM   5056 C  CA  . LYS B  1  310 ? -9.955  4.376   60.089 1.00 49.29  ? 323 LYS B CA  1 
ATOM   5057 C  C   . LYS B  1  310 ? -8.900  3.266   60.065 1.00 45.30  ? 323 LYS B C   1 
ATOM   5058 O  O   . LYS B  1  310 ? -9.131  2.197   59.504 1.00 45.52  ? 323 LYS B O   1 
ATOM   5059 C  CB  . LYS B  1  310 ? -9.581  5.498   59.120 1.00 53.77  ? 323 LYS B CB  1 
ATOM   5060 C  CG  . LYS B  1  310 ? -10.709 6.448   58.804 1.00 57.87  ? 323 LYS B CG  1 
ATOM   5061 C  CD  . LYS B  1  310 ? -10.280 7.561   57.860 1.00 65.40  ? 323 LYS B CD  1 
ATOM   5062 C  CE  . LYS B  1  310 ? -11.426 8.262   57.206 1.00 72.24  ? 323 LYS B CE  1 
ATOM   5063 N  NZ  . LYS B  1  310 ? -10.989 9.506   56.575 1.00 76.04  ? 323 LYS B NZ  1 
ATOM   5064 N  N   . ASN B  1  311 ? -7.747  3.516   60.688 1.00 42.30  ? 324 ASN B N   1 
ATOM   5065 C  CA  . ASN B  1  311 ? -6.654  2.557   60.664 1.00 43.62  ? 324 ASN B CA  1 
ATOM   5066 C  C   . ASN B  1  311 ? -7.040  1.285   61.415 1.00 44.44  ? 324 ASN B C   1 
ATOM   5067 O  O   . ASN B  1  311 ? -6.624  0.200   61.038 1.00 43.91  ? 324 ASN B O   1 
ATOM   5068 C  CB  . ASN B  1  311 ? -5.362  3.157   61.206 1.00 44.44  ? 324 ASN B CB  1 
ATOM   5069 C  CG  . ASN B  1  311 ? -4.644  3.966   60.151 1.00 47.22  ? 324 ASN B CG  1 
ATOM   5070 O  OD1 . ASN B  1  311 ? -3.922  3.397   59.328 1.00 48.00  ? 324 ASN B OD1 1 
ATOM   5071 N  ND2 . ASN B  1  311 ? -4.807  5.282   60.155 1.00 50.32  ? 324 ASN B ND2 1 
ATOM   5072 N  N   . LEU B  1  312 ? -7.847  1.412   62.467 1.00 44.68  ? 325 LEU B N   1 
ATOM   5073 C  CA  . LEU B  1  312 ? -8.289  0.251   63.220 1.00 44.05  ? 325 LEU B CA  1 
ATOM   5074 C  C   . LEU B  1  312 ? -9.209  -0.604  62.359 1.00 43.67  ? 325 LEU B C   1 
ATOM   5075 O  O   . LEU B  1  312 ? -9.118  -1.833  62.405 1.00 43.15  ? 325 LEU B O   1 
ATOM   5076 C  CB  . LEU B  1  312 ? -8.960  0.684   64.523 1.00 47.17  ? 325 LEU B CB  1 
ATOM   5077 C  CG  . LEU B  1  312 ? -7.995  1.053   65.655 1.00 45.96  ? 325 LEU B CG  1 
ATOM   5078 C  CD1 . LEU B  1  312 ? -8.687  1.899   66.710 1.00 47.30  ? 325 LEU B CD1 1 
ATOM   5079 C  CD2 . LEU B  1  312 ? -7.401  -0.204  66.273 1.00 44.67  ? 325 LEU B CD2 1 
ATOM   5080 N  N   . HIS B  1  313 ? -10.086 0.058   61.588 1.00 43.09  ? 326 HIS B N   1 
ATOM   5081 C  CA  . HIS B  1  313 ? -10.961 -0.637  60.662 1.00 46.33  ? 326 HIS B CA  1 
ATOM   5082 C  C   . HIS B  1  313 ? -10.121 -1.330  59.583 1.00 46.73  ? 326 HIS B C   1 
ATOM   5083 O  O   . HIS B  1  313 ? -10.326 -2.507  59.288 1.00 46.06  ? 326 HIS B O   1 
ATOM   5084 C  CB  . HIS B  1  313 ? -12.042 0.287   60.073 1.00 43.65  ? 326 HIS B CB  1 
ATOM   5085 C  CG  . HIS B  1  313 ? -12.924 -0.461  59.123 1.00 43.74  ? 326 HIS B CG  1 
ATOM   5086 N  ND1 . HIS B  1  313 ? -13.721 -1.502  59.552 1.00 44.80  ? 326 HIS B ND1 1 
ATOM   5087 C  CD2 . HIS B  1  313 ? -13.066 -0.410  57.789 1.00 45.41  ? 326 HIS B CD2 1 
ATOM   5088 C  CE1 . HIS B  1  313 ? -14.350 -2.027  58.513 1.00 47.94  ? 326 HIS B CE1 1 
ATOM   5089 N  NE2 . HIS B  1  313 ? -13.968 -1.374  57.426 1.00 45.79  ? 326 HIS B NE2 1 
ATOM   5090 N  N   . TYR B  1  314 ? -9.170  -0.596  58.995 1.00 47.23  ? 327 TYR B N   1 
ATOM   5091 C  CA  . TYR B  1  314 ? -8.312  -1.160  57.966 1.00 45.60  ? 327 TYR B CA  1 
ATOM   5092 C  C   . TYR B  1  314 ? -7.629  -2.418  58.487 1.00 44.03  ? 327 TYR B C   1 
ATOM   5093 O  O   . TYR B  1  314 ? -7.610  -3.433  57.799 1.00 45.94  ? 327 TYR B O   1 
ATOM   5094 C  CB  . TYR B  1  314 ? -7.252  -0.159  57.520 1.00 46.03  ? 327 TYR B CB  1 
ATOM   5095 C  CG  . TYR B  1  314 ? -7.779  1.106   56.858 1.00 46.59  ? 327 TYR B CG  1 
ATOM   5096 C  CD1 . TYR B  1  314 ? -9.051  1.171   56.293 1.00 45.16  ? 327 TYR B CD1 1 
ATOM   5097 C  CD2 . TYR B  1  314 ? -6.988  2.245   56.804 1.00 47.17  ? 327 TYR B CD2 1 
ATOM   5098 C  CE1 . TYR B  1  314 ? -9.510  2.328   55.679 1.00 45.27  ? 327 TYR B CE1 1 
ATOM   5099 C  CE2 . TYR B  1  314 ? -7.439  3.409   56.206 1.00 51.02  ? 327 TYR B CE2 1 
ATOM   5100 C  CZ  . TYR B  1  314 ? -8.703  3.450   55.639 1.00 48.38  ? 327 TYR B CZ  1 
ATOM   5101 O  OH  . TYR B  1  314 ? -9.120  4.592   55.021 1.00 49.58  ? 327 TYR B OH  1 
ATOM   5102 N  N   . TRP B  1  315 ? -7.074  -2.351  59.702 1.00 44.43  ? 328 TRP B N   1 
ATOM   5103 C  CA  . TRP B  1  315 ? -6.383  -3.492  60.277 1.00 41.82  ? 328 TRP B CA  1 
ATOM   5104 C  C   . TRP B  1  315 ? -7.348  -4.667  60.411 1.00 42.08  ? 328 TRP B C   1 
ATOM   5105 O  O   . TRP B  1  315 ? -7.039  -5.787  59.997 1.00 42.04  ? 328 TRP B O   1 
ATOM   5106 C  CB  . TRP B  1  315 ? -5.741  -3.134  61.622 1.00 39.26  ? 328 TRP B CB  1 
ATOM   5107 C  CG  . TRP B  1  315 ? -4.814  -4.195  62.151 1.00 41.47  ? 328 TRP B CG  1 
ATOM   5108 C  CD1 . TRP B  1  315 ? -3.821  -4.848  61.474 1.00 42.39  ? 328 TRP B CD1 1 
ATOM   5109 C  CD2 . TRP B  1  315 ? -4.799  -4.734  63.488 1.00 43.31  ? 328 TRP B CD2 1 
ATOM   5110 N  NE1 . TRP B  1  315 ? -3.199  -5.753  62.289 1.00 42.90  ? 328 TRP B NE1 1 
ATOM   5111 C  CE2 . TRP B  1  315 ? -3.766  -5.699  63.533 1.00 43.18  ? 328 TRP B CE2 1 
ATOM   5112 C  CE3 . TRP B  1  315 ? -5.525  -4.480  64.653 1.00 44.92  ? 328 TRP B CE3 1 
ATOM   5113 C  CZ2 . TRP B  1  315 ? -3.466  -6.421  64.683 1.00 41.60  ? 328 TRP B CZ2 1 
ATOM   5114 C  CZ3 . TRP B  1  315 ? -5.220  -5.185  65.799 1.00 45.68  ? 328 TRP B CZ3 1 
ATOM   5115 C  CH2 . TRP B  1  315 ? -4.198  -6.138  65.815 1.00 44.53  ? 328 TRP B CH2 1 
ATOM   5116 N  N   . TRP B  1  316 ? -8.540  -4.388  60.950 1.00 44.04  ? 329 TRP B N   1 
ATOM   5117 C  CA  . TRP B  1  316 ? -9.542  -5.421  61.136 1.00 39.43  ? 329 TRP B CA  1 
ATOM   5118 C  C   . TRP B  1  316 ? -9.869  -6.140  59.827 1.00 39.39  ? 329 TRP B C   1 
ATOM   5119 O  O   . TRP B  1  316 ? -10.110 -7.346  59.863 1.00 37.06  ? 329 TRP B O   1 
ATOM   5120 C  CB  . TRP B  1  316 ? -10.813 -4.856  61.774 1.00 42.24  ? 329 TRP B CB  1 
ATOM   5121 C  CG  . TRP B  1  316 ? -11.910 -5.888  61.836 1.00 42.50  ? 329 TRP B CG  1 
ATOM   5122 C  CD1 . TRP B  1  316 ? -12.078 -6.847  62.790 1.00 43.93  ? 329 TRP B CD1 1 
ATOM   5123 C  CD2 . TRP B  1  316 ? -12.937 -6.115  60.852 1.00 42.51  ? 329 TRP B CD2 1 
ATOM   5124 N  NE1 . TRP B  1  316 ? -13.158 -7.633  62.490 1.00 42.56  ? 329 TRP B NE1 1 
ATOM   5125 C  CE2 . TRP B  1  316 ? -13.704 -7.204  61.313 1.00 43.21  ? 329 TRP B CE2 1 
ATOM   5126 C  CE3 . TRP B  1  316 ? -13.292 -5.490  59.650 1.00 46.37  ? 329 TRP B CE3 1 
ATOM   5127 C  CZ2 . TRP B  1  316 ? -14.799 -7.690  60.606 1.00 47.22  ? 329 TRP B CZ2 1 
ATOM   5128 C  CZ3 . TRP B  1  316 ? -14.383 -5.968  58.956 1.00 49.33  ? 329 TRP B CZ3 1 
ATOM   5129 C  CH2 . TRP B  1  316 ? -15.115 -7.062  59.424 1.00 47.05  ? 329 TRP B CH2 1 
ATOM   5130 N  N   . THR B  1  317 ? -9.894  -5.425  58.687 1.00 42.91  ? 330 THR B N   1 
ATOM   5131 C  CA  . THR B  1  317 ? -10.277 -6.054  57.429 1.00 46.74  ? 330 THR B CA  1 
ATOM   5132 C  C   . THR B  1  317 ? -9.305  -7.187  57.117 1.00 43.46  ? 330 THR B C   1 
ATOM   5133 O  O   . THR B  1  317 ? -9.717  -8.225  56.611 1.00 43.70  ? 330 THR B O   1 
ATOM   5134 C  CB  . THR B  1  317 ? -10.363 -5.087  56.248 1.00 51.49  ? 330 THR B CB  1 
ATOM   5135 O  OG1 . THR B  1  317 ? -9.064  -4.583  55.962 1.00 51.46  ? 330 THR B OG1 1 
ATOM   5136 C  CG2 . THR B  1  317 ? -11.322 -3.935  56.488 1.00 51.82  ? 330 THR B CG2 1 
ATOM   5137 N  N   . GLY B  1  318 ? -8.021  -6.987  57.427 1.00 43.29  ? 331 GLY B N   1 
ATOM   5138 C  CA  . GLY B  1  318 ? -7.044  -8.047  57.243 1.00 41.04  ? 331 GLY B CA  1 
ATOM   5139 C  C   . GLY B  1  318 ? -7.157  -9.119  58.326 1.00 39.56  ? 331 GLY B C   1 
ATOM   5140 O  O   . GLY B  1  318 ? -7.094  -10.313 58.032 1.00 37.64  ? 331 GLY B O   1 
ATOM   5141 N  N   . VAL B  1  319 ? -7.302  -8.680  59.582 1.00 39.06  ? 332 VAL B N   1 
ATOM   5142 C  CA  . VAL B  1  319 ? -7.345  -9.592  60.715 1.00 41.23  ? 332 VAL B CA  1 
ATOM   5143 C  C   . VAL B  1  319 ? -8.517  -10.556 60.558 1.00 42.39  ? 332 VAL B C   1 
ATOM   5144 O  O   . VAL B  1  319 ? -8.379  -11.753 60.824 1.00 43.20  ? 332 VAL B O   1 
ATOM   5145 C  CB  . VAL B  1  319 ? -7.434  -8.782  62.023 1.00 43.13  ? 332 VAL B CB  1 
ATOM   5146 C  CG1 . VAL B  1  319 ? -7.896  -9.616  63.211 1.00 45.28  ? 332 VAL B CG1 1 
ATOM   5147 C  CG2 . VAL B  1  319 ? -6.107  -8.122  62.351 1.00 45.59  ? 332 VAL B CG2 1 
ATOM   5148 N  N   . ASN B  1  320 ? -9.670  -10.022 60.132 1.00 41.86  ? 333 ASN B N   1 
ATOM   5149 C  CA  . ASN B  1  320 ? -10.886 -10.818 60.058 1.00 45.22  ? 333 ASN B CA  1 
ATOM   5150 C  C   . ASN B  1  320 ? -10.659 -12.054 59.190 1.00 50.37  ? 333 ASN B C   1 
ATOM   5151 O  O   . ASN B  1  320 ? -11.097 -13.144 59.544 1.00 47.91  ? 333 ASN B O   1 
ATOM   5152 C  CB  . ASN B  1  320 ? -12.069 -10.015 59.534 1.00 44.95  ? 333 ASN B CB  1 
ATOM   5153 C  CG  . ASN B  1  320 ? -13.374 -10.733 59.780 1.00 45.29  ? 333 ASN B CG  1 
ATOM   5154 O  OD1 . ASN B  1  320 ? -13.642 -11.176 60.899 1.00 44.97  ? 333 ASN B OD1 1 
ATOM   5155 N  ND2 . ASN B  1  320 ? -14.187 -10.891 58.754 1.00 44.76  ? 333 ASN B ND2 1 
ATOM   5156 N  N   . VAL B  1  321 ? -9.952  -11.876 58.067 1.00 54.29  ? 334 VAL B N   1 
ATOM   5157 C  CA  . VAL B  1  321 ? -9.690  -12.977 57.155 1.00 50.35  ? 334 VAL B CA  1 
ATOM   5158 C  C   . VAL B  1  321 ? -8.546  -13.824 57.711 1.00 50.50  ? 334 VAL B C   1 
ATOM   5159 O  O   . VAL B  1  321 ? -8.673  -15.036 57.833 1.00 45.98  ? 334 VAL B O   1 
ATOM   5160 C  CB  . VAL B  1  321 ? -9.388  -12.506 55.718 1.00 51.96  ? 334 VAL B CB  1 
ATOM   5161 C  CG1 . VAL B  1  321 ? -9.193  -13.702 54.794 1.00 51.75  ? 334 VAL B CG1 1 
ATOM   5162 C  CG2 . VAL B  1  321 ? -10.461 -11.573 55.165 1.00 49.71  ? 334 VAL B CG2 1 
ATOM   5163 N  N   . ALA B  1  322 ? -7.421  -13.194 58.063 1.00 49.72  ? 335 ALA B N   1 
ATOM   5164 C  CA  . ALA B  1  322 ? -6.226  -13.950 58.407 1.00 51.55  ? 335 ALA B CA  1 
ATOM   5165 C  C   . ALA B  1  322 ? -6.432  -14.793 59.666 1.00 52.92  ? 335 ALA B C   1 
ATOM   5166 O  O   . ALA B  1  322 ? -5.818  -15.850 59.798 1.00 55.01  ? 335 ALA B O   1 
ATOM   5167 C  CB  . ALA B  1  322 ? -5.039  -13.023 58.562 1.00 51.75  ? 335 ALA B CB  1 
ATOM   5168 N  N   . PHE B  1  323 ? -7.274  -14.323 60.598 1.00 54.24  ? 336 PHE B N   1 
ATOM   5169 C  CA  . PHE B  1  323 ? -7.443  -15.005 61.872 1.00 53.55  ? 336 PHE B CA  1 
ATOM   5170 C  C   . PHE B  1  323 ? -8.714  -15.852 61.874 1.00 52.66  ? 336 PHE B C   1 
ATOM   5171 O  O   . PHE B  1  323 ? -9.032  -16.455 62.893 1.00 55.39  ? 336 PHE B O   1 
ATOM   5172 C  CB  . PHE B  1  323 ? -7.478  -14.016 63.040 1.00 52.05  ? 336 PHE B CB  1 
ATOM   5173 C  CG  . PHE B  1  323 ? -6.182  -13.286 63.359 1.00 52.10  ? 336 PHE B CG  1 
ATOM   5174 C  CD1 . PHE B  1  323 ? -5.004  -13.536 62.658 1.00 50.51  ? 336 PHE B CD1 1 
ATOM   5175 C  CD2 . PHE B  1  323 ? -6.144  -12.360 64.394 1.00 49.22  ? 336 PHE B CD2 1 
ATOM   5176 C  CE1 . PHE B  1  323 ? -3.839  -12.852 62.966 1.00 50.15  ? 336 PHE B CE1 1 
ATOM   5177 C  CE2 . PHE B  1  323 ? -4.972  -11.691 64.705 1.00 50.87  ? 336 PHE B CE2 1 
ATOM   5178 C  CZ  . PHE B  1  323 ? -3.819  -11.939 63.993 1.00 51.75  ? 336 PHE B CZ  1 
ATOM   5179 N  N   . GLY B  1  324 ? -9.432  -15.890 60.747 1.00 52.19  ? 337 GLY B N   1 
ATOM   5180 C  CA  . GLY B  1  324 ? -10.602 -16.741 60.607 1.00 55.48  ? 337 GLY B CA  1 
ATOM   5181 C  C   . GLY B  1  324 ? -11.821 -16.211 61.362 1.00 54.54  ? 337 GLY B C   1 
ATOM   5182 O  O   . GLY B  1  324 ? -12.669 -16.997 61.770 1.00 55.30  ? 337 GLY B O   1 
ATOM   5183 N  N   . GLY B  1  325 ? -11.909 -14.884 61.528 1.00 52.90  ? 338 GLY B N   1 
ATOM   5184 C  CA  . GLY B  1  325 ? -13.105 -14.235 62.049 1.00 51.79  ? 338 GLY B CA  1 
ATOM   5185 C  C   . GLY B  1  325 ? -12.901 -13.712 63.472 1.00 47.91  ? 338 GLY B C   1 
ATOM   5186 O  O   . GLY B  1  325 ? -12.712 -14.490 64.400 1.00 45.00  ? 338 GLY B O   1 
ATOM   5187 N  N   . CYS B  1  326 ? -12.917 -12.384 63.619 1.00 48.30  ? 339 CYS B N   1 
ATOM   5188 C  CA  . CYS B  1  326 ? -12.852 -11.723 64.915 1.00 51.17  ? 339 CYS B CA  1 
ATOM   5189 C  C   . CYS B  1  326 ? -13.899 -10.615 64.951 1.00 52.36  ? 339 CYS B C   1 
ATOM   5190 O  O   . CYS B  1  326 ? -14.100 -9.914  63.954 1.00 47.59  ? 339 CYS B O   1 
ATOM   5191 C  CB  . CYS B  1  326 ? -11.495 -11.074 65.155 1.00 51.27  ? 339 CYS B CB  1 
ATOM   5192 S  SG  . CYS B  1  326 ? -10.105 -12.237 65.198 1.00 60.11  ? 339 CYS B SG  1 
ATOM   5193 N  N   . ASP B  1  327 ? -14.542 -10.450 66.111 1.00 55.95  ? 340 ASP B N   1 
ATOM   5194 C  CA  . ASP B  1  327 ? -15.527 -9.391  66.281 1.00 56.84  ? 340 ASP B CA  1 
ATOM   5195 C  C   . ASP B  1  327 ? -14.793 -8.053  66.280 1.00 55.01  ? 340 ASP B C   1 
ATOM   5196 O  O   . ASP B  1  327 ? -13.863 -7.859  67.068 1.00 50.14  ? 340 ASP B O   1 
ATOM   5197 C  CB  . ASP B  1  327 ? -16.324 -9.552  67.569 1.00 64.29  ? 340 ASP B CB  1 
ATOM   5198 C  CG  . ASP B  1  327 ? -17.096 -10.852 67.735 1.00 66.40  ? 340 ASP B CG  1 
ATOM   5199 O  OD1 . ASP B  1  327 ? -17.342 -11.521 66.708 1.00 62.11  ? 340 ASP B OD1 1 
ATOM   5200 O  OD2 . ASP B  1  327 ? -17.414 -11.192 68.897 1.00 74.44  ? 340 ASP B OD2 1 
ATOM   5201 N  N   . GLU B  1  328 ? -15.218 -7.134  65.402 1.00 49.76  ? 341 GLU B N   1 
ATOM   5202 C  CA  . GLU B  1  328 ? -14.563 -5.842  65.295 1.00 48.03  ? 341 GLU B CA  1 
ATOM   5203 C  C   . GLU B  1  328 ? -14.814 -5.037  66.568 1.00 47.96  ? 341 GLU B C   1 
ATOM   5204 O  O   . GLU B  1  328 ? -15.939 -4.990  67.060 1.00 45.06  ? 341 GLU B O   1 
ATOM   5205 C  CB  . GLU B  1  328 ? -15.031 -5.078  64.058 1.00 46.36  ? 341 GLU B CB  1 
ATOM   5206 C  CG  . GLU B  1  328 ? -14.216 -3.809  63.812 1.00 47.87  ? 341 GLU B CG  1 
ATOM   5207 C  CD  . GLU B  1  328 ? -14.471 -3.148  62.466 1.00 48.47  ? 341 GLU B CD  1 
ATOM   5208 O  OE1 . GLU B  1  328 ? -15.356 -3.623  61.725 1.00 51.79  ? 341 GLU B OE1 1 
ATOM   5209 O  OE2 . GLU B  1  328 ? -13.775 -2.166  62.162 1.00 48.15  ? 341 GLU B OE2 1 
ATOM   5210 N  N   . LEU B  1  329 ? -13.745 -4.427  67.097 1.00 47.42  ? 342 LEU B N   1 
ATOM   5211 C  CA  . LEU B  1  329 ? -13.858 -3.555  68.254 1.00 48.56  ? 342 LEU B CA  1 
ATOM   5212 C  C   . LEU B  1  329 ? -13.786 -2.108  67.770 1.00 51.87  ? 342 LEU B C   1 
ATOM   5213 O  O   . LEU B  1  329 ? -13.110 -1.814  66.782 1.00 53.61  ? 342 LEU B O   1 
ATOM   5214 C  CB  . LEU B  1  329 ? -12.762 -3.860  69.271 1.00 47.65  ? 342 LEU B CB  1 
ATOM   5215 C  CG  . LEU B  1  329 ? -12.747 -5.279  69.845 1.00 50.25  ? 342 LEU B CG  1 
ATOM   5216 C  CD1 . LEU B  1  329 ? -11.483 -5.478  70.660 1.00 52.92  ? 342 LEU B CD1 1 
ATOM   5217 C  CD2 . LEU B  1  329 ? -13.978 -5.614  70.676 1.00 54.29  ? 342 LEU B CD2 1 
ATOM   5218 N  N   . PHE B  1  330 ? -14.489 -1.216  68.478 1.00 46.42  ? 343 PHE B N   1 
ATOM   5219 C  CA  . PHE B  1  330 ? -14.583 0.188   68.110 1.00 48.09  ? 343 PHE B CA  1 
ATOM   5220 C  C   . PHE B  1  330 ? -14.305 1.044   69.344 1.00 52.12  ? 343 PHE B C   1 
ATOM   5221 O  O   . PHE B  1  330 ? -15.198 1.702   69.882 1.00 52.37  ? 343 PHE B O   1 
ATOM   5222 C  CB  . PHE B  1  330 ? -15.964 0.517   67.554 1.00 49.09  ? 343 PHE B CB  1 
ATOM   5223 C  CG  . PHE B  1  330 ? -16.378 -0.342  66.375 1.00 49.18  ? 343 PHE B CG  1 
ATOM   5224 C  CD1 . PHE B  1  330 ? -15.901 -0.066  65.101 1.00 50.45  ? 343 PHE B CD1 1 
ATOM   5225 C  CD2 . PHE B  1  330 ? -17.246 -1.414  66.541 1.00 49.64  ? 343 PHE B CD2 1 
ATOM   5226 C  CE1 . PHE B  1  330 ? -16.340 -0.800  64.010 1.00 50.05  ? 343 PHE B CE1 1 
ATOM   5227 C  CE2 . PHE B  1  330 ? -17.645 -2.173  65.454 1.00 52.19  ? 343 PHE B CE2 1 
ATOM   5228 C  CZ  . PHE B  1  330 ? -17.200 -1.863  64.190 1.00 51.65  ? 343 PHE B CZ  1 
ATOM   5229 N  N   . PRO B  1  331 ? -13.041 1.076   69.814 1.00 49.84  ? 344 PRO B N   1 
ATOM   5230 C  CA  . PRO B  1  331 ? -12.712 1.774   71.054 1.00 49.47  ? 344 PRO B CA  1 
ATOM   5231 C  C   . PRO B  1  331 ? -12.957 3.277   71.031 1.00 46.27  ? 344 PRO B C   1 
ATOM   5232 O  O   . PRO B  1  331 ? -13.052 3.881   72.094 1.00 53.35  ? 344 PRO B O   1 
ATOM   5233 C  CB  . PRO B  1  331 ? -11.227 1.422   71.252 1.00 52.40  ? 344 PRO B CB  1 
ATOM   5234 C  CG  . PRO B  1  331 ? -10.725 1.175   69.850 1.00 55.11  ? 344 PRO B CG  1 
ATOM   5235 C  CD  . PRO B  1  331 ? -11.874 0.445   69.175 1.00 50.48  ? 344 PRO B CD  1 
ATOM   5236 N  N   . TYR B  1  332 ? -13.049 3.875   69.842 1.00 43.38  ? 345 TYR B N   1 
ATOM   5237 C  CA  . TYR B  1  332 ? -13.310 5.305   69.737 1.00 46.58  ? 345 TYR B CA  1 
ATOM   5238 C  C   . TYR B  1  332 ? -14.637 5.567   69.018 1.00 48.73  ? 345 TYR B C   1 
ATOM   5239 O  O   . TYR B  1  332 ? -14.868 6.676   68.536 1.00 49.52  ? 345 TYR B O   1 
ATOM   5240 C  CB  . TYR B  1  332 ? -12.150 5.990   69.016 1.00 46.22  ? 345 TYR B CB  1 
ATOM   5241 C  CG  . TYR B  1  332 ? -10.797 5.651   69.616 1.00 48.35  ? 345 TYR B CG  1 
ATOM   5242 C  CD1 . TYR B  1  332 ? -10.423 6.196   70.833 1.00 46.31  ? 345 TYR B CD1 1 
ATOM   5243 C  CD2 . TYR B  1  332 ? -9.887  4.828   68.954 1.00 47.11  ? 345 TYR B CD2 1 
ATOM   5244 C  CE1 . TYR B  1  332 ? -9.195  5.903   71.403 1.00 51.07  ? 345 TYR B CE1 1 
ATOM   5245 C  CE2 . TYR B  1  332 ? -8.663  4.513   69.522 1.00 48.95  ? 345 TYR B CE2 1 
ATOM   5246 C  CZ  . TYR B  1  332 ? -8.309  5.067   70.739 1.00 51.02  ? 345 TYR B CZ  1 
ATOM   5247 O  OH  . TYR B  1  332 ? -7.102  4.759   71.290 1.00 49.79  ? 345 TYR B OH  1 
ATOM   5248 N  N   . GLY B  1  333 ? -15.503 4.550   68.956 1.00 51.91  ? 346 GLY B N   1 
ATOM   5249 C  CA  . GLY B  1  333 ? -16.776 4.682   68.264 1.00 56.79  ? 346 GLY B CA  1 
ATOM   5250 C  C   . GLY B  1  333 ? -16.608 4.626   66.746 1.00 61.40  ? 346 GLY B C   1 
ATOM   5251 O  O   . GLY B  1  333 ? -15.664 4.013   66.248 1.00 57.22  ? 346 GLY B O   1 
ATOM   5252 N  N   . GLN B  1  334 ? -17.531 5.292   66.034 1.00 67.49  ? 347 GLN B N   1 
ATOM   5253 C  CA  A GLN B  1  334 ? -17.615 5.263   64.582 0.50 71.86  ? 347 GLN B CA  1 
ATOM   5254 C  CA  B GLN B  1  334 ? -17.587 5.258   64.578 0.50 68.83  ? 347 GLN B CA  1 
ATOM   5255 C  C   . GLN B  1  334 ? -17.480 6.677   64.020 1.00 72.55  ? 347 GLN B C   1 
ATOM   5256 O  O   . GLN B  1  334 ? -17.546 7.653   64.766 1.00 75.00  ? 347 GLN B O   1 
ATOM   5257 C  CB  A GLN B  1  334 ? -18.954 4.655   64.163 0.50 75.43  ? 347 GLN B CB  1 
ATOM   5258 C  CB  B GLN B  1  334 ? -18.834 4.500   64.115 0.50 68.13  ? 347 GLN B CB  1 
ATOM   5259 C  CG  A GLN B  1  334 ? -19.078 3.173   64.476 0.50 78.80  ? 347 GLN B CG  1 
ATOM   5260 C  CG  B GLN B  1  334 ? -18.701 2.991   64.308 0.50 66.82  ? 347 GLN B CG  1 
ATOM   5261 C  CD  A GLN B  1  334 ? -18.009 2.357   63.794 0.50 82.46  ? 347 GLN B CD  1 
ATOM   5262 C  CD  B GLN B  1  334 ? -19.916 2.196   63.882 0.50 63.34  ? 347 GLN B CD  1 
ATOM   5263 O  OE1 A GLN B  1  334 ? -17.914 2.267   62.543 0.50 83.60  ? 347 GLN B OE1 1 
ATOM   5264 O  OE1 B GLN B  1  334 ? -20.980 2.748   63.581 0.50 70.72  ? 347 GLN B OE1 1 
ATOM   5265 N  NE2 A GLN B  1  334 ? -17.184 1.772   64.649 0.50 86.77  ? 347 GLN B NE2 1 
ATOM   5266 N  NE2 B GLN B  1  334 ? -19.770 0.879   63.869 0.50 58.46  ? 347 GLN B NE2 1 
ATOM   5267 N  N   . LEU B  1  335 ? -17.293 6.774   62.694 1.00 74.63  ? 348 LEU B N   1 
ATOM   5268 C  CA  . LEU B  1  335 ? -17.166 8.061   62.021 1.00 82.46  ? 348 LEU B CA  1 
ATOM   5269 C  C   . LEU B  1  335 ? -18.551 8.686   61.759 1.00 80.94  ? 348 LEU B C   1 
ATOM   5270 O  O   . LEU B  1  335 ? -19.576 8.008   61.997 1.00 83.63  ? 348 LEU B O   1 
ATOM   5271 C  CB  . LEU B  1  335 ? -16.359 7.915   60.728 1.00 85.53  ? 348 LEU B CB  1 
ATOM   5272 C  CG  . LEU B  1  335 ? -14.860 7.644   60.908 1.00 85.56  ? 348 LEU B CG  1 
ATOM   5273 C  CD1 . LEU B  1  335 ? -14.160 7.603   59.569 1.00 82.05  ? 348 LEU B CD1 1 
ATOM   5274 C  CD2 . LEU B  1  335 ? -14.154 8.643   61.824 1.00 89.81  ? 348 LEU B CD2 1 
ATOM   5275 N  N   . GLN C  1  1   ? 2.633   -17.537 25.297 1.00 148.05 ? 14  GLN C N   1 
ATOM   5276 C  CA  . GLN C  1  1   ? 2.810   -16.180 25.884 1.00 144.39 ? 14  GLN C CA  1 
ATOM   5277 C  C   . GLN C  1  1   ? 3.144   -15.169 24.780 1.00 133.87 ? 14  GLN C C   1 
ATOM   5278 O  O   . GLN C  1  1   ? 2.443   -14.166 24.633 1.00 129.28 ? 14  GLN C O   1 
ATOM   5279 C  CB  . GLN C  1  1   ? 3.806   -16.228 27.051 1.00 148.78 ? 14  GLN C CB  1 
ATOM   5280 C  CG  . GLN C  1  1   ? 5.257   -16.542 26.691 1.00 149.68 ? 14  GLN C CG  1 
ATOM   5281 C  CD  . GLN C  1  1   ? 5.507   -17.974 26.274 1.00 150.57 ? 14  GLN C CD  1 
ATOM   5282 O  OE1 . GLN C  1  1   ? 4.709   -18.881 26.538 1.00 152.38 ? 14  GLN C OE1 1 
ATOM   5283 N  NE2 . GLN C  1  1   ? 6.640   -18.193 25.623 1.00 148.24 ? 14  GLN C NE2 1 
ATOM   5284 N  N   . GLY C  1  2   ? 4.188   -15.459 23.984 1.00 119.69 ? 15  GLY C N   1 
ATOM   5285 C  CA  . GLY C  1  2   ? 4.791   -14.485 23.086 1.00 101.80 ? 15  GLY C CA  1 
ATOM   5286 C  C   . GLY C  1  2   ? 4.309   -14.642 21.643 1.00 85.91  ? 15  GLY C C   1 
ATOM   5287 O  O   . GLY C  1  2   ? 4.195   -15.754 21.137 1.00 76.69  ? 15  GLY C O   1 
ATOM   5288 N  N   . VAL C  1  3   ? 4.046   -13.503 20.992 1.00 76.48  ? 16  VAL C N   1 
ATOM   5289 C  CA  . VAL C  1  3   ? 3.524   -13.454 19.636 1.00 69.22  ? 16  VAL C CA  1 
ATOM   5290 C  C   . VAL C  1  3   ? 4.593   -12.876 18.713 1.00 60.87  ? 16  VAL C C   1 
ATOM   5291 O  O   . VAL C  1  3   ? 5.401   -12.055 19.132 1.00 53.05  ? 16  VAL C O   1 
ATOM   5292 C  CB  . VAL C  1  3   ? 2.234   -12.608 19.612 1.00 73.37  ? 16  VAL C CB  1 
ATOM   5293 C  CG1 . VAL C  1  3   ? 1.855   -12.155 18.207 1.00 74.78  ? 16  VAL C CG1 1 
ATOM   5294 C  CG2 . VAL C  1  3   ? 1.065   -13.340 20.266 1.00 75.44  ? 16  VAL C CG2 1 
ATOM   5295 N  N   . ASP C  1  4   ? 4.576   -13.302 17.446 1.00 58.57  ? 17  ASP C N   1 
ATOM   5296 C  CA  . ASP C  1  4   ? 5.432   -12.744 16.411 1.00 58.70  ? 17  ASP C CA  1 
ATOM   5297 C  C   . ASP C  1  4   ? 4.624   -11.707 15.627 1.00 55.60  ? 17  ASP C C   1 
ATOM   5298 O  O   . ASP C  1  4   ? 3.754   -12.075 14.843 1.00 54.83  ? 17  ASP C O   1 
ATOM   5299 C  CB  . ASP C  1  4   ? 5.986   -13.868 15.550 1.00 66.18  ? 17  ASP C CB  1 
ATOM   5300 C  CG  . ASP C  1  4   ? 7.193   -13.524 14.689 1.00 76.99  ? 17  ASP C CG  1 
ATOM   5301 O  OD1 . ASP C  1  4   ? 7.463   -12.311 14.497 1.00 81.57  ? 17  ASP C OD1 1 
ATOM   5302 O  OD2 . ASP C  1  4   ? 7.855   -14.478 14.219 1.00 85.79  ? 17  ASP C OD2 1 
ATOM   5303 N  N   . PRO C  1  5   ? 4.861   -10.384 15.810 1.00 48.98  ? 18  PRO C N   1 
ATOM   5304 C  CA  . PRO C  1  5   ? 3.956   -9.370  15.264 1.00 46.91  ? 18  PRO C CA  1 
ATOM   5305 C  C   . PRO C  1  5   ? 4.138   -9.186  13.758 1.00 45.07  ? 18  PRO C C   1 
ATOM   5306 O  O   . PRO C  1  5   ? 5.242   -8.933  13.297 1.00 40.95  ? 18  PRO C O   1 
ATOM   5307 C  CB  . PRO C  1  5   ? 4.315   -8.101  16.054 1.00 48.30  ? 18  PRO C CB  1 
ATOM   5308 C  CG  . PRO C  1  5   ? 5.758   -8.303  16.490 1.00 46.70  ? 18  PRO C CG  1 
ATOM   5309 C  CD  . PRO C  1  5   ? 6.020   -9.798  16.504 1.00 45.70  ? 18  PRO C CD  1 
ATOM   5310 N  N   . PRO C  1  6   ? 3.056   -9.277  12.953 1.00 43.75  ? 19  PRO C N   1 
ATOM   5311 C  CA  . PRO C  1  6   ? 3.159   -9.156  11.501 1.00 48.40  ? 19  PRO C CA  1 
ATOM   5312 C  C   . PRO C  1  6   ? 3.317   -7.694  11.097 1.00 48.97  ? 19  PRO C C   1 
ATOM   5313 O  O   . PRO C  1  6   ? 3.012   -6.797  11.883 1.00 44.72  ? 19  PRO C O   1 
ATOM   5314 C  CB  . PRO C  1  6   ? 1.828   -9.747  11.014 1.00 48.99  ? 19  PRO C CB  1 
ATOM   5315 C  CG  . PRO C  1  6   ? 0.848   -9.374  12.104 1.00 49.62  ? 19  PRO C CG  1 
ATOM   5316 C  CD  . PRO C  1  6   ? 1.663   -9.449  13.405 1.00 48.74  ? 19  PRO C CD  1 
ATOM   5317 N  N   . PRO C  1  7   ? 3.805   -7.408  9.871  1.00 50.07  ? 20  PRO C N   1 
ATOM   5318 C  CA  . PRO C  1  7   ? 3.909   -6.033  9.392  1.00 46.10  ? 20  PRO C CA  1 
ATOM   5319 C  C   . PRO C  1  7   ? 2.522   -5.428  9.263  1.00 41.81  ? 20  PRO C C   1 
ATOM   5320 O  O   . PRO C  1  7   ? 1.538   -6.149  9.163  1.00 39.69  ? 20  PRO C O   1 
ATOM   5321 C  CB  . PRO C  1  7   ? 4.660   -6.143  8.054  1.00 52.62  ? 20  PRO C CB  1 
ATOM   5322 C  CG  . PRO C  1  7   ? 4.414   -7.569  7.616  1.00 56.74  ? 20  PRO C CG  1 
ATOM   5323 C  CD  . PRO C  1  7   ? 4.293   -8.390  8.889  1.00 55.98  ? 20  PRO C CD  1 
ATOM   5324 N  N   . PRO C  1  8   ? 2.380   -4.086  9.304  1.00 38.98  ? 21  PRO C N   1 
ATOM   5325 C  CA  . PRO C  1  8   ? 1.066   -3.465  9.197  1.00 38.08  ? 21  PRO C CA  1 
ATOM   5326 C  C   . PRO C  1  8   ? 0.415   -3.749  7.847  1.00 39.70  ? 21  PRO C C   1 
ATOM   5327 O  O   . PRO C  1  8   ? 1.097   -3.892  6.831  1.00 36.71  ? 21  PRO C O   1 
ATOM   5328 C  CB  . PRO C  1  8   ? 1.338   -1.980  9.386  1.00 37.13  ? 21  PRO C CB  1 
ATOM   5329 C  CG  . PRO C  1  8   ? 2.797   -1.825  9.027  1.00 37.68  ? 21  PRO C CG  1 
ATOM   5330 C  CD  . PRO C  1  8   ? 3.455   -3.106  9.460  1.00 36.45  ? 21  PRO C CD  1 
ATOM   5331 N  N   . PRO C  1  9   ? -0.930  -3.805  7.804  1.00 37.00  ? 22  PRO C N   1 
ATOM   5332 C  CA  . PRO C  1  9   ? -1.650  -3.822  6.539  1.00 39.59  ? 22  PRO C CA  1 
ATOM   5333 C  C   . PRO C  1  9   ? -1.273  -2.589  5.726  1.00 36.47  ? 22  PRO C C   1 
ATOM   5334 O  O   . PRO C  1  9   ? -0.935  -1.551  6.293  1.00 36.38  ? 22  PRO C O   1 
ATOM   5335 C  CB  . PRO C  1  9   ? -3.148  -3.812  6.946  1.00 40.66  ? 22  PRO C CB  1 
ATOM   5336 C  CG  . PRO C  1  9   ? -3.141  -4.268  8.391  1.00 41.19  ? 22  PRO C CG  1 
ATOM   5337 C  CD  . PRO C  1  9   ? -1.815  -3.826  8.974  1.00 38.96  ? 22  PRO C CD  1 
ATOM   5338 N  N   . GLY C  1  10  ? -1.367  -2.728  4.400  1.00 33.28  ? 23  GLY C N   1 
ATOM   5339 C  CA  . GLY C  1  10  ? -1.312  -1.602  3.489  1.00 33.17  ? 23  GLY C CA  1 
ATOM   5340 C  C   . GLY C  1  10  ? -2.689  -0.964  3.356  1.00 35.96  ? 23  GLY C C   1 
ATOM   5341 O  O   . GLY C  1  10  ? -3.608  -1.320  4.086  1.00 35.82  ? 23  GLY C O   1 
ATOM   5342 N  N   . PRO C  1  11  ? -2.859  -0.013  2.410  1.00 35.78  ? 24  PRO C N   1 
ATOM   5343 C  CA  . PRO C  1  11  ? -4.146  0.641   2.170  1.00 36.43  ? 24  PRO C CA  1 
ATOM   5344 C  C   . PRO C  1  11  ? -5.228  -0.379  1.864  1.00 37.35  ? 24  PRO C C   1 
ATOM   5345 O  O   . PRO C  1  11  ? -4.929  -1.476  1.405  1.00 37.63  ? 24  PRO C O   1 
ATOM   5346 C  CB  . PRO C  1  11  ? -3.888  1.584   0.971  1.00 36.36  ? 24  PRO C CB  1 
ATOM   5347 C  CG  . PRO C  1  11  ? -2.391  1.750   0.931  1.00 36.05  ? 24  PRO C CG  1 
ATOM   5348 C  CD  . PRO C  1  11  ? -1.807  0.475   1.511  1.00 35.83  ? 24  PRO C CD  1 
ATOM   5349 N  N   . PRO C  1  12  ? -6.521  -0.048  2.070  1.00 38.53  ? 25  PRO C N   1 
ATOM   5350 C  CA  . PRO C  1  12  ? -7.592  -0.978  1.721  1.00 37.53  ? 25  PRO C CA  1 
ATOM   5351 C  C   . PRO C  1  12  ? -7.659  -1.116  0.201  1.00 40.44  ? 25  PRO C C   1 
ATOM   5352 O  O   . PRO C  1  12  ? -7.313  -0.174  -0.518 1.00 43.96  ? 25  PRO C O   1 
ATOM   5353 C  CB  . PRO C  1  12  ? -8.838  -0.332  2.335  1.00 36.85  ? 25  PRO C CB  1 
ATOM   5354 C  CG  . PRO C  1  12  ? -8.523  1.148   2.339  1.00 38.89  ? 25  PRO C CG  1 
ATOM   5355 C  CD  . PRO C  1  12  ? -7.019  1.243   2.577  1.00 38.16  ? 25  PRO C CD  1 
ATOM   5356 N  N   . SER C  1  13  ? -8.093  -2.296  -0.269 1.00 42.39  ? 26  SER C N   1 
ATOM   5357 C  CA  A SER C  1  13  ? -8.189  -2.586  -1.693 0.50 43.37  ? 26  SER C CA  1 
ATOM   5358 C  CA  B SER C  1  13  ? -8.187  -2.584  -1.691 0.50 45.65  ? 26  SER C CA  1 
ATOM   5359 C  C   . SER C  1  13  ? -9.088  -1.563  -2.387 1.00 42.04  ? 26  SER C C   1 
ATOM   5360 O  O   . SER C  1  13  ? -8.753  -1.066  -3.454 1.00 42.71  ? 26  SER C O   1 
ATOM   5361 C  CB  A SER C  1  13  ? -8.690  -3.984  -1.926 0.50 43.20  ? 26  SER C CB  1 
ATOM   5362 C  CB  B SER C  1  13  ? -8.678  -3.994  -1.912 0.50 48.40  ? 26  SER C CB  1 
ATOM   5363 O  OG  A SER C  1  13  ? -7.796  -4.924  -1.351 0.50 41.06  ? 26  SER C OG  1 
ATOM   5364 O  OG  B SER C  1  13  ? -8.837  -4.268  -3.296 0.50 52.61  ? 26  SER C OG  1 
ATOM   5365 N  N   . PHE C  1  14  ? -10.234 -1.268  -1.765 1.00 40.60  ? 27  PHE C N   1 
ATOM   5366 C  CA  . PHE C  1  14  ? -11.182 -0.279  -2.253 1.00 39.04  ? 27  PHE C CA  1 
ATOM   5367 C  C   . PHE C  1  14  ? -11.116 0.946   -1.342 1.00 40.59  ? 27  PHE C C   1 
ATOM   5368 O  O   . PHE C  1  14  ? -11.236 0.804   -0.122 1.00 38.42  ? 27  PHE C O   1 
ATOM   5369 C  CB  . PHE C  1  14  ? -12.581 -0.906  -2.288 1.00 40.65  ? 27  PHE C CB  1 
ATOM   5370 C  CG  . PHE C  1  14  ? -13.687 0.057   -2.687 1.00 41.36  ? 27  PHE C CG  1 
ATOM   5371 C  CD1 . PHE C  1  14  ? -13.829 0.480   -4.004 1.00 42.08  ? 27  PHE C CD1 1 
ATOM   5372 C  CD2 . PHE C  1  14  ? -14.594 0.522   -1.742 1.00 44.93  ? 27  PHE C CD2 1 
ATOM   5373 C  CE1 . PHE C  1  14  ? -14.844 1.357   -4.360 1.00 43.62  ? 27  PHE C CE1 1 
ATOM   5374 C  CE2 . PHE C  1  14  ? -15.609 1.397   -2.101 1.00 46.11  ? 27  PHE C CE2 1 
ATOM   5375 C  CZ  . PHE C  1  14  ? -15.731 1.817   -3.406 1.00 42.86  ? 27  PHE C CZ  1 
ATOM   5376 N  N   . THR C  1  15  ? -10.935 2.137   -1.935 1.00 37.62  ? 28  THR C N   1 
ATOM   5377 C  CA  . THR C  1  15  ? -10.744 3.364   -1.176 1.00 38.04  ? 28  THR C CA  1 
ATOM   5378 C  C   . THR C  1  15  ? -11.853 4.379   -1.448 1.00 39.79  ? 28  THR C C   1 
ATOM   5379 O  O   . THR C  1  15  ? -11.700 5.533   -1.075 1.00 37.67  ? 28  THR C O   1 
ATOM   5380 C  CB  . THR C  1  15  ? -9.391  3.987   -1.520 1.00 39.28  ? 28  THR C CB  1 
ATOM   5381 O  OG1 . THR C  1  15  ? -9.495  4.455   -2.857 1.00 38.82  ? 28  THR C OG1 1 
ATOM   5382 C  CG2 . THR C  1  15  ? -8.226  3.025   -1.376 1.00 41.99  ? 28  THR C CG2 1 
ATOM   5383 N  N   . GLY C  1  16  ? -12.941 3.975   -2.108 1.00 40.98  ? 29  GLY C N   1 
ATOM   5384 C  CA  . GLY C  1  16  ? -14.069 4.864   -2.353 1.00 40.69  ? 29  GLY C CA  1 
ATOM   5385 C  C   . GLY C  1  16  ? -15.032 4.870   -1.162 1.00 48.30  ? 29  GLY C C   1 
ATOM   5386 O  O   . GLY C  1  16  ? -14.765 4.219   -0.154 1.00 46.66  ? 29  GLY C O   1 
ATOM   5387 N  N   . THR C  1  17  ? -16.153 5.597   -1.288 1.00 50.41  ? 30  THR C N   1 
ATOM   5388 C  CA  . THR C  1  17  ? -17.138 5.659   -0.217 1.00 48.99  ? 30  THR C CA  1 
ATOM   5389 C  C   . THR C  1  17  ? -17.907 4.347   -0.177 1.00 51.12  ? 30  THR C C   1 
ATOM   5390 O  O   . THR C  1  17  ? -17.993 3.641   -1.185 1.00 49.41  ? 30  THR C O   1 
ATOM   5391 C  CB  . THR C  1  17  ? -18.099 6.837   -0.380 1.00 50.90  ? 30  THR C CB  1 
ATOM   5392 O  OG1 . THR C  1  17  ? -18.803 6.878   0.862  1.00 52.54  ? 30  THR C OG1 1 
ATOM   5393 C  CG2 . THR C  1  17  ? -19.059 6.656   -1.544 1.00 50.72  ? 30  THR C CG2 1 
ATOM   5394 N  N   . LYS C  1  18  ? -18.451 4.045   1.006  1.00 50.77  ? 31  LYS C N   1 
ATOM   5395 C  CA  . LYS C  1  18  ? -19.396 2.954   1.167  1.00 54.52  ? 31  LYS C CA  1 
ATOM   5396 C  C   . LYS C  1  18  ? -20.131 3.109   2.496  1.00 53.80  ? 31  LYS C C   1 
ATOM   5397 O  O   . LYS C  1  18  ? -19.705 3.878   3.357  1.00 46.47  ? 31  LYS C O   1 
ATOM   5398 C  CB  . LYS C  1  18  ? -18.695 1.594   1.109  1.00 54.78  ? 31  LYS C CB  1 
ATOM   5399 C  CG  . LYS C  1  18  ? -17.748 1.264   2.255  1.00 56.65  ? 31  LYS C CG  1 
ATOM   5400 C  CD  . LYS C  1  18  ? -17.261 -0.174  2.102  1.00 60.70  ? 31  LYS C CD  1 
ATOM   5401 C  CE  . LYS C  1  18  ? -17.137 -0.944  3.365  1.00 64.36  ? 31  LYS C CE  1 
ATOM   5402 N  NZ  . LYS C  1  18  ? -16.486 -2.221  3.072  1.00 67.55  ? 31  LYS C NZ  1 
ATOM   5403 N  N   . LEU C  1  19  ? -21.253 2.394   2.626  1.00 51.30  ? 32  LEU C N   1 
ATOM   5404 C  CA  . LEU C  1  19  ? -21.991 2.321   3.874  1.00 49.35  ? 32  LEU C CA  1 
ATOM   5405 C  C   . LEU C  1  19  ? -21.152 1.547   4.884  1.00 46.17  ? 32  LEU C C   1 
ATOM   5406 O  O   . LEU C  1  19  ? -20.811 0.398   4.629  1.00 46.75  ? 32  LEU C O   1 
ATOM   5407 C  CB  . LEU C  1  19  ? -23.333 1.627   3.644  1.00 49.47  ? 32  LEU C CB  1 
ATOM   5408 C  CG  . LEU C  1  19  ? -24.167 1.350   4.902  1.00 53.05  ? 32  LEU C CG  1 
ATOM   5409 C  CD1 . LEU C  1  19  ? -24.617 2.660   5.534  1.00 53.41  ? 32  LEU C CD1 1 
ATOM   5410 C  CD2 . LEU C  1  19  ? -25.359 0.453   4.599  1.00 54.91  ? 32  LEU C CD2 1 
ATOM   5411 N  N   . VAL C  1  20  ? -20.836 2.163   6.032  1.00 46.49  ? 33  VAL C N   1 
ATOM   5412 C  CA  . VAL C  1  20  ? -20.046 1.472   7.043  1.00 49.45  ? 33  VAL C CA  1 
ATOM   5413 C  C   . VAL C  1  20  ? -20.915 1.100   8.242  1.00 46.24  ? 33  VAL C C   1 
ATOM   5414 O  O   . VAL C  1  20  ? -20.585 0.165   8.974  1.00 41.31  ? 33  VAL C O   1 
ATOM   5415 C  CB  . VAL C  1  20  ? -18.788 2.251   7.468  1.00 52.47  ? 33  VAL C CB  1 
ATOM   5416 C  CG1 . VAL C  1  20  ? -17.832 2.425   6.293  1.00 51.75  ? 33  VAL C CG1 1 
ATOM   5417 C  CG2 . VAL C  1  20  ? -19.115 3.593   8.100  1.00 53.65  ? 33  VAL C CG2 1 
ATOM   5418 N  N   . ASN C  1  21  ? -22.015 1.830   8.434  1.00 46.91  ? 34  ASN C N   1 
ATOM   5419 C  CA  . ASN C  1  21  ? -23.007 1.493   9.443  1.00 48.21  ? 34  ASN C CA  1 
ATOM   5420 C  C   . ASN C  1  21  ? -23.998 0.503   8.841  1.00 50.12  ? 34  ASN C C   1 
ATOM   5421 O  O   . ASN C  1  21  ? -25.122 0.878   8.527  1.00 55.46  ? 34  ASN C O   1 
ATOM   5422 C  CB  . ASN C  1  21  ? -23.695 2.759   9.952  1.00 46.90  ? 34  ASN C CB  1 
ATOM   5423 C  CG  . ASN C  1  21  ? -24.593 2.504   11.141 1.00 46.77  ? 34  ASN C CG  1 
ATOM   5424 O  OD1 . ASN C  1  21  ? -24.700 1.374   11.643 1.00 46.92  ? 34  ASN C OD1 1 
ATOM   5425 N  ND2 . ASN C  1  21  ? -25.225 3.562   11.621 1.00 47.41  ? 34  ASN C ND2 1 
ATOM   5426 N  N   . ASP C  1  22  ? -23.569 -0.754  8.689  1.00 50.58  ? 35  ASP C N   1 
ATOM   5427 C  CA  . ASP C  1  22  ? -24.289 -1.740  7.891  1.00 56.38  ? 35  ASP C CA  1 
ATOM   5428 C  C   . ASP C  1  22  ? -24.691 -2.910  8.785  1.00 60.16  ? 35  ASP C C   1 
ATOM   5429 O  O   . ASP C  1  22  ? -24.446 -2.880  9.983  1.00 64.52  ? 35  ASP C O   1 
ATOM   5430 C  CB  . ASP C  1  22  ? -23.451 -2.179  6.694  1.00 57.99  ? 35  ASP C CB  1 
ATOM   5431 C  CG  . ASP C  1  22  ? -22.110 -2.826  7.029  1.00 57.61  ? 35  ASP C CG  1 
ATOM   5432 O  OD1 . ASP C  1  22  ? -21.794 -2.963  8.231  1.00 54.88  ? 35  ASP C OD1 1 
ATOM   5433 O  OD2 . ASP C  1  22  ? -21.391 -3.205  6.092  1.00 56.45  ? 35  ASP C OD2 1 
ATOM   5434 N  N   . ALA C  1  23  ? -25.277 -3.952  8.188  1.00 61.86  ? 36  ALA C N   1 
ATOM   5435 C  CA  . ALA C  1  23  ? -25.901 -5.026  8.946  1.00 65.11  ? 36  ALA C CA  1 
ATOM   5436 C  C   . ALA C  1  23  ? -24.850 -5.826  9.706  1.00 65.34  ? 36  ALA C C   1 
ATOM   5437 O  O   . ALA C  1  23  ? -25.117 -6.302  10.808 1.00 66.16  ? 36  ALA C O   1 
ATOM   5438 C  CB  . ALA C  1  23  ? -26.704 -5.920  8.025  1.00 64.04  ? 36  ALA C CB  1 
ATOM   5439 N  N   . ASP C  1  24  ? -23.654 -5.948  9.121  1.00 66.26  ? 37  ASP C N   1 
ATOM   5440 C  CA  . ASP C  1  24  ? -22.587 -6.736  9.716  1.00 64.01  ? 37  ASP C CA  1 
ATOM   5441 C  C   . ASP C  1  24  ? -21.919 -5.990  10.875 1.00 53.35  ? 37  ASP C C   1 
ATOM   5442 O  O   . ASP C  1  24  ? -21.193 -6.615  11.645 1.00 52.93  ? 37  ASP C O   1 
ATOM   5443 C  CB  . ASP C  1  24  ? -21.520 -7.117  8.700  1.00 70.08  ? 37  ASP C CB  1 
ATOM   5444 C  CG  . ASP C  1  24  ? -21.990 -7.874  7.471  1.00 76.85  ? 37  ASP C CG  1 
ATOM   5445 O  OD1 . ASP C  1  24  ? -22.619 -8.928  7.663  1.00 77.54  ? 37  ASP C OD1 1 
ATOM   5446 O  OD2 . ASP C  1  24  ? -21.710 -7.400  6.345  1.00 85.16  ? 37  ASP C OD2 1 
ATOM   5447 N  N   . HIS C  1  25  ? -22.136 -4.668  10.981 1.00 47.47  ? 38  HIS C N   1 
ATOM   5448 C  CA  . HIS C  1  25  ? -21.455 -3.845  11.967 1.00 50.04  ? 38  HIS C CA  1 
ATOM   5449 C  C   . HIS C  1  25  ? -22.479 -3.030  12.756 1.00 48.67  ? 38  HIS C C   1 
ATOM   5450 O  O   . HIS C  1  25  ? -22.478 -1.793  12.720 1.00 45.70  ? 38  HIS C O   1 
ATOM   5451 C  CB  . HIS C  1  25  ? -20.384 -2.984  11.294 1.00 50.13  ? 38  HIS C CB  1 
ATOM   5452 C  CG  . HIS C  1  25  ? -19.310 -3.778  10.621 1.00 51.67  ? 38  HIS C CG  1 
ATOM   5453 N  ND1 . HIS C  1  25  ? -19.325 -4.055  9.272  1.00 52.12  ? 38  HIS C ND1 1 
ATOM   5454 C  CD2 . HIS C  1  25  ? -18.192 -4.351  11.102 1.00 53.86  ? 38  HIS C CD2 1 
ATOM   5455 C  CE1 . HIS C  1  25  ? -18.245 -4.767  8.962  1.00 54.72  ? 38  HIS C CE1 1 
ATOM   5456 N  NE2 . HIS C  1  25  ? -17.546 -4.967  10.062 1.00 50.58  ? 38  HIS C NE2 1 
ATOM   5457 N  N   . PRO C  1  26  ? -23.376 -3.701  13.517 1.00 48.86  ? 39  PRO C N   1 
ATOM   5458 C  CA  . PRO C  1  26  ? -24.363 -2.990  14.332 1.00 49.18  ? 39  PRO C CA  1 
ATOM   5459 C  C   . PRO C  1  26  ? -23.741 -2.382  15.585 1.00 49.11  ? 39  PRO C C   1 
ATOM   5460 O  O   . PRO C  1  26  ? -22.879 -2.996  16.218 1.00 47.58  ? 39  PRO C O   1 
ATOM   5461 C  CB  . PRO C  1  26  ? -25.347 -4.113  14.684 1.00 49.67  ? 39  PRO C CB  1 
ATOM   5462 C  CG  . PRO C  1  26  ? -24.458 -5.335  14.808 1.00 50.55  ? 39  PRO C CG  1 
ATOM   5463 C  CD  . PRO C  1  26  ? -23.457 -5.165  13.667 1.00 51.56  ? 39  PRO C CD  1 
ATOM   5464 N  N   . TRP C  1  27  ? -24.201 -1.181  15.947 1.00 46.79  ? 40  TRP C N   1 
ATOM   5465 C  CA  . TRP C  1  27  ? -23.897 -0.640  17.257 1.00 49.17  ? 40  TRP C CA  1 
ATOM   5466 C  C   . TRP C  1  27  ? -24.474 -1.568  18.315 1.00 52.19  ? 40  TRP C C   1 
ATOM   5467 O  O   . TRP C  1  27  ? -25.562 -2.107  18.129 1.00 51.82  ? 40  TRP C O   1 
ATOM   5468 C  CB  . TRP C  1  27  ? -24.466 0.771   17.420 1.00 48.18  ? 40  TRP C CB  1 
ATOM   5469 C  CG  . TRP C  1  27  ? -24.081 1.414   18.725 1.00 54.88  ? 40  TRP C CG  1 
ATOM   5470 C  CD1 . TRP C  1  27  ? -22.998 2.200   18.966 1.00 52.69  ? 40  TRP C CD1 1 
ATOM   5471 C  CD2 . TRP C  1  27  ? -24.806 1.348   19.969 1.00 56.86  ? 40  TRP C CD2 1 
ATOM   5472 N  NE1 . TRP C  1  27  ? -22.986 2.618   20.267 1.00 55.02  ? 40  TRP C NE1 1 
ATOM   5473 C  CE2 . TRP C  1  27  ? -24.083 2.122   20.906 1.00 55.83  ? 40  TRP C CE2 1 
ATOM   5474 C  CE3 . TRP C  1  27  ? -25.983 0.717   20.380 1.00 57.13  ? 40  TRP C CE3 1 
ATOM   5475 C  CZ2 . TRP C  1  27  ? -24.500 2.290   22.223 1.00 54.65  ? 40  TRP C CZ2 1 
ATOM   5476 C  CZ3 . TRP C  1  27  ? -26.395 0.881   21.687 1.00 55.13  ? 40  TRP C CZ3 1 
ATOM   5477 C  CH2 . TRP C  1  27  ? -25.666 1.657   22.591 1.00 53.86  ? 40  TRP C CH2 1 
ATOM   5478 N  N   . GLN C  1  28  ? -23.720 -1.758  19.403 1.00 52.31  ? 41  GLN C N   1 
ATOM   5479 C  CA  . GLN C  1  28  ? -24.184 -2.529  20.543 1.00 50.31  ? 41  GLN C CA  1 
ATOM   5480 C  C   . GLN C  1  28  ? -23.680 -1.880  21.822 1.00 53.13  ? 41  GLN C C   1 
ATOM   5481 O  O   . GLN C  1  28  ? -22.576 -1.336  21.855 1.00 53.44  ? 41  GLN C O   1 
ATOM   5482 C  CB  . GLN C  1  28  ? -23.712 -3.977  20.491 1.00 48.09  ? 41  GLN C CB  1 
ATOM   5483 C  CG  . GLN C  1  28  ? -24.323 -4.770  19.343 1.00 46.59  ? 41  GLN C CG  1 
ATOM   5484 C  CD  . GLN C  1  28  ? -23.775 -6.170  19.238 1.00 48.49  ? 41  GLN C CD  1 
ATOM   5485 O  OE1 . GLN C  1  28  ? -22.945 -6.603  20.046 1.00 55.62  ? 41  GLN C OE1 1 
ATOM   5486 N  NE2 . GLN C  1  28  ? -24.239 -6.892  18.228 1.00 49.96  ? 41  GLN C NE2 1 
ATOM   5487 N  N   . PRO C  1  29  ? -24.488 -1.918  22.906 1.00 56.90  ? 42  PRO C N   1 
ATOM   5488 C  CA  . PRO C  1  29  ? -24.112 -1.261  24.150 1.00 54.67  ? 42  PRO C CA  1 
ATOM   5489 C  C   . PRO C  1  29  ? -22.911 -1.941  24.789 1.00 49.21  ? 42  PRO C C   1 
ATOM   5490 O  O   . PRO C  1  29  ? -22.618 -3.109  24.498 1.00 45.41  ? 42  PRO C O   1 
ATOM   5491 C  CB  . PRO C  1  29  ? -25.383 -1.301  25.016 1.00 56.32  ? 42  PRO C CB  1 
ATOM   5492 C  CG  . PRO C  1  29  ? -26.203 -2.438  24.440 1.00 59.71  ? 42  PRO C CG  1 
ATOM   5493 C  CD  . PRO C  1  29  ? -25.801 -2.575  22.979 1.00 59.58  ? 42  PRO C CD  1 
ATOM   5494 N  N   . LEU C  1  30  ? -22.227 -1.179  25.651 1.00 45.71  ? 43  LEU C N   1 
ATOM   5495 C  CA  . LEU C  1  30  ? -21.079 -1.690  26.379 1.00 49.43  ? 43  LEU C CA  1 
ATOM   5496 C  C   . LEU C  1  30  ? -21.545 -2.781  27.334 1.00 48.47  ? 43  LEU C C   1 
ATOM   5497 O  O   . LEU C  1  30  ? -22.613 -2.667  27.938 1.00 50.74  ? 43  LEU C O   1 
ATOM   5498 C  CB  . LEU C  1  30  ? -20.386 -0.555  27.129 1.00 50.06  ? 43  LEU C CB  1 
ATOM   5499 C  CG  . LEU C  1  30  ? -19.892 0.614   26.271 1.00 53.60  ? 43  LEU C CG  1 
ATOM   5500 C  CD1 . LEU C  1  30  ? -19.301 1.729   27.107 1.00 53.86  ? 43  LEU C CD1 1 
ATOM   5501 C  CD2 . LEU C  1  30  ? -18.879 0.071   25.282 1.00 53.78  ? 43  LEU C CD2 1 
ATOM   5502 N  N   . ARG C  1  31  ? -20.746 -3.849  27.407 1.00 48.49  ? 44  ARG C N   1 
ATOM   5503 C  CA  . ARG C  1  31  ? -20.893 -4.869  28.426 1.00 50.08  ? 44  ARG C CA  1 
ATOM   5504 C  C   . ARG C  1  31  ? -19.842 -4.613  29.504 1.00 52.18  ? 44  ARG C C   1 
ATOM   5505 O  O   . ARG C  1  31  ? -18.857 -3.914  29.257 1.00 53.47  ? 44  ARG C O   1 
ATOM   5506 C  CB  . ARG C  1  31  ? -20.710 -6.271  27.841 1.00 51.94  ? 44  ARG C CB  1 
ATOM   5507 C  CG  . ARG C  1  31  ? -21.614 -6.653  26.676 1.00 56.98  ? 44  ARG C CG  1 
ATOM   5508 C  CD  . ARG C  1  31  ? -20.997 -7.791  25.875 1.00 62.90  ? 44  ARG C CD  1 
ATOM   5509 N  NE  . ARG C  1  31  ? -19.665 -7.405  25.382 1.00 75.38  ? 44  ARG C NE  1 
ATOM   5510 C  CZ  . ARG C  1  31  ? -18.777 -8.174  24.734 1.00 77.49  ? 44  ARG C CZ  1 
ATOM   5511 N  NH1 . ARG C  1  31  ? -19.070 -9.417  24.390 1.00 84.84  ? 44  ARG C NH1 1 
ATOM   5512 N  NH2 . ARG C  1  31  ? -17.579 -7.693  24.432 1.00 75.33  ? 44  ARG C NH2 1 
ATOM   5513 N  N   . GLU C  1  32  ? -20.062 -5.174  30.701 1.00 53.38  ? 45  GLU C N   1 
ATOM   5514 C  CA  . GLU C  1  32  ? -19.051 -5.207  31.751 1.00 56.13  ? 45  GLU C CA  1 
ATOM   5515 C  C   . GLU C  1  32  ? -17.722 -5.715  31.189 1.00 53.69  ? 45  GLU C C   1 
ATOM   5516 O  O   . GLU C  1  32  ? -17.680 -6.786  30.572 1.00 51.50  ? 45  GLU C O   1 
ATOM   5517 C  CB  . GLU C  1  32  ? -19.388 -6.194  32.878 1.00 57.09  ? 45  GLU C CB  1 
ATOM   5518 C  CG  . GLU C  1  32  ? -19.698 -5.579  34.237 1.00 61.81  ? 45  GLU C CG  1 
ATOM   5519 C  CD  . GLU C  1  32  ? -18.736 -4.565  34.821 1.00 58.34  ? 45  GLU C CD  1 
ATOM   5520 O  OE1 . GLU C  1  32  ? -17.518 -4.819  34.856 1.00 55.04  ? 45  GLU C OE1 1 
ATOM   5521 O  OE2 . GLU C  1  32  ? -19.239 -3.520  35.289 1.00 63.70  ? 45  GLU C OE2 1 
ATOM   5522 N  N   . GLY C  1  33  ? -16.644 -4.954  31.415 1.00 54.76  ? 46  GLY C N   1 
ATOM   5523 C  CA  . GLY C  1  33  ? -15.319 -5.391  31.003 1.00 57.27  ? 46  GLY C CA  1 
ATOM   5524 C  C   . GLY C  1  33  ? -14.890 -4.816  29.652 1.00 56.18  ? 46  GLY C C   1 
ATOM   5525 O  O   . GLY C  1  33  ? -13.694 -4.782  29.363 1.00 52.58  ? 46  GLY C O   1 
ATOM   5526 N  N   . ASP C  1  34  ? -15.851 -4.316  28.856 1.00 53.55  ? 47  ASP C N   1 
ATOM   5527 C  CA  . ASP C  1  34  ? -15.527 -3.618  27.617 1.00 53.02  ? 47  ASP C CA  1 
ATOM   5528 C  C   . ASP C  1  34  ? -14.788 -2.323  27.942 1.00 50.21  ? 47  ASP C C   1 
ATOM   5529 O  O   . ASP C  1  34  ? -15.177 -1.594  28.851 1.00 48.49  ? 47  ASP C O   1 
ATOM   5530 C  CB  . ASP C  1  34  ? -16.764 -3.337  26.778 1.00 49.15  ? 47  ASP C CB  1 
ATOM   5531 C  CG  . ASP C  1  34  ? -17.416 -4.553  26.142 1.00 50.19  ? 47  ASP C CG  1 
ATOM   5532 O  OD1 . ASP C  1  34  ? -16.769 -5.623  26.142 1.00 48.65  ? 47  ASP C OD1 1 
ATOM   5533 O  OD2 . ASP C  1  34  ? -18.566 -4.420  25.656 1.00 49.92  ? 47  ASP C OD2 1 
ATOM   5534 N  N   . ILE C  1  35  ? -13.721 -2.057  27.178 1.00 49.00  ? 48  ILE C N   1 
ATOM   5535 C  CA  . ILE C  1  35  ? -12.853 -0.912  27.398 1.00 43.94  ? 48  ILE C CA  1 
ATOM   5536 C  C   . ILE C  1  35  ? -13.097 0.123   26.304 1.00 44.99  ? 48  ILE C C   1 
ATOM   5537 O  O   . ILE C  1  35  ? -13.175 -0.212  25.124 1.00 44.03  ? 48  ILE C O   1 
ATOM   5538 C  CB  . ILE C  1  35  ? -11.378 -1.355  27.429 1.00 48.47  ? 48  ILE C CB  1 
ATOM   5539 C  CG1 . ILE C  1  35  ? -11.115 -2.387  28.539 1.00 50.75  ? 48  ILE C CG1 1 
ATOM   5540 C  CG2 . ILE C  1  35  ? -10.443 -0.147  27.543 1.00 47.32  ? 48  ILE C CG2 1 
ATOM   5541 C  CD1 . ILE C  1  35  ? -11.314 -1.851  29.946 1.00 54.45  ? 48  ILE C CD1 1 
ATOM   5542 N  N   . ARG C  1  36  ? -13.235 1.383   26.729 1.00 42.79  ? 49  ARG C N   1 
ATOM   5543 C  CA  . ARG C  1  36  ? -13.302 2.523   25.830 1.00 44.27  ? 49  ARG C CA  1 
ATOM   5544 C  C   . ARG C  1  36  ? -12.397 3.597   26.420 1.00 44.98  ? 49  ARG C C   1 
ATOM   5545 O  O   . ARG C  1  36  ? -12.072 3.538   27.602 1.00 45.04  ? 49  ARG C O   1 
ATOM   5546 C  CB  . ARG C  1  36  ? -14.750 3.006   25.687 1.00 45.68  ? 49  ARG C CB  1 
ATOM   5547 C  CG  . ARG C  1  36  ? -15.680 1.971   25.070 1.00 44.98  ? 49  ARG C CG  1 
ATOM   5548 C  CD  . ARG C  1  36  ? -15.409 1.775   23.587 1.00 45.35  ? 49  ARG C CD  1 
ATOM   5549 N  NE  . ARG C  1  36  ? -16.319 0.841   22.921 1.00 41.73  ? 49  ARG C NE  1 
ATOM   5550 C  CZ  . ARG C  1  36  ? -16.288 -0.480  23.022 1.00 44.37  ? 49  ARG C CZ  1 
ATOM   5551 N  NH1 . ARG C  1  36  ? -15.330 -1.097  23.691 1.00 46.11  ? 49  ARG C NH1 1 
ATOM   5552 N  NH2 . ARG C  1  36  ? -17.224 -1.199  22.432 1.00 46.24  ? 49  ARG C NH2 1 
ATOM   5553 N  N   . GLY C  1  37  ? -11.988 4.567   25.599 1.00 45.22  ? 50  GLY C N   1 
ATOM   5554 C  CA  . GLY C  1  37  ? -10.990 5.527   26.030 1.00 44.45  ? 50  GLY C CA  1 
ATOM   5555 C  C   . GLY C  1  37  ? -11.179 6.894   25.389 1.00 43.65  ? 50  GLY C C   1 
ATOM   5556 O  O   . GLY C  1  37  ? -12.298 7.296   25.086 1.00 44.61  ? 50  GLY C O   1 
ATOM   5557 N  N   . PRO C  1  38  ? -10.077 7.641   25.165 1.00 40.37  ? 51  PRO C N   1 
ATOM   5558 C  CA  . PRO C  1  38  ? -10.161 9.042   24.754 1.00 39.35  ? 51  PRO C CA  1 
ATOM   5559 C  C   . PRO C  1  38  ? -10.365 9.281   23.263 1.00 41.02  ? 51  PRO C C   1 
ATOM   5560 O  O   . PRO C  1  38  ? -10.474 10.433  22.844 1.00 42.74  ? 51  PRO C O   1 
ATOM   5561 C  CB  . PRO C  1  38  ? -8.787  9.541   25.208 1.00 40.04  ? 51  PRO C CB  1 
ATOM   5562 C  CG  . PRO C  1  38  ? -7.874  8.386   24.889 1.00 41.63  ? 51  PRO C CG  1 
ATOM   5563 C  CD  . PRO C  1  38  ? -8.692  7.165   25.290 1.00 43.77  ? 51  PRO C CD  1 
ATOM   5564 N  N   . CYS C  1  39  ? -10.361 8.202   22.469 1.00 42.42  ? 52  CYS C N   1 
ATOM   5565 C  CA  . CYS C  1  39  ? -10.474 8.329   21.024 1.00 44.32  ? 52  CYS C CA  1 
ATOM   5566 C  C   . CYS C  1  39  ? -11.881 7.976   20.551 1.00 41.33  ? 52  CYS C C   1 
ATOM   5567 O  O   . CYS C  1  39  ? -12.278 6.807   20.574 1.00 40.61  ? 52  CYS C O   1 
ATOM   5568 C  CB  . CYS C  1  39  ? -9.517  7.422   20.263 1.00 43.58  ? 52  CYS C CB  1 
ATOM   5569 S  SG  . CYS C  1  39  ? -9.673  7.660   18.476 1.00 49.58  ? 52  CYS C SG  1 
ATOM   5570 N  N   . PRO C  1  40  ? -12.652 8.962   20.046 1.00 43.23  ? 53  PRO C N   1 
ATOM   5571 C  CA  . PRO C  1  40  ? -13.999 8.699   19.540 1.00 43.26  ? 53  PRO C CA  1 
ATOM   5572 C  C   . PRO C  1  40  ? -13.975 7.812   18.296 1.00 45.95  ? 53  PRO C C   1 
ATOM   5573 O  O   . PRO C  1  40  ? -14.932 7.080   18.052 1.00 39.65  ? 53  PRO C O   1 
ATOM   5574 C  CB  . PRO C  1  40  ? -14.558 10.097  19.263 1.00 42.39  ? 53  PRO C CB  1 
ATOM   5575 C  CG  . PRO C  1  40  ? -13.342 10.964  19.042 1.00 41.42  ? 53  PRO C CG  1 
ATOM   5576 C  CD  . PRO C  1  40  ? -12.261 10.372  19.913 1.00 43.30  ? 53  PRO C CD  1 
ATOM   5577 N  N   . GLY C  1  41  ? -12.872 7.858   17.527 1.00 40.83  ? 54  GLY C N   1 
ATOM   5578 C  CA  . GLY C  1  41  ? -12.760 7.037   16.333 1.00 38.87  ? 54  GLY C CA  1 
ATOM   5579 C  C   . GLY C  1  41  ? -12.701 5.559   16.696 1.00 38.55  ? 54  GLY C C   1 
ATOM   5580 O  O   . GLY C  1  41  ? -13.516 4.760   16.245 1.00 37.48  ? 54  GLY C O   1 
ATOM   5581 N  N   . LEU C  1  42  ? -11.723 5.206   17.532 1.00 40.97  ? 55  LEU C N   1 
ATOM   5582 C  CA  . LEU C  1  42  ? -11.540 3.832   17.965 1.00 41.34  ? 55  LEU C CA  1 
ATOM   5583 C  C   . LEU C  1  42  ? -12.746 3.367   18.781 1.00 40.45  ? 55  LEU C C   1 
ATOM   5584 O  O   . LEU C  1  42  ? -13.196 2.237   18.624 1.00 37.22  ? 55  LEU C O   1 
ATOM   5585 C  CB  . LEU C  1  42  ? -10.241 3.721   18.752 1.00 42.42  ? 55  LEU C CB  1 
ATOM   5586 C  CG  . LEU C  1  42  ? -8.967  4.060   17.967 1.00 45.88  ? 55  LEU C CG  1 
ATOM   5587 C  CD1 . LEU C  1  42  ? -7.759  3.990   18.880 1.00 47.30  ? 55  LEU C CD1 1 
ATOM   5588 C  CD2 . LEU C  1  42  ? -8.797  3.139   16.767 1.00 42.66  ? 55  LEU C CD2 1 
ATOM   5589 N  N   . ASN C  1  43  ? -13.273 4.245   19.637 1.00 39.34  ? 56  ASN C N   1 
ATOM   5590 C  CA  . ASN C  1  43  ? -14.439 3.913   20.438 1.00 42.98  ? 56  ASN C CA  1 
ATOM   5591 C  C   . ASN C  1  43  ? -15.598 3.467   19.545 1.00 42.55  ? 56  ASN C C   1 
ATOM   5592 O  O   . ASN C  1  43  ? -16.219 2.440   19.820 1.00 41.09  ? 56  ASN C O   1 
ATOM   5593 C  CB  . ASN C  1  43  ? -14.887 5.072   21.321 1.00 44.95  ? 56  ASN C CB  1 
ATOM   5594 C  CG  . ASN C  1  43  ? -13.959 5.354   22.481 1.00 47.51  ? 56  ASN C CG  1 
ATOM   5595 O  OD1 . ASN C  1  43  ? -13.089 4.539   22.840 1.00 40.47  ? 56  ASN C OD1 1 
ATOM   5596 N  ND2 . ASN C  1  43  ? -14.143 6.522   23.080 1.00 48.29  ? 56  ASN C ND2 1 
ATOM   5597 N  N   . THR C  1  44  ? -15.871 4.237   18.479 1.00 43.40  ? 57  THR C N   1 
ATOM   5598 C  CA  . THR C  1  44  ? -16.988 3.955   17.580 1.00 44.75  ? 57  THR C CA  1 
ATOM   5599 C  C   . THR C  1  44  ? -16.741 2.658   16.809 1.00 44.57  ? 57  THR C C   1 
ATOM   5600 O  O   . THR C  1  44  ? -17.660 1.868   16.588 1.00 42.38  ? 57  THR C O   1 
ATOM   5601 C  CB  . THR C  1  44  ? -17.211 5.139   16.637 1.00 47.12  ? 57  THR C CB  1 
ATOM   5602 O  OG1 . THR C  1  44  ? -17.482 6.279   17.453 1.00 41.15  ? 57  THR C OG1 1 
ATOM   5603 C  CG2 . THR C  1  44  ? -18.355 4.911   15.658 1.00 48.96  ? 57  THR C CG2 1 
ATOM   5604 N  N   . LEU C  1  45  ? -15.492 2.441   16.389 1.00 41.91  ? 58  LEU C N   1 
ATOM   5605 C  CA  . LEU C  1  45  ? -15.138 1.231   15.670 1.00 41.11  ? 58  LEU C CA  1 
ATOM   5606 C  C   . LEU C  1  45  ? -15.381 0.003   16.547 1.00 41.12  ? 58  LEU C C   1 
ATOM   5607 O  O   . LEU C  1  45  ? -15.895 -1.015  16.079 1.00 43.25  ? 58  LEU C O   1 
ATOM   5608 C  CB  . LEU C  1  45  ? -13.687 1.333   15.188 1.00 42.88  ? 58  LEU C CB  1 
ATOM   5609 C  CG  . LEU C  1  45  ? -13.448 2.378   14.091 1.00 43.81  ? 58  LEU C CG  1 
ATOM   5610 C  CD1 . LEU C  1  45  ? -11.984 2.640   13.850 1.00 43.88  ? 58  LEU C CD1 1 
ATOM   5611 C  CD2 . LEU C  1  45  ? -14.118 1.946   12.798 1.00 43.06  ? 58  LEU C CD2 1 
ATOM   5612 N  N   . ALA C  1  46  ? -15.018 0.099   17.830 1.00 40.84  ? 59  ALA C N   1 
ATOM   5613 C  CA  . ALA C  1  46  ? -15.216 -1.015  18.746 1.00 40.84  ? 59  ALA C CA  1 
ATOM   5614 C  C   . ALA C  1  46  ? -16.708 -1.252  18.979 1.00 40.24  ? 59  ALA C C   1 
ATOM   5615 O  O   . ALA C  1  46  ? -17.169 -2.390  18.968 1.00 43.97  ? 59  ALA C O   1 
ATOM   5616 C  CB  . ALA C  1  46  ? -14.482 -0.769  20.035 1.00 40.80  ? 59  ALA C CB  1 
ATOM   5617 N  N   . SER C  1  47  ? -17.475 -0.176  19.157 1.00 41.73  ? 60  SER C N   1 
ATOM   5618 C  CA  . SER C  1  47  ? -18.895 -0.319  19.455 1.00 48.16  ? 60  SER C CA  1 
ATOM   5619 C  C   . SER C  1  47  ? -19.717 -0.764  18.239 1.00 47.83  ? 60  SER C C   1 
ATOM   5620 O  O   . SER C  1  47  ? -20.889 -1.092  18.401 1.00 52.51  ? 60  SER C O   1 
ATOM   5621 C  CB  . SER C  1  47  ? -19.437 0.941   20.067 1.00 46.11  ? 60  SER C CB  1 
ATOM   5622 O  OG  . SER C  1  47  ? -19.039 1.038   21.428 1.00 47.52  ? 60  SER C OG  1 
ATOM   5623 N  N   . HIS C  1  48  ? -19.119 -0.776  17.035 1.00 48.39  ? 61  HIS C N   1 
ATOM   5624 C  CA  . HIS C  1  48  ? -19.771 -1.292  15.836 1.00 44.49  ? 61  HIS C CA  1 
ATOM   5625 C  C   . HIS C  1  48  ? -19.154 -2.618  15.385 1.00 43.24  ? 61  HIS C C   1 
ATOM   5626 O  O   . HIS C  1  48  ? -19.576 -3.179  14.380 1.00 44.73  ? 61  HIS C O   1 
ATOM   5627 C  CB  . HIS C  1  48  ? -19.726 -0.269  14.695 1.00 43.53  ? 61  HIS C CB  1 
ATOM   5628 C  CG  . HIS C  1  48  ? -20.780 0.776   14.776 1.00 42.03  ? 61  HIS C CG  1 
ATOM   5629 N  ND1 . HIS C  1  48  ? -21.992 0.633   14.132 1.00 40.98  ? 61  HIS C ND1 1 
ATOM   5630 C  CD2 . HIS C  1  48  ? -20.824 1.960   15.403 1.00 42.56  ? 61  HIS C CD2 1 
ATOM   5631 C  CE1 . HIS C  1  48  ? -22.739 1.703   14.382 1.00 40.65  ? 61  HIS C CE1 1 
ATOM   5632 N  NE2 . HIS C  1  48  ? -22.056 2.522   15.152 1.00 38.91  ? 61  HIS C NE2 1 
ATOM   5633 N  N   . GLY C  1  49  ? -18.129 -3.096  16.093 1.00 41.78  ? 62  GLY C N   1 
ATOM   5634 C  CA  . GLY C  1  49  ? -17.556 -4.403  15.812 1.00 42.95  ? 62  GLY C CA  1 
ATOM   5635 C  C   . GLY C  1  49  ? -16.515 -4.378  14.692 1.00 40.43  ? 62  GLY C C   1 
ATOM   5636 O  O   . GLY C  1  49  ? -16.110 -5.437  14.228 1.00 44.37  ? 62  GLY C O   1 
ATOM   5637 N  N   . TYR C  1  50  ? -16.063 -3.194  14.266 1.00 40.69  ? 63  TYR C N   1 
ATOM   5638 C  CA  . TYR C  1  50  ? -14.911 -3.096  13.377 1.00 43.70  ? 63  TYR C CA  1 
ATOM   5639 C  C   . TYR C  1  50  ? -13.651 -3.526  14.135 1.00 46.17  ? 63  TYR C C   1 
ATOM   5640 O  O   . TYR C  1  50  ? -12.753 -4.118  13.545 1.00 47.89  ? 63  TYR C O   1 
ATOM   5641 C  CB  . TYR C  1  50  ? -14.770 -1.692  12.774 1.00 43.52  ? 63  TYR C CB  1 
ATOM   5642 C  CG  . TYR C  1  50  ? -15.725 -1.437  11.618 1.00 45.48  ? 63  TYR C CG  1 
ATOM   5643 C  CD1 . TYR C  1  50  ? -15.403 -1.848  10.332 1.00 48.60  ? 63  TYR C CD1 1 
ATOM   5644 C  CD2 . TYR C  1  50  ? -16.956 -0.816  11.807 1.00 46.15  ? 63  TYR C CD2 1 
ATOM   5645 C  CE1 . TYR C  1  50  ? -16.269 -1.647  9.265  1.00 46.33  ? 63  TYR C CE1 1 
ATOM   5646 C  CE2 . TYR C  1  50  ? -17.839 -0.621  10.753 1.00 46.08  ? 63  TYR C CE2 1 
ATOM   5647 C  CZ  . TYR C  1  50  ? -17.493 -1.033  9.477  1.00 48.36  ? 63  TYR C CZ  1 
ATOM   5648 O  OH  . TYR C  1  50  ? -18.365 -0.857  8.444  1.00 47.16  ? 63  TYR C OH  1 
ATOM   5649 N  N   . LEU C  1  51  ? -13.585 -3.182  15.429 1.00 48.76  ? 64  LEU C N   1 
ATOM   5650 C  CA  . LEU C  1  51  ? -12.603 -3.708  16.366 1.00 50.11  ? 64  LEU C CA  1 
ATOM   5651 C  C   . LEU C  1  51  ? -13.287 -4.719  17.278 1.00 47.62  ? 64  LEU C C   1 
ATOM   5652 O  O   . LEU C  1  51  ? -14.507 -4.711  17.388 1.00 48.60  ? 64  LEU C O   1 
ATOM   5653 C  CB  . LEU C  1  51  ? -12.013 -2.585  17.218 1.00 48.96  ? 64  LEU C CB  1 
ATOM   5654 C  CG  . LEU C  1  51  ? -11.094 -1.593  16.505 1.00 47.84  ? 64  LEU C CG  1 
ATOM   5655 C  CD1 . LEU C  1  51  ? -10.771 -0.418  17.396 1.00 48.36  ? 64  LEU C CD1 1 
ATOM   5656 C  CD2 . LEU C  1  51  ? -9.827  -2.291  16.084 1.00 46.24  ? 64  LEU C CD2 1 
ATOM   5657 N  N   . PRO C  1  52  ? -12.529 -5.585  17.987 1.00 48.49  ? 65  PRO C N   1 
ATOM   5658 C  CA  . PRO C  1  52  ? -13.102 -6.369  19.083 1.00 48.42  ? 65  PRO C CA  1 
ATOM   5659 C  C   . PRO C  1  52  ? -13.893 -5.451  20.013 1.00 49.40  ? 65  PRO C C   1 
ATOM   5660 O  O   . PRO C  1  52  ? -13.422 -4.375  20.381 1.00 50.51  ? 65  PRO C O   1 
ATOM   5661 C  CB  . PRO C  1  52  ? -11.875 -6.991  19.766 1.00 47.96  ? 65  PRO C CB  1 
ATOM   5662 C  CG  . PRO C  1  52  ? -10.850 -7.082  18.649 1.00 47.03  ? 65  PRO C CG  1 
ATOM   5663 C  CD  . PRO C  1  52  ? -11.088 -5.840  17.796 1.00 45.51  ? 65  PRO C CD  1 
ATOM   5664 N  N   . ARG C  1  53  ? -15.104 -5.882  20.375 1.00 48.20  ? 66  ARG C N   1 
ATOM   5665 C  CA  . ARG C  1  53  ? -16.023 -5.035  21.126 1.00 50.18  ? 66  ARG C CA  1 
ATOM   5666 C  C   . ARG C  1  53  ? -15.533 -4.770  22.552 1.00 48.13  ? 66  ARG C C   1 
ATOM   5667 O  O   . ARG C  1  53  ? -16.022 -3.847  23.205 1.00 51.77  ? 66  ARG C O   1 
ATOM   5668 C  CB  . ARG C  1  53  ? -17.423 -5.653  21.160 1.00 51.09  ? 66  ARG C CB  1 
ATOM   5669 C  CG  . ARG C  1  53  ? -18.028 -5.734  19.769 1.00 51.67  ? 66  ARG C CG  1 
ATOM   5670 C  CD  . ARG C  1  53  ? -19.488 -6.096  19.800 1.00 53.38  ? 66  ARG C CD  1 
ATOM   5671 N  NE  . ARG C  1  53  ? -20.002 -6.113  18.425 1.00 49.55  ? 66  ARG C NE  1 
ATOM   5672 C  CZ  . ARG C  1  53  ? -20.623 -5.108  17.820 1.00 43.29  ? 66  ARG C CZ  1 
ATOM   5673 N  NH1 . ARG C  1  53  ? -20.803 -3.949  18.434 1.00 43.87  ? 66  ARG C NH1 1 
ATOM   5674 N  NH2 . ARG C  1  53  ? -21.060 -5.267  16.588 1.00 43.75  ? 66  ARG C NH2 1 
ATOM   5675 N  N   . ASP C  1  54  ? -14.549 -5.539  23.024 1.00 48.31  ? 67  ASP C N   1 
ATOM   5676 C  CA  . ASP C  1  54  ? -14.015 -5.325  24.358 1.00 49.12  ? 67  ASP C CA  1 
ATOM   5677 C  C   . ASP C  1  54  ? -12.940 -4.234  24.358 1.00 45.51  ? 67  ASP C C   1 
ATOM   5678 O  O   . ASP C  1  54  ? -12.419 -3.906  25.420 1.00 45.62  ? 67  ASP C O   1 
ATOM   5679 C  CB  . ASP C  1  54  ? -13.530 -6.630  24.971 1.00 52.16  ? 67  ASP C CB  1 
ATOM   5680 C  CG  . ASP C  1  54  ? -12.333 -7.282  24.289 1.00 56.59  ? 67  ASP C CG  1 
ATOM   5681 O  OD1 . ASP C  1  54  ? -11.862 -6.737  23.243 1.00 58.27  ? 67  ASP C OD1 1 
ATOM   5682 O  OD2 . ASP C  1  54  ? -11.865 -8.310  24.836 1.00 55.28  ? 67  ASP C OD2 1 
ATOM   5683 N  N   . GLY C  1  55  ? -12.613 -3.669  23.190 1.00 42.50  ? 68  GLY C N   1 
ATOM   5684 C  CA  . GLY C  1  55  ? -11.729 -2.510  23.120 1.00 44.03  ? 68  GLY C CA  1 
ATOM   5685 C  C   . GLY C  1  55  ? -10.252 -2.855  23.340 1.00 42.91  ? 68  GLY C C   1 
ATOM   5686 O  O   . GLY C  1  55  ? -9.446  -1.991  23.679 1.00 46.58  ? 68  GLY C O   1 
ATOM   5687 N  N   . VAL C  1  56  ? -9.899  -4.126  23.124 1.00 43.45  ? 69  VAL C N   1 
ATOM   5688 C  CA  . VAL C  1  56  ? -8.513  -4.560  23.113 1.00 48.08  ? 69  VAL C CA  1 
ATOM   5689 C  C   . VAL C  1  56  ? -8.247  -5.209  21.758 1.00 46.64  ? 69  VAL C C   1 
ATOM   5690 O  O   . VAL C  1  56  ? -9.034  -6.045  21.307 1.00 40.27  ? 69  VAL C O   1 
ATOM   5691 C  CB  . VAL C  1  56  ? -8.212  -5.525  24.275 1.00 51.28  ? 69  VAL C CB  1 
ATOM   5692 C  CG1 . VAL C  1  56  ? -6.802  -6.108  24.199 1.00 52.26  ? 69  VAL C CG1 1 
ATOM   5693 C  CG2 . VAL C  1  56  ? -8.432  -4.849  25.627 1.00 54.24  ? 69  VAL C CG2 1 
ATOM   5694 N  N   . ALA C  1  57  ? -7.134  -4.823  21.121 1.00 44.95  ? 70  ALA C N   1 
ATOM   5695 C  CA  . ALA C  1  57  ? -6.900  -5.162  19.729 1.00 43.27  ? 70  ALA C CA  1 
ATOM   5696 C  C   . ALA C  1  57  ? -5.405  -5.173  19.419 1.00 42.15  ? 70  ALA C C   1 
ATOM   5697 O  O   . ALA C  1  57  ? -4.608  -4.561  20.124 1.00 44.64  ? 70  ALA C O   1 
ATOM   5698 C  CB  . ALA C  1  57  ? -7.620  -4.169  18.847 1.00 42.28  ? 70  ALA C CB  1 
ATOM   5699 N  N   . THR C  1  58  ? -5.047  -5.859  18.330 1.00 40.03  ? 71  THR C N   1 
ATOM   5700 C  CA  . THR C  1  58  ? -3.696  -5.817  17.799 1.00 42.05  ? 71  THR C CA  1 
ATOM   5701 C  C   . THR C  1  58  ? -3.543  -4.527  16.997 1.00 42.90  ? 71  THR C C   1 
ATOM   5702 O  O   . THR C  1  58  ? -4.529  -3.928  16.557 1.00 35.86  ? 71  THR C O   1 
ATOM   5703 C  CB  . THR C  1  58  ? -3.396  -7.036  16.927 1.00 41.91  ? 71  THR C CB  1 
ATOM   5704 O  OG1 . THR C  1  58  ? -4.172  -6.878  15.741 1.00 44.38  ? 71  THR C OG1 1 
ATOM   5705 C  CG2 . THR C  1  58  ? -3.719  -8.353  17.615 1.00 42.55  ? 71  THR C CG2 1 
ATOM   5706 N  N   . PRO C  1  59  ? -2.295  -4.048  16.812 1.00 38.29  ? 72  PRO C N   1 
ATOM   5707 C  CA  . PRO C  1  59  ? -2.036  -2.939  15.894 1.00 39.13  ? 72  PRO C CA  1 
ATOM   5708 C  C   . PRO C  1  59  ? -2.624  -3.169  14.505 1.00 35.63  ? 72  PRO C C   1 
ATOM   5709 O  O   . PRO C  1  59  ? -3.214  -2.256  13.937 1.00 33.92  ? 72  PRO C O   1 
ATOM   5710 C  CB  . PRO C  1  59  ? -0.501  -2.879  15.871 1.00 38.68  ? 72  PRO C CB  1 
ATOM   5711 C  CG  . PRO C  1  59  ? -0.094  -3.433  17.215 1.00 40.31  ? 72  PRO C CG  1 
ATOM   5712 C  CD  . PRO C  1  59  ? -1.082  -4.539  17.496 1.00 40.86  ? 72  PRO C CD  1 
ATOM   5713 N  N   . ALA C  1  60  ? -2.458  -4.393  13.985 1.00 35.58  ? 73  ALA C N   1 
ATOM   5714 C  CA  . ALA C  1  60  ? -2.958  -4.758  12.670 1.00 38.64  ? 73  ALA C CA  1 
ATOM   5715 C  C   . ALA C  1  60  ? -4.468  -4.562  12.609 1.00 39.35  ? 73  ALA C C   1 
ATOM   5716 O  O   . ALA C  1  60  ? -4.966  -4.001  11.638 1.00 38.62  ? 73  ALA C O   1 
ATOM   5717 C  CB  . ALA C  1  60  ? -2.598  -6.191  12.326 1.00 39.85  ? 73  ALA C CB  1 
ATOM   5718 N  N   . GLN C  1  61  ? -5.185  -5.019  13.641 1.00 36.48  ? 74  GLN C N   1 
ATOM   5719 C  CA  . GLN C  1  61  ? -6.635  -4.868  13.681 1.00 40.42  ? 74  GLN C CA  1 
ATOM   5720 C  C   . GLN C  1  61  ? -7.041  -3.397  13.687 1.00 39.01  ? 74  GLN C C   1 
ATOM   5721 O  O   . GLN C  1  61  ? -8.020  -3.032  13.050 1.00 42.87  ? 74  GLN C O   1 
ATOM   5722 C  CB  . GLN C  1  61  ? -7.262  -5.546  14.894 1.00 37.97  ? 74  GLN C CB  1 
ATOM   5723 C  CG  . GLN C  1  61  ? -7.279  -7.063  14.784 1.00 41.85  ? 74  GLN C CG  1 
ATOM   5724 C  CD  . GLN C  1  61  ? -7.657  -7.734  16.087 1.00 46.29  ? 74  GLN C CD  1 
ATOM   5725 O  OE1 . GLN C  1  61  ? -7.297  -7.282  17.181 1.00 47.74  ? 74  GLN C OE1 1 
ATOM   5726 N  NE2 . GLN C  1  61  ? -8.391  -8.827  15.980 1.00 48.05  ? 74  GLN C NE2 1 
ATOM   5727 N  N   . ILE C  1  62  ? -6.296  -2.568  14.422 1.00 36.55  ? 75  ILE C N   1 
ATOM   5728 C  CA  . ILE C  1  62  ? -6.628  -1.156  14.560 1.00 37.35  ? 75  ILE C CA  1 
ATOM   5729 C  C   . ILE C  1  62  ? -6.473  -0.464  13.203 1.00 38.91  ? 75  ILE C C   1 
ATOM   5730 O  O   . ILE C  1  62  ? -7.330  0.311   12.785 1.00 40.93  ? 75  ILE C O   1 
ATOM   5731 C  CB  . ILE C  1  62  ? -5.783  -0.515  15.679 1.00 33.63  ? 75  ILE C CB  1 
ATOM   5732 C  CG1 . ILE C  1  62  ? -6.218  -1.044  17.047 1.00 35.47  ? 75  ILE C CG1 1 
ATOM   5733 C  CG2 . ILE C  1  62  ? -5.838  1.010   15.622 1.00 32.10  ? 75  ILE C CG2 1 
ATOM   5734 C  CD1 . ILE C  1  62  ? -5.263  -0.727  18.188 1.00 35.69  ? 75  ILE C CD1 1 
ATOM   5735 N  N   . ILE C  1  63  ? -5.380  -0.766  12.499 1.00 40.73  ? 76  ILE C N   1 
ATOM   5736 C  CA  . ILE C  1  63  ? -5.130  -0.144  11.207 1.00 38.62  ? 76  ILE C CA  1 
ATOM   5737 C  C   . ILE C  1  63  ? -6.244  -0.507  10.227 1.00 37.66  ? 76  ILE C C   1 
ATOM   5738 O  O   . ILE C  1  63  ? -6.798  0.383   9.583  1.00 34.49  ? 76  ILE C O   1 
ATOM   5739 C  CB  . ILE C  1  63  ? -3.744  -0.533  10.679 1.00 38.46  ? 76  ILE C CB  1 
ATOM   5740 C  CG1 . ILE C  1  63  ? -2.651  0.138   11.498 1.00 39.43  ? 76  ILE C CG1 1 
ATOM   5741 C  CG2 . ILE C  1  63  ? -3.623  -0.202  9.193  1.00 40.41  ? 76  ILE C CG2 1 
ATOM   5742 C  CD1 . ILE C  1  63  ? -1.340  -0.600  11.435 1.00 40.90  ? 76  ILE C CD1 1 
ATOM   5743 N  N   . THR C  1  64  ? -6.575  -1.798  10.127 1.00 38.60  ? 77  THR C N   1 
ATOM   5744 C  CA  A THR C  1  64  ? -7.588  -2.240  9.181  0.50 41.15  ? 77  THR C CA  1 
ATOM   5745 C  CA  B THR C  1  64  ? -7.590  -2.248  9.184  0.50 42.98  ? 77  THR C CA  1 
ATOM   5746 C  C   . THR C  1  64  ? -8.936  -1.621  9.557  1.00 40.69  ? 77  THR C C   1 
ATOM   5747 O  O   . THR C  1  64  ? -9.669  -1.157  8.682  1.00 44.75  ? 77  THR C O   1 
ATOM   5748 C  CB  A THR C  1  64  ? -7.660  -3.767  9.125  0.50 40.92  ? 77  THR C CB  1 
ATOM   5749 C  CB  B THR C  1  64  ? -7.637  -3.778  9.103  0.50 46.69  ? 77  THR C CB  1 
ATOM   5750 O  OG1 A THR C  1  64  ? -8.039  -4.117  10.451 0.50 53.50  ? 77  THR C OG1 1 
ATOM   5751 O  OG1 B THR C  1  64  ? -8.886  -4.160  8.531  0.50 46.96  ? 77  THR C OG1 1 
ATOM   5752 C  CG2 A THR C  1  64  ? -6.342  -4.430  8.790  0.50 35.59  ? 77  THR C CG2 1 
ATOM   5753 C  CG2 B THR C  1  64  ? -7.602  -4.464  10.453 0.50 53.13  ? 77  THR C CG2 1 
ATOM   5754 N  N   . ALA C  1  65  ? -9.238  -1.550  10.864 1.00 42.90  ? 78  ALA C N   1 
ATOM   5755 C  CA  . ALA C  1  65  ? -10.507 -1.003  11.327 1.00 41.61  ? 78  ALA C CA  1 
ATOM   5756 C  C   . ALA C  1  65  ? -10.645 0.479   10.977 1.00 38.77  ? 78  ALA C C   1 
ATOM   5757 O  O   . ALA C  1  65  ? -11.724 0.897   10.569 1.00 35.77  ? 78  ALA C O   1 
ATOM   5758 C  CB  . ALA C  1  65  ? -10.672 -1.226  12.813 1.00 43.90  ? 78  ALA C CB  1 
ATOM   5759 N  N   . THR C  1  66  ? -9.581  1.273   11.146 1.00 36.08  ? 79  THR C N   1 
ATOM   5760 C  CA  . THR C  1  66  ? -9.646  2.703   10.846 1.00 37.21  ? 79  THR C CA  1 
ATOM   5761 C  C   . THR C  1  66  ? -9.818  2.925   9.340  1.00 38.11  ? 79  THR C C   1 
ATOM   5762 O  O   . THR C  1  66  ? -10.527 3.841   8.917  1.00 38.20  ? 79  THR C O   1 
ATOM   5763 C  CB  . THR C  1  66  ? -8.430  3.448   11.402 1.00 37.99  ? 79  THR C CB  1 
ATOM   5764 O  OG1 . THR C  1  66  ? -7.218  2.880   10.912 1.00 33.38  ? 79  THR C OG1 1 
ATOM   5765 C  CG2 . THR C  1  66  ? -8.383  3.404   12.918 1.00 41.10  ? 79  THR C CG2 1 
ATOM   5766 N  N   . GLN C  1  67  ? -9.203  2.053   8.533  1.00 37.64  ? 80  GLN C N   1 
ATOM   5767 C  CA  . GLN C  1  67  ? -9.352  2.095   7.085  1.00 37.31  ? 80  GLN C CA  1 
ATOM   5768 C  C   . GLN C  1  67  ? -10.766 1.682   6.671  1.00 38.52  ? 80  GLN C C   1 
ATOM   5769 O  O   . GLN C  1  67  ? -11.430 2.421   5.952  1.00 41.27  ? 80  GLN C O   1 
ATOM   5770 C  CB  . GLN C  1  67  ? -8.244  1.249   6.466  1.00 36.73  ? 80  GLN C CB  1 
ATOM   5771 C  CG  . GLN C  1  67  ? -6.864  1.848   6.719  1.00 37.66  ? 80  GLN C CG  1 
ATOM   5772 C  CD  . GLN C  1  67  ? -5.699  1.089   6.129  1.00 38.95  ? 80  GLN C CD  1 
ATOM   5773 O  OE1 . GLN C  1  67  ? -4.591  1.626   6.058  1.00 40.78  ? 80  GLN C OE1 1 
ATOM   5774 N  NE2 . GLN C  1  67  ? -5.908  -0.152  5.709  1.00 39.28  ? 80  GLN C NE2 1 
ATOM   5775 N  N   . GLU C  1  68  ? -11.220 0.505   7.122  1.00 39.73  ? 81  GLU C N   1 
ATOM   5776 C  CA  . GLU C  1  68  ? -12.513 -0.015  6.706  1.00 43.71  ? 81  GLU C CA  1 
ATOM   5777 C  C   . GLU C  1  68  ? -13.634 0.917   7.159  1.00 40.67  ? 81  GLU C C   1 
ATOM   5778 O  O   . GLU C  1  68  ? -14.539 1.222   6.387  1.00 43.50  ? 81  GLU C O   1 
ATOM   5779 C  CB  . GLU C  1  68  ? -12.795 -1.398  7.289  1.00 48.82  ? 81  GLU C CB  1 
ATOM   5780 C  CG  . GLU C  1  68  ? -11.947 -2.525  6.717  1.00 56.20  ? 81  GLU C CG  1 
ATOM   5781 C  CD  . GLU C  1  68  ? -11.957 -2.607  5.204  1.00 63.54  ? 81  GLU C CD  1 
ATOM   5782 O  OE1 . GLU C  1  68  ? -10.835 -2.791  4.675  1.00 58.07  ? 81  GLU C OE1 1 
ATOM   5783 O  OE2 . GLU C  1  68  ? -13.041 -2.458  4.577  1.00 59.26  ? 81  GLU C OE2 1 
ATOM   5784 N  N   . GLY C  1  69  ? -13.558 1.381   8.414  1.00 42.62  ? 82  GLY C N   1 
ATOM   5785 C  CA  . GLY C  1  69  ? -14.631 2.145   9.025  1.00 39.88  ? 82  GLY C CA  1 
ATOM   5786 C  C   . GLY C  1  69  ? -14.671 3.611   8.599  1.00 40.53  ? 82  GLY C C   1 
ATOM   5787 O  O   . GLY C  1  69  ? -15.755 4.179   8.444  1.00 37.96  ? 82  GLY C O   1 
ATOM   5788 N  N   . PHE C  1  70  ? -13.498 4.241   8.442  1.00 35.95  ? 83  PHE C N   1 
ATOM   5789 C  CA  . PHE C  1  70  ? -13.461 5.685   8.244  1.00 39.36  ? 83  PHE C CA  1 
ATOM   5790 C  C   . PHE C  1  70  ? -12.634 6.128   7.037  1.00 38.85  ? 83  PHE C C   1 
ATOM   5791 O  O   . PHE C  1  70  ? -12.602 7.326   6.740  1.00 37.49  ? 83  PHE C O   1 
ATOM   5792 C  CB  . PHE C  1  70  ? -12.875 6.361   9.484  1.00 40.91  ? 83  PHE C CB  1 
ATOM   5793 C  CG  . PHE C  1  70  ? -13.824 6.470   10.664 1.00 43.32  ? 83  PHE C CG  1 
ATOM   5794 C  CD1 . PHE C  1  70  ? -14.881 7.373   10.642 1.00 43.59  ? 83  PHE C CD1 1 
ATOM   5795 C  CD2 . PHE C  1  70  ? -13.630 5.702   11.799 1.00 42.82  ? 83  PHE C CD2 1 
ATOM   5796 C  CE1 . PHE C  1  70  ? -15.715 7.512   11.739 1.00 42.15  ? 83  PHE C CE1 1 
ATOM   5797 C  CE2 . PHE C  1  70  ? -14.477 5.828   12.888 1.00 44.96  ? 83  PHE C CE2 1 
ATOM   5798 C  CZ  . PHE C  1  70  ? -15.517 6.735   12.853 1.00 43.82  ? 83  PHE C CZ  1 
ATOM   5799 N  N   . ASN C  1  71  ? -11.946 5.184   6.381  1.00 40.41  ? 84  ASN C N   1 
ATOM   5800 C  CA  . ASN C  1  71  ? -11.019 5.491   5.302  1.00 42.42  ? 84  ASN C CA  1 
ATOM   5801 C  C   . ASN C  1  71  ? -9.868  6.357   5.825  1.00 39.31  ? 84  ASN C C   1 
ATOM   5802 O  O   . ASN C  1  71  ? -9.407  7.278   5.153  1.00 37.03  ? 84  ASN C O   1 
ATOM   5803 C  CB  . ASN C  1  71  ? -11.747 6.145   4.132  1.00 41.97  ? 84  ASN C CB  1 
ATOM   5804 C  CG  . ASN C  1  71  ? -11.237 5.682   2.787  1.00 42.51  ? 84  ASN C CG  1 
ATOM   5805 O  OD1 . ASN C  1  71  ? -10.185 5.031   2.686  1.00 44.96  ? 84  ASN C OD1 1 
ATOM   5806 N  ND2 . ASN C  1  71  ? -11.973 6.028   1.746  1.00 40.77  ? 84  ASN C ND2 1 
ATOM   5807 N  N   . PHE C  1  72  ? -9.423  6.071   7.047  1.00 38.42  ? 85  PHE C N   1 
ATOM   5808 C  CA  . PHE C  1  72  ? -8.241  6.731   7.580  1.00 39.32  ? 85  PHE C CA  1 
ATOM   5809 C  C   . PHE C  1  72  ? -7.070  6.326   6.690  1.00 36.11  ? 85  PHE C C   1 
ATOM   5810 O  O   . PHE C  1  72  ? -6.941  5.155   6.348  1.00 36.73  ? 85  PHE C O   1 
ATOM   5811 C  CB  . PHE C  1  72  ? -8.074  6.344   9.055  1.00 37.70  ? 85  PHE C CB  1 
ATOM   5812 C  CG  . PHE C  1  72  ? -7.194  7.259   9.901  1.00 39.93  ? 85  PHE C CG  1 
ATOM   5813 C  CD1 . PHE C  1  72  ? -7.349  8.640   9.862  1.00 42.81  ? 85  PHE C CD1 1 
ATOM   5814 C  CD2 . PHE C  1  72  ? -6.207  6.732   10.733 1.00 41.91  ? 85  PHE C CD2 1 
ATOM   5815 C  CE1 . PHE C  1  72  ? -6.540  9.467   10.635 1.00 44.81  ? 85  PHE C CE1 1 
ATOM   5816 C  CE2 . PHE C  1  72  ? -5.415  7.565   11.510 1.00 43.63  ? 85  PHE C CE2 1 
ATOM   5817 C  CZ  . PHE C  1  72  ? -5.576  8.927   11.454 1.00 41.57  ? 85  PHE C CZ  1 
ATOM   5818 N  N   . GLU C  1  73  ? -6.247  7.297   6.299  1.00 40.66  ? 86  GLU C N   1 
ATOM   5819 C  CA  . GLU C  1  73  ? -5.144  7.041   5.380  1.00 41.54  ? 86  GLU C CA  1 
ATOM   5820 C  C   . GLU C  1  73  ? -4.123  6.120   6.048  1.00 37.93  ? 86  GLU C C   1 
ATOM   5821 O  O   . GLU C  1  73  ? -3.819  6.254   7.226  1.00 37.96  ? 86  GLU C O   1 
ATOM   5822 C  CB  . GLU C  1  73  ? -4.581  8.370   4.874  1.00 41.06  ? 86  GLU C CB  1 
ATOM   5823 C  CG  . GLU C  1  73  ? -3.554  8.220   3.753  1.00 42.13  ? 86  GLU C CG  1 
ATOM   5824 C  CD  . GLU C  1  73  ? -2.134  7.897   4.203  1.00 44.48  ? 86  GLU C CD  1 
ATOM   5825 O  OE1 . GLU C  1  73  ? -1.441  7.083   3.553  1.00 40.44  ? 86  GLU C OE1 1 
ATOM   5826 O  OE2 . GLU C  1  73  ? -1.732  8.458   5.238  1.00 47.87  ? 86  GLU C OE2 1 
ATOM   5827 N  N   . ASN C  1  74  ? -3.598  5.184   5.255  1.00 38.10  ? 87  ASN C N   1 
ATOM   5828 C  CA  . ASN C  1  74  ? -2.785  4.067   5.710  1.00 36.93  ? 87  ASN C CA  1 
ATOM   5829 C  C   . ASN C  1  74  ? -1.610  4.529   6.570  1.00 37.58  ? 87  ASN C C   1 
ATOM   5830 O  O   . ASN C  1  74  ? -1.403  4.003   7.655  1.00 37.14  ? 87  ASN C O   1 
ATOM   5831 C  CB  . ASN C  1  74  ? -2.321  3.255   4.508  1.00 35.29  ? 87  ASN C CB  1 
ATOM   5832 C  CG  . ASN C  1  74  ? -1.421  2.103   4.867  1.00 34.38  ? 87  ASN C CG  1 
ATOM   5833 O  OD1 . ASN C  1  74  ? -0.269  2.047   4.415  1.00 34.40  ? 87  ASN C OD1 1 
ATOM   5834 N  ND2 . ASN C  1  74  ? -1.941  1.174   5.649  1.00 33.87  ? 87  ASN C ND2 1 
ATOM   5835 N  N   . ASN C  1  75  ? -0.829  5.493   6.083  1.00 37.38  ? 88  ASN C N   1 
ATOM   5836 C  CA  . ASN C  1  75  ? 0.371   5.900   6.788  1.00 40.94  ? 88  ASN C CA  1 
ATOM   5837 C  C   . ASN C  1  75  ? 0.004   6.664   8.064  1.00 40.44  ? 88  ASN C C   1 
ATOM   5838 O  O   . ASN C  1  75  ? 0.685   6.522   9.075  1.00 40.69  ? 88  ASN C O   1 
ATOM   5839 C  CB  . ASN C  1  75  ? 1.338   6.634   5.865  1.00 41.96  ? 88  ASN C CB  1 
ATOM   5840 C  CG  . ASN C  1  75  ? 2.146   5.673   5.009  1.00 42.03  ? 88  ASN C CG  1 
ATOM   5841 O  OD1 . ASN C  1  75  ? 2.679   4.669   5.493  1.00 38.18  ? 88  ASN C OD1 1 
ATOM   5842 N  ND2 . ASN C  1  75  ? 2.249   5.941   3.723  1.00 41.94  ? 88  ASN C ND2 1 
ATOM   5843 N  N   . ALA C  1  76  ? -1.060  7.465   8.033  1.00 37.79  ? 89  ALA C N   1 
ATOM   5844 C  CA  . ALA C  1  76  ? -1.537  8.146   9.231  1.00 42.96  ? 89  ALA C CA  1 
ATOM   5845 C  C   . ALA C  1  76  ? -1.976  7.123   10.283 1.00 40.27  ? 89  ALA C C   1 
ATOM   5846 O  O   . ALA C  1  76  ? -1.724  7.304   11.473 1.00 42.33  ? 89  ALA C O   1 
ATOM   5847 C  CB  . ALA C  1  76  ? -2.657  9.106   8.879  1.00 43.91  ? 89  ALA C CB  1 
ATOM   5848 N  N   . ALA C  1  77  ? -2.601  6.036   9.829  1.00 38.07  ? 90  ALA C N   1 
ATOM   5849 C  CA  . ALA C  1  77  ? -3.014  4.945   10.702 1.00 36.82  ? 90  ALA C CA  1 
ATOM   5850 C  C   . ALA C  1  77  ? -1.802  4.260   11.323 1.00 35.56  ? 90  ALA C C   1 
ATOM   5851 O  O   . ALA C  1  77  ? -1.822  3.893   12.492 1.00 36.24  ? 90  ALA C O   1 
ATOM   5852 C  CB  . ALA C  1  77  ? -3.856  3.955   9.931  1.00 36.19  ? 90  ALA C CB  1 
ATOM   5853 N  N   . ILE C  1  78  ? -0.741  4.082   10.532 1.00 36.48  ? 91  ILE C N   1 
ATOM   5854 C  CA  . ILE C  1  78  ? 0.468   3.426   11.007 1.00 36.47  ? 91  ILE C CA  1 
ATOM   5855 C  C   . ILE C  1  78  ? 1.172   4.315   12.027 1.00 33.44  ? 91  ILE C C   1 
ATOM   5856 O  O   . ILE C  1  78  ? 1.580   3.837   13.080 1.00 33.98  ? 91  ILE C O   1 
ATOM   5857 C  CB  . ILE C  1  78  ? 1.346   3.010   9.817  1.00 35.26  ? 91  ILE C CB  1 
ATOM   5858 C  CG1 . ILE C  1  78  ? 0.694   1.831   9.075  1.00 37.84  ? 91  ILE C CG1 1 
ATOM   5859 C  CG2 . ILE C  1  78  ? 2.770   2.685   10.251 1.00 35.22  ? 91  ILE C CG2 1 
ATOM   5860 C  CD1 . ILE C  1  78  ? 1.286   1.551   7.706  1.00 37.01  ? 91  ILE C CD1 1 
ATOM   5861 N  N   . VAL C  1  79  ? 1.263   5.614   11.745 1.00 33.48  ? 92  VAL C N   1 
ATOM   5862 C  CA  . VAL C  1  79  ? 1.898   6.552   12.659 1.00 34.99  ? 92  VAL C CA  1 
ATOM   5863 C  C   . VAL C  1  79  ? 1.167   6.570   14.003 1.00 37.32  ? 92  VAL C C   1 
ATOM   5864 O  O   . VAL C  1  79  ? 1.807   6.473   15.042 1.00 34.77  ? 92  VAL C O   1 
ATOM   5865 C  CB  . VAL C  1  79  ? 2.007   7.959   12.038 1.00 36.25  ? 92  VAL C CB  1 
ATOM   5866 C  CG1 . VAL C  1  79  ? 2.352   9.026   13.068 1.00 36.99  ? 92  VAL C CG1 1 
ATOM   5867 C  CG2 . VAL C  1  79  ? 3.024   7.982   10.898 1.00 37.99  ? 92  VAL C CG2 1 
ATOM   5868 N  N   . ALA C  1  80  ? -0.166  6.687   13.980 1.00 37.38  ? 93  ALA C N   1 
ATOM   5869 C  CA  . ALA C  1  80  ? -0.933  6.760   15.210 1.00 37.30  ? 93  ALA C CA  1 
ATOM   5870 C  C   . ALA C  1  80  ? -0.883  5.431   15.963 1.00 38.25  ? 93  ALA C C   1 
ATOM   5871 O  O   . ALA C  1  80  ? -0.691  5.418   17.171 1.00 38.20  ? 93  ALA C O   1 
ATOM   5872 C  CB  . ALA C  1  80  ? -2.361  7.169   14.908 1.00 39.16  ? 93  ALA C CB  1 
ATOM   5873 N  N   . THR C  1  81  ? -1.047  4.308   15.254 1.00 37.66  ? 94  THR C N   1 
ATOM   5874 C  CA  . THR C  1  81  ? -1.267  3.028   15.912 1.00 34.73  ? 94  THR C CA  1 
ATOM   5875 C  C   . THR C  1  81  ? 0.005   2.565   16.628 1.00 38.31  ? 94  THR C C   1 
ATOM   5876 O  O   . THR C  1  81  ? -0.058  2.155   17.784 1.00 38.84  ? 94  THR C O   1 
ATOM   5877 C  CB  . THR C  1  81  ? -1.755  1.984   14.907 1.00 35.25  ? 94  THR C CB  1 
ATOM   5878 O  OG1 . THR C  1  81  ? -3.008  2.396   14.369 1.00 32.80  ? 94  THR C OG1 1 
ATOM   5879 C  CG2 . THR C  1  81  ? -1.947  0.618   15.539 1.00 37.12  ? 94  THR C CG2 1 
ATOM   5880 N  N   . TYR C  1  82  ? 1.159   2.612   15.948 1.00 36.78  ? 95  TYR C N   1 
ATOM   5881 C  CA  . TYR C  1  82  ? 2.382   2.076   16.526 1.00 35.94  ? 95  TYR C CA  1 
ATOM   5882 C  C   . TYR C  1  82  ? 2.948   3.051   17.555 1.00 35.76  ? 95  TYR C C   1 
ATOM   5883 O  O   . TYR C  1  82  ? 3.638   2.625   18.479 1.00 37.84  ? 95  TYR C O   1 
ATOM   5884 C  CB  . TYR C  1  82  ? 3.400   1.665   15.457 1.00 34.61  ? 95  TYR C CB  1 
ATOM   5885 C  CG  . TYR C  1  82  ? 2.936   0.437   14.691 1.00 37.26  ? 95  TYR C CG  1 
ATOM   5886 C  CD1 . TYR C  1  82  ? 3.017   -0.834  15.247 1.00 38.30  ? 95  TYR C CD1 1 
ATOM   5887 C  CD2 . TYR C  1  82  ? 2.379   0.554   13.423 1.00 39.23  ? 95  TYR C CD2 1 
ATOM   5888 C  CE1 . TYR C  1  82  ? 2.576   -1.954  14.563 1.00 35.45  ? 95  TYR C CE1 1 
ATOM   5889 C  CE2 . TYR C  1  82  ? 1.912   -0.555  12.741 1.00 38.66  ? 95  TYR C CE2 1 
ATOM   5890 C  CZ  . TYR C  1  82  ? 2.016   -1.813  13.304 1.00 38.09  ? 95  TYR C CZ  1 
ATOM   5891 O  OH  . TYR C  1  82  ? 1.569   -2.907  12.612 1.00 37.81  ? 95  TYR C OH  1 
ATOM   5892 N  N   . LEU C  1  83  ? 2.637   4.341   17.427 1.00 36.71  ? 96  LEU C N   1 
ATOM   5893 C  CA  . LEU C  1  83  ? 2.947   5.284   18.493 1.00 39.13  ? 96  LEU C CA  1 
ATOM   5894 C  C   . LEU C  1  83  ? 2.229   4.845   19.768 1.00 39.73  ? 96  LEU C C   1 
ATOM   5895 O  O   . LEU C  1  83  ? 2.850   4.652   20.804 1.00 41.96  ? 96  LEU C O   1 
ATOM   5896 C  CB  . LEU C  1  83  ? 2.539   6.697   18.080 1.00 39.56  ? 96  LEU C CB  1 
ATOM   5897 C  CG  . LEU C  1  83  ? 2.625   7.769   19.171 1.00 40.97  ? 96  LEU C CG  1 
ATOM   5898 C  CD1 . LEU C  1  83  ? 4.054   7.950   19.630 1.00 42.86  ? 96  LEU C CD1 1 
ATOM   5899 C  CD2 . LEU C  1  83  ? 2.066   9.066   18.640 1.00 43.76  ? 96  LEU C CD2 1 
ATOM   5900 N  N   . GLY C  1  84  ? 0.908   4.678   19.668 1.00 38.53  ? 97  GLY C N   1 
ATOM   5901 C  CA  . GLY C  1  84  ? 0.103   4.204   20.784 1.00 39.69  ? 97  GLY C CA  1 
ATOM   5902 C  C   . GLY C  1  84  ? 0.608   2.873   21.338 1.00 36.99  ? 97  GLY C C   1 
ATOM   5903 O  O   . GLY C  1  84  ? 0.706   2.710   22.542 1.00 37.91  ? 97  GLY C O   1 
ATOM   5904 N  N   . HIS C  1  85  ? 0.944   1.932   20.453 1.00 35.92  ? 98  HIS C N   1 
ATOM   5905 C  CA  . HIS C  1  85  ? 1.341   0.593   20.858 1.00 35.68  ? 98  HIS C CA  1 
ATOM   5906 C  C   . HIS C  1  85  ? 2.718   0.608   21.535 1.00 39.37  ? 98  HIS C C   1 
ATOM   5907 O  O   . HIS C  1  85  ? 2.895   -0.001  22.594 1.00 37.53  ? 98  HIS C O   1 
ATOM   5908 C  CB  . HIS C  1  85  ? 1.310   -0.350  19.651 1.00 34.52  ? 98  HIS C CB  1 
ATOM   5909 C  CG  . HIS C  1  85  ? 1.542   -1.774  20.000 1.00 35.37  ? 98  HIS C CG  1 
ATOM   5910 N  ND1 . HIS C  1  85  ? 0.784   -2.428  20.945 1.00 37.49  ? 98  HIS C ND1 1 
ATOM   5911 C  CD2 . HIS C  1  85  ? 2.417   -2.681  19.525 1.00 39.67  ? 98  HIS C CD2 1 
ATOM   5912 C  CE1 . HIS C  1  85  ? 1.208   -3.688  21.042 1.00 41.30  ? 98  HIS C CE1 1 
ATOM   5913 N  NE2 . HIS C  1  85  ? 2.201   -3.865  20.193 1.00 42.85  ? 98  HIS C NE2 1 
ATOM   5914 N  N   . LEU C  1  86  ? 3.699   1.280   20.920 1.00 39.00  ? 99  LEU C N   1 
ATOM   5915 C  CA  . LEU C  1  86  ? 5.053   1.340   21.472 1.00 39.54  ? 99  LEU C CA  1 
ATOM   5916 C  C   . LEU C  1  86  ? 5.032   1.875   22.908 1.00 39.94  ? 99  LEU C C   1 
ATOM   5917 O  O   . LEU C  1  86  ? 5.710   1.345   23.780 1.00 41.46  ? 99  LEU C O   1 
ATOM   5918 C  CB  . LEU C  1  86  ? 5.948   2.207   20.586 1.00 38.50  ? 99  LEU C CB  1 
ATOM   5919 C  CG  . LEU C  1  86  ? 6.467   1.568   19.297 1.00 39.07  ? 99  LEU C CG  1 
ATOM   5920 C  CD1 . LEU C  1  86  ? 7.027   2.645   18.363 1.00 41.81  ? 99  LEU C CD1 1 
ATOM   5921 C  CD2 . LEU C  1  86  ? 7.518   0.513   19.603 1.00 42.19  ? 99  LEU C CD2 1 
ATOM   5922 N  N   . LEU C  1  87  ? 4.239   2.928   23.144 1.00 42.40  ? 100 LEU C N   1 
ATOM   5923 C  CA  . LEU C  1  87  ? 4.212   3.630   24.419 1.00 40.54  ? 100 LEU C CA  1 
ATOM   5924 C  C   . LEU C  1  87  ? 3.263   2.957   25.409 1.00 40.77  ? 100 LEU C C   1 
ATOM   5925 O  O   . LEU C  1  87  ? 3.554   2.944   26.602 1.00 41.30  ? 100 LEU C O   1 
ATOM   5926 C  CB  . LEU C  1  87  ? 3.807   5.087   24.205 1.00 40.86  ? 100 LEU C CB  1 
ATOM   5927 C  CG  . LEU C  1  87  ? 4.779   5.945   23.389 1.00 41.62  ? 100 LEU C CG  1 
ATOM   5928 C  CD1 . LEU C  1  87  ? 4.171   7.322   23.150 1.00 40.91  ? 100 LEU C CD1 1 
ATOM   5929 C  CD2 . LEU C  1  87  ? 6.163   6.053   24.034 1.00 41.75  ? 100 LEU C CD2 1 
ATOM   5930 N  N   . ASN C  1  88  ? 2.133   2.424   24.925 1.00 39.80  ? 101 ASN C N   1 
ATOM   5931 C  CA  . ASN C  1  88  ? 1.019   2.084   25.795 1.00 38.38  ? 101 ASN C CA  1 
ATOM   5932 C  C   . ASN C  1  88  ? 0.517   0.658   25.609 1.00 40.98  ? 101 ASN C C   1 
ATOM   5933 O  O   . ASN C  1  88  ? -0.419  0.259   26.303 1.00 43.21  ? 101 ASN C O   1 
ATOM   5934 C  CB  . ASN C  1  88  ? -0.189  2.978   25.561 1.00 38.04  ? 101 ASN C CB  1 
ATOM   5935 C  CG  . ASN C  1  88  ? 0.118   4.431   25.813 1.00 39.01  ? 101 ASN C CG  1 
ATOM   5936 O  OD1 . ASN C  1  88  ? 0.815   4.764   26.776 1.00 42.75  ? 101 ASN C OD1 1 
ATOM   5937 N  ND2 . ASN C  1  88  ? -0.383  5.308   24.958 1.00 41.59  ? 101 ASN C ND2 1 
ATOM   5938 N  N   . GLY C  1  89  ? 1.117   -0.112  24.698 1.00 40.55  ? 102 GLY C N   1 
ATOM   5939 C  CA  . GLY C  1  89  ? 0.661   -1.472  24.448 1.00 37.36  ? 102 GLY C CA  1 
ATOM   5940 C  C   . GLY C  1  89  ? 1.634   -2.515  24.994 1.00 38.22  ? 102 GLY C C   1 
ATOM   5941 O  O   . GLY C  1  89  ? 2.742   -2.184  25.436 1.00 42.57  ? 102 GLY C O   1 
ATOM   5942 N  N   . ASN C  1  90  ? 1.205   -3.779  24.910 1.00 36.47  ? 103 ASN C N   1 
ATOM   5943 C  CA  . ASN C  1  90  ? 2.015   -4.915  25.308 1.00 40.69  ? 103 ASN C CA  1 
ATOM   5944 C  C   . ASN C  1  90  ? 2.661   -5.532  24.071 1.00 42.91  ? 103 ASN C C   1 
ATOM   5945 O  O   . ASN C  1  90  ? 2.003   -6.185  23.264 1.00 40.41  ? 103 ASN C O   1 
ATOM   5946 C  CB  . ASN C  1  90  ? 1.182   -5.933  26.075 1.00 43.50  ? 103 ASN C CB  1 
ATOM   5947 C  CG  . ASN C  1  90  ? 2.021   -7.020  26.708 1.00 43.41  ? 103 ASN C CG  1 
ATOM   5948 O  OD1 . ASN C  1  90  ? 2.912   -7.580  26.063 1.00 41.30  ? 103 ASN C OD1 1 
ATOM   5949 N  ND2 . ASN C  1  90  ? 1.759   -7.328  27.971 1.00 48.14  ? 103 ASN C ND2 1 
ATOM   5950 N  N   . LEU C  1  91  ? 3.976   -5.348  23.960 1.00 42.74  ? 104 LEU C N   1 
ATOM   5951 C  CA  . LEU C  1  91  ? 4.709   -5.684  22.756 1.00 43.90  ? 104 LEU C CA  1 
ATOM   5952 C  C   . LEU C  1  91  ? 4.883   -7.190  22.623 1.00 44.56  ? 104 LEU C C   1 
ATOM   5953 O  O   . LEU C  1  91  ? 5.024   -7.693  21.513 1.00 42.20  ? 104 LEU C O   1 
ATOM   5954 C  CB  . LEU C  1  91  ? 6.031   -4.928  22.843 1.00 47.59  ? 104 LEU C CB  1 
ATOM   5955 C  CG  . LEU C  1  91  ? 5.862   -3.410  22.726 1.00 51.88  ? 104 LEU C CG  1 
ATOM   5956 C  CD1 . LEU C  1  91  ? 7.078   -2.691  23.221 1.00 56.18  ? 104 LEU C CD1 1 
ATOM   5957 C  CD2 . LEU C  1  91  ? 5.582   -3.012  21.281 1.00 56.22  ? 104 LEU C CD2 1 
ATOM   5958 N  N   . VAL C  1  92  ? 4.825   -7.906  23.756 1.00 47.56  ? 105 VAL C N   1 
ATOM   5959 C  CA  . VAL C  1  92  ? 4.993   -9.349  23.771 1.00 45.63  ? 105 VAL C CA  1 
ATOM   5960 C  C   . VAL C  1  92  ? 3.711   -10.036 23.303 1.00 45.76  ? 105 VAL C C   1 
ATOM   5961 O  O   . VAL C  1  92  ? 3.787   -10.954 22.494 1.00 47.09  ? 105 VAL C O   1 
ATOM   5962 C  CB  . VAL C  1  92  ? 5.452   -9.821  25.162 1.00 47.30  ? 105 VAL C CB  1 
ATOM   5963 C  CG1 . VAL C  1  92  ? 5.345   -11.335 25.318 1.00 46.76  ? 105 VAL C CG1 1 
ATOM   5964 C  CG2 . VAL C  1  92  ? 6.881   -9.340  25.443 1.00 49.94  ? 105 VAL C CG2 1 
ATOM   5965 N  N   . THR C  1  93  ? 2.542   -9.606  23.798 1.00 47.12  ? 106 THR C N   1 
ATOM   5966 C  CA  . THR C  1  93  ? 1.280   -10.207 23.375 1.00 45.57  ? 106 THR C CA  1 
ATOM   5967 C  C   . THR C  1  93  ? 0.724   -9.512  22.132 1.00 48.85  ? 106 THR C C   1 
ATOM   5968 O  O   . THR C  1  93  ? -0.239  -10.009 21.548 1.00 49.58  ? 106 THR C O   1 
ATOM   5969 C  CB  . THR C  1  93  ? 0.253   -10.162 24.506 1.00 47.61  ? 106 THR C CB  1 
ATOM   5970 O  OG1 . THR C  1  93  ? 0.050   -8.780  24.804 1.00 43.98  ? 106 THR C OG1 1 
ATOM   5971 C  CG2 . THR C  1  93  ? 0.704   -10.967 25.713 1.00 51.90  ? 106 THR C CG2 1 
ATOM   5972 N  N   . ASP C  1  94  ? 1.297   -8.355  21.763 1.00 45.14  ? 107 ASP C N   1 
ATOM   5973 C  CA  . ASP C  1  94  ? 0.855   -7.591  20.601 1.00 43.13  ? 107 ASP C CA  1 
ATOM   5974 C  C   . ASP C  1  94  ? -0.582  -7.093  20.778 1.00 44.31  ? 107 ASP C C   1 
ATOM   5975 O  O   . ASP C  1  94  ? -1.366  -7.098  19.824 1.00 45.42  ? 107 ASP C O   1 
ATOM   5976 C  CB  . ASP C  1  94  ? 1.021   -8.395  19.319 1.00 42.86  ? 107 ASP C CB  1 
ATOM   5977 C  CG  . ASP C  1  94  ? 1.024   -7.575  18.032 1.00 47.85  ? 107 ASP C CG  1 
ATOM   5978 O  OD1 . ASP C  1  94  ? 1.674   -6.498  18.025 1.00 44.54  ? 107 ASP C OD1 1 
ATOM   5979 O  OD2 . ASP C  1  94  ? 0.386   -8.022  17.044 1.00 45.49  ? 107 ASP C OD2 1 
ATOM   5980 N  N   . LEU C  1  95  ? -0.921  -6.647  21.996 1.00 42.92  ? 108 LEU C N   1 
ATOM   5981 C  CA  . LEU C  1  95  ? -2.263  -6.160  22.292 1.00 44.38  ? 108 LEU C CA  1 
ATOM   5982 C  C   . LEU C  1  95  ? -2.183  -4.755  22.889 1.00 41.46  ? 108 LEU C C   1 
ATOM   5983 O  O   . LEU C  1  95  ? -1.300  -4.465  23.695 1.00 39.10  ? 108 LEU C O   1 
ATOM   5984 C  CB  . LEU C  1  95  ? -2.996  -7.125  23.224 1.00 47.77  ? 108 LEU C CB  1 
ATOM   5985 C  CG  . LEU C  1  95  ? -3.286  -8.524  22.667 1.00 49.94  ? 108 LEU C CG  1 
ATOM   5986 C  CD1 . LEU C  1  95  ? -3.753  -9.464  23.763 1.00 51.03  ? 108 LEU C CD1 1 
ATOM   5987 C  CD2 . LEU C  1  95  ? -4.317  -8.472  21.547 1.00 50.61  ? 108 LEU C CD2 1 
ATOM   5988 N  N   . LEU C  1  96  ? -3.111  -3.893  22.453 1.00 40.81  ? 109 LEU C N   1 
ATOM   5989 C  CA  . LEU C  1  96  ? -3.236  -2.533  22.941 1.00 39.01  ? 109 LEU C CA  1 
ATOM   5990 C  C   . LEU C  1  96  ? -4.667  -2.309  23.429 1.00 45.56  ? 109 LEU C C   1 
ATOM   5991 O  O   . LEU C  1  96  ? -5.626  -2.631  22.724 1.00 43.66  ? 109 LEU C O   1 
ATOM   5992 C  CB  . LEU C  1  96  ? -2.886  -1.584  21.799 1.00 38.91  ? 109 LEU C CB  1 
ATOM   5993 C  CG  . LEU C  1  96  ? -3.164  -0.095  22.029 1.00 37.50  ? 109 LEU C CG  1 
ATOM   5994 C  CD1 . LEU C  1  96  ? -2.377  0.436   23.234 1.00 41.42  ? 109 LEU C CD1 1 
ATOM   5995 C  CD2 . LEU C  1  96  ? -2.836  0.716   20.794 1.00 36.75  ? 109 LEU C CD2 1 
ATOM   5996 N  N   . SER C  1  97  ? -4.792  -1.738  24.638 1.00 42.41  ? 110 SER C N   1 
ATOM   5997 C  CA  . SER C  1  97  ? -6.064  -1.253  25.151 1.00 41.83  ? 110 SER C CA  1 
ATOM   5998 C  C   . SER C  1  97  ? -6.360  0.134   24.595 1.00 39.89  ? 110 SER C C   1 
ATOM   5999 O  O   . SER C  1  97  ? -5.514  1.020   24.677 1.00 38.69  ? 110 SER C O   1 
ATOM   6000 C  CB  . SER C  1  97  ? -6.047  -1.220  26.659 1.00 41.71  ? 110 SER C CB  1 
ATOM   6001 O  OG  . SER C  1  97  ? -7.223  -0.596  27.155 1.00 45.15  ? 110 SER C OG  1 
ATOM   6002 N  N   . ILE C  1  98  ? -7.583  0.349   24.094 1.00 38.82  ? 111 ILE C N   1 
ATOM   6003 C  CA  . ILE C  1  98  ? -7.914  1.659   23.549 1.00 40.32  ? 111 ILE C CA  1 
ATOM   6004 C  C   . ILE C  1  98  ? -8.309  2.602   24.682 1.00 40.17  ? 111 ILE C C   1 
ATOM   6005 O  O   . ILE C  1  98  ? -8.630  3.762   24.431 1.00 48.88  ? 111 ILE C O   1 
ATOM   6006 C  CB  . ILE C  1  98  ? -8.994  1.587   22.455 1.00 40.21  ? 111 ILE C CB  1 
ATOM   6007 C  CG1 . ILE C  1  98  ? -10.368 1.173   22.991 1.00 41.57  ? 111 ILE C CG1 1 
ATOM   6008 C  CG2 . ILE C  1  98  ? -8.543  0.674   21.317 1.00 41.94  ? 111 ILE C CG2 1 
ATOM   6009 C  CD1 . ILE C  1  98  ? -11.476 1.254   21.950 1.00 42.60  ? 111 ILE C CD1 1 
ATOM   6010 N  N   . GLY C  1  99  ? -8.283  2.093   25.920 1.00 44.21  ? 112 GLY C N   1 
ATOM   6011 C  CA  . GLY C  1  99  ? -8.580  2.895   27.094 1.00 46.90  ? 112 GLY C CA  1 
ATOM   6012 C  C   . GLY C  1  99  ? -7.542  2.659   28.187 1.00 49.65  ? 112 GLY C C   1 
ATOM   6013 O  O   . GLY C  1  99  ? -6.356  2.929   27.984 1.00 44.96  ? 112 GLY C O   1 
ATOM   6014 N  N   . GLY C  1  100 ? -8.006  2.156   29.340 1.00 49.21  ? 113 GLY C N   1 
ATOM   6015 C  CA  . GLY C  1  100 ? -7.163  2.014   30.519 1.00 50.81  ? 113 GLY C CA  1 
ATOM   6016 C  C   . GLY C  1  100 ? -6.594  0.605   30.659 1.00 50.93  ? 113 GLY C C   1 
ATOM   6017 O  O   . GLY C  1  100 ? -6.664  -0.201  29.734 1.00 52.16  ? 113 GLY C O   1 
ATOM   6018 N  N   . ALA C  1  101 ? -6.060  0.318   31.850 1.00 51.46  ? 114 ALA C N   1 
ATOM   6019 C  CA  . ALA C  1  101 ? -5.370  -0.932  32.112 1.00 51.84  ? 114 ALA C CA  1 
ATOM   6020 C  C   . ALA C  1  101 ? -6.373  -2.078  32.147 1.00 49.17  ? 114 ALA C C   1 
ATOM   6021 O  O   . ALA C  1  101 ? -7.519  -1.899  32.547 1.00 54.09  ? 114 ALA C O   1 
ATOM   6022 C  CB  . ALA C  1  101 ? -4.599  -0.833  33.412 1.00 55.96  ? 114 ALA C CB  1 
ATOM   6023 N  N   . THR C  1  102 ? -5.925  -3.254  31.716 1.00 50.53  ? 115 THR C N   1 
ATOM   6024 C  CA  . THR C  1  102 ? -6.776  -4.426  31.704 1.00 56.42  ? 115 THR C CA  1 
ATOM   6025 C  C   . THR C  1  102 ? -5.896  -5.664  31.682 1.00 57.48  ? 115 THR C C   1 
ATOM   6026 O  O   . THR C  1  102 ? -4.875  -5.670  31.006 1.00 59.84  ? 115 THR C O   1 
ATOM   6027 C  CB  . THR C  1  102 ? -7.711  -4.388  30.493 1.00 65.78  ? 115 THR C CB  1 
ATOM   6028 O  OG1 . THR C  1  102 ? -8.451  -5.602  30.549 1.00 64.59  ? 115 THR C OG1 1 
ATOM   6029 C  CG2 . THR C  1  102 ? -6.979  -4.351  29.162 1.00 66.14  ? 115 THR C CG2 1 
ATOM   6030 N  N   . PRO C  1  103 ? -6.274  -6.755  32.388 1.00 63.85  ? 116 PRO C N   1 
ATOM   6031 C  CA  . PRO C  1  103 ? -5.578  -8.036  32.238 1.00 62.96  ? 116 PRO C CA  1 
ATOM   6032 C  C   . PRO C  1  103 ? -5.669  -8.617  30.826 1.00 55.23  ? 116 PRO C C   1 
ATOM   6033 O  O   . PRO C  1  103 ? -4.876  -9.483  30.471 1.00 56.21  ? 116 PRO C O   1 
ATOM   6034 C  CB  . PRO C  1  103 ? -6.261  -8.945  33.291 1.00 66.21  ? 116 PRO C CB  1 
ATOM   6035 C  CG  . PRO C  1  103 ? -7.623  -8.310  33.513 1.00 67.01  ? 116 PRO C CG  1 
ATOM   6036 C  CD  . PRO C  1  103 ? -7.379  -6.815  33.362 1.00 64.67  ? 116 PRO C CD  1 
ATOM   6037 N  N   . LYS C  1  104 ? -6.621  -8.132  30.018 1.00 55.36  ? 117 LYS C N   1 
ATOM   6038 C  CA  . LYS C  1  104 ? -6.812  -8.600  28.652 1.00 58.64  ? 117 LYS C CA  1 
ATOM   6039 C  C   . LYS C  1  104 ? -5.571  -8.377  27.779 1.00 57.62  ? 117 LYS C C   1 
ATOM   6040 O  O   . LYS C  1  104 ? -5.440  -9.035  26.750 1.00 58.06  ? 117 LYS C O   1 
ATOM   6041 C  CB  . LYS C  1  104 ? -8.011  -7.915  27.982 1.00 62.33  ? 117 LYS C CB  1 
ATOM   6042 C  CG  . LYS C  1  104 ? -9.397  -8.278  28.505 1.00 67.38  ? 117 LYS C CG  1 
ATOM   6043 C  CD  . LYS C  1  104 ? -10.421 -7.177  28.228 1.00 72.24  ? 117 LYS C CD  1 
ATOM   6044 C  CE  . LYS C  1  104 ? -11.806 -7.452  28.720 1.00 76.59  ? 117 LYS C CE  1 
ATOM   6045 N  NZ  . LYS C  1  104 ? -12.401 -8.568  27.982 1.00 79.78  ? 117 LYS C NZ  1 
ATOM   6046 N  N   . THR C  1  105 ? -4.667  -7.457  28.164 1.00 54.01  ? 118 THR C N   1 
ATOM   6047 C  CA  . THR C  1  105 ? -3.458  -7.235  27.381 1.00 54.51  ? 118 THR C CA  1 
ATOM   6048 C  C   . THR C  1  105 ? -2.366  -8.205  27.814 1.00 56.99  ? 118 THR C C   1 
ATOM   6049 O  O   . THR C  1  105 ? -1.340  -8.284  27.156 1.00 56.87  ? 118 THR C O   1 
ATOM   6050 C  CB  . THR C  1  105 ? -2.987  -5.777  27.418 1.00 49.49  ? 118 THR C CB  1 
ATOM   6051 O  OG1 . THR C  1  105 ? -2.758  -5.359  28.758 1.00 46.90  ? 118 THR C OG1 1 
ATOM   6052 C  CG2 . THR C  1  105 ? -3.986  -4.825  26.772 1.00 47.48  ? 118 THR C CG2 1 
ATOM   6053 N  N   . GLY C  1  106 ? -2.587  -8.950  28.904 1.00 59.53  ? 119 GLY C N   1 
ATOM   6054 C  CA  . GLY C  1  106 ? -1.695  -10.028 29.309 1.00 55.20  ? 119 GLY C CA  1 
ATOM   6055 C  C   . GLY C  1  106 ? -0.730  -9.603  30.412 1.00 57.86  ? 119 GLY C C   1 
ATOM   6056 O  O   . GLY C  1  106 ? -0.851  -8.509  30.964 1.00 62.83  ? 119 GLY C O   1 
ATOM   6057 N  N   . PRO C  1  107 ? 0.259   -10.460 30.762 1.00 57.78  ? 120 PRO C N   1 
ATOM   6058 C  CA  . PRO C  1  107 ? 1.216   -10.158 31.826 1.00 59.50  ? 120 PRO C CA  1 
ATOM   6059 C  C   . PRO C  1  107 ? 1.857   -8.790  31.625 1.00 60.88  ? 120 PRO C C   1 
ATOM   6060 O  O   . PRO C  1  107 ? 2.364   -8.490  30.548 1.00 63.16  ? 120 PRO C O   1 
ATOM   6061 C  CB  . PRO C  1  107 ? 2.244   -11.298 31.743 1.00 60.53  ? 120 PRO C CB  1 
ATOM   6062 C  CG  . PRO C  1  107 ? 1.493   -12.437 31.087 1.00 62.60  ? 120 PRO C CG  1 
ATOM   6063 C  CD  . PRO C  1  107 ? 0.484   -11.783 30.160 1.00 60.90  ? 120 PRO C CD  1 
ATOM   6064 N  N   . PRO C  1  108 ? 1.864   -7.918  32.654 1.00 64.08  ? 121 PRO C N   1 
ATOM   6065 C  CA  . PRO C  1  108 ? 2.410   -6.573  32.487 1.00 65.54  ? 121 PRO C CA  1 
ATOM   6066 C  C   . PRO C  1  108 ? 3.901   -6.618  32.146 1.00 61.73  ? 121 PRO C C   1 
ATOM   6067 O  O   . PRO C  1  108 ? 4.602   -7.544  32.534 1.00 54.84  ? 121 PRO C O   1 
ATOM   6068 C  CB  . PRO C  1  108 ? 2.108   -5.874  33.824 1.00 67.25  ? 121 PRO C CB  1 
ATOM   6069 C  CG  . PRO C  1  108 ? 1.906   -7.006  34.810 1.00 70.36  ? 121 PRO C CG  1 
ATOM   6070 C  CD  . PRO C  1  108 ? 1.367   -8.183  34.014 1.00 68.07  ? 121 PRO C CD  1 
ATOM   6071 N  N   . PRO C  1  109 ? 4.420   -5.649  31.360 1.00 56.99  ? 122 PRO C N   1 
ATOM   6072 C  CA  . PRO C  1  109 ? 5.834   -5.615  31.008 1.00 52.10  ? 122 PRO C CA  1 
ATOM   6073 C  C   . PRO C  1  109 ? 6.669   -5.120  32.184 1.00 53.62  ? 122 PRO C C   1 
ATOM   6074 O  O   . PRO C  1  109 ? 6.129   -4.558  33.134 1.00 53.45  ? 122 PRO C O   1 
ATOM   6075 C  CB  . PRO C  1  109 ? 5.857   -4.637  29.816 1.00 51.72  ? 122 PRO C CB  1 
ATOM   6076 C  CG  . PRO C  1  109 ? 4.723   -3.688  30.087 1.00 52.81  ? 122 PRO C CG  1 
ATOM   6077 C  CD  . PRO C  1  109 ? 3.670   -4.539  30.763 1.00 54.18  ? 122 PRO C CD  1 
ATOM   6078 N  N   . PRO C  1  110 ? 8.008   -5.295  32.146 1.00 50.43  ? 123 PRO C N   1 
ATOM   6079 C  CA  . PRO C  1  110 ? 8.880   -4.745  33.185 1.00 49.25  ? 123 PRO C CA  1 
ATOM   6080 C  C   . PRO C  1  110 ? 8.819   -3.220  33.267 1.00 51.56  ? 123 PRO C C   1 
ATOM   6081 O  O   . PRO C  1  110 ? 8.889   -2.537  32.246 1.00 48.67  ? 123 PRO C O   1 
ATOM   6082 C  CB  . PRO C  1  110 ? 10.289  -5.276  32.820 1.00 52.49  ? 123 PRO C CB  1 
ATOM   6083 C  CG  . PRO C  1  110 ? 10.193  -5.700  31.370 1.00 55.85  ? 123 PRO C CG  1 
ATOM   6084 C  CD  . PRO C  1  110 ? 8.734   -6.057  31.114 1.00 53.95  ? 123 PRO C CD  1 
ATOM   6085 N  N   . PRO C  1  111 ? 8.652   -2.635  34.477 1.00 54.55  ? 124 PRO C N   1 
ATOM   6086 C  CA  . PRO C  1  111 ? 8.695   -1.178  34.650 1.00 51.28  ? 124 PRO C CA  1 
ATOM   6087 C  C   . PRO C  1  111 ? 10.010  -0.611  34.124 1.00 48.15  ? 124 PRO C C   1 
ATOM   6088 O  O   . PRO C  1  111 ? 11.017  -1.310  34.150 1.00 43.24  ? 124 PRO C O   1 
ATOM   6089 C  CB  . PRO C  1  111 ? 8.553   -0.961  36.171 1.00 55.55  ? 124 PRO C CB  1 
ATOM   6090 C  CG  . PRO C  1  111 ? 7.974   -2.260  36.708 1.00 57.34  ? 124 PRO C CG  1 
ATOM   6091 C  CD  . PRO C  1  111 ? 8.366   -3.351  35.731 1.00 54.36  ? 124 PRO C CD  1 
ATOM   6092 N  N   . PRO C  1  112 ? 10.072  0.659   33.652 1.00 47.81  ? 125 PRO C N   1 
ATOM   6093 C  CA  . PRO C  1  112 ? 8.955   1.608   33.690 1.00 47.77  ? 125 PRO C CA  1 
ATOM   6094 C  C   . PRO C  1  112 ? 7.854   1.474   32.638 1.00 50.76  ? 125 PRO C C   1 
ATOM   6095 O  O   . PRO C  1  112 ? 6.922   2.275   32.628 1.00 50.00  ? 125 PRO C O   1 
ATOM   6096 C  CB  . PRO C  1  112 ? 9.643   2.991   33.545 1.00 49.25  ? 125 PRO C CB  1 
ATOM   6097 C  CG  . PRO C  1  112 ? 11.128  2.722   33.483 1.00 49.68  ? 125 PRO C CG  1 
ATOM   6098 C  CD  . PRO C  1  112 ? 11.276  1.265   33.083 1.00 49.29  ? 125 PRO C CD  1 
ATOM   6099 N  N   . ALA C  1  113 ? 7.965   0.483   31.745 1.00 50.98  ? 126 ALA C N   1 
ATOM   6100 C  CA  . ALA C  1  113 ? 6.907   0.194   30.788 1.00 49.37  ? 126 ALA C CA  1 
ATOM   6101 C  C   . ALA C  1  113 ? 5.672   -0.313  31.533 1.00 51.70  ? 126 ALA C C   1 
ATOM   6102 O  O   . ALA C  1  113 ? 5.805   -0.873  32.615 1.00 52.88  ? 126 ALA C O   1 
ATOM   6103 C  CB  . ALA C  1  113 ? 7.397   -0.820  29.777 1.00 47.47  ? 126 ALA C CB  1 
ATOM   6104 N  N   . HIS C  1  114 ? 4.483   -0.150  30.933 1.00 48.63  ? 127 HIS C N   1 
ATOM   6105 C  CA  . HIS C  1  114 ? 3.227   -0.313  31.659 1.00 46.57  ? 127 HIS C CA  1 
ATOM   6106 C  C   . HIS C  1  114 ? 2.121   -0.989  30.841 1.00 47.51  ? 127 HIS C C   1 
ATOM   6107 O  O   . HIS C  1  114 ? 1.303   -1.715  31.410 1.00 47.64  ? 127 HIS C O   1 
ATOM   6108 C  CB  . HIS C  1  114 ? 2.747   1.042   32.189 1.00 47.19  ? 127 HIS C CB  1 
ATOM   6109 C  CG  . HIS C  1  114 ? 2.793   2.125   31.165 1.00 49.08  ? 127 HIS C CG  1 
ATOM   6110 N  ND1 . HIS C  1  114 ? 1.828   2.236   30.193 1.00 47.17  ? 127 HIS C ND1 1 
ATOM   6111 C  CD2 . HIS C  1  114 ? 3.664   3.120   30.944 1.00 46.71  ? 127 HIS C CD2 1 
ATOM   6112 C  CE1 . HIS C  1  114 ? 2.117   3.273   29.426 1.00 46.02  ? 127 HIS C CE1 1 
ATOM   6113 N  NE2 . HIS C  1  114 ? 3.227   3.823   29.865 1.00 43.91  ? 127 HIS C NE2 1 
ATOM   6114 N  N   . ALA C  1  115 ? 2.071   -0.750  29.521 1.00 46.76  ? 128 ALA C N   1 
ATOM   6115 C  CA  . ALA C  1  115 ? 1.018   -1.287  28.669 1.00 41.96  ? 128 ALA C CA  1 
ATOM   6116 C  C   . ALA C  1  115 ? -0.343  -0.897  29.236 1.00 39.71  ? 128 ALA C C   1 
ATOM   6117 O  O   . ALA C  1  115 ? -1.263  -1.707  29.252 1.00 39.02  ? 128 ALA C O   1 
ATOM   6118 C  CB  . ALA C  1  115 ? 1.142   -2.788  28.517 1.00 42.72  ? 128 ALA C CB  1 
ATOM   6119 N  N   . GLY C  1  116 ? -0.448  0.364   29.664 1.00 39.06  ? 129 GLY C N   1 
ATOM   6120 C  CA  . GLY C  1  116 ? -1.597  0.851   30.404 1.00 45.45  ? 129 GLY C CA  1 
ATOM   6121 C  C   . GLY C  1  116 ? -2.703  1.407   29.497 1.00 47.11  ? 129 GLY C C   1 
ATOM   6122 O  O   . GLY C  1  116 ? -3.736  1.852   29.992 1.00 44.66  ? 129 GLY C O   1 
ATOM   6123 N  N   . GLY C  1  117 ? -2.466  1.418   28.176 1.00 47.14  ? 130 GLY C N   1 
ATOM   6124 C  CA  . GLY C  1  117 ? -3.477  1.803   27.202 1.00 40.76  ? 130 GLY C CA  1 
ATOM   6125 C  C   . GLY C  1  117 ? -3.434  3.292   26.865 1.00 37.33  ? 130 GLY C C   1 
ATOM   6126 O  O   . GLY C  1  117 ? -2.661  4.057   27.435 1.00 38.01  ? 130 GLY C O   1 
ATOM   6127 N  N   . LEU C  1  118 ? -4.300  3.690   25.928 1.00 40.52  ? 131 LEU C N   1 
ATOM   6128 C  CA  . LEU C  1  118 ? -4.336  5.038   25.382 1.00 39.64  ? 131 LEU C CA  1 
ATOM   6129 C  C   . LEU C  1  118 ? -4.684  6.084   26.436 1.00 41.90  ? 131 LEU C C   1 
ATOM   6130 O  O   . LEU C  1  118 ? -4.465  7.275   26.206 1.00 40.70  ? 131 LEU C O   1 
ATOM   6131 C  CB  . LEU C  1  118 ? -5.332  5.064   24.221 1.00 39.12  ? 131 LEU C CB  1 
ATOM   6132 C  CG  . LEU C  1  118 ? -4.958  4.211   23.001 1.00 40.91  ? 131 LEU C CG  1 
ATOM   6133 C  CD1 . LEU C  1  118 ? -5.941  4.387   21.858 1.00 43.34  ? 131 LEU C CD1 1 
ATOM   6134 C  CD2 . LEU C  1  118 ? -3.554  4.535   22.512 1.00 40.79  ? 131 LEU C CD2 1 
ATOM   6135 N  N   . ASN C  1  119 ? -5.245  5.643   27.573 1.00 45.52  ? 132 ASN C N   1 
ATOM   6136 C  CA  . ASN C  1  119 ? -5.580  6.531   28.675 1.00 49.15  ? 132 ASN C CA  1 
ATOM   6137 C  C   . ASN C  1  119 ? -4.344  7.161   29.312 1.00 49.10  ? 132 ASN C C   1 
ATOM   6138 O  O   . ASN C  1  119 ? -4.464  8.219   29.928 1.00 50.24  ? 132 ASN C O   1 
ATOM   6139 C  CB  . ASN C  1  119 ? -6.379  5.814   29.758 1.00 51.22  ? 132 ASN C CB  1 
ATOM   6140 C  CG  . ASN C  1  119 ? -7.847  5.691   29.413 1.00 53.52  ? 132 ASN C CG  1 
ATOM   6141 O  OD1 . ASN C  1  119 ? -8.270  6.024   28.300 1.00 50.55  ? 132 ASN C OD1 1 
ATOM   6142 N  ND2 . ASN C  1  119 ? -8.640  5.204   30.353 1.00 55.67  ? 132 ASN C ND2 1 
ATOM   6143 N  N   . VAL C  1  120 ? -3.170  6.518   29.184 1.00 45.52  ? 133 VAL C N   1 
ATOM   6144 C  CA  . VAL C  1  120 ? -1.971  7.002   29.852 1.00 44.23  ? 133 VAL C CA  1 
ATOM   6145 C  C   . VAL C  1  120 ? -1.610  8.402   29.351 1.00 44.20  ? 133 VAL C C   1 
ATOM   6146 O  O   . VAL C  1  120 ? -1.410  8.619   28.163 1.00 43.91  ? 133 VAL C O   1 
ATOM   6147 C  CB  . VAL C  1  120 ? -0.788  6.031   29.696 1.00 45.12  ? 133 VAL C CB  1 
ATOM   6148 C  CG1 . VAL C  1  120 ? 0.505   6.627   30.238 1.00 47.86  ? 133 VAL C CG1 1 
ATOM   6149 C  CG2 . VAL C  1  120 ? -1.075  4.696   30.359 1.00 46.33  ? 133 VAL C CG2 1 
ATOM   6150 N  N   . HIS C  1  121 ? -1.451  9.328   30.303 1.00 49.32  ? 134 HIS C N   1 
ATOM   6151 C  CA  . HIS C  1  121 ? -1.213  10.735  30.035 1.00 47.77  ? 134 HIS C CA  1 
ATOM   6152 C  C   . HIS C  1  121 ? 0.281   11.032  29.904 1.00 47.64  ? 134 HIS C C   1 
ATOM   6153 O  O   . HIS C  1  121 ? 1.094   10.450  30.606 1.00 49.90  ? 134 HIS C O   1 
ATOM   6154 C  CB  . HIS C  1  121 ? -1.788  11.557  31.194 1.00 48.47  ? 134 HIS C CB  1 
ATOM   6155 C  CG  . HIS C  1  121 ? -1.489  13.010  31.118 1.00 48.81  ? 134 HIS C CG  1 
ATOM   6156 N  ND1 . HIS C  1  121 ? -2.119  13.846  30.222 1.00 53.82  ? 134 HIS C ND1 1 
ATOM   6157 C  CD2 . HIS C  1  121 ? -0.617  13.765  31.793 1.00 49.60  ? 134 HIS C CD2 1 
ATOM   6158 C  CE1 . HIS C  1  121 ? -1.652  15.075  30.378 1.00 55.43  ? 134 HIS C CE1 1 
ATOM   6159 N  NE2 . HIS C  1  121 ? -0.730  15.049  31.323 1.00 55.09  ? 134 HIS C NE2 1 
ATOM   6160 N  N   . GLY C  1  122 ? 0.640   11.966  29.020 1.00 51.66  ? 135 GLY C N   1 
ATOM   6161 C  CA  . GLY C  1  122 ? 1.893   12.689  29.168 1.00 55.07  ? 135 GLY C CA  1 
ATOM   6162 C  C   . GLY C  1  122 ? 2.868   12.522  28.004 1.00 61.35  ? 135 GLY C C   1 
ATOM   6163 O  O   . GLY C  1  122 ? 3.708   13.394  27.799 1.00 62.56  ? 135 GLY C O   1 
ATOM   6164 N  N   . THR C  1  123 ? 2.784   11.411  27.259 1.00 62.18  ? 136 THR C N   1 
ATOM   6165 C  CA  . THR C  1  123 ? 3.637   11.237  26.087 1.00 68.52  ? 136 THR C CA  1 
ATOM   6166 C  C   . THR C  1  123 ? 2.795   11.167  24.807 1.00 64.68  ? 136 THR C C   1 
ATOM   6167 O  O   . THR C  1  123 ? 3.196   11.762  23.813 1.00 59.18  ? 136 THR C O   1 
ATOM   6168 C  CB  . THR C  1  123 ? 4.560   10.028  26.248 1.00 71.74  ? 136 THR C CB  1 
ATOM   6169 O  OG1 . THR C  1  123 ? 5.073   10.073  27.576 1.00 68.45  ? 136 THR C OG1 1 
ATOM   6170 C  CG2 . THR C  1  123 ? 5.750   10.075  25.302 1.00 70.15  ? 136 THR C CG2 1 
ATOM   6171 N  N   . PHE C  1  124 ? 1.653   10.457  24.827 1.00 59.34  ? 137 PHE C N   1 
ATOM   6172 C  CA  . PHE C  1  124 ? 0.682   10.503  23.735 1.00 59.44  ? 137 PHE C CA  1 
ATOM   6173 C  C   . PHE C  1  124 ? -0.525  11.360  24.142 1.00 57.75  ? 137 PHE C C   1 
ATOM   6174 O  O   . PHE C  1  124 ? -0.596  12.524  23.754 1.00 59.90  ? 137 PHE C O   1 
ATOM   6175 C  CB  . PHE C  1  124 ? 0.281   9.097   23.266 1.00 57.10  ? 137 PHE C CB  1 
ATOM   6176 C  CG  . PHE C  1  124 ? -0.463  9.002   21.934 1.00 53.24  ? 137 PHE C CG  1 
ATOM   6177 C  CD1 . PHE C  1  124 ? -0.949  10.125  21.264 1.00 53.93  ? 137 PHE C CD1 1 
ATOM   6178 C  CD2 . PHE C  1  124 ? -0.701  7.764   21.359 1.00 51.61  ? 137 PHE C CD2 1 
ATOM   6179 C  CE1 . PHE C  1  124 ? -1.620  10.005  20.054 1.00 52.50  ? 137 PHE C CE1 1 
ATOM   6180 C  CE2 . PHE C  1  124 ? -1.369  7.652   20.146 1.00 48.49  ? 137 PHE C CE2 1 
ATOM   6181 C  CZ  . PHE C  1  124 ? -1.825  8.771   19.494 1.00 50.64  ? 137 PHE C CZ  1 
ATOM   6182 N  N   . GLU C  1  125 ? -1.481  10.790  24.895 1.00 56.68  ? 138 GLU C N   1 
ATOM   6183 C  CA  . GLU C  1  125 ? -2.669  11.514  25.345 1.00 56.87  ? 138 GLU C CA  1 
ATOM   6184 C  C   . GLU C  1  125 ? -2.238  12.798  26.050 1.00 54.61  ? 138 GLU C C   1 
ATOM   6185 O  O   . GLU C  1  125 ? -1.312  12.785  26.853 1.00 56.19  ? 138 GLU C O   1 
ATOM   6186 C  CB  . GLU C  1  125 ? -3.528  10.669  26.293 1.00 54.24  ? 138 GLU C CB  1 
ATOM   6187 C  CG  . GLU C  1  125 ? -4.871  11.293  26.677 1.00 58.49  ? 138 GLU C CG  1 
ATOM   6188 C  CD  . GLU C  1  125 ? -4.828  12.492  27.626 1.00 58.13  ? 138 GLU C CD  1 
ATOM   6189 O  OE1 . GLU C  1  125 ? -3.991  12.433  28.559 1.00 55.24  ? 138 GLU C OE1 1 
ATOM   6190 O  OE2 . GLU C  1  125 ? -5.623  13.463  27.447 1.00 49.16  ? 138 GLU C OE2 1 
ATOM   6191 N  N   . GLY C  1  126 ? -2.920  13.906  25.746 1.00 55.52  ? 139 GLY C N   1 
ATOM   6192 C  CA  . GLY C  1  126 ? -2.573  15.192  26.323 1.00 57.75  ? 139 GLY C CA  1 
ATOM   6193 C  C   . GLY C  1  126 ? -3.758  16.155  26.378 1.00 56.79  ? 139 GLY C C   1 
ATOM   6194 O  O   . GLY C  1  126 ? -4.919  15.765  26.214 1.00 48.52  ? 139 GLY C O   1 
ATOM   6195 N  N   . ASP C  1  127 ? -3.410  17.435  26.573 1.00 56.76  ? 140 ASP C N   1 
ATOM   6196 C  CA  . ASP C  1  127 ? -4.323  18.440  27.093 1.00 59.45  ? 140 ASP C CA  1 
ATOM   6197 C  C   . ASP C  1  127 ? -5.004  19.206  25.959 1.00 57.55  ? 140 ASP C C   1 
ATOM   6198 O  O   . ASP C  1  127 ? -4.598  19.123  24.802 1.00 55.27  ? 140 ASP C O   1 
ATOM   6199 C  CB  . ASP C  1  127 ? -3.579  19.376  28.036 1.00 57.39  ? 140 ASP C CB  1 
ATOM   6200 C  CG  . ASP C  1  127 ? -2.946  18.729  29.261 1.00 56.61  ? 140 ASP C CG  1 
ATOM   6201 O  OD1 . ASP C  1  127 ? -3.567  17.794  29.812 1.00 55.95  ? 140 ASP C OD1 1 
ATOM   6202 O  OD2 . ASP C  1  127 ? -1.842  19.173  29.669 1.00 58.55  ? 140 ASP C OD2 1 
ATOM   6203 N  N   . ALA C  1  128 ? -6.039  19.972  26.336 1.00 57.20  ? 141 ALA C N   1 
ATOM   6204 C  CA  . ALA C  1  128 ? -6.773  20.869  25.447 1.00 56.97  ? 141 ALA C CA  1 
ATOM   6205 C  C   . ALA C  1  128 ? -7.502  20.097  24.346 1.00 53.10  ? 141 ALA C C   1 
ATOM   6206 O  O   . ALA C  1  128 ? -7.571  20.547  23.203 1.00 59.80  ? 141 ALA C O   1 
ATOM   6207 C  CB  . ALA C  1  128 ? -5.853  21.934  24.872 1.00 55.40  ? 141 ALA C CB  1 
ATOM   6208 N  N   . GLY C  1  129 ? -8.085  18.954  24.711 1.00 56.37  ? 142 GLY C N   1 
ATOM   6209 C  CA  . GLY C  1  129 ? -8.956  18.214  23.811 1.00 59.73  ? 142 GLY C CA  1 
ATOM   6210 C  C   . GLY C  1  129 ? -10.312 18.907  23.670 1.00 63.05  ? 142 GLY C C   1 
ATOM   6211 O  O   . GLY C  1  129 ? -10.622 19.826  24.420 1.00 65.58  ? 142 GLY C O   1 
ATOM   6212 N  N   . MET C  1  130 ? -11.115 18.450  22.705 1.00 63.15  ? 143 MET C N   1 
ATOM   6213 C  CA  . MET C  1  130 ? -12.367 19.103  22.355 1.00 62.62  ? 143 MET C CA  1 
ATOM   6214 C  C   . MET C  1  130 ? -13.500 18.635  23.265 1.00 60.48  ? 143 MET C C   1 
ATOM   6215 O  O   . MET C  1  130 ? -14.294 19.450  23.728 1.00 69.21  ? 143 MET C O   1 
ATOM   6216 C  CB  . MET C  1  130 ? -12.738 18.810  20.898 1.00 64.24  ? 143 MET C CB  1 
ATOM   6217 C  CG  . MET C  1  130 ? -11.855 19.521  19.890 1.00 66.30  ? 143 MET C CG  1 
ATOM   6218 S  SD  . MET C  1  130 ? -12.218 19.006  18.202 1.00 67.20  ? 143 MET C SD  1 
ATOM   6219 C  CE  . MET C  1  130 ? -11.866 17.246  18.252 1.00 55.12  ? 143 MET C CE  1 
ATOM   6220 N  N   . THR C  1  131 ? -13.592 17.320  23.498 1.00 57.03  ? 144 THR C N   1 
ATOM   6221 C  CA  . THR C  1  131 ? -14.690 16.755  24.268 1.00 56.07  ? 144 THR C CA  1 
ATOM   6222 C  C   . THR C  1  131 ? -14.188 16.027  25.517 1.00 54.79  ? 144 THR C C   1 
ATOM   6223 O  O   . THR C  1  131 ? -15.003 15.489  26.264 1.00 54.62  ? 144 THR C O   1 
ATOM   6224 C  CB  . THR C  1  131 ? -15.544 15.839  23.387 1.00 55.06  ? 144 THR C CB  1 
ATOM   6225 O  OG1 . THR C  1  131 ? -14.820 14.646  23.105 1.00 51.25  ? 144 THR C OG1 1 
ATOM   6226 C  CG2 . THR C  1  131 ? -15.945 16.512  22.088 1.00 57.49  ? 144 THR C CG2 1 
ATOM   6227 N  N   . ARG C  1  132 ? -12.867 16.008  25.748 1.00 54.29  ? 145 ARG C N   1 
ATOM   6228 C  CA  . ARG C  1  132 ? -12.300 15.422  26.956 1.00 55.21  ? 145 ARG C CA  1 
ATOM   6229 C  C   . ARG C  1  132 ? -11.561 16.500  27.752 1.00 55.44  ? 145 ARG C C   1 
ATOM   6230 O  O   . ARG C  1  132 ? -10.936 17.378  27.163 1.00 52.59  ? 145 ARG C O   1 
ATOM   6231 C  CB  . ARG C  1  132 ? -11.345 14.268  26.630 1.00 52.98  ? 145 ARG C CB  1 
ATOM   6232 C  CG  . ARG C  1  132 ? -11.998 12.898  26.515 1.00 56.67  ? 145 ARG C CG  1 
ATOM   6233 C  CD  . ARG C  1  132 ? -12.925 12.750  25.321 1.00 54.96  ? 145 ARG C CD  1 
ATOM   6234 N  NE  . ARG C  1  132 ? -13.549 11.423  25.327 1.00 53.81  ? 145 ARG C NE  1 
ATOM   6235 C  CZ  . ARG C  1  132 ? -14.627 11.074  24.630 1.00 51.40  ? 145 ARG C CZ  1 
ATOM   6236 N  NH1 . ARG C  1  132 ? -15.184 11.927  23.785 1.00 50.71  ? 145 ARG C NH1 1 
ATOM   6237 N  NH2 . ARG C  1  132 ? -15.138 9.867   24.787 1.00 51.82  ? 145 ARG C NH2 1 
ATOM   6238 N  N   . ALA C  1  133 ? -11.621 16.405  29.090 1.00 53.51  ? 146 ALA C N   1 
ATOM   6239 C  CA  . ALA C  1  133 ? -10.952 17.341  29.978 1.00 57.51  ? 146 ALA C CA  1 
ATOM   6240 C  C   . ALA C  1  133 ? -9.502  16.909  30.190 1.00 57.57  ? 146 ALA C C   1 
ATOM   6241 O  O   . ALA C  1  133 ? -9.181  15.732  30.060 1.00 53.47  ? 146 ALA C O   1 
ATOM   6242 N  N   . ASP C  1  134 ? -8.637  17.878  30.525 1.00 59.98  ? 147 ASP C N   1 
ATOM   6243 C  CA  . ASP C  1  134 ? -7.241  17.612  30.834 1.00 59.17  ? 147 ASP C CA  1 
ATOM   6244 C  C   . ASP C  1  134 ? -7.147  16.661  32.023 1.00 62.71  ? 147 ASP C C   1 
ATOM   6245 O  O   . ASP C  1  134 ? -7.988  16.684  32.921 1.00 60.38  ? 147 ASP C O   1 
ATOM   6246 C  CB  . ASP C  1  134 ? -6.471  18.887  31.137 1.00 57.16  ? 147 ASP C CB  1 
ATOM   6247 C  CG  . ASP C  1  134 ? -6.455  19.920  30.024 1.00 59.84  ? 147 ASP C CG  1 
ATOM   6248 O  OD1 . ASP C  1  134 ? -7.143  19.689  29.002 1.00 62.19  ? 147 ASP C OD1 1 
ATOM   6249 O  OD2 . ASP C  1  134 ? -5.749  20.938  30.189 1.00 58.65  ? 147 ASP C OD2 1 
ATOM   6250 N  N   . GLU C  1  135 ? -6.094  15.838  32.016 1.00 59.39  ? 148 GLU C N   1 
ATOM   6251 C  CA  . GLU C  1  135 ? -5.881  14.822  33.032 1.00 61.44  ? 148 GLU C CA  1 
ATOM   6252 C  C   . GLU C  1  135 ? -5.772  15.443  34.430 1.00 59.48  ? 148 GLU C C   1 
ATOM   6253 O  O   . GLU C  1  135 ? -6.149  14.798  35.403 1.00 59.79  ? 148 GLU C O   1 
ATOM   6254 C  CB  . GLU C  1  135 ? -4.630  14.013  32.678 1.00 61.37  ? 148 GLU C CB  1 
ATOM   6255 C  CG  . GLU C  1  135 ? -4.405  12.814  33.597 1.00 62.41  ? 148 GLU C CG  1 
ATOM   6256 C  CD  . GLU C  1  135 ? -3.527  13.063  34.813 1.00 68.67  ? 148 GLU C CD  1 
ATOM   6257 O  OE1 . GLU C  1  135 ? -3.042  14.205  35.021 1.00 69.06  ? 148 GLU C OE1 1 
ATOM   6258 O  OE2 . GLU C  1  135 ? -3.329  12.077  35.557 1.00 72.86  ? 148 GLU C OE2 1 
ATOM   6259 N  N   . PHE C  1  136 ? -5.257  16.676  34.530 1.00 61.62  ? 149 PHE C N   1 
ATOM   6260 C  CA  . PHE C  1  136 ? -5.117  17.346  35.814 1.00 68.23  ? 149 PHE C CA  1 
ATOM   6261 C  C   . PHE C  1  136 ? -6.455  17.399  36.554 1.00 67.11  ? 149 PHE C C   1 
ATOM   6262 O  O   . PHE C  1  136 ? -6.481  17.298  37.776 1.00 75.83  ? 149 PHE C O   1 
ATOM   6263 C  CB  . PHE C  1  136 ? -4.552  18.765  35.702 1.00 72.96  ? 149 PHE C CB  1 
ATOM   6264 C  CG  . PHE C  1  136 ? -4.456  19.463  37.054 1.00 82.87  ? 149 PHE C CG  1 
ATOM   6265 C  CD1 . PHE C  1  136 ? -3.495  19.087  38.000 1.00 87.55  ? 149 PHE C CD1 1 
ATOM   6266 C  CD2 . PHE C  1  136 ? -5.343  20.482  37.390 1.00 87.09  ? 149 PHE C CD2 1 
ATOM   6267 C  CE1 . PHE C  1  136 ? -3.435  19.709  39.240 1.00 90.01  ? 149 PHE C CE1 1 
ATOM   6268 C  CE2 . PHE C  1  136 ? -5.255  21.116  38.626 1.00 89.02  ? 149 PHE C CE2 1 
ATOM   6269 C  CZ  . PHE C  1  136 ? -4.309  20.722  39.549 1.00 90.65  ? 149 PHE C CZ  1 
ATOM   6270 N  N   . PHE C  1  137 ? -7.562  17.546  35.819 1.00 67.91  ? 150 PHE C N   1 
ATOM   6271 C  CA  . PHE C  1  137 ? -8.880  17.703  36.423 1.00 64.54  ? 150 PHE C CA  1 
ATOM   6272 C  C   . PHE C  1  137 ? -9.507  16.355  36.789 1.00 68.88  ? 150 PHE C C   1 
ATOM   6273 O  O   . PHE C  1  137 ? -10.610 16.333  37.340 1.00 68.55  ? 150 PHE C O   1 
ATOM   6274 C  CB  . PHE C  1  137 ? -9.791  18.492  35.478 1.00 62.41  ? 150 PHE C CB  1 
ATOM   6275 C  CG  . PHE C  1  137 ? -9.230  19.843  35.064 1.00 64.11  ? 150 PHE C CG  1 
ATOM   6276 C  CD1 . PHE C  1  137 ? -8.719  20.735  36.002 1.00 67.18  ? 150 PHE C CD1 1 
ATOM   6277 C  CD2 . PHE C  1  137 ? -9.161  20.186  33.721 1.00 69.69  ? 150 PHE C CD2 1 
ATOM   6278 C  CE1 . PHE C  1  137 ? -8.180  21.942  35.602 1.00 69.20  ? 150 PHE C CE1 1 
ATOM   6279 C  CE2 . PHE C  1  137 ? -8.646  21.410  33.329 1.00 68.97  ? 150 PHE C CE2 1 
ATOM   6280 C  CZ  . PHE C  1  137 ? -8.161  22.284  34.270 1.00 70.23  ? 150 PHE C CZ  1 
ATOM   6281 N  N   . GLY C  1  138 ? -8.848  15.233  36.461 1.00 66.41  ? 151 GLY C N   1 
ATOM   6282 C  CA  . GLY C  1  138 ? -9.172  13.960  37.088 1.00 65.24  ? 151 GLY C CA  1 
ATOM   6283 C  C   . GLY C  1  138 ? -9.699  12.886  36.132 1.00 65.07  ? 151 GLY C C   1 
ATOM   6284 O  O   . GLY C  1  138 ? -9.788  11.723  36.521 1.00 63.55  ? 151 GLY C O   1 
ATOM   6285 N  N   . ASP C  1  139 ? -10.061 13.249  34.896 1.00 64.62  ? 152 ASP C N   1 
ATOM   6286 C  CA  . ASP C  1  139 ? -10.626 12.278  33.967 1.00 67.62  ? 152 ASP C CA  1 
ATOM   6287 C  C   . ASP C  1  139 ? -10.364 12.720  32.531 1.00 64.24  ? 152 ASP C C   1 
ATOM   6288 O  O   . ASP C  1  139 ? -11.019 13.632  32.032 1.00 59.64  ? 152 ASP C O   1 
ATOM   6289 C  CB  . ASP C  1  139 ? -12.110 12.054  34.207 1.00 69.20  ? 152 ASP C CB  1 
ATOM   6290 C  CG  . ASP C  1  139 ? -12.787 11.054  33.274 1.00 72.32  ? 152 ASP C CG  1 
ATOM   6291 O  OD1 . ASP C  1  139 ? -12.117 10.553  32.329 1.00 71.84  ? 152 ASP C OD1 1 
ATOM   6292 O  OD2 . ASP C  1  139 ? -13.979 10.773  33.501 1.00 72.80  ? 152 ASP C OD2 1 
ATOM   6293 N  N   . ASN C  1  140 ? -9.420  12.027  31.883 1.00 64.66  ? 153 ASN C N   1 
ATOM   6294 C  CA  . ASN C  1  140 ? -8.917  12.424  30.578 1.00 62.69  ? 153 ASN C CA  1 
ATOM   6295 C  C   . ASN C  1  140 ? -9.548  11.592  29.464 1.00 61.03  ? 153 ASN C C   1 
ATOM   6296 O  O   . ASN C  1  140 ? -9.152  11.757  28.309 1.00 64.07  ? 153 ASN C O   1 
ATOM   6297 C  CB  . ASN C  1  140 ? -7.396  12.311  30.519 1.00 58.65  ? 153 ASN C CB  1 
ATOM   6298 C  CG  . ASN C  1  140 ? -6.907  10.880  30.588 1.00 55.85  ? 153 ASN C CG  1 
ATOM   6299 O  OD1 . ASN C  1  140 ? -7.675  9.963   30.904 1.00 59.34  ? 153 ASN C OD1 1 
ATOM   6300 N  ND2 . ASN C  1  140 ? -5.628  10.667  30.316 1.00 58.70  ? 153 ASN C ND2 1 
ATOM   6301 N  N   . HIS C  1  141 ? -10.519 10.723  29.800 1.00 61.16  ? 154 HIS C N   1 
ATOM   6302 C  CA  . HIS C  1  141 ? -11.012 9.732   28.852 1.00 65.81  ? 154 HIS C CA  1 
ATOM   6303 C  C   . HIS C  1  141 ? -12.519 9.850   28.605 1.00 63.31  ? 154 HIS C C   1 
ATOM   6304 O  O   . HIS C  1  141 ? -12.964 9.591   27.488 1.00 64.00  ? 154 HIS C O   1 
ATOM   6305 C  CB  . HIS C  1  141 ? -10.572 8.325   29.272 1.00 69.55  ? 154 HIS C CB  1 
ATOM   6306 C  CG  . HIS C  1  141 ? -11.034 7.928   30.627 1.00 75.23  ? 154 HIS C CG  1 
ATOM   6307 N  ND1 . HIS C  1  141 ? -12.211 7.218   30.756 1.00 81.65  ? 154 HIS C ND1 1 
ATOM   6308 C  CD2 . HIS C  1  141 ? -10.511 8.024   31.843 1.00 73.19  ? 154 HIS C CD2 1 
ATOM   6309 C  CE1 . HIS C  1  141 ? -12.416 6.952   32.035 1.00 78.90  ? 154 HIS C CE1 1 
ATOM   6310 N  NE2 . HIS C  1  141 ? -11.406 7.454   32.716 1.00 76.09  ? 154 HIS C NE2 1 
ATOM   6311 N  N   . SER C  1  142 ? -13.302 10.221  29.628 1.00 62.53  ? 155 SER C N   1 
ATOM   6312 C  CA  . SER C  1  142 ? -14.750 10.304  29.494 1.00 61.79  ? 155 SER C CA  1 
ATOM   6313 C  C   . SER C  1  142 ? -15.159 11.518  28.662 1.00 56.08  ? 155 SER C C   1 
ATOM   6314 O  O   . SER C  1  142 ? -14.530 12.571  28.709 1.00 54.47  ? 155 SER C O   1 
ATOM   6315 C  CB  . SER C  1  142 ? -15.432 10.357  30.840 1.00 61.21  ? 155 SER C CB  1 
ATOM   6316 O  OG  . SER C  1  142 ? -15.179 9.181   31.596 1.00 61.47  ? 155 SER C OG  1 
ATOM   6317 N  N   . PHE C  1  143 ? -16.273 11.369  27.944 1.00 56.61  ? 156 PHE C N   1 
ATOM   6318 C  CA  . PHE C  1  143 ? -16.942 12.505  27.337 1.00 61.34  ? 156 PHE C CA  1 
ATOM   6319 C  C   . PHE C  1  143 ? -17.351 13.503  28.423 1.00 60.27  ? 156 PHE C C   1 
ATOM   6320 O  O   . PHE C  1  143 ? -17.794 13.106  29.497 1.00 58.27  ? 156 PHE C O   1 
ATOM   6321 C  CB  . PHE C  1  143 ? -18.150 11.993  26.553 1.00 60.14  ? 156 PHE C CB  1 
ATOM   6322 C  CG  . PHE C  1  143 ? -19.022 13.089  25.963 1.00 61.27  ? 156 PHE C CG  1 
ATOM   6323 C  CD1 . PHE C  1  143 ? -18.748 13.626  24.710 1.00 59.70  ? 156 PHE C CD1 1 
ATOM   6324 C  CD2 . PHE C  1  143 ? -20.134 13.562  26.664 1.00 62.15  ? 156 PHE C CD2 1 
ATOM   6325 C  CE1 . PHE C  1  143 ? -19.574 14.601  24.173 1.00 58.23  ? 156 PHE C CE1 1 
ATOM   6326 C  CE2 . PHE C  1  143 ? -20.951 14.539  26.123 1.00 61.11  ? 156 PHE C CE2 1 
ATOM   6327 C  CZ  . PHE C  1  143 ? -20.670 15.053  24.883 1.00 59.42  ? 156 PHE C CZ  1 
ATOM   6328 N  N   . ASN C  1  144 ? -17.205 14.795  28.113 1.00 60.77  ? 157 ASN C N   1 
ATOM   6329 C  CA  . ASN C  1  144 ? -17.460 15.878  29.047 1.00 64.91  ? 157 ASN C CA  1 
ATOM   6330 C  C   . ASN C  1  144 ? -18.473 16.822  28.401 1.00 66.76  ? 157 ASN C C   1 
ATOM   6331 O  O   . ASN C  1  144 ? -18.157 17.475  27.412 1.00 59.37  ? 157 ASN C O   1 
ATOM   6332 C  CB  . ASN C  1  144 ? -16.142 16.542  29.429 1.00 69.68  ? 157 ASN C CB  1 
ATOM   6333 C  CG  . ASN C  1  144 ? -16.279 17.785  30.278 1.00 77.20  ? 157 ASN C CG  1 
ATOM   6334 O  OD1 . ASN C  1  144 ? -17.101 18.660  29.986 1.00 79.28  ? 157 ASN C OD1 1 
ATOM   6335 N  ND2 . ASN C  1  144 ? -15.458 17.883  31.317 1.00 81.64  ? 157 ASN C ND2 1 
ATOM   6336 N  N   . GLN C  1  145 ? -19.678 16.885  28.980 1.00 71.55  ? 158 GLN C N   1 
ATOM   6337 C  CA  . GLN C  1  145 ? -20.795 17.624  28.409 1.00 71.91  ? 158 GLN C CA  1 
ATOM   6338 C  C   . GLN C  1  145 ? -20.487 19.122  28.367 1.00 68.41  ? 158 GLN C C   1 
ATOM   6339 O  O   . GLN C  1  145 ? -20.837 19.787  27.392 1.00 66.99  ? 158 GLN C O   1 
ATOM   6340 C  CB  . GLN C  1  145 ? -22.077 17.317  29.193 1.00 70.98  ? 158 GLN C CB  1 
ATOM   6341 C  CG  . GLN C  1  145 ? -23.353 17.952  28.637 1.00 68.65  ? 158 GLN C CG  1 
ATOM   6342 C  CD  . GLN C  1  145 ? -23.720 17.486  27.241 1.00 68.11  ? 158 GLN C CD  1 
ATOM   6343 O  OE1 . GLN C  1  145 ? -23.743 16.287  26.936 1.00 67.28  ? 158 GLN C OE1 1 
ATOM   6344 N  NE2 . GLN C  1  145 ? -24.016 18.435  26.364 1.00 67.28  ? 158 GLN C NE2 1 
ATOM   6345 N  N   . THR C  1  146 ? -19.832 19.644  29.415 1.00 70.70  ? 159 THR C N   1 
ATOM   6346 C  CA  . THR C  1  146 ? -19.507 21.063  29.486 1.00 74.14  ? 159 THR C CA  1 
ATOM   6347 C  C   . THR C  1  146 ? -18.652 21.450  28.280 1.00 72.37  ? 159 THR C C   1 
ATOM   6348 O  O   . THR C  1  146 ? -18.872 22.492  27.661 1.00 76.80  ? 159 THR C O   1 
ATOM   6349 C  CB  . THR C  1  146 ? -18.801 21.409  30.800 1.00 76.49  ? 159 THR C CB  1 
ATOM   6350 O  OG1 . THR C  1  146 ? -19.608 20.929  31.874 1.00 78.81  ? 159 THR C OG1 1 
ATOM   6351 C  CG2 . THR C  1  146 ? -18.604 22.908  30.961 1.00 76.46  ? 159 THR C CG2 1 
ATOM   6352 N  N   . LEU C  1  147 ? -17.680 20.598  27.940 1.00 73.55  ? 160 LEU C N   1 
ATOM   6353 C  CA  . LEU C  1  147 ? -16.802 20.870  26.814 1.00 68.92  ? 160 LEU C CA  1 
ATOM   6354 C  C   . LEU C  1  147 ? -17.546 20.710  25.492 1.00 63.21  ? 160 LEU C C   1 
ATOM   6355 O  O   . LEU C  1  147 ? -17.300 21.465  24.559 1.00 63.95  ? 160 LEU C O   1 
ATOM   6356 C  CB  . LEU C  1  147 ? -15.567 19.978  26.896 1.00 70.62  ? 160 LEU C CB  1 
ATOM   6357 C  CG  . LEU C  1  147 ? -14.551 20.392  27.965 1.00 69.10  ? 160 LEU C CG  1 
ATOM   6358 C  CD1 . LEU C  1  147 ? -13.390 19.418  27.985 1.00 69.39  ? 160 LEU C CD1 1 
ATOM   6359 C  CD2 . LEU C  1  147 ? -14.071 21.822  27.703 1.00 62.96  ? 160 LEU C CD2 1 
ATOM   6360 N  N   . PHE C  1  148 ? -18.463 19.745  25.421 1.00 60.68  ? 161 PHE C N   1 
ATOM   6361 C  CA  . PHE C  1  148 ? -19.269 19.564  24.224 1.00 65.44  ? 161 PHE C CA  1 
ATOM   6362 C  C   . PHE C  1  148 ? -20.187 20.774  24.043 1.00 69.20  ? 161 PHE C C   1 
ATOM   6363 O  O   . PHE C  1  148 ? -20.448 21.175  22.912 1.00 73.41  ? 161 PHE C O   1 
ATOM   6364 C  CB  . PHE C  1  148 ? -20.027 18.232  24.258 1.00 66.88  ? 161 PHE C CB  1 
ATOM   6365 C  CG  . PHE C  1  148 ? -20.835 17.988  22.992 1.00 72.97  ? 161 PHE C CG  1 
ATOM   6366 C  CD1 . PHE C  1  148 ? -20.212 17.567  21.817 1.00 78.04  ? 161 PHE C CD1 1 
ATOM   6367 C  CD2 . PHE C  1  148 ? -22.208 18.217  22.968 1.00 70.96  ? 161 PHE C CD2 1 
ATOM   6368 C  CE1 . PHE C  1  148 ? -20.946 17.356  20.658 1.00 80.47  ? 161 PHE C CE1 1 
ATOM   6369 C  CE2 . PHE C  1  148 ? -22.943 17.979  21.812 1.00 73.03  ? 161 PHE C CE2 1 
ATOM   6370 C  CZ  . PHE C  1  148 ? -22.311 17.549  20.659 1.00 78.29  ? 161 PHE C CZ  1 
ATOM   6371 N  N   . ASP C  1  149 ? -20.651 21.372  25.151 1.00 71.87  ? 162 ASP C N   1 
ATOM   6372 C  CA  . ASP C  1  149 ? -21.439 22.599  25.098 1.00 69.98  ? 162 ASP C CA  1 
ATOM   6373 C  C   . ASP C  1  149 ? -20.640 23.721  24.437 1.00 61.53  ? 162 ASP C C   1 
ATOM   6374 O  O   . ASP C  1  149 ? -21.201 24.487  23.649 1.00 59.59  ? 162 ASP C O   1 
ATOM   6375 C  CB  . ASP C  1  149 ? -21.955 23.000  26.473 1.00 70.33  ? 162 ASP C CB  1 
ATOM   6376 C  CG  . ASP C  1  149 ? -22.985 22.060  27.084 1.00 74.73  ? 162 ASP C CG  1 
ATOM   6377 O  OD1 . ASP C  1  149 ? -23.668 21.359  26.307 1.00 73.50  ? 162 ASP C OD1 1 
ATOM   6378 O  OD2 . ASP C  1  149 ? -23.078 22.009  28.331 1.00 80.08  ? 162 ASP C OD2 1 
ATOM   6379 N  N   . LYS C  1  150 ? -19.337 23.804  24.754 1.00 60.39  ? 163 LYS C N   1 
ATOM   6380 C  CA  . LYS C  1  150 ? -18.447 24.775  24.128 1.00 63.97  ? 163 LYS C CA  1 
ATOM   6381 C  C   . LYS C  1  150 ? -18.310 24.465  22.634 1.00 69.12  ? 163 LYS C C   1 
ATOM   6382 O  O   . LYS C  1  150 ? -18.338 25.375  21.813 1.00 73.95  ? 163 LYS C O   1 
ATOM   6383 C  CB  . LYS C  1  150 ? -17.083 24.798  24.829 1.00 63.86  ? 163 LYS C CB  1 
ATOM   6384 C  CG  . LYS C  1  150 ? -16.142 25.933  24.437 1.00 65.78  ? 163 LYS C CG  1 
ATOM   6385 C  CD  . LYS C  1  150 ? -14.789 25.860  25.142 1.00 67.79  ? 163 LYS C CD  1 
ATOM   6386 C  CE  . LYS C  1  150 ? -13.799 26.900  24.727 1.00 72.20  ? 163 LYS C CE  1 
ATOM   6387 N  NZ  . LYS C  1  150 ? -13.735 28.021  25.660 1.00 79.12  ? 163 LYS C NZ  1 
ATOM   6388 N  N   . PHE C  1  151 ? -18.182 23.179  22.289 1.00 71.02  ? 164 PHE C N   1 
ATOM   6389 C  CA  . PHE C  1  151 ? -18.129 22.743  20.900 1.00 72.85  ? 164 PHE C CA  1 
ATOM   6390 C  C   . PHE C  1  151 ? -19.358 23.250  20.148 1.00 69.58  ? 164 PHE C C   1 
ATOM   6391 O  O   . PHE C  1  151 ? -19.240 23.774  19.039 1.00 67.11  ? 164 PHE C O   1 
ATOM   6392 C  CB  . PHE C  1  151 ? -18.034 21.211  20.862 1.00 71.34  ? 164 PHE C CB  1 
ATOM   6393 C  CG  . PHE C  1  151 ? -17.848 20.566  19.495 1.00 75.02  ? 164 PHE C CG  1 
ATOM   6394 C  CD1 . PHE C  1  151 ? -16.574 20.388  18.965 1.00 79.78  ? 164 PHE C CD1 1 
ATOM   6395 C  CD2 . PHE C  1  151 ? -18.937 20.094  18.765 1.00 74.57  ? 164 PHE C CD2 1 
ATOM   6396 C  CE1 . PHE C  1  151 ? -16.401 19.791  17.726 1.00 81.17  ? 164 PHE C CE1 1 
ATOM   6397 C  CE2 . PHE C  1  151 ? -18.758 19.499  17.526 1.00 75.04  ? 164 PHE C CE2 1 
ATOM   6398 C  CZ  . PHE C  1  151 ? -17.493 19.352  17.007 1.00 76.36  ? 164 PHE C CZ  1 
ATOM   6399 N  N   . VAL C  1  152 ? -20.538 23.079  20.760 1.00 68.85  ? 165 VAL C N   1 
ATOM   6400 C  CA  . VAL C  1  152 ? -21.794 23.506  20.157 1.00 70.35  ? 165 VAL C CA  1 
ATOM   6401 C  C   . VAL C  1  152 ? -21.808 25.030  20.054 1.00 69.11  ? 165 VAL C C   1 
ATOM   6402 O  O   . VAL C  1  152 ? -22.158 25.586  19.012 1.00 64.37  ? 165 VAL C O   1 
ATOM   6403 C  CB  . VAL C  1  152 ? -23.013 22.977  20.937 1.00 77.42  ? 165 VAL C CB  1 
ATOM   6404 C  CG1 . VAL C  1  152 ? -24.332 23.563  20.443 1.00 76.48  ? 165 VAL C CG1 1 
ATOM   6405 C  CG2 . VAL C  1  152 ? -23.090 21.456  20.889 1.00 80.90  ? 165 VAL C CG2 1 
ATOM   6406 N  N   . ASP C  1  153 ? -21.412 25.700  21.139 1.00 73.47  ? 166 ASP C N   1 
ATOM   6407 C  CA  . ASP C  1  153 ? -21.415 27.150  21.145 1.00 80.19  ? 166 ASP C CA  1 
ATOM   6408 C  C   . ASP C  1  153 ? -20.552 27.683  20.004 1.00 72.39  ? 166 ASP C C   1 
ATOM   6409 O  O   . ASP C  1  153 ? -21.000 28.533  19.240 1.00 68.98  ? 166 ASP C O   1 
ATOM   6410 C  CB  . ASP C  1  153 ? -21.001 27.723  22.491 1.00 85.67  ? 166 ASP C CB  1 
ATOM   6411 C  CG  . ASP C  1  153 ? -21.304 29.211  22.626 1.00 88.83  ? 166 ASP C CG  1 
ATOM   6412 O  OD1 . ASP C  1  153 ? -22.486 29.581  22.431 1.00 86.78  ? 166 ASP C OD1 1 
ATOM   6413 O  OD2 . ASP C  1  153 ? -20.373 29.990  22.925 1.00 89.80  ? 166 ASP C OD2 1 
ATOM   6414 N  N   . PHE C  1  154 ? -19.322 27.169  19.878 1.00 72.45  ? 167 PHE C N   1 
ATOM   6415 C  CA  . PHE C  1  154 ? -18.388 27.662  18.876 1.00 71.24  ? 167 PHE C CA  1 
ATOM   6416 C  C   . PHE C  1  154 ? -18.918 27.352  17.477 1.00 70.25  ? 167 PHE C C   1 
ATOM   6417 O  O   . PHE C  1  154 ? -18.748 28.166  16.574 1.00 64.63  ? 167 PHE C O   1 
ATOM   6418 C  CB  . PHE C  1  154 ? -16.977 27.107  19.094 1.00 68.35  ? 167 PHE C CB  1 
ATOM   6419 C  CG  . PHE C  1  154 ? -16.112 27.974  19.997 1.00 69.36  ? 167 PHE C CG  1 
ATOM   6420 C  CD1 . PHE C  1  154 ? -16.477 28.195  21.318 1.00 69.42  ? 167 PHE C CD1 1 
ATOM   6421 C  CD2 . PHE C  1  154 ? -14.929 28.551  19.535 1.00 68.88  ? 167 PHE C CD2 1 
ATOM   6422 C  CE1 . PHE C  1  154 ? -15.696 28.996  22.148 1.00 71.05  ? 167 PHE C CE1 1 
ATOM   6423 C  CE2 . PHE C  1  154 ? -14.147 29.340  20.375 1.00 68.93  ? 167 PHE C CE2 1 
ATOM   6424 C  CZ  . PHE C  1  154 ? -14.528 29.556  21.677 1.00 69.24  ? 167 PHE C CZ  1 
ATOM   6425 N  N   . SER C  1  155 ? -19.557 26.188  17.307 1.00 73.10  ? 168 SER C N   1 
ATOM   6426 C  CA  . SER C  1  155 ? -20.195 25.835  16.047 1.00 76.25  ? 168 SER C CA  1 
ATOM   6427 C  C   . SER C  1  155 ? -21.302 26.833  15.695 1.00 78.91  ? 168 SER C C   1 
ATOM   6428 O  O   . SER C  1  155 ? -21.481 27.186  14.528 1.00 75.25  ? 168 SER C O   1 
ATOM   6429 C  CB  . SER C  1  155 ? -20.743 24.429  16.086 1.00 78.43  ? 168 SER C CB  1 
ATOM   6430 O  OG  . SER C  1  155 ? -19.714 23.467  16.281 1.00 80.22  ? 168 SER C OG  1 
ATOM   6431 N  N   . ASN C  1  156 ? -22.071 27.262  16.705 1.00 76.05  ? 169 ASN C N   1 
ATOM   6432 C  CA  . ASN C  1  156 ? -23.114 28.254  16.497 1.00 76.14  ? 169 ASN C CA  1 
ATOM   6433 C  C   . ASN C  1  156 ? -22.499 29.601  16.124 1.00 75.27  ? 169 ASN C C   1 
ATOM   6434 O  O   . ASN C  1  156 ? -22.998 30.276  15.233 1.00 78.96  ? 169 ASN C O   1 
ATOM   6435 C  CB  . ASN C  1  156 ? -24.013 28.392  17.720 1.00 72.57  ? 169 ASN C CB  1 
ATOM   6436 C  CG  . ASN C  1  156 ? -24.908 27.185  17.921 1.00 73.92  ? 169 ASN C CG  1 
ATOM   6437 O  OD1 . ASN C  1  156 ? -25.245 26.466  16.973 1.00 73.63  ? 169 ASN C OD1 1 
ATOM   6438 N  ND2 . ASN C  1  156 ? -25.347 26.957  19.148 1.00 68.23  ? 169 ASN C ND2 1 
ATOM   6439 N  N   . ARG C  1  157 ? -21.421 29.989  16.812 1.00 74.50  ? 170 ARG C N   1 
ATOM   6440 C  CA  . ARG C  1  157 ? -20.865 31.327  16.676 1.00 77.30  ? 170 ARG C CA  1 
ATOM   6441 C  C   . ARG C  1  157 ? -20.101 31.483  15.362 1.00 73.61  ? 170 ARG C C   1 
ATOM   6442 O  O   . ARG C  1  157 ? -20.066 32.579  14.813 1.00 75.16  ? 170 ARG C O   1 
ATOM   6443 C  CB  . ARG C  1  157 ? -19.951 31.653  17.859 1.00 79.60  ? 170 ARG C CB  1 
ATOM   6444 C  CG  . ARG C  1  157 ? -19.759 33.145  18.107 1.00 83.79  ? 170 ARG C CG  1 
ATOM   6445 C  CD  . ARG C  1  157 ? -18.642 33.449  19.093 1.00 80.13  ? 170 ARG C CD  1 
ATOM   6446 N  NE  . ARG C  1  157 ? -18.741 32.633  20.311 1.00 79.54  ? 170 ARG C NE  1 
ATOM   6447 C  CZ  . ARG C  1  157 ? -17.812 32.455  21.243 1.00 73.75  ? 170 ARG C CZ  1 
ATOM   6448 N  NH1 . ARG C  1  157 ? -16.629 33.040  21.135 1.00 72.15  ? 170 ARG C NH1 1 
ATOM   6449 N  NH2 . ARG C  1  157 ? -18.085 31.674  22.277 1.00 73.04  ? 170 ARG C NH2 1 
ATOM   6450 N  N   . TYR C  1  158 ? -19.494 30.399  14.859 1.00 78.80  ? 171 TYR C N   1 
ATOM   6451 C  CA  . TYR C  1  158 ? -18.532 30.506  13.770 1.00 80.92  ? 171 TYR C CA  1 
ATOM   6452 C  C   . TYR C  1  158 ? -18.849 29.604  12.576 1.00 79.04  ? 171 TYR C C   1 
ATOM   6453 O  O   . TYR C  1  158 ? -18.206 29.746  11.539 1.00 78.29  ? 171 TYR C O   1 
ATOM   6454 C  CB  . TYR C  1  158 ? -17.138 30.165  14.298 1.00 83.46  ? 171 TYR C CB  1 
ATOM   6455 C  CG  . TYR C  1  158 ? -16.638 31.145  15.346 1.00 84.06  ? 171 TYR C CG  1 
ATOM   6456 C  CD1 . TYR C  1  158 ? -16.339 32.456  15.001 1.00 84.67  ? 171 TYR C CD1 1 
ATOM   6457 C  CD2 . TYR C  1  158 ? -16.453 30.756  16.665 1.00 87.74  ? 171 TYR C CD2 1 
ATOM   6458 C  CE1 . TYR C  1  158 ? -15.870 33.360  15.940 1.00 89.87  ? 171 TYR C CE1 1 
ATOM   6459 C  CE2 . TYR C  1  158 ? -15.982 31.647  17.617 1.00 91.21  ? 171 TYR C CE2 1 
ATOM   6460 C  CZ  . TYR C  1  158 ? -15.692 32.954  17.253 1.00 92.77  ? 171 TYR C CZ  1 
ATOM   6461 O  OH  . TYR C  1  158 ? -15.234 33.830  18.197 1.00 93.00  ? 171 TYR C OH  1 
ATOM   6462 N  N   . GLY C  1  159 ? -19.812 28.680  12.704 1.00 79.06  ? 172 GLY C N   1 
ATOM   6463 C  CA  . GLY C  1  159 ? -20.029 27.691  11.659 1.00 76.35  ? 172 GLY C CA  1 
ATOM   6464 C  C   . GLY C  1  159 ? -21.495 27.525  11.266 1.00 72.63  ? 172 GLY C C   1 
ATOM   6465 O  O   . GLY C  1  159 ? -21.854 26.528  10.641 1.00 62.10  ? 172 GLY C O   1 
ATOM   6466 N  N   . GLY C  1  160 ? -22.343 28.500  11.616 1.00 71.49  ? 173 GLY C N   1 
ATOM   6467 C  CA  . GLY C  1  160 ? -23.745 28.452  11.234 1.00 65.10  ? 173 GLY C CA  1 
ATOM   6468 C  C   . GLY C  1  160 ? -24.495 27.317  11.931 1.00 66.49  ? 173 GLY C C   1 
ATOM   6469 O  O   . GLY C  1  160 ? -25.535 26.878  11.445 1.00 66.73  ? 173 GLY C O   1 
ATOM   6470 N  N   . GLY C  1  161 ? -23.964 26.854  13.071 1.00 66.07  ? 174 GLY C N   1 
ATOM   6471 C  CA  . GLY C  1  161 ? -24.560 25.758  13.820 1.00 68.68  ? 174 GLY C CA  1 
ATOM   6472 C  C   . GLY C  1  161 ? -23.958 24.396  13.476 1.00 69.42  ? 174 GLY C C   1 
ATOM   6473 O  O   . GLY C  1  161 ? -24.458 23.367  13.939 1.00 64.25  ? 174 GLY C O   1 
ATOM   6474 N  N   . PHE C  1  162 ? -22.897 24.405  12.656 1.00 72.24  ? 175 PHE C N   1 
ATOM   6475 C  CA  . PHE C  1  162 ? -22.188 23.205  12.241 1.00 72.75  ? 175 PHE C CA  1 
ATOM   6476 C  C   . PHE C  1  162 ? -20.706 23.371  12.565 1.00 67.80  ? 175 PHE C C   1 
ATOM   6477 O  O   . PHE C  1  162 ? -20.219 24.492  12.677 1.00 65.96  ? 175 PHE C O   1 
ATOM   6478 C  CB  . PHE C  1  162 ? -22.369 22.992  10.738 1.00 73.99  ? 175 PHE C CB  1 
ATOM   6479 C  CG  . PHE C  1  162 ? -23.799 22.733  10.287 1.00 75.00  ? 175 PHE C CG  1 
ATOM   6480 C  CD1 . PHE C  1  162 ? -24.275 21.433  10.191 1.00 77.20  ? 175 PHE C CD1 1 
ATOM   6481 C  CD2 . PHE C  1  162 ? -24.651 23.772  9.924  1.00 77.97  ? 175 PHE C CD2 1 
ATOM   6482 C  CE1 . PHE C  1  162 ? -25.566 21.170  9.756  1.00 76.06  ? 175 PHE C CE1 1 
ATOM   6483 C  CE2 . PHE C  1  162 ? -25.949 23.508  9.502  1.00 80.46  ? 175 PHE C CE2 1 
ATOM   6484 C  CZ  . PHE C  1  162 ? -26.404 22.207  9.422  1.00 77.27  ? 175 PHE C CZ  1 
ATOM   6485 N  N   . TYR C  1  163 ? -19.988 22.248  12.693 1.00 65.05  ? 176 TYR C N   1 
ATOM   6486 C  CA  . TYR C  1  163 ? -18.545 22.290  12.880 1.00 60.91  ? 176 TYR C CA  1 
ATOM   6487 C  C   . TYR C  1  163 ? -17.883 22.256  11.507 1.00 61.02  ? 176 TYR C C   1 
ATOM   6488 O  O   . TYR C  1  163 ? -18.077 21.298  10.760 1.00 61.22  ? 176 TYR C O   1 
ATOM   6489 C  CB  . TYR C  1  163 ? -18.082 21.125  13.761 1.00 61.55  ? 176 TYR C CB  1 
ATOM   6490 C  CG  . TYR C  1  163 ? -16.609 21.138  14.156 1.00 60.69  ? 176 TYR C CG  1 
ATOM   6491 C  CD1 . TYR C  1  163 ? -16.152 21.918  15.212 1.00 58.65  ? 176 TYR C CD1 1 
ATOM   6492 C  CD2 . TYR C  1  163 ? -15.679 20.343  13.493 1.00 59.85  ? 176 TYR C CD2 1 
ATOM   6493 C  CE1 . TYR C  1  163 ? -14.816 21.916  15.588 1.00 61.87  ? 176 TYR C CE1 1 
ATOM   6494 C  CE2 . TYR C  1  163 ? -14.340 20.342  13.845 1.00 59.37  ? 176 TYR C CE2 1 
ATOM   6495 C  CZ  . TYR C  1  163 ? -13.910 21.114  14.909 1.00 59.59  ? 176 TYR C CZ  1 
ATOM   6496 O  OH  . TYR C  1  163 ? -12.588 21.095  15.248 1.00 57.33  ? 176 TYR C OH  1 
ATOM   6497 N  N   . ASN C  1  164 ? -17.126 23.313  11.193 1.00 60.97  ? 177 ASN C N   1 
ATOM   6498 C  CA  . ASN C  1  164 ? -16.359 23.398  9.961  1.00 64.35  ? 177 ASN C CA  1 
ATOM   6499 C  C   . ASN C  1  164 ? -14.974 23.942  10.300 1.00 64.05  ? 177 ASN C C   1 
ATOM   6500 O  O   . ASN C  1  164 ? -14.669 24.127  11.477 1.00 66.41  ? 177 ASN C O   1 
ATOM   6501 C  CB  . ASN C  1  164 ? -17.125 24.182  8.901  1.00 69.38  ? 177 ASN C CB  1 
ATOM   6502 C  CG  . ASN C  1  164 ? -17.120 25.681  9.117  1.00 75.53  ? 177 ASN C CG  1 
ATOM   6503 O  OD1 . ASN C  1  164 ? -16.443 26.210  10.016 1.00 78.09  ? 177 ASN C OD1 1 
ATOM   6504 N  ND2 . ASN C  1  164 ? -17.876 26.369  8.270  1.00 83.53  ? 177 ASN C ND2 1 
ATOM   6505 N  N   . LEU C  1  165 ? -14.156 24.208  9.268  1.00 63.42  ? 178 LEU C N   1 
ATOM   6506 C  CA  . LEU C  1  165 ? -12.748 24.533  9.444  1.00 70.66  ? 178 LEU C CA  1 
ATOM   6507 C  C   . LEU C  1  165 ? -12.584 25.835  10.235 1.00 71.95  ? 178 LEU C C   1 
ATOM   6508 O  O   . LEU C  1  165 ? -11.648 25.963  11.022 1.00 74.44  ? 178 LEU C O   1 
ATOM   6509 C  CB  . LEU C  1  165 ? -12.081 24.619  8.070  1.00 74.85  ? 178 LEU C CB  1 
ATOM   6510 C  CG  . LEU C  1  165 ? -10.609 25.045  8.058  1.00 83.10  ? 178 LEU C CG  1 
ATOM   6511 C  CD1 . LEU C  1  165 ? -9.739  23.961  8.666  1.00 81.11  ? 178 LEU C CD1 1 
ATOM   6512 C  CD2 . LEU C  1  165 ? -10.143 25.433  6.674  1.00 85.43  ? 178 LEU C CD2 1 
ATOM   6513 N  N   . THR C  1  166 ? -13.474 26.810  10.013 1.00 74.39  ? 179 THR C N   1 
ATOM   6514 C  CA  . THR C  1  166 ? -13.397 28.065  10.745 1.00 75.58  ? 179 THR C CA  1 
ATOM   6515 C  C   . THR C  1  166 ? -13.594 27.790  12.235 1.00 64.57  ? 179 THR C C   1 
ATOM   6516 O  O   . THR C  1  166 ? -12.877 28.338  13.063 1.00 65.67  ? 179 THR C O   1 
ATOM   6517 C  CB  . THR C  1  166 ? -14.416 29.082  10.234 1.00 83.71  ? 179 THR C CB  1 
ATOM   6518 O  OG1 . THR C  1  166 ? -14.400 29.042  8.809  1.00 84.11  ? 179 THR C OG1 1 
ATOM   6519 C  CG2 . THR C  1  166 ? -14.075 30.482  10.718 1.00 86.15  ? 179 THR C CG2 1 
ATOM   6520 N  N   . VAL C  1  167 ? -14.544 26.913  12.562 1.00 58.53  ? 180 VAL C N   1 
ATOM   6521 C  CA  . VAL C  1  167 ? -14.847 26.597  13.952 1.00 64.64  ? 180 VAL C CA  1 
ATOM   6522 C  C   . VAL C  1  167 ? -13.644 25.911  14.601 1.00 66.68  ? 180 VAL C C   1 
ATOM   6523 O  O   . VAL C  1  167 ? -13.305 26.201  15.746 1.00 66.39  ? 180 VAL C O   1 
ATOM   6524 C  CB  . VAL C  1  167 ? -16.110 25.729  14.097 1.00 61.85  ? 180 VAL C CB  1 
ATOM   6525 C  CG1 . VAL C  1  167 ? -16.484 25.516  15.560 1.00 64.11  ? 180 VAL C CG1 1 
ATOM   6526 C  CG2 . VAL C  1  167 ? -17.300 26.304  13.342 1.00 63.54  ? 180 VAL C CG2 1 
ATOM   6527 N  N   . ALA C  1  168 ? -13.006 25.003  13.854 1.00 70.00  ? 181 ALA C N   1 
ATOM   6528 C  CA  . ALA C  1  168 ? -11.838 24.274  14.330 1.00 69.13  ? 181 ALA C CA  1 
ATOM   6529 C  C   . ALA C  1  168 ? -10.739 25.238  14.766 1.00 63.42  ? 181 ALA C C   1 
ATOM   6530 O  O   . ALA C  1  168 ? -10.184 25.095  15.849 1.00 69.43  ? 181 ALA C O   1 
ATOM   6531 C  CB  . ALA C  1  168 ? -11.341 23.323  13.258 1.00 71.32  ? 181 ALA C CB  1 
ATOM   6532 N  N   . GLY C  1  169 ? -10.445 26.227  13.920 1.00 62.42  ? 182 GLY C N   1 
ATOM   6533 C  CA  . GLY C  1  169 ? -9.423  27.218  14.228 1.00 68.13  ? 182 GLY C CA  1 
ATOM   6534 C  C   . GLY C  1  169 ? -9.725  27.949  15.535 1.00 71.05  ? 182 GLY C C   1 
ATOM   6535 O  O   . GLY C  1  169 ? -8.836  28.124  16.361 1.00 76.90  ? 182 GLY C O   1 
ATOM   6536 N  N   . GLU C  1  170 ? -10.985 28.360  15.719 1.00 67.40  ? 183 GLU C N   1 
ATOM   6537 C  CA  . GLU C  1  170 ? -11.381 29.126  16.888 1.00 71.22  ? 183 GLU C CA  1 
ATOM   6538 C  C   . GLU C  1  170 ? -11.382 28.237  18.131 1.00 69.95  ? 183 GLU C C   1 
ATOM   6539 O  O   . GLU C  1  170 ? -10.899 28.652  19.181 1.00 73.27  ? 183 GLU C O   1 
ATOM   6540 C  CB  . GLU C  1  170 ? -12.740 29.804  16.675 1.00 74.01  ? 183 GLU C CB  1 
ATOM   6541 C  CG  . GLU C  1  170 ? -12.736 30.879  15.592 1.00 76.07  ? 183 GLU C CG  1 
ATOM   6542 C  CD  . GLU C  1  170 ? -11.601 31.882  15.726 1.00 77.08  ? 183 GLU C CD  1 
ATOM   6543 O  OE1 . GLU C  1  170 ? -11.482 32.484  16.806 1.00 83.22  ? 183 GLU C OE1 1 
ATOM   6544 O  OE2 . GLU C  1  170 ? -10.819 32.044  14.773 1.00 85.40  ? 183 GLU C OE2 1 
ATOM   6545 N  N   . LEU C  1  171 ? -11.920 27.018  18.019 1.00 69.66  ? 184 LEU C N   1 
ATOM   6546 C  CA  . LEU C  1  171 ? -12.103 26.170  19.187 1.00 66.55  ? 184 LEU C CA  1 
ATOM   6547 C  C   . LEU C  1  171 ? -10.746 25.706  19.712 1.00 65.20  ? 184 LEU C C   1 
ATOM   6548 O  O   . LEU C  1  171 ? -10.532 25.673  20.917 1.00 64.76  ? 184 LEU C O   1 
ATOM   6549 C  CB  . LEU C  1  171 ? -13.013 24.987  18.865 1.00 67.79  ? 184 LEU C CB  1 
ATOM   6550 C  CG  . LEU C  1  171 ? -13.290 24.020  20.024 1.00 68.19  ? 184 LEU C CG  1 
ATOM   6551 C  CD1 . LEU C  1  171 ? -13.994 24.692  21.190 1.00 68.71  ? 184 LEU C CD1 1 
ATOM   6552 C  CD2 . LEU C  1  171 ? -14.103 22.826  19.559 1.00 68.76  ? 184 LEU C CD2 1 
ATOM   6553 N  N   . ARG C  1  172 ? -9.845  25.337  18.796 1.00 64.03  ? 185 ARG C N   1 
ATOM   6554 C  CA  . ARG C  1  172 ? -8.515  24.862  19.154 1.00 68.12  ? 185 ARG C CA  1 
ATOM   6555 C  C   . ARG C  1  172 ? -7.814  25.896  20.035 1.00 70.97  ? 185 ARG C C   1 
ATOM   6556 O  O   . ARG C  1  172 ? -7.309  25.559  21.107 1.00 68.10  ? 185 ARG C O   1 
ATOM   6557 C  CB  . ARG C  1  172 ? -7.739  24.523  17.871 1.00 65.04  ? 185 ARG C CB  1 
ATOM   6558 C  CG  . ARG C  1  172 ? -6.221  24.428  17.940 1.00 63.82  ? 185 ARG C CG  1 
ATOM   6559 C  CD  . ARG C  1  172 ? -5.700  23.504  19.021 1.00 63.83  ? 185 ARG C CD  1 
ATOM   6560 N  NE  . ARG C  1  172 ? -6.361  22.197  19.067 1.00 64.02  ? 185 ARG C NE  1 
ATOM   6561 C  CZ  . ARG C  1  172 ? -6.832  21.613  20.170 1.00 66.70  ? 185 ARG C CZ  1 
ATOM   6562 N  NH1 . ARG C  1  172 ? -6.696  22.191  21.356 1.00 66.94  ? 185 ARG C NH1 1 
ATOM   6563 N  NH2 . ARG C  1  172 ? -7.437  20.442  20.080 1.00 64.50  ? 185 ARG C NH2 1 
ATOM   6564 N  N   . TYR C  1  173 ? -7.784  27.149  19.567 1.00 74.84  ? 186 TYR C N   1 
ATOM   6565 C  CA  . TYR C  1  173 ? -7.109  28.222  20.280 1.00 77.52  ? 186 TYR C CA  1 
ATOM   6566 C  C   . TYR C  1  173 ? -7.757  28.440  21.647 1.00 73.56  ? 186 TYR C C   1 
ATOM   6567 O  O   . TYR C  1  173 ? -7.065  28.556  22.658 1.00 69.10  ? 186 TYR C O   1 
ATOM   6568 C  CB  . TYR C  1  173 ? -7.139  29.497  19.434 1.00 80.64  ? 186 TYR C CB  1 
ATOM   6569 C  CG  . TYR C  1  173 ? -6.352  30.644  20.047 1.00 91.17  ? 186 TYR C CG  1 
ATOM   6570 C  CD1 . TYR C  1  173 ? -4.974  30.550  20.212 1.00 93.22  ? 186 TYR C CD1 1 
ATOM   6571 C  CD2 . TYR C  1  173 ? -6.975  31.822  20.443 1.00 96.98  ? 186 TYR C CD2 1 
ATOM   6572 C  CE1 . TYR C  1  173 ? -4.241  31.588  20.760 1.00 97.14  ? 186 TYR C CE1 1 
ATOM   6573 C  CE2 . TYR C  1  173 ? -6.248  32.874  20.983 1.00 98.89  ? 186 TYR C CE2 1 
ATOM   6574 C  CZ  . TYR C  1  173 ? -4.877  32.756  21.139 1.00 99.73  ? 186 TYR C CZ  1 
ATOM   6575 O  OH  . TYR C  1  173 ? -4.149  33.774  21.676 1.00 105.56 ? 186 TYR C OH  1 
ATOM   6576 N  N   . SER C  1  174 ? -9.093  28.478  21.672 1.00 66.60  ? 187 SER C N   1 
ATOM   6577 C  CA  . SER C  1  174 ? -9.823  28.777  22.892 1.00 70.51  ? 187 SER C CA  1 
ATOM   6578 C  C   . SER C  1  174 ? -9.564  27.706  23.949 1.00 72.00  ? 187 SER C C   1 
ATOM   6579 O  O   . SER C  1  174 ? -9.406  28.026  25.128 1.00 72.67  ? 187 SER C O   1 
ATOM   6580 C  CB  . SER C  1  174 ? -11.299 28.934  22.618 1.00 72.69  ? 187 SER C CB  1 
ATOM   6581 O  OG  . SER C  1  174 ? -11.998 29.216  23.819 1.00 73.49  ? 187 SER C OG  1 
ATOM   6582 N  N   . ARG C  1  175 ? -9.503  26.440  23.511 1.00 70.07  ? 188 ARG C N   1 
ATOM   6583 C  CA  . ARG C  1  175 ? -9.254  25.322  24.410 1.00 65.94  ? 188 ARG C CA  1 
ATOM   6584 C  C   . ARG C  1  175 ? -7.833  25.397  24.961 1.00 62.88  ? 188 ARG C C   1 
ATOM   6585 O  O   . ARG C  1  175 ? -7.603  25.017  26.106 1.00 64.20  ? 188 ARG C O   1 
ATOM   6586 C  CB  . ARG C  1  175 ? -9.513  23.967  23.741 1.00 64.15  ? 188 ARG C CB  1 
ATOM   6587 C  CG  . ARG C  1  175 ? -10.985 23.722  23.431 1.00 65.42  ? 188 ARG C CG  1 
ATOM   6588 C  CD  . ARG C  1  175 ? -11.837 23.518  24.667 1.00 67.37  ? 188 ARG C CD  1 
ATOM   6589 N  NE  . ARG C  1  175 ? -11.368 22.337  25.399 1.00 69.59  ? 188 ARG C NE  1 
ATOM   6590 C  CZ  . ARG C  1  175 ? -10.799 22.313  26.598 1.00 72.52  ? 188 ARG C CZ  1 
ATOM   6591 N  NH1 . ARG C  1  175 ? -10.750 23.393  27.365 1.00 76.11  ? 188 ARG C NH1 1 
ATOM   6592 N  NH2 . ARG C  1  175 ? -10.293 21.177  27.039 1.00 71.57  ? 188 ARG C NH2 1 
ATOM   6593 N  N   . ILE C  1  176 ? -6.885  25.882  24.151 1.00 61.60  ? 189 ILE C N   1 
ATOM   6594 C  CA  . ILE C  1  176 ? -5.529  26.101  24.634 1.00 66.29  ? 189 ILE C CA  1 
ATOM   6595 C  C   . ILE C  1  176 ? -5.571  27.140  25.758 1.00 67.13  ? 189 ILE C C   1 
ATOM   6596 O  O   . ILE C  1  176 ? -4.991  26.935  26.824 1.00 63.22  ? 189 ILE C O   1 
ATOM   6597 C  CB  . ILE C  1  176 ? -4.578  26.509  23.491 1.00 64.64  ? 189 ILE C CB  1 
ATOM   6598 C  CG1 . ILE C  1  176 ? -4.321  25.340  22.526 1.00 67.17  ? 189 ILE C CG1 1 
ATOM   6599 C  CG2 . ILE C  1  176 ? -3.266  27.066  24.048 1.00 64.86  ? 189 ILE C CG2 1 
ATOM   6600 C  CD1 . ILE C  1  176 ? -3.683  25.739  21.207 1.00 65.70  ? 189 ILE C CD1 1 
ATOM   6601 N  N   . GLN C  1  177 ? -6.285  28.244  25.514 1.00 73.18  ? 190 GLN C N   1 
ATOM   6602 C  CA  . GLN C  1  177 ? -6.393  29.323  26.485 1.00 76.50  ? 190 GLN C CA  1 
ATOM   6603 C  C   . GLN C  1  177 ? -7.019  28.821  27.786 1.00 71.18  ? 190 GLN C C   1 
ATOM   6604 O  O   . GLN C  1  177 ? -6.565  29.207  28.861 1.00 78.85  ? 190 GLN C O   1 
ATOM   6605 C  CB  . GLN C  1  177 ? -7.160  30.515  25.904 1.00 82.26  ? 190 GLN C CB  1 
ATOM   6606 C  CG  . GLN C  1  177 ? -6.432  31.260  24.784 1.00 83.26  ? 190 GLN C CG  1 
ATOM   6607 C  CD  . GLN C  1  177 ? -5.002  31.638  25.124 1.00 84.69  ? 190 GLN C CD  1 
ATOM   6608 O  OE1 . GLN C  1  177 ? -4.679  31.980  26.268 1.00 83.08  ? 190 GLN C OE1 1 
ATOM   6609 N  NE2 . GLN C  1  177 ? -4.110  31.552  24.145 1.00 84.89  ? 190 GLN C NE2 1 
ATOM   6610 N  N   . ASP C  1  178 ? -8.040  27.955  27.692 1.00 68.78  ? 191 ASP C N   1 
ATOM   6611 C  CA  . ASP C  1  178 ? -8.690  27.401  28.873 1.00 68.12  ? 191 ASP C CA  1 
ATOM   6612 C  C   . ASP C  1  178 ? -7.666  26.680  29.753 1.00 72.33  ? 191 ASP C C   1 
ATOM   6613 O  O   . ASP C  1  178 ? -7.635  26.868  30.971 1.00 69.55  ? 191 ASP C O   1 
ATOM   6614 C  CB  . ASP C  1  178 ? -9.808  26.430  28.520 1.00 67.95  ? 191 ASP C CB  1 
ATOM   6615 C  CG  . ASP C  1  178 ? -11.029 27.014  27.816 1.00 71.77  ? 191 ASP C CG  1 
ATOM   6616 O  OD1 . ASP C  1  178 ? -11.150 28.255  27.781 1.00 81.67  ? 191 ASP C OD1 1 
ATOM   6617 O  OD2 . ASP C  1  178 ? -11.849 26.224  27.289 1.00 68.23  ? 191 ASP C OD2 1 
ATOM   6618 N  N   . SER C  1  179 ? -6.844  25.833  29.124 1.00 69.78  ? 192 SER C N   1 
ATOM   6619 C  CA  . SER C  1  179 ? -5.871  25.027  29.844 1.00 71.04  ? 192 SER C CA  1 
ATOM   6620 C  C   . SER C  1  179 ? -4.774  25.899  30.457 1.00 72.61  ? 192 SER C C   1 
ATOM   6621 O  O   . SER C  1  179 ? -4.325  25.630  31.568 1.00 72.28  ? 192 SER C O   1 
ATOM   6622 C  CB  . SER C  1  179 ? -5.290  23.944  28.954 1.00 69.41  ? 192 SER C CB  1 
ATOM   6623 O  OG  . SER C  1  179 ? -6.239  22.912  28.724 1.00 64.56  ? 192 SER C OG  1 
ATOM   6624 N  N   . ILE C  1  180 ? -4.333  26.939  29.735 1.00 74.94  ? 193 ILE C N   1 
ATOM   6625 C  CA  . ILE C  1  180 ? -3.348  27.866  30.276 1.00 76.92  ? 193 ILE C CA  1 
ATOM   6626 C  C   . ILE C  1  180 ? -3.885  28.457  31.581 1.00 79.18  ? 193 ILE C C   1 
ATOM   6627 O  O   . ILE C  1  180 ? -3.187  28.468  32.593 1.00 79.22  ? 193 ILE C O   1 
ATOM   6628 C  CB  . ILE C  1  180 ? -2.995  28.967  29.258 1.00 75.12  ? 193 ILE C CB  1 
ATOM   6629 C  CG1 . ILE C  1  180 ? -2.190  28.406  28.088 1.00 74.47  ? 193 ILE C CG1 1 
ATOM   6630 C  CG2 . ILE C  1  180 ? -2.261  30.126  29.937 1.00 74.16  ? 193 ILE C CG2 1 
ATOM   6631 C  CD1 . ILE C  1  180 ? -2.079  29.345  26.903 1.00 74.64  ? 193 ILE C CD1 1 
ATOM   6632 N  N   . ALA C  1  181 ? -5.144  28.914  31.542 1.00 78.51  ? 194 ALA C N   1 
ATOM   6633 C  CA  . ALA C  1  181 ? -5.742  29.655  32.638 1.00 78.93  ? 194 ALA C CA  1 
ATOM   6634 C  C   . ALA C  1  181 ? -6.043  28.764  33.843 1.00 82.32  ? 194 ALA C C   1 
ATOM   6635 O  O   . ALA C  1  181 ? -6.050  29.253  34.970 1.00 86.20  ? 194 ALA C O   1 
ATOM   6636 C  CB  . ALA C  1  181 ? -6.996  30.354  32.156 1.00 74.82  ? 194 ALA C CB  1 
ATOM   6637 N  N   . THR C  1  182 ? -6.315  27.469  33.616 1.00 81.16  ? 195 THR C N   1 
ATOM   6638 C  CA  . THR C  1  182 ? -6.925  26.652  34.659 1.00 81.28  ? 195 THR C CA  1 
ATOM   6639 C  C   . THR C  1  182 ? -6.069  25.446  35.049 1.00 80.16  ? 195 THR C C   1 
ATOM   6640 O  O   . THR C  1  182 ? -6.330  24.834  36.080 1.00 71.63  ? 195 THR C O   1 
ATOM   6641 C  CB  . THR C  1  182 ? -8.316  26.203  34.211 1.00 84.47  ? 195 THR C CB  1 
ATOM   6642 O  OG1 . THR C  1  182 ? -8.140  25.403  33.047 1.00 84.62  ? 195 THR C OG1 1 
ATOM   6643 C  CG2 . THR C  1  182 ? -9.243  27.367  33.908 1.00 85.00  ? 195 THR C CG2 1 
ATOM   6644 N  N   . ASN C  1  183 ? -5.075  25.078  34.236 1.00 80.84  ? 196 ASN C N   1 
ATOM   6645 C  CA  . ASN C  1  183 ? -4.339  23.846  34.471 1.00 75.47  ? 196 ASN C CA  1 
ATOM   6646 C  C   . ASN C  1  183 ? -2.871  24.188  34.682 1.00 73.30  ? 196 ASN C C   1 
ATOM   6647 O  O   . ASN C  1  183 ? -2.169  24.514  33.729 1.00 70.51  ? 196 ASN C O   1 
ATOM   6648 C  CB  . ASN C  1  183 ? -4.542  22.848  33.335 1.00 76.74  ? 196 ASN C CB  1 
ATOM   6649 C  CG  . ASN C  1  183 ? -3.779  21.557  33.521 1.00 75.06  ? 196 ASN C CG  1 
ATOM   6650 O  OD1 . ASN C  1  183 ? -3.106  21.360  34.543 1.00 75.42  ? 196 ASN C OD1 1 
ATOM   6651 N  ND2 . ASN C  1  183 ? -3.876  20.666  32.539 1.00 72.21  ? 196 ASN C ND2 1 
ATOM   6652 N  N   . PRO C  1  184 ? -2.359  24.112  35.930 1.00 70.78  ? 197 PRO C N   1 
ATOM   6653 C  CA  . PRO C  1  184 ? -0.961  24.462  36.196 1.00 73.64  ? 197 PRO C CA  1 
ATOM   6654 C  C   . PRO C  1  184 ? 0.057   23.479  35.618 1.00 76.65  ? 197 PRO C C   1 
ATOM   6655 O  O   . PRO C  1  184 ? 1.233   23.823  35.494 1.00 74.63  ? 197 PRO C O   1 
ATOM   6656 C  CB  . PRO C  1  184 ? -0.898  24.518  37.733 1.00 74.05  ? 197 PRO C CB  1 
ATOM   6657 C  CG  . PRO C  1  184 ? -1.988  23.562  38.175 1.00 72.86  ? 197 PRO C CG  1 
ATOM   6658 C  CD  . PRO C  1  184 ? -3.094  23.679  37.133 1.00 71.95  ? 197 PRO C CD  1 
ATOM   6659 N  N   . GLU C  1  185 ? -0.405  22.264  35.274 1.00 73.86  ? 198 GLU C N   1 
ATOM   6660 C  CA  . GLU C  1  185 ? 0.443   21.218  34.719 1.00 74.30  ? 198 GLU C CA  1 
ATOM   6661 C  C   . GLU C  1  185 ? 0.275   21.126  33.200 1.00 69.58  ? 198 GLU C C   1 
ATOM   6662 O  O   . GLU C  1  185 ? 0.731   20.167  32.589 1.00 64.02  ? 198 GLU C O   1 
ATOM   6663 C  CB  . GLU C  1  185 ? 0.103   19.865  35.351 1.00 73.36  ? 198 GLU C CB  1 
ATOM   6664 C  CG  . GLU C  1  185 ? 0.404   19.774  36.846 1.00 71.34  ? 198 GLU C CG  1 
ATOM   6665 C  CD  . GLU C  1  185 ? -0.002  18.452  37.479 1.00 73.47  ? 198 GLU C CD  1 
ATOM   6666 O  OE1 . GLU C  1  185 ? -0.498  17.567  36.758 1.00 73.14  ? 198 GLU C OE1 1 
ATOM   6667 O  OE2 . GLU C  1  185 ? 0.153   18.295  38.707 1.00 77.74  ? 198 GLU C OE2 1 
ATOM   6668 N  N   . PHE C  1  186 ? -0.362  22.133  32.591 1.00 67.81  ? 199 PHE C N   1 
ATOM   6669 C  CA  . PHE C  1  186 ? -0.648  22.131  31.166 1.00 68.46  ? 199 PHE C CA  1 
ATOM   6670 C  C   . PHE C  1  186 ? 0.634   21.963  30.352 1.00 70.39  ? 199 PHE C C   1 
ATOM   6671 O  O   . PHE C  1  186 ? 1.584   22.730  30.518 1.00 64.55  ? 199 PHE C O   1 
ATOM   6672 C  CB  . PHE C  1  186 ? -1.314  23.449  30.764 1.00 66.35  ? 199 PHE C CB  1 
ATOM   6673 C  CG  . PHE C  1  186 ? -1.616  23.607  29.280 1.00 64.67  ? 199 PHE C CG  1 
ATOM   6674 C  CD1 . PHE C  1  186 ? -2.171  22.566  28.545 1.00 63.24  ? 199 PHE C CD1 1 
ATOM   6675 C  CD2 . PHE C  1  186 ? -1.340  24.800  28.619 1.00 61.88  ? 199 PHE C CD2 1 
ATOM   6676 C  CE1 . PHE C  1  186 ? -2.452  22.720  27.194 1.00 58.97  ? 199 PHE C CE1 1 
ATOM   6677 C  CE2 . PHE C  1  186 ? -1.619  24.948  27.268 1.00 61.09  ? 199 PHE C CE2 1 
ATOM   6678 C  CZ  . PHE C  1  186 ? -2.173  23.907  26.557 1.00 60.61  ? 199 PHE C CZ  1 
ATOM   6679 N  N   . GLN C  1  187 ? 0.618   20.970  29.450 1.00 72.52  ? 200 GLN C N   1 
ATOM   6680 C  CA  . GLN C  1  187 ? 1.700   20.721  28.508 1.00 70.36  ? 200 GLN C CA  1 
ATOM   6681 C  C   . GLN C  1  187 ? 1.125   20.690  27.095 1.00 65.77  ? 200 GLN C C   1 
ATOM   6682 O  O   . GLN C  1  187 ? 0.044   20.140  26.883 1.00 63.65  ? 200 GLN C O   1 
ATOM   6683 C  CB  . GLN C  1  187 ? 2.366   19.382  28.830 1.00 73.36  ? 200 GLN C CB  1 
ATOM   6684 C  CG  . GLN C  1  187 ? 3.147   19.371  30.141 1.00 76.66  ? 200 GLN C CG  1 
ATOM   6685 C  CD  . GLN C  1  187 ? 4.440   20.153  30.049 1.00 77.85  ? 200 GLN C CD  1 
ATOM   6686 O  OE1 . GLN C  1  187 ? 5.378   19.769  29.335 1.00 79.47  ? 200 GLN C OE1 1 
ATOM   6687 N  NE2 . GLN C  1  187 ? 4.496   21.276  30.754 1.00 75.50  ? 200 GLN C NE2 1 
ATOM   6688 N  N   . PHE C  1  188 ? 1.859   21.274  26.140 1.00 59.86  ? 201 PHE C N   1 
ATOM   6689 C  CA  . PHE C  1  188 ? 1.434   21.303  24.748 1.00 60.47  ? 201 PHE C CA  1 
ATOM   6690 C  C   . PHE C  1  188 ? 2.671   21.247  23.855 1.00 60.26  ? 201 PHE C C   1 
ATOM   6691 O  O   . PHE C  1  188 ? 2.939   22.173  23.096 1.00 61.69  ? 201 PHE C O   1 
ATOM   6692 C  CB  . PHE C  1  188 ? 0.563   22.544  24.549 1.00 57.44  ? 201 PHE C CB  1 
ATOM   6693 C  CG  . PHE C  1  188 ? -0.421  22.448  23.395 1.00 57.17  ? 201 PHE C CG  1 
ATOM   6694 C  CD1 . PHE C  1  188 ? -1.530  21.618  23.475 1.00 54.40  ? 201 PHE C CD1 1 
ATOM   6695 C  CD2 . PHE C  1  188 ? -0.265  23.228  22.256 1.00 56.49  ? 201 PHE C CD2 1 
ATOM   6696 C  CE1 . PHE C  1  188 ? -2.446  21.559  22.435 1.00 56.03  ? 201 PHE C CE1 1 
ATOM   6697 C  CE2 . PHE C  1  188 ? -1.188  23.172  21.223 1.00 53.02  ? 201 PHE C CE2 1 
ATOM   6698 C  CZ  . PHE C  1  188 ? -2.273  22.336  21.314 1.00 53.45  ? 201 PHE C CZ  1 
ATOM   6699 N  N   . LYS C  1  189 ? 3.394   20.125  23.955 1.00 61.78  ? 202 LYS C N   1 
ATOM   6700 C  CA  . LYS C  1  189 ? 4.705   19.930  23.354 1.00 65.96  ? 202 LYS C CA  1 
ATOM   6701 C  C   . LYS C  1  189 ? 4.740   18.607  22.591 1.00 60.00  ? 202 LYS C C   1 
ATOM   6702 O  O   . LYS C  1  189 ? 3.925   17.722  22.850 1.00 55.78  ? 202 LYS C O   1 
ATOM   6703 C  CB  . LYS C  1  189 ? 5.789   19.675  24.408 1.00 72.73  ? 202 LYS C CB  1 
ATOM   6704 C  CG  . LYS C  1  189 ? 6.208   20.783  25.345 1.00 77.20  ? 202 LYS C CG  1 
ATOM   6705 C  CD  . LYS C  1  189 ? 7.135   20.237  26.428 1.00 77.90  ? 202 LYS C CD  1 
ATOM   6706 C  CE  . LYS C  1  189 ? 7.660   21.280  27.356 1.00 83.07  ? 202 LYS C CE  1 
ATOM   6707 N  NZ  . LYS C  1  189 ? 8.294   20.637  28.511 1.00 85.85  ? 202 LYS C NZ  1 
ATOM   6708 N  N   . ASN C  1  190 ? 5.735   18.466  21.708 1.00 60.36  ? 203 ASN C N   1 
ATOM   6709 C  CA  . ASN C  1  190 ? 6.112   17.178  21.144 1.00 56.55  ? 203 ASN C CA  1 
ATOM   6710 C  C   . ASN C  1  190 ? 4.884   16.483  20.555 1.00 52.47  ? 203 ASN C C   1 
ATOM   6711 O  O   . ASN C  1  190 ? 4.231   17.052  19.691 1.00 48.68  ? 203 ASN C O   1 
ATOM   6712 C  CB  . ASN C  1  190 ? 6.897   16.376  22.173 1.00 58.15  ? 203 ASN C CB  1 
ATOM   6713 C  CG  . ASN C  1  190 ? 8.219   17.033  22.495 1.00 61.00  ? 203 ASN C CG  1 
ATOM   6714 O  OD1 . ASN C  1  190 ? 8.973   17.382  21.577 1.00 58.22  ? 203 ASN C OD1 1 
ATOM   6715 N  ND2 . ASN C  1  190 ? 8.513   17.222  23.773 1.00 59.43  ? 203 ASN C ND2 1 
ATOM   6716 N  N   . VAL C  1  191 ? 4.559   15.270  21.015 1.00 50.86  ? 204 VAL C N   1 
ATOM   6717 C  CA  . VAL C  1  191 ? 3.510   14.491  20.376 1.00 54.79  ? 204 VAL C CA  1 
ATOM   6718 C  C   . VAL C  1  191 ? 2.204   15.286  20.417 1.00 54.53  ? 204 VAL C C   1 
ATOM   6719 O  O   . VAL C  1  191 ? 1.519   15.418  19.404 1.00 56.30  ? 204 VAL C O   1 
ATOM   6720 C  CB  . VAL C  1  191 ? 3.312   13.111  21.033 1.00 53.66  ? 204 VAL C CB  1 
ATOM   6721 C  CG1 . VAL C  1  191 ? 2.107   12.376  20.450 1.00 50.99  ? 204 VAL C CG1 1 
ATOM   6722 C  CG2 . VAL C  1  191 ? 4.565   12.248  20.951 1.00 52.27  ? 204 VAL C CG2 1 
ATOM   6723 N  N   . ARG C  1  192 ? 1.862   15.817  21.596 1.00 54.63  ? 205 ARG C N   1 
ATOM   6724 C  CA  . ARG C  1  192 ? 0.564   16.438  21.780 1.00 54.28  ? 205 ARG C CA  1 
ATOM   6725 C  C   . ARG C  1  192 ? 0.403   17.630  20.840 1.00 52.66  ? 205 ARG C C   1 
ATOM   6726 O  O   . ARG C  1  192 ? -0.682  17.869  20.325 1.00 54.32  ? 205 ARG C O   1 
ATOM   6727 C  CB  . ARG C  1  192 ? 0.336   16.885  23.228 1.00 55.90  ? 205 ARG C CB  1 
ATOM   6728 C  CG  . ARG C  1  192 ? -1.044  17.490  23.449 1.00 55.24  ? 205 ARG C CG  1 
ATOM   6729 C  CD  . ARG C  1  192 ? -2.159  16.623  22.882 1.00 55.64  ? 205 ARG C CD  1 
ATOM   6730 N  NE  . ARG C  1  192 ? -3.495  17.210  23.033 1.00 58.14  ? 205 ARG C NE  1 
ATOM   6731 C  CZ  . ARG C  1  192 ? -4.590  16.798  22.396 1.00 59.03  ? 205 ARG C CZ  1 
ATOM   6732 N  NH1 . ARG C  1  192 ? -4.504  15.885  21.435 1.00 59.72  ? 205 ARG C NH1 1 
ATOM   6733 N  NH2 . ARG C  1  192 ? -5.770  17.312  22.719 1.00 57.34  ? 205 ARG C NH2 1 
ATOM   6734 N  N   . PHE C  1  193 ? 1.481   18.389  20.631 1.00 53.17  ? 206 PHE C N   1 
ATOM   6735 C  CA  . PHE C  1  193 ? 1.399   19.596  19.830 1.00 53.62  ? 206 PHE C CA  1 
ATOM   6736 C  C   . PHE C  1  193 ? 1.008   19.223  18.405 1.00 56.40  ? 206 PHE C C   1 
ATOM   6737 O  O   . PHE C  1  193 ? 0.232   19.935  17.777 1.00 55.71  ? 206 PHE C O   1 
ATOM   6738 C  CB  . PHE C  1  193 ? 2.708   20.388  19.846 1.00 54.94  ? 206 PHE C CB  1 
ATOM   6739 C  CG  . PHE C  1  193 ? 2.661   21.613  18.952 1.00 58.54  ? 206 PHE C CG  1 
ATOM   6740 C  CD1 . PHE C  1  193 ? 2.000   22.761  19.372 1.00 62.17  ? 206 PHE C CD1 1 
ATOM   6741 C  CD2 . PHE C  1  193 ? 3.262   21.609  17.700 1.00 62.90  ? 206 PHE C CD2 1 
ATOM   6742 C  CE1 . PHE C  1  193 ? 1.933   23.876  18.554 1.00 64.88  ? 206 PHE C CE1 1 
ATOM   6743 C  CE2 . PHE C  1  193 ? 3.201   22.732  16.887 1.00 68.24  ? 206 PHE C CE2 1 
ATOM   6744 C  CZ  . PHE C  1  193 ? 2.528   23.862  17.312 1.00 66.53  ? 206 PHE C CZ  1 
ATOM   6745 N  N   . ILE C  1  194 ? 1.532   18.092  17.916 1.00 52.57  ? 207 ILE C N   1 
ATOM   6746 C  CA  . ILE C  1  194 ? 1.264   17.667  16.554 1.00 51.08  ? 207 ILE C CA  1 
ATOM   6747 C  C   . ILE C  1  194 ? -0.137  17.058  16.470 1.00 48.04  ? 207 ILE C C   1 
ATOM   6748 O  O   . ILE C  1  194 ? -0.907  17.431  15.588 1.00 48.95  ? 207 ILE C O   1 
ATOM   6749 C  CB  . ILE C  1  194 ? 2.371   16.725  16.050 1.00 52.50  ? 207 ILE C CB  1 
ATOM   6750 C  CG1 . ILE C  1  194 ? 3.762   17.394  16.113 1.00 53.89  ? 207 ILE C CG1 1 
ATOM   6751 C  CG2 . ILE C  1  194 ? 2.058   16.210  14.648 1.00 53.40  ? 207 ILE C CG2 1 
ATOM   6752 C  CD1 . ILE C  1  194 ? 3.918   18.673  15.310 1.00 52.25  ? 207 ILE C CD1 1 
ATOM   6753 N  N   . THR C  1  195 ? -0.488  16.160  17.401 1.00 47.40  ? 208 THR C N   1 
ATOM   6754 C  CA  . THR C  1  195 ? -1.736  15.413  17.302 1.00 46.92  ? 208 THR C CA  1 
ATOM   6755 C  C   . THR C  1  195 ? -2.934  16.324  17.563 1.00 50.91  ? 208 THR C C   1 
ATOM   6756 O  O   . THR C  1  195 ? -4.031  16.041  17.098 1.00 53.05  ? 208 THR C O   1 
ATOM   6757 C  CB  . THR C  1  195 ? -1.755  14.215  18.254 1.00 50.51  ? 208 THR C CB  1 
ATOM   6758 O  OG1 . THR C  1  195 ? -1.616  14.705  19.587 1.00 50.71  ? 208 THR C OG1 1 
ATOM   6759 C  CG2 . THR C  1  195 ? -0.659  13.208  17.948 1.00 49.37  ? 208 THR C CG2 1 
ATOM   6760 N  N   . ALA C  1  196 ? -2.730  17.414  18.303 1.00 57.31  ? 209 ALA C N   1 
ATOM   6761 C  CA  . ALA C  1  196 ? -3.826  18.272  18.721 1.00 59.01  ? 209 ALA C CA  1 
ATOM   6762 C  C   . ALA C  1  196 ? -4.411  19.043  17.543 1.00 58.81  ? 209 ALA C C   1 
ATOM   6763 O  O   . ALA C  1  196 ? -5.576  19.430  17.598 1.00 66.15  ? 209 ALA C O   1 
ATOM   6764 C  CB  . ALA C  1  196 ? -3.364  19.226  19.803 1.00 61.99  ? 209 ALA C CB  1 
ATOM   6765 N  N   . TYR C  1  197 ? -3.618  19.277  16.491 1.00 56.22  ? 210 TYR C N   1 
ATOM   6766 C  CA  . TYR C  1  197 ? -4.117  20.003  15.332 1.00 55.90  ? 210 TYR C CA  1 
ATOM   6767 C  C   . TYR C  1  197 ? -4.837  19.029  14.403 1.00 54.28  ? 210 TYR C C   1 
ATOM   6768 O  O   . TYR C  1  197 ? -5.931  19.324  13.925 1.00 55.15  ? 210 TYR C O   1 
ATOM   6769 C  CB  . TYR C  1  197 ? -2.979  20.830  14.731 1.00 58.30  ? 210 TYR C CB  1 
ATOM   6770 C  CG  . TYR C  1  197 ? -2.746  22.080  15.567 1.00 64.10  ? 210 TYR C CG  1 
ATOM   6771 C  CD1 . TYR C  1  197 ? -3.509  23.229  15.371 1.00 65.27  ? 210 TYR C CD1 1 
ATOM   6772 C  CD2 . TYR C  1  197 ? -1.820  22.085  16.600 1.00 66.54  ? 210 TYR C CD2 1 
ATOM   6773 C  CE1 . TYR C  1  197 ? -3.322  24.360  16.150 1.00 68.79  ? 210 TYR C CE1 1 
ATOM   6774 C  CE2 . TYR C  1  197 ? -1.632  23.206  17.391 1.00 70.96  ? 210 TYR C CE2 1 
ATOM   6775 C  CZ  . TYR C  1  197 ? -2.387  24.345  17.168 1.00 70.21  ? 210 TYR C CZ  1 
ATOM   6776 O  OH  . TYR C  1  197 ? -2.200  25.443  17.951 1.00 77.02  ? 210 TYR C OH  1 
ATOM   6777 N  N   . GLY C  1  198 ? -4.239  17.855  14.173 1.00 51.04  ? 211 GLY C N   1 
ATOM   6778 C  CA  . GLY C  1  198 ? -4.885  16.820  13.383 1.00 49.43  ? 211 GLY C CA  1 
ATOM   6779 C  C   . GLY C  1  198 ? -6.268  16.457  13.921 1.00 47.64  ? 211 GLY C C   1 
ATOM   6780 O  O   . GLY C  1  198 ? -7.215  16.340  13.151 1.00 48.21  ? 211 GLY C O   1 
ATOM   6781 N  N   . GLU C  1  199 ? -6.389  16.306  15.247 1.00 50.43  ? 212 GLU C N   1 
ATOM   6782 C  CA  A GLU C  1  199 ? -7.623  15.825  15.845 0.50 49.88  ? 212 GLU C CA  1 
ATOM   6783 C  CA  B GLU C  1  199 ? -7.610  15.863  15.908 0.50 52.14  ? 212 GLU C CA  1 
ATOM   6784 C  C   . GLU C  1  199 ? -8.760  16.816  15.596 1.00 51.34  ? 212 GLU C C   1 
ATOM   6785 O  O   . GLU C  1  199 ? -9.915  16.401  15.569 1.00 51.18  ? 212 GLU C O   1 
ATOM   6786 C  CB  A GLU C  1  199 ? -7.409  15.449  17.312 0.50 49.08  ? 212 GLU C CB  1 
ATOM   6787 C  CB  B GLU C  1  199 ? -7.475  15.753  17.435 0.50 54.76  ? 212 GLU C CB  1 
ATOM   6788 C  CG  A GLU C  1  199 ? -6.634  14.140  17.473 0.50 48.24  ? 212 GLU C CG  1 
ATOM   6789 C  CG  B GLU C  1  199 ? -7.871  17.016  18.204 0.50 57.69  ? 212 GLU C CG  1 
ATOM   6790 C  CD  A GLU C  1  199 ? -5.995  13.929  18.831 0.50 47.55  ? 212 GLU C CD  1 
ATOM   6791 C  CD  B GLU C  1  199 ? -7.741  16.994  19.720 0.50 57.75  ? 212 GLU C CD  1 
ATOM   6792 O  OE1 A GLU C  1  199 ? -6.384  14.662  19.760 0.50 48.73  ? 212 GLU C OE1 1 
ATOM   6793 O  OE1 B GLU C  1  199 ? -7.418  15.949  20.322 0.50 57.58  ? 212 GLU C OE1 1 
ATOM   6794 O  OE2 A GLU C  1  199 ? -5.105  13.061  18.950 0.50 46.42  ? 212 GLU C OE2 1 
ATOM   6795 O  OE2 B GLU C  1  199 ? -7.974  18.069  20.304 0.50 57.84  ? 212 GLU C OE2 1 
ATOM   6796 N  N   . THR C  1  200 ? -8.442  18.106  15.391 1.00 51.47  ? 213 THR C N   1 
ATOM   6797 C  CA  . THR C  1  200 ? -9.488  19.111  15.224 1.00 56.73  ? 213 THR C CA  1 
ATOM   6798 C  C   . THR C  1  200 ? -10.097 19.058  13.825 1.00 57.07  ? 213 THR C C   1 
ATOM   6799 O  O   . THR C  1  200 ? -11.197 19.579  13.638 1.00 50.82  ? 213 THR C O   1 
ATOM   6800 C  CB  . THR C  1  200 ? -9.003  20.533  15.520 1.00 61.32  ? 213 THR C CB  1 
ATOM   6801 O  OG1 . THR C  1  200 ? -8.149  20.945  14.459 1.00 64.25  ? 213 THR C OG1 1 
ATOM   6802 C  CG2 . THR C  1  200 ? -8.261  20.645  16.836 1.00 60.18  ? 213 THR C CG2 1 
ATOM   6803 N  N   . VAL C  1  201 ? -9.393  18.460  12.847 1.00 55.37  ? 214 VAL C N   1 
ATOM   6804 C  CA  . VAL C  1  201 ? -9.926  18.367  11.492 1.00 52.78  ? 214 VAL C CA  1 
ATOM   6805 C  C   . VAL C  1  201 ? -10.477 16.970  11.202 1.00 49.81  ? 214 VAL C C   1 
ATOM   6806 O  O   . VAL C  1  201 ? -11.211 16.801  10.231 1.00 51.61  ? 214 VAL C O   1 
ATOM   6807 C  CB  . VAL C  1  201 ? -8.917  18.796  10.412 1.00 54.54  ? 214 VAL C CB  1 
ATOM   6808 C  CG1 . VAL C  1  201 ? -8.567  20.276  10.536 1.00 56.66  ? 214 VAL C CG1 1 
ATOM   6809 C  CG2 . VAL C  1  201 ? -7.654  17.947  10.412 1.00 54.02  ? 214 VAL C CG2 1 
ATOM   6810 N  N   . PHE C  1  202 ? -10.167 15.975  12.042 1.00 44.67  ? 215 PHE C N   1 
ATOM   6811 C  CA  . PHE C  1  202 ? -10.661 14.631  11.798 1.00 45.34  ? 215 PHE C CA  1 
ATOM   6812 C  C   . PHE C  1  202 ? -12.192 14.639  11.728 1.00 49.05  ? 215 PHE C C   1 
ATOM   6813 O  O   . PHE C  1  202 ? -12.771 13.951  10.891 1.00 50.88  ? 215 PHE C O   1 
ATOM   6814 C  CB  . PHE C  1  202 ? -10.161 13.611  12.825 1.00 47.52  ? 215 PHE C CB  1 
ATOM   6815 C  CG  . PHE C  1  202 ? -8.677  13.259  12.782 1.00 44.79  ? 215 PHE C CG  1 
ATOM   6816 C  CD1 . PHE C  1  202 ? -7.870  13.599  11.700 1.00 43.80  ? 215 PHE C CD1 1 
ATOM   6817 C  CD2 . PHE C  1  202 ? -8.101  12.548  13.827 1.00 46.06  ? 215 PHE C CD2 1 
ATOM   6818 C  CE1 . PHE C  1  202 ? -6.519  13.273  11.689 1.00 44.71  ? 215 PHE C CE1 1 
ATOM   6819 C  CE2 . PHE C  1  202 ? -6.751  12.212  13.811 1.00 48.10  ? 215 PHE C CE2 1 
ATOM   6820 C  CZ  . PHE C  1  202 ? -5.960  12.580  12.750 1.00 47.11  ? 215 PHE C CZ  1 
ATOM   6821 N  N   . PRO C  1  203 ? -12.916 15.397  12.582 1.00 50.85  ? 216 PRO C N   1 
ATOM   6822 C  CA  . PRO C  1  203 ? -14.376 15.466  12.487 1.00 51.58  ? 216 PRO C CA  1 
ATOM   6823 C  C   . PRO C  1  203 ? -14.877 15.928  11.121 1.00 49.80  ? 216 PRO C C   1 
ATOM   6824 O  O   . PRO C  1  203 ? -15.901 15.449  10.645 1.00 57.08  ? 216 PRO C O   1 
ATOM   6825 C  CB  . PRO C  1  203 ? -14.770 16.454  13.606 1.00 50.81  ? 216 PRO C CB  1 
ATOM   6826 C  CG  . PRO C  1  203 ? -13.627 16.387  14.582 1.00 51.16  ? 216 PRO C CG  1 
ATOM   6827 C  CD  . PRO C  1  203 ? -12.395 16.180  13.708 1.00 53.04  ? 216 PRO C CD  1 
ATOM   6828 N  N   . ILE C  1  204 ? -14.148 16.862  10.500 1.00 50.01  ? 217 ILE C N   1 
ATOM   6829 C  CA  . ILE C  1  204 ? -14.525 17.396  9.201  1.00 50.09  ? 217 ILE C CA  1 
ATOM   6830 C  C   . ILE C  1  204 ? -14.235 16.363  8.114  1.00 49.11  ? 217 ILE C C   1 
ATOM   6831 O  O   . ILE C  1  204 ? -15.087 16.104  7.269  1.00 45.97  ? 217 ILE C O   1 
ATOM   6832 C  CB  . ILE C  1  204 ? -13.798 18.722  8.911  1.00 54.75  ? 217 ILE C CB  1 
ATOM   6833 C  CG1 . ILE C  1  204 ? -14.098 19.777  9.991  1.00 56.32  ? 217 ILE C CG1 1 
ATOM   6834 C  CG2 . ILE C  1  204 ? -14.149 19.225  7.506  1.00 54.40  ? 217 ILE C CG2 1 
ATOM   6835 C  CD1 . ILE C  1  204 ? -13.150 20.964  10.003 1.00 55.71  ? 217 ILE C CD1 1 
ATOM   6836 N  N   . ASN C  1  205 ? -13.030 15.781  8.134  1.00 47.41  ? 218 ASN C N   1 
ATOM   6837 C  CA  . ASN C  1  205 ? -12.572 14.941  7.038  1.00 45.17  ? 218 ASN C CA  1 
ATOM   6838 C  C   . ASN C  1  205 ? -13.120 13.522  7.140  1.00 43.40  ? 218 ASN C C   1 
ATOM   6839 O  O   . ASN C  1  205 ? -13.234 12.865  6.110  1.00 46.01  ? 218 ASN C O   1 
ATOM   6840 C  CB  . ASN C  1  205 ? -11.049 14.888  6.938  1.00 46.46  ? 218 ASN C CB  1 
ATOM   6841 C  CG  . ASN C  1  205 ? -10.445 16.263  6.813  1.00 43.34  ? 218 ASN C CG  1 
ATOM   6842 O  OD1 . ASN C  1  205 ? -11.083 17.161  6.258  1.00 47.50  ? 218 ASN C OD1 1 
ATOM   6843 N  ND2 . ASN C  1  205 ? -9.244  16.457  7.341  1.00 45.06  ? 218 ASN C ND2 1 
ATOM   6844 N  N   . LEU C  1  206 ? -13.437 13.049  8.359  1.00 45.06  ? 219 LEU C N   1 
ATOM   6845 C  CA  . LEU C  1  206 ? -13.761 11.645  8.568  1.00 42.61  ? 219 LEU C CA  1 
ATOM   6846 C  C   . LEU C  1  206 ? -15.150 11.437  9.182  1.00 46.19  ? 219 LEU C C   1 
ATOM   6847 O  O   . LEU C  1  206 ? -15.734 10.374  8.977  1.00 42.27  ? 219 LEU C O   1 
ATOM   6848 C  CB  . LEU C  1  206 ? -12.666 11.013  9.423  1.00 43.85  ? 219 LEU C CB  1 
ATOM   6849 C  CG  . LEU C  1  206 ? -11.247 11.075  8.843  1.00 47.75  ? 219 LEU C CG  1 
ATOM   6850 C  CD1 . LEU C  1  206 ? -10.226 10.705  9.885  1.00 46.39  ? 219 LEU C CD1 1 
ATOM   6851 C  CD2 . LEU C  1  206 ? -11.102 10.166  7.633  1.00 49.88  ? 219 LEU C CD2 1 
ATOM   6852 N  N   . PHE C  1  207 ? -15.675 12.394  9.963  1.00 50.00  ? 220 PHE C N   1 
ATOM   6853 C  CA  . PHE C  1  207 ? -16.972 12.197  10.599 1.00 49.58  ? 220 PHE C CA  1 
ATOM   6854 C  C   . PHE C  1  207 ? -18.094 12.748  9.721  1.00 49.15  ? 220 PHE C C   1 
ATOM   6855 O  O   . PHE C  1  207 ? -19.254 12.400  9.918  1.00 51.84  ? 220 PHE C O   1 
ATOM   6856 C  CB  . PHE C  1  207 ? -17.113 12.840  11.981 1.00 53.91  ? 220 PHE C CB  1 
ATOM   6857 C  CG  . PHE C  1  207 ? -16.225 12.276  13.079 1.00 56.65  ? 220 PHE C CG  1 
ATOM   6858 C  CD1 . PHE C  1  207 ? -15.549 11.072  12.922 1.00 54.67  ? 220 PHE C CD1 1 
ATOM   6859 C  CD2 . PHE C  1  207 ? -16.097 12.954  14.285 1.00 57.68  ? 220 PHE C CD2 1 
ATOM   6860 C  CE1 . PHE C  1  207 ? -14.750 10.577  13.939 1.00 54.32  ? 220 PHE C CE1 1 
ATOM   6861 C  CE2 . PHE C  1  207 ? -15.286 12.463  15.291 1.00 55.40  ? 220 PHE C CE2 1 
ATOM   6862 C  CZ  . PHE C  1  207 ? -14.614 11.278  15.117 1.00 55.74  ? 220 PHE C CZ  1 
ATOM   6863 N  N   . VAL C  1  208 ? -17.754 13.620  8.773  1.00 49.36  ? 221 VAL C N   1 
ATOM   6864 C  CA  . VAL C  1  208 ? -18.713 14.076  7.781  1.00 48.57  ? 221 VAL C CA  1 
ATOM   6865 C  C   . VAL C  1  208 ? -18.889 12.973  6.741  1.00 47.96  ? 221 VAL C C   1 
ATOM   6866 O  O   . VAL C  1  208 ? -17.923 12.359  6.295  1.00 45.24  ? 221 VAL C O   1 
ATOM   6867 C  CB  . VAL C  1  208 ? -18.298 15.402  7.120  1.00 46.01  ? 221 VAL C CB  1 
ATOM   6868 C  CG1 . VAL C  1  208 ? -19.259 15.804  6.008  1.00 49.44  ? 221 VAL C CG1 1 
ATOM   6869 C  CG2 . VAL C  1  208 ? -18.186 16.521  8.144  1.00 47.63  ? 221 VAL C CG2 1 
ATOM   6870 N  N   . ASP C  1  209 ? -20.145 12.748  6.357  1.00 47.78  ? 222 ASP C N   1 
ATOM   6871 C  CA  . ASP C  1  209 ? -20.502 11.684  5.438  1.00 51.04  ? 222 ASP C CA  1 
ATOM   6872 C  C   . ASP C  1  209 ? -19.774 11.884  4.111  1.00 51.03  ? 222 ASP C C   1 
ATOM   6873 O  O   . ASP C  1  209 ? -19.703 13.001  3.609  1.00 49.08  ? 222 ASP C O   1 
ATOM   6874 C  CB  . ASP C  1  209 ? -22.008 11.626  5.242  1.00 48.93  ? 222 ASP C CB  1 
ATOM   6875 C  CG  . ASP C  1  209 ? -22.500 10.426  4.448  1.00 48.22  ? 222 ASP C CG  1 
ATOM   6876 O  OD1 . ASP C  1  209 ? -22.319 10.423  3.213  1.00 52.23  ? 222 ASP C OD1 1 
ATOM   6877 O  OD2 . ASP C  1  209 ? -23.014 9.486   5.077  1.00 44.50  ? 222 ASP C OD2 1 
ATOM   6878 N  N   . GLY C  1  210 ? -19.281 10.780  3.537  1.00 50.03  ? 223 GLY C N   1 
ATOM   6879 C  CA  . GLY C  1  210 ? -18.419 10.834  2.365  1.00 56.57  ? 223 GLY C CA  1 
ATOM   6880 C  C   . GLY C  1  210 ? -19.168 11.228  1.086  1.00 56.55  ? 223 GLY C C   1 
ATOM   6881 O  O   . GLY C  1  210 ? -18.529 11.544  0.087  1.00 55.88  ? 223 GLY C O   1 
ATOM   6882 N  N   . ARG C  1  211 ? -20.510 11.213  1.117  1.00 55.46  ? 224 ARG C N   1 
ATOM   6883 C  CA  . ARG C  1  211 ? -21.311 11.644  -0.019 1.00 53.45  ? 224 ARG C CA  1 
ATOM   6884 C  C   . ARG C  1  211 ? -21.419 13.168  -0.070 1.00 55.60  ? 224 ARG C C   1 
ATOM   6885 O  O   . ARG C  1  211 ? -21.884 13.708  -1.068 1.00 57.92  ? 224 ARG C O   1 
ATOM   6886 C  CB  . ARG C  1  211 ? -22.714 11.031  0.014  1.00 55.10  ? 224 ARG C CB  1 
ATOM   6887 C  CG  . ARG C  1  211 ? -22.722 9.530   -0.225 1.00 56.21  ? 224 ARG C CG  1 
ATOM   6888 C  CD  . ARG C  1  211 ? -24.032 8.876   0.183  1.00 58.79  ? 224 ARG C CD  1 
ATOM   6889 N  NE  . ARG C  1  211 ? -24.256 8.982   1.631  1.00 61.35  ? 224 ARG C NE  1 
ATOM   6890 C  CZ  . ARG C  1  211 ? -25.278 8.463   2.309  1.00 61.61  ? 224 ARG C CZ  1 
ATOM   6891 N  NH1 . ARG C  1  211 ? -26.221 7.782   1.686  1.00 58.66  ? 224 ARG C NH1 1 
ATOM   6892 N  NH2 . ARG C  1  211 ? -25.351 8.619   3.621  1.00 61.99  ? 224 ARG C NH2 1 
ATOM   6893 N  N   . VAL C  1  212 ? -21.013 13.852  1.008  1.00 55.36  ? 225 VAL C N   1 
ATOM   6894 C  CA  . VAL C  1  212 ? -20.979 15.307  1.043  1.00 58.59  ? 225 VAL C CA  1 
ATOM   6895 C  C   . VAL C  1  212 ? -19.657 15.788  0.445  1.00 63.72  ? 225 VAL C C   1 
ATOM   6896 O  O   . VAL C  1  212 ? -18.595 15.566  1.022  1.00 63.55  ? 225 VAL C O   1 
ATOM   6897 C  CB  . VAL C  1  212 ? -21.171 15.813  2.487  1.00 59.99  ? 225 VAL C CB  1 
ATOM   6898 C  CG1 . VAL C  1  212 ? -21.019 17.327  2.622  1.00 58.48  ? 225 VAL C CG1 1 
ATOM   6899 C  CG2 . VAL C  1  212 ? -22.511 15.353  3.053  1.00 62.80  ? 225 VAL C CG2 1 
ATOM   6900 N  N   . THR C  1  213 ? -19.739 16.436  -0.727 1.00 70.23  ? 226 THR C N   1 
ATOM   6901 C  CA  . THR C  1  213 ? -18.567 16.748  -1.535 1.00 76.82  ? 226 THR C CA  1 
ATOM   6902 C  C   . THR C  1  213 ? -18.153 18.206  -1.352 1.00 78.40  ? 226 THR C C   1 
ATOM   6903 O  O   . THR C  1  213 ? -16.959 18.510  -1.383 1.00 75.80  ? 226 THR C O   1 
ATOM   6904 C  CB  . THR C  1  213 ? -18.853 16.431  -3.004 1.00 79.30  ? 226 THR C CB  1 
ATOM   6905 O  OG1 . THR C  1  213 ? -20.006 17.190  -3.362 1.00 78.46  ? 226 THR C OG1 1 
ATOM   6906 C  CG2 . THR C  1  213 ? -19.085 14.947  -3.239 1.00 77.59  ? 226 THR C CG2 1 
ATOM   6907 N  N   . THR C  1  214 ? -19.138 19.100  -1.183 1.00 80.62  ? 227 THR C N   1 
ATOM   6908 C  CA  . THR C  1  214 ? -18.864 20.526  -1.067 1.00 83.21  ? 227 THR C CA  1 
ATOM   6909 C  C   . THR C  1  214 ? -19.253 21.019  0.327  1.00 84.77  ? 227 THR C C   1 
ATOM   6910 O  O   . THR C  1  214 ? -20.247 20.557  0.889  1.00 85.09  ? 227 THR C O   1 
ATOM   6911 C  CB  . THR C  1  214 ? -19.604 21.271  -2.180 1.00 80.18  ? 227 THR C CB  1 
ATOM   6912 O  OG1 . THR C  1  214 ? -19.134 22.609  -2.071 1.00 83.60  ? 227 THR C OG1 1 
ATOM   6913 C  CG2 . THR C  1  214 ? -21.120 21.220  -2.060 1.00 81.35  ? 227 THR C CG2 1 
ATOM   6914 N  N   . ASP C  1  215 ? -18.463 21.958  0.873  1.00 86.33  ? 228 ASP C N   1 
ATOM   6915 C  CA  . ASP C  1  215 ? -18.828 22.669  2.091  1.00 88.09  ? 228 ASP C CA  1 
ATOM   6916 C  C   . ASP C  1  215 ? -18.998 21.657  3.224  1.00 82.12  ? 228 ASP C C   1 
ATOM   6917 O  O   . ASP C  1  215 ? -20.053 21.580  3.852  1.00 84.11  ? 228 ASP C O   1 
ATOM   6918 C  CB  . ASP C  1  215 ? -20.074 23.516  1.858  1.00 99.15  ? 228 ASP C CB  1 
ATOM   6919 C  CG  . ASP C  1  215 ? -20.569 24.367  3.020  1.00 103.32 ? 228 ASP C CG  1 
ATOM   6920 O  OD1 . ASP C  1  215 ? -19.737 24.750  3.870  1.00 111.93 ? 228 ASP C OD1 1 
ATOM   6921 O  OD2 . ASP C  1  215 ? -21.795 24.616  3.077  1.00 96.30  ? 228 ASP C OD2 1 
ATOM   6922 N  N   . ARG C  1  216 ? -17.951 20.865  3.463  1.00 75.75  ? 229 ARG C N   1 
ATOM   6923 C  CA  . ARG C  1  216 ? -18.033 19.770  4.414  1.00 69.65  ? 229 ARG C CA  1 
ATOM   6924 C  C   . ARG C  1  216 ? -18.129 20.340  5.830  1.00 62.06  ? 229 ARG C C   1 
ATOM   6925 O  O   . ARG C  1  216 ? -17.301 21.147  6.246  1.00 57.36  ? 229 ARG C O   1 
ATOM   6926 C  CB  . ARG C  1  216 ? -16.850 18.819  4.206  1.00 70.03  ? 229 ARG C CB  1 
ATOM   6927 C  CG  . ARG C  1  216 ? -16.964 17.972  2.947  1.00 69.20  ? 229 ARG C CG  1 
ATOM   6928 C  CD  . ARG C  1  216 ? -15.723 17.124  2.684  1.00 66.27  ? 229 ARG C CD  1 
ATOM   6929 N  NE  . ARG C  1  216 ? -15.456 16.124  3.728  1.00 64.59  ? 229 ARG C NE  1 
ATOM   6930 C  CZ  . ARG C  1  216 ? -16.114 14.978  3.930  1.00 65.73  ? 229 ARG C CZ  1 
ATOM   6931 N  NH1 . ARG C  1  216 ? -17.072 14.589  3.104  1.00 62.57  ? 229 ARG C NH1 1 
ATOM   6932 N  NH2 . ARG C  1  216 ? -15.788 14.204  4.956  1.00 71.11  ? 229 ARG C NH2 1 
ATOM   6933 N  N   . LYS C  1  217 ? -19.182 19.938  6.549  1.00 61.66  ? 230 LYS C N   1 
ATOM   6934 C  CA  . LYS C  1  217 ? -19.457 20.450  7.883  1.00 61.74  ? 230 LYS C CA  1 
ATOM   6935 C  C   . LYS C  1  217 ? -20.238 19.398  8.669  1.00 61.43  ? 230 LYS C C   1 
ATOM   6936 O  O   . LYS C  1  217 ? -21.032 18.661  8.093  1.00 61.14  ? 230 LYS C O   1 
ATOM   6937 C  CB  . LYS C  1  217 ? -20.242 21.759  7.756  1.00 67.21  ? 230 LYS C CB  1 
ATOM   6938 C  CG  . LYS C  1  217 ? -21.643 21.585  7.177  1.00 73.51  ? 230 LYS C CG  1 
ATOM   6939 C  CD  . LYS C  1  217 ? -22.374 22.888  6.866  1.00 77.16  ? 230 LYS C CD  1 
ATOM   6940 C  CE  . LYS C  1  217 ? -23.784 22.639  6.425  1.00 79.62  ? 230 LYS C CE  1 
ATOM   6941 N  NZ  . LYS C  1  217 ? -24.475 23.892  6.109  1.00 82.24  ? 230 LYS C NZ  1 
ATOM   6942 N  N   . LEU C  1  218 ? -20.006 19.335  9.983  1.00 59.62  ? 231 LEU C N   1 
ATOM   6943 C  CA  . LEU C  1  218 ? -20.562 18.278  10.812 1.00 59.72  ? 231 LEU C CA  1 
ATOM   6944 C  C   . LEU C  1  218 ? -21.706 18.817  11.670 1.00 59.73  ? 231 LEU C C   1 
ATOM   6945 O  O   . LEU C  1  218 ? -21.530 19.813  12.364 1.00 61.22  ? 231 LEU C O   1 
ATOM   6946 C  CB  . LEU C  1  218 ? -19.446 17.716  11.687 1.00 56.84  ? 231 LEU C CB  1 
ATOM   6947 C  CG  . LEU C  1  218 ? -19.832 16.514  12.555 1.00 58.84  ? 231 LEU C CG  1 
ATOM   6948 C  CD1 . LEU C  1  218 ? -20.100 15.286  11.694 1.00 61.13  ? 231 LEU C CD1 1 
ATOM   6949 C  CD2 . LEU C  1  218 ? -18.770 16.224  13.600 1.00 59.51  ? 231 LEU C CD2 1 
ATOM   6950 N  N   . SER C  1  219 ? -22.852 18.123  11.656 1.00 61.97  ? 232 SER C N   1 
ATOM   6951 C  CA  . SER C  1  219 ? -23.984 18.496  12.490 1.00 64.39  ? 232 SER C CA  1 
ATOM   6952 C  C   . SER C  1  219 ? -23.712 18.126  13.950 1.00 67.63  ? 232 SER C C   1 
ATOM   6953 O  O   . SER C  1  219 ? -22.888 17.263  14.239 1.00 68.23  ? 232 SER C O   1 
ATOM   6954 C  CB  . SER C  1  219 ? -25.254 17.854  12.001 1.00 62.46  ? 232 SER C CB  1 
ATOM   6955 O  OG  . SER C  1  219 ? -25.271 16.462  12.291 1.00 63.90  ? 232 SER C OG  1 
ATOM   6956 N  N   . MET C  1  220 ? -24.409 18.793  14.871 1.00 63.60  ? 233 MET C N   1 
ATOM   6957 C  CA  . MET C  1  220 ? -24.205 18.561  16.291 1.00 60.06  ? 233 MET C CA  1 
ATOM   6958 C  C   . MET C  1  220 ? -24.771 17.202  16.693 1.00 59.89  ? 233 MET C C   1 
ATOM   6959 O  O   . MET C  1  220 ? -24.238 16.543  17.585 1.00 64.78  ? 233 MET C O   1 
ATOM   6960 C  CB  . MET C  1  220 ? -24.857 19.677  17.118 1.00 65.07  ? 233 MET C CB  1 
ATOM   6961 C  CG  . MET C  1  220 ? -24.243 21.058  16.927 1.00 61.88  ? 233 MET C CG  1 
ATOM   6962 S  SD  . MET C  1  220 ? -22.465 21.101  17.221 1.00 63.46  ? 233 MET C SD  1 
ATOM   6963 C  CE  . MET C  1  220 ? -21.769 21.022  15.559 1.00 65.34  ? 233 MET C CE  1 
ATOM   6964 N  N   . GLU C  1  221 ? -25.840 16.772  16.014 1.00 59.47  ? 234 GLU C N   1 
ATOM   6965 C  CA  . GLU C  1  221 ? -26.409 15.447  16.213 1.00 64.59  ? 234 GLU C CA  1 
ATOM   6966 C  C   . GLU C  1  221 ? -25.360 14.382  15.890 1.00 62.07  ? 234 GLU C C   1 
ATOM   6967 O  O   . GLU C  1  221 ? -25.176 13.436  16.650 1.00 62.65  ? 234 GLU C O   1 
ATOM   6968 C  CB  . GLU C  1  221 ? -27.650 15.211  15.346 1.00 66.74  ? 234 GLU C CB  1 
ATOM   6969 C  CG  . GLU C  1  221 ? -28.825 16.138  15.654 1.00 77.75  ? 234 GLU C CG  1 
ATOM   6970 C  CD  . GLU C  1  221 ? -28.735 17.602  15.223 1.00 85.12  ? 234 GLU C CD  1 
ATOM   6971 O  OE1 . GLU C  1  221 ? -27.856 17.996  14.411 1.00 80.87  ? 234 GLU C OE1 1 
ATOM   6972 O  OE2 . GLU C  1  221 ? -29.555 18.375  15.764 1.00 94.93  ? 234 GLU C OE2 1 
ATOM   6973 N  N   . ASP C  1  222 ? -24.696 14.524  14.740 1.00 55.59  ? 235 ASP C N   1 
ATOM   6974 C  CA  . ASP C  1  222 ? -23.704 13.553  14.299 1.00 60.09  ? 235 ASP C CA  1 
ATOM   6975 C  C   . ASP C  1  222 ? -22.503 13.584  15.245 1.00 55.43  ? 235 ASP C C   1 
ATOM   6976 O  O   . ASP C  1  222 ? -21.982 12.536  15.613 1.00 55.43  ? 235 ASP C O   1 
ATOM   6977 C  CB  . ASP C  1  222 ? -23.377 13.739  12.822 1.00 59.77  ? 235 ASP C CB  1 
ATOM   6978 C  CG  . ASP C  1  222 ? -24.487 13.318  11.857 1.00 63.19  ? 235 ASP C CG  1 
ATOM   6979 O  OD1 . ASP C  1  222 ? -25.481 12.701  12.317 1.00 62.18  ? 235 ASP C OD1 1 
ATOM   6980 O  OD2 . ASP C  1  222 ? -24.377 13.616  10.647 1.00 59.62  ? 235 ASP C OD2 1 
ATOM   6981 N  N   . ALA C  1  223 ? -22.091 14.786  15.659 1.00 53.42  ? 236 ALA C N   1 
ATOM   6982 C  CA  . ALA C  1  223 ? -20.991 14.943  16.598 1.00 55.86  ? 236 ALA C CA  1 
ATOM   6983 C  C   . ALA C  1  223 ? -21.286 14.218  17.912 1.00 61.22  ? 236 ALA C C   1 
ATOM   6984 O  O   . ALA C  1  223 ? -20.450 13.455  18.398 1.00 59.85  ? 236 ALA C O   1 
ATOM   6985 C  CB  . ALA C  1  223 ? -20.706 16.411  16.826 1.00 55.91  ? 236 ALA C CB  1 
ATOM   6986 N  N   . ALA C  1  224 ? -22.476 14.456  18.480 1.00 56.81  ? 237 ALA C N   1 
ATOM   6987 C  CA  . ALA C  1  224 ? -22.845 13.861  19.756 1.00 56.11  ? 237 ALA C CA  1 
ATOM   6988 C  C   . ALA C  1  224 ? -22.873 12.341  19.637 1.00 55.39  ? 237 ALA C C   1 
ATOM   6989 O  O   . ALA C  1  224 ? -22.382 11.632  20.514 1.00 53.08  ? 237 ALA C O   1 
ATOM   6990 C  CB  . ALA C  1  224 ? -24.189 14.393  20.225 1.00 59.11  ? 237 ALA C CB  1 
ATOM   6991 N  N   . SER C  1  225 ? -23.440 11.854  18.528 1.00 52.98  ? 238 SER C N   1 
ATOM   6992 C  CA  . SER C  1  225 ? -23.541 10.426  18.279 1.00 51.50  ? 238 SER C CA  1 
ATOM   6993 C  C   . SER C  1  225 ? -22.163 9.763   18.355 1.00 52.62  ? 238 SER C C   1 
ATOM   6994 O  O   . SER C  1  225 ? -22.026 8.716   18.974 1.00 52.81  ? 238 SER C O   1 
ATOM   6995 C  CB  . SER C  1  225 ? -24.220 10.168  16.949 1.00 52.01  ? 238 SER C CB  1 
ATOM   6996 O  OG  . SER C  1  225 ? -24.397 8.782   16.711 1.00 49.63  ? 238 SER C OG  1 
ATOM   6997 N  N   . ILE C  1  226 ? -21.139 10.370  17.746 1.00 53.70  ? 239 ILE C N   1 
ATOM   6998 C  CA  . ILE C  1  226 ? -19.813 9.761   17.679 1.00 51.58  ? 239 ILE C CA  1 
ATOM   6999 C  C   . ILE C  1  226 ? -19.037 10.035  18.969 1.00 49.26  ? 239 ILE C C   1 
ATOM   7000 O  O   . ILE C  1  226 ? -18.553 9.096   19.601 1.00 55.67  ? 239 ILE C O   1 
ATOM   7001 C  CB  . ILE C  1  226 ? -19.054 10.239  16.426 1.00 50.70  ? 239 ILE C CB  1 
ATOM   7002 C  CG1 . ILE C  1  226 ? -19.719 9.717   15.155 1.00 51.89  ? 239 ILE C CG1 1 
ATOM   7003 C  CG2 . ILE C  1  226 ? -17.575 9.837   16.486 1.00 50.30  ? 239 ILE C CG2 1 
ATOM   7004 C  CD1 . ILE C  1  226 ? -19.301 10.440  13.891 1.00 52.32  ? 239 ILE C CD1 1 
ATOM   7005 N  N   . PHE C  1  227 ? -18.920 11.316  19.349 1.00 47.24  ? 240 PHE C N   1 
ATOM   7006 C  CA  . PHE C  1  227 ? -18.111 11.730  20.490 1.00 51.30  ? 240 PHE C CA  1 
ATOM   7007 C  C   . PHE C  1  227 ? -18.658 11.185  21.814 1.00 53.27  ? 240 PHE C C   1 
ATOM   7008 O  O   . PHE C  1  227 ? -17.872 10.830  22.691 1.00 53.76  ? 240 PHE C O   1 
ATOM   7009 C  CB  . PHE C  1  227 ? -18.002 13.252  20.628 1.00 49.61  ? 240 PHE C CB  1 
ATOM   7010 C  CG  . PHE C  1  227 ? -17.072 13.959  19.653 1.00 48.08  ? 240 PHE C CG  1 
ATOM   7011 C  CD1 . PHE C  1  227 ? -15.691 13.910  19.823 1.00 52.02  ? 240 PHE C CD1 1 
ATOM   7012 C  CD2 . PHE C  1  227 ? -17.573 14.729  18.612 1.00 51.45  ? 240 PHE C CD2 1 
ATOM   7013 C  CE1 . PHE C  1  227 ? -14.842 14.574  18.952 1.00 49.62  ? 240 PHE C CE1 1 
ATOM   7014 C  CE2 . PHE C  1  227 ? -16.715 15.405  17.756 1.00 50.53  ? 240 PHE C CE2 1 
ATOM   7015 C  CZ  . PHE C  1  227 ? -15.355 15.336  17.931 1.00 51.47  ? 240 PHE C CZ  1 
ATOM   7016 N  N   . ARG C  1  228 ? -19.989 11.164  21.985 1.00 54.73  ? 241 ARG C N   1 
ATOM   7017 C  CA  . ARG C  1  228 ? -20.585 10.730  23.240 1.00 53.03  ? 241 ARG C CA  1 
ATOM   7018 C  C   . ARG C  1  228 ? -20.971 9.255   23.168 1.00 51.05  ? 241 ARG C C   1 
ATOM   7019 O  O   . ARG C  1  228 ? -20.567 8.471   24.023 1.00 49.80  ? 241 ARG C O   1 
ATOM   7020 C  CB  . ARG C  1  228 ? -21.815 11.559  23.637 1.00 58.90  ? 241 ARG C CB  1 
ATOM   7021 C  CG  . ARG C  1  228 ? -22.407 11.175  24.988 1.00 63.07  ? 241 ARG C CG  1 
ATOM   7022 C  CD  . ARG C  1  228 ? -23.546 12.114  25.369 1.00 68.89  ? 241 ARG C CD  1 
ATOM   7023 N  NE  . ARG C  1  228 ? -24.739 11.730  24.601 1.00 72.86  ? 241 ARG C NE  1 
ATOM   7024 C  CZ  . ARG C  1  228 ? -25.491 12.503  23.815 1.00 75.52  ? 241 ARG C CZ  1 
ATOM   7025 N  NH1 . ARG C  1  228 ? -25.265 13.803  23.709 1.00 71.90  ? 241 ARG C NH1 1 
ATOM   7026 N  NH2 . ARG C  1  228 ? -26.500 11.963  23.150 1.00 73.93  ? 241 ARG C NH2 1 
ATOM   7027 N  N   . ASP C  1  229 ? -21.740 8.868   22.143 1.00 48.24  ? 242 ASP C N   1 
ATOM   7028 C  CA  . ASP C  1  229 ? -22.405 7.576   22.140 1.00 51.96  ? 242 ASP C CA  1 
ATOM   7029 C  C   . ASP C  1  229 ? -21.601 6.511   21.401 1.00 49.47  ? 242 ASP C C   1 
ATOM   7030 O  O   . ASP C  1  229 ? -21.970 5.340   21.440 1.00 47.26  ? 242 ASP C O   1 
ATOM   7031 C  CB  . ASP C  1  229 ? -23.826 7.705   21.605 1.00 58.61  ? 242 ASP C CB  1 
ATOM   7032 C  CG  . ASP C  1  229 ? -24.783 8.413   22.555 1.00 62.09  ? 242 ASP C CG  1 
ATOM   7033 O  OD1 . ASP C  1  229 ? -24.733 8.067   23.754 1.00 56.93  ? 242 ASP C OD1 1 
ATOM   7034 O  OD2 . ASP C  1  229 ? -25.573 9.285   22.095 1.00 69.17  ? 242 ASP C OD2 1 
ATOM   7035 N  N   . MET C  1  230 ? -20.506 6.902   20.740 1.00 54.68  ? 243 MET C N   1 
ATOM   7036 C  CA  A MET C  1  230 ? -19.658 5.956   20.033 0.50 49.56  ? 243 MET C CA  1 
ATOM   7037 C  CA  B MET C  1  230 ? -19.656 5.957   20.028 0.50 51.67  ? 243 MET C CA  1 
ATOM   7038 C  C   . MET C  1  230 ? -20.456 5.264   18.925 1.00 49.31  ? 243 MET C C   1 
ATOM   7039 O  O   . MET C  1  230 ? -20.317 4.053   18.722 1.00 45.37  ? 243 MET C O   1 
ATOM   7040 C  CB  A MET C  1  230 ? -19.121 4.890   20.993 0.50 48.66  ? 243 MET C CB  1 
ATOM   7041 C  CB  B MET C  1  230 ? -19.109 4.879   20.973 0.50 53.79  ? 243 MET C CB  1 
ATOM   7042 C  CG  A MET C  1  230 ? -18.463 5.416   22.247 0.50 48.60  ? 243 MET C CG  1 
ATOM   7043 C  CG  B MET C  1  230 ? -18.387 5.419   22.184 0.50 56.76  ? 243 MET C CG  1 
ATOM   7044 S  SD  A MET C  1  230 ? -18.125 4.106   23.441 0.50 45.44  ? 243 MET C SD  1 
ATOM   7045 S  SD  B MET C  1  230 ? -17.910 4.076   23.287 0.50 58.22  ? 243 MET C SD  1 
ATOM   7046 C  CE  A MET C  1  230 ? -17.826 5.095   24.915 0.50 45.86  ? 243 MET C CE  1 
ATOM   7047 C  CE  B MET C  1  230 ? -19.518 3.664   23.972 0.50 62.92  ? 243 MET C CE  1 
ATOM   7048 N  N   . ARG C  1  231 ? -21.288 6.029   18.208 1.00 46.77  ? 244 ARG C N   1 
ATOM   7049 C  CA  A ARG C  1  231 ? -22.221 5.473   17.237 0.50 47.08  ? 244 ARG C CA  1 
ATOM   7050 C  CA  B ARG C  1  231 ? -22.205 5.464   17.235 0.50 48.23  ? 244 ARG C CA  1 
ATOM   7051 C  C   . ARG C  1  231 ? -22.126 6.246   15.928 1.00 44.08  ? 244 ARG C C   1 
ATOM   7052 O  O   . ARG C  1  231 ? -22.169 7.479   15.925 1.00 39.62  ? 244 ARG C O   1 
ATOM   7053 C  CB  A ARG C  1  231 ? -23.648 5.537   17.802 0.50 49.78  ? 244 ARG C CB  1 
ATOM   7054 C  CB  B ARG C  1  231 ? -23.607 5.499   17.849 0.50 52.66  ? 244 ARG C CB  1 
ATOM   7055 C  CG  A ARG C  1  231 ? -24.735 4.865   16.979 0.50 51.94  ? 244 ARG C CG  1 
ATOM   7056 C  CG  B ARG C  1  231 ? -24.717 4.941   16.973 0.50 56.73  ? 244 ARG C CG  1 
ATOM   7057 C  CD  A ARG C  1  231 ? -26.001 4.816   17.830 0.50 54.02  ? 244 ARG C CD  1 
ATOM   7058 C  CD  B ARG C  1  231 ? -26.056 5.168   17.651 0.50 60.41  ? 244 ARG C CD  1 
ATOM   7059 N  NE  A ARG C  1  231 ? -26.883 3.681   17.538 0.50 55.04  ? 244 ARG C NE  1 
ATOM   7060 N  NE  B ARG C  1  231 ? -26.062 4.548   18.979 0.50 62.38  ? 244 ARG C NE  1 
ATOM   7061 C  CZ  A ARG C  1  231 ? -27.817 3.232   18.373 0.50 57.28  ? 244 ARG C CZ  1 
ATOM   7062 C  CZ  B ARG C  1  231 ? -26.903 4.874   19.952 0.50 62.62  ? 244 ARG C CZ  1 
ATOM   7063 N  NH1 A ARG C  1  231 ? -27.959 3.783   19.566 0.50 62.43  ? 244 ARG C NH1 1 
ATOM   7064 N  NH1 B ARG C  1  231 ? -27.761 5.860   19.776 0.50 65.38  ? 244 ARG C NH1 1 
ATOM   7065 N  NH2 A ARG C  1  231 ? -28.591 2.220   18.030 0.50 52.73  ? 244 ARG C NH2 1 
ATOM   7066 N  NH2 B ARG C  1  231 ? -26.877 4.221   21.096 0.50 60.69  ? 244 ARG C NH2 1 
ATOM   7067 N  N   . PHE C  1  232 ? -22.011 5.506   14.820 1.00 44.03  ? 245 PHE C N   1 
ATOM   7068 C  CA  . PHE C  1  232 ? -22.100 6.106   13.498 1.00 45.68  ? 245 PHE C CA  1 
ATOM   7069 C  C   . PHE C  1  232 ? -23.472 6.743   13.317 1.00 50.72  ? 245 PHE C C   1 
ATOM   7070 O  O   . PHE C  1  232 ? -24.471 6.209   13.783 1.00 50.95  ? 245 PHE C O   1 
ATOM   7071 C  CB  . PHE C  1  232 ? -21.915 5.070   12.386 1.00 44.41  ? 245 PHE C CB  1 
ATOM   7072 C  CG  . PHE C  1  232 ? -20.484 4.579   12.199 1.00 44.03  ? 245 PHE C CG  1 
ATOM   7073 C  CD1 . PHE C  1  232 ? -19.482 5.453   11.793 1.00 42.31  ? 245 PHE C CD1 1 
ATOM   7074 C  CD2 . PHE C  1  232 ? -20.164 3.234   12.359 1.00 45.21  ? 245 PHE C CD2 1 
ATOM   7075 C  CE1 . PHE C  1  232 ? -18.194 4.990   11.584 1.00 43.78  ? 245 PHE C CE1 1 
ATOM   7076 C  CE2 . PHE C  1  232 ? -18.875 2.777   12.146 1.00 46.30  ? 245 PHE C CE2 1 
ATOM   7077 C  CZ  . PHE C  1  232 ? -17.895 3.656   11.754 1.00 41.86  ? 245 PHE C CZ  1 
ATOM   7078 N  N   . PRO C  1  233 ? -23.567 7.897   12.625 1.00 54.91  ? 246 PRO C N   1 
ATOM   7079 C  CA  . PRO C  1  233 ? -24.857 8.392   12.148 1.00 53.30  ? 246 PRO C CA  1 
ATOM   7080 C  C   . PRO C  1  233 ? -25.559 7.292   11.359 1.00 56.05  ? 246 PRO C C   1 
ATOM   7081 O  O   . PRO C  1  233 ? -24.900 6.431   10.778 1.00 46.88  ? 246 PRO C O   1 
ATOM   7082 C  CB  . PRO C  1  233 ? -24.489 9.605   11.277 1.00 56.21  ? 246 PRO C CB  1 
ATOM   7083 C  CG  . PRO C  1  233 ? -23.148 10.060  11.811 1.00 56.63  ? 246 PRO C CG  1 
ATOM   7084 C  CD  . PRO C  1  233 ? -22.449 8.793   12.288 1.00 58.20  ? 246 PRO C CD  1 
ATOM   7085 N  N   . ASP C  1  234 ? -26.896 7.318   11.353 1.00 55.77  ? 247 ASP C N   1 
ATOM   7086 C  CA  . ASP C  1  234 ? -27.684 6.402   10.537 1.00 58.64  ? 247 ASP C CA  1 
ATOM   7087 C  C   . ASP C  1  234 ? -27.214 6.503   9.085  1.00 49.99  ? 247 ASP C C   1 
ATOM   7088 O  O   . ASP C  1  234 ? -27.000 7.608   8.595  1.00 47.04  ? 247 ASP C O   1 
ATOM   7089 C  CB  . ASP C  1  234 ? -29.178 6.716   10.568 1.00 66.20  ? 247 ASP C CB  1 
ATOM   7090 C  CG  . ASP C  1  234 ? -29.889 6.638   11.913 1.00 74.34  ? 247 ASP C CG  1 
ATOM   7091 O  OD1 . ASP C  1  234 ? -29.266 6.162   12.886 1.00 81.66  ? 247 ASP C OD1 1 
ATOM   7092 O  OD2 . ASP C  1  234 ? -31.060 7.072   11.974 1.00 83.70  ? 247 ASP C OD2 1 
ATOM   7093 N  N   . ASP C  1  235 ? -27.038 5.348   8.421  1.00 46.02  ? 248 ASP C N   1 
ATOM   7094 C  CA  . ASP C  1  235 ? -26.714 5.295   7.000  1.00 53.91  ? 248 ASP C CA  1 
ATOM   7095 C  C   . ASP C  1  235 ? -25.368 5.971   6.709  1.00 51.48  ? 248 ASP C C   1 
ATOM   7096 O  O   . ASP C  1  235 ? -25.156 6.499   5.618  1.00 53.58  ? 248 ASP C O   1 
ATOM   7097 C  CB  . ASP C  1  235 ? -27.829 5.892   6.148  1.00 52.91  ? 248 ASP C CB  1 
ATOM   7098 C  CG  . ASP C  1  235 ? -27.679 5.680   4.648  1.00 55.15  ? 248 ASP C CG  1 
ATOM   7099 O  OD1 . ASP C  1  235 ? -27.478 4.510   4.251  1.00 50.57  ? 248 ASP C OD1 1 
ATOM   7100 O  OD2 . ASP C  1  235 ? -27.744 6.685   3.894  1.00 51.21  ? 248 ASP C OD2 1 
ATOM   7101 N  N   . PHE C  1  236 ? -24.441 5.933   7.673  1.00 47.73  ? 249 PHE C N   1 
ATOM   7102 C  CA  . PHE C  1  236 ? -23.202 6.683   7.539  1.00 50.09  ? 249 PHE C CA  1 
ATOM   7103 C  C   . PHE C  1  236 ? -22.345 6.081   6.429  1.00 43.99  ? 249 PHE C C   1 
ATOM   7104 O  O   . PHE C  1  236 ? -22.093 4.873   6.429  1.00 40.91  ? 249 PHE C O   1 
ATOM   7105 C  CB  . PHE C  1  236 ? -22.369 6.690   8.819  1.00 45.95  ? 249 PHE C CB  1 
ATOM   7106 C  CG  . PHE C  1  236 ? -21.097 7.510   8.701  1.00 45.15  ? 249 PHE C CG  1 
ATOM   7107 C  CD1 . PHE C  1  236 ? -21.153 8.892   8.625  1.00 42.93  ? 249 PHE C CD1 1 
ATOM   7108 C  CD2 . PHE C  1  236 ? -19.850 6.892   8.683  1.00 44.89  ? 249 PHE C CD2 1 
ATOM   7109 C  CE1 . PHE C  1  236 ? -19.989 9.632   8.540  1.00 44.91  ? 249 PHE C CE1 1 
ATOM   7110 C  CE2 . PHE C  1  236 ? -18.691 7.645   8.594  1.00 42.31  ? 249 PHE C CE2 1 
ATOM   7111 C  CZ  . PHE C  1  236 ? -18.761 9.010   8.516  1.00 40.59  ? 249 PHE C CZ  1 
ATOM   7112 N  N   . HIS C  1  237 ? -21.903 6.950   5.509  1.00 45.75  ? 250 HIS C N   1 
ATOM   7113 C  CA  . HIS C  1  237 ? -20.948 6.577   4.475  1.00 48.97  ? 250 HIS C CA  1 
ATOM   7114 C  C   . HIS C  1  237 ? -19.603 7.230   4.770  1.00 43.40  ? 250 HIS C C   1 
ATOM   7115 O  O   . HIS C  1  237 ? -19.526 8.439   4.969  1.00 42.92  ? 250 HIS C O   1 
ATOM   7116 C  CB  . HIS C  1  237 ? -21.459 6.973   3.083  1.00 49.78  ? 250 HIS C CB  1 
ATOM   7117 C  CG  . HIS C  1  237 ? -22.539 6.092   2.553  1.00 53.80  ? 250 HIS C CG  1 
ATOM   7118 N  ND1 . HIS C  1  237 ? -23.705 5.818   3.240  1.00 57.62  ? 250 HIS C ND1 1 
ATOM   7119 C  CD2 . HIS C  1  237 ? -22.639 5.447   1.384  1.00 57.86  ? 250 HIS C CD2 1 
ATOM   7120 C  CE1 . HIS C  1  237 ? -24.461 5.010   2.515  1.00 60.97  ? 250 HIS C CE1 1 
ATOM   7121 N  NE2 . HIS C  1  237 ? -23.835 4.770   1.382  1.00 61.18  ? 250 HIS C NE2 1 
ATOM   7122 N  N   . ARG C  1  238 ? -18.539 6.426   4.757  1.00 45.70  ? 251 ARG C N   1 
ATOM   7123 C  CA  . ARG C  1  238 ? -17.205 6.923   5.053  1.00 45.45  ? 251 ARG C CA  1 
ATOM   7124 C  C   . ARG C  1  238 ? -16.737 7.880   3.960  1.00 43.67  ? 251 ARG C C   1 
ATOM   7125 O  O   . ARG C  1  238 ? -17.280 7.885   2.859  1.00 44.50  ? 251 ARG C O   1 
ATOM   7126 C  CB  . ARG C  1  238 ? -16.199 5.777   5.184  1.00 46.54  ? 251 ARG C CB  1 
ATOM   7127 C  CG  . ARG C  1  238 ? -15.988 5.009   3.887  1.00 46.04  ? 251 ARG C CG  1 
ATOM   7128 C  CD  . ARG C  1  238 ? -14.978 3.892   4.049  1.00 45.60  ? 251 ARG C CD  1 
ATOM   7129 N  NE  . ARG C  1  238 ? -14.480 3.473   2.737  1.00 47.01  ? 251 ARG C NE  1 
ATOM   7130 C  CZ  . ARG C  1  238 ? -13.711 2.427   2.509  1.00 47.58  ? 251 ARG C CZ  1 
ATOM   7131 N  NH1 . ARG C  1  238 ? -13.315 1.641   3.503  1.00 49.46  ? 251 ARG C NH1 1 
ATOM   7132 N  NH2 . ARG C  1  238 ? -13.358 2.157   1.260  1.00 51.41  ? 251 ARG C NH2 1 
ATOM   7133 N  N   . SER C  1  239 ? -15.691 8.650   4.285  1.00 44.55  ? 252 SER C N   1 
ATOM   7134 C  CA  . SER C  1  239 ? -14.974 9.485   3.337  1.00 41.35  ? 252 SER C CA  1 
ATOM   7135 C  C   . SER C  1  239 ? -14.775 8.747   2.015  1.00 42.84  ? 252 SER C C   1 
ATOM   7136 O  O   . SER C  1  239 ? -14.472 7.554   2.005  1.00 37.82  ? 252 SER C O   1 
ATOM   7137 C  CB  . SER C  1  239 ? -13.643 9.901   3.898  1.00 42.60  ? 252 SER C CB  1 
ATOM   7138 O  OG  . SER C  1  239 ? -12.926 10.670  2.942  1.00 42.84  ? 252 SER C OG  1 
ATOM   7139 N  N   . ALA C  1  240 ? -14.928 9.496   0.912  1.00 43.32  ? 253 ALA C N   1 
ATOM   7140 C  CA  . ALA C  1  240 ? -14.823 8.962   -0.432 1.00 43.28  ? 253 ALA C CA  1 
ATOM   7141 C  C   . ALA C  1  240 ? -13.360 8.767   -0.825 1.00 41.72  ? 253 ALA C C   1 
ATOM   7142 O  O   . ALA C  1  240 ? -13.101 8.166   -1.858 1.00 40.11  ? 253 ALA C O   1 
ATOM   7143 C  CB  . ALA C  1  240 ? -15.535 9.893   -1.398 1.00 42.90  ? 253 ALA C CB  1 
ATOM   7144 N  N   . VAL C  1  241 ? -12.424 9.309   -0.034 1.00 42.67  ? 254 VAL C N   1 
ATOM   7145 C  CA  . VAL C  1  241 ? -10.993 9.118   -0.245 1.00 43.90  ? 254 VAL C CA  1 
ATOM   7146 C  C   . VAL C  1  241 ? -10.320 8.860   1.099  1.00 43.30  ? 254 VAL C C   1 
ATOM   7147 O  O   . VAL C  1  241 ? -10.801 9.323   2.136  1.00 42.85  ? 254 VAL C O   1 
ATOM   7148 C  CB  . VAL C  1  241 ? -10.318 10.325  -0.917 1.00 47.10  ? 254 VAL C CB  1 
ATOM   7149 C  CG1 . VAL C  1  241 ? -10.809 10.529  -2.336 1.00 53.01  ? 254 VAL C CG1 1 
ATOM   7150 C  CG2 . VAL C  1  241 ? -10.499 11.601  -0.106 1.00 49.38  ? 254 VAL C CG2 1 
ATOM   7151 N  N   . PRO C  1  242 ? -9.161  8.163   1.116  1.00 43.18  ? 255 PRO C N   1 
ATOM   7152 C  CA  . PRO C  1  242 ? -8.316  8.105   2.306  1.00 40.95  ? 255 PRO C CA  1 
ATOM   7153 C  C   . PRO C  1  242 ? -8.049  9.529   2.770  1.00 39.94  ? 255 PRO C C   1 
ATOM   7154 O  O   . PRO C  1  242 ? -7.768  10.405  1.958  1.00 39.32  ? 255 PRO C O   1 
ATOM   7155 C  CB  . PRO C  1  242 ? -7.033  7.399   1.840  1.00 40.45  ? 255 PRO C CB  1 
ATOM   7156 C  CG  . PRO C  1  242 ? -7.489  6.583   0.654  1.00 41.68  ? 255 PRO C CG  1 
ATOM   7157 C  CD  . PRO C  1  242 ? -8.579  7.422   -0.009 1.00 41.02  ? 255 PRO C CD  1 
ATOM   7158 N  N   . ALA C  1  243 ? -8.152  9.754   4.080  1.00 43.67  ? 256 ALA C N   1 
ATOM   7159 C  CA  . ALA C  1  243 ? -7.950  11.085  4.611  1.00 42.39  ? 256 ALA C CA  1 
ATOM   7160 C  C   . ALA C  1  243 ? -7.416  10.999  6.031  1.00 43.73  ? 256 ALA C C   1 
ATOM   7161 O  O   . ALA C  1  243 ? -7.480  9.950   6.672  1.00 44.49  ? 256 ALA C O   1 
ATOM   7162 C  CB  . ALA C  1  243 ? -9.238  11.867  4.548  1.00 45.74  ? 256 ALA C CB  1 
ATOM   7163 N  N   . SER C  1  244 ? -6.900  12.143  6.483  1.00 41.96  ? 257 SER C N   1 
ATOM   7164 C  CA  . SER C  1  244 ? -6.397  12.299  7.828  1.00 43.34  ? 257 SER C CA  1 
ATOM   7165 C  C   . SER C  1  244 ? -6.498  13.775  8.210  1.00 45.45  ? 257 SER C C   1 
ATOM   7166 O  O   . SER C  1  244 ? -7.587  14.251  8.521  1.00 45.47  ? 257 SER C O   1 
ATOM   7167 C  CB  . SER C  1  244 ? -4.997  11.742  7.947  1.00 43.30  ? 257 SER C CB  1 
ATOM   7168 O  OG  . SER C  1  244 ? -4.133  12.326  6.980  1.00 41.85  ? 257 SER C OG  1 
ATOM   7169 N  N   . ASN C  1  245 ? -5.378  14.500  8.126  1.00 46.25  ? 258 ASN C N   1 
ATOM   7170 C  CA  . ASN C  1  245 ? -5.248  15.793  8.776  1.00 45.29  ? 258 ASN C CA  1 
ATOM   7171 C  C   . ASN C  1  245 ? -5.267  16.934  7.760  1.00 49.00  ? 258 ASN C C   1 
ATOM   7172 O  O   . ASN C  1  245 ? -4.684  17.986  8.010  1.00 48.94  ? 258 ASN C O   1 
ATOM   7173 C  CB  . ASN C  1  245 ? -3.982  15.865  9.621  1.00 46.70  ? 258 ASN C CB  1 
ATOM   7174 C  CG  . ASN C  1  245 ? -2.726  15.736  8.799  1.00 47.54  ? 258 ASN C CG  1 
ATOM   7175 O  OD1 . ASN C  1  245 ? -2.771  15.264  7.663  1.00 45.13  ? 258 ASN C OD1 1 
ATOM   7176 N  ND2 . ASN C  1  245 ? -1.598  16.147  9.352  1.00 50.77  ? 258 ASN C ND2 1 
ATOM   7177 N  N   . GLU C  1  246 ? -5.959  16.748  6.631  1.00 53.34  ? 259 GLU C N   1 
ATOM   7178 C  CA  . GLU C  1  246 ? -6.103  17.818  5.655  1.00 55.56  ? 259 GLU C CA  1 
ATOM   7179 C  C   . GLU C  1  246 ? -6.735  19.032  6.341  1.00 54.76  ? 259 GLU C C   1 
ATOM   7180 O  O   . GLU C  1  246 ? -7.778  18.906  6.972  1.00 49.51  ? 259 GLU C O   1 
ATOM   7181 C  CB  . GLU C  1  246 ? -6.944  17.416  4.441  1.00 52.67  ? 259 GLU C CB  1 
ATOM   7182 C  CG  . GLU C  1  246 ? -6.284  16.375  3.538  1.00 54.06  ? 259 GLU C CG  1 
ATOM   7183 C  CD  . GLU C  1  246 ? -6.373  14.936  4.029  1.00 55.02  ? 259 GLU C CD  1 
ATOM   7184 O  OE1 . GLU C  1  246 ? -6.926  14.710  5.132  1.00 48.22  ? 259 GLU C OE1 1 
ATOM   7185 O  OE2 . GLU C  1  246 ? -5.896  14.035  3.304  1.00 50.52  ? 259 GLU C OE2 1 
ATOM   7186 N  N   . GLY C  1  247 ? -6.078  20.195  6.231  1.00 54.35  ? 260 GLY C N   1 
ATOM   7187 C  CA  . GLY C  1  247 ? -6.619  21.446  6.739  1.00 58.92  ? 260 GLY C CA  1 
ATOM   7188 C  C   . GLY C  1  247 ? -6.039  21.848  8.096  1.00 58.23  ? 260 GLY C C   1 
ATOM   7189 O  O   . GLY C  1  247 ? -6.303  22.949  8.569  1.00 57.62  ? 260 GLY C O   1 
ATOM   7190 N  N   . ALA C  1  248 ? -5.236  20.973  8.715  1.00 59.85  ? 261 ALA C N   1 
ATOM   7191 C  CA  . ALA C  1  248 ? -4.683  21.228  10.038 1.00 61.31  ? 261 ALA C CA  1 
ATOM   7192 C  C   . ALA C  1  248 ? -3.738  22.431  10.015 1.00 59.38  ? 261 ALA C C   1 
ATOM   7193 O  O   . ALA C  1  248 ? -3.640  23.154  11.004 1.00 55.67  ? 261 ALA C O   1 
ATOM   7194 C  CB  . ALA C  1  248 ? -3.974  19.990  10.552 1.00 61.84  ? 261 ALA C CB  1 
ATOM   7195 N  N   . ASP C  1  249 ? -3.038  22.621  8.889  1.00 62.35  ? 262 ASP C N   1 
ATOM   7196 C  CA  . ASP C  1  249 ? -2.201  23.790  8.644  1.00 68.06  ? 262 ASP C CA  1 
ATOM   7197 C  C   . ASP C  1  249 ? -2.983  25.093  8.850  1.00 67.55  ? 262 ASP C C   1 
ATOM   7198 O  O   . ASP C  1  249 ? -2.469  26.045  9.439  1.00 67.63  ? 262 ASP C O   1 
ATOM   7199 C  CB  . ASP C  1  249 ? -1.573  23.725  7.254  1.00 70.91  ? 262 ASP C CB  1 
ATOM   7200 C  CG  . ASP C  1  249 ? -2.513  23.422  6.088  1.00 72.10  ? 262 ASP C CG  1 
ATOM   7201 O  OD1 . ASP C  1  249 ? -3.713  23.212  6.324  1.00 72.83  ? 262 ASP C OD1 1 
ATOM   7202 O  OD2 . ASP C  1  249 ? -2.040  23.392  4.938  1.00 78.23  ? 262 ASP C OD2 1 
ATOM   7203 N  N   . GLN C  1  250 ? -4.227  25.139  8.355  1.00 68.01  ? 263 GLN C N   1 
ATOM   7204 C  CA  . GLN C  1  250 ? -5.033  26.348  8.402  1.00 67.89  ? 263 GLN C CA  1 
ATOM   7205 C  C   . GLN C  1  250 ? -5.545  26.611  9.812  1.00 70.81  ? 263 GLN C C   1 
ATOM   7206 O  O   . GLN C  1  250 ? -5.804  27.758  10.153 1.00 77.20  ? 263 GLN C O   1 
ATOM   7207 C  CB  . GLN C  1  250 ? -6.245  26.258  7.480  1.00 70.49  ? 263 GLN C CB  1 
ATOM   7208 C  CG  . GLN C  1  250 ? -5.878  26.251  6.003  1.00 72.83  ? 263 GLN C CG  1 
ATOM   7209 C  CD  . GLN C  1  250 ? -7.078  26.257  5.083  1.00 77.86  ? 263 GLN C CD  1 
ATOM   7210 O  OE1 . GLN C  1  250 ? -8.097  26.924  5.318  1.00 77.03  ? 263 GLN C OE1 1 
ATOM   7211 N  NE2 . GLN C  1  250 ? -6.962  25.492  4.003  1.00 86.52  ? 263 GLN C NE2 1 
ATOM   7212 N  N   . VAL C  1  251 ? -5.726  25.545  10.602 1.00 67.67  ? 264 VAL C N   1 
ATOM   7213 C  CA  . VAL C  1  251 ? -6.159  25.664  11.985 1.00 67.22  ? 264 VAL C CA  1 
ATOM   7214 C  C   . VAL C  1  251 ? -5.065  26.359  12.791 1.00 65.81  ? 264 VAL C C   1 
ATOM   7215 O  O   . VAL C  1  251 ? -5.364  27.240  13.593 1.00 73.10  ? 264 VAL C O   1 
ATOM   7216 C  CB  . VAL C  1  251 ? -6.527  24.286  12.573 1.00 68.75  ? 264 VAL C CB  1 
ATOM   7217 C  CG1 . VAL C  1  251 ? -6.732  24.326  14.085 1.00 71.91  ? 264 VAL C CG1 1 
ATOM   7218 C  CG2 . VAL C  1  251 ? -7.769  23.703  11.903 1.00 67.62  ? 264 VAL C CG2 1 
ATOM   7219 N  N   . LEU C  1  252 ? -3.811  25.944  12.572 1.00 63.29  ? 265 LEU C N   1 
ATOM   7220 C  CA  . LEU C  1  252 ? -2.658  26.585  13.183 1.00 65.37  ? 265 LEU C CA  1 
ATOM   7221 C  C   . LEU C  1  252 ? -2.564  28.035  12.710 1.00 69.62  ? 265 LEU C C   1 
ATOM   7222 O  O   . LEU C  1  252 ? -2.355  28.927  13.524 1.00 67.36  ? 265 LEU C O   1 
ATOM   7223 C  CB  . LEU C  1  252 ? -1.369  25.826  12.871 1.00 64.45  ? 265 LEU C CB  1 
ATOM   7224 C  CG  . LEU C  1  252 ? -0.100  26.341  13.558 1.00 67.87  ? 265 LEU C CG  1 
ATOM   7225 C  CD1 . LEU C  1  252 ? -0.200  26.046  15.039 1.00 68.73  ? 265 LEU C CD1 1 
ATOM   7226 C  CD2 . LEU C  1  252 ? 1.179   25.770  12.966 1.00 69.12  ? 265 LEU C CD2 1 
ATOM   7227 N  N   . ALA C  1  253 ? -2.717  28.262  11.397 1.00 71.81  ? 266 ALA C N   1 
ATOM   7228 C  CA  . ALA C  1  253 ? -2.539  29.584  10.811 1.00 76.90  ? 266 ALA C CA  1 
ATOM   7229 C  C   . ALA C  1  253 ? -3.547  30.590  11.379 1.00 77.73  ? 266 ALA C C   1 
ATOM   7230 O  O   . ALA C  1  253 ? -3.227  31.765  11.520 1.00 80.11  ? 266 ALA C O   1 
ATOM   7231 C  CB  . ALA C  1  253 ? -2.635  29.498  9.302  1.00 73.97  ? 266 ALA C CB  1 
ATOM   7232 N  N   . ALA C  1  254 ? -4.759  30.129  11.714 1.00 78.44  ? 267 ALA C N   1 
ATOM   7233 C  CA  . ALA C  1  254 ? -5.802  30.994  12.250 1.00 80.02  ? 267 ALA C CA  1 
ATOM   7234 C  C   . ALA C  1  254 ? -5.395  31.592  13.598 1.00 82.72  ? 267 ALA C C   1 
ATOM   7235 O  O   . ALA C  1  254 ? -5.812  32.699  13.929 1.00 87.47  ? 267 ALA C O   1 
ATOM   7236 C  CB  . ALA C  1  254 ? -7.102  30.227  12.368 1.00 76.61  ? 267 ALA C CB  1 
ATOM   7237 N  N   . HIS C  1  255 ? -4.606  30.852  14.384 1.00 80.20  ? 268 HIS C N   1 
ATOM   7238 C  CA  . HIS C  1  255 ? -4.102  31.346  15.655 1.00 77.43  ? 268 HIS C CA  1 
ATOM   7239 C  C   . HIS C  1  255 ? -2.722  30.753  15.909 1.00 74.61  ? 268 HIS C C   1 
ATOM   7240 O  O   . HIS C  1  255 ? -2.584  29.784  16.658 1.00 77.23  ? 268 HIS C O   1 
ATOM   7241 C  CB  . HIS C  1  255 ? -5.071  31.017  16.791 1.00 79.93  ? 268 HIS C CB  1 
ATOM   7242 C  CG  . HIS C  1  255 ? -6.304  31.853  16.804 1.00 84.47  ? 268 HIS C CG  1 
ATOM   7243 N  ND1 . HIS C  1  255 ? -6.322  33.158  17.251 1.00 85.89  ? 268 HIS C ND1 1 
ATOM   7244 C  CD2 . HIS C  1  255 ? -7.556  31.570  16.420 1.00 87.40  ? 268 HIS C CD2 1 
ATOM   7245 C  CE1 . HIS C  1  255 ? -7.556  33.632  17.150 1.00 90.73  ? 268 HIS C CE1 1 
ATOM   7246 N  NE2 . HIS C  1  255 ? -8.324  32.686  16.645 1.00 87.51  ? 268 HIS C NE2 1 
ATOM   7247 N  N   . PRO C  1  256 ? -1.667  31.314  15.274 1.00 68.83  ? 269 PRO C N   1 
ATOM   7248 C  CA  . PRO C  1  256 ? -0.307  30.793  15.413 1.00 67.06  ? 269 PRO C CA  1 
ATOM   7249 C  C   . PRO C  1  256 ? 0.024   30.498  16.867 1.00 69.74  ? 269 PRO C C   1 
ATOM   7250 O  O   . PRO C  1  256 ? -0.282  31.295  17.752 1.00 76.99  ? 269 PRO C O   1 
ATOM   7251 C  CB  . PRO C  1  256 ? 0.564   31.901  14.819 1.00 63.45  ? 269 PRO C CB  1 
ATOM   7252 C  CG  . PRO C  1  256 ? -0.332  32.518  13.766 1.00 65.87  ? 269 PRO C CG  1 
ATOM   7253 C  CD  . PRO C  1  256 ? -1.736  32.469  14.366 1.00 66.65  ? 269 PRO C CD  1 
ATOM   7254 N  N   . TRP C  1  257 ? 0.636   29.334  17.093 1.00 74.25  ? 270 TRP C N   1 
ATOM   7255 C  CA  . TRP C  1  257 ? 0.937   28.904  18.442 1.00 75.33  ? 270 TRP C CA  1 
ATOM   7256 C  C   . TRP C  1  257 ? 2.211   28.069  18.447 1.00 73.83  ? 270 TRP C C   1 
ATOM   7257 O  O   . TRP C  1  257 ? 2.522   27.384  17.480 1.00 73.38  ? 270 TRP C O   1 
ATOM   7258 C  CB  . TRP C  1  257 ? -0.251  28.143  19.036 1.00 79.74  ? 270 TRP C CB  1 
ATOM   7259 C  CG  . TRP C  1  257 ? -0.116  27.936  20.517 1.00 87.33  ? 270 TRP C CG  1 
ATOM   7260 C  CD1 . TRP C  1  257 ? 0.245   26.791  21.161 1.00 91.59  ? 270 TRP C CD1 1 
ATOM   7261 C  CD2 . TRP C  1  257 ? -0.276  28.942  21.538 1.00 90.46  ? 270 TRP C CD2 1 
ATOM   7262 N  NE1 . TRP C  1  257 ? 0.277   26.996  22.514 1.00 92.73  ? 270 TRP C NE1 1 
ATOM   7263 C  CE2 . TRP C  1  257 ? -0.032  28.307  22.773 1.00 93.26  ? 270 TRP C CE2 1 
ATOM   7264 C  CE3 . TRP C  1  257 ? -0.603  30.302  21.525 1.00 90.97  ? 270 TRP C CE3 1 
ATOM   7265 C  CZ2 . TRP C  1  257 ? -0.115  28.993  23.980 1.00 99.79  ? 270 TRP C CZ2 1 
ATOM   7266 C  CZ3 . TRP C  1  257 ? -0.682  30.979  22.720 1.00 95.02  ? 270 TRP C CZ3 1 
ATOM   7267 C  CH2 . TRP C  1  257 ? -0.437  30.331  23.930 1.00 100.18 ? 270 TRP C CH2 1 
ATOM   7268 N  N   . VAL C  1  258 ? 2.948   28.162  19.553 1.00 73.28  ? 271 VAL C N   1 
ATOM   7269 C  CA  . VAL C  1  258 ? 4.253   27.545  19.668 1.00 75.11  ? 271 VAL C CA  1 
ATOM   7270 C  C   . VAL C  1  258 ? 4.178   26.490  20.767 1.00 75.49  ? 271 VAL C C   1 
ATOM   7271 O  O   . VAL C  1  258 ? 3.529   26.700  21.792 1.00 72.17  ? 271 VAL C O   1 
ATOM   7272 C  CB  . VAL C  1  258 ? 5.314   28.623  19.962 1.00 76.85  ? 271 VAL C CB  1 
ATOM   7273 C  CG1 . VAL C  1  258 ? 6.681   28.025  20.260 1.00 78.83  ? 271 VAL C CG1 1 
ATOM   7274 C  CG2 . VAL C  1  258 ? 5.422   29.637  18.830 1.00 75.23  ? 271 VAL C CG2 1 
ATOM   7275 N  N   . PRO C  1  259 ? 4.820   25.313  20.582 1.00 71.25  ? 272 PRO C N   1 
ATOM   7276 C  CA  . PRO C  1  259 ? 4.847   24.293  21.627 1.00 73.62  ? 272 PRO C CA  1 
ATOM   7277 C  C   . PRO C  1  259 ? 5.472   24.830  22.912 1.00 71.93  ? 272 PRO C C   1 
ATOM   7278 O  O   . PRO C  1  259 ? 6.357   25.685  22.870 1.00 72.56  ? 272 PRO C O   1 
ATOM   7279 C  CB  . PRO C  1  259 ? 5.665   23.143  20.998 1.00 71.72  ? 272 PRO C CB  1 
ATOM   7280 C  CG  . PRO C  1  259 ? 6.448   23.807  19.883 1.00 71.11  ? 272 PRO C CG  1 
ATOM   7281 C  CD  . PRO C  1  259 ? 5.528   24.890  19.364 1.00 71.13  ? 272 PRO C CD  1 
ATOM   7282 N  N   . GLY C  1  260 ? 4.981   24.321  24.046 1.00 68.85  ? 273 GLY C N   1 
ATOM   7283 C  CA  . GLY C  1  260 ? 5.458   24.733  25.355 1.00 70.75  ? 273 GLY C CA  1 
ATOM   7284 C  C   . GLY C  1  260 ? 4.538   24.194  26.447 1.00 72.74  ? 273 GLY C C   1 
ATOM   7285 O  O   . GLY C  1  260 ? 3.923   23.139  26.278 1.00 73.26  ? 273 GLY C O   1 
ATOM   7286 N  N   . GLY C  1  261 ? 4.447   24.936  27.555 1.00 72.09  ? 274 GLY C N   1 
ATOM   7287 C  CA  . GLY C  1  261 ? 3.590   24.570  28.671 1.00 74.38  ? 274 GLY C CA  1 
ATOM   7288 C  C   . GLY C  1  261 ? 3.659   25.612  29.788 1.00 76.65  ? 274 GLY C C   1 
ATOM   7289 O  O   . GLY C  1  261 ? 4.510   26.509  29.773 1.00 69.27  ? 274 GLY C O   1 
ATOM   7290 N  N   . ASN C  1  262 ? 2.740   25.479  30.751 1.00 74.63  ? 275 ASN C N   1 
ATOM   7291 C  CA  . ASN C  1  262 ? 2.791   26.251  31.981 1.00 74.72  ? 275 ASN C CA  1 
ATOM   7292 C  C   . ASN C  1  262 ? 3.993   25.788  32.798 1.00 80.59  ? 275 ASN C C   1 
ATOM   7293 O  O   . ASN C  1  262 ? 4.116   24.596  33.070 1.00 82.97  ? 275 ASN C O   1 
ATOM   7294 C  CB  . ASN C  1  262 ? 1.519   26.089  32.807 1.00 70.09  ? 275 ASN C CB  1 
ATOM   7295 C  CG  . ASN C  1  262 ? 0.405   27.022  32.387 1.00 71.58  ? 275 ASN C CG  1 
ATOM   7296 O  OD1 . ASN C  1  262 ? 0.646   28.055  31.747 1.00 68.10  ? 275 ASN C OD1 1 
ATOM   7297 N  ND2 . ASN C  1  262 ? -0.822  26.690  32.769 1.00 69.90  ? 275 ASN C ND2 1 
ATOM   7298 N  N   . ALA C  1  263 ? 4.862   26.726  33.196 1.00 83.78  ? 276 ALA C N   1 
ATOM   7299 C  CA  . ALA C  1  263 ? 6.059   26.388  33.955 1.00 88.30  ? 276 ALA C CA  1 
ATOM   7300 C  C   . ALA C  1  263 ? 5.808   26.530  35.457 1.00 91.08  ? 276 ALA C C   1 
ATOM   7301 O  O   . ALA C  1  263 ? 4.953   27.309  35.880 1.00 90.14  ? 276 ALA C O   1 
ATOM   7302 C  CB  . ALA C  1  263 ? 7.219   27.252  33.510 1.00 85.00  ? 276 ALA C CB  1 
ATOM   7303 N  N   . ASP C  1  264 ? 6.560   25.743  36.242 1.00 89.79  ? 277 ASP C N   1 
ATOM   7304 C  CA  . ASP C  1  264 ? 6.668   25.887  37.687 1.00 90.04  ? 277 ASP C CA  1 
ATOM   7305 C  C   . ASP C  1  264 ? 5.301   25.781  38.361 1.00 90.42  ? 277 ASP C C   1 
ATOM   7306 O  O   . ASP C  1  264 ? 5.023   26.529  39.292 1.00 95.04  ? 277 ASP C O   1 
ATOM   7307 C  CB  . ASP C  1  264 ? 7.364   27.187  38.066 1.00 93.86  ? 277 ASP C CB  1 
ATOM   7308 C  CG  . ASP C  1  264 ? 8.749   27.392  37.470 1.00 98.30  ? 277 ASP C CG  1 
ATOM   7309 O  OD1 . ASP C  1  264 ? 9.605   26.507  37.670 1.00 91.91  ? 277 ASP C OD1 1 
ATOM   7310 O  OD2 . ASP C  1  264 ? 8.967   28.442  36.825 1.00 101.16 ? 277 ASP C OD2 1 
ATOM   7311 N  N   . ASN C  1  265 ? 4.457   24.855  37.888 1.00 86.27  ? 278 ASN C N   1 
ATOM   7312 C  CA  . ASN C  1  265 ? 3.208   24.504  38.551 1.00 86.29  ? 278 ASN C CA  1 
ATOM   7313 C  C   . ASN C  1  265 ? 2.353   25.753  38.790 1.00 85.96  ? 278 ASN C C   1 
ATOM   7314 O  O   . ASN C  1  265 ? 1.693   25.866  39.820 1.00 80.11  ? 278 ASN C O   1 
ATOM   7315 C  CB  . ASN C  1  265 ? 3.501   23.733  39.836 1.00 87.18  ? 278 ASN C CB  1 
ATOM   7316 C  CG  . ASN C  1  265 ? 2.367   22.838  40.271 1.00 94.22  ? 278 ASN C CG  1 
ATOM   7317 O  OD1 . ASN C  1  265 ? 1.569   22.388  39.438 1.00 103.93 ? 278 ASN C OD1 1 
ATOM   7318 N  ND2 . ASN C  1  265 ? 2.301   22.543  41.561 1.00 97.30  ? 278 ASN C ND2 1 
ATOM   7319 N  N   . GLN C  1  266 ? 2.346   26.675  37.820 1.00 87.64  ? 279 GLN C N   1 
ATOM   7320 C  CA  . GLN C  1  266 ? 1.585   27.913  37.923 1.00 87.22  ? 279 GLN C CA  1 
ATOM   7321 C  C   . GLN C  1  266 ? 0.719   28.084  36.678 1.00 83.01  ? 279 GLN C C   1 
ATOM   7322 O  O   . GLN C  1  266 ? 1.175   27.810  35.569 1.00 86.70  ? 279 GLN C O   1 
ATOM   7323 C  CB  . GLN C  1  266 ? 2.496   29.137  38.009 1.00 90.83  ? 279 GLN C CB  1 
ATOM   7324 C  CG  . GLN C  1  266 ? 3.303   29.282  39.297 1.00 93.09  ? 279 GLN C CG  1 
ATOM   7325 C  CD  . GLN C  1  266 ? 4.411   30.311  39.171 1.00 93.73  ? 279 GLN C CD  1 
ATOM   7326 O  OE1 . GLN C  1  266 ? 4.212   31.373  38.571 1.00 85.64  ? 279 GLN C OE1 1 
ATOM   7327 N  NE2 . GLN C  1  266 ? 5.599   30.001  39.685 1.00 95.69  ? 279 GLN C NE2 1 
ATOM   7328 N  N   . VAL C  1  267 ? -0.520  28.555  36.865 1.00 77.56  ? 280 VAL C N   1 
ATOM   7329 C  CA  . VAL C  1  267 ? -1.400  28.879  35.750 1.00 77.83  ? 280 VAL C CA  1 
ATOM   7330 C  C   . VAL C  1  267 ? -0.917  30.171  35.091 1.00 73.80  ? 280 VAL C C   1 
ATOM   7331 O  O   . VAL C  1  267 ? -0.056  30.862  35.631 1.00 80.37  ? 280 VAL C O   1 
ATOM   7332 C  CB  . VAL C  1  267 ? -2.880  28.993  36.171 1.00 82.38  ? 280 VAL C CB  1 
ATOM   7333 C  CG1 . VAL C  1  267 ? -3.447  27.655  36.623 1.00 84.64  ? 280 VAL C CG1 1 
ATOM   7334 C  CG2 . VAL C  1  267 ? -3.107  30.050  37.249 1.00 84.34  ? 280 VAL C CG2 1 
ATOM   7335 N  N   . ASN C  1  268 ? -1.474  30.473  33.912 1.00 70.58  ? 281 ASN C N   1 
ATOM   7336 C  CA  . ASN C  1  268 ? -1.148  31.672  33.151 1.00 75.44  ? 281 ASN C CA  1 
ATOM   7337 C  C   . ASN C  1  268 ? 0.361   31.909  33.124 1.00 75.67  ? 281 ASN C C   1 
ATOM   7338 O  O   . ASN C  1  268 ? 0.817   33.025  33.352 1.00 81.22  ? 281 ASN C O   1 
ATOM   7339 C  CB  . ASN C  1  268 ? -1.888  32.889  33.693 1.00 75.36  ? 281 ASN C CB  1 
ATOM   7340 C  CG  . ASN C  1  268 ? -3.383  32.764  33.525 1.00 77.52  ? 281 ASN C CG  1 
ATOM   7341 O  OD1 . ASN C  1  268 ? -3.888  32.800  32.398 1.00 73.19  ? 281 ASN C OD1 1 
ATOM   7342 N  ND2 . ASN C  1  268 ? -4.107  32.629  34.626 1.00 79.65  ? 281 ASN C ND2 1 
ATOM   7343 N  N   . ASN C  1  269 ? 1.128   30.863  32.805 1.00 77.84  ? 282 ASN C N   1 
ATOM   7344 C  CA  . ASN C  1  269 ? 2.579   30.931  32.858 1.00 79.74  ? 282 ASN C CA  1 
ATOM   7345 C  C   . ASN C  1  269 ? 3.172   30.085  31.731 1.00 80.30  ? 282 ASN C C   1 
ATOM   7346 O  O   . ASN C  1  269 ? 4.013   29.219  31.973 1.00 77.57  ? 282 ASN C O   1 
ATOM   7347 C  CB  . ASN C  1  269 ? 3.081   30.503  34.234 1.00 76.53  ? 282 ASN C CB  1 
ATOM   7348 C  CG  . ASN C  1  269 ? 4.534   30.853  34.452 1.00 73.60  ? 282 ASN C CG  1 
ATOM   7349 O  OD1 . ASN C  1  269 ? 5.030   31.845  33.905 1.00 68.69  ? 282 ASN C OD1 1 
ATOM   7350 N  ND2 . ASN C  1  269 ? 5.231   30.059  35.250 1.00 74.25  ? 282 ASN C ND2 1 
ATOM   7351 N  N   . TYR C  1  270 ? 2.745   30.367  30.494 1.00 80.58  ? 283 TYR C N   1 
ATOM   7352 C  CA  . TYR C  1  270 ? 3.109   29.545  29.352 1.00 78.01  ? 283 TYR C CA  1 
ATOM   7353 C  C   . TYR C  1  270 ? 4.485   29.963  28.836 1.00 79.45  ? 283 TYR C C   1 
ATOM   7354 O  O   . TYR C  1  270 ? 4.667   31.106  28.424 1.00 76.43  ? 283 TYR C O   1 
ATOM   7355 C  CB  . TYR C  1  270 ? 2.046   29.656  28.255 1.00 75.62  ? 283 TYR C CB  1 
ATOM   7356 C  CG  . TYR C  1  270 ? 2.185   28.627  27.138 1.00 79.22  ? 283 TYR C CG  1 
ATOM   7357 C  CD1 . TYR C  1  270 ? 3.071   28.819  26.083 1.00 78.68  ? 283 TYR C CD1 1 
ATOM   7358 C  CD2 . TYR C  1  270 ? 1.412   27.468  27.126 1.00 81.15  ? 283 TYR C CD2 1 
ATOM   7359 C  CE1 . TYR C  1  270 ? 3.196   27.888  25.065 1.00 80.96  ? 283 TYR C CE1 1 
ATOM   7360 C  CE2 . TYR C  1  270 ? 1.527   26.529  26.112 1.00 80.90  ? 283 TYR C CE2 1 
ATOM   7361 C  CZ  . TYR C  1  270 ? 2.431   26.731  25.083 1.00 80.57  ? 283 TYR C CZ  1 
ATOM   7362 O  OH  . TYR C  1  270 ? 2.528   25.806  24.080 1.00 75.62  ? 283 TYR C OH  1 
ATOM   7363 N  N   . VAL C  1  271 ? 5.431   29.012  28.852 1.00 86.38  ? 284 VAL C N   1 
ATOM   7364 C  CA  . VAL C  1  271 ? 6.779   29.213  28.346 1.00 83.64  ? 284 VAL C CA  1 
ATOM   7365 C  C   . VAL C  1  271 ? 6.970   28.336  27.111 1.00 82.33  ? 284 VAL C C   1 
ATOM   7366 O  O   . VAL C  1  271 ? 6.698   27.136  27.154 1.00 74.14  ? 284 VAL C O   1 
ATOM   7367 C  CB  . VAL C  1  271 ? 7.843   28.874  29.406 1.00 87.59  ? 284 VAL C CB  1 
ATOM   7368 C  CG1 . VAL C  1  271 ? 9.253   29.118  28.876 1.00 86.18  ? 284 VAL C CG1 1 
ATOM   7369 C  CG2 . VAL C  1  271 ? 7.618   29.634  30.709 1.00 91.96  ? 284 VAL C CG2 1 
ATOM   7370 N  N   . GLU C  1  272 ? 7.479   28.949  26.031 1.00 79.53  ? 285 GLU C N   1 
ATOM   7371 C  CA  A GLU C  1  272 ? 7.750   28.235  24.795 0.50 76.42  ? 285 GLU C CA  1 
ATOM   7372 C  CA  B GLU C  1  272 ? 7.788   28.267  24.782 0.50 78.14  ? 285 GLU C CA  1 
ATOM   7373 C  C   . GLU C  1  272 ? 8.905   27.256  25.015 1.00 78.95  ? 285 GLU C C   1 
ATOM   7374 O  O   . GLU C  1  272 ? 9.811   27.522  25.799 1.00 73.38  ? 285 GLU C O   1 
ATOM   7375 C  CB  A GLU C  1  272 ? 8.007   29.254  23.684 0.50 73.15  ? 285 GLU C CB  1 
ATOM   7376 C  CB  B GLU C  1  272 ? 8.269   29.247  23.704 0.50 77.05  ? 285 GLU C CB  1 
ATOM   7377 C  CG  A GLU C  1  272 ? 6.800   30.166  23.441 0.50 68.16  ? 285 GLU C CG  1 
ATOM   7378 C  CG  B GLU C  1  272 ? 9.119   28.593  22.615 0.50 74.75  ? 285 GLU C CG  1 
ATOM   7379 C  CD  A GLU C  1  272 ? 6.977   31.391  22.556 0.50 63.10  ? 285 GLU C CD  1 
ATOM   7380 C  CD  B GLU C  1  272 ? 9.534   29.485  21.459 0.50 71.10  ? 285 GLU C CD  1 
ATOM   7381 O  OE1 A GLU C  1  272 ? 8.076   31.593  22.006 0.50 60.25  ? 285 GLU C OE1 1 
ATOM   7382 O  OE1 B GLU C  1  272 ? 9.097   30.651  21.409 0.50 68.50  ? 285 GLU C OE1 1 
ATOM   7383 O  OE2 A GLU C  1  272 ? 5.992   32.154  22.430 0.50 55.82  ? 285 GLU C OE2 1 
ATOM   7384 O  OE2 B GLU C  1  272 ? 10.300  28.997  20.602 0.50 68.77  ? 285 GLU C OE2 1 
ATOM   7385 N  N   . ASP C  1  273 ? 8.831   26.108  24.319 1.00 83.82  ? 286 ASP C N   1 
ATOM   7386 C  CA  . ASP C  1  273 ? 9.903   25.121  24.303 1.00 83.29  ? 286 ASP C CA  1 
ATOM   7387 C  C   . ASP C  1  273 ? 10.482  25.057  22.892 1.00 82.62  ? 286 ASP C C   1 
ATOM   7388 O  O   . ASP C  1  273 ? 9.868   24.468  22.003 1.00 84.66  ? 286 ASP C O   1 
ATOM   7389 C  CB  . ASP C  1  273 ? 9.442   23.742  24.758 1.00 82.95  ? 286 ASP C CB  1 
ATOM   7390 C  CG  . ASP C  1  273 ? 10.499  22.644  24.701 1.00 82.14  ? 286 ASP C CG  1 
ATOM   7391 O  OD1 . ASP C  1  273 ? 11.655  22.939  24.314 1.00 83.04  ? 286 ASP C OD1 1 
ATOM   7392 O  OD2 . ASP C  1  273 ? 10.164  21.495  25.048 1.00 78.97  ? 286 ASP C OD2 1 
ATOM   7393 N  N   . PRO C  1  274 ? 11.683  25.636  22.653 1.00 84.26  ? 287 PRO C N   1 
ATOM   7394 C  CA  . PRO C  1  274 ? 12.263  25.690  21.309 1.00 83.34  ? 287 PRO C CA  1 
ATOM   7395 C  C   . PRO C  1  274 ? 12.765  24.352  20.764 1.00 76.81  ? 287 PRO C C   1 
ATOM   7396 O  O   . PRO C  1  274 ? 12.996  24.232  19.561 1.00 73.52  ? 287 PRO C O   1 
ATOM   7397 C  CB  . PRO C  1  274 ? 13.420  26.696  21.496 1.00 84.70  ? 287 PRO C CB  1 
ATOM   7398 C  CG  . PRO C  1  274 ? 13.866  26.475  22.929 1.00 88.00  ? 287 PRO C CG  1 
ATOM   7399 C  CD  . PRO C  1  274 ? 12.554  26.253  23.668 1.00 88.63  ? 287 PRO C CD  1 
ATOM   7400 N  N   . ASP C  1  275 ? 12.947  23.365  21.659 1.00 70.08  ? 288 ASP C N   1 
ATOM   7401 C  CA  . ASP C  1  275 ? 13.475  22.057  21.299 1.00 71.41  ? 288 ASP C CA  1 
ATOM   7402 C  C   . ASP C  1  275 ? 12.370  21.112  20.820 1.00 65.31  ? 288 ASP C C   1 
ATOM   7403 O  O   . ASP C  1  275 ? 12.672  20.099  20.200 1.00 57.02  ? 288 ASP C O   1 
ATOM   7404 C  CB  . ASP C  1  275 ? 14.236  21.441  22.465 1.00 73.95  ? 288 ASP C CB  1 
ATOM   7405 C  CG  . ASP C  1  275 ? 15.543  22.133  22.840 1.00 77.88  ? 288 ASP C CG  1 
ATOM   7406 O  OD1 . ASP C  1  275 ? 15.966  23.039  22.092 1.00 79.36  ? 288 ASP C OD1 1 
ATOM   7407 O  OD2 . ASP C  1  275 ? 16.122  21.784  23.889 1.00 74.46  ? 288 ASP C OD2 1 
ATOM   7408 N  N   . SER C  1  276 ? 11.102  21.434  21.117 1.00 61.89  ? 289 SER C N   1 
ATOM   7409 C  CA  . SER C  1  276 ? 9.971   20.583  20.773 1.00 60.82  ? 289 SER C CA  1 
ATOM   7410 C  C   . SER C  1  276 ? 9.854   20.426  19.260 1.00 60.90  ? 289 SER C C   1 
ATOM   7411 O  O   . SER C  1  276 ? 10.238  21.302  18.492 1.00 61.21  ? 289 SER C O   1 
ATOM   7412 C  CB  . SER C  1  276 ? 8.677   21.136  21.345 1.00 65.45  ? 289 SER C CB  1 
ATOM   7413 O  OG  . SER C  1  276 ? 7.529   20.503  20.786 1.00 63.84  ? 289 SER C OG  1 
ATOM   7414 N  N   . ALA C  1  277 ? 9.286   19.296  18.839 1.00 60.59  ? 290 ALA C N   1 
ATOM   7415 C  CA  . ALA C  1  277 ? 8.813   19.147  17.478 1.00 58.16  ? 290 ALA C CA  1 
ATOM   7416 C  C   . ALA C  1  277 ? 7.783   20.233  17.176 1.00 55.26  ? 290 ALA C C   1 
ATOM   7417 O  O   . ALA C  1  277 ? 7.120   20.755  18.072 1.00 56.11  ? 290 ALA C O   1 
ATOM   7418 C  CB  . ALA C  1  277 ? 8.226   17.772  17.293 1.00 57.52  ? 290 ALA C CB  1 
ATOM   7419 N  N   . ASP C  1  278 ? 7.691   20.577  15.892 1.00 53.61  ? 291 ASP C N   1 
ATOM   7420 C  CA  . ASP C  1  278 ? 6.608   21.392  15.365 1.00 56.35  ? 291 ASP C CA  1 
ATOM   7421 C  C   . ASP C  1  278 ? 6.400   20.939  13.920 1.00 55.43  ? 291 ASP C C   1 
ATOM   7422 O  O   . ASP C  1  278 ? 6.982   19.939  13.496 1.00 59.51  ? 291 ASP C O   1 
ATOM   7423 C  CB  . ASP C  1  278 ? 6.894   22.876  15.570 1.00 59.65  ? 291 ASP C CB  1 
ATOM   7424 C  CG  . ASP C  1  278 ? 8.094   23.436  14.813 1.00 62.80  ? 291 ASP C CG  1 
ATOM   7425 O  OD1 . ASP C  1  278 ? 8.513   22.812  13.821 1.00 60.05  ? 291 ASP C OD1 1 
ATOM   7426 O  OD2 . ASP C  1  278 ? 8.613   24.492  15.228 1.00 76.61  ? 291 ASP C OD2 1 
ATOM   7427 N  N   . PHE C  1  279 ? 5.597   21.688  13.159 1.00 55.91  ? 292 PHE C N   1 
ATOM   7428 C  CA  . PHE C  1  279 ? 5.138   21.222  11.864 1.00 56.13  ? 292 PHE C CA  1 
ATOM   7429 C  C   . PHE C  1  279 ? 6.212   21.371  10.788 1.00 60.90  ? 292 PHE C C   1 
ATOM   7430 O  O   . PHE C  1  279 ? 6.067   20.781  9.719  1.00 61.38  ? 292 PHE C O   1 
ATOM   7431 C  CB  . PHE C  1  279 ? 3.823   21.912  11.508 1.00 54.28  ? 292 PHE C CB  1 
ATOM   7432 C  CG  . PHE C  1  279 ? 2.656   21.293  12.263 1.00 58.04  ? 292 PHE C CG  1 
ATOM   7433 C  CD1 . PHE C  1  279 ? 2.084   20.101  11.822 1.00 56.37  ? 292 PHE C CD1 1 
ATOM   7434 C  CD2 . PHE C  1  279 ? 2.157   21.882  13.424 1.00 56.72  ? 292 PHE C CD2 1 
ATOM   7435 C  CE1 . PHE C  1  279 ? 1.029   19.525  12.512 1.00 60.45  ? 292 PHE C CE1 1 
ATOM   7436 C  CE2 . PHE C  1  279 ? 1.093   21.306  14.109 1.00 56.48  ? 292 PHE C CE2 1 
ATOM   7437 C  CZ  . PHE C  1  279 ? 0.531   20.130  13.651 1.00 60.96  ? 292 PHE C CZ  1 
ATOM   7438 N  N   . THR C  1  280 ? 7.288   22.119  11.065 1.00 59.83  ? 293 THR C N   1 
ATOM   7439 C  CA  . THR C  1  280 ? 8.412   22.178  10.140 1.00 58.96  ? 293 THR C CA  1 
ATOM   7440 C  C   . THR C  1  280 ? 9.599   21.397  10.703 1.00 57.88  ? 293 THR C C   1 
ATOM   7441 O  O   . THR C  1  280 ? 10.678  21.414  10.113 1.00 59.18  ? 293 THR C O   1 
ATOM   7442 C  CB  . THR C  1  280 ? 8.777   23.632  9.838  1.00 63.96  ? 293 THR C CB  1 
ATOM   7443 O  OG1 . THR C  1  280 ? 9.174   24.235  11.065 1.00 69.84  ? 293 THR C OG1 1 
ATOM   7444 C  CG2 . THR C  1  280 ? 7.618   24.412  9.242  1.00 63.94  ? 293 THR C CG2 1 
ATOM   7445 N  N   . HIS C  1  281 ? 9.394   20.704  11.834 1.00 60.55  ? 294 HIS C N   1 
ATOM   7446 C  CA  . HIS C  1  281 ? 10.438  19.904  12.458 1.00 60.33  ? 294 HIS C CA  1 
ATOM   7447 C  C   . HIS C  1  281 ? 9.843   18.581  12.943 1.00 58.78  ? 294 HIS C C   1 
ATOM   7448 O  O   . HIS C  1  281 ? 9.991   18.217  14.108 1.00 58.49  ? 294 HIS C O   1 
ATOM   7449 C  CB  . HIS C  1  281 ? 11.116  20.672  13.603 1.00 62.01  ? 294 HIS C CB  1 
ATOM   7450 C  CG  . HIS C  1  281 ? 11.833  21.917  13.195 1.00 67.19  ? 294 HIS C CG  1 
ATOM   7451 N  ND1 . HIS C  1  281 ? 13.186  21.925  12.922 1.00 70.67  ? 294 HIS C ND1 1 
ATOM   7452 C  CD2 . HIS C  1  281 ? 11.414  23.183  13.043 1.00 67.73  ? 294 HIS C CD2 1 
ATOM   7453 C  CE1 . HIS C  1  281 ? 13.561  23.151  12.587 1.00 72.95  ? 294 HIS C CE1 1 
ATOM   7454 N  NE2 . HIS C  1  281 ? 12.500  23.930  12.651 1.00 73.98  ? 294 HIS C NE2 1 
ATOM   7455 N  N   . LEU C  1  282 ? 9.210   17.842  12.022 1.00 56.33  ? 295 LEU C N   1 
ATOM   7456 C  CA  . LEU C  1  282 ? 8.473   16.637  12.369 1.00 51.64  ? 295 LEU C CA  1 
ATOM   7457 C  C   . LEU C  1  282 ? 9.387   15.509  12.852 1.00 48.26  ? 295 LEU C C   1 
ATOM   7458 O  O   . LEU C  1  282 ? 8.987   14.754  13.724 1.00 46.46  ? 295 LEU C O   1 
ATOM   7459 C  CB  . LEU C  1  282 ? 7.604   16.185  11.198 1.00 49.09  ? 295 LEU C CB  1 
ATOM   7460 C  CG  . LEU C  1  282 ? 6.383   17.058  10.904 1.00 49.36  ? 295 LEU C CG  1 
ATOM   7461 C  CD1 . LEU C  1  282 ? 5.688   16.590  9.637  1.00 49.92  ? 295 LEU C CD1 1 
ATOM   7462 C  CD2 . LEU C  1  282 ? 5.408   17.046  12.058 1.00 50.52  ? 295 LEU C CD2 1 
ATOM   7463 N  N   . CYS C  1  283 ? 10.590  15.371  12.297 1.00 46.73  ? 296 CYS C N   1 
ATOM   7464 C  CA  . CYS C  1  283 ? 11.464  14.260  12.645 1.00 51.19  ? 296 CYS C CA  1 
ATOM   7465 C  C   . CYS C  1  283 ? 11.892  14.319  14.108 1.00 49.15  ? 296 CYS C C   1 
ATOM   7466 O  O   . CYS C  1  283 ? 12.231  13.283  14.681 1.00 48.06  ? 296 CYS C O   1 
ATOM   7467 C  CB  . CYS C  1  283 ? 12.692  14.132  11.744 1.00 56.38  ? 296 CYS C CB  1 
ATOM   7468 S  SG  . CYS C  1  283 ? 12.324  13.682  10.020 1.00 63.26  ? 296 CYS C SG  1 
ATOM   7469 N  N   . ARG C  1  284 ? 11.860  15.509  14.718 1.00 49.00  ? 297 ARG C N   1 
ATOM   7470 C  CA  . ARG C  1  284 ? 12.107  15.625  16.148 1.00 51.72  ? 297 ARG C CA  1 
ATOM   7471 C  C   . ARG C  1  284 ? 11.129  14.754  16.929 1.00 48.06  ? 297 ARG C C   1 
ATOM   7472 O  O   . ARG C  1  284 ? 11.480  14.206  17.973 1.00 48.63  ? 297 ARG C O   1 
ATOM   7473 C  CB  . ARG C  1  284 ? 11.925  17.051  16.682 1.00 60.21  ? 297 ARG C CB  1 
ATOM   7474 C  CG  . ARG C  1  284 ? 12.990  18.017  16.191 1.00 64.28  ? 297 ARG C CG  1 
ATOM   7475 C  CD  . ARG C  1  284 ? 12.829  19.376  16.849 1.00 65.61  ? 297 ARG C CD  1 
ATOM   7476 N  NE  . ARG C  1  284 ? 13.840  20.318  16.361 1.00 67.83  ? 297 ARG C NE  1 
ATOM   7477 C  CZ  . ARG C  1  284 ? 13.848  21.620  16.608 1.00 70.44  ? 297 ARG C CZ  1 
ATOM   7478 N  NH1 . ARG C  1  284 ? 12.937  22.156  17.407 1.00 69.14  ? 297 ARG C NH1 1 
ATOM   7479 N  NH2 . ARG C  1  284 ? 14.794  22.372  16.069 1.00 71.87  ? 297 ARG C NH2 1 
ATOM   7480 N  N   . LEU C  1  285 ? 9.889   14.674  16.430 1.00 50.00  ? 298 LEU C N   1 
ATOM   7481 C  CA  . LEU C  1  285 ? 8.865   13.865  17.066 1.00 48.87  ? 298 LEU C CA  1 
ATOM   7482 C  C   . LEU C  1  285 ? 9.292   12.403  17.017 1.00 47.01  ? 298 LEU C C   1 
ATOM   7483 O  O   . LEU C  1  285 ? 9.197   11.703  18.018 1.00 47.24  ? 298 LEU C O   1 
ATOM   7484 C  CB  . LEU C  1  285 ? 7.500   14.098  16.417 1.00 47.47  ? 298 LEU C CB  1 
ATOM   7485 C  CG  . LEU C  1  285 ? 6.305   13.442  17.113 1.00 48.66  ? 298 LEU C CG  1 
ATOM   7486 C  CD1 . LEU C  1  285 ? 5.032   14.186  16.810 1.00 51.04  ? 298 LEU C CD1 1 
ATOM   7487 C  CD2 . LEU C  1  285 ? 6.107   11.998  16.711 1.00 54.08  ? 298 LEU C CD2 1 
ATOM   7488 N  N   . TYR C  1  286 ? 9.789   11.963  15.856 1.00 48.07  ? 299 TYR C N   1 
ATOM   7489 C  CA  . TYR C  1  286 ? 10.275  10.603  15.690 1.00 46.46  ? 299 TYR C CA  1 
ATOM   7490 C  C   . TYR C  1  286 ? 11.353  10.317  16.735 1.00 46.56  ? 299 TYR C C   1 
ATOM   7491 O  O   . TYR C  1  286 ? 11.273  9.324   17.462 1.00 45.04  ? 299 TYR C O   1 
ATOM   7492 C  CB  . TYR C  1  286 ? 10.741  10.369  14.245 1.00 42.53  ? 299 TYR C CB  1 
ATOM   7493 C  CG  . TYR C  1  286 ? 11.441  9.035   14.048 1.00 38.45  ? 299 TYR C CG  1 
ATOM   7494 C  CD1 . TYR C  1  286 ? 10.749  7.841   14.206 1.00 38.32  ? 299 TYR C CD1 1 
ATOM   7495 C  CD2 . TYR C  1  286 ? 12.792  8.968   13.737 1.00 39.42  ? 299 TYR C CD2 1 
ATOM   7496 C  CE1 . TYR C  1  286 ? 11.376  6.617   14.065 1.00 38.21  ? 299 TYR C CE1 1 
ATOM   7497 C  CE2 . TYR C  1  286 ? 13.433  7.750   13.595 1.00 39.78  ? 299 TYR C CE2 1 
ATOM   7498 C  CZ  . TYR C  1  286 ? 12.722  6.575   13.757 1.00 37.70  ? 299 TYR C CZ  1 
ATOM   7499 O  OH  . TYR C  1  286 ? 13.329  5.366   13.603 1.00 39.37  ? 299 TYR C OH  1 
ATOM   7500 N  N   . GLU C  1  287 ? 12.339  11.216  16.827 1.00 48.05  ? 300 GLU C N   1 
ATOM   7501 C  CA  . GLU C  1  287 ? 13.490  11.013  17.697 1.00 52.30  ? 300 GLU C CA  1 
ATOM   7502 C  C   . GLU C  1  287 ? 13.062  11.055  19.166 1.00 47.06  ? 300 GLU C C   1 
ATOM   7503 O  O   . GLU C  1  287 ? 13.519  10.242  19.964 1.00 43.85  ? 300 GLU C O   1 
ATOM   7504 C  CB  . GLU C  1  287 ? 14.571  12.059  17.413 1.00 56.71  ? 300 GLU C CB  1 
ATOM   7505 C  CG  . GLU C  1  287 ? 15.157  11.994  16.005 1.00 64.84  ? 300 GLU C CG  1 
ATOM   7506 C  CD  . GLU C  1  287 ? 15.794  13.288  15.497 1.00 76.80  ? 300 GLU C CD  1 
ATOM   7507 O  OE1 . GLU C  1  287 ? 16.308  14.106  16.292 1.00 84.95  ? 300 GLU C OE1 1 
ATOM   7508 O  OE2 . GLU C  1  287 ? 15.727  13.509  14.271 1.00 83.02  ? 300 GLU C OE2 1 
ATOM   7509 N  N   . PHE C  1  288 ? 12.172  11.993  19.512 1.00 44.51  ? 301 PHE C N   1 
ATOM   7510 C  CA  . PHE C  1  288 ? 11.676  12.107  20.874 1.00 46.40  ? 301 PHE C CA  1 
ATOM   7511 C  C   . PHE C  1  288 ? 11.030  10.786  21.281 1.00 44.79  ? 301 PHE C C   1 
ATOM   7512 O  O   . PHE C  1  288 ? 11.333  10.249  22.337 1.00 44.46  ? 301 PHE C O   1 
ATOM   7513 C  CB  . PHE C  1  288 ? 10.689  13.271  21.006 1.00 52.00  ? 301 PHE C CB  1 
ATOM   7514 C  CG  . PHE C  1  288 ? 10.138  13.465  22.414 1.00 54.31  ? 301 PHE C CG  1 
ATOM   7515 C  CD1 . PHE C  1  288 ? 10.800  14.272  23.336 1.00 55.76  ? 301 PHE C CD1 1 
ATOM   7516 C  CD2 . PHE C  1  288 ? 8.970   12.826  22.817 1.00 53.89  ? 301 PHE C CD2 1 
ATOM   7517 C  CE1 . PHE C  1  288 ? 10.295  14.444  24.621 1.00 57.15  ? 301 PHE C CE1 1 
ATOM   7518 C  CE2 . PHE C  1  288 ? 8.466   13.005  24.100 1.00 54.80  ? 301 PHE C CE2 1 
ATOM   7519 C  CZ  . PHE C  1  288 ? 9.127   13.815  24.999 1.00 54.52  ? 301 PHE C CZ  1 
ATOM   7520 N  N   . VAL C  1  289 ? 10.152  10.248  20.426 1.00 44.32  ? 302 VAL C N   1 
ATOM   7521 C  CA  . VAL C  1  289 ? 9.416   9.041   20.768 1.00 42.76  ? 302 VAL C CA  1 
ATOM   7522 C  C   . VAL C  1  289 ? 10.371  7.855   20.896 1.00 39.53  ? 302 VAL C C   1 
ATOM   7523 O  O   . VAL C  1  289 ? 10.199  7.012   21.779 1.00 39.97  ? 302 VAL C O   1 
ATOM   7524 C  CB  . VAL C  1  289 ? 8.279   8.745   19.779 1.00 44.28  ? 302 VAL C CB  1 
ATOM   7525 C  CG1 . VAL C  1  289 ? 7.713   7.345   19.979 1.00 46.18  ? 302 VAL C CG1 1 
ATOM   7526 C  CG2 . VAL C  1  289 ? 7.168   9.782   19.871 1.00 44.23  ? 302 VAL C CG2 1 
ATOM   7527 N  N   . VAL C  1  290 ? 11.371  7.765   20.014 1.00 38.65  ? 303 VAL C N   1 
ATOM   7528 C  CA  . VAL C  1  290 ? 12.322  6.673   20.126 1.00 42.04  ? 303 VAL C CA  1 
ATOM   7529 C  C   . VAL C  1  290 ? 13.016  6.768   21.488 1.00 40.94  ? 303 VAL C C   1 
ATOM   7530 O  O   . VAL C  1  290 ? 13.189  5.764   22.169 1.00 38.94  ? 303 VAL C O   1 
ATOM   7531 C  CB  . VAL C  1  290 ? 13.313  6.648   18.947 1.00 44.33  ? 303 VAL C CB  1 
ATOM   7532 C  CG1 . VAL C  1  290 ? 14.508  5.732   19.203 1.00 43.33  ? 303 VAL C CG1 1 
ATOM   7533 C  CG2 . VAL C  1  290 ? 12.611  6.253   17.656 1.00 43.03  ? 303 VAL C CG2 1 
ATOM   7534 N  N   . GLY C  1  291 ? 13.374  7.989   21.893 1.00 41.68  ? 304 GLY C N   1 
ATOM   7535 C  CA  . GLY C  1  291 ? 13.923  8.251   23.213 1.00 41.38  ? 304 GLY C CA  1 
ATOM   7536 C  C   . GLY C  1  291 ? 12.991  7.790   24.327 1.00 41.20  ? 304 GLY C C   1 
ATOM   7537 O  O   . GLY C  1  291 ? 13.439  7.139   25.269 1.00 41.39  ? 304 GLY C O   1 
ATOM   7538 N  N   . SER C  1  292 ? 11.694  8.112   24.206 1.00 39.28  ? 305 SER C N   1 
ATOM   7539 C  CA  . SER C  1  292 ? 10.725  7.721   25.215 1.00 39.27  ? 305 SER C CA  1 
ATOM   7540 C  C   . SER C  1  292 ? 10.672  6.199   25.327 1.00 40.02  ? 305 SER C C   1 
ATOM   7541 O  O   . SER C  1  292 ? 10.601  5.658   26.433 1.00 40.09  ? 305 SER C O   1 
ATOM   7542 C  CB  . SER C  1  292 ? 9.358   8.291   24.928 1.00 41.38  ? 305 SER C CB  1 
ATOM   7543 O  OG  . SER C  1  292 ? 9.410   9.694   24.746 1.00 42.02  ? 305 SER C OG  1 
ATOM   7544 N  N   . VAL C  1  293 ? 10.711  5.514   24.179 1.00 38.36  ? 306 VAL C N   1 
ATOM   7545 C  CA  . VAL C  1  293 ? 10.654  4.059   24.169 1.00 38.70  ? 306 VAL C CA  1 
ATOM   7546 C  C   . VAL C  1  293 ? 11.871  3.484   24.893 1.00 40.20  ? 306 VAL C C   1 
ATOM   7547 O  O   . VAL C  1  293 ? 11.737  2.503   25.629 1.00 40.52  ? 306 VAL C O   1 
ATOM   7548 C  CB  . VAL C  1  293 ? 10.524  3.494   22.740 1.00 36.85  ? 306 VAL C CB  1 
ATOM   7549 C  CG1 . VAL C  1  293 ? 10.720  1.978   22.698 1.00 35.94  ? 306 VAL C CG1 1 
ATOM   7550 C  CG2 . VAL C  1  293 ? 9.190   3.884   22.118 1.00 40.04  ? 306 VAL C CG2 1 
ATOM   7551 N  N   . GLN C  1  294 ? 13.049  4.097   24.700 1.00 43.23  ? 307 GLN C N   1 
ATOM   7552 C  CA  . GLN C  1  294 ? 14.266  3.628   25.354 1.00 46.41  ? 307 GLN C CA  1 
ATOM   7553 C  C   . GLN C  1  294 ? 14.146  3.774   26.871 1.00 45.99  ? 307 GLN C C   1 
ATOM   7554 O  O   . GLN C  1  294 ? 14.663  2.938   27.611 1.00 44.61  ? 307 GLN C O   1 
ATOM   7555 C  CB  . GLN C  1  294 ? 15.514  4.376   24.881 1.00 47.55  ? 307 GLN C CB  1 
ATOM   7556 C  CG  . GLN C  1  294 ? 15.905  4.088   23.436 1.00 54.53  ? 307 GLN C CG  1 
ATOM   7557 C  CD  . GLN C  1  294 ? 17.038  4.961   22.922 1.00 53.61  ? 307 GLN C CD  1 
ATOM   7558 O  OE1 . GLN C  1  294 ? 16.850  6.113   22.517 1.00 56.00  ? 307 GLN C OE1 1 
ATOM   7559 N  NE2 . GLN C  1  294 ? 18.240  4.413   22.894 1.00 50.54  ? 307 GLN C NE2 1 
ATOM   7560 N  N   . GLU C  1  295 ? 13.475  4.838   27.329 1.00 47.77  ? 308 GLU C N   1 
ATOM   7561 C  CA  . GLU C  1  295 ? 13.244  5.039   28.754 1.00 51.39  ? 308 GLU C CA  1 
ATOM   7562 C  C   . GLU C  1  295 ? 12.308  3.966   29.299 1.00 47.12  ? 308 GLU C C   1 
ATOM   7563 O  O   . GLU C  1  295 ? 12.516  3.502   30.416 1.00 49.18  ? 308 GLU C O   1 
ATOM   7564 C  CB  . GLU C  1  295 ? 12.667  6.415   29.085 1.00 55.29  ? 308 GLU C CB  1 
ATOM   7565 C  CG  . GLU C  1  295 ? 13.695  7.535   28.953 1.00 60.79  ? 308 GLU C CG  1 
ATOM   7566 C  CD  . GLU C  1  295 ? 13.150  8.930   29.210 1.00 72.67  ? 308 GLU C CD  1 
ATOM   7567 O  OE1 . GLU C  1  295 ? 11.909  9.122   29.242 1.00 75.54  ? 308 GLU C OE1 1 
ATOM   7568 O  OE2 . GLU C  1  295 ? 13.989  9.838   29.390 1.00 80.55  ? 308 GLU C OE2 1 
ATOM   7569 N  N   . LEU C  1  296 ? 11.298  3.573   28.508 1.00 43.20  ? 309 LEU C N   1 
ATOM   7570 C  CA  . LEU C  1  296 ? 10.363  2.541   28.929 1.00 42.54  ? 309 LEU C CA  1 
ATOM   7571 C  C   . LEU C  1  296 ? 11.049  1.176   28.934 1.00 40.22  ? 309 LEU C C   1 
ATOM   7572 O  O   . LEU C  1  296 ? 10.694  0.320   29.747 1.00 40.43  ? 309 LEU C O   1 
ATOM   7573 C  CB  . LEU C  1  296 ? 9.114   2.504   28.043 1.00 43.79  ? 309 LEU C CB  1 
ATOM   7574 C  CG  . LEU C  1  296 ? 8.167   3.706   28.111 1.00 46.33  ? 309 LEU C CG  1 
ATOM   7575 C  CD1 . LEU C  1  296 ? 7.021   3.496   27.144 1.00 47.44  ? 309 LEU C CD1 1 
ATOM   7576 C  CD2 . LEU C  1  296 ? 7.604   3.982   29.495 1.00 50.17  ? 309 LEU C CD2 1 
ATOM   7577 N  N   . TYR C  1  297 ? 11.978  0.968   27.991 1.00 38.21  ? 310 TYR C N   1 
ATOM   7578 C  CA  . TYR C  1  297 ? 12.601  -0.329  27.769 1.00 42.23  ? 310 TYR C CA  1 
ATOM   7579 C  C   . TYR C  1  297 ? 14.121  -0.151  27.681 1.00 46.58  ? 310 TYR C C   1 
ATOM   7580 O  O   . TYR C  1  297 ? 14.699  -0.153  26.589 1.00 45.29  ? 310 TYR C O   1 
ATOM   7581 C  CB  . TYR C  1  297 ? 12.039  -0.989  26.508 1.00 40.28  ? 310 TYR C CB  1 
ATOM   7582 C  CG  . TYR C  1  297 ? 10.547  -1.299  26.557 1.00 38.79  ? 310 TYR C CG  1 
ATOM   7583 C  CD1 . TYR C  1  297 ? 10.068  -2.438  27.196 1.00 39.29  ? 310 TYR C CD1 1 
ATOM   7584 C  CD2 . TYR C  1  297 ? 9.621   -0.469  25.931 1.00 36.12  ? 310 TYR C CD2 1 
ATOM   7585 C  CE1 . TYR C  1  297 ? 8.712   -2.730  27.233 1.00 39.18  ? 310 TYR C CE1 1 
ATOM   7586 C  CE2 . TYR C  1  297 ? 8.263   -0.749  25.964 1.00 37.19  ? 310 TYR C CE2 1 
ATOM   7587 C  CZ  . TYR C  1  297 ? 7.805   -1.880  26.617 1.00 36.27  ? 310 TYR C CZ  1 
ATOM   7588 O  OH  . TYR C  1  297 ? 6.464   -2.146  26.654 1.00 37.16  ? 310 TYR C OH  1 
ATOM   7589 N  N   . PRO C  1  298 ? 14.803  0.070   28.826 1.00 47.97  ? 311 PRO C N   1 
ATOM   7590 C  CA  . PRO C  1  298 ? 16.230  0.404   28.822 1.00 46.10  ? 311 PRO C CA  1 
ATOM   7591 C  C   . PRO C  1  298 ? 17.185  -0.698  28.380 1.00 41.81  ? 311 PRO C C   1 
ATOM   7592 O  O   . PRO C  1  298 ? 18.225  -0.383  27.817 1.00 44.21  ? 311 PRO C O   1 
ATOM   7593 C  CB  . PRO C  1  298 ? 16.499  0.851   30.275 1.00 46.73  ? 311 PRO C CB  1 
ATOM   7594 C  CG  . PRO C  1  298 ? 15.437  0.144   31.084 1.00 51.04  ? 311 PRO C CG  1 
ATOM   7595 C  CD  . PRO C  1  298 ? 14.219  0.074   30.177 1.00 46.84  ? 311 PRO C CD  1 
ATOM   7596 N  N   . ASN C  1  299 ? 16.863  -1.968  28.652 1.00 43.60  ? 312 ASN C N   1 
ATOM   7597 C  CA  . ASN C  1  299 ? 17.773  -3.054  28.327 1.00 43.90  ? 312 ASN C CA  1 
ATOM   7598 C  C   . ASN C  1  299 ? 17.031  -4.355  28.028 1.00 44.99  ? 312 ASN C C   1 
ATOM   7599 O  O   . ASN C  1  299 ? 17.262  -5.354  28.701 1.00 41.32  ? 312 ASN C O   1 
ATOM   7600 C  CB  . ASN C  1  299 ? 18.794  -3.253  29.440 1.00 44.99  ? 312 ASN C CB  1 
ATOM   7601 C  CG  . ASN C  1  299 ? 19.917  -4.165  29.017 1.00 41.00  ? 312 ASN C CG  1 
ATOM   7602 O  OD1 . ASN C  1  299 ? 20.229  -5.128  29.719 1.00 41.44  ? 312 ASN C OD1 1 
ATOM   7603 N  ND2 . ASN C  1  299 ? 20.521  -3.884  27.875 1.00 40.02  ? 312 ASN C ND2 1 
ATOM   7604 N  N   . PRO C  1  300 ? 16.173  -4.405  26.982 1.00 45.53  ? 313 PRO C N   1 
ATOM   7605 C  CA  . PRO C  1  300 ? 15.415  -5.616  26.658 1.00 42.78  ? 313 PRO C CA  1 
ATOM   7606 C  C   . PRO C  1  300 ? 16.238  -6.709  25.977 1.00 43.47  ? 313 PRO C C   1 
ATOM   7607 O  O   . PRO C  1  300 ? 17.221  -6.415  25.296 1.00 45.07  ? 313 PRO C O   1 
ATOM   7608 C  CB  . PRO C  1  300 ? 14.327  -5.055  25.712 1.00 42.79  ? 313 PRO C CB  1 
ATOM   7609 C  CG  . PRO C  1  300 ? 15.060  -3.963  24.966 1.00 43.25  ? 313 PRO C CG  1 
ATOM   7610 C  CD  . PRO C  1  300 ? 15.903  -3.297  26.046 1.00 45.51  ? 313 PRO C CD  1 
ATOM   7611 N  N   . THR C  1  301 ? 15.803  -7.962  26.165 1.00 40.73  ? 314 THR C N   1 
ATOM   7612 C  CA  . THR C  1  301 ? 16.368  -9.128  25.502 1.00 43.89  ? 314 THR C CA  1 
ATOM   7613 C  C   . THR C  1  301 ? 15.222  -10.040 25.059 1.00 45.04  ? 314 THR C C   1 
ATOM   7614 O  O   . THR C  1  301 ? 14.065  -9.796  25.407 1.00 46.35  ? 314 THR C O   1 
ATOM   7615 C  CB  . THR C  1  301 ? 17.329  -9.854  26.450 1.00 51.91  ? 314 THR C CB  1 
ATOM   7616 O  OG1 . THR C  1  301 ? 16.607  -10.184 27.634 1.00 50.11  ? 314 THR C OG1 1 
ATOM   7617 C  CG2 . THR C  1  301 ? 18.529  -9.010  26.844 1.00 50.88  ? 314 THR C CG2 1 
ATOM   7618 N  N   . GLY C  1  302 ? 15.549  -11.080 24.273 1.00 47.27  ? 315 GLY C N   1 
ATOM   7619 C  CA  . GLY C  1  302 ? 14.585  -12.110 23.906 1.00 45.71  ? 315 GLY C CA  1 
ATOM   7620 C  C   . GLY C  1  302 ? 13.447  -11.579 23.029 1.00 45.20  ? 315 GLY C C   1 
ATOM   7621 O  O   . GLY C  1  302 ? 13.664  -10.730 22.172 1.00 45.44  ? 315 GLY C O   1 
ATOM   7622 N  N   . ILE C  1  303 ? 12.234  -12.090 23.259 1.00 44.89  ? 316 ILE C N   1 
ATOM   7623 C  CA  . ILE C  1  303 ? 11.071  -11.771 22.439 1.00 47.52  ? 316 ILE C CA  1 
ATOM   7624 C  C   . ILE C  1  303 ? 10.777  -10.277 22.547 1.00 45.03  ? 316 ILE C C   1 
ATOM   7625 O  O   . ILE C  1  303 ? 10.424  -9.641  21.553 1.00 42.52  ? 316 ILE C O   1 
ATOM   7626 C  CB  . ILE C  1  303 ? 9.836   -12.609 22.827 1.00 57.63  ? 316 ILE C CB  1 
ATOM   7627 C  CG1 . ILE C  1  303 ? 10.145  -14.107 22.907 1.00 69.88  ? 316 ILE C CG1 1 
ATOM   7628 C  CG2 . ILE C  1  303 ? 8.671   -12.340 21.871 1.00 58.82  ? 316 ILE C CG2 1 
ATOM   7629 C  CD1 . ILE C  1  303 ? 8.977   -14.958 23.379 1.00 79.47  ? 316 ILE C CD1 1 
ATOM   7630 N  N   . LEU C  1  304 ? 10.954  -9.714  23.750 1.00 42.02  ? 317 LEU C N   1 
ATOM   7631 C  CA  . LEU C  1  304 ? 10.639  -8.315  23.974 1.00 39.59  ? 317 LEU C CA  1 
ATOM   7632 C  C   . LEU C  1  304 ? 11.529  -7.439  23.089 1.00 42.22  ? 317 LEU C C   1 
ATOM   7633 O  O   . LEU C  1  304 ? 11.041  -6.508  22.448 1.00 40.18  ? 317 LEU C O   1 
ATOM   7634 C  CB  . LEU C  1  304 ? 10.769  -7.966  25.454 1.00 39.98  ? 317 LEU C CB  1 
ATOM   7635 C  CG  . LEU C  1  304 ? 10.535  -6.491  25.803 1.00 42.08  ? 317 LEU C CG  1 
ATOM   7636 C  CD1 . LEU C  1  304 ? 9.148   -5.991  25.346 1.00 42.71  ? 317 LEU C CD1 1 
ATOM   7637 C  CD2 . LEU C  1  304 ? 10.703  -6.282  27.308 1.00 45.60  ? 317 LEU C CD2 1 
ATOM   7638 N  N   . ARG C  1  305 ? 12.837  -7.736  23.061 1.00 42.40  ? 318 ARG C N   1 
ATOM   7639 C  CA  A ARG C  1  305 ? 13.773  -7.003  22.226 0.50 40.46  ? 318 ARG C CA  1 
ATOM   7640 C  CA  B ARG C  1  305 ? 13.773  -7.001  22.226 0.50 44.15  ? 318 ARG C CA  1 
ATOM   7641 C  C   . ARG C  1  305 ? 13.355  -7.140  20.764 1.00 40.90  ? 318 ARG C C   1 
ATOM   7642 O  O   . ARG C  1  305 ? 13.304  -6.153  20.044 1.00 41.95  ? 318 ARG C O   1 
ATOM   7643 C  CB  A ARG C  1  305 ? 15.207  -7.519  22.398 0.50 35.30  ? 318 ARG C CB  1 
ATOM   7644 C  CB  B ARG C  1  305 ? 15.221  -7.474  22.424 0.50 44.03  ? 318 ARG C CB  1 
ATOM   7645 C  CG  A ARG C  1  305 ? 16.244  -6.967  21.440 0.50 33.64  ? 318 ARG C CG  1 
ATOM   7646 C  CG  B ARG C  1  305 ? 16.248  -6.755  21.558 0.50 47.52  ? 318 ARG C CG  1 
ATOM   7647 C  CD  A ARG C  1  305 ? 17.569  -7.699  21.552 0.50 30.88  ? 318 ARG C CD  1 
ATOM   7648 C  CD  B ARG C  1  305 ? 17.677  -7.000  22.037 0.50 49.20  ? 318 ARG C CD  1 
ATOM   7649 N  NE  A ARG C  1  305 ? 18.408  -7.159  20.485 0.50 27.67  ? 318 ARG C NE  1 
ATOM   7650 N  NE  B ARG C  1  305 ? 18.722  -6.500  21.136 0.50 48.19  ? 318 ARG C NE  1 
ATOM   7651 C  CZ  A ARG C  1  305 ? 18.530  -7.718  19.306 0.50 26.19  ? 318 ARG C CZ  1 
ATOM   7652 C  CZ  B ARG C  1  305 ? 19.469  -5.418  21.344 0.50 43.95  ? 318 ARG C CZ  1 
ATOM   7653 N  NH1 A ARG C  1  305 ? 17.987  -8.898  19.101 0.50 24.37  ? 318 ARG C NH1 1 
ATOM   7654 N  NH1 B ARG C  1  305 ? 19.200  -4.581  22.310 0.50 40.94  ? 318 ARG C NH1 1 
ATOM   7655 N  NH2 A ARG C  1  305 ? 19.169  -7.094  18.342 0.50 25.09  ? 318 ARG C NH2 1 
ATOM   7656 N  NH2 B ARG C  1  305 ? 20.469  -5.140  20.540 0.50 51.79  ? 318 ARG C NH2 1 
ATOM   7657 N  N   . ARG C  1  306 ? 13.081  -8.376  20.340 1.00 40.90  ? 319 ARG C N   1 
ATOM   7658 C  CA  . ARG C  1  306 ? 12.707  -8.667  18.964 1.00 44.34  ? 319 ARG C CA  1 
ATOM   7659 C  C   . ARG C  1  306 ? 11.454  -7.880  18.582 1.00 42.27  ? 319 ARG C C   1 
ATOM   7660 O  O   . ARG C  1  306 ? 11.421  -7.227  17.538 1.00 38.20  ? 319 ARG C O   1 
ATOM   7661 C  CB  . ARG C  1  306 ? 12.502  -10.179 18.815 1.00 51.15  ? 319 ARG C CB  1 
ATOM   7662 C  CG  . ARG C  1  306 ? 12.399  -10.685 17.382 1.00 60.44  ? 319 ARG C CG  1 
ATOM   7663 C  CD  . ARG C  1  306 ? 11.762  -12.065 17.268 1.00 63.57  ? 319 ARG C CD  1 
ATOM   7664 N  NE  . ARG C  1  306 ? 10.357  -12.080 17.699 1.00 73.97  ? 319 ARG C NE  1 
ATOM   7665 C  CZ  . ARG C  1  306 ? 9.575   -13.159 17.742 1.00 80.50  ? 319 ARG C CZ  1 
ATOM   7666 N  NH1 . ARG C  1  306 ? 10.035  -14.341 17.369 1.00 86.47  ? 319 ARG C NH1 1 
ATOM   7667 N  NH2 . ARG C  1  306 ? 8.333   -13.058 18.177 1.00 77.32  ? 319 ARG C NH2 1 
ATOM   7668 N  N   . ASN C  1  307 ? 10.429  -7.921  19.439 1.00 40.12  ? 320 ASN C N   1 
ATOM   7669 C  CA  . ASN C  1  307 ? 9.159   -7.280  19.116 1.00 41.61  ? 320 ASN C CA  1 
ATOM   7670 C  C   . ASN C  1  307 ? 9.302   -5.758  19.125 1.00 42.52  ? 320 ASN C C   1 
ATOM   7671 O  O   . ASN C  1  307 ? 8.616   -5.069  18.367 1.00 36.97  ? 320 ASN C O   1 
ATOM   7672 C  CB  . ASN C  1  307 ? 8.032   -7.782  20.006 1.00 43.01  ? 320 ASN C CB  1 
ATOM   7673 C  CG  . ASN C  1  307 ? 7.651   -9.191  19.629 1.00 43.53  ? 320 ASN C CG  1 
ATOM   7674 O  OD1 . ASN C  1  307 ? 8.346   -9.815  18.824 1.00 45.64  ? 320 ASN C OD1 1 
ATOM   7675 N  ND2 . ASN C  1  307 ? 6.557   -9.698  20.173 1.00 47.41  ? 320 ASN C ND2 1 
ATOM   7676 N  N   . LEU C  1  308 ? 10.212  -5.238  19.957 1.00 39.46  ? 321 LEU C N   1 
ATOM   7677 C  CA  . LEU C  1  308 ? 10.489  -3.811  19.967 1.00 39.20  ? 321 LEU C CA  1 
ATOM   7678 C  C   . LEU C  1  308 ? 11.096  -3.389  18.635 1.00 37.12  ? 321 LEU C C   1 
ATOM   7679 O  O   . LEU C  1  308 ? 10.717  -2.367  18.075 1.00 35.29  ? 321 LEU C O   1 
ATOM   7680 C  CB  . LEU C  1  308 ? 11.408  -3.429  21.121 1.00 41.38  ? 321 LEU C CB  1 
ATOM   7681 C  CG  . LEU C  1  308 ? 10.709  -3.071  22.435 1.00 42.90  ? 321 LEU C CG  1 
ATOM   7682 C  CD1 . LEU C  1  308 ? 11.709  -3.142  23.597 1.00 44.24  ? 321 LEU C CD1 1 
ATOM   7683 C  CD2 . LEU C  1  308 ? 10.077  -1.684  22.310 1.00 42.13  ? 321 LEU C CD2 1 
ATOM   7684 N  N   . ILE C  1  309 ? 12.079  -4.157  18.169 1.00 40.58  ? 322 ILE C N   1 
ATOM   7685 C  CA  . ILE C  1  309 ? 12.783  -3.844  16.936 1.00 41.77  ? 322 ILE C CA  1 
ATOM   7686 C  C   . ILE C  1  309 ? 11.781  -3.816  15.780 1.00 38.39  ? 322 ILE C C   1 
ATOM   7687 O  O   . ILE C  1  309 ? 11.808  -2.911  14.946 1.00 40.55  ? 322 ILE C O   1 
ATOM   7688 C  CB  . ILE C  1  309 ? 13.920  -4.852  16.683 1.00 40.37  ? 322 ILE C CB  1 
ATOM   7689 C  CG1 . ILE C  1  309 ? 15.067  -4.648  17.654 1.00 41.85  ? 322 ILE C CG1 1 
ATOM   7690 C  CG2 . ILE C  1  309 ? 14.389  -4.801  15.220 1.00 42.68  ? 322 ILE C CG2 1 
ATOM   7691 C  CD1 . ILE C  1  309 ? 16.056  -5.802  17.723 1.00 39.77  ? 322 ILE C CD1 1 
ATOM   7692 N  N   . LYS C  1  310 ? 10.907  -4.817  15.742 1.00 38.40  ? 323 LYS C N   1 
ATOM   7693 C  CA  . LYS C  1  310 ? 9.920   -4.916  14.680 1.00 41.01  ? 323 LYS C CA  1 
ATOM   7694 C  C   . LYS C  1  310 ? 8.953   -3.738  14.723 1.00 38.93  ? 323 LYS C C   1 
ATOM   7695 O  O   . LYS C  1  310 ? 8.706   -3.097  13.698 1.00 40.26  ? 323 LYS C O   1 
ATOM   7696 C  CB  . LYS C  1  310 ? 9.200   -6.259  14.788 1.00 41.02  ? 323 LYS C CB  1 
ATOM   7697 C  CG  . LYS C  1  310 ? 10.045  -7.404  14.277 1.00 43.99  ? 323 LYS C CG  1 
ATOM   7698 C  CD  . LYS C  1  310 ? 9.404   -8.773  14.463 1.00 50.54  ? 323 LYS C CD  1 
ATOM   7699 C  CE  . LYS C  1  310 ? 10.153  -9.818  13.702 1.00 56.34  ? 323 LYS C CE  1 
ATOM   7700 N  NZ  . LYS C  1  310 ? 9.546   -11.128 13.932 1.00 61.67  ? 323 LYS C NZ  1 
ATOM   7701 N  N   . ASN C  1  311 ? 8.415   -3.454  15.907 1.00 34.85  ? 324 ASN C N   1 
ATOM   7702 C  CA  . ASN C  1  311 ? 7.397   -2.423  16.029 1.00 36.46  ? 324 ASN C CA  1 
ATOM   7703 C  C   . ASN C  1  311 ? 7.984   -1.050  15.718 1.00 36.40  ? 324 ASN C C   1 
ATOM   7704 O  O   . ASN C  1  311 ? 7.298   -0.198  15.154 1.00 38.31  ? 324 ASN C O   1 
ATOM   7705 C  CB  . ASN C  1  311 ? 6.719   -2.460  17.391 1.00 38.22  ? 324 ASN C CB  1 
ATOM   7706 C  CG  . ASN C  1  311 ? 5.628   -3.500  17.443 1.00 37.93  ? 324 ASN C CG  1 
ATOM   7707 O  OD1 . ASN C  1  311 ? 4.507   -3.232  17.007 1.00 37.72  ? 324 ASN C OD1 1 
ATOM   7708 N  ND2 . ASN C  1  311 ? 5.924   -4.665  17.997 1.00 39.39  ? 324 ASN C ND2 1 
ATOM   7709 N  N   . LEU C  1  312 ? 9.255   -0.848  16.073 1.00 37.74  ? 325 LEU C N   1 
ATOM   7710 C  CA  . LEU C  1  312 ? 9.922   0.415   15.806 1.00 40.33  ? 325 LEU C CA  1 
ATOM   7711 C  C   . LEU C  1  312 ? 10.085  0.601   14.299 1.00 37.26  ? 325 LEU C C   1 
ATOM   7712 O  O   . LEU C  1  312 ? 9.905   1.702   13.793 1.00 39.24  ? 325 LEU C O   1 
ATOM   7713 C  CB  . LEU C  1  312 ? 11.266  0.467   16.530 1.00 38.46  ? 325 LEU C CB  1 
ATOM   7714 C  CG  . LEU C  1  312 ? 11.203  0.805   18.023 1.00 41.09  ? 325 LEU C CG  1 
ATOM   7715 C  CD1 . LEU C  1  312 ? 12.508  0.414   18.665 1.00 38.77  ? 325 LEU C CD1 1 
ATOM   7716 C  CD2 . LEU C  1  312 ? 10.925  2.281   18.262 1.00 41.09  ? 325 LEU C CD2 1 
ATOM   7717 N  N   . HIS C  1  313 ? 10.431  -0.484  13.601 1.00 38.32  ? 326 HIS C N   1 
ATOM   7718 C  CA  . HIS C  1  313 ? 10.575  -0.452  12.154 1.00 36.17  ? 326 HIS C CA  1 
ATOM   7719 C  C   . HIS C  1  313 ? 9.210   -0.201  11.518 1.00 36.72  ? 326 HIS C C   1 
ATOM   7720 O  O   . HIS C  1  313 ? 9.089   0.645   10.643 1.00 35.90  ? 326 HIS C O   1 
ATOM   7721 C  CB  . HIS C  1  313 ? 11.261  -1.716  11.618 1.00 36.46  ? 326 HIS C CB  1 
ATOM   7722 C  CG  . HIS C  1  313 ? 11.407  -1.661  10.137 1.00 40.66  ? 326 HIS C CG  1 
ATOM   7723 N  ND1 . HIS C  1  313 ? 12.189  -0.703  9.522  1.00 38.99  ? 326 HIS C ND1 1 
ATOM   7724 C  CD2 . HIS C  1  313 ? 10.784  -2.334  9.149  1.00 39.40  ? 326 HIS C CD2 1 
ATOM   7725 C  CE1 . HIS C  1  313 ? 12.075  -0.840  8.211  1.00 42.87  ? 326 HIS C CE1 1 
ATOM   7726 N  NE2 . HIS C  1  313 ? 11.226  -1.820  7.964  1.00 39.36  ? 326 HIS C NE2 1 
ATOM   7727 N  N   . TYR C  1  314 ? 8.177   -0.918  11.969 1.00 36.86  ? 327 TYR C N   1 
ATOM   7728 C  CA  . TYR C  1  314 ? 6.831   -0.704  11.456 1.00 35.05  ? 327 TYR C CA  1 
ATOM   7729 C  C   . TYR C  1  314 ? 6.440   0.762   11.578 1.00 34.78  ? 327 TYR C C   1 
ATOM   7730 O  O   . TYR C  1  314 ? 5.936   1.344   10.626 1.00 32.91  ? 327 TYR C O   1 
ATOM   7731 C  CB  . TYR C  1  314 ? 5.793   -1.553  12.188 1.00 36.07  ? 327 TYR C CB  1 
ATOM   7732 C  CG  . TYR C  1  314 ? 5.996   -3.055  12.062 1.00 36.53  ? 327 TYR C CG  1 
ATOM   7733 C  CD1 . TYR C  1  314 ? 6.724   -3.608  11.012 1.00 37.65  ? 327 TYR C CD1 1 
ATOM   7734 C  CD2 . TYR C  1  314 ? 5.455   -3.922  13.006 1.00 39.73  ? 327 TYR C CD2 1 
ATOM   7735 C  CE1 . TYR C  1  314 ? 6.918   -4.977  10.911 1.00 39.12  ? 327 TYR C CE1 1 
ATOM   7736 C  CE2 . TYR C  1  314 ? 5.625   -5.293  12.907 1.00 38.45  ? 327 TYR C CE2 1 
ATOM   7737 C  CZ  . TYR C  1  314 ? 6.364   -5.821  11.862 1.00 38.98  ? 327 TYR C CZ  1 
ATOM   7738 O  OH  . TYR C  1  314 ? 6.522   -7.169  11.781 1.00 39.17  ? 327 TYR C OH  1 
ATOM   7739 N  N   . TRP C  1  315 ? 6.664   1.353   12.757 1.00 34.95  ? 328 TRP C N   1 
ATOM   7740 C  CA  . TRP C  1  315 ? 6.306   2.742   12.969 1.00 32.45  ? 328 TRP C CA  1 
ATOM   7741 C  C   . TRP C  1  315 ? 7.067   3.632   11.984 1.00 34.18  ? 328 TRP C C   1 
ATOM   7742 O  O   . TRP C  1  315 ? 6.478   4.498   11.343 1.00 32.41  ? 328 TRP C O   1 
ATOM   7743 C  CB  . TRP C  1  315 ? 6.566   3.147   14.426 1.00 32.63  ? 328 TRP C CB  1 
ATOM   7744 C  CG  . TRP C  1  315 ? 6.009   4.497   14.778 1.00 33.36  ? 328 TRP C CG  1 
ATOM   7745 C  CD1 . TRP C  1  315 ? 4.747   4.956   14.548 1.00 34.67  ? 328 TRP C CD1 1 
ATOM   7746 C  CD2 . TRP C  1  315 ? 6.723   5.582   15.403 1.00 35.34  ? 328 TRP C CD2 1 
ATOM   7747 N  NE1 . TRP C  1  315 ? 4.618   6.244   14.997 1.00 38.39  ? 328 TRP C NE1 1 
ATOM   7748 C  CE2 . TRP C  1  315 ? 5.815   6.658   15.519 1.00 37.34  ? 328 TRP C CE2 1 
ATOM   7749 C  CE3 . TRP C  1  315 ? 8.030   5.735   15.872 1.00 39.19  ? 328 TRP C CE3 1 
ATOM   7750 C  CZ2 . TRP C  1  315 ? 6.177   7.873   16.086 1.00 38.11  ? 328 TRP C CZ2 1 
ATOM   7751 C  CZ3 . TRP C  1  315 ? 8.379   6.935   16.445 1.00 41.38  ? 328 TRP C CZ3 1 
ATOM   7752 C  CH2 . TRP C  1  315 ? 7.471   7.992   16.528 1.00 40.19  ? 328 TRP C CH2 1 
ATOM   7753 N  N   . TRP C  1  316 ? 8.381   3.395   11.858 1.00 33.86  ? 329 TRP C N   1 
ATOM   7754 C  CA  . TRP C  1  316 ? 9.217   4.158   10.953 1.00 34.51  ? 329 TRP C CA  1 
ATOM   7755 C  C   . TRP C  1  316 ? 8.669   4.147   9.522  1.00 35.75  ? 329 TRP C C   1 
ATOM   7756 O  O   . TRP C  1  316 ? 8.769   5.152   8.822  1.00 36.00  ? 329 TRP C O   1 
ATOM   7757 C  CB  . TRP C  1  316 ? 10.684  3.684   10.982 1.00 36.31  ? 329 TRP C CB  1 
ATOM   7758 C  CG  . TRP C  1  316 ? 11.507  4.427   9.960  1.00 38.94  ? 329 TRP C CG  1 
ATOM   7759 C  CD1 . TRP C  1  316 ? 12.070  5.664   10.090 1.00 41.23  ? 329 TRP C CD1 1 
ATOM   7760 C  CD2 . TRP C  1  316 ? 11.771  4.013   8.605  1.00 39.93  ? 329 TRP C CD2 1 
ATOM   7761 N  NE1 . TRP C  1  316 ? 12.683  6.037   8.927  1.00 44.20  ? 329 TRP C NE1 1 
ATOM   7762 C  CE2 . TRP C  1  316 ? 12.505  5.055   7.991  1.00 44.62  ? 329 TRP C CE2 1 
ATOM   7763 C  CE3 . TRP C  1  316 ? 11.450  2.879   7.852  1.00 40.96  ? 329 TRP C CE3 1 
ATOM   7764 C  CZ2 . TRP C  1  316 ? 12.944  4.982   6.672  1.00 43.58  ? 329 TRP C CZ2 1 
ATOM   7765 C  CZ3 . TRP C  1  316 ? 11.863  2.819   6.540  1.00 44.06  ? 329 TRP C CZ3 1 
ATOM   7766 C  CH2 . TRP C  1  316 ? 12.586  3.864   5.957  1.00 43.32  ? 329 TRP C CH2 1 
ATOM   7767 N  N   . THR C  1  317 ? 8.120   3.013   9.062  1.00 37.29  ? 330 THR C N   1 
ATOM   7768 C  CA  . THR C  1  317 ? 7.650   2.919   7.684  1.00 38.88  ? 330 THR C CA  1 
ATOM   7769 C  C   . THR C  1  317 ? 6.543   3.945   7.456  1.00 39.54  ? 330 THR C C   1 
ATOM   7770 O  O   . THR C  1  317 ? 6.457   4.528   6.379  1.00 38.21  ? 330 THR C O   1 
ATOM   7771 C  CB  . THR C  1  317 ? 7.159   1.525   7.286  1.00 38.36  ? 330 THR C CB  1 
ATOM   7772 O  OG1 . THR C  1  317 ? 5.967   1.221   8.005  1.00 35.77  ? 330 THR C OG1 1 
ATOM   7773 C  CG2 . THR C  1  317 ? 8.215   0.455   7.489  1.00 36.45  ? 330 THR C CG2 1 
ATOM   7774 N  N   . GLY C  1  318 ? 5.712   4.173   8.480  1.00 36.95  ? 331 GLY C N   1 
ATOM   7775 C  CA  . GLY C  1  318 ? 4.690   5.204   8.410  1.00 38.76  ? 331 GLY C CA  1 
ATOM   7776 C  C   . GLY C  1  318 ? 5.292   6.606   8.518  1.00 36.37  ? 331 GLY C C   1 
ATOM   7777 O  O   . GLY C  1  318 ? 4.930   7.512   7.768  1.00 37.96  ? 331 GLY C O   1 
ATOM   7778 N  N   . VAL C  1  319 ? 6.205   6.771   9.473  1.00 37.59  ? 332 VAL C N   1 
ATOM   7779 C  CA  . VAL C  1  319 ? 6.811   8.061   9.750  1.00 39.18  ? 332 VAL C CA  1 
ATOM   7780 C  C   . VAL C  1  319 ? 7.547   8.563   8.509  1.00 38.06  ? 332 VAL C C   1 
ATOM   7781 O  O   . VAL C  1  319 ? 7.466   9.739   8.174  1.00 38.91  ? 332 VAL C O   1 
ATOM   7782 C  CB  . VAL C  1  319 ? 7.731   7.924   10.979 1.00 40.61  ? 332 VAL C CB  1 
ATOM   7783 C  CG1 . VAL C  1  319 ? 8.751   9.055   11.078 1.00 40.51  ? 332 VAL C CG1 1 
ATOM   7784 C  CG2 . VAL C  1  319 ? 6.918   7.773   12.271 1.00 41.41  ? 332 VAL C CG2 1 
ATOM   7785 N  N   . ASN C  1  320 ? 8.267   7.669   7.830  1.00 38.97  ? 333 ASN C N   1 
ATOM   7786 C  CA  . ASN C  1  320 ? 9.100   8.074   6.709  1.00 37.55  ? 333 ASN C CA  1 
ATOM   7787 C  C   . ASN C  1  320 ? 8.270   8.798   5.654  1.00 40.03  ? 333 ASN C C   1 
ATOM   7788 O  O   . ASN C  1  320 ? 8.700   9.830   5.130  1.00 43.53  ? 333 ASN C O   1 
ATOM   7789 C  CB  . ASN C  1  320 ? 9.851   6.911   6.081  1.00 36.64  ? 333 ASN C CB  1 
ATOM   7790 C  CG  . ASN C  1  320 ? 10.969  7.415   5.192  1.00 39.26  ? 333 ASN C CG  1 
ATOM   7791 O  OD1 . ASN C  1  320 ? 11.778  8.254   5.615  1.00 38.22  ? 333 ASN C OD1 1 
ATOM   7792 N  ND2 . ASN C  1  320 ? 11.020  6.923   3.960  1.00 37.98  ? 333 ASN C ND2 1 
ATOM   7793 N  N   . VAL C  1  321 ? 7.063   8.278   5.387  1.00 37.43  ? 334 VAL C N   1 
ATOM   7794 C  CA  . VAL C  1  321 ? 6.197   8.884   4.393  1.00 40.36  ? 334 VAL C CA  1 
ATOM   7795 C  C   . VAL C  1  321 ? 5.502   10.098  5.009  1.00 41.51  ? 334 VAL C C   1 
ATOM   7796 O  O   . VAL C  1  321 ? 5.541   11.189  4.444  1.00 45.43  ? 334 VAL C O   1 
ATOM   7797 C  CB  . VAL C  1  321 ? 5.192   7.887   3.777  1.00 41.42  ? 334 VAL C CB  1 
ATOM   7798 C  CG1 . VAL C  1  321 ? 4.296   8.564   2.749  1.00 42.26  ? 334 VAL C CG1 1 
ATOM   7799 C  CG2 . VAL C  1  321 ? 5.913   6.704   3.131  1.00 39.69  ? 334 VAL C CG2 1 
ATOM   7800 N  N   . ALA C  1  322 ? 4.877   9.922   6.176  1.00 43.07  ? 335 ALA C N   1 
ATOM   7801 C  CA  . ALA C  1  322 ? 4.017   10.972  6.711  1.00 45.37  ? 335 ALA C CA  1 
ATOM   7802 C  C   . ALA C  1  322 ? 4.814   12.224  7.077  1.00 41.19  ? 335 ALA C C   1 
ATOM   7803 O  O   . ALA C  1  322 ? 4.270   13.320  7.031  1.00 44.48  ? 335 ALA C O   1 
ATOM   7804 C  CB  . ALA C  1  322 ? 3.215   10.460  7.893  1.00 46.93  ? 335 ALA C CB  1 
ATOM   7805 N  N   . PHE C  1  323 ? 6.085   12.073  7.454  1.00 40.31  ? 336 PHE C N   1 
ATOM   7806 C  CA  . PHE C  1  323 ? 6.879   13.202  7.920  1.00 45.29  ? 336 PHE C CA  1 
ATOM   7807 C  C   . PHE C  1  323 ? 7.807   13.705  6.814  1.00 47.19  ? 336 PHE C C   1 
ATOM   7808 O  O   . PHE C  1  323 ? 8.602   14.610  7.057  1.00 49.33  ? 336 PHE C O   1 
ATOM   7809 C  CB  . PHE C  1  323 ? 7.707   12.828  9.160  1.00 44.81  ? 336 PHE C CB  1 
ATOM   7810 C  CG  . PHE C  1  323 ? 6.931   12.594  10.451 1.00 44.65  ? 336 PHE C CG  1 
ATOM   7811 C  CD1 . PHE C  1  323 ? 5.541   12.668  10.506 1.00 45.14  ? 336 PHE C CD1 1 
ATOM   7812 C  CD2 . PHE C  1  323 ? 7.613   12.268  11.620 1.00 46.78  ? 336 PHE C CD2 1 
ATOM   7813 C  CE1 . PHE C  1  323 ? 4.861   12.418  11.686 1.00 47.12  ? 336 PHE C CE1 1 
ATOM   7814 C  CE2 . PHE C  1  323 ? 6.934   12.029  12.803 1.00 44.04  ? 336 PHE C CE2 1 
ATOM   7815 C  CZ  . PHE C  1  323 ? 5.558   12.099  12.832 1.00 49.32  ? 336 PHE C CZ  1 
ATOM   7816 N  N   . GLY C  1  324 ? 7.724   13.102  5.620  1.00 47.74  ? 337 GLY C N   1 
ATOM   7817 C  CA  . GLY C  1  324 ? 8.483   13.573  4.473  1.00 45.29  ? 337 GLY C CA  1 
ATOM   7818 C  C   . GLY C  1  324 ? 9.963   13.192  4.544  1.00 48.19  ? 337 GLY C C   1 
ATOM   7819 O  O   . GLY C  1  324 ? 10.796  13.889  3.977  1.00 48.12  ? 337 GLY C O   1 
ATOM   7820 N  N   . GLY C  1  325 ? 10.287  12.087  5.234  1.00 45.61  ? 338 GLY C N   1 
ATOM   7821 C  CA  . GLY C  1  325 ? 11.633  11.541  5.270  1.00 46.93  ? 338 GLY C CA  1 
ATOM   7822 C  C   . GLY C  1  325 ? 12.315  11.767  6.618  1.00 48.26  ? 338 GLY C C   1 
ATOM   7823 O  O   . GLY C  1  325 ? 12.568  12.909  6.984  1.00 43.60  ? 338 GLY C O   1 
ATOM   7824 N  N   . CYS C  1  326 ? 12.602  10.672  7.340  1.00 47.82  ? 339 CYS C N   1 
ATOM   7825 C  CA  . CYS C  1  326 ? 13.411  10.714  8.550  1.00 48.44  ? 339 CYS C CA  1 
ATOM   7826 C  C   . CYS C  1  326 ? 14.389  9.544   8.534  1.00 47.06  ? 339 CYS C C   1 
ATOM   7827 O  O   . CYS C  1  326 ? 14.020  8.442   8.138  1.00 44.64  ? 339 CYS C O   1 
ATOM   7828 C  CB  . CYS C  1  326 ? 12.585  10.581  9.834  1.00 51.93  ? 339 CYS C CB  1 
ATOM   7829 S  SG  . CYS C  1  326 ? 11.322  11.862  10.065 1.00 61.66  ? 339 CYS C SG  1 
ATOM   7830 N  N   . ASP C  1  327 ? 15.622  9.777   8.998  1.00 42.53  ? 340 ASP C N   1 
ATOM   7831 C  CA  . ASP C  1  327 ? 16.590  8.706   9.151  1.00 44.72  ? 340 ASP C CA  1 
ATOM   7832 C  C   . ASP C  1  327 ? 16.143  7.775   10.280 1.00 44.26  ? 340 ASP C C   1 
ATOM   7833 O  O   . ASP C  1  327 ? 15.872  8.201   11.399 1.00 40.40  ? 340 ASP C O   1 
ATOM   7834 C  CB  . ASP C  1  327 ? 17.988  9.243   9.419  1.00 48.50  ? 340 ASP C CB  1 
ATOM   7835 C  CG  . ASP C  1  327 ? 18.672  9.939   8.247  1.00 53.76  ? 340 ASP C CG  1 
ATOM   7836 O  OD1 . ASP C  1  327 ? 18.057  10.078  7.178  1.00 50.91  ? 340 ASP C OD1 1 
ATOM   7837 O  OD2 . ASP C  1  327 ? 19.846  10.317  8.401  1.00 60.31  ? 340 ASP C OD2 1 
ATOM   7838 N  N   . GLU C  1  328 ? 16.081  6.485   9.964  1.00 42.70  ? 341 GLU C N   1 
ATOM   7839 C  CA  . GLU C  1  328 ? 15.647  5.478   10.909 1.00 43.39  ? 341 GLU C CA  1 
ATOM   7840 C  C   . GLU C  1  328 ? 16.690  5.327   12.012 1.00 44.05  ? 341 GLU C C   1 
ATOM   7841 O  O   . GLU C  1  328 ? 17.883  5.272   11.736 1.00 43.66  ? 341 GLU C O   1 
ATOM   7842 C  CB  . GLU C  1  328 ? 15.407  4.163   10.167 1.00 42.47  ? 341 GLU C CB  1 
ATOM   7843 C  CG  . GLU C  1  328 ? 14.774  3.091   11.048 1.00 42.96  ? 341 GLU C CG  1 
ATOM   7844 C  CD  . GLU C  1  328 ? 14.312  1.852   10.317 1.00 46.40  ? 341 GLU C CD  1 
ATOM   7845 O  OE1 . GLU C  1  328 ? 14.533  1.782   9.088  1.00 46.91  ? 341 GLU C OE1 1 
ATOM   7846 O  OE2 . GLU C  1  328 ? 13.733  0.960   10.994 1.00 45.48  ? 341 GLU C OE2 1 
ATOM   7847 N  N   . LEU C  1  329 ? 16.220  5.220   13.256 1.00 43.43  ? 342 LEU C N   1 
ATOM   7848 C  CA  . LEU C  1  329 ? 17.074  4.903   14.394 1.00 46.50  ? 342 LEU C CA  1 
ATOM   7849 C  C   . LEU C  1  329 ? 16.935  3.422   14.738 1.00 43.69  ? 342 LEU C C   1 
ATOM   7850 O  O   . LEU C  1  329 ? 15.871  2.835   14.535 1.00 40.81  ? 342 LEU C O   1 
ATOM   7851 C  CB  . LEU C  1  329 ? 16.701  5.785   15.587 1.00 48.24  ? 342 LEU C CB  1 
ATOM   7852 C  CG  . LEU C  1  329 ? 16.885  7.292   15.391 1.00 52.06  ? 342 LEU C CG  1 
ATOM   7853 C  CD1 . LEU C  1  329 ? 16.244  8.077   16.508 1.00 52.63  ? 342 LEU C CD1 1 
ATOM   7854 C  CD2 . LEU C  1  329 ? 18.363  7.634   15.308 1.00 52.92  ? 342 LEU C CD2 1 
ATOM   7855 N  N   . PHE C  1  330 ? 18.012  2.843   15.287 1.00 39.65  ? 343 PHE C N   1 
ATOM   7856 C  CA  . PHE C  1  330 ? 18.063  1.430   15.626 1.00 42.21  ? 343 PHE C CA  1 
ATOM   7857 C  C   . PHE C  1  330 ? 18.539  1.271   17.066 1.00 44.70  ? 343 PHE C C   1 
ATOM   7858 O  O   . PHE C  1  330 ? 19.628  0.752   17.303 1.00 48.82  ? 343 PHE C O   1 
ATOM   7859 C  CB  . PHE C  1  330 ? 18.987  0.682   14.653 1.00 44.65  ? 343 PHE C CB  1 
ATOM   7860 C  CG  . PHE C  1  330 ? 18.571  0.820   13.194 1.00 45.79  ? 343 PHE C CG  1 
ATOM   7861 C  CD1 . PHE C  1  330 ? 17.503  0.077   12.690 1.00 46.77  ? 343 PHE C CD1 1 
ATOM   7862 C  CD2 . PHE C  1  330 ? 19.216  1.711   12.338 1.00 45.80  ? 343 PHE C CD2 1 
ATOM   7863 C  CE1 . PHE C  1  330 ? 17.097  0.215   11.369 1.00 48.18  ? 343 PHE C CE1 1 
ATOM   7864 C  CE2 . PHE C  1  330 ? 18.817  1.833   11.011 1.00 48.56  ? 343 PHE C CE2 1 
ATOM   7865 C  CZ  . PHE C  1  330 ? 17.741  1.102   10.532 1.00 48.31  ? 343 PHE C CZ  1 
ATOM   7866 N  N   . PRO C  1  331 ? 17.734  1.676   18.071 1.00 43.41  ? 344 PRO C N   1 
ATOM   7867 C  CA  . PRO C  1  331 ? 18.193  1.678   19.464 1.00 40.99  ? 344 PRO C CA  1 
ATOM   7868 C  C   . PRO C  1  331 ? 18.535  0.296   20.015 1.00 38.24  ? 344 PRO C C   1 
ATOM   7869 O  O   . PRO C  1  331 ? 19.287  0.193   20.975 1.00 39.23  ? 344 PRO C O   1 
ATOM   7870 C  CB  . PRO C  1  331 ? 17.026  2.339   20.221 1.00 41.86  ? 344 PRO C CB  1 
ATOM   7871 C  CG  . PRO C  1  331 ? 15.816  2.022   19.355 1.00 41.35  ? 344 PRO C CG  1 
ATOM   7872 C  CD  . PRO C  1  331 ? 16.344  2.143   17.922 1.00 42.90  ? 344 PRO C CD  1 
ATOM   7873 N  N   . TYR C  1  332 ? 17.986  -0.760  19.404 1.00 40.00  ? 345 TYR C N   1 
ATOM   7874 C  CA  . TYR C  1  332 ? 18.255  -2.121  19.839 1.00 38.87  ? 345 TYR C CA  1 
ATOM   7875 C  C   . TYR C  1  332 ? 18.931  -2.914  18.728 1.00 40.20  ? 345 TYR C C   1 
ATOM   7876 O  O   . TYR C  1  332 ? 18.985  -4.140  18.802 1.00 41.48  ? 345 TYR C O   1 
ATOM   7877 C  CB  . TYR C  1  332 ? 16.961  -2.801  20.291 1.00 40.77  ? 345 TYR C CB  1 
ATOM   7878 C  CG  . TYR C  1  332 ? 16.195  -1.951  21.289 1.00 40.70  ? 345 TYR C CG  1 
ATOM   7879 C  CD1 . TYR C  1  332 ? 16.720  -1.674  22.547 1.00 41.72  ? 345 TYR C CD1 1 
ATOM   7880 C  CD2 . TYR C  1  332 ? 14.973  -1.390  20.957 1.00 39.83  ? 345 TYR C CD2 1 
ATOM   7881 C  CE1 . TYR C  1  332 ? 16.041  -0.876  23.452 1.00 43.80  ? 345 TYR C CE1 1 
ATOM   7882 C  CE2 . TYR C  1  332 ? 14.280  -0.594  21.856 1.00 43.18  ? 345 TYR C CE2 1 
ATOM   7883 C  CZ  . TYR C  1  332 ? 14.809  -0.343  23.111 1.00 43.49  ? 345 TYR C CZ  1 
ATOM   7884 O  OH  . TYR C  1  332 ? 14.126  0.443   23.992 1.00 42.17  ? 345 TYR C OH  1 
ATOM   7885 N  N   . GLY C  1  333 ? 19.471  -2.217  17.724 1.00 44.87  ? 346 GLY C N   1 
ATOM   7886 C  CA  . GLY C  1  333 ? 20.150  -2.879  16.623 1.00 49.12  ? 346 GLY C CA  1 
ATOM   7887 C  C   . GLY C  1  333 ? 19.157  -3.559  15.683 1.00 47.70  ? 346 GLY C C   1 
ATOM   7888 O  O   . GLY C  1  333 ? 18.061  -3.059  15.484 1.00 48.83  ? 346 GLY C O   1 
ATOM   7889 N  N   . GLN C  1  334 ? 19.564  -4.711  15.141 1.00 51.52  ? 347 GLN C N   1 
ATOM   7890 C  CA  A GLN C  1  334 ? 18.851  -5.404  14.080 0.50 50.35  ? 347 GLN C CA  1 
ATOM   7891 C  CA  B GLN C  1  334 ? 18.818  -5.396  14.100 0.50 53.22  ? 347 GLN C CA  1 
ATOM   7892 C  C   . GLN C  1  334 ? 18.515  -6.819  14.553 1.00 48.61  ? 347 GLN C C   1 
ATOM   7893 O  O   . GLN C  1  334 ? 19.091  -7.300  15.533 1.00 47.66  ? 347 GLN C O   1 
ATOM   7894 C  CB  A GLN C  1  334 ? 19.704  -5.473  12.809 0.50 51.97  ? 347 GLN C CB  1 
ATOM   7895 C  CB  B GLN C  1  334 ? 19.625  -5.317  12.804 0.50 59.55  ? 347 GLN C CB  1 
ATOM   7896 C  CG  A GLN C  1  334 ? 20.472  -4.214  12.406 0.50 51.14  ? 347 GLN C CG  1 
ATOM   7897 C  CG  B GLN C  1  334 ? 19.623  -3.928  12.174 0.50 62.78  ? 347 GLN C CG  1 
ATOM   7898 C  CD  A GLN C  1  334 ? 19.609  -3.154  11.759 0.50 49.41  ? 347 GLN C CD  1 
ATOM   7899 C  CD  B GLN C  1  334 ? 20.542  -3.816  10.978 0.50 69.06  ? 347 GLN C CD  1 
ATOM   7900 O  OE1 A GLN C  1  334 ? 19.775  -1.953  11.998 0.50 48.60  ? 347 GLN C OE1 1 
ATOM   7901 O  OE1 B GLN C  1  334 ? 21.496  -4.590  10.822 0.50 71.00  ? 347 GLN C OE1 1 
ATOM   7902 N  NE2 A GLN C  1  334 ? 18.724  -3.586  10.872 0.50 49.62  ? 347 GLN C NE2 1 
ATOM   7903 N  NE2 B GLN C  1  334 ? 20.271  -2.832  10.133 0.50 69.81  ? 347 GLN C NE2 1 
ATOM   7904 N  N   . LEU C  1  335 ? 17.579  -7.472  13.849 1.00 45.51  ? 348 LEU C N   1 
ATOM   7905 C  CA  . LEU C  1  335 ? 17.122  -8.808  14.208 1.00 49.28  ? 348 LEU C CA  1 
ATOM   7906 C  C   . LEU C  1  335 ? 18.259  -9.837  14.060 1.00 51.15  ? 348 LEU C C   1 
ATOM   7907 O  O   . LEU C  1  335 ? 19.013  -9.675  13.084 1.00 53.71  ? 348 LEU C O   1 
ATOM   7908 C  CB  . LEU C  1  335 ? 15.932  -9.198  13.334 1.00 50.49  ? 348 LEU C CB  1 
ATOM   7909 C  CG  . LEU C  1  335 ? 14.630  -8.423  13.563 1.00 53.55  ? 348 LEU C CG  1 
ATOM   7910 C  CD1 . LEU C  1  335 ? 13.566  -8.869  12.572 1.00 56.69  ? 348 LEU C CD1 1 
ATOM   7911 C  CD2 . LEU C  1  335 ? 14.148  -8.631  14.980 1.00 53.82  ? 348 LEU C CD2 1 
HETATM 7912 C  C1  . NAG D  2  .   ? 29.167  12.523  33.833 1.00 56.21  ? 1   NAG G C1  1 
HETATM 7913 C  C2  . NAG D  2  .   ? 29.228  13.933  34.422 1.00 60.09  ? 1   NAG G C2  1 
HETATM 7914 C  C3  . NAG D  2  .   ? 28.548  14.916  33.474 1.00 62.12  ? 1   NAG G C3  1 
HETATM 7915 C  C4  . NAG D  2  .   ? 29.164  14.867  32.083 1.00 60.13  ? 1   NAG G C4  1 
HETATM 7916 C  C5  . NAG D  2  .   ? 29.203  13.432  31.561 1.00 59.53  ? 1   NAG G C5  1 
HETATM 7917 C  C6  . NAG D  2  .   ? 30.070  13.283  30.322 1.00 58.10  ? 1   NAG G C6  1 
HETATM 7918 C  C7  . NAG D  2  .   ? 27.611  13.445  36.243 1.00 71.31  ? 1   NAG G C7  1 
HETATM 7919 C  C8  . NAG D  2  .   ? 27.602  13.266  37.730 1.00 73.71  ? 1   NAG G C8  1 
HETATM 7920 N  N2  . NAG D  2  .   ? 28.674  14.093  35.752 1.00 64.49  ? 1   NAG G N2  1 
HETATM 7921 O  O3  . NAG D  2  .   ? 28.688  16.207  34.043 1.00 59.95  ? 1   NAG G O3  1 
HETATM 7922 O  O4  . NAG D  2  .   ? 28.369  15.684  31.214 1.00 61.06  ? 1   NAG G O4  1 
HETATM 7923 O  O5  . NAG D  2  .   ? 29.781  12.551  32.548 1.00 57.07  ? 1   NAG G O5  1 
HETATM 7924 O  O6  . NAG D  2  .   ? 31.473  13.463  30.635 1.00 49.65  ? 1   NAG G O6  1 
HETATM 7925 O  O7  . NAG D  2  .   ? 26.691  13.033  35.538 1.00 76.78  ? 1   NAG G O7  1 
HETATM 7926 C  C1  . NAG D  2  .   ? 29.050  16.550  30.359 1.00 62.98  ? 2   NAG G C1  1 
HETATM 7927 C  C2  . NAG D  2  .   ? 28.231  16.825  29.105 1.00 62.01  ? 2   NAG G C2  1 
HETATM 7928 C  C3  . NAG D  2  .   ? 28.972  17.810  28.201 1.00 68.81  ? 2   NAG G C3  1 
HETATM 7929 C  C4  . NAG D  2  .   ? 29.335  19.073  28.982 1.00 72.37  ? 2   NAG G C4  1 
HETATM 7930 C  C5  . NAG D  2  .   ? 30.106  18.683  30.243 1.00 66.61  ? 2   NAG G C5  1 
HETATM 7931 C  C6  . NAG D  2  .   ? 30.408  19.862  31.132 1.00 63.76  ? 2   NAG G C6  1 
HETATM 7932 C  C7  . NAG D  2  .   ? 26.811  14.882  28.622 1.00 57.44  ? 2   NAG G C7  1 
HETATM 7933 C  C8  . NAG D  2  .   ? 26.658  13.629  27.811 1.00 55.57  ? 2   NAG G C8  1 
HETATM 7934 N  N2  . NAG D  2  .   ? 27.920  15.598  28.401 1.00 61.01  ? 2   NAG G N2  1 
HETATM 7935 O  O3  . NAG D  2  .   ? 28.160  18.095  27.067 1.00 67.00  ? 2   NAG G O3  1 
HETATM 7936 O  O4  . NAG D  2  .   ? 30.174  19.949  28.208 1.00 81.42  ? 2   NAG G O4  1 
HETATM 7937 O  O5  . NAG D  2  .   ? 29.322  17.771  31.039 1.00 61.74  ? 2   NAG G O5  1 
HETATM 7938 O  O6  . NAG D  2  .   ? 29.200  20.376  31.656 1.00 61.71  ? 2   NAG G O6  1 
HETATM 7939 O  O7  . NAG D  2  .   ? 25.962  15.235  29.437 1.00 53.14  ? 2   NAG G O7  1 
HETATM 7940 C  C1  . BMA D  2  .   ? 29.640  20.946  27.395 1.00 80.93  ? 3   BMA G C1  1 
HETATM 7941 C  C2  . BMA D  2  .   ? 30.758  21.945  27.105 1.00 82.93  ? 3   BMA G C2  1 
HETATM 7942 C  C3  . BMA D  2  .   ? 30.338  22.951  26.017 1.00 88.67  ? 3   BMA G C3  1 
HETATM 7943 C  C4  . BMA D  2  .   ? 29.743  22.246  24.796 1.00 95.89  ? 3   BMA G C4  1 
HETATM 7944 C  C5  . BMA D  2  .   ? 28.651  21.250  25.198 1.00 94.12  ? 3   BMA G C5  1 
HETATM 7945 C  C6  . BMA D  2  .   ? 28.174  20.392  24.041 1.00 94.69  ? 3   BMA G C6  1 
HETATM 7946 O  O2  . BMA D  2  .   ? 31.965  21.235  26.807 1.00 70.12  ? 3   BMA G O2  1 
HETATM 7947 O  O3  . BMA D  2  .   ? 31.471  23.757  25.625 1.00 88.64  ? 3   BMA G O3  1 
HETATM 7948 O  O4  . BMA D  2  .   ? 29.157  23.210  23.919 1.00 106.70 ? 3   BMA G O4  1 
HETATM 7949 O  O5  . BMA D  2  .   ? 29.157  20.338  26.198 1.00 82.96  ? 3   BMA G O5  1 
HETATM 7950 O  O6  . BMA D  2  .   ? 27.121  19.500  24.475 1.00 94.94  ? 3   BMA G O6  1 
HETATM 7951 C  C1  . MAN D  2  .   ? 31.709  24.927  26.353 1.00 84.96  ? 4   MAN G C1  1 
HETATM 7952 C  C2  . MAN D  2  .   ? 32.404  25.945  25.453 1.00 83.69  ? 4   MAN G C2  1 
HETATM 7953 C  C3  . MAN D  2  .   ? 33.837  25.484  25.104 1.00 78.32  ? 4   MAN G C3  1 
HETATM 7954 C  C4  . MAN D  2  .   ? 34.638  25.204  26.370 1.00 77.97  ? 4   MAN G C4  1 
HETATM 7955 C  C5  . MAN D  2  .   ? 33.869  24.228  27.271 1.00 80.96  ? 4   MAN G C5  1 
HETATM 7956 C  C6  . MAN D  2  .   ? 34.526  24.060  28.623 1.00 78.12  ? 4   MAN G C6  1 
HETATM 7957 O  O2  . MAN D  2  .   ? 32.345  27.234  26.075 1.00 76.54  ? 4   MAN G O2  1 
HETATM 7958 O  O3  . MAN D  2  .   ? 34.516  26.455  24.304 1.00 78.62  ? 4   MAN G O3  1 
HETATM 7959 O  O4  . MAN D  2  .   ? 35.921  24.642  26.046 1.00 69.28  ? 4   MAN G O4  1 
HETATM 7960 O  O5  . MAN D  2  .   ? 32.506  24.698  27.519 1.00 80.03  ? 4   MAN G O5  1 
HETATM 7961 O  O6  . MAN D  2  .   ? 34.649  25.309  29.310 1.00 67.98  ? 4   MAN G O6  1 
HETATM 7962 C  C1  . MAN D  2  .   ? 26.311  18.951  23.466 1.00 100.29 ? 5   MAN G C1  1 
HETATM 7963 C  C2  . MAN D  2  .   ? 25.170  18.209  24.158 1.00 91.82  ? 5   MAN G C2  1 
HETATM 7964 C  C3  . MAN D  2  .   ? 25.632  16.943  24.867 1.00 92.29  ? 5   MAN G C3  1 
HETATM 7965 C  C4  . MAN D  2  .   ? 26.487  16.067  23.942 1.00 98.66  ? 5   MAN G C4  1 
HETATM 7966 C  C5  . MAN D  2  .   ? 27.595  16.886  23.249 1.00 103.67 ? 5   MAN G C5  1 
HETATM 7967 C  C6  . MAN D  2  .   ? 28.311  16.095  22.172 1.00 105.28 ? 5   MAN G C6  1 
HETATM 7968 O  O2  . MAN D  2  .   ? 24.159  17.891  23.207 1.00 92.86  ? 5   MAN G O2  1 
HETATM 7969 O  O3  . MAN D  2  .   ? 24.474  16.245  25.338 1.00 73.61  ? 5   MAN G O3  1 
HETATM 7970 O  O4  . MAN D  2  .   ? 27.120  15.016  24.685 1.00 92.28  ? 5   MAN G O4  1 
HETATM 7971 O  O5  . MAN D  2  .   ? 27.039  18.067  22.607 1.00 100.94 ? 5   MAN G O5  1 
HETATM 7972 O  O6  . MAN D  2  .   ? 29.085  16.938  21.325 1.00 105.91 ? 5   MAN G O6  1 
HETATM 7973 C  C1  . NAG E  3  .   ? 28.109  -8.600  19.594 1.00 52.88  ? 1   NAG H C1  1 
HETATM 7974 C  C2  . NAG E  3  .   ? 28.710  -9.595  18.607 1.00 52.73  ? 1   NAG H C2  1 
HETATM 7975 C  C3  . NAG E  3  .   ? 28.005  -9.534  17.261 1.00 51.72  ? 1   NAG H C3  1 
HETATM 7976 C  C4  . NAG E  3  .   ? 26.492  -9.574  17.442 1.00 54.57  ? 1   NAG H C4  1 
HETATM 7977 C  C5  . NAG E  3  .   ? 26.030  -8.541  18.465 1.00 54.51  ? 1   NAG H C5  1 
HETATM 7978 C  C6  . NAG E  3  .   ? 24.559  -8.647  18.751 1.00 53.99  ? 1   NAG H C6  1 
HETATM 7979 C  C7  . NAG E  3  .   ? 31.022  -10.311 18.816 1.00 50.24  ? 1   NAG H C7  1 
HETATM 7980 C  C8  . NAG E  3  .   ? 32.438  -10.099 18.376 1.00 53.90  ? 1   NAG H C8  1 
HETATM 7981 N  N2  . NAG E  3  .   ? 30.136  -9.389  18.448 1.00 55.32  ? 1   NAG H N2  1 
HETATM 7982 O  O3  . NAG E  3  .   ? 28.486  -10.650 16.522 1.00 49.71  ? 1   NAG H O3  1 
HETATM 7983 O  O4  . NAG E  3  .   ? 25.845  -9.274  16.214 1.00 56.17  ? 1   NAG H O4  1 
HETATM 7984 O  O5  . NAG E  3  .   ? 26.703  -8.796  19.706 1.00 48.66  ? 1   NAG H O5  1 
HETATM 7985 O  O6  . NAG E  3  .   ? 24.229  -9.986  19.133 1.00 49.77  ? 1   NAG H O6  1 
HETATM 7986 O  O7  . NAG E  3  .   ? 30.683  -11.303 19.449 1.00 47.54  ? 1   NAG H O7  1 
HETATM 7987 C  C1  . NAG E  3  .   ? 25.491  -10.422 15.523 1.00 62.64  ? 2   NAG H C1  1 
HETATM 7988 C  C2  . NAG E  3  .   ? 24.086  -10.373 14.914 1.00 64.99  ? 2   NAG H C2  1 
HETATM 7989 C  C3  . NAG E  3  .   ? 23.920  -11.531 13.934 1.00 71.38  ? 2   NAG H C3  1 
HETATM 7990 C  C4  . NAG E  3  .   ? 25.049  -11.464 12.914 1.00 76.50  ? 2   NAG H C4  1 
HETATM 7991 C  C5  . NAG E  3  .   ? 26.376  -11.618 13.651 1.00 73.97  ? 2   NAG H C5  1 
HETATM 7992 C  C6  . NAG E  3  .   ? 27.583  -11.606 12.745 1.00 73.86  ? 2   NAG H C6  1 
HETATM 7993 C  C7  . NAG E  3  .   ? 22.339  -9.272  16.223 1.00 73.76  ? 2   NAG H C7  1 
HETATM 7994 C  C8  . NAG E  3  .   ? 21.541  -9.327  17.497 1.00 79.02  ? 2   NAG H C8  1 
HETATM 7995 N  N2  . NAG E  3  .   ? 23.008  -10.378 15.884 1.00 68.22  ? 2   NAG H N2  1 
HETATM 7996 O  O3  . NAG E  3  .   ? 22.655  -11.506 13.282 1.00 74.59  ? 2   NAG H O3  1 
HETATM 7997 O  O4  . NAG E  3  .   ? 24.932  -12.491 11.918 1.00 85.78  ? 2   NAG H O4  1 
HETATM 7998 O  O5  . NAG E  3  .   ? 26.518  -10.493 14.537 1.00 66.82  ? 2   NAG H O5  1 
HETATM 7999 O  O6  . NAG E  3  .   ? 28.788  -11.574 13.492 1.00 76.86  ? 2   NAG H O6  1 
HETATM 8000 O  O7  . NAG E  3  .   ? 22.408  -8.256  15.537 1.00 66.48  ? 2   NAG H O7  1 
HETATM 8001 C  C1  . BMA E  3  .   ? 25.386  -12.178 10.635 1.00 90.67  ? 3   BMA H C1  1 
HETATM 8002 C  C2  . BMA E  3  .   ? 25.791  -13.488 9.970  1.00 92.14  ? 3   BMA H C2  1 
HETATM 8003 C  C3  . BMA E  3  .   ? 26.141  -13.304 8.494  1.00 100.76 ? 3   BMA H C3  1 
HETATM 8004 C  C4  . BMA E  3  .   ? 25.073  -12.494 7.783  1.00 96.33  ? 3   BMA H C4  1 
HETATM 8005 C  C5  . BMA E  3  .   ? 24.859  -11.186 8.524  1.00 92.32  ? 3   BMA H C5  1 
HETATM 8006 C  C6  . BMA E  3  .   ? 23.836  -10.269 7.886  1.00 95.17  ? 3   BMA H C6  1 
HETATM 8007 O  O2  . BMA E  3  .   ? 24.751  -14.451 10.131 1.00 77.71  ? 3   BMA H O2  1 
HETATM 8008 O  O3  . BMA E  3  .   ? 26.286  -14.577 7.858  1.00 117.14 ? 3   BMA H O3  1 
HETATM 8009 O  O4  . BMA E  3  .   ? 25.482  -12.229 6.439  1.00 92.40  ? 3   BMA H O4  1 
HETATM 8010 O  O5  . BMA E  3  .   ? 24.401  -11.505 9.850  1.00 95.95  ? 3   BMA H O5  1 
HETATM 8011 O  O6  . BMA E  3  .   ? 22.493  -10.779 7.922  1.00 100.44 ? 3   BMA H O6  1 
HETATM 8012 C  C1  . MAN E  3  .   ? 21.659  -10.195 6.954  1.00 111.40 ? 4   MAN H C1  1 
HETATM 8013 C  C2  . MAN E  3  .   ? 20.229  -10.661 7.209  1.00 112.14 ? 4   MAN H C2  1 
HETATM 8014 C  C3  . MAN E  3  .   ? 20.051  -12.145 6.877  1.00 116.18 ? 4   MAN H C3  1 
HETATM 8015 C  C4  . MAN E  3  .   ? 20.620  -12.485 5.510  1.00 122.81 ? 4   MAN H C4  1 
HETATM 8016 C  C5  . MAN E  3  .   ? 22.068  -12.024 5.437  1.00 128.01 ? 4   MAN H C5  1 
HETATM 8017 C  C6  . MAN E  3  .   ? 22.739  -12.311 4.107  1.00 132.56 ? 4   MAN H C6  1 
HETATM 8018 O  O2  . MAN E  3  .   ? 19.325  -9.830  6.485  1.00 110.26 ? 4   MAN H O2  1 
HETATM 8019 O  O3  . MAN E  3  .   ? 18.674  -12.516 6.928  1.00 110.54 ? 4   MAN H O3  1 
HETATM 8020 O  O4  . MAN E  3  .   ? 20.550  -13.894 5.304  1.00 126.65 ? 4   MAN H O4  1 
HETATM 8021 O  O5  . MAN E  3  .   ? 22.091  -10.592 5.650  1.00 122.16 ? 4   MAN H O5  1 
HETATM 8022 O  O6  . MAN E  3  .   ? 22.185  -11.513 3.038  1.00 142.97 ? 4   MAN H O6  1 
HETATM 8023 C  C1  . MAN E  3  .   ? 18.415  -13.640 7.710  1.00 110.76 ? 5   MAN H C1  1 
HETATM 8024 C  C2  . MAN E  3  .   ? 16.981  -14.073 7.494  1.00 110.44 ? 5   MAN H C2  1 
HETATM 8025 C  C3  . MAN E  3  .   ? 16.014  -13.007 7.987  1.00 109.32 ? 5   MAN H C3  1 
HETATM 8026 C  C4  . MAN E  3  .   ? 16.316  -12.625 9.433  1.00 107.23 ? 5   MAN H C4  1 
HETATM 8027 C  C5  . MAN E  3  .   ? 17.805  -12.276 9.614  1.00 106.80 ? 5   MAN H C5  1 
HETATM 8028 C  C6  . MAN E  3  .   ? 18.197  -12.082 11.065 1.00 100.54 ? 5   MAN H C6  1 
HETATM 8029 O  O2  . MAN E  3  .   ? 16.754  -15.323 8.142  1.00 109.15 ? 5   MAN H O2  1 
HETATM 8030 O  O3  . MAN E  3  .   ? 14.667  -13.484 7.857  1.00 108.12 ? 5   MAN H O3  1 
HETATM 8031 O  O4  . MAN E  3  .   ? 15.523  -11.498 9.802  1.00 96.85  ? 5   MAN H O4  1 
HETATM 8032 O  O5  . MAN E  3  .   ? 18.634  -13.349 9.097  1.00 108.14 ? 5   MAN H O5  1 
HETATM 8033 O  O6  . MAN E  3  .   ? 19.544  -11.624 11.193 1.00 89.86  ? 5   MAN H O6  1 
HETATM 8034 C  C1  . MAN E  3  .   ? 22.353  -12.021 1.739  1.00 142.63 ? 6   MAN H C1  1 
HETATM 8035 C  C2  . MAN E  3  .   ? 22.733  -10.853 0.841  1.00 141.91 ? 6   MAN H C2  1 
HETATM 8036 C  C3  . MAN E  3  .   ? 21.582  -9.860  0.703  1.00 140.86 ? 6   MAN H C3  1 
HETATM 8037 C  C4  . MAN E  3  .   ? 20.288  -10.565 0.302  1.00 136.62 ? 6   MAN H C4  1 
HETATM 8038 C  C5  . MAN E  3  .   ? 19.989  -11.744 1.234  1.00 132.98 ? 6   MAN H C5  1 
HETATM 8039 C  C6  . MAN E  3  .   ? 18.799  -12.563 0.781  1.00 121.75 ? 6   MAN H C6  1 
HETATM 8040 O  O2  . MAN E  3  .   ? 23.164  -11.334 -0.429 1.00 138.46 ? 6   MAN H O2  1 
HETATM 8041 O  O3  . MAN E  3  .   ? 21.926  -8.861  -0.259 1.00 132.61 ? 6   MAN H O3  1 
HETATM 8042 O  O4  . MAN E  3  .   ? 19.200  -9.644  0.359  1.00 130.84 ? 6   MAN H O4  1 
HETATM 8043 O  O5  . MAN E  3  .   ? 21.134  -12.637 1.278  1.00 139.76 ? 6   MAN H O5  1 
HETATM 8044 O  O6  . MAN E  3  .   ? 18.253  -13.351 1.854  1.00 115.05 ? 6   MAN H O6  1 
HETATM 8045 C  C1  . MAN E  3  .   ? 27.575  -15.113 7.799  1.00 131.20 ? 7   MAN H C1  1 
HETATM 8046 C  C2  . MAN E  3  .   ? 28.030  -15.155 6.335  1.00 135.22 ? 7   MAN H C2  1 
HETATM 8047 C  C3  . MAN E  3  .   ? 27.412  -16.311 5.550  1.00 135.43 ? 7   MAN H C3  1 
HETATM 8048 C  C4  . MAN E  3  .   ? 27.489  -17.613 6.336  1.00 134.92 ? 7   MAN H C4  1 
HETATM 8049 C  C5  . MAN E  3  .   ? 26.852  -17.422 7.705  1.00 128.89 ? 7   MAN H C5  1 
HETATM 8050 C  C6  . MAN E  3  .   ? 26.862  -18.670 8.557  1.00 119.40 ? 7   MAN H C6  1 
HETATM 8051 O  O2  . MAN E  3  .   ? 29.454  -15.212 6.264  1.00 131.68 ? 7   MAN H O2  1 
HETATM 8052 O  O3  . MAN E  3  .   ? 28.088  -16.444 4.292  1.00 131.60 ? 7   MAN H O3  1 
HETATM 8053 O  O4  . MAN E  3  .   ? 26.809  -18.656 5.644  1.00 136.70 ? 7   MAN H O4  1 
HETATM 8054 O  O5  . MAN E  3  .   ? 27.601  -16.415 8.414  1.00 131.94 ? 7   MAN H O5  1 
HETATM 8055 O  O6  . MAN E  3  .   ? 25.990  -18.533 9.671  1.00 114.06 ? 7   MAN H O6  1 
HETATM 8056 C  C1  . NAG F  4  .   ? 24.971  -10.782 68.871 1.00 60.13  ? 1   NAG X C1  1 
HETATM 8057 C  C2  . NAG F  4  .   ? 25.463  -9.816  69.952 1.00 66.07  ? 1   NAG X C2  1 
HETATM 8058 C  C3  . NAG F  4  .   ? 26.205  -10.638 71.000 1.00 66.76  ? 1   NAG X C3  1 
HETATM 8059 C  C4  . NAG F  4  .   ? 25.261  -11.676 71.588 1.00 65.40  ? 1   NAG X C4  1 
HETATM 8060 C  C5  . NAG F  4  .   ? 24.679  -12.554 70.481 1.00 65.21  ? 1   NAG X C5  1 
HETATM 8061 C  C6  . NAG F  4  .   ? 23.607  -13.522 70.958 1.00 62.96  ? 1   NAG X C6  1 
HETATM 8062 C  C7  . NAG F  4  .   ? 27.361  -8.819  68.740 1.00 78.93  ? 1   NAG X C7  1 
HETATM 8063 C  C8  . NAG F  4  .   ? 28.016  -7.536  68.326 1.00 82.33  ? 1   NAG X C8  1 
HETATM 8064 N  N2  . NAG F  4  .   ? 26.235  -8.697  69.449 1.00 70.71  ? 1   NAG X N2  1 
HETATM 8065 O  O3  . NAG F  4  .   ? 26.764  -9.828  72.023 1.00 69.62  ? 1   NAG X O3  1 
HETATM 8066 O  O4  . NAG F  4  .   ? 26.020  -12.491 72.475 1.00 67.06  ? 1   NAG X O4  1 
HETATM 8067 O  O5  . NAG F  4  .   ? 24.079  -11.720 69.470 1.00 61.72  ? 1   NAG X O5  1 
HETATM 8068 O  O6  . NAG F  4  .   ? 22.472  -12.873 71.567 1.00 55.91  ? 1   NAG X O6  1 
HETATM 8069 O  O7  . NAG F  4  .   ? 27.837  -9.914  68.452 1.00 81.73  ? 1   NAG X O7  1 
HETATM 8070 C  C1  . NAG F  4  .   ? 25.468  -12.766 73.723 1.00 67.77  ? 2   NAG X C1  1 
HETATM 8071 C  C2  . NAG F  4  .   ? 26.036  -14.089 74.212 1.00 64.18  ? 2   NAG X C2  1 
HETATM 8072 C  C3  . NAG F  4  .   ? 25.445  -14.397 75.582 1.00 68.56  ? 2   NAG X C3  1 
HETATM 8073 C  C4  . NAG F  4  .   ? 25.693  -13.241 76.544 1.00 74.10  ? 2   NAG X C4  1 
HETATM 8074 C  C5  . NAG F  4  .   ? 25.196  -11.924 75.951 1.00 75.26  ? 2   NAG X C5  1 
HETATM 8075 C  C6  . NAG F  4  .   ? 25.565  -10.719 76.793 1.00 75.43  ? 2   NAG X C6  1 
HETATM 8076 C  C7  . NAG F  4  .   ? 26.751  -15.728 72.495 1.00 70.01  ? 2   NAG X C7  1 
HETATM 8077 C  C8  . NAG F  4  .   ? 26.276  -16.778 71.534 1.00 68.45  ? 2   NAG X C8  1 
HETATM 8078 N  N2  . NAG F  4  .   ? 25.818  -15.195 73.299 1.00 64.58  ? 2   NAG X N2  1 
HETATM 8079 O  O3  . NAG F  4  .   ? 26.017  -15.604 76.071 1.00 66.22  ? 2   NAG X O3  1 
HETATM 8080 O  O4  . NAG F  4  .   ? 24.978  -13.495 77.755 1.00 78.42  ? 2   NAG X O4  1 
HETATM 8081 O  O5  . NAG F  4  .   ? 25.784  -11.727 74.650 1.00 69.37  ? 2   NAG X O5  1 
HETATM 8082 O  O6  . NAG F  4  .   ? 26.978  -10.597 76.935 1.00 76.84  ? 2   NAG X O6  1 
HETATM 8083 O  O7  . NAG F  4  .   ? 27.932  -15.387 72.538 1.00 69.37  ? 2   NAG X O7  1 
HETATM 8084 C  C1  . BMA F  4  .   ? 25.667  -14.091 78.810 1.00 89.74  ? 3   BMA X C1  1 
HETATM 8085 C  C2  . BMA F  4  .   ? 24.922  -13.658 80.063 1.00 91.16  ? 3   BMA X C2  1 
HETATM 8086 C  C3  . BMA F  4  .   ? 25.550  -14.289 81.297 1.00 98.13  ? 3   BMA X C3  1 
HETATM 8087 C  C4  . BMA F  4  .   ? 25.672  -15.804 81.154 1.00 100.63 ? 3   BMA X C4  1 
HETATM 8088 C  C5  . BMA F  4  .   ? 26.350  -16.196 79.825 1.00 98.45  ? 3   BMA X C5  1 
HETATM 8089 C  C6  . BMA F  4  .   ? 26.251  -17.683 79.543 1.00 97.49  ? 3   BMA X C6  1 
HETATM 8090 O  O2  . BMA F  4  .   ? 23.526  -13.943 79.958 1.00 77.88  ? 3   BMA X O2  1 
HETATM 8091 O  O3  . BMA F  4  .   ? 24.768  -13.919 82.450 1.00 98.65  ? 3   BMA X O3  1 
HETATM 8092 O  O4  . BMA F  4  .   ? 26.464  -16.316 82.225 1.00 99.61  ? 3   BMA X O4  1 
HETATM 8093 O  O5  . BMA F  4  .   ? 25.713  -15.516 78.708 1.00 96.23  ? 3   BMA X O5  1 
HETATM 8094 O  O6  . BMA F  4  .   ? 26.901  -18.046 78.322 1.00 94.72  ? 3   BMA X O6  1 
HETATM 8095 C  C1  . MAN F  4  .   ? 24.852  -12.557 82.760 1.00 102.79 ? 4   MAN X C1  1 
HETATM 8096 C  C2  . MAN F  4  .   ? 26.143  -12.366 83.559 1.00 104.84 ? 4   MAN X C2  1 
HETATM 8097 C  C3  . MAN F  4  .   ? 26.017  -12.947 84.973 1.00 104.56 ? 4   MAN X C3  1 
HETATM 8098 C  C4  . MAN F  4  .   ? 24.745  -12.459 85.658 1.00 99.53  ? 4   MAN X C4  1 
HETATM 8099 C  C5  . MAN F  4  .   ? 23.504  -12.715 84.767 1.00 98.30  ? 4   MAN X C5  1 
HETATM 8100 C  C6  . MAN F  4  .   ? 22.214  -12.152 85.331 1.00 90.31  ? 4   MAN X C6  1 
HETATM 8101 O  O2  . MAN F  4  .   ? 26.523  -10.989 83.557 1.00 102.69 ? 4   MAN X O2  1 
HETATM 8102 O  O3  . MAN F  4  .   ? 27.159  -12.609 85.768 1.00 91.73  ? 4   MAN X O3  1 
HETATM 8103 O  O4  . MAN F  4  .   ? 24.623  -13.143 86.903 1.00 100.91 ? 4   MAN X O4  1 
HETATM 8104 O  O5  . MAN F  4  .   ? 23.712  -12.078 83.482 1.00 96.07  ? 4   MAN X O5  1 
HETATM 8105 O  O6  . MAN F  4  .   ? 21.167  -12.117 84.355 1.00 77.18  ? 4   MAN X O6  1 
HETATM 8106 C  C1  . NAG G  5  .   ? 15.827  -30.289 54.839 1.00 50.37  ? 1   NAG Y C1  1 
HETATM 8107 C  C2  . NAG G  5  .   ? 14.696  -31.223 54.413 1.00 50.91  ? 1   NAG Y C2  1 
HETATM 8108 C  C3  . NAG G  5  .   ? 15.010  -32.656 54.819 1.00 49.42  ? 1   NAG Y C3  1 
HETATM 8109 C  C4  . NAG G  5  .   ? 16.366  -33.073 54.258 1.00 50.00  ? 1   NAG Y C4  1 
HETATM 8110 C  C5  . NAG G  5  .   ? 17.440  -32.095 54.727 1.00 49.46  ? 1   NAG Y C5  1 
HETATM 8111 C  C6  . NAG G  5  .   ? 18.792  -32.369 54.103 1.00 45.53  ? 1   NAG Y C6  1 
HETATM 8112 C  C7  . NAG G  5  .   ? 12.411  -30.429 54.116 1.00 54.68  ? 1   NAG Y C7  1 
HETATM 8113 C  C8  . NAG G  5  .   ? 11.051  -30.299 54.733 1.00 57.31  ? 1   NAG Y C8  1 
HETATM 8114 N  N2  . NAG G  5  .   ? 13.409  -30.787 54.926 1.00 51.20  ? 1   NAG Y N2  1 
HETATM 8115 O  O3  . NAG G  5  .   ? 13.965  -33.491 54.344 1.00 49.22  ? 1   NAG Y O3  1 
HETATM 8116 O  O4  . NAG G  5  .   ? 16.699  -34.380 54.719 1.00 51.94  ? 1   NAG Y O4  1 
HETATM 8117 O  O5  . NAG G  5  .   ? 17.082  -30.752 54.340 1.00 48.10  ? 1   NAG Y O5  1 
HETATM 8118 O  O6  . NAG G  5  .   ? 18.713  -32.282 52.680 1.00 44.64  ? 1   NAG Y O6  1 
HETATM 8119 O  O7  . NAG G  5  .   ? 12.595  -30.242 52.918 1.00 55.84  ? 1   NAG Y O7  1 
HETATM 8120 C  C1  . NAG G  5  .   ? 16.411  -35.476 53.908 1.00 59.41  ? 2   NAG Y C1  1 
HETATM 8121 C  C2  . NAG G  5  .   ? 17.491  -36.518 54.175 1.00 60.68  ? 2   NAG Y C2  1 
HETATM 8122 C  C3  . NAG G  5  .   ? 17.130  -37.877 53.582 1.00 68.97  ? 2   NAG Y C3  1 
HETATM 8123 C  C4  . NAG G  5  .   ? 15.705  -38.272 53.946 1.00 75.45  ? 2   NAG Y C4  1 
HETATM 8124 C  C5  . NAG G  5  .   ? 14.762  -37.166 53.484 1.00 74.80  ? 2   NAG Y C5  1 
HETATM 8125 C  C6  . NAG G  5  .   ? 13.300  -37.444 53.759 1.00 74.01  ? 2   NAG Y C6  1 
HETATM 8126 C  C7  . NAG G  5  .   ? 19.780  -35.668 54.392 1.00 54.15  ? 2   NAG Y C7  1 
HETATM 8127 C  C8  . NAG G  5  .   ? 21.028  -35.261 53.665 1.00 53.64  ? 2   NAG Y C8  1 
HETATM 8128 N  N2  . NAG G  5  .   ? 18.761  -36.081 53.635 1.00 54.61  ? 2   NAG Y N2  1 
HETATM 8129 O  O3  . NAG G  5  .   ? 18.064  -38.832 54.067 1.00 68.75  ? 2   NAG Y O3  1 
HETATM 8130 O  O4  . NAG G  5  .   ? 15.379  -39.524 53.324 1.00 84.24  ? 2   NAG Y O4  1 
HETATM 8131 O  O5  . NAG G  5  .   ? 15.109  -35.973 54.215 1.00 66.09  ? 2   NAG Y O5  1 
HETATM 8132 O  O6  . NAG G  5  .   ? 13.024  -37.356 55.152 1.00 74.09  ? 2   NAG Y O6  1 
HETATM 8133 O  O7  . NAG G  5  .   ? 19.694  -35.605 55.614 1.00 53.76  ? 2   NAG Y O7  1 
HETATM 8134 C  C1  . BMA G  5  .   ? 14.817  -40.485 54.163 1.00 93.35  ? 3   BMA Y C1  1 
HETATM 8135 C  C2  . BMA G  5  .   ? 14.090  -41.511 53.308 1.00 96.37  ? 3   BMA Y C2  1 
HETATM 8136 C  C3  . BMA G  5  .   ? 13.382  -42.478 54.244 1.00 105.31 ? 3   BMA Y C3  1 
HETATM 8137 C  C4  . BMA G  5  .   ? 14.440  -43.175 55.103 1.00 100.95 ? 3   BMA Y C4  1 
HETATM 8138 C  C5  . BMA G  5  .   ? 15.216  -42.102 55.897 1.00 99.38  ? 3   BMA Y C5  1 
HETATM 8139 C  C6  . BMA G  5  .   ? 16.353  -42.639 56.748 1.00 103.11 ? 3   BMA Y C6  1 
HETATM 8140 O  O2  . BMA G  5  .   ? 15.023  -42.122 52.422 1.00 88.49  ? 3   BMA Y O2  1 
HETATM 8141 O  O3  . BMA G  5  .   ? 12.484  -43.369 53.549 1.00 118.02 ? 3   BMA Y O3  1 
HETATM 8142 O  O4  . BMA G  5  .   ? 13.836  -44.087 56.026 1.00 98.53  ? 3   BMA Y O4  1 
HETATM 8143 O  O5  . BMA G  5  .   ? 15.790  -41.151 54.969 1.00 92.17  ? 3   BMA Y O5  1 
HETATM 8144 O  O6  . BMA G  5  .   ? 17.261  -43.445 55.991 1.00 111.14 ? 3   BMA Y O6  1 
HETATM 8145 C  C1  . MAN G  5  .   ? 18.375  -43.952 56.684 1.00 109.24 ? 4   MAN Y C1  1 
HETATM 8146 C  C2  . MAN G  5  .   ? 19.508  -44.055 55.676 1.00 107.79 ? 4   MAN Y C2  1 
HETATM 8147 C  C3  . MAN G  5  .   ? 19.167  -45.042 54.563 1.00 108.93 ? 4   MAN Y C3  1 
HETATM 8148 C  C4  . MAN G  5  .   ? 18.586  -46.362 55.073 1.00 109.47 ? 4   MAN Y C4  1 
HETATM 8149 C  C5  . MAN G  5  .   ? 17.643  -46.221 56.286 1.00 109.09 ? 4   MAN Y C5  1 
HETATM 8150 C  C6  . MAN G  5  .   ? 17.496  -47.521 57.051 1.00 109.63 ? 4   MAN Y C6  1 
HETATM 8151 O  O2  . MAN G  5  .   ? 20.719  -44.396 56.342 1.00 105.13 ? 4   MAN Y O2  1 
HETATM 8152 O  O3  . MAN G  5  .   ? 20.353  -45.325 53.822 1.00 108.64 ? 4   MAN Y O3  1 
HETATM 8153 O  O4  . MAN G  5  .   ? 17.843  -46.961 54.010 1.00 103.82 ? 4   MAN Y O4  1 
HETATM 8154 O  O5  . MAN G  5  .   ? 18.129  -45.245 57.237 1.00 107.08 ? 4   MAN Y O5  1 
HETATM 8155 O  O6  . MAN G  5  .   ? 16.304  -48.234 56.667 1.00 111.14 ? 4   MAN Y O6  1 
HETATM 8156 C  C1  . MAN G  5  .   ? 20.246  -45.297 52.433 1.00 106.73 ? 5   MAN Y C1  1 
HETATM 8157 C  C2  . MAN G  5  .   ? 21.370  -46.147 51.869 1.00 106.78 ? 5   MAN Y C2  1 
HETATM 8158 C  C3  . MAN G  5  .   ? 22.728  -45.523 52.166 1.00 107.66 ? 5   MAN Y C3  1 
HETATM 8159 C  C4  . MAN G  5  .   ? 22.761  -44.068 51.713 1.00 107.50 ? 5   MAN Y C4  1 
HETATM 8160 C  C5  . MAN G  5  .   ? 21.585  -43.307 52.341 1.00 104.20 ? 5   MAN Y C5  1 
HETATM 8161 C  C6  . MAN G  5  .   ? 21.477  -41.864 51.908 1.00 97.62  ? 5   MAN Y C6  1 
HETATM 8162 O  O2  . MAN G  5  .   ? 21.175  -46.336 50.470 1.00 104.81 ? 5   MAN Y O2  1 
HETATM 8163 O  O3  . MAN G  5  .   ? 23.761  -46.277 51.523 1.00 111.34 ? 5   MAN Y O3  1 
HETATM 8164 O  O4  . MAN G  5  .   ? 23.997  -43.468 52.104 1.00 102.45 ? 5   MAN Y O4  1 
HETATM 8165 O  O5  . MAN G  5  .   ? 20.346  -43.949 51.963 1.00 104.63 ? 5   MAN Y O5  1 
HETATM 8166 O  O6  . MAN G  5  .   ? 20.715  -41.115 52.854 1.00 88.81  ? 5   MAN Y O6  1 
HETATM 8167 C  C1  . MAN G  5  .   ? 12.861  -44.236 52.520 1.00 131.10 ? 6   MAN Y C1  1 
HETATM 8168 C  C2  . MAN G  5  .   ? 12.641  -43.599 51.132 1.00 132.33 ? 6   MAN Y C2  1 
HETATM 8169 C  C3  . MAN G  5  .   ? 11.193  -43.637 50.653 1.00 136.62 ? 6   MAN Y C3  1 
HETATM 8170 C  C4  . MAN G  5  .   ? 10.599  -45.021 50.839 1.00 144.92 ? 6   MAN Y C4  1 
HETATM 8171 C  C5  . MAN G  5  .   ? 10.719  -45.418 52.305 1.00 145.18 ? 6   MAN Y C5  1 
HETATM 8172 C  C6  . MAN G  5  .   ? 10.115  -46.773 52.610 1.00 143.01 ? 6   MAN Y C6  1 
HETATM 8173 O  O2  . MAN G  5  .   ? 13.478  -44.234 50.168 1.00 128.17 ? 6   MAN Y O2  1 
HETATM 8174 O  O3  . MAN G  5  .   ? 11.133  -43.244 49.275 1.00 129.59 ? 6   MAN Y O3  1 
HETATM 8175 O  O4  . MAN G  5  .   ? 9.225   -45.031 50.450 1.00 147.82 ? 6   MAN Y O4  1 
HETATM 8176 O  O5  . MAN G  5  .   ? 12.126  -45.474 52.663 1.00 141.07 ? 6   MAN Y O5  1 
HETATM 8177 O  O6  . MAN G  5  .   ? 9.015   -46.653 53.512 1.00 139.84 ? 6   MAN Y O6  1 
HETATM 8178 C  C1  . NAG H  4  .   ? -15.370 19.032  32.221 1.00 87.83  ? 1   NAG l C1  1 
HETATM 8179 C  C2  . NAG H  4  .   ? -14.913 18.685  33.633 1.00 88.45  ? 1   NAG l C2  1 
HETATM 8180 C  C3  . NAG H  4  .   ? -14.938 19.941  34.498 1.00 87.40  ? 1   NAG l C3  1 
HETATM 8181 C  C4  . NAG H  4  .   ? -14.145 21.086  33.874 1.00 87.34  ? 1   NAG l C4  1 
HETATM 8182 C  C5  . NAG H  4  .   ? -14.426 21.245  32.378 1.00 87.47  ? 1   NAG l C5  1 
HETATM 8183 C  C6  . NAG H  4  .   ? -13.389 22.102  31.681 1.00 80.86  ? 1   NAG l C6  1 
HETATM 8184 C  C7  . NAG H  4  .   ? -16.948 17.492  34.326 1.00 91.99  ? 1   NAG l C7  1 
HETATM 8185 C  C8  . NAG H  4  .   ? -17.479 16.131  34.663 1.00 89.54  ? 1   NAG l C8  1 
HETATM 8186 N  N2  . NAG H  4  .   ? -15.619 17.605  34.293 1.00 88.69  ? 1   NAG l N2  1 
HETATM 8187 O  O3  . NAG H  4  .   ? -14.408 19.590  35.768 1.00 82.54  ? 1   NAG l O3  1 
HETATM 8188 O  O4  . NAG H  4  .   ? -14.531 22.300  34.513 1.00 90.55  ? 1   NAG l O4  1 
HETATM 8189 O  O5  . NAG H  4  .   ? -14.434 19.974  31.693 1.00 89.12  ? 1   NAG l O5  1 
HETATM 8190 O  O6  . NAG H  4  .   ? -12.074 21.557  31.812 1.00 79.20  ? 1   NAG l O6  1 
HETATM 8191 O  O7  . NAG H  4  .   ? -17.688 18.446  34.100 1.00 97.64  ? 1   NAG l O7  1 
HETATM 8192 C  C1  . NAG H  4  .   ? -13.547 23.123  35.025 1.00 95.00  ? 2   NAG l C1  1 
HETATM 8193 C  C2  . NAG H  4  .   ? -13.702 24.627  34.898 1.00 96.63  ? 2   NAG l C2  1 
HETATM 8194 C  C3  . NAG H  4  .   ? -12.383 25.305  35.260 1.00 101.44 ? 2   NAG l C3  1 
HETATM 8195 C  C4  . NAG H  4  .   ? -11.893 24.819  36.620 1.00 103.98 ? 2   NAG l C4  1 
HETATM 8196 C  C5  . NAG H  4  .   ? -11.730 23.305  36.566 1.00 102.97 ? 2   NAG l C5  1 
HETATM 8197 C  C6  . NAG H  4  .   ? -11.219 22.694  37.858 1.00 100.23 ? 2   NAG l C6  1 
HETATM 8198 C  C7  . NAG H  4  .   ? -15.386 25.431  33.278 1.00 98.83  ? 2   NAG l C7  1 
HETATM 8199 C  C8  . NAG H  4  .   ? -15.529 26.581  32.326 1.00 95.08  ? 2   NAG l C8  1 
HETATM 8200 N  N2  . NAG H  4  .   ? -14.134 25.072  33.586 1.00 94.78  ? 2   NAG l N2  1 
HETATM 8201 O  O3  . NAG H  4  .   ? -12.557 26.715  35.235 1.00 103.97 ? 2   NAG l O3  1 
HETATM 8202 O  O4  . NAG H  4  .   ? -10.632 25.412  36.958 1.00 106.54 ? 2   NAG l O4  1 
HETATM 8203 O  O5  . NAG H  4  .   ? -13.021 22.729  36.282 1.00 98.25  ? 2   NAG l O5  1 
HETATM 8204 O  O6  . NAG H  4  .   ? -12.243 22.565  38.842 1.00 95.82  ? 2   NAG l O6  1 
HETATM 8205 O  O7  . NAG H  4  .   ? -16.365 24.848  33.737 1.00 100.80 ? 2   NAG l O7  1 
HETATM 8206 C  C1  . BMA H  4  .   ? -10.645 26.535  37.783 1.00 120.87 ? 3   BMA l C1  1 
HETATM 8207 C  C2  . BMA H  4  .   ? -9.369  26.530  38.619 1.00 126.94 ? 3   BMA l C2  1 
HETATM 8208 C  C3  . BMA H  4  .   ? -9.178  27.853  39.367 1.00 134.54 ? 3   BMA l C3  1 
HETATM 8209 C  C4  . BMA H  4  .   ? -9.374  29.044  38.436 1.00 134.93 ? 3   BMA l C4  1 
HETATM 8210 C  C5  . BMA H  4  .   ? -10.716 28.943  37.719 1.00 128.02 ? 3   BMA l C5  1 
HETATM 8211 C  C6  . BMA H  4  .   ? -10.977 30.070  36.737 1.00 121.23 ? 3   BMA l C6  1 
HETATM 8212 O  O2  . BMA H  4  .   ? -8.253  26.205  37.794 1.00 117.98 ? 3   BMA l O2  1 
HETATM 8213 O  O3  . BMA H  4  .   ? -7.872  27.909  39.949 1.00 137.95 ? 3   BMA l O3  1 
HETATM 8214 O  O4  . BMA H  4  .   ? -9.343  30.262  39.188 1.00 141.85 ? 3   BMA l O4  1 
HETATM 8215 O  O5  . BMA H  4  .   ? -10.735 27.709  36.976 1.00 127.88 ? 3   BMA l O5  1 
HETATM 8216 O  O6  . BMA H  4  .   ? -9.776  30.584  36.163 1.00 117.10 ? 3   BMA l O6  1 
HETATM 8217 C  C1  . MAN H  4  .   ? -7.687  27.404  41.237 1.00 139.80 ? 4   MAN l C1  1 
HETATM 8218 C  C2  . MAN H  4  .   ? -6.520  28.184  41.840 1.00 135.97 ? 4   MAN l C2  1 
HETATM 8219 C  C3  . MAN H  4  .   ? -5.192  27.775  41.203 1.00 132.24 ? 4   MAN l C3  1 
HETATM 8220 C  C4  . MAN H  4  .   ? -5.017  26.264  41.264 1.00 130.84 ? 4   MAN l C4  1 
HETATM 8221 C  C5  . MAN H  4  .   ? -6.199  25.596  40.562 1.00 140.83 ? 4   MAN l C5  1 
HETATM 8222 C  C6  . MAN H  4  .   ? -6.134  24.084  40.578 1.00 141.31 ? 4   MAN l C6  1 
HETATM 8223 O  O2  . MAN H  4  .   ? -6.501  28.033  43.259 1.00 129.54 ? 4   MAN l O2  1 
HETATM 8224 O  O3  . MAN H  4  .   ? -4.111  28.444  41.862 1.00 129.31 ? 4   MAN l O3  1 
HETATM 8225 O  O4  . MAN H  4  .   ? -3.795  25.868  40.642 1.00 112.05 ? 4   MAN l O4  1 
HETATM 8226 O  O5  . MAN H  4  .   ? -7.429  25.986  41.228 1.00 146.93 ? 4   MAN l O5  1 
HETATM 8227 O  O6  . MAN H  4  .   ? -5.746  23.579  41.860 1.00 135.93 ? 4   MAN l O6  1 
HETATM 8228 C  C1  . NAG I  6  .   ? -18.058 27.804  8.212  1.00 89.38  ? 1   NAG n C1  1 
HETATM 8229 C  C2  . NAG I  6  .   ? -17.350 28.471  7.027  1.00 85.64  ? 1   NAG n C2  1 
HETATM 8230 C  C3  . NAG I  6  .   ? -17.542 29.982  7.069  1.00 89.21  ? 1   NAG n C3  1 
HETATM 8231 C  C4  . NAG I  6  .   ? -19.023 30.322  7.173  1.00 92.73  ? 1   NAG n C4  1 
HETATM 8232 C  C5  . NAG I  6  .   ? -19.617 29.630  8.397  1.00 96.48  ? 1   NAG n C5  1 
HETATM 8233 C  C6  . NAG I  6  .   ? -21.108 29.851  8.546  1.00 97.00  ? 1   NAG n C6  1 
HETATM 8234 C  C7  . NAG I  6  .   ? -15.447 27.261  6.095  1.00 84.96  ? 1   NAG n C7  1 
HETATM 8235 C  C8  . NAG I  6  .   ? -13.964 27.286  5.885  1.00 84.18  ? 1   NAG n C8  1 
HETATM 8236 N  N2  . NAG I  6  .   ? -15.941 28.145  6.963  1.00 85.98  ? 1   NAG n N2  1 
HETATM 8237 O  O3  . NAG I  6  .   ? -16.951 30.541  5.903  1.00 85.14  ? 1   NAG n O3  1 
HETATM 8238 O  O4  . NAG I  6  .   ? -19.177 31.742  7.303  1.00 99.42  ? 1   NAG n O4  1 
HETATM 8239 O  O5  . NAG I  6  .   ? -19.421 28.204  8.290  1.00 93.52  ? 1   NAG n O5  1 
HETATM 8240 O  O6  . NAG I  6  .   ? -21.840 29.210  7.503  1.00 96.39  ? 1   NAG n O6  1 
HETATM 8241 O  O7  . NAG I  6  .   ? -16.173 26.468  5.505  1.00 79.50  ? 1   NAG n O7  1 
HETATM 8242 C  C1  . NAG I  6  .   ? -19.447 32.511  6.171  1.00 106.65 ? 2   NAG n C1  1 
HETATM 8243 C  C2  . NAG I  6  .   ? -20.099 33.820  6.609  1.00 102.71 ? 2   NAG n C2  1 
HETATM 8244 C  C3  . NAG I  6  .   ? -20.284 34.736  5.402  1.00 100.03 ? 2   NAG n C3  1 
HETATM 8245 C  C4  . NAG I  6  .   ? -18.955 34.938  4.684  1.00 106.06 ? 2   NAG n C4  1 
HETATM 8246 C  C5  . NAG I  6  .   ? -18.411 33.571  4.273  1.00 109.04 ? 2   NAG n C5  1 
HETATM 8247 C  C6  . NAG I  6  .   ? -17.068 33.628  3.571  1.00 105.55 ? 2   NAG n C6  1 
HETATM 8248 C  C7  . NAG I  6  .   ? -21.471 33.636  8.642  1.00 104.43 ? 2   NAG n C7  1 
HETATM 8249 C  C8  . NAG I  6  .   ? -22.868 33.633  9.193  1.00 93.88  ? 2   NAG n C8  1 
HETATM 8250 N  N2  . NAG I  6  .   ? -21.355 33.617  7.307  1.00 103.13 ? 2   NAG n N2  1 
HETATM 8251 O  O3  . NAG I  6  .   ? -20.833 35.980  5.811  1.00 92.17  ? 2   NAG n O3  1 
HETATM 8252 O  O4  . NAG I  6  .   ? -19.147 35.764  3.537  1.00 102.53 ? 2   NAG n O4  1 
HETATM 8253 O  O5  . NAG I  6  .   ? -18.234 32.770  5.461  1.00 110.68 ? 2   NAG n O5  1 
HETATM 8254 O  O6  . NAG I  6  .   ? -15.993 33.842  4.491  1.00 101.57 ? 2   NAG n O6  1 
HETATM 8255 O  O7  . NAG I  6  .   ? -20.484 33.652  9.376  1.00 101.61 ? 2   NAG n O7  1 
HETATM 8256 O  O1  . DAO J  7  .   ? 44.270  -0.003  33.385 1.00 76.62  ? 401 DAO A O1  1 
HETATM 8257 O  O2  . DAO J  7  .   ? 44.531  -1.901  34.489 1.00 79.80  ? 401 DAO A O2  1 
HETATM 8258 C  C1  . DAO J  7  .   ? 44.814  -1.115  33.555 1.00 79.25  ? 401 DAO A C1  1 
HETATM 8259 C  C2  . DAO J  7  .   ? 45.885  -1.536  32.566 1.00 77.13  ? 401 DAO A C2  1 
HETATM 8260 C  C3  . DAO J  7  .   ? 47.201  -0.855  32.756 1.00 76.16  ? 401 DAO A C3  1 
HETATM 8261 C  C4  . DAO J  7  .   ? 48.228  -1.344  31.757 1.00 74.99  ? 401 DAO A C4  1 
HETATM 8262 C  C5  . DAO J  7  .   ? 49.530  -0.555  31.706 1.00 76.25  ? 401 DAO A C5  1 
HETATM 8263 C  C6  . DAO J  7  .   ? 50.265  -0.631  30.369 1.00 76.00  ? 401 DAO A C6  1 
HETATM 8264 C  C7  . DAO J  7  .   ? 49.543  -1.451  29.315 1.00 72.82  ? 401 DAO A C7  1 
HETATM 8265 C  C8  . DAO J  7  .   ? 50.426  -2.151  28.326 1.00 75.08  ? 401 DAO A C8  1 
HETATM 8266 C  C9  . DAO J  7  .   ? 49.663  -3.075  27.405 1.00 72.00  ? 401 DAO A C9  1 
HETATM 8267 C  C10 . DAO J  7  .   ? 50.487  -3.724  26.323 1.00 71.04  ? 401 DAO A C10 1 
HETATM 8268 C  C11 . DAO J  7  .   ? 49.721  -3.905  25.029 1.00 71.74  ? 401 DAO A C11 1 
HETATM 8269 C  C12 . DAO J  7  .   ? 50.331  -4.904  24.075 1.00 70.79  ? 401 DAO A C12 1 
HETATM 8270 N  N1  . EPE K  8  .   ? 61.110  3.040   19.443 1.00 94.83  ? 402 EPE A N1  1 
HETATM 8271 C  C2  . EPE K  8  .   ? 60.542  3.237   18.092 1.00 87.46  ? 402 EPE A C2  1 
HETATM 8272 C  C3  . EPE K  8  .   ? 61.333  4.241   17.296 1.00 81.21  ? 402 EPE A C3  1 
HETATM 8273 N  N4  . EPE K  8  .   ? 61.305  5.537   17.976 1.00 76.19  ? 402 EPE A N4  1 
HETATM 8274 C  C5  . EPE K  8  .   ? 61.969  5.373   19.276 1.00 81.99  ? 402 EPE A C5  1 
HETATM 8275 C  C6  . EPE K  8  .   ? 61.246  4.348   20.126 1.00 89.45  ? 402 EPE A C6  1 
HETATM 8276 C  C7  . EPE K  8  .   ? 61.919  6.583   17.146 1.00 82.49  ? 402 EPE A C7  1 
HETATM 8277 C  C8  . EPE K  8  .   ? 61.400  6.642   15.711 1.00 83.29  ? 402 EPE A C8  1 
HETATM 8278 O  O8  . EPE K  8  .   ? 61.307  7.969   15.227 1.00 77.65  ? 402 EPE A O8  1 
HETATM 8279 C  C9  . EPE K  8  .   ? 60.299  2.063   20.227 1.00 84.50  ? 402 EPE A C9  1 
HETATM 8280 C  C10 . EPE K  8  .   ? 59.711  0.969   19.331 1.00 85.90  ? 402 EPE A C10 1 
HETATM 8281 S  S   . EPE K  8  .   ? 59.460  -0.623  20.074 1.00 89.31  ? 402 EPE A S   1 
HETATM 8282 O  O1S . EPE K  8  .   ? 59.030  -1.501  19.012 1.00 90.94  ? 402 EPE A O1S 1 
HETATM 8283 O  O2S . EPE K  8  .   ? 58.565  -0.433  21.184 1.00 77.79  ? 402 EPE A O2S 1 
HETATM 8284 O  O3S . EPE K  8  .   ? 60.936  -0.952  20.544 1.00 73.40  ? 402 EPE A O3S 1 
HETATM 8285 C  C1  . GOL L  9  .   ? 41.708  -6.075  55.793 1.00 65.97  ? 403 GOL A C1  1 
HETATM 8286 O  O1  . GOL L  9  .   ? 40.544  -6.014  54.976 1.00 64.44  ? 403 GOL A O1  1 
HETATM 8287 C  C2  . GOL L  9  .   ? 42.339  -4.709  55.921 1.00 66.64  ? 403 GOL A C2  1 
HETATM 8288 O  O2  . GOL L  9  .   ? 43.502  -4.775  56.747 1.00 69.94  ? 403 GOL A O2  1 
HETATM 8289 C  C3  . GOL L  9  .   ? 41.386  -3.659  56.448 1.00 61.54  ? 403 GOL A C3  1 
HETATM 8290 O  O3  . GOL L  9  .   ? 41.704  -2.381  55.900 1.00 57.92  ? 403 GOL A O3  1 
HETATM 8291 C  C1  . GOL M  9  .   ? 31.915  3.218   59.698 1.00 64.68  ? 404 GOL A C1  1 
HETATM 8292 O  O1  . GOL M  9  .   ? 31.939  4.411   58.921 1.00 64.95  ? 404 GOL A O1  1 
HETATM 8293 C  C2  . GOL M  9  .   ? 33.297  2.870   60.208 1.00 65.77  ? 404 GOL A C2  1 
HETATM 8294 O  O2  . GOL M  9  .   ? 33.825  3.958   60.965 1.00 74.32  ? 404 GOL A O2  1 
HETATM 8295 C  C3  . GOL M  9  .   ? 33.328  1.598   61.033 1.00 71.37  ? 404 GOL A C3  1 
HETATM 8296 O  O3  . GOL M  9  .   ? 34.629  1.344   61.565 1.00 70.01  ? 404 GOL A O3  1 
HETATM 8297 C  CHA . HEM N  10 .   ? 40.668  1.472   34.978 1.00 33.24  ? 405 HEM A CHA 1 
HETATM 8298 C  CHB . HEM N  10 .   ? 44.729  0.768   37.435 1.00 30.47  ? 405 HEM A CHB 1 
HETATM 8299 C  CHC . HEM N  10 .   ? 43.981  -4.067  37.406 1.00 32.64  ? 405 HEM A CHC 1 
HETATM 8300 C  CHD . HEM N  10 .   ? 39.818  -3.293  35.066 1.00 31.50  ? 405 HEM A CHD 1 
HETATM 8301 C  C1A . HEM N  10 .   ? 41.846  1.663   35.659 1.00 32.52  ? 405 HEM A C1A 1 
HETATM 8302 C  C2A . HEM N  10 .   ? 42.414  2.933   35.902 1.00 35.97  ? 405 HEM A C2A 1 
HETATM 8303 C  C3A . HEM N  10 .   ? 43.571  2.758   36.585 1.00 38.16  ? 405 HEM A C3A 1 
HETATM 8304 C  C4A . HEM N  10 .   ? 43.702  1.364   36.792 1.00 34.81  ? 405 HEM A C4A 1 
HETATM 8305 C  CMA . HEM N  10 .   ? 44.543  3.831   37.047 1.00 38.93  ? 405 HEM A CMA 1 
HETATM 8306 C  CAA . HEM N  10 .   ? 41.846  4.242   35.438 1.00 36.47  ? 405 HEM A CAA 1 
HETATM 8307 C  CBA . HEM N  10 .   ? 42.451  4.491   34.082 1.00 41.40  ? 405 HEM A CBA 1 
HETATM 8308 C  CGA . HEM N  10 .   ? 42.094  5.842   33.500 1.00 46.60  ? 405 HEM A CGA 1 
HETATM 8309 O  O1A . HEM N  10 .   ? 41.192  6.603   33.933 1.00 38.94  ? 405 HEM A O1A 1 
HETATM 8310 O  O2A . HEM N  10 .   ? 42.793  6.198   32.518 1.00 52.38  ? 405 HEM A O2A 1 
HETATM 8311 C  C1B . HEM N  10 .   ? 44.844  -0.613  37.584 1.00 33.23  ? 405 HEM A C1B 1 
HETATM 8312 C  C2B . HEM N  10 .   ? 46.001  -1.213  38.211 1.00 33.43  ? 405 HEM A C2B 1 
HETATM 8313 C  C3B . HEM N  10 .   ? 45.814  -2.561  38.235 1.00 33.39  ? 405 HEM A C3B 1 
HETATM 8314 C  C4B . HEM N  10 .   ? 44.513  -2.792  37.572 1.00 33.14  ? 405 HEM A C4B 1 
HETATM 8315 C  CMB . HEM N  10 .   ? 47.204  -0.530  38.795 1.00 33.92  ? 405 HEM A CMB 1 
HETATM 8316 C  CAB . HEM N  10 .   ? 46.818  -3.508  38.725 1.00 37.24  ? 405 HEM A CAB 1 
HETATM 8317 C  CBB . HEM N  10 .   ? 46.867  -4.761  38.297 1.00 42.05  ? 405 HEM A CBB 1 
HETATM 8318 C  C1C . HEM N  10 .   ? 42.749  -4.288  36.801 1.00 34.05  ? 405 HEM A C1C 1 
HETATM 8319 C  C2C . HEM N  10 .   ? 42.097  -5.515  36.703 1.00 33.15  ? 405 HEM A C2C 1 
HETATM 8320 C  C3C . HEM N  10 .   ? 40.908  -5.256  36.023 1.00 36.47  ? 405 HEM A C3C 1 
HETATM 8321 C  C4C . HEM N  10 .   ? 40.850  -3.880  35.739 1.00 33.70  ? 405 HEM A C4C 1 
HETATM 8322 C  CMC . HEM N  10 .   ? 42.596  -6.844  37.226 1.00 32.78  ? 405 HEM A CMC 1 
HETATM 8323 C  CAC . HEM N  10 .   ? 39.792  -6.143  35.679 1.00 39.31  ? 405 HEM A CAC 1 
HETATM 8324 C  CBC . HEM N  10 .   ? 39.640  -7.311  36.288 1.00 45.06  ? 405 HEM A CBC 1 
HETATM 8325 C  C1D . HEM N  10 .   ? 39.765  -1.923  34.834 1.00 32.99  ? 405 HEM A C1D 1 
HETATM 8326 C  C2D . HEM N  10 .   ? 38.704  -1.320  33.992 1.00 32.71  ? 405 HEM A C2D 1 
HETATM 8327 C  C3D . HEM N  10 .   ? 38.940  0.001   33.984 1.00 34.33  ? 405 HEM A C3D 1 
HETATM 8328 C  C4D . HEM N  10 .   ? 40.149  0.195   34.790 1.00 36.09  ? 405 HEM A C4D 1 
HETATM 8329 C  CMD . HEM N  10 .   ? 37.549  -2.007  33.295 1.00 32.93  ? 405 HEM A CMD 1 
HETATM 8330 C  CAD . HEM N  10 .   ? 38.153  1.073   33.253 1.00 35.14  ? 405 HEM A CAD 1 
HETATM 8331 C  CBD . HEM N  10 .   ? 36.998  1.677   34.029 1.00 35.18  ? 405 HEM A CBD 1 
HETATM 8332 C  CGD . HEM N  10 .   ? 36.219  2.652   33.165 1.00 34.94  ? 405 HEM A CGD 1 
HETATM 8333 O  O1D . HEM N  10 .   ? 36.694  3.159   32.118 1.00 35.89  ? 405 HEM A O1D 1 
HETATM 8334 O  O2D . HEM N  10 .   ? 35.042  2.944   33.486 1.00 38.40  ? 405 HEM A O2D 1 
HETATM 8335 N  NA  . HEM N  10 .   ? 42.623  0.714   36.251 1.00 35.37  ? 405 HEM A NA  1 
HETATM 8336 N  NB  . HEM N  10 .   ? 44.004  -1.569  37.225 1.00 30.18  ? 405 HEM A NB  1 
HETATM 8337 N  NC  . HEM N  10 .   ? 41.989  -3.315  36.217 1.00 32.19  ? 405 HEM A NC  1 
HETATM 8338 N  ND  . HEM N  10 .   ? 40.598  -0.983  35.301 1.00 32.32  ? 405 HEM A ND  1 
HETATM 8339 FE FE  . HEM N  10 .   ? 42.159  -1.228  36.355 1.00 33.95  ? 405 HEM A FE  1 
HETATM 8340 S  S   . SO4 O  11 .   ? 29.045  1.207   50.018 1.00 71.33  ? 406 SO4 A S   1 
HETATM 8341 O  O1  . SO4 O  11 .   ? 29.954  0.421   49.178 1.00 52.49  ? 406 SO4 A O1  1 
HETATM 8342 O  O2  . SO4 O  11 .   ? 28.722  2.436   49.325 1.00 84.54  ? 406 SO4 A O2  1 
HETATM 8343 O  O3  . SO4 O  11 .   ? 27.825  0.477   50.282 1.00 70.07  ? 406 SO4 A O3  1 
HETATM 8344 O  O4  . SO4 O  11 .   ? 29.665  1.515   51.282 1.00 63.07  ? 406 SO4 A O4  1 
HETATM 8345 S  S   . SO4 P  11 .   ? 26.173  8.475   19.057 1.00 84.73  ? 407 SO4 A S   1 
HETATM 8346 O  O1  . SO4 P  11 .   ? 27.401  8.156   18.354 1.00 71.48  ? 407 SO4 A O1  1 
HETATM 8347 O  O2  . SO4 P  11 .   ? 25.055  8.555   18.143 1.00 78.79  ? 407 SO4 A O2  1 
HETATM 8348 O  O3  . SO4 P  11 .   ? 25.912  7.451   20.037 1.00 90.61  ? 407 SO4 A O3  1 
HETATM 8349 O  O4  . SO4 P  11 .   ? 26.315  9.736   19.732 1.00 89.78  ? 407 SO4 A O4  1 
HETATM 8350 MG MG  . MG  Q  12 .   ? 39.913  8.295   33.682 1.00 41.63  ? 408 MG  A MG  1 
HETATM 8351 O  O1  . DAO R  7  .   ? 6.948   -9.503  61.243 1.00 86.19  ? 401 DAO B O1  1 
HETATM 8352 O  O2  . DAO R  7  .   ? 6.241   -9.483  59.162 1.00 82.23  ? 401 DAO B O2  1 
HETATM 8353 C  C1  . DAO R  7  .   ? 6.186   -9.902  60.344 1.00 85.97  ? 401 DAO B C1  1 
HETATM 8354 C  C2  . DAO R  7  .   ? 5.158   -10.964 60.712 1.00 86.29  ? 401 DAO B C2  1 
HETATM 8355 C  C3  . DAO R  7  .   ? 3.840   -10.898 59.979 1.00 87.41  ? 401 DAO B C3  1 
HETATM 8356 C  C4  . DAO R  7  .   ? 2.675   -10.466 60.867 1.00 88.74  ? 401 DAO B C4  1 
HETATM 8357 C  C5  . DAO R  7  .   ? 1.549   -11.468 60.940 1.00 91.88  ? 401 DAO B C5  1 
HETATM 8358 C  C6  . DAO R  7  .   ? 0.943   -11.647 62.318 1.00 86.57  ? 401 DAO B C6  1 
HETATM 8359 C  C7  . DAO R  7  .   ? -0.031  -12.807 62.438 1.00 82.89  ? 401 DAO B C7  1 
HETATM 8360 C  C8  . DAO R  7  .   ? 0.133   -13.909 61.403 1.00 78.27  ? 401 DAO B C8  1 
HETATM 8361 C  C9  . DAO R  7  .   ? -1.146  -14.601 61.005 1.00 73.73  ? 401 DAO B C9  1 
HETATM 8362 C  C10 . DAO R  7  .   ? -1.360  -15.944 61.674 1.00 74.03  ? 401 DAO B C10 1 
HETATM 8363 C  C11 . DAO R  7  .   ? -2.242  -16.939 60.936 1.00 74.43  ? 401 DAO B C11 1 
HETATM 8364 C  C12 . DAO R  7  .   ? -2.685  -16.541 59.535 1.00 72.03  ? 401 DAO B C12 1 
HETATM 8365 N  N1  . EPE S  8  .   ? -10.114 -16.825 71.078 1.00 79.44  ? 402 EPE B N1  1 
HETATM 8366 C  C2  . EPE S  8  .   ? -11.356 -17.263 70.414 1.00 82.79  ? 402 EPE B C2  1 
HETATM 8367 C  C3  . EPE S  8  .   ? -11.070 -17.780 69.023 1.00 81.21  ? 402 EPE B C3  1 
HETATM 8368 N  N4  . EPE S  8  .   ? -10.514 -16.718 68.172 1.00 79.28  ? 402 EPE B N4  1 
HETATM 8369 C  C5  . EPE S  8  .   ? -10.286 -15.526 69.013 1.00 81.62  ? 402 EPE B C5  1 
HETATM 8370 C  C6  . EPE S  8  .   ? -9.462  -15.812 70.246 1.00 78.57  ? 402 EPE B C6  1 
HETATM 8371 C  C7  . EPE S  8  .   ? -9.282  -17.094 67.459 1.00 74.98  ? 402 EPE B C7  1 
HETATM 8372 C  C8  . EPE S  8  .   ? -9.276  -18.405 66.685 1.00 75.96  ? 402 EPE B C8  1 
HETATM 8373 O  O8  . EPE S  8  .   ? -7.954  -18.793 66.320 1.00 61.61  ? 402 EPE B O8  1 
HETATM 8374 C  C9  . EPE S  8  .   ? -10.357 -16.326 72.441 1.00 86.87  ? 402 EPE B C9  1 
HETATM 8375 C  C10 . EPE S  8  .   ? -10.790 -17.437 73.388 1.00 89.01  ? 402 EPE B C10 1 
HETATM 8376 S  S   . EPE S  8  .   ? -11.058 -16.874 75.046 1.00 88.33  ? 402 EPE B S   1 
HETATM 8377 O  O1S . EPE S  8  .   ? -11.030 -18.050 75.877 1.00 87.13  ? 402 EPE B O1S 1 
HETATM 8378 O  O2S . EPE S  8  .   ? -12.258 -16.076 75.008 1.00 85.98  ? 402 EPE B O2S 1 
HETATM 8379 O  O3S . EPE S  8  .   ? -9.836  -15.948 75.358 1.00 76.08  ? 402 EPE B O3S 1 
HETATM 8380 C  C1  . GOL T  9  .   ? 13.502  7.411   47.032 1.00 63.86  ? 403 GOL B C1  1 
HETATM 8381 O  O1  . GOL T  9  .   ? 12.414  6.568   46.655 1.00 66.91  ? 403 GOL B O1  1 
HETATM 8382 C  C2  . GOL T  9  .   ? 13.044  8.526   47.950 1.00 69.25  ? 403 GOL B C2  1 
HETATM 8383 O  O2  . GOL T  9  .   ? 11.651  8.769   47.738 1.00 76.41  ? 403 GOL B O2  1 
HETATM 8384 C  C3  . GOL T  9  .   ? 13.290  8.258   49.423 1.00 65.83  ? 403 GOL B C3  1 
HETATM 8385 O  O3  . GOL T  9  .   ? 14.274  9.133   49.966 1.00 71.47  ? 403 GOL B O3  1 
HETATM 8386 C  CHA . HEM U  10 .   ? 11.044  -9.361  61.155 1.00 37.90  ? 404 HEM B CHA 1 
HETATM 8387 C  CHB . HEM U  10 .   ? 7.794   -5.896  60.439 1.00 37.91  ? 404 HEM B CHB 1 
HETATM 8388 C  CHC . HEM U  10 .   ? 6.924   -7.678  55.995 1.00 35.87  ? 404 HEM B CHC 1 
HETATM 8389 C  CHD . HEM U  10 .   ? 10.430  -10.916 56.653 1.00 39.28  ? 404 HEM B CHD 1 
HETATM 8390 C  C1A . HEM U  10 .   ? 10.223  -8.274  61.303 1.00 38.64  ? 404 HEM B C1A 1 
HETATM 8391 C  C2A . HEM U  10 .   ? 10.183  -7.492  62.479 1.00 38.92  ? 404 HEM B C2A 1 
HETATM 8392 C  C3A . HEM U  10 .   ? 9.263   -6.516  62.286 1.00 38.96  ? 404 HEM B C3A 1 
HETATM 8393 C  C4A . HEM U  10 .   ? 8.750   -6.690  60.993 1.00 37.33  ? 404 HEM B C4A 1 
HETATM 8394 C  CMA . HEM U  10 .   ? 8.881   -5.446  63.276 1.00 38.97  ? 404 HEM B CMA 1 
HETATM 8395 C  CAA . HEM U  10 .   ? 11.002  -7.718  63.728 1.00 41.79  ? 404 HEM B CAA 1 
HETATM 8396 C  CBA . HEM U  10 .   ? 10.413  -8.904  64.479 1.00 46.36  ? 404 HEM B CBA 1 
HETATM 8397 C  CGA . HEM U  10 .   ? 10.929  -9.031  65.893 1.00 50.87  ? 404 HEM B CGA 1 
HETATM 8398 O  O1A . HEM U  10 .   ? 10.088  -9.428  66.740 1.00 56.80  ? 404 HEM B O1A 1 
HETATM 8399 O  O2A . HEM U  10 .   ? 12.112  -8.781  66.265 1.00 50.05  ? 404 HEM B O2A 1 
HETATM 8400 C  C1B . HEM U  10 .   ? 7.261   -6.137  59.176 1.00 38.24  ? 404 HEM B C1B 1 
HETATM 8401 C  C2B . HEM U  10 .   ? 6.189   -5.373  58.688 1.00 35.17  ? 404 HEM B C2B 1 
HETATM 8402 C  C3B . HEM U  10 .   ? 5.933   -5.826  57.441 1.00 37.58  ? 404 HEM B C3B 1 
HETATM 8403 C  C4B . HEM U  10 .   ? 6.870   -6.945  57.181 1.00 35.94  ? 404 HEM B C4B 1 
HETATM 8404 C  CMB . HEM U  10 .   ? 5.459   -4.230  59.356 1.00 39.93  ? 404 HEM B CMB 1 
HETATM 8405 C  CAB . HEM U  10 .   ? 4.807   -5.316  56.629 1.00 36.67  ? 404 HEM B CAB 1 
HETATM 8406 C  CBB . HEM U  10 .   ? 4.266   -6.044  55.685 1.00 40.26  ? 404 HEM B CBB 1 
HETATM 8407 C  C1C . HEM U  10 .   ? 7.816   -8.691  55.741 1.00 37.95  ? 404 HEM B C1C 1 
HETATM 8408 C  C2C . HEM U  10 .   ? 7.970   -9.383  54.535 1.00 40.24  ? 404 HEM B C2C 1 
HETATM 8409 C  C3C . HEM U  10 .   ? 8.979   -10.326 54.750 1.00 40.75  ? 404 HEM B C3C 1 
HETATM 8410 C  C4C . HEM U  10 .   ? 9.441   -10.156 56.080 1.00 39.80  ? 404 HEM B C4C 1 
HETATM 8411 C  CMC . HEM U  10 .   ? 7.157   -9.151  53.287 1.00 42.17  ? 404 HEM B CMC 1 
HETATM 8412 C  CAC . HEM U  10 .   ? 9.622   -11.270 53.822 1.00 40.87  ? 404 HEM B CAC 1 
HETATM 8413 C  CBC . HEM U  10 .   ? 9.613   -11.043 52.521 1.00 43.32  ? 404 HEM B CBC 1 
HETATM 8414 C  C1D . HEM U  10 .   ? 10.832  -10.746 57.966 1.00 37.36  ? 404 HEM B C1D 1 
HETATM 8415 C  C2D . HEM U  10 .   ? 11.781  -11.669 58.583 1.00 35.71  ? 404 HEM B C2D 1 
HETATM 8416 C  C3D . HEM U  10 .   ? 11.948  -11.230 59.827 1.00 34.11  ? 404 HEM B C3D 1 
HETATM 8417 C  C4D . HEM U  10 .   ? 11.098  -10.050 59.960 1.00 37.71  ? 404 HEM B C4D 1 
HETATM 8418 C  CMD . HEM U  10 .   ? 12.472  -12.870 57.967 1.00 34.05  ? 404 HEM B CMD 1 
HETATM 8419 C  CAD . HEM U  10 .   ? 12.841  -11.862 60.864 1.00 35.52  ? 404 HEM B CAD 1 
HETATM 8420 C  CBD . HEM U  10 .   ? 14.228  -11.233 60.923 1.00 34.48  ? 404 HEM B CBD 1 
HETATM 8421 C  CGD . HEM U  10 .   ? 15.107  -12.091 61.788 1.00 36.45  ? 404 HEM B CGD 1 
HETATM 8422 O  O1D . HEM U  10 .   ? 16.330  -12.182 61.533 1.00 39.60  ? 404 HEM B O1D 1 
HETATM 8423 O  O2D . HEM U  10 .   ? 14.648  -12.709 62.777 1.00 39.08  ? 404 HEM B O2D 1 
HETATM 8424 N  NA  . HEM U  10 .   ? 9.348   -7.754  60.381 1.00 35.92  ? 404 HEM B NA  1 
HETATM 8425 N  NB  . HEM U  10 .   ? 7.634   -7.044  58.263 1.00 37.30  ? 404 HEM B NB  1 
HETATM 8426 N  NC  . HEM U  10 .   ? 8.713   -9.166  56.651 1.00 37.71  ? 404 HEM B NC  1 
HETATM 8427 N  ND  . HEM U  10 .   ? 10.445  -9.784  58.814 1.00 38.36  ? 404 HEM B ND  1 
HETATM 8428 FE FE  . HEM U  10 .   ? 9.200   -8.379  58.493 1.00 35.79  ? 404 HEM B FE  1 
HETATM 8429 S  S   . SO4 V  11 .   ? 22.932  -26.324 70.072 1.00 81.69  ? 405 SO4 B S   1 
HETATM 8430 O  O1  . SO4 V  11 .   ? 23.491  -25.433 69.078 1.00 75.97  ? 405 SO4 B O1  1 
HETATM 8431 O  O2  . SO4 V  11 .   ? 22.034  -27.277 69.455 1.00 70.37  ? 405 SO4 B O2  1 
HETATM 8432 O  O3  . SO4 V  11 .   ? 24.026  -27.020 70.722 1.00 71.58  ? 405 SO4 B O3  1 
HETATM 8433 O  O4  . SO4 V  11 .   ? 22.185  -25.547 71.035 1.00 75.98  ? 405 SO4 B O4  1 
HETATM 8434 MG MG  . MG  W  12 .   ? 14.336  -8.974  67.990 1.00 64.75  ? 406 MG  B MG  1 
HETATM 8435 N  N1  . EPE X  8  .   ? 14.218  18.032  11.683 1.00 78.51  ? 401 EPE C N1  1 
HETATM 8436 C  C2  . EPE X  8  .   ? 12.782  17.896  11.954 1.00 73.80  ? 401 EPE C C2  1 
HETATM 8437 C  C3  . EPE X  8  .   ? 12.044  17.219  10.821 1.00 74.61  ? 401 EPE C C3  1 
HETATM 8438 N  N4  . EPE X  8  .   ? 12.220  17.914  9.544  1.00 77.46  ? 401 EPE C N4  1 
HETATM 8439 C  C5  . EPE X  8  .   ? 13.665  17.931  9.262  1.00 80.89  ? 401 EPE C C5  1 
HETATM 8440 C  C6  . EPE X  8  .   ? 14.407  18.666  10.358 1.00 85.26  ? 401 EPE C C6  1 
HETATM 8441 C  C7  . EPE X  8  .   ? 11.456  17.246  8.478  1.00 79.12  ? 401 EPE C C7  1 
HETATM 8442 C  C8  . EPE X  8  .   ? 9.933   17.314  8.601  1.00 78.47  ? 401 EPE C C8  1 
HETATM 8443 O  O8  . EPE X  8  .   ? 9.426   18.601  8.934  1.00 68.53  ? 401 EPE C O8  1 
HETATM 8444 C  C9  . EPE X  8  .   ? 14.821  18.836  12.758 1.00 87.32  ? 401 EPE C C9  1 
HETATM 8445 C  C10 . EPE X  8  .   ? 16.286  19.212  12.588 1.00 88.51  ? 401 EPE C C10 1 
HETATM 8446 S  S   . EPE X  8  .   ? 16.953  19.781  14.133 1.00 91.74  ? 401 EPE C S   1 
HETATM 8447 O  O1S . EPE X  8  .   ? 18.382  19.844  13.971 1.00 81.37  ? 401 EPE C O1S 1 
HETATM 8448 O  O2S . EPE X  8  .   ? 16.424  18.925  15.165 1.00 86.42  ? 401 EPE C O2S 1 
HETATM 8449 O  O3S . EPE X  8  .   ? 16.317  21.212  14.247 1.00 84.30  ? 401 EPE C O3S 1 
HETATM 8450 C  CHA . HEM Y  10 .   ? -8.163  11.501  20.069 1.00 45.10  ? 402 HEM C CHA 1 
HETATM 8451 C  CHB . HEM Y  10 .   ? -5.421  7.561   19.473 1.00 45.13  ? 402 HEM C CHB 1 
HETATM 8452 C  CHC . HEM Y  10 .   ? -7.482  6.911   15.083 1.00 39.57  ? 402 HEM C CHC 1 
HETATM 8453 C  CHD . HEM Y  10 .   ? -10.386 10.674  15.861 1.00 44.99  ? 402 HEM C CHD 1 
HETATM 8454 C  C1A . HEM Y  10 .   ? -7.270  10.487  20.264 1.00 43.75  ? 402 HEM C C1A 1 
HETATM 8455 C  C2A . HEM Y  10 .   ? -6.489  10.345  21.416 1.00 48.12  ? 402 HEM C C2A 1 
HETATM 8456 C  C3A . HEM Y  10 .   ? -5.711  9.244   21.249 1.00 43.88  ? 402 HEM C C3A 1 
HETATM 8457 C  C4A . HEM Y  10 .   ? -6.009  8.694   20.002 1.00 43.84  ? 402 HEM C C4A 1 
HETATM 8458 C  CMA . HEM Y  10 .   ? -4.728  8.690   22.241 1.00 43.20  ? 402 HEM C CMA 1 
HETATM 8459 C  CAA . HEM Y  10 .   ? -6.493  11.235  22.639 1.00 52.34  ? 402 HEM C CAA 1 
HETATM 8460 C  CBA . HEM Y  10 .   ? -5.525  12.375  22.365 1.00 59.83  ? 402 HEM C CBA 1 
HETATM 8461 C  CGA . HEM Y  10 .   ? -5.458  13.381  23.501 1.00 65.72  ? 402 HEM C CGA 1 
HETATM 8462 O  O1A . HEM Y  10 .   ? -4.396  14.050  23.638 1.00 64.04  ? 402 HEM C O1A 1 
HETATM 8463 O  O2A . HEM Y  10 .   ? -6.414  13.567  24.296 1.00 67.56  ? 402 HEM C O2A 1 
HETATM 8464 C  C1B . HEM Y  10 .   ? -5.747  7.078   18.192 1.00 43.73  ? 402 HEM C C1B 1 
HETATM 8465 C  C2B . HEM Y  10 .   ? -5.066  5.981   17.629 1.00 40.90  ? 402 HEM C C2B 1 
HETATM 8466 C  C3B . HEM Y  10 .   ? -5.616  5.772   16.408 1.00 42.91  ? 402 HEM C C3B 1 
HETATM 8467 C  C4B . HEM Y  10 .   ? -6.676  6.803   16.221 1.00 43.08  ? 402 HEM C C4B 1 
HETATM 8468 C  CMB . HEM Y  10 .   ? -3.942  5.155   18.244 1.00 40.83  ? 402 HEM C CMB 1 
HETATM 8469 C  CAB . HEM Y  10 .   ? -5.111  4.742   15.487 1.00 43.92  ? 402 HEM C CAB 1 
HETATM 8470 C  CBB . HEM Y  10 .   ? -5.323  4.833   14.181 1.00 48.40  ? 402 HEM C CBB 1 
HETATM 8471 C  C1C . HEM Y  10 .   ? -8.473  7.851   14.908 1.00 42.61  ? 402 HEM C C1C 1 
HETATM 8472 C  C2C . HEM Y  10 .   ? -9.407  7.887   13.834 1.00 44.32  ? 402 HEM C C2C 1 
HETATM 8473 C  C3C . HEM Y  10 .   ? -10.225 8.988   14.079 1.00 42.07  ? 402 HEM C C3C 1 
HETATM 8474 C  C4C . HEM Y  10 .   ? -9.799  9.568   15.306 1.00 42.76  ? 402 HEM C C4C 1 
HETATM 8475 C  CMC . HEM Y  10 .   ? -9.491  6.940   12.642 1.00 42.13  ? 402 HEM C CMC 1 
HETATM 8476 C  CAC . HEM Y  10 .   ? -11.391 9.481   13.314 1.00 43.57  ? 402 HEM C CAC 1 
HETATM 8477 C  CBC . HEM Y  10 .   ? -11.997 8.764   12.390 1.00 45.18  ? 402 HEM C CBC 1 
HETATM 8478 C  C1D . HEM Y  10 .   ? -9.965  11.189  17.081 1.00 45.06  ? 402 HEM C C1D 1 
HETATM 8479 C  C2D . HEM Y  10 .   ? -10.516 12.445  17.599 1.00 44.95  ? 402 HEM C C2D 1 
HETATM 8480 C  C3D . HEM Y  10 .   ? -9.905  12.677  18.763 1.00 48.68  ? 402 HEM C C3D 1 
HETATM 8481 C  C4D . HEM Y  10 .   ? -8.965  11.569  18.947 1.00 45.51  ? 402 HEM C C4D 1 
HETATM 8482 C  CMD . HEM Y  10 .   ? -11.565 13.324  16.980 1.00 47.36  ? 402 HEM C CMD 1 
HETATM 8483 C  CAD . HEM Y  10 .   ? -10.119 13.872  19.673 1.00 51.20  ? 402 HEM C CAD 1 
HETATM 8484 C  CBD . HEM Y  10 .   ? -11.204 13.666  20.729 1.00 50.51  ? 402 HEM C CBD 1 
HETATM 8485 C  CGD . HEM Y  10 .   ? -11.400 14.981  21.465 1.00 51.33  ? 402 HEM C CGD 1 
HETATM 8486 O  O1D . HEM Y  10 .   ? -10.476 15.840  21.540 1.00 45.48  ? 402 HEM C O1D 1 
HETATM 8487 O  O2D . HEM Y  10 .   ? -12.524 15.202  21.987 1.00 46.85  ? 402 HEM C O2D 1 
HETATM 8488 N  NA  . HEM Y  10 .   ? -6.982  9.452   19.412 1.00 43.63  ? 402 HEM C NA  1 
HETATM 8489 N  NB  . HEM Y  10 .   ? -6.685  7.535   17.347 1.00 42.40  ? 402 HEM C NB  1 
HETATM 8490 N  NC  . HEM Y  10 .   ? -8.734  8.862   15.797 1.00 41.98  ? 402 HEM C NC  1 
HETATM 8491 N  ND  . HEM Y  10 .   ? -9.041  10.692  17.918 1.00 47.54  ? 402 HEM C ND  1 
HETATM 8492 FE FE  . HEM Y  10 .   ? -7.981  9.131   17.737 1.00 42.17  ? 402 HEM C FE  1 
HETATM 8493 S  S   . SO4 Z  11 .   ? 12.679  -14.588 26.297 1.00 103.64 ? 403 SO4 C S   1 
HETATM 8494 O  O1  . SO4 Z  11 .   ? 12.536  -14.579 24.855 1.00 84.70  ? 403 SO4 C O1  1 
HETATM 8495 O  O2  . SO4 Z  11 .   ? 14.007  -14.122 26.662 1.00 91.13  ? 403 SO4 C O2  1 
HETATM 8496 O  O3  . SO4 Z  11 .   ? 12.485  -15.936 26.784 1.00 101.45 ? 403 SO4 C O3  1 
HETATM 8497 O  O4  . SO4 Z  11 .   ? 11.683  -13.721 26.890 1.00 91.14  ? 403 SO4 C O4  1 
HETATM 8498 S  S   . SO4 AA 11 .   ? -15.145 32.572  24.549 1.00 114.85 ? 404 SO4 C S   1 
HETATM 8499 O  O1  . SO4 AA 11 .   ? -13.879 32.011  24.968 1.00 101.34 ? 404 SO4 C O1  1 
HETATM 8500 O  O2  . SO4 AA 11 .   ? -15.053 32.993  23.170 1.00 95.59  ? 404 SO4 C O2  1 
HETATM 8501 O  O3  . SO4 AA 11 .   ? -16.184 31.577  24.688 1.00 104.06 ? 404 SO4 C O3  1 
HETATM 8502 O  O4  . SO4 AA 11 .   ? -15.459 33.713  25.376 1.00 113.98 ? 404 SO4 C O4  1 
HETATM 8503 MG MG  . MG  BA 12 .   ? -6.992  14.908  25.967 1.00 61.51  ? 405 MG  C MG  1 
HETATM 8504 O  O   . HOH CA 13 .   ? 27.143  -10.816 45.010 1.00 44.86  ? 501 HOH A O   1 
HETATM 8505 O  O   . HOH CA 13 .   ? 63.345  0.380   34.611 1.00 38.65  ? 502 HOH A O   1 
HETATM 8506 O  O   . HOH CA 13 .   ? 39.271  6.867   32.460 1.00 52.60  ? 503 HOH A O   1 
HETATM 8507 O  O   . HOH CA 13 .   ? 48.519  14.080  30.478 1.00 60.84  ? 504 HOH A O   1 
HETATM 8508 O  O   . HOH CA 13 .   ? 30.048  3.823   47.745 1.00 58.06  ? 505 HOH A O   1 
HETATM 8509 O  O   . HOH CA 13 .   ? 74.758  5.883   40.796 1.00 41.21  ? 506 HOH A O   1 
HETATM 8510 O  O   . HOH CA 13 .   ? 36.546  -20.500 45.987 1.00 42.53  ? 507 HOH A O   1 
HETATM 8511 O  O   . HOH CA 13 .   ? 51.993  -15.512 32.807 1.00 40.78  ? 508 HOH A O   1 
HETATM 8512 O  O   . HOH CA 13 .   ? 65.666  8.197   31.475 1.00 50.80  ? 509 HOH A O   1 
HETATM 8513 O  O   . HOH CA 13 .   ? 22.906  -1.608  42.107 1.00 36.35  ? 510 HOH A O   1 
HETATM 8514 O  O   . HOH CA 13 .   ? 23.992  1.172   43.251 1.00 35.61  ? 511 HOH A O   1 
HETATM 8515 O  O   . HOH CA 13 .   ? 56.202  -4.621  51.326 1.00 52.21  ? 512 HOH A O   1 
HETATM 8516 O  O   . HOH CA 13 .   ? 42.449  -9.939  18.616 1.00 47.38  ? 513 HOH A O   1 
HETATM 8517 O  O   . HOH CA 13 .   ? 39.484  3.990   18.473 1.00 39.53  ? 514 HOH A O   1 
HETATM 8518 O  O   . HOH CA 13 .   ? 25.830  -4.494  47.367 1.00 51.04  ? 515 HOH A O   1 
HETATM 8519 O  O   . HOH CA 13 .   ? 45.189  5.124   31.933 1.00 41.46  ? 516 HOH A O   1 
HETATM 8520 O  O   . HOH CA 13 .   ? 68.591  2.895   38.375 1.00 34.59  ? 517 HOH A O   1 
HETATM 8521 O  O   . HOH CA 13 .   ? 46.762  -12.105 28.936 1.00 41.17  ? 518 HOH A O   1 
HETATM 8522 O  O   . HOH CA 13 .   ? 41.394  10.358  49.691 1.00 45.02  ? 519 HOH A O   1 
HETATM 8523 O  O   . HOH CA 13 .   ? 44.449  21.903  25.153 1.00 56.36  ? 520 HOH A O   1 
HETATM 8524 O  O   . HOH CA 13 .   ? 38.214  8.165   44.919 1.00 43.38  ? 521 HOH A O   1 
HETATM 8525 O  O   . HOH CA 13 .   ? 46.909  7.778   37.997 1.00 36.45  ? 522 HOH A O   1 
HETATM 8526 O  O   . HOH CA 13 .   ? 44.090  -15.136 27.933 1.00 40.58  ? 523 HOH A O   1 
HETATM 8527 O  O   . HOH CA 13 .   ? 69.976  9.656   43.062 1.00 41.13  ? 524 HOH A O   1 
HETATM 8528 O  O   . HOH CA 13 .   ? 55.840  7.574   43.710 1.00 35.57  ? 525 HOH A O   1 
HETATM 8529 O  O   . HOH CA 13 .   ? 23.803  -11.517 34.287 1.00 49.62  ? 526 HOH A O   1 
HETATM 8530 O  O   . HOH CA 13 .   ? 40.636  15.802  31.632 1.00 31.65  ? 527 HOH A O   1 
HETATM 8531 O  O   . HOH CA 13 .   ? 20.392  -10.236 22.508 1.00 36.82  ? 528 HOH A O   1 
HETATM 8532 O  O   . HOH CA 13 .   ? 44.170  11.608  29.271 1.00 44.32  ? 529 HOH A O   1 
HETATM 8533 O  O   . HOH CA 13 .   ? 54.770  14.826  48.942 1.00 41.98  ? 530 HOH A O   1 
HETATM 8534 O  O   . HOH CA 13 .   ? 57.532  -2.850  45.479 1.00 35.13  ? 531 HOH A O   1 
HETATM 8535 O  O   . HOH CA 13 .   ? 51.091  -21.076 36.930 1.00 57.03  ? 532 HOH A O   1 
HETATM 8536 O  O   . HOH CA 13 .   ? 61.286  13.645  44.851 1.00 50.42  ? 533 HOH A O   1 
HETATM 8537 O  O   . HOH CA 13 .   ? 23.229  5.346   39.807 1.00 44.23  ? 534 HOH A O   1 
HETATM 8538 O  O   . HOH CA 13 .   ? 64.561  15.182  37.546 1.00 47.81  ? 535 HOH A O   1 
HETATM 8539 O  O   . HOH CA 13 .   ? 40.651  23.283  33.943 1.00 62.71  ? 536 HOH A O   1 
HETATM 8540 O  O   . HOH CA 13 .   ? 38.062  -13.269 35.660 1.00 36.47  ? 537 HOH A O   1 
HETATM 8541 O  O   . HOH CA 13 .   ? 44.830  -2.927  15.709 1.00 49.87  ? 538 HOH A O   1 
HETATM 8542 O  O   . HOH CA 13 .   ? 46.386  0.672   55.594 1.00 57.33  ? 539 HOH A O   1 
HETATM 8543 O  O   . HOH CA 13 .   ? 38.632  -17.486 46.992 1.00 37.98  ? 540 HOH A O   1 
HETATM 8544 O  O   . HOH CA 13 .   ? 52.377  8.520   51.728 1.00 29.59  ? 541 HOH A O   1 
HETATM 8545 O  O   . HOH CA 13 .   ? 30.603  -13.948 49.021 1.00 41.53  ? 542 HOH A O   1 
HETATM 8546 O  O   . HOH CA 13 .   ? 22.042  -7.075  29.481 1.00 40.89  ? 543 HOH A O   1 
HETATM 8547 O  O   . HOH CA 13 .   ? 34.766  14.668  36.052 1.00 43.94  ? 544 HOH A O   1 
HETATM 8548 O  O   . HOH CA 13 .   ? 46.650  -9.925  47.897 1.00 37.61  ? 545 HOH A O   1 
HETATM 8549 O  O   . HOH CA 13 .   ? 24.816  -10.334 21.881 1.00 47.69  ? 546 HOH A O   1 
HETATM 8550 O  O   . HOH CA 13 .   ? 52.818  -7.580  50.556 1.00 43.75  ? 547 HOH A O   1 
HETATM 8551 O  O   . HOH CA 13 .   ? 42.081  7.100   54.476 1.00 41.91  ? 548 HOH A O   1 
HETATM 8552 O  O   . HOH CA 13 .   ? 36.838  9.605   31.216 1.00 32.50  ? 549 HOH A O   1 
HETATM 8553 O  O   . HOH CA 13 .   ? 37.553  1.907   18.626 1.00 45.41  ? 550 HOH A O   1 
HETATM 8554 O  O   . HOH CA 13 .   ? 33.673  10.362  37.129 1.00 36.90  ? 551 HOH A O   1 
HETATM 8555 O  O   . HOH CA 13 .   ? 45.969  -1.399  54.073 1.00 42.68  ? 552 HOH A O   1 
HETATM 8556 O  O   . HOH CA 13 .   ? 57.148  -5.550  45.292 1.00 33.71  ? 553 HOH A O   1 
HETATM 8557 O  O   . HOH CA 13 .   ? 41.015  -0.893  10.408 1.00 49.32  ? 554 HOH A O   1 
HETATM 8558 O  O   . HOH CA 13 .   ? 34.933  -1.955  53.951 1.00 32.64  ? 555 HOH A O   1 
HETATM 8559 O  O   . HOH CA 13 .   ? 20.927  3.781   28.736 1.00 43.18  ? 556 HOH A O   1 
HETATM 8560 O  O   . HOH CA 13 .   ? 27.051  -16.120 25.684 1.00 52.90  ? 557 HOH A O   1 
HETATM 8561 O  O   . HOH CA 13 .   ? 29.537  -12.280 34.784 1.00 39.79  ? 558 HOH A O   1 
HETATM 8562 O  O   . HOH CA 13 .   ? 28.131  -19.337 44.886 1.00 48.32  ? 559 HOH A O   1 
HETATM 8563 O  O   . HOH CA 13 .   ? 54.116  9.844   43.615 1.00 38.68  ? 560 HOH A O   1 
HETATM 8564 O  O   . HOH CA 13 .   ? 46.769  -15.171 36.393 1.00 33.68  ? 561 HOH A O   1 
HETATM 8565 O  O   . HOH CA 13 .   ? 58.592  -13.794 43.279 1.00 56.27  ? 562 HOH A O   1 
HETATM 8566 O  O   . HOH CA 13 .   ? 33.319  -2.524  16.869 1.00 48.62  ? 563 HOH A O   1 
HETATM 8567 O  O   . HOH CA 13 .   ? 37.118  -13.228 26.391 1.00 51.86  ? 564 HOH A O   1 
HETATM 8568 O  O   . HOH CA 13 .   ? 48.393  8.834   49.913 1.00 41.22  ? 565 HOH A O   1 
HETATM 8569 O  O   . HOH CA 13 .   ? 34.228  12.923  27.760 1.00 45.74  ? 566 HOH A O   1 
HETATM 8570 O  O   . HOH CA 13 .   ? 30.680  -10.060 56.048 1.00 42.49  ? 567 HOH A O   1 
HETATM 8571 O  O   . HOH CA 13 .   ? 50.201  13.859  35.741 1.00 51.96  ? 568 HOH A O   1 
HETATM 8572 O  O   . HOH CA 13 .   ? 40.617  12.080  33.235 1.00 38.45  ? 569 HOH A O   1 
HETATM 8573 O  O   . HOH CA 13 .   ? 48.851  10.411  36.484 1.00 40.14  ? 570 HOH A O   1 
HETATM 8574 O  O   . HOH CA 13 .   ? 58.365  0.228   47.221 1.00 36.80  ? 571 HOH A O   1 
HETATM 8575 O  O   . HOH CA 13 .   ? 73.268  4.628   35.339 1.00 41.11  ? 572 HOH A O   1 
HETATM 8576 O  O   . HOH CA 13 .   ? 49.479  5.962   46.977 1.00 36.69  ? 573 HOH A O   1 
HETATM 8577 O  O   . HOH CA 13 .   ? 64.567  1.693   26.555 1.00 52.02  ? 574 HOH A O   1 
HETATM 8578 O  O   . HOH CA 13 .   ? 39.073  7.617   35.400 1.00 31.44  ? 575 HOH A O   1 
HETATM 8579 O  O   . HOH CA 13 .   ? 38.855  -14.967 29.711 1.00 39.78  ? 576 HOH A O   1 
HETATM 8580 O  O   . HOH CA 13 .   ? 29.297  3.842   42.790 1.00 45.63  ? 577 HOH A O   1 
HETATM 8581 O  O   . HOH CA 13 .   ? 35.284  4.971   42.751 1.00 42.83  ? 578 HOH A O   1 
HETATM 8582 O  O   . HOH CA 13 .   ? 57.879  -12.869 39.644 1.00 55.72  ? 579 HOH A O   1 
HETATM 8583 O  O   . HOH CA 13 .   ? 68.777  13.488  48.256 1.00 46.42  ? 580 HOH A O   1 
HETATM 8584 O  O   . HOH CA 13 .   ? 36.694  -10.539 54.853 1.00 50.99  ? 581 HOH A O   1 
HETATM 8585 O  O   . HOH CA 13 .   ? 49.039  -3.662  53.031 1.00 38.48  ? 582 HOH A O   1 
HETATM 8586 O  O   . HOH CA 13 .   ? 70.279  -1.758  29.672 1.00 51.30  ? 583 HOH A O   1 
HETATM 8587 O  O   . HOH CA 13 .   ? 43.899  -22.319 32.754 1.00 44.90  ? 584 HOH A O   1 
HETATM 8588 O  O   . HOH CA 13 .   ? 55.689  13.148  32.474 1.00 54.24  ? 585 HOH A O   1 
HETATM 8589 O  O   . HOH CA 13 .   ? 46.246  -1.904  26.723 1.00 56.28  ? 586 HOH A O   1 
HETATM 8590 O  O   . HOH CA 13 .   ? 61.495  -4.686  54.964 1.00 39.56  ? 587 HOH A O   1 
HETATM 8591 O  O   . HOH CA 13 .   ? 51.857  -16.247 42.784 1.00 47.94  ? 588 HOH A O   1 
HETATM 8592 O  O   . HOH CA 13 .   ? 55.202  -0.252  55.192 1.00 49.42  ? 589 HOH A O   1 
HETATM 8593 O  O   . HOH CA 13 .   ? 36.617  5.524   12.127 1.00 53.87  ? 590 HOH A O   1 
HETATM 8594 O  O   . HOH CA 13 .   ? 25.171  -8.988  38.888 1.00 42.62  ? 591 HOH A O   1 
HETATM 8595 O  O   . HOH CA 13 .   ? 32.395  -20.215 49.603 1.00 45.46  ? 592 HOH A O   1 
HETATM 8596 O  O   . HOH CA 13 .   ? 29.085  11.285  26.952 1.00 44.80  ? 593 HOH A O   1 
HETATM 8597 O  O   . HOH CA 13 .   ? 45.545  12.353  44.948 1.00 39.37  ? 594 HOH A O   1 
HETATM 8598 O  O   . HOH CA 13 .   ? 42.438  -13.376 50.066 1.00 53.86  ? 595 HOH A O   1 
HETATM 8599 O  O   . HOH CA 13 .   ? 30.358  5.157   28.299 1.00 34.05  ? 596 HOH A O   1 
HETATM 8600 O  O   . HOH CA 13 .   ? 28.856  7.812   41.827 1.00 56.48  ? 597 HOH A O   1 
HETATM 8601 O  O   . HOH CA 13 .   ? 21.738  -0.962  37.232 1.00 48.16  ? 598 HOH A O   1 
HETATM 8602 O  O   . HOH CA 13 .   ? 49.279  -15.279 35.256 1.00 32.38  ? 599 HOH A O   1 
HETATM 8603 O  O   . HOH CA 13 .   ? 31.971  -1.609  49.400 1.00 33.93  ? 600 HOH A O   1 
HETATM 8604 O  O   . HOH CA 13 .   ? 20.548  5.940   21.373 1.00 51.82  ? 601 HOH A O   1 
HETATM 8605 O  O   . HOH CA 13 .   ? 65.774  -0.220  35.907 1.00 38.24  ? 602 HOH A O   1 
HETATM 8606 O  O   . HOH CA 13 .   ? 57.929  7.454   47.615 1.00 37.41  ? 603 HOH A O   1 
HETATM 8607 O  O   . HOH CA 13 .   ? 39.116  -5.782  57.331 1.00 55.15  ? 604 HOH A O   1 
HETATM 8608 O  O   . HOH CA 13 .   ? 37.121  -18.104 30.925 1.00 44.00  ? 605 HOH A O   1 
HETATM 8609 O  O   . HOH CA 13 .   ? 38.191  5.028   35.400 1.00 35.34  ? 606 HOH A O   1 
HETATM 8610 O  O   . HOH CA 13 .   ? 26.530  -5.028  16.080 1.00 45.95  ? 607 HOH A O   1 
HETATM 8611 O  O   . HOH CA 13 .   ? 47.048  -17.158 29.577 1.00 42.99  ? 608 HOH A O   1 
HETATM 8612 O  O   . HOH CA 13 .   ? 37.067  2.683   59.921 1.00 55.85  ? 609 HOH A O   1 
HETATM 8613 O  O   . HOH CA 13 .   ? 38.051  -9.531  24.243 1.00 54.25  ? 610 HOH A O   1 
HETATM 8614 O  O   . HOH CA 13 .   ? 22.790  8.216   16.556 1.00 58.34  ? 611 HOH A O   1 
HETATM 8615 O  O   . HOH CA 13 .   ? 29.611  10.846  38.805 1.00 45.54  ? 612 HOH A O   1 
HETATM 8616 O  O   . HOH CA 13 .   ? 43.696  15.747  30.229 1.00 40.62  ? 613 HOH A O   1 
HETATM 8617 O  O   . HOH CA 13 .   ? 23.873  -3.881  15.673 1.00 42.97  ? 614 HOH A O   1 
HETATM 8618 O  O   . HOH CA 13 .   ? 40.426  2.115   42.037 1.00 28.68  ? 615 HOH A O   1 
HETATM 8619 O  O   . HOH CA 13 .   ? 54.692  -14.585 34.071 1.00 48.44  ? 616 HOH A O   1 
HETATM 8620 O  O   . HOH CA 13 .   ? 32.971  -10.203 22.612 1.00 44.49  ? 617 HOH A O   1 
HETATM 8621 O  O   . HOH CA 13 .   ? 44.469  -11.586 47.226 1.00 38.91  ? 618 HOH A O   1 
HETATM 8622 O  O   . HOH CA 13 .   ? 65.637  7.827   51.571 1.00 41.81  ? 619 HOH A O   1 
HETATM 8623 O  O   . HOH CA 13 .   ? 60.959  17.778  38.392 1.00 52.94  ? 620 HOH A O   1 
HETATM 8624 O  O   . HOH CA 13 .   ? 39.105  -24.226 34.650 1.00 48.43  ? 621 HOH A O   1 
HETATM 8625 O  O   . HOH CA 13 .   ? 31.250  11.950  36.929 1.00 43.73  ? 622 HOH A O   1 
HETATM 8626 O  O   . HOH CA 13 .   ? 28.674  -0.352  46.657 1.00 39.74  ? 623 HOH A O   1 
HETATM 8627 O  O   . HOH CA 13 .   ? 55.314  -5.497  47.427 1.00 35.74  ? 624 HOH A O   1 
HETATM 8628 O  O   . HOH CA 13 .   ? 48.828  -4.503  31.919 1.00 53.87  ? 625 HOH A O   1 
HETATM 8629 O  O   . HOH CA 13 .   ? 63.666  7.965   29.681 1.00 51.71  ? 626 HOH A O   1 
HETATM 8630 O  O   . HOH CA 13 .   ? 27.375  -11.309 32.164 1.00 38.09  ? 627 HOH A O   1 
HETATM 8631 O  O   . HOH CA 13 .   ? 45.190  14.640  39.777 1.00 49.10  ? 628 HOH A O   1 
HETATM 8632 O  O   . HOH CA 13 .   ? 65.845  -6.199  26.765 1.00 55.70  ? 629 HOH A O   1 
HETATM 8633 O  O   . HOH CA 13 .   ? 47.781  4.365   16.554 1.00 50.31  ? 630 HOH A O   1 
HETATM 8634 O  O   . HOH CA 13 .   ? 38.482  9.756   33.394 1.00 43.72  ? 631 HOH A O   1 
HETATM 8635 O  O   . HOH CA 13 .   ? 32.107  14.606  27.964 1.00 45.08  ? 632 HOH A O   1 
HETATM 8636 O  O   . HOH CA 13 .   ? 34.674  -3.856  51.880 1.00 39.58  ? 633 HOH A O   1 
HETATM 8637 O  O   . HOH CA 13 .   ? 20.681  2.782   31.373 1.00 44.42  ? 634 HOH A O   1 
HETATM 8638 O  O   . HOH CA 13 .   ? 30.204  11.093  20.186 1.00 49.51  ? 635 HOH A O   1 
HETATM 8639 O  O   . HOH CA 13 .   ? 46.072  -24.739 36.710 1.00 40.57  ? 636 HOH A O   1 
HETATM 8640 O  O   . HOH CA 13 .   ? 60.763  -9.972  25.303 1.00 53.99  ? 637 HOH A O   1 
HETATM 8641 O  O   . HOH CA 13 .   ? 34.985  5.501   52.968 1.00 51.24  ? 638 HOH A O   1 
HETATM 8642 O  O   . HOH CA 13 .   ? 54.124  12.122  36.473 1.00 40.91  ? 639 HOH A O   1 
HETATM 8643 O  O   . HOH CA 13 .   ? 36.267  15.114  42.724 1.00 52.65  ? 640 HOH A O   1 
HETATM 8644 O  O   . HOH CA 13 .   ? 22.961  2.595   16.364 1.00 42.66  ? 641 HOH A O   1 
HETATM 8645 O  O   . HOH CA 13 .   ? 23.096  -5.533  39.223 1.00 51.52  ? 642 HOH A O   1 
HETATM 8646 O  O   . HOH CA 13 .   ? 34.641  -3.786  55.905 1.00 39.33  ? 643 HOH A O   1 
HETATM 8647 O  O   . HOH CA 13 .   ? 67.141  14.887  37.999 1.00 44.93  ? 644 HOH A O   1 
HETATM 8648 O  O   . HOH CA 13 .   ? 39.532  2.454   57.092 1.00 48.31  ? 645 HOH A O   1 
HETATM 8649 O  O   . HOH CA 13 .   ? 66.627  0.198   38.226 1.00 45.19  ? 646 HOH A O   1 
HETATM 8650 O  O   . HOH CA 13 .   ? 70.337  4.382   31.828 1.00 67.47  ? 647 HOH A O   1 
HETATM 8651 O  O   . HOH CA 13 .   ? 47.205  9.855   31.639 1.00 57.99  ? 648 HOH A O   1 
HETATM 8652 O  O   . HOH CA 13 .   ? 40.069  8.623   47.593 1.00 42.12  ? 649 HOH A O   1 
HETATM 8653 O  O   . HOH CA 13 .   ? 50.840  10.030  37.973 1.00 43.88  ? 650 HOH A O   1 
HETATM 8654 O  O   . HOH CA 13 .   ? 43.291  12.786  46.573 1.00 45.76  ? 651 HOH A O   1 
HETATM 8655 O  O   . HOH CA 13 .   ? 35.678  -23.134 42.872 1.00 43.13  ? 652 HOH A O   1 
HETATM 8656 O  O   . HOH CA 13 .   ? 64.841  14.521  44.876 1.00 52.38  ? 653 HOH A O   1 
HETATM 8657 O  O   . HOH CA 13 .   ? 57.001  -12.818 37.442 1.00 45.82  ? 654 HOH A O   1 
HETATM 8658 O  O   . HOH CA 13 .   ? 43.777  12.715  14.362 1.00 57.72  ? 655 HOH A O   1 
HETATM 8659 O  O   . HOH CA 13 .   ? 31.250  4.741   17.340 1.00 47.88  ? 656 HOH A O   1 
HETATM 8660 O  O   . HOH CA 13 .   ? 56.475  13.415  36.516 1.00 43.64  ? 657 HOH A O   1 
HETATM 8661 O  O   . HOH CA 13 .   ? 44.791  -18.939 42.075 1.00 51.12  ? 658 HOH A O   1 
HETATM 8662 O  O   . HOH CA 13 .   ? 70.828  4.143   48.185 1.00 48.15  ? 659 HOH A O   1 
HETATM 8663 O  O   . HOH CA 13 .   ? 32.272  2.239   41.933 1.00 36.32  ? 660 HOH A O   1 
HETATM 8664 O  O   . HOH CA 13 .   ? 20.695  -8.932  30.526 1.00 51.92  ? 661 HOH A O   1 
HETATM 8665 O  O   . HOH CA 13 .   ? 51.365  9.448   29.940 1.00 40.92  ? 662 HOH A O   1 
HETATM 8666 O  O   . HOH CA 13 .   ? 31.619  5.684   42.686 1.00 43.37  ? 663 HOH A O   1 
HETATM 8667 O  O   . HOH CA 13 .   ? 27.254  1.600   45.250 1.00 45.26  ? 664 HOH A O   1 
HETATM 8668 O  O   . HOH CA 13 .   ? 48.809  9.463   29.506 1.00 41.50  ? 665 HOH A O   1 
HETATM 8669 O  O   . HOH CA 13 .   ? 22.083  1.021   35.842 1.00 46.44  ? 666 HOH A O   1 
HETATM 8670 O  O   . HOH CA 13 .   ? 34.055  12.256  30.397 1.00 38.78  ? 667 HOH A O   1 
HETATM 8671 O  O   . HOH CA 13 .   ? 62.955  13.425  32.989 1.00 43.98  ? 668 HOH A O   1 
HETATM 8672 O  O   . HOH CA 13 .   ? 65.996  11.122  48.854 1.00 42.40  ? 669 HOH A O   1 
HETATM 8673 O  O   . HOH CA 13 .   ? 71.096  -2.866  40.643 1.00 54.87  ? 670 HOH A O   1 
HETATM 8674 O  O   . HOH CA 13 .   ? 32.696  -24.271 41.723 1.00 55.92  ? 671 HOH A O   1 
HETATM 8675 O  O   . HOH CA 13 .   ? 55.263  -16.319 43.458 1.00 48.40  ? 672 HOH A O   1 
HETATM 8676 O  O   . HOH CA 13 .   ? 49.259  12.915  48.236 1.00 57.77  ? 673 HOH A O   1 
HETATM 8677 O  O   . HOH CA 13 .   ? 54.612  -2.506  53.613 1.00 51.49  ? 674 HOH A O   1 
HETATM 8678 O  O   . HOH CA 13 .   ? 46.924  -20.744 42.854 1.00 40.91  ? 675 HOH A O   1 
HETATM 8679 O  O   . HOH CA 13 .   ? 49.720  6.122   15.559 1.00 48.23  ? 676 HOH A O   1 
HETATM 8680 O  O   . HOH CA 13 .   ? 42.028  17.552  32.516 1.00 49.96  ? 677 HOH A O   1 
HETATM 8681 O  O   . HOH CA 13 .   ? 35.663  7.977   54.762 1.00 53.73  ? 678 HOH A O   1 
HETATM 8682 O  O   . HOH CA 13 .   ? 36.399  17.675  16.136 1.00 62.83  ? 679 HOH A O   1 
HETATM 8683 O  O   . HOH CA 13 .   ? 48.341  -15.144 42.910 1.00 50.40  ? 680 HOH A O   1 
HETATM 8684 O  O   . HOH CA 13 .   ? 51.844  10.860  50.591 1.00 46.76  ? 681 HOH A O   1 
HETATM 8685 O  O   . HOH CA 13 .   ? 38.816  22.051  35.304 1.00 55.09  ? 682 HOH A O   1 
HETATM 8686 O  O   . HOH CA 13 .   ? 38.365  -8.962  55.651 1.00 54.89  ? 683 HOH A O   1 
HETATM 8687 O  O   . HOH CA 13 .   ? 45.743  -8.598  50.192 1.00 42.90  ? 684 HOH A O   1 
HETATM 8688 O  O   . HOH CA 13 .   ? 29.137  -24.415 37.801 1.00 53.18  ? 685 HOH A O   1 
HETATM 8689 O  O   . HOH CA 13 .   ? 29.044  -13.763 32.372 1.00 48.62  ? 686 HOH A O   1 
HETATM 8690 O  O   . HOH CA 13 .   ? 29.291  -11.291 48.811 1.00 34.38  ? 687 HOH A O   1 
HETATM 8691 O  O   . HOH CA 13 .   ? 31.862  -2.822  56.702 1.00 50.86  ? 688 HOH A O   1 
HETATM 8692 O  O   . HOH CA 13 .   ? 33.362  8.499   12.223 1.00 65.73  ? 689 HOH A O   1 
HETATM 8693 O  O   . HOH CA 13 .   ? 28.773  -14.614 37.074 1.00 51.41  ? 690 HOH A O   1 
HETATM 8694 O  O   . HOH CA 13 .   ? 33.902  0.121   40.880 1.00 34.53  ? 691 HOH A O   1 
HETATM 8695 O  O   . HOH CA 13 .   ? 47.905  -5.493  54.715 1.00 47.16  ? 692 HOH A O   1 
HETATM 8696 O  O   . HOH CA 13 .   ? 37.988  7.045   48.288 1.00 39.96  ? 693 HOH A O   1 
HETATM 8697 O  O   . HOH CA 13 .   ? 75.341  3.081   40.525 1.00 43.64  ? 694 HOH A O   1 
HETATM 8698 O  O   . HOH CA 13 .   ? 38.896  14.351  40.167 1.00 43.59  ? 695 HOH A O   1 
HETATM 8699 O  O   . HOH CA 13 .   ? 45.389  3.382   14.519 1.00 57.17  ? 696 HOH A O   1 
HETATM 8700 O  O   . HOH CA 13 .   ? 24.809  3.950   14.119 1.00 54.92  ? 697 HOH A O   1 
HETATM 8701 O  O   . HOH CA 13 .   ? 56.183  -2.218  19.995 1.00 58.74  ? 698 HOH A O   1 
HETATM 8702 O  O   . HOH CA 13 .   ? 35.446  -10.695 17.059 1.00 62.09  ? 699 HOH A O   1 
HETATM 8703 O  O   . HOH CA 13 .   ? 25.874  -13.315 46.909 1.00 56.21  ? 700 HOH A O   1 
HETATM 8704 O  O   . HOH CA 13 .   ? 25.310  -13.883 35.127 1.00 61.19  ? 701 HOH A O   1 
HETATM 8705 O  O   . HOH CA 13 .   ? 29.455  -21.229 27.069 1.00 59.05  ? 702 HOH A O   1 
HETATM 8706 O  O   . HOH CA 13 .   ? 72.707  7.157   49.909 1.00 48.57  ? 703 HOH A O   1 
HETATM 8707 O  O   . HOH CA 13 .   ? 48.663  2.316   17.503 1.00 45.60  ? 704 HOH A O   1 
HETATM 8708 O  O   . HOH CA 13 .   ? 47.266  11.239  27.928 1.00 47.64  ? 705 HOH A O   1 
HETATM 8709 O  O   . HOH CA 13 .   ? 53.269  13.279  32.267 1.00 56.26  ? 706 HOH A O   1 
HETATM 8710 O  O   . HOH CA 13 .   ? 33.771  -15.667 22.062 1.00 66.92  ? 707 HOH A O   1 
HETATM 8711 O  O   . HOH CA 13 .   ? 65.346  -4.879  24.112 1.00 59.94  ? 708 HOH A O   1 
HETATM 8712 O  O   . HOH CA 13 .   ? 53.326  9.043   12.901 1.00 71.20  ? 709 HOH A O   1 
HETATM 8713 O  O   . HOH CA 13 .   ? 48.875  13.280  27.932 1.00 52.20  ? 710 HOH A O   1 
HETATM 8714 O  O   . HOH CA 13 .   ? 58.687  8.129   50.221 1.00 48.39  ? 711 HOH A O   1 
HETATM 8715 O  O   . HOH CA 13 .   ? 57.753  15.641  52.136 1.00 49.89  ? 712 HOH A O   1 
HETATM 8716 O  O   . HOH CA 13 .   ? 27.017  -15.453 45.730 1.00 49.87  ? 713 HOH A O   1 
HETATM 8717 O  O   . HOH CA 13 .   ? 48.834  -7.409  28.642 1.00 58.27  ? 714 HOH A O   1 
HETATM 8718 O  O   . HOH CA 13 .   ? 45.829  19.592  28.003 1.00 54.91  ? 715 HOH A O   1 
HETATM 8719 O  O   . HOH CA 13 .   ? 48.870  -11.044 49.269 1.00 42.11  ? 716 HOH A O   1 
HETATM 8720 O  O   . HOH CA 13 .   ? 37.125  26.090  22.037 1.00 68.83  ? 717 HOH A O   1 
HETATM 8721 O  O   . HOH CA 13 .   ? 52.697  8.499   58.534 1.00 56.26  ? 718 HOH A O   1 
HETATM 8722 O  O   . HOH CA 13 .   ? 20.640  2.386   38.243 1.00 52.98  ? 719 HOH A O   1 
HETATM 8723 O  O   . HOH CA 13 .   ? 64.489  -1.656  55.044 1.00 53.27  ? 720 HOH A O   1 
HETATM 8724 O  O   . HOH CA 13 .   ? 41.177  12.724  44.892 1.00 45.32  ? 721 HOH A O   1 
HETATM 8725 O  O   . HOH CA 13 .   ? 36.149  -3.314  60.877 1.00 66.47  ? 722 HOH A O   1 
HETATM 8726 O  O   . HOH CA 13 .   ? 39.082  17.718  16.051 1.00 50.05  ? 723 HOH A O   1 
HETATM 8727 O  O   . HOH CA 13 .   ? 49.271  -10.255 52.343 1.00 52.60  ? 724 HOH A O   1 
HETATM 8728 O  O   . HOH CA 13 .   ? 32.713  7.318   44.689 1.00 52.70  ? 725 HOH A O   1 
HETATM 8729 O  O   . HOH CA 13 .   ? 48.778  22.864  23.579 1.00 61.44  ? 726 HOH A O   1 
HETATM 8730 O  O   . HOH CA 13 .   ? 25.427  0.506   52.615 1.00 37.03  ? 727 HOH A O   1 
HETATM 8731 O  O   . HOH CA 13 .   ? 36.121  -7.351  58.113 1.00 57.42  ? 728 HOH A O   1 
HETATM 8732 O  O   . HOH CA 13 .   ? 42.303  -11.774 20.517 1.00 55.26  ? 729 HOH A O   1 
HETATM 8733 O  O   . HOH CA 13 .   ? 50.126  -19.450 44.162 1.00 48.78  ? 730 HOH A O   1 
HETATM 8734 O  O   . HOH CA 13 .   ? 51.134  -11.112 48.105 1.00 39.88  ? 731 HOH A O   1 
HETATM 8735 O  O   . HOH CA 13 .   ? 48.549  17.514  21.848 1.00 63.11  ? 732 HOH A O   1 
HETATM 8736 O  O   . HOH CA 13 .   ? 30.058  -16.483 19.675 1.00 59.25  ? 733 HOH A O   1 
HETATM 8737 O  O   . HOH CA 13 .   ? 65.191  -5.238  41.819 1.00 57.65  ? 734 HOH A O   1 
HETATM 8738 O  O   . HOH CA 13 .   ? 23.252  7.365   26.523 1.00 47.94  ? 735 HOH A O   1 
HETATM 8739 O  O   . HOH CA 13 .   ? 48.075  19.692  23.467 1.00 60.97  ? 736 HOH A O   1 
HETATM 8740 O  O   . HOH CA 13 .   ? 26.601  10.089  38.823 1.00 51.83  ? 737 HOH A O   1 
HETATM 8741 O  O   . HOH CA 13 .   ? 67.508  6.752   54.298 1.00 48.04  ? 738 HOH A O   1 
HETATM 8742 O  O   . HOH CA 13 .   ? 52.909  -10.394 28.196 1.00 53.99  ? 739 HOH A O   1 
HETATM 8743 O  O   . HOH CA 13 .   ? 45.613  -7.583  21.508 1.00 52.71  ? 740 HOH A O   1 
HETATM 8744 O  O   . HOH CA 13 .   ? 50.888  -14.752 45.261 1.00 57.20  ? 741 HOH A O   1 
HETATM 8745 O  O   . HOH CA 13 .   ? 49.998  -21.876 46.310 1.00 56.32  ? 742 HOH A O   1 
HETATM 8746 O  O   . HOH CA 13 .   ? 58.039  4.366   12.314 1.00 70.67  ? 743 HOH A O   1 
HETATM 8747 O  O   . HOH CA 13 .   ? 27.818  -17.814 34.813 1.00 49.47  ? 744 HOH A O   1 
HETATM 8748 O  O   . HOH CA 13 .   ? 30.484  4.485   13.198 1.00 66.49  ? 745 HOH A O   1 
HETATM 8749 O  O   . HOH CA 13 .   ? 66.687  -9.283  27.530 1.00 63.58  ? 746 HOH A O   1 
HETATM 8750 O  O   . HOH CA 13 .   ? 33.894  24.463  18.632 1.00 66.48  ? 747 HOH A O   1 
HETATM 8751 O  O   . HOH CA 13 .   ? 42.873  -6.540  14.760 1.00 59.31  ? 748 HOH A O   1 
HETATM 8752 O  O   . HOH CA 13 .   ? 64.956  12.986  47.647 1.00 51.48  ? 749 HOH A O   1 
HETATM 8753 O  O   . HOH CA 13 .   ? 68.804  7.003   32.583 1.00 61.42  ? 750 HOH A O   1 
HETATM 8754 O  O   . HOH CA 13 .   ? 48.957  11.430  50.749 1.00 43.18  ? 751 HOH A O   1 
HETATM 8755 O  O   . HOH CA 13 .   ? 38.147  10.119  46.536 1.00 54.52  ? 752 HOH A O   1 
HETATM 8756 O  O   . HOH CA 13 .   ? 35.277  7.343   44.040 1.00 39.03  ? 753 HOH A O   1 
HETATM 8757 O  O   . HOH CA 13 .   ? 34.928  -13.800 56.031 1.00 63.29  ? 754 HOH A O   1 
HETATM 8758 O  O   . HOH CA 13 .   ? 55.385  -7.001  49.447 1.00 61.11  ? 755 HOH A O   1 
HETATM 8759 O  O   . HOH CA 13 .   ? 46.070  12.669  30.504 1.00 56.20  ? 756 HOH A O   1 
HETATM 8760 O  O   . HOH CA 13 .   ? 44.430  -0.698  13.761 1.00 48.55  ? 757 HOH A O   1 
HETATM 8761 O  O   . HOH CA 13 .   ? 51.674  14.408  38.801 1.00 49.65  ? 758 HOH A O   1 
HETATM 8762 O  O   . HOH CA 13 .   ? 25.049  -16.924 45.073 1.00 57.87  ? 759 HOH A O   1 
HETATM 8763 O  O   . HOH CA 13 .   ? 21.763  -1.702  34.792 1.00 58.30  ? 760 HOH A O   1 
HETATM 8764 O  O   . HOH CA 13 .   ? 63.521  -3.710  56.230 1.00 59.59  ? 761 HOH A O   1 
HETATM 8765 O  O   . HOH CA 13 .   ? 60.113  10.217  26.538 1.00 60.74  ? 762 HOH A O   1 
HETATM 8766 O  O   . HOH CA 13 .   ? 44.071  -7.753  54.307 1.00 57.67  ? 763 HOH A O   1 
HETATM 8767 O  O   . HOH CA 13 .   ? 68.408  -2.450  39.143 1.00 60.51  ? 764 HOH A O   1 
HETATM 8768 O  O   . HOH CA 13 .   ? 33.520  3.258   44.231 1.00 41.20  ? 765 HOH A O   1 
HETATM 8769 O  O   . HOH CA 13 .   ? 55.670  -13.736 46.113 1.00 55.72  ? 766 HOH A O   1 
HETATM 8770 O  O   . HOH CA 13 .   ? 67.335  -3.982  41.538 1.00 54.33  ? 767 HOH A O   1 
HETATM 8771 O  O   . HOH CA 13 .   ? 44.896  -4.975  13.904 1.00 54.22  ? 768 HOH A O   1 
HETATM 8772 O  O   . HOH CA 13 .   ? 24.282  3.853   43.556 1.00 45.01  ? 769 HOH A O   1 
HETATM 8773 O  O   . HOH CA 13 .   ? 56.454  15.636  38.298 1.00 52.18  ? 770 HOH A O   1 
HETATM 8774 O  O   . HOH CA 13 .   ? 42.475  7.857   57.073 1.00 45.84  ? 771 HOH A O   1 
HETATM 8775 O  O   . HOH CA 13 .   ? 35.362  10.568  47.399 1.00 54.35  ? 772 HOH A O   1 
HETATM 8776 O  O   . HOH CA 13 .   ? 63.708  -9.308  24.230 1.00 61.55  ? 773 HOH A O   1 
HETATM 8777 O  O   . HOH CA 13 .   ? 57.055  4.532   57.842 1.00 54.59  ? 774 HOH A O   1 
HETATM 8778 O  O   . HOH CA 13 .   ? 35.872  -13.871 24.018 1.00 62.56  ? 775 HOH A O   1 
HETATM 8779 O  O   . HOH CA 13 .   ? 26.989  -20.146 33.991 1.00 60.74  ? 776 HOH A O   1 
HETATM 8780 O  O   . HOH CA 13 .   ? 52.816  -10.055 49.612 1.00 53.19  ? 777 HOH A O   1 
HETATM 8781 O  O   . HOH CA 13 .   ? 39.546  10.060  51.385 1.00 52.39  ? 778 HOH A O   1 
HETATM 8782 O  O   . HOH CA 13 .   ? 43.719  -14.208 47.985 1.00 50.51  ? 779 HOH A O   1 
HETATM 8783 O  O   . HOH CA 13 .   ? 72.317  4.007   51.351 1.00 61.15  ? 780 HOH A O   1 
HETATM 8784 O  O   . HOH CA 13 .   ? 32.207  -17.667 57.124 1.00 61.71  ? 781 HOH A O   1 
HETATM 8785 O  O   . HOH CA 13 .   ? 47.124  -4.990  29.871 1.00 50.70  ? 782 HOH A O   1 
HETATM 8786 O  O   . HOH CA 13 .   ? 46.104  -2.549  29.338 1.00 55.55  ? 783 HOH A O   1 
HETATM 8787 O  O   . HOH CA 13 .   ? 49.249  15.434  42.748 1.00 54.50  ? 784 HOH A O   1 
HETATM 8788 O  O   . HOH CA 13 .   ? 49.994  -17.255 33.246 1.00 45.03  ? 785 HOH A O   1 
HETATM 8789 O  O   . HOH CA 13 .   ? 47.769  3.443   58.959 1.00 59.35  ? 786 HOH A O   1 
HETATM 8790 O  O   . HOH CA 13 .   ? 44.507  6.795   58.848 1.00 49.86  ? 787 HOH A O   1 
HETATM 8791 O  O   . HOH CA 13 .   ? 65.538  -8.050  41.914 1.00 65.19  ? 788 HOH A O   1 
HETATM 8792 O  O   . HOH CA 13 .   ? 23.358  13.729  29.560 1.00 57.49  ? 789 HOH A O   1 
HETATM 8793 O  O   . HOH CA 13 .   ? 24.975  -17.508 36.864 1.00 62.02  ? 790 HOH A O   1 
HETATM 8794 O  O   . HOH CA 13 .   ? 31.180  5.769   52.736 1.00 58.79  ? 791 HOH A O   1 
HETATM 8795 O  O   . HOH CA 13 .   ? 50.871  -19.893 34.543 1.00 44.70  ? 792 HOH A O   1 
HETATM 8796 O  O   . HOH CA 13 .   ? 68.698  19.049  43.968 1.00 57.88  ? 793 HOH A O   1 
HETATM 8797 O  O   . HOH CA 13 .   ? 27.325  5.612   42.371 1.00 50.57  ? 794 HOH A O   1 
HETATM 8798 O  O   . HOH CA 13 .   ? 50.608  -4.891  29.708 1.00 63.67  ? 795 HOH A O   1 
HETATM 8799 O  O   . HOH CA 13 .   ? 63.720  10.292  50.996 1.00 58.14  ? 796 HOH A O   1 
HETATM 8800 O  O   . HOH CA 13 .   ? 35.402  -11.835 19.429 1.00 54.63  ? 797 HOH A O   1 
HETATM 8801 O  O   . HOH CA 13 .   ? 27.315  -15.778 33.395 1.00 51.94  ? 798 HOH A O   1 
HETATM 8802 O  O   . HOH CA 13 .   ? 71.909  5.269   53.596 1.00 62.62  ? 799 HOH A O   1 
HETATM 8803 O  O   . HOH CA 13 .   ? 29.605  -24.773 34.145 1.00 57.71  ? 800 HOH A O   1 
HETATM 8804 O  O   . HOH CA 13 .   ? 49.209  -17.635 30.873 1.00 45.38  ? 801 HOH A O   1 
HETATM 8805 O  O   . HOH CA 13 .   ? 59.638  -12.138 48.942 1.00 55.69  ? 802 HOH A O   1 
HETATM 8806 O  O   . HOH CA 13 .   ? 32.602  4.550   46.567 1.00 43.98  ? 803 HOH A O   1 
HETATM 8807 O  O   . HOH CA 13 .   ? 27.799  -3.237  14.145 1.00 53.29  ? 804 HOH A O   1 
HETATM 8808 O  O   . HOH CA 13 .   ? 55.528  -10.344 49.225 1.00 56.70  ? 805 HOH A O   1 
HETATM 8809 O  O   . HOH CA 13 .   ? 32.240  -22.590 48.127 1.00 40.96  ? 806 HOH A O   1 
HETATM 8810 O  O   . HOH CA 13 .   ? 25.845  -18.713 29.285 1.00 59.85  ? 807 HOH A O   1 
HETATM 8811 O  O   . HOH CA 13 .   ? 27.058  18.092  32.865 1.00 55.05  ? 808 HOH A O   1 
HETATM 8812 O  O   . HOH CA 13 .   ? 20.272  16.219  28.509 1.00 65.81  ? 809 HOH A O   1 
HETATM 8813 O  O   . HOH CA 13 .   ? 31.363  30.210  25.703 1.00 63.69  ? 810 HOH A O   1 
HETATM 8814 O  O   . HOH DA 13 .   ? 13.653  -10.440 66.681 1.00 58.70  ? 501 HOH B O   1 
HETATM 8815 O  O   . HOH DA 13 .   ? -5.722  11.405  78.935 1.00 56.21  ? 502 HOH B O   1 
HETATM 8816 O  O   . HOH DA 13 .   ? -9.383  -2.751  75.176 1.00 48.98  ? 503 HOH B O   1 
HETATM 8817 O  O   . HOH DA 13 .   ? 28.244  -7.409  53.919 1.00 30.36  ? 504 HOH B O   1 
HETATM 8818 O  O   . HOH DA 13 .   ? 5.563   11.806  70.900 1.00 56.78  ? 505 HOH B O   1 
HETATM 8819 O  O   . HOH DA 13 .   ? -3.283  4.516   56.764 1.00 44.76  ? 506 HOH B O   1 
HETATM 8820 O  O   . HOH DA 13 .   ? 12.173  4.493   68.213 1.00 46.35  ? 507 HOH B O   1 
HETATM 8821 O  O   . HOH DA 13 .   ? 22.940  -30.414 50.628 1.00 46.26  ? 508 HOH B O   1 
HETATM 8822 O  O   . HOH DA 13 .   ? 28.094  -9.644  51.749 1.00 31.86  ? 509 HOH B O   1 
HETATM 8823 O  O   . HOH DA 13 .   ? 7.344   10.526  66.445 1.00 47.85  ? 510 HOH B O   1 
HETATM 8824 O  O   . HOH DA 13 .   ? 16.355  -11.438 68.928 1.00 37.65  ? 511 HOH B O   1 
HETATM 8825 O  O   . HOH DA 13 .   ? 14.867  -8.261  75.141 1.00 37.90  ? 512 HOH B O   1 
HETATM 8826 O  O   . HOH DA 13 .   ? 17.639  -32.739 59.023 1.00 46.37  ? 513 HOH B O   1 
HETATM 8827 O  O   . HOH DA 13 .   ? 5.905   8.144   51.614 1.00 50.80  ? 514 HOH B O   1 
HETATM 8828 O  O   . HOH DA 13 .   ? 24.039  -22.728 51.506 1.00 34.11  ? 515 HOH B O   1 
HETATM 8829 O  O   . HOH DA 13 .   ? 9.604   -10.473 73.148 1.00 48.14  ? 516 HOH B O   1 
HETATM 8830 O  O   . HOH DA 13 .   ? 1.227   5.096   66.639 1.00 42.26  ? 517 HOH B O   1 
HETATM 8831 O  O   . HOH DA 13 .   ? -1.526  9.764   73.098 1.00 51.11  ? 518 HOH B O   1 
HETATM 8832 O  O   . HOH DA 13 .   ? -0.517  -22.161 74.053 1.00 47.35  ? 519 HOH B O   1 
HETATM 8833 O  O   . HOH DA 13 .   ? 24.796  -12.664 38.241 1.00 49.28  ? 520 HOH B O   1 
HETATM 8834 O  O   . HOH DA 13 .   ? 17.786  0.753   62.957 1.00 52.02  ? 521 HOH B O   1 
HETATM 8835 O  O   . HOH DA 13 .   ? -10.168 -2.649  64.759 1.00 42.84  ? 522 HOH B O   1 
HETATM 8836 O  O   . HOH DA 13 .   ? 18.987  -16.914 37.496 1.00 54.17  ? 523 HOH B O   1 
HETATM 8837 O  O   . HOH DA 13 .   ? 14.446  -7.621  66.187 1.00 39.18  ? 524 HOH B O   1 
HETATM 8838 O  O   . HOH DA 13 .   ? 3.105   5.126   68.579 1.00 44.78  ? 525 HOH B O   1 
HETATM 8839 O  O   . HOH DA 13 .   ? 23.728  -4.976  57.744 1.00 51.11  ? 526 HOH B O   1 
HETATM 8840 O  O   . HOH DA 13 .   ? 7.498   -9.485  66.377 1.00 48.58  ? 527 HOH B O   1 
HETATM 8841 O  O   . HOH DA 13 .   ? -5.343  -12.300 49.025 1.00 49.12  ? 528 HOH B O   1 
HETATM 8842 O  O   . HOH DA 13 .   ? -5.179  -10.425 42.406 1.00 51.58  ? 529 HOH B O   1 
HETATM 8843 O  O   . HOH DA 13 .   ? 1.442   -26.722 65.187 1.00 53.24  ? 530 HOH B O   1 
HETATM 8844 O  O   . HOH DA 13 .   ? 25.262  -22.635 49.026 1.00 47.20  ? 531 HOH B O   1 
HETATM 8845 O  O   . HOH DA 13 .   ? -3.630  3.286   54.570 1.00 41.18  ? 532 HOH B O   1 
HETATM 8846 O  O   . HOH DA 13 .   ? 18.578  -4.092  39.701 1.00 39.76  ? 533 HOH B O   1 
HETATM 8847 O  O   . HOH DA 13 .   ? 1.052   -19.472 49.292 1.00 43.56  ? 534 HOH B O   1 
HETATM 8848 O  O   . HOH DA 13 .   ? 19.628  4.969   49.694 1.00 39.70  ? 535 HOH B O   1 
HETATM 8849 O  O   . HOH DA 13 .   ? 16.840  -16.920 46.332 1.00 43.90  ? 536 HOH B O   1 
HETATM 8850 O  O   . HOH DA 13 .   ? -11.315 8.272   74.137 1.00 54.22  ? 537 HOH B O   1 
HETATM 8851 O  O   . HOH DA 13 .   ? 20.860  -6.532  71.308 1.00 44.62  ? 538 HOH B O   1 
HETATM 8852 O  O   . HOH DA 13 .   ? 11.732  -8.701  76.280 1.00 42.14  ? 539 HOH B O   1 
HETATM 8853 O  O   . HOH DA 13 .   ? -1.088  -12.004 78.071 1.00 55.24  ? 540 HOH B O   1 
HETATM 8854 O  O   . HOH DA 13 .   ? 12.403  -29.184 62.679 1.00 46.62  ? 541 HOH B O   1 
HETATM 8855 O  O   . HOH DA 13 .   ? 18.724  -19.732 47.719 1.00 39.66  ? 542 HOH B O   1 
HETATM 8856 O  O   . HOH DA 13 .   ? -2.551  7.066   59.406 1.00 44.70  ? 543 HOH B O   1 
HETATM 8857 O  O   . HOH DA 13 .   ? 14.037  -7.830  71.430 1.00 38.62  ? 544 HOH B O   1 
HETATM 8858 O  O   . HOH DA 13 .   ? 24.002  -3.245  52.498 1.00 54.06  ? 545 HOH B O   1 
HETATM 8859 O  O   . HOH DA 13 .   ? 25.163  -22.902 66.196 1.00 54.05  ? 546 HOH B O   1 
HETATM 8860 O  O   . HOH DA 13 .   ? 10.342  -7.367  35.907 1.00 51.69  ? 547 HOH B O   1 
HETATM 8861 O  O   . HOH DA 13 .   ? 7.358   -23.077 54.336 1.00 51.57  ? 548 HOH B O   1 
HETATM 8862 O  O   . HOH DA 13 .   ? -1.382  8.759   52.810 1.00 58.18  ? 549 HOH B O   1 
HETATM 8863 O  O   . HOH DA 13 .   ? 27.142  -18.537 66.572 1.00 44.76  ? 550 HOH B O   1 
HETATM 8864 O  O   . HOH DA 13 .   ? 5.553   -0.855  69.814 1.00 47.59  ? 551 HOH B O   1 
HETATM 8865 O  O   . HOH DA 13 .   ? 20.593  12.179  52.291 1.00 55.69  ? 552 HOH B O   1 
HETATM 8866 O  O   . HOH DA 13 .   ? 9.727   8.621   63.998 1.00 50.98  ? 553 HOH B O   1 
HETATM 8867 O  O   . HOH DA 13 .   ? 14.137  -27.552 42.818 1.00 61.46  ? 554 HOH B O   1 
HETATM 8868 O  O   . HOH DA 13 .   ? 8.248   0.485   42.680 1.00 57.28  ? 555 HOH B O   1 
HETATM 8869 O  O   . HOH DA 13 .   ? -1.832  -17.193 47.307 1.00 49.12  ? 556 HOH B O   1 
HETATM 8870 O  O   . HOH DA 13 .   ? 3.904   -31.773 67.685 1.00 53.47  ? 557 HOH B O   1 
HETATM 8871 O  O   . HOH DA 13 .   ? 22.932  -19.385 46.045 1.00 53.49  ? 558 HOH B O   1 
HETATM 8872 O  O   . HOH DA 13 .   ? 28.085  -27.079 61.178 1.00 40.89  ? 559 HOH B O   1 
HETATM 8873 O  O   . HOH DA 13 .   ? 20.926  -7.204  66.781 1.00 38.20  ? 560 HOH B O   1 
HETATM 8874 O  O   . HOH DA 13 .   ? 21.329  -0.015  51.063 1.00 31.58  ? 561 HOH B O   1 
HETATM 8875 O  O   . HOH DA 13 .   ? 9.509   13.524  64.287 1.00 55.26  ? 562 HOH B O   1 
HETATM 8876 O  O   . HOH DA 13 .   ? -12.162 -8.447  55.494 1.00 52.95  ? 563 HOH B O   1 
HETATM 8877 O  O   . HOH DA 13 .   ? 6.476   -19.383 47.701 1.00 44.67  ? 564 HOH B O   1 
HETATM 8878 O  O   . HOH DA 13 .   ? 29.519  -9.620  58.897 1.00 53.82  ? 565 HOH B O   1 
HETATM 8879 O  O   . HOH DA 13 .   ? 20.055  6.011   47.165 1.00 46.26  ? 566 HOH B O   1 
HETATM 8880 O  O   . HOH DA 13 .   ? -4.891  10.807  74.839 1.00 53.84  ? 567 HOH B O   1 
HETATM 8881 O  O   . HOH DA 13 .   ? 8.971   -13.901 46.958 1.00 33.63  ? 568 HOH B O   1 
HETATM 8882 O  O   . HOH DA 13 .   ? 5.133   1.179   47.416 1.00 44.53  ? 569 HOH B O   1 
HETATM 8883 O  O   . HOH DA 13 .   ? 0.371   0.453   74.634 1.00 53.28  ? 570 HOH B O   1 
HETATM 8884 O  O   . HOH DA 13 .   ? 11.582  -26.358 53.455 1.00 42.26  ? 571 HOH B O   1 
HETATM 8885 O  O   . HOH DA 13 .   ? 6.490   11.574  64.017 1.00 51.92  ? 572 HOH B O   1 
HETATM 8886 O  O   . HOH DA 13 .   ? 25.823  -13.321 49.541 1.00 44.90  ? 573 HOH B O   1 
HETATM 8887 O  O   . HOH DA 13 .   ? 7.084   5.640   62.628 1.00 38.54  ? 574 HOH B O   1 
HETATM 8888 O  O   . HOH DA 13 .   ? -2.389  -19.080 75.593 1.00 59.50  ? 575 HOH B O   1 
HETATM 8889 O  O   . HOH DA 13 .   ? 17.157  -15.994 42.877 1.00 59.70  ? 576 HOH B O   1 
HETATM 8890 O  O   . HOH DA 13 .   ? 20.381  -17.743 64.677 1.00 35.60  ? 577 HOH B O   1 
HETATM 8891 O  O   . HOH DA 13 .   ? 28.932  -18.771 59.364 1.00 49.31  ? 578 HOH B O   1 
HETATM 8892 O  O   . HOH DA 13 .   ? 19.490  -17.556 43.850 1.00 50.36  ? 579 HOH B O   1 
HETATM 8893 O  O   . HOH DA 13 .   ? -12.317 -0.959  64.122 1.00 43.67  ? 580 HOH B O   1 
HETATM 8894 O  O   . HOH DA 13 .   ? 10.317  -24.976 66.834 1.00 42.80  ? 581 HOH B O   1 
HETATM 8895 O  O   . HOH DA 13 .   ? 9.548   -4.436  39.071 1.00 41.71  ? 582 HOH B O   1 
HETATM 8896 O  O   . HOH DA 13 .   ? 7.779   -22.449 50.116 1.00 50.01  ? 583 HOH B O   1 
HETATM 8897 O  O   . HOH DA 13 .   ? 6.631   -2.791  70.195 1.00 49.85  ? 584 HOH B O   1 
HETATM 8898 O  O   . HOH DA 13 .   ? 0.584   -10.572 46.718 1.00 41.98  ? 585 HOH B O   1 
HETATM 8899 O  O   . HOH DA 13 .   ? 20.294  -30.072 49.523 1.00 46.07  ? 586 HOH B O   1 
HETATM 8900 O  O   . HOH DA 13 .   ? -17.036 -2.114  60.173 1.00 50.65  ? 587 HOH B O   1 
HETATM 8901 O  O   . HOH DA 13 .   ? 20.421  -33.910 59.769 1.00 44.39  ? 588 HOH B O   1 
HETATM 8902 O  O   . HOH DA 13 .   ? 16.680  6.501   64.087 1.00 49.27  ? 589 HOH B O   1 
HETATM 8903 O  O   . HOH DA 13 .   ? 9.925   9.265   53.145 1.00 49.91  ? 590 HOH B O   1 
HETATM 8904 O  O   . HOH DA 13 .   ? 25.857  -4.465  54.043 1.00 44.61  ? 591 HOH B O   1 
HETATM 8905 O  O   . HOH DA 13 .   ? 6.368   -1.710  74.050 1.00 48.34  ? 592 HOH B O   1 
HETATM 8906 O  O   . HOH DA 13 .   ? -12.471 1.687   64.120 1.00 51.83  ? 593 HOH B O   1 
HETATM 8907 O  O   . HOH DA 13 .   ? 16.714  3.759   62.751 1.00 46.23  ? 594 HOH B O   1 
HETATM 8908 O  O   . HOH DA 13 .   ? 22.182  8.713   58.536 1.00 54.41  ? 595 HOH B O   1 
HETATM 8909 O  O   . HOH DA 13 .   ? -9.280  -4.914  73.656 1.00 45.34  ? 596 HOH B O   1 
HETATM 8910 O  O   . HOH DA 13 .   ? 6.931   -19.853 43.932 1.00 43.74  ? 597 HOH B O   1 
HETATM 8911 O  O   . HOH DA 13 .   ? 5.030   -15.274 81.643 1.00 59.20  ? 598 HOH B O   1 
HETATM 8912 O  O   . HOH DA 13 .   ? -0.168  -16.628 52.051 1.00 50.47  ? 599 HOH B O   1 
HETATM 8913 O  O   . HOH DA 13 .   ? 21.439  -14.926 73.734 1.00 50.81  ? 600 HOH B O   1 
HETATM 8914 O  O   . HOH DA 13 .   ? -2.249  10.979  75.994 1.00 63.85  ? 601 HOH B O   1 
HETATM 8915 O  O   . HOH DA 13 .   ? -0.081  9.370   65.532 1.00 48.66  ? 602 HOH B O   1 
HETATM 8916 O  O   . HOH DA 13 .   ? 7.943   -2.842  66.879 1.00 39.07  ? 603 HOH B O   1 
HETATM 8917 O  O   . HOH DA 13 .   ? 19.018  -2.992  60.256 1.00 38.28  ? 604 HOH B O   1 
HETATM 8918 O  O   . HOH DA 13 .   ? 18.990  -14.791 72.541 1.00 39.54  ? 605 HOH B O   1 
HETATM 8919 O  O   . HOH DA 13 .   ? -7.790  -5.992  50.753 1.00 45.14  ? 606 HOH B O   1 
HETATM 8920 O  O   . HOH DA 13 .   ? 15.657  -13.442 33.910 1.00 50.94  ? 607 HOH B O   1 
HETATM 8921 O  O   . HOH DA 13 .   ? 18.658  2.286   48.564 1.00 41.42  ? 608 HOH B O   1 
HETATM 8922 O  O   . HOH DA 13 .   ? -6.766  -18.331 60.657 1.00 53.27  ? 609 HOH B O   1 
HETATM 8923 O  O   . HOH DA 13 .   ? 22.899  -17.397 70.448 1.00 54.55  ? 610 HOH B O   1 
HETATM 8924 O  O   . HOH DA 13 .   ? 28.638  -20.847 61.235 1.00 43.77  ? 611 HOH B O   1 
HETATM 8925 O  O   . HOH DA 13 .   ? 14.656  -8.719  63.695 1.00 43.66  ? 612 HOH B O   1 
HETATM 8926 O  O   . HOH DA 13 .   ? -13.127 3.029   66.966 1.00 37.93  ? 613 HOH B O   1 
HETATM 8927 O  O   . HOH DA 13 .   ? -17.385 -5.600  61.544 1.00 48.32  ? 614 HOH B O   1 
HETATM 8928 O  O   . HOH DA 13 .   ? 4.612   -21.845 84.055 1.00 58.82  ? 615 HOH B O   1 
HETATM 8929 O  O   . HOH DA 13 .   ? 2.802   -16.722 62.281 1.00 51.47  ? 616 HOH B O   1 
HETATM 8930 O  O   . HOH DA 13 .   ? -6.911  -13.596 77.440 1.00 56.18  ? 617 HOH B O   1 
HETATM 8931 O  O   . HOH DA 13 .   ? 11.266  -32.003 59.229 1.00 61.00  ? 618 HOH B O   1 
HETATM 8932 O  O   . HOH DA 13 .   ? -16.242 -10.478 62.145 1.00 51.27  ? 619 HOH B O   1 
HETATM 8933 O  O   . HOH DA 13 .   ? 6.219   -0.635  45.403 1.00 42.27  ? 620 HOH B O   1 
HETATM 8934 O  O   . HOH DA 13 .   ? -13.528 -15.251 67.043 1.00 61.22  ? 621 HOH B O   1 
HETATM 8935 O  O   . HOH DA 13 .   ? 23.485  -31.655 64.785 1.00 49.92  ? 622 HOH B O   1 
HETATM 8936 O  O   . HOH DA 13 .   ? 14.349  -6.377  76.853 1.00 50.71  ? 623 HOH B O   1 
HETATM 8937 O  O   . HOH DA 13 .   ? 13.056  -2.923  58.929 1.00 33.80  ? 624 HOH B O   1 
HETATM 8938 O  O   . HOH DA 13 .   ? 28.306  -14.377 53.982 1.00 52.02  ? 625 HOH B O   1 
HETATM 8939 O  O   . HOH DA 13 .   ? -13.846 -12.324 68.204 1.00 47.55  ? 626 HOH B O   1 
HETATM 8940 O  O   . HOH DA 13 .   ? -1.679  4.636   53.441 1.00 46.94  ? 627 HOH B O   1 
HETATM 8941 O  O   . HOH DA 13 .   ? -3.362  -4.941  75.942 1.00 53.91  ? 628 HOH B O   1 
HETATM 8942 O  O   . HOH DA 13 .   ? 25.374  -3.999  67.816 1.00 60.06  ? 629 HOH B O   1 
HETATM 8943 O  O   . HOH DA 13 .   ? 9.272   -30.437 47.506 1.00 64.91  ? 630 HOH B O   1 
HETATM 8944 O  O   . HOH DA 13 .   ? 19.524  -12.512 71.073 1.00 39.74  ? 631 HOH B O   1 
HETATM 8945 O  O   . HOH DA 13 .   ? 20.711  -5.639  57.426 1.00 40.16  ? 632 HOH B O   1 
HETATM 8946 O  O   . HOH DA 13 .   ? 23.691  -21.335 72.448 1.00 63.96  ? 633 HOH B O   1 
HETATM 8947 O  O   . HOH DA 13 .   ? 2.373   -0.543  72.958 1.00 45.94  ? 634 HOH B O   1 
HETATM 8948 O  O   . HOH DA 13 .   ? -14.591 -2.287  54.704 1.00 65.96  ? 635 HOH B O   1 
HETATM 8949 O  O   . HOH DA 13 .   ? 17.772  5.495   40.951 1.00 58.72  ? 636 HOH B O   1 
HETATM 8950 O  O   . HOH DA 13 .   ? 0.702   -23.757 57.605 1.00 51.81  ? 637 HOH B O   1 
HETATM 8951 O  O   . HOH DA 13 .   ? 10.413  -28.419 75.504 1.00 55.41  ? 638 HOH B O   1 
HETATM 8952 O  O   . HOH DA 13 .   ? -11.247 -16.995 64.966 1.00 59.83  ? 639 HOH B O   1 
HETATM 8953 O  O   . HOH DA 13 .   ? 0.452   -4.491  44.784 1.00 53.59  ? 640 HOH B O   1 
HETATM 8954 O  O   . HOH DA 13 .   ? 4.021   -17.197 37.158 1.00 51.43  ? 641 HOH B O   1 
HETATM 8955 O  O   . HOH DA 13 .   ? 6.749   3.032   47.605 1.00 46.47  ? 642 HOH B O   1 
HETATM 8956 O  O   . HOH DA 13 .   ? 2.522   -8.192  72.345 1.00 43.74  ? 643 HOH B O   1 
HETATM 8957 O  O   . HOH DA 13 .   ? 31.543  -15.693 60.353 1.00 56.58  ? 644 HOH B O   1 
HETATM 8958 O  O   . HOH DA 13 .   ? 17.835  -1.610  70.383 1.00 51.08  ? 645 HOH B O   1 
HETATM 8959 O  O   . HOH DA 13 .   ? 2.852   -4.096  75.547 1.00 56.35  ? 646 HOH B O   1 
HETATM 8960 O  O   . HOH DA 13 .   ? 3.171   -6.944  74.921 1.00 57.15  ? 647 HOH B O   1 
HETATM 8961 O  O   . HOH DA 13 .   ? 16.802  -27.603 68.405 1.00 61.73  ? 648 HOH B O   1 
HETATM 8962 O  O   . HOH DA 13 .   ? -0.317  -22.353 69.722 1.00 44.39  ? 649 HOH B O   1 
HETATM 8963 O  O   . HOH DA 13 .   ? 22.613  -4.267  59.980 1.00 45.50  ? 650 HOH B O   1 
HETATM 8964 O  O   . HOH DA 13 .   ? 21.456  3.198   40.341 1.00 45.59  ? 651 HOH B O   1 
HETATM 8965 O  O   . HOH DA 13 .   ? 6.375   -10.916 73.837 1.00 42.66  ? 652 HOH B O   1 
HETATM 8966 O  O   . HOH DA 13 .   ? -17.057 -8.167  63.254 1.00 51.65  ? 653 HOH B O   1 
HETATM 8967 O  O   . HOH DA 13 .   ? 28.395  -14.767 56.374 1.00 41.40  ? 654 HOH B O   1 
HETATM 8968 O  O   . HOH DA 13 .   ? 14.560  1.856   34.588 1.00 52.99  ? 655 HOH B O   1 
HETATM 8969 O  O   . HOH DA 13 .   ? -2.093  -11.102 47.490 1.00 38.24  ? 656 HOH B O   1 
HETATM 8970 O  O   . HOH DA 13 .   ? 4.803   -9.294  72.019 1.00 46.55  ? 657 HOH B O   1 
HETATM 8971 O  O   . HOH DA 13 .   ? 6.997   -7.873  71.585 1.00 50.89  ? 658 HOH B O   1 
HETATM 8972 O  O   . HOH DA 13 .   ? -6.090  -2.001  45.062 1.00 50.41  ? 659 HOH B O   1 
HETATM 8973 O  O   . HOH DA 13 .   ? 18.392  3.382   60.628 1.00 47.08  ? 660 HOH B O   1 
HETATM 8974 O  O   . HOH DA 13 .   ? 14.961  5.329   67.887 1.00 54.28  ? 661 HOH B O   1 
HETATM 8975 O  O   . HOH DA 13 .   ? 1.005   -22.010 59.279 1.00 54.17  ? 662 HOH B O   1 
HETATM 8976 O  O   . HOH DA 13 .   ? 20.501  -4.356  41.884 1.00 50.29  ? 663 HOH B O   1 
HETATM 8977 O  O   . HOH DA 13 .   ? -7.317  17.966  64.191 1.00 57.95  ? 664 HOH B O   1 
HETATM 8978 O  O   . HOH DA 13 .   ? 23.222  -13.792 46.885 1.00 49.51  ? 665 HOH B O   1 
HETATM 8979 O  O   . HOH DA 13 .   ? 23.343  -7.353  67.618 1.00 36.36  ? 666 HOH B O   1 
HETATM 8980 O  O   . HOH DA 13 .   ? 22.635  6.031   47.161 1.00 51.29  ? 667 HOH B O   1 
HETATM 8981 O  O   . HOH DA 13 .   ? 18.457  -1.801  73.149 1.00 57.21  ? 668 HOH B O   1 
HETATM 8982 O  O   . HOH DA 13 .   ? 18.215  -6.541  56.130 1.00 34.46  ? 669 HOH B O   1 
HETATM 8983 O  O   . HOH DA 13 .   ? 9.936   -11.137 34.514 1.00 52.06  ? 670 HOH B O   1 
HETATM 8984 O  O   . HOH DA 13 .   ? 6.723   -23.872 76.918 1.00 57.08  ? 671 HOH B O   1 
HETATM 8985 O  O   . HOH DA 13 .   ? 24.709  10.989  51.931 1.00 53.25  ? 672 HOH B O   1 
HETATM 8986 O  O   . HOH DA 13 .   ? 21.575  -28.368 45.185 1.00 58.19  ? 673 HOH B O   1 
HETATM 8987 O  O   . HOH DA 13 .   ? -7.463  -10.348 49.501 1.00 51.68  ? 674 HOH B O   1 
HETATM 8988 O  O   . HOH DA 13 .   ? 9.155   -27.654 49.037 1.00 56.16  ? 675 HOH B O   1 
HETATM 8989 O  O   . HOH DA 13 .   ? 14.137  -17.517 33.728 1.00 53.61  ? 676 HOH B O   1 
HETATM 8990 O  O   . HOH DA 13 .   ? 24.587  -4.004  71.566 1.00 54.76  ? 677 HOH B O   1 
HETATM 8991 O  O   . HOH DA 13 .   ? 21.008  -9.189  38.720 1.00 49.91  ? 678 HOH B O   1 
HETATM 8992 O  O   . HOH DA 13 .   ? -16.220 -13.062 64.107 1.00 56.42  ? 679 HOH B O   1 
HETATM 8993 O  O   . HOH DA 13 .   ? 25.183  -6.627  66.094 1.00 52.88  ? 680 HOH B O   1 
HETATM 8994 O  O   . HOH DA 13 .   ? 12.190  -26.789 40.856 1.00 66.58  ? 681 HOH B O   1 
HETATM 8995 O  O   . HOH DA 13 .   ? 20.440  -22.501 75.835 1.00 62.81  ? 682 HOH B O   1 
HETATM 8996 O  O   . HOH DA 13 .   ? 8.959   -7.996  75.271 1.00 61.38  ? 683 HOH B O   1 
HETATM 8997 O  O   . HOH DA 13 .   ? -2.034  -3.841  40.844 1.00 58.01  ? 684 HOH B O   1 
HETATM 8998 O  O   . HOH DA 13 .   ? 7.207   -32.472 64.487 1.00 60.71  ? 685 HOH B O   1 
HETATM 8999 O  O   . HOH DA 13 .   ? 7.863   -30.578 55.175 1.00 56.27  ? 686 HOH B O   1 
HETATM 9000 O  O   . HOH DA 13 .   ? 15.205  5.855   42.970 1.00 55.54  ? 687 HOH B O   1 
HETATM 9001 O  O   . HOH DA 13 .   ? 8.054   -10.375 86.147 1.00 60.17  ? 688 HOH B O   1 
HETATM 9002 O  O   . HOH DA 13 .   ? 13.011  -22.417 82.009 1.00 49.73  ? 689 HOH B O   1 
HETATM 9003 O  O   . HOH DA 13 .   ? 30.020  -11.143 69.277 1.00 56.33  ? 690 HOH B O   1 
HETATM 9004 O  O   . HOH DA 13 .   ? -14.541 2.019   62.077 1.00 49.99  ? 691 HOH B O   1 
HETATM 9005 O  O   . HOH DA 13 .   ? 3.579   5.362   45.913 1.00 60.38  ? 692 HOH B O   1 
HETATM 9006 O  O   . HOH DA 13 .   ? -11.348 15.137  61.530 1.00 60.12  ? 693 HOH B O   1 
HETATM 9007 O  O   . HOH DA 13 .   ? 3.432   2.871   46.162 1.00 47.24  ? 694 HOH B O   1 
HETATM 9008 O  O   . HOH DA 13 .   ? 16.081  0.602   69.408 1.00 62.11  ? 695 HOH B O   1 
HETATM 9009 O  O   . HOH DA 13 .   ? 30.826  -12.669 56.579 1.00 44.50  ? 696 HOH B O   1 
HETATM 9010 O  O   . HOH DA 13 .   ? 16.572  2.928   68.024 1.00 50.58  ? 697 HOH B O   1 
HETATM 9011 O  O   . HOH DA 13 .   ? 1.131   10.466  53.177 1.00 60.70  ? 698 HOH B O   1 
HETATM 9012 O  O   . HOH DA 13 .   ? 5.710   -9.037  75.864 1.00 54.78  ? 699 HOH B O   1 
HETATM 9013 O  O   . HOH DA 13 .   ? 19.969  -20.508 86.589 1.00 58.29  ? 700 HOH B O   1 
HETATM 9014 O  O   . HOH DA 13 .   ? 27.258  -21.114 65.662 1.00 44.92  ? 701 HOH B O   1 
HETATM 9015 O  O   . HOH DA 13 .   ? 2.051   -27.790 67.660 1.00 56.65  ? 702 HOH B O   1 
HETATM 9016 O  O   . HOH DA 13 .   ? -18.535 9.370   70.006 1.00 61.96  ? 703 HOH B O   1 
HETATM 9017 O  O   . HOH DA 13 .   ? 17.221  1.658   34.012 1.00 59.20  ? 704 HOH B O   1 
HETATM 9018 O  O   . HOH DA 13 .   ? 19.972  -1.302  61.854 1.00 46.90  ? 705 HOH B O   1 
HETATM 9019 O  O   . HOH DA 13 .   ? -1.510  6.384   51.250 1.00 55.61  ? 706 HOH B O   1 
HETATM 9020 O  O   . HOH DA 13 .   ? 16.529  -19.815 40.166 1.00 59.27  ? 707 HOH B O   1 
HETATM 9021 O  O   . HOH DA 13 .   ? 20.239  13.517  57.636 1.00 64.10  ? 708 HOH B O   1 
HETATM 9022 O  O   . HOH DA 13 .   ? 11.462  -22.794 84.892 1.00 61.81  ? 709 HOH B O   1 
HETATM 9023 O  O   . HOH DA 13 .   ? -9.795  -21.092 77.614 1.00 64.75  ? 710 HOH B O   1 
HETATM 9024 O  O   . HOH DA 13 .   ? -11.183 -21.386 74.104 1.00 64.60  ? 711 HOH B O   1 
HETATM 9025 O  O   . HOH DA 13 .   ? -4.899  13.835  70.935 1.00 59.93  ? 712 HOH B O   1 
HETATM 9026 O  O   . HOH DA 13 .   ? 21.670  -10.864 36.989 1.00 54.41  ? 713 HOH B O   1 
HETATM 9027 O  O   . HOH DA 13 .   ? 6.261   1.359   73.951 1.00 52.64  ? 714 HOH B O   1 
HETATM 9028 O  O   . HOH DA 13 .   ? -18.030 -10.477 59.489 1.00 58.08  ? 715 HOH B O   1 
HETATM 9029 O  O   . HOH DA 13 .   ? -2.098  -17.817 42.654 1.00 58.39  ? 716 HOH B O   1 
HETATM 9030 O  O   . HOH DA 13 .   ? 28.820  -6.227  56.208 1.00 43.56  ? 717 HOH B O   1 
HETATM 9031 O  O   . HOH DA 13 .   ? 18.375  7.610   62.628 1.00 55.12  ? 718 HOH B O   1 
HETATM 9032 O  O   . HOH DA 13 .   ? 3.635   -14.046 60.768 1.00 64.09  ? 719 HOH B O   1 
HETATM 9033 O  O   . HOH DA 13 .   ? 19.328  -32.487 48.081 1.00 56.46  ? 720 HOH B O   1 
HETATM 9034 O  O   . HOH DA 13 .   ? 23.188  -16.592 73.255 1.00 53.70  ? 721 HOH B O   1 
HETATM 9035 O  O   . HOH DA 13 .   ? -5.238  13.839  76.899 1.00 65.02  ? 722 HOH B O   1 
HETATM 9036 O  O   . HOH DA 13 .   ? -16.800 -8.703  56.089 1.00 52.00  ? 723 HOH B O   1 
HETATM 9037 O  O   . HOH DA 13 .   ? 9.176   -3.738  77.263 1.00 59.20  ? 724 HOH B O   1 
HETATM 9038 O  O   . HOH DA 13 .   ? 11.401  -23.624 80.660 1.00 61.42  ? 725 HOH B O   1 
HETATM 9039 O  O   . HOH DA 13 .   ? 31.995  -10.083 60.612 1.00 60.10  ? 726 HOH B O   1 
HETATM 9040 O  O   . HOH DA 13 .   ? -7.348  -2.945  77.519 1.00 57.27  ? 727 HOH B O   1 
HETATM 9041 O  O   . HOH DA 13 .   ? 16.778  13.340  58.924 1.00 53.78  ? 728 HOH B O   1 
HETATM 9042 O  O   . HOH DA 13 .   ? -4.055  -12.935 46.792 1.00 53.04  ? 729 HOH B O   1 
HETATM 9043 O  O   . HOH DA 13 .   ? 28.109  -7.501  60.135 1.00 53.57  ? 730 HOH B O   1 
HETATM 9044 O  O   . HOH DA 13 .   ? 17.294  -19.853 42.944 1.00 57.14  ? 731 HOH B O   1 
HETATM 9045 O  O   . HOH DA 13 .   ? 11.189  6.489   70.138 1.00 52.47  ? 732 HOH B O   1 
HETATM 9046 O  O   . HOH DA 13 .   ? 26.262  -5.980  58.977 1.00 48.15  ? 733 HOH B O   1 
HETATM 9047 O  O   . HOH DA 13 .   ? -5.286  -12.347 44.353 1.00 53.71  ? 734 HOH B O   1 
HETATM 9048 O  O   . HOH DA 13 .   ? -3.706  -15.593 46.993 1.00 53.18  ? 735 HOH B O   1 
HETATM 9049 O  O   . HOH DA 13 .   ? 13.409  -6.734  33.245 1.00 56.80  ? 736 HOH B O   1 
HETATM 9050 O  O   . HOH DA 13 .   ? -11.356 5.233   48.946 1.00 59.66  ? 737 HOH B O   1 
HETATM 9051 O  O   . HOH DA 13 .   ? 8.767   6.884   74.162 1.00 59.63  ? 738 HOH B O   1 
HETATM 9052 O  O   . HOH DA 13 .   ? -2.139  16.621  73.205 1.00 60.75  ? 739 HOH B O   1 
HETATM 9053 O  O   . HOH DA 13 .   ? 8.096   -19.085 35.515 1.00 56.75  ? 740 HOH B O   1 
HETATM 9054 O  O   . HOH DA 13 .   ? -0.952  -6.828  79.460 1.00 61.42  ? 741 HOH B O   1 
HETATM 9055 O  O   . HOH DA 13 .   ? 22.103  -0.636  57.870 1.00 50.17  ? 742 HOH B O   1 
HETATM 9056 O  O   . HOH DA 13 .   ? 21.858  -8.123  84.113 1.00 62.62  ? 743 HOH B O   1 
HETATM 9057 O  O   . HOH DA 13 .   ? 25.257  -0.131  55.957 1.00 56.25  ? 744 HOH B O   1 
HETATM 9058 O  O   . HOH DA 13 .   ? -8.984  -22.847 80.133 1.00 68.53  ? 745 HOH B O   1 
HETATM 9059 O  O   . HOH DA 13 .   ? 14.875  -40.437 50.605 1.00 65.21  ? 746 HOH B O   1 
HETATM 9060 O  O   . HOH EA 13 .   ? 18.608  -4.408  24.362 1.00 40.03  ? 501 HOH C O   1 
HETATM 9061 O  O   . HOH EA 13 .   ? -23.362 15.650  9.966  1.00 48.07  ? 502 HOH C O   1 
HETATM 9062 O  O   . HOH EA 13 .   ? 4.859   -2.887  34.243 1.00 57.44  ? 503 HOH C O   1 
HETATM 9063 O  O   . HOH EA 13 .   ? -0.555  -10.187 16.752 1.00 48.87  ? 504 HOH C O   1 
HETATM 9064 O  O   . HOH EA 13 .   ? -10.811 29.495  12.457 1.00 60.49  ? 505 HOH C O   1 
HETATM 9065 O  O   . HOH EA 13 .   ? -7.854  13.172  26.247 1.00 54.10  ? 506 HOH C O   1 
HETATM 9066 O  O   . HOH EA 13 .   ? 16.269  10.139  12.862 1.00 57.76  ? 507 HOH C O   1 
HETATM 9067 O  O   . HOH EA 13 .   ? -2.267  13.320  21.516 1.00 58.13  ? 508 HOH C O   1 
HETATM 9068 O  O   . HOH EA 13 .   ? 12.268  3.277   14.380 1.00 38.43  ? 509 HOH C O   1 
HETATM 9069 O  O   . HOH EA 13 .   ? -13.142 13.120  3.212  1.00 43.41  ? 510 HOH C O   1 
HETATM 9070 O  O   . HOH EA 13 .   ? -0.389  17.828  31.190 1.00 43.70  ? 511 HOH C O   1 
HETATM 9071 O  O   . HOH EA 13 .   ? 2.085   6.914   26.966 1.00 48.99  ? 512 HOH C O   1 
HETATM 9072 O  O   . HOH EA 13 .   ? -11.738 4.515   29.886 1.00 55.53  ? 513 HOH C O   1 
HETATM 9073 O  O   . HOH EA 13 .   ? 7.354   32.429  33.162 1.00 61.04  ? 514 HOH C O   1 
HETATM 9074 O  O   . HOH EA 13 .   ? -5.238  -3.234  4.024  1.00 47.14  ? 515 HOH C O   1 
HETATM 9075 O  O   . HOH EA 13 .   ? 22.493  -4.919  19.056 1.00 40.45  ? 516 HOH C O   1 
HETATM 9076 O  O   . HOH EA 13 .   ? -20.554 -4.204  23.494 1.00 44.25  ? 517 HOH C O   1 
HETATM 9077 O  O   . HOH EA 13 .   ? 7.404   3.309   4.324  1.00 35.09  ? 518 HOH C O   1 
HETATM 9078 O  O   . HOH EA 13 .   ? -3.452  -3.119  29.811 1.00 45.49  ? 519 HOH C O   1 
HETATM 9079 O  O   . HOH EA 13 .   ? -1.794  5.978   1.256  1.00 40.20  ? 520 HOH C O   1 
HETATM 9080 O  O   . HOH EA 13 .   ? 2.735   -5.049  16.177 1.00 37.61  ? 521 HOH C O   1 
HETATM 9081 O  O   . HOH EA 13 .   ? 10.867  -2.166  30.630 1.00 47.10  ? 522 HOH C O   1 
HETATM 9082 O  O   . HOH EA 13 .   ? 2.396   -2.075  5.527  1.00 47.25  ? 523 HOH C O   1 
HETATM 9083 O  O   . HOH EA 13 .   ? 3.885   -6.284  19.382 1.00 36.49  ? 524 HOH C O   1 
HETATM 9084 O  O   . HOH EA 13 .   ? 4.749   -0.504  25.585 1.00 36.04  ? 525 HOH C O   1 
HETATM 9085 O  O   . HOH EA 13 .   ? -25.741 21.096  13.880 1.00 61.06  ? 526 HOH C O   1 
HETATM 9086 O  O   . HOH EA 13 .   ? 14.146  8.456   4.535  1.00 38.60  ? 527 HOH C O   1 
HETATM 9087 O  O   . HOH EA 13 .   ? -1.811  7.830   25.705 1.00 39.49  ? 528 HOH C O   1 
HETATM 9088 O  O   . HOH EA 13 .   ? -8.368  17.790  27.415 1.00 50.65  ? 529 HOH C O   1 
HETATM 9089 O  O   . HOH EA 13 .   ? -18.401 -2.202  6.191  1.00 52.20  ? 530 HOH C O   1 
HETATM 9090 O  O   . HOH EA 13 .   ? 1.676   -5.374  13.642 1.00 38.26  ? 531 HOH C O   1 
HETATM 9091 O  O   . HOH EA 13 .   ? 1.205   9.191   27.093 1.00 54.01  ? 532 HOH C O   1 
HETATM 9092 O  O   . HOH EA 13 .   ? 5.364   -1.163  7.050  1.00 41.64  ? 533 HOH C O   1 
HETATM 9093 O  O   . HOH EA 13 .   ? -4.323  -9.091  14.313 1.00 41.12  ? 534 HOH C O   1 
HETATM 9094 O  O   . HOH EA 13 .   ? 4.193   0.779   27.970 1.00 33.34  ? 535 HOH C O   1 
HETATM 9095 O  O   . HOH EA 13 .   ? -14.938 8.534   7.058  1.00 39.18  ? 536 HOH C O   1 
HETATM 9096 O  O   . HOH EA 13 .   ? -7.768  13.175  1.638  1.00 47.26  ? 537 HOH C O   1 
HETATM 9097 O  O   . HOH EA 13 .   ? -21.310 0.805   22.780 1.00 43.20  ? 538 HOH C O   1 
HETATM 9098 O  O   . HOH EA 13 .   ? -4.622  15.354  29.582 1.00 47.96  ? 539 HOH C O   1 
HETATM 9099 O  O   . HOH EA 13 .   ? 16.661  -8.437  29.651 1.00 59.59  ? 540 HOH C O   1 
HETATM 9100 O  O   . HOH EA 13 .   ? 0.984   8.185   3.020  1.00 41.15  ? 541 HOH C O   1 
HETATM 9101 O  O   . HOH EA 13 .   ? 15.206  -0.667  8.249  1.00 47.84  ? 542 HOH C O   1 
HETATM 9102 O  O   . HOH EA 13 .   ? -9.599  12.731  23.900 1.00 50.40  ? 543 HOH C O   1 
HETATM 9103 O  O   . HOH EA 13 .   ? -2.931  -3.165  0.840  1.00 43.16  ? 544 HOH C O   1 
HETATM 9104 O  O   . HOH EA 13 .   ? -26.722 11.145  14.109 1.00 62.95  ? 545 HOH C O   1 
HETATM 9105 O  O   . HOH EA 13 .   ? -14.403 6.492   29.376 1.00 55.24  ? 546 HOH C O   1 
HETATM 9106 O  O   . HOH EA 13 .   ? -27.254 2.733   9.016  1.00 56.57  ? 547 HOH C O   1 
HETATM 9107 O  O   . HOH EA 13 .   ? -13.137 17.338  4.378  1.00 51.95  ? 548 HOH C O   1 
HETATM 9108 O  O   . HOH EA 13 .   ? 16.158  9.681   20.045 1.00 44.88  ? 549 HOH C O   1 
HETATM 9109 O  O   . HOH EA 13 .   ? 1.863   0.419   4.724  1.00 34.50  ? 550 HOH C O   1 
HETATM 9110 O  O   . HOH EA 13 .   ? -2.517  -1.454  26.340 1.00 39.33  ? 551 HOH C O   1 
HETATM 9111 O  O   . HOH EA 13 .   ? -3.539  2.921   32.485 1.00 47.64  ? 552 HOH C O   1 
HETATM 9112 O  O   . HOH EA 13 .   ? -0.717  17.441  27.011 1.00 60.39  ? 553 HOH C O   1 
HETATM 9113 O  O   . HOH EA 13 .   ? -9.956  20.219  30.037 1.00 58.27  ? 554 HOH C O   1 
HETATM 9114 O  O   . HOH EA 13 .   ? 1.154   -5.982  5.074  1.00 51.37  ? 555 HOH C O   1 
HETATM 9115 O  O   . HOH EA 13 .   ? 13.803  1.198   13.790 1.00 36.15  ? 556 HOH C O   1 
HETATM 9116 O  O   . HOH EA 13 .   ? -9.825  -5.062  12.304 1.00 46.57  ? 557 HOH C O   1 
HETATM 9117 O  O   . HOH EA 13 .   ? -6.180  27.440  16.292 1.00 59.00  ? 558 HOH C O   1 
HETATM 9118 O  O   . HOH EA 13 .   ? -14.780 22.126  23.345 1.00 59.51  ? 559 HOH C O   1 
HETATM 9119 O  O   . HOH EA 13 .   ? -28.152 9.311   12.773 1.00 55.63  ? 560 HOH C O   1 
HETATM 9120 O  O   . HOH EA 13 .   ? 11.611  -11.004 26.466 1.00 45.45  ? 561 HOH C O   1 
HETATM 9121 O  O   . HOH EA 13 .   ? -9.935  -8.488  22.351 1.00 54.02  ? 562 HOH C O   1 
HETATM 9122 O  O   . HOH EA 13 .   ? 1.024   2.674   2.061  1.00 41.19  ? 563 HOH C O   1 
HETATM 9123 O  O   . HOH EA 13 .   ? 19.251  1.795   23.220 1.00 36.94  ? 564 HOH C O   1 
HETATM 9124 O  O   . HOH EA 13 .   ? -23.048 1.439   25.291 1.00 38.92  ? 565 HOH C O   1 
HETATM 9125 O  O   . HOH EA 13 .   ? -5.068  -0.400  -2.121 1.00 48.58  ? 566 HOH C O   1 
HETATM 9126 O  O   . HOH EA 13 .   ? 16.431  -1.214  16.755 1.00 39.62  ? 567 HOH C O   1 
HETATM 9127 O  O   . HOH EA 13 .   ? 14.293  3.969   32.490 1.00 52.44  ? 568 HOH C O   1 
HETATM 9128 O  O   . HOH EA 13 .   ? -12.782 -1.018  2.221  1.00 56.71  ? 569 HOH C O   1 
HETATM 9129 O  O   . HOH EA 13 .   ? -12.136 -4.112  10.833 1.00 45.58  ? 570 HOH C O   1 
HETATM 9130 O  O   . HOH EA 13 .   ? 18.985  2.295   27.880 1.00 55.33  ? 571 HOH C O   1 
HETATM 9131 O  O   . HOH EA 13 .   ? 10.774  -2.209  5.244  1.00 48.61  ? 572 HOH C O   1 
HETATM 9132 O  O   . HOH EA 13 .   ? -4.570  11.677  4.307  1.00 51.21  ? 573 HOH C O   1 
HETATM 9133 O  O   . HOH EA 13 .   ? 0.289   -4.297  31.673 1.00 57.36  ? 574 HOH C O   1 
HETATM 9134 O  O   . HOH EA 13 .   ? -10.318 5.454   22.939 1.00 38.60  ? 575 HOH C O   1 
HETATM 9135 O  O   . HOH EA 13 .   ? -0.236  -6.025  29.744 1.00 44.02  ? 576 HOH C O   1 
HETATM 9136 O  O   . HOH EA 13 .   ? 16.847  4.367   28.617 1.00 54.71  ? 577 HOH C O   1 
HETATM 9137 O  O   . HOH EA 13 .   ? 14.143  -1.361  14.886 1.00 35.70  ? 578 HOH C O   1 
HETATM 9138 O  O   . HOH EA 13 .   ? -9.534  0.041   32.314 1.00 56.41  ? 579 HOH C O   1 
HETATM 9139 O  O   . HOH EA 13 .   ? 18.180  -11.429 23.347 1.00 46.28  ? 580 HOH C O   1 
HETATM 9140 O  O   . HOH EA 13 .   ? -9.497  1.476   -4.410 1.00 35.21  ? 581 HOH C O   1 
HETATM 9141 O  O   . HOH EA 13 .   ? -17.747 8.981   28.199 1.00 59.01  ? 582 HOH C O   1 
HETATM 9142 O  O   . HOH EA 13 .   ? -23.717 -5.665  24.049 1.00 52.11  ? 583 HOH C O   1 
HETATM 9143 O  O   . HOH EA 13 .   ? -16.343 23.279  -0.433 1.00 68.54  ? 584 HOH C O   1 
HETATM 9144 O  O   . HOH EA 13 .   ? -21.434 -6.321  22.410 1.00 53.06  ? 585 HOH C O   1 
HETATM 9145 O  O   . HOH EA 13 .   ? -7.716  4.107   3.719  1.00 34.93  ? 586 HOH C O   1 
HETATM 9146 O  O   . HOH EA 13 .   ? -0.550  -6.725  14.705 1.00 37.51  ? 587 HOH C O   1 
HETATM 9147 O  O   . HOH EA 13 .   ? 6.533   7.646   27.806 1.00 46.75  ? 588 HOH C O   1 
HETATM 9148 O  O   . HOH EA 13 .   ? 5.490   -4.797  26.311 1.00 43.30  ? 589 HOH C O   1 
HETATM 9149 O  O   . HOH EA 13 .   ? -20.328 -2.935  21.050 1.00 42.84  ? 590 HOH C O   1 
HETATM 9150 O  O   . HOH EA 13 .   ? 22.231  0.130   16.333 1.00 44.19  ? 591 HOH C O   1 
HETATM 9151 O  O   . HOH EA 13 .   ? -15.349 12.296  1.263  1.00 53.98  ? 592 HOH C O   1 
HETATM 9152 O  O   . HOH EA 13 .   ? -8.188  -2.129  5.525  1.00 48.98  ? 593 HOH C O   1 
HETATM 9153 O  O   . HOH EA 13 .   ? -13.800 -7.087  14.687 1.00 58.43  ? 594 HOH C O   1 
HETATM 9154 O  O   . HOH EA 13 .   ? 2.959   15.280  24.209 1.00 48.74  ? 595 HOH C O   1 
HETATM 9155 O  O   . HOH EA 13 .   ? -17.739 8.295   24.615 1.00 48.95  ? 596 HOH C O   1 
HETATM 9156 O  O   . HOH EA 13 .   ? -27.038 4.600   13.893 1.00 53.21  ? 597 HOH C O   1 
HETATM 9157 O  O   . HOH EA 13 .   ? 9.129   7.164   28.442 1.00 50.96  ? 598 HOH C O   1 
HETATM 9158 O  O   . HOH EA 13 .   ? -5.033  4.267   2.883  1.00 34.10  ? 599 HOH C O   1 
HETATM 9159 O  O   . HOH EA 13 .   ? 13.940  -8.417  28.369 1.00 54.40  ? 600 HOH C O   1 
HETATM 9160 O  O   . HOH EA 13 .   ? 22.048  -5.665  16.351 1.00 42.04  ? 601 HOH C O   1 
HETATM 9161 O  O   . HOH EA 13 .   ? -22.603 14.163  7.083  1.00 48.89  ? 602 HOH C O   1 
HETATM 9162 O  O   . HOH EA 13 .   ? -21.466 -11.080 24.102 1.00 64.19  ? 603 HOH C O   1 
HETATM 9163 O  O   . HOH EA 13 .   ? -11.312 -2.789  0.513  1.00 42.30  ? 604 HOH C O   1 
HETATM 9164 O  O   . HOH EA 13 .   ? -1.663  10.057  12.537 1.00 58.01  ? 605 HOH C O   1 
HETATM 9165 O  O   . HOH EA 13 .   ? 5.178   13.952  23.720 1.00 48.63  ? 606 HOH C O   1 
HETATM 9166 O  O   . HOH EA 13 .   ? 5.469   -7.012  27.441 1.00 53.40  ? 607 HOH C O   1 
HETATM 9167 O  O   . HOH EA 13 .   ? -3.760  20.070  4.383  1.00 59.31  ? 608 HOH C O   1 
HETATM 9168 O  O   . HOH EA 13 .   ? -7.245  -9.459  19.209 1.00 50.62  ? 609 HOH C O   1 
HETATM 9169 O  O   . HOH EA 13 .   ? 1.044   8.849   33.123 1.00 59.19  ? 610 HOH C O   1 
HETATM 9170 O  O   . HOH EA 13 .   ? -14.312 -0.724  31.571 1.00 52.52  ? 611 HOH C O   1 
HETATM 9171 O  O   . HOH EA 13 .   ? -10.731 1.698   30.478 1.00 53.94  ? 612 HOH C O   1 
HETATM 9172 O  O   . HOH EA 13 .   ? -16.551 8.263   21.917 1.00 43.95  ? 613 HOH C O   1 
HETATM 9173 O  O   . HOH EA 13 .   ? 3.932   1.961   5.693  1.00 42.28  ? 614 HOH C O   1 
HETATM 9174 O  O   . HOH EA 13 .   ? -2.483  19.824  7.121  1.00 59.01  ? 615 HOH C O   1 
HETATM 9175 O  O   . HOH EA 13 .   ? -6.164  2.586   33.834 1.00 52.43  ? 616 HOH C O   1 
HETATM 9176 O  O   . HOH EA 13 .   ? 16.532  -5.595  11.733 1.00 54.10  ? 617 HOH C O   1 
HETATM 9177 O  O   . HOH EA 13 .   ? -15.168 -2.289  0.332  1.00 57.10  ? 618 HOH C O   1 
HETATM 9178 O  O   . HOH EA 13 .   ? 15.991  12.635  9.971  1.00 44.05  ? 619 HOH C O   1 
HETATM 9179 O  O   . HOH EA 13 .   ? 20.646  4.041   16.224 1.00 44.14  ? 620 HOH C O   1 
HETATM 9180 O  O   . HOH EA 13 .   ? -11.738 -4.544  31.703 1.00 59.48  ? 621 HOH C O   1 
HETATM 9181 O  O   . HOH EA 13 .   ? -13.245 1.689   29.790 1.00 50.06  ? 622 HOH C O   1 
HETATM 9182 O  O   . HOH EA 13 .   ? -26.330 0.333   14.067 1.00 47.75  ? 623 HOH C O   1 
HETATM 9183 O  O   . HOH EA 13 .   ? -22.310 18.031  -1.418 1.00 61.22  ? 624 HOH C O   1 
HETATM 9184 O  O   . HOH EA 13 .   ? 2.760   -15.589 16.387 1.00 52.30  ? 625 HOH C O   1 
HETATM 9185 O  O   . HOH EA 13 .   ? 2.443   17.808  25.811 1.00 46.46  ? 626 HOH C O   1 
HETATM 9186 O  O   . HOH EA 13 .   ? -9.447  -10.744 18.216 1.00 54.68  ? 627 HOH C O   1 
HETATM 9187 O  O   . HOH EA 13 .   ? -2.098  8.143   33.128 1.00 58.51  ? 628 HOH C O   1 
HETATM 9188 O  O   . HOH EA 13 .   ? -14.977 -8.532  22.168 1.00 57.12  ? 629 HOH C O   1 
HETATM 9189 O  O   . HOH EA 13 .   ? -11.598 -11.351 29.212 1.00 58.87  ? 630 HOH C O   1 
HETATM 9190 O  O   . HOH EA 13 .   ? -16.328 6.765   -4.208 1.00 48.39  ? 631 HOH C O   1 
HETATM 9191 O  O   . HOH EA 13 .   ? -4.718  10.853  16.726 1.00 59.80  ? 632 HOH C O   1 
HETATM 9192 O  O   . HOH EA 13 .   ? 3.707   3.656   2.095  1.00 34.70  ? 633 HOH C O   1 
HETATM 9193 O  O   . HOH EA 13 .   ? -2.259  -5.489  3.012  1.00 48.90  ? 634 HOH C O   1 
HETATM 9194 O  O   . HOH EA 13 .   ? 1.442   17.204  8.839  1.00 59.82  ? 635 HOH C O   1 
HETATM 9195 O  O   . HOH EA 13 .   ? -1.054  12.409  8.155  1.00 60.72  ? 636 HOH C O   1 
HETATM 9196 O  O   . HOH EA 13 .   ? -15.836 -8.883  19.179 1.00 54.52  ? 637 HOH C O   1 
HETATM 9197 O  O   . HOH EA 13 .   ? -22.638 1.087   -0.091 1.00 60.08  ? 638 HOH C O   1 
HETATM 9198 O  O   . HOH EA 13 .   ? -26.220 29.054  14.161 1.00 57.77  ? 639 HOH C O   1 
HETATM 9199 O  O   . HOH EA 13 .   ? -2.744  -3.931  32.922 1.00 61.72  ? 640 HOH C O   1 
HETATM 9200 O  O   . HOH EA 13 .   ? 14.924  26.264  12.424 1.00 61.97  ? 641 HOH C O   1 
HETATM 9201 O  O   . HOH EA 13 .   ? -9.213  -4.650  1.871  1.00 51.22  ? 642 HOH C O   1 
HETATM 9202 O  O   . HOH EA 13 .   ? -26.570 6.653   -1.487 1.00 64.84  ? 643 HOH C O   1 
HETATM 9203 O  O   . HOH EA 13 .   ? -19.108 -9.134  17.006 1.00 55.27  ? 644 HOH C O   1 
HETATM 9204 O  O   . HOH EA 13 .   ? -19.550 17.514  32.402 1.00 65.80  ? 645 HOH C O   1 
HETATM 9205 O  O   . HOH EA 13 .   ? -6.197  -7.071  10.169 1.00 56.93  ? 646 HOH C O   1 
HETATM 9206 O  O   . HOH EA 13 .   ? -2.019  -9.006  13.979 1.00 44.98  ? 647 HOH C O   1 
HETATM 9207 O  O   . HOH EA 13 .   ? -7.622  4.985   33.708 1.00 52.22  ? 648 HOH C O   1 
HETATM 9208 O  O   . HOH EA 13 .   ? -9.057  -9.914  12.698 1.00 50.88  ? 649 HOH C O   1 
HETATM 9209 O  O   . HOH EA 13 .   ? -26.422 -3.361  4.814  1.00 64.59  ? 650 HOH C O   1 
HETATM 9210 O  O   . HOH EA 13 .   ? -15.828 -11.071 24.134 1.00 63.93  ? 651 HOH C O   1 
HETATM 9211 O  O   . HOH EA 13 .   ? 7.133   23.894  29.846 1.00 61.99  ? 652 HOH C O   1 
HETATM 9212 O  O   . HOH EA 13 .   ? 12.751  -12.881 14.418 1.00 56.98  ? 653 HOH C O   1 
HETATM 9213 O  O   . HOH EA 13 .   ? -22.572 5.191   -2.069 1.00 54.53  ? 654 HOH C O   1 
HETATM 9214 O  O   . HOH EA 13 .   ? 1.237   -4.562  2.464  1.00 52.22  ? 655 HOH C O   1 
HETATM 9215 O  O   . HOH EA 13 .   ? 2.019   -0.003  2.039  1.00 39.73  ? 656 HOH C O   1 
HETATM 9216 O  O   . HOH EA 13 .   ? 19.817  5.072   18.280 1.00 57.18  ? 657 HOH C O   1 
HETATM 9217 O  O   . HOH EA 13 .   ? 1.845   14.913  11.067 1.00 68.43  ? 658 HOH C O   1 
HETATM 9218 O  O   . HOH EA 13 .   ? 7.664   -3.692  7.554  1.00 52.41  ? 659 HOH C O   1 
HETATM 9219 O  O   . HOH EA 13 .   ? -2.716  12.307  10.774 1.00 54.30  ? 660 HOH C O   1 
HETATM 9220 O  O   . HOH EA 13 .   ? -5.293  2.202   -3.144 1.00 44.40  ? 661 HOH C O   1 
HETATM 9221 O  O   . HOH EA 13 .   ? -3.218  12.399  15.376 1.00 61.53  ? 662 HOH C O   1 
HETATM 9222 O  O   . HOH EA 13 .   ? 1.162   4.358   33.682 1.00 59.59  ? 663 HOH C O   1 
HETATM 9223 O  O   . HOH EA 13 .   ? -1.314  8.399   -0.391 1.00 46.09  ? 664 HOH C O   1 
HETATM 9224 O  O   . HOH EA 13 .   ? -2.155  14.119  13.177 1.00 62.40  ? 665 HOH C O   1 
HETATM 9225 O  O   . HOH EA 13 .   ? 9.188   6.230   31.138 1.00 55.36  ? 666 HOH C O   1 
HETATM 9226 O  O   . HOH EA 13 .   ? -1.098  -2.203  -0.856 1.00 38.08  ? 667 HOH C O   1 
HETATM 9227 O  O   . HOH EA 13 .   ? -13.005 -5.451  8.482  1.00 61.17  ? 668 HOH C O   1 
HETATM 9228 O  O   . HOH EA 13 .   ? 1.576   24.541  9.766  1.00 63.68  ? 669 HOH C O   1 
HETATM 9229 O  O   . HOH EA 13 .   ? -24.563 -3.160  3.068  1.00 66.85  ? 670 HOH C O   1 
HETATM 9230 O  O   . HOH EA 13 .   ? -13.161 -4.488  -1.051 1.00 60.83  ? 671 HOH C O   1 
HETATM 9231 O  O   . HOH EA 13 .   ? 7.615   14.087  0.892  1.00 47.51  ? 672 HOH C O   1 
HETATM 9232 O  O   . HOH EA 13 .   ? 19.922  -12.828 18.054 1.00 62.10  ? 673 HOH C O   1 
HETATM 9233 O  O   . HOH EA 13 .   ? -20.169 -7.804  2.041  1.00 65.53  ? 674 HOH C O   1 
HETATM 9234 O  O   . HOH EA 13 .   ? -0.000  4.347   -0.000 0.50 38.66  ? 675 HOH C O   1 
HETATM 9235 O  O   . HOH EA 13 .   ? 19.962  -1.683  32.851 1.00 52.68  ? 676 HOH C O   1 
HETATM 9236 O  O   . HOH EA 13 .   ? 4.416   5.189   -0.349 1.00 40.91  ? 677 HOH C O   1 
HETATM 9237 O  O   . HOH EA 13 .   ? 16.884  4.120   32.073 1.00 53.77  ? 678 HOH C O   1 
HETATM 9238 O  O   . HOH EA 13 .   ? 17.682  -13.636 20.878 1.00 55.01  ? 679 HOH C O   1 
HETATM 9239 O  O   . HOH EA 13 .   ? -20.688 -7.008  38.303 1.00 61.80  ? 680 HOH C O   1 
HETATM 9240 O  O   . HOH EA 13 .   ? -2.888  -12.999 25.275 1.00 59.00  ? 681 HOH C O   1 
HETATM 9241 O  O   . HOH EA 13 .   ? 22.107  -13.647 16.784 1.00 57.99  ? 682 HOH C O   1 
# 
