data_9HE7
# 
_entry.id   9HE7 
# 
_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   9HE7         pdb_00009he7 10.2210/pdb9he7/pdb 
WWPDB D_1292136243 ?            ?                   
# 
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                        9HE7 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xjulia@iqfr.csic.es 
_pdbx_contact_author.name_first         Julia 
_pdbx_contact_author.name_last          Sanz-Aparicio 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6849-8621 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fernandez-Garcia, A.' 1 0000-0003-2052-6483 
'Sanz-Aparicio, J.'    2 0000-0002-6849-8621 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Characterization of Recombinant Unspecific Peroxygenase from Candolleomyces aberdarensis through Crystallographic and Substrate Selectivity Studies
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202402015 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Menes-Rubio, A.'      1 ? 
primary 'Fernandez-Garcia, A.' 2 ? 
primary 'Monterrey, D.T.'      3 ? 
primary 'de Santos, P.G.'      4 ? 
primary 'Sanchez-Moreno, I.'   5 ? 
primary 'Sanz-Aparicio, J.'    6 ? 
primary 'Alcalde, M.'          7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Heme-thiolate peroxidase' 36630.445 3   1.11.2.1 ? ? ? 
2  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1   ?        ? ? ? 
3  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1235.105  1   ?        ? ? ? 
4  branched    man 
;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 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   1   
?        ? ? ? 
7  non-polymer syn 'MYRISTIC ACID' 228.371   3   ?        ? ? ? 
8  non-polymer syn GLYCEROL 92.094    6   ?        ? ? ? 
9  non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   3   ?        ? ? ? 
10 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   3   ?        ? ? ? 
11 non-polymer syn 'SULFATE ION' 96.063    7   ?        ? ? ? 
12 non-polymer syn 'MAGNESIUM ION' 24.305    3   ?        ? ? ? 
13 water       nat water 18.015    888 ?        ? ? ? 
# 
_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  'MYRISTIC ACID'                                       MYR 
8  GLYCEROL                                              GOL 
9  '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
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 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}' LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3  2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4  2 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
5  3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
7  3 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
8  3 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
9  3 6 MAN C1 O1 4 MAN O6 HO6 sing ? 
10 3 7 MAN C1 O1 3 BMA O3 HO3 sing ? 
11 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
12 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
13 4 4 MAN C1 O1 3 BMA 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 ? 
20 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                               ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking'           y ARGININE                                              ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking'           y ASPARAGINE                                            ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                                       ? 'C4 H7 N O4'       133.103 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                                  'beta-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
CYS 'L-peptide linking'           y CYSTEINE                                              ? 'C3 H7 N O2 S'     121.158 
EPE non-polymer                   . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'   238.305 
GLN 'L-peptide linking'           y GLUTAMINE                                             ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'             y GLYCINE                                               ? 'C2 H5 N O2'       75.067  
GOL non-polymer                   . GLYCEROL                                              'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'         92.094  
HEM non-polymer                   . 'PROTOPORPHYRIN IX CONTAINING FE'                     HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking'           y HISTIDINE                                             ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer                   . WATER                                                 ? 'H2 O'             18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                                            ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking'           y LEUCINE                                               ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking'           y LYSINE                                                ? 'C6 H15 N2 O2 1'   147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                                 'alpha-D-mannose; D-mannose; mannose' 
'C6 H12 O6'        180.156 
MET 'L-peptide linking'           y METHIONINE                                            ? 'C5 H11 N O2 S'    149.211 
MG  non-polymer                   . 'MAGNESIUM ION'                                       ? 'Mg 2'             24.305  
MYR non-polymer                   . 'MYRISTIC ACID'                                       ? 'C14 H28 O2'       228.371 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose              
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                                         ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking'           y PROLINE                                               ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking'           y SERINE                                                ? 'C3 H7 N O3'       105.093 
SO4 non-polymer                   . 'SULFATE ION'                                         ? 'O4 S -2'          96.063  
THR 'L-peptide linking'           y THREONINE                                             ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking'           y TYROSINE                                              ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking'           y VALINE                                                ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   14  14  GLN GLN A . n 
A 1 2   GLY 2   15  15  GLY GLY A . n 
A 1 3   VAL 3   16  16  VAL VAL A . n 
A 1 4   ASP 4   17  17  ASP ASP A . n 
A 1 5   PRO 5   18  18  PRO PRO A . n 
A 1 6   PRO 6   19  19  PRO PRO A . n 
A 1 7   PRO 7   20  20  PRO PRO A . n 
A 1 8   PRO 8   21  21  PRO PRO A . n 
A 1 9   PRO 9   22  22  PRO PRO A . n 
A 1 10  GLY 10  23  23  GLY GLY A . n 
A 1 11  PRO 11  24  24  PRO PRO A . n 
A 1 12  PRO 12  25  25  PRO PRO A . n 
A 1 13  SER 13  26  26  SER SER A . n 
A 1 14  PHE 14  27  27  PHE PHE A . n 
A 1 15  THR 15  28  28  THR THR A . n 
A 1 16  GLY 16  29  29  GLY GLY A . n 
A 1 17  THR 17  30  30  THR THR A . n 
A 1 18  LYS 18  31  31  LYS LYS A . n 
A 1 19  LEU 19  32  32  LEU LEU A . n 
A 1 20  VAL 20  33  33  VAL VAL A . n 
A 1 21  ASN 21  34  34  ASN ASN A . n 
A 1 22  ASP 22  35  35  ASP ASP A . n 
A 1 23  ALA 23  36  36  ALA ALA A . n 
A 1 24  ASP 24  37  37  ASP ASP A . n 
A 1 25  HIS 25  38  38  HIS HIS A . n 
A 1 26  PRO 26  39  39  PRO PRO A . n 
A 1 27  TRP 27  40  40  TRP TRP A . n 
A 1 28  GLN 28  41  41  GLN GLN A . n 
A 1 29  PRO 29  42  42  PRO PRO A . n 
A 1 30  LEU 30  43  43  LEU LEU A . n 
A 1 31  ARG 31  44  44  ARG ARG A . n 
A 1 32  GLU 32  45  45  GLU GLU A . n 
A 1 33  GLY 33  46  46  GLY GLY A . n 
A 1 34  ASP 34  47  47  ASP ASP A . n 
A 1 35  ILE 35  48  48  ILE ILE A . n 
A 1 36  ARG 36  49  49  ARG ARG A . n 
A 1 37  GLY 37  50  50  GLY GLY A . n 
A 1 38  PRO 38  51  51  PRO PRO A . n 
A 1 39  CYS 39  52  52  CYS CYS A . n 
A 1 40  PRO 40  53  53  PRO PRO A . n 
A 1 41  GLY 41  54  54  GLY GLY A . n 
A 1 42  LEU 42  55  55  LEU LEU A . n 
A 1 43  ASN 43  56  56  ASN ASN A . n 
A 1 44  THR 44  57  57  THR THR A . n 
A 1 45  LEU 45  58  58  LEU LEU A . n 
A 1 46  ALA 46  59  59  ALA ALA A . n 
A 1 47  SER 47  60  60  SER SER A . n 
A 1 48  HIS 48  61  61  HIS HIS A . n 
A 1 49  GLY 49  62  62  GLY GLY A . n 
A 1 50  TYR 50  63  63  TYR TYR A . n 
A 1 51  LEU 51  64  64  LEU LEU A . n 
A 1 52  PRO 52  65  65  PRO PRO A . n 
A 1 53  ARG 53  66  66  ARG ARG A . n 
A 1 54  ASP 54  67  67  ASP ASP A . n 
A 1 55  GLY 55  68  68  GLY GLY A . n 
A 1 56  VAL 56  69  69  VAL VAL A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  THR 58  71  71  THR THR A . n 
A 1 59  PRO 59  72  72  PRO PRO A . n 
A 1 60  ALA 60  73  73  ALA ALA A . n 
A 1 61  GLN 61  74  74  GLN GLN A . n 
A 1 62  ILE 62  75  75  ILE ILE A . n 
A 1 63  ILE 63  76  76  ILE ILE A . n 
A 1 64  THR 64  77  77  THR THR A . n 
A 1 65  ALA 65  78  78  ALA ALA A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  GLN 67  80  80  GLN GLN A . n 
A 1 68  GLU 68  81  81  GLU GLU A . n 
A 1 69  GLY 69  82  82  GLY GLY A . n 
A 1 70  PHE 70  83  83  PHE PHE A . n 
A 1 71  ASN 71  84  84  ASN ASN A . n 
A 1 72  PHE 72  85  85  PHE PHE A . n 
A 1 73  GLU 73  86  86  GLU GLU A . n 
A 1 74  ASN 74  87  87  ASN ASN A . n 
A 1 75  ASN 75  88  88  ASN ASN A . n 
A 1 76  ALA 76  89  89  ALA ALA A . n 
A 1 77  ALA 77  90  90  ALA ALA A . n 
A 1 78  ILE 78  91  91  ILE ILE A . n 
A 1 79  VAL 79  92  92  VAL VAL A . n 
A 1 80  ALA 80  93  93  ALA ALA A . n 
A 1 81  THR 81  94  94  THR THR A . n 
A 1 82  TYR 82  95  95  TYR TYR A . n 
A 1 83  LEU 83  96  96  LEU LEU A . n 
A 1 84  GLY 84  97  97  GLY GLY A . n 
A 1 85  HIS 85  98  98  HIS HIS A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  LEU 87  100 100 LEU LEU A . n 
A 1 88  ASN 88  101 101 ASN ASN A . n 
A 1 89  GLY 89  102 102 GLY GLY A . n 
A 1 90  ASN 90  103 103 ASN ASN A . n 
A 1 91  LEU 91  104 104 LEU LEU A . n 
A 1 92  VAL 92  105 105 VAL VAL A . n 
A 1 93  THR 93  106 106 THR THR A . n 
A 1 94  ASP 94  107 107 ASP ASP A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LEU 96  109 109 LEU LEU A . n 
A 1 97  SER 97  110 110 SER SER A . n 
A 1 98  ILE 98  111 111 ILE ILE A . n 
A 1 99  GLY 99  112 112 GLY GLY A . n 
A 1 100 GLY 100 113 113 GLY GLY A . n 
A 1 101 ALA 101 114 114 ALA ALA A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 PRO 103 116 116 PRO PRO A . n 
A 1 104 LYS 104 117 117 LYS LYS A . n 
A 1 105 THR 105 118 118 THR THR A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 PRO 107 120 120 PRO PRO A . n 
A 1 108 PRO 108 121 121 PRO PRO A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PRO 110 123 123 PRO PRO A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 PRO 112 125 125 PRO PRO A . n 
A 1 113 ALA 113 126 126 ALA ALA A . n 
A 1 114 HIS 114 127 127 HIS HIS A . n 
A 1 115 ALA 115 128 128 ALA ALA A . n 
A 1 116 GLY 116 129 129 GLY GLY A . n 
A 1 117 GLY 117 130 130 GLY GLY A . n 
A 1 118 LEU 118 131 131 LEU LEU A . n 
A 1 119 ASN 119 132 132 ASN ASN A . n 
A 1 120 VAL 120 133 133 VAL VAL A . n 
A 1 121 HIS 121 134 134 HIS HIS A . n 
A 1 122 GLY 122 135 135 GLY GLY A . n 
A 1 123 THR 123 136 136 THR THR A . n 
A 1 124 PHE 124 137 137 PHE PHE A . n 
A 1 125 GLU 125 138 138 GLU GLU A . n 
A 1 126 GLY 126 139 139 GLY GLY A . n 
A 1 127 ASP 127 140 140 ASP ASP A . n 
A 1 128 ALA 128 141 141 ALA ALA A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 MET 130 143 143 MET MET A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 ARG 132 145 145 ARG ARG A . n 
A 1 133 ALA 133 146 146 ALA ALA A . n 
A 1 134 ASP 134 147 147 ASP ASP A . n 
A 1 135 GLU 135 148 148 GLU GLU A . n 
A 1 136 PHE 136 149 149 PHE PHE A . n 
A 1 137 PHE 137 150 150 PHE PHE A . n 
A 1 138 GLY 138 151 151 GLY GLY A . n 
A 1 139 ASP 139 152 152 ASP ASP A . n 
A 1 140 ASN 140 153 153 ASN ASN A . n 
A 1 141 HIS 141 154 154 HIS HIS A . n 
A 1 142 SER 142 155 155 SER SER A . n 
A 1 143 PHE 143 156 156 PHE PHE A . n 
A 1 144 ASN 144 157 157 ASN ASN A . n 
A 1 145 GLN 145 158 158 GLN GLN A . n 
A 1 146 THR 146 159 159 THR THR A . n 
A 1 147 LEU 147 160 160 LEU LEU A . n 
A 1 148 PHE 148 161 161 PHE PHE A . n 
A 1 149 ASP 149 162 162 ASP ASP A . n 
A 1 150 LYS 150 163 163 LYS LYS A . n 
A 1 151 PHE 151 164 164 PHE PHE A . n 
A 1 152 VAL 152 165 165 VAL VAL A . n 
A 1 153 ASP 153 166 166 ASP ASP A . n 
A 1 154 PHE 154 167 167 PHE PHE A . n 
A 1 155 SER 155 168 168 SER SER A . n 
A 1 156 ASN 156 169 169 ASN ASN A . n 
A 1 157 ARG 157 170 170 ARG ARG A . n 
A 1 158 TYR 158 171 171 TYR TYR A . n 
A 1 159 GLY 159 172 172 GLY GLY A . n 
A 1 160 GLY 160 173 173 GLY GLY A . n 
A 1 161 GLY 161 174 174 GLY GLY A . n 
A 1 162 PHE 162 175 175 PHE PHE A . n 
A 1 163 TYR 163 176 176 TYR TYR A . n 
A 1 164 ASN 164 177 177 ASN ASN A . n 
A 1 165 LEU 165 178 178 LEU LEU A . n 
A 1 166 THR 166 179 179 THR THR A . n 
A 1 167 VAL 167 180 180 VAL VAL A . n 
A 1 168 ALA 168 181 181 ALA ALA A . n 
A 1 169 GLY 169 182 182 GLY GLY A . n 
A 1 170 GLU 170 183 183 GLU GLU A . n 
A 1 171 LEU 171 184 184 LEU LEU A . n 
A 1 172 ARG 172 185 185 ARG ARG A . n 
A 1 173 TYR 173 186 186 TYR TYR A . n 
A 1 174 SER 174 187 187 SER SER A . n 
A 1 175 ARG 175 188 188 ARG ARG A . n 
A 1 176 ILE 176 189 189 ILE ILE A . n 
A 1 177 GLN 177 190 190 GLN GLN A . n 
A 1 178 ASP 178 191 191 ASP ASP A . n 
A 1 179 SER 179 192 192 SER SER A . n 
A 1 180 ILE 180 193 193 ILE ILE A . n 
A 1 181 ALA 181 194 194 ALA ALA A . n 
A 1 182 THR 182 195 195 THR THR A . n 
A 1 183 ASN 183 196 196 ASN ASN A . n 
A 1 184 PRO 184 197 197 PRO PRO A . n 
A 1 185 GLU 185 198 198 GLU GLU A . n 
A 1 186 PHE 186 199 199 PHE PHE A . n 
A 1 187 GLN 187 200 200 GLN GLN A . n 
A 1 188 PHE 188 201 201 PHE PHE A . n 
A 1 189 LYS 189 202 202 LYS LYS A . n 
A 1 190 ASN 190 203 203 ASN ASN A . n 
A 1 191 VAL 191 204 204 VAL VAL A . n 
A 1 192 ARG 192 205 205 ARG ARG A . n 
A 1 193 PHE 193 206 206 PHE PHE A . n 
A 1 194 ILE 194 207 207 ILE ILE A . n 
A 1 195 THR 195 208 208 THR THR A . n 
A 1 196 ALA 196 209 209 ALA ALA A . n 
A 1 197 TYR 197 210 210 TYR TYR A . n 
A 1 198 GLY 198 211 211 GLY GLY A . n 
A 1 199 GLU 199 212 212 GLU GLU A . n 
A 1 200 THR 200 213 213 THR THR A . n 
A 1 201 VAL 201 214 214 VAL VAL A . n 
A 1 202 PHE 202 215 215 PHE PHE A . n 
A 1 203 PRO 203 216 216 PRO PRO A . n 
A 1 204 ILE 204 217 217 ILE ILE A . n 
A 1 205 ASN 205 218 218 ASN ASN A . n 
A 1 206 LEU 206 219 219 LEU LEU A . n 
A 1 207 PHE 207 220 220 PHE PHE A . n 
A 1 208 VAL 208 221 221 VAL VAL A . n 
A 1 209 ASP 209 222 222 ASP ASP A . n 
A 1 210 GLY 210 223 223 GLY GLY A . n 
A 1 211 ARG 211 224 224 ARG ARG A . n 
A 1 212 VAL 212 225 225 VAL VAL A . n 
A 1 213 THR 213 226 226 THR THR A . n 
A 1 214 THR 214 227 227 THR THR A . n 
A 1 215 ASP 215 228 228 ASP ASP A . n 
A 1 216 ARG 216 229 229 ARG ARG A . n 
A 1 217 LYS 217 230 230 LYS LYS A . n 
A 1 218 LEU 218 231 231 LEU LEU A . n 
A 1 219 SER 219 232 232 SER SER A . n 
A 1 220 MET 220 233 233 MET MET A . n 
A 1 221 GLU 221 234 234 GLU GLU A . n 
A 1 222 ASP 222 235 235 ASP ASP A . n 
A 1 223 ALA 223 236 236 ALA ALA A . n 
A 1 224 ALA 224 237 237 ALA ALA A . n 
A 1 225 SER 225 238 238 SER SER A . n 
A 1 226 ILE 226 239 239 ILE ILE A . n 
A 1 227 PHE 227 240 240 PHE PHE A . n 
A 1 228 ARG 228 241 241 ARG ARG A . n 
A 1 229 ASP 229 242 242 ASP ASP A . n 
A 1 230 MET 230 243 243 MET MET A . n 
A 1 231 ARG 231 244 244 ARG ARG A . n 
A 1 232 PHE 232 245 245 PHE PHE A . n 
A 1 233 PRO 233 246 246 PRO PRO A . n 
A 1 234 ASP 234 247 247 ASP ASP A . n 
A 1 235 ASP 235 248 248 ASP ASP A . n 
A 1 236 PHE 236 249 249 PHE PHE A . n 
A 1 237 HIS 237 250 250 HIS HIS A . n 
A 1 238 ARG 238 251 251 ARG ARG A . n 
A 1 239 SER 239 252 252 SER SER A . n 
A 1 240 ALA 240 253 253 ALA ALA A . n 
A 1 241 VAL 241 254 254 VAL VAL A . n 
A 1 242 PRO 242 255 255 PRO PRO A . n 
A 1 243 ALA 243 256 256 ALA ALA A . n 
A 1 244 SER 244 257 257 SER SER A . n 
A 1 245 ASN 245 258 258 ASN ASN A . n 
A 1 246 GLU 246 259 259 GLU GLU A . n 
A 1 247 GLY 247 260 260 GLY GLY A . n 
A 1 248 ALA 248 261 261 ALA ALA A . n 
A 1 249 ASP 249 262 262 ASP ASP A . n 
A 1 250 GLN 250 263 263 GLN GLN A . n 
A 1 251 VAL 251 264 264 VAL VAL A . n 
A 1 252 LEU 252 265 265 LEU LEU A . n 
A 1 253 ALA 253 266 266 ALA ALA A . n 
A 1 254 ALA 254 267 267 ALA ALA A . n 
A 1 255 HIS 255 268 268 HIS HIS A . n 
A 1 256 PRO 256 269 269 PRO PRO A . n 
A 1 257 TRP 257 270 270 TRP TRP A . n 
A 1 258 VAL 258 271 271 VAL VAL A . n 
A 1 259 PRO 259 272 272 PRO PRO A . n 
A 1 260 GLY 260 273 273 GLY GLY A . n 
A 1 261 GLY 261 274 274 GLY GLY A . n 
A 1 262 ASN 262 275 275 ASN ASN A . n 
A 1 263 ALA 263 276 276 ALA ALA A . n 
A 1 264 ASP 264 277 277 ASP ASP A . n 
A 1 265 ASN 265 278 278 ASN ASN A . n 
A 1 266 GLN 266 279 279 GLN GLN A . n 
A 1 267 VAL 267 280 280 VAL VAL A . n 
A 1 268 ASN 268 281 281 ASN ASN A . n 
A 1 269 ASN 269 282 282 ASN ASN A . n 
A 1 270 TYR 270 283 283 TYR TYR A . n 
A 1 271 VAL 271 284 284 VAL VAL A . n 
A 1 272 GLU 272 285 285 GLU GLU A . n 
A 1 273 ASP 273 286 286 ASP ASP A . n 
A 1 274 PRO 274 287 287 PRO PRO A . n 
A 1 275 ASP 275 288 288 ASP ASP A . n 
A 1 276 SER 276 289 289 SER SER A . n 
A 1 277 ALA 277 290 290 ALA ALA A . n 
A 1 278 ASP 278 291 291 ASP ASP A . n 
A 1 279 PHE 279 292 292 PHE PHE A . n 
A 1 280 THR 280 293 293 THR THR A . n 
A 1 281 HIS 281 294 294 HIS HIS A . n 
A 1 282 LEU 282 295 295 LEU LEU A . n 
A 1 283 CYS 283 296 296 CYS CYS A . n 
A 1 284 ARG 284 297 297 ARG ARG A . n 
A 1 285 LEU 285 298 298 LEU LEU A . n 
A 1 286 TYR 286 299 299 TYR TYR A . n 
A 1 287 GLU 287 300 300 GLU GLU A . n 
A 1 288 PHE 288 301 301 PHE PHE A . n 
A 1 289 VAL 289 302 302 VAL VAL A . n 
A 1 290 VAL 290 303 303 VAL VAL A . n 
A 1 291 GLY 291 304 304 GLY GLY A . n 
A 1 292 SER 292 305 305 SER SER A . n 
A 1 293 VAL 293 306 306 VAL VAL A . n 
A 1 294 GLN 294 307 307 GLN GLN A . n 
A 1 295 GLU 295 308 308 GLU GLU A . n 
A 1 296 LEU 296 309 309 LEU LEU A . n 
A 1 297 TYR 297 310 310 TYR TYR A . n 
A 1 298 PRO 298 311 311 PRO PRO A . n 
A 1 299 ASN 299 312 312 ASN ASN A . n 
A 1 300 PRO 300 313 313 PRO PRO A . n 
A 1 301 THR 301 314 314 THR THR A . n 
A 1 302 GLY 302 315 315 GLY GLY A . n 
A 1 303 ILE 303 316 316 ILE ILE A . n 
A 1 304 LEU 304 317 317 LEU LEU A . n 
A 1 305 ARG 305 318 318 ARG ARG A . n 
A 1 306 ARG 306 319 319 ARG ARG A . n 
A 1 307 ASN 307 320 320 ASN ASN A . n 
A 1 308 LEU 308 321 321 LEU LEU A . n 
A 1 309 ILE 309 322 322 ILE ILE A . n 
A 1 310 LYS 310 323 323 LYS LYS A . n 
A 1 311 ASN 311 324 324 ASN ASN A . n 
A 1 312 LEU 312 325 325 LEU LEU A . n 
A 1 313 HIS 313 326 326 HIS HIS A . n 
A 1 314 TYR 314 327 327 TYR TYR A . n 
A 1 315 TRP 315 328 328 TRP TRP A . n 
A 1 316 TRP 316 329 329 TRP TRP A . n 
A 1 317 THR 317 330 330 THR THR A . n 
A 1 318 GLY 318 331 331 GLY GLY A . n 
A 1 319 VAL 319 332 332 VAL VAL A . n 
A 1 320 ASN 320 333 333 ASN ASN A . n 
A 1 321 VAL 321 334 334 VAL VAL A . n 
A 1 322 ALA 322 335 335 ALA ALA A . n 
A 1 323 PHE 323 336 336 PHE PHE A . n 
A 1 324 GLY 324 337 337 GLY GLY A . n 
A 1 325 GLY 325 338 338 GLY GLY A . n 
A 1 326 CYS 326 339 339 CYS CYS A . n 
A 1 327 ASP 327 340 340 ASP ASP A . n 
A 1 328 GLU 328 341 341 GLU GLU A . n 
A 1 329 LEU 329 342 342 LEU LEU A . n 
A 1 330 PHE 330 343 343 PHE PHE A . n 
A 1 331 PRO 331 344 344 PRO PRO A . n 
A 1 332 TYR 332 345 345 TYR TYR A . n 
A 1 333 GLY 333 346 346 GLY GLY A . n 
A 1 334 GLN 334 347 347 GLN GLN A . n 
A 1 335 LEU 335 348 348 LEU LEU A . n 
B 1 1   GLN 1   14  14  GLN GLN B . n 
B 1 2   GLY 2   15  15  GLY GLY B . n 
B 1 3   VAL 3   16  16  VAL VAL B . n 
B 1 4   ASP 4   17  17  ASP ASP B . n 
B 1 5   PRO 5   18  18  PRO PRO B . n 
B 1 6   PRO 6   19  19  PRO PRO B . n 
B 1 7   PRO 7   20  20  PRO PRO B . n 
B 1 8   PRO 8   21  21  PRO PRO B . n 
B 1 9   PRO 9   22  22  PRO PRO B . n 
B 1 10  GLY 10  23  23  GLY GLY B . n 
B 1 11  PRO 11  24  24  PRO PRO B . n 
B 1 12  PRO 12  25  25  PRO PRO B . n 
B 1 13  SER 13  26  26  SER SER B . n 
B 1 14  PHE 14  27  27  PHE PHE B . n 
B 1 15  THR 15  28  28  THR THR B . n 
B 1 16  GLY 16  29  29  GLY GLY B . n 
B 1 17  THR 17  30  30  THR THR B . n 
B 1 18  LYS 18  31  31  LYS LYS B . n 
B 1 19  LEU 19  32  32  LEU LEU B . n 
B 1 20  VAL 20  33  33  VAL VAL B . n 
B 1 21  ASN 21  34  34  ASN ASN B . n 
B 1 22  ASP 22  35  35  ASP ASP B . n 
B 1 23  ALA 23  36  36  ALA ALA B . n 
B 1 24  ASP 24  37  37  ASP ASP B . n 
B 1 25  HIS 25  38  38  HIS HIS B . n 
B 1 26  PRO 26  39  39  PRO PRO B . n 
B 1 27  TRP 27  40  40  TRP TRP B . n 
B 1 28  GLN 28  41  41  GLN GLN B . n 
B 1 29  PRO 29  42  42  PRO PRO B . n 
B 1 30  LEU 30  43  43  LEU LEU B . n 
B 1 31  ARG 31  44  44  ARG ARG B . n 
B 1 32  GLU 32  45  45  GLU GLU B . n 
B 1 33  GLY 33  46  46  GLY GLY B . n 
B 1 34  ASP 34  47  47  ASP ASP B . n 
B 1 35  ILE 35  48  48  ILE ILE B . n 
B 1 36  ARG 36  49  49  ARG ARG B . n 
B 1 37  GLY 37  50  50  GLY GLY B . n 
B 1 38  PRO 38  51  51  PRO PRO B . n 
B 1 39  CYS 39  52  52  CYS CYS B . n 
B 1 40  PRO 40  53  53  PRO PRO B . n 
B 1 41  GLY 41  54  54  GLY GLY B . n 
B 1 42  LEU 42  55  55  LEU LEU B . n 
B 1 43  ASN 43  56  56  ASN ASN B . n 
B 1 44  THR 44  57  57  THR THR B . n 
B 1 45  LEU 45  58  58  LEU LEU B . n 
B 1 46  ALA 46  59  59  ALA ALA B . n 
B 1 47  SER 47  60  60  SER SER B . n 
B 1 48  HIS 48  61  61  HIS HIS B . n 
B 1 49  GLY 49  62  62  GLY GLY B . n 
B 1 50  TYR 50  63  63  TYR TYR B . n 
B 1 51  LEU 51  64  64  LEU LEU B . n 
B 1 52  PRO 52  65  65  PRO PRO B . n 
B 1 53  ARG 53  66  66  ARG ARG B . n 
B 1 54  ASP 54  67  67  ASP ASP B . n 
B 1 55  GLY 55  68  68  GLY GLY B . n 
B 1 56  VAL 56  69  69  VAL VAL B . n 
B 1 57  ALA 57  70  70  ALA ALA B . n 
B 1 58  THR 58  71  71  THR THR B . n 
B 1 59  PRO 59  72  72  PRO PRO B . n 
B 1 60  ALA 60  73  73  ALA ALA B . n 
B 1 61  GLN 61  74  74  GLN GLN B . n 
B 1 62  ILE 62  75  75  ILE ILE B . n 
B 1 63  ILE 63  76  76  ILE ILE B . n 
B 1 64  THR 64  77  77  THR THR B . n 
B 1 65  ALA 65  78  78  ALA ALA B . n 
B 1 66  THR 66  79  79  THR THR B . n 
B 1 67  GLN 67  80  80  GLN GLN B . n 
B 1 68  GLU 68  81  81  GLU GLU B . n 
B 1 69  GLY 69  82  82  GLY GLY B . n 
B 1 70  PHE 70  83  83  PHE PHE B . n 
B 1 71  ASN 71  84  84  ASN ASN B . n 
B 1 72  PHE 72  85  85  PHE PHE B . n 
B 1 73  GLU 73  86  86  GLU GLU B . n 
B 1 74  ASN 74  87  87  ASN ASN B . n 
B 1 75  ASN 75  88  88  ASN ASN B . n 
B 1 76  ALA 76  89  89  ALA ALA B . n 
B 1 77  ALA 77  90  90  ALA ALA B . n 
B 1 78  ILE 78  91  91  ILE ILE B . n 
B 1 79  VAL 79  92  92  VAL VAL B . n 
B 1 80  ALA 80  93  93  ALA ALA B . n 
B 1 81  THR 81  94  94  THR THR B . n 
B 1 82  TYR 82  95  95  TYR TYR B . n 
B 1 83  LEU 83  96  96  LEU LEU B . n 
B 1 84  GLY 84  97  97  GLY GLY B . n 
B 1 85  HIS 85  98  98  HIS HIS B . n 
B 1 86  LEU 86  99  99  LEU LEU B . n 
B 1 87  LEU 87  100 100 LEU LEU B . n 
B 1 88  ASN 88  101 101 ASN ASN B . n 
B 1 89  GLY 89  102 102 GLY GLY B . n 
B 1 90  ASN 90  103 103 ASN ASN B . n 
B 1 91  LEU 91  104 104 LEU LEU B . n 
B 1 92  VAL 92  105 105 VAL VAL B . n 
B 1 93  THR 93  106 106 THR THR B . n 
B 1 94  ASP 94  107 107 ASP ASP B . n 
B 1 95  LEU 95  108 108 LEU LEU B . n 
B 1 96  LEU 96  109 109 LEU LEU B . n 
B 1 97  SER 97  110 110 SER SER B . n 
B 1 98  ILE 98  111 111 ILE ILE B . n 
B 1 99  GLY 99  112 112 GLY GLY B . n 
B 1 100 GLY 100 113 113 GLY GLY B . n 
B 1 101 ALA 101 114 114 ALA ALA B . n 
B 1 102 THR 102 115 115 THR THR B . n 
B 1 103 PRO 103 116 116 PRO PRO B . n 
B 1 104 LYS 104 117 117 LYS LYS B . n 
B 1 105 THR 105 118 118 THR THR B . n 
B 1 106 GLY 106 119 119 GLY GLY B . n 
B 1 107 PRO 107 120 120 PRO PRO B . n 
B 1 108 PRO 108 121 121 PRO PRO B . n 
B 1 109 PRO 109 122 122 PRO PRO B . n 
B 1 110 PRO 110 123 123 PRO PRO B . n 
B 1 111 PRO 111 124 124 PRO PRO B . n 
B 1 112 PRO 112 125 125 PRO PRO B . n 
B 1 113 ALA 113 126 126 ALA ALA B . n 
B 1 114 HIS 114 127 127 HIS HIS B . n 
B 1 115 ALA 115 128 128 ALA ALA B . n 
B 1 116 GLY 116 129 129 GLY GLY B . n 
B 1 117 GLY 117 130 130 GLY GLY B . n 
B 1 118 LEU 118 131 131 LEU LEU B . n 
B 1 119 ASN 119 132 132 ASN ASN B . n 
B 1 120 VAL 120 133 133 VAL VAL B . n 
B 1 121 HIS 121 134 134 HIS HIS B . n 
B 1 122 GLY 122 135 135 GLY GLY B . n 
B 1 123 THR 123 136 136 THR THR B . n 
B 1 124 PHE 124 137 137 PHE PHE B . n 
B 1 125 GLU 125 138 138 GLU GLU B . n 
B 1 126 GLY 126 139 139 GLY GLY B . n 
B 1 127 ASP 127 140 140 ASP ASP B . n 
B 1 128 ALA 128 141 141 ALA ALA B . n 
B 1 129 GLY 129 142 142 GLY GLY B . n 
B 1 130 MET 130 143 143 MET MET B . n 
B 1 131 THR 131 144 144 THR THR B . n 
B 1 132 ARG 132 145 145 ARG ARG B . n 
B 1 133 ALA 133 146 146 ALA ALA B . n 
B 1 134 ASP 134 147 147 ASP ASP B . n 
B 1 135 GLU 135 148 148 GLU GLU B . n 
B 1 136 PHE 136 149 149 PHE PHE B . n 
B 1 137 PHE 137 150 150 PHE PHE B . n 
B 1 138 GLY 138 151 151 GLY GLY B . n 
B 1 139 ASP 139 152 152 ASP ASP B . n 
B 1 140 ASN 140 153 153 ASN ASN B . n 
B 1 141 HIS 141 154 154 HIS HIS B . n 
B 1 142 SER 142 155 155 SER SER B . n 
B 1 143 PHE 143 156 156 PHE PHE B . n 
B 1 144 ASN 144 157 157 ASN ASN B . n 
B 1 145 GLN 145 158 158 GLN GLN B . n 
B 1 146 THR 146 159 159 THR THR B . n 
B 1 147 LEU 147 160 160 LEU LEU B . n 
B 1 148 PHE 148 161 161 PHE PHE B . n 
B 1 149 ASP 149 162 162 ASP ASP B . n 
B 1 150 LYS 150 163 163 LYS LYS B . n 
B 1 151 PHE 151 164 164 PHE PHE B . n 
B 1 152 VAL 152 165 165 VAL VAL B . n 
B 1 153 ASP 153 166 166 ASP ASP B . n 
B 1 154 PHE 154 167 167 PHE PHE B . n 
B 1 155 SER 155 168 168 SER SER B . n 
B 1 156 ASN 156 169 169 ASN ASN B . n 
B 1 157 ARG 157 170 170 ARG ARG B . n 
B 1 158 TYR 158 171 171 TYR TYR B . n 
B 1 159 GLY 159 172 172 GLY GLY B . n 
B 1 160 GLY 160 173 173 GLY GLY B . n 
B 1 161 GLY 161 174 174 GLY GLY B . n 
B 1 162 PHE 162 175 175 PHE PHE B . n 
B 1 163 TYR 163 176 176 TYR TYR B . n 
B 1 164 ASN 164 177 177 ASN ASN B . n 
B 1 165 LEU 165 178 178 LEU LEU B . n 
B 1 166 THR 166 179 179 THR THR B . n 
B 1 167 VAL 167 180 180 VAL VAL B . n 
B 1 168 ALA 168 181 181 ALA ALA B . n 
B 1 169 GLY 169 182 182 GLY GLY B . n 
B 1 170 GLU 170 183 183 GLU GLU B . n 
B 1 171 LEU 171 184 184 LEU LEU B . n 
B 1 172 ARG 172 185 185 ARG ARG B . n 
B 1 173 TYR 173 186 186 TYR TYR B . n 
B 1 174 SER 174 187 187 SER SER B . n 
B 1 175 ARG 175 188 188 ARG ARG B . n 
B 1 176 ILE 176 189 189 ILE ILE B . n 
B 1 177 GLN 177 190 190 GLN GLN B . n 
B 1 178 ASP 178 191 191 ASP ASP B . n 
B 1 179 SER 179 192 192 SER SER B . n 
B 1 180 ILE 180 193 193 ILE ILE B . n 
B 1 181 ALA 181 194 194 ALA ALA B . n 
B 1 182 THR 182 195 195 THR THR B . n 
B 1 183 ASN 183 196 196 ASN ASN B . n 
B 1 184 PRO 184 197 197 PRO PRO B . n 
B 1 185 GLU 185 198 198 GLU GLU B . n 
B 1 186 PHE 186 199 199 PHE PHE B . n 
B 1 187 GLN 187 200 200 GLN GLN B . n 
B 1 188 PHE 188 201 201 PHE PHE B . n 
B 1 189 LYS 189 202 202 LYS LYS B . n 
B 1 190 ASN 190 203 203 ASN ASN B . n 
B 1 191 VAL 191 204 204 VAL VAL B . n 
B 1 192 ARG 192 205 205 ARG ARG B . n 
B 1 193 PHE 193 206 206 PHE PHE B . n 
B 1 194 ILE 194 207 207 ILE ILE B . n 
B 1 195 THR 195 208 208 THR THR B . n 
B 1 196 ALA 196 209 209 ALA ALA B . n 
B 1 197 TYR 197 210 210 TYR TYR B . n 
B 1 198 GLY 198 211 211 GLY GLY B . n 
B 1 199 GLU 199 212 212 GLU GLU B . n 
B 1 200 THR 200 213 213 THR THR B . n 
B 1 201 VAL 201 214 214 VAL VAL B . n 
B 1 202 PHE 202 215 215 PHE PHE B . n 
B 1 203 PRO 203 216 216 PRO PRO B . n 
B 1 204 ILE 204 217 217 ILE ILE B . n 
B 1 205 ASN 205 218 218 ASN ASN B . n 
B 1 206 LEU 206 219 219 LEU LEU B . n 
B 1 207 PHE 207 220 220 PHE PHE B . n 
B 1 208 VAL 208 221 221 VAL VAL B . n 
B 1 209 ASP 209 222 222 ASP ASP B . n 
B 1 210 GLY 210 223 223 GLY GLY B . n 
B 1 211 ARG 211 224 224 ARG ARG B . n 
B 1 212 VAL 212 225 225 VAL VAL B . n 
B 1 213 THR 213 226 226 THR THR B . n 
B 1 214 THR 214 227 227 THR THR B . n 
B 1 215 ASP 215 228 228 ASP ASP B . n 
B 1 216 ARG 216 229 229 ARG ARG B . n 
B 1 217 LYS 217 230 230 LYS LYS B . n 
B 1 218 LEU 218 231 231 LEU LEU B . n 
B 1 219 SER 219 232 232 SER SER B . n 
B 1 220 MET 220 233 233 MET MET B . n 
B 1 221 GLU 221 234 234 GLU GLU B . n 
B 1 222 ASP 222 235 235 ASP ASP B . n 
B 1 223 ALA 223 236 236 ALA ALA B . n 
B 1 224 ALA 224 237 237 ALA ALA B . n 
B 1 225 SER 225 238 238 SER SER B . n 
B 1 226 ILE 226 239 239 ILE ILE B . n 
B 1 227 PHE 227 240 240 PHE PHE B . n 
B 1 228 ARG 228 241 241 ARG ARG B . n 
B 1 229 ASP 229 242 242 ASP ASP B . n 
B 1 230 MET 230 243 243 MET MET B . n 
B 1 231 ARG 231 244 244 ARG ARG B . n 
B 1 232 PHE 232 245 245 PHE PHE B . n 
B 1 233 PRO 233 246 246 PRO PRO B . n 
B 1 234 ASP 234 247 247 ASP ASP B . n 
B 1 235 ASP 235 248 248 ASP ASP B . n 
B 1 236 PHE 236 249 249 PHE PHE B . n 
B 1 237 HIS 237 250 250 HIS HIS B . n 
B 1 238 ARG 238 251 251 ARG ARG B . n 
B 1 239 SER 239 252 252 SER SER B . n 
B 1 240 ALA 240 253 253 ALA ALA B . n 
B 1 241 VAL 241 254 254 VAL VAL B . n 
B 1 242 PRO 242 255 255 PRO PRO B . n 
B 1 243 ALA 243 256 256 ALA ALA B . n 
B 1 244 SER 244 257 257 SER SER B . n 
B 1 245 ASN 245 258 258 ASN ASN B . n 
B 1 246 GLU 246 259 259 GLU GLU B . n 
B 1 247 GLY 247 260 260 GLY GLY B . n 
B 1 248 ALA 248 261 261 ALA ALA B . n 
B 1 249 ASP 249 262 262 ASP ASP B . n 
B 1 250 GLN 250 263 263 GLN GLN B . n 
B 1 251 VAL 251 264 264 VAL VAL B . n 
B 1 252 LEU 252 265 265 LEU LEU B . n 
B 1 253 ALA 253 266 266 ALA ALA B . n 
B 1 254 ALA 254 267 267 ALA ALA B . n 
B 1 255 HIS 255 268 268 HIS HIS B . n 
B 1 256 PRO 256 269 269 PRO PRO B . n 
B 1 257 TRP 257 270 270 TRP TRP B . n 
B 1 258 VAL 258 271 271 VAL VAL B . n 
B 1 259 PRO 259 272 272 PRO PRO B . n 
B 1 260 GLY 260 273 273 GLY GLY B . n 
B 1 261 GLY 261 274 274 GLY GLY B . n 
B 1 262 ASN 262 275 275 ASN ASN B . n 
B 1 263 ALA 263 276 276 ALA ALA B . n 
B 1 264 ASP 264 277 277 ASP ASP B . n 
B 1 265 ASN 265 278 278 ASN ASN B . n 
B 1 266 GLN 266 279 279 GLN GLN B . n 
B 1 267 VAL 267 280 280 VAL VAL B . n 
B 1 268 ASN 268 281 281 ASN ASN B . n 
B 1 269 ASN 269 282 282 ASN ASN B . n 
B 1 270 TYR 270 283 283 TYR TYR B . n 
B 1 271 VAL 271 284 284 VAL VAL B . n 
B 1 272 GLU 272 285 285 GLU GLU B . n 
B 1 273 ASP 273 286 286 ASP ASP B . n 
B 1 274 PRO 274 287 287 PRO PRO B . n 
B 1 275 ASP 275 288 288 ASP ASP B . n 
B 1 276 SER 276 289 289 SER SER B . n 
B 1 277 ALA 277 290 290 ALA ALA B . n 
B 1 278 ASP 278 291 291 ASP ASP B . n 
B 1 279 PHE 279 292 292 PHE PHE B . n 
B 1 280 THR 280 293 293 THR THR B . n 
B 1 281 HIS 281 294 294 HIS HIS B . n 
B 1 282 LEU 282 295 295 LEU LEU B . n 
B 1 283 CYS 283 296 296 CYS CYS B . n 
B 1 284 ARG 284 297 297 ARG ARG B . n 
B 1 285 LEU 285 298 298 LEU LEU B . n 
B 1 286 TYR 286 299 299 TYR TYR B . n 
B 1 287 GLU 287 300 300 GLU GLU B . n 
B 1 288 PHE 288 301 301 PHE PHE B . n 
B 1 289 VAL 289 302 302 VAL VAL B . n 
B 1 290 VAL 290 303 303 VAL VAL B . n 
B 1 291 GLY 291 304 304 GLY GLY B . n 
B 1 292 SER 292 305 305 SER SER B . n 
B 1 293 VAL 293 306 306 VAL VAL B . n 
B 1 294 GLN 294 307 307 GLN GLN B . n 
B 1 295 GLU 295 308 308 GLU GLU B . n 
B 1 296 LEU 296 309 309 LEU LEU B . n 
B 1 297 TYR 297 310 310 TYR TYR B . n 
B 1 298 PRO 298 311 311 PRO PRO B . n 
B 1 299 ASN 299 312 312 ASN ASN B . n 
B 1 300 PRO 300 313 313 PRO PRO B . n 
B 1 301 THR 301 314 314 THR THR B . n 
B 1 302 GLY 302 315 315 GLY GLY B . n 
B 1 303 ILE 303 316 316 ILE ILE B . n 
B 1 304 LEU 304 317 317 LEU LEU B . n 
B 1 305 ARG 305 318 318 ARG ARG B . n 
B 1 306 ARG 306 319 319 ARG ARG B . n 
B 1 307 ASN 307 320 320 ASN ASN B . n 
B 1 308 LEU 308 321 321 LEU LEU B . n 
B 1 309 ILE 309 322 322 ILE ILE B . n 
B 1 310 LYS 310 323 323 LYS LYS B . n 
B 1 311 ASN 311 324 324 ASN ASN B . n 
B 1 312 LEU 312 325 325 LEU LEU B . n 
B 1 313 HIS 313 326 326 HIS HIS B . n 
B 1 314 TYR 314 327 327 TYR TYR B . n 
B 1 315 TRP 315 328 328 TRP TRP B . n 
B 1 316 TRP 316 329 329 TRP TRP B . n 
B 1 317 THR 317 330 330 THR THR B . n 
B 1 318 GLY 318 331 331 GLY GLY B . n 
B 1 319 VAL 319 332 332 VAL VAL B . n 
B 1 320 ASN 320 333 333 ASN ASN B . n 
B 1 321 VAL 321 334 334 VAL VAL B . n 
B 1 322 ALA 322 335 335 ALA ALA B . n 
B 1 323 PHE 323 336 336 PHE PHE B . n 
B 1 324 GLY 324 337 337 GLY GLY B . n 
B 1 325 GLY 325 338 338 GLY GLY B . n 
B 1 326 CYS 326 339 339 CYS CYS B . n 
B 1 327 ASP 327 340 340 ASP ASP B . n 
B 1 328 GLU 328 341 341 GLU GLU B . n 
B 1 329 LEU 329 342 342 LEU LEU B . n 
B 1 330 PHE 330 343 343 PHE PHE B . n 
B 1 331 PRO 331 344 344 PRO PRO B . n 
B 1 332 TYR 332 345 345 TYR TYR B . n 
B 1 333 GLY 333 346 346 GLY GLY B . n 
B 1 334 GLN 334 347 347 GLN GLN B . n 
B 1 335 LEU 335 348 348 LEU LEU B . n 
C 1 1   GLN 1   14  14  GLN GLN C . n 
C 1 2   GLY 2   15  15  GLY GLY C . n 
C 1 3   VAL 3   16  16  VAL VAL C . n 
C 1 4   ASP 4   17  17  ASP ASP C . n 
C 1 5   PRO 5   18  18  PRO PRO C . n 
C 1 6   PRO 6   19  19  PRO PRO C . n 
C 1 7   PRO 7   20  20  PRO PRO C . n 
C 1 8   PRO 8   21  21  PRO PRO C . n 
C 1 9   PRO 9   22  22  PRO PRO C . n 
C 1 10  GLY 10  23  23  GLY GLY C . n 
C 1 11  PRO 11  24  24  PRO PRO C . n 
C 1 12  PRO 12  25  25  PRO PRO C . n 
C 1 13  SER 13  26  26  SER SER C . n 
C 1 14  PHE 14  27  27  PHE PHE C . n 
C 1 15  THR 15  28  28  THR THR C . n 
C 1 16  GLY 16  29  29  GLY GLY C . n 
C 1 17  THR 17  30  30  THR THR C . n 
C 1 18  LYS 18  31  31  LYS LYS C . n 
C 1 19  LEU 19  32  32  LEU LEU C . n 
C 1 20  VAL 20  33  33  VAL VAL C . n 
C 1 21  ASN 21  34  34  ASN ASN C . n 
C 1 22  ASP 22  35  35  ASP ASP C . n 
C 1 23  ALA 23  36  36  ALA ALA C . n 
C 1 24  ASP 24  37  37  ASP ASP C . n 
C 1 25  HIS 25  38  38  HIS HIS C . n 
C 1 26  PRO 26  39  39  PRO PRO C . n 
C 1 27  TRP 27  40  40  TRP TRP C . n 
C 1 28  GLN 28  41  41  GLN GLN C . n 
C 1 29  PRO 29  42  42  PRO PRO C . n 
C 1 30  LEU 30  43  43  LEU LEU C . n 
C 1 31  ARG 31  44  44  ARG ARG C . n 
C 1 32  GLU 32  45  45  GLU GLU C . n 
C 1 33  GLY 33  46  46  GLY GLY C . n 
C 1 34  ASP 34  47  47  ASP ASP C . n 
C 1 35  ILE 35  48  48  ILE ILE C . n 
C 1 36  ARG 36  49  49  ARG ARG C . n 
C 1 37  GLY 37  50  50  GLY GLY C . n 
C 1 38  PRO 38  51  51  PRO PRO C . n 
C 1 39  CYS 39  52  52  CYS CYS C . n 
C 1 40  PRO 40  53  53  PRO PRO C . n 
C 1 41  GLY 41  54  54  GLY GLY C . n 
C 1 42  LEU 42  55  55  LEU LEU C . n 
C 1 43  ASN 43  56  56  ASN ASN C . n 
C 1 44  THR 44  57  57  THR THR C . n 
C 1 45  LEU 45  58  58  LEU LEU C . n 
C 1 46  ALA 46  59  59  ALA ALA C . n 
C 1 47  SER 47  60  60  SER SER C . n 
C 1 48  HIS 48  61  61  HIS HIS C . n 
C 1 49  GLY 49  62  62  GLY GLY C . n 
C 1 50  TYR 50  63  63  TYR TYR C . n 
C 1 51  LEU 51  64  64  LEU LEU C . n 
C 1 52  PRO 52  65  65  PRO PRO C . n 
C 1 53  ARG 53  66  66  ARG ARG C . n 
C 1 54  ASP 54  67  67  ASP ASP C . n 
C 1 55  GLY 55  68  68  GLY GLY C . n 
C 1 56  VAL 56  69  69  VAL VAL C . n 
C 1 57  ALA 57  70  70  ALA ALA C . n 
C 1 58  THR 58  71  71  THR THR C . n 
C 1 59  PRO 59  72  72  PRO PRO C . n 
C 1 60  ALA 60  73  73  ALA ALA C . n 
C 1 61  GLN 61  74  74  GLN GLN C . n 
C 1 62  ILE 62  75  75  ILE ILE C . n 
C 1 63  ILE 63  76  76  ILE ILE C . n 
C 1 64  THR 64  77  77  THR THR C . n 
C 1 65  ALA 65  78  78  ALA ALA C . n 
C 1 66  THR 66  79  79  THR THR C . n 
C 1 67  GLN 67  80  80  GLN GLN C . n 
C 1 68  GLU 68  81  81  GLU GLU C . n 
C 1 69  GLY 69  82  82  GLY GLY C . n 
C 1 70  PHE 70  83  83  PHE PHE C . n 
C 1 71  ASN 71  84  84  ASN ASN C . n 
C 1 72  PHE 72  85  85  PHE PHE C . n 
C 1 73  GLU 73  86  86  GLU GLU C . n 
C 1 74  ASN 74  87  87  ASN ASN C . n 
C 1 75  ASN 75  88  88  ASN ASN C . n 
C 1 76  ALA 76  89  89  ALA ALA C . n 
C 1 77  ALA 77  90  90  ALA ALA C . n 
C 1 78  ILE 78  91  91  ILE ILE C . n 
C 1 79  VAL 79  92  92  VAL VAL C . n 
C 1 80  ALA 80  93  93  ALA ALA C . n 
C 1 81  THR 81  94  94  THR THR C . n 
C 1 82  TYR 82  95  95  TYR TYR C . n 
C 1 83  LEU 83  96  96  LEU LEU C . n 
C 1 84  GLY 84  97  97  GLY GLY C . n 
C 1 85  HIS 85  98  98  HIS HIS C . n 
C 1 86  LEU 86  99  99  LEU LEU C . n 
C 1 87  LEU 87  100 100 LEU LEU C . n 
C 1 88  ASN 88  101 101 ASN ASN C . n 
C 1 89  GLY 89  102 102 GLY GLY C . n 
C 1 90  ASN 90  103 103 ASN ASN C . n 
C 1 91  LEU 91  104 104 LEU LEU C . n 
C 1 92  VAL 92  105 105 VAL VAL C . n 
C 1 93  THR 93  106 106 THR THR C . n 
C 1 94  ASP 94  107 107 ASP ASP C . n 
C 1 95  LEU 95  108 108 LEU LEU C . n 
C 1 96  LEU 96  109 109 LEU LEU C . n 
C 1 97  SER 97  110 110 SER SER C . n 
C 1 98  ILE 98  111 111 ILE ILE C . n 
C 1 99  GLY 99  112 112 GLY GLY C . n 
C 1 100 GLY 100 113 113 GLY GLY C . n 
C 1 101 ALA 101 114 114 ALA ALA C . n 
C 1 102 THR 102 115 115 THR THR C . n 
C 1 103 PRO 103 116 116 PRO PRO C . n 
C 1 104 LYS 104 117 117 LYS LYS C . n 
C 1 105 THR 105 118 118 THR THR C . n 
C 1 106 GLY 106 119 119 GLY GLY C . n 
C 1 107 PRO 107 120 120 PRO PRO C . n 
C 1 108 PRO 108 121 121 PRO PRO C . n 
C 1 109 PRO 109 122 122 PRO PRO C . n 
C 1 110 PRO 110 123 123 PRO PRO C . n 
C 1 111 PRO 111 124 124 PRO PRO C . n 
C 1 112 PRO 112 125 125 PRO PRO C . n 
C 1 113 ALA 113 126 126 ALA ALA C . n 
C 1 114 HIS 114 127 127 HIS HIS C . n 
C 1 115 ALA 115 128 128 ALA ALA C . n 
C 1 116 GLY 116 129 129 GLY GLY C . n 
C 1 117 GLY 117 130 130 GLY GLY C . n 
C 1 118 LEU 118 131 131 LEU LEU C . n 
C 1 119 ASN 119 132 132 ASN ASN C . n 
C 1 120 VAL 120 133 133 VAL VAL C . n 
C 1 121 HIS 121 134 134 HIS HIS C . n 
C 1 122 GLY 122 135 135 GLY GLY C . n 
C 1 123 THR 123 136 136 THR THR C . n 
C 1 124 PHE 124 137 137 PHE PHE C . n 
C 1 125 GLU 125 138 138 GLU GLU C . n 
C 1 126 GLY 126 139 139 GLY GLY C . n 
C 1 127 ASP 127 140 140 ASP ASP C . n 
C 1 128 ALA 128 141 141 ALA ALA C . n 
C 1 129 GLY 129 142 142 GLY GLY C . n 
C 1 130 MET 130 143 143 MET MET C . n 
C 1 131 THR 131 144 144 THR THR C . n 
C 1 132 ARG 132 145 145 ARG ARG C . n 
C 1 133 ALA 133 146 146 ALA ALA C . n 
C 1 134 ASP 134 147 147 ASP ASP C . n 
C 1 135 GLU 135 148 148 GLU GLU C . n 
C 1 136 PHE 136 149 149 PHE PHE C . n 
C 1 137 PHE 137 150 150 PHE PHE C . n 
C 1 138 GLY 138 151 151 GLY GLY C . n 
C 1 139 ASP 139 152 152 ASP ASP C . n 
C 1 140 ASN 140 153 153 ASN ASN C . n 
C 1 141 HIS 141 154 154 HIS HIS C . n 
C 1 142 SER 142 155 155 SER SER C . n 
C 1 143 PHE 143 156 156 PHE PHE C . n 
C 1 144 ASN 144 157 157 ASN ASN C . n 
C 1 145 GLN 145 158 158 GLN GLN C . n 
C 1 146 THR 146 159 159 THR THR C . n 
C 1 147 LEU 147 160 160 LEU LEU C . n 
C 1 148 PHE 148 161 161 PHE PHE C . n 
C 1 149 ASP 149 162 162 ASP ASP C . n 
C 1 150 LYS 150 163 163 LYS LYS C . n 
C 1 151 PHE 151 164 164 PHE PHE C . n 
C 1 152 VAL 152 165 165 VAL VAL C . n 
C 1 153 ASP 153 166 166 ASP ASP C . n 
C 1 154 PHE 154 167 167 PHE PHE C . n 
C 1 155 SER 155 168 168 SER SER C . n 
C 1 156 ASN 156 169 169 ASN ASN C . n 
C 1 157 ARG 157 170 170 ARG ARG C . n 
C 1 158 TYR 158 171 171 TYR TYR C . n 
C 1 159 GLY 159 172 172 GLY GLY C . n 
C 1 160 GLY 160 173 173 GLY GLY C . n 
C 1 161 GLY 161 174 174 GLY GLY C . n 
C 1 162 PHE 162 175 175 PHE PHE C . n 
C 1 163 TYR 163 176 176 TYR TYR C . n 
C 1 164 ASN 164 177 177 ASN ASN C . n 
C 1 165 LEU 165 178 178 LEU LEU C . n 
C 1 166 THR 166 179 179 THR THR C . n 
C 1 167 VAL 167 180 180 VAL VAL C . n 
C 1 168 ALA 168 181 181 ALA ALA C . n 
C 1 169 GLY 169 182 182 GLY GLY C . n 
C 1 170 GLU 170 183 183 GLU GLU C . n 
C 1 171 LEU 171 184 184 LEU LEU C . n 
C 1 172 ARG 172 185 185 ARG ARG C . n 
C 1 173 TYR 173 186 186 TYR TYR C . n 
C 1 174 SER 174 187 187 SER SER C . n 
C 1 175 ARG 175 188 188 ARG ARG C . n 
C 1 176 ILE 176 189 189 ILE ILE C . n 
C 1 177 GLN 177 190 190 GLN GLN C . n 
C 1 178 ASP 178 191 191 ASP ASP C . n 
C 1 179 SER 179 192 192 SER SER C . n 
C 1 180 ILE 180 193 193 ILE ILE C . n 
C 1 181 ALA 181 194 194 ALA ALA C . n 
C 1 182 THR 182 195 195 THR THR C . n 
C 1 183 ASN 183 196 196 ASN ASN C . n 
C 1 184 PRO 184 197 197 PRO PRO C . n 
C 1 185 GLU 185 198 198 GLU GLU C . n 
C 1 186 PHE 186 199 199 PHE PHE C . n 
C 1 187 GLN 187 200 200 GLN GLN C . n 
C 1 188 PHE 188 201 201 PHE PHE C . n 
C 1 189 LYS 189 202 202 LYS LYS C . n 
C 1 190 ASN 190 203 203 ASN ASN C . n 
C 1 191 VAL 191 204 204 VAL VAL C . n 
C 1 192 ARG 192 205 205 ARG ARG C . n 
C 1 193 PHE 193 206 206 PHE PHE C . n 
C 1 194 ILE 194 207 207 ILE ILE C . n 
C 1 195 THR 195 208 208 THR THR C . n 
C 1 196 ALA 196 209 209 ALA ALA C . n 
C 1 197 TYR 197 210 210 TYR TYR C . n 
C 1 198 GLY 198 211 211 GLY GLY C . n 
C 1 199 GLU 199 212 212 GLU GLU C . n 
C 1 200 THR 200 213 213 THR THR C . n 
C 1 201 VAL 201 214 214 VAL VAL C . n 
C 1 202 PHE 202 215 215 PHE PHE C . n 
C 1 203 PRO 203 216 216 PRO PRO C . n 
C 1 204 ILE 204 217 217 ILE ILE C . n 
C 1 205 ASN 205 218 218 ASN ASN C . n 
C 1 206 LEU 206 219 219 LEU LEU C . n 
C 1 207 PHE 207 220 220 PHE PHE C . n 
C 1 208 VAL 208 221 221 VAL VAL C . n 
C 1 209 ASP 209 222 222 ASP ASP C . n 
C 1 210 GLY 210 223 223 GLY GLY C . n 
C 1 211 ARG 211 224 224 ARG ARG C . n 
C 1 212 VAL 212 225 225 VAL VAL C . n 
C 1 213 THR 213 226 226 THR THR C . n 
C 1 214 THR 214 227 227 THR THR C . n 
C 1 215 ASP 215 228 228 ASP ASP C . n 
C 1 216 ARG 216 229 229 ARG ARG C . n 
C 1 217 LYS 217 230 230 LYS LYS C . n 
C 1 218 LEU 218 231 231 LEU LEU C . n 
C 1 219 SER 219 232 232 SER SER C . n 
C 1 220 MET 220 233 233 MET MET C . n 
C 1 221 GLU 221 234 234 GLU GLU C . n 
C 1 222 ASP 222 235 235 ASP ASP C . n 
C 1 223 ALA 223 236 236 ALA ALA C . n 
C 1 224 ALA 224 237 237 ALA ALA C . n 
C 1 225 SER 225 238 238 SER SER C . n 
C 1 226 ILE 226 239 239 ILE ILE C . n 
C 1 227 PHE 227 240 240 PHE PHE C . n 
C 1 228 ARG 228 241 241 ARG ARG C . n 
C 1 229 ASP 229 242 242 ASP ASP C . n 
C 1 230 MET 230 243 243 MET MET C . n 
C 1 231 ARG 231 244 244 ARG ARG C . n 
C 1 232 PHE 232 245 245 PHE PHE C . n 
C 1 233 PRO 233 246 246 PRO PRO C . n 
C 1 234 ASP 234 247 247 ASP ASP C . n 
C 1 235 ASP 235 248 248 ASP ASP C . n 
C 1 236 PHE 236 249 249 PHE PHE C . n 
C 1 237 HIS 237 250 250 HIS HIS C . n 
C 1 238 ARG 238 251 251 ARG ARG C . n 
C 1 239 SER 239 252 252 SER SER C . n 
C 1 240 ALA 240 253 253 ALA ALA C . n 
C 1 241 VAL 241 254 254 VAL VAL C . n 
C 1 242 PRO 242 255 255 PRO PRO C . n 
C 1 243 ALA 243 256 256 ALA ALA C . n 
C 1 244 SER 244 257 257 SER SER C . n 
C 1 245 ASN 245 258 258 ASN ASN C . n 
C 1 246 GLU 246 259 259 GLU GLU C . n 
C 1 247 GLY 247 260 260 GLY GLY C . n 
C 1 248 ALA 248 261 261 ALA ALA C . n 
C 1 249 ASP 249 262 262 ASP ASP C . n 
C 1 250 GLN 250 263 263 GLN GLN C . n 
C 1 251 VAL 251 264 264 VAL VAL C . n 
C 1 252 LEU 252 265 265 LEU LEU C . n 
C 1 253 ALA 253 266 266 ALA ALA C . n 
C 1 254 ALA 254 267 267 ALA ALA C . n 
C 1 255 HIS 255 268 268 HIS HIS C . n 
C 1 256 PRO 256 269 269 PRO PRO C . n 
C 1 257 TRP 257 270 270 TRP TRP C . n 
C 1 258 VAL 258 271 271 VAL VAL C . n 
C 1 259 PRO 259 272 272 PRO PRO C . n 
C 1 260 GLY 260 273 273 GLY GLY C . n 
C 1 261 GLY 261 274 274 GLY GLY C . n 
C 1 262 ASN 262 275 275 ASN ASN C . n 
C 1 263 ALA 263 276 276 ALA ALA C . n 
C 1 264 ASP 264 277 277 ASP ASP C . n 
C 1 265 ASN 265 278 278 ASN ASN C . n 
C 1 266 GLN 266 279 279 GLN GLN C . n 
C 1 267 VAL 267 280 280 VAL VAL C . n 
C 1 268 ASN 268 281 281 ASN ASN C . n 
C 1 269 ASN 269 282 282 ASN ASN C . n 
C 1 270 TYR 270 283 283 TYR TYR C . n 
C 1 271 VAL 271 284 284 VAL VAL C . n 
C 1 272 GLU 272 285 285 GLU GLU C . n 
C 1 273 ASP 273 286 286 ASP ASP C . n 
C 1 274 PRO 274 287 287 PRO PRO C . n 
C 1 275 ASP 275 288 288 ASP ASP C . n 
C 1 276 SER 276 289 289 SER SER C . n 
C 1 277 ALA 277 290 290 ALA ALA C . n 
C 1 278 ASP 278 291 291 ASP ASP C . n 
C 1 279 PHE 279 292 292 PHE PHE C . n 
C 1 280 THR 280 293 293 THR THR C . n 
C 1 281 HIS 281 294 294 HIS HIS C . n 
C 1 282 LEU 282 295 295 LEU LEU C . n 
C 1 283 CYS 283 296 296 CYS CYS C . n 
C 1 284 ARG 284 297 297 ARG ARG C . n 
C 1 285 LEU 285 298 298 LEU LEU C . n 
C 1 286 TYR 286 299 299 TYR TYR C . n 
C 1 287 GLU 287 300 300 GLU GLU C . n 
C 1 288 PHE 288 301 301 PHE PHE C . n 
C 1 289 VAL 289 302 302 VAL VAL C . n 
C 1 290 VAL 290 303 303 VAL VAL C . n 
C 1 291 GLY 291 304 304 GLY GLY C . n 
C 1 292 SER 292 305 305 SER SER C . n 
C 1 293 VAL 293 306 306 VAL VAL C . n 
C 1 294 GLN 294 307 307 GLN GLN C . n 
C 1 295 GLU 295 308 308 GLU GLU C . n 
C 1 296 LEU 296 309 309 LEU LEU C . n 
C 1 297 TYR 297 310 310 TYR TYR C . n 
C 1 298 PRO 298 311 311 PRO PRO C . n 
C 1 299 ASN 299 312 312 ASN ASN C . n 
C 1 300 PRO 300 313 313 PRO PRO C . n 
C 1 301 THR 301 314 314 THR THR C . n 
C 1 302 GLY 302 315 315 GLY GLY C . n 
C 1 303 ILE 303 316 316 ILE ILE C . n 
C 1 304 LEU 304 317 317 LEU LEU C . n 
C 1 305 ARG 305 318 318 ARG ARG C . n 
C 1 306 ARG 306 319 319 ARG ARG C . n 
C 1 307 ASN 307 320 320 ASN ASN C . n 
C 1 308 LEU 308 321 321 LEU LEU C . n 
C 1 309 ILE 309 322 322 ILE ILE C . n 
C 1 310 LYS 310 323 323 LYS LYS C . n 
C 1 311 ASN 311 324 324 ASN ASN C . n 
C 1 312 LEU 312 325 325 LEU LEU C . n 
C 1 313 HIS 313 326 326 HIS HIS C . n 
C 1 314 TYR 314 327 327 TYR TYR C . n 
C 1 315 TRP 315 328 328 TRP TRP C . n 
C 1 316 TRP 316 329 329 TRP TRP C . n 
C 1 317 THR 317 330 330 THR THR C . n 
C 1 318 GLY 318 331 331 GLY GLY C . n 
C 1 319 VAL 319 332 332 VAL VAL C . n 
C 1 320 ASN 320 333 333 ASN ASN C . n 
C 1 321 VAL 321 334 334 VAL VAL C . n 
C 1 322 ALA 322 335 335 ALA ALA C . n 
C 1 323 PHE 323 336 336 PHE PHE C . n 
C 1 324 GLY 324 337 337 GLY GLY C . n 
C 1 325 GLY 325 338 338 GLY GLY C . n 
C 1 326 CYS 326 339 339 CYS CYS C . n 
C 1 327 ASP 327 340 340 ASP ASP C . n 
C 1 328 GLU 328 341 341 GLU GLU C . n 
C 1 329 LEU 329 342 342 LEU LEU C . n 
C 1 330 PHE 330 343 343 PHE PHE C . n 
C 1 331 PRO 331 344 344 PRO PRO C . n 
C 1 332 TYR 332 345 345 TYR TYR C . n 
C 1 333 GLY 333 346 346 GLY GLY C . n 
C 1 334 GLN 334 347 347 GLN GLN C . n 
C 1 335 LEU 335 348 348 LEU LEU C . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
D 2 NAG 1 G NAG 1 A NAG 402 n 
D 2 NAG 2 G NAG 2 A NAG 403 n 
D 2 BMA 3 G BMA 3 A BMA 425 n 
D 2 MAN 4 G MAN 4 A MAN 427 n 
D 2 MAN 5 G MAN 5 A MAN 426 n 
E 3 NAG 1 I NAG 1 A NAG 404 n 
E 3 NAG 2 I NAG 2 A NAG 405 n 
E 3 BMA 3 I BMA 3 A BMA 406 n 
E 3 MAN 4 I MAN 4 A MAN 407 n 
E 3 MAN 5 I MAN 5 A MAN 408 n 
E 3 MAN 6 I MAN 6 A MAN 409 n 
E 3 MAN 7 I MAN 7 A MAN 414 n 
F 4 NAG 1 Z NAG 1 B NAG 402 n 
F 4 NAG 2 Z NAG 2 B NAG 413 n 
F 4 BMA 3 Z BMA 3 B BMA 416 n 
F 4 MAN 4 Z MAN 4 B MAN 419 n 
G 5 NAG 1 a NAG 1 B NAG 404 n 
G 5 NAG 2 a NAG 2 B NAG 405 n 
G 5 BMA 3 a BMA 3 B BMA 406 n 
G 5 MAN 4 a MAN 4 B MAN 408 n 
G 5 MAN 5 a MAN 5 B MAN 409 n 
G 5 MAN 6 a MAN 6 B MAN 407 n 
H 4 NAG 1 q NAG 1 C NAG 402 n 
H 4 NAG 2 q NAG 2 C NAG 403 n 
H 4 BMA 3 q BMA 3 C BMA 407 n 
H 4 MAN 4 q MAN 4 C MAN 411 n 
I 6 NAG 1 s NAG 1 C NAG 404 n 
I 6 NAG 2 s NAG 2 C NAG 405 n 
I 6 BMA 3 s BMA 3 C BMA 406 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MYR ? ? MYR ? ? '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  MYR 1   401 421 MYR MYR A . 
K  8  GOL 1   402 423 GOL GOL A . 
L  9  EPE 1   403 424 EPE EPE A . 
M  8  GOL 1   404 428 GOL GOL A . 
N  8  GOL 1   405 429 GOL GOL A . 
O  10 HEM 1   406 431 HEM HEM A . 
P  11 SO4 1   407 1   SO4 SO4 A . 
Q  11 SO4 1   408 2   SO4 SO4 A . 
R  11 SO4 1   409 3   SO4 SO4 A . 
S  11 SO4 1   410 7   SO4 SO4 A . 
T  12 MG  1   411 1   MG  MG  A . 
U  7  MYR 1   401 410 MYR MYR B . 
V  9  EPE 1   402 412 EPE EPE B . 
W  8  GOL 1   403 414 GOL GOL B . 
X  9  EPE 1   404 415 EPE EPE B . 
Y  8  GOL 1   405 417 GOL GOL B . 
Z  10 HEM 1   406 421 HEM HEM B . 
AA 11 SO4 1   407 4   SO4 SO4 B . 
BA 12 MG  1   408 2   MG  MG  B . 
CA 7  MYR 1   401 412 MYR MYR C . 
DA 8  GOL 1   402 413 GOL GOL C . 
EA 10 HEM 1   403 414 HEM HEM C . 
FA 11 SO4 1   404 5   SO4 SO4 C . 
GA 11 SO4 1   405 6   SO4 SO4 C . 
HA 12 MG  1   406 3   MG  MG  C . 
IA 13 HOH 1   501 505 HOH HOH A . 
IA 13 HOH 2   502 378 HOH HOH A . 
IA 13 HOH 3   503 890 HOH HOH A . 
IA 13 HOH 4   504 504 HOH HOH A . 
IA 13 HOH 5   505 735 HOH HOH A . 
IA 13 HOH 6   506 579 HOH HOH A . 
IA 13 HOH 7   507 465 HOH HOH A . 
IA 13 HOH 8   508 173 HOH HOH A . 
IA 13 HOH 9   509 313 HOH HOH A . 
IA 13 HOH 10  510 48  HOH HOH A . 
IA 13 HOH 11  511 7   HOH HOH A . 
IA 13 HOH 12  512 773 HOH HOH A . 
IA 13 HOH 13  513 132 HOH HOH A . 
IA 13 HOH 14  514 756 HOH HOH A . 
IA 13 HOH 15  515 767 HOH HOH A . 
IA 13 HOH 16  516 760 HOH HOH A . 
IA 13 HOH 17  517 209 HOH HOH A . 
IA 13 HOH 18  518 316 HOH HOH A . 
IA 13 HOH 19  519 73  HOH HOH A . 
IA 13 HOH 20  520 363 HOH HOH A . 
IA 13 HOH 21  521 1   HOH HOH A . 
IA 13 HOH 22  522 264 HOH HOH A . 
IA 13 HOH 23  523 878 HOH HOH A . 
IA 13 HOH 24  524 40  HOH HOH A . 
IA 13 HOH 25  525 23  HOH HOH A . 
IA 13 HOH 26  526 388 HOH HOH A . 
IA 13 HOH 27  527 456 HOH HOH A . 
IA 13 HOH 28  528 718 HOH HOH A . 
IA 13 HOH 29  529 99  HOH HOH A . 
IA 13 HOH 30  530 411 HOH HOH A . 
IA 13 HOH 31  531 747 HOH HOH A . 
IA 13 HOH 32  532 752 HOH HOH A . 
IA 13 HOH 33  533 147 HOH HOH A . 
IA 13 HOH 34  534 328 HOH HOH A . 
IA 13 HOH 35  535 493 HOH HOH A . 
IA 13 HOH 36  536 15  HOH HOH A . 
IA 13 HOH 37  537 651 HOH HOH A . 
IA 13 HOH 38  538 360 HOH HOH A . 
IA 13 HOH 39  539 715 HOH HOH A . 
IA 13 HOH 40  540 126 HOH HOH A . 
IA 13 HOH 41  541 525 HOH HOH A . 
IA 13 HOH 42  542 13  HOH HOH A . 
IA 13 HOH 43  543 35  HOH HOH A . 
IA 13 HOH 44  544 399 HOH HOH A . 
IA 13 HOH 45  545 26  HOH HOH A . 
IA 13 HOH 46  546 425 HOH HOH A . 
IA 13 HOH 47  547 89  HOH HOH A . 
IA 13 HOH 48  548 186 HOH HOH A . 
IA 13 HOH 49  549 183 HOH HOH A . 
IA 13 HOH 50  550 3   HOH HOH A . 
IA 13 HOH 51  551 691 HOH HOH A . 
IA 13 HOH 52  552 203 HOH HOH A . 
IA 13 HOH 53  553 83  HOH HOH A . 
IA 13 HOH 54  554 44  HOH HOH A . 
IA 13 HOH 55  555 750 HOH HOH A . 
IA 13 HOH 56  556 45  HOH HOH A . 
IA 13 HOH 57  557 383 HOH HOH A . 
IA 13 HOH 58  558 294 HOH HOH A . 
IA 13 HOH 59  559 189 HOH HOH A . 
IA 13 HOH 60  560 196 HOH HOH A . 
IA 13 HOH 61  561 778 HOH HOH A . 
IA 13 HOH 62  562 286 HOH HOH A . 
IA 13 HOH 63  563 379 HOH HOH A . 
IA 13 HOH 64  564 63  HOH HOH A . 
IA 13 HOH 65  565 707 HOH HOH A . 
IA 13 HOH 66  566 705 HOH HOH A . 
IA 13 HOH 67  567 754 HOH HOH A . 
IA 13 HOH 68  568 103 HOH HOH A . 
IA 13 HOH 69  569 104 HOH HOH A . 
IA 13 HOH 70  570 713 HOH HOH A . 
IA 13 HOH 71  571 683 HOH HOH A . 
IA 13 HOH 72  572 131 HOH HOH A . 
IA 13 HOH 73  573 748 HOH HOH A . 
IA 13 HOH 74  574 18  HOH HOH A . 
IA 13 HOH 75  575 350 HOH HOH A . 
IA 13 HOH 76  576 221 HOH HOH A . 
IA 13 HOH 77  577 69  HOH HOH A . 
IA 13 HOH 78  578 295 HOH HOH A . 
IA 13 HOH 79  579 476 HOH HOH A . 
IA 13 HOH 80  580 176 HOH HOH A . 
IA 13 HOH 81  581 389 HOH HOH A . 
IA 13 HOH 82  582 75  HOH HOH A . 
IA 13 HOH 83  583 348 HOH HOH A . 
IA 13 HOH 84  584 355 HOH HOH A . 
IA 13 HOH 85  585 303 HOH HOH A . 
IA 13 HOH 86  586 226 HOH HOH A . 
IA 13 HOH 87  587 120 HOH HOH A . 
IA 13 HOH 88  588 271 HOH HOH A . 
IA 13 HOH 89  589 140 HOH HOH A . 
IA 13 HOH 90  590 373 HOH HOH A . 
IA 13 HOH 91  591 708 HOH HOH A . 
IA 13 HOH 92  592 74  HOH HOH A . 
IA 13 HOH 93  593 150 HOH HOH A . 
IA 13 HOH 94  594 96  HOH HOH A . 
IA 13 HOH 95  595 148 HOH HOH A . 
IA 13 HOH 96  596 37  HOH HOH A . 
IA 13 HOH 97  597 272 HOH HOH A . 
IA 13 HOH 98  598 92  HOH HOH A . 
IA 13 HOH 99  599 518 HOH HOH A . 
IA 13 HOH 100 600 258 HOH HOH A . 
IA 13 HOH 101 601 133 HOH HOH A . 
IA 13 HOH 102 602 134 HOH HOH A . 
IA 13 HOH 103 603 17  HOH HOH A . 
IA 13 HOH 104 604 359 HOH HOH A . 
IA 13 HOH 105 605 308 HOH HOH A . 
IA 13 HOH 106 606 265 HOH HOH A . 
IA 13 HOH 107 607 6   HOH HOH A . 
IA 13 HOH 108 608 755 HOH HOH A . 
IA 13 HOH 109 609 19  HOH HOH A . 
IA 13 HOH 110 610 53  HOH HOH A . 
IA 13 HOH 111 611 726 HOH HOH A . 
IA 13 HOH 112 612 60  HOH HOH A . 
IA 13 HOH 113 613 244 HOH HOH A . 
IA 13 HOH 114 614 168 HOH HOH A . 
IA 13 HOH 115 615 70  HOH HOH A . 
IA 13 HOH 116 616 320 HOH HOH A . 
IA 13 HOH 117 617 129 HOH HOH A . 
IA 13 HOH 118 618 215 HOH HOH A . 
IA 13 HOH 119 619 392 HOH HOH A . 
IA 13 HOH 120 620 426 HOH HOH A . 
IA 13 HOH 121 621 897 HOH HOH A . 
IA 13 HOH 122 622 292 HOH HOH A . 
IA 13 HOH 123 623 93  HOH HOH A . 
IA 13 HOH 124 624 245 HOH HOH A . 
IA 13 HOH 125 625 109 HOH HOH A . 
IA 13 HOH 126 626 758 HOH HOH A . 
IA 13 HOH 127 627 266 HOH HOH A . 
IA 13 HOH 128 628 421 HOH HOH A . 
IA 13 HOH 129 629 68  HOH HOH A . 
IA 13 HOH 130 630 693 HOH HOH A . 
IA 13 HOH 131 631 770 HOH HOH A . 
IA 13 HOH 132 632 356 HOH HOH A . 
IA 13 HOH 133 633 480 HOH HOH A . 
IA 13 HOH 134 634 163 HOH HOH A . 
IA 13 HOH 135 635 20  HOH HOH A . 
IA 13 HOH 136 636 274 HOH HOH A . 
IA 13 HOH 137 637 387 HOH HOH A . 
IA 13 HOH 138 638 232 HOH HOH A . 
IA 13 HOH 139 639 777 HOH HOH A . 
IA 13 HOH 140 640 502 HOH HOH A . 
IA 13 HOH 141 641 740 HOH HOH A . 
IA 13 HOH 142 642 49  HOH HOH A . 
IA 13 HOH 143 643 489 HOH HOH A . 
IA 13 HOH 144 644 270 HOH HOH A . 
IA 13 HOH 145 645 187 HOH HOH A . 
IA 13 HOH 146 646 222 HOH HOH A . 
IA 13 HOH 147 647 227 HOH HOH A . 
IA 13 HOH 148 648 466 HOH HOH A . 
IA 13 HOH 149 649 12  HOH HOH A . 
IA 13 HOH 150 650 278 HOH HOH A . 
IA 13 HOH 151 651 302 HOH HOH A . 
IA 13 HOH 152 652 146 HOH HOH A . 
IA 13 HOH 153 653 194 HOH HOH A . 
IA 13 HOH 154 654 157 HOH HOH A . 
IA 13 HOH 155 655 136 HOH HOH A . 
IA 13 HOH 156 656 11  HOH HOH A . 
IA 13 HOH 157 657 333 HOH HOH A . 
IA 13 HOH 158 658 478 HOH HOH A . 
IA 13 HOH 159 659 97  HOH HOH A . 
IA 13 HOH 160 660 589 HOH HOH A . 
IA 13 HOH 161 661 181 HOH HOH A . 
IA 13 HOH 162 662 454 HOH HOH A . 
IA 13 HOH 163 663 330 HOH HOH A . 
IA 13 HOH 164 664 236 HOH HOH A . 
IA 13 HOH 165 665 282 HOH HOH A . 
IA 13 HOH 166 666 357 HOH HOH A . 
IA 13 HOH 167 667 380 HOH HOH A . 
IA 13 HOH 168 668 115 HOH HOH A . 
IA 13 HOH 169 669 404 HOH HOH A . 
IA 13 HOH 170 670 769 HOH HOH A . 
IA 13 HOH 171 671 312 HOH HOH A . 
IA 13 HOH 172 672 771 HOH HOH A . 
IA 13 HOH 173 673 344 HOH HOH A . 
IA 13 HOH 174 674 453 HOH HOH A . 
IA 13 HOH 175 675 369 HOH HOH A . 
IA 13 HOH 176 676 72  HOH HOH A . 
IA 13 HOH 177 677 142 HOH HOH A . 
IA 13 HOH 178 678 526 HOH HOH A . 
IA 13 HOH 179 679 90  HOH HOH A . 
IA 13 HOH 180 680 216 HOH HOH A . 
IA 13 HOH 181 681 745 HOH HOH A . 
IA 13 HOH 182 682 395 HOH HOH A . 
IA 13 HOH 183 683 739 HOH HOH A . 
IA 13 HOH 184 684 177 HOH HOH A . 
IA 13 HOH 185 685 382 HOH HOH A . 
IA 13 HOH 186 686 285 HOH HOH A . 
IA 13 HOH 187 687 116 HOH HOH A . 
IA 13 HOH 188 688 113 HOH HOH A . 
IA 13 HOH 189 689 503 HOH HOH A . 
IA 13 HOH 190 690 385 HOH HOH A . 
IA 13 HOH 191 691 65  HOH HOH A . 
IA 13 HOH 192 692 33  HOH HOH A . 
IA 13 HOH 193 693 720 HOH HOH A . 
IA 13 HOH 194 694 391 HOH HOH A . 
IA 13 HOH 195 695 709 HOH HOH A . 
IA 13 HOH 196 696 108 HOH HOH A . 
IA 13 HOH 197 697 58  HOH HOH A . 
IA 13 HOH 198 698 39  HOH HOH A . 
IA 13 HOH 199 699 16  HOH HOH A . 
IA 13 HOH 200 700 110 HOH HOH A . 
IA 13 HOH 201 701 155 HOH HOH A . 
IA 13 HOH 202 702 114 HOH HOH A . 
IA 13 HOH 203 703 301 HOH HOH A . 
IA 13 HOH 204 704 145 HOH HOH A . 
IA 13 HOH 205 705 523 HOH HOH A . 
IA 13 HOH 206 706 296 HOH HOH A . 
IA 13 HOH 207 707 64  HOH HOH A . 
IA 13 HOH 208 708 193 HOH HOH A . 
IA 13 HOH 209 709 246 HOH HOH A . 
IA 13 HOH 210 710 768 HOH HOH A . 
IA 13 HOH 211 711 59  HOH HOH A . 
IA 13 HOH 212 712 164 HOH HOH A . 
IA 13 HOH 213 713 591 HOH HOH A . 
IA 13 HOH 214 714 124 HOH HOH A . 
IA 13 HOH 215 715 240 HOH HOH A . 
IA 13 HOH 216 716 481 HOH HOH A . 
IA 13 HOH 217 717 753 HOH HOH A . 
IA 13 HOH 218 718 84  HOH HOH A . 
IA 13 HOH 219 719 654 HOH HOH A . 
IA 13 HOH 220 720 61  HOH HOH A . 
IA 13 HOH 221 721 484 HOH HOH A . 
IA 13 HOH 222 722 418 HOH HOH A . 
IA 13 HOH 223 723 742 HOH HOH A . 
IA 13 HOH 224 724 336 HOH HOH A . 
IA 13 HOH 225 725 812 HOH HOH A . 
IA 13 HOH 226 726 325 HOH HOH A . 
IA 13 HOH 227 727 751 HOH HOH A . 
IA 13 HOH 228 728 242 HOH HOH A . 
IA 13 HOH 229 729 515 HOH HOH A . 
IA 13 HOH 230 730 260 HOH HOH A . 
IA 13 HOH 231 731 262 HOH HOH A . 
IA 13 HOH 232 732 457 HOH HOH A . 
IA 13 HOH 233 733 208 HOH HOH A . 
IA 13 HOH 234 734 341 HOH HOH A . 
IA 13 HOH 235 735 335 HOH HOH A . 
IA 13 HOH 236 736 106 HOH HOH A . 
IA 13 HOH 237 737 512 HOH HOH A . 
IA 13 HOH 238 738 746 HOH HOH A . 
IA 13 HOH 239 739 248 HOH HOH A . 
IA 13 HOH 240 740 766 HOH HOH A . 
IA 13 HOH 241 741 138 HOH HOH A . 
IA 13 HOH 242 742 728 HOH HOH A . 
IA 13 HOH 243 743 41  HOH HOH A . 
IA 13 HOH 244 744 10  HOH HOH A . 
IA 13 HOH 245 745 600 HOH HOH A . 
IA 13 HOH 246 746 776 HOH HOH A . 
IA 13 HOH 247 747 228 HOH HOH A . 
IA 13 HOH 248 748 520 HOH HOH A . 
IA 13 HOH 249 749 420 HOH HOH A . 
IA 13 HOH 250 750 590 HOH HOH A . 
IA 13 HOH 251 751 463 HOH HOH A . 
IA 13 HOH 252 752 327 HOH HOH A . 
IA 13 HOH 253 753 886 HOH HOH A . 
IA 13 HOH 254 754 417 HOH HOH A . 
IA 13 HOH 255 755 519 HOH HOH A . 
IA 13 HOH 256 756 737 HOH HOH A . 
IA 13 HOH 257 757 774 HOH HOH A . 
IA 13 HOH 258 758 451 HOH HOH A . 
IA 13 HOH 259 759 309 HOH HOH A . 
IA 13 HOH 260 760 452 HOH HOH A . 
IA 13 HOH 261 761 513 HOH HOH A . 
IA 13 HOH 262 762 432 HOH HOH A . 
IA 13 HOH 263 763 436 HOH HOH A . 
IA 13 HOH 264 764 111 HOH HOH A . 
IA 13 HOH 265 765 161 HOH HOH A . 
IA 13 HOH 266 766 738 HOH HOH A . 
IA 13 HOH 267 767 472 HOH HOH A . 
IA 13 HOH 268 768 761 HOH HOH A . 
IA 13 HOH 269 769 687 HOH HOH A . 
IA 13 HOH 270 770 346 HOH HOH A . 
IA 13 HOH 271 771 876 HOH HOH A . 
IA 13 HOH 272 772 247 HOH HOH A . 
IA 13 HOH 273 773 437 HOH HOH A . 
IA 13 HOH 274 774 701 HOH HOH A . 
IA 13 HOH 275 775 541 HOH HOH A . 
IA 13 HOH 276 776 641 HOH HOH A . 
IA 13 HOH 277 777 449 HOH HOH A . 
IA 13 HOH 278 778 514 HOH HOH A . 
IA 13 HOH 279 779 702 HOH HOH A . 
IA 13 HOH 280 780 442 HOH HOH A . 
IA 13 HOH 281 781 415 HOH HOH A . 
IA 13 HOH 282 782 474 HOH HOH A . 
IA 13 HOH 283 783 684 HOH HOH A . 
IA 13 HOH 284 784 401 HOH HOH A . 
IA 13 HOH 285 785 483 HOH HOH A . 
IA 13 HOH 286 786 539 HOH HOH A . 
IA 13 HOH 287 787 322 HOH HOH A . 
IA 13 HOH 288 788 524 HOH HOH A . 
IA 13 HOH 289 789 759 HOH HOH A . 
IA 13 HOH 290 790 393 HOH HOH A . 
IA 13 HOH 291 791 891 HOH HOH A . 
IA 13 HOH 292 792 730 HOH HOH A . 
IA 13 HOH 293 793 482 HOH HOH A . 
IA 13 HOH 294 794 714 HOH HOH A . 
IA 13 HOH 295 795 772 HOH HOH A . 
IA 13 HOH 296 796 775 HOH HOH A . 
IA 13 HOH 297 797 724 HOH HOH A . 
IA 13 HOH 298 798 889 HOH HOH A . 
IA 13 HOH 299 799 506 HOH HOH A . 
IA 13 HOH 300 800 464 HOH HOH A . 
IA 13 HOH 301 801 877 HOH HOH A . 
IA 13 HOH 302 802 710 HOH HOH A . 
IA 13 HOH 303 803 646 HOH HOH A . 
IA 13 HOH 304 804 736 HOH HOH A . 
IA 13 HOH 305 805 507 HOH HOH A . 
IA 13 HOH 306 806 712 HOH HOH A . 
IA 13 HOH 307 807 521 HOH HOH A . 
IA 13 HOH 308 808 509 HOH HOH A . 
IA 13 HOH 309 809 287 HOH HOH A . 
IA 13 HOH 310 810 704 HOH HOH A . 
IA 13 HOH 311 811 510 HOH HOH A . 
IA 13 HOH 312 812 469 HOH HOH A . 
IA 13 HOH 313 813 460 HOH HOH A . 
IA 13 HOH 314 814 716 HOH HOH A . 
IA 13 HOH 315 815 749 HOH HOH A . 
IA 13 HOH 316 816 731 HOH HOH A . 
IA 13 HOH 317 817 211 HOH HOH A . 
IA 13 HOH 318 818 765 HOH HOH A . 
IA 13 HOH 319 819 443 HOH HOH A . 
IA 13 HOH 320 820 764 HOH HOH A . 
IA 13 HOH 321 821 500 HOH HOH A . 
IA 13 HOH 322 822 473 HOH HOH A . 
IA 13 HOH 323 823 875 HOH HOH A . 
IA 13 HOH 324 824 479 HOH HOH A . 
IA 13 HOH 325 825 495 HOH HOH A . 
IA 13 HOH 326 826 660 HOH HOH A . 
IA 13 HOH 327 827 652 HOH HOH A . 
IA 13 HOH 328 828 699 HOH HOH A . 
IA 13 HOH 329 829 743 HOH HOH A . 
IA 13 HOH 330 830 477 HOH HOH A . 
IA 13 HOH 331 831 423 HOH HOH A . 
IA 13 HOH 332 832 446 HOH HOH A . 
IA 13 HOH 333 833 458 HOH HOH A . 
IA 13 HOH 334 834 682 HOH HOH A . 
IA 13 HOH 335 835 511 HOH HOH A . 
IA 13 HOH 336 836 416 HOH HOH A . 
IA 13 HOH 337 837 364 HOH HOH A . 
IA 13 HOH 338 838 439 HOH HOH A . 
IA 13 HOH 339 839 522 HOH HOH A . 
IA 13 HOH 340 840 706 HOH HOH A . 
IA 13 HOH 341 841 703 HOH HOH A . 
IA 13 HOH 342 842 475 HOH HOH A . 
IA 13 HOH 343 843 491 HOH HOH A . 
IA 13 HOH 344 844 685 HOH HOH A . 
IA 13 HOH 345 845 448 HOH HOH A . 
IA 13 HOH 346 846 311 HOH HOH A . 
IA 13 HOH 347 847 431 HOH HOH A . 
IA 13 HOH 348 848 485 HOH HOH A . 
IA 13 HOH 349 849 310 HOH HOH A . 
IA 13 HOH 350 850 700 HOH HOH A . 
IA 13 HOH 351 851 471 HOH HOH A . 
IA 13 HOH 352 852 501 HOH HOH A . 
IA 13 HOH 353 853 280 HOH HOH A . 
IA 13 HOH 354 854 686 HOH HOH A . 
IA 13 HOH 355 855 711 HOH HOH A . 
IA 13 HOH 356 856 492 HOH HOH A . 
IA 13 HOH 357 857 470 HOH HOH A . 
IA 13 HOH 358 858 757 HOH HOH A . 
IA 13 HOH 359 859 741 HOH HOH A . 
IA 13 HOH 360 860 455 HOH HOH A . 
IA 13 HOH 361 861 744 HOH HOH A . 
IA 13 HOH 362 862 450 HOH HOH A . 
IA 13 HOH 363 863 218 HOH HOH A . 
JA 13 HOH 1   501 537 HOH HOH B . 
JA 13 HOH 2   502 207 HOH HOH B . 
JA 13 HOH 3   503 561 HOH HOH B . 
JA 13 HOH 4   504 412 HOH HOH B . 
JA 13 HOH 5   505 527 HOH HOH B . 
JA 13 HOH 6   506 430 HOH HOH B . 
JA 13 HOH 7   507 544 HOH HOH B . 
JA 13 HOH 8   508 762 HOH HOH B . 
JA 13 HOH 9   509 107 HOH HOH B . 
JA 13 HOH 10  510 535 HOH HOH B . 
JA 13 HOH 11  511 825 HOH HOH B . 
JA 13 HOH 12  512 552 HOH HOH B . 
JA 13 HOH 13  513 371 HOH HOH B . 
JA 13 HOH 14  514 528 HOH HOH B . 
JA 13 HOH 15  515 559 HOH HOH B . 
JA 13 HOH 16  516 253 HOH HOH B . 
JA 13 HOH 17  517 188 HOH HOH B . 
JA 13 HOH 18  518 566 HOH HOH B . 
JA 13 HOH 19  519 153 HOH HOH B . 
JA 13 HOH 20  520 560 HOH HOH B . 
JA 13 HOH 21  521 42  HOH HOH B . 
JA 13 HOH 22  522 28  HOH HOH B . 
JA 13 HOH 23  523 381 HOH HOH B . 
JA 13 HOH 24  524 547 HOH HOH B . 
JA 13 HOH 25  525 823 HOH HOH B . 
JA 13 HOH 26  526 555 HOH HOH B . 
JA 13 HOH 27  527 241 HOH HOH B . 
JA 13 HOH 28  528 534 HOH HOH B . 
JA 13 HOH 29  529 144 HOH HOH B . 
JA 13 HOH 30  530 599 HOH HOH B . 
JA 13 HOH 31  531 588 HOH HOH B . 
JA 13 HOH 32  532 81  HOH HOH B . 
JA 13 HOH 33  533 529 HOH HOH B . 
JA 13 HOH 34  534 571 HOH HOH B . 
JA 13 HOH 35  535 668 HOH HOH B . 
JA 13 HOH 36  536 342 HOH HOH B . 
JA 13 HOH 37  537 317 HOH HOH B . 
JA 13 HOH 38  538 67  HOH HOH B . 
JA 13 HOH 39  539 297 HOH HOH B . 
JA 13 HOH 40  540 602 HOH HOH B . 
JA 13 HOH 41  541 669 HOH HOH B . 
JA 13 HOH 42  542 338 HOH HOH B . 
JA 13 HOH 43  543 172 HOH HOH B . 
JA 13 HOH 44  544 224 HOH HOH B . 
JA 13 HOH 45  545 210 HOH HOH B . 
JA 13 HOH 46  546 66  HOH HOH B . 
JA 13 HOH 47  547 568 HOH HOH B . 
JA 13 HOH 48  548 261 HOH HOH B . 
JA 13 HOH 49  549 304 HOH HOH B . 
JA 13 HOH 50  550 815 HOH HOH B . 
JA 13 HOH 51  551 830 HOH HOH B . 
JA 13 HOH 52  552 14  HOH HOH B . 
JA 13 HOH 53  553 4   HOH HOH B . 
JA 13 HOH 54  554 80  HOH HOH B . 
JA 13 HOH 55  555 813 HOH HOH B . 
JA 13 HOH 56  556 293 HOH HOH B . 
JA 13 HOH 57  557 151 HOH HOH B . 
JA 13 HOH 58  558 494 HOH HOH B . 
JA 13 HOH 59  559 662 HOH HOH B . 
JA 13 HOH 60  560 663 HOH HOH B . 
JA 13 HOH 61  561 180 HOH HOH B . 
JA 13 HOH 62  562 249 HOH HOH B . 
JA 13 HOH 63  563 32  HOH HOH B . 
JA 13 HOH 64  564 429 HOH HOH B . 
JA 13 HOH 65  565 122 HOH HOH B . 
JA 13 HOH 66  566 553 HOH HOH B . 
JA 13 HOH 67  567 165 HOH HOH B . 
JA 13 HOH 68  568 78  HOH HOH B . 
JA 13 HOH 69  569 413 HOH HOH B . 
JA 13 HOH 70  570 508 HOH HOH B . 
JA 13 HOH 71  571 895 HOH HOH B . 
JA 13 HOH 72  572 202 HOH HOH B . 
JA 13 HOH 73  573 101 HOH HOH B . 
JA 13 HOH 74  574 190 HOH HOH B . 
JA 13 HOH 75  575 29  HOH HOH B . 
JA 13 HOH 76  576 30  HOH HOH B . 
JA 13 HOH 77  577 874 HOH HOH B . 
JA 13 HOH 78  578 299 HOH HOH B . 
JA 13 HOH 79  579 326 HOH HOH B . 
JA 13 HOH 80  580 572 HOH HOH B . 
JA 13 HOH 81  581 52  HOH HOH B . 
JA 13 HOH 82  582 252 HOH HOH B . 
JA 13 HOH 83  583 542 HOH HOH B . 
JA 13 HOH 84  584 105 HOH HOH B . 
JA 13 HOH 85  585 71  HOH HOH B . 
JA 13 HOH 86  586 87  HOH HOH B . 
JA 13 HOH 87  587 672 HOH HOH B . 
JA 13 HOH 88  588 809 HOH HOH B . 
JA 13 HOH 89  589 235 HOH HOH B . 
JA 13 HOH 90  590 24  HOH HOH B . 
JA 13 HOH 91  591 347 HOH HOH B . 
JA 13 HOH 92  592 405 HOH HOH B . 
JA 13 HOH 93  593 828 HOH HOH B . 
JA 13 HOH 94  594 275 HOH HOH B . 
JA 13 HOH 95  595 337 HOH HOH B . 
JA 13 HOH 96  596 496 HOH HOH B . 
JA 13 HOH 97  597 314 HOH HOH B . 
JA 13 HOH 98  598 137 HOH HOH B . 
JA 13 HOH 99  599 229 HOH HOH B . 
JA 13 HOH 100 600 182 HOH HOH B . 
JA 13 HOH 101 601 46  HOH HOH B . 
JA 13 HOH 102 602 789 HOH HOH B . 
JA 13 HOH 103 603 307 HOH HOH B . 
JA 13 HOH 104 604 324 HOH HOH B . 
JA 13 HOH 105 605 820 HOH HOH B . 
JA 13 HOH 106 606 376 HOH HOH B . 
JA 13 HOH 107 607 690 HOH HOH B . 
JA 13 HOH 108 608 76  HOH HOH B . 
JA 13 HOH 109 609 281 HOH HOH B . 
JA 13 HOH 110 610 811 HOH HOH B . 
JA 13 HOH 111 611 256 HOH HOH B . 
JA 13 HOH 112 612 213 HOH HOH B . 
JA 13 HOH 113 613 536 HOH HOH B . 
JA 13 HOH 114 614 269 HOH HOH B . 
JA 13 HOH 115 615 562 HOH HOH B . 
JA 13 HOH 116 616 98  HOH HOH B . 
JA 13 HOH 117 617 808 HOH HOH B . 
JA 13 HOH 118 618 803 HOH HOH B . 
JA 13 HOH 119 619 143 HOH HOH B . 
JA 13 HOH 120 620 563 HOH HOH B . 
JA 13 HOH 121 621 259 HOH HOH B . 
JA 13 HOH 122 622 217 HOH HOH B . 
JA 13 HOH 123 623 82  HOH HOH B . 
JA 13 HOH 124 624 9   HOH HOH B . 
JA 13 HOH 125 625 368 HOH HOH B . 
JA 13 HOH 126 626 192 HOH HOH B . 
JA 13 HOH 127 627 112 HOH HOH B . 
JA 13 HOH 128 628 237 HOH HOH B . 
JA 13 HOH 129 629 782 HOH HOH B . 
JA 13 HOH 130 630 34  HOH HOH B . 
JA 13 HOH 131 631 546 HOH HOH B . 
JA 13 HOH 132 632 57  HOH HOH B . 
JA 13 HOH 133 633 574 HOH HOH B . 
JA 13 HOH 134 634 158 HOH HOH B . 
JA 13 HOH 135 635 349 HOH HOH B . 
JA 13 HOH 136 636 577 HOH HOH B . 
JA 13 HOH 137 637 239 HOH HOH B . 
JA 13 HOH 138 638 818 HOH HOH B . 
JA 13 HOH 139 639 55  HOH HOH B . 
JA 13 HOH 140 640 123 HOH HOH B . 
JA 13 HOH 141 641 424 HOH HOH B . 
JA 13 HOH 142 642 798 HOH HOH B . 
JA 13 HOH 143 643 238 HOH HOH B . 
JA 13 HOH 144 644 289 HOH HOH B . 
JA 13 HOH 145 645 386 HOH HOH B . 
JA 13 HOH 146 646 283 HOH HOH B . 
JA 13 HOH 147 647 394 HOH HOH B . 
JA 13 HOH 148 648 554 HOH HOH B . 
JA 13 HOH 149 649 290 HOH HOH B . 
JA 13 HOH 150 650 601 HOH HOH B . 
JA 13 HOH 151 651 670 HOH HOH B . 
JA 13 HOH 152 652 339 HOH HOH B . 
JA 13 HOH 153 653 576 HOH HOH B . 
JA 13 HOH 154 654 377 HOH HOH B . 
JA 13 HOH 155 655 802 HOH HOH B . 
JA 13 HOH 156 656 427 HOH HOH B . 
JA 13 HOH 157 657 139 HOH HOH B . 
JA 13 HOH 158 658 806 HOH HOH B . 
JA 13 HOH 159 659 833 HOH HOH B . 
JA 13 HOH 160 660 595 HOH HOH B . 
JA 13 HOH 161 661 550 HOH HOH B . 
JA 13 HOH 162 662 398 HOH HOH B . 
JA 13 HOH 163 663 230 HOH HOH B . 
JA 13 HOH 164 664 575 HOH HOH B . 
JA 13 HOH 165 665 604 HOH HOH B . 
JA 13 HOH 166 666 22  HOH HOH B . 
JA 13 HOH 167 667 551 HOH HOH B . 
JA 13 HOH 168 668 300 HOH HOH B . 
JA 13 HOH 169 669 573 HOH HOH B . 
JA 13 HOH 170 670 725 HOH HOH B . 
JA 13 HOH 171 671 794 HOH HOH B . 
JA 13 HOH 172 672 51  HOH HOH B . 
JA 13 HOH 173 673 100 HOH HOH B . 
JA 13 HOH 174 674 95  HOH HOH B . 
JA 13 HOH 175 675 117 HOH HOH B . 
JA 13 HOH 176 676 179 HOH HOH B . 
JA 13 HOH 177 677 821 HOH HOH B . 
JA 13 HOH 178 678 288 HOH HOH B . 
JA 13 HOH 179 679 251 HOH HOH B . 
JA 13 HOH 180 680 894 HOH HOH B . 
JA 13 HOH 181 681 409 HOH HOH B . 
JA 13 HOH 182 682 160 HOH HOH B . 
JA 13 HOH 183 683 733 HOH HOH B . 
JA 13 HOH 184 684 822 HOH HOH B . 
JA 13 HOH 185 685 422 HOH HOH B . 
JA 13 HOH 186 686 159 HOH HOH B . 
JA 13 HOH 187 687 807 HOH HOH B . 
JA 13 HOH 188 688 837 HOH HOH B . 
JA 13 HOH 189 689 284 HOH HOH B . 
JA 13 HOH 190 690 674 HOH HOH B . 
JA 13 HOH 191 691 36  HOH HOH B . 
JA 13 HOH 192 692 786 HOH HOH B . 
JA 13 HOH 193 693 829 HOH HOH B . 
JA 13 HOH 194 694 800 HOH HOH B . 
JA 13 HOH 195 695 799 HOH HOH B . 
JA 13 HOH 196 696 191 HOH HOH B . 
JA 13 HOH 197 697 556 HOH HOH B . 
JA 13 HOH 198 698 667 HOH HOH B . 
JA 13 HOH 199 699 565 HOH HOH B . 
JA 13 HOH 200 700 793 HOH HOH B . 
JA 13 HOH 201 701 717 HOH HOH B . 
JA 13 HOH 202 702 531 HOH HOH B . 
JA 13 HOH 203 703 79  HOH HOH B . 
JA 13 HOH 204 704 331 HOH HOH B . 
JA 13 HOH 205 705 532 HOH HOH B . 
JA 13 HOH 206 706 810 HOH HOH B . 
JA 13 HOH 207 707 892 HOH HOH B . 
JA 13 HOH 208 708 827 HOH HOH B . 
JA 13 HOH 209 709 673 HOH HOH B . 
JA 13 HOH 210 710 834 HOH HOH B . 
JA 13 HOH 211 711 785 HOH HOH B . 
JA 13 HOH 212 712 692 HOH HOH B . 
JA 13 HOH 213 713 804 HOH HOH B . 
JA 13 HOH 214 714 597 HOH HOH B . 
JA 13 HOH 215 715 832 HOH HOH B . 
JA 13 HOH 216 716 779 HOH HOH B . 
JA 13 HOH 217 717 819 HOH HOH B . 
JA 13 HOH 218 718 795 HOH HOH B . 
JA 13 HOH 219 719 585 HOH HOH B . 
JA 13 HOH 220 720 517 HOH HOH B . 
JA 13 HOH 221 721 444 HOH HOH B . 
JA 13 HOH 222 722 727 HOH HOH B . 
JA 13 HOH 223 723 433 HOH HOH B . 
JA 13 HOH 224 724 332 HOH HOH B . 
JA 13 HOH 225 725 558 HOH HOH B . 
JA 13 HOH 226 726 831 HOH HOH B . 
JA 13 HOH 227 727 826 HOH HOH B . 
JA 13 HOH 228 728 461 HOH HOH B . 
JA 13 HOH 229 729 666 HOH HOH B . 
JA 13 HOH 230 730 533 HOH HOH B . 
JA 13 HOH 231 731 175 HOH HOH B . 
JA 13 HOH 232 732 805 HOH HOH B . 
JA 13 HOH 233 733 596 HOH HOH B . 
JA 13 HOH 234 734 594 HOH HOH B . 
JA 13 HOH 235 735 185 HOH HOH B . 
JA 13 HOH 236 736 459 HOH HOH B . 
JA 13 HOH 237 737 225 HOH HOH B . 
JA 13 HOH 238 738 814 HOH HOH B . 
JA 13 HOH 239 739 664 HOH HOH B . 
JA 13 HOH 240 740 835 HOH HOH B . 
JA 13 HOH 241 741 817 HOH HOH B . 
JA 13 HOH 242 742 587 HOH HOH B . 
JA 13 HOH 243 743 721 HOH HOH B . 
JA 13 HOH 244 744 445 HOH HOH B . 
JA 13 HOH 245 745 540 HOH HOH B . 
JA 13 HOH 246 746 543 HOH HOH B . 
JA 13 HOH 247 747 783 HOH HOH B . 
JA 13 HOH 248 748 665 HOH HOH B . 
JA 13 HOH 249 749 467 HOH HOH B . 
JA 13 HOH 250 750 688 HOH HOH B . 
JA 13 HOH 251 751 468 HOH HOH B . 
JA 13 HOH 252 752 167 HOH HOH B . 
JA 13 HOH 253 753 410 HOH HOH B . 
JA 13 HOH 254 754 205 HOH HOH B . 
JA 13 HOH 255 755 787 HOH HOH B . 
JA 13 HOH 256 756 801 HOH HOH B . 
JA 13 HOH 257 757 781 HOH HOH B . 
JA 13 HOH 258 758 797 HOH HOH B . 
JA 13 HOH 259 759 570 HOH HOH B . 
JA 13 HOH 260 760 722 HOH HOH B . 
JA 13 HOH 261 761 893 HOH HOH B . 
JA 13 HOH 262 762 603 HOH HOH B . 
JA 13 HOH 263 763 352 HOH HOH B . 
JA 13 HOH 264 764 567 HOH HOH B . 
JA 13 HOH 265 765 689 HOH HOH B . 
JA 13 HOH 266 766 564 HOH HOH B . 
JA 13 HOH 267 767 397 HOH HOH B . 
JA 13 HOH 268 768 530 HOH HOH B . 
JA 13 HOH 269 769 606 HOH HOH B . 
JA 13 HOH 270 770 273 HOH HOH B . 
JA 13 HOH 271 771 545 HOH HOH B . 
JA 13 HOH 272 772 586 HOH HOH B . 
JA 13 HOH 273 773 365 HOH HOH B . 
JA 13 HOH 274 774 824 HOH HOH B . 
JA 13 HOH 275 775 671 HOH HOH B . 
JA 13 HOH 276 776 447 HOH HOH B . 
JA 13 HOH 277 777 578 HOH HOH B . 
JA 13 HOH 278 778 792 HOH HOH B . 
JA 13 HOH 279 779 816 HOH HOH B . 
JA 13 HOH 280 780 375 HOH HOH B . 
JA 13 HOH 281 781 557 HOH HOH B . 
JA 13 HOH 282 782 780 HOH HOH B . 
JA 13 HOH 283 783 661 HOH HOH B . 
JA 13 HOH 284 784 569 HOH HOH B . 
JA 13 HOH 285 785 723 HOH HOH B . 
JA 13 HOH 286 786 650 HOH HOH B . 
JA 13 HOH 287 787 887 HOH HOH B . 
KA 13 HOH 1   501 645 HOH HOH C . 
KA 13 HOH 2   502 374 HOH HOH C . 
KA 13 HOH 3   503 254 HOH HOH C . 
KA 13 HOH 4   504 345 HOH HOH C . 
KA 13 HOH 5   505 871 HOH HOH C . 
KA 13 HOH 6   506 647 HOH HOH C . 
KA 13 HOH 7   507 872 HOH HOH C . 
KA 13 HOH 8   508 400 HOH HOH C . 
KA 13 HOH 9   509 659 HOH HOH C . 
KA 13 HOH 10  510 184 HOH HOH C . 
KA 13 HOH 11  511 618 HOH HOH C . 
KA 13 HOH 12  512 255 HOH HOH C . 
KA 13 HOH 13  513 219 HOH HOH C . 
KA 13 HOH 14  514 851 HOH HOH C . 
KA 13 HOH 15  515 637 HOH HOH C . 
KA 13 HOH 16  516 583 HOH HOH C . 
KA 13 HOH 17  517 197 HOH HOH C . 
KA 13 HOH 18  518 677 HOH HOH C . 
KA 13 HOH 19  519 855 HOH HOH C . 
KA 13 HOH 20  520 234 HOH HOH C . 
KA 13 HOH 21  521 615 HOH HOH C . 
KA 13 HOH 22  522 407 HOH HOH C . 
KA 13 HOH 23  523 678 HOH HOH C . 
KA 13 HOH 24  524 640 HOH HOH C . 
KA 13 HOH 25  525 130 HOH HOH C . 
KA 13 HOH 26  526 25  HOH HOH C . 
KA 13 HOH 27  527 396 HOH HOH C . 
KA 13 HOH 28  528 853 HOH HOH C . 
KA 13 HOH 29  529 343 HOH HOH C . 
KA 13 HOH 30  530 233 HOH HOH C . 
KA 13 HOH 31  531 788 HOH HOH C . 
KA 13 HOH 32  532 694 HOH HOH C . 
KA 13 HOH 33  533 649 HOH HOH C . 
KA 13 HOH 34  534 852 HOH HOH C . 
KA 13 HOH 35  535 201 HOH HOH C . 
KA 13 HOH 36  536 643 HOH HOH C . 
KA 13 HOH 37  537 881 HOH HOH C . 
KA 13 HOH 38  538 277 HOH HOH C . 
KA 13 HOH 39  539 843 HOH HOH C . 
KA 13 HOH 40  540 204 HOH HOH C . 
KA 13 HOH 41  541 198 HOH HOH C . 
KA 13 HOH 42  542 617 HOH HOH C . 
KA 13 HOH 43  543 212 HOH HOH C . 
KA 13 HOH 44  544 178 HOH HOH C . 
KA 13 HOH 45  545 250 HOH HOH C . 
KA 13 HOH 46  546 135 HOH HOH C . 
KA 13 HOH 47  547 868 HOH HOH C . 
KA 13 HOH 48  548 152 HOH HOH C . 
KA 13 HOH 49  549 43  HOH HOH C . 
KA 13 HOH 50  550 841 HOH HOH C . 
KA 13 HOH 51  551 54  HOH HOH C . 
KA 13 HOH 52  552 223 HOH HOH C . 
KA 13 HOH 53  553 898 HOH HOH C . 
KA 13 HOH 54  554 639 HOH HOH C . 
KA 13 HOH 55  555 538 HOH HOH C . 
KA 13 HOH 56  556 613 HOH HOH C . 
KA 13 HOH 57  557 548 HOH HOH C . 
KA 13 HOH 58  558 206 HOH HOH C . 
KA 13 HOH 59  559 200 HOH HOH C . 
KA 13 HOH 60  560 362 HOH HOH C . 
KA 13 HOH 61  561 8   HOH HOH C . 
KA 13 HOH 62  562 848 HOH HOH C . 
KA 13 HOH 63  563 631 HOH HOH C . 
KA 13 HOH 64  564 695 HOH HOH C . 
KA 13 HOH 65  565 351 HOH HOH C . 
KA 13 HOH 66  566 632 HOH HOH C . 
KA 13 HOH 67  567 592 HOH HOH C . 
KA 13 HOH 68  568 170 HOH HOH C . 
KA 13 HOH 69  569 865 HOH HOH C . 
KA 13 HOH 70  570 549 HOH HOH C . 
KA 13 HOH 71  571 94  HOH HOH C . 
KA 13 HOH 72  572 56  HOH HOH C . 
KA 13 HOH 73  573 372 HOH HOH C . 
KA 13 HOH 74  574 628 HOH HOH C . 
KA 13 HOH 75  575 156 HOH HOH C . 
KA 13 HOH 76  576 220 HOH HOH C . 
KA 13 HOH 77  577 366 HOH HOH C . 
KA 13 HOH 78  578 154 HOH HOH C . 
KA 13 HOH 79  579 321 HOH HOH C . 
KA 13 HOH 80  580 862 HOH HOH C . 
KA 13 HOH 81  581 118 HOH HOH C . 
KA 13 HOH 82  582 2   HOH HOH C . 
KA 13 HOH 83  583 864 HOH HOH C . 
KA 13 HOH 84  584 428 HOH HOH C . 
KA 13 HOH 85  585 21  HOH HOH C . 
KA 13 HOH 86  586 630 HOH HOH C . 
KA 13 HOH 87  587 609 HOH HOH C . 
KA 13 HOH 88  588 866 HOH HOH C . 
KA 13 HOH 89  589 267 HOH HOH C . 
KA 13 HOH 90  590 358 HOH HOH C . 
KA 13 HOH 91  591 844 HOH HOH C . 
KA 13 HOH 92  592 119 HOH HOH C . 
KA 13 HOH 93  593 276 HOH HOH C . 
KA 13 HOH 94  594 47  HOH HOH C . 
KA 13 HOH 95  595 873 HOH HOH C . 
KA 13 HOH 96  596 279 HOH HOH C . 
KA 13 HOH 97  597 141 HOH HOH C . 
KA 13 HOH 98  598 334 HOH HOH C . 
KA 13 HOH 99  599 340 HOH HOH C . 
KA 13 HOH 100 600 50  HOH HOH C . 
KA 13 HOH 101 601 612 HOH HOH C . 
KA 13 HOH 102 602 85  HOH HOH C . 
KA 13 HOH 103 603 487 HOH HOH C . 
KA 13 HOH 104 604 619 HOH HOH C . 
KA 13 HOH 105 605 62  HOH HOH C . 
KA 13 HOH 106 606 315 HOH HOH C . 
KA 13 HOH 107 607 679 HOH HOH C . 
KA 13 HOH 108 608 127 HOH HOH C . 
KA 13 HOH 109 609 38  HOH HOH C . 
KA 13 HOH 110 610 644 HOH HOH C . 
KA 13 HOH 111 611 370 HOH HOH C . 
KA 13 HOH 112 612 166 HOH HOH C . 
KA 13 HOH 113 613 125 HOH HOH C . 
KA 13 HOH 114 614 86  HOH HOH C . 
KA 13 HOH 115 615 31  HOH HOH C . 
KA 13 HOH 116 616 214 HOH HOH C . 
KA 13 HOH 117 617 582 HOH HOH C . 
KA 13 HOH 118 618 598 HOH HOH C . 
KA 13 HOH 119 619 195 HOH HOH C . 
KA 13 HOH 120 620 403 HOH HOH C . 
KA 13 HOH 121 621 323 HOH HOH C . 
KA 13 HOH 122 622 231 HOH HOH C . 
KA 13 HOH 123 623 859 HOH HOH C . 
KA 13 HOH 124 624 490 HOH HOH C . 
KA 13 HOH 125 625 77  HOH HOH C . 
KA 13 HOH 126 626 675 HOH HOH C . 
KA 13 HOH 127 627 791 HOH HOH C . 
KA 13 HOH 128 628 329 HOH HOH C . 
KA 13 HOH 129 629 842 HOH HOH C . 
KA 13 HOH 130 630 419 HOH HOH C . 
KA 13 HOH 131 631 839 HOH HOH C . 
KA 13 HOH 132 632 729 HOH HOH C . 
KA 13 HOH 133 633 169 HOH HOH C . 
KA 13 HOH 134 634 408 HOH HOH C . 
KA 13 HOH 135 635 638 HOH HOH C . 
KA 13 HOH 136 636 298 HOH HOH C . 
KA 13 HOH 137 637 149 HOH HOH C . 
KA 13 HOH 138 638 614 HOH HOH C . 
KA 13 HOH 139 639 27  HOH HOH C . 
KA 13 HOH 140 640 162 HOH HOH C . 
KA 13 HOH 141 641 402 HOH HOH C . 
KA 13 HOH 142 642 121 HOH HOH C . 
KA 13 HOH 143 643 367 HOH HOH C . 
KA 13 HOH 144 644 636 HOH HOH C . 
KA 13 HOH 145 645 91  HOH HOH C . 
KA 13 HOH 146 646 849 HOH HOH C . 
KA 13 HOH 147 647 584 HOH HOH C . 
KA 13 HOH 148 648 845 HOH HOH C . 
KA 13 HOH 149 649 497 HOH HOH C . 
KA 13 HOH 150 650 354 HOH HOH C . 
KA 13 HOH 151 651 318 HOH HOH C . 
KA 13 HOH 152 652 681 HOH HOH C . 
KA 13 HOH 153 653 680 HOH HOH C . 
KA 13 HOH 154 654 384 HOH HOH C . 
KA 13 HOH 155 655 441 HOH HOH C . 
KA 13 HOH 156 656 306 HOH HOH C . 
KA 13 HOH 157 657 869 HOH HOH C . 
KA 13 HOH 158 658 128 HOH HOH C . 
KA 13 HOH 159 659 199 HOH HOH C . 
KA 13 HOH 160 660 857 HOH HOH C . 
KA 13 HOH 161 661 305 HOH HOH C . 
KA 13 HOH 162 662 633 HOH HOH C . 
KA 13 HOH 163 663 625 HOH HOH C . 
KA 13 HOH 164 664 243 HOH HOH C . 
KA 13 HOH 165 665 622 HOH HOH C . 
KA 13 HOH 166 666 846 HOH HOH C . 
KA 13 HOH 167 667 88  HOH HOH C . 
KA 13 HOH 168 668 655 HOH HOH C . 
KA 13 HOH 169 669 516 HOH HOH C . 
KA 13 HOH 170 670 434 HOH HOH C . 
KA 13 HOH 171 671 5   HOH HOH C . 
KA 13 HOH 172 672 171 HOH HOH C . 
KA 13 HOH 173 673 624 HOH HOH C . 
KA 13 HOH 174 674 790 HOH HOH C . 
KA 13 HOH 175 675 861 HOH HOH C . 
KA 13 HOH 176 676 763 HOH HOH C . 
KA 13 HOH 177 677 676 HOH HOH C . 
KA 13 HOH 178 678 581 HOH HOH C . 
KA 13 HOH 179 679 610 HOH HOH C . 
KA 13 HOH 180 680 840 HOH HOH C . 
KA 13 HOH 181 681 634 HOH HOH C . 
KA 13 HOH 182 682 867 HOH HOH C . 
KA 13 HOH 183 683 414 HOH HOH C . 
KA 13 HOH 184 684 623 HOH HOH C . 
KA 13 HOH 185 685 854 HOH HOH C . 
KA 13 HOH 186 686 435 HOH HOH C . 
KA 13 HOH 187 687 884 HOH HOH C . 
KA 13 HOH 188 688 882 HOH HOH C . 
KA 13 HOH 189 689 608 HOH HOH C . 
KA 13 HOH 190 690 796 HOH HOH C . 
KA 13 HOH 191 691 593 HOH HOH C . 
KA 13 HOH 192 692 607 HOH HOH C . 
KA 13 HOH 193 693 658 HOH HOH C . 
KA 13 HOH 194 694 880 HOH HOH C . 
KA 13 HOH 195 695 697 HOH HOH C . 
KA 13 HOH 196 696 635 HOH HOH C . 
KA 13 HOH 197 697 268 HOH HOH C . 
KA 13 HOH 198 698 499 HOH HOH C . 
KA 13 HOH 199 699 319 HOH HOH C . 
KA 13 HOH 200 700 860 HOH HOH C . 
KA 13 HOH 201 701 698 HOH HOH C . 
KA 13 HOH 202 702 174 HOH HOH C . 
KA 13 HOH 203 703 611 HOH HOH C . 
KA 13 HOH 204 704 856 HOH HOH C . 
KA 13 HOH 205 705 836 HOH HOH C . 
KA 13 HOH 206 706 642 HOH HOH C . 
KA 13 HOH 207 707 440 HOH HOH C . 
KA 13 HOH 208 708 627 HOH HOH C . 
KA 13 HOH 209 709 696 HOH HOH C . 
KA 13 HOH 210 710 847 HOH HOH C . 
KA 13 HOH 211 711 406 HOH HOH C . 
KA 13 HOH 212 712 361 HOH HOH C . 
KA 13 HOH 213 713 883 HOH HOH C . 
KA 13 HOH 214 714 888 HOH HOH C . 
KA 13 HOH 215 715 257 HOH HOH C . 
KA 13 HOH 216 716 498 HOH HOH C . 
KA 13 HOH 217 717 629 HOH HOH C . 
KA 13 HOH 218 718 858 HOH HOH C . 
KA 13 HOH 219 719 626 HOH HOH C . 
KA 13 HOH 220 720 605 HOH HOH C . 
KA 13 HOH 221 721 438 HOH HOH C . 
KA 13 HOH 222 722 870 HOH HOH C . 
KA 13 HOH 223 723 616 HOH HOH C . 
KA 13 HOH 224 724 879 HOH HOH C . 
KA 13 HOH 225 725 488 HOH HOH C . 
KA 13 HOH 226 726 653 HOH HOH C . 
KA 13 HOH 227 727 580 HOH HOH C . 
KA 13 HOH 228 728 850 HOH HOH C . 
KA 13 HOH 229 729 291 HOH HOH C . 
KA 13 HOH 230 730 784 HOH HOH C . 
KA 13 HOH 231 731 102 HOH HOH C . 
KA 13 HOH 232 732 656 HOH HOH C . 
KA 13 HOH 233 733 657 HOH HOH C . 
KA 13 HOH 234 734 390 HOH HOH C . 
KA 13 HOH 235 735 885 HOH HOH C . 
KA 13 HOH 236 736 648 HOH HOH C . 
KA 13 HOH 237 737 838 HOH HOH C . 
KA 13 HOH 238 738 863 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                   111.81 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HE7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     271.960 
_cell.length_a_esd                 ? 
_cell.length_b                     74.864 
_cell.length_b_esd                 ? 
_cell.length_c                     105.826 
_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                         9HE7 
_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                   9HE7 
_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             4.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.13 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.85M ammonium sulphate, 100 mM HEPES pH 7.5

Soaking: 15 mM myristic acid 3 hours, cryoprotected with 20% glycerol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'KB MIRRORS' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-22 
_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                                       9HE7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               49.18 
_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                                     133390 
_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                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_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                                0.077 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.071 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.03 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6556 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              0.92 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.717 
_reflns_shell.pdbx_Rpim_I_all                               0.271 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.931 
_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                                  0.663 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -2.72 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.28 
_refine.aniso_B[2][2]                            3.95 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.10 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               39.771 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_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                                 9HE7 
_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                            2.00 
_refine.ls_d_res_low                             49.18 
_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                     126710 
_refine.ls_number_reflns_R_free                  6667 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17754 
_refine.ls_R_factor_R_free                       0.19643 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17653 
_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                       0.117 
_refine.pdbx_overall_ESU_R_Free                  0.109 
_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                             3.417 
_refine.overall_SU_ML                            0.090 
_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                       2.00 
_refine_hist.d_res_low                        49.18 
_refine_hist.number_atoms_solvent             888 
_refine_hist.number_atoms_total               9344 
_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        8418 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.012  8902  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7882  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.446  1.845  12260 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.523  1.742  18262 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.190  5.000  1051  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.579  5.000  54    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.740 10.000 1141  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.130  0.200  1341  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  10453 ? 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' ? 2.941  3.957  4069  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.940  3.957  4069  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.170  7.102  5094  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.170  7.102  5095  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.056  4.788  4833  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.972  4.764  4803  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.038  8.556  7098  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.703  39.33  10257 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.666  39.13  10036 ? 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                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             512 
_refine_ls_shell.number_reflns_R_work             9273 
_refine_ls_shell.percent_reflns_obs               99.91 
_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                  0.272 
_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                  0.266 
# 
_struct.entry_id                     9HE7 
_struct.title                        
'Unspecific peroxygenase from Psathyrella aberdarensis (PabUPO-II) in complex with myristic 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        9HE7 
_struct_keywords.text            'Peroxygenase, peroxidase, complex, myristic 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 8  ? 
N  N N 8  ? 
O  N N 10 ? 
P  N N 11 ? 
Q  N N 11 ? 
R  N N 11 ? 
S  N N 11 ? 
T  N N 12 ? 
U  N N 7  ? 
V  N N 9  ? 
W  N N 8  ? 
X  N N 9  ? 
Y  N N 8  ? 
Z  N N 10 ? 
AA N N 11 ? 
BA N N 12 ? 
CA N N 7  ? 
DA N N 8  ? 
EA N N 10 ? 
FA N N 11 ? 
GA N N 11 ? 
HA N N 12 ? 
IA N N 13 ? 
JA N N 13 ? 
KA 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 9HE7 A 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
2 1 9HE7 B 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
3 1 9HE7 C 1 ? 335 ? A0A4V1Q376 52 ? 386 ? 14 348 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,J,K,L,M,N,O,P,Q,R,S,T,IA 
2 1 B,F,G,U,V,W,X,Y,Z,AA,BA,JA     
3 1 C,H,I,CA,DA,EA,FA,GA,HA,KA     
# 
_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 ? LEU C 206 ? LYS C 202 LEU C 219 1 ? 18 
HELX_P HELX_P33 AD6 SER C 219 ? ARG C 228 ? SER C 232 ARG C 241 1 ? 10 
HELX_P HELX_P34 AD7 GLY C 247 ? HIS C 255 ? GLY C 260 HIS C 268 1 ? 9  
HELX_P HELX_P35 AD8 LEU C 282 ? TYR C 297 ? LEU C 295 TYR C 310 1 ? 16 
HELX_P HELX_P36 AD9 THR C 301 ? PHE C 323 ? THR C 314 PHE C 336 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A  CYS 283 SG  ? ? ? 1_555 A  CYS 326 SG ? ? A CYS 296 A CYS 339 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
disulf2  disulf ?    ? B  CYS 283 SG  ? ? ? 1_555 B  CYS 326 SG ? ? B CYS 296 B CYS 339 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
disulf3  disulf ?    ? C  CYS 283 SG  ? ? ? 1_555 C  CYS 326 SG ? ? C CYS 296 C CYS 339 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
covale1  covale one  ? A  ASN 144 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 157 G NAG 1   1_555 ? ? ? ? ? ? ? 1.461 ? 
N-Glycosylation 
covale2  covale one  ? A  ASN 164 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 177 I NAG 1   1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale3  covale one  ? B  ASN 144 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 157 Z NAG 1   1_555 ? ? ? ? ? ? ? 1.470 ? 
N-Glycosylation 
covale4  covale one  ? B  ASN 164 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 177 a NAG 1   1_555 ? ? ? ? ? ? ? 1.453 ? 
N-Glycosylation 
covale5  covale one  ? C  ASN 144 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? C ASN 157 q NAG 1   1_555 ? ? ? ? ? ? ? 1.452 ? 
N-Glycosylation 
covale6  covale one  ? C  ASN 164 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? C ASN 177 s NAG 1   1_555 ? ? ? ? ? ? ? 1.456 ? 
N-Glycosylation 
covale7  covale both ? D  NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale8  covale both ? D  NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale9  covale both ? D  BMA .   O3  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale10 covale both ? D  BMA .   O6  ? ? ? 1_555 D  MAN .   C1 ? ? G BMA 3   G MAN 5   1_555 ? ? ? ? ? ? ? 1.405 ? ? 
covale11 covale both ? E  NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale12 covale both ? E  NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? I NAG 2   I BMA 3   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale13 covale both ? E  BMA .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 4   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale14 covale both ? E  BMA .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I BMA 3   I MAN 7   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale15 covale both ? E  MAN .   O3  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 5   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale16 covale both ? E  MAN .   O6  ? ? ? 1_555 E  MAN .   C1 ? ? I MAN 4   I MAN 6   1_555 ? ? ? ? ? ? ? 1.408 ? ? 
covale17 covale both ? F  NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? Z NAG 1   Z NAG 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale18 covale both ? F  NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? Z NAG 2   Z BMA 3   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale19 covale both ? F  BMA .   O3  ? ? ? 1_555 F  MAN .   C1 ? ? Z BMA 3   Z MAN 4   1_555 ? ? ? ? ? ? ? 1.401 ? ? 
covale20 covale both ? G  NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? a NAG 1   a NAG 2   1_555 ? ? ? ? ? ? ? 1.391 ? ? 
covale21 covale both ? G  NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? a NAG 2   a BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale22 covale both ? G  BMA .   O6  ? ? ? 1_555 G  MAN .   C1 ? ? a BMA 3   a MAN 4   1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale23 covale both ? G  BMA .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? a BMA 3   a MAN 6   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale24 covale both ? G  MAN .   O3  ? ? ? 1_555 G  MAN .   C1 ? ? a MAN 4   a MAN 5   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale25 covale both ? H  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? q NAG 1   q NAG 2   1_555 ? ? ? ? ? ? ? 1.376 ? ? 
covale26 covale both ? H  NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? q NAG 2   q BMA 3   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale27 covale both ? H  BMA .   O3  ? ? ? 1_555 H  MAN .   C1 ? ? q BMA 3   q MAN 4   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale28 covale both ? I  NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? s NAG 1   s NAG 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale29 covale both ? I  NAG .   O4  ? ? ? 1_555 I  BMA .   C1 ? ? s NAG 2   s BMA 3   1_555 ? ? ? ? ? ? ? 1.393 ? ? 
metalc1  metalc ?    ? A  CYS 39  SG  ? ? ? 1_555 O  HEM .   FE ? ? A CYS 52  A HEM 406 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc2  metalc ?    ? A  GLU 125 OE2 ? ? ? 1_555 T  MG  .   MG ? ? A GLU 138 A MG  411 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc3  metalc ?    ? A  GLY 126 O   ? ? ? 1_555 T  MG  .   MG ? ? A GLY 139 A MG  411 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc4  metalc ?    ? J  MYR .   O2  B ? ? 1_555 O  HEM .   FE ? ? A MYR 401 A HEM 406 1_555 ? ? ? ? ? ? ? 2.550 ? ? 
metalc5  metalc ?    ? O  HEM .   O2A ? ? ? 1_555 T  MG  .   MG ? ? A HEM 406 A MG  411 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc6  metalc ?    ? T  MG  .   MG  ? ? ? 1_555 IA HOH .   O  ? ? A MG  411 A HOH 521 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc7  metalc ?    ? T  MG  .   MG  ? ? ? 1_555 IA HOH .   O  ? ? A MG  411 A HOH 541 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc8  metalc ?    ? T  MG  .   MG  ? ? ? 1_555 IA HOH .   O  ? ? A MG  411 A HOH 678 1_555 ? ? ? ? ? ? ? 2.135 ? ? 
metalc9  metalc ?    ? B  CYS 39  SG  ? ? ? 1_555 Z  HEM .   FE ? ? B CYS 52  B HEM 406 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc10 metalc ?    ? B  GLU 125 OE2 ? ? ? 1_555 BA MG  .   MG ? ? B GLU 138 B MG  408 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc11 metalc ?    ? B  GLY 126 O   ? ? ? 1_555 BA MG  .   MG ? ? B GLY 139 B MG  408 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc12 metalc ?    ? Z  HEM .   O2A ? ? ? 1_555 BA MG  .   MG ? ? B HEM 406 B MG  408 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc13 metalc ?    ? BA MG  .   MG  ? ? ? 1_555 JA HOH .   O  ? ? B MG  408 B HOH 512 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc14 metalc ?    ? BA MG  .   MG  ? ? ? 1_555 JA HOH .   O  ? ? B MG  408 B HOH 566 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc15 metalc ?    ? BA MG  .   MG  ? ? ? 1_555 JA HOH .   O  ? ? B MG  408 B HOH 648 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc16 metalc ?    ? C  CYS 39  SG  ? ? ? 1_555 EA HEM .   FE ? ? C CYS 52  C HEM 403 1_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc17 metalc ?    ? C  GLU 125 OE2 ? ? ? 1_555 HA MG  .   MG ? ? C GLU 138 C MG  406 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc18 metalc ?    ? C  GLY 126 O   ? ? ? 1_555 HA MG  .   MG ? ? C GLY 139 C MG  406 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc19 metalc ?    ? EA HEM .   O1A ? ? ? 1_555 HA MG  .   MG ? ? C HEM 403 C MG  406 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc20 metalc ?    ? HA MG  .   MG  ? ? ? 1_555 KA HOH .   O  ? ? C MG  406 C HOH 547 1_555 ? ? ? ? ? ? ? 1.820 ? ? 
metalc21 metalc ?    ? HA MG  .   MG  ? ? ? 1_555 KA HOH .   O  ? ? C MG  406 C HOH 553 1_555 ? ? ? ? ? ? ? 1.934 ? ? 
metalc22 metalc ?    ? HA MG  .   MG  ? ? ? 1_555 KA HOH .   O  ? ? C MG  406 C HOH 604 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
# 
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 ? O  HEM . ? A HEM 406 ? 1_555 NA  ? O  HEM .   ? A HEM 406 ? 1_555 102.1 ? 
2  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 NB  ? O  HEM .   ? A HEM 406 ? 1_555 94.2  ? 
3  NA  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 NB  ? O  HEM .   ? A HEM 406 ? 1_555 87.7  ? 
4  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 NC  ? O  HEM .   ? A HEM 406 ? 1_555 89.6  ? 
5  NA  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 NC  ? O  HEM .   ? A HEM 406 ? 1_555 168.0 ? 
6  NB  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 NC  ? O  HEM .   ? A HEM 406 ? 1_555 88.7  ? 
7  SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 ND  ? O  HEM .   ? A HEM 406 ? 1_555 97.3  ? 
8  NA  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 ND  ? O  HEM .   ? A HEM 406 ? 1_555 91.2  ? 
9  NB  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 ND  ? O  HEM .   ? A HEM 406 ? 1_555 168.4 ? 
10 NC  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 ND  ? O  HEM .   ? A HEM 406 ? 1_555 90.0  ? 
11 SG  ? A  CYS 39  ? A CYS 52  ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 O2  B J  MYR .   ? A MYR 401 ? 1_555 171.8 ? 
12 NA  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 O2  B J  MYR .   ? A MYR 401 ? 1_555 76.3  ? 
13 NB  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 O2  B J  MYR .   ? A MYR 401 ? 1_555 77.7  ? 
14 NC  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 O2  B J  MYR .   ? A MYR 401 ? 1_555 91.7  ? 
15 ND  ? O  HEM .   ? A HEM 406 ? 1_555 FE ? O  HEM . ? A HEM 406 ? 1_555 O2  B J  MYR .   ? A MYR 401 ? 1_555 90.8  ? 
16 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? A  GLY 126 ? A GLY 139 ? 1_555 84.7  ? 
17 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O2A ? O  HEM .   ? A HEM 406 ? 1_555 99.3  ? 
18 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O2A ? O  HEM .   ? A HEM 406 ? 1_555 95.9  ? 
19 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 521 ? 1_555 92.9  ? 
20 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 521 ? 1_555 174.2 ? 
21 O2A ? O  HEM .   ? A HEM 406 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 521 ? 1_555 79.3  ? 
22 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 541 ? 1_555 169.5 ? 
23 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 541 ? 1_555 84.9  ? 
24 O2A ? O  HEM .   ? A HEM 406 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 541 ? 1_555 81.5  ? 
25 O   ? IA HOH .   ? A HOH 521 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 541 ? 1_555 97.5  ? 
26 OE2 ? A  GLU 125 ? A GLU 138 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 678 ? 1_555 88.0  ? 
27 O   ? A  GLY 126 ? A GLY 139 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 678 ? 1_555 87.2  ? 
28 O2A ? O  HEM .   ? A HEM 406 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 678 ? 1_555 172.3 ? 
29 O   ? IA HOH .   ? A HOH 521 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 678 ? 1_555 98.0  ? 
30 O   ? IA HOH .   ? A HOH 541 ? 1_555 MG ? T  MG  . ? A MG  411 ? 1_555 O   ? IA HOH .   ? A HOH 678 ? 1_555 91.8  ? 
31 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NA  ? Z  HEM .   ? B HEM 406 ? 1_555 101.0 ? 
32 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NB  ? Z  HEM .   ? B HEM 406 ? 1_555 91.1  ? 
33 NA  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NB  ? Z  HEM .   ? B HEM 406 ? 1_555 87.8  ? 
34 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NC  ? Z  HEM .   ? B HEM 406 ? 1_555 89.8  ? 
35 NA  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NC  ? Z  HEM .   ? B HEM 406 ? 1_555 168.5 ? 
36 NB  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 NC  ? Z  HEM .   ? B HEM 406 ? 1_555 88.2  ? 
37 SG  ? B  CYS 39  ? B CYS 52  ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 ND  ? Z  HEM .   ? B HEM 406 ? 1_555 99.3  ? 
38 NA  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 ND  ? Z  HEM .   ? B HEM 406 ? 1_555 90.6  ? 
39 NB  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 ND  ? Z  HEM .   ? B HEM 406 ? 1_555 169.6 ? 
40 NC  ? Z  HEM .   ? B HEM 406 ? 1_555 FE ? Z  HEM . ? B HEM 406 ? 1_555 ND  ? Z  HEM .   ? B HEM 406 ? 1_555 91.5  ? 
41 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? B  GLY 126 ? B GLY 139 ? 1_555 81.5  ? 
42 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O2A ? Z  HEM .   ? B HEM 406 ? 1_555 101.4 ? 
43 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O2A ? Z  HEM .   ? B HEM 406 ? 1_555 93.5  ? 
44 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 512 ? 1_555 166.7 ? 
45 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 512 ? 1_555 85.4  ? 
46 O2A ? Z  HEM .   ? B HEM 406 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 512 ? 1_555 77.3  ? 
47 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 566 ? 1_555 94.4  ? 
48 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 566 ? 1_555 174.2 ? 
49 O2A ? Z  HEM .   ? B HEM 406 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 566 ? 1_555 83.2  ? 
50 O   ? JA HOH .   ? B HOH 512 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 566 ? 1_555 98.5  ? 
51 OE2 ? B  GLU 125 ? B GLU 138 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 648 ? 1_555 87.6  ? 
52 O   ? B  GLY 126 ? B GLY 139 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 648 ? 1_555 86.4  ? 
53 O2A ? Z  HEM .   ? B HEM 406 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 648 ? 1_555 170.9 ? 
54 O   ? JA HOH .   ? B HOH 512 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 648 ? 1_555 93.6  ? 
55 O   ? JA HOH .   ? B HOH 566 ? 1_555 MG ? BA MG  . ? B MG  408 ? 1_555 O   ? JA HOH .   ? B HOH 648 ? 1_555 97.6  ? 
56 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NA  ? EA HEM .   ? C HEM 403 ? 1_555 100.5 ? 
57 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NB  ? EA HEM .   ? C HEM 403 ? 1_555 89.7  ? 
58 NA  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NB  ? EA HEM .   ? C HEM 403 ? 1_555 87.4  ? 
59 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NC  ? EA HEM .   ? C HEM 403 ? 1_555 88.2  ? 
60 NA  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NC  ? EA HEM .   ? C HEM 403 ? 1_555 170.0 ? 
61 NB  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 NC  ? EA HEM .   ? C HEM 403 ? 1_555 87.7  ? 
62 SG  ? C  CYS 39  ? C CYS 52  ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 ND  ? EA HEM .   ? C HEM 403 ? 1_555 97.8  ? 
63 NA  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 ND  ? EA HEM .   ? C HEM 403 ? 1_555 93.3  ? 
64 NB  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 ND  ? EA HEM .   ? C HEM 403 ? 1_555 172.2 ? 
65 NC  ? EA HEM .   ? C HEM 403 ? 1_555 FE ? EA HEM . ? C HEM 403 ? 1_555 ND  ? EA HEM .   ? C HEM 403 ? 1_555 90.3  ? 
66 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? C  GLY 126 ? C GLY 139 ? 1_555 79.8  ? 
67 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O1A ? EA HEM .   ? C HEM 403 ? 1_555 99.3  ? 
68 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O1A ? EA HEM .   ? C HEM 403 ? 1_555 94.9  ? 
69 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 547 ? 1_555 162.9 ? 
70 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 547 ? 1_555 83.8  ? 
71 O1A ? EA HEM .   ? C HEM 403 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 547 ? 1_555 86.7  ? 
72 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 553 ? 1_555 97.8  ? 
73 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 553 ? 1_555 177.2 ? 
74 O1A ? EA HEM .   ? C HEM 403 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 553 ? 1_555 84.2  ? 
75 O   ? KA HOH .   ? C HOH 547 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 553 ? 1_555 98.8  ? 
76 OE2 ? C  GLU 125 ? C GLU 138 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 604 ? 1_555 90.6  ? 
77 O   ? C  GLY 126 ? C GLY 139 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 604 ? 1_555 79.1  ? 
78 O1A ? EA HEM .   ? C HEM 403 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 604 ? 1_555 167.3 ? 
79 O   ? KA HOH .   ? C HOH 547 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 604 ? 1_555 81.6  ? 
80 O   ? KA HOH .   ? C HOH 553 ? 1_555 MG ? HA MG  . ? C MG  406 ? 1_555 O   ? KA HOH .   ? C HOH 604 ? 1_555 102.3 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG D .   ? ASN A 144 ? NAG G 1   ? 1_555 ASN A 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN A 164 ? NAG I 1   ? 1_555 ASN A 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG F .   ? ASN B 144 ? NAG Z 1   ? 1_555 ASN B 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG G .   ? ASN B 164 ? NAG a 1   ? 1_555 ASN B 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG H .   ? ASN C 144 ? NAG q 1   ? 1_555 ASN C 157 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG I .   ? ASN C 164 ? NAG s 1   ? 1_555 ASN C 177 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 283 ? CYS A 326 ? CYS A 296 ? 1_555 CYS A 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 283 ? CYS B 326 ? CYS B 296 ? 1_555 CYS B 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS C 283 ? CYS C 326 ? CYS C 296 ? 1_555 CYS C 339 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 111 A . ? PRO 124 A PRO 112 A ? PRO 125 A 1 5.52  
2 PRO 111 B . ? PRO 124 B PRO 112 B ? PRO 125 B 1 12.43 
3 PRO 111 C . ? PRO 124 C PRO 112 C ? PRO 125 C 1 3.49  
# 
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                   9HE7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CE  A MET 243 ? B O A HOH 812 ? ? 2.00 
2 1 O   B HOH 680 ? ? O B HOH 761 ? ? 2.03 
3 1 NH2 A ARG 229 ? ? O A HOH 501 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              318 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                123.64 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.34 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 127 ? ? -140.30 -32.98  
2  1 PHE A 137 ? ? -106.97 -84.49  
3  1 ASN A 203 ? ? 50.76   -125.70 
4  1 SER A 257 ? ? -158.25 -100.69 
5  1 ASN A 282 ? ? -143.33 53.33   
6  1 ASN A 312 ? ? -153.24 65.08   
7  1 HIS B 127 ? ? -138.54 -35.48  
8  1 PHE B 137 ? ? -105.60 -83.64  
9  1 ASN B 203 ? ? 52.04   -126.33 
10 1 SER B 257 ? ? -157.42 -98.34  
11 1 ASN B 282 ? ? -142.09 53.63   
12 1 HIS C 127 ? ? -139.79 -33.45  
13 1 PHE C 137 ? ? -107.38 -84.20  
14 1 ASN C 203 ? ? 49.87   -124.23 
15 1 SER C 257 ? ? -156.79 -101.15 
16 1 ASN C 282 ? ? -142.36 54.21   
17 1 ASN C 312 ? ? -154.39 62.28   
# 
_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     731 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   KA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BMA C1   C  N R 74  
BMA C2   C  N S 75  
BMA C3   C  N S 76  
BMA C4   C  N S 77  
BMA C5   C  N R 78  
BMA C6   C  N N 79  
BMA O1   O  N N 80  
BMA O2   O  N N 81  
BMA O3   O  N N 82  
BMA O4   O  N N 83  
BMA O5   O  N N 84  
BMA O6   O  N N 85  
BMA H1   H  N N 86  
BMA H2   H  N N 87  
BMA H3   H  N N 88  
BMA H4   H  N N 89  
BMA H5   H  N N 90  
BMA H61  H  N N 91  
BMA H62  H  N N 92  
BMA HO1  H  N N 93  
BMA HO2  H  N N 94  
BMA HO3  H  N N 95  
BMA HO4  H  N N 96  
BMA HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
EPE N1   N  N N 112 
EPE C2   C  N N 113 
EPE C3   C  N N 114 
EPE N4   N  N N 115 
EPE C5   C  N N 116 
EPE C6   C  N N 117 
EPE C7   C  N N 118 
EPE C8   C  N N 119 
EPE O8   O  N N 120 
EPE C9   C  N N 121 
EPE C10  C  N N 122 
EPE S    S  N N 123 
EPE O1S  O  N N 124 
EPE O2S  O  N N 125 
EPE O3S  O  N N 126 
EPE H21  H  N N 127 
EPE H22  H  N N 128 
EPE H31  H  N N 129 
EPE H32  H  N N 130 
EPE H51  H  N N 131 
EPE H52  H  N N 132 
EPE H61  H  N N 133 
EPE H62  H  N N 134 
EPE H71  H  N N 135 
EPE H72  H  N N 136 
EPE H81  H  N N 137 
EPE H82  H  N N 138 
EPE HO8  H  N N 139 
EPE H91  H  N N 140 
EPE H92  H  N N 141 
EPE H101 H  N N 142 
EPE H102 H  N N 143 
EPE HOS3 H  N N 144 
GLN N    N  N N 145 
GLN CA   C  N S 146 
GLN C    C  N N 147 
GLN O    O  N N 148 
GLN CB   C  N N 149 
GLN CG   C  N N 150 
GLN CD   C  N N 151 
GLN OE1  O  N N 152 
GLN NE2  N  N N 153 
GLN OXT  O  N N 154 
GLN H    H  N N 155 
GLN H2   H  N N 156 
GLN HA   H  N N 157 
GLN HB2  H  N N 158 
GLN HB3  H  N N 159 
GLN HG2  H  N N 160 
GLN HG3  H  N N 161 
GLN HE21 H  N N 162 
GLN HE22 H  N N 163 
GLN HXT  H  N N 164 
GLU N    N  N N 165 
GLU CA   C  N S 166 
GLU C    C  N N 167 
GLU O    O  N N 168 
GLU CB   C  N N 169 
GLU CG   C  N N 170 
GLU CD   C  N N 171 
GLU OE1  O  N N 172 
GLU OE2  O  N N 173 
GLU OXT  O  N N 174 
GLU H    H  N N 175 
GLU H2   H  N N 176 
GLU HA   H  N N 177 
GLU HB2  H  N N 178 
GLU HB3  H  N N 179 
GLU HG2  H  N N 180 
GLU HG3  H  N N 181 
GLU HE2  H  N N 182 
GLU HXT  H  N N 183 
GLY N    N  N N 184 
GLY CA   C  N N 185 
GLY C    C  N N 186 
GLY O    O  N N 187 
GLY OXT  O  N N 188 
GLY H    H  N N 189 
GLY H2   H  N N 190 
GLY HA2  H  N N 191 
GLY HA3  H  N N 192 
GLY HXT  H  N N 193 
GOL C1   C  N N 194 
GOL O1   O  N N 195 
GOL C2   C  N N 196 
GOL O2   O  N N 197 
GOL C3   C  N N 198 
GOL O3   O  N N 199 
GOL H11  H  N N 200 
GOL H12  H  N N 201 
GOL HO1  H  N N 202 
GOL H2   H  N N 203 
GOL HO2  H  N N 204 
GOL H31  H  N N 205 
GOL H32  H  N N 206 
GOL HO3  H  N N 207 
HEM CHA  C  N N 208 
HEM CHB  C  N N 209 
HEM CHC  C  N N 210 
HEM CHD  C  N N 211 
HEM C1A  C  Y N 212 
HEM C2A  C  Y N 213 
HEM C3A  C  Y N 214 
HEM C4A  C  Y N 215 
HEM CMA  C  N N 216 
HEM CAA  C  N N 217 
HEM CBA  C  N N 218 
HEM CGA  C  N N 219 
HEM O1A  O  N N 220 
HEM O2A  O  N N 221 
HEM C1B  C  N N 222 
HEM C2B  C  N N 223 
HEM C3B  C  N N 224 
HEM C4B  C  N N 225 
HEM CMB  C  N N 226 
HEM CAB  C  N N 227 
HEM CBB  C  N N 228 
HEM C1C  C  Y N 229 
HEM C2C  C  Y N 230 
HEM C3C  C  Y N 231 
HEM C4C  C  Y N 232 
HEM CMC  C  N N 233 
HEM CAC  C  N N 234 
HEM CBC  C  N N 235 
HEM C1D  C  N N 236 
HEM C2D  C  N N 237 
HEM C3D  C  N N 238 
HEM C4D  C  N N 239 
HEM CMD  C  N N 240 
HEM CAD  C  N N 241 
HEM CBD  C  N N 242 
HEM CGD  C  N N 243 
HEM O1D  O  N N 244 
HEM O2D  O  N N 245 
HEM NA   N  Y N 246 
HEM NB   N  N N 247 
HEM NC   N  Y N 248 
HEM ND   N  N N 249 
HEM FE   FE N N 250 
HEM HHB  H  N N 251 
HEM HHC  H  N N 252 
HEM HHD  H  N N 253 
HEM HMA  H  N N 254 
HEM HMAA H  N N 255 
HEM HMAB H  N N 256 
HEM HAA  H  N N 257 
HEM HAAA H  N N 258 
HEM HBA  H  N N 259 
HEM HBAA H  N N 260 
HEM HMB  H  N N 261 
HEM HMBA H  N N 262 
HEM HMBB H  N N 263 
HEM HAB  H  N N 264 
HEM HBB  H  N N 265 
HEM HBBA H  N N 266 
HEM HMC  H  N N 267 
HEM HMCA H  N N 268 
HEM HMCB H  N N 269 
HEM HAC  H  N N 270 
HEM HBC  H  N N 271 
HEM HBCA H  N N 272 
HEM HMD  H  N N 273 
HEM HMDA H  N N 274 
HEM HMDB H  N N 275 
HEM HAD  H  N N 276 
HEM HADA H  N N 277 
HEM HBD  H  N N 278 
HEM HBDA H  N N 279 
HEM H2A  H  N N 280 
HEM H2D  H  N N 281 
HEM HHA  H  N N 282 
HIS N    N  N N 283 
HIS CA   C  N S 284 
HIS C    C  N N 285 
HIS O    O  N N 286 
HIS CB   C  N N 287 
HIS CG   C  Y N 288 
HIS ND1  N  Y N 289 
HIS CD2  C  Y N 290 
HIS CE1  C  Y N 291 
HIS NE2  N  Y N 292 
HIS OXT  O  N N 293 
HIS H    H  N N 294 
HIS H2   H  N N 295 
HIS HA   H  N N 296 
HIS HB2  H  N N 297 
HIS HB3  H  N N 298 
HIS HD1  H  N N 299 
HIS HD2  H  N N 300 
HIS HE1  H  N N 301 
HIS HE2  H  N N 302 
HIS HXT  H  N N 303 
HOH O    O  N N 304 
HOH H1   H  N N 305 
HOH H2   H  N N 306 
ILE N    N  N N 307 
ILE CA   C  N S 308 
ILE C    C  N N 309 
ILE O    O  N N 310 
ILE CB   C  N S 311 
ILE CG1  C  N N 312 
ILE CG2  C  N N 313 
ILE CD1  C  N N 314 
ILE OXT  O  N N 315 
ILE H    H  N N 316 
ILE H2   H  N N 317 
ILE HA   H  N N 318 
ILE HB   H  N N 319 
ILE HG12 H  N N 320 
ILE HG13 H  N N 321 
ILE HG21 H  N N 322 
ILE HG22 H  N N 323 
ILE HG23 H  N N 324 
ILE HD11 H  N N 325 
ILE HD12 H  N N 326 
ILE HD13 H  N N 327 
ILE HXT  H  N N 328 
LEU N    N  N N 329 
LEU CA   C  N S 330 
LEU C    C  N N 331 
LEU O    O  N N 332 
LEU CB   C  N N 333 
LEU CG   C  N N 334 
LEU CD1  C  N N 335 
LEU CD2  C  N N 336 
LEU OXT  O  N N 337 
LEU H    H  N N 338 
LEU H2   H  N N 339 
LEU HA   H  N N 340 
LEU HB2  H  N N 341 
LEU HB3  H  N N 342 
LEU HG   H  N N 343 
LEU HD11 H  N N 344 
LEU HD12 H  N N 345 
LEU HD13 H  N N 346 
LEU HD21 H  N N 347 
LEU HD22 H  N N 348 
LEU HD23 H  N N 349 
LEU HXT  H  N N 350 
LYS N    N  N N 351 
LYS CA   C  N S 352 
LYS C    C  N N 353 
LYS O    O  N N 354 
LYS CB   C  N N 355 
LYS CG   C  N N 356 
LYS CD   C  N N 357 
LYS CE   C  N N 358 
LYS NZ   N  N N 359 
LYS OXT  O  N N 360 
LYS H    H  N N 361 
LYS H2   H  N N 362 
LYS HA   H  N N 363 
LYS HB2  H  N N 364 
LYS HB3  H  N N 365 
LYS HG2  H  N N 366 
LYS HG3  H  N N 367 
LYS HD2  H  N N 368 
LYS HD3  H  N N 369 
LYS HE2  H  N N 370 
LYS HE3  H  N N 371 
LYS HZ1  H  N N 372 
LYS HZ2  H  N N 373 
LYS HZ3  H  N N 374 
LYS HXT  H  N N 375 
MAN C1   C  N S 376 
MAN C2   C  N S 377 
MAN C3   C  N S 378 
MAN C4   C  N S 379 
MAN C5   C  N R 380 
MAN C6   C  N N 381 
MAN O1   O  N N 382 
MAN O2   O  N N 383 
MAN O3   O  N N 384 
MAN O4   O  N N 385 
MAN O5   O  N N 386 
MAN O6   O  N N 387 
MAN H1   H  N N 388 
MAN H2   H  N N 389 
MAN H3   H  N N 390 
MAN H4   H  N N 391 
MAN H5   H  N N 392 
MAN H61  H  N N 393 
MAN H62  H  N N 394 
MAN HO1  H  N N 395 
MAN HO2  H  N N 396 
MAN HO3  H  N N 397 
MAN HO4  H  N N 398 
MAN HO6  H  N N 399 
MET N    N  N N 400 
MET CA   C  N S 401 
MET C    C  N N 402 
MET O    O  N N 403 
MET CB   C  N N 404 
MET CG   C  N N 405 
MET SD   S  N N 406 
MET CE   C  N N 407 
MET OXT  O  N N 408 
MET H    H  N N 409 
MET H2   H  N N 410 
MET HA   H  N N 411 
MET HB2  H  N N 412 
MET HB3  H  N N 413 
MET HG2  H  N N 414 
MET HG3  H  N N 415 
MET HE1  H  N N 416 
MET HE2  H  N N 417 
MET HE3  H  N N 418 
MET HXT  H  N N 419 
MG  MG   MG N N 420 
MYR C1   C  N N 421 
MYR O1   O  N N 422 
MYR O2   O  N N 423 
MYR C2   C  N N 424 
MYR C3   C  N N 425 
MYR C4   C  N N 426 
MYR C5   C  N N 427 
MYR C6   C  N N 428 
MYR C7   C  N N 429 
MYR C8   C  N N 430 
MYR C9   C  N N 431 
MYR C10  C  N N 432 
MYR C11  C  N N 433 
MYR C12  C  N N 434 
MYR C13  C  N N 435 
MYR C14  C  N N 436 
MYR HO2  H  N N 437 
MYR H21  H  N N 438 
MYR H22  H  N N 439 
MYR H31  H  N N 440 
MYR H32  H  N N 441 
MYR H41  H  N N 442 
MYR H42  H  N N 443 
MYR H51  H  N N 444 
MYR H52  H  N N 445 
MYR H61  H  N N 446 
MYR H62  H  N N 447 
MYR H71  H  N N 448 
MYR H72  H  N N 449 
MYR H81  H  N N 450 
MYR H82  H  N N 451 
MYR H91  H  N N 452 
MYR H92  H  N N 453 
MYR H101 H  N N 454 
MYR H102 H  N N 455 
MYR H111 H  N N 456 
MYR H112 H  N N 457 
MYR H121 H  N N 458 
MYR H122 H  N N 459 
MYR H131 H  N N 460 
MYR H132 H  N N 461 
MYR H141 H  N N 462 
MYR H142 H  N N 463 
MYR H143 H  N N 464 
NAG C1   C  N R 465 
NAG C2   C  N R 466 
NAG C3   C  N R 467 
NAG C4   C  N S 468 
NAG C5   C  N R 469 
NAG C6   C  N N 470 
NAG C7   C  N N 471 
NAG C8   C  N N 472 
NAG N2   N  N N 473 
NAG O1   O  N N 474 
NAG O3   O  N N 475 
NAG O4   O  N N 476 
NAG O5   O  N N 477 
NAG O6   O  N N 478 
NAG O7   O  N N 479 
NAG H1   H  N N 480 
NAG H2   H  N N 481 
NAG H3   H  N N 482 
NAG H4   H  N N 483 
NAG H5   H  N N 484 
NAG H61  H  N N 485 
NAG H62  H  N N 486 
NAG H81  H  N N 487 
NAG H82  H  N N 488 
NAG H83  H  N N 489 
NAG HN2  H  N N 490 
NAG HO1  H  N N 491 
NAG HO3  H  N N 492 
NAG HO4  H  N N 493 
NAG HO6  H  N N 494 
PHE N    N  N N 495 
PHE CA   C  N S 496 
PHE C    C  N N 497 
PHE O    O  N N 498 
PHE CB   C  N N 499 
PHE CG   C  Y N 500 
PHE CD1  C  Y N 501 
PHE CD2  C  Y N 502 
PHE CE1  C  Y N 503 
PHE CE2  C  Y N 504 
PHE CZ   C  Y N 505 
PHE OXT  O  N N 506 
PHE H    H  N N 507 
PHE H2   H  N N 508 
PHE HA   H  N N 509 
PHE HB2  H  N N 510 
PHE HB3  H  N N 511 
PHE HD1  H  N N 512 
PHE HD2  H  N N 513 
PHE HE1  H  N N 514 
PHE HE2  H  N N 515 
PHE HZ   H  N N 516 
PHE HXT  H  N N 517 
PRO N    N  N N 518 
PRO CA   C  N S 519 
PRO C    C  N N 520 
PRO O    O  N N 521 
PRO CB   C  N N 522 
PRO CG   C  N N 523 
PRO CD   C  N N 524 
PRO OXT  O  N N 525 
PRO H    H  N N 526 
PRO HA   H  N N 527 
PRO HB2  H  N N 528 
PRO HB3  H  N N 529 
PRO HG2  H  N N 530 
PRO HG3  H  N N 531 
PRO HD2  H  N N 532 
PRO HD3  H  N N 533 
PRO HXT  H  N N 534 
SER N    N  N N 535 
SER CA   C  N S 536 
SER C    C  N N 537 
SER O    O  N N 538 
SER CB   C  N N 539 
SER OG   O  N N 540 
SER OXT  O  N N 541 
SER H    H  N N 542 
SER H2   H  N N 543 
SER HA   H  N N 544 
SER HB2  H  N N 545 
SER HB3  H  N N 546 
SER HG   H  N N 547 
SER HXT  H  N N 548 
SO4 S    S  N N 549 
SO4 O1   O  N N 550 
SO4 O2   O  N N 551 
SO4 O3   O  N N 552 
SO4 O4   O  N N 553 
THR N    N  N N 554 
THR CA   C  N S 555 
THR C    C  N N 556 
THR O    O  N N 557 
THR CB   C  N R 558 
THR OG1  O  N N 559 
THR CG2  C  N N 560 
THR OXT  O  N N 561 
THR H    H  N N 562 
THR H2   H  N N 563 
THR HA   H  N N 564 
THR HB   H  N N 565 
THR HG1  H  N N 566 
THR HG21 H  N N 567 
THR HG22 H  N N 568 
THR HG23 H  N N 569 
THR HXT  H  N N 570 
TRP N    N  N N 571 
TRP CA   C  N S 572 
TRP C    C  N N 573 
TRP O    O  N N 574 
TRP CB   C  N N 575 
TRP CG   C  Y N 576 
TRP CD1  C  Y N 577 
TRP CD2  C  Y N 578 
TRP NE1  N  Y N 579 
TRP CE2  C  Y N 580 
TRP CE3  C  Y N 581 
TRP CZ2  C  Y N 582 
TRP CZ3  C  Y N 583 
TRP CH2  C  Y N 584 
TRP OXT  O  N N 585 
TRP H    H  N N 586 
TRP H2   H  N N 587 
TRP HA   H  N N 588 
TRP HB2  H  N N 589 
TRP HB3  H  N N 590 
TRP HD1  H  N N 591 
TRP HE1  H  N N 592 
TRP HE3  H  N N 593 
TRP HZ2  H  N N 594 
TRP HZ3  H  N N 595 
TRP HH2  H  N N 596 
TRP HXT  H  N N 597 
TYR N    N  N N 598 
TYR CA   C  N S 599 
TYR C    C  N N 600 
TYR O    O  N N 601 
TYR CB   C  N N 602 
TYR CG   C  Y N 603 
TYR CD1  C  Y N 604 
TYR CD2  C  Y N 605 
TYR CE1  C  Y N 606 
TYR CE2  C  Y N 607 
TYR CZ   C  Y N 608 
TYR OH   O  N N 609 
TYR OXT  O  N N 610 
TYR H    H  N N 611 
TYR H2   H  N N 612 
TYR HA   H  N N 613 
TYR HB2  H  N N 614 
TYR HB3  H  N N 615 
TYR HD1  H  N N 616 
TYR HD2  H  N N 617 
TYR HE1  H  N N 618 
TYR HE2  H  N N 619 
TYR HH   H  N N 620 
TYR HXT  H  N N 621 
VAL N    N  N N 622 
VAL CA   C  N S 623 
VAL C    C  N N 624 
VAL O    O  N N 625 
VAL CB   C  N N 626 
VAL CG1  C  N N 627 
VAL CG2  C  N N 628 
VAL OXT  O  N N 629 
VAL H    H  N N 630 
VAL H2   H  N N 631 
VAL HA   H  N N 632 
VAL HB   H  N N 633 
VAL HG11 H  N N 634 
VAL HG12 H  N N 635 
VAL HG13 H  N N 636 
VAL HG21 H  N N 637 
VAL HG22 H  N N 638 
VAL HG23 H  N N 639 
VAL HXT  H  N N 640 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
EPE N1  C2   sing N N 107 
EPE N1  C6   sing N N 108 
EPE N1  C9   sing N N 109 
EPE C2  C3   sing N N 110 
EPE C2  H21  sing N N 111 
EPE C2  H22  sing N N 112 
EPE C3  N4   sing N N 113 
EPE C3  H31  sing N N 114 
EPE C3  H32  sing N N 115 
EPE N4  C5   sing N N 116 
EPE N4  C7   sing N N 117 
EPE C5  C6   sing N N 118 
EPE C5  H51  sing N N 119 
EPE C5  H52  sing N N 120 
EPE C6  H61  sing N N 121 
EPE C6  H62  sing N N 122 
EPE C7  C8   sing N N 123 
EPE C7  H71  sing N N 124 
EPE C7  H72  sing N N 125 
EPE C8  O8   sing N N 126 
EPE C8  H81  sing N N 127 
EPE C8  H82  sing N N 128 
EPE O8  HO8  sing N N 129 
EPE C9  C10  sing N N 130 
EPE C9  H91  sing N N 131 
EPE C9  H92  sing N N 132 
EPE C10 S    sing N N 133 
EPE C10 H101 sing N N 134 
EPE C10 H102 sing N N 135 
EPE S   O1S  doub N N 136 
EPE S   O2S  doub N N 137 
EPE S   O3S  sing N N 138 
EPE O3S HOS3 sing N N 139 
GLN N   CA   sing N N 140 
GLN N   H    sing N N 141 
GLN N   H2   sing N N 142 
GLN CA  C    sing N N 143 
GLN CA  CB   sing N N 144 
GLN CA  HA   sing N N 145 
GLN C   O    doub N N 146 
GLN C   OXT  sing N N 147 
GLN CB  CG   sing N N 148 
GLN CB  HB2  sing N N 149 
GLN CB  HB3  sing N N 150 
GLN CG  CD   sing N N 151 
GLN CG  HG2  sing N N 152 
GLN CG  HG3  sing N N 153 
GLN CD  OE1  doub N N 154 
GLN CD  NE2  sing N N 155 
GLN NE2 HE21 sing N N 156 
GLN NE2 HE22 sing N N 157 
GLN OXT HXT  sing N N 158 
GLU N   CA   sing N N 159 
GLU N   H    sing N N 160 
GLU N   H2   sing N N 161 
GLU CA  C    sing N N 162 
GLU CA  CB   sing N N 163 
GLU CA  HA   sing N N 164 
GLU C   O    doub N N 165 
GLU C   OXT  sing N N 166 
GLU CB  CG   sing N N 167 
GLU CB  HB2  sing N N 168 
GLU CB  HB3  sing N N 169 
GLU CG  CD   sing N N 170 
GLU CG  HG2  sing N N 171 
GLU CG  HG3  sing N N 172 
GLU CD  OE1  doub N N 173 
GLU CD  OE2  sing N N 174 
GLU OE2 HE2  sing N N 175 
GLU OXT HXT  sing N N 176 
GLY N   CA   sing N N 177 
GLY N   H    sing N N 178 
GLY N   H2   sing N N 179 
GLY CA  C    sing N N 180 
GLY CA  HA2  sing N N 181 
GLY CA  HA3  sing N N 182 
GLY C   O    doub N N 183 
GLY C   OXT  sing N N 184 
GLY OXT HXT  sing N N 185 
GOL C1  O1   sing N N 186 
GOL C1  C2   sing N N 187 
GOL C1  H11  sing N N 188 
GOL C1  H12  sing N N 189 
GOL O1  HO1  sing N N 190 
GOL C2  O2   sing N N 191 
GOL C2  C3   sing N N 192 
GOL C2  H2   sing N N 193 
GOL O2  HO2  sing N N 194 
GOL C3  O3   sing N N 195 
GOL C3  H31  sing N N 196 
GOL C3  H32  sing N N 197 
GOL O3  HO3  sing N N 198 
HEM CHA C1A  sing N N 199 
HEM CHA C4D  doub N N 200 
HEM CHA HHA  sing N N 201 
HEM CHB C4A  sing N N 202 
HEM CHB C1B  doub N N 203 
HEM CHB HHB  sing N N 204 
HEM CHC C4B  sing N N 205 
HEM CHC C1C  doub N N 206 
HEM CHC HHC  sing N N 207 
HEM CHD C4C  doub N N 208 
HEM CHD C1D  sing N N 209 
HEM CHD HHD  sing N N 210 
HEM C1A C2A  doub Y N 211 
HEM C1A NA   sing Y N 212 
HEM C2A C3A  sing Y N 213 
HEM C2A CAA  sing N N 214 
HEM C3A C4A  doub Y N 215 
HEM C3A CMA  sing N N 216 
HEM C4A NA   sing Y N 217 
HEM CMA HMA  sing N N 218 
HEM CMA HMAA sing N N 219 
HEM CMA HMAB sing N N 220 
HEM CAA CBA  sing N N 221 
HEM CAA HAA  sing N N 222 
HEM CAA HAAA sing N N 223 
HEM CBA CGA  sing N N 224 
HEM CBA HBA  sing N N 225 
HEM CBA HBAA sing N N 226 
HEM CGA O1A  doub N N 227 
HEM CGA O2A  sing N N 228 
HEM C1B C2B  sing N N 229 
HEM C1B NB   sing N N 230 
HEM C2B C3B  doub N N 231 
HEM C2B CMB  sing N N 232 
HEM C3B C4B  sing N N 233 
HEM C3B CAB  sing N N 234 
HEM C4B NB   doub N N 235 
HEM CMB HMB  sing N N 236 
HEM CMB HMBA sing N N 237 
HEM CMB HMBB sing N N 238 
HEM CAB CBB  doub N N 239 
HEM CAB HAB  sing N N 240 
HEM CBB HBB  sing N N 241 
HEM CBB HBBA sing N N 242 
HEM C1C C2C  sing Y N 243 
HEM C1C NC   sing Y N 244 
HEM C2C C3C  doub Y N 245 
HEM C2C CMC  sing N N 246 
HEM C3C C4C  sing Y N 247 
HEM C3C CAC  sing N N 248 
HEM C4C NC   sing Y N 249 
HEM CMC HMC  sing N N 250 
HEM CMC HMCA sing N N 251 
HEM CMC HMCB sing N N 252 
HEM CAC CBC  doub N N 253 
HEM CAC HAC  sing N N 254 
HEM CBC HBC  sing N N 255 
HEM CBC HBCA sing N N 256 
HEM C1D C2D  sing N N 257 
HEM C1D ND   doub N N 258 
HEM C2D C3D  doub N N 259 
HEM C2D CMD  sing N N 260 
HEM C3D C4D  sing N N 261 
HEM C3D CAD  sing N N 262 
HEM C4D ND   sing N N 263 
HEM CMD HMD  sing N N 264 
HEM CMD HMDA sing N N 265 
HEM CMD HMDB sing N N 266 
HEM CAD CBD  sing N N 267 
HEM CAD HAD  sing N N 268 
HEM CAD HADA sing N N 269 
HEM CBD CGD  sing N N 270 
HEM CBD HBD  sing N N 271 
HEM CBD HBDA sing N N 272 
HEM CGD O1D  doub N N 273 
HEM CGD O2D  sing N N 274 
HEM O2A H2A  sing N N 275 
HEM O2D H2D  sing N N 276 
HEM FE  NA   sing N N 277 
HEM FE  NB   sing N N 278 
HEM FE  NC   sing N N 279 
HEM FE  ND   sing N N 280 
HIS N   CA   sing N N 281 
HIS N   H    sing N N 282 
HIS N   H2   sing N N 283 
HIS CA  C    sing N N 284 
HIS CA  CB   sing N N 285 
HIS CA  HA   sing N N 286 
HIS C   O    doub N N 287 
HIS C   OXT  sing N N 288 
HIS CB  CG   sing N N 289 
HIS CB  HB2  sing N N 290 
HIS CB  HB3  sing N N 291 
HIS CG  ND1  sing Y N 292 
HIS CG  CD2  doub Y N 293 
HIS ND1 CE1  doub Y N 294 
HIS ND1 HD1  sing N N 295 
HIS CD2 NE2  sing Y N 296 
HIS CD2 HD2  sing N N 297 
HIS CE1 NE2  sing Y N 298 
HIS CE1 HE1  sing N N 299 
HIS NE2 HE2  sing N N 300 
HIS OXT HXT  sing N N 301 
HOH O   H1   sing N N 302 
HOH O   H2   sing N N 303 
ILE N   CA   sing N N 304 
ILE N   H    sing N N 305 
ILE N   H2   sing N N 306 
ILE CA  C    sing N N 307 
ILE CA  CB   sing N N 308 
ILE CA  HA   sing N N 309 
ILE C   O    doub N N 310 
ILE C   OXT  sing N N 311 
ILE CB  CG1  sing N N 312 
ILE CB  CG2  sing N N 313 
ILE CB  HB   sing N N 314 
ILE CG1 CD1  sing N N 315 
ILE CG1 HG12 sing N N 316 
ILE CG1 HG13 sing N N 317 
ILE CG2 HG21 sing N N 318 
ILE CG2 HG22 sing N N 319 
ILE CG2 HG23 sing N N 320 
ILE CD1 HD11 sing N N 321 
ILE CD1 HD12 sing N N 322 
ILE CD1 HD13 sing N N 323 
ILE OXT HXT  sing N N 324 
LEU N   CA   sing N N 325 
LEU N   H    sing N N 326 
LEU N   H2   sing N N 327 
LEU CA  C    sing N N 328 
LEU CA  CB   sing N N 329 
LEU CA  HA   sing N N 330 
LEU C   O    doub N N 331 
LEU C   OXT  sing N N 332 
LEU CB  CG   sing N N 333 
LEU CB  HB2  sing N N 334 
LEU CB  HB3  sing N N 335 
LEU CG  CD1  sing N N 336 
LEU CG  CD2  sing N N 337 
LEU CG  HG   sing N N 338 
LEU CD1 HD11 sing N N 339 
LEU CD1 HD12 sing N N 340 
LEU CD1 HD13 sing N N 341 
LEU CD2 HD21 sing N N 342 
LEU CD2 HD22 sing N N 343 
LEU CD2 HD23 sing N N 344 
LEU OXT HXT  sing N N 345 
LYS N   CA   sing N N 346 
LYS N   H    sing N N 347 
LYS N   H2   sing N N 348 
LYS CA  C    sing N N 349 
LYS CA  CB   sing N N 350 
LYS CA  HA   sing N N 351 
LYS C   O    doub N N 352 
LYS C   OXT  sing N N 353 
LYS CB  CG   sing N N 354 
LYS CB  HB2  sing N N 355 
LYS CB  HB3  sing N N 356 
LYS CG  CD   sing N N 357 
LYS CG  HG2  sing N N 358 
LYS CG  HG3  sing N N 359 
LYS CD  CE   sing N N 360 
LYS CD  HD2  sing N N 361 
LYS CD  HD3  sing N N 362 
LYS CE  NZ   sing N N 363 
LYS CE  HE2  sing N N 364 
LYS CE  HE3  sing N N 365 
LYS NZ  HZ1  sing N N 366 
LYS NZ  HZ2  sing N N 367 
LYS NZ  HZ3  sing N N 368 
LYS OXT HXT  sing N N 369 
MAN C1  C2   sing N N 370 
MAN C1  O1   sing N N 371 
MAN C1  O5   sing N N 372 
MAN C1  H1   sing N N 373 
MAN C2  C3   sing N N 374 
MAN C2  O2   sing N N 375 
MAN C2  H2   sing N N 376 
MAN C3  C4   sing N N 377 
MAN C3  O3   sing N N 378 
MAN C3  H3   sing N N 379 
MAN C4  C5   sing N N 380 
MAN C4  O4   sing N N 381 
MAN C4  H4   sing N N 382 
MAN C5  C6   sing N N 383 
MAN C5  O5   sing N N 384 
MAN C5  H5   sing N N 385 
MAN C6  O6   sing N N 386 
MAN C6  H61  sing N N 387 
MAN C6  H62  sing N N 388 
MAN O1  HO1  sing N N 389 
MAN O2  HO2  sing N N 390 
MAN O3  HO3  sing N N 391 
MAN O4  HO4  sing N N 392 
MAN O6  HO6  sing N N 393 
MET N   CA   sing N N 394 
MET N   H    sing N N 395 
MET N   H2   sing N N 396 
MET CA  C    sing N N 397 
MET CA  CB   sing N N 398 
MET CA  HA   sing N N 399 
MET C   O    doub N N 400 
MET C   OXT  sing N N 401 
MET CB  CG   sing N N 402 
MET CB  HB2  sing N N 403 
MET CB  HB3  sing N N 404 
MET CG  SD   sing N N 405 
MET CG  HG2  sing N N 406 
MET CG  HG3  sing N N 407 
MET SD  CE   sing N N 408 
MET CE  HE1  sing N N 409 
MET CE  HE2  sing N N 410 
MET CE  HE3  sing N N 411 
MET OXT HXT  sing N N 412 
MYR C1  O1   doub N N 413 
MYR C1  O2   sing N N 414 
MYR C1  C2   sing N N 415 
MYR O2  HO2  sing N N 416 
MYR C2  C3   sing N N 417 
MYR C2  H21  sing N N 418 
MYR C2  H22  sing N N 419 
MYR C3  C4   sing N N 420 
MYR C3  H31  sing N N 421 
MYR C3  H32  sing N N 422 
MYR C4  C5   sing N N 423 
MYR C4  H41  sing N N 424 
MYR C4  H42  sing N N 425 
MYR C5  C6   sing N N 426 
MYR C5  H51  sing N N 427 
MYR C5  H52  sing N N 428 
MYR C6  C7   sing N N 429 
MYR C6  H61  sing N N 430 
MYR C6  H62  sing N N 431 
MYR C7  C8   sing N N 432 
MYR C7  H71  sing N N 433 
MYR C7  H72  sing N N 434 
MYR C8  C9   sing N N 435 
MYR C8  H81  sing N N 436 
MYR C8  H82  sing N N 437 
MYR C9  C10  sing N N 438 
MYR C9  H91  sing N N 439 
MYR C9  H92  sing N N 440 
MYR C10 C11  sing N N 441 
MYR C10 H101 sing N N 442 
MYR C10 H102 sing N N 443 
MYR C11 C12  sing N N 444 
MYR C11 H111 sing N N 445 
MYR C11 H112 sing N N 446 
MYR C12 C13  sing N N 447 
MYR C12 H121 sing N N 448 
MYR C12 H122 sing N N 449 
MYR C13 C14  sing N N 450 
MYR C13 H131 sing N N 451 
MYR C13 H132 sing N N 452 
MYR C14 H141 sing N N 453 
MYR C14 H142 sing N N 454 
MYR C14 H143 sing N N 455 
NAG C1  C2   sing N N 456 
NAG C1  O1   sing N N 457 
NAG C1  O5   sing N N 458 
NAG C1  H1   sing N N 459 
NAG C2  C3   sing N N 460 
NAG C2  N2   sing N N 461 
NAG C2  H2   sing N N 462 
NAG C3  C4   sing N N 463 
NAG C3  O3   sing N N 464 
NAG C3  H3   sing N N 465 
NAG C4  C5   sing N N 466 
NAG C4  O4   sing N N 467 
NAG C4  H4   sing N N 468 
NAG C5  C6   sing N N 469 
NAG C5  O5   sing N N 470 
NAG C5  H5   sing N N 471 
NAG C6  O6   sing N N 472 
NAG C6  H61  sing N N 473 
NAG C6  H62  sing N N 474 
NAG C7  C8   sing N N 475 
NAG C7  N2   sing N N 476 
NAG C7  O7   doub N N 477 
NAG C8  H81  sing N N 478 
NAG C8  H82  sing N N 479 
NAG C8  H83  sing N N 480 
NAG N2  HN2  sing N N 481 
NAG O1  HO1  sing N N 482 
NAG O3  HO3  sing N N 483 
NAG O4  HO4  sing N N 484 
NAG O6  HO6  sing N N 485 
PHE N   CA   sing N N 486 
PHE N   H    sing N N 487 
PHE N   H2   sing N N 488 
PHE CA  C    sing N N 489 
PHE CA  CB   sing N N 490 
PHE CA  HA   sing N N 491 
PHE C   O    doub N N 492 
PHE C   OXT  sing N N 493 
PHE CB  CG   sing N N 494 
PHE CB  HB2  sing N N 495 
PHE CB  HB3  sing N N 496 
PHE CG  CD1  doub Y N 497 
PHE CG  CD2  sing Y N 498 
PHE CD1 CE1  sing Y N 499 
PHE CD1 HD1  sing N N 500 
PHE CD2 CE2  doub Y N 501 
PHE CD2 HD2  sing N N 502 
PHE CE1 CZ   doub Y N 503 
PHE CE1 HE1  sing N N 504 
PHE CE2 CZ   sing Y N 505 
PHE CE2 HE2  sing N N 506 
PHE CZ  HZ   sing N N 507 
PHE OXT HXT  sing N N 508 
PRO N   CA   sing N N 509 
PRO N   CD   sing N N 510 
PRO N   H    sing N N 511 
PRO CA  C    sing N N 512 
PRO CA  CB   sing N N 513 
PRO CA  HA   sing N N 514 
PRO C   O    doub N N 515 
PRO C   OXT  sing N N 516 
PRO CB  CG   sing N N 517 
PRO CB  HB2  sing N N 518 
PRO CB  HB3  sing N N 519 
PRO CG  CD   sing N N 520 
PRO CG  HG2  sing N N 521 
PRO CG  HG3  sing N N 522 
PRO CD  HD2  sing N N 523 
PRO CD  HD3  sing N N 524 
PRO OXT HXT  sing N N 525 
SER N   CA   sing N N 526 
SER N   H    sing N N 527 
SER N   H2   sing N N 528 
SER CA  C    sing N N 529 
SER CA  CB   sing N N 530 
SER CA  HA   sing N N 531 
SER C   O    doub N N 532 
SER C   OXT  sing N N 533 
SER CB  OG   sing N N 534 
SER CB  HB2  sing N N 535 
SER CB  HB3  sing N N 536 
SER OG  HG   sing N N 537 
SER OXT HXT  sing N N 538 
SO4 S   O1   doub N N 539 
SO4 S   O2   doub N N 540 
SO4 S   O3   sing N N 541 
SO4 S   O4   sing N N 542 
THR N   CA   sing N N 543 
THR N   H    sing N N 544 
THR N   H2   sing N N 545 
THR CA  C    sing N N 546 
THR CA  CB   sing N N 547 
THR CA  HA   sing N N 548 
THR C   O    doub N N 549 
THR C   OXT  sing N N 550 
THR CB  OG1  sing N N 551 
THR CB  CG2  sing N N 552 
THR CB  HB   sing N N 553 
THR OG1 HG1  sing N N 554 
THR CG2 HG21 sing N N 555 
THR CG2 HG22 sing N N 556 
THR CG2 HG23 sing N N 557 
THR OXT HXT  sing N N 558 
TRP N   CA   sing N N 559 
TRP N   H    sing N N 560 
TRP N   H2   sing N N 561 
TRP CA  C    sing N N 562 
TRP CA  CB   sing N N 563 
TRP CA  HA   sing N N 564 
TRP C   O    doub N N 565 
TRP C   OXT  sing N N 566 
TRP CB  CG   sing N N 567 
TRP CB  HB2  sing N N 568 
TRP CB  HB3  sing N N 569 
TRP CG  CD1  doub Y N 570 
TRP CG  CD2  sing Y N 571 
TRP CD1 NE1  sing Y N 572 
TRP CD1 HD1  sing N N 573 
TRP CD2 CE2  doub Y N 574 
TRP CD2 CE3  sing Y N 575 
TRP NE1 CE2  sing Y N 576 
TRP NE1 HE1  sing N N 577 
TRP CE2 CZ2  sing Y N 578 
TRP CE3 CZ3  doub Y N 579 
TRP CE3 HE3  sing N N 580 
TRP CZ2 CH2  doub Y N 581 
TRP CZ2 HZ2  sing N N 582 
TRP CZ3 CH2  sing Y N 583 
TRP CZ3 HZ3  sing N N 584 
TRP CH2 HH2  sing N N 585 
TRP OXT HXT  sing N N 586 
TYR N   CA   sing N N 587 
TYR N   H    sing N N 588 
TYR N   H2   sing N N 589 
TYR CA  C    sing N N 590 
TYR CA  CB   sing N N 591 
TYR CA  HA   sing N N 592 
TYR C   O    doub N N 593 
TYR C   OXT  sing N N 594 
TYR CB  CG   sing N N 595 
TYR CB  HB2  sing N N 596 
TYR CB  HB3  sing N N 597 
TYR CG  CD1  doub Y N 598 
TYR CG  CD2  sing Y N 599 
TYR CD1 CE1  sing Y N 600 
TYR CD1 HD1  sing N N 601 
TYR CD2 CE2  doub Y N 602 
TYR CD2 HD2  sing N N 603 
TYR CE1 CZ   doub Y N 604 
TYR CE1 HE1  sing N N 605 
TYR CE2 CZ   sing Y N 606 
TYR CE2 HE2  sing N N 607 
TYR CZ  OH   sing N N 608 
TYR OH  HH   sing N N 609 
TYR OXT HXT  sing N N 610 
VAL N   CA   sing N N 611 
VAL N   H    sing N N 612 
VAL N   H2   sing N N 613 
VAL CA  C    sing N N 614 
VAL CA  CB   sing N N 615 
VAL CA  HA   sing N N 616 
VAL C   O    doub N N 617 
VAL C   OXT  sing N N 618 
VAL CB  CG1  sing N N 619 
VAL CB  CG2  sing N N 620 
VAL CB  HB   sing N N 621 
VAL CG1 HG11 sing N N 622 
VAL CG1 HG12 sing N N 623 
VAL CG1 HG13 sing N N 624 
VAL CG2 HG21 sing N N 625 
VAL CG2 HG22 sing N N 626 
VAL CG2 HG23 sing N N 627 
VAL OXT HXT  sing N N 628 
# 
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 
6 BMA 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5OXU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HE7 
_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]   0.003677 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001471 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013358 
_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]   0.010178 
_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   ? 60.927  3.682   59.415 1.00 105.88 ? 14  GLN A N   1 
ATOM   2    C  CA  . GLN A  1  1   ? 62.071  4.160   58.587 1.00 106.17 ? 14  GLN A CA  1 
ATOM   3    C  C   . GLN A  1  1   ? 61.996  3.614   57.153 1.00 96.97  ? 14  GLN A C   1 
ATOM   4    O  O   . GLN A  1  1   ? 62.488  4.271   56.237 1.00 87.68  ? 14  GLN A O   1 
ATOM   5    C  CB  . GLN A  1  1   ? 63.393  3.842   59.289 1.00 112.73 ? 14  GLN A CB  1 
ATOM   6    C  CG  . GLN A  1  1   ? 63.707  2.354   59.389 1.00 123.62 ? 14  GLN A CG  1 
ATOM   7    C  CD  . GLN A  1  1   ? 65.003  2.055   60.107 1.00 129.40 ? 14  GLN A CD  1 
ATOM   8    O  OE1 . GLN A  1  1   ? 65.675  2.942   60.647 1.00 131.14 ? 14  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A  1  1   ? 65.364  0.781   60.120 1.00 130.66 ? 14  GLN A NE2 1 
ATOM   10   N  N   . GLY A  1  2   ? 61.427  2.405   56.962 1.00 82.77  ? 15  GLY A N   1 
ATOM   11   C  CA  . GLY A  1  2   ? 61.016  1.945   55.645 1.00 68.91  ? 15  GLY A CA  1 
ATOM   12   C  C   . GLY A  1  2   ? 61.016  0.423   55.499 1.00 59.16  ? 15  GLY A C   1 
ATOM   13   O  O   . GLY A  1  2   ? 61.514  -0.306  56.348 1.00 53.42  ? 15  GLY A O   1 
ATOM   14   N  N   . VAL A  1  3   ? 60.519  -0.024  54.346 1.00 46.26  ? 16  VAL A N   1 
ATOM   15   C  CA  . VAL A  1  3   ? 60.387  -1.431  54.005 1.00 45.59  ? 16  VAL A CA  1 
ATOM   16   C  C   . VAL A  1  3   ? 61.419  -1.797  52.937 1.00 43.33  ? 16  VAL A C   1 
ATOM   17   O  O   . VAL A  1  3   ? 61.820  -0.962  52.132 1.00 40.73  ? 16  VAL A O   1 
ATOM   18   C  CB  . VAL A  1  3   ? 58.931  -1.603  53.514 1.00 51.78  ? 16  VAL A CB  1 
ATOM   19   C  CG1 . VAL A  1  3   ? 58.677  -2.902  52.783 1.00 57.16  ? 16  VAL A CG1 1 
ATOM   20   C  CG2 . VAL A  1  3   ? 57.964  -1.451  54.675 1.00 56.75  ? 16  VAL A CG2 1 
ATOM   21   N  N   . ASP A  1  4   ? 61.795  -3.079  52.892 1.00 41.23  ? 17  ASP A N   1 
ATOM   22   C  CA  . ASP A  1  4   ? 62.560  -3.642  51.792 1.00 43.77  ? 17  ASP A CA  1 
ATOM   23   C  C   . ASP A  1  4   ? 61.594  -4.382  50.856 1.00 43.42  ? 17  ASP A C   1 
ATOM   24   O  O   . ASP A  1  4   ? 61.104  -5.448  51.205 1.00 49.69  ? 17  ASP A O   1 
ATOM   25   C  CB  . ASP A  1  4   ? 63.650  -4.548  52.340 1.00 55.30  ? 17  ASP A CB  1 
ATOM   26   C  CG  . ASP A  1  4   ? 64.796  -4.852  51.388 1.00 68.09  ? 17  ASP A CG  1 
ATOM   27   O  OD1 . ASP A  1  4   ? 64.764  -4.359  50.241 1.00 67.65  ? 17  ASP A OD1 1 
ATOM   28   O  OD2 . ASP A  1  4   ? 65.722  -5.569  51.808 1.00 87.82  ? 17  ASP A OD2 1 
ATOM   29   N  N   . PRO A  1  5   ? 61.253  -3.845  49.657 1.00 42.36  ? 18  PRO A N   1 
ATOM   30   C  CA  . PRO A  1  5   ? 60.146  -4.386  48.852 1.00 43.08  ? 18  PRO A CA  1 
ATOM   31   C  C   . PRO A  1  5   ? 60.524  -5.689  48.147 1.00 37.02  ? 18  PRO A C   1 
ATOM   32   O  O   . PRO A  1  5   ? 61.528  -5.720  47.450 1.00 38.25  ? 18  PRO A O   1 
ATOM   33   C  CB  . PRO A  1  5   ? 59.841  -3.297  47.828 1.00 38.91  ? 18  PRO A CB  1 
ATOM   34   C  CG  . PRO A  1  5   ? 61.082  -2.421  47.786 1.00 42.02  ? 18  PRO A CG  1 
ATOM   35   C  CD  . PRO A  1  5   ? 61.939  -2.718  49.002 1.00 39.94  ? 18  PRO A CD  1 
ATOM   36   N  N   . PRO A  1  6   ? 59.723  -6.770  48.266 1.00 35.77  ? 19  PRO A N   1 
ATOM   37   C  CA  . PRO A  1  6   ? 60.071  -8.057  47.659 1.00 40.09  ? 19  PRO A CA  1 
ATOM   38   C  C   . PRO A  1  6   ? 59.771  -8.035  46.165 1.00 40.22  ? 19  PRO A C   1 
ATOM   39   O  O   . PRO A  1  6   ? 59.015  -7.187  45.703 1.00 36.38  ? 19  PRO A O   1 
ATOM   40   C  CB  . PRO A  1  6   ? 59.183  -9.052  48.414 1.00 39.46  ? 19  PRO A CB  1 
ATOM   41   C  CG  . PRO A  1  6   ? 57.953  -8.250  48.717 1.00 42.67  ? 19  PRO A CG  1 
ATOM   42   C  CD  . PRO A  1  6   ? 58.439  -6.821  48.981 1.00 41.63  ? 19  PRO A CD  1 
ATOM   43   N  N   . PRO A  1  7   ? 60.374  -8.942  45.365 1.00 42.10  ? 20  PRO A N   1 
ATOM   44   C  CA  . PRO A  1  7   ? 60.027  -9.073  43.957 1.00 40.40  ? 20  PRO A CA  1 
ATOM   45   C  C   . PRO A  1  7   ? 58.558  -9.463  43.813 1.00 34.50  ? 20  PRO A C   1 
ATOM   46   O  O   . PRO A  1  7   ? 57.942  -9.982  44.738 1.00 32.39  ? 20  PRO A O   1 
ATOM   47   C  CB  . PRO A  1  7   ? 60.982  -10.152 43.415 1.00 46.57  ? 20  PRO A CB  1 
ATOM   48   C  CG  . PRO A  1  7   ? 61.477  -10.876 44.647 1.00 49.20  ? 20  PRO A CG  1 
ATOM   49   C  CD  . PRO A  1  7   ? 61.458  -9.857  45.765 1.00 49.23  ? 20  PRO A CD  1 
ATOM   50   N  N   . PRO A  1  8   ? 57.931  -9.165  42.662 1.00 31.02  ? 21  PRO A N   1 
ATOM   51   C  CA  . PRO A  1  8   ? 56.511  -9.466  42.484 1.00 32.18  ? 21  PRO A CA  1 
ATOM   52   C  C   . PRO A  1  8   ? 56.239  -10.970 42.533 1.00 32.48  ? 21  PRO A C   1 
ATOM   53   O  O   . PRO A  1  8   ? 57.079  -11.769 42.141 1.00 31.65  ? 21  PRO A O   1 
ATOM   54   C  CB  . PRO A  1  8   ? 56.204  -8.890  41.123 1.00 31.61  ? 21  PRO A CB  1 
ATOM   55   C  CG  . PRO A  1  8   ? 57.529  -8.870  40.423 1.00 33.32  ? 21  PRO A CG  1 
ATOM   56   C  CD  . PRO A  1  8   ? 58.537  -8.501  41.498 1.00 32.95  ? 21  PRO A CD  1 
ATOM   57   N  N   . PRO A  1  9   ? 55.047  -11.387 42.993 1.00 31.72  ? 22  PRO A N   1 
ATOM   58   C  CA  . PRO A  1  9   ? 54.611  -12.773 42.851 1.00 31.27  ? 22  PRO A CA  1 
ATOM   59   C  C   . PRO A  1  9   ? 54.658  -13.177 41.385 1.00 31.17  ? 22  PRO A C   1 
ATOM   60   O  O   . PRO A  1  9   ? 54.510  -12.347 40.498 1.00 30.33  ? 22  PRO A O   1 
ATOM   61   C  CB  . PRO A  1  9   ? 53.186  -12.774 43.386 1.00 34.42  ? 22  PRO A CB  1 
ATOM   62   C  CG  . PRO A  1  9   ? 53.142  -11.576 44.306 1.00 36.20  ? 22  PRO A CG  1 
ATOM   63   C  CD  . PRO A  1  9   ? 54.053  -10.551 43.677 1.00 34.59  ? 22  PRO A CD  1 
ATOM   64   N  N   . GLY A  1  10  ? 54.879  -14.475 41.157 1.00 30.89  ? 23  GLY A N   1 
ATOM   65   C  CA  . GLY A  1  10  ? 54.684  -15.097 39.870 1.00 29.10  ? 23  GLY A CA  1 
ATOM   66   C  C   . GLY A  1  10  ? 53.226  -15.496 39.674 1.00 30.45  ? 23  GLY A C   1 
ATOM   67   O  O   . GLY A  1  10  ? 52.361  -15.167 40.494 1.00 29.73  ? 23  GLY A O   1 
ATOM   68   N  N   . PRO A  1  11  ? 52.919  -16.194 38.561 1.00 33.47  ? 24  PRO A N   1 
ATOM   69   C  CA  . PRO A  1  11  ? 51.555  -16.649 38.271 1.00 34.00  ? 24  PRO A CA  1 
ATOM   70   C  C   . PRO A  1  11  ? 51.025  -17.529 39.398 1.00 32.56  ? 24  PRO A C   1 
ATOM   71   O  O   . PRO A  1  11  ? 51.796  -18.129 40.114 1.00 32.08  ? 24  PRO A O   1 
ATOM   72   C  CB  . PRO A  1  11  ? 51.702  -17.454 36.965 1.00 35.98  ? 24  PRO A CB  1 
ATOM   73   C  CG  . PRO A  1  11  ? 53.006  -16.958 36.367 1.00 37.49  ? 24  PRO A CG  1 
ATOM   74   C  CD  . PRO A  1  11  ? 53.891  -16.610 37.536 1.00 36.19  ? 24  PRO A CD  1 
ATOM   75   N  N   . PRO A  1  12  ? 49.697  -17.643 39.604 1.00 32.02  ? 25  PRO A N   1 
ATOM   76   C  CA  . PRO A  1  12  ? 49.194  -18.563 40.620 1.00 35.09  ? 25  PRO A CA  1 
ATOM   77   C  C   . PRO A  1  12  ? 49.467  -20.014 40.200 1.00 37.64  ? 25  PRO A C   1 
ATOM   78   O  O   . PRO A  1  12  ? 49.507  -20.324 39.018 1.00 34.09  ? 25  PRO A O   1 
ATOM   79   C  CB  . PRO A  1  12  ? 47.713  -18.199 40.691 1.00 34.43  ? 25  PRO A CB  1 
ATOM   80   C  CG  . PRO A  1  12  ? 47.383  -17.672 39.303 1.00 34.98  ? 25  PRO A CG  1 
ATOM   81   C  CD  . PRO A  1  12  ? 48.647  -17.003 38.808 1.00 33.06  ? 25  PRO A CD  1 
ATOM   82   N  N   . SER A  1  13  ? 49.685  -20.877 41.196 1.00 38.35  ? 26  SER A N   1 
ATOM   83   C  CA  A SER A  1  13  ? 49.873  -22.306 41.006 0.50 38.66  ? 26  SER A CA  1 
ATOM   84   C  CA  B SER A  1  13  ? 49.869  -22.309 41.016 0.50 39.48  ? 26  SER A CA  1 
ATOM   85   C  C   . SER A  1  13  ? 48.677  -22.914 40.281 1.00 36.34  ? 26  SER A C   1 
ATOM   86   O  O   . SER A  1  13  ? 48.846  -23.772 39.434 1.00 36.43  ? 26  SER A O   1 
ATOM   87   C  CB  A SER A  1  13  ? 50.092  -22.983 42.337 0.50 40.92  ? 26  SER A CB  1 
ATOM   88   C  CB  B SER A  1  13  ? 50.061  -22.990 42.359 0.50 42.79  ? 26  SER A CB  1 
ATOM   89   O  OG  A SER A  1  13  ? 51.324  -22.546 42.889 0.50 41.66  ? 26  SER A OG  1 
ATOM   90   O  OG  B SER A  1  13  ? 49.966  -24.402 42.235 0.50 46.23  ? 26  SER A OG  1 
ATOM   91   N  N   . PHE A  1  14  ? 47.466  -22.486 40.648 1.00 32.61  ? 27  PHE A N   1 
ATOM   92   C  CA  . PHE A  1  14  ? 46.251  -22.942 39.986 1.00 31.41  ? 27  PHE A CA  1 
ATOM   93   C  C   . PHE A  1  14  ? 45.703  -21.804 39.119 1.00 31.54  ? 27  PHE A C   1 
ATOM   94   O  O   . PHE A  1  14  ? 45.419  -20.729 39.642 1.00 31.06  ? 27  PHE A O   1 
ATOM   95   C  CB  . PHE A  1  14  ? 45.236  -23.405 41.043 1.00 31.79  ? 27  PHE A CB  1 
ATOM   96   C  CG  . PHE A  1  14  ? 43.914  -23.835 40.418 1.00 31.70  ? 27  PHE A CG  1 
ATOM   97   C  CD1 . PHE A  1  14  ? 43.807  -25.048 39.736 1.00 32.78  ? 27  PHE A CD1 1 
ATOM   98   C  CD2 . PHE A  1  14  ? 42.784  -23.030 40.508 1.00 30.76  ? 27  PHE A CD2 1 
ATOM   99   C  CE1 . PHE A  1  14  ? 42.617  -25.410 39.110 1.00 35.00  ? 27  PHE A CE1 1 
ATOM   100  C  CE2 . PHE A  1  14  ? 41.584  -23.421 39.922 1.00 34.14  ? 27  PHE A CE2 1 
ATOM   101  C  CZ  . PHE A  1  14  ? 41.498  -24.608 39.225 1.00 34.06  ? 27  PHE A CZ  1 
ATOM   102  N  N   . THR A  1  15  ? 45.516  -22.060 37.814 1.00 30.26  ? 28  THR A N   1 
ATOM   103  C  CA  . THR A  1  15  ? 45.123  -21.036 36.859 1.00 34.01  ? 28  THR A CA  1 
ATOM   104  C  C   . THR A  1  15  ? 43.770  -21.339 36.230 1.00 31.67  ? 28  THR A C   1 
ATOM   105  O  O   . THR A  1  15  ? 43.418  -20.684 35.248 1.00 32.58  ? 28  THR A O   1 
ATOM   106  C  CB  . THR A  1  15  ? 46.183  -20.913 35.766 1.00 36.28  ? 28  THR A CB  1 
ATOM   107  O  OG1 . THR A  1  15  ? 46.164  -22.177 35.109 1.00 38.51  ? 28  THR A OG1 1 
ATOM   108  C  CG2 . THR A  1  15  ? 47.545  -20.567 36.329 1.00 39.61  ? 28  THR A CG2 1 
ATOM   109  N  N   . GLY A  1  16  ? 43.017  -22.304 36.782 1.00 31.35  ? 29  GLY A N   1 
ATOM   110  C  CA  . GLY A  1  16  ? 41.696  -22.622 36.253 1.00 29.57  ? 29  GLY A CA  1 
ATOM   111  C  C   . GLY A  1  16  ? 40.609  -21.723 36.846 1.00 31.14  ? 29  GLY A C   1 
ATOM   112  O  O   . GLY A  1  16  ? 40.890  -20.837 37.660 1.00 29.33  ? 29  GLY A O   1 
ATOM   113  N  N   . THR A  1  17  ? 39.354  -21.969 36.449 1.00 28.11  ? 30  THR A N   1 
ATOM   114  C  CA  . THR A  1  17  ? 38.229  -21.239 37.004 1.00 29.75  ? 30  THR A CA  1 
ATOM   115  C  C   . THR A  1  17  ? 38.032  -21.696 38.444 1.00 32.23  ? 30  THR A C   1 
ATOM   116  O  O   . THR A  1  17  ? 38.434  -22.792 38.836 1.00 31.15  ? 30  THR A O   1 
ATOM   117  C  CB  . THR A  1  17  ? 36.946  -21.417 36.184 1.00 33.98  ? 30  THR A CB  1 
ATOM   118  O  OG1 . THR A  1  17  ? 36.049  -20.442 36.712 1.00 33.66  ? 30  THR A OG1 1 
ATOM   119  C  CG2 . THR A  1  17  ? 36.341  -22.811 36.321 1.00 32.41  ? 30  THR A CG2 1 
ATOM   120  N  N   . LYS A  1  18  ? 37.412  -20.820 39.228 1.00 29.87  ? 31  LYS A N   1 
ATOM   121  C  CA  . LYS A  1  18  ? 36.986  -21.163 40.570 1.00 30.23  ? 31  LYS A CA  1 
ATOM   122  C  C   . LYS A  1  18  ? 35.998  -20.101 41.024 1.00 29.57  ? 31  LYS A C   1 
ATOM   123  O  O   . LYS A  1  18  ? 35.957  -19.008 40.454 1.00 30.33  ? 31  LYS A O   1 
ATOM   124  C  CB  . LYS A  1  18  ? 38.147  -21.239 41.571 1.00 33.33  ? 31  LYS A CB  1 
ATOM   125  C  CG  . LYS A  1  18  ? 38.950  -19.963 41.781 1.00 36.74  ? 31  LYS A CG  1 
ATOM   126  C  CD  . LYS A  1  18  ? 40.068  -20.138 42.809 1.00 42.72  ? 31  LYS A CD  1 
ATOM   127  C  CE  . LYS A  1  18  ? 40.504  -18.815 43.352 1.00 53.49  ? 31  LYS A CE  1 
ATOM   128  N  NZ  . LYS A  1  18  ? 41.713  -18.836 44.185 1.00 57.73  ? 31  LYS A NZ  1 
ATOM   129  N  N   . LEU A  1  19  ? 35.241  -20.440 42.067 1.00 29.93  ? 32  LEU A N   1 
ATOM   130  C  CA  . LEU A  1  19  ? 34.357  -19.496 42.717 1.00 30.12  ? 32  LEU A CA  1 
ATOM   131  C  C   . LEU A  1  19  ? 35.202  -18.461 43.450 1.00 27.79  ? 32  LEU A C   1 
ATOM   132  O  O   . LEU A  1  19  ? 36.003  -18.816 44.305 1.00 29.85  ? 32  LEU A O   1 
ATOM   133  C  CB  . LEU A  1  19  ? 33.435  -20.220 43.695 1.00 33.68  ? 32  LEU A CB  1 
ATOM   134  C  CG  . LEU A  1  19  ? 32.549  -19.291 44.535 1.00 32.14  ? 32  LEU A CG  1 
ATOM   135  C  CD1 . LEU A  1  19  ? 31.528  -18.611 43.669 1.00 30.64  ? 32  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A  1  19  ? 31.879  -20.050 45.669 1.00 36.75  ? 32  LEU A CD2 1 
ATOM   137  N  N   . VAL A  1  20  ? 35.004  -17.181 43.136 1.00 31.57  ? 33  VAL A N   1 
ATOM   138  C  CA  . VAL A  1  20  ? 35.771  -16.149 43.813 1.00 31.26  ? 33  VAL A CA  1 
ATOM   139  C  C   . VAL A  1  20  ? 34.864  -15.349 44.734 1.00 26.05  ? 33  VAL A C   1 
ATOM   140  O  O   . VAL A  1  20  ? 35.354  -14.791 45.708 1.00 28.02  ? 33  VAL A O   1 
ATOM   141  C  CB  . VAL A  1  20  ? 36.567  -15.243 42.858 1.00 33.70  ? 33  VAL A CB  1 
ATOM   142  C  CG1 . VAL A  1  20  ? 37.572  -16.031 42.039 1.00 32.10  ? 33  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A  1  20  ? 35.682  -14.426 41.959 1.00 34.14  ? 33  VAL A CG2 1 
ATOM   144  N  N   . ASN A  1  21  ? 33.568  -15.287 44.432 1.00 25.78  ? 34  ASN A N   1 
ATOM   145  C  CA  . ASN A  1  21  ? 32.617  -14.660 45.340 1.00 27.66  ? 34  ASN A CA  1 
ATOM   146  C  C   . ASN A  1  21  ? 32.168  -15.713 46.341 1.00 29.34  ? 34  ASN A C   1 
ATOM   147  O  O   . ASN A  1  21  ? 31.089  -16.250 46.209 1.00 28.54  ? 34  ASN A O   1 
ATOM   148  C  CB  . ASN A  1  21  ? 31.425  -14.070 44.607 1.00 28.87  ? 34  ASN A CB  1 
ATOM   149  C  CG  . ASN A  1  21  ? 30.489  -13.294 45.507 1.00 28.63  ? 34  ASN A CG  1 
ATOM   150  O  OD1 . ASN A  1  21  ? 30.735  -13.147 46.710 1.00 28.69  ? 34  ASN A OD1 1 
ATOM   151  N  ND2 . ASN A  1  21  ? 29.423  -12.773 44.923 1.00 27.30  ? 34  ASN A ND2 1 
ATOM   152  N  N   . ASP A  1  22  ? 33.019  -16.005 47.322 1.00 30.69  ? 35  ASP A N   1 
ATOM   153  C  CA  . ASP A  1  22  ? 32.830  -17.137 48.212 1.00 33.10  ? 35  ASP A CA  1 
ATOM   154  C  C   . ASP A  1  22  ? 32.656  -16.612 49.630 1.00 33.11  ? 35  ASP A C   1 
ATOM   155  O  O   . ASP A  1  22  ? 32.722  -15.403 49.889 1.00 34.05  ? 35  ASP A O   1 
ATOM   156  C  CB  . ASP A  1  22  ? 33.977  -18.131 48.070 1.00 33.43  ? 35  ASP A CB  1 
ATOM   157  C  CG  . ASP A  1  22  ? 35.373  -17.600 48.398 1.00 37.48  ? 35  ASP A CG  1 
ATOM   158  O  OD1 . ASP A  1  22  ? 35.486  -16.427 48.789 1.00 42.00  ? 35  ASP A OD1 1 
ATOM   159  O  OD2 . ASP A  1  22  ? 36.345  -18.337 48.229 1.00 37.66  ? 35  ASP A OD2 1 
ATOM   160  N  N   . ALA A  1  23  ? 32.450  -17.543 50.548 1.00 34.87  ? 36  ALA A N   1 
ATOM   161  C  CA  . ALA A  1  23  ? 32.067  -17.222 51.913 1.00 36.37  ? 36  ALA A CA  1 
ATOM   162  C  C   . ALA A  1  23  ? 33.175  -16.436 52.609 1.00 36.19  ? 36  ALA A C   1 
ATOM   163  O  O   . ALA A  1  23  ? 32.905  -15.607 53.464 1.00 35.57  ? 36  ALA A O   1 
ATOM   164  C  CB  . ALA A  1  23  ? 31.749  -18.508 52.660 1.00 40.72  ? 36  ALA A CB  1 
ATOM   165  N  N   . ASP A  1  24  ? 34.425  -16.696 52.234 1.00 34.13  ? 37  ASP A N   1 
ATOM   166  C  CA  . ASP A  1  24  ? 35.553  -16.051 52.871 1.00 35.18  ? 37  ASP A CA  1 
ATOM   167  C  C   . ASP A  1  24  ? 35.793  -14.637 52.323 1.00 33.16  ? 37  ASP A C   1 
ATOM   168  O  O   . ASP A  1  24  ? 36.595  -13.926 52.895 1.00 27.55  ? 37  ASP A O   1 
ATOM   169  C  CB  . ASP A  1  24  ? 36.799  -16.899 52.689 1.00 37.72  ? 37  ASP A CB  1 
ATOM   170  C  CG  . ASP A  1  24  ? 37.941  -16.601 53.651 1.00 43.47  ? 37  ASP A CG  1 
ATOM   171  O  OD1 . ASP A  1  24  ? 37.674  -16.649 54.864 1.00 47.27  ? 37  ASP A OD1 1 
ATOM   172  O  OD2 . ASP A  1  24  ? 39.074  -16.348 53.172 1.00 47.13  ? 37  ASP A OD2 1 
ATOM   173  N  N   . HIS A  1  25  ? 35.133  -14.256 51.220 1.00 31.00  ? 38  HIS A N   1 
ATOM   174  C  CA  . HIS A  1  25  ? 35.352  -12.970 50.560 1.00 28.57  ? 38  HIS A CA  1 
ATOM   175  C  C   . HIS A  1  25  ? 34.002  -12.281 50.375 1.00 28.82  ? 38  HIS A C   1 
ATOM   176  O  O   . HIS A  1  25  ? 33.559  -12.065 49.259 1.00 28.73  ? 38  HIS A O   1 
ATOM   177  C  CB  . HIS A  1  25  ? 36.122  -13.176 49.243 1.00 29.79  ? 38  HIS A CB  1 
ATOM   178  C  CG  . HIS A  1  25  ? 37.511  -13.690 49.458 1.00 30.33  ? 38  HIS A CG  1 
ATOM   179  N  ND1 . HIS A  1  25  ? 37.841  -15.029 49.364 1.00 30.12  ? 38  HIS A ND1 1 
ATOM   180  C  CD2 . HIS A  1  25  ? 38.644  -13.062 49.817 1.00 29.80  ? 38  HIS A CD2 1 
ATOM   181  C  CE1 . HIS A  1  25  ? 39.149  -15.173 49.606 1.00 32.73  ? 38  HIS A CE1 1 
ATOM   182  N  NE2 . HIS A  1  25  ? 39.653  -13.993 49.900 1.00 30.99  ? 38  HIS A NE2 1 
ATOM   183  N  N   . PRO A  1  26  ? 33.263  -11.986 51.464 1.00 26.67  ? 39  PRO A N   1 
ATOM   184  C  CA  . PRO A  1  26  ? 31.950  -11.360 51.360 1.00 28.88  ? 39  PRO A CA  1 
ATOM   185  C  C   . PRO A  1  26  ? 32.082  -9.882  50.988 1.00 27.51  ? 39  PRO A C   1 
ATOM   186  O  O   . PRO A  1  26  ? 32.997  -9.205  51.455 1.00 25.69  ? 39  PRO A O   1 
ATOM   187  C  CB  . PRO A  1  26  ? 31.378  -11.515 52.758 1.00 26.56  ? 39  PRO A CB  1 
ATOM   188  C  CG  . PRO A  1  26  ? 32.604  -11.491 53.658 1.00 29.29  ? 39  PRO A CG  1 
ATOM   189  C  CD  . PRO A  1  26  ? 33.680  -12.192 52.868 1.00 29.59  ? 39  PRO A CD  1 
ATOM   190  N  N   . TRP A  1  27  ? 31.172  -9.398  50.148 1.00 24.49  ? 40  TRP A N   1 
ATOM   191  C  CA  . TRP A  1  27  ? 31.010  -7.964  49.977 1.00 26.93  ? 40  TRP A CA  1 
ATOM   192  C  C   . TRP A  1  27  ? 30.670  -7.332  51.323 1.00 26.68  ? 40  TRP A C   1 
ATOM   193  O  O   . TRP A  1  27  ? 29.839  -7.867  52.069 1.00 26.85  ? 40  TRP A O   1 
ATOM   194  C  CB  . TRP A  1  27  ? 29.909  -7.671  48.951 1.00 27.52  ? 40  TRP A CB  1 
ATOM   195  C  CG  . TRP A  1  27  ? 29.749  -6.202  48.656 1.00 27.56  ? 40  TRP A CG  1 
ATOM   196  C  CD1 . TRP A  1  27  ? 30.410  -5.480  47.709 1.00 27.17  ? 40  TRP A CD1 1 
ATOM   197  C  CD2 . TRP A  1  27  ? 28.916  -5.267  49.372 1.00 27.87  ? 40  TRP A CD2 1 
ATOM   198  N  NE1 . TRP A  1  27  ? 30.035  -4.165  47.773 1.00 28.31  ? 40  TRP A NE1 1 
ATOM   199  C  CE2 . TRP A  1  27  ? 29.122  -4.003  48.782 1.00 28.19  ? 40  TRP A CE2 1 
ATOM   200  C  CE3 . TRP A  1  27  ? 28.021  -5.378  50.445 1.00 29.92  ? 40  TRP A CE3 1 
ATOM   201  C  CZ2 . TRP A  1  27  ? 28.452  -2.864  49.227 1.00 27.00  ? 40  TRP A CZ2 1 
ATOM   202  C  CZ3 . TRP A  1  27  ? 27.367  -4.245  50.891 1.00 30.29  ? 40  TRP A CZ3 1 
ATOM   203  C  CH2 . TRP A  1  27  ? 27.589  -3.010  50.290 1.00 30.66  ? 40  TRP A CH2 1 
ATOM   204  N  N   . GLN A  1  28  ? 31.309  -6.192  51.616 1.00 26.97  ? 41  GLN A N   1 
ATOM   205  C  CA  . GLN A  1  28  ? 30.960  -5.411  52.788 1.00 26.94  ? 41  GLN A CA  1 
ATOM   206  C  C   . GLN A  1  28  ? 30.949  -3.936  52.423 1.00 29.43  ? 41  GLN A C   1 
ATOM   207  O  O   . GLN A  1  28  ? 31.694  -3.491  51.556 1.00 28.20  ? 41  GLN A O   1 
ATOM   208  C  CB  . GLN A  1  28  ? 31.911  -5.650  53.960 1.00 29.07  ? 41  GLN A CB  1 
ATOM   209  C  CG  . GLN A  1  28  ? 31.911  -7.088  54.453 1.00 29.09  ? 41  GLN A CG  1 
ATOM   210  C  CD  . GLN A  1  28  ? 32.924  -7.354  55.543 1.00 30.51  ? 41  GLN A CD  1 
ATOM   211  O  OE1 . GLN A  1  28  ? 33.739  -6.497  55.934 1.00 30.91  ? 41  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A  1  28  ? 32.880  -8.581  56.024 1.00 30.66  ? 41  GLN A NE2 1 
ATOM   213  N  N   . PRO A  1  29  ? 30.087  -3.142  53.090 1.00 28.67  ? 42  PRO A N   1 
ATOM   214  C  CA  . PRO A  1  29  ? 30.025  -1.707  52.844 1.00 30.41  ? 42  PRO A CA  1 
ATOM   215  C  C   . PRO A  1  29  ? 31.293  -0.999  53.320 1.00 29.45  ? 42  PRO A C   1 
ATOM   216  O  O   . PRO A  1  29  ? 32.067  -1.530  54.118 1.00 28.00  ? 42  PRO A O   1 
ATOM   217  C  CB  . PRO A  1  29  ? 28.771  -1.255  53.613 1.00 31.75  ? 42  PRO A CB  1 
ATOM   218  C  CG  . PRO A  1  29  ? 28.491  -2.354  54.620 1.00 33.90  ? 42  PRO A CG  1 
ATOM   219  C  CD  . PRO A  1  29  ? 29.126  -3.609  54.105 1.00 31.76  ? 42  PRO A CD  1 
ATOM   220  N  N   . LEU A  1  30  ? 31.491  0.214   52.794 1.00 29.41  ? 43  LEU A N   1 
ATOM   221  C  CA  . LEU A  1  30  ? 32.632  1.038   53.145 1.00 28.86  ? 43  LEU A CA  1 
ATOM   222  C  C   . LEU A  1  30  ? 32.536  1.464   54.605 1.00 29.36  ? 43  LEU A C   1 
ATOM   223  O  O   . LEU A  1  30  ? 31.452  1.729   55.101 1.00 32.19  ? 43  LEU A O   1 
ATOM   224  C  CB  . LEU A  1  30  ? 32.661  2.262   52.236 1.00 34.65  ? 43  LEU A CB  1 
ATOM   225  C  CG  . LEU A  1  30  ? 32.937  2.006   50.753 1.00 36.30  ? 43  LEU A CG  1 
ATOM   226  C  CD1 . LEU A  1  30  ? 33.124  3.359   50.077 1.00 38.47  ? 43  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A  1  30  ? 34.136  1.109   50.491 1.00 34.62  ? 43  LEU A CD2 1 
ATOM   228  N  N   . ARG A  1  31  ? 33.679  1.505   55.276 1.00 30.91  ? 44  ARG A N   1 
ATOM   229  C  CA  . ARG A  1  31  ? 33.817  2.129   56.586 1.00 35.69  ? 44  ARG A CA  1 
ATOM   230  C  C   . ARG A  1  31  ? 34.521  3.479   56.421 1.00 37.69  ? 44  ARG A C   1 
ATOM   231  O  O   . ARG A  1  31  ? 35.136  3.762   55.388 1.00 34.61  ? 44  ARG A O   1 
ATOM   232  C  CB  . ARG A  1  31  ? 34.674  1.264   57.520 1.00 38.45  ? 44  ARG A CB  1 
ATOM   233  C  CG  . ARG A  1  31  ? 34.271  -0.196  57.707 1.00 43.39  ? 44  ARG A CG  1 
ATOM   234  C  CD  . ARG A  1  31  ? 35.469  -1.033  58.187 1.00 54.41  ? 44  ARG A CD  1 
ATOM   235  N  NE  . ARG A  1  31  ? 36.647  -0.860  57.317 1.00 59.34  ? 44  ARG A NE  1 
ATOM   236  C  CZ  . ARG A  1  31  ? 37.767  -1.565  57.308 1.00 60.00  ? 44  ARG A CZ  1 
ATOM   237  N  NH1 . ARG A  1  31  ? 37.866  -2.714  57.959 1.00 76.10  ? 44  ARG A NH1 1 
ATOM   238  N  NH2 . ARG A  1  31  ? 38.772  -1.149  56.575 1.00 54.38  ? 44  ARG A NH2 1 
ATOM   239  N  N   . GLU A  1  32  ? 34.487  4.286   57.479 1.00 37.81  ? 45  GLU A N   1 
ATOM   240  C  CA  . GLU A  1  32  ? 35.198  5.554   57.521 1.00 43.86  ? 45  GLU A CA  1 
ATOM   241  C  C   . GLU A  1  32  ? 36.672  5.303   57.221 1.00 35.97  ? 45  GLU A C   1 
ATOM   242  O  O   . GLU A  1  32  ? 37.289  4.405   57.794 1.00 38.05  ? 45  GLU A O   1 
ATOM   243  C  CB  . GLU A  1  32  ? 34.997  6.216   58.893 1.00 54.31  ? 45  GLU A CB  1 
ATOM   244  C  CG  . GLU A  1  32  ? 35.690  7.569   59.072 1.00 68.75  ? 45  GLU A CG  1 
ATOM   245  C  CD  . GLU A  1  32  ? 37.066  7.570   59.747 1.00 91.58  ? 45  GLU A CD  1 
ATOM   246  O  OE1 . GLU A  1  32  ? 37.867  8.481   59.427 1.00 100.86 ? 45  GLU A OE1 1 
ATOM   247  O  OE2 . GLU A  1  32  ? 37.350  6.698   60.612 1.00 109.30 ? 45  GLU A OE2 1 
ATOM   248  N  N   . GLY A  1  33  ? 37.215  6.092   56.289 1.00 38.91  ? 46  GLY A N   1 
ATOM   249  C  CA  . GLY A  1  33  ? 38.621  6.014   55.920 1.00 36.61  ? 46  GLY A CA  1 
ATOM   250  C  C   . GLY A  1  33  ? 38.915  5.024   54.784 1.00 35.06  ? 46  GLY A C   1 
ATOM   251  O  O   . GLY A  1  33  ? 40.052  4.963   54.307 1.00 35.64  ? 46  GLY A O   1 
ATOM   252  N  N   . ASP A  1  34  ? 37.935  4.198   54.385 1.00 32.77  ? 47  ASP A N   1 
ATOM   253  C  CA  . ASP A  1  34  ? 38.148  3.258   53.283 1.00 32.72  ? 47  ASP A CA  1 
ATOM   254  C  C   . ASP A  1  34  ? 38.291  4.027   51.977 1.00 30.94  ? 47  ASP A C   1 
ATOM   255  O  O   . ASP A  1  34  ? 37.533  4.946   51.725 1.00 32.64  ? 47  ASP A O   1 
ATOM   256  C  CB  . ASP A  1  34  ? 37.050  2.211   53.183 1.00 34.36  ? 47  ASP A CB  1 
ATOM   257  C  CG  . ASP A  1  34  ? 37.073  1.131   54.260 1.00 35.31  ? 47  ASP A CG  1 
ATOM   258  O  OD1 . ASP A  1  34  ? 38.085  1.050   55.010 1.00 33.59  ? 47  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A  1  34  ? 36.080  0.382   54.355 1.00 34.02  ? 47  ASP A OD2 1 
ATOM   260  N  N   . ILE A  1  35  ? 39.250  3.626   51.142 1.00 28.12  ? 48  ILE A N   1 
ATOM   261  C  CA  . ILE A  1  35  ? 39.544  4.322   49.902 1.00 27.43  ? 48  ILE A CA  1 
ATOM   262  C  C   . ILE A  1  35  ? 39.103  3.474   48.709 1.00 28.05  ? 48  ILE A C   1 
ATOM   263  O  O   . ILE A  1  35  ? 39.390  2.273   48.640 1.00 24.86  ? 48  ILE A O   1 
ATOM   264  C  CB  . ILE A  1  35  ? 41.054  4.621   49.817 1.00 29.37  ? 48  ILE A CB  1 
ATOM   265  C  CG1 . ILE A  1  35  ? 41.565  5.502   50.958 1.00 33.21  ? 48  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A  1  35  ? 41.378  5.230   48.469 1.00 29.79  ? 48  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A  1  35  ? 40.947  6.893   51.010 1.00 34.41  ? 48  ILE A CD1 1 
ATOM   268  N  N   . ARG A  1  36  ? 38.429  4.118   47.749 1.00 25.64  ? 49  ARG A N   1 
ATOM   269  C  CA  . ARG A  1  36  ? 38.090  3.506   46.477 1.00 26.57  ? 49  ARG A CA  1 
ATOM   270  C  C   . ARG A  1  36  ? 38.420  4.525   45.403 1.00 28.15  ? 49  ARG A C   1 
ATOM   271  O  O   . ARG A  1  36  ? 38.545  5.700   45.721 1.00 29.13  ? 49  ARG A O   1 
ATOM   272  C  CB  . ARG A  1  36  ? 36.605  3.123   46.416 1.00 25.82  ? 49  ARG A CB  1 
ATOM   273  C  CG  . ARG A  1  36  ? 36.197  2.073   47.443 1.00 23.07  ? 49  ARG A CG  1 
ATOM   274  C  CD  . ARG A  1  36  ? 36.828  0.711   47.130 1.00 22.88  ? 49  ARG A CD  1 
ATOM   275  N  NE  . ARG A  1  36  ? 36.387  -0.304  48.098 1.00 21.65  ? 49  ARG A NE  1 
ATOM   276  C  CZ  . ARG A  1  36  ? 36.918  -0.529  49.295 1.00 23.53  ? 49  ARG A CZ  1 
ATOM   277  N  NH1 . ARG A  1  36  ? 37.970  0.152   49.722 1.00 25.69  ? 49  ARG A NH1 1 
ATOM   278  N  NH2 . ARG A  1  36  ? 36.395  -1.454  50.080 1.00 23.15  ? 49  ARG A NH2 1 
ATOM   279  N  N   . GLY A  1  37  ? 38.554  4.082   44.150 1.00 28.78  ? 50  GLY A N   1 
ATOM   280  C  CA  . GLY A  1  37  ? 39.063  4.947   43.106 1.00 25.55  ? 50  GLY A CA  1 
ATOM   281  C  C   . GLY A  1  37  ? 38.495  4.624   41.735 1.00 24.01  ? 50  GLY A C   1 
ATOM   282  O  O   . GLY A  1  37  ? 37.356  4.162   41.601 1.00 24.96  ? 50  GLY A O   1 
ATOM   283  N  N   . PRO A  1  38  ? 39.285  4.880   40.675 1.00 24.43  ? 51  PRO A N   1 
ATOM   284  C  CA  . PRO A  1  38  ? 38.793  4.800   39.309 1.00 25.25  ? 51  PRO A CA  1 
ATOM   285  C  C   . PRO A  1  38  ? 38.799  3.404   38.692 1.00 26.70  ? 51  PRO A C   1 
ATOM   286  O  O   . PRO A  1  38  ? 38.265  3.228   37.590 1.00 27.06  ? 51  PRO A O   1 
ATOM   287  C  CB  . PRO A  1  38  ? 39.767  5.716   38.614 1.00 25.38  ? 51  PRO A CB  1 
ATOM   288  C  CG  . PRO A  1  38  ? 41.076  5.418   39.287 1.00 25.31  ? 51  PRO A CG  1 
ATOM   289  C  CD  . PRO A  1  38  ? 40.707  5.255   40.742 1.00 25.95  ? 51  PRO A CD  1 
ATOM   290  N  N   . CYS A  1  39  ? 39.375  2.428   39.410 1.00 26.09  ? 52  CYS A N   1 
ATOM   291  C  CA  . CYS A  1  39  ? 39.467  1.073   38.881 1.00 26.66  ? 52  CYS A CA  1 
ATOM   292  C  C   . CYS A  1  39  ? 38.393  0.177   39.483 1.00 26.41  ? 52  CYS A C   1 
ATOM   293  O  O   . CYS A  1  39  ? 38.430  -0.137  40.670 1.00 24.90  ? 52  CYS A O   1 
ATOM   294  C  CB  . CYS A  1  39  ? 40.810  0.427   39.186 1.00 28.49  ? 52  CYS A CB  1 
ATOM   295  S  SG  . CYS A  1  39  ? 40.926  -1.250  38.499 1.00 28.34  ? 52  CYS A SG  1 
ATOM   296  N  N   . PRO A  1  40  ? 37.446  -0.333  38.673 1.00 26.39  ? 53  PRO A N   1 
ATOM   297  C  CA  . PRO A  1  40  ? 36.395  -1.216  39.185 1.00 25.97  ? 53  PRO A CA  1 
ATOM   298  C  C   . PRO A  1  40  ? 36.919  -2.587  39.610 1.00 25.73  ? 53  PRO A C   1 
ATOM   299  O  O   . PRO A  1  40  ? 36.366  -3.210  40.504 1.00 24.36  ? 53  PRO A O   1 
ATOM   300  C  CB  . PRO A  1  40  ? 35.398  -1.310  38.032 1.00 25.56  ? 53  PRO A CB  1 
ATOM   301  C  CG  . PRO A  1  40  ? 36.250  -1.071  36.806 1.00 27.51  ? 53  PRO A CG  1 
ATOM   302  C  CD  . PRO A  1  40  ? 37.337  -0.098  37.230 1.00 28.51  ? 53  PRO A CD  1 
ATOM   303  N  N   . GLY A  1  41  ? 38.028  -3.018  39.012 1.00 27.47  ? 54  GLY A N   1 
ATOM   304  C  CA  . GLY A  1  41  ? 38.655  -4.276  39.398 1.00 24.67  ? 54  GLY A CA  1 
ATOM   305  C  C   . GLY A  1  41  ? 39.181  -4.215  40.826 1.00 23.73  ? 54  GLY A C   1 
ATOM   306  O  O   . GLY A  1  41  ? 38.797  -5.011  41.684 1.00 25.08  ? 54  GLY A O   1 
ATOM   307  N  N   . LEU A  1  42  ? 40.058  -3.249  41.087 1.00 23.04  ? 55  LEU A N   1 
ATOM   308  C  CA  . LEU A  1  42  ? 40.627  -3.078  42.414 1.00 22.21  ? 55  LEU A CA  1 
ATOM   309  C  C   . LEU A  1  42  ? 39.547  -2.748  43.434 1.00 22.35  ? 55  LEU A C   1 
ATOM   310  O  O   . LEU A  1  42  ? 39.614  -3.232  44.565 1.00 24.72  ? 55  LEU A O   1 
ATOM   311  C  CB  . LEU A  1  42  ? 41.719  -2.012  42.387 1.00 23.72  ? 55  LEU A CB  1 
ATOM   312  C  CG  . LEU A  1  42  ? 42.898  -2.308  41.460 1.00 24.68  ? 55  LEU A CG  1 
ATOM   313  C  CD1 . LEU A  1  42  ? 43.901  -1.171  41.467 1.00 25.28  ? 55  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A  1  42  ? 43.603  -3.607  41.844 1.00 26.22  ? 55  LEU A CD2 1 
ATOM   315  N  N   . ASN A  1  43  ? 38.583  -1.899  43.043 1.00 23.06  ? 56  ASN A N   1 
ATOM   316  C  CA  . ASN A  1  43  ? 37.490  -1.552  43.939 1.00 25.61  ? 56  ASN A CA  1 
ATOM   317  C  C   . ASN A  1  43  ? 36.746  -2.807  44.410 1.00 24.02  ? 56  ASN A C   1 
ATOM   318  O  O   . ASN A  1  43  ? 36.468  -2.951  45.607 1.00 22.84  ? 56  ASN A O   1 
ATOM   319  C  CB  . ASN A  1  43  ? 36.501  -0.584  43.296 1.00 24.41  ? 56  ASN A CB  1 
ATOM   320  C  CG  . ASN A  1  43  ? 37.037  0.825   43.119 1.00 26.93  ? 56  ASN A CG  1 
ATOM   321  O  OD1 . ASN A  1  43  ? 38.043  1.225   43.716 1.00 25.08  ? 56  ASN A OD1 1 
ATOM   322  N  ND2 . ASN A  1  43  ? 36.360  1.591   42.284 1.00 26.31  ? 56  ASN A ND2 1 
ATOM   323  N  N   . THR A  1  44  ? 36.386  -3.678  43.468 1.00 23.95  ? 57  THR A N   1 
ATOM   324  C  CA  . THR A  1  44  ? 35.666  -4.908  43.800 1.00 23.38  ? 57  THR A CA  1 
ATOM   325  C  C   . THR A  1  44  ? 36.527  -5.832  44.684 1.00 23.65  ? 57  THR A C   1 
ATOM   326  O  O   . THR A  1  44  ? 36.039  -6.403  45.652 1.00 23.45  ? 57  THR A O   1 
ATOM   327  C  CB  . THR A  1  44  ? 35.205  -5.590  42.519 1.00 25.78  ? 57  THR A CB  1 
ATOM   328  O  OG1 . THR A  1  44  ? 34.373  -4.637  41.847 1.00 25.14  ? 57  THR A OG1 1 
ATOM   329  C  CG2 . THR A  1  44  ? 34.412  -6.852  42.801 1.00 24.01  ? 57  THR A CG2 1 
ATOM   330  N  N   . LEU A  1  45  ? 37.823  -5.959  44.389 1.00 25.71  ? 58  LEU A N   1 
ATOM   331  C  CA  . LEU A  1  45  ? 38.711  -6.784  45.199 1.00 23.60  ? 58  LEU A CA  1 
ATOM   332  C  C   . LEU A  1  45  ? 38.788  -6.248  46.631 1.00 25.60  ? 58  LEU A C   1 
ATOM   333  O  O   . LEU A  1  45  ? 38.788  -7.019  47.584 1.00 25.36  ? 58  LEU A O   1 
ATOM   334  C  CB  . LEU A  1  45  ? 40.080  -6.839  44.545 1.00 23.94  ? 58  LEU A CB  1 
ATOM   335  C  CG  . LEU A  1  45  ? 40.141  -7.543  43.186 1.00 23.81  ? 58  LEU A CG  1 
ATOM   336  C  CD1 . LEU A  1  45  ? 41.457  -7.301  42.452 1.00 23.64  ? 58  LEU A CD1 1 
ATOM   337  C  CD2 . LEU A  1  45  ? 39.928  -9.025  43.370 1.00 25.41  ? 58  LEU A CD2 1 
ATOM   338  N  N   . ALA A  1  46  ? 38.835  -4.921  46.794 1.00 24.66  ? 59  ALA A N   1 
ATOM   339  C  CA  . ALA A  1  46  ? 38.880  -4.339  48.124 1.00 25.05  ? 59  ALA A CA  1 
ATOM   340  C  C   . ALA A  1  46  ? 37.566  -4.589  48.853 1.00 20.61  ? 59  ALA A C   1 
ATOM   341  O  O   . ALA A  1  46  ? 37.570  -4.920  50.040 1.00 24.06  ? 59  ALA A O   1 
ATOM   342  C  CB  . ALA A  1  46  ? 39.186  -2.845  48.055 1.00 26.19  ? 59  ALA A CB  1 
ATOM   343  N  N   . SER A  1  47  ? 36.445  -4.428  48.162 1.00 21.16  ? 60  SER A N   1 
ATOM   344  C  CA  . SER A  1  47  ? 35.147  -4.513  48.816 1.00 22.66  ? 60  SER A CA  1 
ATOM   345  C  C   . SER A  1  47  ? 34.748  -5.959  49.122 1.00 24.34  ? 60  SER A C   1 
ATOM   346  O  O   . SER A  1  47  ? 33.790  -6.169  49.867 1.00 28.02  ? 60  SER A O   1 
ATOM   347  C  CB  . SER A  1  47  ? 34.070  -3.762  48.047 1.00 23.86  ? 60  SER A CB  1 
ATOM   348  O  OG  . SER A  1  47  ? 34.188  -2.366  48.277 1.00 24.25  ? 60  SER A OG  1 
ATOM   349  N  N   . HIS A  1  48  ? 35.489  -6.943  48.577 1.00 23.35  ? 61  HIS A N   1 
ATOM   350  C  CA  . HIS A  1  48  ? 35.320  -8.348  48.931 1.00 24.08  ? 61  HIS A CA  1 
ATOM   351  C  C   . HIS A  1  48  ? 36.472  -8.883  49.784 1.00 26.82  ? 61  HIS A C   1 
ATOM   352  O  O   . HIS A  1  48  ? 36.502  -10.076 50.067 1.00 26.00  ? 61  HIS A O   1 
ATOM   353  C  CB  . HIS A  1  48  ? 35.179  -9.223  47.684 1.00 24.57  ? 61  HIS A CB  1 
ATOM   354  C  CG  . HIS A  1  48  ? 33.828  -9.150  47.065 1.00 24.68  ? 61  HIS A CG  1 
ATOM   355  N  ND1 . HIS A  1  48  ? 32.869  -10.097 47.321 1.00 26.29  ? 61  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A  1  48  ? 33.279  -8.289  46.206 1.00 25.53  ? 61  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A  1  48  ? 31.778  -9.803  46.624 1.00 26.14  ? 61  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A  1  48  ? 31.991  -8.695  45.971 1.00 25.43  ? 61  HIS A NE2 1 
ATOM   359  N  N   . GLY A  1  49  ? 37.442  -8.026  50.142 1.00 24.25  ? 62  GLY A N   1 
ATOM   360  C  CA  . GLY A  1  49  ? 38.521  -8.436  51.032 1.00 24.83  ? 62  GLY A CA  1 
ATOM   361  C  C   . GLY A  1  49  ? 39.622  -9.268  50.366 1.00 24.87  ? 62  GLY A C   1 
ATOM   362  O  O   . GLY A  1  49  ? 40.443  -9.840  51.062 1.00 26.24  ? 62  GLY A O   1 
ATOM   363  N  N   . TYR A  1  50  ? 39.693  -9.308  49.038 1.00 24.41  ? 63  TYR A N   1 
ATOM   364  C  CA  . TYR A  1  50  ? 40.870  -9.813  48.348 1.00 25.02  ? 63  TYR A CA  1 
ATOM   365  C  C   . TYR A  1  50  ? 42.057  -8.866  48.543 1.00 28.82  ? 63  TYR A C   1 
ATOM   366  O  O   . TYR A  1  50  ? 43.202  -9.303  48.622 1.00 27.76  ? 63  TYR A O   1 
ATOM   367  C  CB  . TYR A  1  50  ? 40.609  -10.043 46.853 1.00 26.46  ? 63  TYR A CB  1 
ATOM   368  C  CG  . TYR A  1  50  ? 39.870  -11.347 46.578 1.00 26.48  ? 63  TYR A CG  1 
ATOM   369  C  CD1 . TYR A  1  50  ? 40.567  -12.560 46.499 1.00 28.64  ? 63  TYR A CD1 1 
ATOM   370  C  CD2 . TYR A  1  50  ? 38.491  -11.379 46.440 1.00 24.72  ? 63  TYR A CD2 1 
ATOM   371  C  CE1 . TYR A  1  50  ? 39.903  -13.754 46.275 1.00 27.64  ? 63  TYR A CE1 1 
ATOM   372  C  CE2 . TYR A  1  50  ? 37.818  -12.564 46.197 1.00 25.65  ? 63  TYR A CE2 1 
ATOM   373  C  CZ  . TYR A  1  50  ? 38.522  -13.756 46.136 1.00 29.00  ? 63  TYR A CZ  1 
ATOM   374  O  OH  . TYR A  1  50  ? 37.853  -14.926 45.936 1.00 29.58  ? 63  TYR A OH  1 
ATOM   375  N  N   . LEU A  1  51  ? 41.774  -7.560  48.547 1.00 28.47  ? 64  LEU A N   1 
ATOM   376  C  CA  . LEU A  1  51  ? 42.700  -6.534  49.015 1.00 30.59  ? 64  LEU A CA  1 
ATOM   377  C  C   . LEU A  1  51  ? 42.281  -6.111  50.421 1.00 29.28  ? 64  LEU A C   1 
ATOM   378  O  O   . LEU A  1  51  ? 41.129  -6.316  50.795 1.00 29.05  ? 64  LEU A O   1 
ATOM   379  C  CB  . LEU A  1  51  ? 42.642  -5.331  48.075 1.00 28.06  ? 64  LEU A CB  1 
ATOM   380  C  CG  . LEU A  1  51  ? 43.266  -5.545  46.693 1.00 30.21  ? 64  LEU A CG  1 
ATOM   381  C  CD1 . LEU A  1  51  ? 42.949  -4.370  45.800 1.00 30.08  ? 64  LEU A CD1 1 
ATOM   382  C  CD2 . LEU A  1  51  ? 44.764  -5.759  46.771 1.00 31.71  ? 64  LEU A CD2 1 
ATOM   383  N  N   . PRO A  1  52  ? 43.166  -5.444  51.194 1.00 29.20  ? 65  PRO A N   1 
ATOM   384  C  CA  . PRO A  1  52  ? 42.746  -4.752  52.407 1.00 30.15  ? 65  PRO A CA  1 
ATOM   385  C  C   . PRO A  1  52  ? 41.515  -3.904  52.093 1.00 28.25  ? 65  PRO A C   1 
ATOM   386  O  O   . PRO A  1  52  ? 41.454  -3.234  51.065 1.00 26.32  ? 65  PRO A O   1 
ATOM   387  C  CB  . PRO A  1  52  ? 43.983  -3.905  52.748 1.00 32.69  ? 65  PRO A CB  1 
ATOM   388  C  CG  . PRO A  1  52  ? 45.140  -4.685  52.178 1.00 30.75  ? 65  PRO A CG  1 
ATOM   389  C  CD  . PRO A  1  52  ? 44.597  -5.251  50.892 1.00 30.08  ? 65  PRO A CD  1 
ATOM   390  N  N   . ARG A  1  53  ? 40.502  -3.987  52.952 1.00 25.12  ? 66  ARG A N   1 
ATOM   391  C  CA  . ARG A  1  53  ? 39.224  -3.347  52.702 1.00 27.83  ? 66  ARG A CA  1 
ATOM   392  C  C   . ARG A  1  53  ? 39.343  -1.826  52.718 1.00 28.54  ? 66  ARG A C   1 
ATOM   393  O  O   . ARG A  1  53  ? 38.459  -1.139  52.227 1.00 27.16  ? 66  ARG A O   1 
ATOM   394  C  CB  . ARG A  1  53  ? 38.182  -3.858  53.697 1.00 30.47  ? 66  ARG A CB  1 
ATOM   395  C  CG  . ARG A  1  53  ? 37.837  -5.318  53.411 1.00 30.96  ? 66  ARG A CG  1 
ATOM   396  C  CD  . ARG A  1  53  ? 36.735  -5.838  54.302 1.00 31.58  ? 66  ARG A CD  1 
ATOM   397  N  NE  . ARG A  1  53  ? 36.461  -7.241  53.996 1.00 30.71  ? 66  ARG A NE  1 
ATOM   398  C  CZ  . ARG A  1  53  ? 35.551  -7.676  53.156 1.00 29.81  ? 66  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A  1  53  ? 34.868  -6.827  52.405 1.00 27.57  ? 66  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A  1  53  ? 35.331  -8.980  53.042 1.00 28.54  ? 66  ARG A NH2 1 
ATOM   401  N  N   . ASP A  1  54  ? 40.437  -1.301  53.269 1.00 29.62  ? 67  ASP A N   1 
ATOM   402  C  CA  . ASP A  1  54  ? 40.640  0.139   53.295 1.00 30.07  ? 67  ASP A CA  1 
ATOM   403  C  C   . ASP A  1  54  ? 41.186  0.663   51.978 1.00 27.50  ? 67  ASP A C   1 
ATOM   404  O  O   . ASP A  1  54  ? 41.348  1.860   51.831 1.00 28.64  ? 67  ASP A O   1 
ATOM   405  C  CB  . ASP A  1  54  ? 41.477  0.574   54.484 1.00 31.70  ? 67  ASP A CB  1 
ATOM   406  C  CG  . ASP A  1  54  ? 42.917  0.095   54.528 1.00 36.87  ? 67  ASP A CG  1 
ATOM   407  O  OD1 . ASP A  1  54  ? 43.375  -0.560  53.561 1.00 36.09  ? 67  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A  1  54  ? 43.562  0.362   55.547 1.00 40.52  ? 67  ASP A OD2 1 
ATOM   409  N  N   . GLY A  1  55  ? 41.497  -0.211  51.022 1.00 26.71  ? 68  GLY A N   1 
ATOM   410  C  CA  . GLY A  1  55  ? 41.890  0.241   49.695 1.00 25.73  ? 68  GLY A CA  1 
ATOM   411  C  C   . GLY A  1  55  ? 43.337  0.717   49.612 1.00 24.59  ? 68  GLY A C   1 
ATOM   412  O  O   . GLY A  1  55  ? 43.694  1.424   48.684 1.00 25.42  ? 68  GLY A O   1 
ATOM   413  N  N   . VAL A  1  56  ? 44.174  0.323   50.574 1.00 26.84  ? 69  VAL A N   1 
ATOM   414  C  CA  . VAL A  1  56  ? 45.592  0.630   50.530 1.00 28.59  ? 69  VAL A CA  1 
ATOM   415  C  C   . VAL A  1  56  ? 46.346  -0.686  50.642 1.00 27.23  ? 69  VAL A C   1 
ATOM   416  O  O   . VAL A  1  56  ? 46.072  -1.471  51.544 1.00 29.91  ? 69  VAL A O   1 
ATOM   417  C  CB  . VAL A  1  56  ? 45.979  1.616   51.656 1.00 32.99  ? 69  VAL A CB  1 
ATOM   418  C  CG1 . VAL A  1  56  ? 47.480  1.839   51.749 1.00 32.80  ? 69  VAL A CG1 1 
ATOM   419  C  CG2 . VAL A  1  56  ? 45.284  2.958   51.454 1.00 34.52  ? 69  VAL A CG2 1 
ATOM   420  N  N   . ALA A  1  57  ? 47.277  -0.918  49.725 1.00 26.68  ? 70  ALA A N   1 
ATOM   421  C  CA  . ALA A  1  57  ? 47.909  -2.222  49.620 1.00 26.49  ? 70  ALA A CA  1 
ATOM   422  C  C   . ALA A  1  57  ? 49.331  -2.113  49.092 1.00 26.00  ? 70  ALA A C   1 
ATOM   423  O  O   . ALA A  1  57  ? 49.686  -1.120  48.476 1.00 28.32  ? 70  ALA A O   1 
ATOM   424  C  CB  . ALA A  1  57  ? 47.081  -3.111  48.710 1.00 26.14  ? 70  ALA A CB  1 
ATOM   425  N  N   . THR A  1  58  ? 50.114  -3.180  49.292 1.00 25.25  ? 71  THR A N   1 
ATOM   426  C  CA  . THR A  1  58  ? 51.424  -3.306  48.689 1.00 25.78  ? 71  THR A CA  1 
ATOM   427  C  C   . THR A  1  58  ? 51.256  -3.740  47.246 1.00 26.01  ? 71  THR A C   1 
ATOM   428  O  O   . THR A  1  58  ? 50.240  -4.326  46.879 1.00 25.82  ? 71  THR A O   1 
ATOM   429  C  CB  . THR A  1  58  ? 52.309  -4.302  49.442 1.00 28.63  ? 71  THR A CB  1 
ATOM   430  O  OG1 . THR A  1  58  ? 51.760  -5.592  49.186 1.00 28.67  ? 71  THR A OG1 1 
ATOM   431  C  CG2 . THR A  1  58  ? 52.383  -4.050  50.941 1.00 28.38  ? 71  THR A CG2 1 
ATOM   432  N  N   . PRO A  1  59  ? 52.240  -3.451  46.373 1.00 26.53  ? 72  PRO A N   1 
ATOM   433  C  CA  . PRO A  1  59  ? 52.265  -4.009  45.031 1.00 27.35  ? 72  PRO A CA  1 
ATOM   434  C  C   . PRO A  1  59  ? 52.048  -5.523  44.985 1.00 28.33  ? 72  PRO A C   1 
ATOM   435  O  O   . PRO A  1  59  ? 51.294  -6.002  44.145 1.00 26.31  ? 72  PRO A O   1 
ATOM   436  C  CB  . PRO A  1  59  ? 53.671  -3.615  44.543 1.00 28.42  ? 72  PRO A CB  1 
ATOM   437  C  CG  . PRO A  1  59  ? 53.883  -2.277  45.224 1.00 30.01  ? 72  PRO A CG  1 
ATOM   438  C  CD  . PRO A  1  59  ? 53.368  -2.530  46.621 1.00 28.24  ? 72  PRO A CD  1 
ATOM   439  N  N   . ALA A  1  60  ? 52.723  -6.251  45.879 1.00 27.13  ? 73  ALA A N   1 
ATOM   440  C  CA  . ALA A  1  60  ? 52.595  -7.696  45.920 1.00 28.56  ? 73  ALA A CA  1 
ATOM   441  C  C   . ALA A  1  60  ? 51.152  -8.084  46.232 1.00 28.46  ? 73  ALA A C   1 
ATOM   442  O  O   . ALA A  1  60  ? 50.631  -8.981  45.599 1.00 27.61  ? 73  ALA A O   1 
ATOM   443  C  CB  . ALA A  1  60  ? 53.556  -8.304  46.917 1.00 28.16  ? 73  ALA A CB  1 
ATOM   444  N  N   . GLN A  1  61  ? 50.503  -7.402  47.182 1.00 25.27  ? 74  GLN A N   1 
ATOM   445  C  CA  . GLN A  1  61  ? 49.115  -7.691  47.492 1.00 25.18  ? 74  GLN A CA  1 
ATOM   446  C  C   . GLN A  1  61  ? 48.199  -7.454  46.292 1.00 28.51  ? 74  GLN A C   1 
ATOM   447  O  O   . GLN A  1  61  ? 47.287  -8.243  46.058 1.00 26.42  ? 74  GLN A O   1 
ATOM   448  C  CB  . GLN A  1  61  ? 48.601  -6.891  48.667 1.00 26.44  ? 74  GLN A CB  1 
ATOM   449  C  CG  . GLN A  1  61  ? 49.177  -7.346  49.998 1.00 30.99  ? 74  GLN A CG  1 
ATOM   450  C  CD  . GLN A  1  61  ? 48.786  -6.403  51.113 1.00 33.54  ? 74  GLN A CD  1 
ATOM   451  O  OE1 . GLN A  1  61  ? 48.769  -5.185  50.940 1.00 31.05  ? 74  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A  1  61  ? 48.411  -6.961  52.251 1.00 38.78  ? 74  GLN A NE2 1 
ATOM   453  N  N   . ILE A  1  62  ? 48.455  -6.391  45.519 1.00 25.88  ? 75  ILE A N   1 
ATOM   454  C  CA  . ILE A  1  62  ? 47.634  -6.076  44.369 1.00 26.26  ? 75  ILE A CA  1 
ATOM   455  C  C   . ILE A  1  62  ? 47.792  -7.170  43.311 1.00 28.04  ? 75  ILE A C   1 
ATOM   456  O  O   . ILE A  1  62  ? 46.807  -7.621  42.733 1.00 27.44  ? 75  ILE A O   1 
ATOM   457  C  CB  . ILE A  1  62  ? 47.978  -4.669  43.836 1.00 26.59  ? 75  ILE A CB  1 
ATOM   458  C  CG1 . ILE A  1  62  ? 47.492  -3.616  44.846 1.00 29.96  ? 75  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A  1  62  ? 47.399  -4.429  42.440 1.00 25.71  ? 75  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A  1  62  ? 48.085  -2.234  44.667 1.00 30.65  ? 75  ILE A CD1 1 
ATOM   461  N  N   . ILE A  1  63  ? 49.033  -7.584  43.049 1.00 24.13  ? 76  ILE A N   1 
ATOM   462  C  CA  . ILE A  1  63  ? 49.283  -8.578  42.022 1.00 27.49  ? 76  ILE A CA  1 
ATOM   463  C  C   . ILE A  1  63  ? 48.560  -9.873  42.400 1.00 25.10  ? 76  ILE A C   1 
ATOM   464  O  O   . ILE A  1  63  ? 47.837  -10.424 41.581 1.00 25.35  ? 76  ILE A O   1 
ATOM   465  C  CB  . ILE A  1  63  ? 50.790  -8.761  41.787 1.00 26.92  ? 76  ILE A CB  1 
ATOM   466  C  CG1 . ILE A  1  63  ? 51.353  -7.532  41.062 1.00 29.21  ? 76  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A  1  63  ? 51.064  -10.036 41.002 1.00 27.96  ? 76  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A  1  63  ? 52.841  -7.325  41.245 1.00 32.70  ? 76  ILE A CD1 1 
ATOM   469  N  N   . THR A  1  64  ? 48.699  -10.309 43.642 1.00 24.85  ? 77  THR A N   1 
ATOM   470  C  CA  A THR A  1  64  ? 48.099  -11.565 44.065 0.50 27.55  ? 77  THR A CA  1 
ATOM   471  C  CA  B THR A  1  64  ? 48.100  -11.568 44.073 0.50 29.38  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A  1  64  ? 46.575  -11.449 44.036 1.00 28.43  ? 77  THR A C   1 
ATOM   473  O  O   . THR A  1  64  ? 45.894  -12.362 43.596 1.00 27.10  ? 77  THR A O   1 
ATOM   474  C  CB  A THR A  1  64  ? 48.632  -11.942 45.440 0.50 26.05  ? 77  THR A CB  1 
ATOM   475  C  CB  B THR A  1  64  ? 48.655  -12.017 45.430 0.50 32.24  ? 77  THR A CB  1 
ATOM   476  O  OG1 A THR A  1  64  ? 48.201  -10.829 46.209 0.50 42.00  ? 77  THR A OG1 1 
ATOM   477  O  OG1 B THR A  1  64  ? 47.838  -13.026 46.039 0.50 29.52  ? 77  THR A OG1 1 
ATOM   478  C  CG2 A THR A  1  64  ? 50.130  -12.113 45.472 0.50 20.09  ? 77  THR A CG2 1 
ATOM   479  C  CG2 B THR A  1  64  ? 48.645  -10.951 46.500 0.50 41.18  ? 77  THR A CG2 1 
ATOM   480  N  N   . ALA A  1  65  ? 46.022  -10.288 44.441 1.00 26.44  ? 78  ALA A N   1 
ATOM   481  C  CA  . ALA A  1  65  ? 44.574  -10.108 44.444 1.00 24.25  ? 78  ALA A CA  1 
ATOM   482  C  C   . ALA A  1  65  ? 43.993  -10.133 43.031 1.00 23.76  ? 78  ALA A C   1 
ATOM   483  O  O   . ALA A  1  65  ? 42.952  -10.739 42.816 1.00 24.53  ? 78  ALA A O   1 
ATOM   484  C  CB  . ALA A  1  65  ? 44.163  -8.868  45.174 1.00 25.36  ? 78  ALA A CB  1 
ATOM   485  N  N   . THR A  1  66  ? 44.658  -9.497  42.063 1.00 23.28  ? 79  THR A N   1 
ATOM   486  C  CA  . THR A  1  66  ? 44.135  -9.475  40.705 1.00 24.79  ? 79  THR A CA  1 
ATOM   487  C  C   . THR A  1  66  ? 44.200  -10.885 40.098 1.00 25.41  ? 79  THR A C   1 
ATOM   488  O  O   . THR A  1  66  ? 43.341  -11.253 39.306 1.00 25.22  ? 79  THR A O   1 
ATOM   489  C  CB  . THR A  1  66  ? 44.833  -8.440  39.826 1.00 25.48  ? 79  THR A CB  1 
ATOM   490  O  OG1 . THR A  1  66  ? 46.217  -8.750  39.737 1.00 26.46  ? 79  THR A OG1 1 
ATOM   491  C  CG2 . THR A  1  66  ? 44.625  -7.023  40.349 1.00 27.60  ? 79  THR A CG2 1 
ATOM   492  N  N   . GLN A  1  67  ? 45.251  -11.642 40.416 1.00 27.65  ? 80  GLN A N   1 
ATOM   493  C  CA  . GLN A  1  67  ? 45.363  -13.039 39.989 1.00 26.97  ? 80  GLN A CA  1 
ATOM   494  C  C   . GLN A  1  67  ? 44.305  -13.914 40.660 1.00 27.75  ? 80  GLN A C   1 
ATOM   495  O  O   . GLN A  1  67  ? 43.585  -14.629 39.985 1.00 29.03  ? 80  GLN A O   1 
ATOM   496  C  CB  . GLN A  1  67  ? 46.777  -13.560 40.241 1.00 27.07  ? 80  GLN A CB  1 
ATOM   497  C  CG  . GLN A  1  67  ? 47.793  -12.820 39.384 1.00 28.45  ? 80  GLN A CG  1 
ATOM   498  C  CD  . GLN A  1  67  ? 49.232  -13.253 39.535 1.00 28.38  ? 80  GLN A CD  1 
ATOM   499  O  OE1 . GLN A  1  67  ? 50.046  -12.905 38.687 1.00 30.06  ? 80  GLN A OE1 1 
ATOM   500  N  NE2 . GLN A  1  67  ? 49.572  -14.001 40.573 1.00 30.15  ? 80  GLN A NE2 1 
ATOM   501  N  N   . GLU A  1  68  ? 44.177  -13.835 41.972 1.00 27.83  ? 81  GLU A N   1 
ATOM   502  C  CA  . GLU A  1  68  ? 43.271  -14.697 42.715 1.00 31.47  ? 81  GLU A CA  1 
ATOM   503  C  C   . GLU A  1  68  ? 41.818  -14.404 42.358 1.00 31.43  ? 81  GLU A C   1 
ATOM   504  O  O   . GLU A  1  68  ? 41.048  -15.332 42.143 1.00 29.36  ? 81  GLU A O   1 
ATOM   505  C  CB  . GLU A  1  68  ? 43.461  -14.576 44.228 1.00 32.66  ? 81  GLU A CB  1 
ATOM   506  C  CG  . GLU A  1  68  ? 44.806  -15.139 44.692 1.00 40.07  ? 81  GLU A CG  1 
ATOM   507  C  CD  . GLU A  1  68  ? 45.116  -16.590 44.322 1.00 49.38  ? 81  GLU A CD  1 
ATOM   508  O  OE1 . GLU A  1  68  ? 46.210  -16.940 43.772 1.00 48.86  ? 81  GLU A OE1 1 
ATOM   509  O  OE2 . GLU A  1  68  ? 44.184  -17.368 44.592 1.00 53.22  ? 81  GLU A OE2 1 
ATOM   510  N  N   . GLY A  1  69  ? 41.464  -13.116 42.253 1.00 28.70  ? 82  GLY A N   1 
ATOM   511  C  CA  . GLY A  1  69  ? 40.077  -12.708 42.121 1.00 25.57  ? 82  GLY A CA  1 
ATOM   512  C  C   . GLY A  1  69  ? 39.583  -12.755 40.681 1.00 26.47  ? 82  GLY A C   1 
ATOM   513  O  O   . GLY A  1  69  ? 38.404  -13.018 40.454 1.00 25.87  ? 82  GLY A O   1 
ATOM   514  N  N   . PHE A  1  70  ? 40.464  -12.452 39.710 1.00 25.97  ? 83  PHE A N   1 
ATOM   515  C  CA  . PHE A  1  70  ? 40.035  -12.333 38.329 1.00 26.71  ? 83  PHE A CA  1 
ATOM   516  C  C   . PHE A  1  70  ? 40.869  -13.154 37.349 1.00 25.55  ? 83  PHE A C   1 
ATOM   517  O  O   . PHE A  1  70  ? 40.584  -13.113 36.155 1.00 24.96  ? 83  PHE A O   1 
ATOM   518  C  CB  . PHE A  1  70  ? 40.114  -10.866 37.877 1.00 26.16  ? 83  PHE A CB  1 
ATOM   519  C  CG  . PHE A  1  70  ? 39.020  -9.986  38.450 1.00 27.31  ? 83  PHE A CG  1 
ATOM   520  C  CD1 . PHE A  1  70  ? 37.712  -10.080 37.972 1.00 28.77  ? 83  PHE A CD1 1 
ATOM   521  C  CD2 . PHE A  1  70  ? 39.292  -9.054  39.437 1.00 27.65  ? 83  PHE A CD2 1 
ATOM   522  C  CE1 . PHE A  1  70  ? 36.712  -9.277  38.484 1.00 27.68  ? 83  PHE A CE1 1 
ATOM   523  C  CE2 . PHE A  1  70  ? 38.289  -8.225  39.914 1.00 27.89  ? 83  PHE A CE2 1 
ATOM   524  C  CZ  . PHE A  1  70  ? 37.012  -8.346  39.449 1.00 26.45  ? 83  PHE A CZ  1 
ATOM   525  N  N   . ASN A  1  71  ? 41.941  -13.809 37.809 1.00 29.31  ? 84  ASN A N   1 
ATOM   526  C  CA  . ASN A  1  71  ? 42.878  -14.474 36.901 1.00 27.58  ? 84  ASN A CA  1 
ATOM   527  C  C   . ASN A  1  71  ? 43.524  -13.470 35.946 1.00 26.68  ? 84  ASN A C   1 
ATOM   528  O  O   . ASN A  1  71  ? 43.788  -13.781 34.786 1.00 27.10  ? 84  ASN A O   1 
ATOM   529  C  CB  . ASN A  1  71  ? 42.205  -15.614 36.137 1.00 29.40  ? 84  ASN A CB  1 
ATOM   530  C  CG  . ASN A  1  71  ? 43.076  -16.853 36.032 1.00 31.94  ? 84  ASN A CG  1 
ATOM   531  O  OD1 . ASN A  1  71  ? 44.275  -16.822 36.341 1.00 30.82  ? 84  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A  1  71  ? 42.475  -17.973 35.644 1.00 31.41  ? 84  ASN A ND2 1 
ATOM   533  N  N   . PHE A  1  72  ? 43.790  -12.243 36.430 1.00 25.63  ? 85  PHE A N   1 
ATOM   534  C  CA  . PHE A  1  72  ? 44.572  -11.297 35.647 1.00 24.34  ? 85  PHE A CA  1 
ATOM   535  C  C   . PHE A  1  72  ? 45.940  -11.925 35.375 1.00 24.61  ? 85  PHE A C   1 
ATOM   536  O  O   . PHE A  1  72  ? 46.568  -12.471 36.279 1.00 27.31  ? 85  PHE A O   1 
ATOM   537  C  CB  . PHE A  1  72  ? 44.690  -9.971  36.411 1.00 26.13  ? 85  PHE A CB  1 
ATOM   538  C  CG  . PHE A  1  72  ? 45.012  -8.748  35.565 1.00 27.80  ? 85  PHE A CG  1 
ATOM   539  C  CD1 . PHE A  1  72  ? 44.387  -8.544  34.344 1.00 31.72  ? 85  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A  1  72  ? 45.914  -7.790  36.010 1.00 29.52  ? 85  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A  1  72  ? 44.659  -7.408  33.596 1.00 33.68  ? 85  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A  1  72  ? 46.189  -6.659  35.259 1.00 29.65  ? 85  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A  1  72  ? 45.568  -6.473  34.049 1.00 29.50  ? 85  PHE A CZ  1 
ATOM   544  N  N   . GLU A  1  73  ? 46.401  -11.866 34.131 1.00 26.04  ? 86  GLU A N   1 
ATOM   545  C  CA  . GLU A  1  73  ? 47.659  -12.504 33.757 1.00 29.96  ? 86  GLU A CA  1 
ATOM   546  C  C   . GLU A  1  73  ? 48.831  -11.801 34.457 1.00 30.83  ? 86  GLU A C   1 
ATOM   547  O  O   . GLU A  1  73  ? 48.850  -10.578 34.593 1.00 28.16  ? 86  GLU A O   1 
ATOM   548  C  CB  . GLU A  1  73  ? 47.755  -12.510 32.236 1.00 36.17  ? 86  GLU A CB  1 
ATOM   549  C  CG  . GLU A  1  73  ? 48.930  -13.319 31.681 1.00 37.99  ? 86  GLU A CG  1 
ATOM   550  C  CD  . GLU A  1  73  ? 50.253  -12.575 31.650 1.00 42.12  ? 86  GLU A CD  1 
ATOM   551  O  OE1 . GLU A  1  73  ? 51.311  -13.204 31.967 1.00 42.34  ? 86  GLU A OE1 1 
ATOM   552  O  OE2 . GLU A  1  73  ? 50.220  -11.353 31.346 1.00 39.79  ? 86  GLU A OE2 1 
ATOM   553  N  N   . ASN A  1  74  ? 49.820  -12.596 34.870 1.00 27.64  ? 87  ASN A N   1 
ATOM   554  C  CA  . ASN A  1  74  ? 50.893  -12.172 35.759 1.00 29.64  ? 87  ASN A CA  1 
ATOM   555  C  C   . ASN A  1  74  ? 51.667  -10.965 35.223 1.00 29.68  ? 87  ASN A C   1 
ATOM   556  O  O   . ASN A  1  74  ? 51.882  -9.998  35.955 1.00 27.61  ? 87  ASN A O   1 
ATOM   557  C  CB  . ASN A  1  74  ? 51.826  -13.339 36.053 1.00 30.28  ? 87  ASN A CB  1 
ATOM   558  C  CG  . ASN A  1  74  ? 52.978  -12.986 36.958 1.00 30.40  ? 87  ASN A CG  1 
ATOM   559  O  OD1 . ASN A  1  74  ? 54.135  -13.053 36.531 1.00 31.61  ? 87  ASN A OD1 1 
ATOM   560  N  ND2 . ASN A  1  74  ? 52.696  -12.623 38.195 1.00 28.31  ? 87  ASN A ND2 1 
ATOM   561  N  N   . ASN A  1  75  ? 52.102  -11.000 33.961 1.00 30.73  ? 88  ASN A N   1 
ATOM   562  C  CA  A ASN A  1  75  ? 52.888  -9.896  33.429 0.50 30.26  ? 88  ASN A CA  1 
ATOM   563  C  CA  B ASN A  1  75  ? 52.879  -9.907  33.400 0.50 32.62  ? 88  ASN A CA  1 
ATOM   564  C  C   . ASN A  1  75  ? 52.034  -8.634  33.277 1.00 31.32  ? 88  ASN A C   1 
ATOM   565  O  O   . ASN A  1  75  ? 52.521  -7.533  33.523 1.00 32.23  ? 88  ASN A O   1 
ATOM   566  C  CB  A ASN A  1  75  ? 53.631  -10.277 32.157 0.50 31.75  ? 88  ASN A CB  1 
ATOM   567  C  CB  B ASN A  1  75  ? 53.441  -10.314 32.047 0.50 37.48  ? 88  ASN A CB  1 
ATOM   568  C  CG  A ASN A  1  75  ? 54.814  -11.169 32.466 0.50 30.12  ? 88  ASN A CG  1 
ATOM   569  C  CG  B ASN A  1  75  ? 54.850  -9.837  31.883 0.50 41.33  ? 88  ASN A CG  1 
ATOM   570  O  OD1 A ASN A  1  75  ? 54.874  -12.274 31.934 0.50 32.66  ? 88  ASN A OD1 1 
ATOM   571  O  OD1 B ASN A  1  75  ? 55.774  -10.353 32.528 0.50 44.16  ? 88  ASN A OD1 1 
ATOM   572  N  ND2 A ASN A  1  75  ? 55.739  -10.743 33.321 0.50 28.14  ? 88  ASN A ND2 1 
ATOM   573  N  ND2 B ASN A  1  75  ? 55.011  -8.856  31.016 0.50 46.43  ? 88  ASN A ND2 1 
ATOM   574  N  N   . ALA A  1  76  ? 50.768  -8.787  32.874 1.00 29.40  ? 89  ALA A N   1 
ATOM   575  C  CA  . ALA A  1  76  ? 49.862  -7.656  32.808 1.00 31.61  ? 89  ALA A CA  1 
ATOM   576  C  C   . ALA A  1  76  ? 49.689  -7.031  34.197 1.00 30.03  ? 89  ALA A C   1 
ATOM   577  O  O   . ALA A  1  76  ? 49.645  -5.806  34.324 1.00 30.62  ? 89  ALA A O   1 
ATOM   578  C  CB  . ALA A  1  76  ? 48.522  -8.080  32.218 1.00 33.10  ? 89  ALA A CB  1 
ATOM   579  N  N   . ALA A  1  77  ? 49.594  -7.870  35.232 1.00 28.33  ? 90  ALA A N   1 
ATOM   580  C  CA  . ALA A  1  77  ? 49.480  -7.408  36.605 1.00 26.71  ? 90  ALA A CA  1 
ATOM   581  C  C   . ALA A  1  77  ? 50.734  -6.636  37.029 1.00 27.04  ? 90  ALA A C   1 
ATOM   582  O  O   . ALA A  1  77  ? 50.619  -5.573  37.656 1.00 28.66  ? 90  ALA A O   1 
ATOM   583  C  CB  . ALA A  1  77  ? 49.217  -8.567  37.545 1.00 25.32  ? 90  ALA A CB  1 
ATOM   584  N  N   . ILE A  1  78  ? 51.912  -7.156  36.669 1.00 26.34  ? 91  ILE A N   1 
ATOM   585  C  CA  . ILE A  1  78  ? 53.172  -6.519  37.014 1.00 28.75  ? 91  ILE A CA  1 
ATOM   586  C  C   . ILE A  1  78  ? 53.280  -5.157  36.317 1.00 28.54  ? 91  ILE A C   1 
ATOM   587  O  O   . ILE A  1  78  ? 53.607  -4.156  36.956 1.00 27.94  ? 91  ILE A O   1 
ATOM   588  C  CB  . ILE A  1  78  ? 54.352  -7.467  36.719 1.00 27.77  ? 91  ILE A CB  1 
ATOM   589  C  CG1 . ILE A  1  78  ? 54.349  -8.619  37.717 1.00 27.69  ? 91  ILE A CG1 1 
ATOM   590  C  CG2 . ILE A  1  78  ? 55.698  -6.727  36.741 1.00 27.53  ? 91  ILE A CG2 1 
ATOM   591  C  CD1 . ILE A  1  78  ? 55.288  -9.752  37.350 1.00 30.68  ? 91  ILE A CD1 1 
ATOM   592  N  N   . VAL A  1  79  ? 52.943  -5.109  35.024 1.00 29.17  ? 92  VAL A N   1 
ATOM   593  C  CA  . VAL A  1  79  ? 53.033  -3.867  34.267 1.00 31.33  ? 92  VAL A CA  1 
ATOM   594  C  C   . VAL A  1  79  ? 52.113  -2.794  34.857 1.00 31.04  ? 92  VAL A C   1 
ATOM   595  O  O   . VAL A  1  79  ? 52.546  -1.656  35.055 1.00 32.30  ? 92  VAL A O   1 
ATOM   596  C  CB  . VAL A  1  79  ? 52.749  -4.077  32.774 1.00 34.42  ? 92  VAL A CB  1 
ATOM   597  C  CG1 . VAL A  1  79  ? 52.588  -2.746  32.045 1.00 35.21  ? 92  VAL A CG1 1 
ATOM   598  C  CG2 . VAL A  1  79  ? 53.838  -4.916  32.110 1.00 35.55  ? 92  VAL A CG2 1 
ATOM   599  N  N   . ALA A  1  80  ? 50.846  -3.139  35.128 1.00 28.66  ? 93  ALA A N   1 
ATOM   600  C  CA  . ALA A  1  80  ? 49.904  -2.172  35.674 1.00 25.86  ? 93  ALA A CA  1 
ATOM   601  C  C   . ALA A  1  80  ? 50.290  -1.758  37.091 1.00 27.02  ? 93  ALA A C   1 
ATOM   602  O  O   . ALA A  1  80  ? 50.219  -0.568  37.430 1.00 25.45  ? 93  ALA A O   1 
ATOM   603  C  CB  . ALA A  1  80  ? 48.492  -2.698  35.646 1.00 28.16  ? 93  ALA A CB  1 
ATOM   604  N  N   . THR A  1  81  ? 50.704  -2.715  37.927 1.00 26.09  ? 94  THR A N   1 
ATOM   605  C  CA  . THR A  1  81  ? 50.838  -2.440  39.349 1.00 26.99  ? 94  THR A CA  1 
ATOM   606  C  C   . THR A  1  81  ? 52.032  -1.523  39.617 1.00 27.40  ? 94  THR A C   1 
ATOM   607  O  O   . THR A  1  81  ? 51.919  -0.573  40.381 1.00 29.04  ? 94  THR A O   1 
ATOM   608  C  CB  . THR A  1  81  ? 50.956  -3.736  40.152 1.00 28.74  ? 94  THR A CB  1 
ATOM   609  O  OG1 . THR A  1  81  ? 49.731  -4.454  40.011 1.00 30.15  ? 94  THR A OG1 1 
ATOM   610  C  CG2 . THR A  1  81  ? 51.199  -3.473  41.629 1.00 28.34  ? 94  THR A CG2 1 
ATOM   611  N  N   . TYR A  1  82  ? 53.192  -1.828  39.035 1.00 27.34  ? 95  TYR A N   1 
ATOM   612  C  CA  . TYR A  1  82  ? 54.385  -1.044  39.318 1.00 30.48  ? 95  TYR A CA  1 
ATOM   613  C  C   . TYR A  1  82  ? 54.336  0.301   38.577 1.00 28.80  ? 95  TYR A C   1 
ATOM   614  O  O   . TYR A  1  82  ? 54.921  1.265   39.052 1.00 32.43  ? 95  TYR A O   1 
ATOM   615  C  CB  . TYR A  1  82  ? 55.658  -1.854  39.056 1.00 28.31  ? 95  TYR A CB  1 
ATOM   616  C  CG  . TYR A  1  82  ? 55.830  -2.973  40.075 1.00 29.96  ? 95  TYR A CG  1 
ATOM   617  C  CD1 . TYR A  1  82  ? 56.286  -2.719  41.363 1.00 29.78  ? 95  TYR A CD1 1 
ATOM   618  C  CD2 . TYR A  1  82  ? 55.516  -4.290  39.750 1.00 29.92  ? 95  TYR A CD2 1 
ATOM   619  C  CE1 . TYR A  1  82  ? 56.424  -3.735  42.298 1.00 27.93  ? 95  TYR A CE1 1 
ATOM   620  C  CE2 . TYR A  1  82  ? 55.619  -5.307  40.685 1.00 32.02  ? 95  TYR A CE2 1 
ATOM   621  C  CZ  . TYR A  1  82  ? 56.080  -5.035  41.956 1.00 30.33  ? 95  TYR A CZ  1 
ATOM   622  O  OH  . TYR A  1  82  ? 56.204  -6.042  42.865 1.00 32.54  ? 95  TYR A OH  1 
ATOM   623  N  N   . LEU A  1  83  ? 53.588  0.388   37.471 1.00 29.71  ? 96  LEU A N   1 
ATOM   624  C  CA  . LEU A  1  83  ? 53.324  1.678   36.840 1.00 30.75  ? 96  LEU A CA  1 
ATOM   625  C  C   . LEU A  1  83  ? 52.589  2.564   37.846 1.00 31.58  ? 96  LEU A C   1 
ATOM   626  O  O   . LEU A  1  83  ? 52.986  3.695   38.111 1.00 30.57  ? 96  LEU A O   1 
ATOM   627  C  CB  . LEU A  1  83  ? 52.533  1.488   35.548 1.00 30.30  ? 96  LEU A CB  1 
ATOM   628  C  CG  . LEU A  1  83  ? 51.974  2.756   34.883 1.00 33.77  ? 96  LEU A CG  1 
ATOM   629  C  CD1 . LEU A  1  83  ? 53.076  3.715   34.475 1.00 33.65  ? 96  LEU A CD1 1 
ATOM   630  C  CD2 . LEU A  1  83  ? 51.117  2.394   33.672 1.00 37.11  ? 96  LEU A CD2 1 
ATOM   631  N  N   . GLY A  1  84  ? 51.508  2.020   38.413 1.00 31.62  ? 97  GLY A N   1 
ATOM   632  C  CA  . GLY A  1  84  ? 50.717  2.744   39.385 1.00 29.70  ? 97  GLY A CA  1 
ATOM   633  C  C   . GLY A  1  84  ? 51.543  3.098   40.619 1.00 29.70  ? 97  GLY A C   1 
ATOM   634  O  O   . GLY A  1  84  ? 51.431  4.202   41.156 1.00 29.33  ? 97  GLY A O   1 
ATOM   635  N  N   . HIS A  1  85  ? 52.363  2.159   41.087 1.00 27.82  ? 98  HIS A N   1 
ATOM   636  C  CA  . HIS A  1  85  ? 53.132  2.366   42.306 1.00 28.26  ? 98  HIS A CA  1 
ATOM   637  C  C   . HIS A  1  85  ? 54.250  3.402   42.101 1.00 26.97  ? 98  HIS A C   1 
ATOM   638  O  O   . HIS A  1  85  ? 54.415  4.297   42.923 1.00 28.64  ? 98  HIS A O   1 
ATOM   639  C  CB  . HIS A  1  85  ? 53.708  1.032   42.792 1.00 28.99  ? 98  HIS A CB  1 
ATOM   640  C  CG  . HIS A  1  85  ? 54.342  1.119   44.123 1.00 28.25  ? 98  HIS A CG  1 
ATOM   641  N  ND1 . HIS A  1  85  ? 53.691  1.635   45.219 1.00 27.30  ? 98  HIS A ND1 1 
ATOM   642  C  CD2 . HIS A  1  85  ? 55.553  0.732   44.543 1.00 27.89  ? 98  HIS A CD2 1 
ATOM   643  C  CE1 . HIS A  1  85  ? 54.497  1.561   46.269 1.00 28.71  ? 98  HIS A CE1 1 
ATOM   644  N  NE2 . HIS A  1  85  ? 55.640  1.021   45.886 1.00 27.44  ? 98  HIS A NE2 1 
ATOM   645  N  N   . LEU A  1  86  ? 55.017  3.292   41.018 1.00 27.56  ? 99  LEU A N   1 
ATOM   646  C  CA  . LEU A  1  86  ? 56.106  4.229   40.742 1.00 28.66  ? 99  LEU A CA  1 
ATOM   647  C  C   . LEU A  1  86  ? 55.595  5.677   40.714 1.00 30.37  ? 99  LEU A C   1 
ATOM   648  O  O   . LEU A  1  86  ? 56.194  6.556   41.331 1.00 30.03  ? 99  LEU A O   1 
ATOM   649  C  CB  . LEU A  1  86  ? 56.810  3.861   39.441 1.00 28.84  ? 99  LEU A CB  1 
ATOM   650  C  CG  . LEU A  1  86  ? 57.748  2.650   39.532 1.00 31.02  ? 99  LEU A CG  1 
ATOM   651  C  CD1 . LEU A  1  86  ? 58.116  2.077   38.190 1.00 30.69  ? 99  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A  1  86  ? 59.018  3.023   40.278 1.00 31.58  ? 99  LEU A CD2 1 
ATOM   653  N  N   . LEU A  1  87  ? 54.457  5.897   40.045 1.00 28.38  ? 100 LEU A N   1 
ATOM   654  C  CA  . LEU A  1  87  ? 53.921  7.233   39.833 1.00 28.43  ? 100 LEU A CA  1 
ATOM   655  C  C   . LEU A  1  87  ? 53.097  7.710   41.021 1.00 29.95  ? 100 LEU A C   1 
ATOM   656  O  O   . LEU A  1  87  ? 53.084  8.906   41.307 1.00 30.94  ? 100 LEU A O   1 
ATOM   657  C  CB  . LEU A  1  87  ? 53.075  7.238   38.562 1.00 29.52  ? 100 LEU A CB  1 
ATOM   658  C  CG  . LEU A  1  87  ? 53.804  6.949   37.253 1.00 31.86  ? 100 LEU A CG  1 
ATOM   659  C  CD1 . LEU A  1  87  ? 52.814  6.845   36.119 1.00 34.04  ? 100 LEU A CD1 1 
ATOM   660  C  CD2 . LEU A  1  87  ? 54.825  8.024   36.941 1.00 34.05  ? 100 LEU A CD2 1 
ATOM   661  N  N   . ASN A  1  88  ? 52.395  6.793   41.709 1.00 27.97  ? 101 ASN A N   1 
ATOM   662  C  CA  . ASN A  1  88  ? 51.324  7.186   42.611 1.00 26.62  ? 101 ASN A CA  1 
ATOM   663  C  C   . ASN A  1  88  ? 51.412  6.567   43.998 1.00 25.16  ? 101 ASN A C   1 
ATOM   664  O  O   . ASN A  1  88  ? 50.600  6.910   44.851 1.00 26.31  ? 101 ASN A O   1 
ATOM   665  C  CB  . ASN A  1  88  ? 49.941  6.845   42.077 1.00 27.22  ? 101 ASN A CB  1 
ATOM   666  C  CG  . ASN A  1  88  ? 49.657  7.511   40.755 1.00 29.12  ? 101 ASN A CG  1 
ATOM   667  O  OD1 . ASN A  1  88  ? 49.941  8.703   40.563 1.00 32.08  ? 101 ASN A OD1 1 
ATOM   668  N  ND2 . ASN A  1  88  ? 49.086  6.762   39.827 1.00 34.60  ? 101 ASN A ND2 1 
ATOM   669  N  N   . GLY A  1  89  ? 52.404  5.701   44.239 1.00 25.50  ? 102 GLY A N   1 
ATOM   670  C  CA  . GLY A  1  89  ? 52.517  5.071   45.542 1.00 26.33  ? 102 GLY A CA  1 
ATOM   671  C  C   . GLY A  1  89  ? 53.668  5.635   46.372 1.00 28.37  ? 102 GLY A C   1 
ATOM   672  O  O   . GLY A  1  89  ? 54.476  6.427   45.891 1.00 29.19  ? 102 GLY A O   1 
ATOM   673  N  N   . ASN A  1  90  ? 53.736  5.157   47.612 1.00 25.24  ? 103 ASN A N   1 
ATOM   674  C  CA  . ASN A  1  90  ? 54.809  5.482   48.527 1.00 26.29  ? 103 ASN A CA  1 
ATOM   675  C  C   . ASN A  1  90  ? 55.860  4.376   48.478 1.00 28.76  ? 103 ASN A C   1 
ATOM   676  O  O   . ASN A  1  90  ? 55.636  3.275   48.977 1.00 28.92  ? 103 ASN A O   1 
ATOM   677  C  CB  . ASN A  1  90  ? 54.255  5.679   49.922 1.00 25.81  ? 103 ASN A CB  1 
ATOM   678  C  CG  . ASN A  1  90  ? 55.276  6.270   50.860 1.00 29.58  ? 103 ASN A CG  1 
ATOM   679  O  OD1 . ASN A  1  90  ? 56.420  5.812   50.902 1.00 27.19  ? 103 ASN A OD1 1 
ATOM   680  N  ND2 . ASN A  1  90  ? 54.889  7.313   51.583 1.00 30.50  ? 103 ASN A ND2 1 
ATOM   681  N  N   . LEU A  1  91  ? 57.009  4.692   47.889 1.00 29.10  ? 104 LEU A N   1 
ATOM   682  C  CA  . LEU A  1  91  ? 58.044  3.705   47.624 1.00 31.82  ? 104 LEU A CA  1 
ATOM   683  C  C   . LEU A  1  91  ? 58.777  3.286   48.895 1.00 31.72  ? 104 LEU A C   1 
ATOM   684  O  O   . LEU A  1  91  ? 59.334  2.195   48.939 1.00 30.28  ? 104 LEU A O   1 
ATOM   685  C  CB  . LEU A  1  91  ? 58.983  4.304   46.583 1.00 35.65  ? 104 LEU A CB  1 
ATOM   686  C  CG  . LEU A  1  91  ? 58.307  4.602   45.243 1.00 43.84  ? 104 LEU A CG  1 
ATOM   687  C  CD1 . LEU A  1  91  ? 59.264  5.307   44.353 1.00 47.95  ? 104 LEU A CD1 1 
ATOM   688  C  CD2 . LEU A  1  91  ? 57.842  3.350   44.560 1.00 50.45  ? 104 LEU A CD2 1 
ATOM   689  N  N   . VAL A  1  92  ? 58.738  4.129   49.933 1.00 30.47  ? 105 VAL A N   1 
ATOM   690  C  CA  . VAL A  1  92  ? 59.429  3.834   51.172 1.00 30.54  ? 105 VAL A CA  1 
ATOM   691  C  C   . VAL A  1  92  ? 58.601  2.894   52.037 1.00 31.73  ? 105 VAL A C   1 
ATOM   692  O  O   . VAL A  1  92  ? 59.147  1.953   52.597 1.00 31.74  ? 105 VAL A O   1 
ATOM   693  C  CB  . VAL A  1  92  ? 59.797  5.132   51.913 1.00 30.44  ? 105 VAL A CB  1 
ATOM   694  C  CG1 . VAL A  1  92  ? 60.368  4.853   53.299 1.00 33.67  ? 105 VAL A CG1 1 
ATOM   695  C  CG2 . VAL A  1  92  ? 60.807  5.930   51.102 1.00 32.36  ? 105 VAL A CG2 1 
ATOM   696  N  N   . THR A  1  93  ? 57.287  3.150   52.154 1.00 30.68  ? 106 THR A N   1 
ATOM   697  C  CA  . THR A  1  93  ? 56.424  2.283   52.938 1.00 30.23  ? 106 THR A CA  1 
ATOM   698  C  C   . THR A  1  93  ? 55.913  1.105   52.100 1.00 30.63  ? 106 THR A C   1 
ATOM   699  O  O   . THR A  1  93  ? 55.312  0.206   52.656 1.00 32.33  ? 106 THR A O   1 
ATOM   700  C  CB  . THR A  1  93  ? 55.261  3.068   53.530 1.00 33.20  ? 106 THR A CB  1 
ATOM   701  O  OG1 . THR A  1  93  ? 54.512  3.505   52.398 1.00 31.23  ? 106 THR A OG1 1 
ATOM   702  C  CG2 . THR A  1  93  ? 55.724  4.209   54.424 1.00 34.20  ? 106 THR A CG2 1 
ATOM   703  N  N   . ASP A  1  94  ? 56.108  1.149   50.774 1.00 28.64  ? 107 ASP A N   1 
ATOM   704  C  CA  . ASP A  1  94  ? 55.648  0.135   49.835 1.00 30.96  ? 107 ASP A CA  1 
ATOM   705  C  C   . ASP A  1  94  ? 54.121  0.030   49.824 1.00 29.35  ? 107 ASP A C   1 
ATOM   706  O  O   . ASP A  1  94  ? 53.589  -1.075  49.748 1.00 27.80  ? 107 ASP A O   1 
ATOM   707  C  CB  . ASP A  1  94  ? 56.304  -1.215  50.111 1.00 31.42  ? 107 ASP A CB  1 
ATOM   708  C  CG  . ASP A  1  94  ? 56.313  -2.204  48.948 1.00 33.41  ? 107 ASP A CG  1 
ATOM   709  O  OD1 . ASP A  1  94  ? 56.566  -1.769  47.800 1.00 31.72  ? 107 ASP A OD1 1 
ATOM   710  O  OD2 . ASP A  1  94  ? 56.089  -3.421  49.192 1.00 34.88  ? 107 ASP A OD2 1 
ATOM   711  N  N   . LEU A  1  95  ? 53.418  1.171   49.919 1.00 29.01  ? 108 LEU A N   1 
ATOM   712  C  CA  . LEU A  1  95  ? 51.963  1.184   49.939 1.00 29.18  ? 108 LEU A CA  1 
ATOM   713  C  C   . LEU A  1  95  ? 51.419  2.081   48.831 1.00 29.16  ? 108 LEU A C   1 
ATOM   714  O  O   . LEU A  1  95  ? 51.947  3.155   48.582 1.00 31.62  ? 108 LEU A O   1 
ATOM   715  C  CB  . LEU A  1  95  ? 51.476  1.635   51.312 1.00 29.13  ? 108 LEU A CB  1 
ATOM   716  C  CG  . LEU A  1  95  ? 51.791  0.709   52.483 1.00 31.39  ? 108 LEU A CG  1 
ATOM   717  C  CD1 . LEU A  1  95  ? 51.495  1.442   53.798 1.00 33.13  ? 108 LEU A CD1 1 
ATOM   718  C  CD2 . LEU A  1  95  ? 51.028  -0.609  52.422 1.00 32.44  ? 108 LEU A CD2 1 
ATOM   719  N  N   . LEU A  1  96  ? 50.330  1.632   48.197 1.00 28.69  ? 109 LEU A N   1 
ATOM   720  C  CA  . LEU A  1  96  ? 49.654  2.355   47.136 1.00 26.83  ? 109 LEU A CA  1 
ATOM   721  C  C   . LEU A  1  96  ? 48.169  2.467   47.466 1.00 28.87  ? 109 LEU A C   1 
ATOM   722  O  O   . LEU A  1  96  ? 47.512  1.460   47.765 1.00 25.38  ? 109 LEU A O   1 
ATOM   723  C  CB  . LEU A  1  96  ? 49.876  1.639   45.812 1.00 28.32  ? 109 LEU A CB  1 
ATOM   724  C  CG  . LEU A  1  96  ? 49.017  2.103   44.632 1.00 28.75  ? 109 LEU A CG  1 
ATOM   725  C  CD1 . LEU A  1  96  ? 49.295  3.556   44.247 1.00 28.68  ? 109 LEU A CD1 1 
ATOM   726  C  CD2 . LEU A  1  96  ? 49.258  1.213   43.441 1.00 29.71  ? 109 LEU A CD2 1 
ATOM   727  N  N   . SER A  1  97  ? 47.651  3.706   47.413 1.00 28.20  ? 110 SER A N   1 
ATOM   728  C  CA  . SER A  1  97  ? 46.219  3.948   47.489 1.00 28.26  ? 110 SER A CA  1 
ATOM   729  C  C   . SER A  1  97  ? 45.568  3.649   46.144 1.00 25.69  ? 110 SER A C   1 
ATOM   730  O  O   . SER A  1  97  ? 46.022  4.158   45.131 1.00 25.69  ? 110 SER A O   1 
ATOM   731  C  CB  . SER A  1  97  ? 45.933  5.361   47.930 1.00 29.39  ? 110 SER A CB  1 
ATOM   732  O  OG  . SER A  1  97  ? 44.570  5.718   47.711 1.00 27.52  ? 110 SER A OG  1 
ATOM   733  N  N   . ILE A  1  98  ? 44.454  2.901   46.139 1.00 24.01  ? 111 ILE A N   1 
ATOM   734  C  CA  . ILE A  1  98  ? 43.769  2.618   44.882 1.00 24.73  ? 111 ILE A CA  1 
ATOM   735  C  C   . ILE A  1  98  ? 42.857  3.788   44.504 1.00 27.06  ? 111 ILE A C   1 
ATOM   736  O  O   . ILE A  1  98  ? 42.164  3.719   43.488 1.00 28.00  ? 111 ILE A O   1 
ATOM   737  C  CB  . ILE A  1  98  ? 42.983  1.298   44.931 1.00 25.39  ? 111 ILE A CB  1 
ATOM   738  C  CG1 . ILE A  1  98  ? 41.758  1.364   45.872 1.00 25.82  ? 111 ILE A CG1 1 
ATOM   739  C  CG2 . ILE A  1  98  ? 43.909  0.146   45.298 1.00 25.88  ? 111 ILE A CG2 1 
ATOM   740  C  CD1 . ILE A  1  98  ? 40.891  0.117   45.838 1.00 27.21  ? 111 ILE A CD1 1 
ATOM   741  N  N   . GLY A  1  99  ? 42.810  4.814   45.356 1.00 27.44  ? 112 GLY A N   1 
ATOM   742  C  CA  . GLY A  1  99  ? 42.045  6.015   45.075 1.00 30.67  ? 112 GLY A CA  1 
ATOM   743  C  C   . GLY A  1  99  ? 42.862  7.274   45.318 1.00 28.22  ? 112 GLY A C   1 
ATOM   744  O  O   . GLY A  1  99  ? 43.839  7.493   44.617 1.00 27.97  ? 112 GLY A O   1 
ATOM   745  N  N   . GLY A  1  100 ? 42.431  8.080   46.290 1.00 32.69  ? 113 GLY A N   1 
ATOM   746  C  CA  . GLY A  1  100 ? 43.013  9.390   46.536 1.00 34.77  ? 113 GLY A CA  1 
ATOM   747  C  C   . GLY A  1  100 ? 43.985  9.372   47.707 1.00 36.87  ? 113 GLY A C   1 
ATOM   748  O  O   . GLY A  1  100 ? 44.402  8.316   48.188 1.00 29.90  ? 113 GLY A O   1 
ATOM   749  N  N   . ALA A  1  101 ? 44.333  10.578  48.174 1.00 38.73  ? 114 ALA A N   1 
ATOM   750  C  CA  . ALA A  1  101 ? 45.348  10.744  49.200 1.00 35.11  ? 114 ALA A CA  1 
ATOM   751  C  C   . ALA A  1  101 ? 44.827  10.220  50.529 1.00 31.10  ? 114 ALA A C   1 
ATOM   752  O  O   . ALA A  1  101 ? 43.656  10.335  50.835 1.00 32.34  ? 114 ALA A O   1 
ATOM   753  C  CB  . ALA A  1  101 ? 45.737  12.217  49.293 1.00 41.90  ? 114 ALA A CB  1 
ATOM   754  N  N   . THR A  1  102 ? 45.716  9.650   51.328 1.00 30.06  ? 115 THR A N   1 
ATOM   755  C  CA  . THR A  1  102 ? 45.315  9.093   52.599 1.00 31.24  ? 115 THR A CA  1 
ATOM   756  C  C   . THR A  1  102 ? 46.559  9.013   53.471 1.00 32.71  ? 115 THR A C   1 
ATOM   757  O  O   . THR A  1  102 ? 47.631  8.671   52.980 1.00 34.29  ? 115 THR A O   1 
ATOM   758  C  CB  . THR A  1  102 ? 44.690  7.709   52.409 1.00 32.92  ? 115 THR A CB  1 
ATOM   759  O  OG1 . THR A  1  102 ? 44.476  7.200   53.728 1.00 31.84  ? 115 THR A OG1 1 
ATOM   760  C  CG2 . THR A  1  102 ? 45.579  6.769   51.609 1.00 31.57  ? 115 THR A CG2 1 
ATOM   761  N  N   . PRO A  1  103 ? 46.436  9.305   54.780 1.00 36.16  ? 116 PRO A N   1 
ATOM   762  C  CA  . PRO A  1  103 ? 47.547  9.091   55.715 1.00 37.95  ? 116 PRO A CA  1 
ATOM   763  C  C   . PRO A  1  103 ? 47.967  7.622   55.808 1.00 35.71  ? 116 PRO A C   1 
ATOM   764  O  O   . PRO A  1  103 ? 49.068  7.329   56.269 1.00 33.49  ? 116 PRO A O   1 
ATOM   765  C  CB  . PRO A  1  103 ? 47.003  9.623   57.071 1.00 40.37  ? 116 PRO A CB  1 
ATOM   766  C  CG  . PRO A  1  103 ? 45.484  9.675   56.908 1.00 39.60  ? 116 PRO A CG  1 
ATOM   767  C  CD  . PRO A  1  103 ? 45.225  9.850   55.424 1.00 37.48  ? 116 PRO A CD  1 
ATOM   768  N  N   . LYS A  1  104 ? 47.089  6.703   55.362 1.00 30.99  ? 117 LYS A N   1 
ATOM   769  C  CA  . LYS A  1  104 ? 47.364  5.278   55.456 1.00 32.20  ? 117 LYS A CA  1 
ATOM   770  C  C   . LYS A  1  104 ? 48.590  4.867   54.637 1.00 29.73  ? 117 LYS A C   1 
ATOM   771  O  O   . LYS A  1  104 ? 49.116  3.790   54.876 1.00 31.93  ? 117 LYS A O   1 
ATOM   772  C  CB  . LYS A  1  104 ? 46.145  4.456   55.024 1.00 33.58  ? 117 LYS A CB  1 
ATOM   773  C  CG  . LYS A  1  104 ? 44.989  4.485   56.021 1.00 35.48  ? 117 LYS A CG  1 
ATOM   774  C  CD  . LYS A  1  104 ? 43.653  4.100   55.394 1.00 40.86  ? 117 LYS A CD  1 
ATOM   775  C  CE  . LYS A  1  104 ? 42.526  4.072   56.377 1.00 43.99  ? 117 LYS A CE  1 
ATOM   776  N  NZ  . LYS A  1  104 ? 42.700  2.973   57.327 1.00 47.80  ? 117 LYS A NZ  1 
ATOM   777  N  N   . THR A  1  105 ? 49.032  5.673   53.659 1.00 29.11  ? 118 THR A N   1 
ATOM   778  C  CA  . THR A  1  105 ? 50.222  5.300   52.890 1.00 33.37  ? 118 THR A CA  1 
ATOM   779  C  C   . THR A  1  105 ? 51.500  5.703   53.630 1.00 34.19  ? 118 THR A C   1 
ATOM   780  O  O   . THR A  1  105 ? 52.584  5.374   53.170 1.00 30.80  ? 118 THR A O   1 
ATOM   781  C  CB  . THR A  1  105 ? 50.193  5.874   51.473 1.00 33.28  ? 118 THR A CB  1 
ATOM   782  O  OG1 . THR A  1  105 ? 49.994  7.289   51.495 1.00 29.00  ? 118 THR A OG1 1 
ATOM   783  C  CG2 . THR A  1  105 ? 49.094  5.246   50.632 1.00 32.57  ? 118 THR A CG2 1 
ATOM   784  N  N   . GLY A  1  106 ? 51.362  6.428   54.754 1.00 36.00  ? 119 GLY A N   1 
ATOM   785  C  CA  . GLY A  1  106 ? 52.497  6.780   55.589 1.00 33.76  ? 119 GLY A CA  1 
ATOM   786  C  C   . GLY A  1  106 ? 53.041  8.184   55.289 1.00 35.65  ? 119 GLY A C   1 
ATOM   787  O  O   . GLY A  1  106 ? 52.465  8.935   54.504 1.00 31.76  ? 119 GLY A O   1 
ATOM   788  N  N   . PRO A  1  107 ? 54.202  8.548   55.884 1.00 38.37  ? 120 PRO A N   1 
ATOM   789  C  CA  . PRO A  1  107 ? 54.817  9.864   55.690 1.00 40.46  ? 120 PRO A CA  1 
ATOM   790  C  C   . PRO A  1  107 ? 54.999  10.232  54.221 1.00 38.53  ? 120 PRO A C   1 
ATOM   791  O  O   . PRO A  1  107 ? 55.507  9.441   53.447 1.00 41.25  ? 120 PRO A O   1 
ATOM   792  C  CB  . PRO A  1  107 ? 56.187  9.738   56.390 1.00 42.54  ? 120 PRO A CB  1 
ATOM   793  C  CG  . PRO A  1  107 ? 55.995  8.636   57.413 1.00 42.06  ? 120 PRO A CG  1 
ATOM   794  C  CD  . PRO A  1  107 ? 54.973  7.696   56.809 1.00 40.83  ? 120 PRO A CD  1 
ATOM   795  N  N   . PRO A  1  108 ? 54.602  11.443  53.794 1.00 41.53  ? 121 PRO A N   1 
ATOM   796  C  CA  . PRO A  1  108 ? 54.674  11.819  52.385 1.00 40.13  ? 121 PRO A CA  1 
ATOM   797  C  C   . PRO A  1  108 ? 56.094  11.795  51.833 1.00 36.84  ? 121 PRO A C   1 
ATOM   798  O  O   . PRO A  1  108 ? 57.061  12.023  52.546 1.00 36.07  ? 121 PRO A O   1 
ATOM   799  C  CB  . PRO A  1  108 ? 54.029  13.217  52.300 1.00 44.22  ? 121 PRO A CB  1 
ATOM   800  C  CG  . PRO A  1  108 ? 53.931  13.706  53.734 1.00 51.11  ? 121 PRO A CG  1 
ATOM   801  C  CD  . PRO A  1  108 ? 53.990  12.487  54.634 1.00 47.56  ? 121 PRO A CD  1 
ATOM   802  N  N   . PRO A  1  109 ? 56.262  11.451  50.537 1.00 35.09  ? 122 PRO A N   1 
ATOM   803  C  CA  . PRO A  1  109 ? 57.559  11.539  49.882 1.00 37.07  ? 122 PRO A CA  1 
ATOM   804  C  C   . PRO A  1  109 ? 57.942  13.000  49.647 1.00 38.31  ? 122 PRO A C   1 
ATOM   805  O  O   . PRO A  1  109 ? 57.094  13.878  49.742 1.00 35.66  ? 122 PRO A O   1 
ATOM   806  C  CB  . PRO A  1  109 ? 57.310  10.801  48.558 1.00 37.04  ? 122 PRO A CB  1 
ATOM   807  C  CG  . PRO A  1  109 ? 55.871  11.013  48.275 1.00 37.82  ? 122 PRO A CG  1 
ATOM   808  C  CD  . PRO A  1  109 ? 55.184  11.019  49.624 1.00 37.55  ? 122 PRO A CD  1 
ATOM   809  N  N   . PRO A  1  110 ? 59.213  13.302  49.318 1.00 42.27  ? 123 PRO A N   1 
ATOM   810  C  CA  . PRO A  1  110 ? 59.595  14.660  48.910 1.00 42.28  ? 123 PRO A CA  1 
ATOM   811  C  C   . PRO A  1  110 ? 58.923  15.106  47.611 1.00 37.12  ? 123 PRO A C   1 
ATOM   812  O  O   . PRO A  1  110 ? 58.950  14.388  46.608 1.00 37.61  ? 123 PRO A O   1 
ATOM   813  C  CB  . PRO A  1  110 ? 61.130  14.614  48.776 1.00 42.90  ? 123 PRO A CB  1 
ATOM   814  C  CG  . PRO A  1  110 ? 61.466  13.141  48.702 1.00 44.81  ? 123 PRO A CG  1 
ATOM   815  C  CD  . PRO A  1  110 ? 60.343  12.358  49.344 1.00 43.41  ? 123 PRO A CD  1 
ATOM   816  N  N   . PRO A  1  111 ? 58.297  16.300  47.571 1.00 39.06  ? 124 PRO A N   1 
ATOM   817  C  CA  . PRO A  1  111 ? 57.707  16.796  46.333 1.00 38.98  ? 124 PRO A CA  1 
ATOM   818  C  C   . PRO A  1  111 ? 58.804  16.917  45.280 1.00 36.60  ? 124 PRO A C   1 
ATOM   819  O  O   . PRO A  1  111 ? 59.977  17.044  45.610 1.00 36.86  ? 124 PRO A O   1 
ATOM   820  C  CB  . PRO A  1  111 ? 57.027  18.136  46.687 1.00 40.26  ? 124 PRO A CB  1 
ATOM   821  C  CG  . PRO A  1  111 ? 57.315  18.376  48.138 1.00 41.76  ? 124 PRO A CG  1 
ATOM   822  C  CD  . PRO A  1  111 ? 58.082  17.199  48.711 1.00 40.31  ? 124 PRO A CD  1 
ATOM   823  N  N   . PRO A  1  112 ? 58.481  16.849  43.973 1.00 36.51  ? 125 PRO A N   1 
ATOM   824  C  CA  . PRO A  1  112 ? 57.092  16.779  43.491 1.00 37.76  ? 125 PRO A CA  1 
ATOM   825  C  C   . PRO A  1  112 ? 56.394  15.416  43.511 1.00 36.78  ? 125 PRO A C   1 
ATOM   826  O  O   . PRO A  1  112 ? 55.232  15.319  43.113 1.00 36.02  ? 125 PRO A O   1 
ATOM   827  C  CB  . PRO A  1  112 ? 57.215  17.327  42.063 1.00 38.43  ? 125 PRO A CB  1 
ATOM   828  C  CG  . PRO A  1  112 ? 58.612  16.970  41.654 1.00 40.52  ? 125 PRO A CG  1 
ATOM   829  C  CD  . PRO A  1  112 ? 59.478  16.880  42.900 1.00 38.91  ? 125 PRO A CD  1 
ATOM   830  N  N   . ALA A  1  113 ? 57.065  14.381  44.035 1.00 32.36  ? 126 ALA A N   1 
ATOM   831  C  CA  . ALA A  1  113 ? 56.393  13.113  44.318 1.00 33.87  ? 126 ALA A CA  1 
ATOM   832  C  C   . ALA A  1  113 ? 55.317  13.321  45.381 1.00 35.04  ? 126 ALA A C   1 
ATOM   833  O  O   . ALA A  1  113 ? 55.423  14.233  46.189 1.00 35.52  ? 126 ALA A O   1 
ATOM   834  C  CB  . ALA A  1  113 ? 57.396  12.073  44.745 1.00 33.60  ? 126 ALA A CB  1 
ATOM   835  N  N   . HIS A  1  114 ? 54.279  12.473  45.374 1.00 35.10  ? 127 HIS A N   1 
ATOM   836  C  CA  . HIS A  1  114 ? 53.039  12.764  46.089 1.00 31.57  ? 127 HIS A CA  1 
ATOM   837  C  C   . HIS A  1  114 ? 52.448  11.523  46.777 1.00 30.87  ? 127 HIS A C   1 
ATOM   838  O  O   . HIS A  1  114 ? 51.823  11.649  47.827 1.00 28.21  ? 127 HIS A O   1 
ATOM   839  C  CB  . HIS A  1  114 ? 52.050  13.445  45.129 1.00 31.87  ? 127 HIS A CB  1 
ATOM   840  C  CG  . HIS A  1  114 ? 51.907  12.748  43.818 1.00 32.73  ? 127 HIS A CG  1 
ATOM   841  N  ND1 . HIS A  1  114 ? 51.144  11.609  43.700 1.00 29.81  ? 127 HIS A ND1 1 
ATOM   842  C  CD2 . HIS A  1  114 ? 52.435  12.970  42.599 1.00 31.20  ? 127 HIS A CD2 1 
ATOM   843  C  CE1 . HIS A  1  114 ? 51.185  11.184  42.444 1.00 33.32  ? 127 HIS A CE1 1 
ATOM   844  N  NE2 . HIS A  1  114 ? 51.988  11.987  41.751 1.00 32.57  ? 127 HIS A NE2 1 
ATOM   845  N  N   . ALA A  1  115 ? 52.612  10.324  46.200 1.00 31.76  ? 128 ALA A N   1 
ATOM   846  C  CA  . ALA A  1  115 ? 51.929  9.128   46.698 1.00 28.04  ? 128 ALA A CA  1 
ATOM   847  C  C   . ALA A  1  115 ? 50.428  9.389   46.855 1.00 26.52  ? 128 ALA A C   1 
ATOM   848  O  O   . ALA A  1  115 ? 49.780  8.951   47.806 1.00 27.74  ? 128 ALA A O   1 
ATOM   849  C  CB  . ALA A  1  115 ? 52.552  8.663   47.991 1.00 26.77  ? 128 ALA A CB  1 
ATOM   850  N  N   . GLY A  1  116 ? 49.872  10.090  45.871 1.00 28.47  ? 129 GLY A N   1 
ATOM   851  C  CA  . GLY A  1  116 ? 48.507  10.588  45.902 1.00 30.60  ? 129 GLY A CA  1 
ATOM   852  C  C   . GLY A  1  116 ? 47.490  9.557   45.407 1.00 32.16  ? 129 GLY A C   1 
ATOM   853  O  O   . GLY A  1  116 ? 46.308  9.853   45.429 1.00 29.67  ? 129 GLY A O   1 
ATOM   854  N  N   . GLY A  1  117 ? 47.940  8.368   44.959 1.00 28.69  ? 130 GLY A N   1 
ATOM   855  C  CA  . GLY A  1  117 ? 47.024  7.293   44.628 1.00 28.05  ? 130 GLY A CA  1 
ATOM   856  C  C   . GLY A  1  117 ? 46.630  7.288   43.161 1.00 29.80  ? 130 GLY A C   1 
ATOM   857  O  O   . GLY A  1  117 ? 46.991  8.189   42.400 1.00 28.57  ? 130 GLY A O   1 
ATOM   858  N  N   . LEU A  1  118 ? 45.857  6.262   42.772 1.00 27.63  ? 131 LEU A N   1 
ATOM   859  C  CA  . LEU A  1  118 ? 45.457  6.076   41.388 1.00 27.93  ? 131 LEU A CA  1 
ATOM   860  C  C   . LEU A  1  118 ? 44.562  7.209   40.869 1.00 27.71  ? 131 LEU A C   1 
ATOM   861  O  O   . LEU A  1  118 ? 44.442  7.354   39.659 1.00 29.01  ? 131 LEU A O   1 
ATOM   862  C  CB  . LEU A  1  118 ? 44.762  4.731   41.238 1.00 28.81  ? 131 LEU A CB  1 
ATOM   863  C  CG  . LEU A  1  118 ? 45.616  3.488   41.503 1.00 29.07  ? 131 LEU A CG  1 
ATOM   864  C  CD1 . LEU A  1  118 ? 44.784  2.216   41.229 1.00 30.28  ? 131 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A  1  118 ? 46.894  3.494   40.695 1.00 29.01  ? 131 LEU A CD2 1 
ATOM   866  N  N   . ASN A  1  119 ? 43.931  7.985   41.760 1.00 30.27  ? 132 ASN A N   1 
ATOM   867  C  CA  . ASN A  1  119 ? 43.139  9.144   41.351 1.00 34.15  ? 132 ASN A CA  1 
ATOM   868  C  C   . ASN A  1  119 ? 43.975  10.226  40.657 1.00 33.62  ? 132 ASN A C   1 
ATOM   869  O  O   . ASN A  1  119 ? 43.410  11.033  39.931 1.00 33.70  ? 132 ASN A O   1 
ATOM   870  C  CB  . ASN A  1  119 ? 42.439  9.821   42.527 1.00 33.53  ? 132 ASN A CB  1 
ATOM   871  C  CG  . ASN A  1  119 ? 41.251  9.035   43.031 1.00 33.00  ? 132 ASN A CG  1 
ATOM   872  O  OD1 . ASN A  1  119 ? 40.940  7.949   42.532 1.00 32.93  ? 132 ASN A OD1 1 
ATOM   873  N  ND2 . ASN A  1  119 ? 40.561  9.575   44.011 1.00 33.86  ? 132 ASN A ND2 1 
ATOM   874  N  N   . VAL A  1  120 ? 45.296  10.260  40.857 1.00 29.11  ? 133 VAL A N   1 
ATOM   875  C  CA  . VAL A  1  120 ? 46.108  11.331  40.276 1.00 31.45  ? 133 VAL A CA  1 
ATOM   876  C  C   . VAL A  1  120 ? 46.056  11.309  38.747 1.00 32.60  ? 133 VAL A C   1 
ATOM   877  O  O   . VAL A  1  120 ? 46.358  10.306  38.099 1.00 35.43  ? 133 VAL A O   1 
ATOM   878  C  CB  . VAL A  1  120 ? 47.560  11.314  40.787 1.00 34.83  ? 133 VAL A CB  1 
ATOM   879  C  CG1 . VAL A  1  120 ? 48.434  12.361  40.101 1.00 35.92  ? 133 VAL A CG1 1 
ATOM   880  C  CG2 . VAL A  1  120 ? 47.607  11.521  42.292 1.00 33.79  ? 133 VAL A CG2 1 
ATOM   881  N  N   . HIS A  1  121 ? 45.692  12.459  38.166 1.00 33.50  ? 134 HIS A N   1 
ATOM   882  C  CA  . HIS A  1  121 ? 45.412  12.606  36.739 1.00 34.28  ? 134 HIS A CA  1 
ATOM   883  C  C   . HIS A  1  121 ? 46.668  12.993  35.953 1.00 34.86  ? 134 HIS A C   1 
ATOM   884  O  O   . HIS A  1  121 ? 47.510  13.724  36.460 1.00 37.30  ? 134 HIS A O   1 
ATOM   885  C  CB  . HIS A  1  121 ? 44.358  13.705  36.535 1.00 36.40  ? 134 HIS A CB  1 
ATOM   886  C  CG  . HIS A  1  121 ? 44.113  14.069  35.115 1.00 37.78  ? 134 HIS A CG  1 
ATOM   887  N  ND1 . HIS A  1  121 ? 43.419  13.247  34.253 1.00 38.85  ? 134 HIS A ND1 1 
ATOM   888  C  CD2 . HIS A  1  121 ? 44.498  15.153  34.384 1.00 40.51  ? 134 HIS A CD2 1 
ATOM   889  C  CE1 . HIS A  1  121 ? 43.351  13.833  33.053 1.00 41.90  ? 134 HIS A CE1 1 
ATOM   890  N  NE2 . HIS A  1  121 ? 43.999  14.990  33.108 1.00 37.87  ? 134 HIS A NE2 1 
ATOM   891  N  N   . GLY A  1  122 ? 46.775  12.517  34.710 1.00 38.86  ? 135 GLY A N   1 
ATOM   892  C  CA  . GLY A  1  122 ? 47.651  13.144  33.735 1.00 41.73  ? 135 GLY A CA  1 
ATOM   893  C  C   . GLY A  1  122 ? 48.807  12.275  33.231 1.00 41.55  ? 135 GLY A C   1 
ATOM   894  O  O   . GLY A  1  122 ? 49.273  12.518  32.118 1.00 41.11  ? 135 GLY A O   1 
ATOM   895  N  N   . THR A  1  123 ? 49.328  11.327  34.028 1.00 38.14  ? 136 THR A N   1 
ATOM   896  C  CA  A THR A  1  123 ? 50.403  10.455  33.575 0.50 39.36  ? 136 THR A CA  1 
ATOM   897  C  CA  B THR A  1  123 ? 50.398  10.457  33.537 0.50 39.99  ? 136 THR A CA  1 
ATOM   898  C  C   . THR A  1  123 ? 49.910  9.008   33.454 1.00 36.98  ? 136 THR A C   1 
ATOM   899  O  O   . THR A  1  123 ? 50.261  8.315   32.503 1.00 37.77  ? 136 THR A O   1 
ATOM   900  C  CB  A THR A  1  123 ? 51.576  10.605  34.541 0.50 40.04  ? 136 THR A CB  1 
ATOM   901  C  CB  B THR A  1  123 ? 51.707  10.600  34.327 0.50 43.06  ? 136 THR A CB  1 
ATOM   902  O  OG1 A THR A  1  123 ? 51.069  10.189  35.804 0.50 57.68  ? 136 THR A OG1 1 
ATOM   903  O  OG1 B THR A  1  123 ? 52.746  9.870   33.673 0.50 38.56  ? 136 THR A OG1 1 
ATOM   904  C  CG2 A THR A  1  123 ? 52.010  12.044  34.724 0.50 33.27  ? 136 THR A CG2 1 
ATOM   905  C  CG2 B THR A  1  123 ? 51.648  10.013  35.721 0.50 50.78  ? 136 THR A CG2 1 
ATOM   906  N  N   . PHE A  1  124 ? 49.104  8.544   34.435 1.00 35.24  ? 137 PHE A N   1 
ATOM   907  C  CA  . PHE A  1  124 ? 48.438  7.241   34.363 1.00 33.48  ? 137 PHE A CA  1 
ATOM   908  C  C   . PHE A  1  124 ? 46.935  7.446   34.099 1.00 34.46  ? 137 PHE A C   1 
ATOM   909  O  O   . PHE A  1  124 ? 46.515  7.384   32.943 1.00 38.46  ? 137 PHE A O   1 
ATOM   910  C  CB  . PHE A  1  124 ? 48.765  6.391   35.599 1.00 34.14  ? 137 PHE A CB  1 
ATOM   911  C  CG  . PHE A  1  124 ? 48.319  4.926   35.584 1.00 34.78  ? 137 PHE A CG  1 
ATOM   912  C  CD1 . PHE A  1  124 ? 47.691  4.351   34.484 1.00 37.32  ? 137 PHE A CD1 1 
ATOM   913  C  CD2 . PHE A  1  124 ? 48.589  4.094   36.673 1.00 37.42  ? 137 PHE A CD2 1 
ATOM   914  C  CE1 . PHE A  1  124 ? 47.290  3.015   34.494 1.00 34.89  ? 137 PHE A CE1 1 
ATOM   915  C  CE2 . PHE A  1  124 ? 48.226  2.744   36.661 1.00 33.89  ? 137 PHE A CE2 1 
ATOM   916  C  CZ  . PHE A  1  124 ? 47.586  2.213   35.572 1.00 34.72  ? 137 PHE A CZ  1 
ATOM   917  N  N   . GLU A  1  125 ? 46.114  7.682   35.137 1.00 35.46  ? 138 GLU A N   1 
ATOM   918  C  CA  . GLU A  1  125 ? 44.688  7.964   34.962 1.00 33.57  ? 138 GLU A CA  1 
ATOM   919  C  C   . GLU A  1  125 ? 44.510  9.043   33.885 1.00 36.81  ? 138 GLU A C   1 
ATOM   920  O  O   . GLU A  1  125 ? 45.258  10.021  33.842 1.00 35.35  ? 138 GLU A O   1 
ATOM   921  C  CB  . GLU A  1  125 ? 44.055  8.405   36.287 1.00 36.85  ? 138 GLU A CB  1 
ATOM   922  C  CG  . GLU A  1  125 ? 42.537  8.598   36.281 1.00 35.96  ? 138 GLU A CG  1 
ATOM   923  C  CD  . GLU A  1  125 ? 42.011  9.796   35.481 1.00 37.10  ? 138 GLU A CD  1 
ATOM   924  O  OE1 . GLU A  1  125 ? 42.662  10.860  35.605 1.00 35.50  ? 138 GLU A OE1 1 
ATOM   925  O  OE2 . GLU A  1  125 ? 40.986  9.671   34.747 1.00 36.03  ? 138 GLU A OE2 1 
ATOM   926  N  N   . GLY A  1  126 ? 43.513  8.860   33.010 1.00 33.74  ? 139 GLY A N   1 
ATOM   927  C  CA  . GLY A  1  126 ? 43.224  9.824   31.963 1.00 34.11  ? 139 GLY A CA  1 
ATOM   928  C  C   . GLY A  1  126 ? 41.793  9.735   31.428 1.00 34.13  ? 139 GLY A C   1 
ATOM   929  O  O   . GLY A  1  126 ? 40.900  9.116   32.029 1.00 30.55  ? 139 GLY A O   1 
ATOM   930  N  N   . ASP A  1  127 ? 41.619  10.306  30.230 1.00 35.09  ? 140 ASP A N   1 
ATOM   931  C  CA  . ASP A  1  127 ? 40.312  10.739  29.747 1.00 32.40  ? 140 ASP A CA  1 
ATOM   932  C  C   . ASP A  1  127 ? 39.628  9.652   28.919 1.00 28.74  ? 140 ASP A C   1 
ATOM   933  O  O   . ASP A  1  127 ? 40.240  8.663   28.513 1.00 29.39  ? 140 ASP A O   1 
ATOM   934  C  CB  . ASP A  1  127 ? 40.458  12.026  28.956 1.00 35.48  ? 140 ASP A CB  1 
ATOM   935  C  CG  . ASP A  1  127 ? 41.042  13.221  29.693 1.00 36.65  ? 140 ASP A CG  1 
ATOM   936  O  OD1 . ASP A  1  127 ? 40.762  13.369  30.906 1.00 34.60  ? 140 ASP A OD1 1 
ATOM   937  O  OD2 . ASP A  1  127 ? 41.759  14.030  29.032 1.00 39.14  ? 140 ASP A OD2 1 
ATOM   938  N  N   . ALA A  1  128 ? 38.335  9.873   28.655 1.00 30.70  ? 141 ALA A N   1 
ATOM   939  C  CA  . ALA A  1  128 ? 37.527  9.026   27.790 1.00 30.96  ? 141 ALA A CA  1 
ATOM   940  C  C   . ALA A  1  128 ? 37.325  7.622   28.385 1.00 33.18  ? 141 ALA A C   1 
ATOM   941  O  O   . ALA A  1  128 ? 37.271  6.624   27.669 1.00 33.09  ? 141 ALA A O   1 
ATOM   942  C  CB  . ALA A  1  128 ? 38.108  8.980   26.390 1.00 34.22  ? 141 ALA A CB  1 
ATOM   943  N  N   . GLY A  1  129 ? 37.154  7.549   29.706 1.00 33.61  ? 142 GLY A N   1 
ATOM   944  C  CA  . GLY A  1  129 ? 36.785  6.299   30.354 1.00 32.01  ? 142 GLY A CA  1 
ATOM   945  C  C   . GLY A  1  129 ? 35.329  5.932   30.078 1.00 32.08  ? 142 GLY A C   1 
ATOM   946  O  O   . GLY A  1  129 ? 34.560  6.739   29.562 1.00 31.46  ? 142 GLY A O   1 
ATOM   947  N  N   . MET A  1  130 ? 34.964  4.703   30.454 1.00 31.44  ? 143 MET A N   1 
ATOM   948  C  CA  . MET A  1  130 ? 33.661  4.143   30.152 1.00 31.55  ? 143 MET A CA  1 
ATOM   949  C  C   . MET A  1  130 ? 32.631  4.579   31.186 1.00 32.18  ? 143 MET A C   1 
ATOM   950  O  O   . MET A  1  130 ? 31.514  4.923   30.796 1.00 31.49  ? 143 MET A O   1 
ATOM   951  C  CB  . MET A  1  130 ? 33.691  2.612   30.118 1.00 35.25  ? 143 MET A CB  1 
ATOM   952  C  CG  . MET A  1  130 ? 34.400  2.013   28.908 1.00 38.22  ? 143 MET A CG  1 
ATOM   953  S  SD  . MET A  1  130 ? 34.509  0.207   29.003 1.00 39.67  ? 143 MET A SD  1 
ATOM   954  C  CE  . MET A  1  130 ? 35.653  0.070   30.378 1.00 35.61  ? 143 MET A CE  1 
ATOM   955  N  N   . THR A  1  131 ? 32.974  4.506   32.486 1.00 29.17  ? 144 THR A N   1 
ATOM   956  C  CA  . THR A  1  131 ? 32.011  4.816   33.532 1.00 29.09  ? 144 THR A CA  1 
ATOM   957  C  C   . THR A  1  131 ? 32.489  5.949   34.436 1.00 31.12  ? 144 THR A C   1 
ATOM   958  O  O   . THR A  1  131 ? 31.796  6.264   35.405 1.00 30.45  ? 144 THR A O   1 
ATOM   959  C  CB  . THR A  1  131 ? 31.687  3.579   34.372 1.00 30.36  ? 144 THR A CB  1 
ATOM   960  O  OG1 . THR A  1  131 ? 32.819  3.266   35.189 1.00 25.87  ? 144 THR A OG1 1 
ATOM   961  C  CG2 . THR A  1  131 ? 31.217  2.419   33.510 1.00 29.23  ? 144 THR A CG2 1 
ATOM   962  N  N   . ARG A  1  132 ? 33.676  6.509   34.158 1.00 30.38  ? 145 ARG A N   1 
ATOM   963  C  CA  . ARG A  1  132 ? 34.199  7.653   34.881 1.00 31.41  ? 145 ARG A CA  1 
ATOM   964  C  C   . ARG A  1  132 ? 34.360  8.826   33.917 1.00 31.48  ? 145 ARG A C   1 
ATOM   965  O  O   . ARG A  1  132 ? 34.812  8.629   32.796 1.00 34.21  ? 145 ARG A O   1 
ATOM   966  C  CB  . ARG A  1  132 ? 35.552  7.326   35.528 1.00 33.29  ? 145 ARG A CB  1 
ATOM   967  C  CG  . ARG A  1  132 ? 35.470  6.754   36.937 1.00 34.21  ? 145 ARG A CG  1 
ATOM   968  C  CD  . ARG A  1  132 ? 34.846  5.362   37.029 1.00 34.38  ? 145 ARG A CD  1 
ATOM   969  N  NE  . ARG A  1  132 ? 34.680  4.961   38.432 1.00 34.06  ? 145 ARG A NE  1 
ATOM   970  C  CZ  . ARG A  1  132 ? 33.954  3.927   38.893 1.00 34.35  ? 145 ARG A CZ  1 
ATOM   971  N  NH1 . ARG A  1  132 ? 33.845  3.764   40.206 1.00 34.35  ? 145 ARG A NH1 1 
ATOM   972  N  NH2 . ARG A  1  132 ? 33.286  3.100   38.086 1.00 31.59  ? 145 ARG A NH2 1 
ATOM   973  N  N   . ALA A  1  133 ? 34.065  10.038  34.400 1.00 31.41  ? 146 ALA A N   1 
ATOM   974  C  CA  . ALA A  1  133 ? 34.177  11.269  33.629 1.00 32.76  ? 146 ALA A CA  1 
ATOM   975  C  C   . ALA A  1  133 ? 35.608  11.808  33.655 1.00 32.33  ? 146 ALA A C   1 
ATOM   976  O  O   . ALA A  1  133 ? 36.365  11.552  34.583 1.00 29.50  ? 146 ALA A O   1 
ATOM   977  N  N   . ASP A  1  134 ? 35.955  12.604  32.634 1.00 33.21  ? 147 ASP A N   1 
ATOM   978  C  CA  . ASP A  1  134 ? 37.255  13.242  32.525 1.00 33.71  ? 147 ASP A CA  1 
ATOM   979  C  C   . ASP A  1  134 ? 37.473  14.171  33.708 1.00 30.51  ? 147 ASP A C   1 
ATOM   980  O  O   . ASP A  1  134 ? 36.531  14.778  34.195 1.00 34.14  ? 147 ASP A O   1 
ATOM   981  C  CB  . ASP A  1  134 ? 37.396  14.027  31.230 1.00 34.18  ? 147 ASP A CB  1 
ATOM   982  C  CG  . ASP A  1  134 ? 37.312  13.221  29.952 1.00 37.22  ? 147 ASP A CG  1 
ATOM   983  O  OD1 . ASP A  1  134 ? 37.077  11.991  30.052 1.00 35.79  ? 147 ASP A OD1 1 
ATOM   984  O  OD2 . ASP A  1  134 ? 37.497  13.832  28.861 1.00 36.35  ? 147 ASP A OD2 1 
ATOM   985  N  N   . GLU A  1  135 ? 38.728  14.262  34.162 1.00 32.72  ? 148 GLU A N   1 
ATOM   986  C  CA  . GLU A  1  135 ? 39.102  15.063  35.317 1.00 34.82  ? 148 GLU A CA  1 
ATOM   987  C  C   . GLU A  1  135 ? 38.703  16.535  35.135 1.00 35.55  ? 148 GLU A C   1 
ATOM   988  O  O   . GLU A  1  135 ? 38.419  17.210  36.116 1.00 35.47  ? 148 GLU A O   1 
ATOM   989  C  CB  . GLU A  1  135 ? 40.611  14.956  35.537 1.00 37.89  ? 148 GLU A CB  1 
ATOM   990  C  CG  . GLU A  1  135 ? 41.093  15.633  36.818 1.00 42.48  ? 148 GLU A CG  1 
ATOM   991  C  CD  . GLU A  1  135 ? 41.556  17.075  36.655 1.00 50.60  ? 148 GLU A CD  1 
ATOM   992  O  OE1 . GLU A  1  135 ? 41.520  17.645  35.527 1.00 52.75  ? 148 GLU A OE1 1 
ATOM   993  O  OE2 . GLU A  1  135 ? 41.945  17.639  37.699 1.00 56.34  ? 148 GLU A OE2 1 
ATOM   994  N  N   . PHE A  1  136 ? 38.689  17.018  33.891 1.00 35.77  ? 149 PHE A N   1 
ATOM   995  C  CA  . PHE A  1  136 ? 38.316  18.390  33.586 1.00 40.39  ? 149 PHE A CA  1 
ATOM   996  C  C   . PHE A  1  136 ? 36.945  18.720  34.168 1.00 39.75  ? 149 PHE A C   1 
ATOM   997  O  O   . PHE A  1  136 ? 36.748  19.831  34.632 1.00 37.66  ? 149 PHE A O   1 
ATOM   998  C  CB  . PHE A  1  136 ? 38.306  18.658  32.076 1.00 46.26  ? 149 PHE A CB  1 
ATOM   999  C  CG  . PHE A  1  136 ? 37.848  20.071  31.725 1.00 50.82  ? 149 PHE A CG  1 
ATOM   1000 C  CD1 . PHE A  1  136 ? 38.674  21.166  31.972 1.00 49.69  ? 149 PHE A CD1 1 
ATOM   1001 C  CD2 . PHE A  1  136 ? 36.591  20.300  31.165 1.00 50.82  ? 149 PHE A CD2 1 
ATOM   1002 C  CE1 . PHE A  1  136 ? 38.254  22.450  31.660 1.00 49.60  ? 149 PHE A CE1 1 
ATOM   1003 C  CE2 . PHE A  1  136 ? 36.168  21.588  30.872 1.00 50.41  ? 149 PHE A CE2 1 
ATOM   1004 C  CZ  . PHE A  1  136 ? 37.000  22.657  31.120 1.00 48.10  ? 149 PHE A CZ  1 
ATOM   1005 N  N   . PHE A  1  137 ? 36.014  17.760  34.201 1.00 38.97  ? 150 PHE A N   1 
ATOM   1006 C  CA  . PHE A  1  137 ? 34.657  18.034  34.659 1.00 39.72  ? 150 PHE A CA  1 
ATOM   1007 C  C   . PHE A  1  137 ? 34.532  17.966  36.178 1.00 40.10  ? 150 PHE A C   1 
ATOM   1008 O  O   . PHE A  1  137 ? 33.453  18.213  36.693 1.00 39.75  ? 150 PHE A O   1 
ATOM   1009 C  CB  . PHE A  1  137 ? 33.681  17.083  33.965 1.00 38.79  ? 150 PHE A CB  1 
ATOM   1010 C  CG  . PHE A  1  137 ? 33.760  17.150  32.446 1.00 41.08  ? 150 PHE A CG  1 
ATOM   1011 C  CD1 . PHE A  1  137 ? 33.578  18.354  31.774 1.00 44.29  ? 150 PHE A CD1 1 
ATOM   1012 C  CD2 . PHE A  1  137 ? 34.062  16.024  31.691 1.00 40.03  ? 150 PHE A CD2 1 
ATOM   1013 C  CE1 . PHE A  1  137 ? 33.663  18.417  30.391 1.00 42.67  ? 150 PHE A CE1 1 
ATOM   1014 C  CE2 . PHE A  1  137 ? 34.151  16.092  30.311 1.00 42.33  ? 150 PHE A CE2 1 
ATOM   1015 C  CZ  . PHE A  1  137 ? 33.940  17.285  29.663 1.00 43.68  ? 150 PHE A CZ  1 
ATOM   1016 N  N   . GLY A  1  138 ? 35.610  17.622  36.894 1.00 39.22  ? 151 GLY A N   1 
ATOM   1017 C  CA  . GLY A  1  138 ? 35.645  17.796  38.339 1.00 41.19  ? 151 GLY A CA  1 
ATOM   1018 C  C   . GLY A  1  138 ? 35.735  16.490  39.146 1.00 44.00  ? 151 GLY A C   1 
ATOM   1019 O  O   . GLY A  1  138 ? 35.998  16.557  40.345 1.00 40.54  ? 151 GLY A O   1 
ATOM   1020 N  N   . ASP A  1  139 ? 35.514  15.317  38.529 1.00 39.31  ? 152 ASP A N   1 
ATOM   1021 C  CA  . ASP A  1  139 ? 35.532  14.066  39.286 1.00 38.50  ? 152 ASP A CA  1 
ATOM   1022 C  C   . ASP A  1  139 ? 35.927  12.896  38.382 1.00 33.37  ? 152 ASP A C   1 
ATOM   1023 O  O   . ASP A  1  139 ? 35.109  12.403  37.603 1.00 33.21  ? 152 ASP A O   1 
ATOM   1024 C  CB  . ASP A  1  139 ? 34.187  13.799  39.948 1.00 41.96  ? 152 ASP A CB  1 
ATOM   1025 C  CG  . ASP A  1  139 ? 34.104  12.514  40.763 1.00 45.26  ? 152 ASP A CG  1 
ATOM   1026 O  OD1 . ASP A  1  139 ? 35.028  11.678  40.647 1.00 39.79  ? 152 ASP A OD1 1 
ATOM   1027 O  OD2 . ASP A  1  139 ? 33.138  12.366  41.541 1.00 43.64  ? 152 ASP A OD2 1 
ATOM   1028 N  N   . ASN A  1  140 ? 37.173  12.430  38.520 1.00 30.20  ? 153 ASN A N   1 
ATOM   1029 C  CA  . ASN A  1  140 ? 37.713  11.426  37.612 1.00 32.93  ? 153 ASN A CA  1 
ATOM   1030 C  C   . ASN A  1  140 ? 37.596  10.013  38.199 1.00 31.84  ? 153 ASN A C   1 
ATOM   1031 O  O   . ASN A  1  140 ? 38.097  9.071   37.590 1.00 33.39  ? 153 ASN A O   1 
ATOM   1032 C  CB  . ASN A  1  140 ? 39.162  11.714  37.240 1.00 33.53  ? 153 ASN A CB  1 
ATOM   1033 C  CG  . ASN A  1  140 ? 40.118  11.605  38.413 1.00 34.11  ? 153 ASN A CG  1 
ATOM   1034 O  OD1 . ASN A  1  140 ? 39.699  11.490  39.567 1.00 36.69  ? 153 ASN A OD1 1 
ATOM   1035 N  ND2 . ASN A  1  140 ? 41.411  11.642  38.139 1.00 34.17  ? 153 ASN A ND2 1 
ATOM   1036 N  N   . HIS A  1  141 ? 36.957  9.869   39.365 1.00 29.95  ? 154 HIS A N   1 
ATOM   1037 C  CA  . HIS A  1  141 ? 37.038  8.626   40.125 1.00 34.10  ? 154 HIS A CA  1 
ATOM   1038 C  C   . HIS A  1  141 ? 35.666  7.984   40.385 1.00 34.70  ? 154 HIS A C   1 
ATOM   1039 O  O   . HIS A  1  141 ? 35.555  6.753   40.443 1.00 31.43  ? 154 HIS A O   1 
ATOM   1040 C  CB  . HIS A  1  141 ? 37.875  8.832   41.393 1.00 32.63  ? 154 HIS A CB  1 
ATOM   1041 C  CG  . HIS A  1  141 ? 37.408  9.932   42.258 1.00 39.63  ? 154 HIS A CG  1 
ATOM   1042 N  ND1 . HIS A  1  141 ? 36.452  9.721   43.226 1.00 40.81  ? 154 HIS A ND1 1 
ATOM   1043 C  CD2 . HIS A  1  141 ? 37.726  11.244  42.313 1.00 39.87  ? 154 HIS A CD2 1 
ATOM   1044 C  CE1 . HIS A  1  141 ? 36.204  10.869  43.841 1.00 44.10  ? 154 HIS A CE1 1 
ATOM   1045 N  NE2 . HIS A  1  141 ? 36.955  11.811  43.292 1.00 42.34  ? 154 HIS A NE2 1 
ATOM   1046 N  N   . SER A  1  142 ? 34.630  8.798   40.597 1.00 30.54  ? 155 SER A N   1 
ATOM   1047 C  CA  . SER A  1  142 ? 33.317  8.286   40.939 1.00 32.86  ? 155 SER A CA  1 
ATOM   1048 C  C   . SER A  1  142 ? 32.654  7.671   39.715 1.00 30.80  ? 155 SER A C   1 
ATOM   1049 O  O   . SER A  1  142 ? 32.831  8.138   38.592 1.00 28.28  ? 155 SER A O   1 
ATOM   1050 C  CB  . SER A  1  142 ? 32.417  9.357   41.499 1.00 34.40  ? 155 SER A CB  1 
ATOM   1051 O  OG  . SER A  1  142 ? 32.993  9.934   42.653 1.00 37.12  ? 155 SER A OG  1 
ATOM   1052 N  N   . PHE A  1  143 ? 31.842  6.649   39.969 1.00 29.46  ? 156 PHE A N   1 
ATOM   1053 C  CA  . PHE A  1  143 ? 30.933  6.132   38.965 1.00 31.35  ? 156 PHE A CA  1 
ATOM   1054 C  C   . PHE A  1  143 ? 30.016  7.257   38.491 1.00 32.91  ? 156 PHE A C   1 
ATOM   1055 O  O   . PHE A  1  143 ? 29.538  8.038   39.308 1.00 30.72  ? 156 PHE A O   1 
ATOM   1056 C  CB  . PHE A  1  143 ? 30.134  4.972   39.562 1.00 27.96  ? 156 PHE A CB  1 
ATOM   1057 C  CG  . PHE A  1  143 ? 29.049  4.427   38.650 1.00 28.55  ? 156 PHE A CG  1 
ATOM   1058 C  CD1 . PHE A  1  143 ? 29.342  3.452   37.701 1.00 29.15  ? 156 PHE A CD1 1 
ATOM   1059 C  CD2 . PHE A  1  143 ? 27.745  4.890   38.751 1.00 28.70  ? 156 PHE A CD2 1 
ATOM   1060 C  CE1 . PHE A  1  143 ? 28.348  2.946   36.886 1.00 30.68  ? 156 PHE A CE1 1 
ATOM   1061 C  CE2 . PHE A  1  143 ? 26.755  4.389   37.928 1.00 29.37  ? 156 PHE A CE2 1 
ATOM   1062 C  CZ  . PHE A  1  143 ? 27.052  3.415   37.001 1.00 29.17  ? 156 PHE A CZ  1 
ATOM   1063 N  N   . ASN A  1  144 ? 29.774  7.301   37.177 1.00 30.81  ? 157 ASN A N   1 
ATOM   1064 C  CA  . ASN A  1  144 ? 28.941  8.313   36.565 1.00 31.24  ? 157 ASN A CA  1 
ATOM   1065 C  C   . ASN A  1  144 ? 27.788  7.634   35.830 1.00 28.83  ? 157 ASN A C   1 
ATOM   1066 O  O   . ASN A  1  144 ? 28.012  6.953   34.837 1.00 26.82  ? 157 ASN A O   1 
ATOM   1067 C  CB  . ASN A  1  144 ? 29.800  9.169   35.641 1.00 33.79  ? 157 ASN A CB  1 
ATOM   1068 C  CG  . ASN A  1  144 ? 29.017  10.254  34.926 1.00 36.36  ? 157 ASN A CG  1 
ATOM   1069 O  OD1 . ASN A  1  144 ? 28.059  9.924   34.219 1.00 32.12  ? 157 ASN A OD1 1 
ATOM   1070 N  ND2 . ASN A  1  144 ? 29.392  11.519  35.110 1.00 45.42  ? 157 ASN A ND2 1 
ATOM   1071 N  N   . GLN A  1  145 ? 26.562  7.854   36.306 1.00 27.57  ? 158 GLN A N   1 
ATOM   1072 C  CA  . GLN A  1  145 ? 25.390  7.131   35.839 1.00 30.98  ? 158 GLN A CA  1 
ATOM   1073 C  C   . GLN A  1  145 ? 25.094  7.476   34.377 1.00 30.75  ? 158 GLN A C   1 
ATOM   1074 O  O   . GLN A  1  145 ? 24.668  6.609   33.614 1.00 31.12  ? 158 GLN A O   1 
ATOM   1075 C  CB  . GLN A  1  145 ? 24.174  7.387   36.731 1.00 31.71  ? 158 GLN A CB  1 
ATOM   1076 C  CG  . GLN A  1  145 ? 22.917  6.595   36.354 1.00 33.97  ? 158 GLN A CG  1 
ATOM   1077 C  CD  . GLN A  1  145 ? 23.082  5.086   36.442 1.00 35.81  ? 158 GLN A CD  1 
ATOM   1078 O  OE1 . GLN A  1  145 ? 23.531  4.536   37.453 1.00 36.77  ? 158 GLN A OE1 1 
ATOM   1079 N  NE2 . GLN A  1  145 ? 22.684  4.372   35.400 1.00 36.11  ? 158 GLN A NE2 1 
ATOM   1080 N  N   . THR A  1  146 ? 25.300  8.737   33.993 1.00 29.46  ? 159 THR A N   1 
ATOM   1081 C  CA  . THR A  1  146 ? 25.087  9.166   32.619 1.00 33.02  ? 159 THR A CA  1 
ATOM   1082 C  C   . THR A  1  146 ? 25.978  8.360   31.679 1.00 32.03  ? 159 THR A C   1 
ATOM   1083 O  O   . THR A  1  146 ? 25.530  7.929   30.619 1.00 31.29  ? 159 THR A O   1 
ATOM   1084 C  CB  . THR A  1  146 ? 25.359  10.664  32.454 1.00 35.98  ? 159 THR A CB  1 
ATOM   1085 O  OG1 . THR A  1  146 ? 24.455  11.316  33.333 1.00 37.66  ? 159 THR A OG1 1 
ATOM   1086 C  CG2 . THR A  1  146 ? 25.075  11.174  31.053 1.00 35.96  ? 159 THR A CG2 1 
ATOM   1087 N  N   . LEU A  1  147 ? 27.248  8.176   32.050 1.00 28.60  ? 160 LEU A N   1 
ATOM   1088 C  CA  . LEU A  1  147 ? 28.159  7.424   31.201 1.00 29.59  ? 160 LEU A CA  1 
ATOM   1089 C  C   . LEU A  1  147 ? 27.761  5.949   31.169 1.00 28.89  ? 160 LEU A C   1 
ATOM   1090 O  O   . LEU A  1  147 ? 27.879  5.284   30.141 1.00 28.48  ? 160 LEU A O   1 
ATOM   1091 C  CB  . LEU A  1  147 ? 29.591  7.619   31.697 1.00 31.41  ? 160 LEU A CB  1 
ATOM   1092 C  CG  . LEU A  1  147 ? 30.183  9.005   31.428 1.00 34.15  ? 160 LEU A CG  1 
ATOM   1093 C  CD1 . LEU A  1  147 ? 31.593  9.120   31.966 1.00 36.61  ? 160 LEU A CD1 1 
ATOM   1094 C  CD2 . LEU A  1  147 ? 30.174  9.318   29.938 1.00 34.89  ? 160 LEU A CD2 1 
ATOM   1095 N  N   . PHE A  1  148 ? 27.286  5.432   32.306 1.00 29.28  ? 161 PHE A N   1 
ATOM   1096 C  CA  . PHE A  1  148 ? 26.855  4.048   32.343 1.00 28.60  ? 161 PHE A CA  1 
ATOM   1097 C  C   . PHE A  1  148 ? 25.624  3.877   31.452 1.00 30.32  ? 161 PHE A C   1 
ATOM   1098 O  O   . PHE A  1  148 ? 25.482  2.842   30.819 1.00 30.89  ? 161 PHE A O   1 
ATOM   1099 C  CB  . PHE A  1  148 ? 26.576  3.571   33.768 1.00 28.85  ? 161 PHE A CB  1 
ATOM   1100 C  CG  . PHE A  1  148 ? 26.260  2.088   33.806 1.00 27.57  ? 161 PHE A CG  1 
ATOM   1101 C  CD1 . PHE A  1  148 ? 27.263  1.151   33.618 1.00 30.56  ? 161 PHE A CD1 1 
ATOM   1102 C  CD2 . PHE A  1  148 ? 24.963  1.644   33.969 1.00 28.27  ? 161 PHE A CD2 1 
ATOM   1103 C  CE1 . PHE A  1  148 ? 26.975  -0.203  33.613 1.00 29.26  ? 161 PHE A CE1 1 
ATOM   1104 C  CE2 . PHE A  1  148 ? 24.680  0.293   33.985 1.00 30.32  ? 161 PHE A CE2 1 
ATOM   1105 C  CZ  . PHE A  1  148 ? 25.681  -0.623  33.809 1.00 29.89  ? 161 PHE A CZ  1 
ATOM   1106 N  N   . ASP A  1  149 ? 24.749  4.889   31.400 1.00 30.98  ? 162 ASP A N   1 
ATOM   1107 C  CA  . ASP A  1  149 ? 23.581  4.849   30.534 1.00 33.33  ? 162 ASP A CA  1 
ATOM   1108 C  C   . ASP A  1  149 ? 24.008  4.747   29.062 1.00 30.60  ? 162 ASP A C   1 
ATOM   1109 O  O   . ASP A  1  149 ? 23.347  4.075   28.284 1.00 32.01  ? 162 ASP A O   1 
ATOM   1110 C  CB  . ASP A  1  149 ? 22.689  6.062   30.760 1.00 32.57  ? 162 ASP A CB  1 
ATOM   1111 C  CG  . ASP A  1  149 ? 21.951  6.113   32.088 1.00 37.79  ? 162 ASP A CG  1 
ATOM   1112 O  OD1 . ASP A  1  149 ? 21.773  5.039   32.709 1.00 39.37  ? 162 ASP A OD1 1 
ATOM   1113 O  OD2 . ASP A  1  149 ? 21.572  7.233   32.488 1.00 38.84  ? 162 ASP A OD2 1 
ATOM   1114 N  N   . LYS A  1  150 ? 25.101  5.418   28.681 1.00 31.07  ? 163 LYS A N   1 
ATOM   1115 C  CA  . LYS A  1  150 ? 25.660  5.293   27.333 1.00 31.49  ? 163 LYS A CA  1 
ATOM   1116 C  C   . LYS A  1  150 ? 26.216  3.887   27.088 1.00 32.14  ? 163 LYS A C   1 
ATOM   1117 O  O   . LYS A  1  150 ? 26.035  3.320   26.016 1.00 32.92  ? 163 LYS A O   1 
ATOM   1118 C  CB  . LYS A  1  150 ? 26.727  6.368   27.106 1.00 32.89  ? 163 LYS A CB  1 
ATOM   1119 C  CG  . LYS A  1  150 ? 27.349  6.410   25.717 1.00 35.25  ? 163 LYS A CG  1 
ATOM   1120 C  CD  . LYS A  1  150 ? 28.416  7.476   25.596 1.00 41.08  ? 163 LYS A CD  1 
ATOM   1121 C  CE  . LYS A  1  150 ? 29.088  7.541   24.259 1.00 42.93  ? 163 LYS A CE  1 
ATOM   1122 N  NZ  . LYS A  1  150 ? 28.697  8.777   23.603 1.00 43.70  ? 163 LYS A NZ  1 
ATOM   1123 N  N   . PHE A  1  151 ? 26.885  3.308   28.092 1.00 31.17  ? 164 PHE A N   1 
ATOM   1124 C  CA  . PHE A  1  151 ? 27.362  1.931   28.019 1.00 29.32  ? 164 PHE A CA  1 
ATOM   1125 C  C   . PHE A  1  151 ? 26.198  0.995   27.709 1.00 29.06  ? 164 PHE A C   1 
ATOM   1126 O  O   . PHE A  1  151 ? 26.310  0.101   26.867 1.00 30.40  ? 164 PHE A O   1 
ATOM   1127 C  CB  . PHE A  1  151 ? 28.063  1.634   29.355 1.00 29.26  ? 164 PHE A CB  1 
ATOM   1128 C  CG  . PHE A  1  151 ? 28.618  0.233   29.529 1.00 28.45  ? 164 PHE A CG  1 
ATOM   1129 C  CD1 . PHE A  1  151 ? 27.821  -0.805  29.990 1.00 29.93  ? 164 PHE A CD1 1 
ATOM   1130 C  CD2 . PHE A  1  151 ? 29.957  -0.029  29.279 1.00 30.76  ? 164 PHE A CD2 1 
ATOM   1131 C  CE1 . PHE A  1  151 ? 28.352  -2.077  30.163 1.00 30.66  ? 164 PHE A CE1 1 
ATOM   1132 C  CE2 . PHE A  1  151 ? 30.483  -1.298  29.452 1.00 30.82  ? 164 PHE A CE2 1 
ATOM   1133 C  CZ  . PHE A  1  151 ? 29.685  -2.316  29.895 1.00 31.19  ? 164 PHE A CZ  1 
ATOM   1134 N  N   . VAL A  1  152 ? 25.077  1.185   28.422 1.00 29.75  ? 165 VAL A N   1 
ATOM   1135 C  CA  . VAL A  1  152 ? 23.879  0.387   28.214 1.00 30.21  ? 165 VAL A CA  1 
ATOM   1136 C  C   . VAL A  1  152 ? 23.329  0.646   26.803 1.00 30.29  ? 165 VAL A C   1 
ATOM   1137 O  O   . VAL A  1  152 ? 22.971  -0.285  26.097 1.00 29.06  ? 165 VAL A O   1 
ATOM   1138 C  CB  . VAL A  1  152 ? 22.810  0.676   29.286 1.00 32.14  ? 165 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A  1  152 ? 21.490  -0.002  28.969 1.00 32.64  ? 165 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A  1  152 ? 23.259  0.265   30.685 1.00 31.30  ? 165 VAL A CG2 1 
ATOM   1141 N  N   . ASP A  1  153 ? 23.258  1.917   26.404 1.00 29.65  ? 166 ASP A N   1 
ATOM   1142 C  CA  . ASP A  1  153 ? 22.751  2.280   25.082 1.00 32.15  ? 166 ASP A CA  1 
ATOM   1143 C  C   . ASP A  1  153 ? 23.576  1.592   23.988 1.00 32.44  ? 166 ASP A C   1 
ATOM   1144 O  O   . ASP A  1  153 ? 23.028  0.982   23.075 1.00 34.73  ? 166 ASP A O   1 
ATOM   1145 C  CB  . ASP A  1  153 ? 22.682  3.791   24.916 1.00 33.31  ? 166 ASP A CB  1 
ATOM   1146 C  CG  . ASP A  1  153 ? 22.110  4.299   23.594 1.00 38.84  ? 166 ASP A CG  1 
ATOM   1147 O  OD1 . ASP A  1  153 ? 20.982  3.881   23.252 1.00 37.98  ? 166 ASP A OD1 1 
ATOM   1148 O  OD2 . ASP A  1  153 ? 22.785  5.113   22.929 1.00 36.96  ? 166 ASP A OD2 1 
ATOM   1149 N  N   . PHE A  1  154 ? 24.908  1.654   24.094 1.00 28.62  ? 167 PHE A N   1 
ATOM   1150 C  CA  . PHE A  1  154 ? 25.760  1.043   23.091 1.00 30.48  ? 167 PHE A CA  1 
ATOM   1151 C  C   . PHE A  1  154 ? 25.630  -0.473  23.125 1.00 30.10  ? 167 PHE A C   1 
ATOM   1152 O  O   . PHE A  1  154 ? 25.707  -1.118  22.081 1.00 31.02  ? 167 PHE A O   1 
ATOM   1153 C  CB  . PHE A  1  154 ? 27.199  1.527   23.217 1.00 31.94  ? 167 PHE A CB  1 
ATOM   1154 C  CG  . PHE A  1  154 ? 27.431  2.820   22.454 1.00 32.31  ? 167 PHE A CG  1 
ATOM   1155 C  CD1 . PHE A  1  154 ? 26.752  3.982   22.793 1.00 33.86  ? 167 PHE A CD1 1 
ATOM   1156 C  CD2 . PHE A  1  154 ? 28.337  2.868   21.407 1.00 36.59  ? 167 PHE A CD2 1 
ATOM   1157 C  CE1 . PHE A  1  154 ? 26.980  5.165   22.105 1.00 34.83  ? 167 PHE A CE1 1 
ATOM   1158 C  CE2 . PHE A  1  154 ? 28.552  4.045   20.709 1.00 36.24  ? 167 PHE A CE2 1 
ATOM   1159 C  CZ  . PHE A  1  154 ? 27.879  5.189   21.064 1.00 36.71  ? 167 PHE A CZ  1 
ATOM   1160 N  N   . SER A  1  155 ? 25.434  -1.045  24.307 1.00 27.85  ? 168 SER A N   1 
ATOM   1161 C  CA  . SER A  1  155 ? 25.211  -2.480  24.420 1.00 29.16  ? 168 SER A CA  1 
ATOM   1162 C  C   . SER A  1  155 ? 23.892  -2.869  23.728 1.00 31.27  ? 168 SER A C   1 
ATOM   1163 O  O   . SER A  1  155 ? 23.805  -3.916  23.100 1.00 29.41  ? 168 SER A O   1 
ATOM   1164 C  CB  . SER A  1  155 ? 25.236  -2.918  25.873 1.00 32.58  ? 168 SER A CB  1 
ATOM   1165 O  OG  . SER A  1  155 ? 26.497  -2.619  26.469 1.00 30.64  ? 168 SER A OG  1 
ATOM   1166 N  N   . ASN A  1  156 ? 22.848  -2.037  23.863 1.00 30.06  ? 169 ASN A N   1 
ATOM   1167 C  CA  . ASN A  1  156 ? 21.578  -2.314  23.194 1.00 29.59  ? 169 ASN A CA  1 
ATOM   1168 C  C   . ASN A  1  156 ? 21.763  -2.209  21.672 1.00 31.00  ? 169 ASN A C   1 
ATOM   1169 O  O   . ASN A  1  156 ? 21.244  -3.029  20.919 1.00 31.71  ? 169 ASN A O   1 
ATOM   1170 C  CB  . ASN A  1  156 ? 20.493  -1.333  23.604 1.00 29.75  ? 169 ASN A CB  1 
ATOM   1171 C  CG  . ASN A  1  156 ? 20.049  -1.464  25.038 1.00 29.21  ? 169 ASN A CG  1 
ATOM   1172 O  OD1 . ASN A  1  156 ? 20.112  -2.537  25.634 1.00 32.29  ? 169 ASN A OD1 1 
ATOM   1173 N  ND2 . ASN A  1  156 ? 19.489  -0.391  25.555 1.00 33.95  ? 169 ASN A ND2 1 
ATOM   1174 N  N   . ARG A  1  157 ? 22.509  -1.194  21.223 1.00 30.20  ? 170 ARG A N   1 
ATOM   1175 C  CA  . ARG A  1  157 ? 22.613  -0.866  19.813 1.00 31.98  ? 170 ARG A CA  1 
ATOM   1176 C  C   . ARG A  1  157 ? 23.504  -1.851  19.068 1.00 36.33  ? 170 ARG A C   1 
ATOM   1177 O  O   . ARG A  1  157 ? 23.253  -2.096  17.894 1.00 38.38  ? 170 ARG A O   1 
ATOM   1178 C  CB  . ARG A  1  157 ? 23.138  0.559   19.633 1.00 31.32  ? 170 ARG A CB  1 
ATOM   1179 C  CG  . ARG A  1  157 ? 22.085  1.585   20.019 1.00 32.29  ? 170 ARG A CG  1 
ATOM   1180 C  CD  . ARG A  1  157 ? 22.602  2.979   20.190 1.00 32.95  ? 170 ARG A CD  1 
ATOM   1181 N  NE  . ARG A  1  157 ? 23.457  3.431   19.092 1.00 37.27  ? 170 ARG A NE  1 
ATOM   1182 C  CZ  . ARG A  1  157 ? 24.080  4.596   19.104 1.00 37.44  ? 170 ARG A CZ  1 
ATOM   1183 N  NH1 . ARG A  1  157 ? 24.814  4.932   18.066 1.00 43.88  ? 170 ARG A NH1 1 
ATOM   1184 N  NH2 . ARG A  1  157 ? 23.986  5.406   20.148 1.00 38.80  ? 170 ARG A NH2 1 
ATOM   1185 N  N   . TYR A  1  158 ? 24.541  -2.400  19.726 1.00 33.16  ? 171 TYR A N   1 
ATOM   1186 C  CA  . TYR A  1  158 ? 25.552  -3.170  19.007 1.00 33.92  ? 171 TYR A CA  1 
ATOM   1187 C  C   . TYR A  1  158 ? 25.776  -4.567  19.581 1.00 34.44  ? 171 TYR A C   1 
ATOM   1188 O  O   . TYR A  1  158 ? 26.442  -5.372  18.932 1.00 35.36  ? 171 TYR A O   1 
ATOM   1189 C  CB  . TYR A  1  158 ? 26.887  -2.425  18.958 1.00 34.39  ? 171 TYR A CB  1 
ATOM   1190 C  CG  . TYR A  1  158 ? 26.780  -1.060  18.299 1.00 33.94  ? 171 TYR A CG  1 
ATOM   1191 C  CD1 . TYR A  1  158 ? 26.569  -0.939  16.926 1.00 39.51  ? 171 TYR A CD1 1 
ATOM   1192 C  CD2 . TYR A  1  158 ? 26.871  0.106   19.036 1.00 34.72  ? 171 TYR A CD2 1 
ATOM   1193 C  CE1 . TYR A  1  158 ? 26.439  0.300   16.323 1.00 36.44  ? 171 TYR A CE1 1 
ATOM   1194 C  CE2 . TYR A  1  158 ? 26.762  1.353   18.443 1.00 36.49  ? 171 TYR A CE2 1 
ATOM   1195 C  CZ  . TYR A  1  158 ? 26.543  1.449   17.083 1.00 38.90  ? 171 TYR A CZ  1 
ATOM   1196 O  OH  . TYR A  1  158 ? 26.411  2.693   16.533 1.00 44.65  ? 171 TYR A OH  1 
ATOM   1197 N  N   . GLY A  1  159 ? 25.229  -4.880  20.764 1.00 32.24  ? 172 GLY A N   1 
ATOM   1198 C  CA  . GLY A  1  159 ? 25.537  -6.140  21.414 1.00 31.14  ? 172 GLY A CA  1 
ATOM   1199 C  C   . GLY A  1  159 ? 24.310  -6.933  21.864 1.00 35.70  ? 172 GLY A C   1 
ATOM   1200 O  O   . GLY A  1  159 ? 24.430  -7.831  22.696 1.00 32.66  ? 172 GLY A O   1 
ATOM   1201 N  N   . GLY A  1  160 ? 23.129  -6.625  21.312 1.00 34.62  ? 173 GLY A N   1 
ATOM   1202 C  CA  . GLY A  1  160 ? 21.942  -7.392  21.653 1.00 31.48  ? 173 GLY A CA  1 
ATOM   1203 C  C   . GLY A  1  160 ? 21.525  -7.171  23.108 1.00 32.74  ? 173 GLY A C   1 
ATOM   1204 O  O   . GLY A  1  160 ? 20.794  -7.994  23.661 1.00 34.14  ? 173 GLY A O   1 
ATOM   1205 N  N   . GLY A  1  161 ? 21.947  -6.047  23.707 1.00 32.58  ? 174 GLY A N   1 
ATOM   1206 C  CA  . GLY A  1  161 ? 21.648  -5.752  25.110 1.00 34.93  ? 174 GLY A CA  1 
ATOM   1207 C  C   . GLY A  1  161 ? 22.768  -6.193  26.069 1.00 34.84  ? 174 GLY A C   1 
ATOM   1208 O  O   . GLY A  1  161 ? 22.648  -6.024  27.286 1.00 33.86  ? 174 GLY A O   1 
ATOM   1209 N  N   . PHE A  1  162 ? 23.866  -6.717  25.506 1.00 32.22  ? 175 PHE A N   1 
ATOM   1210 C  CA  . PHE A  1  162 ? 25.032  -7.135  26.262 1.00 31.59  ? 175 PHE A CA  1 
ATOM   1211 C  C   . PHE A  1  162 ? 26.273  -6.409  25.750 1.00 33.83  ? 175 PHE A C   1 
ATOM   1212 O  O   . PHE A  1  162 ? 26.300  -5.913  24.625 1.00 30.19  ? 175 PHE A O   1 
ATOM   1213 C  CB  . PHE A  1  162 ? 25.215  -8.644  26.106 1.00 31.99  ? 175 PHE A CB  1 
ATOM   1214 C  CG  . PHE A  1  162 ? 24.050  -9.484  26.598 1.00 32.98  ? 175 PHE A CG  1 
ATOM   1215 C  CD1 . PHE A  1  162 ? 22.955  -9.757  25.766 1.00 33.65  ? 175 PHE A CD1 1 
ATOM   1216 C  CD2 . PHE A  1  162 ? 24.054  -10.004 27.881 1.00 33.42  ? 175 PHE A CD2 1 
ATOM   1217 C  CE1 . PHE A  1  162 ? 21.895  -10.512 26.227 1.00 35.51  ? 175 PHE A CE1 1 
ATOM   1218 C  CE2 . PHE A  1  162 ? 22.986  -10.778 28.339 1.00 33.27  ? 175 PHE A CE2 1 
ATOM   1219 C  CZ  . PHE A  1  162 ? 21.905  -11.017 27.520 1.00 35.19  ? 175 PHE A CZ  1 
ATOM   1220 N  N   . TYR A  1  163 ? 27.308  -6.342  26.592 1.00 31.72  ? 176 TYR A N   1 
ATOM   1221 C  CA  . TYR A  1  163 ? 28.569  -5.749  26.197 1.00 29.96  ? 176 TYR A CA  1 
ATOM   1222 C  C   . TYR A  1  163 ? 29.448  -6.849  25.621 1.00 31.32  ? 176 TYR A C   1 
ATOM   1223 O  O   . TYR A  1  163 ? 29.746  -7.828  26.301 1.00 32.69  ? 176 TYR A O   1 
ATOM   1224 C  CB  . TYR A  1  163 ? 29.264  -5.069  27.377 1.00 30.30  ? 176 TYR A CB  1 
ATOM   1225 C  CG  . TYR A  1  163 ? 30.526  -4.289  27.035 1.00 30.26  ? 176 TYR A CG  1 
ATOM   1226 C  CD1 . TYR A  1  163 ? 30.459  -3.010  26.520 1.00 30.01  ? 176 TYR A CD1 1 
ATOM   1227 C  CD2 . TYR A  1  163 ? 31.784  -4.812  27.269 1.00 29.29  ? 176 TYR A CD2 1 
ATOM   1228 C  CE1 . TYR A  1  163 ? 31.600  -2.279  26.236 1.00 32.50  ? 176 TYR A CE1 1 
ATOM   1229 C  CE2 . TYR A  1  163 ? 32.934  -4.085  27.003 1.00 29.06  ? 176 TYR A CE2 1 
ATOM   1230 C  CZ  . TYR A  1  163 ? 32.850  -2.811  26.486 1.00 30.44  ? 176 TYR A CZ  1 
ATOM   1231 O  OH  . TYR A  1  163 ? 33.983  -2.093  26.203 1.00 28.74  ? 176 TYR A OH  1 
ATOM   1232 N  N   . ASN A  1  164 ? 29.850  -6.678  24.360 1.00 31.04  ? 177 ASN A N   1 
ATOM   1233 C  CA  . ASN A  1  164 ? 30.743  -7.629  23.715 1.00 32.82  ? 177 ASN A CA  1 
ATOM   1234 C  C   . ASN A  1  164 ? 31.763  -6.850  22.900 1.00 30.87  ? 177 ASN A C   1 
ATOM   1235 O  O   . ASN A  1  164 ? 31.789  -5.615  22.938 1.00 30.13  ? 177 ASN A O   1 
ATOM   1236 C  CB  . ASN A  1  164 ? 29.928  -8.668  22.954 1.00 35.53  ? 177 ASN A CB  1 
ATOM   1237 C  CG  . ASN A  1  164 ? 29.354  -8.167  21.644 1.00 34.66  ? 177 ASN A CG  1 
ATOM   1238 O  OD1 . ASN A  1  164 ? 29.625  -7.041  21.204 1.00 33.94  ? 177 ASN A OD1 1 
ATOM   1239 N  ND2 . ASN A  1  164 ? 28.550  -9.017  21.029 1.00 37.99  ? 177 ASN A ND2 1 
ATOM   1240 N  N   . LEU A  1  165 ? 32.622  -7.563  22.175 1.00 30.99  ? 178 LEU A N   1 
ATOM   1241 C  CA  . LEU A  1  165 ? 33.743  -6.901  21.520 1.00 32.87  ? 178 LEU A CA  1 
ATOM   1242 C  C   . LEU A  1  165 ? 33.286  -5.866  20.487 1.00 33.77  ? 178 LEU A C   1 
ATOM   1243 O  O   . LEU A  1  165 ? 33.937  -4.838  20.310 1.00 31.35  ? 178 LEU A O   1 
ATOM   1244 C  CB  . LEU A  1  165 ? 34.643  -7.964  20.907 1.00 39.00  ? 178 LEU A CB  1 
ATOM   1245 C  CG  . LEU A  1  165 ? 35.997  -7.470  20.401 1.00 43.18  ? 178 LEU A CG  1 
ATOM   1246 C  CD1 . LEU A  1  165 ? 36.859  -6.930  21.503 1.00 43.60  ? 178 LEU A CD1 1 
ATOM   1247 C  CD2 . LEU A  1  165 ? 36.731  -8.610  19.727 1.00 51.14  ? 178 LEU A CD2 1 
ATOM   1248 N  N   . THR A  1  166 ? 32.146  -6.104  19.824 1.00 34.42  ? 179 THR A N   1 
ATOM   1249 C  CA  . THR A  1  166 ? 31.627  -5.149  18.846 1.00 33.24  ? 179 THR A CA  1 
ATOM   1250 C  C   . THR A  1  166 ? 31.236  -3.849  19.548 1.00 31.02  ? 179 THR A C   1 
ATOM   1251 O  O   . THR A  1  166 ? 31.553  -2.755  19.086 1.00 33.29  ? 179 THR A O   1 
ATOM   1252 C  CB  . THR A  1  166 ? 30.432  -5.769  18.104 1.00 34.60  ? 179 THR A CB  1 
ATOM   1253 O  OG1 . THR A  1  166 ? 30.753  -7.105  17.710 1.00 34.27  ? 179 THR A OG1 1 
ATOM   1254 C  CG2 . THR A  1  166 ? 29.971  -4.923  16.930 1.00 34.79  ? 179 THR A CG2 1 
ATOM   1255 N  N   . VAL A  1  167 ? 30.579  -3.972  20.711 1.00 30.61  ? 180 VAL A N   1 
ATOM   1256 C  CA  . VAL A  1  167 ? 30.187  -2.810  21.491 1.00 31.85  ? 180 VAL A CA  1 
ATOM   1257 C  C   . VAL A  1  167 ? 31.426  -2.023  21.901 1.00 30.63  ? 180 VAL A C   1 
ATOM   1258 O  O   . VAL A  1  167 ? 31.453  -0.797  21.807 1.00 32.33  ? 180 VAL A O   1 
ATOM   1259 C  CB  . VAL A  1  167 ? 29.364  -3.204  22.738 1.00 32.11  ? 180 VAL A CB  1 
ATOM   1260 C  CG1 . VAL A  1  167 ? 28.857  -1.975  23.474 1.00 29.44  ? 180 VAL A CG1 1 
ATOM   1261 C  CG2 . VAL A  1  167 ? 28.199  -4.125  22.406 1.00 30.04  ? 180 VAL A CG2 1 
ATOM   1262 N  N   . ALA A  1  168 ? 32.466  -2.739  22.358 1.00 33.03  ? 181 ALA A N   1 
ATOM   1263 C  CA  . ALA A  1  168 ? 33.694  -2.115  22.830 1.00 30.40  ? 181 ALA A CA  1 
ATOM   1264 C  C   . ALA A  1  168 ? 34.293  -1.205  21.763 1.00 29.86  ? 181 ALA A C   1 
ATOM   1265 O  O   . ALA A  1  168 ? 34.687  -0.076  22.050 1.00 31.43  ? 181 ALA A O   1 
ATOM   1266 C  CB  . ALA A  1  168 ? 34.682  -3.189  23.243 1.00 33.58  ? 181 ALA A CB  1 
ATOM   1267 N  N   . GLY A  1  169 ? 34.351  -1.692  20.519 1.00 32.33  ? 182 GLY A N   1 
ATOM   1268 C  CA  . GLY A  1  169 ? 34.890  -0.898  19.426 1.00 33.04  ? 182 GLY A CA  1 
ATOM   1269 C  C   . GLY A  1  169 ? 34.122  0.409   19.244 1.00 34.26  ? 182 GLY A C   1 
ATOM   1270 O  O   . GLY A  1  169 ? 34.726  1.473   19.095 1.00 35.08  ? 182 GLY A O   1 
ATOM   1271 N  N   . GLU A  1  170 ? 32.784  0.314   19.260 1.00 35.77  ? 183 GLU A N   1 
ATOM   1272 C  CA  . GLU A  1  170 ? 31.935  1.472   19.024 1.00 33.81  ? 183 GLU A CA  1 
ATOM   1273 C  C   . GLU A  1  170 ? 32.013  2.431   20.209 1.00 35.02  ? 183 GLU A C   1 
ATOM   1274 O  O   . GLU A  1  170 ? 32.112  3.641   20.019 1.00 36.03  ? 183 GLU A O   1 
ATOM   1275 C  CB  . GLU A  1  170 ? 30.487  1.049   18.769 1.00 34.58  ? 183 GLU A CB  1 
ATOM   1276 C  CG  . GLU A  1  170 ? 30.299  0.202   17.518 1.00 38.18  ? 183 GLU A CG  1 
ATOM   1277 C  CD  . GLU A  1  170 ? 30.645  0.962   16.246 1.00 44.73  ? 183 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A  1  170 ? 30.697  2.215   16.197 1.00 45.99  ? 183 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A  1  170 ? 30.818  0.237   15.259 1.00 57.39  ? 183 GLU A OE2 1 
ATOM   1280 N  N   . LEU A  1  171 ? 31.978  1.900   21.438 1.00 33.50  ? 184 LEU A N   1 
ATOM   1281 C  CA  . LEU A  1  171 ? 31.914  2.762   22.609 1.00 33.73  ? 184 LEU A CA  1 
ATOM   1282 C  C   . LEU A  1  171 ? 33.217  3.536   22.775 1.00 32.50  ? 184 LEU A C   1 
ATOM   1283 O  O   . LEU A  1  171 ? 33.205  4.723   23.089 1.00 32.58  ? 184 LEU A O   1 
ATOM   1284 C  CB  . LEU A  1  171 ? 31.576  1.948   23.864 1.00 33.15  ? 184 LEU A CB  1 
ATOM   1285 C  CG  . LEU A  1  171 ? 31.440  2.749   25.164 1.00 34.60  ? 184 LEU A CG  1 
ATOM   1286 C  CD1 . LEU A  1  171 ? 30.320  3.784   25.075 1.00 33.80  ? 184 LEU A CD1 1 
ATOM   1287 C  CD2 . LEU A  1  171 ? 31.230  1.811   26.348 1.00 34.34  ? 184 LEU A CD2 1 
ATOM   1288 N  N   . ARG A  1  172 ? 34.346  2.858   22.585 1.00 32.45  ? 185 ARG A N   1 
ATOM   1289 C  CA  . ARG A  1  172 ? 35.647  3.486   22.765 1.00 33.32  ? 185 ARG A CA  1 
ATOM   1290 C  C   . ARG A  1  172 ? 35.757  4.718   21.870 1.00 33.10  ? 185 ARG A C   1 
ATOM   1291 O  O   . ARG A  1  172 ? 36.151  5.792   22.320 1.00 32.03  ? 185 ARG A O   1 
ATOM   1292 C  CB  . ARG A  1  172 ? 36.727  2.436   22.483 1.00 33.06  ? 185 ARG A CB  1 
ATOM   1293 C  CG  . ARG A  1  172 ? 38.138  2.920   22.194 1.00 35.04  ? 185 ARG A CG  1 
ATOM   1294 C  CD  . ARG A  1  172 ? 38.726  3.880   23.174 1.00 37.12  ? 185 ARG A CD  1 
ATOM   1295 N  NE  . ARG A  1  172 ? 38.586  3.482   24.579 1.00 37.05  ? 185 ARG A NE  1 
ATOM   1296 C  CZ  . ARG A  1  172 ? 38.161  4.265   25.545 1.00 39.92  ? 185 ARG A CZ  1 
ATOM   1297 N  NH1 . ARG A  1  172 ? 37.721  5.483   25.268 1.00 45.40  ? 185 ARG A NH1 1 
ATOM   1298 N  NH2 . ARG A  1  172 ? 38.178  3.833   26.792 1.00 39.96  ? 185 ARG A NH2 1 
ATOM   1299 N  N   . TYR A  1  173 ? 35.404  4.556   20.593 1.00 35.40  ? 186 TYR A N   1 
ATOM   1300 C  CA  . TYR A  1  173 ? 35.514  5.652   19.638 1.00 37.09  ? 186 TYR A CA  1 
ATOM   1301 C  C   . TYR A  1  173 ? 34.571  6.784   20.037 1.00 33.66  ? 186 TYR A C   1 
ATOM   1302 O  O   . TYR A  1  173 ? 34.959  7.948   20.049 1.00 38.34  ? 186 TYR A O   1 
ATOM   1303 C  CB  . TYR A  1  173 ? 35.201  5.115   18.236 1.00 38.63  ? 186 TYR A CB  1 
ATOM   1304 C  CG  . TYR A  1  173 ? 35.269  6.175   17.144 1.00 40.15  ? 186 TYR A CG  1 
ATOM   1305 C  CD1 . TYR A  1  173 ? 36.485  6.747   16.793 1.00 44.47  ? 186 TYR A CD1 1 
ATOM   1306 C  CD2 . TYR A  1  173 ? 34.130  6.591   16.459 1.00 42.83  ? 186 TYR A CD2 1 
ATOM   1307 C  CE1 . TYR A  1  173 ? 36.566  7.730   15.818 1.00 47.30  ? 186 TYR A CE1 1 
ATOM   1308 C  CE2 . TYR A  1  173 ? 34.200  7.552   15.462 1.00 47.75  ? 186 TYR A CE2 1 
ATOM   1309 C  CZ  . TYR A  1  173 ? 35.422  8.126   15.149 1.00 48.72  ? 186 TYR A CZ  1 
ATOM   1310 O  OH  . TYR A  1  173 ? 35.521  9.069   14.179 1.00 53.11  ? 186 TYR A OH  1 
ATOM   1311 N  N   . SER A  1  174 ? 33.324  6.430   20.384 1.00 36.06  ? 187 SER A N   1 
ATOM   1312 C  CA  . SER A  1  174 ? 32.330  7.440   20.695 1.00 34.97  ? 187 SER A CA  1 
ATOM   1313 C  C   . SER A  1  174 ? 32.754  8.234   21.927 1.00 35.52  ? 187 SER A C   1 
ATOM   1314 O  O   . SER A  1  174 ? 32.540  9.445   21.986 1.00 34.21  ? 187 SER A O   1 
ATOM   1315 C  CB  . SER A  1  174 ? 30.960  6.829   20.841 1.00 35.89  ? 187 SER A CB  1 
ATOM   1316 O  OG  . SER A  1  174 ? 30.026  7.829   21.201 1.00 39.13  ? 187 SER A OG  1 
ATOM   1317 N  N   . ARG A  1  175 ? 33.390  7.573   22.902 1.00 33.41  ? 188 ARG A N   1 
ATOM   1318 C  CA  . ARG A  1  175 ? 33.834  8.264   24.108 1.00 32.28  ? 188 ARG A CA  1 
ATOM   1319 C  C   . ARG A  1  175 ? 34.980  9.227   23.778 1.00 29.87  ? 188 ARG A C   1 
ATOM   1320 O  O   . ARG A  1  175 ? 35.050  10.316  24.332 1.00 29.44  ? 188 ARG A O   1 
ATOM   1321 C  CB  . ARG A  1  175 ? 34.193  7.287   25.240 1.00 32.21  ? 188 ARG A CB  1 
ATOM   1322 C  CG  . ARG A  1  175 ? 32.992  6.559   25.828 1.00 32.38  ? 188 ARG A CG  1 
ATOM   1323 C  CD  . ARG A  1  175 ? 32.090  7.466   26.648 1.00 30.90  ? 188 ARG A CD  1 
ATOM   1324 N  NE  . ARG A  1  175 ? 32.814  7.988   27.806 1.00 30.74  ? 188 ARG A NE  1 
ATOM   1325 C  CZ  . ARG A  1  175 ? 33.154  9.244   28.057 1.00 32.42  ? 188 ARG A CZ  1 
ATOM   1326 N  NH1 . ARG A  1  175 ? 32.675  10.246  27.331 1.00 33.97  ? 188 ARG A NH1 1 
ATOM   1327 N  NH2 . ARG A  1  175 ? 33.953  9.517   29.066 1.00 31.71  ? 188 ARG A NH2 1 
ATOM   1328 N  N   . ILE A  1  176 ? 35.892  8.830   22.890 1.00 32.99  ? 189 ILE A N   1 
ATOM   1329 C  CA  . ILE A  1  176 ? 36.925  9.742   22.408 1.00 32.32  ? 189 ILE A CA  1 
ATOM   1330 C  C   . ILE A  1  176 ? 36.269  10.994  21.795 1.00 31.14  ? 189 ILE A C   1 
ATOM   1331 O  O   . ILE A  1  176 ? 36.633  12.120  22.142 1.00 33.44  ? 189 ILE A O   1 
ATOM   1332 C  CB  . ILE A  1  176 ? 37.844  9.019   21.410 1.00 35.13  ? 189 ILE A CB  1 
ATOM   1333 C  CG1 . ILE A  1  176 ? 38.683  7.932   22.093 1.00 36.42  ? 189 ILE A CG1 1 
ATOM   1334 C  CG2 . ILE A  1  176 ? 38.731  10.013  20.653 1.00 34.99  ? 189 ILE A CG2 1 
ATOM   1335 C  CD1 . ILE A  1  176 ? 39.326  6.952   21.128 1.00 36.69  ? 189 ILE A CD1 1 
ATOM   1336 N  N   . GLN A  1  177 ? 35.260  10.797  20.937 1.00 33.65  ? 190 GLN A N   1 
ATOM   1337 C  CA  . GLN A  1  177 ? 34.555  11.914  20.303 1.00 36.33  ? 190 GLN A CA  1 
ATOM   1338 C  C   . GLN A  1  177 ? 33.864  12.812  21.327 1.00 38.57  ? 190 GLN A C   1 
ATOM   1339 O  O   . GLN A  1  177 ? 33.936  14.030  21.205 1.00 37.24  ? 190 GLN A O   1 
ATOM   1340 C  CB  . GLN A  1  177 ? 33.564  11.411  19.249 1.00 38.00  ? 190 GLN A CB  1 
ATOM   1341 C  CG  . GLN A  1  177 ? 34.243  10.716  18.074 1.00 39.03  ? 190 GLN A CG  1 
ATOM   1342 C  CD  . GLN A  1  177 ? 35.190  11.624  17.314 1.00 50.54  ? 190 GLN A CD  1 
ATOM   1343 O  OE1 . GLN A  1  177 ? 35.107  12.861  17.366 1.00 51.94  ? 190 GLN A OE1 1 
ATOM   1344 N  NE2 . GLN A  1  177 ? 36.109  11.010  16.584 1.00 55.16  ? 190 GLN A NE2 1 
ATOM   1345 N  N   . ASP A  1  178 ? 33.222  12.233  22.353 1.00 39.62  ? 191 ASP A N   1 
ATOM   1346 C  CA  . ASP A  1  178 ? 32.614  13.032  23.413 1.00 37.11  ? 191 ASP A CA  1 
ATOM   1347 C  C   . ASP A  1  178 ? 33.654  13.957  24.033 1.00 36.61  ? 191 ASP A C   1 
ATOM   1348 O  O   . ASP A  1  178 ? 33.386  15.134  24.270 1.00 39.66  ? 191 ASP A O   1 
ATOM   1349 C  CB  . ASP A  1  178 ? 32.049  12.198  24.556 1.00 37.95  ? 191 ASP A CB  1 
ATOM   1350 C  CG  . ASP A  1  178 ? 30.889  11.270  24.236 1.00 46.60  ? 191 ASP A CG  1 
ATOM   1351 O  OD1 . ASP A  1  178 ? 30.240  11.480  23.189 1.00 47.54  ? 191 ASP A OD1 1 
ATOM   1352 O  OD2 . ASP A  1  178 ? 30.635  10.344  25.057 1.00 44.99  ? 191 ASP A OD2 1 
ATOM   1353 N  N   . SER A  1  179 ? 34.835  13.415  24.359 1.00 36.03  ? 192 SER A N   1 
ATOM   1354 C  CA  . SER A  1  179 ? 35.862  14.208  25.026 1.00 35.27  ? 192 SER A CA  1 
ATOM   1355 C  C   . SER A  1  179 ? 36.421  15.284  24.079 1.00 34.77  ? 192 SER A C   1 
ATOM   1356 O  O   . SER A  1  179 ? 36.716  16.394  24.506 1.00 36.03  ? 192 SER A O   1 
ATOM   1357 C  CB  . SER A  1  179 ? 36.969  13.318  25.608 1.00 37.67  ? 192 SER A CB  1 
ATOM   1358 O  OG  . SER A  1  179 ? 36.575  12.693  26.828 1.00 35.50  ? 192 SER A OG  1 
ATOM   1359 N  N   . ILE A  1  180 ? 36.595  14.965  22.793 1.00 38.36  ? 193 ILE A N   1 
ATOM   1360 C  CA  . ILE A  1  180 ? 37.061  15.959  21.833 1.00 40.74  ? 193 ILE A CA  1 
ATOM   1361 C  C   . ILE A  1  180 ? 36.098  17.153  21.834 1.00 42.00  ? 193 ILE A C   1 
ATOM   1362 O  O   . ILE A  1  180 ? 36.530  18.299  21.935 1.00 38.90  ? 193 ILE A O   1 
ATOM   1363 C  CB  . ILE A  1  180 ? 37.207  15.360  20.423 1.00 39.94  ? 193 ILE A CB  1 
ATOM   1364 C  CG1 . ILE A  1  180 ? 38.403  14.408  20.341 1.00 38.02  ? 193 ILE A CG1 1 
ATOM   1365 C  CG2 . ILE A  1  180 ? 37.313  16.478  19.375 1.00 43.22  ? 193 ILE A CG2 1 
ATOM   1366 C  CD1 . ILE A  1  180 ? 38.471  13.605  19.056 1.00 37.66  ? 193 ILE A CD1 1 
ATOM   1367 N  N   . ALA A  1  181 ? 34.798  16.853  21.776 1.00 40.86  ? 194 ALA A N   1 
ATOM   1368 C  CA  . ALA A  1  181 ? 33.751  17.854  21.648 1.00 44.68  ? 194 ALA A CA  1 
ATOM   1369 C  C   . ALA A  1  181 ? 33.550  18.667  22.923 1.00 45.20  ? 194 ALA A C   1 
ATOM   1370 O  O   . ALA A  1  181 ? 33.097  19.799  22.822 1.00 46.85  ? 194 ALA A O   1 
ATOM   1371 C  CB  . ALA A  1  181 ? 32.458  17.187  21.227 1.00 42.66  ? 194 ALA A CB  1 
ATOM   1372 N  N   . THR A  1  182 ? 33.882  18.136  24.110 1.00 39.82  ? 195 THR A N   1 
ATOM   1373 C  CA  . THR A  1  182 ? 33.431  18.778  25.339 1.00 38.63  ? 195 THR A CA  1 
ATOM   1374 C  C   . THR A  1  182 ? 34.566  19.119  26.296 1.00 39.01  ? 195 THR A C   1 
ATOM   1375 O  O   . THR A  1  182 ? 34.341  19.835  27.268 1.00 36.86  ? 195 THR A O   1 
ATOM   1376 C  CB  . THR A  1  182 ? 32.393  17.892  26.038 1.00 46.16  ? 195 THR A CB  1 
ATOM   1377 O  OG1 . THR A  1  182 ? 33.024  16.664  26.420 1.00 41.03  ? 195 THR A OG1 1 
ATOM   1378 C  CG2 . THR A  1  182 ? 31.184  17.599  25.162 1.00 44.83  ? 195 THR A CG2 1 
ATOM   1379 N  N   . ASN A  1  183 ? 35.761  18.565  26.088 1.00 39.16  ? 196 ASN A N   1 
ATOM   1380 C  CA  . ASN A  1  183 ? 36.830  18.726  27.065 1.00 39.97  ? 196 ASN A CA  1 
ATOM   1381 C  C   . ASN A  1  183 ? 37.997  19.432  26.386 1.00 38.91  ? 196 ASN A C   1 
ATOM   1382 O  O   . ASN A  1  183 ? 38.717  18.829  25.593 1.00 37.91  ? 196 ASN A O   1 
ATOM   1383 C  CB  . ASN A  1  183 ? 37.265  17.381  27.647 1.00 37.34  ? 196 ASN A CB  1 
ATOM   1384 C  CG  . ASN A  1  183 ? 38.406  17.491  28.631 1.00 39.57  ? 196 ASN A CG  1 
ATOM   1385 O  OD1 . ASN A  1  183 ? 38.902  18.590  28.911 1.00 36.14  ? 196 ASN A OD1 1 
ATOM   1386 N  ND2 . ASN A  1  183 ? 38.829  16.362  29.189 1.00 38.26  ? 196 ASN A ND2 1 
ATOM   1387 N  N   . PRO A  1  184 ? 38.217  20.730  26.667 1.00 41.54  ? 197 PRO A N   1 
ATOM   1388 C  CA  . PRO A  1  184 ? 39.286  21.476  26.002 1.00 43.15  ? 197 PRO A CA  1 
ATOM   1389 C  C   . PRO A  1  184 ? 40.691  21.044  26.415 1.00 41.95  ? 197 PRO A C   1 
ATOM   1390 O  O   . PRO A  1  184 ? 41.652  21.371  25.723 1.00 46.68  ? 197 PRO A O   1 
ATOM   1391 C  CB  . PRO A  1  184 ? 38.972  22.930  26.400 1.00 43.94  ? 197 PRO A CB  1 
ATOM   1392 C  CG  . PRO A  1  184 ? 38.324  22.802  27.748 1.00 45.12  ? 197 PRO A CG  1 
ATOM   1393 C  CD  . PRO A  1  184 ? 37.480  21.535  27.650 1.00 44.41  ? 197 PRO A CD  1 
ATOM   1394 N  N   . GLU A  1  185 ? 40.798  20.306  27.532 1.00 45.09  ? 198 GLU A N   1 
ATOM   1395 C  CA  . GLU A  1  185 ? 42.069  19.785  28.026 1.00 44.11  ? 198 GLU A CA  1 
ATOM   1396 C  C   . GLU A  1  185 ? 42.248  18.302  27.689 1.00 41.39  ? 198 GLU A C   1 
ATOM   1397 O  O   . GLU A  1  185 ? 43.178  17.677  28.184 1.00 44.77  ? 198 GLU A O   1 
ATOM   1398 C  CB  . GLU A  1  185 ? 42.179  19.959  29.542 1.00 46.13  ? 198 GLU A CB  1 
ATOM   1399 C  CG  . GLU A  1  185 ? 42.161  21.415  29.998 1.00 52.10  ? 198 GLU A CG  1 
ATOM   1400 C  CD  . GLU A  1  185 ? 42.197  21.595  31.503 1.00 55.47  ? 198 GLU A CD  1 
ATOM   1401 O  OE1 . GLU A  1  185 ? 42.338  20.571  32.192 1.00 56.62  ? 198 GLU A OE1 1 
ATOM   1402 O  OE2 . GLU A  1  185 ? 42.087  22.738  31.991 1.00 63.84  ? 198 GLU A OE2 1 
ATOM   1403 N  N   . PHE A  1  186 ? 41.395  17.750  26.823 1.00 39.48  ? 199 PHE A N   1 
ATOM   1404 C  CA  . PHE A  1  186 ? 41.442  16.337  26.470 1.00 35.32  ? 199 PHE A CA  1 
ATOM   1405 C  C   . PHE A  1  186 ? 42.826  15.924  25.969 1.00 40.00  ? 199 PHE A C   1 
ATOM   1406 O  O   . PHE A  1  186 ? 43.343  16.493  25.012 1.00 41.23  ? 199 PHE A O   1 
ATOM   1407 C  CB  . PHE A  1  186 ? 40.424  16.045  25.370 1.00 35.11  ? 199 PHE A CB  1 
ATOM   1408 C  CG  . PHE A  1  186 ? 40.385  14.608  24.873 1.00 35.99  ? 199 PHE A CG  1 
ATOM   1409 C  CD1 . PHE A  1  186 ? 40.411  13.536  25.761 1.00 34.42  ? 199 PHE A CD1 1 
ATOM   1410 C  CD2 . PHE A  1  186 ? 40.345  14.328  23.515 1.00 35.30  ? 199 PHE A CD2 1 
ATOM   1411 C  CE1 . PHE A  1  186 ? 40.361  12.236  25.298 1.00 32.96  ? 199 PHE A CE1 1 
ATOM   1412 C  CE2 . PHE A  1  186 ? 40.319  13.023  23.056 1.00 38.96  ? 199 PHE A CE2 1 
ATOM   1413 C  CZ  . PHE A  1  186 ? 40.326  11.976  23.949 1.00 36.50  ? 199 PHE A CZ  1 
ATOM   1414 N  N   . GLN A  1  187 ? 43.384  14.886  26.604 1.00 40.06  ? 200 GLN A N   1 
ATOM   1415 C  CA  . GLN A  1  187 ? 44.649  14.269  26.234 1.00 40.49  ? 200 GLN A CA  1 
ATOM   1416 C  C   . GLN A  1  187 ? 44.394  12.781  26.028 1.00 37.64  ? 200 GLN A C   1 
ATOM   1417 O  O   . GLN A  1  187 ? 43.674  12.155  26.804 1.00 38.61  ? 200 GLN A O   1 
ATOM   1418 C  CB  . GLN A  1  187 ? 45.683  14.448  27.347 1.00 42.10  ? 200 GLN A CB  1 
ATOM   1419 C  CG  . GLN A  1  187 ? 46.170  15.883  27.509 1.00 47.91  ? 200 GLN A CG  1 
ATOM   1420 C  CD  . GLN A  1  187 ? 47.125  16.268  26.403 1.00 53.38  ? 200 GLN A CD  1 
ATOM   1421 O  OE1 . GLN A  1  187 ? 48.276  15.817  26.383 1.00 61.94  ? 200 GLN A OE1 1 
ATOM   1422 N  NE2 . GLN A  1  187 ? 46.655  17.060  25.451 1.00 49.01  ? 200 GLN A NE2 1 
ATOM   1423 N  N   . PHE A  1  188 ? 44.981  12.222  24.973 1.00 37.01  ? 201 PHE A N   1 
ATOM   1424 C  CA  . PHE A  1  188 ? 44.833  10.812  24.677 1.00 33.11  ? 201 PHE A CA  1 
ATOM   1425 C  C   . PHE A  1  188 ? 46.122  10.294  24.059 1.00 33.11  ? 201 PHE A C   1 
ATOM   1426 O  O   . PHE A  1  188 ? 46.157  9.877   22.906 1.00 37.38  ? 201 PHE A O   1 
ATOM   1427 C  CB  . PHE A  1  188 ? 43.619  10.633  23.775 1.00 33.53  ? 201 PHE A CB  1 
ATOM   1428 C  CG  . PHE A  1  188 ? 43.025  9.234   23.786 1.00 31.14  ? 201 PHE A CG  1 
ATOM   1429 C  CD1 . PHE A  1  188 ? 42.355  8.770   24.902 1.00 34.20  ? 201 PHE A CD1 1 
ATOM   1430 C  CD2 . PHE A  1  188 ? 43.075  8.432   22.666 1.00 34.11  ? 201 PHE A CD2 1 
ATOM   1431 C  CE1 . PHE A  1  188 ? 41.800  7.503   24.919 1.00 35.08  ? 201 PHE A CE1 1 
ATOM   1432 C  CE2 . PHE A  1  188 ? 42.506  7.168   22.682 1.00 36.05  ? 201 PHE A CE2 1 
ATOM   1433 C  CZ  . PHE A  1  188 ? 41.871  6.708   23.804 1.00 35.98  ? 201 PHE A CZ  1 
ATOM   1434 N  N   . LYS A  1  189 ? 47.179  10.289  24.863 1.00 35.98  ? 202 LYS A N   1 
ATOM   1435 C  CA  . LYS A  1  189 ? 48.495  9.916   24.374 1.00 38.62  ? 202 LYS A CA  1 
ATOM   1436 C  C   . LYS A  1  189 ? 49.286  9.193   25.465 1.00 36.44  ? 202 LYS A C   1 
ATOM   1437 O  O   . LYS A  1  189 ? 48.835  9.060   26.598 1.00 34.20  ? 202 LYS A O   1 
ATOM   1438 C  CB  . LYS A  1  189 ? 49.189  11.204  23.912 1.00 39.57  ? 202 LYS A CB  1 
ATOM   1439 C  CG  . LYS A  1  189 ? 49.422  12.216  25.018 1.00 43.33  ? 202 LYS A CG  1 
ATOM   1440 C  CD  . LYS A  1  189 ? 50.306  13.388  24.617 1.00 47.67  ? 202 LYS A CD  1 
ATOM   1441 C  CE  . LYS A  1  189 ? 49.601  14.311  23.686 1.00 51.83  ? 202 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A  1  189 ? 50.304  15.580  23.509 1.00 57.34  ? 202 LYS A NZ  1 
ATOM   1443 N  N   . ASN A  1  190 ? 50.486  8.728   25.099 1.00 36.56  ? 203 ASN A N   1 
ATOM   1444 C  CA  . ASN A  1  190 ? 51.399  8.059   26.014 1.00 36.06  ? 203 ASN A CA  1 
ATOM   1445 C  C   . ASN A  1  190 ? 50.659  6.937   26.759 1.00 32.63  ? 203 ASN A C   1 
ATOM   1446 O  O   . ASN A  1  190 ? 50.055  6.065   26.139 1.00 36.53  ? 203 ASN A O   1 
ATOM   1447 C  CB  . ASN A  1  190 ? 52.118  9.115   26.847 1.00 36.69  ? 203 ASN A CB  1 
ATOM   1448 C  CG  . ASN A  1  190 ? 53.015  9.964   25.966 1.00 41.85  ? 203 ASN A CG  1 
ATOM   1449 O  OD1 . ASN A  1  190 ? 53.759  9.429   25.129 1.00 41.61  ? 203 ASN A OD1 1 
ATOM   1450 N  ND2 . ASN A  1  190 ? 52.958  11.275  26.134 1.00 45.45  ? 203 ASN A ND2 1 
ATOM   1451 N  N   . VAL A  1  191 ? 50.701  6.951   28.089 1.00 33.51  ? 204 VAL A N   1 
ATOM   1452 C  CA  . VAL A  1  191 ? 50.158  5.840   28.852 1.00 33.87  ? 204 VAL A CA  1 
ATOM   1453 C  C   . VAL A  1  191 ? 48.681  5.648   28.506 1.00 32.47  ? 204 VAL A C   1 
ATOM   1454 O  O   . VAL A  1  191 ? 48.225  4.542   28.268 1.00 32.48  ? 204 VAL A O   1 
ATOM   1455 C  CB  . VAL A  1  191 ? 50.348  6.035   30.368 1.00 36.31  ? 204 VAL A CB  1 
ATOM   1456 C  CG1 . VAL A  1  191 ? 49.630  4.942   31.165 1.00 37.82  ? 204 VAL A CG1 1 
ATOM   1457 C  CG2 . VAL A  1  191 ? 51.827  6.077   30.755 1.00 37.76  ? 204 VAL A CG2 1 
ATOM   1458 N  N   . ARG A  1  192 ? 47.918  6.733   28.513 1.00 33.62  ? 205 ARG A N   1 
ATOM   1459 C  CA  . ARG A  1  192 ? 46.474  6.646   28.404 1.00 30.31  ? 205 ARG A CA  1 
ATOM   1460 C  C   . ARG A  1  192 ? 46.066  6.016   27.087 1.00 30.54  ? 205 ARG A C   1 
ATOM   1461 O  O   . ARG A  1  192 ? 45.099  5.261   27.041 1.00 32.20  ? 205 ARG A O   1 
ATOM   1462 C  CB  . ARG A  1  192 ? 45.826  8.029   28.530 1.00 33.32  ? 205 ARG A CB  1 
ATOM   1463 C  CG  . ARG A  1  192 ? 44.305  7.988   28.479 1.00 33.28  ? 205 ARG A CG  1 
ATOM   1464 C  CD  . ARG A  1  192 ? 43.744  6.976   29.467 1.00 32.60  ? 205 ARG A CD  1 
ATOM   1465 N  NE  . ARG A  1  192 ? 42.284  6.915   29.426 1.00 33.23  ? 205 ARG A NE  1 
ATOM   1466 C  CZ  . ARG A  1  192 ? 41.548  5.877   29.807 1.00 35.89  ? 205 ARG A CZ  1 
ATOM   1467 N  NH1 . ARG A  1  192 ? 42.122  4.788   30.312 1.00 34.69  ? 205 ARG A NH1 1 
ATOM   1468 N  NH2 . ARG A  1  192 ? 40.231  5.929   29.681 1.00 32.57  ? 205 ARG A NH2 1 
ATOM   1469 N  N   . PHE A  1  193 ? 46.786  6.330   26.006 1.00 33.36  ? 206 PHE A N   1 
ATOM   1470 C  CA  . PHE A  1  193 ? 46.418  5.823   24.704 1.00 33.86  ? 206 PHE A CA  1 
ATOM   1471 C  C   . PHE A  1  193 ? 46.468  4.295   24.733 1.00 36.60  ? 206 PHE A C   1 
ATOM   1472 O  O   . PHE A  1  193 ? 45.608  3.626   24.166 1.00 37.78  ? 206 PHE A O   1 
ATOM   1473 C  CB  . PHE A  1  193 ? 47.318  6.397   23.607 1.00 37.12  ? 206 PHE A CB  1 
ATOM   1474 C  CG  . PHE A  1  193 ? 46.996  5.827   22.240 1.00 36.76  ? 206 PHE A CG  1 
ATOM   1475 C  CD1 . PHE A  1  193 ? 45.903  6.287   21.523 1.00 39.17  ? 206 PHE A CD1 1 
ATOM   1476 C  CD2 . PHE A  1  193 ? 47.780  4.832   21.684 1.00 39.02  ? 206 PHE A CD2 1 
ATOM   1477 C  CE1 . PHE A  1  193 ? 45.595  5.745   20.286 1.00 40.58  ? 206 PHE A CE1 1 
ATOM   1478 C  CE2 . PHE A  1  193 ? 47.471  4.295   20.450 1.00 41.42  ? 206 PHE A CE2 1 
ATOM   1479 C  CZ  . PHE A  1  193 ? 46.373  4.749   19.755 1.00 42.70  ? 206 PHE A CZ  1 
ATOM   1480 N  N   . ILE A  1  194 ? 47.466  3.742   25.426 1.00 34.88  ? 207 ILE A N   1 
ATOM   1481 C  CA  . ILE A  1  194 ? 47.639  2.298   25.474 1.00 33.97  ? 207 ILE A CA  1 
ATOM   1482 C  C   . ILE A  1  194 ? 46.611  1.680   26.425 1.00 34.99  ? 207 ILE A C   1 
ATOM   1483 O  O   . ILE A  1  194 ? 45.935  0.737   26.042 1.00 33.80  ? 207 ILE A O   1 
ATOM   1484 C  CB  . ILE A  1  194 ? 49.105  1.963   25.805 1.00 36.19  ? 207 ILE A CB  1 
ATOM   1485 C  CG1 . ILE A  1  194 ? 50.009  2.474   24.654 1.00 44.29  ? 207 ILE A CG1 1 
ATOM   1486 C  CG2 . ILE A  1  194 ? 49.283  0.471   26.071 1.00 35.50  ? 207 ILE A CG2 1 
ATOM   1487 C  CD1 . ILE A  1  194 ? 51.492  2.354   24.890 1.00 58.16  ? 207 ILE A CD1 1 
ATOM   1488 N  N   . THR A  1  195 ? 46.454  2.234   27.636 1.00 34.97  ? 208 THR A N   1 
ATOM   1489 C  CA  . THR A  1  195 ? 45.596  1.627   28.647 1.00 34.36  ? 208 THR A CA  1 
ATOM   1490 C  C   . THR A  1  195 ? 44.121  1.731   28.260 1.00 34.39  ? 208 THR A C   1 
ATOM   1491 O  O   . THR A  1  195 ? 43.321  0.899   28.673 1.00 36.15  ? 208 THR A O   1 
ATOM   1492 C  CB  . THR A  1  195 ? 45.831  2.235   30.028 1.00 36.26  ? 208 THR A CB  1 
ATOM   1493 O  OG1 . THR A  1  195 ? 45.443  3.606   29.985 1.00 36.74  ? 208 THR A OG1 1 
ATOM   1494 C  CG2 . THR A  1  195 ? 47.262  2.092   30.492 1.00 38.39  ? 208 THR A CG2 1 
ATOM   1495 N  N   . ALA A  1  196 ? 43.743  2.732   27.461 1.00 33.88  ? 209 ALA A N   1 
ATOM   1496 C  CA  . ALA A  1  196 ? 42.341  2.942   27.124 1.00 33.33  ? 209 ALA A CA  1 
ATOM   1497 C  C   . ALA A  1  196 ? 41.767  1.816   26.268 1.00 37.98  ? 209 ALA A C   1 
ATOM   1498 O  O   . ALA A  1  196 ? 40.558  1.621   26.280 1.00 39.66  ? 209 ALA A O   1 
ATOM   1499 C  CB  . ALA A  1  196 ? 42.155  4.273   26.437 1.00 33.58  ? 209 ALA A CB  1 
ATOM   1500 N  N   . TYR A  1  197 ? 42.599  1.118   25.482 1.00 34.43  ? 210 TYR A N   1 
ATOM   1501 C  CA  . TYR A  1  197 ? 42.103  0.043   24.632 1.00 33.18  ? 210 TYR A CA  1 
ATOM   1502 C  C   . TYR A  1  197 ? 41.964  -1.222  25.480 1.00 33.58  ? 210 TYR A C   1 
ATOM   1503 O  O   . TYR A  1  197 ? 40.930  -1.896  25.443 1.00 32.58  ? 210 TYR A O   1 
ATOM   1504 C  CB  . TYR A  1  197 ? 42.951  -0.037  23.345 1.00 34.52  ? 210 TYR A CB  1 
ATOM   1505 C  CG  . TYR A  1  197 ? 42.593  1.111   22.411 1.00 33.57  ? 210 TYR A CG  1 
ATOM   1506 C  CD1 . TYR A  1  197 ? 41.519  1.012   21.528 1.00 34.29  ? 210 TYR A CD1 1 
ATOM   1507 C  CD2 . TYR A  1  197 ? 43.230  2.336   22.506 1.00 36.30  ? 210 TYR A CD2 1 
ATOM   1508 C  CE1 . TYR A  1  197 ? 41.137  2.074   20.727 1.00 32.92  ? 210 TYR A CE1 1 
ATOM   1509 C  CE2 . TYR A  1  197 ? 42.862  3.413   21.712 1.00 36.79  ? 210 TYR A CE2 1 
ATOM   1510 C  CZ  . TYR A  1  197 ? 41.811  3.282   20.824 1.00 35.80  ? 210 TYR A CZ  1 
ATOM   1511 O  OH  . TYR A  1  197 ? 41.454  4.361   20.079 1.00 35.29  ? 210 TYR A OH  1 
ATOM   1512 N  N   . GLY A  1  198 ? 42.972  -1.521  26.300 1.00 32.05  ? 211 GLY A N   1 
ATOM   1513 C  CA  . GLY A  1  198 ? 42.903  -2.673  27.199 1.00 33.66  ? 211 GLY A CA  1 
ATOM   1514 C  C   . GLY A  1  198 ? 41.702  -2.629  28.150 1.00 30.41  ? 211 GLY A C   1 
ATOM   1515 O  O   . GLY A  1  198 ? 41.012  -3.628  28.351 1.00 29.02  ? 211 GLY A O   1 
ATOM   1516 N  N   . GLU A  1  199 ? 41.418  -1.446  28.709 1.00 31.38  ? 212 GLU A N   1 
ATOM   1517 C  CA  A GLU A  1  199 ? 40.355  -1.334  29.695 0.50 31.27  ? 212 GLU A CA  1 
ATOM   1518 C  CA  B GLU A  1  199 ? 40.351  -1.301  29.688 0.50 31.16  ? 212 GLU A CA  1 
ATOM   1519 C  C   . GLU A  1  199 ? 39.001  -1.658  29.058 1.00 30.38  ? 212 GLU A C   1 
ATOM   1520 O  O   . GLU A  1  199 ? 38.091  -2.102  29.755 1.00 31.58  ? 212 GLU A O   1 
ATOM   1521 C  CB  A GLU A  1  199 ? 40.413  0.027   30.389 0.50 31.68  ? 212 GLU A CB  1 
ATOM   1522 C  CB  B GLU A  1  199 ? 40.352  0.104   30.308 0.50 31.39  ? 212 GLU A CB  1 
ATOM   1523 C  CG  A GLU A  1  199 ? 41.558  0.113   31.396 0.50 32.03  ? 212 GLU A CG  1 
ATOM   1524 C  CG  B GLU A  1  199 ? 39.629  1.169   29.481 0.50 31.48  ? 212 GLU A CG  1 
ATOM   1525 C  CD  A GLU A  1  199 ? 41.967  1.510   31.787 0.50 31.08  ? 212 GLU A CD  1 
ATOM   1526 C  CD  B GLU A  1  199 ? 39.567  2.569   30.086 0.50 29.36  ? 212 GLU A CD  1 
ATOM   1527 O  OE1 A GLU A  1  199 ? 41.206  2.451   31.467 0.50 32.29  ? 212 GLU A OE1 1 
ATOM   1528 O  OE1 B GLU A  1  199 ? 40.192  2.830   31.122 0.50 29.40  ? 212 GLU A OE1 1 
ATOM   1529 O  OE2 A GLU A  1  199 ? 43.047  1.646   32.389 0.50 34.06  ? 212 GLU A OE2 1 
ATOM   1530 O  OE2 B GLU A  1  199 ? 38.900  3.433   29.511 0.50 27.76  ? 212 GLU A OE2 1 
ATOM   1531 N  N   . THR A  1  200 ? 38.860  -1.497  27.726 1.00 30.80  ? 213 THR A N   1 
ATOM   1532 C  CA  . THR A  1  200 ? 37.556  -1.719  27.107 1.00 30.64  ? 213 THR A CA  1 
ATOM   1533 C  C   . THR A  1  200 ? 37.289  -3.206  26.881 1.00 29.68  ? 213 THR A C   1 
ATOM   1534 O  O   . THR A  1  200 ? 36.131  -3.573  26.684 1.00 30.27  ? 213 THR A O   1 
ATOM   1535 C  CB  . THR A  1  200 ? 37.370  -0.942  25.799 1.00 37.05  ? 213 THR A CB  1 
ATOM   1536 O  OG1 . THR A  1  200 ? 38.152  -1.552  24.789 1.00 42.24  ? 213 THR A OG1 1 
ATOM   1537 C  CG2 . THR A  1  200 ? 37.770  0.509   25.934 1.00 39.04  ? 213 THR A CG2 1 
ATOM   1538 N  N   . VAL A  1  201 ? 38.324  -4.062  26.940 1.00 27.88  ? 214 VAL A N   1 
ATOM   1539 C  CA  . VAL A  1  201 ? 38.110  -5.498  26.809 1.00 28.41  ? 214 VAL A CA  1 
ATOM   1540 C  C   . VAL A  1  201 ? 38.165  -6.211  28.158 1.00 27.89  ? 214 VAL A C   1 
ATOM   1541 O  O   . VAL A  1  201 ? 37.687  -7.340  28.264 1.00 28.73  ? 214 VAL A O   1 
ATOM   1542 C  CB  . VAL A  1  201 ? 39.068  -6.149  25.799 1.00 29.27  ? 214 VAL A CB  1 
ATOM   1543 C  CG1 . VAL A  1  201 ? 38.843  -5.572  24.409 1.00 28.93  ? 214 VAL A CG1 1 
ATOM   1544 C  CG2 . VAL A  1  201 ? 40.537  -6.028  26.199 1.00 29.51  ? 214 VAL A CG2 1 
ATOM   1545 N  N   . PHE A  1  202 ? 38.699  -5.571  29.202 1.00 28.91  ? 215 PHE A N   1 
ATOM   1546 C  CA  . PHE A  1  202 ? 38.724  -6.220  30.509 1.00 29.31  ? 215 PHE A CA  1 
ATOM   1547 C  C   . PHE A  1  202 ? 37.323  -6.682  30.920 1.00 28.73  ? 215 PHE A C   1 
ATOM   1548 O  O   . PHE A  1  202 ? 37.168  -7.756  31.480 1.00 29.42  ? 215 PHE A O   1 
ATOM   1549 C  CB  . PHE A  1  202 ? 39.345  -5.363  31.613 1.00 27.22  ? 215 PHE A CB  1 
ATOM   1550 C  CG  . PHE A  1  202 ? 40.835  -5.091  31.457 1.00 29.74  ? 215 PHE A CG  1 
ATOM   1551 C  CD1 . PHE A  1  202 ? 41.630  -5.817  30.573 1.00 31.23  ? 215 PHE A CD1 1 
ATOM   1552 C  CD2 . PHE A  1  202 ? 41.444  -4.097  32.215 1.00 34.57  ? 215 PHE A CD2 1 
ATOM   1553 C  CE1 . PHE A  1  202 ? 42.985  -5.539  30.446 1.00 31.01  ? 215 PHE A CE1 1 
ATOM   1554 C  CE2 . PHE A  1  202 ? 42.801  -3.847  32.106 1.00 37.93  ? 215 PHE A CE2 1 
ATOM   1555 C  CZ  . PHE A  1  202 ? 43.567  -4.561  31.219 1.00 32.74  ? 215 PHE A CZ  1 
ATOM   1556 N  N   . PRO A  1  203 ? 36.237  -5.915  30.697 1.00 31.53  ? 216 PRO A N   1 
ATOM   1557 C  CA  . PRO A  1  203 ? 34.903  -6.397  31.068 1.00 31.92  ? 216 PRO A CA  1 
ATOM   1558 C  C   . PRO A  1  203 ? 34.520  -7.702  30.366 1.00 33.58  ? 216 PRO A C   1 
ATOM   1559 O  O   . PRO A  1  203 ? 33.817  -8.521  30.947 1.00 34.02  ? 216 PRO A O   1 
ATOM   1560 C  CB  . PRO A  1  203 ? 33.994  -5.223  30.699 1.00 30.21  ? 216 PRO A CB  1 
ATOM   1561 C  CG  . PRO A  1  203 ? 34.916  -4.037  30.729 1.00 29.78  ? 216 PRO A CG  1 
ATOM   1562 C  CD  . PRO A  1  203 ? 36.211  -4.554  30.141 1.00 29.97  ? 216 PRO A CD  1 
ATOM   1563 N  N   . ILE A  1  204 ? 34.988  -7.897  29.123 1.00 31.80  ? 217 ILE A N   1 
ATOM   1564 C  CA  . ILE A  1  204 ? 34.680  -9.108  28.380 1.00 32.21  ? 217 ILE A CA  1 
ATOM   1565 C  C   . ILE A  1  204 ? 35.535  -10.265 28.895 1.00 31.07  ? 217 ILE A C   1 
ATOM   1566 O  O   . ILE A  1  204 ? 35.041  -11.361 29.122 1.00 33.64  ? 217 ILE A O   1 
ATOM   1567 C  CB  . ILE A  1  204 ? 34.896  -8.885  26.869 1.00 32.34  ? 217 ILE A CB  1 
ATOM   1568 C  CG1 . ILE A  1  204 ? 34.042  -7.748  26.344 1.00 36.71  ? 217 ILE A CG1 1 
ATOM   1569 C  CG2 . ILE A  1  204 ? 34.639  -10.181 26.102 1.00 33.88  ? 217 ILE A CG2 1 
ATOM   1570 C  CD1 . ILE A  1  204 ? 34.488  -7.178  25.014 1.00 36.44  ? 217 ILE A CD1 1 
ATOM   1571 N  N   . ASN A  1  205 ? 36.838  -10.025 29.046 1.00 29.43  ? 218 ASN A N   1 
ATOM   1572 C  CA  . ASN A  1  205 ? 37.772  -11.096 29.351 1.00 28.87  ? 218 ASN A CA  1 
ATOM   1573 C  C   . ASN A  1  205 ? 37.730  -11.478 30.824 1.00 29.74  ? 218 ASN A C   1 
ATOM   1574 O  O   . ASN A  1  205 ? 38.017  -12.625 31.146 1.00 29.12  ? 218 ASN A O   1 
ATOM   1575 C  CB  . ASN A  1  205 ? 39.194  -10.724 28.950 1.00 30.51  ? 218 ASN A CB  1 
ATOM   1576 C  CG  . ASN A  1  205 ? 39.287  -10.430 27.470 1.00 31.61  ? 218 ASN A CG  1 
ATOM   1577 O  OD1 . ASN A  1  205 ? 38.490  -10.951 26.690 1.00 34.69  ? 218 ASN A OD1 1 
ATOM   1578 N  ND2 . ASN A  1  205 ? 40.222  -9.587  27.066 1.00 34.73  ? 218 ASN A ND2 1 
ATOM   1579 N  N   . LEU A  1  206 ? 37.402  -10.525 31.711 1.00 29.88  ? 219 LEU A N   1 
ATOM   1580 C  CA  . LEU A  1  206 ? 37.587  -10.730 33.143 1.00 27.20  ? 219 LEU A CA  1 
ATOM   1581 C  C   . LEU A  1  206 ? 36.292  -10.602 33.948 1.00 29.02  ? 219 LEU A C   1 
ATOM   1582 O  O   . LEU A  1  206 ? 36.205  -11.195 35.026 1.00 28.02  ? 219 LEU A O   1 
ATOM   1583 C  CB  . LEU A  1  206 ? 38.646  -9.761  33.653 1.00 27.02  ? 219 LEU A CB  1 
ATOM   1584 C  CG  . LEU A  1  206 ? 40.019  -9.894  32.988 1.00 28.37  ? 219 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A  1  206 ? 40.919  -8.735  33.343 1.00 28.75  ? 219 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A  1  206 ? 40.685  -11.205 33.393 1.00 32.04  ? 219 LEU A CD2 1 
ATOM   1587 N  N   . PHE A  1  207 ? 35.298  -9.844  33.464 1.00 25.93  ? 220 PHE A N   1 
ATOM   1588 C  CA  . PHE A  1  207 ? 34.065  -9.659  34.222 1.00 28.06  ? 220 PHE A CA  1 
ATOM   1589 C  C   . PHE A  1  207 ? 32.983  -10.654 33.817 1.00 26.60  ? 220 PHE A C   1 
ATOM   1590 O  O   . PHE A  1  207 ? 31.988  -10.801 34.520 1.00 29.70  ? 220 PHE A O   1 
ATOM   1591 C  CB  . PHE A  1  207 ? 33.457  -8.262  34.102 1.00 27.22  ? 220 PHE A CB  1 
ATOM   1592 C  CG  . PHE A  1  207 ? 34.274  -7.136  34.705 1.00 27.65  ? 220 PHE A CG  1 
ATOM   1593 C  CD1 . PHE A  1  207 ? 35.349  -7.387  35.554 1.00 27.93  ? 220 PHE A CD1 1 
ATOM   1594 C  CD2 . PHE A  1  207 ? 33.933  -5.814  34.445 1.00 26.72  ? 220 PHE A CD2 1 
ATOM   1595 C  CE1 . PHE A  1  207 ? 36.081  -6.342  36.093 1.00 31.98  ? 220 PHE A CE1 1 
ATOM   1596 C  CE2 . PHE A  1  207 ? 34.688  -4.782  34.985 1.00 26.86  ? 220 PHE A CE2 1 
ATOM   1597 C  CZ  . PHE A  1  207 ? 35.748  -5.048  35.803 1.00 29.32  ? 220 PHE A CZ  1 
ATOM   1598 N  N   . VAL A  1  208 ? 33.147  -11.296 32.666 1.00 31.26  ? 221 VAL A N   1 
ATOM   1599 C  CA  . VAL A  1  208 ? 32.262  -12.371 32.263 1.00 31.47  ? 221 VAL A CA  1 
ATOM   1600 C  C   . VAL A  1  208 ? 32.699  -13.635 32.986 1.00 29.65  ? 221 VAL A C   1 
ATOM   1601 O  O   . VAL A  1  208 ? 33.883  -13.941 33.051 1.00 34.42  ? 221 VAL A O   1 
ATOM   1602 C  CB  . VAL A  1  208 ? 32.282  -12.568 30.733 1.00 33.09  ? 221 VAL A CB  1 
ATOM   1603 C  CG1 . VAL A  1  208 ? 31.473  -13.789 30.300 1.00 34.24  ? 221 VAL A CG1 1 
ATOM   1604 C  CG2 . VAL A  1  208 ? 31.802  -11.318 30.020 1.00 31.19  ? 221 VAL A CG2 1 
ATOM   1605 N  N   . ASP A  1  209 ? 31.717  -14.365 33.513 1.00 30.90  ? 222 ASP A N   1 
ATOM   1606 C  CA  . ASP A  1  209 ? 31.949  -15.552 34.312 1.00 30.28  ? 222 ASP A CA  1 
ATOM   1607 C  C   . ASP A  1  209 ? 32.784  -16.549 33.512 1.00 32.10  ? 222 ASP A C   1 
ATOM   1608 O  O   . ASP A  1  209 ? 32.537  -16.745 32.325 1.00 31.78  ? 222 ASP A O   1 
ATOM   1609 C  CB  . ASP A  1  209 ? 30.618  -16.141 34.747 1.00 32.86  ? 222 ASP A CB  1 
ATOM   1610 C  CG  . ASP A  1  209 ? 30.742  -17.271 35.744 1.00 33.53  ? 222 ASP A CG  1 
ATOM   1611 O  OD1 . ASP A  1  209 ? 31.217  -18.356 35.329 1.00 35.49  ? 222 ASP A OD1 1 
ATOM   1612 O  OD2 . ASP A  1  209 ? 30.428  -17.030 36.935 1.00 30.04  ? 222 ASP A OD2 1 
ATOM   1613 N  N   . GLY A  1  210 ? 33.758  -17.179 34.184 1.00 31.51  ? 223 GLY A N   1 
ATOM   1614 C  CA  . GLY A  1  210 ? 34.721  -18.057 33.534 1.00 33.43  ? 223 GLY A CA  1 
ATOM   1615 C  C   . GLY A  1  210 ? 34.102  -19.365 33.034 1.00 34.85  ? 223 GLY A C   1 
ATOM   1616 O  O   . GLY A  1  210 ? 34.715  -20.067 32.240 1.00 34.73  ? 223 GLY A O   1 
ATOM   1617 N  N   . ARG A  1  211 ? 32.902  -19.705 33.504 1.00 36.95  ? 224 ARG A N   1 
ATOM   1618 C  CA  . ARG A  1  211 ? 32.191  -20.881 33.014 1.00 39.76  ? 224 ARG A CA  1 
ATOM   1619 C  C   . ARG A  1  211 ? 31.557  -20.618 31.647 1.00 39.70  ? 224 ARG A C   1 
ATOM   1620 O  O   . ARG A  1  211 ? 31.129  -21.548 30.985 1.00 40.19  ? 224 ARG A O   1 
ATOM   1621 C  CB  . ARG A  1  211 ? 31.121  -21.338 34.004 1.00 40.69  ? 224 ARG A CB  1 
ATOM   1622 C  CG  . ARG A  1  211 ? 31.723  -21.870 35.297 1.00 40.99  ? 224 ARG A CG  1 
ATOM   1623 C  CD  . ARG A  1  211 ? 30.681  -21.994 36.386 1.00 40.27  ? 224 ARG A CD  1 
ATOM   1624 N  NE  . ARG A  1  211 ? 30.153  -20.673 36.759 1.00 39.01  ? 224 ARG A NE  1 
ATOM   1625 C  CZ  . ARG A  1  211 ? 29.319  -20.446 37.767 1.00 41.49  ? 224 ARG A CZ  1 
ATOM   1626 N  NH1 . ARG A  1  211 ? 28.855  -21.454 38.500 1.00 38.65  ? 224 ARG A NH1 1 
ATOM   1627 N  NH2 . ARG A  1  211 ? 28.939  -19.206 38.051 1.00 38.49  ? 224 ARG A NH2 1 
ATOM   1628 N  N   . VAL A  1  212 ? 31.528  -19.359 31.194 1.00 37.32  ? 225 VAL A N   1 
ATOM   1629 C  CA  . VAL A  1  212 ? 31.076  -19.057 29.849 1.00 39.80  ? 225 VAL A CA  1 
ATOM   1630 C  C   . VAL A  1  212 ? 32.264  -19.168 28.886 1.00 45.02  ? 225 VAL A C   1 
ATOM   1631 O  O   . VAL A  1  212 ? 33.151  -18.322 28.906 1.00 44.22  ? 225 VAL A O   1 
ATOM   1632 C  CB  . VAL A  1  212 ? 30.446  -17.656 29.806 1.00 39.40  ? 225 VAL A CB  1 
ATOM   1633 C  CG1 . VAL A  1  212 ? 30.017  -17.273 28.399 1.00 40.17  ? 225 VAL A CG1 1 
ATOM   1634 C  CG2 . VAL A  1  212 ? 29.273  -17.541 30.783 1.00 40.93  ? 225 VAL A CG2 1 
ATOM   1635 N  N   . THR A  1  213 ? 32.267  -20.192 28.026 1.00 52.56  ? 226 THR A N   1 
ATOM   1636 C  CA  . THR A  1  213 ? 33.404  -20.461 27.144 1.00 65.21  ? 226 THR A CA  1 
ATOM   1637 C  C   . THR A  1  213 ? 33.194  -19.859 25.749 1.00 66.07  ? 226 THR A C   1 
ATOM   1638 O  O   . THR A  1  213 ? 34.167  -19.526 25.077 1.00 55.86  ? 226 THR A O   1 
ATOM   1639 C  CB  . THR A  1  213 ? 33.675  -21.967 27.078 1.00 64.40  ? 226 THR A CB  1 
ATOM   1640 O  OG1 . THR A  1  213 ? 32.466  -22.586 26.638 1.00 67.06  ? 226 THR A OG1 1 
ATOM   1641 C  CG2 . THR A  1  213 ? 34.117  -22.509 28.429 1.00 67.05  ? 226 THR A CG2 1 
ATOM   1642 N  N   . THR A  1  214 ? 31.933  -19.691 25.333 1.00 66.30  ? 227 THR A N   1 
ATOM   1643 C  CA  . THR A  1  214 ? 31.638  -19.198 23.993 1.00 71.25  ? 227 THR A CA  1 
ATOM   1644 C  C   . THR A  1  214 ? 30.729  -17.965 24.044 1.00 63.88  ? 227 THR A C   1 
ATOM   1645 O  O   . THR A  1  214 ? 29.852  -17.870 24.896 1.00 60.05  ? 227 THR A O   1 
ATOM   1646 C  CB  . THR A  1  214 ? 31.006  -20.350 23.203 1.00 70.68  ? 227 THR A CB  1 
ATOM   1647 O  OG1 . THR A  1  214 ? 30.930  -19.843 21.874 1.00 76.17  ? 227 THR A OG1 1 
ATOM   1648 C  CG2 . THR A  1  214 ? 29.644  -20.774 23.736 1.00 65.89  ? 227 THR A CG2 1 
ATOM   1649 N  N   . ASP A  1  215 ? 30.891  -17.046 23.079 1.00 64.43  ? 228 ASP A N   1 
ATOM   1650 C  CA  . ASP A  1  215 ? 29.984  -15.917 22.928 1.00 68.20  ? 228 ASP A CA  1 
ATOM   1651 C  C   . ASP A  1  215 ? 30.024  -15.109 24.225 1.00 54.03  ? 228 ASP A C   1 
ATOM   1652 O  O   . ASP A  1  215 ? 29.013  -14.907 24.885 1.00 50.64  ? 228 ASP A O   1 
ATOM   1653 C  CB  . ASP A  1  215 ? 28.579  -16.370 22.534 1.00 79.15  ? 228 ASP A CB  1 
ATOM   1654 C  CG  . ASP A  1  215 ? 27.570  -15.261 22.233 1.00 96.80  ? 228 ASP A CG  1 
ATOM   1655 O  OD1 . ASP A  1  215 ? 28.013  -14.113 21.985 1.00 97.16  ? 228 ASP A OD1 1 
ATOM   1656 O  OD2 . ASP A  1  215 ? 26.337  -15.537 22.275 1.00 100.36 ? 228 ASP A OD2 1 
ATOM   1657 N  N   . ARG A  1  216 ? 31.231  -14.681 24.602 1.00 44.84  ? 229 ARG A N   1 
ATOM   1658 C  CA  . ARG A  1  216 ? 31.443  -14.037 25.880 1.00 43.97  ? 229 ARG A CA  1 
ATOM   1659 C  C   . ARG A  1  216 ? 30.863  -12.631 25.800 1.00 34.64  ? 229 ARG A C   1 
ATOM   1660 O  O   . ARG A  1  216 ? 31.199  -11.859 24.920 1.00 36.38  ? 229 ARG A O   1 
ATOM   1661 C  CB  . ARG A  1  216 ? 32.920  -14.156 26.276 1.00 44.93  ? 229 ARG A CB  1 
ATOM   1662 C  CG  . ARG A  1  216 ? 33.272  -15.562 26.759 1.00 48.20  ? 229 ARG A CG  1 
ATOM   1663 C  CD  . ARG A  1  216 ? 34.752  -15.740 27.072 1.00 49.62  ? 229 ARG A CD  1 
ATOM   1664 N  NE  . ARG A  1  216 ? 35.186  -14.886 28.185 1.00 53.23  ? 229 ARG A NE  1 
ATOM   1665 C  CZ  . ARG A  1  216 ? 34.958  -15.092 29.487 1.00 53.12  ? 229 ARG A CZ  1 
ATOM   1666 N  NH1 . ARG A  1  216 ? 34.408  -16.216 29.931 1.00 47.09  ? 229 ARG A NH1 1 
ATOM   1667 N  NH2 . ARG A  1  216 ? 35.332  -14.165 30.355 1.00 53.72  ? 229 ARG A NH2 1 
ATOM   1668 N  N   . LYS A  1  217 ? 29.965  -12.319 26.729 1.00 34.93  ? 230 LYS A N   1 
ATOM   1669 C  CA  . LYS A  1  217 ? 29.262  -11.050 26.706 1.00 31.85  ? 230 LYS A CA  1 
ATOM   1670 C  C   . LYS A  1  217 ? 28.827  -10.741 28.132 1.00 29.80  ? 230 LYS A C   1 
ATOM   1671 O  O   . LYS A  1  217 ? 28.482  -11.646 28.871 1.00 29.39  ? 230 LYS A O   1 
ATOM   1672 C  CB  . LYS A  1  217 ? 28.074  -11.158 25.743 1.00 33.10  ? 230 LYS A CB  1 
ATOM   1673 C  CG  . LYS A  1  217 ? 26.990  -12.113 26.201 1.00 34.85  ? 230 LYS A CG  1 
ATOM   1674 C  CD  . LYS A  1  217 ? 25.858  -12.381 25.208 1.00 38.51  ? 230 LYS A CD  1 
ATOM   1675 C  CE  . LYS A  1  217 ? 24.756  -13.181 25.827 1.00 40.44  ? 230 LYS A CE  1 
ATOM   1676 N  NZ  . LYS A  1  217 ? 23.755  -13.538 24.817 1.00 43.07  ? 230 LYS A NZ  1 
ATOM   1677 N  N   . LEU A  1  218 ? 28.824  -9.456  28.491 1.00 33.08  ? 231 LEU A N   1 
ATOM   1678 C  CA  . LEU A  1  218 ? 28.528  -9.058  29.858 1.00 30.99  ? 231 LEU A CA  1 
ATOM   1679 C  C   . LEU A  1  218 ? 27.120  -8.474  29.939 1.00 29.52  ? 231 LEU A C   1 
ATOM   1680 O  O   . LEU A  1  218 ? 26.804  -7.549  29.207 1.00 30.21  ? 231 LEU A O   1 
ATOM   1681 C  CB  . LEU A  1  218 ? 29.580  -8.039  30.279 1.00 28.85  ? 231 LEU A CB  1 
ATOM   1682 C  CG  . LEU A  1  218 ? 29.543  -7.590  31.739 1.00 29.65  ? 231 LEU A CG  1 
ATOM   1683 C  CD1 . LEU A  1  218 ? 29.884  -8.734  32.647 1.00 30.05  ? 231 LEU A CD1 1 
ATOM   1684 C  CD2 . LEU A  1  218 ? 30.490  -6.431  31.944 1.00 30.51  ? 231 LEU A CD2 1 
ATOM   1685 N  N   . SER A  1  219 ? 26.327  -8.959  30.893 1.00 28.60  ? 232 SER A N   1 
ATOM   1686 C  CA  . SER A  1  219 ? 25.000  -8.418  31.142 1.00 29.51  ? 232 SER A CA  1 
ATOM   1687 C  C   . SER A  1  219 ? 25.125  -7.051  31.814 1.00 31.41  ? 232 SER A C   1 
ATOM   1688 O  O   . SER A  1  219 ? 26.125  -6.754  32.481 1.00 31.42  ? 232 SER A O   1 
ATOM   1689 C  CB  . SER A  1  219 ? 24.190  -9.358  31.975 1.00 31.31  ? 232 SER A CB  1 
ATOM   1690 O  OG  . SER A  1  219 ? 24.621  -9.331  33.339 1.00 31.35  ? 232 SER A OG  1 
ATOM   1691 N  N   . MET A  1  220 ? 24.093  -6.227  31.662 1.00 30.36  ? 233 MET A N   1 
ATOM   1692 C  CA  . MET A  1  220 ? 24.104  -4.901  32.253 1.00 30.02  ? 233 MET A CA  1 
ATOM   1693 C  C   . MET A  1  220 ? 23.980  -5.004  33.776 1.00 30.91  ? 233 MET A C   1 
ATOM   1694 O  O   . MET A  1  220 ? 24.486  -4.139  34.489 1.00 28.78  ? 233 MET A O   1 
ATOM   1695 C  CB  . MET A  1  220 ? 22.996  -4.035  31.659 1.00 29.73  ? 233 MET A CB  1 
ATOM   1696 C  CG  . MET A  1  220 ? 23.182  -3.722  30.172 1.00 29.84  ? 233 MET A CG  1 
ATOM   1697 S  SD  . MET A  1  220 ? 24.770  -2.958  29.768 1.00 32.38  ? 233 MET A SD  1 
ATOM   1698 C  CE  . MET A  1  220 ? 25.643  -4.406  29.154 1.00 31.38  ? 233 MET A CE  1 
ATOM   1699 N  N   . GLU A  1  221 ? 23.327  -6.071  34.268 1.00 29.68  ? 234 GLU A N   1 
ATOM   1700 C  CA  . GLU A  1  221 ? 23.194  -6.285  35.698 1.00 32.68  ? 234 GLU A CA  1 
ATOM   1701 C  C   . GLU A  1  221 ? 24.583  -6.532  36.315 1.00 30.01  ? 234 GLU A C   1 
ATOM   1702 O  O   . GLU A  1  221 ? 24.919  -5.989  37.357 1.00 29.52  ? 234 GLU A O   1 
ATOM   1703 C  CB  . GLU A  1  221 ? 22.279  -7.474  35.993 1.00 37.70  ? 234 GLU A CB  1 
ATOM   1704 C  CG  . GLU A  1  221 ? 20.827  -7.259  35.558 1.00 45.22  ? 234 GLU A CG  1 
ATOM   1705 C  CD  . GLU A  1  221 ? 20.460  -7.555  34.094 1.00 47.95  ? 234 GLU A CD  1 
ATOM   1706 O  OE1 . GLU A  1  221 ? 21.291  -7.750  33.167 1.00 37.93  ? 234 GLU A OE1 1 
ATOM   1707 O  OE2 . GLU A  1  221 ? 19.227  -7.631  33.891 1.00 56.92  ? 234 GLU A OE2 1 
ATOM   1708 N  N   . ASP A  1  222 ? 25.374  -7.404  35.685 1.00 28.70  ? 235 ASP A N   1 
ATOM   1709 C  CA  . ASP A  1  222 ? 26.716  -7.721  36.152 1.00 30.64  ? 235 ASP A CA  1 
ATOM   1710 C  C   . ASP A  1  222 ? 27.625  -6.499  36.029 1.00 31.39  ? 235 ASP A C   1 
ATOM   1711 O  O   . ASP A  1  222 ? 28.431  -6.222  36.924 1.00 28.87  ? 235 ASP A O   1 
ATOM   1712 C  CB  . ASP A  1  222 ? 27.281  -8.933  35.435 1.00 29.32  ? 235 ASP A CB  1 
ATOM   1713 C  CG  . ASP A  1  222 ? 26.623  -10.259 35.803 1.00 32.54  ? 235 ASP A CG  1 
ATOM   1714 O  OD1 . ASP A  1  222 ? 25.744  -10.271 36.703 1.00 35.16  ? 235 ASP A OD1 1 
ATOM   1715 O  OD2 . ASP A  1  222 ? 27.018  -11.282 35.209 1.00 32.33  ? 235 ASP A OD2 1 
ATOM   1716 N  N   . ALA A  1  223 ? 27.499  -5.774  34.916 1.00 27.78  ? 236 ALA A N   1 
ATOM   1717 C  CA  . ALA A  1  223 ? 28.257  -4.554  34.732 1.00 28.05  ? 236 ALA A CA  1 
ATOM   1718 C  C   . ALA A  1  223 ? 27.961  -3.551  35.850 1.00 27.90  ? 236 ALA A C   1 
ATOM   1719 O  O   . ALA A  1  223 ? 28.886  -2.983  36.431 1.00 28.35  ? 236 ALA A O   1 
ATOM   1720 C  CB  . ALA A  1  223 ? 27.987  -3.972  33.377 1.00 26.79  ? 236 ALA A CB  1 
ATOM   1721 N  N   . ALA A  1  224 ? 26.683  -3.327  36.175 1.00 27.43  ? 237 ALA A N   1 
ATOM   1722 C  CA  . ALA A  1  224 ? 26.349  -2.348  37.211 1.00 28.83  ? 237 ALA A CA  1 
ATOM   1723 C  C   . ALA A  1  224 ? 26.914  -2.804  38.556 1.00 27.59  ? 237 ALA A C   1 
ATOM   1724 O  O   . ALA A  1  224 ? 27.445  -2.006  39.333 1.00 25.90  ? 237 ALA A O   1 
ATOM   1725 C  CB  . ALA A  1  224 ? 24.858  -2.132  37.298 1.00 28.71  ? 237 ALA A CB  1 
ATOM   1726 N  N   . SER A  1  225 ? 26.799  -4.105  38.813 1.00 25.51  ? 238 SER A N   1 
ATOM   1727 C  CA  . SER A  1  225 ? 27.245  -4.663  40.070 1.00 28.79  ? 238 SER A CA  1 
ATOM   1728 C  C   . SER A  1  225 ? 28.727  -4.340  40.307 1.00 28.68  ? 238 SER A C   1 
ATOM   1729 O  O   . SER A  1  225 ? 29.104  -3.891  41.396 1.00 27.76  ? 238 SER A O   1 
ATOM   1730 C  CB  . SER A  1  225 ? 26.933  -6.147  40.104 1.00 30.60  ? 238 SER A CB  1 
ATOM   1731 O  OG  . SER A  1  225 ? 27.344  -6.717  41.331 1.00 36.38  ? 238 SER A OG  1 
ATOM   1732 N  N   . ILE A  1  226 ? 29.553  -4.513  39.268 1.00 26.33  ? 239 ILE A N   1 
ATOM   1733 C  CA  . ILE A  1  226 ? 30.991  -4.297  39.396 1.00 27.39  ? 239 ILE A CA  1 
ATOM   1734 C  C   . ILE A  1  226 ? 31.353  -2.807  39.301 1.00 27.15  ? 239 ILE A C   1 
ATOM   1735 O  O   . ILE A  1  226 ? 32.023  -2.277  40.187 1.00 25.76  ? 239 ILE A O   1 
ATOM   1736 C  CB  . ILE A  1  226 ? 31.742  -5.156  38.371 1.00 26.75  ? 239 ILE A CB  1 
ATOM   1737 C  CG1 . ILE A  1  226 ? 31.560  -6.637  38.678 1.00 30.27  ? 239 ILE A CG1 1 
ATOM   1738 C  CG2 . ILE A  1  226 ? 33.227  -4.798  38.328 1.00 26.48  ? 239 ILE A CG2 1 
ATOM   1739 C  CD1 . ILE A  1  226 ? 31.909  -7.552  37.514 1.00 32.69  ? 239 ILE A CD1 1 
ATOM   1740 N  N   . PHE A  1  227 ? 30.893  -2.132  38.244 1.00 27.00  ? 240 PHE A N   1 
ATOM   1741 C  CA  . PHE A  1  227 ? 31.273  -0.751  37.974 1.00 28.05  ? 240 PHE A CA  1 
ATOM   1742 C  C   . PHE A  1  227 ? 30.697  0.226   39.000 1.00 25.97  ? 240 PHE A C   1 
ATOM   1743 O  O   . PHE A  1  227 ? 31.353  1.204   39.349 1.00 26.30  ? 240 PHE A O   1 
ATOM   1744 C  CB  . PHE A  1  227 ? 30.793  -0.333  36.585 1.00 28.56  ? 240 PHE A CB  1 
ATOM   1745 C  CG  . PHE A  1  227 ? 31.624  -0.817  35.407 1.00 30.05  ? 240 PHE A CG  1 
ATOM   1746 C  CD1 . PHE A  1  227 ? 32.847  -0.221  35.112 1.00 31.54  ? 240 PHE A CD1 1 
ATOM   1747 C  CD2 . PHE A  1  227 ? 31.147  -1.794  34.546 1.00 33.36  ? 240 PHE A CD2 1 
ATOM   1748 C  CE1 . PHE A  1  227 ? 33.571  -0.612  34.000 1.00 30.21  ? 240 PHE A CE1 1 
ATOM   1749 C  CE2 . PHE A  1  227 ? 31.881  -2.177  33.432 1.00 33.00  ? 240 PHE A CE2 1 
ATOM   1750 C  CZ  . PHE A  1  227 ? 33.089  -1.592  33.170 1.00 31.71  ? 240 PHE A CZ  1 
ATOM   1751 N  N   . ARG A  1  228 ? 29.464  -0.015  39.449 1.00 24.44  ? 241 ARG A N   1 
ATOM   1752 C  CA  . ARG A  1  228 ? 28.812  0.883   40.385 1.00 26.93  ? 241 ARG A CA  1 
ATOM   1753 C  C   . ARG A  1  228 ? 29.009  0.377   41.809 1.00 25.90  ? 241 ARG A C   1 
ATOM   1754 O  O   . ARG A  1  228 ? 29.475  1.130   42.653 1.00 27.47  ? 241 ARG A O   1 
ATOM   1755 C  CB  . ARG A  1  228 ? 27.337  1.116   40.047 1.00 28.52  ? 241 ARG A CB  1 
ATOM   1756 C  CG  . ARG A  1  228 ? 26.619  2.090   40.970 1.00 31.64  ? 241 ARG A CG  1 
ATOM   1757 C  CD  . ARG A  1  228 ? 25.222  2.488   40.530 1.00 32.30  ? 241 ARG A CD  1 
ATOM   1758 N  NE  . ARG A  1  228 ? 24.298  1.354   40.476 1.00 33.15  ? 241 ARG A NE  1 
ATOM   1759 C  CZ  . ARG A  1  228 ? 23.577  0.936   39.446 1.00 35.30  ? 241 ARG A CZ  1 
ATOM   1760 N  NH1 . ARG A  1  228 ? 23.629  1.538   38.267 1.00 36.10  ? 241 ARG A NH1 1 
ATOM   1761 N  NH2 . ARG A  1  228 ? 22.793  -0.117  39.595 1.00 33.50  ? 241 ARG A NH2 1 
ATOM   1762 N  N   . ASP A  1  229 ? 28.655  -0.883  42.091 1.00 25.31  ? 242 ASP A N   1 
ATOM   1763 C  CA  . ASP A  1  229 ? 28.556  -1.322  43.474 1.00 25.04  ? 242 ASP A CA  1 
ATOM   1764 C  C   . ASP A  1  229 ? 29.837  -1.967  44.017 1.00 23.42  ? 242 ASP A C   1 
ATOM   1765 O  O   . ASP A  1  229 ? 29.919  -2.249  45.220 1.00 24.09  ? 242 ASP A O   1 
ATOM   1766 C  CB  . ASP A  1  229 ? 27.347  -2.219  43.657 1.00 27.46  ? 242 ASP A CB  1 
ATOM   1767 C  CG  . ASP A  1  229 ? 26.006  -1.545  43.397 1.00 31.26  ? 242 ASP A CG  1 
ATOM   1768 O  OD1 . ASP A  1  229 ? 25.913  -0.294  43.489 1.00 34.29  ? 242 ASP A OD1 1 
ATOM   1769 O  OD2 . ASP A  1  229 ? 25.054  -2.275  43.101 1.00 32.52  ? 242 ASP A OD2 1 
ATOM   1770 N  N   . MET A  1  230 ? 30.821  -2.225  43.160 1.00 23.88  ? 243 MET A N   1 
ATOM   1771 C  CA  A MET A  1  230 ? 32.071  -2.853  43.570 0.50 24.75  ? 243 MET A CA  1 
ATOM   1772 C  CA  B MET A  1  230 ? 32.071  -2.855  43.567 0.50 25.76  ? 243 MET A CA  1 
ATOM   1773 C  C   . MET A  1  230 ? 31.799  -4.248  44.126 1.00 25.05  ? 243 MET A C   1 
ATOM   1774 O  O   . MET A  1  230 ? 32.427  -4.655  45.113 1.00 26.40  ? 243 MET A O   1 
ATOM   1775 C  CB  A MET A  1  230 ? 32.796  -2.013  44.631 0.50 25.51  ? 243 MET A CB  1 
ATOM   1776 C  CB  B MET A  1  230 ? 32.797  -2.025  44.633 0.50 28.16  ? 243 MET A CB  1 
ATOM   1777 C  CG  A MET A  1  230 ? 32.930  -0.543  44.267 0.50 27.83  ? 243 MET A CG  1 
ATOM   1778 C  CG  B MET A  1  230 ? 32.951  -0.570  44.272 0.50 32.61  ? 243 MET A CG  1 
ATOM   1779 S  SD  A MET A  1  230 ? 33.675  0.438   45.588 0.50 26.22  ? 243 MET A SD  1 
ATOM   1780 S  SD  B MET A  1  230 ? 33.639  0.371   45.648 0.50 33.70  ? 243 MET A SD  1 
ATOM   1781 C  CE  A MET A  1  230 ? 32.390  0.486   46.842 0.50 23.35  ? 243 MET A CE  1 
ATOM   1782 C  CE  B MET A  1  230 ? 32.681  1.845   45.296 0.50 43.47  ? 243 MET A CE  1 
ATOM   1783 N  N   . ARG A  1  231 ? 30.867  -4.963  43.478 1.00 24.22  ? 244 ARG A N   1 
ATOM   1784 C  CA  A ARG A  1  231 ? 30.372  -6.241  43.964 0.50 24.91  ? 244 ARG A CA  1 
ATOM   1785 C  CA  B ARG A  1  231 ? 30.376  -6.241  43.963 0.50 24.81  ? 244 ARG A CA  1 
ATOM   1786 C  C   . ARG A  1  231 ? 30.441  -7.274  42.840 1.00 25.47  ? 244 ARG A C   1 
ATOM   1787 O  O   . ARG A  1  231 ? 29.945  -7.049  41.733 1.00 24.64  ? 244 ARG A O   1 
ATOM   1788 C  CB  A ARG A  1  231 ? 28.939  -6.079  44.481 0.50 26.40  ? 244 ARG A CB  1 
ATOM   1789 C  CB  B ARG A  1  231 ? 28.945  -6.073  44.479 0.50 26.08  ? 244 ARG A CB  1 
ATOM   1790 C  CG  A ARG A  1  231 ? 28.355  -7.333  45.137 0.50 28.16  ? 244 ARG A CG  1 
ATOM   1791 C  CG  B ARG A  1  231 ? 28.336  -7.313  45.133 0.50 27.57  ? 244 ARG A CG  1 
ATOM   1792 C  CD  A ARG A  1  231 ? 26.910  -7.219  45.613 0.50 29.77  ? 244 ARG A CD  1 
ATOM   1793 C  CD  B ARG A  1  231 ? 26.890  -7.069  45.576 0.50 28.78  ? 244 ARG A CD  1 
ATOM   1794 N  NE  A ARG A  1  231 ? 25.997  -7.240  44.465 0.50 35.06  ? 244 ARG A NE  1 
ATOM   1795 N  NE  B ARG A  1  231 ? 26.020  -6.770  44.431 0.50 33.11  ? 244 ARG A NE  1 
ATOM   1796 C  CZ  A ARG A  1  231 ? 25.697  -8.326  43.728 0.50 36.97  ? 244 ARG A CZ  1 
ATOM   1797 C  CZ  B ARG A  1  231 ? 25.368  -5.635  44.152 0.50 32.36  ? 244 ARG A CZ  1 
ATOM   1798 N  NH1 A ARG A  1  231 ? 26.001  -9.544  44.169 0.50 36.54  ? 244 ARG A NH1 1 
ATOM   1799 N  NH1 B ARG A  1  231 ? 25.394  -4.609  44.982 0.50 33.05  ? 244 ARG A NH1 1 
ATOM   1800 N  NH2 A ARG A  1  231 ? 25.046  -8.178  42.585 0.50 31.91  ? 244 ARG A NH2 1 
ATOM   1801 N  NH2 B ARG A  1  231 ? 24.670  -5.555  43.042 0.50 29.52  ? 244 ARG A NH2 1 
ATOM   1802 N  N   . PHE A  1  232 ? 31.053  -8.421  43.132 1.00 26.12  ? 245 PHE A N   1 
ATOM   1803 C  CA  . PHE A  1  232 ? 31.018  -9.550  42.211 1.00 26.22  ? 245 PHE A CA  1 
ATOM   1804 C  C   . PHE A  1  232 ? 29.581  -9.986  41.982 1.00 27.03  ? 245 PHE A C   1 
ATOM   1805 O  O   . PHE A  1  232 ? 28.780  -10.011 42.916 1.00 25.83  ? 245 PHE A O   1 
ATOM   1806 C  CB  . PHE A  1  232 ? 31.758  -10.760 42.776 1.00 23.70  ? 245 PHE A CB  1 
ATOM   1807 C  CG  . PHE A  1  232 ? 33.268  -10.652 42.763 1.00 27.80  ? 245 PHE A CG  1 
ATOM   1808 C  CD1 . PHE A  1  232 ? 33.955  -10.596 41.557 1.00 28.60  ? 245 PHE A CD1 1 
ATOM   1809 C  CD2 . PHE A  1  232 ? 34.005  -10.703 43.944 1.00 30.45  ? 245 PHE A CD2 1 
ATOM   1810 C  CE1 . PHE A  1  232 ? 35.336  -10.561 41.536 1.00 30.68  ? 245 PHE A CE1 1 
ATOM   1811 C  CE2 . PHE A  1  232 ? 35.393  -10.660 43.907 1.00 27.90  ? 245 PHE A CE2 1 
ATOM   1812 C  CZ  . PHE A  1  232 ? 36.051  -10.597 42.712 1.00 30.62  ? 245 PHE A CZ  1 
ATOM   1813 N  N   . PRO A  1  233 ? 29.213  -10.404 40.758 1.00 26.59  ? 246 PRO A N   1 
ATOM   1814 C  CA  . PRO A  1  233 ? 27.953  -11.126 40.566 1.00 27.55  ? 246 PRO A CA  1 
ATOM   1815 C  C   . PRO A  1  233 ? 27.852  -12.303 41.532 1.00 28.79  ? 246 PRO A C   1 
ATOM   1816 O  O   . PRO A  1  233 ? 28.867  -12.878 41.950 1.00 26.18  ? 246 PRO A O   1 
ATOM   1817 C  CB  . PRO A  1  233 ? 28.028  -11.579 39.082 1.00 27.61  ? 246 PRO A CB  1 
ATOM   1818 C  CG  . PRO A  1  233 ? 28.926  -10.541 38.442 1.00 27.53  ? 246 PRO A CG  1 
ATOM   1819 C  CD  . PRO A  1  233 ? 29.970  -10.212 39.509 1.00 26.09  ? 246 PRO A CD  1 
ATOM   1820 N  N   . ASP A  1  234 ? 26.618  -12.648 41.912 1.00 27.52  ? 247 ASP A N   1 
ATOM   1821 C  CA  . ASP A  1  234 ? 26.393  -13.830 42.732 1.00 29.50  ? 247 ASP A CA  1 
ATOM   1822 C  C   . ASP A  1  234 ? 27.067  -15.032 42.067 1.00 28.85  ? 247 ASP A C   1 
ATOM   1823 O  O   . ASP A  1  234 ? 26.975  -15.181 40.860 1.00 28.07  ? 247 ASP A O   1 
ATOM   1824 C  CB  . ASP A  1  234 ? 24.910  -14.108 42.929 1.00 30.95  ? 247 ASP A CB  1 
ATOM   1825 C  CG  . ASP A  1  234 ? 24.159  -13.138 43.836 1.00 34.64  ? 247 ASP A CG  1 
ATOM   1826 O  OD1 . ASP A  1  234 ? 24.785  -12.176 44.374 1.00 32.69  ? 247 ASP A OD1 1 
ATOM   1827 O  OD2 . ASP A  1  234 ? 22.934  -13.354 43.996 1.00 32.51  ? 247 ASP A OD2 1 
ATOM   1828 N  N   . ASP A  1  235 ? 27.744  -15.861 42.862 1.00 29.32  ? 248 ASP A N   1 
ATOM   1829 C  CA  . ASP A  1  235 ? 28.339  -17.108 42.401 1.00 29.83  ? 248 ASP A CA  1 
ATOM   1830 C  C   . ASP A  1  235 ? 29.405  -16.882 41.327 1.00 32.50  ? 248 ASP A C   1 
ATOM   1831 O  O   . ASP A  1  235 ? 29.681  -17.774 40.533 1.00 28.39  ? 248 ASP A O   1 
ATOM   1832 C  CB  . ASP A  1  235 ? 27.268  -18.072 41.900 1.00 36.45  ? 248 ASP A CB  1 
ATOM   1833 C  CG  . ASP A  1  235 ? 27.753  -19.506 41.680 1.00 36.66  ? 248 ASP A CG  1 
ATOM   1834 O  OD1 . ASP A  1  235 ? 28.419  -20.040 42.583 1.00 40.43  ? 248 ASP A OD1 1 
ATOM   1835 O  OD2 . ASP A  1  235 ? 27.482  -20.066 40.603 1.00 38.44  ? 248 ASP A OD2 1 
ATOM   1836 N  N   . PHE A  1  236 ? 30.050  -15.708 41.310 1.00 27.85  ? 249 PHE A N   1 
ATOM   1837 C  CA  . PHE A  1  236 ? 30.977  -15.387 40.242 1.00 26.60  ? 249 PHE A CA  1 
ATOM   1838 C  C   . PHE A  1  236 ? 32.175  -16.333 40.232 1.00 24.50  ? 249 PHE A C   1 
ATOM   1839 O  O   . PHE A  1  236 ? 32.857  -16.495 41.244 1.00 25.88  ? 249 PHE A O   1 
ATOM   1840 C  CB  . PHE A  1  236 ? 31.495  -13.956 40.399 1.00 28.87  ? 249 PHE A CB  1 
ATOM   1841 C  CG  . PHE A  1  236 ? 32.405  -13.519 39.262 1.00 27.85  ? 249 PHE A CG  1 
ATOM   1842 C  CD1 . PHE A  1  236 ? 31.902  -13.278 37.997 1.00 28.71  ? 249 PHE A CD1 1 
ATOM   1843 C  CD2 . PHE A  1  236 ? 33.761  -13.347 39.473 1.00 32.24  ? 249 PHE A CD2 1 
ATOM   1844 C  CE1 . PHE A  1  236 ? 32.742  -12.888 36.971 1.00 29.36  ? 249 PHE A CE1 1 
ATOM   1845 C  CE2 . PHE A  1  236 ? 34.596  -12.946 38.440 1.00 31.59  ? 249 PHE A CE2 1 
ATOM   1846 C  CZ  . PHE A  1  236 ? 34.075  -12.681 37.215 1.00 28.35  ? 249 PHE A CZ  1 
ATOM   1847 N  N   . HIS A  1  237 ? 32.463  -16.881 39.052 1.00 28.01  ? 250 HIS A N   1 
ATOM   1848 C  CA  . HIS A  1  237 ? 33.664  -17.669 38.802 1.00 28.08  ? 250 HIS A CA  1 
ATOM   1849 C  C   . HIS A  1  237 ? 34.571  -16.879 37.869 1.00 26.52  ? 250 HIS A C   1 
ATOM   1850 O  O   . HIS A  1  237 ? 34.125  -16.397 36.836 1.00 28.37  ? 250 HIS A O   1 
ATOM   1851 C  CB  . HIS A  1  237 ? 33.336  -19.028 38.159 1.00 28.54  ? 250 HIS A CB  1 
ATOM   1852 C  CG  . HIS A  1  237 ? 32.696  -20.009 39.077 1.00 30.00  ? 250 HIS A CG  1 
ATOM   1853 N  ND1 . HIS A  1  237 ? 31.613  -19.692 39.866 1.00 30.54  ? 250 HIS A ND1 1 
ATOM   1854 C  CD2 . HIS A  1  237 ? 32.996  -21.306 39.342 1.00 30.53  ? 250 HIS A CD2 1 
ATOM   1855 C  CE1 . HIS A  1  237 ? 31.287  -20.757 40.596 1.00 34.55  ? 250 HIS A CE1 1 
ATOM   1856 N  NE2 . HIS A  1  237 ? 32.128  -21.749 40.299 1.00 31.77  ? 250 HIS A NE2 1 
ATOM   1857 N  N   . ARG A  1  238 ? 35.851  -16.790 38.228 1.00 27.12  ? 251 ARG A N   1 
ATOM   1858 C  CA  . ARG A  1  238 ? 36.827  -16.044 37.450 1.00 27.58  ? 251 ARG A CA  1 
ATOM   1859 C  C   . ARG A  1  238 ? 37.084  -16.753 36.128 1.00 27.88  ? 251 ARG A C   1 
ATOM   1860 O  O   . ARG A  1  238 ? 36.775  -17.936 36.001 1.00 28.20  ? 251 ARG A O   1 
ATOM   1861 C  CB  . ARG A  1  238 ? 38.136  -15.901 38.231 1.00 27.33  ? 251 ARG A CB  1 
ATOM   1862 C  CG  . ARG A  1  238 ? 38.887  -17.212 38.434 1.00 28.48  ? 251 ARG A CG  1 
ATOM   1863 C  CD  . ARG A  1  238 ? 40.160  -17.055 39.214 1.00 27.58  ? 251 ARG A CD  1 
ATOM   1864 N  NE  . ARG A  1  238 ? 41.021  -18.220 39.021 1.00 29.14  ? 251 ARG A NE  1 
ATOM   1865 C  CZ  . ARG A  1  238 ? 42.156  -18.469 39.646 1.00 33.44  ? 251 ARG A CZ  1 
ATOM   1866 N  NH1 . ARG A  1  238 ? 42.673  -17.582 40.502 1.00 33.82  ? 251 ARG A NH1 1 
ATOM   1867 N  NH2 . ARG A  1  238 ? 42.789  -19.612 39.388 1.00 32.29  ? 251 ARG A NH2 1 
ATOM   1868 N  N   . SER A  1  239 ? 37.673  -16.010 35.182 1.00 27.46  ? 252 SER A N   1 
ATOM   1869 C  CA  . SER A  1  239 ? 38.191  -16.533 33.924 1.00 28.91  ? 252 SER A CA  1 
ATOM   1870 C  C   . SER A  1  239 ? 38.886  -17.878 34.144 1.00 32.23  ? 252 SER A C   1 
ATOM   1871 O  O   . SER A  1  239 ? 39.617  -18.046 35.126 1.00 29.27  ? 252 SER A O   1 
ATOM   1872 C  CB  . SER A  1  239 ? 39.156  -15.557 33.301 1.00 30.12  ? 252 SER A CB  1 
ATOM   1873 O  OG  . SER A  1  239 ? 39.798  -16.072 32.142 1.00 31.50  ? 252 SER A OG  1 
ATOM   1874 N  N   . ALA A  1  240 ? 38.666  -18.805 33.201 1.00 30.11  ? 253 ALA A N   1 
ATOM   1875 C  CA  . ALA A  1  240 ? 39.212  -20.160 33.256 1.00 32.54  ? 253 ALA A CA  1 
ATOM   1876 C  C   . ALA A  1  240 ? 40.684  -20.187 32.854 1.00 29.99  ? 253 ALA A C   1 
ATOM   1877 O  O   . ALA A  1  240 ? 41.335  -21.202 33.048 1.00 33.90  ? 253 ALA A O   1 
ATOM   1878 C  CB  . ALA A  1  240 ? 38.404  -21.081 32.345 1.00 36.75  ? 253 ALA A CB  1 
ATOM   1879 N  N   . VAL A  1  241 ? 41.195  -19.084 32.290 1.00 30.45  ? 254 VAL A N   1 
ATOM   1880 C  CA  . VAL A  1  241 ? 42.605  -18.935 31.934 1.00 32.03  ? 254 VAL A CA  1 
ATOM   1881 C  C   . VAL A  1  241 ? 43.090  -17.543 32.346 1.00 30.27  ? 254 VAL A C   1 
ATOM   1882 O  O   . VAL A  1  241 ? 42.302  -16.600 32.383 1.00 32.74  ? 254 VAL A O   1 
ATOM   1883 C  CB  . VAL A  1  241 ? 42.848  -19.125 30.425 1.00 36.39  ? 254 VAL A CB  1 
ATOM   1884 C  CG1 . VAL A  1  241 ? 42.557  -20.554 29.966 1.00 39.92  ? 254 VAL A CG1 1 
ATOM   1885 C  CG2 . VAL A  1  241 ? 42.027  -18.144 29.610 1.00 36.99  ? 254 VAL A CG2 1 
ATOM   1886 N  N   . PRO A  1  242 ? 44.393  -17.361 32.657 1.00 29.60  ? 255 PRO A N   1 
ATOM   1887 C  CA  . PRO A  1  242 ? 44.965  -16.030 32.832 1.00 28.54  ? 255 PRO A CA  1 
ATOM   1888 C  C   . PRO A  1  242 ? 44.622  -15.194 31.611 1.00 30.82  ? 255 PRO A C   1 
ATOM   1889 O  O   . PRO A  1  242 ? 44.704  -15.682 30.488 1.00 29.01  ? 255 PRO A O   1 
ATOM   1890 C  CB  . PRO A  1  242 ? 46.464  -16.309 32.973 1.00 30.14  ? 255 PRO A CB  1 
ATOM   1891 C  CG  . PRO A  1  242 ? 46.481  -17.671 33.637 1.00 31.78  ? 255 PRO A CG  1 
ATOM   1892 C  CD  . PRO A  1  242 ? 45.390  -18.425 32.880 1.00 31.68  ? 255 PRO A CD  1 
ATOM   1893 N  N   . ALA A  1  243 ? 44.182  -13.953 31.836 1.00 28.33  ? 256 ALA A N   1 
ATOM   1894 C  CA  . ALA A  1  243 ? 43.766  -13.115 30.728 1.00 28.30  ? 256 ALA A CA  1 
ATOM   1895 C  C   . ALA A  1  243 ? 43.987  -11.652 31.071 1.00 29.07  ? 256 ALA A C   1 
ATOM   1896 O  O   . ALA A  1  243 ? 44.204  -11.295 32.225 1.00 28.72  ? 256 ALA A O   1 
ATOM   1897 C  CB  . ALA A  1  243 ? 42.318  -13.380 30.397 1.00 31.26  ? 256 ALA A CB  1 
ATOM   1898 N  N   . SER A  1  244 ? 43.929  -10.817 30.034 1.00 27.49  ? 257 SER A N   1 
ATOM   1899 C  CA  . SER A  1  244 ? 44.156  -9.389  30.164 1.00 28.34  ? 257 SER A CA  1 
ATOM   1900 C  C   . SER A  1  244 ? 43.500  -8.700  28.973 1.00 28.29  ? 257 SER A C   1 
ATOM   1901 O  O   . SER A  1  244 ? 42.284  -8.567  28.949 1.00 28.13  ? 257 SER A O   1 
ATOM   1902 C  CB  . SER A  1  244 ? 45.634  -9.064  30.319 1.00 30.32  ? 257 SER A CB  1 
ATOM   1903 O  OG  . SER A  1  244 ? 46.395  -9.594  29.240 1.00 31.85  ? 257 SER A OG  1 
ATOM   1904 N  N   . ASN A  1  245 ? 44.294  -8.331  27.967 1.00 30.69  ? 258 ASN A N   1 
ATOM   1905 C  CA  . ASN A  1  245 ? 43.874  -7.385  26.951 1.00 30.98  ? 258 ASN A CA  1 
ATOM   1906 C  C   . ASN A  1  245 ? 43.570  -8.061  25.609 1.00 33.93  ? 258 ASN A C   1 
ATOM   1907 O  O   . ASN A  1  245 ? 43.656  -7.395  24.580 1.00 33.03  ? 258 ASN A O   1 
ATOM   1908 C  CB  . ASN A  1  245 ? 44.949  -6.323  26.747 1.00 33.41  ? 258 ASN A CB  1 
ATOM   1909 C  CG  . ASN A  1  245 ? 46.210  -6.904  26.150 1.00 37.25  ? 258 ASN A CG  1 
ATOM   1910 O  OD1 . ASN A  1  245 ? 46.413  -8.122  26.184 1.00 37.70  ? 258 ASN A OD1 1 
ATOM   1911 N  ND2 . ASN A  1  245 ? 47.056  -6.065  25.580 1.00 48.39  ? 258 ASN A ND2 1 
ATOM   1912 N  N   . GLU A  1  246 ? 43.192  -9.351  25.608 1.00 32.23  ? 259 GLU A N   1 
ATOM   1913 C  CA  . GLU A  1  246 ? 42.854  -10.036 24.369 1.00 34.40  ? 259 GLU A CA  1 
ATOM   1914 C  C   . GLU A  1  246 ? 41.705  -9.295  23.678 1.00 33.08  ? 259 GLU A C   1 
ATOM   1915 O  O   . GLU A  1  246 ? 40.673  -9.001  24.285 1.00 29.46  ? 259 GLU A O   1 
ATOM   1916 C  CB  . GLU A  1  246 ? 42.475  -11.505 24.607 1.00 36.88  ? 259 GLU A CB  1 
ATOM   1917 C  CG  . GLU A  1  246 ? 43.641  -12.371 25.086 1.00 39.52  ? 259 GLU A CG  1 
ATOM   1918 C  CD  . GLU A  1  246 ? 43.995  -12.274 26.575 1.00 40.18  ? 259 GLU A CD  1 
ATOM   1919 O  OE1 . GLU A  1  246 ? 43.349  -11.486 27.302 1.00 35.35  ? 259 GLU A OE1 1 
ATOM   1920 O  OE2 . GLU A  1  246 ? 44.892  -13.019 27.027 1.00 41.73  ? 259 GLU A OE2 1 
ATOM   1921 N  N   . GLY A  1  247 ? 41.913  -8.961  22.397 1.00 33.40  ? 260 GLY A N   1 
ATOM   1922 C  CA  . GLY A  1  247 ? 40.912  -8.323  21.560 1.00 33.93  ? 260 GLY A CA  1 
ATOM   1923 C  C   . GLY A  1  247 ? 41.065  -6.807  21.482 1.00 32.67  ? 260 GLY A C   1 
ATOM   1924 O  O   . GLY A  1  247 ? 40.351  -6.165  20.716 1.00 36.58  ? 260 GLY A O   1 
ATOM   1925 N  N   . ALA A  1  248 ? 41.987  -6.228  22.256 1.00 31.76  ? 261 ALA A N   1 
ATOM   1926 C  CA  . ALA A  1  248 ? 42.183  -4.782  22.242 1.00 34.37  ? 261 ALA A CA  1 
ATOM   1927 C  C   . ALA A  1  248 ? 42.567  -4.283  20.843 1.00 37.16  ? 261 ALA A C   1 
ATOM   1928 O  O   . ALA A  1  248 ? 42.207  -3.171  20.449 1.00 34.81  ? 261 ALA A O   1 
ATOM   1929 C  CB  . ALA A  1  248 ? 43.229  -4.379  23.271 1.00 35.38  ? 261 ALA A CB  1 
ATOM   1930 N  N   . ASP A  1  249 ? 43.327  -5.099  20.113 1.00 37.37  ? 262 ASP A N   1 
ATOM   1931 C  CA  . ASP A  1  249 ? 43.732  -4.802  18.747 1.00 40.07  ? 262 ASP A CA  1 
ATOM   1932 C  C   . ASP A  1  249 ? 42.501  -4.631  17.853 1.00 37.57  ? 262 ASP A C   1 
ATOM   1933 O  O   . ASP A  1  249 ? 42.489  -3.765  16.987 1.00 40.09  ? 262 ASP A O   1 
ATOM   1934 C  CB  . ASP A  1  249 ? 44.680  -5.866  18.206 1.00 43.40  ? 262 ASP A CB  1 
ATOM   1935 C  CG  . ASP A  1  249 ? 44.182  -7.309  18.275 1.00 51.56  ? 262 ASP A CG  1 
ATOM   1936 O  OD1 . ASP A  1  249 ? 43.182  -7.578  19.013 1.00 48.45  ? 262 ASP A OD1 1 
ATOM   1937 O  OD2 . ASP A  1  249 ? 44.802  -8.173  17.610 1.00 60.58  ? 262 ASP A OD2 1 
ATOM   1938 N  N   . GLN A  1  250 ? 41.469  -5.450  18.066 1.00 34.80  ? 263 GLN A N   1 
ATOM   1939 C  CA  . GLN A  1  250 ? 40.264  -5.384  17.255 1.00 38.19  ? 263 GLN A CA  1 
ATOM   1940 C  C   . GLN A  1  250 ? 39.455  -4.134  17.579 1.00 41.00  ? 263 GLN A C   1 
ATOM   1941 O  O   . GLN A  1  250 ? 38.769  -3.604  16.709 1.00 43.33  ? 263 GLN A O   1 
ATOM   1942 C  CB  . GLN A  1  250 ? 39.382  -6.609  17.449 1.00 37.07  ? 263 GLN A CB  1 
ATOM   1943 C  CG  . GLN A  1  250 ? 40.015  -7.902  16.957 1.00 39.69  ? 263 GLN A CG  1 
ATOM   1944 C  CD  . GLN A  1  250 ? 39.093  -9.086  17.155 1.00 41.25  ? 263 GLN A CD  1 
ATOM   1945 O  OE1 . GLN A  1  250 ? 37.958  -9.080  16.678 1.00 44.98  ? 263 GLN A OE1 1 
ATOM   1946 N  NE2 . GLN A  1  250 ? 39.527  -10.079 17.917 1.00 42.76  ? 263 GLN A NE2 1 
ATOM   1947 N  N   . VAL A  1  251 ? 39.534  -3.669  18.829 1.00 35.45  ? 264 VAL A N   1 
ATOM   1948 C  CA  . VAL A  1  251 ? 38.836  -2.465  19.238 1.00 34.93  ? 264 VAL A CA  1 
ATOM   1949 C  C   . VAL A  1  251 ? 39.428  -1.265  18.497 1.00 35.70  ? 264 VAL A C   1 
ATOM   1950 O  O   . VAL A  1  251 ? 38.686  -0.430  17.978 1.00 38.71  ? 264 VAL A O   1 
ATOM   1951 C  CB  . VAL A  1  251 ? 38.875  -2.285  20.766 1.00 34.19  ? 264 VAL A CB  1 
ATOM   1952 C  CG1 . VAL A  1  251 ? 38.383  -0.911  21.193 1.00 36.19  ? 264 VAL A CG1 1 
ATOM   1953 C  CG2 . VAL A  1  251 ? 38.065  -3.358  21.468 1.00 34.69  ? 264 VAL A CG2 1 
ATOM   1954 N  N   . LEU A  1  252 ? 40.761  -1.195  18.441 1.00 33.94  ? 265 LEU A N   1 
ATOM   1955 C  CA  . LEU A  1  252 ? 41.444  -0.154  17.693 1.00 37.84  ? 265 LEU A CA  1 
ATOM   1956 C  C   . LEU A  1  252 ? 41.136  -0.264  16.197 1.00 38.45  ? 265 LEU A C   1 
ATOM   1957 O  O   . LEU A  1  252 ? 40.857  0.748   15.564 1.00 44.94  ? 265 LEU A O   1 
ATOM   1958 C  CB  . LEU A  1  252 ? 42.946  -0.201  17.937 1.00 42.29  ? 265 LEU A CB  1 
ATOM   1959 C  CG  . LEU A  1  252 ? 43.759  0.900   17.246 1.00 44.44  ? 265 LEU A CG  1 
ATOM   1960 C  CD1 . LEU A  1  252 ? 43.383  2.275   17.785 1.00 45.37  ? 265 LEU A CD1 1 
ATOM   1961 C  CD2 . LEU A  1  252 ? 45.244  0.640   17.432 1.00 47.66  ? 265 LEU A CD2 1 
ATOM   1962 N  N   . ALA A  1  253 ? 41.159  -1.483  15.647 1.00 37.10  ? 266 ALA A N   1 
ATOM   1963 C  CA  . ALA A  1  253 ? 40.952  -1.694  14.217 1.00 40.79  ? 266 ALA A CA  1 
ATOM   1964 C  C   . ALA A  1  253 ? 39.554  -1.253  13.769 1.00 46.33  ? 266 ALA A C   1 
ATOM   1965 O  O   . ALA A  1  253 ? 39.387  -0.794  12.644 1.00 43.93  ? 266 ALA A O   1 
ATOM   1966 C  CB  . ALA A  1  253 ? 41.209  -3.148  13.864 1.00 43.88  ? 266 ALA A CB  1 
ATOM   1967 N  N   . ALA A  1  254 ? 38.547  -1.365  14.642 1.00 47.05  ? 267 ALA A N   1 
ATOM   1968 C  CA  . ALA A  1  254 ? 37.185  -0.960  14.320 1.00 45.69  ? 267 ALA A CA  1 
ATOM   1969 C  C   . ALA A  1  254 ? 37.095  0.536   14.022 1.00 46.11  ? 267 ALA A C   1 
ATOM   1970 O  O   . ALA A  1  254 ? 36.231  0.957   13.248 1.00 45.52  ? 267 ALA A O   1 
ATOM   1971 C  CB  . ALA A  1  254 ? 36.246  -1.332  15.455 1.00 45.90  ? 267 ALA A CB  1 
ATOM   1972 N  N   . HIS A  1  255 ? 37.932  1.344   14.690 1.00 42.02  ? 268 HIS A N   1 
ATOM   1973 C  CA  . HIS A  1  255 ? 37.974  2.778   14.450 1.00 40.48  ? 268 HIS A CA  1 
ATOM   1974 C  C   . HIS A  1  255 ? 39.399  3.275   14.667 1.00 40.76  ? 268 HIS A C   1 
ATOM   1975 O  O   . HIS A  1  255 ? 39.716  3.801   15.738 1.00 42.50  ? 268 HIS A O   1 
ATOM   1976 C  CB  . HIS A  1  255 ? 36.988  3.544   15.343 1.00 44.40  ? 268 HIS A CB  1 
ATOM   1977 C  CG  . HIS A  1  255 ? 35.547  3.348   15.023 1.00 48.30  ? 268 HIS A CG  1 
ATOM   1978 N  ND1 . HIS A  1  255 ? 34.927  4.030   14.002 1.00 52.91  ? 268 HIS A ND1 1 
ATOM   1979 C  CD2 . HIS A  1  255 ? 34.600  2.570   15.585 1.00 48.44  ? 268 HIS A CD2 1 
ATOM   1980 C  CE1 . HIS A  1  255 ? 33.651  3.665   13.957 1.00 58.33  ? 268 HIS A CE1 1 
ATOM   1981 N  NE2 . HIS A  1  255 ? 33.427  2.778   14.920 1.00 50.48  ? 268 HIS A NE2 1 
ATOM   1982 N  N   . PRO A  1  256 ? 40.297  3.111   13.665 1.00 38.98  ? 269 PRO A N   1 
ATOM   1983 C  CA  . PRO A  1  256 ? 41.697  3.512   13.800 1.00 41.06  ? 269 PRO A CA  1 
ATOM   1984 C  C   . PRO A  1  256 ? 41.823  4.925   14.341 1.00 39.63  ? 269 PRO A C   1 
ATOM   1985 O  O   . PRO A  1  256 ? 41.039  5.810   13.985 1.00 38.67  ? 269 PRO A O   1 
ATOM   1986 C  CB  . PRO A  1  256 ? 42.244  3.374   12.371 1.00 47.66  ? 269 PRO A CB  1 
ATOM   1987 C  CG  . PRO A  1  256 ? 41.436  2.221   11.811 1.00 47.44  ? 269 PRO A CG  1 
ATOM   1988 C  CD  . PRO A  1  256 ? 40.025  2.464   12.375 1.00 43.79  ? 269 PRO A CD  1 
ATOM   1989 N  N   . TRP A  1  257 ? 42.763  5.095   15.273 1.00 37.02  ? 270 TRP A N   1 
ATOM   1990 C  CA  . TRP A  1  257 ? 42.904  6.353   15.990 1.00 37.55  ? 270 TRP A CA  1 
ATOM   1991 C  C   . TRP A  1  257 ? 44.369  6.553   16.374 1.00 39.09  ? 270 TRP A C   1 
ATOM   1992 O  O   . TRP A  1  257 ? 45.090  5.590   16.625 1.00 41.26  ? 270 TRP A O   1 
ATOM   1993 C  CB  . TRP A  1  257 ? 41.992  6.358   17.229 1.00 39.50  ? 270 TRP A CB  1 
ATOM   1994 C  CG  . TRP A  1  257 ? 41.869  7.730   17.828 1.00 36.59  ? 270 TRP A CG  1 
ATOM   1995 C  CD1 . TRP A  1  257 ? 42.533  8.232   18.901 1.00 38.06  ? 270 TRP A CD1 1 
ATOM   1996 C  CD2 . TRP A  1  257 ? 41.119  8.829   17.268 1.00 39.34  ? 270 TRP A CD2 1 
ATOM   1997 N  NE1 . TRP A  1  257 ? 42.217  9.551   19.082 1.00 39.60  ? 270 TRP A NE1 1 
ATOM   1998 C  CE2 . TRP A  1  257 ? 41.367  9.948   18.086 1.00 38.45  ? 270 TRP A CE2 1 
ATOM   1999 C  CE3 . TRP A  1  257 ? 40.281  8.971   16.154 1.00 41.32  ? 270 TRP A CE3 1 
ATOM   2000 C  CZ2 . TRP A  1  257 ? 40.800  11.190  17.834 1.00 44.12  ? 270 TRP A CZ2 1 
ATOM   2001 C  CZ3 . TRP A  1  257 ? 39.721  10.206  15.906 1.00 42.89  ? 270 TRP A CZ3 1 
ATOM   2002 C  CH2 . TRP A  1  257 ? 39.995  11.303  16.722 1.00 44.21  ? 270 TRP A CH2 1 
ATOM   2003 N  N   . VAL A  1  258 ? 44.775  7.817   16.463 1.00 40.37  ? 271 VAL A N   1 
ATOM   2004 C  CA  . VAL A  1  258 ? 46.158  8.187   16.653 1.00 40.33  ? 271 VAL A CA  1 
ATOM   2005 C  C   . VAL A  1  258 ? 46.285  8.971   17.952 1.00 38.12  ? 271 VAL A C   1 
ATOM   2006 O  O   . VAL A  1  258 ? 45.454  9.816   18.250 1.00 42.88  ? 271 VAL A O   1 
ATOM   2007 C  CB  . VAL A  1  258 ? 46.593  9.012   15.424 1.00 45.85  ? 271 VAL A CB  1 
ATOM   2008 C  CG1 . VAL A  1  258 ? 47.893  9.777   15.620 1.00 51.95  ? 271 VAL A CG1 1 
ATOM   2009 C  CG2 . VAL A  1  258 ? 46.689  8.118   14.196 1.00 48.85  ? 271 VAL A CG2 1 
ATOM   2010 N  N   . PRO A  1  259 ? 47.342  8.735   18.753 1.00 37.15  ? 272 PRO A N   1 
ATOM   2011 C  CA  . PRO A  1  259 ? 47.525  9.477   19.995 1.00 37.69  ? 272 PRO A CA  1 
ATOM   2012 C  C   . PRO A  1  259 ? 47.639  10.971  19.724 1.00 40.34  ? 272 PRO A C   1 
ATOM   2013 O  O   . PRO A  1  259 ? 48.170  11.381  18.699 1.00 48.69  ? 272 PRO A O   1 
ATOM   2014 C  CB  . PRO A  1  259 ? 48.796  8.873   20.610 1.00 38.47  ? 272 PRO A CB  1 
ATOM   2015 C  CG  . PRO A  1  259 ? 49.505  8.238   19.435 1.00 37.44  ? 272 PRO A CG  1 
ATOM   2016 C  CD  . PRO A  1  259 ? 48.393  7.729   18.535 1.00 36.83  ? 272 PRO A CD  1 
ATOM   2017 N  N   . GLY A  1  260 ? 47.144  11.770  20.664 1.00 38.33  ? 273 GLY A N   1 
ATOM   2018 C  CA  . GLY A  1  260 ? 47.143  13.212  20.542 1.00 39.71  ? 273 GLY A CA  1 
ATOM   2019 C  C   . GLY A  1  260 ? 46.300  13.841  21.645 1.00 44.26  ? 273 GLY A C   1 
ATOM   2020 O  O   . GLY A  1  260 ? 46.206  13.288  22.747 1.00 41.71  ? 273 GLY A O   1 
ATOM   2021 N  N   . GLY A  1  261 ? 45.711  15.001  21.330 1.00 40.45  ? 274 GLY A N   1 
ATOM   2022 C  CA  . GLY A  1  261 ? 44.910  15.761  22.274 1.00 44.51  ? 274 GLY A CA  1 
ATOM   2023 C  C   . GLY A  1  261 ? 44.348  17.029  21.633 1.00 42.91  ? 274 GLY A C   1 
ATOM   2024 O  O   . GLY A  1  261 ? 44.755  17.399  20.541 1.00 46.56  ? 274 GLY A O   1 
ATOM   2025 N  N   . ASN A  1  262 ? 43.387  17.663  22.312 1.00 42.03  ? 275 ASN A N   1 
ATOM   2026 C  CA  . ASN A  1  262 ? 42.913  18.987  21.943 1.00 45.78  ? 275 ASN A CA  1 
ATOM   2027 C  C   . ASN A  1  262 ? 44.022  20.000  22.227 1.00 47.29  ? 275 ASN A C   1 
ATOM   2028 O  O   . ASN A  1  262 ? 44.497  20.084  23.358 1.00 46.24  ? 275 ASN A O   1 
ATOM   2029 C  CB  . ASN A  1  262 ? 41.662  19.393  22.714 1.00 41.46  ? 275 ASN A CB  1 
ATOM   2030 C  CG  . ASN A  1  262 ? 40.375  18.909  22.089 1.00 42.51  ? 275 ASN A CG  1 
ATOM   2031 O  OD1 . ASN A  1  262 ? 40.317  18.655  20.881 1.00 42.17  ? 275 ASN A OD1 1 
ATOM   2032 N  ND2 . ASN A  1  262 ? 39.322  18.775  22.887 1.00 44.87  ? 275 ASN A ND2 1 
ATOM   2033 N  N   . ALA A  1  263 ? 44.412  20.779  21.207 1.00 50.93  ? 276 ALA A N   1 
ATOM   2034 C  CA  . ALA A  1  263 ? 45.433  21.804  21.390 1.00 54.44  ? 276 ALA A CA  1 
ATOM   2035 C  C   . ALA A  1  263 ? 44.805  23.143  21.783 1.00 54.13  ? 276 ALA A C   1 
ATOM   2036 O  O   . ALA A  1  263 ? 43.642  23.417  21.478 1.00 57.35  ? 276 ALA A O   1 
ATOM   2037 C  CB  . ALA A  1  263 ? 46.268  21.927  20.128 1.00 58.59  ? 276 ALA A CB  1 
ATOM   2038 N  N   . ASP A  1  264 ? 45.602  23.956  22.491 1.00 58.93  ? 277 ASP A N   1 
ATOM   2039 C  CA  . ASP A  1  264 ? 45.348  25.377  22.714 1.00 65.70  ? 277 ASP A CA  1 
ATOM   2040 C  C   . ASP A  1  264 ? 44.052  25.595  23.493 1.00 63.98  ? 277 ASP A C   1 
ATOM   2041 O  O   . ASP A  1  264 ? 43.363  26.586  23.261 1.00 53.52  ? 277 ASP A O   1 
ATOM   2042 C  CB  . ASP A  1  264 ? 45.351  26.170  21.411 1.00 71.91  ? 277 ASP A CB  1 
ATOM   2043 C  CG  . ASP A  1  264 ? 46.614  26.041  20.567 1.00 82.23  ? 277 ASP A CG  1 
ATOM   2044 O  OD1 . ASP A  1  264 ? 47.713  26.232  21.138 1.00 85.96  ? 277 ASP A OD1 1 
ATOM   2045 O  OD2 . ASP A  1  264 ? 46.491  25.754  19.346 1.00 81.73  ? 277 ASP A OD2 1 
ATOM   2046 N  N   . ASN A  1  265 ? 43.732  24.670  24.409 1.00 59.03  ? 278 ASN A N   1 
ATOM   2047 C  CA  . ASN A  1  265 ? 42.632  24.840  25.339 1.00 55.94  ? 278 ASN A CA  1 
ATOM   2048 C  C   . ASN A  1  265 ? 41.322  25.080  24.589 1.00 48.17  ? 278 ASN A C   1 
ATOM   2049 O  O   . ASN A  1  265 ? 40.491  25.874  25.014 1.00 48.98  ? 278 ASN A O   1 
ATOM   2050 C  CB  . ASN A  1  265 ? 42.959  25.921  26.362 1.00 59.27  ? 278 ASN A CB  1 
ATOM   2051 C  CG  . ASN A  1  265 ? 42.114  25.786  27.609 1.00 68.97  ? 278 ASN A CG  1 
ATOM   2052 O  OD1 . ASN A  1  265 ? 41.915  24.676  28.119 1.00 76.89  ? 278 ASN A OD1 1 
ATOM   2053 N  ND2 . ASN A  1  265 ? 41.587  26.892  28.113 1.00 71.37  ? 278 ASN A ND2 1 
ATOM   2054 N  N   . GLN A  1  266 ? 41.126  24.344  23.496 1.00 47.83  ? 279 GLN A N   1 
ATOM   2055 C  CA  . GLN A  1  266 ? 39.920  24.455  22.690 1.00 52.69  ? 279 GLN A CA  1 
ATOM   2056 C  C   . GLN A  1  266 ? 39.341  23.076  22.405 1.00 48.40  ? 279 GLN A C   1 
ATOM   2057 O  O   . GLN A  1  266 ? 40.083  22.131  22.168 1.00 49.50  ? 279 GLN A O   1 
ATOM   2058 C  CB  . GLN A  1  266 ? 40.222  25.126  21.350 1.00 60.33  ? 279 GLN A CB  1 
ATOM   2059 C  CG  . GLN A  1  266 ? 40.341  26.642  21.476 1.00 69.32  ? 279 GLN A CG  1 
ATOM   2060 C  CD  . GLN A  1  266 ? 40.844  27.317  20.224 1.00 78.44  ? 279 GLN A CD  1 
ATOM   2061 O  OE1 . GLN A  1  266 ? 41.097  26.679  19.196 1.00 73.17  ? 279 GLN A OE1 1 
ATOM   2062 N  NE2 . GLN A  1  266 ? 40.972  28.631  20.303 1.00 87.76  ? 279 GLN A NE2 1 
ATOM   2063 N  N   . VAL A  1  267 ? 38.013  22.998  22.370 1.00 42.89  ? 280 VAL A N   1 
ATOM   2064 C  CA  . VAL A  1  267 ? 37.330  21.792  21.941 1.00 45.07  ? 280 VAL A CA  1 
ATOM   2065 C  C   . VAL A  1  267 ? 37.420  21.661  20.421 1.00 49.89  ? 280 VAL A C   1 
ATOM   2066 O  O   . VAL A  1  267 ? 37.860  22.572  19.740 1.00 55.62  ? 280 VAL A O   1 
ATOM   2067 C  CB  . VAL A  1  267 ? 35.877  21.757  22.449 1.00 47.52  ? 280 VAL A CB  1 
ATOM   2068 C  CG1 . VAL A  1  267 ? 35.832  21.738  23.973 1.00 47.95  ? 280 VAL A CG1 1 
ATOM   2069 C  CG2 . VAL A  1  267 ? 35.031  22.907  21.911 1.00 49.27  ? 280 VAL A CG2 1 
ATOM   2070 N  N   . ASN A  1  268 ? 37.046  20.480  19.922 1.00 49.95  ? 281 ASN A N   1 
ATOM   2071 C  CA  . ASN A  1  268 ? 37.069  20.125  18.511 1.00 55.31  ? 281 ASN A CA  1 
ATOM   2072 C  C   . ASN A  1  268 ? 38.367  20.574  17.850 1.00 56.78  ? 281 ASN A C   1 
ATOM   2073 O  O   . ASN A  1  268 ? 38.345  21.108  16.748 1.00 49.52  ? 281 ASN A O   1 
ATOM   2074 C  CB  . ASN A  1  268 ? 35.847  20.666  17.783 1.00 55.43  ? 281 ASN A CB  1 
ATOM   2075 C  CG  . ASN A  1  268 ? 34.583  20.062  18.336 1.00 53.54  ? 281 ASN A CG  1 
ATOM   2076 O  OD1 . ASN A  1  268 ? 34.365  18.850  18.215 1.00 64.78  ? 281 ASN A OD1 1 
ATOM   2077 N  ND2 . ASN A  1  268 ? 33.753  20.884  18.951 1.00 51.86  ? 281 ASN A ND2 1 
ATOM   2078 N  N   . ASN A  1  269 ? 39.495  20.293  18.501 1.00 52.50  ? 282 ASN A N   1 
ATOM   2079 C  CA  . ASN A  1  269 ? 40.775  20.774  18.017 1.00 50.13  ? 282 ASN A CA  1 
ATOM   2080 C  C   . ASN A  1  269 ? 41.849  19.714  18.267 1.00 44.54  ? 282 ASN A C   1 
ATOM   2081 O  O   . ASN A  1  269 ? 42.900  20.005  18.839 1.00 42.88  ? 282 ASN A O   1 
ATOM   2082 C  CB  . ASN A  1  269 ? 41.065  22.147  18.621 1.00 50.43  ? 282 ASN A CB  1 
ATOM   2083 C  CG  . ASN A  1  269 ? 42.233  22.816  17.934 1.00 48.70  ? 282 ASN A CG  1 
ATOM   2084 O  OD1 . ASN A  1  269 ? 42.382  22.677  16.717 1.00 50.57  ? 282 ASN A OD1 1 
ATOM   2085 N  ND2 . ASN A  1  269 ? 43.091  23.479  18.695 1.00 49.18  ? 282 ASN A ND2 1 
ATOM   2086 N  N   . TYR A  1  270 ? 41.591  18.487  17.796 1.00 46.51  ? 283 TYR A N   1 
ATOM   2087 C  CA  . TYR A  1  270 ? 42.449  17.358  18.122 1.00 46.53  ? 283 TYR A CA  1 
ATOM   2088 C  C   . TYR A  1  270 ? 43.652  17.309  17.179 1.00 44.58  ? 283 TYR A C   1 
ATOM   2089 O  O   . TYR A  1  270 ? 43.476  17.143  15.979 1.00 42.45  ? 283 TYR A O   1 
ATOM   2090 C  CB  . TYR A  1  270 ? 41.662  16.048  18.032 1.00 45.48  ? 283 TYR A CB  1 
ATOM   2091 C  CG  . TYR A  1  270 ? 42.394  14.815  18.550 1.00 42.47  ? 283 TYR A CG  1 
ATOM   2092 C  CD1 . TYR A  1  270 ? 42.331  14.464  19.893 1.00 42.63  ? 283 TYR A CD1 1 
ATOM   2093 C  CD2 . TYR A  1  270 ? 43.136  13.994  17.707 1.00 41.96  ? 283 TYR A CD2 1 
ATOM   2094 C  CE1 . TYR A  1  270 ? 42.975  13.337  20.382 1.00 41.17  ? 283 TYR A CE1 1 
ATOM   2095 C  CE2 . TYR A  1  270 ? 43.793  12.866  18.184 1.00 40.37  ? 283 TYR A CE2 1 
ATOM   2096 C  CZ  . TYR A  1  270 ? 43.705  12.533  19.524 1.00 39.83  ? 283 TYR A CZ  1 
ATOM   2097 O  OH  . TYR A  1  270 ? 44.317  11.411  19.998 1.00 40.04  ? 283 TYR A OH  1 
ATOM   2098 N  N   . VAL A  1  271 ? 44.861  17.371  17.754 1.00 44.99  ? 284 VAL A N   1 
ATOM   2099 C  CA  . VAL A  1  271 ? 46.119  17.305  17.020 1.00 49.72  ? 284 VAL A CA  1 
ATOM   2100 C  C   . VAL A  1  271 ? 46.884  16.033  17.396 1.00 47.55  ? 284 VAL A C   1 
ATOM   2101 O  O   . VAL A  1  271 ? 47.076  15.760  18.580 1.00 45.88  ? 284 VAL A O   1 
ATOM   2102 C  CB  . VAL A  1  271 ? 46.947  18.561  17.366 1.00 53.39  ? 284 VAL A CB  1 
ATOM   2103 C  CG1 . VAL A  1  271 ? 48.357  18.525  16.779 1.00 54.00  ? 284 VAL A CG1 1 
ATOM   2104 C  CG2 . VAL A  1  271 ? 46.224  19.841  16.961 1.00 54.00  ? 284 VAL A CG2 1 
ATOM   2105 N  N   . GLU A  1  272 ? 47.383  15.320  16.383 1.00 48.65  ? 285 GLU A N   1 
ATOM   2106 C  CA  A GLU A  1  272 ? 48.159  14.110  16.587 0.50 46.00  ? 285 GLU A CA  1 
ATOM   2107 C  CA  B GLU A  1  272 ? 48.169  14.109  16.571 0.50 48.79  ? 285 GLU A CA  1 
ATOM   2108 C  C   . GLU A  1  272 ? 49.485  14.455  17.268 1.00 48.74  ? 285 GLU A C   1 
ATOM   2109 O  O   . GLU A  1  272 ? 50.033  15.541  17.079 1.00 50.19  ? 285 GLU A O   1 
ATOM   2110 C  CB  A GLU A  1  272 ? 48.316  13.399  15.243 0.50 45.63  ? 285 GLU A CB  1 
ATOM   2111 C  CB  B GLU A  1  272 ? 48.444  13.384  15.246 0.50 52.81  ? 285 GLU A CB  1 
ATOM   2112 C  CG  A GLU A  1  272 ? 46.980  13.040  14.594 0.50 45.34  ? 285 GLU A CG  1 
ATOM   2113 C  CG  B GLU A  1  272 ? 49.682  12.480  15.302 0.50 56.38  ? 285 GLU A CG  1 
ATOM   2114 C  CD  A GLU A  1  272 ? 47.049  12.467  13.191 0.50 43.27  ? 285 GLU A CD  1 
ATOM   2115 C  CD  B GLU A  1  272 ? 50.047  11.634  14.089 0.50 56.90  ? 285 GLU A CD  1 
ATOM   2116 O  OE1 A GLU A  1  272 ? 48.147  12.163  12.696 0.50 42.78  ? 285 GLU A OE1 1 
ATOM   2117 O  OE1 B GLU A  1  272 ? 49.401  11.753  13.028 0.50 56.18  ? 285 GLU A OE1 1 
ATOM   2118 O  OE2 A GLU A  1  272 ? 45.968  12.326  12.596 0.50 44.44  ? 285 GLU A OE2 1 
ATOM   2119 O  OE2 B GLU A  1  272 ? 50.987  10.821  14.226 0.50 56.45  ? 285 GLU A OE2 1 
ATOM   2120 N  N   . ASP A  1  273 ? 49.977  13.522  18.103 1.00 49.25  ? 286 ASP A N   1 
ATOM   2121 C  CA  . ASP A  1  273 ? 51.304  13.597  18.692 1.00 49.02  ? 286 ASP A CA  1 
ATOM   2122 C  C   . ASP A  1  273 ? 52.149  12.457  18.129 1.00 53.62  ? 286 ASP A C   1 
ATOM   2123 O  O   . ASP A  1  273 ? 51.981  11.306  18.532 1.00 48.25  ? 286 ASP A O   1 
ATOM   2124 C  CB  . ASP A  1  273 ? 51.277  13.529  20.208 1.00 51.35  ? 286 ASP A CB  1 
ATOM   2125 C  CG  . ASP A  1  273 ? 52.641  13.573  20.879 1.00 55.49  ? 286 ASP A CG  1 
ATOM   2126 O  OD1 . ASP A  1  273 ? 53.659  13.617  20.153 1.00 54.71  ? 286 ASP A OD1 1 
ATOM   2127 O  OD2 . ASP A  1  273 ? 52.668  13.567  22.122 1.00 55.93  ? 286 ASP A OD2 1 
ATOM   2128 N  N   . PRO A  1  274 ? 53.087  12.740  17.192 1.00 56.28  ? 287 PRO A N   1 
ATOM   2129 C  CA  . PRO A  1  274 ? 53.874  11.686  16.546 1.00 52.48  ? 287 PRO A CA  1 
ATOM   2130 C  C   . PRO A  1  274 ? 54.939  11.044  17.434 1.00 45.17  ? 287 PRO A C   1 
ATOM   2131 O  O   . PRO A  1  274 ? 55.451  9.979   17.104 1.00 43.36  ? 287 PRO A O   1 
ATOM   2132 C  CB  . PRO A  1  274 ? 54.505  12.433  15.343 1.00 56.30  ? 287 PRO A CB  1 
ATOM   2133 C  CG  . PRO A  1  274 ? 54.671  13.849  15.839 1.00 58.84  ? 287 PRO A CG  1 
ATOM   2134 C  CD  . PRO A  1  274 ? 53.452  14.089  16.722 1.00 59.81  ? 287 PRO A CD  1 
ATOM   2135 N  N   . ASP A  1  275 ? 55.269  11.700  18.554 1.00 43.78  ? 288 ASP A N   1 
ATOM   2136 C  CA  . ASP A  1  275 ? 56.267  11.227  19.502 1.00 46.35  ? 288 ASP A CA  1 
ATOM   2137 C  C   . ASP A  1  275 ? 55.678  10.259  20.537 1.00 49.27  ? 288 ASP A C   1 
ATOM   2138 O  O   . ASP A  1  275 ? 56.429  9.637   21.284 1.00 42.65  ? 288 ASP A O   1 
ATOM   2139 C  CB  . ASP A  1  275 ? 56.910  12.401  20.227 1.00 51.76  ? 288 ASP A CB  1 
ATOM   2140 C  CG  . ASP A  1  275 ? 57.697  13.354  19.336 1.00 60.71  ? 288 ASP A CG  1 
ATOM   2141 O  OD1 . ASP A  1  275 ? 57.944  12.973  18.162 1.00 58.40  ? 288 ASP A OD1 1 
ATOM   2142 O  OD2 . ASP A  1  275 ? 58.019  14.464  19.814 1.00 69.74  ? 288 ASP A OD2 1 
ATOM   2143 N  N   . SER A  1  276 ? 54.343  10.153  20.607 1.00 44.59  ? 289 SER A N   1 
ATOM   2144 C  CA  . SER A  1  276 ? 53.682  9.341   21.616 1.00 43.28  ? 289 SER A CA  1 
ATOM   2145 C  C   . SER A  1  276 ? 53.935  7.863   21.364 1.00 37.53  ? 289 SER A C   1 
ATOM   2146 O  O   . SER A  1  276 ? 54.081  7.426   20.228 1.00 37.38  ? 289 SER A O   1 
ATOM   2147 C  CB  . SER A  1  276 ? 52.189  9.625   21.645 1.00 45.07  ? 289 SER A CB  1 
ATOM   2148 O  OG  . SER A  1  276 ? 51.479  8.636   22.379 1.00 43.84  ? 289 SER A OG  1 
ATOM   2149 N  N   . ALA A  1  277 ? 53.913  7.076   22.442 1.00 38.50  ? 290 ALA A N   1 
ATOM   2150 C  CA  . ALA A  1  277 ? 53.768  5.638   22.303 1.00 36.10  ? 290 ALA A CA  1 
ATOM   2151 C  C   . ALA A  1  277 ? 52.501  5.322   21.520 1.00 34.97  ? 290 ALA A C   1 
ATOM   2152 O  O   . ALA A  1  277 ? 51.547  6.092   21.529 1.00 37.60  ? 290 ALA A O   1 
ATOM   2153 C  CB  . ALA A  1  277 ? 53.730  4.984   23.661 1.00 40.01  ? 290 ALA A CB  1 
ATOM   2154 N  N   . ASP A  1  278 ? 52.519  4.177   20.840 1.00 34.79  ? 291 ASP A N   1 
ATOM   2155 C  CA  . ASP A  1  278 ? 51.342  3.582   20.227 1.00 36.21  ? 291 ASP A CA  1 
ATOM   2156 C  C   . ASP A  1  278 ? 51.605  2.086   20.195 1.00 35.28  ? 291 ASP A C   1 
ATOM   2157 O  O   . ASP A  1  278 ? 52.628  1.642   20.714 1.00 36.31  ? 291 ASP A O   1 
ATOM   2158 C  CB  . ASP A  1  278 ? 51.015  4.187   18.869 1.00 41.35  ? 291 ASP A CB  1 
ATOM   2159 C  CG  . ASP A  1  278 ? 52.056  3.986   17.771 1.00 46.87  ? 291 ASP A CG  1 
ATOM   2160 O  OD1 . ASP A  1  278 ? 52.746  2.939   17.793 1.00 47.86  ? 291 ASP A OD1 1 
ATOM   2161 O  OD2 . ASP A  1  278 ? 52.166  4.895   16.914 1.00 51.91  ? 291 ASP A OD2 1 
ATOM   2162 N  N   . PHE A  1  279 ? 50.719  1.316   19.569 1.00 34.24  ? 292 PHE A N   1 
ATOM   2163 C  CA  . PHE A  1  279 ? 50.775  -0.132  19.706 1.00 37.75  ? 292 PHE A CA  1 
ATOM   2164 C  C   . PHE A  1  279 ? 51.909  -0.755  18.889 1.00 42.11  ? 292 PHE A C   1 
ATOM   2165 O  O   . PHE A  1  279 ? 52.252  -1.907  19.145 1.00 43.08  ? 292 PHE A O   1 
ATOM   2166 C  CB  . PHE A  1  279 ? 49.407  -0.739  19.410 1.00 39.86  ? 292 PHE A CB  1 
ATOM   2167 C  CG  . PHE A  1  279 ? 48.447  -0.486  20.567 1.00 40.21  ? 292 PHE A CG  1 
ATOM   2168 C  CD1 . PHE A  1  279 ? 48.510  -1.259  21.718 1.00 41.01  ? 292 PHE A CD1 1 
ATOM   2169 C  CD2 . PHE A  1  279 ? 47.515  0.541   20.512 1.00 38.65  ? 292 PHE A CD2 1 
ATOM   2170 C  CE1 . PHE A  1  279 ? 47.642  -1.033  22.778 1.00 40.92  ? 292 PHE A CE1 1 
ATOM   2171 C  CE2 . PHE A  1  279 ? 46.631  0.756   21.568 1.00 42.16  ? 292 PHE A CE2 1 
ATOM   2172 C  CZ  . PHE A  1  279 ? 46.708  -0.027  22.700 1.00 41.72  ? 292 PHE A CZ  1 
ATOM   2173 N  N   . THR A  1  280 ? 52.540  -0.007  17.974 1.00 42.28  ? 293 THR A N   1 
ATOM   2174 C  CA  . THR A  1  280 ? 53.746  -0.511  17.325 1.00 48.07  ? 293 THR A CA  1 
ATOM   2175 C  C   . THR A  1  280 ? 54.991  0.197   17.867 1.00 51.80  ? 293 THR A C   1 
ATOM   2176 O  O   . THR A  1  280 ? 56.078  0.006   17.327 1.00 44.85  ? 293 THR A O   1 
ATOM   2177 C  CB  . THR A  1  280 ? 53.643  -0.369  15.801 1.00 48.99  ? 293 THR A CB  1 
ATOM   2178 O  OG1 . THR A  1  280 ? 53.474  1.013   15.495 1.00 46.89  ? 293 THR A OG1 1 
ATOM   2179 C  CG2 . THR A  1  280 ? 52.484  -1.155  15.214 1.00 50.46  ? 293 THR A CG2 1 
ATOM   2180 N  N   . HIS A  1  281 ? 54.840  1.012   18.924 1.00 49.25  ? 294 HIS A N   1 
ATOM   2181 C  CA  . HIS A  1  281 ? 55.973  1.701   19.532 1.00 46.12  ? 294 HIS A CA  1 
ATOM   2182 C  C   . HIS A  1  281 ? 55.838  1.694   21.055 1.00 44.11  ? 294 HIS A C   1 
ATOM   2183 O  O   . HIS A  1  281 ? 55.857  2.748   21.695 1.00 40.20  ? 294 HIS A O   1 
ATOM   2184 C  CB  . HIS A  1  281 ? 56.097  3.145   19.025 1.00 49.53  ? 294 HIS A CB  1 
ATOM   2185 C  CG  . HIS A  1  281 ? 56.290  3.293   17.554 1.00 60.08  ? 294 HIS A CG  1 
ATOM   2186 N  ND1 . HIS A  1  281 ? 55.227  3.484   16.696 1.00 64.68  ? 294 HIS A ND1 1 
ATOM   2187 C  CD2 . HIS A  1  281 ? 57.393  3.304   16.795 1.00 62.31  ? 294 HIS A CD2 1 
ATOM   2188 C  CE1 . HIS A  1  281 ? 55.682  3.599   15.459 1.00 68.55  ? 294 HIS A CE1 1 
ATOM   2189 N  NE2 . HIS A  1  281 ? 56.994  3.485   15.499 1.00 63.47  ? 294 HIS A NE2 1 
ATOM   2190 N  N   . LEU A  1  282 ? 55.705  0.497   21.633 1.00 41.89  ? 295 LEU A N   1 
ATOM   2191 C  CA  . LEU A  1  282 ? 55.345  0.357   23.034 1.00 42.58  ? 295 LEU A CA  1 
ATOM   2192 C  C   . LEU A  1  282 ? 56.488  0.797   23.941 1.00 41.35  ? 295 LEU A C   1 
ATOM   2193 O  O   . LEU A  1  282 ? 56.234  1.282   25.040 1.00 41.33  ? 295 LEU A O   1 
ATOM   2194 C  CB  . LEU A  1  282 ? 54.936  -1.081  23.336 1.00 42.44  ? 295 LEU A CB  1 
ATOM   2195 C  CG  . LEU A  1  282 ? 53.582  -1.527  22.789 1.00 41.95  ? 295 LEU A CG  1 
ATOM   2196 C  CD1 . LEU A  1  282 ? 53.377  -3.037  22.959 1.00 44.68  ? 295 LEU A CD1 1 
ATOM   2197 C  CD2 . LEU A  1  282 ? 52.468  -0.753  23.463 1.00 42.59  ? 295 LEU A CD2 1 
ATOM   2198 N  N   . CYS A  1  283 ? 57.741  0.626   23.502 1.00 39.26  ? 296 CYS A N   1 
ATOM   2199 C  CA  . CYS A  1  283 ? 58.874  0.943   24.356 1.00 42.18  ? 296 CYS A CA  1 
ATOM   2200 C  C   . CYS A  1  283 ? 58.930  2.438   24.660 1.00 40.54  ? 296 CYS A C   1 
ATOM   2201 O  O   . CYS A  1  283 ? 59.481  2.830   25.687 1.00 39.88  ? 296 CYS A O   1 
ATOM   2202 C  CB  . CYS A  1  283 ? 60.200  0.438   23.783 1.00 50.06  ? 296 CYS A CB  1 
ATOM   2203 S  SG  . CYS A  1  283 ? 60.404  -1.363  23.896 1.00 61.02  ? 296 CYS A SG  1 
ATOM   2204 N  N   . ARG A  1  284 ? 58.322  3.272   23.806 1.00 39.04  ? 297 ARG A N   1 
ATOM   2205 C  CA  . ARG A  1  284 ? 58.215  4.686   24.115 1.00 40.98  ? 297 ARG A CA  1 
ATOM   2206 C  C   . ARG A  1  284 ? 57.479  4.902   25.437 1.00 37.61  ? 297 ARG A C   1 
ATOM   2207 O  O   . ARG A  1  284 ? 57.768  5.858   26.144 1.00 38.76  ? 297 ARG A O   1 
ATOM   2208 C  CB  . ARG A  1  284 ? 57.449  5.463   23.044 1.00 45.51  ? 297 ARG A CB  1 
ATOM   2209 C  CG  . ARG A  1  284 ? 58.222  5.599   21.746 1.00 46.20  ? 297 ARG A CG  1 
ATOM   2210 C  CD  . ARG A  1  284 ? 57.393  6.344   20.736 1.00 48.13  ? 297 ARG A CD  1 
ATOM   2211 N  NE  . ARG A  1  284 ? 58.001  6.302   19.407 1.00 51.24  ? 297 ARG A NE  1 
ATOM   2212 C  CZ  . ARG A  1  284 ? 57.536  6.926   18.331 1.00 57.88  ? 297 ARG A CZ  1 
ATOM   2213 N  NH1 . ARG A  1  284 ? 56.390  7.582   18.371 1.00 51.74  ? 297 ARG A NH1 1 
ATOM   2214 N  NH2 . ARG A  1  284 ? 58.195  6.848   17.187 1.00 61.16  ? 297 ARG A NH2 1 
ATOM   2215 N  N   . LEU A  1  285 ? 56.511  4.032   25.747 1.00 35.17  ? 298 LEU A N   1 
ATOM   2216 C  CA  . LEU A  1  285 ? 55.761  4.150   26.987 1.00 35.03  ? 298 LEU A CA  1 
ATOM   2217 C  C   . LEU A  1  285 ? 56.712  3.923   28.159 1.00 33.49  ? 298 LEU A C   1 
ATOM   2218 O  O   . LEU A  1  285 ? 56.672  4.672   29.124 1.00 33.49  ? 298 LEU A O   1 
ATOM   2219 C  CB  . LEU A  1  285 ? 54.564  3.204   27.012 1.00 35.64  ? 298 LEU A CB  1 
ATOM   2220 C  CG  . LEU A  1  285 ? 53.623  3.321   28.218 1.00 38.18  ? 298 LEU A CG  1 
ATOM   2221 C  CD1 . LEU A  1  285 ? 52.240  2.784   27.878 1.00 38.40  ? 298 LEU A CD1 1 
ATOM   2222 C  CD2 . LEU A  1  285 ? 54.144  2.574   29.426 1.00 40.66  ? 298 LEU A CD2 1 
ATOM   2223 N  N   . TYR A  1  286 ? 57.580  2.916   28.059 1.00 36.36  ? 299 TYR A N   1 
ATOM   2224 C  CA  . TYR A  1  286 ? 58.550  2.630   29.110 1.00 37.26  ? 299 TYR A CA  1 
ATOM   2225 C  C   . TYR A  1  286 ? 59.463  3.841   29.325 1.00 33.95  ? 299 TYR A C   1 
ATOM   2226 O  O   . TYR A  1  286 ? 59.655  4.289   30.455 1.00 38.34  ? 299 TYR A O   1 
ATOM   2227 C  CB  . TYR A  1  286 ? 59.338  1.356   28.782 1.00 35.06  ? 299 TYR A CB  1 
ATOM   2228 C  CG  . TYR A  1  286 ? 60.509  1.083   29.713 1.00 35.63  ? 299 TYR A CG  1 
ATOM   2229 C  CD1 . TYR A  1  286 ? 60.306  0.760   31.048 1.00 35.62  ? 299 TYR A CD1 1 
ATOM   2230 C  CD2 . TYR A  1  286 ? 61.821  1.155   29.261 1.00 36.32  ? 299 TYR A CD2 1 
ATOM   2231 C  CE1 . TYR A  1  286 ? 61.367  0.517   31.907 1.00 33.71  ? 299 TYR A CE1 1 
ATOM   2232 C  CE2 . TYR A  1  286 ? 62.888  0.937   30.118 1.00 36.94  ? 299 TYR A CE2 1 
ATOM   2233 C  CZ  . TYR A  1  286 ? 62.666  0.626   31.446 1.00 34.38  ? 299 TYR A CZ  1 
ATOM   2234 O  OH  . TYR A  1  286 ? 63.730  0.398   32.279 1.00 31.77  ? 299 TYR A OH  1 
ATOM   2235 N  N   . GLU A  1  287 ? 60.008  4.382   28.237 1.00 34.90  ? 300 GLU A N   1 
ATOM   2236 C  CA  . GLU A  1  287 ? 60.946  5.498   28.317 1.00 40.54  ? 300 GLU A CA  1 
ATOM   2237 C  C   . GLU A  1  287 ? 60.246  6.722   28.907 1.00 36.02  ? 300 GLU A C   1 
ATOM   2238 O  O   . GLU A  1  287 ? 60.797  7.395   29.773 1.00 33.93  ? 300 GLU A O   1 
ATOM   2239 C  CB  . GLU A  1  287 ? 61.557  5.799   26.946 1.00 42.43  ? 300 GLU A CB  1 
ATOM   2240 C  CG  . GLU A  1  287 ? 62.458  4.667   26.450 1.00 52.98  ? 300 GLU A CG  1 
ATOM   2241 C  CD  . GLU A  1  287 ? 62.865  4.713   24.976 1.00 67.27  ? 300 GLU A CD  1 
ATOM   2242 O  OE1 . GLU A  1  287 ? 62.039  5.101   24.114 1.00 69.39  ? 300 GLU A OE1 1 
ATOM   2243 O  OE2 . GLU A  1  287 ? 64.019  4.322   24.668 1.00 78.99  ? 300 GLU A OE2 1 
ATOM   2244 N  N   . PHE A  1  288 ? 59.008  6.957   28.464 1.00 35.34  ? 301 PHE A N   1 
ATOM   2245 C  CA  . PHE A  1  288 ? 58.228  8.095   28.911 1.00 36.64  ? 301 PHE A CA  1 
ATOM   2246 C  C   . PHE A  1  288 ? 58.029  8.019   30.417 1.00 33.56  ? 301 PHE A C   1 
ATOM   2247 O  O   . PHE A  1  288 ? 58.211  9.001   31.124 1.00 32.56  ? 301 PHE A O   1 
ATOM   2248 C  CB  . PHE A  1  288 ? 56.874  8.160   28.186 1.00 40.03  ? 301 PHE A CB  1 
ATOM   2249 C  CG  . PHE A  1  288 ? 56.066  9.387   28.595 1.00 41.45  ? 301 PHE A CG  1 
ATOM   2250 C  CD1 . PHE A  1  288 ? 56.251  10.608  27.948 1.00 43.54  ? 301 PHE A CD1 1 
ATOM   2251 C  CD2 . PHE A  1  288 ? 55.165  9.333   29.654 1.00 39.98  ? 301 PHE A CD2 1 
ATOM   2252 C  CE1 . PHE A  1  288 ? 55.524  11.730  28.327 1.00 43.32  ? 301 PHE A CE1 1 
ATOM   2253 C  CE2 . PHE A  1  288 ? 54.447  10.464  30.037 1.00 39.22  ? 301 PHE A CE2 1 
ATOM   2254 C  CZ  . PHE A  1  288 ? 54.627  11.656  29.375 1.00 39.41  ? 301 PHE A CZ  1 
ATOM   2255 N  N   . VAL A  1  289 ? 57.647  6.840   30.914 1.00 31.18  ? 302 VAL A N   1 
ATOM   2256 C  CA  . VAL A  1  289 ? 57.337  6.689   32.326 1.00 29.53  ? 302 VAL A CA  1 
ATOM   2257 C  C   . VAL A  1  289 ? 58.607  6.814   33.166 1.00 27.31  ? 302 VAL A C   1 
ATOM   2258 O  O   . VAL A  1  289 ? 58.566  7.355   34.267 1.00 27.60  ? 302 VAL A O   1 
ATOM   2259 C  CB  . VAL A  1  289 ? 56.605  5.359   32.616 1.00 30.16  ? 302 VAL A CB  1 
ATOM   2260 C  CG1 . VAL A  1  289 ? 56.547  5.080   34.106 1.00 29.94  ? 302 VAL A CG1 1 
ATOM   2261 C  CG2 . VAL A  1  289 ? 55.200  5.330   32.017 1.00 31.41  ? 302 VAL A CG2 1 
ATOM   2262 N  N   . VAL A  1  290 ? 59.736  6.282   32.684 1.00 31.93  ? 303 VAL A N   1 
ATOM   2263 C  CA  . VAL A  1  290 ? 60.976  6.425   33.436 1.00 31.60  ? 303 VAL A CA  1 
ATOM   2264 C  C   . VAL A  1  290 ? 61.331  7.911   33.568 1.00 30.55  ? 303 VAL A C   1 
ATOM   2265 O  O   . VAL A  1  290 ? 61.747  8.368   34.630 1.00 31.49  ? 303 VAL A O   1 
ATOM   2266 C  CB  . VAL A  1  290 ? 62.111  5.595   32.821 1.00 32.09  ? 303 VAL A CB  1 
ATOM   2267 C  CG1 . VAL A  1  290 ? 63.451  5.924   33.470 1.00 34.26  ? 303 VAL A CG1 1 
ATOM   2268 C  CG2 . VAL A  1  290 ? 61.825  4.101   32.949 1.00 32.86  ? 303 VAL A CG2 1 
ATOM   2269 N  N   . GLY A  1  291 ? 61.124  8.672   32.488 1.00 33.98  ? 304 GLY A N   1 
ATOM   2270 C  CA  . GLY A  1  291 ? 61.279  10.124  32.501 1.00 34.03  ? 304 GLY A CA  1 
ATOM   2271 C  C   . GLY A  1  291 ? 60.355  10.775  33.528 1.00 35.02  ? 304 GLY A C   1 
ATOM   2272 O  O   . GLY A  1  291 ? 60.783  11.635  34.305 1.00 33.30  ? 304 GLY A O   1 
ATOM   2273 N  N   . SER A  1  292 ? 59.088  10.325  33.565 1.00 34.95  ? 305 SER A N   1 
ATOM   2274 C  CA  . SER A  1  292 ? 58.145  10.864  34.528 1.00 32.52  ? 305 SER A CA  1 
ATOM   2275 C  C   . SER A  1  292 ? 58.626  10.592  35.942 1.00 31.24  ? 305 SER A C   1 
ATOM   2276 O  O   . SER A  1  292 ? 58.504  11.448  36.810 1.00 32.20  ? 305 SER A O   1 
ATOM   2277 C  CB  . SER A  1  292 ? 56.738  10.353  34.310 1.00 31.85  ? 305 SER A CB  1 
ATOM   2278 O  OG  . SER A  1  292 ? 56.347  10.512  32.957 1.00 34.00  ? 305 SER A OG  1 
ATOM   2279 N  N   . VAL A  1  293 ? 59.138  9.389   36.196 1.00 30.95  ? 306 VAL A N   1 
ATOM   2280 C  CA  . VAL A  1  293 ? 59.627  9.048   37.521 1.00 28.85  ? 306 VAL A CA  1 
ATOM   2281 C  C   . VAL A  1  293 ? 60.795  9.970   37.896 1.00 29.46  ? 306 VAL A C   1 
ATOM   2282 O  O   . VAL A  1  293 ? 60.921  10.352  39.053 1.00 29.10  ? 306 VAL A O   1 
ATOM   2283 C  CB  . VAL A  1  293 ? 60.030  7.564   37.633 1.00 31.97  ? 306 VAL A CB  1 
ATOM   2284 C  CG1 . VAL A  1  293 ? 60.778  7.269   38.939 1.00 31.51  ? 306 VAL A CG1 1 
ATOM   2285 C  CG2 . VAL A  1  293 ? 58.808  6.662   37.491 1.00 32.61  ? 306 VAL A CG2 1 
ATOM   2286 N  N   . GLN A  1  294 ? 61.663  10.310  36.942 1.00 29.96  ? 307 GLN A N   1 
ATOM   2287 C  CA  . GLN A  1  294 ? 62.789  11.183  37.247 1.00 34.59  ? 307 GLN A CA  1 
ATOM   2288 C  C   . GLN A  1  294 ? 62.314  12.590  37.627 1.00 33.50  ? 307 GLN A C   1 
ATOM   2289 O  O   . GLN A  1  294 ? 62.938  13.239  38.470 1.00 34.77  ? 307 GLN A O   1 
ATOM   2290 C  CB  . GLN A  1  294 ? 63.750  11.262  36.067 1.00 35.57  ? 307 GLN A CB  1 
ATOM   2291 C  CG  . GLN A  1  294 ? 64.513  9.970   35.817 1.00 41.02  ? 307 GLN A CG  1 
ATOM   2292 C  CD  . GLN A  1  294 ? 65.306  10.019  34.534 1.00 40.22  ? 307 GLN A CD  1 
ATOM   2293 O  OE1 . GLN A  1  294 ? 64.798  9.703   33.453 1.00 46.73  ? 307 GLN A OE1 1 
ATOM   2294 N  NE2 . GLN A  1  294 ? 66.574  10.385  34.656 1.00 39.24  ? 307 GLN A NE2 1 
ATOM   2295 N  N   . GLU A  1  295 ? 61.201  13.043  37.024 1.00 33.79  ? 308 GLU A N   1 
ATOM   2296 C  CA  . GLU A  1  295 ? 60.620  14.339  37.367 1.00 36.76  ? 308 GLU A CA  1 
ATOM   2297 C  C   . GLU A  1  295 ? 60.059  14.306  38.784 1.00 35.16  ? 308 GLU A C   1 
ATOM   2298 O  O   . GLU A  1  295 ? 60.191  15.292  39.497 1.00 36.74  ? 308 GLU A O   1 
ATOM   2299 C  CB  . GLU A  1  295 ? 59.515  14.794  36.409 1.00 39.46  ? 308 GLU A CB  1 
ATOM   2300 C  CG  . GLU A  1  295 ? 59.996  15.077  34.990 1.00 48.07  ? 308 GLU A CG  1 
ATOM   2301 C  CD  . GLU A  1  295 ? 58.884  15.130  33.938 1.00 60.45  ? 308 GLU A CD  1 
ATOM   2302 O  OE1 . GLU A  1  295 ? 57.730  14.701  34.217 1.00 67.78  ? 308 GLU A OE1 1 
ATOM   2303 O  OE2 . GLU A  1  295 ? 59.188  15.558  32.803 1.00 64.84  ? 308 GLU A OE2 1 
ATOM   2304 N  N   . LEU A  1  296 ? 59.441  13.180  39.194 1.00 31.26  ? 309 LEU A N   1 
ATOM   2305 C  CA  . LEU A  1  296 ? 58.930  13.027  40.552 1.00 31.60  ? 309 LEU A CA  1 
ATOM   2306 C  C   . LEU A  1  296 ? 60.065  12.908  41.561 1.00 30.87  ? 309 LEU A C   1 
ATOM   2307 O  O   . LEU A  1  296 ? 59.894  13.318  42.700 1.00 30.68  ? 309 LEU A O   1 
ATOM   2308 C  CB  . LEU A  1  296 ? 58.018  11.808  40.685 1.00 31.94  ? 309 LEU A CB  1 
ATOM   2309 C  CG  . LEU A  1  296 ? 56.732  11.858  39.855 1.00 34.32  ? 309 LEU A CG  1 
ATOM   2310 C  CD1 . LEU A  1  296 ? 55.995  10.535  39.966 1.00 37.27  ? 309 LEU A CD1 1 
ATOM   2311 C  CD2 . LEU A  1  296 ? 55.793  13.004  40.257 1.00 33.19  ? 309 LEU A CD2 1 
ATOM   2312 N  N   . TYR A  1  297 ? 61.176  12.269  41.164 1.00 29.53  ? 310 TYR A N   1 
ATOM   2313 C  CA  . TYR A  1  297 ? 62.258  11.941  42.083 1.00 30.76  ? 310 TYR A CA  1 
ATOM   2314 C  C   . TYR A  1  297 ? 63.583  12.419  41.477 1.00 34.02  ? 310 TYR A C   1 
ATOM   2315 O  O   . TYR A  1  297 ? 64.356  11.625  40.942 1.00 31.84  ? 310 TYR A O   1 
ATOM   2316 C  CB  . TYR A  1  297 ? 62.294  10.436  42.396 1.00 31.99  ? 310 TYR A CB  1 
ATOM   2317 C  CG  . TYR A  1  297 ? 61.060  9.923   43.132 1.00 28.95  ? 310 TYR A CG  1 
ATOM   2318 C  CD1 . TYR A  1  297 ? 60.925  10.082  44.501 1.00 30.85  ? 310 TYR A CD1 1 
ATOM   2319 C  CD2 . TYR A  1  297 ? 60.016  9.309   42.446 1.00 29.45  ? 310 TYR A CD2 1 
ATOM   2320 C  CE1 . TYR A  1  297 ? 59.804  9.623   45.170 1.00 30.66  ? 310 TYR A CE1 1 
ATOM   2321 C  CE2 . TYR A  1  297 ? 58.891  8.834   43.108 1.00 27.44  ? 310 TYR A CE2 1 
ATOM   2322 C  CZ  . TYR A  1  297 ? 58.788  8.986   44.473 1.00 27.32  ? 310 TYR A CZ  1 
ATOM   2323 O  OH  . TYR A  1  297 ? 57.683  8.580   45.162 1.00 30.78  ? 310 TYR A OH  1 
ATOM   2324 N  N   . PRO A  1  298 ? 63.855  13.747  41.483 1.00 34.88  ? 311 PRO A N   1 
ATOM   2325 C  CA  . PRO A  1  298 ? 65.055  14.278  40.843 1.00 35.19  ? 311 PRO A CA  1 
ATOM   2326 C  C   . PRO A  1  298 ? 66.387  13.857  41.457 1.00 29.11  ? 311 PRO A C   1 
ATOM   2327 O  O   . PRO A  1  298 ? 67.358  13.791  40.715 1.00 30.11  ? 311 PRO A O   1 
ATOM   2328 C  CB  . PRO A  1  298 ? 64.874  15.802  40.844 1.00 39.97  ? 311 PRO A CB  1 
ATOM   2329 C  CG  . PRO A  1  298 ? 63.782  16.067  41.859 1.00 47.13  ? 311 PRO A CG  1 
ATOM   2330 C  CD  . PRO A  1  298 ? 62.981  14.795  42.009 1.00 37.71  ? 311 PRO A CD  1 
ATOM   2331 N  N   . ASN A  1  299 ? 66.454  13.643  42.768 1.00 29.15  ? 312 ASN A N   1 
ATOM   2332 C  CA  . ASN A  1  299 ? 67.734  13.328  43.394 1.00 32.82  ? 312 ASN A CA  1 
ATOM   2333 C  C   . ASN A  1  299 ? 67.544  12.510  44.662 1.00 31.50  ? 312 ASN A C   1 
ATOM   2334 O  O   . ASN A  1  299 ? 67.876  12.968  45.758 1.00 30.96  ? 312 ASN A O   1 
ATOM   2335 C  CB  . ASN A  1  299 ? 68.555  14.587  43.668 1.00 33.02  ? 312 ASN A CB  1 
ATOM   2336 C  CG  . ASN A  1  299 ? 69.952  14.298  44.174 1.00 28.31  ? 312 ASN A CG  1 
ATOM   2337 O  OD1 . ASN A  1  299 ? 70.734  13.511  43.596 1.00 30.96  ? 312 ASN A OD1 1 
ATOM   2338 N  ND2 . ASN A  1  299 ? 70.277  14.920  45.282 1.00 27.60  ? 312 ASN A ND2 1 
ATOM   2339 N  N   . PRO A  1  300 ? 67.026  11.262  44.568 1.00 29.91  ? 313 PRO A N   1 
ATOM   2340 C  CA  . PRO A  1  300 ? 66.798  10.457  45.773 1.00 31.72  ? 313 PRO A CA  1 
ATOM   2341 C  C   . PRO A  1  300 ? 68.090  9.863   46.325 1.00 30.09  ? 313 PRO A C   1 
ATOM   2342 O  O   . PRO A  1  300 ? 69.008  9.607   45.568 1.00 33.91  ? 313 PRO A O   1 
ATOM   2343 C  CB  . PRO A  1  300 ? 65.824  9.365   45.269 1.00 30.76  ? 313 PRO A CB  1 
ATOM   2344 C  CG  . PRO A  1  300 ? 66.246  9.165   43.827 1.00 30.24  ? 313 PRO A CG  1 
ATOM   2345 C  CD  . PRO A  1  300 ? 66.664  10.566  43.322 1.00 30.41  ? 313 PRO A CD  1 
ATOM   2346 N  N   . THR A  1  301 ? 68.128  9.632   47.639 1.00 30.52  ? 314 THR A N   1 
ATOM   2347 C  CA  . THR A  1  301 ? 69.233  8.938   48.290 1.00 37.65  ? 314 THR A CA  1 
ATOM   2348 C  C   . THR A  1  301 ? 68.642  7.962   49.302 1.00 35.48  ? 314 THR A C   1 
ATOM   2349 O  O   . THR A  1  301 ? 67.425  7.939   49.495 1.00 37.68  ? 314 THR A O   1 
ATOM   2350 C  CB  . THR A  1  301 ? 70.205  9.934   48.939 1.00 41.27  ? 314 THR A CB  1 
ATOM   2351 O  OG1 . THR A  1  301 ? 69.452  10.732  49.837 1.00 41.04  ? 314 THR A OG1 1 
ATOM   2352 C  CG2 . THR A  1  301 ? 70.813  10.911  47.944 1.00 43.46  ? 314 THR A CG2 1 
ATOM   2353 N  N   . GLY A  1  302 ? 69.507  7.155   49.934 1.00 34.89  ? 315 GLY A N   1 
ATOM   2354 C  CA  . GLY A  1  302 ? 69.118  6.264   51.015 1.00 32.90  ? 315 GLY A CA  1 
ATOM   2355 C  C   . GLY A  1  302 ? 68.078  5.223   50.582 1.00 33.68  ? 315 GLY A C   1 
ATOM   2356 O  O   . GLY A  1  302 ? 68.156  4.693   49.473 1.00 35.40  ? 315 GLY A O   1 
ATOM   2357 N  N   . ILE A  1  303 ? 67.124  4.946   51.477 1.00 34.70  ? 316 ILE A N   1 
ATOM   2358 C  CA  . ILE A  1  303 ? 66.102  3.922   51.290 1.00 37.28  ? 316 ILE A CA  1 
ATOM   2359 C  C   . ILE A  1  303 ? 65.233  4.272   50.082 1.00 33.08  ? 316 ILE A C   1 
ATOM   2360 O  O   . ILE A  1  303 ? 64.860  3.382   49.310 1.00 33.26  ? 316 ILE A O   1 
ATOM   2361 C  CB  . ILE A  1  303 ? 65.246  3.721   52.561 1.00 44.28  ? 316 ILE A CB  1 
ATOM   2362 C  CG1 . ILE A  1  303 ? 66.103  3.495   53.815 1.00 63.23  ? 316 ILE A CG1 1 
ATOM   2363 C  CG2 . ILE A  1  303 ? 64.253  2.569   52.373 1.00 50.00  ? 316 ILE A CG2 1 
ATOM   2364 C  CD1 . ILE A  1  303 ? 66.998  2.257   53.794 1.00 69.77  ? 316 ILE A CD1 1 
ATOM   2365 N  N   . LEU A  1  304 ? 64.918  5.569   49.901 1.00 33.37  ? 317 LEU A N   1 
ATOM   2366 C  CA  . LEU A  1  304 ? 64.092  5.980   48.776 1.00 31.94  ? 317 LEU A CA  1 
ATOM   2367 C  C   . LEU A  1  304 ? 64.773  5.607   47.460 1.00 32.58  ? 317 LEU A C   1 
ATOM   2368 O  O   . LEU A  1  304 ? 64.141  5.057   46.556 1.00 29.86  ? 317 LEU A O   1 
ATOM   2369 C  CB  . LEU A  1  304 ? 63.768  7.474   48.844 1.00 33.04  ? 317 LEU A CB  1 
ATOM   2370 C  CG  . LEU A  1  304 ? 62.977  8.032   47.659 1.00 31.65  ? 317 LEU A CG  1 
ATOM   2371 C  CD1 . LEU A  1  304 ? 61.655  7.288   47.433 1.00 32.99  ? 317 LEU A CD1 1 
ATOM   2372 C  CD2 . LEU A  1  304 ? 62.713  9.508   47.847 1.00 35.30  ? 317 LEU A CD2 1 
ATOM   2373 N  N   . ARG A  1  305 ? 66.075  5.892   47.341 1.00 30.73  ? 318 ARG A N   1 
ATOM   2374 C  CA  A ARG A  1  305 ? 66.805  5.567   46.129 0.50 29.57  ? 318 ARG A CA  1 
ATOM   2375 C  CA  B ARG A  1  305 ? 66.808  5.568   46.130 0.50 32.12  ? 318 ARG A CA  1 
ATOM   2376 C  C   . ARG A  1  305 ? 66.784  4.055   45.908 1.00 28.89  ? 318 ARG A C   1 
ATOM   2377 O  O   . ARG A  1  305 ? 66.543  3.604   44.797 1.00 29.69  ? 318 ARG A O   1 
ATOM   2378 C  CB  A ARG A  1  305 ? 68.250  6.069   46.201 0.50 28.85  ? 318 ARG A CB  1 
ATOM   2379 C  CB  B ARG A  1  305 ? 68.262  6.051   46.198 0.50 35.22  ? 318 ARG A CB  1 
ATOM   2380 C  CG  A ARG A  1  305 ? 69.233  5.483   45.197 0.50 27.52  ? 318 ARG A CG  1 
ATOM   2381 C  CG  B ARG A  1  305 ? 69.124  5.620   45.018 0.50 37.70  ? 318 ARG A CG  1 
ATOM   2382 C  CD  A ARG A  1  305 ? 70.660  5.999   45.382 0.50 26.52  ? 318 ARG A CD  1 
ATOM   2383 C  CD  B ARG A  1  305 ? 70.608  5.927   45.227 0.50 40.82  ? 318 ARG A CD  1 
ATOM   2384 N  NE  A ARG A  1  305 ? 71.494  5.412   44.334 0.50 23.18  ? 318 ARG A NE  1 
ATOM   2385 N  NE  B ARG A  1  305 ? 71.280  6.171   43.946 0.50 42.13  ? 318 ARG A NE  1 
ATOM   2386 C  CZ  A ARG A  1  305 ? 71.970  4.207   44.382 0.50 20.90  ? 318 ARG A CZ  1 
ATOM   2387 C  CZ  B ARG A  1  305 ? 71.086  7.249   43.169 0.50 38.56  ? 318 ARG A CZ  1 
ATOM   2388 N  NH1 A ARG A  1  305 ? 71.899  3.552   45.519 0.50 21.02  ? 318 ARG A NH1 1 
ATOM   2389 N  NH1 B ARG A  1  305 ? 70.297  8.254   43.530 0.50 51.29  ? 318 ARG A NH1 1 
ATOM   2390 N  NH2 A ARG A  1  305 ? 72.569  3.718   43.323 0.50 20.46  ? 318 ARG A NH2 1 
ATOM   2391 N  NH2 B ARG A  1  305 ? 71.671  7.352   42.012 0.50 28.52  ? 318 ARG A NH2 1 
ATOM   2392 N  N   . ARG A  1  306 ? 67.071  3.299   46.964 1.00 31.00  ? 319 ARG A N   1 
ATOM   2393 C  CA  . ARG A  1  306 ? 67.130  1.847   46.874 1.00 35.48  ? 319 ARG A CA  1 
ATOM   2394 C  C   . ARG A  1  306 ? 65.784  1.299   46.391 1.00 31.90  ? 319 ARG A C   1 
ATOM   2395 O  O   . ARG A  1  306 ? 65.743  0.439   45.515 1.00 32.31  ? 319 ARG A O   1 
ATOM   2396 C  CB  . ARG A  1  306 ? 67.499  1.276   48.247 1.00 37.88  ? 319 ARG A CB  1 
ATOM   2397 C  CG  . ARG A  1  306 ? 67.728  -0.232  48.261 1.00 47.52  ? 319 ARG A CG  1 
ATOM   2398 C  CD  . ARG A  1  306 ? 67.713  -0.828  49.667 1.00 56.74  ? 319 ARG A CD  1 
ATOM   2399 N  NE  . ARG A  1  306 ? 66.375  -0.801  50.284 1.00 64.41  ? 319 ARG A NE  1 
ATOM   2400 C  CZ  . ARG A  1  306 ? 66.107  -1.164  51.548 1.00 70.57  ? 319 ARG A CZ  1 
ATOM   2401 N  NH1 . ARG A  1  306 ? 67.062  -1.654  52.336 1.00 70.61  ? 319 ARG A NH1 1 
ATOM   2402 N  NH2 . ARG A  1  306 ? 64.879  -1.035  52.036 1.00 69.28  ? 319 ARG A NH2 1 
ATOM   2403 N  N   . ASN A  1  307 ? 64.687  1.787   46.985 1.00 30.84  ? 320 ASN A N   1 
ATOM   2404 C  CA  . ASN A  1  307 ? 63.369  1.253   46.660 1.00 31.06  ? 320 ASN A CA  1 
ATOM   2405 C  C   . ASN A  1  307 ? 62.937  1.673   45.257 1.00 30.54  ? 320 ASN A C   1 
ATOM   2406 O  O   . ASN A  1  307 ? 62.260  0.916   44.566 1.00 31.19  ? 320 ASN A O   1 
ATOM   2407 C  CB  . ASN A  1  307 ? 62.355  1.588   47.730 1.00 29.30  ? 320 ASN A CB  1 
ATOM   2408 C  CG  . ASN A  1  307 ? 62.591  0.814   49.005 1.00 31.43  ? 320 ASN A CG  1 
ATOM   2409 O  OD1 . ASN A  1  307 ? 63.583  0.088   49.124 1.00 32.30  ? 320 ASN A OD1 1 
ATOM   2410 N  ND2 . ASN A  1  307 ? 61.704  0.975   49.976 1.00 31.03  ? 320 ASN A ND2 1 
ATOM   2411 N  N   . LEU A  1  308 ? 63.374  2.856   44.803 1.00 31.75  ? 321 LEU A N   1 
ATOM   2412 C  CA  . LEU A  1  308 ? 63.112  3.267   43.435 1.00 32.61  ? 321 LEU A CA  1 
ATOM   2413 C  C   . LEU A  1  308 ? 63.814  2.332   42.455 1.00 30.14  ? 321 LEU A C   1 
ATOM   2414 O  O   . LEU A  1  308 ? 63.244  1.959   41.435 1.00 29.60  ? 321 LEU A O   1 
ATOM   2415 C  CB  . LEU A  1  308 ? 63.579  4.697   43.179 1.00 34.72  ? 321 LEU A CB  1 
ATOM   2416 C  CG  . LEU A  1  308 ? 62.558  5.790   43.455 1.00 41.51  ? 321 LEU A CG  1 
ATOM   2417 C  CD1 . LEU A  1  308 ? 63.267  7.099   43.632 1.00 43.07  ? 321 LEU A CD1 1 
ATOM   2418 C  CD2 . LEU A  1  308 ? 61.571  5.833   42.284 1.00 42.65  ? 321 LEU A CD2 1 
ATOM   2419 N  N   . ILE A  1  309 ? 65.082  2.025   42.729 1.00 29.42  ? 322 ILE A N   1 
ATOM   2420 C  CA  . ILE A  1  309 ? 65.860  1.169   41.843 1.00 29.02  ? 322 ILE A CA  1 
ATOM   2421 C  C   . ILE A  1  309 ? 65.178  -0.198  41.734 1.00 28.31  ? 322 ILE A C   1 
ATOM   2422 O  O   . ILE A  1  309 ? 65.016  -0.728  40.642 1.00 31.49  ? 322 ILE A O   1 
ATOM   2423 C  CB  . ILE A  1  309 ? 67.315  1.068   42.338 1.00 29.94  ? 322 ILE A CB  1 
ATOM   2424 C  CG1 . ILE A  1  309 ? 68.061  2.406   42.109 1.00 32.45  ? 322 ILE A CG1 1 
ATOM   2425 C  CG2 . ILE A  1  309 ? 68.049  -0.096  41.679 1.00 29.73  ? 322 ILE A CG2 1 
ATOM   2426 C  CD1 . ILE A  1  309 ? 69.391  2.490   42.841 1.00 32.98  ? 322 ILE A CD1 1 
ATOM   2427 N  N   . LYS A  1  310 ? 64.759  -0.745  42.865 1.00 28.10  ? 323 LYS A N   1 
ATOM   2428 C  CA  . LYS A  1  310 ? 64.127  -2.058  42.886 1.00 32.72  ? 323 LYS A CA  1 
ATOM   2429 C  C   . LYS A  1  310 ? 62.797  -2.064  42.138 1.00 30.88  ? 323 LYS A C   1 
ATOM   2430 O  O   . LYS A  1  310 ? 62.573  -2.942  41.311 1.00 30.47  ? 323 LYS A O   1 
ATOM   2431 C  CB  . LYS A  1  310 ? 63.933  -2.526  44.323 1.00 32.68  ? 323 LYS A CB  1 
ATOM   2432 C  CG  . LYS A  1  310 ? 65.219  -2.947  44.961 1.00 33.03  ? 323 LYS A CG  1 
ATOM   2433 C  CD  . LYS A  1  310 ? 65.047  -3.372  46.408 1.00 38.58  ? 323 LYS A CD  1 
ATOM   2434 C  CE  . LYS A  1  310 ? 66.264  -4.139  46.864 1.00 45.65  ? 323 LYS A CE  1 
ATOM   2435 N  NZ  . LYS A  1  310 ? 66.176  -4.281  48.316 1.00 51.50  ? 323 LYS A NZ  1 
ATOM   2436 N  N   . ASN A  1  311 ? 61.950  -1.058  42.392 1.00 31.69  ? 324 ASN A N   1 
ATOM   2437 C  CA  . ASN A  1  311 ? 60.635  -1.000  41.769 1.00 30.03  ? 324 ASN A CA  1 
ATOM   2438 C  C   . ASN A  1  311 ? 60.775  -0.781  40.266 1.00 28.09  ? 324 ASN A C   1 
ATOM   2439 O  O   . ASN A  1  311 ? 60.037  -1.364  39.485 1.00 29.64  ? 324 ASN A O   1 
ATOM   2440 C  CB  . ASN A  1  311 ? 59.756  0.047   42.438 1.00 29.40  ? 324 ASN A CB  1 
ATOM   2441 C  CG  . ASN A  1  311 ? 59.120  -0.485  43.688 1.00 29.82  ? 324 ASN A CG  1 
ATOM   2442 O  OD1 . ASN A  1  311 ? 58.122  -1.212  43.610 1.00 30.90  ? 324 ASN A OD1 1 
ATOM   2443 N  ND2 . ASN A  1  311 ? 59.661  -0.135  44.841 1.00 31.23  ? 324 ASN A ND2 1 
ATOM   2444 N  N   . LEU A  1  312 ? 61.752  0.029   39.844 1.00 28.73  ? 325 LEU A N   1 
ATOM   2445 C  CA  . LEU A  1  312 ? 61.971  0.248   38.426 1.00 27.82  ? 325 LEU A CA  1 
ATOM   2446 C  C   . LEU A  1  312 ? 62.353  -1.074  37.761 1.00 29.26  ? 325 LEU A C   1 
ATOM   2447 O  O   . LEU A  1  312 ? 61.879  -1.370  36.664 1.00 28.32  ? 325 LEU A O   1 
ATOM   2448 C  CB  . LEU A  1  312 ? 63.038  1.318   38.194 1.00 30.02  ? 325 LEU A CB  1 
ATOM   2449 C  CG  . LEU A  1  312 ? 62.565  2.767   38.336 1.00 33.82  ? 325 LEU A CG  1 
ATOM   2450 C  CD1 . LEU A  1  312 ? 63.776  3.696   38.519 1.00 37.55  ? 325 LEU A CD1 1 
ATOM   2451 C  CD2 . LEU A  1  312 ? 61.727  3.163   37.126 1.00 33.32  ? 325 LEU A CD2 1 
ATOM   2452 N  N   . HIS A  1  313 ? 63.220  -1.842  38.421 1.00 29.21  ? 326 HIS A N   1 
ATOM   2453 C  CA  . HIS A  1  313 ? 63.632  -3.142  37.907 1.00 33.77  ? 326 HIS A CA  1 
ATOM   2454 C  C   . HIS A  1  313 ? 62.439  -4.100  37.849 1.00 31.75  ? 326 HIS A C   1 
ATOM   2455 O  O   . HIS A  1  313 ? 62.232  -4.742  36.833 1.00 32.03  ? 326 HIS A O   1 
ATOM   2456 C  CB  . HIS A  1  313 ? 64.805  -3.719  38.712 1.00 35.53  ? 326 HIS A CB  1 
ATOM   2457 C  CG  . HIS A  1  313 ? 65.252  -5.020  38.143 1.00 40.06  ? 326 HIS A CG  1 
ATOM   2458 N  ND1 . HIS A  1  313 ? 65.826  -5.078  36.891 1.00 43.04  ? 326 HIS A ND1 1 
ATOM   2459 C  CD2 . HIS A  1  313 ? 65.124  -6.292  38.565 1.00 40.11  ? 326 HIS A CD2 1 
ATOM   2460 C  CE1 . HIS A  1  313 ? 66.104  -6.346  36.607 1.00 43.71  ? 326 HIS A CE1 1 
ATOM   2461 N  NE2 . HIS A  1  313 ? 65.667  -7.102  37.596 1.00 41.48  ? 326 HIS A NE2 1 
ATOM   2462 N  N   . TYR A  1  314 ? 61.638  -4.173  38.917 1.00 33.59  ? 327 TYR A N   1 
ATOM   2463 C  CA  . TYR A  1  314 ? 60.465  -5.048  38.929 1.00 33.58  ? 327 TYR A CA  1 
ATOM   2464 C  C   . TYR A  1  314 ? 59.555  -4.713  37.752 1.00 34.48  ? 327 TYR A C   1 
ATOM   2465 O  O   . TYR A  1  314 ? 59.097  -5.601  37.024 1.00 32.08  ? 327 TYR A O   1 
ATOM   2466 C  CB  . TYR A  1  314 ? 59.654  -4.939  40.224 1.00 32.11  ? 327 TYR A CB  1 
ATOM   2467 C  CG  . TYR A  1  314 ? 60.425  -5.318  41.481 1.00 31.87  ? 327 TYR A CG  1 
ATOM   2468 C  CD1 . TYR A  1  314 ? 61.523  -6.167  41.445 1.00 34.20  ? 327 TYR A CD1 1 
ATOM   2469 C  CD2 . TYR A  1  314 ? 60.033  -4.818  42.709 1.00 32.51  ? 327 TYR A CD2 1 
ATOM   2470 C  CE1 . TYR A  1  314 ? 62.218  -6.504  42.602 1.00 32.94  ? 327 TYR A CE1 1 
ATOM   2471 C  CE2 . TYR A  1  314 ? 60.705  -5.150  43.871 1.00 34.02  ? 327 TYR A CE2 1 
ATOM   2472 C  CZ  . TYR A  1  314 ? 61.812  -5.987  43.817 1.00 33.83  ? 327 TYR A CZ  1 
ATOM   2473 O  OH  . TYR A  1  314 ? 62.436  -6.283  45.001 1.00 34.02  ? 327 TYR A OH  1 
ATOM   2474 N  N   . TRP A  1  315 ? 59.327  -3.411  37.535 1.00 32.76  ? 328 TRP A N   1 
ATOM   2475 C  CA  . TRP A  1  315 ? 58.448  -2.991  36.457 1.00 29.20  ? 328 TRP A CA  1 
ATOM   2476 C  C   . TRP A  1  315 ? 59.024  -3.436  35.113 1.00 31.80  ? 328 TRP A C   1 
ATOM   2477 O  O   . TRP A  1  315 ? 58.313  -3.977  34.271 1.00 29.89  ? 328 TRP A O   1 
ATOM   2478 C  CB  . TRP A  1  315 ? 58.225  -1.475  36.487 1.00 32.17  ? 328 TRP A CB  1 
ATOM   2479 C  CG  . TRP A  1  315 ? 57.129  -1.025  35.562 1.00 30.31  ? 328 TRP A CG  1 
ATOM   2480 C  CD1 . TRP A  1  315 ? 55.881  -1.572  35.438 1.00 30.57  ? 328 TRP A CD1 1 
ATOM   2481 C  CD2 . TRP A  1  315 ? 57.208  0.042   34.592 1.00 31.65  ? 328 TRP A CD2 1 
ATOM   2482 N  NE1 . TRP A  1  315 ? 55.173  -0.920  34.465 1.00 30.70  ? 328 TRP A NE1 1 
ATOM   2483 C  CE2 . TRP A  1  315 ? 55.961  0.072   33.930 1.00 29.24  ? 328 TRP A CE2 1 
ATOM   2484 C  CE3 . TRP A  1  315 ? 58.204  0.954   34.221 1.00 29.10  ? 328 TRP A CE3 1 
ATOM   2485 C  CZ2 . TRP A  1  315 ? 55.687  0.997   32.931 1.00 31.59  ? 328 TRP A CZ2 1 
ATOM   2486 C  CZ3 . TRP A  1  315 ? 57.937  1.841   33.205 1.00 31.88  ? 328 TRP A CZ3 1 
ATOM   2487 C  CH2 . TRP A  1  315 ? 56.702  1.846   32.556 1.00 32.37  ? 328 TRP A CH2 1 
ATOM   2488 N  N   . TRP A  1  316 ? 60.328  -3.229  34.929 1.00 32.23  ? 329 TRP A N   1 
ATOM   2489 C  CA  . TRP A  1  316 ? 60.987  -3.616  33.697 1.00 33.49  ? 329 TRP A CA  1 
ATOM   2490 C  C   . TRP A  1  316 ? 60.828  -5.120  33.436 1.00 33.85  ? 329 TRP A C   1 
ATOM   2491 O  O   . TRP A  1  316 ? 60.643  -5.497  32.287 1.00 35.42  ? 329 TRP A O   1 
ATOM   2492 C  CB  . TRP A  1  316 ? 62.468  -3.197  33.699 1.00 35.17  ? 329 TRP A CB  1 
ATOM   2493 C  CG  . TRP A  1  316 ? 63.187  -3.731  32.492 1.00 36.73  ? 329 TRP A CG  1 
ATOM   2494 C  CD1 . TRP A  1  316 ? 63.211  -3.204  31.235 1.00 37.42  ? 329 TRP A CD1 1 
ATOM   2495 C  CD2 . TRP A  1  316 ? 63.874  -4.991  32.411 1.00 35.68  ? 329 TRP A CD2 1 
ATOM   2496 N  NE1 . TRP A  1  316 ? 63.904  -4.025  30.386 1.00 37.15  ? 329 TRP A NE1 1 
ATOM   2497 C  CE2 . TRP A  1  316 ? 64.316  -5.130  31.079 1.00 39.45  ? 329 TRP A CE2 1 
ATOM   2498 C  CE3 . TRP A  1  316 ? 64.163  -5.999  33.330 1.00 38.72  ? 329 TRP A CE3 1 
ATOM   2499 C  CZ2 . TRP A  1  316 ? 65.031  -6.245  30.645 1.00 40.29  ? 329 TRP A CZ2 1 
ATOM   2500 C  CZ3 . TRP A  1  316 ? 64.864  -7.106  32.900 1.00 41.66  ? 329 TRP A CZ3 1 
ATOM   2501 C  CH2 . TRP A  1  316 ? 65.279  -7.235  31.569 1.00 38.45  ? 329 TRP A CH2 1 
ATOM   2502 N  N   . THR A  1  317 ? 60.841  -5.963  34.474 1.00 34.98  ? 330 THR A N   1 
ATOM   2503 C  CA  . THR A  1  317 ? 60.717  -7.402  34.260 1.00 39.60  ? 330 THR A CA  1 
ATOM   2504 C  C   . THR A  1  317 ? 59.398  -7.699  33.559 1.00 38.64  ? 330 THR A C   1 
ATOM   2505 O  O   . THR A  1  317 ? 59.349  -8.568  32.699 1.00 40.48  ? 330 THR A O   1 
ATOM   2506 C  CB  . THR A  1  317 ? 60.843  -8.253  35.526 1.00 40.50  ? 330 THR A CB  1 
ATOM   2507 O  OG1 . THR A  1  317 ? 59.734  -8.037  36.406 1.00 40.20  ? 330 THR A OG1 1 
ATOM   2508 C  CG2 . THR A  1  317 ? 62.179  -8.064  36.226 1.00 43.30  ? 330 THR A CG2 1 
ATOM   2509 N  N   . GLY A  1  318 ? 58.323  -6.987  33.918 1.00 34.85  ? 331 GLY A N   1 
ATOM   2510 C  CA  . GLY A  1  318 ? 57.055  -7.176  33.241 1.00 31.44  ? 331 GLY A CA  1 
ATOM   2511 C  C   . GLY A  1  318 ? 57.030  -6.517  31.862 1.00 32.32  ? 331 GLY A C   1 
ATOM   2512 O  O   . GLY A  1  318 ? 56.534  -7.085  30.891 1.00 32.67  ? 331 GLY A O   1 
ATOM   2513 N  N   . VAL A  1  319 ? 57.528  -5.283  31.783 1.00 35.65  ? 332 VAL A N   1 
ATOM   2514 C  CA  . VAL A  1  319 ? 57.502  -4.531  30.539 1.00 34.39  ? 332 VAL A CA  1 
ATOM   2515 C  C   . VAL A  1  319 ? 58.287  -5.278  29.466 1.00 35.17  ? 332 VAL A C   1 
ATOM   2516 O  O   . VAL A  1  319 ? 57.878  -5.327  28.311 1.00 34.36  ? 332 VAL A O   1 
ATOM   2517 C  CB  . VAL A  1  319 ? 58.093  -3.131  30.777 1.00 37.54  ? 332 VAL A CB  1 
ATOM   2518 C  CG1 . VAL A  1  319 ? 58.507  -2.443  29.487 1.00 37.80  ? 332 VAL A CG1 1 
ATOM   2519 C  CG2 . VAL A  1  319 ? 57.121  -2.268  31.566 1.00 39.29  ? 332 VAL A CG2 1 
ATOM   2520 N  N   . ASN A  1  320 ? 59.444  -5.823  29.847 1.00 36.76  ? 333 ASN A N   1 
ATOM   2521 C  CA  . ASN A  1  320 ? 60.329  -6.474  28.891 1.00 37.45  ? 333 ASN A CA  1 
ATOM   2522 C  C   . ASN A  1  320 ? 59.593  -7.590  28.152 1.00 36.50  ? 333 ASN A C   1 
ATOM   2523 O  O   . ASN A  1  320 ? 59.744  -7.728  26.946 1.00 41.16  ? 333 ASN A O   1 
ATOM   2524 C  CB  . ASN A  1  320 ? 61.581  -7.019  29.564 1.00 38.74  ? 333 ASN A CB  1 
ATOM   2525 C  CG  . ASN A  1  320 ? 62.606  -7.429  28.538 1.00 42.21  ? 333 ASN A CG  1 
ATOM   2526 O  OD1 . ASN A  1  320 ? 62.931  -6.637  27.649 1.00 42.40  ? 333 ASN A OD1 1 
ATOM   2527 N  ND2 . ASN A  1  320 ? 63.084  -8.656  28.617 1.00 38.86  ? 333 ASN A ND2 1 
ATOM   2528 N  N   . VAL A  1  321 ? 58.759  -8.342  28.874 1.00 36.06  ? 334 VAL A N   1 
ATOM   2529 C  CA  . VAL A  1  321 ? 57.969  -9.405  28.281 1.00 37.87  ? 334 VAL A CA  1 
ATOM   2530 C  C   . VAL A  1  321 ? 56.760  -8.812  27.566 1.00 40.10  ? 334 VAL A C   1 
ATOM   2531 O  O   . VAL A  1  321 ? 56.557  -9.089  26.395 1.00 38.95  ? 334 VAL A O   1 
ATOM   2532 C  CB  . VAL A  1  321 ? 57.567  -10.470 29.319 1.00 40.40  ? 334 VAL A CB  1 
ATOM   2533 C  CG1 . VAL A  1  321 ? 56.636  -11.545 28.747 1.00 44.04  ? 334 VAL A CG1 1 
ATOM   2534 C  CG2 . VAL A  1  321 ? 58.797  -11.096 29.968 1.00 41.21  ? 334 VAL A CG2 1 
ATOM   2535 N  N   . ALA A  1  322 ? 55.964  -7.978  28.241 1.00 40.40  ? 335 ALA A N   1 
ATOM   2536 C  CA  . ALA A  1  322 ? 54.704  -7.528  27.673 1.00 41.31  ? 335 ALA A CA  1 
ATOM   2537 C  C   . ALA A  1  322 ? 54.921  -6.732  26.387 1.00 43.26  ? 335 ALA A C   1 
ATOM   2538 O  O   . ALA A  1  322 ? 54.064  -6.742  25.502 1.00 41.45  ? 335 ALA A O   1 
ATOM   2539 C  CB  . ALA A  1  322 ? 53.931  -6.696  28.688 1.00 46.72  ? 335 ALA A CB  1 
ATOM   2540 N  N   . PHE A  1  323 ? 56.029  -5.989  26.303 1.00 41.25  ? 336 PHE A N   1 
ATOM   2541 C  CA  . PHE A  1  323 ? 56.229  -5.083  25.184 1.00 43.53  ? 336 PHE A CA  1 
ATOM   2542 C  C   . PHE A  1  323 ? 57.164  -5.700  24.145 1.00 46.57  ? 336 PHE A C   1 
ATOM   2543 O  O   . PHE A  1  323 ? 57.479  -5.049  23.163 1.00 44.54  ? 336 PHE A O   1 
ATOM   2544 C  CB  . PHE A  1  323 ? 56.815  -3.740  25.624 1.00 41.06  ? 336 PHE A CB  1 
ATOM   2545 C  CG  . PHE A  1  323 ? 55.906  -2.851  26.459 1.00 42.43  ? 336 PHE A CG  1 
ATOM   2546 C  CD1 . PHE A  1  323 ? 54.606  -3.231  26.770 1.00 44.58  ? 336 PHE A CD1 1 
ATOM   2547 C  CD2 . PHE A  1  323 ? 56.344  -1.615  26.906 1.00 39.40  ? 336 PHE A CD2 1 
ATOM   2548 C  CE1 . PHE A  1  323 ? 53.785  -2.417  27.528 1.00 47.56  ? 336 PHE A CE1 1 
ATOM   2549 C  CE2 . PHE A  1  323 ? 55.513  -0.801  27.659 1.00 41.88  ? 336 PHE A CE2 1 
ATOM   2550 C  CZ  . PHE A  1  323 ? 54.236  -1.200  27.969 1.00 44.86  ? 336 PHE A CZ  1 
ATOM   2551 N  N   . GLY A  1  324 ? 57.605  -6.941  24.351 1.00 47.27  ? 337 GLY A N   1 
ATOM   2552 C  CA  . GLY A  1  324 ? 58.415  -7.638  23.362 1.00 48.20  ? 337 GLY A CA  1 
ATOM   2553 C  C   . GLY A  1  324 ? 59.856  -7.128  23.305 1.00 50.29  ? 337 GLY A C   1 
ATOM   2554 O  O   . GLY A  1  324 ? 60.468  -7.165  22.246 1.00 50.76  ? 337 GLY A O   1 
ATOM   2555 N  N   . GLY A  1  325 ? 60.398  -6.682  24.447 1.00 50.40  ? 338 GLY A N   1 
ATOM   2556 C  CA  . GLY A  1  325 ? 61.815  -6.368  24.585 1.00 46.03  ? 338 GLY A CA  1 
ATOM   2557 C  C   . GLY A  1  325 ? 62.061  -4.859  24.609 1.00 47.47  ? 338 GLY A C   1 
ATOM   2558 O  O   . GLY A  1  325 ? 61.797  -4.186  23.621 1.00 45.41  ? 338 GLY A O   1 
ATOM   2559 N  N   . CYS A  1  326 ? 62.510  -4.330  25.759 1.00 41.84  ? 339 CYS A N   1 
ATOM   2560 C  CA  . CYS A  1  326 ? 62.903  -2.932  25.882 1.00 44.43  ? 339 CYS A CA  1 
ATOM   2561 C  C   . CYS A  1  326 ? 64.216  -2.906  26.655 1.00 39.74  ? 339 CYS A C   1 
ATOM   2562 O  O   . CYS A  1  326 ? 64.379  -3.657  27.615 1.00 41.92  ? 339 CYS A O   1 
ATOM   2563 C  CB  . CYS A  1  326 ? 61.890  -2.076  26.657 1.00 50.37  ? 339 CYS A CB  1 
ATOM   2564 S  SG  . CYS A  1  326 ? 60.221  -1.971  25.942 1.00 60.67  ? 339 CYS A SG  1 
ATOM   2565 N  N   . ASP A  1  327 ? 65.142  -2.045  26.236 1.00 40.74  ? 340 ASP A N   1 
ATOM   2566 C  CA  . ASP A  1  327 ? 66.404  -1.887  26.943 1.00 42.77  ? 340 ASP A CA  1 
ATOM   2567 C  C   . ASP A  1  327 ? 66.133  -1.248  28.298 1.00 41.15  ? 340 ASP A C   1 
ATOM   2568 O  O   . ASP A  1  327 ? 65.537  -0.171  28.361 1.00 41.84  ? 340 ASP A O   1 
ATOM   2569 C  CB  . ASP A  1  327 ? 67.379  -1.012  26.165 1.00 47.65  ? 340 ASP A CB  1 
ATOM   2570 C  CG  . ASP A  1  327 ? 67.828  -1.549  24.811 1.00 53.26  ? 340 ASP A CG  1 
ATOM   2571 O  OD1 . ASP A  1  327 ? 67.672  -2.760  24.590 1.00 55.05  ? 340 ASP A OD1 1 
ATOM   2572 O  OD2 . ASP A  1  327 ? 68.294  -0.742  23.982 1.00 61.78  ? 340 ASP A OD2 1 
ATOM   2573 N  N   . GLU A  1  328 ? 66.598  -1.899  29.364 1.00 39.87  ? 341 GLU A N   1 
ATOM   2574 C  CA  . GLU A  1  328 ? 66.374  -1.389  30.706 1.00 40.43  ? 341 GLU A CA  1 
ATOM   2575 C  C   . GLU A  1  328 ? 67.133  -0.076  30.896 1.00 41.07  ? 341 GLU A C   1 
ATOM   2576 O  O   . GLU A  1  328 ? 68.273  0.044   30.462 1.00 38.45  ? 341 GLU A O   1 
ATOM   2577 C  CB  . GLU A  1  328 ? 66.814  -2.421  31.739 1.00 40.24  ? 341 GLU A CB  1 
ATOM   2578 C  CG  . GLU A  1  328 ? 66.424  -2.032  33.162 1.00 40.07  ? 341 GLU A CG  1 
ATOM   2579 C  CD  . GLU A  1  328 ? 66.619  -3.132  34.192 1.00 40.19  ? 341 GLU A CD  1 
ATOM   2580 O  OE1 . GLU A  1  328 ? 67.182  -4.184  33.812 1.00 42.61  ? 341 GLU A OE1 1 
ATOM   2581 O  OE2 . GLU A  1  328 ? 66.228  -2.941  35.366 1.00 36.10  ? 341 GLU A OE2 1 
ATOM   2582 N  N   . LEU A  1  329 ? 66.490  0.891   31.564 1.00 40.10  ? 342 LEU A N   1 
ATOM   2583 C  CA  . LEU A  1  329 ? 67.125  2.147   31.933 1.00 39.30  ? 342 LEU A CA  1 
ATOM   2584 C  C   . LEU A  1  329 ? 67.502  2.120   33.414 1.00 36.79  ? 342 LEU A C   1 
ATOM   2585 O  O   . LEU A  1  329 ? 66.800  1.519   34.235 1.00 35.13  ? 342 LEU A O   1 
ATOM   2586 C  CB  . LEU A  1  329 ? 66.187  3.304   31.593 1.00 39.55  ? 342 LEU A CB  1 
ATOM   2587 C  CG  . LEU A  1  329 ? 65.876  3.488   30.104 1.00 42.19  ? 342 LEU A CG  1 
ATOM   2588 C  CD1 . LEU A  1  329 ? 64.735  4.447   29.878 1.00 40.69  ? 342 LEU A CD1 1 
ATOM   2589 C  CD2 . LEU A  1  329 ? 67.107  3.978   29.345 1.00 44.68  ? 342 LEU A CD2 1 
ATOM   2590 N  N   . PHE A  1  330 ? 68.601  2.817   33.739 1.00 38.54  ? 343 PHE A N   1 
ATOM   2591 C  CA  . PHE A  1  330 ? 69.132  2.882   35.089 1.00 38.15  ? 343 PHE A CA  1 
ATOM   2592 C  C   . PHE A  1  330 ? 69.331  4.337   35.491 1.00 43.94  ? 343 PHE A C   1 
ATOM   2593 O  O   . PHE A  1  330 ? 70.461  4.774   35.737 1.00 41.69  ? 343 PHE A O   1 
ATOM   2594 C  CB  . PHE A  1  330 ? 70.445  2.096   35.168 1.00 41.39  ? 343 PHE A CB  1 
ATOM   2595 C  CG  . PHE A  1  330 ? 70.277  0.633   34.780 1.00 42.50  ? 343 PHE A CG  1 
ATOM   2596 C  CD1 . PHE A  1  330 ? 69.726  -0.288  35.669 1.00 43.85  ? 343 PHE A CD1 1 
ATOM   2597 C  CD2 . PHE A  1  330 ? 70.652  0.195   33.515 1.00 44.22  ? 343 PHE A CD2 1 
ATOM   2598 C  CE1 . PHE A  1  330 ? 69.520  -1.614  35.284 1.00 48.34  ? 343 PHE A CE1 1 
ATOM   2599 C  CE2 . PHE A  1  330 ? 70.477  -1.135  33.150 1.00 43.75  ? 343 PHE A CE2 1 
ATOM   2600 C  CZ  . PHE A  1  330 ? 69.923  -2.035  34.034 1.00 43.08  ? 343 PHE A CZ  1 
ATOM   2601 N  N   . PRO A  1  331 ? 68.240  5.120   35.661 1.00 39.33  ? 344 PRO A N   1 
ATOM   2602 C  CA  . PRO A  1  331 ? 68.370  6.537   36.013 1.00 37.26  ? 344 PRO A CA  1 
ATOM   2603 C  C   . PRO A  1  331 ? 69.079  6.803   37.339 1.00 33.45  ? 344 PRO A C   1 
ATOM   2604 O  O   . PRO A  1  331 ? 69.616  7.894   37.527 1.00 34.89  ? 344 PRO A O   1 
ATOM   2605 C  CB  . PRO A  1  331 ? 66.899  7.019   36.033 1.00 38.09  ? 344 PRO A CB  1 
ATOM   2606 C  CG  . PRO A  1  331 ? 66.090  5.753   36.335 1.00 37.31  ? 344 PRO A CG  1 
ATOM   2607 C  CD  . PRO A  1  331 ? 66.836  4.683   35.563 1.00 37.61  ? 344 PRO A CD  1 
ATOM   2608 N  N   . TYR A  1  332 ? 69.100  5.808   38.239 1.00 30.46  ? 345 TYR A N   1 
ATOM   2609 C  CA  . TYR A  1  332 ? 69.721  5.967   39.545 1.00 33.38  ? 345 TYR A CA  1 
ATOM   2610 C  C   . TYR A  1  332 ? 70.863  4.971   39.752 1.00 32.48  ? 345 TYR A C   1 
ATOM   2611 O  O   . TYR A  1  332 ? 71.281  4.741   40.879 1.00 32.68  ? 345 TYR A O   1 
ATOM   2612 C  CB  . TYR A  1  332 ? 68.681  5.846   40.655 1.00 35.20  ? 345 TYR A CB  1 
ATOM   2613 C  CG  . TYR A  1  332 ? 67.493  6.769   40.429 1.00 39.00  ? 345 TYR A CG  1 
ATOM   2614 C  CD1 . TYR A  1  332 ? 67.622  8.159   40.510 1.00 35.20  ? 345 TYR A CD1 1 
ATOM   2615 C  CD2 . TYR A  1  332 ? 66.239  6.244   40.126 1.00 37.52  ? 345 TYR A CD2 1 
ATOM   2616 C  CE1 . TYR A  1  332 ? 66.541  8.990   40.261 1.00 35.15  ? 345 TYR A CE1 1 
ATOM   2617 C  CE2 . TYR A  1  332 ? 65.152  7.069   39.886 1.00 37.73  ? 345 TYR A CE2 1 
ATOM   2618 C  CZ  . TYR A  1  332 ? 65.300  8.445   39.962 1.00 39.50  ? 345 TYR A CZ  1 
ATOM   2619 O  OH  . TYR A  1  332 ? 64.195  9.216   39.723 1.00 35.92  ? 345 TYR A OH  1 
ATOM   2620 N  N   . GLY A  1  333 ? 71.376  4.402   38.659 1.00 34.43  ? 346 GLY A N   1 
ATOM   2621 C  CA  . GLY A  1  333 ? 72.440  3.418   38.741 1.00 38.23  ? 346 GLY A CA  1 
ATOM   2622 C  C   . GLY A  1  333 ? 71.916  2.083   39.272 1.00 42.47  ? 346 GLY A C   1 
ATOM   2623 O  O   . GLY A  1  333 ? 70.738  1.772   39.076 1.00 37.46  ? 346 GLY A O   1 
ATOM   2624 N  N   . GLN A  1  334 ? 72.790  1.354   39.988 1.00 43.74  ? 347 GLN A N   1 
ATOM   2625 C  CA  A GLN A  1  334 ? 72.491  0.034   40.511 0.50 47.32  ? 347 GLN A CA  1 
ATOM   2626 C  CA  B GLN A  1  334 ? 72.465  0.035   40.512 0.50 47.28  ? 347 GLN A CA  1 
ATOM   2627 C  C   . GLN A  1  334 ? 72.615  0.036   42.027 1.00 46.56  ? 347 GLN A C   1 
ATOM   2628 O  O   . GLN A  1  334 ? 73.143  0.987   42.592 1.00 42.89  ? 347 GLN A O   1 
ATOM   2629 C  CB  A GLN A  1  334 ? 73.472  -0.968  39.910 0.50 52.50  ? 347 GLN A CB  1 
ATOM   2630 C  CB  B GLN A  1  334 ? 73.309  -1.044  39.833 0.50 52.69  ? 347 GLN A CB  1 
ATOM   2631 C  CG  A GLN A  1  334 ? 73.075  -1.418  38.510 0.50 59.37  ? 347 GLN A CG  1 
ATOM   2632 C  CG  B GLN A  1  334 ? 72.965  -1.208  38.355 0.50 58.18  ? 347 GLN A CG  1 
ATOM   2633 C  CD  A GLN A  1  334 ? 73.622  -0.548  37.406 0.50 60.51  ? 347 GLN A CD  1 
ATOM   2634 C  CD  B GLN A  1  334 ? 72.837  -2.642  37.881 0.50 58.01  ? 347 GLN A CD  1 
ATOM   2635 O  OE1 A GLN A  1  334 ? 74.455  0.339   37.628 0.50 64.34  ? 347 GLN A OE1 1 
ATOM   2636 O  OE1 B GLN A  1  334 ? 72.697  -3.592  38.662 0.50 65.19  ? 347 GLN A OE1 1 
ATOM   2637 N  NE2 A GLN A  1  334 ? 73.153  -0.824  36.199 0.50 57.51  ? 347 GLN A NE2 1 
ATOM   2638 N  NE2 B GLN A  1  334 ? 72.848  -2.807  36.570 0.50 56.27  ? 347 GLN A NE2 1 
ATOM   2639 N  N   . LEU A  1  335 ? 72.144  -1.049  42.664 1.00 45.96  ? 348 LEU A N   1 
ATOM   2640 C  CA  . LEU A  1  335 ? 72.208  -1.196  44.113 1.00 52.51  ? 348 LEU A CA  1 
ATOM   2641 C  C   . LEU A  1  335 ? 73.671  -1.322  44.601 1.00 54.11  ? 348 LEU A C   1 
ATOM   2642 O  O   . LEU A  1  335 ? 74.472  -1.858  43.807 1.00 54.78  ? 348 LEU A O   1 
ATOM   2643 C  CB  . LEU A  1  335 ? 71.383  -2.408  44.544 1.00 47.59  ? 348 LEU A CB  1 
ATOM   2644 C  CG  . LEU A  1  335 ? 69.865  -2.292  44.398 1.00 51.38  ? 348 LEU A CG  1 
ATOM   2645 C  CD1 . LEU A  1  335 ? 69.208  -3.604  44.807 1.00 51.62  ? 348 LEU A CD1 1 
ATOM   2646 C  CD2 . LEU A  1  335 ? 69.358  -1.137  45.245 1.00 50.47  ? 348 LEU A CD2 1 
ATOM   2647 N  N   . GLN B  1  1   ? -1.898  20.204  59.288 1.00 129.01 ? 14  GLN B N   1 
ATOM   2648 C  CA  . GLN B  1  1   ? -3.158  19.829  59.987 1.00 130.81 ? 14  GLN B CA  1 
ATOM   2649 C  C   . GLN B  1  1   ? -3.177  18.318  60.218 1.00 124.94 ? 14  GLN B C   1 
ATOM   2650 O  O   . GLN B  1  1   ? -3.127  17.859  61.360 1.00 112.77 ? 14  GLN B O   1 
ATOM   2651 C  CB  . GLN B  1  1   ? -4.384  20.268  59.181 1.00 136.81 ? 14  GLN B CB  1 
ATOM   2652 C  CG  . GLN B  1  1   ? -4.501  21.778  58.995 1.00 138.87 ? 14  GLN B CG  1 
ATOM   2653 C  CD  . GLN B  1  1   ? -5.692  22.175  58.152 1.00 132.17 ? 14  GLN B CD  1 
ATOM   2654 O  OE1 . GLN B  1  1   ? -5.841  21.711  57.017 1.00 124.06 ? 14  GLN B OE1 1 
ATOM   2655 N  NE2 . GLN B  1  1   ? -6.552  23.029  58.694 1.00 130.88 ? 14  GLN B NE2 1 
ATOM   2656 N  N   . GLY B  1  2   ? -3.237  17.564  59.105 1.00 116.73 ? 15  GLY B N   1 
ATOM   2657 C  CA  . GLY B  1  2   ? -3.334  16.107  59.112 1.00 102.49 ? 15  GLY B CA  1 
ATOM   2658 C  C   . GLY B  1  2   ? -3.915  15.570  57.799 1.00 88.46  ? 15  GLY B C   1 
ATOM   2659 O  O   . GLY B  1  2   ? -4.612  16.288  57.072 1.00 88.36  ? 15  GLY B O   1 
ATOM   2660 N  N   . VAL B  1  3   ? -3.654  14.286  57.517 1.00 75.36  ? 16  VAL B N   1 
ATOM   2661 C  CA  . VAL B  1  3   ? -3.992  13.669  56.242 1.00 69.35  ? 16  VAL B CA  1 
ATOM   2662 C  C   . VAL B  1  3   ? -5.150  12.682  56.404 1.00 56.34  ? 16  VAL B C   1 
ATOM   2663 O  O   . VAL B  1  3   ? -5.428  12.223  57.508 1.00 59.33  ? 16  VAL B O   1 
ATOM   2664 C  CB  . VAL B  1  3   ? -2.748  12.954  55.683 1.00 81.94  ? 16  VAL B CB  1 
ATOM   2665 C  CG1 . VAL B  1  3   ? -2.883  12.746  54.180 1.00 81.72  ? 16  VAL B CG1 1 
ATOM   2666 C  CG2 . VAL B  1  3   ? -1.442  13.696  55.974 1.00 86.44  ? 16  VAL B CG2 1 
ATOM   2667 N  N   . ASP B  1  4   ? -5.821  12.379  55.289 1.00 59.14  ? 17  ASP B N   1 
ATOM   2668 C  CA  . ASP B  1  4   ? -6.977  11.498  55.292 1.00 63.80  ? 17  ASP B CA  1 
ATOM   2669 C  C   . ASP B  1  4   ? -6.557  10.132  54.748 1.00 63.25  ? 17  ASP B C   1 
ATOM   2670 O  O   . ASP B  1  4   ? -6.379  9.991   53.545 1.00 56.82  ? 17  ASP B O   1 
ATOM   2671 C  CB  . ASP B  1  4   ? -8.113  12.129  54.497 1.00 68.71  ? 17  ASP B CB  1 
ATOM   2672 C  CG  . ASP B  1  4   ? -9.497  11.605  54.832 1.00 78.04  ? 17  ASP B CG  1 
ATOM   2673 O  OD1 . ASP B  1  4   ? -9.890  11.760  56.001 1.00 94.77  ? 17  ASP B OD1 1 
ATOM   2674 O  OD2 . ASP B  1  4   ? -10.159 11.056  53.922 1.00 79.49  ? 17  ASP B OD2 1 
ATOM   2675 N  N   . PRO B  1  5   ? -6.391  9.078   55.586 1.00 63.64  ? 18  PRO B N   1 
ATOM   2676 C  CA  . PRO B  1  5   ? -5.736  7.843   55.149 1.00 57.51  ? 18  PRO B CA  1 
ATOM   2677 C  C   . PRO B  1  5   ? -6.639  6.974   54.286 1.00 52.02  ? 18  PRO B C   1 
ATOM   2678 O  O   . PRO B  1  5   ? -7.744  6.653   54.708 1.00 50.98  ? 18  PRO B O   1 
ATOM   2679 C  CB  . PRO B  1  5   ? -5.374  7.147   56.468 1.00 61.38  ? 18  PRO B CB  1 
ATOM   2680 C  CG  . PRO B  1  5   ? -6.450  7.595   57.437 1.00 65.33  ? 18  PRO B CG  1 
ATOM   2681 C  CD  . PRO B  1  5   ? -6.834  9.003   56.985 1.00 63.94  ? 18  PRO B CD  1 
ATOM   2682 N  N   . PRO B  1  6   ? -6.180  6.512   53.099 1.00 50.80  ? 19  PRO B N   1 
ATOM   2683 C  CA  . PRO B  1  6   ? -7.004  5.691   52.219 1.00 51.16  ? 19  PRO B CA  1 
ATOM   2684 C  C   . PRO B  1  6   ? -7.096  4.265   52.750 1.00 48.15  ? 19  PRO B C   1 
ATOM   2685 O  O   . PRO B  1  6   ? -6.269  3.846   53.547 1.00 48.46  ? 19  PRO B O   1 
ATOM   2686 C  CB  . PRO B  1  6   ? -6.228  5.773   50.886 1.00 53.31  ? 19  PRO B CB  1 
ATOM   2687 C  CG  . PRO B  1  6   ? -4.781  5.852   51.317 1.00 54.08  ? 19  PRO B CG  1 
ATOM   2688 C  CD  . PRO B  1  6   ? -4.831  6.723   52.556 1.00 54.41  ? 19  PRO B CD  1 
ATOM   2689 N  N   . PRO B  1  7   ? -8.108  3.483   52.328 1.00 53.59  ? 20  PRO B N   1 
ATOM   2690 C  CA  . PRO B  1  7   ? -8.174  2.068   52.691 1.00 52.93  ? 20  PRO B CA  1 
ATOM   2691 C  C   . PRO B  1  7   ? -6.967  1.323   52.121 1.00 50.87  ? 20  PRO B C   1 
ATOM   2692 O  O   . PRO B  1  7   ? -6.314  1.785   51.196 1.00 44.62  ? 20  PRO B O   1 
ATOM   2693 C  CB  . PRO B  1  7   ? -9.521  1.594   52.111 1.00 53.26  ? 20  PRO B CB  1 
ATOM   2694 C  CG  . PRO B  1  7   ? -9.847  2.605   51.027 1.00 58.70  ? 20  PRO B CG  1 
ATOM   2695 C  CD  . PRO B  1  7   ? -9.224  3.920   51.467 1.00 55.91  ? 20  PRO B CD  1 
ATOM   2696 N  N   . PRO B  1  8   ? -6.602  0.158   52.677 1.00 49.91  ? 21  PRO B N   1 
ATOM   2697 C  CA  . PRO B  1  8   ? -5.458  -0.586  52.163 1.00 46.47  ? 21  PRO B CA  1 
ATOM   2698 C  C   . PRO B  1  8   ? -5.688  -1.059  50.732 1.00 43.27  ? 21  PRO B C   1 
ATOM   2699 O  O   . PRO B  1  8   ? -6.813  -1.348  50.333 1.00 42.05  ? 21  PRO B O   1 
ATOM   2700 C  CB  . PRO B  1  8   ? -5.325  -1.743  53.133 1.00 48.88  ? 21  PRO B CB  1 
ATOM   2701 C  CG  . PRO B  1  8   ? -6.718  -1.910  53.675 1.00 52.21  ? 21  PRO B CG  1 
ATOM   2702 C  CD  . PRO B  1  8   ? -7.232  -0.487  53.832 1.00 48.15  ? 21  PRO B CD  1 
ATOM   2703 N  N   . PRO B  1  9   ? -4.618  -1.155  49.919 1.00 40.93  ? 22  PRO B N   1 
ATOM   2704 C  CA  . PRO B  1  9   ? -4.702  -1.820  48.624 1.00 39.25  ? 22  PRO B CA  1 
ATOM   2705 C  C   . PRO B  1  9   ? -5.227  -3.234  48.809 1.00 35.72  ? 22  PRO B C   1 
ATOM   2706 O  O   . PRO B  1  9   ? -5.022  -3.847  49.853 1.00 38.67  ? 22  PRO B O   1 
ATOM   2707 C  CB  . PRO B  1  9   ? -3.255  -1.820  48.121 1.00 40.92  ? 22  PRO B CB  1 
ATOM   2708 C  CG  . PRO B  1  9   ? -2.624  -0.662  48.846 1.00 42.42  ? 22  PRO B CG  1 
ATOM   2709 C  CD  . PRO B  1  9   ? -3.282  -0.621  50.210 1.00 39.63  ? 22  PRO B CD  1 
ATOM   2710 N  N   . GLY B  1  10  ? -5.886  -3.737  47.768 1.00 36.64  ? 23  GLY B N   1 
ATOM   2711 C  CA  . GLY B  1  10  ? -6.208  -5.150  47.665 1.00 38.94  ? 23  GLY B CA  1 
ATOM   2712 C  C   . GLY B  1  10  ? -5.032  -5.923  47.070 1.00 38.41  ? 23  GLY B C   1 
ATOM   2713 O  O   . GLY B  1  10  ? -3.946  -5.369  46.871 1.00 37.92  ? 23  GLY B O   1 
ATOM   2714 N  N   . PRO B  1  11  ? -5.224  -7.224  46.774 1.00 39.38  ? 24  PRO B N   1 
ATOM   2715 C  CA  . PRO B  1  11  ? -4.173  -8.047  46.165 1.00 43.46  ? 24  PRO B CA  1 
ATOM   2716 C  C   . PRO B  1  11  ? -3.702  -7.436  44.846 1.00 46.94  ? 24  PRO B C   1 
ATOM   2717 O  O   . PRO B  1  11  ? -4.435  -6.696  44.206 1.00 43.73  ? 24  PRO B O   1 
ATOM   2718 C  CB  . PRO B  1  11  ? -4.837  -9.408  45.960 1.00 44.52  ? 24  PRO B CB  1 
ATOM   2719 C  CG  . PRO B  1  11  ? -6.044  -9.388  46.899 1.00 43.96  ? 24  PRO B CG  1 
ATOM   2720 C  CD  . PRO B  1  11  ? -6.485  -7.947  46.963 1.00 41.73  ? 24  PRO B CD  1 
ATOM   2721 N  N   . PRO B  1  12  ? -2.464  -7.705  44.384 1.00 49.95  ? 25  PRO B N   1 
ATOM   2722 C  CA  . PRO B  1  12  ? -2.032  -7.157  43.099 1.00 46.67  ? 25  PRO B CA  1 
ATOM   2723 C  C   . PRO B  1  12  ? -2.819  -7.813  41.963 1.00 49.11  ? 25  PRO B C   1 
ATOM   2724 O  O   . PRO B  1  12  ? -3.249  -8.967  42.091 1.00 41.40  ? 25  PRO B O   1 
ATOM   2725 C  CB  . PRO B  1  12  ? -0.534  -7.484  43.081 1.00 49.33  ? 25  PRO B CB  1 
ATOM   2726 C  CG  . PRO B  1  12  ? -0.400  -8.708  43.962 1.00 45.66  ? 25  PRO B CG  1 
ATOM   2727 C  CD  . PRO B  1  12  ? -1.483  -8.599  45.011 1.00 44.46  ? 25  PRO B CD  1 
ATOM   2728 N  N   . SER B  1  13  ? -3.011  -7.053  40.873 1.00 51.44  ? 26  SER B N   1 
ATOM   2729 C  CA  A SER B  1  13  ? -3.689  -7.528  39.672 0.50 54.37  ? 26  SER B CA  1 
ATOM   2730 C  CA  B SER B  1  13  ? -3.700  -7.540  39.684 0.50 55.09  ? 26  SER B CA  1 
ATOM   2731 C  C   . SER B  1  13  ? -3.023  -8.799  39.148 1.00 55.11  ? 26  SER B C   1 
ATOM   2732 O  O   . SER B  1  13  ? -3.697  -9.758  38.781 1.00 50.90  ? 26  SER B O   1 
ATOM   2733 C  CB  A SER B  1  13  ? -3.692  -6.473  38.580 0.50 56.35  ? 26  SER B CB  1 
ATOM   2734 C  CB  B SER B  1  13  ? -3.761  -6.484  38.612 0.50 58.34  ? 26  SER B CB  1 
ATOM   2735 O  OG  A SER B  1  13  ? -4.096  -5.189  39.039 0.50 56.62  ? 26  SER B OG  1 
ATOM   2736 O  OG  B SER B  1  13  ? -4.460  -6.972  37.474 0.50 60.13  ? 26  SER B OG  1 
ATOM   2737 N  N   . PHE B  1  14  ? -1.679  -8.786  39.096 1.00 48.45  ? 27  PHE B N   1 
ATOM   2738 C  CA  . PHE B  1  14  ? -0.915  -9.943  38.651 1.00 49.10  ? 27  PHE B CA  1 
ATOM   2739 C  C   . PHE B  1  14  ? -0.239  -10.577 39.871 1.00 40.54  ? 27  PHE B C   1 
ATOM   2740 O  O   . PHE B  1  14  ? 0.496   -9.886  40.576 1.00 37.67  ? 27  PHE B O   1 
ATOM   2741 C  CB  . PHE B  1  14  ? 0.092   -9.500  37.576 1.00 49.73  ? 27  PHE B CB  1 
ATOM   2742 C  CG  . PHE B  1  14  ? 1.052   -10.607 37.154 1.00 50.92  ? 27  PHE B CG  1 
ATOM   2743 C  CD1 . PHE B  1  14  ? 0.610   -11.635 36.322 1.00 53.36  ? 27  PHE B CD1 1 
ATOM   2744 C  CD2 . PHE B  1  14  ? 2.374   -10.646 37.601 1.00 50.44  ? 27  PHE B CD2 1 
ATOM   2745 C  CE1 . PHE B  1  14  ? 1.459   -12.665 35.947 1.00 55.50  ? 27  PHE B CE1 1 
ATOM   2746 C  CE2 . PHE B  1  14  ? 3.217   -11.687 37.223 1.00 48.63  ? 27  PHE B CE2 1 
ATOM   2747 C  CZ  . PHE B  1  14  ? 2.760   -12.688 36.397 1.00 50.50  ? 27  PHE B CZ  1 
ATOM   2748 N  N   . THR B  1  15  ? -0.473  -11.881 40.089 1.00 39.62  ? 28  THR B N   1 
ATOM   2749 C  CA  . THR B  1  15  ? 0.003   -12.560 41.290 1.00 44.86  ? 28  THR B CA  1 
ATOM   2750 C  C   . THR B  1  15  ? 0.986   -13.682 40.953 1.00 45.94  ? 28  THR B C   1 
ATOM   2751 O  O   . THR B  1  15  ? 1.258   -14.527 41.816 1.00 42.88  ? 28  THR B O   1 
ATOM   2752 C  CB  . THR B  1  15  ? -1.180  -13.123 42.078 1.00 45.98  ? 28  THR B CB  1 
ATOM   2753 O  OG1 . THR B  1  15  ? -1.741  -14.107 41.221 1.00 45.98  ? 28  THR B OG1 1 
ATOM   2754 C  CG2 . THR B  1  15  ? -2.237  -12.085 42.392 1.00 46.75  ? 28  THR B CG2 1 
ATOM   2755 N  N   . GLY B  1  16  ? 1.488   -13.722 39.702 1.00 42.93  ? 29  GLY B N   1 
ATOM   2756 C  CA  . GLY B  1  16  ? 2.462   -14.734 39.325 1.00 44.27  ? 29  GLY B CA  1 
ATOM   2757 C  C   . GLY B  1  16  ? 3.894   -14.314 39.681 1.00 42.99  ? 29  GLY B C   1 
ATOM   2758 O  O   . GLY B  1  16  ? 4.114   -13.236 40.232 1.00 38.08  ? 29  GLY B O   1 
ATOM   2759 N  N   . THR B  1  17  ? 4.872   -15.167 39.340 1.00 42.08  ? 30  THR B N   1 
ATOM   2760 C  CA  . THR B  1  17  ? 6.271   -14.840 39.552 1.00 40.32  ? 30  THR B CA  1 
ATOM   2761 C  C   . THR B  1  17  ? 6.656   -13.769 38.549 1.00 41.94  ? 30  THR B C   1 
ATOM   2762 O  O   . THR B  1  17  ? 6.028   -13.594 37.510 1.00 42.05  ? 30  THR B O   1 
ATOM   2763 C  CB  . THR B  1  17  ? 7.188   -16.063 39.428 1.00 44.61  ? 30  THR B CB  1 
ATOM   2764 O  OG1 . THR B  1  17  ? 8.452   -15.608 39.907 1.00 41.46  ? 30  THR B OG1 1 
ATOM   2765 C  CG2 . THR B  1  17  ? 7.309   -16.585 38.006 1.00 44.28  ? 30  THR B CG2 1 
ATOM   2766 N  N   . LYS B  1  18  ? 7.685   -13.020 38.908 1.00 38.68  ? 31  LYS B N   1 
ATOM   2767 C  CA  . LYS B  1  18  ? 8.278   -12.048 38.013 1.00 41.68  ? 31  LYS B CA  1 
ATOM   2768 C  C   . LYS B  1  18  ? 9.621   -11.650 38.596 1.00 40.36  ? 31  LYS B C   1 
ATOM   2769 O  O   . LYS B  1  18  ? 9.860   -11.857 39.789 1.00 35.34  ? 31  LYS B O   1 
ATOM   2770 C  CB  . LYS B  1  18  ? 7.428   -10.789 37.815 1.00 45.76  ? 31  LYS B CB  1 
ATOM   2771 C  CG  . LYS B  1  18  ? 7.140   -9.968  39.064 1.00 48.67  ? 31  LYS B CG  1 
ATOM   2772 C  CD  . LYS B  1  18  ? 6.484   -8.629  38.749 1.00 56.56  ? 31  LYS B CD  1 
ATOM   2773 C  CE  . LYS B  1  18  ? 6.688   -7.621  39.828 1.00 65.91  ? 31  LYS B CE  1 
ATOM   2774 N  NZ  . LYS B  1  18  ? 5.658   -6.578  39.788 1.00 72.75  ? 31  LYS B NZ  1 
ATOM   2775 N  N   . LEU B  1  19  ? 10.449  -11.058 37.735 1.00 37.46  ? 32  LEU B N   1 
ATOM   2776 C  CA  . LEU B  1  19  ? 11.718  -10.499 38.148 1.00 41.19  ? 32  LEU B CA  1 
ATOM   2777 C  C   . LEU B  1  19  ? 11.445  -9.260  38.989 1.00 37.90  ? 32  LEU B C   1 
ATOM   2778 O  O   . LEU B  1  19  ? 10.805  -8.326  38.520 1.00 40.36  ? 32  LEU B O   1 
ATOM   2779 C  CB  . LEU B  1  19  ? 12.562  -10.138 36.929 1.00 39.41  ? 32  LEU B CB  1 
ATOM   2780 C  CG  . LEU B  1  19  ? 13.868  -9.411  37.259 1.00 40.50  ? 32  LEU B CG  1 
ATOM   2781 C  CD1 . LEU B  1  19  ? 14.818  -10.339 37.987 1.00 40.06  ? 32  LEU B CD1 1 
ATOM   2782 C  CD2 . LEU B  1  19  ? 14.504  -8.821  36.009 1.00 44.05  ? 32  LEU B CD2 1 
ATOM   2783 N  N   . VAL B  1  20  ? 11.954  -9.239  40.225 1.00 35.82  ? 33  VAL B N   1 
ATOM   2784 C  CA  . VAL B  1  20  ? 11.727  -8.078  41.064 1.00 32.96  ? 33  VAL B CA  1 
ATOM   2785 C  C   . VAL B  1  20  ? 13.021  -7.309  41.249 1.00 33.04  ? 33  VAL B C   1 
ATOM   2786 O  O   . VAL B  1  20  ? 12.984  -6.112  41.539 1.00 32.31  ? 33  VAL B O   1 
ATOM   2787 C  CB  . VAL B  1  20  ? 11.070  -8.420  42.413 1.00 35.03  ? 33  VAL B CB  1 
ATOM   2788 C  CG1 . VAL B  1  20  ? 9.711   -9.065  42.227 1.00 36.51  ? 33  VAL B CG1 1 
ATOM   2789 C  CG2 . VAL B  1  20  ? 11.940  -9.282  43.298 1.00 36.90  ? 33  VAL B CG2 1 
ATOM   2790 N  N   . ASN B  1  21  ? 14.163  -8.004  41.111 1.00 33.51  ? 34  ASN B N   1 
ATOM   2791 C  CA  . ASN B  1  21  ? 15.445  -7.336  41.149 1.00 32.90  ? 34  ASN B CA  1 
ATOM   2792 C  C   . ASN B  1  21  ? 15.748  -6.851  39.735 1.00 36.94  ? 34  ASN B C   1 
ATOM   2793 O  O   . ASN B  1  21  ? 16.561  -7.459  39.043 1.00 34.08  ? 34  ASN B O   1 
ATOM   2794 C  CB  . ASN B  1  21  ? 16.535  -8.257  41.672 1.00 33.03  ? 34  ASN B CB  1 
ATOM   2795 C  CG  . ASN B  1  21  ? 17.859  -7.558  41.848 1.00 33.97  ? 34  ASN B CG  1 
ATOM   2796 O  OD1 . ASN B  1  21  ? 17.971  -6.351  41.622 1.00 33.85  ? 34  ASN B OD1 1 
ATOM   2797 N  ND2 . ASN B  1  21  ? 18.848  -8.288  42.342 1.00 33.72  ? 34  ASN B ND2 1 
ATOM   2798 N  N   . ASP B  1  22  ? 15.098  -5.760  39.325 1.00 37.57  ? 35  ASP B N   1 
ATOM   2799 C  CA  . ASP B  1  22  ? 15.062  -5.379  37.920 1.00 40.75  ? 35  ASP B CA  1 
ATOM   2800 C  C   . ASP B  1  22  ? 15.691  -4.002  37.782 1.00 41.79  ? 35  ASP B C   1 
ATOM   2801 O  O   . ASP B  1  22  ? 16.098  -3.385  38.771 1.00 34.54  ? 35  ASP B O   1 
ATOM   2802 C  CB  . ASP B  1  22  ? 13.647  -5.454  37.359 1.00 42.14  ? 35  ASP B CB  1 
ATOM   2803 C  CG  . ASP B  1  22  ? 12.607  -4.543  38.012 1.00 42.52  ? 35  ASP B CG  1 
ATOM   2804 O  OD1 . ASP B  1  22  ? 12.975  -3.810  38.933 1.00 39.16  ? 35  ASP B OD1 1 
ATOM   2805 O  OD2 . ASP B  1  22  ? 11.442  -4.533  37.546 1.00 45.62  ? 35  ASP B OD2 1 
ATOM   2806 N  N   . ALA B  1  23  ? 15.742  -3.524  36.534 1.00 44.11  ? 36  ALA B N   1 
ATOM   2807 C  CA  . ALA B  1  23  ? 16.486  -2.321  36.199 1.00 46.03  ? 36  ALA B CA  1 
ATOM   2808 C  C   . ALA B  1  23  ? 15.909  -1.113  36.932 1.00 37.65  ? 36  ALA B C   1 
ATOM   2809 O  O   . ALA B  1  23  ? 16.628  -0.188  37.301 1.00 41.45  ? 36  ALA B O   1 
ATOM   2810 C  CB  . ALA B  1  23  ? 16.446  -2.119  34.692 1.00 52.50  ? 36  ALA B CB  1 
ATOM   2811 N  N   . ASP B  1  24  ? 14.591  -1.132  37.129 1.00 38.05  ? 37  ASP B N   1 
ATOM   2812 C  CA  . ASP B  1  24  ? 13.914  -0.012  37.743 1.00 42.04  ? 37  ASP B CA  1 
ATOM   2813 C  C   . ASP B  1  24  ? 14.051  0.002   39.264 1.00 41.96  ? 37  ASP B C   1 
ATOM   2814 O  O   . ASP B  1  24  ? 13.735  1.013   39.870 1.00 41.02  ? 37  ASP B O   1 
ATOM   2815 C  CB  . ASP B  1  24  ? 12.450  -0.013  37.353 1.00 48.66  ? 37  ASP B CB  1 
ATOM   2816 C  CG  . ASP B  1  24  ? 11.861  1.384   37.335 1.00 49.09  ? 37  ASP B CG  1 
ATOM   2817 O  OD1 . ASP B  1  24  ? 12.527  2.292   36.766 1.00 51.52  ? 37  ASP B OD1 1 
ATOM   2818 O  OD2 . ASP B  1  24  ? 10.771  1.533   37.891 1.00 56.64  ? 37  ASP B OD2 1 
ATOM   2819 N  N   . HIS B  1  25  ? 14.524  -1.107  39.871 1.00 38.82  ? 38  HIS B N   1 
ATOM   2820 C  CA  . HIS B  1  25  ? 14.613  -1.238  41.320 1.00 37.22  ? 38  HIS B CA  1 
ATOM   2821 C  C   . HIS B  1  25  ? 16.028  -1.677  41.708 1.00 42.48  ? 38  HIS B C   1 
ATOM   2822 O  O   . HIS B  1  25  ? 16.235  -2.772  42.246 1.00 37.88  ? 38  HIS B O   1 
ATOM   2823 C  CB  . HIS B  1  25  ? 13.533  -2.211  41.807 1.00 35.75  ? 38  HIS B CB  1 
ATOM   2824 C  CG  . HIS B  1  25  ? 12.148  -1.708  41.580 1.00 36.64  ? 38  HIS B CG  1 
ATOM   2825 N  ND1 . HIS B  1  25  ? 11.392  -2.091  40.488 1.00 37.18  ? 38  HIS B ND1 1 
ATOM   2826 C  CD2 . HIS B  1  25  ? 11.398  -0.819  42.274 1.00 37.42  ? 38  HIS B CD2 1 
ATOM   2827 C  CE1 . HIS B  1  25  ? 10.213  -1.468  40.540 1.00 42.09  ? 38  HIS B CE1 1 
ATOM   2828 N  NE2 . HIS B  1  25  ? 10.193  -0.689  41.614 1.00 36.15  ? 38  HIS B NE2 1 
ATOM   2829 N  N   . PRO B  1  26  ? 17.051  -0.843  41.422 1.00 40.84  ? 39  PRO B N   1 
ATOM   2830 C  CA  . PRO B  1  26  ? 18.436  -1.186  41.757 1.00 37.88  ? 39  PRO B CA  1 
ATOM   2831 C  C   . PRO B  1  26  ? 18.687  -1.059  43.248 1.00 36.75  ? 39  PRO B C   1 
ATOM   2832 O  O   . PRO B  1  26  ? 18.193  -0.128  43.877 1.00 33.71  ? 39  PRO B O   1 
ATOM   2833 C  CB  . PRO B  1  26  ? 19.229  -0.145  40.975 1.00 41.75  ? 39  PRO B CB  1 
ATOM   2834 C  CG  . PRO B  1  26  ? 18.316  1.083   40.980 1.00 40.31  ? 39  PRO B CG  1 
ATOM   2835 C  CD  . PRO B  1  26  ? 16.935  0.483   40.794 1.00 39.12  ? 39  PRO B CD  1 
ATOM   2836 N  N   . TRP B  1  27  ? 19.484  -1.978  43.804 1.00 34.36  ? 40  TRP B N   1 
ATOM   2837 C  CA  . TRP B  1  27  ? 20.037  -1.759  45.131 1.00 29.15  ? 40  TRP B CA  1 
ATOM   2838 C  C   . TRP B  1  27  ? 20.883  -0.489  45.119 1.00 29.23  ? 40  TRP B C   1 
ATOM   2839 O  O   . TRP B  1  27  ? 21.642  -0.254  44.181 1.00 31.02  ? 40  TRP B O   1 
ATOM   2840 C  CB  . TRP B  1  27  ? 20.874  -2.967  45.561 1.00 30.35  ? 40  TRP B CB  1 
ATOM   2841 C  CG  . TRP B  1  27  ? 21.455  -2.852  46.937 1.00 27.71  ? 40  TRP B CG  1 
ATOM   2842 C  CD1 . TRP B  1  27  ? 20.896  -3.284  48.102 1.00 29.68  ? 40  TRP B CD1 1 
ATOM   2843 C  CD2 . TRP B  1  27  ? 22.716  -2.253  47.286 1.00 28.75  ? 40  TRP B CD2 1 
ATOM   2844 N  NE1 . TRP B  1  27  ? 21.721  -2.993  49.159 1.00 30.61  ? 40  TRP B NE1 1 
ATOM   2845 C  CE2 . TRP B  1  27  ? 22.843  -2.351  48.688 1.00 27.94  ? 40  TRP B CE2 1 
ATOM   2846 C  CE3 . TRP B  1  27  ? 23.740  -1.632  46.557 1.00 33.62  ? 40  TRP B CE3 1 
ATOM   2847 C  CZ2 . TRP B  1  27  ? 23.949  -1.847  49.358 1.00 29.89  ? 40  TRP B CZ2 1 
ATOM   2848 C  CZ3 . TRP B  1  27  ? 24.831  -1.126  47.229 1.00 31.00  ? 40  TRP B CZ3 1 
ATOM   2849 C  CH2 . TRP B  1  27  ? 24.929  -1.233  48.608 1.00 32.55  ? 40  TRP B CH2 1 
ATOM   2850 N  N   . GLN B  1  28  ? 20.766  0.310   46.179 1.00 30.64  ? 41  GLN B N   1 
ATOM   2851 C  CA  . GLN B  1  28  ? 21.623  1.463   46.380 1.00 32.00  ? 41  GLN B CA  1 
ATOM   2852 C  C   . GLN B  1  28  ? 22.027  1.543   47.839 1.00 30.46  ? 41  GLN B C   1 
ATOM   2853 O  O   . GLN B  1  28  ? 21.289  1.134   48.728 1.00 33.25  ? 41  GLN B O   1 
ATOM   2854 C  CB  . GLN B  1  28  ? 20.954  2.769   45.950 1.00 33.22  ? 41  GLN B CB  1 
ATOM   2855 C  CG  . GLN B  1  28  ? 20.606  2.811   44.467 1.00 32.43  ? 41  GLN B CG  1 
ATOM   2856 C  CD  . GLN B  1  28  ? 19.840  4.055   44.071 1.00 39.92  ? 41  GLN B CD  1 
ATOM   2857 O  OE1 . GLN B  1  28  ? 19.506  4.909   44.899 1.00 43.10  ? 41  GLN B OE1 1 
ATOM   2858 N  NE2 . GLN B  1  28  ? 19.533  4.152   42.793 1.00 40.55  ? 41  GLN B NE2 1 
ATOM   2859 N  N   . PRO B  1  29  ? 23.231  2.077   48.128 1.00 33.30  ? 42  PRO B N   1 
ATOM   2860 C  CA  . PRO B  1  29  ? 23.683  2.265   49.496 1.00 33.24  ? 42  PRO B CA  1 
ATOM   2861 C  C   . PRO B  1  29  ? 22.863  3.315   50.242 1.00 33.60  ? 42  PRO B C   1 
ATOM   2862 O  O   . PRO B  1  29  ? 22.148  4.102   49.650 1.00 35.05  ? 42  PRO B O   1 
ATOM   2863 C  CB  . PRO B  1  29  ? 25.159  2.696   49.338 1.00 35.57  ? 42  PRO B CB  1 
ATOM   2864 C  CG  . PRO B  1  29  ? 25.291  3.176   47.927 1.00 36.21  ? 42  PRO B CG  1 
ATOM   2865 C  CD  . PRO B  1  29  ? 24.208  2.538   47.131 1.00 34.87  ? 42  PRO B CD  1 
ATOM   2866 N  N   . LEU B  1  30  ? 22.963  3.292   51.561 1.00 33.45  ? 43  LEU B N   1 
ATOM   2867 C  CA  . LEU B  1  30  ? 22.243  4.208   52.422 1.00 36.56  ? 43  LEU B CA  1 
ATOM   2868 C  C   . LEU B  1  30  ? 22.824  5.606   52.245 1.00 41.21  ? 43  LEU B C   1 
ATOM   2869 O  O   . LEU B  1  30  ? 24.032  5.757   52.104 1.00 40.31  ? 43  LEU B O   1 
ATOM   2870 C  CB  . LEU B  1  30  ? 22.374  3.756   53.874 1.00 39.47  ? 43  LEU B CB  1 
ATOM   2871 C  CG  . LEU B  1  30  ? 21.723  2.414   54.220 1.00 41.86  ? 43  LEU B CG  1 
ATOM   2872 C  CD1 . LEU B  1  30  ? 21.851  2.153   55.703 1.00 42.73  ? 43  LEU B CD1 1 
ATOM   2873 C  CD2 . LEU B  1  30  ? 20.262  2.329   53.800 1.00 43.62  ? 43  LEU B CD2 1 
ATOM   2874 N  N   . ARG B  1  31  ? 21.943  6.606   52.258 1.00 43.53  ? 44  ARG B N   1 
ATOM   2875 C  CA  . ARG B  1  31  ? 22.321  8.005   52.371 1.00 45.92  ? 44  ARG B CA  1 
ATOM   2876 C  C   . ARG B  1  31  ? 22.071  8.472   53.806 1.00 48.02  ? 44  ARG B C   1 
ATOM   2877 O  O   . ARG B  1  31  ? 21.367  7.821   54.581 1.00 45.13  ? 44  ARG B O   1 
ATOM   2878 C  CB  . ARG B  1  31  ? 21.468  8.871   51.439 1.00 46.75  ? 44  ARG B CB  1 
ATOM   2879 C  CG  . ARG B  1  31  ? 21.412  8.508   49.962 1.00 51.92  ? 44  ARG B CG  1 
ATOM   2880 C  CD  . ARG B  1  31  ? 20.153  9.072   49.285 1.00 60.39  ? 44  ARG B CD  1 
ATOM   2881 N  NE  . ARG B  1  31  ? 18.923  8.786   50.045 1.00 66.22  ? 44  ARG B NE  1 
ATOM   2882 C  CZ  . ARG B  1  31  ? 17.661  8.861   49.627 1.00 70.06  ? 44  ARG B CZ  1 
ATOM   2883 N  NH1 . ARG B  1  31  ? 17.372  9.099   48.358 1.00 81.12  ? 44  ARG B NH1 1 
ATOM   2884 N  NH2 . ARG B  1  31  ? 16.685  8.632   50.491 1.00 64.45  ? 44  ARG B NH2 1 
ATOM   2885 N  N   . GLU B  1  32  ? 22.619  9.642   54.130 1.00 51.60  ? 45  GLU B N   1 
ATOM   2886 C  CA  . GLU B  1  32  ? 22.378  10.283  55.413 1.00 60.11  ? 45  GLU B CA  1 
ATOM   2887 C  C   . GLU B  1  32  ? 20.870  10.421  55.630 1.00 50.60  ? 45  GLU B C   1 
ATOM   2888 O  O   . GLU B  1  32  ? 20.149  10.864  54.738 1.00 46.76  ? 45  GLU B O   1 
ATOM   2889 C  CB  . GLU B  1  32  ? 23.065  11.655  55.458 1.00 68.64  ? 45  GLU B CB  1 
ATOM   2890 C  CG  . GLU B  1  32  ? 22.954  12.364  56.806 1.00 77.65  ? 45  GLU B CG  1 
ATOM   2891 C  CD  . GLU B  1  32  ? 23.611  11.631  57.965 1.00 95.37  ? 45  GLU B CD  1 
ATOM   2892 O  OE1 . GLU B  1  32  ? 24.279  10.584  57.782 1.00 104.09 ? 45  GLU B OE1 1 
ATOM   2893 O  OE2 . GLU B  1  32  ? 23.455  12.143  59.092 1.00 110.91 ? 45  GLU B OE2 1 
ATOM   2894 N  N   . GLY B  1  33  ? 20.405  9.987   56.805 1.00 51.47  ? 46  GLY B N   1 
ATOM   2895 C  CA  . GLY B  1  33  ? 19.003  10.105  57.173 1.00 52.29  ? 46  GLY B CA  1 
ATOM   2896 C  C   . GLY B  1  33  ? 18.158  8.881   56.806 1.00 52.09  ? 46  GLY B C   1 
ATOM   2897 O  O   . GLY B  1  33  ? 17.003  8.802   57.231 1.00 47.16  ? 46  GLY B O   1 
ATOM   2898 N  N   . ASP B  1  34  ? 18.681  7.970   55.973 1.00 46.16  ? 47  ASP B N   1 
ATOM   2899 C  CA  . ASP B  1  34  ? 17.932  6.782   55.583 1.00 44.06  ? 47  ASP B CA  1 
ATOM   2900 C  C   . ASP B  1  34  ? 17.753  5.866   56.796 1.00 38.73  ? 47  ASP B C   1 
ATOM   2901 O  O   . ASP B  1  34  ? 18.676  5.662   57.560 1.00 36.61  ? 47  ASP B O   1 
ATOM   2902 C  CB  . ASP B  1  34  ? 18.594  6.041   54.427 1.00 45.49  ? 47  ASP B CB  1 
ATOM   2903 C  CG  . ASP B  1  34  ? 18.468  6.702   53.053 1.00 51.91  ? 47  ASP B CG  1 
ATOM   2904 O  OD1 . ASP B  1  34  ? 17.692  7.676   52.915 1.00 45.08  ? 47  ASP B OD1 1 
ATOM   2905 O  OD2 . ASP B  1  34  ? 19.158  6.242   52.110 1.00 49.97  ? 47  ASP B OD2 1 
ATOM   2906 N  N   . ILE B  1  35  ? 16.546  5.320   56.970 1.00 36.94  ? 48  ILE B N   1 
ATOM   2907 C  CA  . ILE B  1  35  ? 16.213  4.509   58.132 1.00 35.16  ? 48  ILE B CA  1 
ATOM   2908 C  C   . ILE B  1  35  ? 16.062  3.043   57.718 1.00 29.42  ? 48  ILE B C   1 
ATOM   2909 O  O   . ILE B  1  35  ? 15.399  2.726   56.742 1.00 30.96  ? 48  ILE B O   1 
ATOM   2910 C  CB  . ILE B  1  35  ? 14.909  5.026   58.773 1.00 38.33  ? 48  ILE B CB  1 
ATOM   2911 C  CG1 . ILE B  1  35  ? 15.024  6.478   59.277 1.00 39.94  ? 48  ILE B CG1 1 
ATOM   2912 C  CG2 . ILE B  1  35  ? 14.469  4.090   59.892 1.00 37.72  ? 48  ILE B CG2 1 
ATOM   2913 C  CD1 . ILE B  1  35  ? 16.040  6.680   60.393 1.00 40.36  ? 48  ILE B CD1 1 
ATOM   2914 N  N   . ARG B  1  36  ? 16.669  2.153   58.497 1.00 31.87  ? 49  ARG B N   1 
ATOM   2915 C  CA  . ARG B  1  36  ? 16.506  0.718   58.345 1.00 33.62  ? 49  ARG B CA  1 
ATOM   2916 C  C   . ARG B  1  36  ? 16.278  0.157   59.744 1.00 34.03  ? 49  ARG B C   1 
ATOM   2917 O  O   . ARG B  1  36  ? 16.609  0.828   60.706 1.00 35.56  ? 49  ARG B O   1 
ATOM   2918 C  CB  . ARG B  1  36  ? 17.732  0.069   57.688 1.00 30.84  ? 49  ARG B CB  1 
ATOM   2919 C  CG  . ARG B  1  36  ? 18.002  0.556   56.272 1.00 30.86  ? 49  ARG B CG  1 
ATOM   2920 C  CD  . ARG B  1  36  ? 16.944  0.082   55.314 1.00 31.20  ? 49  ARG B CD  1 
ATOM   2921 N  NE  . ARG B  1  36  ? 17.179  0.503   53.928 1.00 29.64  ? 49  ARG B NE  1 
ATOM   2922 C  CZ  . ARG B  1  36  ? 16.902  1.698   53.405 1.00 32.81  ? 49  ARG B CZ  1 
ATOM   2923 N  NH1 . ARG B  1  36  ? 16.271  2.622   54.108 1.00 34.44  ? 49  ARG B NH1 1 
ATOM   2924 N  NH2 . ARG B  1  36  ? 17.247  1.959   52.157 1.00 34.06  ? 49  ARG B NH2 1 
ATOM   2925 N  N   . GLY B  1  37  ? 15.724  -1.059  59.842 1.00 33.83  ? 50  GLY B N   1 
ATOM   2926 C  CA  . GLY B  1  37  ? 15.295  -1.569  61.130 1.00 31.50  ? 50  GLY B CA  1 
ATOM   2927 C  C   . GLY B  1  37  ? 15.367  -3.090  61.203 1.00 32.12  ? 50  GLY B C   1 
ATOM   2928 O  O   . GLY B  1  37  ? 16.230  -3.730  60.584 1.00 28.75  ? 50  GLY B O   1 
ATOM   2929 N  N   . PRO B  1  38  ? 14.478  -3.707  62.008 1.00 29.02  ? 51  PRO B N   1 
ATOM   2930 C  CA  . PRO B  1  38  ? 14.587  -5.126  62.343 1.00 29.88  ? 51  PRO B CA  1 
ATOM   2931 C  C   . PRO B  1  38  ? 13.986  -6.078  61.324 1.00 30.01  ? 51  PRO B C   1 
ATOM   2932 O  O   . PRO B  1  38  ? 14.143  -7.287  61.456 1.00 31.38  ? 51  PRO B O   1 
ATOM   2933 C  CB  . PRO B  1  38  ? 13.819  -5.167  63.653 1.00 29.82  ? 51  PRO B CB  1 
ATOM   2934 C  CG  . PRO B  1  38  ? 12.693  -4.199  63.434 1.00 30.14  ? 51  PRO B CG  1 
ATOM   2935 C  CD  . PRO B  1  38  ? 13.333  -3.064  62.660 1.00 30.88  ? 51  PRO B CD  1 
ATOM   2936 N  N   . CYS B  1  39  ? 13.320  -5.526  60.303 1.00 29.59  ? 52  CYS B N   1 
ATOM   2937 C  CA  . CYS B  1  39  ? 12.685  -6.349  59.292 1.00 29.35  ? 52  CYS B CA  1 
ATOM   2938 C  C   . CYS B  1  39  ? 13.531  -6.424  58.020 1.00 28.40  ? 52  CYS B C   1 
ATOM   2939 O  O   . CYS B  1  39  ? 13.662  -5.440  57.293 1.00 26.94  ? 52  CYS B O   1 
ATOM   2940 C  CB  . CYS B  1  39  ? 11.331  -5.807  58.876 1.00 28.11  ? 52  CYS B CB  1 
ATOM   2941 S  SG  . CYS B  1  39  ? 10.544  -6.882  57.658 1.00 32.39  ? 52  CYS B SG  1 
ATOM   2942 N  N   . PRO B  1  40  ? 14.053  -7.614  57.659 1.00 29.66  ? 53  PRO B N   1 
ATOM   2943 C  CA  . PRO B  1  40  ? 14.848  -7.757  56.436 1.00 26.04  ? 53  PRO B CA  1 
ATOM   2944 C  C   . PRO B  1  40  ? 14.014  -7.598  55.174 1.00 28.24  ? 53  PRO B C   1 
ATOM   2945 O  O   . PRO B  1  40  ? 14.540  -7.180  54.146 1.00 27.80  ? 53  PRO B O   1 
ATOM   2946 C  CB  . PRO B  1  40  ? 15.456  -9.152  56.575 1.00 28.63  ? 53  PRO B CB  1 
ATOM   2947 C  CG  . PRO B  1  40  ? 14.489  -9.896  57.439 1.00 28.90  ? 53  PRO B CG  1 
ATOM   2948 C  CD  . PRO B  1  40  ? 13.897  -8.874  58.393 1.00 28.71  ? 53  PRO B CD  1 
ATOM   2949 N  N   . GLY B  1  41  ? 12.700  -7.908  55.261 1.00 25.70  ? 54  GLY B N   1 
ATOM   2950 C  CA  . GLY B  1  41  ? 11.826  -7.722  54.121 1.00 25.78  ? 54  GLY B CA  1 
ATOM   2951 C  C   . GLY B  1  41  ? 11.692  -6.246  53.754 1.00 27.47  ? 54  GLY B C   1 
ATOM   2952 O  O   . GLY B  1  41  ? 11.986  -5.848  52.630 1.00 26.26  ? 54  GLY B O   1 
ATOM   2953 N  N   . LEU B  1  42  ? 11.255  -5.440  54.719 1.00 25.85  ? 55  LEU B N   1 
ATOM   2954 C  CA  . LEU B  1  42  ? 11.095  -4.009  54.496 1.00 27.30  ? 55  LEU B CA  1 
ATOM   2955 C  C   . LEU B  1  42  ? 12.444  -3.359  54.173 1.00 28.70  ? 55  LEU B C   1 
ATOM   2956 O  O   . LEU B  1  42  ? 12.497  -2.463  53.344 1.00 30.92  ? 55  LEU B O   1 
ATOM   2957 C  CB  . LEU B  1  42  ? 10.441  -3.350  55.705 1.00 25.83  ? 55  LEU B CB  1 
ATOM   2958 C  CG  . LEU B  1  42  ? 9.046   -3.872  56.067 1.00 27.03  ? 55  LEU B CG  1 
ATOM   2959 C  CD1 . LEU B  1  42  ? 8.533   -3.184  57.307 1.00 30.22  ? 55  LEU B CD1 1 
ATOM   2960 C  CD2 . LEU B  1  42  ? 8.050   -3.709  54.927 1.00 29.51  ? 55  LEU B CD2 1 
ATOM   2961 N  N   . ASN B  1  43  ? 13.510  -3.765  54.876 1.00 27.89  ? 56  ASN B N   1 
ATOM   2962 C  CA  . ASN B  1  43  ? 14.838  -3.218  54.617 1.00 30.45  ? 56  ASN B CA  1 
ATOM   2963 C  C   . ASN B  1  43  ? 15.230  -3.410  53.151 1.00 29.50  ? 56  ASN B C   1 
ATOM   2964 O  O   . ASN B  1  43  ? 15.694  -2.455  52.518 1.00 26.57  ? 56  ASN B O   1 
ATOM   2965 C  CB  . ASN B  1  43  ? 15.907  -3.829  55.499 1.00 29.32  ? 56  ASN B CB  1 
ATOM   2966 C  CG  . ASN B  1  43  ? 15.830  -3.423  56.948 1.00 31.92  ? 56  ASN B CG  1 
ATOM   2967 O  OD1 . ASN B  1  43  ? 15.197  -2.423  57.305 1.00 29.34  ? 56  ASN B OD1 1 
ATOM   2968 N  ND2 . ASN B  1  43  ? 16.508  -4.187  57.792 1.00 29.35  ? 56  ASN B ND2 1 
ATOM   2969 N  N   . THR B  1  44  ? 15.043  -4.637  52.627 1.00 26.75  ? 57  THR B N   1 
ATOM   2970 C  CA  . THR B  1  44  ? 15.394  -4.921  51.244 1.00 28.92  ? 57  THR B CA  1 
ATOM   2971 C  C   . THR B  1  44  ? 14.516  -4.101  50.286 1.00 29.78  ? 57  THR B C   1 
ATOM   2972 O  O   . THR B  1  44  ? 15.002  -3.586  49.285 1.00 28.09  ? 57  THR B O   1 
ATOM   2973 C  CB  . THR B  1  44  ? 15.302  -6.427  50.991 1.00 27.89  ? 57  THR B CB  1 
ATOM   2974 O  OG1 . THR B  1  44  ? 16.221  -7.025  51.908 1.00 28.39  ? 57  THR B OG1 1 
ATOM   2975 C  CG2 . THR B  1  44  ? 15.679  -6.793  49.566 1.00 28.53  ? 57  THR B CG2 1 
ATOM   2976 N  N   . LEU B  1  45  ? 13.212  -3.994  50.566 1.00 28.40  ? 58  LEU B N   1 
ATOM   2977 C  CA  . LEU B  1  45  ? 12.315  -3.223  49.714 1.00 30.89  ? 58  LEU B CA  1 
ATOM   2978 C  C   . LEU B  1  45  ? 12.739  -1.757  49.657 1.00 31.90  ? 58  LEU B C   1 
ATOM   2979 O  O   . LEU B  1  45  ? 12.704  -1.135  48.590 1.00 31.88  ? 58  LEU B O   1 
ATOM   2980 C  CB  . LEU B  1  45  ? 10.886  -3.384  50.223 1.00 31.16  ? 58  LEU B CB  1 
ATOM   2981 C  CG  . LEU B  1  45  ? 10.304  -4.788  50.066 1.00 29.68  ? 58  LEU B CG  1 
ATOM   2982 C  CD1 . LEU B  1  45  ? 9.008   -4.974  50.831 1.00 31.36  ? 58  LEU B CD1 1 
ATOM   2983 C  CD2 . LEU B  1  45  ? 10.093  -5.100  48.585 1.00 30.33  ? 58  LEU B CD2 1 
ATOM   2984 N  N   . ALA B  1  46  ? 13.154  -1.210  50.795 1.00 29.17  ? 59  ALA B N   1 
ATOM   2985 C  CA  . ALA B  1  46  ? 13.601  0.169   50.837 1.00 30.69  ? 59  ALA B CA  1 
ATOM   2986 C  C   . ALA B  1  46  ? 14.898  0.330   50.045 1.00 34.61  ? 59  ALA B C   1 
ATOM   2987 O  O   . ALA B  1  46  ? 15.058  1.294   49.297 1.00 33.27  ? 59  ALA B O   1 
ATOM   2988 C  CB  . ALA B  1  46  ? 13.787  0.637   52.274 1.00 28.33  ? 59  ALA B CB  1 
ATOM   2989 N  N   . SER B  1  47  ? 15.831  -0.608  50.211 1.00 31.74  ? 60  SER B N   1 
ATOM   2990 C  CA  . SER B  1  47  ? 17.145  -0.469  49.598 1.00 29.77  ? 60  SER B CA  1 
ATOM   2991 C  C   . SER B  1  47  ? 17.112  -0.743  48.091 1.00 31.57  ? 60  SER B C   1 
ATOM   2992 O  O   . SER B  1  47  ? 18.092  -0.446  47.410 1.00 29.89  ? 60  SER B O   1 
ATOM   2993 C  CB  . SER B  1  47  ? 18.177  -1.299  50.332 1.00 28.83  ? 60  SER B CB  1 
ATOM   2994 O  OG  . SER B  1  47  ? 18.576  -0.630  51.536 1.00 26.40  ? 60  SER B OG  1 
ATOM   2995 N  N   . HIS B  1  48  ? 15.994  -1.277  47.572 1.00 30.34  ? 61  HIS B N   1 
ATOM   2996 C  CA  . HIS B  1  48  ? 15.777  -1.415  46.138 1.00 32.14  ? 61  HIS B CA  1 
ATOM   2997 C  C   . HIS B  1  48  ? 14.741  -0.423  45.591 1.00 32.63  ? 61  HIS B C   1 
ATOM   2998 O  O   . HIS B  1  48  ? 14.388  -0.498  44.406 1.00 34.19  ? 61  HIS B O   1 
ATOM   2999 C  CB  . HIS B  1  48  ? 15.336  -2.837  45.777 1.00 29.67  ? 61  HIS B CB  1 
ATOM   3000 C  CG  . HIS B  1  48  ? 16.459  -3.817  45.765 1.00 32.22  ? 61  HIS B CG  1 
ATOM   3001 N  ND1 . HIS B  1  48  ? 17.063  -4.196  44.590 1.00 31.56  ? 61  HIS B ND1 1 
ATOM   3002 C  CD2 . HIS B  1  48  ? 17.061  -4.515  46.746 1.00 32.45  ? 61  HIS B CD2 1 
ATOM   3003 C  CE1 . HIS B  1  48  ? 18.020  -5.082  44.867 1.00 33.09  ? 61  HIS B CE1 1 
ATOM   3004 N  NE2 . HIS B  1  48  ? 18.045  -5.279  46.178 1.00 30.42  ? 61  HIS B NE2 1 
ATOM   3005 N  N   . GLY B  1  49  ? 14.215  0.463   46.444 1.00 36.20  ? 62  GLY B N   1 
ATOM   3006 C  CA  . GLY B  1  49  ? 13.303  1.513   45.997 1.00 36.18  ? 62  GLY B CA  1 
ATOM   3007 C  C   . GLY B  1  49  ? 11.867  1.049   45.744 1.00 36.56  ? 62  GLY B C   1 
ATOM   3008 O  O   . GLY B  1  49  ? 11.094  1.790   45.148 1.00 38.83  ? 62  GLY B O   1 
ATOM   3009 N  N   . TYR B  1  50  ? 11.483  -0.143  46.214 1.00 33.69  ? 63  TYR B N   1 
ATOM   3010 C  CA  . TYR B  1  50  ? 10.085  -0.530  46.261 1.00 35.37  ? 63  TYR B CA  1 
ATOM   3011 C  C   . TYR B  1  50  ? 9.332   0.302   47.302 1.00 35.69  ? 63  TYR B C   1 
ATOM   3012 O  O   . TYR B  1  50  ? 8.157   0.595   47.115 1.00 36.85  ? 63  TYR B O   1 
ATOM   3013 C  CB  . TYR B  1  50  ? 9.910   -2.026  46.532 1.00 33.96  ? 63  TYR B CB  1 
ATOM   3014 C  CG  . TYR B  1  50  ? 10.087  -2.867  45.275 1.00 33.64  ? 63  TYR B CG  1 
ATOM   3015 C  CD1 . TYR B  1  50  ? 9.050   -3.045  44.368 1.00 35.44  ? 63  TYR B CD1 1 
ATOM   3016 C  CD2 . TYR B  1  50  ? 11.311  -3.464  44.990 1.00 34.18  ? 63  TYR B CD2 1 
ATOM   3017 C  CE1 . TYR B  1  50  ? 9.214   -3.810  43.221 1.00 39.83  ? 63  TYR B CE1 1 
ATOM   3018 C  CE2 . TYR B  1  50  ? 11.486  -4.236  43.855 1.00 33.40  ? 63  TYR B CE2 1 
ATOM   3019 C  CZ  . TYR B  1  50  ? 10.446  -4.394  42.956 1.00 37.40  ? 63  TYR B CZ  1 
ATOM   3020 O  OH  . TYR B  1  50  ? 10.628  -5.153  41.841 1.00 36.89  ? 63  TYR B OH  1 
ATOM   3021 N  N   . LEU B  1  51  ? 10.003  0.600   48.417 1.00 38.28  ? 64  LEU B N   1 
ATOM   3022 C  CA  . LEU B  1  51  ? 9.577   1.607   49.372 1.00 38.35  ? 64  LEU B CA  1 
ATOM   3023 C  C   . LEU B  1  51  ? 10.426  2.847   49.147 1.00 39.85  ? 64  LEU B C   1 
ATOM   3024 O  O   . LEU B  1  51  ? 11.510  2.743   48.570 1.00 40.68  ? 64  LEU B O   1 
ATOM   3025 C  CB  . LEU B  1  51  ? 9.801   1.097   50.797 1.00 40.91  ? 64  LEU B CB  1 
ATOM   3026 C  CG  . LEU B  1  51  ? 8.865   -0.018  51.267 1.00 41.12  ? 64  LEU B CG  1 
ATOM   3027 C  CD1 . LEU B  1  51  ? 9.329   -0.599  52.598 1.00 41.92  ? 64  LEU B CD1 1 
ATOM   3028 C  CD2 . LEU B  1  51  ? 7.467   0.519   51.380 1.00 45.10  ? 64  LEU B CD2 1 
ATOM   3029 N  N   . PRO B  1  52  ? 10.018  4.026   49.669 1.00 39.95  ? 65  PRO B N   1 
ATOM   3030 C  CA  . PRO B  1  52  ? 10.922  5.171   49.754 1.00 38.58  ? 65  PRO B CA  1 
ATOM   3031 C  C   . PRO B  1  52  ? 12.240  4.700   50.356 1.00 38.86  ? 65  PRO B C   1 
ATOM   3032 O  O   . PRO B  1  52  ? 12.249  3.968   51.339 1.00 37.70  ? 65  PRO B O   1 
ATOM   3033 C  CB  . PRO B  1  52  ? 10.164  6.154   50.653 1.00 41.43  ? 65  PRO B CB  1 
ATOM   3034 C  CG  . PRO B  1  52  ? 8.712   5.831   50.379 1.00 40.58  ? 65  PRO B CG  1 
ATOM   3035 C  CD  . PRO B  1  52  ? 8.685   4.314   50.222 1.00 42.13  ? 65  PRO B CD  1 
ATOM   3036 N  N   . ARG B  1  53  ? 13.351  5.091   49.725 1.00 36.45  ? 66  ARG B N   1 
ATOM   3037 C  CA  . ARG B  1  53  ? 14.672  4.652   50.120 1.00 36.55  ? 66  ARG B CA  1 
ATOM   3038 C  C   . ARG B  1  53  ? 15.053  5.172   51.495 1.00 35.29  ? 66  ARG B C   1 
ATOM   3039 O  O   . ARG B  1  53  ? 15.981  4.658   52.098 1.00 37.78  ? 66  ARG B O   1 
ATOM   3040 C  CB  . ARG B  1  53  ? 15.713  5.045   49.067 1.00 39.89  ? 66  ARG B CB  1 
ATOM   3041 C  CG  . ARG B  1  53  ? 15.471  4.353   47.737 1.00 38.33  ? 66  ARG B CG  1 
ATOM   3042 C  CD  . ARG B  1  53  ? 16.580  4.616   46.738 1.00 35.44  ? 66  ARG B CD  1 
ATOM   3043 N  NE  . ARG B  1  53  ? 16.276  3.858   45.521 1.00 37.40  ? 66  ARG B NE  1 
ATOM   3044 C  CZ  . ARG B  1  53  ? 16.754  2.661   45.223 1.00 35.05  ? 66  ARG B CZ  1 
ATOM   3045 N  NH1 . ARG B  1  53  ? 17.487  1.998   46.094 1.00 34.43  ? 66  ARG B NH1 1 
ATOM   3046 N  NH2 . ARG B  1  53  ? 16.479  2.128   44.055 1.00 34.14  ? 66  ARG B NH2 1 
ATOM   3047 N  N   . ASP B  1  54  ? 14.346  6.176   52.008 1.00 38.58  ? 67  ASP B N   1 
ATOM   3048 C  CA  . ASP B  1  54  ? 14.649  6.687   53.334 1.00 35.85  ? 67  ASP B CA  1 
ATOM   3049 C  C   . ASP B  1  54  ? 13.991  5.848   54.430 1.00 34.32  ? 67  ASP B C   1 
ATOM   3050 O  O   . ASP B  1  54  ? 14.212  6.109   55.601 1.00 36.29  ? 67  ASP B O   1 
ATOM   3051 C  CB  . ASP B  1  54  ? 14.310  8.160   53.492 1.00 44.69  ? 67  ASP B CB  1 
ATOM   3052 C  CG  . ASP B  1  54  ? 12.850  8.551   53.349 1.00 46.41  ? 67  ASP B CG  1 
ATOM   3053 O  OD1 . ASP B  1  54  ? 11.987  7.646   53.238 1.00 42.22  ? 67  ASP B OD1 1 
ATOM   3054 O  OD2 . ASP B  1  54  ? 12.612  9.781   53.302 1.00 52.09  ? 67  ASP B OD2 1 
ATOM   3055 N  N   . GLY B  1  55  ? 13.210  4.833   54.069 1.00 34.35  ? 68  GLY B N   1 
ATOM   3056 C  CA  . GLY B  1  55  ? 12.693  3.901   55.064 1.00 36.53  ? 68  GLY B CA  1 
ATOM   3057 C  C   . GLY B  1  55  ? 11.493  4.447   55.849 1.00 36.44  ? 68  GLY B C   1 
ATOM   3058 O  O   . GLY B  1  55  ? 11.195  3.963   56.939 1.00 35.63  ? 68  GLY B O   1 
ATOM   3059 N  N   . VAL B  1  56  ? 10.814  5.455   55.298 1.00 39.49  ? 69  VAL B N   1 
ATOM   3060 C  CA  . VAL B  1  56  ? 9.608   5.995   55.901 1.00 36.99  ? 69  VAL B CA  1 
ATOM   3061 C  C   . VAL B  1  56  ? 8.526   5.951   54.838 1.00 37.21  ? 69  VAL B C   1 
ATOM   3062 O  O   . VAL B  1  56  ? 8.740   6.422   53.730 1.00 39.34  ? 69  VAL B O   1 
ATOM   3063 C  CB  . VAL B  1  56  ? 9.826   7.417   56.441 1.00 40.96  ? 69  VAL B CB  1 
ATOM   3064 C  CG1 . VAL B  1  56  ? 8.522   8.071   56.896 1.00 43.93  ? 69  VAL B CG1 1 
ATOM   3065 C  CG2 . VAL B  1  56  ? 10.844  7.416   57.568 1.00 39.19  ? 69  VAL B CG2 1 
ATOM   3066 N  N   . ALA B  1  57  ? 7.376   5.360   55.174 1.00 34.60  ? 70  ALA B N   1 
ATOM   3067 C  CA  . ALA B  1  57  ? 6.366   5.093   54.174 1.00 38.98  ? 70  ALA B CA  1 
ATOM   3068 C  C   . ALA B  1  57  ? 4.967   5.138   54.786 1.00 38.25  ? 70  ALA B C   1 
ATOM   3069 O  O   . ALA B  1  57  ? 4.813   4.980   55.996 1.00 37.78  ? 70  ALA B O   1 
ATOM   3070 C  CB  . ALA B  1  57  ? 6.644   3.736   53.560 1.00 37.71  ? 70  ALA B CB  1 
ATOM   3071 N  N   . THR B  1  58  ? 3.965   5.272   53.912 1.00 39.00  ? 71  THR B N   1 
ATOM   3072 C  CA  . THR B  1  58  ? 2.576   5.131   54.299 1.00 37.15  ? 71  THR B CA  1 
ATOM   3073 C  C   . THR B  1  58  ? 2.259   3.646   54.404 1.00 38.36  ? 71  THR B C   1 
ATOM   3074 O  O   . THR B  1  58  ? 2.917   2.813   53.792 1.00 38.16  ? 71  THR B O   1 
ATOM   3075 C  CB  . THR B  1  58  ? 1.621   5.804   53.317 1.00 36.05  ? 71  THR B CB  1 
ATOM   3076 O  OG1 . THR B  1  58  ? 1.660   5.031   52.124 1.00 38.00  ? 71  THR B OG1 1 
ATOM   3077 C  CG2 . THR B  1  58  ? 1.960   7.251   53.033 1.00 42.08  ? 71  THR B CG2 1 
ATOM   3078 N  N   . PRO B  1  59  ? 1.235   3.270   55.188 1.00 37.75  ? 72  PRO B N   1 
ATOM   3079 C  CA  . PRO B  1  59  ? 0.755   1.891   55.196 1.00 35.95  ? 72  PRO B CA  1 
ATOM   3080 C  C   . PRO B  1  59  ? 0.452   1.351   53.809 1.00 38.31  ? 72  PRO B C   1 
ATOM   3081 O  O   . PRO B  1  59  ? 0.786   0.209   53.521 1.00 34.56  ? 72  PRO B O   1 
ATOM   3082 C  CB  . PRO B  1  59  ? -0.509  2.013   56.066 1.00 38.73  ? 72  PRO B CB  1 
ATOM   3083 C  CG  . PRO B  1  59  ? -0.149  3.101   57.054 1.00 35.66  ? 72  PRO B CG  1 
ATOM   3084 C  CD  . PRO B  1  59  ? 0.561   4.121   56.185 1.00 38.04  ? 72  PRO B CD  1 
ATOM   3085 N  N   . ALA B  1  60  ? -0.187  2.172   52.960 1.00 38.34  ? 73  ALA B N   1 
ATOM   3086 C  CA  . ALA B  1  60  ? -0.519  1.746   51.613 1.00 38.37  ? 73  ALA B CA  1 
ATOM   3087 C  C   . ALA B  1  60  ? 0.756   1.436   50.830 1.00 33.25  ? 73  ALA B C   1 
ATOM   3088 O  O   . ALA B  1  60  ? 0.785   0.438   50.140 1.00 37.58  ? 73  ALA B O   1 
ATOM   3089 C  CB  . ALA B  1  60  ? -1.355  2.770   50.888 1.00 36.10  ? 73  ALA B CB  1 
ATOM   3090 N  N   . GLN B  1  61  ? 1.784   2.275   50.947 1.00 38.70  ? 74  GLN B N   1 
ATOM   3091 C  CA  . GLN B  1  61  ? 3.055   2.021   50.273 1.00 38.24  ? 74  GLN B CA  1 
ATOM   3092 C  C   . GLN B  1  61  ? 3.674   0.700   50.738 1.00 36.64  ? 74  GLN B C   1 
ATOM   3093 O  O   . GLN B  1  61  ? 4.202   -0.041  49.924 1.00 37.46  ? 74  GLN B O   1 
ATOM   3094 C  CB  . GLN B  1  61  ? 4.053   3.149   50.501 1.00 39.17  ? 74  GLN B CB  1 
ATOM   3095 C  CG  . GLN B  1  61  ? 3.688   4.410   49.739 1.00 41.02  ? 74  GLN B CG  1 
ATOM   3096 C  CD  . GLN B  1  61  ? 4.595   5.569   50.059 1.00 42.91  ? 74  GLN B CD  1 
ATOM   3097 O  OE1 . GLN B  1  61  ? 4.944   5.823   51.215 1.00 38.64  ? 74  GLN B OE1 1 
ATOM   3098 N  NE2 . GLN B  1  61  ? 5.007   6.274   49.017 1.00 49.91  ? 74  GLN B NE2 1 
ATOM   3099 N  N   . ILE B  1  62  ? 3.595   0.405   52.037 1.00 36.46  ? 75  ILE B N   1 
ATOM   3100 C  CA  . ILE B  1  62  ? 4.179   -0.807  52.590 1.00 36.66  ? 75  ILE B CA  1 
ATOM   3101 C  C   . ILE B  1  62  ? 3.456   -2.027  52.038 1.00 35.58  ? 75  ILE B C   1 
ATOM   3102 O  O   . ILE B  1  62  ? 4.096   -2.990  51.609 1.00 35.57  ? 75  ILE B O   1 
ATOM   3103 C  CB  . ILE B  1  62  ? 4.188   -0.752  54.130 1.00 33.77  ? 75  ILE B CB  1 
ATOM   3104 C  CG1 . ILE B  1  62  ? 5.153   0.313   54.603 1.00 31.57  ? 75  ILE B CG1 1 
ATOM   3105 C  CG2 . ILE B  1  62  ? 4.518   -2.122  54.728 1.00 34.76  ? 75  ILE B CG2 1 
ATOM   3106 C  CD1 . ILE B  1  62  ? 5.023   0.716   56.056 1.00 33.59  ? 75  ILE B CD1 1 
ATOM   3107 N  N   . ILE B  1  63  ? 2.123   -1.979  52.038 1.00 31.97  ? 76  ILE B N   1 
ATOM   3108 C  CA  . ILE B  1  63  ? 1.339   -3.098  51.559 1.00 33.05  ? 76  ILE B CA  1 
ATOM   3109 C  C   . ILE B  1  63  ? 1.675   -3.371  50.096 1.00 35.25  ? 76  ILE B C   1 
ATOM   3110 O  O   . ILE B  1  63  ? 1.957   -4.513  49.739 1.00 33.71  ? 76  ILE B O   1 
ATOM   3111 C  CB  . ILE B  1  63  ? -0.160  -2.875  51.808 1.00 33.36  ? 76  ILE B CB  1 
ATOM   3112 C  CG1 . ILE B  1  63  ? -0.450  -2.989  53.311 1.00 35.09  ? 76  ILE B CG1 1 
ATOM   3113 C  CG2 . ILE B  1  63  ? -0.998  -3.860  51.009 1.00 32.44  ? 76  ILE B CG2 1 
ATOM   3114 C  CD1 . ILE B  1  63  ? -1.722  -2.296  53.743 1.00 42.91  ? 76  ILE B CD1 1 
ATOM   3115 N  N   . THR B  1  64  ? 1.700   -2.333  49.263 1.00 34.84  ? 77  THR B N   1 
ATOM   3116 C  CA  A THR B  1  64  ? 1.935   -2.529  47.839 0.50 35.61  ? 77  THR B CA  1 
ATOM   3117 C  CA  B THR B  1  64  ? 1.927   -2.551  47.838 0.50 37.23  ? 77  THR B CA  1 
ATOM   3118 C  C   . THR B  1  64  ? 3.366   -3.029  47.617 1.00 32.78  ? 77  THR B C   1 
ATOM   3119 O  O   . THR B  1  64  ? 3.591   -3.895  46.792 1.00 33.60  ? 77  THR B O   1 
ATOM   3120 C  CB  A THR B  1  64  ? 1.649   -1.232  47.089 0.50 35.08  ? 77  THR B CB  1 
ATOM   3121 C  CB  B THR B  1  64  ? 1.558   -1.339  46.978 0.50 40.42  ? 77  THR B CB  1 
ATOM   3122 O  OG1 A THR B  1  64  ? 2.566   -0.350  47.723 0.50 47.19  ? 77  THR B OG1 1 
ATOM   3123 O  OG1 B THR B  1  64  ? 2.109   -1.517  45.668 0.50 37.15  ? 77  THR B OG1 1 
ATOM   3124 C  CG2 A THR B  1  64  ? 0.222   -0.761  47.247 0.50 29.75  ? 77  THR B CG2 1 
ATOM   3125 C  CG2 B THR B  1  64  ? 2.177   -0.039  47.434 0.50 47.10  ? 77  THR B CG2 1 
ATOM   3126 N  N   . ALA B  1  65  ? 4.331   -2.517  48.389 1.00 33.25  ? 78  ALA B N   1 
ATOM   3127 C  CA  . ALA B  1  65  ? 5.730   -2.914  48.222 1.00 34.47  ? 78  ALA B CA  1 
ATOM   3128 C  C   . ALA B  1  65  ? 5.938   -4.380  48.597 1.00 34.00  ? 78  ALA B C   1 
ATOM   3129 O  O   . ALA B  1  65  ? 6.653   -5.086  47.895 1.00 32.41  ? 78  ALA B O   1 
ATOM   3130 C  CB  . ALA B  1  65  ? 6.653   -2.038  49.022 1.00 31.19  ? 78  ALA B CB  1 
ATOM   3131 N  N   . THR B  1  66  ? 5.310   -4.850  49.678 1.00 32.31  ? 79  THR B N   1 
ATOM   3132 C  CA  . THR B  1  66  ? 5.478   -6.237  50.081 1.00 30.75  ? 79  THR B CA  1 
ATOM   3133 C  C   . THR B  1  66  ? 4.832   -7.158  49.058 1.00 30.63  ? 79  THR B C   1 
ATOM   3134 O  O   . THR B  1  66  ? 5.310   -8.262  48.836 1.00 32.46  ? 79  THR B O   1 
ATOM   3135 C  CB  . THR B  1  66  ? 4.950   -6.498  51.495 1.00 33.31  ? 79  THR B CB  1 
ATOM   3136 O  OG1 . THR B  1  66  ? 3.557   -6.222  51.552 1.00 31.53  ? 79  THR B OG1 1 
ATOM   3137 C  CG2 . THR B  1  66  ? 5.709   -5.713  52.550 1.00 31.67  ? 79  THR B CG2 1 
ATOM   3138 N  N   . GLN B  1  67  ? 3.708   -6.737  48.466 1.00 32.29  ? 80  GLN B N   1 
ATOM   3139 C  CA  . GLN B  1  67  ? 3.051   -7.508  47.417 1.00 33.12  ? 80  GLN B CA  1 
ATOM   3140 C  C   . GLN B  1  67  ? 3.897   -7.505  46.142 1.00 33.11  ? 80  GLN B C   1 
ATOM   3141 O  O   . GLN B  1  67  ? 4.145   -8.556  45.576 1.00 37.14  ? 80  GLN B O   1 
ATOM   3142 C  CB  . GLN B  1  67  ? 1.639   -6.962  47.171 1.00 32.85  ? 80  GLN B CB  1 
ATOM   3143 C  CG  . GLN B  1  67  ? 0.760   -7.126  48.402 1.00 33.27  ? 80  GLN B CG  1 
ATOM   3144 C  CD  . GLN B  1  67  ? -0.683  -6.693  48.250 1.00 39.17  ? 80  GLN B CD  1 
ATOM   3145 O  OE1 . GLN B  1  67  ? -1.516  -7.122  49.046 1.00 36.64  ? 80  GLN B OE1 1 
ATOM   3146 N  NE2 . GLN B  1  67  ? -0.993  -5.833  47.282 1.00 35.99  ? 80  GLN B NE2 1 
ATOM   3147 N  N   . GLU B  1  68  ? 4.340   -6.334  45.693 1.00 33.19  ? 81  GLU B N   1 
ATOM   3148 C  CA  . GLU B  1  68  ? 5.067   -6.216  44.436 1.00 35.13  ? 81  GLU B CA  1 
ATOM   3149 C  C   . GLU B  1  68  ? 6.410   -6.930  44.517 1.00 36.92  ? 81  GLU B C   1 
ATOM   3150 O  O   . GLU B  1  68  ? 6.757   -7.654  43.597 1.00 39.02  ? 81  GLU B O   1 
ATOM   3151 C  CB  . GLU B  1  68  ? 5.294   -4.762  44.026 1.00 41.87  ? 81  GLU B CB  1 
ATOM   3152 C  CG  . GLU B  1  68  ? 4.011   -4.033  43.618 1.00 52.02  ? 81  GLU B CG  1 
ATOM   3153 C  CD  . GLU B  1  68  ? 3.237   -4.691  42.475 1.00 62.88  ? 81  GLU B CD  1 
ATOM   3154 O  OE1 . GLU B  1  68  ? 1.997   -4.911  42.555 1.00 65.51  ? 81  GLU B OE1 1 
ATOM   3155 O  OE2 . GLU B  1  68  ? 3.920   -5.027  41.488 1.00 65.16  ? 81  GLU B OE2 1 
ATOM   3156 N  N   . GLY B  1  69  ? 7.135   -6.748  45.630 1.00 33.44  ? 82  GLY B N   1 
ATOM   3157 C  CA  . GLY B  1  69  ? 8.504   -7.222  45.760 1.00 30.95  ? 82  GLY B CA  1 
ATOM   3158 C  C   . GLY B  1  69  ? 8.593   -8.702  46.144 1.00 31.00  ? 82  GLY B C   1 
ATOM   3159 O  O   . GLY B  1  69  ? 9.528   -9.367  45.715 1.00 32.50  ? 82  GLY B O   1 
ATOM   3160 N  N   . PHE B  1  70  ? 7.654   -9.197  46.966 1.00 30.76  ? 83  PHE B N   1 
ATOM   3161 C  CA  . PHE B  1  70  ? 7.764   -10.536 47.517 1.00 29.67  ? 83  PHE B CA  1 
ATOM   3162 C  C   . PHE B  1  70  ? 6.510   -11.384 47.334 1.00 31.53  ? 83  PHE B C   1 
ATOM   3163 O  O   . PHE B  1  70  ? 6.497   -12.545 47.746 1.00 29.52  ? 83  PHE B O   1 
ATOM   3164 C  CB  . PHE B  1  70  ? 8.059   -10.488 49.016 1.00 30.62  ? 83  PHE B CB  1 
ATOM   3165 C  CG  . PHE B  1  70  ? 9.482   -10.091 49.354 1.00 29.50  ? 83  PHE B CG  1 
ATOM   3166 C  CD1 . PHE B  1  70  ? 10.537  -10.967 49.143 1.00 30.59  ? 83  PHE B CD1 1 
ATOM   3167 C  CD2 . PHE B  1  70  ? 9.758   -8.862  49.922 1.00 31.92  ? 83  PHE B CD2 1 
ATOM   3168 C  CE1 . PHE B  1  70  ? 11.834  -10.620 49.495 1.00 30.43  ? 83  PHE B CE1 1 
ATOM   3169 C  CE2 . PHE B  1  70  ? 11.055  -8.514  50.265 1.00 31.80  ? 83  PHE B CE2 1 
ATOM   3170 C  CZ  . PHE B  1  70  ? 12.092  -9.384  50.038 1.00 31.66  ? 83  PHE B CZ  1 
ATOM   3171 N  N   . ASN B  1  71  ? 5.433   -10.812 46.793 1.00 31.60  ? 84  ASN B N   1 
ATOM   3172 C  CA  . ASN B  1  71  ? 4.151   -11.499 46.727 1.00 31.88  ? 84  ASN B CA  1 
ATOM   3173 C  C   . ASN B  1  71  ? 3.647   -11.845 48.125 1.00 30.17  ? 84  ASN B C   1 
ATOM   3174 O  O   . ASN B  1  71  ? 3.062   -12.893 48.343 1.00 31.70  ? 84  ASN B O   1 
ATOM   3175 C  CB  . ASN B  1  71  ? 4.215   -12.731 45.833 1.00 34.22  ? 84  ASN B CB  1 
ATOM   3176 C  CG  . ASN B  1  71  ? 3.004   -12.861 44.927 1.00 36.98  ? 84  ASN B CG  1 
ATOM   3177 O  OD1 . ASN B  1  71  ? 1.981   -12.196 45.123 1.00 35.78  ? 84  ASN B OD1 1 
ATOM   3178 N  ND2 . ASN B  1  71  ? 3.104   -13.713 43.920 1.00 34.50  ? 84  ASN B ND2 1 
ATOM   3179 N  N   . PHE B  1  72  ? 3.903   -10.973 49.099 1.00 32.40  ? 85  PHE B N   1 
ATOM   3180 C  CA  . PHE B  1  72  ? 3.319   -11.155 50.415 1.00 32.26  ? 85  PHE B CA  1 
ATOM   3181 C  C   . PHE B  1  72  ? 1.795   -11.118 50.256 1.00 31.46  ? 85  PHE B C   1 
ATOM   3182 O  O   . PHE B  1  72  ? 1.260   -10.241 49.580 1.00 33.43  ? 85  PHE B O   1 
ATOM   3183 C  CB  . PHE B  1  72  ? 3.815   -10.054 51.352 1.00 30.45  ? 85  PHE B CB  1 
ATOM   3184 C  CG  . PHE B  1  72  ? 3.738   -10.368 52.836 1.00 33.17  ? 85  PHE B CG  1 
ATOM   3185 C  CD1 . PHE B  1  72  ? 4.079   -11.625 53.323 1.00 37.18  ? 85  PHE B CD1 1 
ATOM   3186 C  CD2 . PHE B  1  72  ? 3.309   -9.411  53.742 1.00 33.61  ? 85  PHE B CD2 1 
ATOM   3187 C  CE1 . PHE B  1  72  ? 4.016   -11.903 54.681 1.00 36.91  ? 85  PHE B CE1 1 
ATOM   3188 C  CE2 . PHE B  1  72  ? 3.260   -9.691  55.102 1.00 36.69  ? 85  PHE B CE2 1 
ATOM   3189 C  CZ  . PHE B  1  72  ? 3.604   -10.941 55.565 1.00 36.60  ? 85  PHE B CZ  1 
ATOM   3190 N  N   . GLU B  1  73  ? 1.109   -12.071 50.875 1.00 30.85  ? 86  GLU B N   1 
ATOM   3191 C  CA  . GLU B  1  73  ? -0.336  -12.181 50.735 1.00 37.78  ? 86  GLU B CA  1 
ATOM   3192 C  C   . GLU B  1  73  ? -1.017  -10.959 51.366 1.00 36.52  ? 86  GLU B C   1 
ATOM   3193 O  O   . GLU B  1  73  ? -0.602  -10.473 52.409 1.00 33.61  ? 86  GLU B O   1 
ATOM   3194 C  CB  . GLU B  1  73  ? -0.773  -13.515 51.328 1.00 37.30  ? 86  GLU B CB  1 
ATOM   3195 C  CG  . GLU B  1  73  ? -2.231  -13.880 51.072 1.00 41.48  ? 86  GLU B CG  1 
ATOM   3196 C  CD  . GLU B  1  73  ? -3.221  -13.236 52.040 1.00 48.04  ? 86  GLU B CD  1 
ATOM   3197 O  OE1 . GLU B  1  73  ? -4.311  -12.780 51.595 1.00 47.75  ? 86  GLU B OE1 1 
ATOM   3198 O  OE2 . GLU B  1  73  ? -2.883  -13.165 53.245 1.00 45.86  ? 86  GLU B OE2 1 
ATOM   3199 N  N   . ASN B  1  74  ? -2.090  -10.500 50.733 1.00 35.44  ? 87  ASN B N   1 
ATOM   3200 C  CA  . ASN B  1  74  ? -2.728  -9.217  51.014 1.00 36.65  ? 87  ASN B CA  1 
ATOM   3201 C  C   . ASN B  1  74  ? -3.170  -9.088  52.477 1.00 34.79  ? 87  ASN B C   1 
ATOM   3202 O  O   . ASN B  1  74  ? -2.876  -8.080  53.113 1.00 33.68  ? 87  ASN B O   1 
ATOM   3203 C  CB  . ASN B  1  74  ? -3.889  -9.007  50.039 1.00 37.89  ? 87  ASN B CB  1 
ATOM   3204 C  CG  . ASN B  1  74  ? -4.642  -7.722  50.280 1.00 38.56  ? 87  ASN B CG  1 
ATOM   3205 O  OD1 . ASN B  1  74  ? -5.833  -7.779  50.614 1.00 40.13  ? 87  ASN B OD1 1 
ATOM   3206 N  ND2 . ASN B  1  74  ? -3.984  -6.584  50.094 1.00 32.68  ? 87  ASN B ND2 1 
ATOM   3207 N  N   . ASN B  1  75  ? -3.866  -10.088 53.016 1.00 33.01  ? 88  ASN B N   1 
ATOM   3208 C  CA  . ASN B  1  75  ? -4.347  -9.998  54.388 1.00 36.89  ? 88  ASN B CA  1 
ATOM   3209 C  C   . ASN B  1  75  ? -3.183  -10.054 55.378 1.00 37.96  ? 88  ASN B C   1 
ATOM   3210 O  O   . ASN B  1  75  ? -3.211  -9.350  56.383 1.00 33.95  ? 88  ASN B O   1 
ATOM   3211 C  CB  . ASN B  1  75  ? -5.404  -11.051 54.701 1.00 37.67  ? 88  ASN B CB  1 
ATOM   3212 C  CG  . ASN B  1  75  ? -6.729  -10.686 54.082 1.00 43.40  ? 88  ASN B CG  1 
ATOM   3213 O  OD1 . ASN B  1  75  ? -7.207  -9.562  54.279 1.00 44.02  ? 88  ASN B OD1 1 
ATOM   3214 N  ND2 . ASN B  1  75  ? -7.301  -11.587 53.301 1.00 43.46  ? 88  ASN B ND2 1 
ATOM   3215 N  N   . ALA B  1  76  ? -2.169  -10.887 55.094 1.00 34.00  ? 89  ALA B N   1 
ATOM   3216 C  CA  . ALA B  1  76  ? -0.978  -10.925 55.925 1.00 33.87  ? 89  ALA B CA  1 
ATOM   3217 C  C   . ALA B  1  76  ? -0.297  -9.560  55.937 1.00 30.29  ? 89  ALA B C   1 
ATOM   3218 O  O   . ALA B  1  76  ? 0.167   -9.113  56.985 1.00 32.21  ? 89  ALA B O   1 
ATOM   3219 C  CB  . ALA B  1  76  ? -0.047  -12.017 55.468 1.00 33.53  ? 89  ALA B CB  1 
ATOM   3220 N  N   . ALA B  1  77  ? -0.255  -8.893  54.776 1.00 30.14  ? 90  ALA B N   1 
ATOM   3221 C  CA  . ALA B  1  77  ? 0.330   -7.563  54.672 1.00 29.97  ? 90  ALA B CA  1 
ATOM   3222 C  C   . ALA B  1  77  ? -0.466  -6.549  55.498 1.00 31.06  ? 90  ALA B C   1 
ATOM   3223 O  O   . ALA B  1  77  ? 0.118   -5.715  56.198 1.00 34.08  ? 90  ALA B O   1 
ATOM   3224 C  CB  . ALA B  1  77  ? 0.419   -7.144  53.225 1.00 30.72  ? 90  ALA B CB  1 
ATOM   3225 N  N   . ILE B  1  78  ? -1.797  -6.634  55.425 1.00 32.09  ? 91  ILE B N   1 
ATOM   3226 C  CA  . ILE B  1  78  ? -2.668  -5.717  56.155 1.00 32.74  ? 91  ILE B CA  1 
ATOM   3227 C  C   . ILE B  1  78  ? -2.488  -5.926  57.660 1.00 28.68  ? 91  ILE B C   1 
ATOM   3228 O  O   . ILE B  1  78  ? -2.330  -4.971  58.404 1.00 31.75  ? 91  ILE B O   1 
ATOM   3229 C  CB  . ILE B  1  78  ? -4.130  -5.866  55.676 1.00 33.19  ? 91  ILE B CB  1 
ATOM   3230 C  CG1 . ILE B  1  78  ? -4.295  -5.326  54.265 1.00 35.04  ? 91  ILE B CG1 1 
ATOM   3231 C  CG2 . ILE B  1  78  ? -5.098  -5.184  56.638 1.00 34.41  ? 91  ILE B CG2 1 
ATOM   3232 C  CD1 . ILE B  1  78  ? -5.609  -5.685  53.591 1.00 36.75  ? 91  ILE B CD1 1 
ATOM   3233 N  N   . VAL B  1  79  ? -2.453  -7.178  58.107 1.00 30.30  ? 92  VAL B N   1 
ATOM   3234 C  CA  . VAL B  1  79  ? -2.298  -7.489  59.518 1.00 31.34  ? 92  VAL B CA  1 
ATOM   3235 C  C   . VAL B  1  79  ? -0.977  -6.946  60.060 1.00 32.52  ? 92  VAL B C   1 
ATOM   3236 O  O   . VAL B  1  79  ? -0.974  -6.305  61.110 1.00 30.93  ? 92  VAL B O   1 
ATOM   3237 C  CB  . VAL B  1  79  ? -2.413  -9.000  59.795 1.00 33.23  ? 92  VAL B CB  1 
ATOM   3238 C  CG1 . VAL B  1  79  ? -1.986  -9.343  61.220 1.00 34.98  ? 92  VAL B CG1 1 
ATOM   3239 C  CG2 . VAL B  1  79  ? -3.819  -9.504  59.524 1.00 34.88  ? 92  VAL B CG2 1 
ATOM   3240 N  N   . ALA B  1  80  ? 0.141   -7.209  59.362 1.00 29.56  ? 93  ALA B N   1 
ATOM   3241 C  CA  . ALA B  1  80  ? 1.446   -6.750  59.809 1.00 30.30  ? 93  ALA B CA  1 
ATOM   3242 C  C   . ALA B  1  80  ? 1.532   -5.226  59.767 1.00 29.49  ? 93  ALA B C   1 
ATOM   3243 O  O   . ALA B  1  80  ? 2.042   -4.611  60.700 1.00 30.81  ? 93  ALA B O   1 
ATOM   3244 C  CB  . ALA B  1  80  ? 2.546   -7.373  58.977 1.00 32.29  ? 93  ALA B CB  1 
ATOM   3245 N  N   . THR B  1  81  ? 1.028   -4.616  58.698 1.00 28.60  ? 94  THR B N   1 
ATOM   3246 C  CA  . THR B  1  81  ? 1.325   -3.211  58.435 1.00 31.93  ? 94  THR B CA  1 
ATOM   3247 C  C   . THR B  1  81  ? 0.564   -2.324  59.419 1.00 32.03  ? 94  THR B C   1 
ATOM   3248 O  O   . THR B  1  81  ? 1.140   -1.400  59.981 1.00 35.71  ? 94  THR B O   1 
ATOM   3249 C  CB  . THR B  1  81  ? 0.969   -2.837  56.993 1.00 31.06  ? 94  THR B CB  1 
ATOM   3250 O  OG1 . THR B  1  81  ? 1.825   -3.557  56.115 1.00 33.86  ? 94  THR B OG1 1 
ATOM   3251 C  CG2 . THR B  1  81  ? 1.140   -1.356  56.725 1.00 32.92  ? 94  THR B CG2 1 
ATOM   3252 N  N   . TYR B  1  82  ? -0.739  -2.572  59.605 1.00 32.38  ? 95  TYR B N   1 
ATOM   3253 C  CA  . TYR B  1  82  ? -1.534  -1.698  60.463 1.00 33.97  ? 95  TYR B CA  1 
ATOM   3254 C  C   . TYR B  1  82  ? -1.240  -1.990  61.936 1.00 35.21  ? 95  TYR B C   1 
ATOM   3255 O  O   . TYR B  1  82  ? -1.374  -1.091  62.765 1.00 38.20  ? 95  TYR B O   1 
ATOM   3256 C  CB  . TYR B  1  82  ? -3.012  -1.752  60.076 1.00 34.17  ? 95  TYR B CB  1 
ATOM   3257 C  CG  . TYR B  1  82  ? -3.281  -1.097  58.731 1.00 32.53  ? 95  TYR B CG  1 
ATOM   3258 C  CD1 . TYR B  1  82  ? -3.324  0.283   58.598 1.00 34.62  ? 95  TYR B CD1 1 
ATOM   3259 C  CD2 . TYR B  1  82  ? -3.453  -1.856  57.587 1.00 35.44  ? 95  TYR B CD2 1 
ATOM   3260 C  CE1 . TYR B  1  82  ? -3.578  0.889   57.374 1.00 33.39  ? 95  TYR B CE1 1 
ATOM   3261 C  CE2 . TYR B  1  82  ? -3.704  -1.267  56.357 1.00 36.76  ? 95  TYR B CE2 1 
ATOM   3262 C  CZ  . TYR B  1  82  ? -3.760  0.110   56.246 1.00 35.07  ? 95  TYR B CZ  1 
ATOM   3263 O  OH  . TYR B  1  82  ? -3.981  0.699   55.033 1.00 42.17  ? 95  TYR B OH  1 
ATOM   3264 N  N   . LEU B  1  83  ? -0.785  -3.205  62.270 1.00 34.15  ? 96  LEU B N   1 
ATOM   3265 C  CA  . LEU B  1  83  ? -0.290  -3.476  63.616 1.00 33.78  ? 96  LEU B CA  1 
ATOM   3266 C  C   . LEU B  1  83  ? 0.898   -2.560  63.888 1.00 38.23  ? 96  LEU B C   1 
ATOM   3267 O  O   . LEU B  1  83  ? 0.956   -1.859  64.908 1.00 32.14  ? 96  LEU B O   1 
ATOM   3268 C  CB  . LEU B  1  83  ? 0.088   -4.948  63.754 1.00 35.86  ? 96  LEU B CB  1 
ATOM   3269 C  CG  . LEU B  1  83  ? 0.824   -5.366  65.034 1.00 38.78  ? 96  LEU B CG  1 
ATOM   3270 C  CD1 . LEU B  1  83  ? 0.025   -5.102  66.302 1.00 39.72  ? 96  LEU B CD1 1 
ATOM   3271 C  CD2 . LEU B  1  83  ? 1.167   -6.848  64.979 1.00 38.94  ? 96  LEU B CD2 1 
ATOM   3272 N  N   . GLY B  1  84  ? 1.854   -2.555  62.949 1.00 33.56  ? 97  GLY B N   1 
ATOM   3273 C  CA  . GLY B  1  84  ? 3.028   -1.725  63.105 1.00 32.35  ? 97  GLY B CA  1 
ATOM   3274 C  C   . GLY B  1  84  ? 2.659   -0.243  63.139 1.00 32.06  ? 97  GLY B C   1 
ATOM   3275 O  O   . GLY B  1  84  ? 3.211   0.509   63.929 1.00 33.40  ? 97  GLY B O   1 
ATOM   3276 N  N   . HIS B  1  85  ? 1.721   0.168   62.283 1.00 31.41  ? 98  HIS B N   1 
ATOM   3277 C  CA  . HIS B  1  85  ? 1.360   1.576   62.180 1.00 35.45  ? 98  HIS B CA  1 
ATOM   3278 C  C   . HIS B  1  85  ? 0.593   2.053   63.429 1.00 36.17  ? 98  HIS B C   1 
ATOM   3279 O  O   . HIS B  1  85  ? 0.906   3.104   63.972 1.00 33.36  ? 98  HIS B O   1 
ATOM   3280 C  CB  . HIS B  1  85  ? 0.541   1.810   60.918 1.00 37.07  ? 98  HIS B CB  1 
ATOM   3281 C  CG  . HIS B  1  85  ? 0.258   3.232   60.647 1.00 37.40  ? 98  HIS B CG  1 
ATOM   3282 N  ND1 . HIS B  1  85  ? 1.262   4.169   60.565 1.00 37.34  ? 98  HIS B ND1 1 
ATOM   3283 C  CD2 . HIS B  1  85  ? -0.904  3.875   60.394 1.00 39.70  ? 98  HIS B CD2 1 
ATOM   3284 C  CE1 . HIS B  1  85  ? 0.724   5.348   60.277 1.00 40.37  ? 98  HIS B CE1 1 
ATOM   3285 N  NE2 . HIS B  1  85  ? -0.593  5.198   60.172 1.00 39.82  ? 98  HIS B NE2 1 
ATOM   3286 N  N   . LEU B  1  86  ? -0.396  1.282   63.900 1.00 36.73  ? 99  LEU B N   1 
ATOM   3287 C  CA  . LEU B  1  86  ? -1.186  1.674   65.068 1.00 36.02  ? 99  LEU B CA  1 
ATOM   3288 C  C   . LEU B  1  86  ? -0.280  1.901   66.277 1.00 35.77  ? 99  LEU B C   1 
ATOM   3289 O  O   . LEU B  1  86  ? -0.419  2.909   66.965 1.00 36.67  ? 99  LEU B O   1 
ATOM   3290 C  CB  . LEU B  1  86  ? -2.246  0.612   65.359 1.00 34.06  ? 99  LEU B CB  1 
ATOM   3291 C  CG  . LEU B  1  86  ? -3.463  0.629   64.430 1.00 33.74  ? 99  LEU B CG  1 
ATOM   3292 C  CD1 . LEU B  1  86  ? -4.247  -0.653  64.497 1.00 34.39  ? 99  LEU B CD1 1 
ATOM   3293 C  CD2 . LEU B  1  86  ? -4.362  1.794   64.791 1.00 37.63  ? 99  LEU B CD2 1 
ATOM   3294 N  N   . LEU B  1  87  ? 0.670   0.985   66.497 1.00 34.83  ? 100 LEU B N   1 
ATOM   3295 C  CA  . LEU B  1  87  ? 1.528   1.018   67.670 1.00 34.38  ? 100 LEU B CA  1 
ATOM   3296 C  C   . LEU B  1  87  ? 2.716   1.959   67.493 1.00 37.54  ? 100 LEU B C   1 
ATOM   3297 O  O   . LEU B  1  87  ? 3.173   2.538   68.486 1.00 35.09  ? 100 LEU B O   1 
ATOM   3298 C  CB  . LEU B  1  87  ? 2.032   -0.391  67.963 1.00 37.03  ? 100 LEU B CB  1 
ATOM   3299 C  CG  . LEU B  1  87  ? 0.980   -1.424  68.362 1.00 35.06  ? 100 LEU B CG  1 
ATOM   3300 C  CD1 . LEU B  1  87  ? 1.628   -2.790  68.502 1.00 40.48  ? 100 LEU B CD1 1 
ATOM   3301 C  CD2 . LEU B  1  87  ? 0.287   -1.080  69.672 1.00 37.97  ? 100 LEU B CD2 1 
ATOM   3302 N  N   . ASN B  1  88  ? 3.244   2.083   66.257 1.00 36.77  ? 101 ASN B N   1 
ATOM   3303 C  CA  . ASN B  1  88  ? 4.561   2.665   66.073 1.00 37.21  ? 101 ASN B CA  1 
ATOM   3304 C  C   . ASN B  1  88  ? 4.605   3.767   65.021 1.00 39.16  ? 101 ASN B C   1 
ATOM   3305 O  O   . ASN B  1  88  ? 5.663   4.359   64.823 1.00 38.10  ? 101 ASN B O   1 
ATOM   3306 C  CB  . ASN B  1  88  ? 5.596   1.627   65.652 1.00 37.11  ? 101 ASN B CB  1 
ATOM   3307 C  CG  . ASN B  1  88  ? 5.771   0.543   66.678 1.00 39.48  ? 101 ASN B CG  1 
ATOM   3308 O  OD1 . ASN B  1  88  ? 5.849   0.839   67.876 1.00 39.44  ? 101 ASN B OD1 1 
ATOM   3309 N  ND2 . ASN B  1  88  ? 5.855   -0.705  66.232 1.00 42.83  ? 101 ASN B ND2 1 
ATOM   3310 N  N   . GLY B  1  89  ? 3.487   4.041   64.341 1.00 35.73  ? 102 GLY B N   1 
ATOM   3311 C  CA  . GLY B  1  89  ? 3.462   5.053   63.305 1.00 37.22  ? 102 GLY B CA  1 
ATOM   3312 C  C   . GLY B  1  89  ? 2.787   6.347   63.761 1.00 39.76  ? 102 GLY B C   1 
ATOM   3313 O  O   . GLY B  1  89  ? 2.216   6.432   64.854 1.00 41.79  ? 102 GLY B O   1 
ATOM   3314 N  N   . ASN B  1  90  ? 2.838   7.333   62.865 1.00 41.98  ? 103 ASN B N   1 
ATOM   3315 C  CA  . ASN B  1  90  ? 2.191   8.615   63.072 1.00 42.79  ? 103 ASN B CA  1 
ATOM   3316 C  C   . ASN B  1  90  ? 0.861   8.594   62.334 1.00 42.32  ? 103 ASN B C   1 
ATOM   3317 O  O   . ASN B  1  90  ? 0.819   8.643   61.100 1.00 39.59  ? 103 ASN B O   1 
ATOM   3318 C  CB  . ASN B  1  90  ? 3.092   9.751   62.609 1.00 42.16  ? 103 ASN B CB  1 
ATOM   3319 C  CG  . ASN B  1  90  ? 2.547   11.098  63.016 1.00 46.61  ? 103 ASN B CG  1 
ATOM   3320 O  OD1 . ASN B  1  90  ? 1.355   11.362  62.836 1.00 44.21  ? 103 ASN B OD1 1 
ATOM   3321 N  ND2 . ASN B  1  90  ? 3.389   11.955  63.566 1.00 42.76  ? 103 ASN B ND2 1 
ATOM   3322 N  N   . LEU B  1  91  ? -0.230  8.540   63.106 1.00 43.70  ? 104 LEU B N   1 
ATOM   3323 C  CA  . LEU B  1  91  ? -1.552  8.330   62.536 1.00 44.59  ? 104 LEU B CA  1 
ATOM   3324 C  C   . LEU B  1  91  ? -2.077  9.591   61.855 1.00 42.22  ? 104 LEU B C   1 
ATOM   3325 O  O   . LEU B  1  91  ? -2.904  9.485   60.952 1.00 45.04  ? 104 LEU B O   1 
ATOM   3326 C  CB  . LEU B  1  91  ? -2.471  7.834   63.645 1.00 47.52  ? 104 LEU B CB  1 
ATOM   3327 C  CG  . LEU B  1  91  ? -2.022  6.518   64.289 1.00 53.90  ? 104 LEU B CG  1 
ATOM   3328 C  CD1 . LEU B  1  91  ? -2.803  6.217   65.534 1.00 64.30  ? 104 LEU B CD1 1 
ATOM   3329 C  CD2 . LEU B  1  91  ? -2.179  5.391   63.279 1.00 58.28  ? 104 LEU B CD2 1 
ATOM   3330 N  N   . VAL B  1  92  ? -1.552  10.760  62.226 1.00 44.99  ? 105 VAL B N   1 
ATOM   3331 C  CA  . VAL B  1  92  ? -1.978  12.021  61.634 1.00 45.83  ? 105 VAL B CA  1 
ATOM   3332 C  C   . VAL B  1  92  ? -1.315  12.234  60.276 1.00 46.27  ? 105 VAL B C   1 
ATOM   3333 O  O   . VAL B  1  92  ? -1.992  12.655  59.346 1.00 45.05  ? 105 VAL B O   1 
ATOM   3334 C  CB  . VAL B  1  92  ? -1.665  13.183  62.599 1.00 47.59  ? 105 VAL B CB  1 
ATOM   3335 C  CG1 . VAL B  1  92  ? -1.869  14.551  61.964 1.00 47.66  ? 105 VAL B CG1 1 
ATOM   3336 C  CG2 . VAL B  1  92  ? -2.476  13.058  63.877 1.00 51.83  ? 105 VAL B CG2 1 
ATOM   3337 N  N   . THR B  1  93  ? 0.000   11.975  60.161 1.00 48.52  ? 106 THR B N   1 
ATOM   3338 C  CA  . THR B  1  93  ? 0.695   12.154  58.889 1.00 47.89  ? 106 THR B CA  1 
ATOM   3339 C  C   . THR B  1  93  ? 0.598   10.892  58.036 1.00 47.02  ? 106 THR B C   1 
ATOM   3340 O  O   . THR B  1  93  ? 0.944   10.943  56.859 1.00 48.27  ? 106 THR B O   1 
ATOM   3341 C  CB  . THR B  1  93  ? 2.157   12.524  59.108 1.00 51.18  ? 106 THR B CB  1 
ATOM   3342 O  OG1 . THR B  1  93  ? 2.724   11.396  59.764 1.00 51.50  ? 106 THR B OG1 1 
ATOM   3343 C  CG2 . THR B  1  93  ? 2.322   13.792  59.927 1.00 50.67  ? 106 THR B CG2 1 
ATOM   3344 N  N   . ASP B  1  94  ? 0.145   9.773   58.626 1.00 41.32  ? 107 ASP B N   1 
ATOM   3345 C  CA  . ASP B  1  94  ? 0.026   8.496   57.934 1.00 40.08  ? 107 ASP B CA  1 
ATOM   3346 C  C   . ASP B  1  94  ? 1.404   7.975   57.498 1.00 37.03  ? 107 ASP B C   1 
ATOM   3347 O  O   . ASP B  1  94  ? 1.525   7.412   56.418 1.00 43.77  ? 107 ASP B O   1 
ATOM   3348 C  CB  . ASP B  1  94  ? -0.947  8.575   56.767 1.00 39.86  ? 107 ASP B CB  1 
ATOM   3349 C  CG  . ASP B  1  94  ? -1.532  7.248   56.294 1.00 40.50  ? 107 ASP B CG  1 
ATOM   3350 O  OD1 . ASP B  1  94  ? -1.890  6.422   57.151 1.00 47.67  ? 107 ASP B OD1 1 
ATOM   3351 O  OD2 . ASP B  1  94  ? -1.649  7.046   55.068 1.00 41.87  ? 107 ASP B OD2 1 
ATOM   3352 N  N   . LEU B  1  95  ? 2.425   8.150   58.334 1.00 39.25  ? 108 LEU B N   1 
ATOM   3353 C  CA  . LEU B  1  95  ? 3.776   7.709   58.014 1.00 43.07  ? 108 LEU B CA  1 
ATOM   3354 C  C   . LEU B  1  95  ? 4.317   6.823   59.136 1.00 40.99  ? 108 LEU B C   1 
ATOM   3355 O  O   . LEU B  1  95  ? 4.106   7.097   60.316 1.00 38.16  ? 108 LEU B O   1 
ATOM   3356 C  CB  . LEU B  1  95  ? 4.698   8.910   57.788 1.00 42.95  ? 108 LEU B CB  1 
ATOM   3357 C  CG  . LEU B  1  95  ? 4.361   9.815   56.602 1.00 44.64  ? 108 LEU B CG  1 
ATOM   3358 C  CD1 . LEU B  1  95  ? 5.204   11.079  56.722 1.00 48.40  ? 108 LEU B CD1 1 
ATOM   3359 C  CD2 . LEU B  1  95  ? 4.617   9.153   55.275 1.00 44.55  ? 108 LEU B CD2 1 
ATOM   3360 N  N   . LEU B  1  96  ? 5.042   5.765   58.737 1.00 39.47  ? 109 LEU B N   1 
ATOM   3361 C  CA  . LEU B  1  96  ? 5.670   4.829   59.655 1.00 35.36  ? 109 LEU B CA  1 
ATOM   3362 C  C   . LEU B  1  96  ? 7.139   4.662   59.282 1.00 34.77  ? 109 LEU B C   1 
ATOM   3363 O  O   . LEU B  1  96  ? 7.465   4.408   58.120 1.00 36.13  ? 109 LEU B O   1 
ATOM   3364 C  CB  . LEU B  1  96  ? 4.926   3.496   59.565 1.00 34.49  ? 109 LEU B CB  1 
ATOM   3365 C  CG  . LEU B  1  96  ? 5.586   2.281   60.228 1.00 33.87  ? 109 LEU B CG  1 
ATOM   3366 C  CD1 . LEU B  1  96  ? 5.707   2.432   61.731 1.00 34.77  ? 109 LEU B CD1 1 
ATOM   3367 C  CD2 . LEU B  1  96  ? 4.796   1.039   59.877 1.00 34.71  ? 109 LEU B CD2 1 
ATOM   3368 N  N   . SER B  1  97  ? 8.003   4.768   60.284 1.00 34.08  ? 110 SER B N   1 
ATOM   3369 C  CA  . SER B  1  97  ? 9.410   4.451   60.158 1.00 36.99  ? 110 SER B CA  1 
ATOM   3370 C  C   . SER B  1  97  ? 9.599   2.941   60.281 1.00 36.76  ? 110 SER B C   1 
ATOM   3371 O  O   . SER B  1  97  ? 9.109   2.337   61.232 1.00 35.17  ? 110 SER B O   1 
ATOM   3372 C  CB  . SER B  1  97  ? 10.213  5.155   61.215 1.00 37.61  ? 110 SER B CB  1 
ATOM   3373 O  OG  . SER B  1  97  ? 11.529  4.621   61.315 1.00 35.33  ? 110 SER B OG  1 
ATOM   3374 N  N   . ILE B  1  98  ? 10.372  2.340   59.360 1.00 33.10  ? 111 ILE B N   1 
ATOM   3375 C  CA  . ILE B  1  98  ? 10.639  0.915   59.427 1.00 31.67  ? 111 ILE B CA  1 
ATOM   3376 C  C   . ILE B  1  98  ? 11.763  0.630   60.418 1.00 31.82  ? 111 ILE B C   1 
ATOM   3377 O  O   . ILE B  1  98  ? 12.145  -0.523  60.600 1.00 35.18  ? 111 ILE B O   1 
ATOM   3378 C  CB  . ILE B  1  98  ? 10.942  0.324   58.042 1.00 31.74  ? 111 ILE B CB  1 
ATOM   3379 C  CG1 . ILE B  1  98  ? 12.289  0.771   57.476 1.00 31.88  ? 111 ILE B CG1 1 
ATOM   3380 C  CG2 . ILE B  1  98  ? 9.795   0.616   57.086 1.00 31.68  ? 111 ILE B CG2 1 
ATOM   3381 C  CD1 . ILE B  1  98  ? 12.665  0.082   56.178 1.00 33.75  ? 111 ILE B CD1 1 
ATOM   3382 N  N   . GLY B  1  99  ? 12.309  1.679   61.034 1.00 31.00  ? 112 GLY B N   1 
ATOM   3383 C  CA  . GLY B  1  99  ? 13.351  1.532   62.042 1.00 30.87  ? 112 GLY B CA  1 
ATOM   3384 C  C   . GLY B  1  99  ? 13.012  2.356   63.283 1.00 37.21  ? 112 GLY B C   1 
ATOM   3385 O  O   . GLY B  1  99  ? 12.006  2.102   63.955 1.00 37.18  ? 112 GLY B O   1 
ATOM   3386 N  N   . GLY B  1  100 ? 13.869  3.339   63.578 1.00 39.13  ? 113 GLY B N   1 
ATOM   3387 C  CA  . GLY B  1  100 ? 13.762  4.125   64.791 1.00 38.24  ? 113 GLY B CA  1 
ATOM   3388 C  C   . GLY B  1  100 ? 13.130  5.491   64.536 1.00 37.17  ? 113 GLY B C   1 
ATOM   3389 O  O   . GLY B  1  100 ? 12.539  5.740   63.485 1.00 36.39  ? 113 GLY B O   1 
ATOM   3390 N  N   . ALA B  1  101 ? 13.284  6.385   65.518 1.00 42.78  ? 114 ALA B N   1 
ATOM   3391 C  CA  . ALA B  1  101 ? 12.639  7.690   65.484 1.00 47.46  ? 114 ALA B CA  1 
ATOM   3392 C  C   . ALA B  1  101 ? 13.294  8.563   64.425 1.00 48.33  ? 114 ALA B C   1 
ATOM   3393 O  O   . ALA B  1  101 ? 14.491  8.482   64.193 1.00 49.25  ? 114 ALA B O   1 
ATOM   3394 C  CB  . ALA B  1  101 ? 12.717  8.351   66.849 1.00 51.78  ? 114 ALA B CB  1 
ATOM   3395 N  N   . THR B  1  102 ? 12.495  9.404   63.779 1.00 49.07  ? 115 THR B N   1 
ATOM   3396 C  CA  . THR B  1  102 ? 12.998  10.253  62.724 1.00 46.59  ? 115 THR B CA  1 
ATOM   3397 C  C   . THR B  1  102 ? 12.038  11.424  62.589 1.00 47.89  ? 115 THR B C   1 
ATOM   3398 O  O   . THR B  1  102 ? 10.835  11.238  62.707 1.00 47.56  ? 115 THR B O   1 
ATOM   3399 C  CB  . THR B  1  102 ? 13.105  9.459   61.422 1.00 46.32  ? 115 THR B CB  1 
ATOM   3400 O  OG1 . THR B  1  102 ? 13.394  10.410  60.400 1.00 41.98  ? 115 THR B OG1 1 
ATOM   3401 C  CG2 . THR B  1  102 ? 11.812  8.756   61.046 1.00 45.36  ? 115 THR B CG2 1 
ATOM   3402 N  N   . PRO B  1  103 ? 12.538  12.642  62.308 1.00 52.22  ? 116 PRO B N   1 
ATOM   3403 C  CA  . PRO B  1  103 ? 11.661  13.776  62.006 1.00 50.94  ? 116 PRO B CA  1 
ATOM   3404 C  C   . PRO B  1  103 ? 10.839  13.552  60.740 1.00 50.77  ? 116 PRO B C   1 
ATOM   3405 O  O   . PRO B  1  103 ? 9.829   14.221  60.532 1.00 52.46  ? 116 PRO B O   1 
ATOM   3406 C  CB  . PRO B  1  103 ? 12.606  15.002  61.863 1.00 56.21  ? 116 PRO B CB  1 
ATOM   3407 C  CG  . PRO B  1  103 ? 14.019  14.438  61.874 1.00 54.22  ? 116 PRO B CG  1 
ATOM   3408 C  CD  . PRO B  1  103 ? 13.973  12.985  62.312 1.00 55.70  ? 116 PRO B CD  1 
ATOM   3409 N  N   . LYS B  1  104 ? 11.266  12.606  59.891 1.00 44.85  ? 117 LYS B N   1 
ATOM   3410 C  CA  . LYS B  1  104 ? 10.580  12.346  58.635 1.00 44.26  ? 117 LYS B CA  1 
ATOM   3411 C  C   . LYS B  1  104 ? 9.146   11.848  58.844 1.00 43.23  ? 117 LYS B C   1 
ATOM   3412 O  O   . LYS B  1  104 ? 8.374   11.879  57.895 1.00 45.74  ? 117 LYS B O   1 
ATOM   3413 C  CB  . LYS B  1  104 ? 11.356  11.328  57.792 1.00 47.94  ? 117 LYS B CB  1 
ATOM   3414 C  CG  . LYS B  1  104 ? 12.651  11.838  57.176 1.00 50.68  ? 117 LYS B CG  1 
ATOM   3415 C  CD  . LYS B  1  104 ? 13.612  10.717  56.790 1.00 54.28  ? 117 LYS B CD  1 
ATOM   3416 C  CE  . LYS B  1  104 ? 14.901  11.225  56.203 1.00 53.50  ? 117 LYS B CE  1 
ATOM   3417 N  NZ  . LYS B  1  104 ? 14.683  11.811  54.881 1.00 52.24  ? 117 LYS B NZ  1 
ATOM   3418 N  N   . THR B  1  105 ? 8.777   11.356  60.036 1.00 45.31  ? 118 THR B N   1 
ATOM   3419 C  CA  . THR B  1  105 ? 7.395   10.922  60.248 1.00 47.11  ? 118 THR B CA  1 
ATOM   3420 C  C   . THR B  1  105 ? 6.507   12.112  60.630 1.00 52.81  ? 118 THR B C   1 
ATOM   3421 O  O   . THR B  1  105 ? 5.291   11.956  60.728 1.00 46.31  ? 118 THR B O   1 
ATOM   3422 C  CB  . THR B  1  105 ? 7.282   9.796   61.275 1.00 42.26  ? 118 THR B CB  1 
ATOM   3423 O  OG1 . THR B  1  105 ? 7.947   10.129  62.486 1.00 40.49  ? 118 THR B OG1 1 
ATOM   3424 C  CG2 . THR B  1  105 ? 7.889   8.512   60.746 1.00 46.08  ? 118 THR B CG2 1 
ATOM   3425 N  N   . GLY B  1  106 ? 7.116   13.286  60.855 1.00 57.00  ? 119 GLY B N   1 
ATOM   3426 C  CA  . GLY B  1  106 ? 6.366   14.513  61.100 1.00 58.99  ? 119 GLY B CA  1 
ATOM   3427 C  C   . GLY B  1  106 ? 6.245   14.840  62.588 1.00 59.32  ? 119 GLY B C   1 
ATOM   3428 O  O   . GLY B  1  106 ? 6.857   14.182  63.429 1.00 50.96  ? 119 GLY B O   1 
ATOM   3429 N  N   . PRO B  1  107 ? 5.455   15.884  62.951 1.00 64.57  ? 120 PRO B N   1 
ATOM   3430 C  CA  . PRO B  1  107 ? 5.296   16.296  64.351 1.00 60.19  ? 120 PRO B CA  1 
ATOM   3431 C  C   . PRO B  1  107 ? 4.874   15.153  65.273 1.00 54.52  ? 120 PRO B C   1 
ATOM   3432 O  O   . PRO B  1  107 ? 3.917   14.450  64.975 1.00 49.73  ? 120 PRO B O   1 
ATOM   3433 C  CB  . PRO B  1  107 ? 4.214   17.392  64.292 1.00 61.29  ? 120 PRO B CB  1 
ATOM   3434 C  CG  . PRO B  1  107 ? 4.266   17.912  62.866 1.00 63.89  ? 120 PRO B CG  1 
ATOM   3435 C  CD  . PRO B  1  107 ? 4.689   16.727  62.017 1.00 61.76  ? 120 PRO B CD  1 
ATOM   3436 N  N   . PRO B  1  108 ? 5.551   14.944  66.420 1.00 52.20  ? 121 PRO B N   1 
ATOM   3437 C  CA  . PRO B  1  108 ? 5.255   13.796  67.277 1.00 55.61  ? 121 PRO B CA  1 
ATOM   3438 C  C   . PRO B  1  108 ? 3.830   13.811  67.825 1.00 65.79  ? 121 PRO B C   1 
ATOM   3439 O  O   . PRO B  1  108 ? 3.241   14.871  68.013 1.00 67.56  ? 121 PRO B O   1 
ATOM   3440 C  CB  . PRO B  1  108 ? 6.312   13.845  68.399 1.00 57.31  ? 121 PRO B CB  1 
ATOM   3441 C  CG  . PRO B  1  108 ? 6.973   15.204  68.278 1.00 58.49  ? 121 PRO B CG  1 
ATOM   3442 C  CD  . PRO B  1  108 ? 6.658   15.781  66.911 1.00 55.48  ? 121 PRO B CD  1 
ATOM   3443 N  N   . PRO B  1  109 ? 3.222   12.628  68.073 1.00 68.37  ? 122 PRO B N   1 
ATOM   3444 C  CA  . PRO B  1  109 ? 1.906   12.558  68.709 1.00 67.15  ? 122 PRO B CA  1 
ATOM   3445 C  C   . PRO B  1  109 ? 2.018   12.908  70.190 1.00 62.64  ? 122 PRO B C   1 
ATOM   3446 O  O   . PRO B  1  109 ? 3.121   12.905  70.731 1.00 54.77  ? 122 PRO B O   1 
ATOM   3447 C  CB  . PRO B  1  109 ? 1.507   11.090  68.502 1.00 64.99  ? 122 PRO B CB  1 
ATOM   3448 C  CG  . PRO B  1  109 ? 2.837   10.337  68.508 1.00 63.65  ? 122 PRO B CG  1 
ATOM   3449 C  CD  . PRO B  1  109 ? 3.792   11.292  67.816 1.00 65.78  ? 122 PRO B CD  1 
ATOM   3450 N  N   . PRO B  1  110 ? 0.893   13.201  70.886 1.00 64.37  ? 123 PRO B N   1 
ATOM   3451 C  CA  . PRO B  1  110 ? 0.913   13.385  72.338 1.00 58.37  ? 123 PRO B CA  1 
ATOM   3452 C  C   . PRO B  1  110 ? 1.372   12.141  73.099 1.00 58.30  ? 123 PRO B C   1 
ATOM   3453 O  O   . PRO B  1  110 ? 0.867   11.035  72.872 1.00 53.35  ? 123 PRO B O   1 
ATOM   3454 C  CB  . PRO B  1  110 ? -0.533  13.775  72.693 1.00 62.73  ? 123 PRO B CB  1 
ATOM   3455 C  CG  . PRO B  1  110 ? -1.368  13.326  71.504 1.00 64.32  ? 123 PRO B CG  1 
ATOM   3456 C  CD  . PRO B  1  110 ? -0.438  13.429  70.300 1.00 63.68  ? 123 PRO B CD  1 
ATOM   3457 N  N   . PRO B  1  111 ? 2.369   12.256  74.012 1.00 57.25  ? 124 PRO B N   1 
ATOM   3458 C  CA  . PRO B  1  111 ? 2.767   11.120  74.850 1.00 58.55  ? 124 PRO B CA  1 
ATOM   3459 C  C   . PRO B  1  111 ? 1.523   10.687  75.615 1.00 57.60  ? 124 PRO B C   1 
ATOM   3460 O  O   . PRO B  1  111 ? 0.666   11.517  75.914 1.00 64.25  ? 124 PRO B O   1 
ATOM   3461 C  CB  . PRO B  1  111 ? 3.885   11.709  75.748 1.00 58.81  ? 124 PRO B CB  1 
ATOM   3462 C  CG  . PRO B  1  111 ? 4.431   12.853  74.912 1.00 63.62  ? 124 PRO B CG  1 
ATOM   3463 C  CD  . PRO B  1  111 ? 3.196   13.456  74.245 1.00 61.84  ? 124 PRO B CD  1 
ATOM   3464 N  N   . PRO B  1  112 ? 1.314   9.395   75.943 1.00 52.81  ? 125 PRO B N   1 
ATOM   3465 C  CA  . PRO B  1  112 ? 2.333   8.341   75.849 1.00 53.25  ? 125 PRO B CA  1 
ATOM   3466 C  C   . PRO B  1  112 ? 2.617   7.701   74.481 1.00 52.82  ? 125 PRO B C   1 
ATOM   3467 O  O   . PRO B  1  112 ? 3.409   6.770   74.379 1.00 54.66  ? 125 PRO B O   1 
ATOM   3468 C  CB  . PRO B  1  112 ? 1.746   7.304   76.857 1.00 53.05  ? 125 PRO B CB  1 
ATOM   3469 C  CG  . PRO B  1  112 ? 0.229   7.475   76.770 1.00 54.76  ? 125 PRO B CG  1 
ATOM   3470 C  CD  . PRO B  1  112 ? 0.000   8.919   76.402 1.00 56.39  ? 125 PRO B CD  1 
ATOM   3471 N  N   . ALA B  1  113 ? 1.940   8.162   73.429 1.00 52.39  ? 126 ALA B N   1 
ATOM   3472 C  CA  . ALA B  1  113 ? 2.201   7.703   72.073 1.00 52.01  ? 126 ALA B CA  1 
ATOM   3473 C  C   . ALA B  1  113 ? 3.529   8.291   71.593 1.00 54.09  ? 126 ALA B C   1 
ATOM   3474 O  O   . ALA B  1  113 ? 3.938   9.335   72.104 1.00 50.05  ? 126 ALA B O   1 
ATOM   3475 C  CB  . ALA B  1  113 ? 1.055   8.095   71.169 1.00 47.35  ? 126 ALA B CB  1 
ATOM   3476 N  N   . HIS B  1  114 ? 4.160   7.651   70.588 1.00 50.35  ? 127 HIS B N   1 
ATOM   3477 C  CA  . HIS B  1  114 ? 5.552   7.936   70.262 1.00 45.18  ? 127 HIS B CA  1 
ATOM   3478 C  C   . HIS B  1  114 ? 5.830   8.007   68.754 1.00 43.71  ? 127 HIS B C   1 
ATOM   3479 O  O   . HIS B  1  114 ? 6.657   8.805   68.326 1.00 43.26  ? 127 HIS B O   1 
ATOM   3480 C  CB  . HIS B  1  114 ? 6.444   6.940   71.010 1.00 45.37  ? 127 HIS B CB  1 
ATOM   3481 C  CG  . HIS B  1  114 ? 6.047   5.514   70.825 1.00 44.94  ? 127 HIS B CG  1 
ATOM   3482 N  ND1 . HIS B  1  114 ? 6.338   4.833   69.665 1.00 46.13  ? 127 HIS B ND1 1 
ATOM   3483 C  CD2 . HIS B  1  114 ? 5.379   4.647   71.596 1.00 47.33  ? 127 HIS B CD2 1 
ATOM   3484 C  CE1 . HIS B  1  114 ? 5.890   3.592   69.751 1.00 42.84  ? 127 HIS B CE1 1 
ATOM   3485 N  NE2 . HIS B  1  114 ? 5.296   3.453   70.912 1.00 42.75  ? 127 HIS B NE2 1 
ATOM   3486 N  N   . ALA B  1  115 ? 5.166   7.189   67.932 1.00 43.65  ? 128 ALA B N   1 
ATOM   3487 C  CA  . ALA B  1  115 ? 5.508   7.068   66.514 1.00 40.53  ? 128 ALA B CA  1 
ATOM   3488 C  C   . ALA B  1  115 ? 7.017   6.816   66.340 1.00 38.16  ? 128 ALA B C   1 
ATOM   3489 O  O   . ALA B  1  115 ? 7.661   7.337   65.429 1.00 38.70  ? 128 ALA B O   1 
ATOM   3490 C  CB  . ALA B  1  115 ? 5.046   8.283   65.757 1.00 42.90  ? 128 ALA B CB  1 
ATOM   3491 N  N   . GLY B  1  116 ? 7.550   5.958   67.209 1.00 36.83  ? 129 GLY B N   1 
ATOM   3492 C  CA  . GLY B  1  116 ? 8.974   5.705   67.323 1.00 42.85  ? 129 GLY B CA  1 
ATOM   3493 C  C   . GLY B  1  116 ? 9.480   4.625   66.358 1.00 41.34  ? 129 GLY B C   1 
ATOM   3494 O  O   . GLY B  1  116 ? 10.665  4.329   66.370 1.00 42.53  ? 129 GLY B O   1 
ATOM   3495 N  N   . GLY B  1  117 ? 8.589   4.013   65.561 1.00 37.76  ? 130 GLY B N   1 
ATOM   3496 C  CA  . GLY B  1  117 ? 9.002   3.120   64.487 1.00 36.94  ? 130 GLY B CA  1 
ATOM   3497 C  C   . GLY B  1  117 ? 9.041   1.665   64.939 1.00 35.88  ? 130 GLY B C   1 
ATOM   3498 O  O   . GLY B  1  117 ? 8.827   1.364   66.109 1.00 34.99  ? 130 GLY B O   1 
ATOM   3499 N  N   . LEU B  1  118 ? 9.330   0.763   63.984 1.00 35.55  ? 131 LEU B N   1 
ATOM   3500 C  CA  . LEU B  1  118 ? 9.340   -0.673  64.223 1.00 32.92  ? 131 LEU B CA  1 
ATOM   3501 C  C   . LEU B  1  118 ? 10.383  -1.103  65.252 1.00 33.24  ? 131 LEU B C   1 
ATOM   3502 O  O   . LEU B  1  118 ? 10.258  -2.199  65.798 1.00 36.91  ? 131 LEU B O   1 
ATOM   3503 C  CB  . LEU B  1  118 ? 9.548   -1.421  62.905 1.00 32.20  ? 131 LEU B CB  1 
ATOM   3504 C  CG  . LEU B  1  118 ? 8.437   -1.250  61.863 1.00 34.82  ? 131 LEU B CG  1 
ATOM   3505 C  CD1 . LEU B  1  118 ? 8.707   -2.122  60.649 1.00 35.36  ? 131 LEU B CD1 1 
ATOM   3506 C  CD2 . LEU B  1  118 ? 7.045   -1.527  62.429 1.00 36.20  ? 131 LEU B CD2 1 
ATOM   3507 N  N   . ASN B  1  119 ? 11.413  -0.283  65.498 1.00 34.44  ? 132 ASN B N   1 
ATOM   3508 C  CA  . ASN B  1  119 ? 12.412  -0.583  66.517 1.00 35.69  ? 132 ASN B CA  1 
ATOM   3509 C  C   . ASN B  1  119 ? 11.821  -0.637  67.929 1.00 37.96  ? 132 ASN B C   1 
ATOM   3510 O  O   . ASN B  1  119 ? 12.429  -1.243  68.811 1.00 34.74  ? 132 ASN B O   1 
ATOM   3511 C  CB  . ASN B  1  119 ? 13.553  0.427   66.531 1.00 36.31  ? 132 ASN B CB  1 
ATOM   3512 C  CG  . ASN B  1  119 ? 14.511  0.273   65.371 1.00 41.24  ? 132 ASN B CG  1 
ATOM   3513 O  OD1 . ASN B  1  119 ? 14.328  -0.581  64.495 1.00 40.33  ? 132 ASN B OD1 1 
ATOM   3514 N  ND2 . ASN B  1  119 ? 15.549  1.098   65.358 1.00 42.57  ? 132 ASN B ND2 1 
ATOM   3515 N  N   . VAL B  1  120 ? 10.660  -0.009  68.174 1.00 37.10  ? 133 VAL B N   1 
ATOM   3516 C  CA  . VAL B  1  120 ? 10.124  0.034   69.534 1.00 38.82  ? 133 VAL B CA  1 
ATOM   3517 C  C   . VAL B  1  120 ? 9.816   -1.372  70.057 1.00 38.40  ? 133 VAL B C   1 
ATOM   3518 O  O   . VAL B  1  120 ? 9.061   -2.134  69.443 1.00 37.31  ? 133 VAL B O   1 
ATOM   3519 C  CB  . VAL B  1  120 ? 8.898   0.962   69.647 1.00 43.88  ? 133 VAL B CB  1 
ATOM   3520 C  CG1 . VAL B  1  120 ? 8.243   0.895   71.030 1.00 44.64  ? 133 VAL B CG1 1 
ATOM   3521 C  CG2 . VAL B  1  120 ? 9.265   2.402   69.308 1.00 43.35  ? 133 VAL B CG2 1 
ATOM   3522 N  N   . HIS B  1  121 ? 10.377  -1.681  71.242 1.00 39.38  ? 134 HIS B N   1 
ATOM   3523 C  CA  . HIS B  1  121 ? 10.338  -3.015  71.828 1.00 38.66  ? 134 HIS B CA  1 
ATOM   3524 C  C   . HIS B  1  121 ? 9.122   -3.197  72.736 1.00 40.14  ? 134 HIS B C   1 
ATOM   3525 O  O   . HIS B  1  121 ? 8.704   -2.260  73.399 1.00 37.54  ? 134 HIS B O   1 
ATOM   3526 C  CB  . HIS B  1  121 ? 11.605  -3.244  72.658 1.00 39.54  ? 134 HIS B CB  1 
ATOM   3527 C  CG  . HIS B  1  121 ? 11.603  -4.504  73.458 1.00 40.36  ? 134 HIS B CG  1 
ATOM   3528 N  ND1 . HIS B  1  121 ? 11.772  -5.740  72.872 1.00 40.13  ? 134 HIS B ND1 1 
ATOM   3529 C  CD2 . HIS B  1  121 ? 11.427  -4.735  74.778 1.00 41.48  ? 134 HIS B CD2 1 
ATOM   3530 C  CE1 . HIS B  1  121 ? 11.727  -6.686  73.809 1.00 44.45  ? 134 HIS B CE1 1 
ATOM   3531 N  NE2 . HIS B  1  121 ? 11.519  -6.095  74.981 1.00 42.31  ? 134 HIS B NE2 1 
ATOM   3532 N  N   . GLY B  1  122 ? 8.575   -4.418  72.786 1.00 42.03  ? 135 GLY B N   1 
ATOM   3533 C  CA  . GLY B  1  122 ? 7.743   -4.834  73.906 1.00 45.04  ? 135 GLY B CA  1 
ATOM   3534 C  C   . GLY B  1  122 ? 6.288   -5.148  73.552 1.00 45.70  ? 135 GLY B C   1 
ATOM   3535 O  O   . GLY B  1  122 ? 5.666   -5.916  74.273 1.00 44.61  ? 135 GLY B O   1 
ATOM   3536 N  N   . THR B  1  123 ? 5.725   -4.545  72.499 1.00 46.00  ? 136 THR B N   1 
ATOM   3537 C  CA  . THR B  1  123 ? 4.345   -4.843  72.116 1.00 45.28  ? 136 THR B CA  1 
ATOM   3538 C  C   . THR B  1  123 ? 4.315   -5.516  70.742 1.00 44.54  ? 136 THR B C   1 
ATOM   3539 O  O   . THR B  1  123 ? 3.574   -6.483  70.568 1.00 40.09  ? 136 THR B O   1 
ATOM   3540 C  CB  . THR B  1  123 ? 3.471   -3.587  72.131 1.00 44.37  ? 136 THR B CB  1 
ATOM   3541 O  OG1 . THR B  1  123 ? 3.757   -2.886  73.329 1.00 45.24  ? 136 THR B OG1 1 
ATOM   3542 C  CG2 . THR B  1  123 ? 1.987   -3.910  72.056 1.00 45.29  ? 136 THR B CG2 1 
ATOM   3543 N  N   . PHE B  1  124 ? 5.131   -5.019  69.785 1.00 42.25  ? 137 PHE B N   1 
ATOM   3544 C  CA  . PHE B  1  124 ? 5.337   -5.691  68.501 1.00 42.52  ? 137 PHE B CA  1 
ATOM   3545 C  C   . PHE B  1  124 ? 6.723   -6.358  68.475 1.00 40.94  ? 137 PHE B C   1 
ATOM   3546 O  O   . PHE B  1  124 ? 6.815   -7.557  68.742 1.00 43.53  ? 137 PHE B O   1 
ATOM   3547 C  CB  . PHE B  1  124 ? 5.068   -4.719  67.348 1.00 38.74  ? 137 PHE B CB  1 
ATOM   3548 C  CG  . PHE B  1  124 ? 4.998   -5.308  65.941 1.00 39.24  ? 137 PHE B CG  1 
ATOM   3549 C  CD1 . PHE B  1  124 ? 5.125   -6.674  65.703 1.00 38.34  ? 137 PHE B CD1 1 
ATOM   3550 C  CD2 . PHE B  1  124 ? 4.779   -4.478  64.840 1.00 39.30  ? 137 PHE B CD2 1 
ATOM   3551 C  CE1 . PHE B  1  124 ? 5.054   -7.185  64.410 1.00 41.33  ? 137 PHE B CE1 1 
ATOM   3552 C  CE2 . PHE B  1  124 ? 4.681   -5.000  63.556 1.00 38.43  ? 137 PHE B CE2 1 
ATOM   3553 C  CZ  . PHE B  1  124 ? 4.824   -6.348  63.340 1.00 39.20  ? 137 PHE B CZ  1 
ATOM   3554 N  N   . GLU B  1  125 ? 7.792   -5.610  68.145 1.00 37.94  ? 138 GLU B N   1 
ATOM   3555 C  CA  . GLU B  1  125 ? 9.148   -6.163  68.141 1.00 39.95  ? 138 GLU B CA  1 
ATOM   3556 C  C   . GLU B  1  125 ? 9.406   -6.905  69.458 1.00 39.82  ? 138 GLU B C   1 
ATOM   3557 O  O   . GLU B  1  125 ? 9.029   -6.430  70.525 1.00 42.56  ? 138 GLU B O   1 
ATOM   3558 C  CB  . GLU B  1  125 ? 10.181  -5.050  67.915 1.00 40.07  ? 138 GLU B CB  1 
ATOM   3559 C  CG  . GLU B  1  125 ? 11.629  -5.515  67.748 1.00 40.75  ? 138 GLU B CG  1 
ATOM   3560 C  CD  . GLU B  1  125 ? 12.310  -6.053  69.004 1.00 39.75  ? 138 GLU B CD  1 
ATOM   3561 O  OE1 . GLU B  1  125 ? 12.079  -5.408  70.058 1.00 43.47  ? 138 GLU B OE1 1 
ATOM   3562 O  OE2 . GLU B  1  125 ? 13.035  -7.081  68.954 1.00 39.98  ? 138 GLU B OE2 1 
ATOM   3563 N  N   . GLY B  1  126 ? 10.058  -8.069  69.382 1.00 39.07  ? 139 GLY B N   1 
ATOM   3564 C  CA  . GLY B  1  126 ? 10.383  -8.854  70.562 1.00 37.48  ? 139 GLY B CA  1 
ATOM   3565 C  C   . GLY B  1  126 ? 11.556  -9.820  70.357 1.00 36.95  ? 139 GLY B C   1 
ATOM   3566 O  O   . GLY B  1  126 ? 12.331  -9.731  69.400 1.00 37.16  ? 139 GLY B O   1 
ATOM   3567 N  N   . ASP B  1  127 ? 11.625  -10.793 71.263 1.00 35.84  ? 140 ASP B N   1 
ATOM   3568 C  CA  . ASP B  1  127 ? 12.842  -11.529 71.556 1.00 37.86  ? 140 ASP B CA  1 
ATOM   3569 C  C   . ASP B  1  127 ? 12.932  -12.823 70.737 1.00 35.30  ? 140 ASP B C   1 
ATOM   3570 O  O   . ASP B  1  127 ? 11.965  -13.275 70.123 1.00 33.89  ? 140 ASP B O   1 
ATOM   3571 C  CB  . ASP B  1  127 ? 12.921  -11.829 73.050 1.00 36.36  ? 140 ASP B CB  1 
ATOM   3572 C  CG  . ASP B  1  127 ? 12.923  -10.628 73.984 1.00 37.08  ? 140 ASP B CG  1 
ATOM   3573 O  OD1 . ASP B  1  127 ? 13.507  -9.580  73.617 1.00 39.93  ? 140 ASP B OD1 1 
ATOM   3574 O  OD2 . ASP B  1  127 ? 12.356  -10.755 75.098 1.00 41.72  ? 140 ASP B OD2 1 
ATOM   3575 N  N   . ALA B  1  128 ? 14.123  -13.426 70.768 1.00 34.90  ? 141 ALA B N   1 
ATOM   3576 C  CA  . ALA B  1  128 ? 14.410  -14.718 70.159 1.00 35.89  ? 141 ALA B CA  1 
ATOM   3577 C  C   . ALA B  1  128 ? 14.286  -14.659 68.632 1.00 35.23  ? 141 ALA B C   1 
ATOM   3578 O  O   . ALA B  1  128 ? 13.856  -15.612 67.985 1.00 34.50  ? 141 ALA B O   1 
ATOM   3579 C  CB  . ALA B  1  128 ? 13.540  -15.799 70.762 1.00 36.67  ? 141 ALA B CB  1 
ATOM   3580 N  N   . GLY B  1  129 ? 14.730  -13.553 68.038 1.00 35.98  ? 142 GLY B N   1 
ATOM   3581 C  CA  . GLY B  1  129 ? 14.809  -13.465 66.588 1.00 35.26  ? 142 GLY B CA  1 
ATOM   3582 C  C   . GLY B  1  129 ? 15.975  -14.290 66.052 1.00 33.86  ? 142 GLY B C   1 
ATOM   3583 O  O   . GLY B  1  129 ? 16.822  -14.747 66.817 1.00 31.48  ? 142 GLY B O   1 
ATOM   3584 N  N   . MET B  1  130 ? 16.021  -14.429 64.724 1.00 29.81  ? 143 MET B N   1 
ATOM   3585 C  CA  . MET B  1  130 ? 16.988  -15.263 64.040 1.00 30.78  ? 143 MET B CA  1 
ATOM   3586 C  C   . MET B  1  130 ? 18.313  -14.531 63.857 1.00 33.74  ? 143 MET B C   1 
ATOM   3587 O  O   . MET B  1  130 ? 19.358  -15.133 64.088 1.00 36.47  ? 143 MET B O   1 
ATOM   3588 C  CB  . MET B  1  130 ? 16.463  -15.685 62.663 1.00 35.00  ? 143 MET B CB  1 
ATOM   3589 C  CG  . MET B  1  130 ? 15.376  -16.755 62.725 1.00 39.23  ? 143 MET B CG  1 
ATOM   3590 S  SD  . MET B  1  130 ? 14.605  -17.103 61.133 1.00 40.54  ? 143 MET B SD  1 
ATOM   3591 C  CE  . MET B  1  130 ? 13.902  -15.499 60.730 1.00 35.92  ? 143 MET B CE  1 
ATOM   3592 N  N   . THR B  1  131 ? 18.272  -13.280 63.371 1.00 32.74  ? 144 THR B N   1 
ATOM   3593 C  CA  . THR B  1  131 ? 19.493  -12.559 63.028 1.00 30.77  ? 144 THR B CA  1 
ATOM   3594 C  C   . THR B  1  131 ? 19.605  -11.243 63.793 1.00 32.67  ? 144 THR B C   1 
ATOM   3595 O  O   . THR B  1  131 ? 20.557  -10.502 63.567 1.00 29.98  ? 144 THR B O   1 
ATOM   3596 C  CB  . THR B  1  131 ? 19.591  -12.308 61.522 1.00 30.84  ? 144 THR B CB  1 
ATOM   3597 O  OG1 . THR B  1  131 ? 18.671  -11.286 61.152 1.00 31.13  ? 144 THR B OG1 1 
ATOM   3598 C  CG2 . THR B  1  131 ? 19.372  -13.573 60.709 1.00 31.76  ? 144 THR B CG2 1 
ATOM   3599 N  N   . ARG B  1  132 ? 18.621  -10.941 64.652 1.00 34.15  ? 145 ARG B N   1 
ATOM   3600 C  CA  . ARG B  1  132 ? 18.662  -9.782  65.531 1.00 33.80  ? 145 ARG B CA  1 
ATOM   3601 C  C   . ARG B  1  132 ? 18.653  -10.252 66.984 1.00 34.57  ? 145 ARG B C   1 
ATOM   3602 O  O   . ARG B  1  132 ? 17.939  -11.200 67.317 1.00 33.13  ? 145 ARG B O   1 
ATOM   3603 C  CB  . ARG B  1  132 ? 17.473  -8.850  65.301 1.00 33.92  ? 145 ARG B CB  1 
ATOM   3604 C  CG  . ARG B  1  132 ? 17.653  -7.791  64.229 1.00 37.07  ? 145 ARG B CG  1 
ATOM   3605 C  CD  . ARG B  1  132 ? 17.816  -8.337  62.803 1.00 36.16  ? 145 ARG B CD  1 
ATOM   3606 N  NE  . ARG B  1  132 ? 18.165  -7.251  61.885 1.00 36.90  ? 145 ARG B NE  1 
ATOM   3607 C  CZ  . ARG B  1  132 ? 18.606  -7.399  60.636 1.00 39.78  ? 145 ARG B CZ  1 
ATOM   3608 N  NH1 . ARG B  1  132 ? 18.775  -8.616  60.109 1.00 34.95  ? 145 ARG B NH1 1 
ATOM   3609 N  NH2 . ARG B  1  132 ? 18.888  -6.313  59.924 1.00 36.29  ? 145 ARG B NH2 1 
ATOM   3610 N  N   . ALA B  1  133 ? 19.420  -9.553  67.836 1.00 34.22  ? 146 ALA B N   1 
ATOM   3611 C  CA  . ALA B  1  133 ? 19.539  -9.882  69.255 1.00 35.41  ? 146 ALA B CA  1 
ATOM   3612 C  C   . ALA B  1  133 ? 18.397  -9.231  70.051 1.00 36.15  ? 146 ALA B C   1 
ATOM   3613 O  O   . ALA B  1  133 ? 17.846  -8.209  69.646 1.00 30.88  ? 146 ALA B O   1 
ATOM   3614 N  N   . ASP B  1  134 ? 18.084  -9.818  71.215 1.00 36.08  ? 147 ASP B N   1 
ATOM   3615 C  CA  . ASP B  1  134 ? 17.069  -9.303  72.121 1.00 37.98  ? 147 ASP B CA  1 
ATOM   3616 C  C   . ASP B  1  134 ? 17.435  -7.888  72.557 1.00 37.33  ? 147 ASP B C   1 
ATOM   3617 O  O   . ASP B  1  134 ? 18.613  -7.569  72.718 1.00 40.48  ? 147 ASP B O   1 
ATOM   3618 C  CB  . ASP B  1  134 ? 16.888  -10.183 73.347 1.00 35.69  ? 147 ASP B CB  1 
ATOM   3619 C  CG  . ASP B  1  134 ? 16.422  -11.605 73.080 1.00 40.29  ? 147 ASP B CG  1 
ATOM   3620 O  OD1 . ASP B  1  134 ? 16.265  -11.958 71.886 1.00 39.40  ? 147 ASP B OD1 1 
ATOM   3621 O  OD2 . ASP B  1  134 ? 16.214  -12.355 74.066 1.00 39.34  ? 147 ASP B OD2 1 
ATOM   3622 N  N   . GLU B  1  135 ? 16.405  -7.056  72.747 1.00 36.10  ? 148 GLU B N   1 
ATOM   3623 C  CA  . GLU B  1  135 ? 16.563  -5.664  73.138 1.00 40.68  ? 148 GLU B CA  1 
ATOM   3624 C  C   . GLU B  1  135 ? 17.367  -5.530  74.437 1.00 40.71  ? 148 GLU B C   1 
ATOM   3625 O  O   . GLU B  1  135 ? 18.063  -4.535  74.613 1.00 41.02  ? 148 GLU B O   1 
ATOM   3626 C  CB  . GLU B  1  135 ? 15.195  -5.008  73.307 1.00 43.67  ? 148 GLU B CB  1 
ATOM   3627 C  CG  . GLU B  1  135 ? 15.260  -3.503  73.576 1.00 47.35  ? 148 GLU B CG  1 
ATOM   3628 C  CD  . GLU B  1  135 ? 15.256  -3.098  75.047 1.00 54.29  ? 148 GLU B CD  1 
ATOM   3629 O  OE1 . GLU B  1  135 ? 15.243  -3.959  75.951 1.00 52.42  ? 148 GLU B OE1 1 
ATOM   3630 O  OE2 . GLU B  1  135 ? 15.251  -1.878  75.293 1.00 62.02  ? 148 GLU B OE2 1 
ATOM   3631 N  N   . PHE B  1  136 ? 17.260  -6.523  75.325 1.00 39.57  ? 149 PHE B N   1 
ATOM   3632 C  CA  . PHE B  1  136 ? 17.963  -6.507  76.599 1.00 46.13  ? 149 PHE B CA  1 
ATOM   3633 C  C   . PHE B  1  136 ? 19.463  -6.289  76.383 1.00 49.05  ? 149 PHE B C   1 
ATOM   3634 O  O   . PHE B  1  136 ? 20.092  -5.605  77.177 1.00 48.71  ? 149 PHE B O   1 
ATOM   3635 C  CB  . PHE B  1  136 ? 17.714  -7.791  77.395 1.00 47.49  ? 149 PHE B CB  1 
ATOM   3636 C  CG  . PHE B  1  136 ? 18.523  -7.859  78.685 1.00 55.06  ? 149 PHE B CG  1 
ATOM   3637 C  CD1 . PHE B  1  136 ? 18.194  -7.050  79.772 1.00 57.88  ? 149 PHE B CD1 1 
ATOM   3638 C  CD2 . PHE B  1  136 ? 19.602  -8.727  78.810 1.00 55.83  ? 149 PHE B CD2 1 
ATOM   3639 C  CE1 . PHE B  1  136 ? 18.931  -7.097  80.946 1.00 57.54  ? 149 PHE B CE1 1 
ATOM   3640 C  CE2 . PHE B  1  136 ? 20.325  -8.790  79.998 1.00 57.61  ? 149 PHE B CE2 1 
ATOM   3641 C  CZ  . PHE B  1  136 ? 19.997  -7.966  81.053 1.00 55.53  ? 149 PHE B CZ  1 
ATOM   3642 N  N   . PHE B  1  137 ? 20.031  -6.841  75.303 1.00 45.93  ? 150 PHE B N   1 
ATOM   3643 C  CA  . PHE B  1  137 ? 21.467  -6.787  75.080 1.00 42.83  ? 150 PHE B CA  1 
ATOM   3644 C  C   . PHE B  1  137 ? 21.895  -5.481  74.422 1.00 40.63  ? 150 PHE B C   1 
ATOM   3645 O  O   . PHE B  1  137 ? 23.082  -5.297  74.187 1.00 44.20  ? 150 PHE B O   1 
ATOM   3646 C  CB  . PHE B  1  137 ? 21.908  -8.010  74.277 1.00 41.35  ? 150 PHE B CB  1 
ATOM   3647 C  CG  . PHE B  1  137 ? 21.508  -9.325  74.937 1.00 43.13  ? 150 PHE B CG  1 
ATOM   3648 C  CD1 . PHE B  1  137 ? 21.991  -9.644  76.199 1.00 46.13  ? 150 PHE B CD1 1 
ATOM   3649 C  CD2 . PHE B  1  137 ? 20.671  -10.242 74.306 1.00 42.49  ? 150 PHE B CD2 1 
ATOM   3650 C  CE1 . PHE B  1  137 ? 21.660  -10.854 76.804 1.00 46.53  ? 150 PHE B CE1 1 
ATOM   3651 C  CE2 . PHE B  1  137 ? 20.312  -11.428 74.933 1.00 44.37  ? 150 PHE B CE2 1 
ATOM   3652 C  CZ  . PHE B  1  137 ? 20.802  -11.736 76.183 1.00 45.90  ? 150 PHE B CZ  1 
ATOM   3653 N  N   . GLY B  1  138 ? 20.951  -4.594  74.079 1.00 39.81  ? 151 GLY B N   1 
ATOM   3654 C  CA  . GLY B  1  138 ? 21.299  -3.226  73.715 1.00 40.04  ? 151 GLY B CA  1 
ATOM   3655 C  C   . GLY B  1  138 ? 20.983  -2.834  72.267 1.00 42.25  ? 151 GLY B C   1 
ATOM   3656 O  O   . GLY B  1  138 ? 21.064  -1.655  71.925 1.00 43.21  ? 151 GLY B O   1 
ATOM   3657 N  N   . ASP B  1  139 ? 20.664  -3.796  71.395 1.00 40.14  ? 152 ASP B N   1 
ATOM   3658 C  CA  . ASP B  1  139 ? 20.468  -3.495  69.981 1.00 42.40  ? 152 ASP B CA  1 
ATOM   3659 C  C   . ASP B  1  139 ? 19.543  -4.540  69.361 1.00 36.79  ? 152 ASP B C   1 
ATOM   3660 O  O   . ASP B  1  139 ? 19.970  -5.648  69.052 1.00 38.24  ? 152 ASP B O   1 
ATOM   3661 C  CB  . ASP B  1  139 ? 21.787  -3.402  69.213 1.00 41.93  ? 152 ASP B CB  1 
ATOM   3662 C  CG  . ASP B  1  139 ? 21.654  -3.098  67.726 1.00 45.14  ? 152 ASP B CG  1 
ATOM   3663 O  OD1 . ASP B  1  139 ? 20.520  -3.145  67.204 1.00 43.43  ? 152 ASP B OD1 1 
ATOM   3664 O  OD2 . ASP B  1  139 ? 22.671  -2.769  67.090 1.00 47.35  ? 152 ASP B OD2 1 
ATOM   3665 N  N   . ASN B  1  140 ? 18.289  -4.146  69.128 1.00 33.82  ? 153 ASN B N   1 
ATOM   3666 C  CA  . ASN B  1  140 ? 17.263  -5.071  68.693 1.00 36.86  ? 153 ASN B CA  1 
ATOM   3667 C  C   . ASN B  1  140 ? 17.062  -4.995  67.181 1.00 36.84  ? 153 ASN B C   1 
ATOM   3668 O  O   . ASN B  1  140 ? 16.150  -5.649  66.673 1.00 36.18  ? 153 ASN B O   1 
ATOM   3669 C  CB  . ASN B  1  140 ? 15.940  -4.838  69.416 1.00 35.42  ? 153 ASN B CB  1 
ATOM   3670 C  CG  . ASN B  1  140 ? 15.302  -3.506  69.084 1.00 40.01  ? 153 ASN B CG  1 
ATOM   3671 O  OD1 . ASN B  1  140 ? 15.927  -2.632  68.473 1.00 38.21  ? 153 ASN B OD1 1 
ATOM   3672 N  ND2 . ASN B  1  140 ? 14.066  -3.311  69.516 1.00 41.36  ? 153 ASN B ND2 1 
ATOM   3673 N  N   . HIS B  1  141 ? 17.883  -4.202  66.476 1.00 35.08  ? 154 HIS B N   1 
ATOM   3674 C  CA  . HIS B  1  141 ? 17.585  -3.863  65.087 1.00 35.97  ? 154 HIS B CA  1 
ATOM   3675 C  C   . HIS B  1  141 ? 18.702  -4.279  64.117 1.00 34.23  ? 154 HIS B C   1 
ATOM   3676 O  O   . HIS B  1  141 ? 18.430  -4.627  62.959 1.00 34.97  ? 154 HIS B O   1 
ATOM   3677 C  CB  . HIS B  1  141 ? 17.160  -2.391  64.982 1.00 38.12  ? 154 HIS B CB  1 
ATOM   3678 C  CG  . HIS B  1  141 ? 18.151  -1.437  65.540 1.00 44.69  ? 154 HIS B CG  1 
ATOM   3679 N  ND1 . HIS B  1  141 ? 19.185  -0.951  64.769 1.00 50.40  ? 154 HIS B ND1 1 
ATOM   3680 C  CD2 . HIS B  1  141 ? 18.304  -0.899  66.756 1.00 45.03  ? 154 HIS B CD2 1 
ATOM   3681 C  CE1 . HIS B  1  141 ? 19.932  -0.139  65.505 1.00 50.02  ? 154 HIS B CE1 1 
ATOM   3682 N  NE2 . HIS B  1  141 ? 19.413  -0.092  66.712 1.00 47.71  ? 154 HIS B NE2 1 
ATOM   3683 N  N   . SER B  1  142 ? 19.960  -4.184  64.543 1.00 34.55  ? 155 SER B N   1 
ATOM   3684 C  CA  . SER B  1  142 ? 21.091  -4.467  63.673 1.00 36.57  ? 155 SER B CA  1 
ATOM   3685 C  C   . SER B  1  142 ? 21.204  -5.963  63.402 1.00 32.69  ? 155 SER B C   1 
ATOM   3686 O  O   . SER B  1  142 ? 20.937  -6.783  64.272 1.00 29.67  ? 155 SER B O   1 
ATOM   3687 C  CB  . SER B  1  142 ? 22.382  -3.967  64.261 1.00 39.45  ? 155 SER B CB  1 
ATOM   3688 O  OG  . SER B  1  142 ? 22.326  -2.562  64.440 1.00 46.40  ? 155 SER B OG  1 
ATOM   3689 N  N   . PHE B  1  143 ? 21.680  -6.293  62.202 1.00 33.27  ? 156 PHE B N   1 
ATOM   3690 C  CA  . PHE B  1  143 ? 22.125  -7.645  61.909 1.00 33.83  ? 156 PHE B CA  1 
ATOM   3691 C  C   . PHE B  1  143 ? 23.224  -8.037  62.895 1.00 33.49  ? 156 PHE B C   1 
ATOM   3692 O  O   . PHE B  1  143 ? 24.100  -7.238  63.198 1.00 32.06  ? 156 PHE B O   1 
ATOM   3693 C  CB  . PHE B  1  143 ? 22.639  -7.708  60.474 1.00 33.09  ? 156 PHE B CB  1 
ATOM   3694 C  CG  . PHE B  1  143 ? 23.243  -9.049  60.082 1.00 32.44  ? 156 PHE B CG  1 
ATOM   3695 C  CD1 . PHE B  1  143 ? 22.450  -10.079 59.603 1.00 31.01  ? 156 PHE B CD1 1 
ATOM   3696 C  CD2 . PHE B  1  143 ? 24.610  -9.261  60.185 1.00 33.64  ? 156 PHE B CD2 1 
ATOM   3697 C  CE1 . PHE B  1  143 ? 23.010  -11.295 59.238 1.00 30.66  ? 156 PHE B CE1 1 
ATOM   3698 C  CE2 . PHE B  1  143 ? 25.167  -10.474 59.816 1.00 31.19  ? 156 PHE B CE2 1 
ATOM   3699 C  CZ  . PHE B  1  143 ? 24.370  -11.485 59.340 1.00 31.16  ? 156 PHE B CZ  1 
ATOM   3700 N  N   . ASN B  1  144 ? 23.164  -9.282  63.375 1.00 33.68  ? 157 ASN B N   1 
ATOM   3701 C  CA  . ASN B  1  144 ? 24.105  -9.811  64.335 1.00 32.67  ? 157 ASN B CA  1 
ATOM   3702 C  C   . ASN B  1  144 ? 24.746  -11.067 63.752 1.00 34.27  ? 157 ASN B C   1 
ATOM   3703 O  O   . ASN B  1  144 ? 24.092  -12.101 63.593 1.00 27.47  ? 157 ASN B O   1 
ATOM   3704 C  CB  . ASN B  1  144 ? 23.372  -10.079 65.635 1.00 35.58  ? 157 ASN B CB  1 
ATOM   3705 C  CG  . ASN B  1  144 ? 24.200  -10.709 66.726 1.00 38.80  ? 157 ASN B CG  1 
ATOM   3706 O  OD1 . ASN B  1  144 ? 24.861  -11.724 66.491 1.00 35.06  ? 157 ASN B OD1 1 
ATOM   3707 N  ND2 . ASN B  1  144 ? 24.114  -10.137 67.923 1.00 47.05  ? 157 ASN B ND2 1 
ATOM   3708 N  N   . GLN B  1  145 ? 26.056  -10.977 63.495 1.00 32.23  ? 158 GLN B N   1 
ATOM   3709 C  CA  . GLN B  1  145 ? 26.799  -12.003 62.782 1.00 30.24  ? 158 GLN B CA  1 
ATOM   3710 C  C   . GLN B  1  145 ? 26.851  -13.293 63.595 1.00 29.68  ? 158 GLN B C   1 
ATOM   3711 O  O   . GLN B  1  145 ? 26.811  -14.376 63.023 1.00 30.64  ? 158 GLN B O   1 
ATOM   3712 C  CB  . GLN B  1  145 ? 28.207  -11.515 62.419 1.00 33.82  ? 158 GLN B CB  1 
ATOM   3713 C  CG  . GLN B  1  145 ? 29.028  -12.482 61.563 1.00 32.26  ? 158 GLN B CG  1 
ATOM   3714 C  CD  . GLN B  1  145 ? 28.420  -12.798 60.211 1.00 35.44  ? 158 GLN B CD  1 
ATOM   3715 O  OE1 . GLN B  1  145 ? 28.069  -11.914 59.420 1.00 33.57  ? 158 GLN B OE1 1 
ATOM   3716 N  NE2 . GLN B  1  145 ? 28.342  -14.083 59.890 1.00 37.53  ? 158 GLN B NE2 1 
ATOM   3717 N  N   . THR B  1  146 ? 26.970  -13.189 64.920 1.00 30.73  ? 159 THR B N   1 
ATOM   3718 C  CA  . THR B  1  146 ? 27.020  -14.369 65.782 1.00 33.24  ? 159 THR B CA  1 
ATOM   3719 C  C   . THR B  1  146 ? 25.727  -15.171 65.626 1.00 31.58  ? 159 THR B C   1 
ATOM   3720 O  O   . THR B  1  146 ? 25.760  -16.389 65.528 1.00 30.17  ? 159 THR B O   1 
ATOM   3721 C  CB  . THR B  1  146 ? 27.217  -13.967 67.247 1.00 38.21  ? 159 THR B CB  1 
ATOM   3722 O  OG1 . THR B  1  146 ? 28.428  -13.227 67.286 1.00 37.44  ? 159 THR B OG1 1 
ATOM   3723 C  CG2 . THR B  1  146 ? 27.361  -15.161 68.180 1.00 39.30  ? 159 THR B CG2 1 
ATOM   3724 N  N   . LEU B  1  147 ? 24.584  -14.482 65.586 1.00 29.97  ? 160 LEU B N   1 
ATOM   3725 C  CA  . LEU B  1  147 ? 23.320  -15.174 65.407 1.00 31.48  ? 160 LEU B CA  1 
ATOM   3726 C  C   . LEU B  1  147 ? 23.207  -15.762 64.002 1.00 30.86  ? 160 LEU B C   1 
ATOM   3727 O  O   . LEU B  1  147 ? 22.656  -16.840 63.805 1.00 28.39  ? 160 LEU B O   1 
ATOM   3728 C  CB  . LEU B  1  147 ? 22.182  -14.211 65.720 1.00 31.68  ? 160 LEU B CB  1 
ATOM   3729 C  CG  . LEU B  1  147 ? 21.986  -13.857 67.193 1.00 36.23  ? 160 LEU B CG  1 
ATOM   3730 C  CD1 . LEU B  1  147 ? 20.823  -12.869 67.347 1.00 36.69  ? 160 LEU B CD1 1 
ATOM   3731 C  CD2 . LEU B  1  147 ? 21.749  -15.120 68.005 1.00 35.95  ? 160 LEU B CD2 1 
ATOM   3732 N  N   . PHE B  1  148 ? 23.739  -15.051 63.009 1.00 31.22  ? 161 PHE B N   1 
ATOM   3733 C  CA  . PHE B  1  148 ? 23.710  -15.565 61.654 1.00 28.85  ? 161 PHE B CA  1 
ATOM   3734 C  C   . PHE B  1  148 ? 24.575  -16.819 61.568 1.00 30.94  ? 161 PHE B C   1 
ATOM   3735 O  O   . PHE B  1  148 ? 24.225  -17.754 60.838 1.00 28.98  ? 161 PHE B O   1 
ATOM   3736 C  CB  . PHE B  1  148 ? 24.121  -14.512 60.627 1.00 30.38  ? 161 PHE B CB  1 
ATOM   3737 C  CG  . PHE B  1  148 ? 23.972  -15.015 59.204 1.00 29.82  ? 161 PHE B CG  1 
ATOM   3738 C  CD1 . PHE B  1  148 ? 22.714  -15.126 58.631 1.00 30.74  ? 161 PHE B CD1 1 
ATOM   3739 C  CD2 . PHE B  1  148 ? 25.071  -15.437 58.474 1.00 30.74  ? 161 PHE B CD2 1 
ATOM   3740 C  CE1 . PHE B  1  148 ? 22.566  -15.606 57.340 1.00 32.67  ? 161 PHE B CE1 1 
ATOM   3741 C  CE2 . PHE B  1  148 ? 24.923  -15.906 57.171 1.00 32.18  ? 161 PHE B CE2 1 
ATOM   3742 C  CZ  . PHE B  1  148 ? 23.674  -15.986 56.606 1.00 29.88  ? 161 PHE B CZ  1 
ATOM   3743 N  N   . ASP B  1  149 ? 25.683  -16.849 62.328 1.00 30.96  ? 162 ASP B N   1 
ATOM   3744 C  CA  . ASP B  1  149 ? 26.547  -18.022 62.367 1.00 32.73  ? 162 ASP B CA  1 
ATOM   3745 C  C   . ASP B  1  149 ? 25.778  -19.240 62.899 1.00 30.59  ? 162 ASP B C   1 
ATOM   3746 O  O   . ASP B  1  149 ? 26.008  -20.365 62.459 1.00 30.34  ? 162 ASP B O   1 
ATOM   3747 C  CB  . ASP B  1  149 ? 27.801  -17.746 63.182 1.00 33.85  ? 162 ASP B CB  1 
ATOM   3748 C  CG  . ASP B  1  149 ? 28.799  -16.768 62.555 1.00 41.10  ? 162 ASP B CG  1 
ATOM   3749 O  OD1 . ASP B  1  149 ? 28.743  -16.565 61.324 1.00 42.51  ? 162 ASP B OD1 1 
ATOM   3750 O  OD2 . ASP B  1  149 ? 29.612  -16.194 63.309 1.00 42.37  ? 162 ASP B OD2 1 
ATOM   3751 N  N   . LYS B  1  150 ? 24.885  -19.025 63.874 1.00 29.48  ? 163 LYS B N   1 
ATOM   3752 C  CA  . LYS B  1  150 ? 24.042  -20.094 64.404 1.00 30.19  ? 163 LYS B CA  1 
ATOM   3753 C  C   . LYS B  1  150 ? 23.033  -20.559 63.348 1.00 31.68  ? 163 LYS B C   1 
ATOM   3754 O  O   . LYS B  1  150 ? 22.796  -21.755 63.193 1.00 33.44  ? 163 LYS B O   1 
ATOM   3755 C  CB  . LYS B  1  150 ? 23.323  -19.622 65.673 1.00 34.95  ? 163 LYS B CB  1 
ATOM   3756 C  CG  . LYS B  1  150 ? 22.459  -20.666 66.367 1.00 38.24  ? 163 LYS B CG  1 
ATOM   3757 C  CD  . LYS B  1  150 ? 21.758  -20.095 67.587 1.00 44.24  ? 163 LYS B CD  1 
ATOM   3758 C  CE  . LYS B  1  150 ? 20.873  -21.073 68.300 1.00 45.83  ? 163 LYS B CE  1 
ATOM   3759 N  NZ  . LYS B  1  150 ? 21.485  -21.450 69.571 1.00 48.16  ? 163 LYS B NZ  1 
ATOM   3760 N  N   . PHE B  1  151 ? 22.455  -19.609 62.600 1.00 31.33  ? 164 PHE B N   1 
ATOM   3761 C  CA  . PHE B  1  151 ? 21.571  -19.935 61.486 1.00 29.73  ? 164 PHE B CA  1 
ATOM   3762 C  C   . PHE B  1  151 ? 22.276  -20.864 60.497 1.00 30.08  ? 164 PHE B C   1 
ATOM   3763 O  O   . PHE B  1  151 ? 21.707  -21.849 60.034 1.00 29.29  ? 164 PHE B O   1 
ATOM   3764 C  CB  . PHE B  1  151 ? 21.134  -18.594 60.889 1.00 29.62  ? 164 PHE B CB  1 
ATOM   3765 C  CG  . PHE B  1  151 ? 20.217  -18.649 59.674 1.00 30.57  ? 164 PHE B CG  1 
ATOM   3766 C  CD1 . PHE B  1  151 ? 20.727  -18.776 58.393 1.00 29.96  ? 164 PHE B CD1 1 
ATOM   3767 C  CD2 . PHE B  1  151 ? 18.842  -18.479 59.819 1.00 32.79  ? 164 PHE B CD2 1 
ATOM   3768 C  CE1 . PHE B  1  151 ? 19.879  -18.759 57.289 1.00 30.57  ? 164 PHE B CE1 1 
ATOM   3769 C  CE2 . PHE B  1  151 ? 17.991  -18.496 58.721 1.00 30.15  ? 164 PHE B CE2 1 
ATOM   3770 C  CZ  . PHE B  1  151 ? 18.511  -18.646 57.456 1.00 30.34  ? 164 PHE B CZ  1 
ATOM   3771 N  N   . VAL B  1  152 ? 23.525  -20.533 60.156 1.00 28.17  ? 165 VAL B N   1 
ATOM   3772 C  CA  . VAL B  1  152 ? 24.329  -21.346 59.256 1.00 29.28  ? 165 VAL B CA  1 
ATOM   3773 C  C   . VAL B  1  152 ? 24.592  -22.713 59.899 1.00 30.10  ? 165 VAL B C   1 
ATOM   3774 O  O   . VAL B  1  152 ? 24.469  -23.742 59.240 1.00 29.23  ? 165 VAL B O   1 
ATOM   3775 C  CB  . VAL B  1  152 ? 25.652  -20.643 58.890 1.00 30.17  ? 165 VAL B CB  1 
ATOM   3776 C  CG1 . VAL B  1  152 ? 26.608  -21.582 58.149 1.00 30.26  ? 165 VAL B CG1 1 
ATOM   3777 C  CG2 . VAL B  1  152 ? 25.418  -19.364 58.084 1.00 31.10  ? 165 VAL B CG2 1 
ATOM   3778 N  N   . ASP B  1  153 ? 24.981  -22.718 61.175 1.00 30.48  ? 166 ASP B N   1 
ATOM   3779 C  CA  . ASP B  1  153 ? 25.263  -23.970 61.872 1.00 33.26  ? 166 ASP B CA  1 
ATOM   3780 C  C   . ASP B  1  153 ? 24.033  -24.890 61.841 1.00 35.73  ? 166 ASP B C   1 
ATOM   3781 O  O   . ASP B  1  153 ? 24.133  -26.077 61.520 1.00 30.82  ? 166 ASP B O   1 
ATOM   3782 C  CB  . ASP B  1  153 ? 25.780  -23.705 63.278 1.00 33.83  ? 166 ASP B CB  1 
ATOM   3783 C  CG  . ASP B  1  153 ? 26.173  -24.941 64.080 1.00 38.89  ? 166 ASP B CG  1 
ATOM   3784 O  OD1 . ASP B  1  153 ? 26.967  -25.772 63.543 1.00 39.67  ? 166 ASP B OD1 1 
ATOM   3785 O  OD2 . ASP B  1  153 ? 25.649  -25.071 65.218 1.00 39.64  ? 166 ASP B OD2 1 
ATOM   3786 N  N   . PHE B  1  154 ? 22.858  -24.343 62.168 1.00 33.07  ? 167 PHE B N   1 
ATOM   3787 C  CA  . PHE B  1  154 ? 21.643  -25.146 62.172 1.00 31.87  ? 167 PHE B CA  1 
ATOM   3788 C  C   . PHE B  1  154 ? 21.293  -25.607 60.769 1.00 30.30  ? 167 PHE B C   1 
ATOM   3789 O  O   . PHE B  1  154 ? 20.779  -26.709 60.599 1.00 32.09  ? 167 PHE B O   1 
ATOM   3790 C  CB  . PHE B  1  154 ? 20.496  -24.388 62.851 1.00 32.14  ? 167 PHE B CB  1 
ATOM   3791 C  CG  . PHE B  1  154 ? 20.503  -24.617 64.351 1.00 34.27  ? 167 PHE B CG  1 
ATOM   3792 C  CD1 . PHE B  1  154 ? 21.584  -24.204 65.133 1.00 38.67  ? 167 PHE B CD1 1 
ATOM   3793 C  CD2 . PHE B  1  154 ? 19.437  -25.252 64.974 1.00 37.89  ? 167 PHE B CD2 1 
ATOM   3794 C  CE1 . PHE B  1  154 ? 21.588  -24.410 66.507 1.00 37.63  ? 167 PHE B CE1 1 
ATOM   3795 C  CE2 . PHE B  1  154 ? 19.444  -25.454 66.341 1.00 37.63  ? 167 PHE B CE2 1 
ATOM   3796 C  CZ  . PHE B  1  154 ? 20.513  -25.030 67.105 1.00 37.23  ? 167 PHE B CZ  1 
ATOM   3797 N  N   . SER B  1  155 ? 21.549  -24.764 59.765 1.00 31.10  ? 168 SER B N   1 
ATOM   3798 C  CA  . SER B  1  155 ? 21.325  -25.155 58.379 1.00 30.23  ? 168 SER B CA  1 
ATOM   3799 C  C   . SER B  1  155 ? 22.247  -26.319 57.999 1.00 32.91  ? 168 SER B C   1 
ATOM   3800 O  O   . SER B  1  155 ? 21.843  -27.222 57.263 1.00 31.52  ? 168 SER B O   1 
ATOM   3801 C  CB  . SER B  1  155 ? 21.478  -23.968 57.440 1.00 33.72  ? 168 SER B CB  1 
ATOM   3802 O  OG  . SER B  1  155 ? 20.549  -22.934 57.764 1.00 32.03  ? 168 SER B OG  1 
ATOM   3803 N  N   . ASN B  1  156 ? 23.505  -26.294 58.470 1.00 28.70  ? 169 ASN B N   1 
ATOM   3804 C  CA  . ASN B  1  156 ? 24.426  -27.393 58.188 1.00 31.55  ? 169 ASN B CA  1 
ATOM   3805 C  C   . ASN B  1  156 ? 23.952  -28.675 58.890 1.00 28.39  ? 169 ASN B C   1 
ATOM   3806 O  O   . ASN B  1  156 ? 24.028  -29.757 58.323 1.00 32.82  ? 169 ASN B O   1 
ATOM   3807 C  CB  . ASN B  1  156 ? 25.838  -27.100 58.682 1.00 32.25  ? 169 ASN B CB  1 
ATOM   3808 C  CG  . ASN B  1  156 ? 26.543  -26.016 57.920 1.00 31.59  ? 169 ASN B CG  1 
ATOM   3809 O  OD1 . ASN B  1  156 ? 26.232  -25.732 56.757 1.00 33.22  ? 169 ASN B OD1 1 
ATOM   3810 N  ND2 . ASN B  1  156 ? 27.528  -25.432 58.581 1.00 36.67  ? 169 ASN B ND2 1 
ATOM   3811 N  N   . ARG B  1  157 ? 23.482  -28.548 60.133 1.00 31.06  ? 170 ARG B N   1 
ATOM   3812 C  CA  . ARG B  1  157 ? 23.168  -29.694 60.967 1.00 33.59  ? 170 ARG B CA  1 
ATOM   3813 C  C   . ARG B  1  157 ? 21.863  -30.365 60.540 1.00 38.18  ? 170 ARG B C   1 
ATOM   3814 O  O   . ARG B  1  157 ? 21.741  -31.580 60.682 1.00 36.57  ? 170 ARG B O   1 
ATOM   3815 C  CB  . ARG B  1  157 ? 23.100  -29.278 62.433 1.00 35.06  ? 170 ARG B CB  1 
ATOM   3816 C  CG  . ARG B  1  157 ? 24.484  -29.044 63.009 1.00 38.77  ? 170 ARG B CG  1 
ATOM   3817 C  CD  . ARG B  1  157 ? 24.491  -28.237 64.294 1.00 41.50  ? 170 ARG B CD  1 
ATOM   3818 N  NE  . ARG B  1  157 ? 23.550  -28.748 65.291 1.00 42.74  ? 170 ARG B NE  1 
ATOM   3819 C  CZ  . ARG B  1  157 ? 23.335  -28.165 66.457 1.00 43.93  ? 170 ARG B CZ  1 
ATOM   3820 N  NH1 . ARG B  1  157 ? 22.491  -28.711 67.308 1.00 46.98  ? 170 ARG B NH1 1 
ATOM   3821 N  NH2 . ARG B  1  157 ? 23.974  -27.049 66.793 1.00 43.08  ? 170 ARG B NH2 1 
ATOM   3822 N  N   . TYR B  1  158 ? 20.892  -29.593 60.031 1.00 39.52  ? 171 TYR B N   1 
ATOM   3823 C  CA  . TYR B  1  158 ? 19.548  -30.127 59.827 1.00 37.18  ? 171 TYR B CA  1 
ATOM   3824 C  C   . TYR B  1  158 ? 19.025  -29.940 58.410 1.00 36.85  ? 171 TYR B C   1 
ATOM   3825 O  O   . TYR B  1  158 ? 18.008  -30.547 58.076 1.00 39.94  ? 171 TYR B O   1 
ATOM   3826 C  CB  . TYR B  1  158 ? 18.559  -29.498 60.804 1.00 37.11  ? 171 TYR B CB  1 
ATOM   3827 C  CG  . TYR B  1  158 ? 18.926  -29.747 62.254 1.00 38.69  ? 171 TYR B CG  1 
ATOM   3828 C  CD1 . TYR B  1  158 ? 18.819  -31.018 62.825 1.00 44.17  ? 171 TYR B CD1 1 
ATOM   3829 C  CD2 . TYR B  1  158 ? 19.372  -28.710 63.056 1.00 36.92  ? 171 TYR B CD2 1 
ATOM   3830 C  CE1 . TYR B  1  158 ? 19.164  -31.245 64.149 1.00 44.06  ? 171 TYR B CE1 1 
ATOM   3831 C  CE2 . TYR B  1  158 ? 19.709  -28.923 64.380 1.00 40.15  ? 171 TYR B CE2 1 
ATOM   3832 C  CZ  . TYR B  1  158 ? 19.612  -30.190 64.929 1.00 42.96  ? 171 TYR B CZ  1 
ATOM   3833 O  OH  . TYR B  1  158 ? 19.986  -30.329 66.232 1.00 43.95  ? 171 TYR B OH  1 
ATOM   3834 N  N   . GLY B  1  159 ? 19.697  -29.129 57.573 1.00 34.74  ? 172 GLY B N   1 
ATOM   3835 C  CA  . GLY B  1  159 ? 19.166  -28.833 56.255 1.00 30.93  ? 172 GLY B CA  1 
ATOM   3836 C  C   . GLY B  1  159 ? 20.160  -29.046 55.116 1.00 31.79  ? 172 GLY B C   1 
ATOM   3837 O  O   . GLY B  1  159 ? 19.957  -28.518 54.011 1.00 31.58  ? 172 GLY B O   1 
ATOM   3838 N  N   . GLY B  1  160 ? 21.227  -29.817 55.364 1.00 32.69  ? 173 GLY B N   1 
ATOM   3839 C  CA  . GLY B  1  160 ? 22.186  -30.121 54.312 1.00 32.08  ? 173 GLY B CA  1 
ATOM   3840 C  C   . GLY B  1  160 ? 22.929  -28.875 53.831 1.00 32.75  ? 173 GLY B C   1 
ATOM   3841 O  O   . GLY B  1  160 ? 23.420  -28.852 52.704 1.00 35.27  ? 173 GLY B O   1 
ATOM   3842 N  N   . GLY B  1  161 ? 23.027  -27.857 54.702 1.00 31.54  ? 174 GLY B N   1 
ATOM   3843 C  CA  . GLY B  1  161 ? 23.699  -26.605 54.373 1.00 34.03  ? 174 GLY B CA  1 
ATOM   3844 C  C   . GLY B  1  161 ? 22.732  -25.516 53.877 1.00 34.58  ? 174 GLY B C   1 
ATOM   3845 O  O   . GLY B  1  161 ? 23.140  -24.404 53.554 1.00 33.51  ? 174 GLY B O   1 
ATOM   3846 N  N   . PHE B  1  162 ? 21.434  -25.833 53.865 1.00 35.45  ? 175 PHE B N   1 
ATOM   3847 C  CA  . PHE B  1  162 ? 20.390  -24.915 53.435 1.00 32.71  ? 175 PHE B CA  1 
ATOM   3848 C  C   . PHE B  1  162 ? 19.360  -24.747 54.546 1.00 31.69  ? 175 PHE B C   1 
ATOM   3849 O  O   . PHE B  1  162 ? 19.241  -25.604 55.428 1.00 32.57  ? 175 PHE B O   1 
ATOM   3850 C  CB  . PHE B  1  162 ? 19.706  -25.448 52.179 1.00 32.45  ? 175 PHE B CB  1 
ATOM   3851 C  CG  . PHE B  1  162 ? 20.616  -25.591 50.977 1.00 32.17  ? 175 PHE B CG  1 
ATOM   3852 C  CD1 . PHE B  1  162 ? 20.802  -24.522 50.103 1.00 35.30  ? 175 PHE B CD1 1 
ATOM   3853 C  CD2 . PHE B  1  162 ? 21.286  -26.781 50.716 1.00 34.38  ? 175 PHE B CD2 1 
ATOM   3854 C  CE1 . PHE B  1  162 ? 21.623  -24.646 48.993 1.00 37.17  ? 175 PHE B CE1 1 
ATOM   3855 C  CE2 . PHE B  1  162 ? 22.109  -26.899 49.598 1.00 37.71  ? 175 PHE B CE2 1 
ATOM   3856 C  CZ  . PHE B  1  162 ? 22.278  -25.828 48.741 1.00 37.68  ? 175 PHE B CZ  1 
ATOM   3857 N  N   . TYR B  1  163 ? 18.643  -23.612 54.502 1.00 30.42  ? 176 TYR B N   1 
ATOM   3858 C  CA  . TYR B  1  163 ? 17.593  -23.353 55.459 1.00 29.72  ? 176 TYR B CA  1 
ATOM   3859 C  C   . TYR B  1  163 ? 16.294  -23.896 54.876 1.00 31.82  ? 176 TYR B C   1 
ATOM   3860 O  O   . TYR B  1  163 ? 15.869  -23.475 53.806 1.00 32.91  ? 176 TYR B O   1 
ATOM   3861 C  CB  . TYR B  1  163 ? 17.458  -21.869 55.782 1.00 29.90  ? 176 TYR B CB  1 
ATOM   3862 C  CG  . TYR B  1  163 ? 16.473  -21.524 56.888 1.00 29.97  ? 176 TYR B CG  1 
ATOM   3863 C  CD1 . TYR B  1  163 ? 16.812  -21.670 58.231 1.00 32.02  ? 176 TYR B CD1 1 
ATOM   3864 C  CD2 . TYR B  1  163 ? 15.206  -21.037 56.590 1.00 33.77  ? 176 TYR B CD2 1 
ATOM   3865 C  CE1 . TYR B  1  163 ? 15.923  -21.349 59.243 1.00 32.51  ? 176 TYR B CE1 1 
ATOM   3866 C  CE2 . TYR B  1  163 ? 14.311  -20.689 57.599 1.00 33.09  ? 176 TYR B CE2 1 
ATOM   3867 C  CZ  . TYR B  1  163 ? 14.668  -20.844 58.926 1.00 32.81  ? 176 TYR B CZ  1 
ATOM   3868 O  OH  . TYR B  1  163 ? 13.789  -20.496 59.906 1.00 31.71  ? 176 TYR B OH  1 
ATOM   3869 N  N   . ASN B  1  164 ? 15.689  -24.846 55.592 1.00 32.08  ? 177 ASN B N   1 
ATOM   3870 C  CA  . ASN B  1  164 ? 14.432  -25.424 55.152 1.00 34.33  ? 177 ASN B CA  1 
ATOM   3871 C  C   . ASN B  1  164 ? 13.550  -25.589 56.382 1.00 32.14  ? 177 ASN B C   1 
ATOM   3872 O  O   . ASN B  1  164 ? 13.931  -25.200 57.480 1.00 30.18  ? 177 ASN B O   1 
ATOM   3873 C  CB  . ASN B  1  164 ? 14.669  -26.679 54.314 1.00 35.03  ? 177 ASN B CB  1 
ATOM   3874 C  CG  . ASN B  1  164 ? 15.049  -27.896 55.129 1.00 33.66  ? 177 ASN B CG  1 
ATOM   3875 O  OD1 . ASN B  1  164 ? 15.049  -27.877 56.362 1.00 33.49  ? 177 ASN B OD1 1 
ATOM   3876 N  ND2 . ASN B  1  164 ? 15.385  -28.976 54.439 1.00 39.44  ? 177 ASN B ND2 1 
ATOM   3877 N  N   . LEU B  1  165 ? 12.362  -26.165 56.193 1.00 35.94  ? 178 LEU B N   1 
ATOM   3878 C  CA  . LEU B  1  165 ? 11.384  -26.200 57.271 1.00 36.39  ? 178 LEU B CA  1 
ATOM   3879 C  C   . LEU B  1  165 ? 11.895  -26.990 58.479 1.00 34.39  ? 178 LEU B C   1 
ATOM   3880 O  O   . LEU B  1  165 ? 11.582  -26.642 59.613 1.00 31.83  ? 178 LEU B O   1 
ATOM   3881 C  CB  . LEU B  1  165 ? 10.084  -26.766 56.708 1.00 42.84  ? 178 LEU B CB  1 
ATOM   3882 C  CG  . LEU B  1  165 ? 8.873   -26.681 57.637 1.00 47.69  ? 178 LEU B CG  1 
ATOM   3883 C  CD1 . LEU B  1  165 ? 8.492   -25.248 57.943 1.00 44.68  ? 178 LEU B CD1 1 
ATOM   3884 C  CD2 . LEU B  1  165 ? 7.682   -27.394 57.012 1.00 51.62  ? 178 LEU B CD2 1 
ATOM   3885 N  N   . THR B  1  166 ? 12.712  -28.034 58.259 1.00 37.09  ? 179 THR B N   1 
ATOM   3886 C  CA  . THR B  1  166 ? 13.265  -28.800 59.374 1.00 36.36  ? 179 THR B CA  1 
ATOM   3887 C  C   . THR B  1  166 ? 14.190  -27.909 60.211 1.00 33.90  ? 179 THR B C   1 
ATOM   3888 O  O   . THR B  1  166 ? 14.156  -27.900 61.442 1.00 34.85  ? 179 THR B O   1 
ATOM   3889 C  CB  . THR B  1  166 ? 14.001  -30.039 58.851 1.00 38.19  ? 179 THR B CB  1 
ATOM   3890 O  OG1 . THR B  1  166 ? 13.171  -30.691 57.889 1.00 39.65  ? 179 THR B OG1 1 
ATOM   3891 C  CG2 . THR B  1  166 ? 14.392  -30.996 59.961 1.00 39.77  ? 179 THR B CG2 1 
ATOM   3892 N  N   . VAL B  1  167 ? 15.026  -27.124 59.528 1.00 35.22  ? 180 VAL B N   1 
ATOM   3893 C  CA  . VAL B  1  167 ? 15.947  -26.216 60.195 1.00 31.54  ? 180 VAL B CA  1 
ATOM   3894 C  C   . VAL B  1  167 ? 15.156  -25.202 61.021 1.00 30.48  ? 180 VAL B C   1 
ATOM   3895 O  O   . VAL B  1  167 ? 15.504  -24.917 62.169 1.00 34.08  ? 180 VAL B O   1 
ATOM   3896 C  CB  . VAL B  1  167 ? 16.888  -25.503 59.201 1.00 31.92  ? 180 VAL B CB  1 
ATOM   3897 C  CG1 . VAL B  1  167 ? 17.920  -24.664 59.934 1.00 31.71  ? 180 VAL B CG1 1 
ATOM   3898 C  CG2 . VAL B  1  167 ? 17.580  -26.484 58.273 1.00 35.32  ? 180 VAL B CG2 1 
ATOM   3899 N  N   . ALA B  1  168 ? 14.077  -24.675 60.435 1.00 31.97  ? 181 ALA B N   1 
ATOM   3900 C  CA  . ALA B  1  168 ? 13.254  -23.655 61.075 1.00 32.20  ? 181 ALA B CA  1 
ATOM   3901 C  C   . ALA B  1  168 ? 12.741  -24.146 62.427 1.00 32.72  ? 181 ALA B C   1 
ATOM   3902 O  O   . ALA B  1  168 ? 12.822  -23.431 63.423 1.00 32.19  ? 181 ALA B O   1 
ATOM   3903 C  CB  . ALA B  1  168 ? 12.118  -23.273 60.146 1.00 32.63  ? 181 ALA B CB  1 
ATOM   3904 N  N   . GLY B  1  169 ? 12.237  -25.386 62.460 1.00 34.07  ? 182 GLY B N   1 
ATOM   3905 C  CA  . GLY B  1  169 ? 11.758  -25.964 63.705 1.00 35.81  ? 182 GLY B CA  1 
ATOM   3906 C  C   . GLY B  1  169 ? 12.839  -26.007 64.782 1.00 34.59  ? 182 GLY B C   1 
ATOM   3907 O  O   . GLY B  1  169 ? 12.597  -25.648 65.934 1.00 36.89  ? 182 GLY B O   1 
ATOM   3908 N  N   . GLU B  1  170 ? 14.044  -26.448 64.395 1.00 35.84  ? 183 GLU B N   1 
ATOM   3909 C  CA  . GLU B  1  170 ? 15.138  -26.606 65.345 1.00 33.88  ? 183 GLU B CA  1 
ATOM   3910 C  C   . GLU B  1  170 ? 15.636  -25.241 65.811 1.00 32.64  ? 183 GLU B C   1 
ATOM   3911 O  O   . GLU B  1  170 ? 15.876  -25.033 66.995 1.00 34.34  ? 183 GLU B O   1 
ATOM   3912 C  CB  . GLU B  1  170 ? 16.274  -27.441 64.743 1.00 37.57  ? 183 GLU B CB  1 
ATOM   3913 C  CG  . GLU B  1  170 ? 15.898  -28.888 64.423 1.00 40.06  ? 183 GLU B CG  1 
ATOM   3914 C  CD  . GLU B  1  170 ? 15.365  -29.661 65.621 1.00 48.05  ? 183 GLU B CD  1 
ATOM   3915 O  OE1 . GLU B  1  170 ? 15.799  -29.391 66.761 1.00 50.56  ? 183 GLU B OE1 1 
ATOM   3916 O  OE2 . GLU B  1  170 ? 14.452  -30.479 65.410 1.00 60.52  ? 183 GLU B OE2 1 
ATOM   3917 N  N   . LEU B  1  171 ? 15.798  -24.304 64.871 1.00 34.07  ? 184 LEU B N   1 
ATOM   3918 C  CA  . LEU B  1  171 ? 16.396  -23.023 65.202 1.00 32.62  ? 184 LEU B CA  1 
ATOM   3919 C  C   . LEU B  1  171 ? 15.477  -22.224 66.116 1.00 32.23  ? 184 LEU B C   1 
ATOM   3920 O  O   . LEU B  1  171 ? 15.932  -21.594 67.065 1.00 36.66  ? 184 LEU B O   1 
ATOM   3921 C  CB  . LEU B  1  171 ? 16.742  -22.250 63.923 1.00 34.31  ? 184 LEU B CB  1 
ATOM   3922 C  CG  . LEU B  1  171 ? 17.417  -20.889 64.139 1.00 33.96  ? 184 LEU B CG  1 
ATOM   3923 C  CD1 . LEU B  1  171 ? 18.766  -21.052 64.855 1.00 35.89  ? 184 LEU B CD1 1 
ATOM   3924 C  CD2 . LEU B  1  171 ? 17.588  -20.157 62.812 1.00 35.27  ? 184 LEU B CD2 1 
ATOM   3925 N  N   . ARG B  1  172 ? 14.180  -22.220 65.816 1.00 35.84  ? 185 ARG B N   1 
ATOM   3926 C  CA  . ARG B  1  172 ? 13.222  -21.442 66.592 1.00 36.86  ? 185 ARG B CA  1 
ATOM   3927 C  C   . ARG B  1  172 ? 13.290  -21.852 68.067 1.00 35.24  ? 185 ARG B C   1 
ATOM   3928 O  O   . ARG B  1  172 ? 13.374  -21.005 68.950 1.00 32.73  ? 185 ARG B O   1 
ATOM   3929 C  CB  . ARG B  1  172 ? 11.837  -21.650 65.967 1.00 38.33  ? 185 ARG B CB  1 
ATOM   3930 C  CG  . ARG B  1  172 ? 10.616  -21.308 66.805 1.00 39.11  ? 185 ARG B CG  1 
ATOM   3931 C  CD  . ARG B  1  172 ? 10.603  -19.955 67.465 1.00 37.91  ? 185 ARG B CD  1 
ATOM   3932 N  NE  . ARG B  1  172 ? 10.930  -18.850 66.564 1.00 41.07  ? 185 ARG B NE  1 
ATOM   3933 C  CZ  . ARG B  1  172 ? 11.801  -17.891 66.823 1.00 39.90  ? 185 ARG B CZ  1 
ATOM   3934 N  NH1 . ARG B  1  172 ? 12.543  -17.938 67.917 1.00 39.96  ? 185 ARG B NH1 1 
ATOM   3935 N  NH2 . ARG B  1  172 ? 11.936  -16.885 65.981 1.00 41.62  ? 185 ARG B NH2 1 
ATOM   3936 N  N   . TYR B  1  173 ? 13.273  -23.164 68.321 1.00 35.95  ? 186 TYR B N   1 
ATOM   3937 C  CA  . TYR B  1  173 ? 13.306  -23.670 69.686 1.00 36.75  ? 186 TYR B CA  1 
ATOM   3938 C  C   . TYR B  1  173 ? 14.624  -23.298 70.356 1.00 33.30  ? 186 TYR B C   1 
ATOM   3939 O  O   . TYR B  1  173 ? 14.643  -22.835 71.491 1.00 37.10  ? 186 TYR B O   1 
ATOM   3940 C  CB  . TYR B  1  173 ? 13.075  -25.184 69.646 1.00 39.13  ? 186 TYR B CB  1 
ATOM   3941 C  CG  . TYR B  1  173 ? 13.084  -25.836 71.020 1.00 44.36  ? 186 TYR B CG  1 
ATOM   3942 C  CD1 . TYR B  1  173 ? 12.058  -25.584 71.923 1.00 50.47  ? 186 TYR B CD1 1 
ATOM   3943 C  CD2 . TYR B  1  173 ? 14.096  -26.710 71.411 1.00 47.63  ? 186 TYR B CD2 1 
ATOM   3944 C  CE1 . TYR B  1  173 ? 12.047  -26.164 73.183 1.00 52.57  ? 186 TYR B CE1 1 
ATOM   3945 C  CE2 . TYR B  1  173 ? 14.093  -27.301 72.665 1.00 50.36  ? 186 TYR B CE2 1 
ATOM   3946 C  CZ  . TYR B  1  173 ? 13.067  -27.022 73.552 1.00 53.76  ? 186 TYR B CZ  1 
ATOM   3947 O  OH  . TYR B  1  173 ? 13.044  -27.592 74.788 1.00 58.91  ? 186 TYR B OH  1 
ATOM   3948 N  N   . SER B  1  174 ? 15.734  -23.488 69.641 1.00 36.65  ? 187 SER B N   1 
ATOM   3949 C  CA  . SER B  1  174 ? 17.045  -23.250 70.222 1.00 36.51  ? 187 SER B CA  1 
ATOM   3950 C  C   . SER B  1  174 ? 17.204  -21.774 70.579 1.00 38.97  ? 187 SER B C   1 
ATOM   3951 O  O   . SER B  1  174 ? 17.800  -21.448 71.617 1.00 34.35  ? 187 SER B O   1 
ATOM   3952 C  CB  . SER B  1  174 ? 18.142  -23.724 69.309 1.00 37.84  ? 187 SER B CB  1 
ATOM   3953 O  OG  . SER B  1  174 ? 19.402  -23.413 69.883 1.00 38.65  ? 187 SER B OG  1 
ATOM   3954 N  N   . ARG B  1  175 ? 16.627  -20.882 69.751 1.00 37.27  ? 188 ARG B N   1 
ATOM   3955 C  CA  . ARG B  1  175 ? 16.716  -19.451 70.026 1.00 36.45  ? 188 ARG B CA  1 
ATOM   3956 C  C   . ARG B  1  175 ? 15.898  -19.094 71.268 1.00 35.92  ? 188 ARG B C   1 
ATOM   3957 O  O   . ARG B  1  175 ? 16.304  -18.241 72.056 1.00 34.18  ? 188 ARG B O   1 
ATOM   3958 C  CB  . ARG B  1  175 ? 16.338  -18.595 68.807 1.00 36.00  ? 188 ARG B CB  1 
ATOM   3959 C  CG  . ARG B  1  175 ? 17.344  -18.674 67.660 1.00 33.28  ? 188 ARG B CG  1 
ATOM   3960 C  CD  . ARG B  1  175 ? 18.647  -17.966 67.990 1.00 33.46  ? 188 ARG B CD  1 
ATOM   3961 N  NE  . ARG B  1  175 ? 18.430  -16.535 68.185 1.00 34.25  ? 188 ARG B NE  1 
ATOM   3962 C  CZ  . ARG B  1  175 ? 18.561  -15.838 69.309 1.00 35.97  ? 188 ARG B CZ  1 
ATOM   3963 N  NH1 . ARG B  1  175 ? 19.147  -16.362 70.372 1.00 35.99  ? 188 ARG B NH1 1 
ATOM   3964 N  NH2 . ARG B  1  175 ? 18.150  -14.576 69.345 1.00 33.61  ? 188 ARG B NH2 1 
ATOM   3965 N  N   . ILE B  1  176 ? 14.731  -19.725 71.439 1.00 36.08  ? 189 ILE B N   1 
ATOM   3966 C  CA  . ILE B  1  176 ? 13.956  -19.548 72.658 1.00 37.40  ? 189 ILE B CA  1 
ATOM   3967 C  C   . ILE B  1  176 ? 14.813  -19.939 73.875 1.00 37.87  ? 189 ILE B C   1 
ATOM   3968 O  O   . ILE B  1  176 ? 14.903  -19.187 74.846 1.00 36.19  ? 189 ILE B O   1 
ATOM   3969 C  CB  . ILE B  1  176 ? 12.646  -20.349 72.572 1.00 35.46  ? 189 ILE B CB  1 
ATOM   3970 C  CG1 . ILE B  1  176 ? 11.686  -19.750 71.533 1.00 39.33  ? 189 ILE B CG1 1 
ATOM   3971 C  CG2 . ILE B  1  176 ? 11.972  -20.465 73.940 1.00 37.63  ? 189 ILE B CG2 1 
ATOM   3972 C  CD1 . ILE B  1  176 ? 10.560  -20.685 71.129 1.00 37.67  ? 189 ILE B CD1 1 
ATOM   3973 N  N   . GLN B  1  177 ? 15.470  -21.102 73.804 1.00 40.96  ? 190 GLN B N   1 
ATOM   3974 C  CA  . GLN B  1  177 ? 16.317  -21.573 74.901 1.00 43.01  ? 190 GLN B CA  1 
ATOM   3975 C  C   . GLN B  1  177 ? 17.469  -20.602 75.187 1.00 41.14  ? 190 GLN B C   1 
ATOM   3976 O  O   . GLN B  1  177 ? 17.746  -20.329 76.351 1.00 43.58  ? 190 GLN B O   1 
ATOM   3977 C  CB  . GLN B  1  177 ? 16.827  -22.990 74.630 1.00 43.06  ? 190 GLN B CB  1 
ATOM   3978 C  CG  . GLN B  1  177 ? 15.720  -24.039 74.565 1.00 46.97  ? 190 GLN B CG  1 
ATOM   3979 C  CD  . GLN B  1  177 ? 14.902  -24.126 75.842 1.00 61.50  ? 190 GLN B CD  1 
ATOM   3980 O  OE1 . GLN B  1  177 ? 15.336  -23.737 76.934 1.00 61.45  ? 190 GLN B OE1 1 
ATOM   3981 N  NE2 . GLN B  1  177 ? 13.695  -24.655 75.723 1.00 71.73  ? 190 GLN B NE2 1 
ATOM   3982 N  N   . ASP B  1  178 ? 18.122  -20.059 74.145 1.00 41.59  ? 191 ASP B N   1 
ATOM   3983 C  CA  . ASP B  1  178 ? 19.166  -19.059 74.337 1.00 42.33  ? 191 ASP B CA  1 
ATOM   3984 C  C   . ASP B  1  178 ? 18.651  -17.889 75.172 1.00 44.98  ? 191 ASP B C   1 
ATOM   3985 O  O   . ASP B  1  178 ? 19.327  -17.423 76.093 1.00 46.12  ? 191 ASP B O   1 
ATOM   3986 C  CB  . ASP B  1  178 ? 19.695  -18.472 73.036 1.00 43.52  ? 191 ASP B CB  1 
ATOM   3987 C  CG  . ASP B  1  178 ? 20.417  -19.416 72.085 1.00 48.24  ? 191 ASP B CG  1 
ATOM   3988 O  OD1 . ASP B  1  178 ? 20.841  -20.500 72.548 1.00 45.24  ? 191 ASP B OD1 1 
ATOM   3989 O  OD2 . ASP B  1  178 ? 20.536  -19.056 70.878 1.00 47.86  ? 191 ASP B OD2 1 
ATOM   3990 N  N   . SER B  1  179 ? 17.462  -17.381 74.819 1.00 40.08  ? 192 SER B N   1 
ATOM   3991 C  CA  . SER B  1  179 ? 16.914  -16.214 75.500 1.00 40.14  ? 192 SER B CA  1 
ATOM   3992 C  C   . SER B  1  179 ? 16.519  -16.570 76.943 1.00 39.28  ? 192 SER B C   1 
ATOM   3993 O  O   . SER B  1  179 ? 16.687  -15.760 77.846 1.00 38.24  ? 192 SER B O   1 
ATOM   3994 C  CB  . SER B  1  179 ? 15.756  -15.603 74.713 1.00 41.56  ? 192 SER B CB  1 
ATOM   3995 O  OG  . SER B  1  179 ? 16.220  -14.814 73.618 1.00 37.82  ? 192 SER B OG  1 
ATOM   3996 N  N   . ILE B  1  180 ? 15.970  -17.770 77.169 1.00 39.74  ? 193 ILE B N   1 
ATOM   3997 C  CA  . ILE B  1  180 ? 15.627  -18.189 78.522 1.00 43.28  ? 193 ILE B CA  1 
ATOM   3998 C  C   . ILE B  1  180 ? 16.889  -18.153 79.394 1.00 43.54  ? 193 ILE B C   1 
ATOM   3999 O  O   . ILE B  1  180 ? 16.869  -17.601 80.486 1.00 41.39  ? 193 ILE B O   1 
ATOM   4000 C  CB  . ILE B  1  180 ? 14.975  -19.584 78.534 1.00 44.87  ? 193 ILE B CB  1 
ATOM   4001 C  CG1 . ILE B  1  180 ? 13.558  -19.545 77.970 1.00 43.79  ? 193 ILE B CG1 1 
ATOM   4002 C  CG2 . ILE B  1  180 ? 14.993  -20.189 79.943 1.00 46.11  ? 193 ILE B CG2 1 
ATOM   4003 C  CD1 . ILE B  1  180 ? 12.944  -20.914 77.732 1.00 43.46  ? 193 ILE B CD1 1 
ATOM   4004 N  N   . ALA B  1  181 ? 17.985  -18.707 78.868 1.00 44.34  ? 194 ALA B N   1 
ATOM   4005 C  CA  . ALA B  1  181 ? 19.229  -18.879 79.601 1.00 44.05  ? 194 ALA B CA  1 
ATOM   4006 C  C   . ALA B  1  181 ? 19.956  -17.557 79.832 1.00 48.47  ? 194 ALA B C   1 
ATOM   4007 O  O   . ALA B  1  181 ? 20.695  -17.457 80.801 1.00 48.14  ? 194 ALA B O   1 
ATOM   4008 C  CB  . ALA B  1  181 ? 20.112  -19.862 78.877 1.00 46.57  ? 194 ALA B CB  1 
ATOM   4009 N  N   . THR B  1  182 ? 19.755  -16.534 78.988 1.00 43.60  ? 195 THR B N   1 
ATOM   4010 C  CA  . THR B  1  182 ? 20.654  -15.385 79.025 1.00 41.44  ? 195 THR B CA  1 
ATOM   4011 C  C   . THR B  1  182 ? 19.925  -14.059 79.216 1.00 42.96  ? 195 THR B C   1 
ATOM   4012 O  O   . THR B  1  182 ? 20.571  -13.032 79.448 1.00 44.37  ? 195 THR B O   1 
ATOM   4013 C  CB  . THR B  1  182 ? 21.496  -15.341 77.743 1.00 48.74  ? 195 THR B CB  1 
ATOM   4014 O  OG1 . THR B  1  182 ? 20.611  -15.148 76.632 1.00 48.53  ? 195 THR B OG1 1 
ATOM   4015 C  CG2 . THR B  1  182 ? 22.329  -16.599 77.554 1.00 46.96  ? 195 THR B CG2 1 
ATOM   4016 N  N   . ASN B  1  183 ? 18.595  -14.037 79.053 1.00 43.57  ? 196 ASN B N   1 
ATOM   4017 C  CA  . ASN B  1  183 ? 17.885  -12.769 79.043 1.00 42.23  ? 196 ASN B CA  1 
ATOM   4018 C  C   . ASN B  1  183 ? 16.882  -12.795 80.185 1.00 46.98  ? 196 ASN B C   1 
ATOM   4019 O  O   . ASN B  1  183 ? 15.845  -13.445 80.085 1.00 42.23  ? 196 ASN B O   1 
ATOM   4020 C  CB  . ASN B  1  183 ? 17.206  -12.498 77.703 1.00 43.08  ? 196 ASN B CB  1 
ATOM   4021 C  CG  . ASN B  1  183 ? 16.433  -11.196 77.676 1.00 42.79  ? 196 ASN B CG  1 
ATOM   4022 O  OD1 . ASN B  1  183 ? 16.383  -10.464 78.672 1.00 43.40  ? 196 ASN B OD1 1 
ATOM   4023 N  ND2 . ASN B  1  183 ? 15.830  -10.869 76.538 1.00 41.69  ? 196 ASN B ND2 1 
ATOM   4024 N  N   . PRO B  1  184 ? 17.157  -12.088 81.300 1.00 49.42  ? 197 PRO B N   1 
ATOM   4025 C  CA  . PRO B  1  184 ? 16.252  -12.125 82.448 1.00 53.86  ? 197 PRO B CA  1 
ATOM   4026 C  C   . PRO B  1  184 ? 14.915  -11.421 82.197 1.00 55.53  ? 197 PRO B C   1 
ATOM   4027 O  O   . PRO B  1  184 ? 13.974  -11.630 82.958 1.00 56.35  ? 197 PRO B O   1 
ATOM   4028 C  CB  . PRO B  1  184 ? 17.101  -11.442 83.541 1.00 52.03  ? 197 PRO B CB  1 
ATOM   4029 C  CG  . PRO B  1  184 ? 17.953  -10.441 82.768 1.00 51.13  ? 197 PRO B CG  1 
ATOM   4030 C  CD  . PRO B  1  184 ? 18.311  -11.194 81.494 1.00 47.93  ? 197 PRO B CD  1 
ATOM   4031 N  N   . GLU B  1  185 ? 14.842  -10.600 81.134 1.00 52.87  ? 198 GLU B N   1 
ATOM   4032 C  CA  . GLU B  1  185 ? 13.622  -9.890  80.766 1.00 47.94  ? 198 GLU B CA  1 
ATOM   4033 C  C   . GLU B  1  185 ? 12.922  -10.551 79.575 1.00 43.99  ? 198 GLU B C   1 
ATOM   4034 O  O   . GLU B  1  185 ? 11.994  -9.982  79.014 1.00 46.22  ? 198 GLU B O   1 
ATOM   4035 C  CB  . GLU B  1  185 ? 13.923  -8.435  80.410 1.00 49.10  ? 198 GLU B CB  1 
ATOM   4036 C  CG  . GLU B  1  185 ? 14.611  -7.621  81.505 1.00 51.95  ? 198 GLU B CG  1 
ATOM   4037 C  CD  . GLU B  1  185 ? 14.975  -6.215  81.045 1.00 60.07  ? 198 GLU B CD  1 
ATOM   4038 O  OE1 . GLU B  1  185 ? 14.675  -5.871  79.872 1.00 57.63  ? 198 GLU B OE1 1 
ATOM   4039 O  OE2 . GLU B  1  185 ? 15.554  -5.445  81.846 1.00 64.28  ? 198 GLU B OE2 1 
ATOM   4040 N  N   . PHE B  1  186 ? 13.333  -11.768 79.208 1.00 44.78  ? 199 PHE B N   1 
ATOM   4041 C  CA  . PHE B  1  186 ? 12.781  -12.485 78.069 1.00 41.50  ? 199 PHE B CA  1 
ATOM   4042 C  C   . PHE B  1  186 ? 11.261  -12.612 78.171 1.00 46.62  ? 199 PHE B C   1 
ATOM   4043 O  O   . PHE B  1  186 ? 10.741  -13.141 79.152 1.00 43.60  ? 199 PHE B O   1 
ATOM   4044 C  CB  . PHE B  1  186 ? 13.355  -13.902 78.011 1.00 38.51  ? 199 PHE B CB  1 
ATOM   4045 C  CG  . PHE B  1  186 ? 12.830  -14.783 76.886 1.00 38.33  ? 199 PHE B CG  1 
ATOM   4046 C  CD1 . PHE B  1  186 ? 12.690  -14.289 75.589 1.00 37.15  ? 199 PHE B CD1 1 
ATOM   4047 C  CD2 . PHE B  1  186 ? 12.477  -16.103 77.128 1.00 37.00  ? 199 PHE B CD2 1 
ATOM   4048 C  CE1 . PHE B  1  186 ? 12.221  -15.106 74.573 1.00 34.16  ? 199 PHE B CE1 1 
ATOM   4049 C  CE2 . PHE B  1  186 ? 12.003  -16.912 76.106 1.00 38.05  ? 199 PHE B CE2 1 
ATOM   4050 C  CZ  . PHE B  1  186 ? 11.878  -16.410 74.827 1.00 36.62  ? 199 PHE B CZ  1 
ATOM   4051 N  N   . GLN B  1  187 ? 10.573  -12.165 77.115 1.00 45.05  ? 200 GLN B N   1 
ATOM   4052 C  CA  . GLN B  1  187 ? 9.129   -12.297 76.978 1.00 45.19  ? 200 GLN B CA  1 
ATOM   4053 C  C   . GLN B  1  187 ? 8.845   -12.999 75.652 1.00 44.28  ? 200 GLN B C   1 
ATOM   4054 O  O   . GLN B  1  187 ? 9.489   -12.707 74.645 1.00 38.49  ? 200 GLN B O   1 
ATOM   4055 C  CB  . GLN B  1  187 ? 8.452   -10.925 76.956 1.00 46.27  ? 200 GLN B CB  1 
ATOM   4056 C  CG  . GLN B  1  187 ? 8.500   -10.177 78.287 1.00 51.50  ? 200 GLN B CG  1 
ATOM   4057 C  CD  . GLN B  1  187 ? 7.582   -10.806 79.315 1.00 56.73  ? 200 GLN B CD  1 
ATOM   4058 O  OE1 . GLN B  1  187 ? 6.358   -10.722 79.200 1.00 59.67  ? 200 GLN B OE1 1 
ATOM   4059 N  NE2 . GLN B  1  187 ? 8.153   -11.496 80.289 1.00 56.70  ? 200 GLN B NE2 1 
ATOM   4060 N  N   . PHE B  1  188 ? 7.907   -13.945 75.676 1.00 37.34  ? 201 PHE B N   1 
ATOM   4061 C  CA  . PHE B  1  188 ? 7.513   -14.659 74.483 1.00 36.45  ? 201 PHE B CA  1 
ATOM   4062 C  C   . PHE B  1  188 ? 6.012   -14.930 74.524 1.00 35.63  ? 201 PHE B C   1 
ATOM   4063 O  O   . PHE B  1  188 ? 5.581   -16.076 74.577 1.00 34.78  ? 201 PHE B O   1 
ATOM   4064 C  CB  . PHE B  1  188 ? 8.367   -15.921 74.404 1.00 36.26  ? 201 PHE B CB  1 
ATOM   4065 C  CG  . PHE B  1  188 ? 8.481   -16.509 73.008 1.00 36.56  ? 201 PHE B CG  1 
ATOM   4066 C  CD1 . PHE B  1  188 ? 9.212   -15.850 72.028 1.00 38.80  ? 201 PHE B CD1 1 
ATOM   4067 C  CD2 . PHE B  1  188 ? 7.902   -17.717 72.687 1.00 37.30  ? 201 PHE B CD2 1 
ATOM   4068 C  CE1 . PHE B  1  188 ? 9.333   -16.378 70.762 1.00 36.41  ? 201 PHE B CE1 1 
ATOM   4069 C  CE2 . PHE B  1  188 ? 8.034   -18.250 71.424 1.00 36.24  ? 201 PHE B CE2 1 
ATOM   4070 C  CZ  . PHE B  1  188 ? 8.736   -17.574 70.462 1.00 36.67  ? 201 PHE B CZ  1 
ATOM   4071 N  N   . LYS B  1  189 ? 5.228   -13.859 74.470 1.00 38.64  ? 202 LYS B N   1 
ATOM   4072 C  CA  . LYS B  1  189 ? 3.784   -13.976 74.602 1.00 42.80  ? 202 LYS B CA  1 
ATOM   4073 C  C   . LYS B  1  189 ? 3.084   -12.941 73.718 1.00 41.64  ? 202 LYS B C   1 
ATOM   4074 O  O   . LYS B  1  189 ? 3.727   -12.098 73.089 1.00 39.26  ? 202 LYS B O   1 
ATOM   4075 C  CB  . LYS B  1  189 ? 3.421   -13.802 76.079 1.00 42.76  ? 202 LYS B CB  1 
ATOM   4076 C  CG  . LYS B  1  189 ? 3.794   -12.440 76.648 1.00 46.95  ? 202 LYS B CG  1 
ATOM   4077 C  CD  . LYS B  1  189 ? 3.258   -12.151 78.048 1.00 52.83  ? 202 LYS B CD  1 
ATOM   4078 C  CE  . LYS B  1  189 ? 3.898   -12.995 79.089 1.00 58.47  ? 202 LYS B CE  1 
ATOM   4079 N  NZ  . LYS B  1  189 ? 3.583   -12.514 80.435 1.00 64.56  ? 202 LYS B NZ  1 
ATOM   4080 N  N   . ASN B  1  190 ? 1.748   -13.026 73.670 1.00 40.18  ? 203 ASN B N   1 
ATOM   4081 C  CA  . ASN B  1  190 ? 0.924   -12.076 72.933 1.00 38.69  ? 203 ASN B CA  1 
ATOM   4082 C  C   . ASN B  1  190 ? 1.434   -11.953 71.494 1.00 35.73  ? 203 ASN B C   1 
ATOM   4083 O  O   . ASN B  1  190 ? 1.548   -12.948 70.783 1.00 35.18  ? 203 ASN B O   1 
ATOM   4084 C  CB  . ASN B  1  190 ? 0.797   -10.785 73.739 1.00 41.33  ? 203 ASN B CB  1 
ATOM   4085 C  CG  . ASN B  1  190 ? 0.025   -11.043 75.021 1.00 46.83  ? 203 ASN B CG  1 
ATOM   4086 O  OD1 . ASN B  1  190 ? -1.015  -11.718 75.002 1.00 46.49  ? 203 ASN B OD1 1 
ATOM   4087 N  ND2 . ASN B  1  190 ? 0.528   -10.525 76.129 1.00 46.88  ? 203 ASN B ND2 1 
ATOM   4088 N  N   . VAL B  1  191 ? 1.715   -10.733 71.035 1.00 35.01  ? 204 VAL B N   1 
ATOM   4089 C  CA  . VAL B  1  191 ? 2.039   -10.532 69.632 1.00 35.61  ? 204 VAL B CA  1 
ATOM   4090 C  C   . VAL B  1  191 ? 3.256   -11.381 69.269 1.00 35.18  ? 204 VAL B C   1 
ATOM   4091 O  O   . VAL B  1  191 ? 3.269   -12.069 68.249 1.00 37.20  ? 204 VAL B O   1 
ATOM   4092 C  CB  . VAL B  1  191 ? 2.292   -9.050  69.298 1.00 37.74  ? 204 VAL B CB  1 
ATOM   4093 C  CG1 . VAL B  1  191 ? 2.816   -8.869  67.872 1.00 36.63  ? 204 VAL B CG1 1 
ATOM   4094 C  CG2 . VAL B  1  191 ? 1.047   -8.205  69.497 1.00 38.23  ? 204 VAL B CG2 1 
ATOM   4095 N  N   . ARG B  1  192 ? 4.295   -11.318 70.098 1.00 32.24  ? 205 ARG B N   1 
ATOM   4096 C  CA  . ARG B  1  192 ? 5.565   -11.926 69.739 1.00 32.58  ? 205 ARG B CA  1 
ATOM   4097 C  C   . ARG B  1  192 ? 5.432   -13.435 69.561 1.00 33.61  ? 205 ARG B C   1 
ATOM   4098 O  O   . ARG B  1  192 ? 6.065   -14.016 68.688 1.00 32.44  ? 205 ARG B O   1 
ATOM   4099 C  CB  . ARG B  1  192 ? 6.629   -11.605 70.790 1.00 33.91  ? 205 ARG B CB  1 
ATOM   4100 C  CG  . ARG B  1  192 ? 7.998   -12.179 70.448 1.00 36.19  ? 205 ARG B CG  1 
ATOM   4101 C  CD  . ARG B  1  192 ? 8.432   -11.758 69.051 1.00 33.80  ? 205 ARG B CD  1 
ATOM   4102 N  NE  . ARG B  1  192 ? 9.745   -12.313 68.698 1.00 34.12  ? 205 ARG B NE  1 
ATOM   4103 C  CZ  . ARG B  1  192 ? 10.189  -12.486 67.449 1.00 37.31  ? 205 ARG B CZ  1 
ATOM   4104 N  NH1 . ARG B  1  192 ? 9.445   -12.147 66.408 1.00 35.30  ? 205 ARG B NH1 1 
ATOM   4105 N  NH2 . ARG B  1  192 ? 11.374  -13.035 67.245 1.00 35.97  ? 205 ARG B NH2 1 
ATOM   4106 N  N   . PHE B  1  193 ? 4.604   -14.078 70.387 1.00 34.17  ? 206 PHE B N   1 
ATOM   4107 C  CA  . PHE B  1  193 ? 4.461   -15.523 70.316 1.00 34.17  ? 206 PHE B CA  1 
ATOM   4108 C  C   . PHE B  1  193 ? 3.944   -15.910 68.936 1.00 34.40  ? 206 PHE B C   1 
ATOM   4109 O  O   . PHE B  1  193 ? 4.391   -16.899 68.359 1.00 39.68  ? 206 PHE B O   1 
ATOM   4110 C  CB  . PHE B  1  193 ? 3.559   -16.058 71.430 1.00 36.20  ? 206 PHE B CB  1 
ATOM   4111 C  CG  . PHE B  1  193 ? 3.371   -17.566 71.342 1.00 37.79  ? 206 PHE B CG  1 
ATOM   4112 C  CD1 . PHE B  1  193 ? 4.360   -18.427 71.792 1.00 37.08  ? 206 PHE B CD1 1 
ATOM   4113 C  CD2 . PHE B  1  193 ? 2.225   -18.117 70.784 1.00 39.62  ? 206 PHE B CD2 1 
ATOM   4114 C  CE1 . PHE B  1  193 ? 4.196   -19.796 71.701 1.00 39.86  ? 206 PHE B CE1 1 
ATOM   4115 C  CE2 . PHE B  1  193 ? 2.066   -19.483 70.698 1.00 41.55  ? 206 PHE B CE2 1 
ATOM   4116 C  CZ  . PHE B  1  193 ? 3.055   -20.321 71.147 1.00 41.88  ? 206 PHE B CZ  1 
ATOM   4117 N  N   . ILE B  1  194 ? 3.027   -15.107 68.394 1.00 34.48  ? 207 ILE B N   1 
ATOM   4118 C  CA  . ILE B  1  194 ? 2.444   -15.419 67.100 1.00 35.36  ? 207 ILE B CA  1 
ATOM   4119 C  C   . ILE B  1  194 ? 3.428   -15.080 65.977 1.00 33.80  ? 207 ILE B C   1 
ATOM   4120 O  O   . ILE B  1  194 ? 3.678   -15.921 65.115 1.00 35.89  ? 207 ILE B O   1 
ATOM   4121 C  CB  . ILE B  1  194 ? 1.077   -14.727 66.946 1.00 38.82  ? 207 ILE B CB  1 
ATOM   4122 C  CG1 . ILE B  1  194 ? 0.092   -15.167 68.041 1.00 38.89  ? 207 ILE B CG1 1 
ATOM   4123 C  CG2 . ILE B  1  194 ? 0.510   -14.962 65.551 1.00 40.92  ? 207 ILE B CG2 1 
ATOM   4124 C  CD1 . ILE B  1  194 ? -0.171  -16.664 68.101 1.00 38.65  ? 207 ILE B CD1 1 
ATOM   4125 N  N   . THR B  1  195 ? 4.029   -13.881 66.011 1.00 34.42  ? 208 THR B N   1 
ATOM   4126 C  CA  . THR B  1  195 ? 4.877   -13.421 64.913 1.00 36.11  ? 208 THR B CA  1 
ATOM   4127 C  C   . THR B  1  195 ? 6.172   -14.231 64.824 1.00 36.28  ? 208 THR B C   1 
ATOM   4128 O  O   . THR B  1  195 ? 6.732   -14.359 63.740 1.00 37.44  ? 208 THR B O   1 
ATOM   4129 C  CB  . THR B  1  195 ? 5.194   -11.933 65.021 1.00 35.04  ? 208 THR B CB  1 
ATOM   4130 O  OG1 . THR B  1  195 ? 5.971   -11.710 66.190 1.00 38.86  ? 208 THR B OG1 1 
ATOM   4131 C  CG2 . THR B  1  195 ? 3.948   -11.075 65.063 1.00 36.49  ? 208 THR B CG2 1 
ATOM   4132 N  N   . ALA B  1  196 ? 6.637   -14.795 65.943 1.00 36.90  ? 209 ALA B N   1 
ATOM   4133 C  CA  . ALA B  1  196 ? 7.912   -15.494 65.961 1.00 40.62  ? 209 ALA B CA  1 
ATOM   4134 C  C   . ALA B  1  196 ? 7.885   -16.778 65.135 1.00 42.60  ? 209 ALA B C   1 
ATOM   4135 O  O   . ALA B  1  196 ? 8.943   -17.206 64.689 1.00 45.18  ? 209 ALA B O   1 
ATOM   4136 C  CB  . ALA B  1  196 ? 8.330   -15.793 67.376 1.00 40.85  ? 209 ALA B CB  1 
ATOM   4137 N  N   . TYR B  1  197 ? 6.717   -17.416 64.969 1.00 36.21  ? 210 TYR B N   1 
ATOM   4138 C  CA  . TYR B  1  197 ? 6.651   -18.651 64.203 1.00 36.26  ? 210 TYR B CA  1 
ATOM   4139 C  C   . TYR B  1  197 ? 6.588   -18.298 62.715 1.00 38.41  ? 210 TYR B C   1 
ATOM   4140 O  O   . TYR B  1  197 ? 7.314   -18.876 61.904 1.00 37.26  ? 210 TYR B O   1 
ATOM   4141 C  CB  . TYR B  1  197 ? 5.547   -19.576 64.754 1.00 35.97  ? 210 TYR B CB  1 
ATOM   4142 C  CG  . TYR B  1  197 ? 6.008   -20.201 66.062 1.00 35.82  ? 210 TYR B CG  1 
ATOM   4143 C  CD1 . TYR B  1  197 ? 6.766   -21.364 66.066 1.00 35.12  ? 210 TYR B CD1 1 
ATOM   4144 C  CD2 . TYR B  1  197 ? 5.810   -19.558 67.275 1.00 35.87  ? 210 TYR B CD2 1 
ATOM   4145 C  CE1 . TYR B  1  197 ? 7.258   -21.900 67.245 1.00 35.63  ? 210 TYR B CE1 1 
ATOM   4146 C  CE2 . TYR B  1  197 ? 6.298   -20.080 68.460 1.00 37.03  ? 210 TYR B CE2 1 
ATOM   4147 C  CZ  . TYR B  1  197 ? 7.024   -21.255 68.442 1.00 35.75  ? 210 TYR B CZ  1 
ATOM   4148 O  OH  . TYR B  1  197 ? 7.521   -21.742 69.615 1.00 38.99  ? 210 TYR B OH  1 
ATOM   4149 N  N   . GLY B  1  198 ? 5.756   -17.319 62.355 1.00 36.27  ? 211 GLY B N   1 
ATOM   4150 C  CA  . GLY B  1  198 ? 5.655   -16.882 60.966 1.00 33.96  ? 211 GLY B CA  1 
ATOM   4151 C  C   . GLY B  1  198 ? 6.993   -16.406 60.404 1.00 31.50  ? 211 GLY B C   1 
ATOM   4152 O  O   . GLY B  1  198 ? 7.349   -16.737 59.275 1.00 31.71  ? 211 GLY B O   1 
ATOM   4153 N  N   . GLU B  1  199 ? 7.750   -15.647 61.204 1.00 32.82  ? 212 GLU B N   1 
ATOM   4154 C  CA  A GLU B  1  199 ? 8.993   -15.071 60.720 0.50 32.86  ? 212 GLU B CA  1 
ATOM   4155 C  CA  B GLU B  1  199 ? 9.009   -15.066 60.757 0.50 31.93  ? 212 GLU B CA  1 
ATOM   4156 C  C   . GLU B  1  199 ? 9.990   -16.174 60.357 1.00 33.02  ? 212 GLU B C   1 
ATOM   4157 O  O   . GLU B  1  199 ? 10.848  -15.964 59.499 1.00 30.26  ? 212 GLU B O   1 
ATOM   4158 C  CB  A GLU B  1  199 ? 9.525   -14.021 61.691 0.50 35.06  ? 212 GLU B CB  1 
ATOM   4159 C  CB  B GLU B  1  199 ? 9.581   -14.082 61.793 0.50 32.73  ? 212 GLU B CB  1 
ATOM   4160 C  CG  A GLU B  1  199 ? 8.742   -12.711 61.624 0.50 35.54  ? 212 GLU B CG  1 
ATOM   4161 C  CG  B GLU B  1  199 ? 10.322  -14.681 62.996 0.50 31.58  ? 212 GLU B CG  1 
ATOM   4162 C  CD  A GLU B  1  199 ? 8.922   -11.846 62.853 0.50 34.69  ? 212 GLU B CD  1 
ATOM   4163 C  CD  B GLU B  1  199 ? 10.987  -13.701 63.978 0.50 29.94  ? 212 GLU B CD  1 
ATOM   4164 O  OE1 A GLU B  1  199 ? 9.839   -12.137 63.649 0.50 39.17  ? 212 GLU B OE1 1 
ATOM   4165 O  OE1 B GLU B  1  199 ? 10.654  -12.506 63.984 0.50 27.48  ? 212 GLU B OE1 1 
ATOM   4166 O  OE2 A GLU B  1  199 ? 8.133   -10.900 63.018 0.50 37.59  ? 212 GLU B OE2 1 
ATOM   4167 O  OE2 B GLU B  1  199 ? 11.888  -14.099 64.735 0.50 26.76  ? 212 GLU B OE2 1 
ATOM   4168 N  N   . THR B  1  200 ? 9.876   -17.363 60.970 1.00 30.97  ? 213 THR B N   1 
ATOM   4169 C  CA  . THR B  1  200 ? 10.844  -18.416 60.698 1.00 34.57  ? 213 THR B CA  1 
ATOM   4170 C  C   . THR B  1  200 ? 10.564  -19.133 59.379 1.00 33.75  ? 213 THR B C   1 
ATOM   4171 O  O   . THR B  1  200 ? 11.468  -19.803 58.864 1.00 34.04  ? 213 THR B O   1 
ATOM   4172 C  CB  . THR B  1  200 ? 10.955  -19.420 61.845 1.00 42.90  ? 213 THR B CB  1 
ATOM   4173 O  OG1 . THR B  1  200 ? 9.815   -20.267 61.813 1.00 42.91  ? 213 THR B OG1 1 
ATOM   4174 C  CG2 . THR B  1  200 ? 11.102  -18.752 63.196 1.00 41.14  ? 213 THR B CG2 1 
ATOM   4175 N  N   . VAL B  1  201 ? 9.352   -18.992 58.811 1.00 31.29  ? 214 VAL B N   1 
ATOM   4176 C  CA  . VAL B  1  201 ? 9.067   -19.593 57.513 1.00 30.06  ? 214 VAL B CA  1 
ATOM   4177 C  C   . VAL B  1  201 ? 9.089   -18.562 56.388 1.00 27.80  ? 214 VAL B C   1 
ATOM   4178 O  O   . VAL B  1  201 ? 9.188   -18.938 55.217 1.00 30.95  ? 214 VAL B O   1 
ATOM   4179 C  CB  . VAL B  1  201 ? 7.746   -20.388 57.497 1.00 33.21  ? 214 VAL B CB  1 
ATOM   4180 C  CG1 . VAL B  1  201 ? 7.819   -21.558 58.466 1.00 32.80  ? 214 VAL B CG1 1 
ATOM   4181 C  CG2 . VAL B  1  201 ? 6.521   -19.521 57.789 1.00 32.74  ? 214 VAL B CG2 1 
ATOM   4182 N  N   . PHE B  1  202 ? 9.047   -17.265 56.707 1.00 28.43  ? 215 PHE B N   1 
ATOM   4183 C  CA  . PHE B  1  202 ? 9.118   -16.260 55.648 1.00 29.38  ? 215 PHE B CA  1 
ATOM   4184 C  C   . PHE B  1  202 ? 10.354  -16.477 54.766 1.00 29.21  ? 215 PHE B C   1 
ATOM   4185 O  O   . PHE B  1  202 ? 10.277  -16.324 53.546 1.00 29.41  ? 215 PHE B O   1 
ATOM   4186 C  CB  . PHE B  1  202 ? 9.083   -14.824 56.178 1.00 29.92  ? 215 PHE B CB  1 
ATOM   4187 C  CG  . PHE B  1  202 ? 7.768   -14.393 56.813 1.00 31.10  ? 215 PHE B CG  1 
ATOM   4188 C  CD1 . PHE B  1  202 ? 6.595   -15.122 56.637 1.00 35.34  ? 215 PHE B CD1 1 
ATOM   4189 C  CD2 . PHE B  1  202 ? 7.703   -13.236 57.580 1.00 37.07  ? 215 PHE B CD2 1 
ATOM   4190 C  CE1 . PHE B  1  202 ? 5.400   -14.716 57.225 1.00 34.07  ? 215 PHE B CE1 1 
ATOM   4191 C  CE2 . PHE B  1  202 ? 6.509   -12.830 58.152 1.00 39.56  ? 215 PHE B CE2 1 
ATOM   4192 C  CZ  . PHE B  1  202 ? 5.353   -13.563 57.958 1.00 37.19  ? 215 PHE B CZ  1 
ATOM   4193 N  N   . PRO B  1  203 ? 11.541  -16.825 55.300 1.00 28.17  ? 216 PRO B N   1 
ATOM   4194 C  CA  . PRO B  1  203 ? 12.698  -17.063 54.439 1.00 30.42  ? 216 PRO B CA  1 
ATOM   4195 C  C   . PRO B  1  203 ? 12.466  -18.196 53.432 1.00 31.83  ? 216 PRO B C   1 
ATOM   4196 O  O   . PRO B  1  203 ? 12.977  -18.141 52.322 1.00 35.11  ? 216 PRO B O   1 
ATOM   4197 C  CB  . PRO B  1  203 ? 13.832  -17.362 55.428 1.00 31.50  ? 216 PRO B CB  1 
ATOM   4198 C  CG  . PRO B  1  203 ? 13.377  -16.753 56.724 1.00 30.29  ? 216 PRO B CG  1 
ATOM   4199 C  CD  . PRO B  1  203 ? 11.872  -16.949 56.726 1.00 31.35  ? 216 PRO B CD  1 
ATOM   4200 N  N   . ILE B  1  204 ? 11.684  -19.209 53.808 1.00 29.44  ? 217 ILE B N   1 
ATOM   4201 C  CA  . ILE B  1  204 ? 11.396  -20.323 52.915 1.00 31.98  ? 217 ILE B CA  1 
ATOM   4202 C  C   . ILE B  1  204 ? 10.360  -19.904 51.872 1.00 30.98  ? 217 ILE B C   1 
ATOM   4203 O  O   . ILE B  1  204 ? 10.528  -20.159 50.685 1.00 34.74  ? 217 ILE B O   1 
ATOM   4204 C  CB  . ILE B  1  204 ? 10.935  -21.556 53.712 1.00 33.13  ? 217 ILE B CB  1 
ATOM   4205 C  CG1 . ILE B  1  204 ? 11.996  -21.984 54.725 1.00 35.02  ? 217 ILE B CG1 1 
ATOM   4206 C  CG2 . ILE B  1  204 ? 10.557  -22.695 52.773 1.00 34.52  ? 217 ILE B CG2 1 
ATOM   4207 C  CD1 . ILE B  1  204 ? 11.489  -22.883 55.829 1.00 37.46  ? 217 ILE B CD1 1 
ATOM   4208 N  N   . ASN B  1  205 ? 9.284   -19.264 52.317 1.00 32.56  ? 218 ASN B N   1 
ATOM   4209 C  CA  . ASN B  1  205 ? 8.155   -18.997 51.445 1.00 29.65  ? 218 ASN B CA  1 
ATOM   4210 C  C   . ASN B  1  205 ? 8.398   -17.792 50.553 1.00 31.11  ? 218 ASN B C   1 
ATOM   4211 O  O   . ASN B  1  205 ? 7.835   -17.743 49.453 1.00 33.41  ? 218 ASN B O   1 
ATOM   4212 C  CB  . ASN B  1  205 ? 6.862   -18.800 52.226 1.00 31.89  ? 218 ASN B CB  1 
ATOM   4213 C  CG  . ASN B  1  205 ? 6.529   -20.013 53.054 1.00 31.57  ? 218 ASN B CG  1 
ATOM   4214 O  OD1 . ASN B  1  205 ? 6.923   -21.119 52.703 1.00 31.60  ? 218 ASN B OD1 1 
ATOM   4215 N  ND2 . ASN B  1  205 ? 5.866   -19.828 54.182 1.00 36.01  ? 218 ASN B ND2 1 
ATOM   4216 N  N   . LEU B  1  206 ? 9.205   -16.824 51.020 1.00 29.61  ? 219 LEU B N   1 
ATOM   4217 C  CA  . LEU B  1  206 ? 9.316   -15.547 50.330 1.00 29.27  ? 219 LEU B CA  1 
ATOM   4218 C  C   . LEU B  1  206 ? 10.735  -15.225 49.864 1.00 28.58  ? 219 LEU B C   1 
ATOM   4219 O  O   . LEU B  1  206 ? 10.875  -14.437 48.927 1.00 28.57  ? 219 LEU B O   1 
ATOM   4220 C  CB  . LEU B  1  206 ? 8.783   -14.460 51.256 1.00 29.78  ? 219 LEU B CB  1 
ATOM   4221 C  CG  . LEU B  1  206 ? 7.330   -14.624 51.701 1.00 32.97  ? 219 LEU B CG  1 
ATOM   4222 C  CD1 . LEU B  1  206 ? 7.017   -13.668 52.830 1.00 35.23  ? 219 LEU B CD1 1 
ATOM   4223 C  CD2 . LEU B  1  206 ? 6.391   -14.411 50.532 1.00 36.03  ? 219 LEU B CD2 1 
ATOM   4224 N  N   . PHE B  1  207 ? 11.774  -15.766 50.523 1.00 30.48  ? 220 PHE B N   1 
ATOM   4225 C  CA  . PHE B  1  207 ? 13.143  -15.422 50.149 1.00 31.80  ? 220 PHE B CA  1 
ATOM   4226 C  C   . PHE B  1  207 ? 13.733  -16.426 49.159 1.00 32.68  ? 220 PHE B C   1 
ATOM   4227 O  O   . PHE B  1  207 ? 14.761  -16.148 48.534 1.00 32.79  ? 220 PHE B O   1 
ATOM   4228 C  CB  . PHE B  1  207 ? 14.122  -15.335 51.318 1.00 32.61  ? 220 PHE B CB  1 
ATOM   4229 C  CG  . PHE B  1  207 ? 13.864  -14.198 52.295 1.00 33.05  ? 220 PHE B CG  1 
ATOM   4230 C  CD1 . PHE B  1  207 ? 12.989  -13.154 51.993 1.00 31.89  ? 220 PHE B CD1 1 
ATOM   4231 C  CD2 . PHE B  1  207 ? 14.538  -14.167 53.514 1.00 31.10  ? 220 PHE B CD2 1 
ATOM   4232 C  CE1 . PHE B  1  207 ? 12.789  -12.116 52.892 1.00 32.87  ? 220 PHE B CE1 1 
ATOM   4233 C  CE2 . PHE B  1  207 ? 14.300  -13.151 54.427 1.00 30.51  ? 220 PHE B CE2 1 
ATOM   4234 C  CZ  . PHE B  1  207 ? 13.430  -12.131 54.115 1.00 32.89  ? 220 PHE B CZ  1 
ATOM   4235 N  N   . VAL B  1  208 ? 13.119  -17.603 49.052 1.00 34.49  ? 221 VAL B N   1 
ATOM   4236 C  CA  . VAL B  1  208 ? 13.482  -18.563 48.026 1.00 31.95  ? 221 VAL B CA  1 
ATOM   4237 C  C   . VAL B  1  208 ? 12.835  -18.129 46.717 1.00 33.69  ? 221 VAL B C   1 
ATOM   4238 O  O   . VAL B  1  208 ? 11.666  -17.775 46.685 1.00 32.71  ? 221 VAL B O   1 
ATOM   4239 C  CB  . VAL B  1  208 ? 13.030  -19.981 48.434 1.00 33.74  ? 221 VAL B CB  1 
ATOM   4240 C  CG1 . VAL B  1  208 ? 13.258  -21.000 47.330 1.00 34.67  ? 221 VAL B CG1 1 
ATOM   4241 C  CG2 . VAL B  1  208 ? 13.727  -20.436 49.707 1.00 33.92  ? 221 VAL B CG2 1 
ATOM   4242 N  N   . ASP B  1  209 ? 13.613  -18.187 45.639 1.00 31.31  ? 222 ASP B N   1 
ATOM   4243 C  CA  . ASP B  1  209 ? 13.200  -17.720 44.335 1.00 32.37  ? 222 ASP B CA  1 
ATOM   4244 C  C   . ASP B  1  209 ? 11.923  -18.445 43.915 1.00 33.67  ? 222 ASP B C   1 
ATOM   4245 O  O   . ASP B  1  209 ? 11.799  -19.647 44.120 1.00 32.33  ? 222 ASP B O   1 
ATOM   4246 C  CB  . ASP B  1  209 ? 14.336  -17.920 43.347 1.00 34.51  ? 222 ASP B CB  1 
ATOM   4247 C  CG  . ASP B  1  209 ? 14.087  -17.322 41.983 1.00 34.99  ? 222 ASP B CG  1 
ATOM   4248 O  OD1 . ASP B  1  209 ? 13.227  -17.889 41.261 1.00 37.71  ? 222 ASP B OD1 1 
ATOM   4249 O  OD2 . ASP B  1  209 ? 14.731  -16.293 41.684 1.00 33.99  ? 222 ASP B OD2 1 
ATOM   4250 N  N   . GLY B  1  210 ? 10.990  -17.699 43.307 1.00 35.74  ? 223 GLY B N   1 
ATOM   4251 C  CA  . GLY B  1  210 ? 9.674   -18.225 42.966 1.00 39.65  ? 223 GLY B CA  1 
ATOM   4252 C  C   . GLY B  1  210 ? 9.705   -19.265 41.844 1.00 44.26  ? 223 GLY B C   1 
ATOM   4253 O  O   . GLY B  1  210 ? 8.732   -19.994 41.663 1.00 44.25  ? 223 GLY B O   1 
ATOM   4254 N  N   . ARG B  1  211 ? 10.815  -19.326 41.090 1.00 40.59  ? 224 ARG B N   1 
ATOM   4255 C  CA  . ARG B  1  211 ? 10.979  -20.340 40.061 1.00 43.01  ? 224 ARG B CA  1 
ATOM   4256 C  C   . ARG B  1  211 ? 11.354  -21.690 40.661 1.00 41.85  ? 224 ARG B C   1 
ATOM   4257 O  O   . ARG B  1  211 ? 11.346  -22.686 39.958 1.00 45.19  ? 224 ARG B O   1 
ATOM   4258 C  CB  . ARG B  1  211 ? 12.028  -19.932 39.022 1.00 41.61  ? 224 ARG B CB  1 
ATOM   4259 C  CG  . ARG B  1  211 ? 11.602  -18.719 38.211 1.00 40.98  ? 224 ARG B CG  1 
ATOM   4260 C  CD  . ARG B  1  211 ? 12.783  -18.151 37.467 1.00 43.98  ? 224 ARG B CD  1 
ATOM   4261 N  NE  . ARG B  1  211 ? 13.775  -17.594 38.399 1.00 46.41  ? 224 ARG B NE  1 
ATOM   4262 C  CZ  . ARG B  1  211 ? 14.851  -16.907 38.052 1.00 47.66  ? 224 ARG B CZ  1 
ATOM   4263 N  NH1 . ARG B  1  211 ? 15.133  -16.701 36.779 1.00 45.15  ? 224 ARG B NH1 1 
ATOM   4264 N  NH2 . ARG B  1  211 ? 15.659  -16.426 38.981 1.00 45.40  ? 224 ARG B NH2 1 
ATOM   4265 N  N   . VAL B  1  212 ? 11.669  -21.743 41.953 1.00 41.41  ? 225 VAL B N   1 
ATOM   4266 C  CA  . VAL B  1  212 ? 11.883  -23.011 42.627 1.00 43.65  ? 225 VAL B CA  1 
ATOM   4267 C  C   . VAL B  1  212 ? 10.534  -23.531 43.124 1.00 50.67  ? 225 VAL B C   1 
ATOM   4268 O  O   . VAL B  1  212 ? 9.978   -22.998 44.084 1.00 51.41  ? 225 VAL B O   1 
ATOM   4269 C  CB  . VAL B  1  212 ? 12.885  -22.855 43.787 1.00 44.51  ? 225 VAL B CB  1 
ATOM   4270 C  CG1 . VAL B  1  212 ? 13.101  -24.171 44.515 1.00 44.21  ? 225 VAL B CG1 1 
ATOM   4271 C  CG2 . VAL B  1  212 ? 14.217  -22.282 43.317 1.00 46.22  ? 225 VAL B CG2 1 
ATOM   4272 N  N   . THR B  1  213 ? 10.032  -24.604 42.497 1.00 58.27  ? 226 THR B N   1 
ATOM   4273 C  CA  . THR B  1  213 ? 8.708   -25.134 42.817 1.00 67.58  ? 226 THR B CA  1 
ATOM   4274 C  C   . THR B  1  213 ? 8.822   -26.311 43.788 1.00 67.32  ? 226 THR B C   1 
ATOM   4275 O  O   . THR B  1  213 ? 7.896   -26.582 44.546 1.00 64.22  ? 226 THR B O   1 
ATOM   4276 C  CB  . THR B  1  213 ? 7.980   -25.534 41.529 1.00 70.86  ? 226 THR B CB  1 
ATOM   4277 O  OG1 . THR B  1  213 ? 8.804   -26.477 40.849 1.00 70.62  ? 226 THR B OG1 1 
ATOM   4278 C  CG2 . THR B  1  213 ? 7.736   -24.351 40.609 1.00 69.68  ? 226 THR B CG2 1 
ATOM   4279 N  N   . THR B  1  214 ? 9.972   -26.989 43.785 1.00 71.40  ? 227 THR B N   1 
ATOM   4280 C  CA  . THR B  1  214 ? 10.137  -28.215 44.543 1.00 77.05  ? 227 THR B CA  1 
ATOM   4281 C  C   . THR B  1  214 ? 11.298  -28.086 45.538 1.00 68.75  ? 227 THR B C   1 
ATOM   4282 O  O   . THR B  1  214 ? 12.345  -27.528 45.221 1.00 64.46  ? 227 THR B O   1 
ATOM   4283 C  CB  . THR B  1  214 ? 10.340  -29.341 43.529 1.00 79.31  ? 227 THR B CB  1 
ATOM   4284 O  OG1 . THR B  1  214 ? 10.303  -30.519 44.329 1.00 80.90  ? 227 THR B OG1 1 
ATOM   4285 C  CG2 . THR B  1  214 ? 11.646  -29.237 42.754 1.00 80.70  ? 227 THR B CG2 1 
ATOM   4286 N  N   . ASP B  1  215 ? 11.097  -28.621 46.747 1.00 66.77  ? 228 ASP B N   1 
ATOM   4287 C  CA  . ASP B  1  215 ? 12.177  -28.762 47.715 1.00 68.63  ? 228 ASP B CA  1 
ATOM   4288 C  C   . ASP B  1  215 ? 12.745  -27.376 48.024 1.00 54.97  ? 228 ASP B C   1 
ATOM   4289 O  O   . ASP B  1  215 ? 13.922  -27.103 47.795 1.00 52.36  ? 228 ASP B O   1 
ATOM   4290 C  CB  . ASP B  1  215 ? 13.210  -29.757 47.201 1.00 83.11  ? 228 ASP B CB  1 
ATOM   4291 C  CG  . ASP B  1  215 ? 14.342  -30.134 48.149 1.00 101.36 ? 228 ASP B CG  1 
ATOM   4292 O  OD1 . ASP B  1  215 ? 14.441  -29.545 49.252 1.00 102.55 ? 228 ASP B OD1 1 
ATOM   4293 O  OD2 . ASP B  1  215 ? 15.117  -31.052 47.783 1.00 107.89 ? 228 ASP B OD2 1 
ATOM   4294 N  N   . ARG B  1  216 ? 11.875  -26.494 48.520 1.00 45.93  ? 229 ARG B N   1 
ATOM   4295 C  CA  . ARG B  1  216 ? 12.227  -25.100 48.689 1.00 40.04  ? 229 ARG B CA  1 
ATOM   4296 C  C   . ARG B  1  216 ? 13.185  -24.965 49.872 1.00 36.02  ? 229 ARG B C   1 
ATOM   4297 O  O   . ARG B  1  216 ? 12.920  -25.435 50.972 1.00 37.97  ? 229 ARG B O   1 
ATOM   4298 C  CB  . ARG B  1  216 ? 10.967  -24.233 48.767 1.00 41.24  ? 229 ARG B CB  1 
ATOM   4299 C  CG  . ARG B  1  216 ? 10.305  -24.072 47.401 1.00 47.16  ? 229 ARG B CG  1 
ATOM   4300 C  CD  . ARG B  1  216 ? 8.943   -23.390 47.470 1.00 49.31  ? 229 ARG B CD  1 
ATOM   4301 N  NE  . ARG B  1  216 ? 9.039   -22.000 47.925 1.00 50.73  ? 229 ARG B NE  1 
ATOM   4302 C  CZ  . ARG B  1  216 ? 9.472   -20.958 47.192 1.00 56.25  ? 229 ARG B CZ  1 
ATOM   4303 N  NH1 . ARG B  1  216 ? 9.723   -21.063 45.891 1.00 49.18  ? 229 ARG B NH1 1 
ATOM   4304 N  NH2 . ARG B  1  216 ? 9.624   -19.779 47.772 1.00 56.23  ? 229 ARG B NH2 1 
ATOM   4305 N  N   . LYS B  1  217 ? 14.314  -24.298 49.627 1.00 34.41  ? 230 LYS B N   1 
ATOM   4306 C  CA  . LYS B  1  217 ? 15.354  -24.182 50.634 1.00 35.03  ? 230 LYS B CA  1 
ATOM   4307 C  C   . LYS B  1  217 ? 16.196  -22.958 50.298 1.00 32.85  ? 230 LYS B C   1 
ATOM   4308 O  O   . LYS B  1  217 ? 16.390  -22.649 49.130 1.00 31.00  ? 230 LYS B O   1 
ATOM   4309 C  CB  . LYS B  1  217 ? 16.192  -25.471 50.633 1.00 36.99  ? 230 LYS B CB  1 
ATOM   4310 C  CG  . LYS B  1  217 ? 16.990  -25.699 49.361 1.00 36.77  ? 230 LYS B CG  1 
ATOM   4311 C  CD  . LYS B  1  217 ? 17.672  -27.060 49.254 1.00 41.83  ? 230 LYS B CD  1 
ATOM   4312 C  CE  . LYS B  1  217 ? 18.619  -27.061 48.076 1.00 45.31  ? 230 LYS B CE  1 
ATOM   4313 N  NZ  . LYS B  1  217 ? 19.142  -28.406 47.808 1.00 48.44  ? 230 LYS B NZ  1 
ATOM   4314 N  N   . LEU B  1  218 ? 16.712  -22.285 51.328 1.00 31.64  ? 231 LEU B N   1 
ATOM   4315 C  CA  . LEU B  1  218 ? 17.418  -21.031 51.123 1.00 28.81  ? 231 LEU B CA  1 
ATOM   4316 C  C   . LEU B  1  218 ? 18.916  -21.245 51.309 1.00 26.90  ? 231 LEU B C   1 
ATOM   4317 O  O   . LEU B  1  218 ? 19.340  -21.764 52.335 1.00 29.31  ? 231 LEU B O   1 
ATOM   4318 C  CB  . LEU B  1  218 ? 16.868  -20.009 52.110 1.00 27.59  ? 231 LEU B CB  1 
ATOM   4319 C  CG  . LEU B  1  218 ? 17.384  -18.580 51.946 1.00 29.44  ? 231 LEU B CG  1 
ATOM   4320 C  CD1 . LEU B  1  218 ? 16.931  -17.966 50.635 1.00 30.37  ? 231 LEU B CD1 1 
ATOM   4321 C  CD2 . LEU B  1  218 ? 16.923  -17.746 53.120 1.00 30.88  ? 231 LEU B CD2 1 
ATOM   4322 N  N   . SER B  1  219 ? 19.704  -20.782 50.340 1.00 29.78  ? 232 SER B N   1 
ATOM   4323 C  CA  . SER B  1  219 ? 21.161  -20.813 50.453 1.00 30.60  ? 232 SER B CA  1 
ATOM   4324 C  C   . SER B  1  219 ? 21.628  -19.768 51.453 1.00 28.64  ? 232 SER B C   1 
ATOM   4325 O  O   . SER B  1  219 ? 20.953  -18.762 51.693 1.00 31.05  ? 232 SER B O   1 
ATOM   4326 C  CB  . SER B  1  219 ? 21.798  -20.601 49.110 1.00 32.52  ? 232 SER B CB  1 
ATOM   4327 O  OG  . SER B  1  219 ? 21.702  -19.229 48.721 1.00 33.12  ? 232 SER B OG  1 
ATOM   4328 N  N   . MET B  1  220 ? 22.807  -19.990 52.028 1.00 29.59  ? 233 MET B N   1 
ATOM   4329 C  CA  . MET B  1  220 ? 23.351  -19.081 53.013 1.00 28.97  ? 233 MET B CA  1 
ATOM   4330 C  C   . MET B  1  220 ? 23.789  -17.789 52.325 1.00 29.74  ? 233 MET B C   1 
ATOM   4331 O  O   . MET B  1  220 ? 23.749  -16.730 52.946 1.00 29.17  ? 233 MET B O   1 
ATOM   4332 C  CB  . MET B  1  220 ? 24.501  -19.730 53.793 1.00 29.67  ? 233 MET B CB  1 
ATOM   4333 C  CG  . MET B  1  220 ? 24.087  -20.925 54.650 1.00 28.66  ? 233 MET B CG  1 
ATOM   4334 S  SD  . MET B  1  220 ? 22.753  -20.569 55.824 1.00 33.39  ? 233 MET B SD  1 
ATOM   4335 C  CE  . MET B  1  220 ? 21.377  -21.286 54.921 1.00 31.57  ? 233 MET B CE  1 
ATOM   4336 N  N   . GLU B  1  221 ? 24.165  -17.870 51.041 1.00 29.54  ? 234 GLU B N   1 
ATOM   4337 C  CA  . GLU B  1  221 ? 24.527  -16.689 50.269 1.00 31.96  ? 234 GLU B CA  1 
ATOM   4338 C  C   . GLU B  1  221 ? 23.314  -15.754 50.128 1.00 29.07  ? 234 GLU B C   1 
ATOM   4339 O  O   . GLU B  1  221 ? 23.424  -14.551 50.311 1.00 28.47  ? 234 GLU B O   1 
ATOM   4340 C  CB  . GLU B  1  221 ? 25.039  -17.080 48.882 1.00 32.20  ? 234 GLU B CB  1 
ATOM   4341 C  CG  . GLU B  1  221 ? 26.350  -17.871 48.897 1.00 39.41  ? 234 GLU B CG  1 
ATOM   4342 C  CD  . GLU B  1  221 ? 26.292  -19.373 49.211 1.00 44.41  ? 234 GLU B CD  1 
ATOM   4343 O  OE1 . GLU B  1  221 ? 25.213  -19.998 49.441 1.00 39.36  ? 234 GLU B OE1 1 
ATOM   4344 O  OE2 . GLU B  1  221 ? 27.402  -19.934 49.219 1.00 55.02  ? 234 GLU B OE2 1 
ATOM   4345 N  N   . ASP B  1  222 ? 22.165  -16.313 49.756 1.00 29.64  ? 235 ASP B N   1 
ATOM   4346 C  CA  . ASP B  1  222 ? 20.936  -15.545 49.580 1.00 30.79  ? 235 ASP B CA  1 
ATOM   4347 C  C   . ASP B  1  222 ? 20.448  -15.010 50.919 1.00 30.36  ? 235 ASP B C   1 
ATOM   4348 O  O   . ASP B  1  222 ? 20.021  -13.850 51.004 1.00 28.76  ? 235 ASP B O   1 
ATOM   4349 C  CB  . ASP B  1  222 ? 19.869  -16.360 48.873 1.00 30.94  ? 235 ASP B CB  1 
ATOM   4350 C  CG  . ASP B  1  222 ? 20.131  -16.622 47.393 1.00 34.31  ? 235 ASP B CG  1 
ATOM   4351 O  OD1 . ASP B  1  222 ? 21.142  -16.080 46.863 1.00 30.99  ? 235 ASP B OD1 1 
ATOM   4352 O  OD2 . ASP B  1  222 ? 19.310  -17.341 46.776 1.00 38.15  ? 235 ASP B OD2 1 
ATOM   4353 N  N   . ALA B  1  223 ? 20.536  -15.845 51.959 1.00 28.01  ? 236 ALA B N   1 
ATOM   4354 C  CA  . ALA B  1  223 ? 20.194  -15.407 53.304 1.00 29.09  ? 236 ALA B CA  1 
ATOM   4355 C  C   . ALA B  1  223 ? 21.045  -14.203 53.718 1.00 29.29  ? 236 ALA B C   1 
ATOM   4356 O  O   . ALA B  1  223 ? 20.513  -13.216 54.205 1.00 29.83  ? 236 ALA B O   1 
ATOM   4357 C  CB  . ALA B  1  223 ? 20.340  -16.556 54.282 1.00 30.15  ? 236 ALA B CB  1 
ATOM   4358 N  N   . ALA B  1  224 ? 22.366  -14.259 53.520 1.00 27.81  ? 237 ALA B N   1 
ATOM   4359 C  CA  . ALA B  1  224 ? 23.217  -13.155 53.947 1.00 28.19  ? 237 ALA B CA  1 
ATOM   4360 C  C   . ALA B  1  224 ? 22.879  -11.893 53.150 1.00 27.44  ? 237 ALA B C   1 
ATOM   4361 O  O   . ALA B  1  224 ? 22.827  -10.793 53.694 1.00 28.47  ? 237 ALA B O   1 
ATOM   4362 C  CB  . ALA B  1  224 ? 24.677  -13.494 53.805 1.00 28.43  ? 237 ALA B CB  1 
ATOM   4363 N  N   . SER B  1  225 ? 22.646  -12.069 51.854 1.00 26.70  ? 238 SER B N   1 
ATOM   4364 C  CA  . SER B  1  225 ? 22.344  -10.963 50.973 1.00 29.86  ? 238 SER B CA  1 
ATOM   4365 C  C   . SER B  1  225 ? 21.147  -10.166 51.508 1.00 29.60  ? 238 SER B C   1 
ATOM   4366 O  O   . SER B  1  225 ? 21.199  -8.933  51.587 1.00 29.75  ? 238 SER B O   1 
ATOM   4367 C  CB  . SER B  1  225 ? 22.143  -11.467 49.560 1.00 31.16  ? 238 SER B CB  1 
ATOM   4368 O  OG  . SER B  1  225 ? 21.896  -10.399 48.667 1.00 35.62  ? 238 SER B OG  1 
ATOM   4369 N  N   . ILE B  1  226 ? 20.099  -10.869 51.931 1.00 26.74  ? 239 ILE B N   1 
ATOM   4370 C  CA  . ILE B  1  226 ? 18.870  -10.236 52.389 1.00 29.92  ? 239 ILE B CA  1 
ATOM   4371 C  C   . ILE B  1  226 ? 18.992  -9.774  53.845 1.00 28.45  ? 239 ILE B C   1 
ATOM   4372 O  O   . ILE B  1  226 ? 18.735  -8.605  54.144 1.00 28.76  ? 239 ILE B O   1 
ATOM   4373 C  CB  . ILE B  1  226 ? 17.673  -11.177 52.168 1.00 28.39  ? 239 ILE B CB  1 
ATOM   4374 C  CG1 . ILE B  1  226 ? 17.429  -11.373 50.681 1.00 28.43  ? 239 ILE B CG1 1 
ATOM   4375 C  CG2 . ILE B  1  226 ? 16.419  -10.645 52.865 1.00 30.62  ? 239 ILE B CG2 1 
ATOM   4376 C  CD1 . ILE B  1  226 ? 16.540  -12.552 50.345 1.00 31.51  ? 239 ILE B CD1 1 
ATOM   4377 N  N   . PHE B  1  227 ? 19.374  -10.684 54.752 1.00 27.93  ? 240 PHE B N   1 
ATOM   4378 C  CA  . PHE B  1  227 ? 19.411  -10.384 56.179 1.00 27.45  ? 240 PHE B CA  1 
ATOM   4379 C  C   . PHE B  1  227 ? 20.482  -9.342  56.523 1.00 28.67  ? 240 PHE B C   1 
ATOM   4380 O  O   . PHE B  1  227 ? 20.281  -8.525  57.422 1.00 29.93  ? 240 PHE B O   1 
ATOM   4381 C  CB  . PHE B  1  227 ? 19.655  -11.650 56.997 1.00 30.41  ? 240 PHE B CB  1 
ATOM   4382 C  CG  . PHE B  1  227 ? 18.477  -12.597 57.167 1.00 30.38  ? 240 PHE B CG  1 
ATOM   4383 C  CD1 . PHE B  1  227 ? 17.460  -12.312 58.065 1.00 31.23  ? 240 PHE B CD1 1 
ATOM   4384 C  CD2 . PHE B  1  227 ? 18.446  -13.819 56.526 1.00 36.10  ? 240 PHE B CD2 1 
ATOM   4385 C  CE1 . PHE B  1  227 ? 16.419  -13.210 58.269 1.00 29.26  ? 240 PHE B CE1 1 
ATOM   4386 C  CE2 . PHE B  1  227 ? 17.401  -14.703 56.721 1.00 38.73  ? 240 PHE B CE2 1 
ATOM   4387 C  CZ  . PHE B  1  227 ? 16.390  -14.392 57.597 1.00 35.66  ? 240 PHE B CZ  1 
ATOM   4388 N  N   . ARG B  1  228 ? 21.647  -9.419  55.869 1.00 27.51  ? 241 ARG B N   1 
ATOM   4389 C  CA  . ARG B  1  228 ? 22.758  -8.542  56.198 1.00 26.72  ? 241 ARG B CA  1 
ATOM   4390 C  C   . ARG B  1  228 ? 22.766  -7.347  55.252 1.00 28.09  ? 241 ARG B C   1 
ATOM   4391 O  O   . ARG B  1  228 ? 22.807  -6.221  55.711 1.00 28.50  ? 241 ARG B O   1 
ATOM   4392 C  CB  . ARG B  1  228 ? 24.103  -9.268  56.212 1.00 27.29  ? 241 ARG B CB  1 
ATOM   4393 C  CG  . ARG B  1  228 ? 25.284  -8.388  56.608 1.00 28.98  ? 241 ARG B CG  1 
ATOM   4394 C  CD  . ARG B  1  228 ? 26.602  -9.109  56.826 1.00 31.47  ? 241 ARG B CD  1 
ATOM   4395 N  NE  . ARG B  1  228 ? 27.108  -9.768  55.620 1.00 31.90  ? 241 ARG B NE  1 
ATOM   4396 C  CZ  . ARG B  1  228 ? 27.378  -11.062 55.453 1.00 32.81  ? 241 ARG B CZ  1 
ATOM   4397 N  NH1 . ARG B  1  228 ? 27.220  -11.937 56.436 1.00 35.58  ? 241 ARG B NH1 1 
ATOM   4398 N  NH2 . ARG B  1  228 ? 27.826  -11.489 54.283 1.00 33.04  ? 241 ARG B NH2 1 
ATOM   4399 N  N   . ASP B  1  229 ? 22.729  -7.584  53.936 1.00 29.92  ? 242 ASP B N   1 
ATOM   4400 C  CA  . ASP B  1  229 ? 23.002  -6.504  53.001 1.00 28.72  ? 242 ASP B CA  1 
ATOM   4401 C  C   . ASP B  1  229 ? 21.740  -5.785  52.509 1.00 27.76  ? 242 ASP B C   1 
ATOM   4402 O  O   . ASP B  1  229 ? 21.854  -4.774  51.820 1.00 27.27  ? 242 ASP B O   1 
ATOM   4403 C  CB  . ASP B  1  229 ? 23.849  -7.011  51.847 1.00 30.52  ? 242 ASP B CB  1 
ATOM   4404 C  CG  . ASP B  1  229 ? 25.229  -7.521  52.218 1.00 31.99  ? 242 ASP B CG  1 
ATOM   4405 O  OD1 . ASP B  1  229 ? 25.777  -7.111  53.289 1.00 30.18  ? 242 ASP B OD1 1 
ATOM   4406 O  OD2 . ASP B  1  229 ? 25.722  -8.371  51.442 1.00 30.73  ? 242 ASP B OD2 1 
ATOM   4407 N  N   . MET B  1  230 ? 20.542  -6.312  52.817 1.00 27.33  ? 243 MET B N   1 
ATOM   4408 C  CA  A MET B  1  230 ? 19.295  -5.713  52.362 0.50 28.48  ? 243 MET B CA  1 
ATOM   4409 C  CA  B MET B  1  230 ? 19.293  -5.713  52.362 0.50 27.86  ? 243 MET B CA  1 
ATOM   4410 C  C   . MET B  1  230 ? 19.228  -5.708  50.838 1.00 28.60  ? 243 MET B C   1 
ATOM   4411 O  O   . MET B  1  230 ? 18.755  -4.744  50.232 1.00 29.35  ? 243 MET B O   1 
ATOM   4412 C  CB  A MET B  1  230 ? 19.148  -4.273  52.869 0.50 30.11  ? 243 MET B CB  1 
ATOM   4413 C  CB  B MET B  1  230 ? 19.143  -4.275  52.872 0.50 28.50  ? 243 MET B CB  1 
ATOM   4414 C  CG  A MET B  1  230 ? 19.385  -4.125  54.358 0.50 32.03  ? 243 MET B CG  1 
ATOM   4415 C  CG  B MET B  1  230 ? 19.404  -4.135  54.362 0.50 29.21  ? 243 MET B CG  1 
ATOM   4416 S  SD  A MET B  1  230 ? 19.414  -2.402  54.892 0.50 35.21  ? 243 MET B SD  1 
ATOM   4417 S  SD  B MET B  1  230 ? 19.319  -2.425  54.923 0.50 30.63  ? 243 MET B SD  1 
ATOM   4418 C  CE  A MET B  1  230 ? 21.207  -2.268  54.981 0.50 39.20  ? 243 MET B CE  1 
ATOM   4419 C  CE  B MET B  1  230 ? 20.788  -1.756  54.129 0.50 28.24  ? 243 MET B CE  1 
ATOM   4420 N  N   . ARG B  1  231 ? 19.694  -6.814  50.232 1.00 29.32  ? 244 ARG B N   1 
ATOM   4421 C  CA  A ARG B  1  231 ? 19.853  -6.904  48.789 0.50 27.02  ? 244 ARG B CA  1 
ATOM   4422 C  CA  B ARG B  1  231 ? 19.845  -6.902  48.789 0.50 27.74  ? 244 ARG B CA  1 
ATOM   4423 C  C   . ARG B  1  231 ? 19.202  -8.190  48.293 1.00 27.36  ? 244 ARG B C   1 
ATOM   4424 O  O   . ARG B  1  231 ? 19.484  -9.272  48.805 1.00 27.28  ? 244 ARG B O   1 
ATOM   4425 C  CB  A ARG B  1  231 ? 21.343  -6.857  48.426 0.50 28.25  ? 244 ARG B CB  1 
ATOM   4426 C  CB  B ARG B  1  231 ? 21.338  -6.850  48.446 0.50 30.10  ? 244 ARG B CB  1 
ATOM   4427 C  CG  A ARG B  1  231 ? 21.638  -6.810  46.931 0.50 29.65  ? 244 ARG B CG  1 
ATOM   4428 C  CG  B ARG B  1  231 ? 21.681  -6.813  46.963 0.50 32.75  ? 244 ARG B CG  1 
ATOM   4429 C  CD  A ARG B  1  231 ? 23.131  -6.889  46.566 0.50 29.48  ? 244 ARG B CD  1 
ATOM   4430 C  CD  B ARG B  1  231 ? 23.207  -6.738  46.759 0.50 33.27  ? 244 ARG B CD  1 
ATOM   4431 N  NE  A ARG B  1  231 ? 23.646  -8.258  46.704 0.50 32.22  ? 244 ARG B NE  1 
ATOM   4432 N  NE  B ARG B  1  231 ? 23.832  -7.966  47.264 0.50 38.07  ? 244 ARG B NE  1 
ATOM   4433 C  CZ  A ARG B  1  231 ? 23.400  -9.282  45.891 0.50 35.44  ? 244 ARG B CZ  1 
ATOM   4434 C  CZ  B ARG B  1  231 ? 24.747  -8.084  48.237 0.50 37.32  ? 244 ARG B CZ  1 
ATOM   4435 N  NH1 A ARG B  1  231 ? 22.873  -9.062  44.692 0.50 39.15  ? 244 ARG B NH1 1 
ATOM   4436 N  NH1 B ARG B  1  231 ? 25.428  -7.042  48.683 0.50 35.01  ? 244 ARG B NH1 1 
ATOM   4437 N  NH2 A ARG B  1  231 ? 23.692  -10.516 46.274 0.50 33.91  ? 244 ARG B NH2 1 
ATOM   4438 N  NH2 B ARG B  1  231 ? 25.007  -9.281  48.712 0.50 33.25  ? 244 ARG B NH2 1 
ATOM   4439 N  N   . PHE B  1  232 ? 18.333  -8.062  47.283 1.00 26.69  ? 245 PHE B N   1 
ATOM   4440 C  CA  . PHE B  1  232 ? 17.800  -9.222  46.600 1.00 28.83  ? 245 PHE B CA  1 
ATOM   4441 C  C   . PHE B  1  232 ? 18.941  -10.024 45.979 1.00 29.02  ? 245 PHE B C   1 
ATOM   4442 O  O   . PHE B  1  232 ? 19.885  -9.452  45.444 1.00 26.53  ? 245 PHE B O   1 
ATOM   4443 C  CB  . PHE B  1  232 ? 16.870  -8.816  45.460 1.00 30.44  ? 245 PHE B CB  1 
ATOM   4444 C  CG  . PHE B  1  232 ? 15.502  -8.306  45.890 1.00 28.28  ? 245 PHE B CG  1 
ATOM   4445 C  CD1 . PHE B  1  232 ? 14.619  -9.139  46.543 1.00 30.75  ? 245 PHE B CD1 1 
ATOM   4446 C  CD2 . PHE B  1  232 ? 15.082  -7.022  45.571 1.00 33.92  ? 245 PHE B CD2 1 
ATOM   4447 C  CE1 . PHE B  1  232 ? 13.350  -8.695  46.891 1.00 31.20  ? 245 PHE B CE1 1 
ATOM   4448 C  CE2 . PHE B  1  232 ? 13.805  -6.579  45.906 1.00 34.81  ? 245 PHE B CE2 1 
ATOM   4449 C  CZ  . PHE B  1  232 ? 12.949  -7.419  46.571 1.00 31.77  ? 245 PHE B CZ  1 
ATOM   4450 N  N   . PRO B  1  233 ? 18.877  -11.368 45.972 1.00 27.19  ? 246 PRO B N   1 
ATOM   4451 C  CA  . PRO B  1  233 ? 19.777  -12.147 45.123 1.00 27.90  ? 246 PRO B CA  1 
ATOM   4452 C  C   . PRO B  1  233 ? 19.708  -11.668 43.675 1.00 30.13  ? 246 PRO B C   1 
ATOM   4453 O  O   . PRO B  1  233 ? 18.686  -11.151 43.225 1.00 33.24  ? 246 PRO B O   1 
ATOM   4454 C  CB  . PRO B  1  233 ? 19.242  -13.598 45.275 1.00 29.23  ? 246 PRO B CB  1 
ATOM   4455 C  CG  . PRO B  1  233 ? 18.556  -13.599 46.620 1.00 28.87  ? 246 PRO B CG  1 
ATOM   4456 C  CD  . PRO B  1  233 ? 17.958  -12.193 46.768 1.00 28.44  ? 246 PRO B CD  1 
ATOM   4457 N  N   . ASP B  1  234 ? 20.814  -11.829 42.943 1.00 29.14  ? 247 ASP B N   1 
ATOM   4458 C  CA  . ASP B  1  234 ? 20.832  -11.547 41.524 1.00 32.34  ? 247 ASP B CA  1 
ATOM   4459 C  C   . ASP B  1  234 ? 19.658  -12.263 40.845 1.00 32.95  ? 247 ASP B C   1 
ATOM   4460 O  O   . ASP B  1  234 ? 19.396  -13.429 41.125 1.00 30.14  ? 247 ASP B O   1 
ATOM   4461 C  CB  . ASP B  1  234 ? 22.151  -11.980 40.901 1.00 34.31  ? 247 ASP B CB  1 
ATOM   4462 C  CG  . ASP B  1  234 ? 23.360  -11.102 41.215 1.00 35.43  ? 247 ASP B CG  1 
ATOM   4463 O  OD1 . ASP B  1  234 ? 23.238  -10.137 42.015 1.00 33.39  ? 247 ASP B OD1 1 
ATOM   4464 O  OD2 . ASP B  1  234 ? 24.438  -11.388 40.645 1.00 32.10  ? 247 ASP B OD2 1 
ATOM   4465 N  N   . ASP B  1  235 ? 18.973  -11.555 39.946 1.00 34.05  ? 248 ASP B N   1 
ATOM   4466 C  CA  . ASP B  1  235 ? 17.921  -12.126 39.111 1.00 36.17  ? 248 ASP B CA  1 
ATOM   4467 C  C   . ASP B  1  235 ? 16.747  -12.661 39.944 1.00 36.19  ? 248 ASP B C   1 
ATOM   4468 O  O   . ASP B  1  235 ? 16.037  -13.562 39.504 1.00 33.17  ? 248 ASP B O   1 
ATOM   4469 C  CB  . ASP B  1  235 ? 18.471  -13.214 38.196 1.00 37.33  ? 248 ASP B CB  1 
ATOM   4470 C  CG  . ASP B  1  235 ? 17.515  -13.653 37.089 1.00 38.65  ? 248 ASP B CG  1 
ATOM   4471 O  OD1 . ASP B  1  235 ? 16.944  -12.759 36.434 1.00 39.54  ? 248 ASP B OD1 1 
ATOM   4472 O  OD2 . ASP B  1  235 ? 17.328  -14.882 36.903 1.00 38.89  ? 248 ASP B OD2 1 
ATOM   4473 N  N   . PHE B  1  236 ? 16.520  -12.108 41.140 1.00 32.49  ? 249 PHE B N   1 
ATOM   4474 C  CA  . PHE B  1  236 ? 15.539  -12.677 42.044 1.00 31.84  ? 249 PHE B CA  1 
ATOM   4475 C  C   . PHE B  1  236 ? 14.127  -12.556 41.464 1.00 29.23  ? 249 PHE B C   1 
ATOM   4476 O  O   . PHE B  1  236 ? 13.687  -11.470 41.113 1.00 26.70  ? 249 PHE B O   1 
ATOM   4477 C  CB  . PHE B  1  236 ? 15.580  -11.977 43.402 1.00 31.07  ? 249 PHE B CB  1 
ATOM   4478 C  CG  . PHE B  1  236 ? 14.593  -12.562 44.397 1.00 29.95  ? 249 PHE B CG  1 
ATOM   4479 C  CD1 . PHE B  1  236 ? 14.832  -13.789 44.981 1.00 31.56  ? 249 PHE B CD1 1 
ATOM   4480 C  CD2 . PHE B  1  236 ? 13.459  -11.860 44.783 1.00 33.55  ? 249 PHE B CD2 1 
ATOM   4481 C  CE1 . PHE B  1  236 ? 13.946  -14.310 45.907 1.00 33.67  ? 249 PHE B CE1 1 
ATOM   4482 C  CE2 . PHE B  1  236 ? 12.569  -12.397 45.706 1.00 32.13  ? 249 PHE B CE2 1 
ATOM   4483 C  CZ  . PHE B  1  236 ? 12.830  -13.610 46.269 1.00 29.78  ? 249 PHE B CZ  1 
ATOM   4484 N  N   . HIS B  1  237 ? 13.418  -13.682 41.451 1.00 31.20  ? 250 HIS B N   1 
ATOM   4485 C  CA  . HIS B  1  237 ? 12.002  -13.727 41.098 1.00 33.46  ? 250 HIS B CA  1 
ATOM   4486 C  C   . HIS B  1  237 ? 11.202  -14.037 42.360 1.00 33.96  ? 250 HIS B C   1 
ATOM   4487 O  O   . HIS B  1  237 ? 11.503  -14.993 43.071 1.00 33.12  ? 250 HIS B O   1 
ATOM   4488 C  CB  . HIS B  1  237 ? 11.722  -14.808 40.048 1.00 34.88  ? 250 HIS B CB  1 
ATOM   4489 C  CG  . HIS B  1  237 ? 12.206  -14.474 38.677 1.00 38.45  ? 250 HIS B CG  1 
ATOM   4490 N  ND1 . HIS B  1  237 ? 13.485  -14.035 38.433 1.00 39.74  ? 250 HIS B ND1 1 
ATOM   4491 C  CD2 . HIS B  1  237 ? 11.587  -14.520 37.470 1.00 42.18  ? 250 HIS B CD2 1 
ATOM   4492 C  CE1 . HIS B  1  237 ? 13.624  -13.802 37.129 1.00 42.49  ? 250 HIS B CE1 1 
ATOM   4493 N  NE2 . HIS B  1  237 ? 12.478  -14.075 36.530 1.00 42.08  ? 250 HIS B NE2 1 
ATOM   4494 N  N   . ARG B  1  238 ? 10.165  -13.237 42.603 1.00 30.95  ? 251 ARG B N   1 
ATOM   4495 C  CA  . ARG B  1  238 ? 9.309   -13.422 43.765 1.00 32.80  ? 251 ARG B CA  1 
ATOM   4496 C  C   . ARG B  1  238 ? 8.531   -14.728 43.670 1.00 33.27  ? 251 ARG B C   1 
ATOM   4497 O  O   . ARG B  1  238 ? 8.419   -15.296 42.592 1.00 32.86  ? 251 ARG B O   1 
ATOM   4498 C  CB  . ARG B  1  238 ? 8.330   -12.256 43.891 1.00 31.22  ? 251 ARG B CB  1 
ATOM   4499 C  CG  . ARG B  1  238 ? 7.293   -12.201 42.778 1.00 34.31  ? 251 ARG B CG  1 
ATOM   4500 C  CD  . ARG B  1  238 ? 6.357   -11.033 42.948 1.00 35.05  ? 251 ARG B CD  1 
ATOM   4501 N  NE  . ARG B  1  238 ? 5.163   -11.253 42.138 1.00 36.96  ? 251 ARG B NE  1 
ATOM   4502 C  CZ  . ARG B  1  238 ? 4.199   -10.376 41.903 1.00 40.98  ? 251 ARG B CZ  1 
ATOM   4503 N  NH1 . ARG B  1  238 ? 4.226   -9.189  42.464 1.00 41.90  ? 251 ARG B NH1 1 
ATOM   4504 N  NH2 . ARG B  1  238 ? 3.208   -10.693 41.096 1.00 45.84  ? 251 ARG B NH2 1 
ATOM   4505 N  N   . SER B  1  239 ? 7.990   -15.159 44.817 1.00 31.83  ? 252 SER B N   1 
ATOM   4506 C  CA  . SER B  1  239 ? 7.073   -16.279 44.920 1.00 33.81  ? 252 SER B CA  1 
ATOM   4507 C  C   . SER B  1  239 ? 6.052   -16.245 43.782 1.00 33.19  ? 252 SER B C   1 
ATOM   4508 O  O   . SER B  1  239 ? 5.571   -15.169 43.424 1.00 32.17  ? 252 SER B O   1 
ATOM   4509 C  CB  . SER B  1  239 ? 6.364   -16.268 46.254 1.00 33.77  ? 252 SER B CB  1 
ATOM   4510 O  OG  . SER B  1  239 ? 5.379   -17.291 46.332 1.00 35.18  ? 252 SER B OG  1 
ATOM   4511 N  N   . ALA B  1  240 ? 5.744   -17.440 43.238 1.00 34.52  ? 253 ALA B N   1 
ATOM   4512 C  CA  . ALA B  1  240 ? 4.833   -17.591 42.108 1.00 37.57  ? 253 ALA B CA  1 
ATOM   4513 C  C   . ALA B  1  240 ? 3.373   -17.446 42.554 1.00 41.27  ? 253 ALA B C   1 
ATOM   4514 O  O   . ALA B  1  240 ? 2.499   -17.336 41.709 1.00 40.27  ? 253 ALA B O   1 
ATOM   4515 C  CB  . ALA B  1  240 ? 5.056   -18.937 41.443 1.00 38.24  ? 253 ALA B CB  1 
ATOM   4516 N  N   . VAL B  1  241 ? 3.125   -17.467 43.875 1.00 42.41  ? 254 VAL B N   1 
ATOM   4517 C  CA  . VAL B  1  241 ? 1.805   -17.277 44.454 1.00 43.20  ? 254 VAL B CA  1 
ATOM   4518 C  C   . VAL B  1  241 ? 1.911   -16.352 45.664 1.00 41.18  ? 254 VAL B C   1 
ATOM   4519 O  O   . VAL B  1  241 ? 2.943   -16.312 46.336 1.00 37.55  ? 254 VAL B O   1 
ATOM   4520 C  CB  . VAL B  1  241 ? 1.182   -18.617 44.889 1.00 45.61  ? 254 VAL B CB  1 
ATOM   4521 C  CG1 . VAL B  1  241 ? 0.857   -19.520 43.699 1.00 48.85  ? 254 VAL B CG1 1 
ATOM   4522 C  CG2 . VAL B  1  241 ? 2.060   -19.346 45.895 1.00 44.20  ? 254 VAL B CG2 1 
ATOM   4523 N  N   . PRO B  1  242 ? 0.838   -15.602 46.005 1.00 39.38  ? 255 PRO B N   1 
ATOM   4524 C  CA  . PRO B  1  242 ? 0.786   -14.875 47.274 1.00 34.54  ? 255 PRO B CA  1 
ATOM   4525 C  C   . PRO B  1  242 ? 1.091   -15.856 48.397 1.00 36.09  ? 255 PRO B C   1 
ATOM   4526 O  O   . PRO B  1  242 ? 0.612   -16.986 48.373 1.00 34.57  ? 255 PRO B O   1 
ATOM   4527 C  CB  . PRO B  1  242 ? -0.644  -14.329 47.316 1.00 37.28  ? 255 PRO B CB  1 
ATOM   4528 C  CG  . PRO B  1  242 ? -1.006  -14.185 45.845 1.00 36.22  ? 255 PRO B CG  1 
ATOM   4529 C  CD  . PRO B  1  242 ? -0.375  -15.394 45.184 1.00 37.29  ? 255 PRO B CD  1 
ATOM   4530 N  N   . ALA B  1  243 ? 1.937   -15.447 49.356 1.00 34.45  ? 256 ALA B N   1 
ATOM   4531 C  CA  . ALA B  1  243 ? 2.323   -16.355 50.424 1.00 31.91  ? 256 ALA B CA  1 
ATOM   4532 C  C   . ALA B  1  243 ? 2.660   -15.570 51.685 1.00 31.47  ? 256 ALA B C   1 
ATOM   4533 O  O   . ALA B  1  243 ? 2.861   -14.357 51.627 1.00 33.93  ? 256 ALA B O   1 
ATOM   4534 C  CB  . ALA B  1  243 ? 3.503   -17.188 49.971 1.00 34.02  ? 256 ALA B CB  1 
ATOM   4535 N  N   . SER B  1  244 ? 2.736   -16.292 52.806 1.00 33.12  ? 257 SER B N   1 
ATOM   4536 C  CA  . SER B  1  244 ? 3.057   -15.702 54.095 1.00 35.59  ? 257 SER B CA  1 
ATOM   4537 C  C   . SER B  1  244 ? 3.608   -16.778 55.021 1.00 35.26  ? 257 SER B C   1 
ATOM   4538 O  O   . SER B  1  244 ? 4.768   -17.154 54.879 1.00 35.93  ? 257 SER B O   1 
ATOM   4539 C  CB  . SER B  1  244 ? 1.857   -14.978 54.681 1.00 37.32  ? 257 SER B CB  1 
ATOM   4540 O  OG  . SER B  1  244 ? 0.755   -15.854 54.806 1.00 35.72  ? 257 SER B OG  1 
ATOM   4541 N  N   . ASN B  1  245 ? 2.763   -17.334 55.903 1.00 36.10  ? 258 ASN B N   1 
ATOM   4542 C  CA  . ASN B  1  245 ? 3.236   -18.137 57.018 1.00 35.36  ? 258 ASN B CA  1 
ATOM   4543 C  C   . ASN B  1  245 ? 2.940   -19.621 56.829 1.00 35.34  ? 258 ASN B C   1 
ATOM   4544 O  O   . ASN B  1  245 ? 2.838   -20.339 57.818 1.00 33.79  ? 258 ASN B O   1 
ATOM   4545 C  CB  . ASN B  1  245 ? 2.628   -17.672 58.337 1.00 38.90  ? 258 ASN B CB  1 
ATOM   4546 C  CG  . ASN B  1  245 ? 1.136   -17.907 58.371 1.00 42.96  ? 258 ASN B CG  1 
ATOM   4547 O  OD1 . ASN B  1  245 ? 0.511   -18.120 57.326 1.00 42.10  ? 258 ASN B OD1 1 
ATOM   4548 N  ND2 . ASN B  1  245 ? 0.550   -17.882 59.557 1.00 51.28  ? 258 ASN B ND2 1 
ATOM   4549 N  N   . GLU B  1  246 ? 2.871   -20.100 55.585 1.00 34.85  ? 259 GLU B N   1 
ATOM   4550 C  CA  . GLU B  1  246 ? 2.695   -21.526 55.336 1.00 40.82  ? 259 GLU B CA  1 
ATOM   4551 C  C   . GLU B  1  246 ? 3.813   -22.318 56.024 1.00 39.77  ? 259 GLU B C   1 
ATOM   4552 O  O   . GLU B  1  246 ? 4.993   -22.022 55.838 1.00 38.13  ? 259 GLU B O   1 
ATOM   4553 C  CB  . GLU B  1  246 ? 2.623   -21.854 53.844 1.00 40.60  ? 259 GLU B CB  1 
ATOM   4554 C  CG  . GLU B  1  246 ? 1.390   -21.273 53.153 1.00 44.46  ? 259 GLU B CG  1 
ATOM   4555 C  CD  . GLU B  1  246 ? 1.472   -19.813 52.729 1.00 47.78  ? 259 GLU B CD  1 
ATOM   4556 O  OE1 . GLU B  1  246 ? 2.467   -19.118 53.056 1.00 41.15  ? 259 GLU B OE1 1 
ATOM   4557 O  OE2 . GLU B  1  246 ? 0.525   -19.364 52.041 1.00 47.06  ? 259 GLU B OE2 1 
ATOM   4558 N  N   . GLY B  1  247 ? 3.417   -23.311 56.840 1.00 35.96  ? 260 GLY B N   1 
ATOM   4559 C  CA  . GLY B  1  247 ? 4.328   -24.221 57.513 1.00 35.91  ? 260 GLY B CA  1 
ATOM   4560 C  C   . GLY B  1  247 ? 4.667   -23.793 58.941 1.00 37.25  ? 260 GLY B C   1 
ATOM   4561 O  O   . GLY B  1  247 ? 5.344   -24.524 59.657 1.00 38.68  ? 260 GLY B O   1 
ATOM   4562 N  N   . ALA B  1  248 ? 4.199   -22.623 59.378 1.00 34.47  ? 261 ALA B N   1 
ATOM   4563 C  CA  . ALA B  1  248 ? 4.497   -22.166 60.729 1.00 38.09  ? 261 ALA B CA  1 
ATOM   4564 C  C   . ALA B  1  248 ? 3.949   -23.134 61.781 1.00 38.82  ? 261 ALA B C   1 
ATOM   4565 O  O   . ALA B  1  248 ? 4.548   -23.292 62.852 1.00 36.67  ? 261 ALA B O   1 
ATOM   4566 C  CB  . ALA B  1  248 ? 3.958   -20.770 60.941 1.00 36.29  ? 261 ALA B CB  1 
ATOM   4567 N  N   . ASP B  1  249 ? 2.802   -23.756 61.477 1.00 38.71  ? 262 ASP B N   1 
ATOM   4568 C  CA  . ASP B  1  249 ? 2.208   -24.770 62.338 1.00 44.81  ? 262 ASP B CA  1 
ATOM   4569 C  C   . ASP B  1  249 ? 3.183   -25.930 62.567 1.00 41.78  ? 262 ASP B C   1 
ATOM   4570 O  O   . ASP B  1  249 ? 3.250   -26.468 63.669 1.00 40.98  ? 262 ASP B O   1 
ATOM   4571 C  CB  . ASP B  1  249 ? 0.876   -25.267 61.783 1.00 48.15  ? 262 ASP B CB  1 
ATOM   4572 C  CG  . ASP B  1  249 ? 0.887   -25.772 60.341 1.00 59.89  ? 262 ASP B CG  1 
ATOM   4573 O  OD1 . ASP B  1  249 ? 1.891   -25.531 59.616 1.00 58.60  ? 262 ASP B OD1 1 
ATOM   4574 O  OD2 . ASP B  1  249 ? -0.129  -26.375 59.930 1.00 63.90  ? 262 ASP B OD2 1 
ATOM   4575 N  N   . GLN B  1  250 ? 3.916   -26.329 61.521 1.00 38.35  ? 263 GLN B N   1 
ATOM   4576 C  CA  . GLN B  1  250 ? 4.854   -27.437 61.621 1.00 41.67  ? 263 GLN B CA  1 
ATOM   4577 C  C   . GLN B  1  250 ? 6.079   -27.058 62.450 1.00 41.08  ? 263 GLN B C   1 
ATOM   4578 O  O   . GLN B  1  250 ? 6.680   -27.914 63.088 1.00 42.07  ? 263 GLN B O   1 
ATOM   4579 C  CB  . GLN B  1  250 ? 5.324   -27.897 60.248 1.00 44.69  ? 263 GLN B CB  1 
ATOM   4580 C  CG  . GLN B  1  250 ? 4.224   -28.496 59.381 1.00 46.32  ? 263 GLN B CG  1 
ATOM   4581 C  CD  . GLN B  1  250 ? 4.775   -29.046 58.087 1.00 48.23  ? 263 GLN B CD  1 
ATOM   4582 O  OE1 . GLN B  1  250 ? 5.719   -29.843 58.097 1.00 53.34  ? 263 GLN B OE1 1 
ATOM   4583 N  NE2 . GLN B  1  250 ? 4.238   -28.590 56.965 1.00 46.79  ? 263 GLN B NE2 1 
ATOM   4584 N  N   . VAL B  1  251 ? 6.455   -25.773 62.429 1.00 38.16  ? 264 VAL B N   1 
ATOM   4585 C  CA  . VAL B  1  251 ? 7.585   -25.296 63.201 1.00 36.97  ? 264 VAL B CA  1 
ATOM   4586 C  C   . VAL B  1  251 ? 7.255   -25.427 64.685 1.00 40.63  ? 264 VAL B C   1 
ATOM   4587 O  O   . VAL B  1  251 ? 8.081   -25.896 65.468 1.00 37.61  ? 264 VAL B O   1 
ATOM   4588 C  CB  . VAL B  1  251 ? 7.957   -23.855 62.806 1.00 36.51  ? 264 VAL B CB  1 
ATOM   4589 C  CG1 . VAL B  1  251 ? 8.943   -23.224 63.767 1.00 37.51  ? 264 VAL B CG1 1 
ATOM   4590 C  CG2 . VAL B  1  251 ? 8.516   -23.793 61.391 1.00 36.82  ? 264 VAL B CG2 1 
ATOM   4591 N  N   . LEU B  1  252 ? 6.034   -25.025 65.062 1.00 44.37  ? 265 LEU B N   1 
ATOM   4592 C  CA  . LEU B  1  252 ? 5.560   -25.170 66.432 1.00 45.59  ? 265 LEU B CA  1 
ATOM   4593 C  C   . LEU B  1  252 ? 5.455   -26.650 66.812 1.00 43.90  ? 265 LEU B C   1 
ATOM   4594 O  O   . LEU B  1  252 ? 5.876   -27.024 67.899 1.00 48.49  ? 265 LEU B O   1 
ATOM   4595 C  CB  . LEU B  1  252 ? 4.224   -24.458 66.627 1.00 44.88  ? 265 LEU B CB  1 
ATOM   4596 C  CG  . LEU B  1  252 ? 3.669   -24.497 68.051 1.00 46.41  ? 265 LEU B CG  1 
ATOM   4597 C  CD1 . LEU B  1  252 ? 4.576   -23.771 69.024 1.00 45.68  ? 265 LEU B CD1 1 
ATOM   4598 C  CD2 . LEU B  1  252 ? 2.269   -23.926 68.093 1.00 47.68  ? 265 LEU B CD2 1 
ATOM   4599 N  N   . ALA B  1  253 ? 4.912   -27.483 65.917 1.00 41.80  ? 266 ALA B N   1 
ATOM   4600 C  CA  . ALA B  1  253 ? 4.703   -28.903 66.196 1.00 47.11  ? 266 ALA B CA  1 
ATOM   4601 C  C   . ALA B  1  253 ? 6.022   -29.639 66.469 1.00 51.52  ? 266 ALA B C   1 
ATOM   4602 O  O   . ALA B  1  253 ? 6.054   -30.567 67.274 1.00 47.29  ? 266 ALA B O   1 
ATOM   4603 C  CB  . ALA B  1  253 ? 3.935   -29.551 65.061 1.00 45.56  ? 266 ALA B CB  1 
ATOM   4604 N  N   . ALA B  1  254 ? 7.119   -29.220 65.821 1.00 52.22  ? 267 ALA B N   1 
ATOM   4605 C  CA  . ALA B  1  254 ? 8.421   -29.847 66.021 1.00 53.50  ? 267 ALA B CA  1 
ATOM   4606 C  C   . ALA B  1  254 ? 8.912   -29.708 67.466 1.00 51.41  ? 267 ALA B C   1 
ATOM   4607 O  O   . ALA B  1  254 ? 9.659   -30.560 67.951 1.00 48.38  ? 267 ALA B O   1 
ATOM   4608 C  CB  . ALA B  1  254 ? 9.431   -29.252 65.057 1.00 56.29  ? 267 ALA B CB  1 
ATOM   4609 N  N   . HIS B  1  255 ? 8.554   -28.596 68.127 1.00 47.84  ? 268 HIS B N   1 
ATOM   4610 C  CA  . HIS B  1  255 ? 8.909   -28.367 69.517 1.00 46.53  ? 268 HIS B CA  1 
ATOM   4611 C  C   . HIS B  1  255 ? 7.802   -27.554 70.182 1.00 52.54  ? 268 HIS B C   1 
ATOM   4612 O  O   . HIS B  1  255 ? 7.922   -26.329 70.328 1.00 47.71  ? 268 HIS B O   1 
ATOM   4613 C  CB  . HIS B  1  255 ? 10.263  -27.664 69.671 1.00 52.44  ? 268 HIS B CB  1 
ATOM   4614 C  CG  . HIS B  1  255 ? 11.453  -28.488 69.316 1.00 54.66  ? 268 HIS B CG  1 
ATOM   4615 N  ND1 . HIS B  1  255 ? 11.987  -29.411 70.186 1.00 61.05  ? 268 HIS B ND1 1 
ATOM   4616 C  CD2 . HIS B  1  255 ? 12.214  -28.531 68.211 1.00 58.93  ? 268 HIS B CD2 1 
ATOM   4617 C  CE1 . HIS B  1  255 ? 13.032  -29.996 69.614 1.00 64.19  ? 268 HIS B CE1 1 
ATOM   4618 N  NE2 . HIS B  1  255 ? 13.191  -29.476 68.414 1.00 63.47  ? 268 HIS B NE2 1 
ATOM   4619 N  N   . PRO B  1  256 ? 6.697   -28.220 70.605 1.00 49.41  ? 269 PRO B N   1 
ATOM   4620 C  CA  . PRO B  1  256 ? 5.574   -27.544 71.256 1.00 47.08  ? 269 PRO B CA  1 
ATOM   4621 C  C   . PRO B  1  256 ? 6.052   -26.595 72.343 1.00 43.11  ? 269 PRO B C   1 
ATOM   4622 O  O   . PRO B  1  256 ? 6.968   -26.903 73.093 1.00 46.20  ? 269 PRO B O   1 
ATOM   4623 C  CB  . PRO B  1  256 ? 4.755   -28.720 71.824 1.00 51.53  ? 269 PRO B CB  1 
ATOM   4624 C  CG  . PRO B  1  256 ? 4.986   -29.811 70.799 1.00 54.98  ? 269 PRO B CG  1 
ATOM   4625 C  CD  . PRO B  1  256 ? 6.466   -29.667 70.462 1.00 50.80  ? 269 PRO B CD  1 
ATOM   4626 N  N   . TRP B  1  257 ? 5.436   -25.420 72.385 1.00 42.07  ? 270 TRP B N   1 
ATOM   4627 C  CA  . TRP B  1  257 ? 5.871   -24.355 73.263 1.00 44.28  ? 270 TRP B CA  1 
ATOM   4628 C  C   . TRP B  1  257 ? 4.676   -23.472 73.613 1.00 45.46  ? 270 TRP B C   1 
ATOM   4629 O  O   . TRP B  1  257 ? 3.768   -23.284 72.805 1.00 41.59  ? 270 TRP B O   1 
ATOM   4630 C  CB  . TRP B  1  257 ? 6.999   -23.536 72.607 1.00 44.27  ? 270 TRP B CB  1 
ATOM   4631 C  CG  . TRP B  1  257 ? 7.686   -22.648 73.601 1.00 40.09  ? 270 TRP B CG  1 
ATOM   4632 C  CD1 . TRP B  1  257 ? 7.489   -21.314 73.786 1.00 39.60  ? 270 TRP B CD1 1 
ATOM   4633 C  CD2 . TRP B  1  257 ? 8.584   -23.075 74.645 1.00 40.72  ? 270 TRP B CD2 1 
ATOM   4634 N  NE1 . TRP B  1  257 ? 8.244   -20.864 74.833 1.00 40.55  ? 270 TRP B NE1 1 
ATOM   4635 C  CE2 . TRP B  1  257 ? 8.917   -21.925 75.385 1.00 40.86  ? 270 TRP B CE2 1 
ATOM   4636 C  CE3 . TRP B  1  257 ? 9.134   -24.305 75.020 1.00 43.26  ? 270 TRP B CE3 1 
ATOM   4637 C  CZ2 . TRP B  1  257 ? 9.778   -21.969 76.474 1.00 43.66  ? 270 TRP B CZ2 1 
ATOM   4638 C  CZ3 . TRP B  1  257 ? 9.973   -24.349 76.110 1.00 40.48  ? 270 TRP B CZ3 1 
ATOM   4639 C  CH2 . TRP B  1  257 ? 10.284  -23.196 76.826 1.00 43.08  ? 270 TRP B CH2 1 
ATOM   4640 N  N   . VAL B  1  258 ? 4.726   -22.892 74.808 1.00 45.31  ? 271 VAL B N   1 
ATOM   4641 C  CA  . VAL B  1  258 ? 3.596   -22.182 75.366 1.00 48.95  ? 271 VAL B CA  1 
ATOM   4642 C  C   . VAL B  1  258 ? 4.027   -20.746 75.631 1.00 42.54  ? 271 VAL B C   1 
ATOM   4643 O  O   . VAL B  1  258 ? 5.132   -20.513 76.111 1.00 45.48  ? 271 VAL B O   1 
ATOM   4644 C  CB  . VAL B  1  258 ? 3.117   -22.868 76.663 1.00 53.42  ? 271 VAL B CB  1 
ATOM   4645 C  CG1 . VAL B  1  258 ? 1.904   -22.166 77.239 1.00 62.00  ? 271 VAL B CG1 1 
ATOM   4646 C  CG2 . VAL B  1  258 ? 2.809   -24.350 76.476 1.00 57.88  ? 271 VAL B CG2 1 
ATOM   4647 N  N   . PRO B  1  259 ? 3.175   -19.743 75.336 1.00 37.99  ? 272 PRO B N   1 
ATOM   4648 C  CA  . PRO B  1  259 ? 3.531   -18.354 75.586 1.00 42.11  ? 272 PRO B CA  1 
ATOM   4649 C  C   . PRO B  1  259 ? 3.830   -18.127 77.058 1.00 44.09  ? 272 PRO B C   1 
ATOM   4650 O  O   . PRO B  1  259 ? 3.232   -18.755 77.920 1.00 46.63  ? 272 PRO B O   1 
ATOM   4651 C  CB  . PRO B  1  259 ? 2.304   -17.558 75.095 1.00 42.15  ? 272 PRO B CB  1 
ATOM   4652 C  CG  . PRO B  1  259 ? 1.177   -18.577 75.095 1.00 42.87  ? 272 PRO B CG  1 
ATOM   4653 C  CD  . PRO B  1  259 ? 1.842   -19.880 74.718 1.00 41.92  ? 272 PRO B CD  1 
ATOM   4654 N  N   . GLY B  1  260 ? 4.760   -17.214 77.324 1.00 45.66  ? 273 GLY B N   1 
ATOM   4655 C  CA  . GLY B  1  260 ? 5.177   -16.906 78.673 1.00 45.15  ? 273 GLY B CA  1 
ATOM   4656 C  C   . GLY B  1  260 ? 6.395   -15.993 78.656 1.00 48.10  ? 273 GLY B C   1 
ATOM   4657 O  O   . GLY B  1  260 ? 6.564   -15.195 77.739 1.00 43.47  ? 273 GLY B O   1 
ATOM   4658 N  N   . GLY B  1  261 ? 7.231   -16.127 79.688 1.00 44.74  ? 274 GLY B N   1 
ATOM   4659 C  CA  . GLY B  1  261 ? 8.416   -15.305 79.850 1.00 46.87  ? 274 GLY B CA  1 
ATOM   4660 C  C   . GLY B  1  261 ? 9.187   -15.703 81.106 1.00 51.91  ? 274 GLY B C   1 
ATOM   4661 O  O   . GLY B  1  261 ? 8.677   -16.441 81.940 1.00 49.85  ? 274 GLY B O   1 
ATOM   4662 N  N   . ASN B  1  262 ? 10.431  -15.227 81.211 1.00 51.47  ? 275 ASN B N   1 
ATOM   4663 C  CA  . ASN B  1  262 ? 11.196  -15.324 82.443 1.00 50.95  ? 275 ASN B CA  1 
ATOM   4664 C  C   . ASN B  1  262 ? 10.567  -14.395 83.474 1.00 55.49  ? 275 ASN B C   1 
ATOM   4665 O  O   . ASN B  1  262 ? 10.436  -13.203 83.215 1.00 52.77  ? 275 ASN B O   1 
ATOM   4666 C  CB  . ASN B  1  262 ? 12.658  -14.924 82.253 1.00 46.40  ? 275 ASN B CB  1 
ATOM   4667 C  CG  . ASN B  1  262 ? 13.533  -16.054 81.767 1.00 46.33  ? 275 ASN B CG  1 
ATOM   4668 O  OD1 . ASN B  1  262 ? 13.223  -17.232 81.975 1.00 44.74  ? 275 ASN B OD1 1 
ATOM   4669 N  ND2 . ASN B  1  262 ? 14.652  -15.713 81.144 1.00 49.84  ? 275 ASN B ND2 1 
ATOM   4670 N  N   . ALA B  1  263 ? 10.212  -14.938 84.648 1.00 59.13  ? 276 ALA B N   1 
ATOM   4671 C  CA  . ALA B  1  263 ? 9.629   -14.123 85.706 1.00 62.80  ? 276 ALA B CA  1 
ATOM   4672 C  C   . ALA B  1  263 ? 10.714  -13.572 86.632 1.00 62.39  ? 276 ALA B C   1 
ATOM   4673 O  O   . ALA B  1  263 ? 11.787  -14.154 86.766 1.00 63.62  ? 276 ALA B O   1 
ATOM   4674 C  CB  . ALA B  1  263 ? 8.598   -14.931 86.464 1.00 64.55  ? 276 ALA B CB  1 
ATOM   4675 N  N   . ASP B  1  264 ? 10.420  -12.410 87.230 1.00 70.51  ? 277 ASP B N   1 
ATOM   4676 C  CA  . ASP B  1  264 ? 11.125  -11.878 88.391 1.00 75.93  ? 277 ASP B CA  1 
ATOM   4677 C  C   . ASP B  1  264 ? 12.591  -11.596 88.073 1.00 75.16  ? 277 ASP B C   1 
ATOM   4678 O  O   . ASP B  1  264 ? 13.458  -11.777 88.931 1.00 70.79  ? 277 ASP B O   1 
ATOM   4679 C  CB  . ASP B  1  264 ? 10.989  -12.780 89.610 1.00 85.73  ? 277 ASP B CB  1 
ATOM   4680 C  CG  . ASP B  1  264 ? 9.564   -13.122 90.029 1.00 92.04  ? 277 ASP B CG  1 
ATOM   4681 O  OD1 . ASP B  1  264 ? 8.721   -12.194 90.115 1.00 83.77  ? 277 ASP B OD1 1 
ATOM   4682 O  OD2 . ASP B  1  264 ? 9.299   -14.323 90.247 1.00 98.17  ? 277 ASP B OD2 1 
ATOM   4683 N  N   . ASN B  1  265 ? 12.849  -11.138 86.841 1.00 66.25  ? 278 ASN B N   1 
ATOM   4684 C  CA  . ASN B  1  265 ? 14.151  -10.610 86.464 1.00 59.24  ? 278 ASN B CA  1 
ATOM   4685 C  C   . ASN B  1  265 ? 15.227  -11.676 86.669 1.00 55.29  ? 278 ASN B C   1 
ATOM   4686 O  O   . ASN B  1  265 ? 16.348  -11.360 87.055 1.00 58.63  ? 278 ASN B O   1 
ATOM   4687 C  CB  . ASN B  1  265 ? 14.451  -9.329  87.240 1.00 66.14  ? 278 ASN B CB  1 
ATOM   4688 C  CG  . ASN B  1  265 ? 15.284  -8.358  86.444 1.00 73.43  ? 278 ASN B CG  1 
ATOM   4689 O  OD1 . ASN B  1  265 ? 14.945  -8.055  85.293 1.00 78.71  ? 278 ASN B OD1 1 
ATOM   4690 N  ND2 . ASN B  1  265 ? 16.355  -7.848  87.034 1.00 77.44  ? 278 ASN B ND2 1 
ATOM   4691 N  N   . GLN B  1  266 ? 14.896  -12.938 86.367 1.00 53.12  ? 279 GLN B N   1 
ATOM   4692 C  CA  . GLN B  1  266 ? 15.832  -14.039 86.500 1.00 59.93  ? 279 GLN B CA  1 
ATOM   4693 C  C   . GLN B  1  266 ? 15.854  -14.879 85.227 1.00 60.88  ? 279 GLN B C   1 
ATOM   4694 O  O   . GLN B  1  266 ? 14.823  -15.117 84.608 1.00 62.02  ? 279 GLN B O   1 
ATOM   4695 C  CB  . GLN B  1  266 ? 15.408  -14.962 87.639 1.00 68.37  ? 279 GLN B CB  1 
ATOM   4696 C  CG  . GLN B  1  266 ? 15.715  -14.419 89.026 1.00 74.58  ? 279 GLN B CG  1 
ATOM   4697 C  CD  . GLN B  1  266 ? 15.087  -15.244 90.128 1.00 80.44  ? 279 GLN B CD  1 
ATOM   4698 O  OE1 . GLN B  1  266 ? 14.342  -16.206 89.900 1.00 77.31  ? 279 GLN B OE1 1 
ATOM   4699 N  NE2 . GLN B  1  266 ? 15.411  -14.879 91.356 1.00 91.86  ? 279 GLN B NE2 1 
ATOM   4700 N  N   . VAL B  1  267 ? 17.043  -15.378 84.886 1.00 54.29  ? 280 VAL B N   1 
ATOM   4701 C  CA  . VAL B  1  267 ? 17.195  -16.338 83.811 1.00 52.01  ? 280 VAL B CA  1 
ATOM   4702 C  C   . VAL B  1  267 ? 16.717  -17.710 84.273 1.00 51.13  ? 280 VAL B C   1 
ATOM   4703 O  O   . VAL B  1  267 ? 16.446  -17.918 85.447 1.00 56.30  ? 280 VAL B O   1 
ATOM   4704 C  CB  . VAL B  1  267 ? 18.647  -16.355 83.297 1.00 52.80  ? 280 VAL B CB  1 
ATOM   4705 C  CG1 . VAL B  1  267 ? 19.037  -14.994 82.714 1.00 50.21  ? 280 VAL B CG1 1 
ATOM   4706 C  CG2 . VAL B  1  267 ? 19.648  -16.795 84.364 1.00 55.64  ? 280 VAL B CG2 1 
ATOM   4707 N  N   . ASN B  1  268 ? 16.570  -18.618 83.308 1.00 48.72  ? 281 ASN B N   1 
ATOM   4708 C  CA  . ASN B  1  268 ? 16.097  -19.983 83.508 1.00 57.01  ? 281 ASN B CA  1 
ATOM   4709 C  C   . ASN B  1  268 ? 14.899  -20.016 84.452 1.00 58.73  ? 281 ASN B C   1 
ATOM   4710 O  O   . ASN B  1  268 ? 14.829  -20.864 85.335 1.00 59.71  ? 281 ASN B O   1 
ATOM   4711 C  CB  . ASN B  1  268 ? 17.216  -20.899 83.989 1.00 58.19  ? 281 ASN B CB  1 
ATOM   4712 C  CG  . ASN B  1  268 ? 18.330  -20.972 82.975 1.00 58.03  ? 281 ASN B CG  1 
ATOM   4713 O  OD1 . ASN B  1  268 ? 18.135  -21.496 81.874 1.00 63.91  ? 281 ASN B OD1 1 
ATOM   4714 N  ND2 . ASN B  1  268 ? 19.495  -20.449 83.316 1.00 57.76  ? 281 ASN B ND2 1 
ATOM   4715 N  N   . ASN B  1  269 ? 13.932  -19.131 84.215 1.00 55.60  ? 282 ASN B N   1 
ATOM   4716 C  CA  . ASN B  1  269 ? 12.788  -19.004 85.095 1.00 53.34  ? 282 ASN B CA  1 
ATOM   4717 C  C   . ASN B  1  269 ? 11.531  -18.738 84.266 1.00 51.30  ? 282 ASN B C   1 
ATOM   4718 O  O   . ASN B  1  269 ? 10.794  -17.791 84.527 1.00 52.56  ? 282 ASN B O   1 
ATOM   4719 C  CB  . ASN B  1  269 ? 13.097  -17.964 86.163 1.00 54.40  ? 282 ASN B CB  1 
ATOM   4720 C  CG  . ASN B  1  269 ? 12.068  -17.959 87.271 1.00 53.39  ? 282 ASN B CG  1 
ATOM   4721 O  OD1 . ASN B  1  269 ? 11.569  -19.022 87.645 1.00 50.49  ? 282 ASN B OD1 1 
ATOM   4722 N  ND2 . ASN B  1  269 ? 11.693  -16.783 87.750 1.00 51.32  ? 282 ASN B ND2 1 
ATOM   4723 N  N   . TYR B  1  270 ? 11.275  -19.608 83.282 1.00 52.34  ? 283 TYR B N   1 
ATOM   4724 C  CA  . TYR B  1  270 ? 10.214  -19.374 82.312 1.00 53.21  ? 283 TYR B CA  1 
ATOM   4725 C  C   . TYR B  1  270 ? 8.872   -19.842 82.874 1.00 54.09  ? 283 TYR B C   1 
ATOM   4726 O  O   . TYR B  1  270 ? 8.710   -21.024 83.151 1.00 50.69  ? 283 TYR B O   1 
ATOM   4727 C  CB  . TYR B  1  270 ? 10.509  -20.109 81.004 1.00 47.70  ? 283 TYR B CB  1 
ATOM   4728 C  CG  . TYR B  1  270 ? 9.578   -19.759 79.850 1.00 48.97  ? 283 TYR B CG  1 
ATOM   4729 C  CD1 . TYR B  1  270 ? 9.844   -18.675 79.016 1.00 48.95  ? 283 TYR B CD1 1 
ATOM   4730 C  CD2 . TYR B  1  270 ? 8.453   -20.529 79.571 1.00 47.35  ? 283 TYR B CD2 1 
ATOM   4731 C  CE1 . TYR B  1  270 ? 9.016   -18.359 77.953 1.00 47.30  ? 283 TYR B CE1 1 
ATOM   4732 C  CE2 . TYR B  1  270 ? 7.618   -20.228 78.506 1.00 50.64  ? 283 TYR B CE2 1 
ATOM   4733 C  CZ  . TYR B  1  270 ? 7.900   -19.136 77.698 1.00 50.04  ? 283 TYR B CZ  1 
ATOM   4734 O  OH  . TYR B  1  270 ? 7.078   -18.846 76.651 1.00 45.18  ? 283 TYR B OH  1 
ATOM   4735 N  N   . VAL B  1  271 ? 7.910   -18.909 82.960 1.00 51.96  ? 284 VAL B N   1 
ATOM   4736 C  CA  . VAL B  1  271 ? 6.564   -19.168 83.450 1.00 51.40  ? 284 VAL B CA  1 
ATOM   4737 C  C   . VAL B  1  271 ? 5.558   -18.972 82.320 1.00 49.89  ? 284 VAL B C   1 
ATOM   4738 O  O   . VAL B  1  271 ? 5.549   -17.919 81.682 1.00 51.24  ? 284 VAL B O   1 
ATOM   4739 C  CB  . VAL B  1  271 ? 6.259   -18.197 84.607 1.00 57.56  ? 284 VAL B CB  1 
ATOM   4740 C  CG1 . VAL B  1  271 ? 4.818   -18.304 85.106 1.00 58.47  ? 284 VAL B CG1 1 
ATOM   4741 C  CG2 . VAL B  1  271 ? 7.244   -18.361 85.759 1.00 63.03  ? 284 VAL B CG2 1 
ATOM   4742 N  N   . GLU B  1  272 ? 4.670   -19.956 82.145 1.00 48.63  ? 285 GLU B N   1 
ATOM   4743 C  CA  A GLU B  1  272 ? 3.619   -19.893 81.144 0.50 49.71  ? 285 GLU B CA  1 
ATOM   4744 C  CA  B GLU B  1  272 ? 3.610   -19.901 81.149 0.50 51.06  ? 285 GLU B CA  1 
ATOM   4745 C  C   . GLU B  1  272 ? 2.637   -18.772 81.493 1.00 52.43  ? 285 GLU B C   1 
ATOM   4746 O  O   . GLU B  1  272 ? 2.406   -18.489 82.663 1.00 54.93  ? 285 GLU B O   1 
ATOM   4747 C  CB  A GLU B  1  272 ? 2.971   -21.273 81.023 0.50 50.63  ? 285 GLU B CB  1 
ATOM   4748 C  CB  B GLU B  1  272 ? 2.863   -21.235 81.038 0.50 54.10  ? 285 GLU B CB  1 
ATOM   4749 C  CG  A GLU B  1  272 ? 3.966   -22.379 80.667 0.50 50.37  ? 285 GLU B CG  1 
ATOM   4750 C  CG  B GLU B  1  272 ? 1.484   -21.090 80.390 0.50 56.13  ? 285 GLU B CG  1 
ATOM   4751 C  CD  A GLU B  1  272 ? 3.455   -23.794 80.878 0.50 50.95  ? 285 GLU B CD  1 
ATOM   4752 C  CD  B GLU B  1  272 ? 0.676   -22.352 80.139 0.50 57.70  ? 285 GLU B CD  1 
ATOM   4753 O  OE1 A GLU B  1  272 ? 2.468   -23.949 81.624 0.50 57.20  ? 285 GLU B OE1 1 
ATOM   4754 O  OE1 B GLU B  1  272 ? 1.149   -23.469 80.434 0.50 54.62  ? 285 GLU B OE1 1 
ATOM   4755 O  OE2 A GLU B  1  272 ? 4.025   -24.739 80.298 0.50 46.02  ? 285 GLU B OE2 1 
ATOM   4756 O  OE2 B GLU B  1  272 ? -0.451  -22.194 79.616 0.50 58.53  ? 285 GLU B OE2 1 
ATOM   4757 N  N   . ASP B  1  273 ? 2.084   -18.119 80.453 1.00 51.93  ? 286 ASP B N   1 
ATOM   4758 C  CA  . ASP B  1  273 ? 1.013   -17.140 80.598 1.00 52.67  ? 286 ASP B CA  1 
ATOM   4759 C  C   . ASP B  1  273 ? -0.243  -17.688 79.923 1.00 55.63  ? 286 ASP B C   1 
ATOM   4760 O  O   . ASP B  1  273 ? -0.345  -17.684 78.700 1.00 53.41  ? 286 ASP B O   1 
ATOM   4761 C  CB  . ASP B  1  273 ? 1.368   -15.776 80.034 1.00 53.33  ? 286 ASP B CB  1 
ATOM   4762 C  CG  . ASP B  1  273 ? 0.252   -14.737 80.058 1.00 54.26  ? 286 ASP B CG  1 
ATOM   4763 O  OD1 . ASP B  1  273 ? -0.840  -15.060 80.562 1.00 59.02  ? 286 ASP B OD1 1 
ATOM   4764 O  OD2 . ASP B  1  273 ? 0.483   -13.613 79.565 1.00 57.89  ? 286 ASP B OD2 1 
ATOM   4765 N  N   . PRO B  1  274 ? -1.246  -18.170 80.695 1.00 59.97  ? 287 PRO B N   1 
ATOM   4766 C  CA  . PRO B  1  274 ? -2.428  -18.804 80.101 1.00 54.13  ? 287 PRO B CA  1 
ATOM   4767 C  C   . PRO B  1  274 ? -3.422  -17.839 79.454 1.00 47.30  ? 287 PRO B C   1 
ATOM   4768 O  O   . PRO B  1  274 ? -4.276  -18.277 78.688 1.00 52.43  ? 287 PRO B O   1 
ATOM   4769 C  CB  . PRO B  1  274 ? -3.039  -19.545 81.307 1.00 60.67  ? 287 PRO B CB  1 
ATOM   4770 C  CG  . PRO B  1  274 ? -2.667  -18.677 82.490 1.00 61.82  ? 287 PRO B CG  1 
ATOM   4771 C  CD  . PRO B  1  274 ? -1.288  -18.117 82.169 1.00 61.92  ? 287 PRO B CD  1 
ATOM   4772 N  N   . ASP B  1  275 ? -3.292  -16.538 79.753 1.00 44.40  ? 288 ASP B N   1 
ATOM   4773 C  CA  . ASP B  1  275 ? -4.138  -15.502 79.174 1.00 49.42  ? 288 ASP B CA  1 
ATOM   4774 C  C   . ASP B  1  275 ? -3.655  -15.013 77.797 1.00 51.00  ? 288 ASP B C   1 
ATOM   4775 O  O   . ASP B  1  275 ? -4.376  -14.277 77.116 1.00 42.31  ? 288 ASP B O   1 
ATOM   4776 C  CB  . ASP B  1  275 ? -4.235  -14.305 80.105 1.00 53.85  ? 288 ASP B CB  1 
ATOM   4777 C  CG  . ASP B  1  275 ? -4.987  -14.562 81.404 1.00 63.53  ? 288 ASP B CG  1 
ATOM   4778 O  OD1 . ASP B  1  275 ? -5.384  -15.730 81.648 1.00 56.36  ? 288 ASP B OD1 1 
ATOM   4779 O  OD2 . ASP B  1  275 ? -5.194  -13.579 82.148 1.00 69.23  ? 288 ASP B OD2 1 
ATOM   4780 N  N   . SER B  1  276 ? -2.434  -15.398 77.397 1.00 52.19  ? 289 SER B N   1 
ATOM   4781 C  CA  . SER B  1  276 ? -1.841  -14.926 76.152 1.00 45.73  ? 289 SER B CA  1 
ATOM   4782 C  C   . SER B  1  276 ? -2.587  -15.501 74.955 1.00 44.14  ? 289 SER B C   1 
ATOM   4783 O  O   . SER B  1  276 ? -3.119  -16.621 75.014 1.00 43.27  ? 289 SER B O   1 
ATOM   4784 C  CB  . SER B  1  276 ? -0.368  -15.302 76.091 1.00 44.12  ? 289 SER B CB  1 
ATOM   4785 O  OG  . SER B  1  276 ? 0.152   -15.166 74.780 1.00 45.14  ? 289 SER B OG  1 
ATOM   4786 N  N   . ALA B  1  277 ? -2.549  -14.766 73.840 1.00 42.98  ? 290 ALA B N   1 
ATOM   4787 C  CA  . ALA B  1  277 ? -2.874  -15.366 72.551 1.00 39.90  ? 290 ALA B CA  1 
ATOM   4788 C  C   . ALA B  1  277 ? -1.990  -16.585 72.303 1.00 40.50  ? 290 ALA B C   1 
ATOM   4789 O  O   . ALA B  1  277 ? -0.868  -16.661 72.808 1.00 39.75  ? 290 ALA B O   1 
ATOM   4790 C  CB  . ALA B  1  277 ? -2.687  -14.356 71.443 1.00 40.74  ? 290 ALA B CB  1 
ATOM   4791 N  N   . ASP B  1  278 ? -2.528  -17.531 71.531 1.00 40.01  ? 291 ASP B N   1 
ATOM   4792 C  CA  . ASP B  1  278 ? -1.775  -18.619 70.942 1.00 41.01  ? 291 ASP B CA  1 
ATOM   4793 C  C   . ASP B  1  278 ? -2.463  -18.974 69.629 1.00 38.99  ? 291 ASP B C   1 
ATOM   4794 O  O   . ASP B  1  278 ? -3.395  -18.284 69.228 1.00 38.29  ? 291 ASP B O   1 
ATOM   4795 C  CB  . ASP B  1  278 ? -1.604  -19.761 71.928 1.00 48.00  ? 291 ASP B CB  1 
ATOM   4796 C  CG  . ASP B  1  278 ? -2.864  -20.523 72.296 1.00 50.49  ? 291 ASP B CG  1 
ATOM   4797 O  OD1 . ASP B  1  278 ? -3.829  -20.518 71.495 1.00 48.70  ? 291 ASP B OD1 1 
ATOM   4798 O  OD2 . ASP B  1  278 ? -2.863  -21.130 73.376 1.00 53.34  ? 291 ASP B OD2 1 
ATOM   4799 N  N   . PHE B  1  279 ? -2.032  -20.051 68.966 1.00 39.89  ? 292 PHE B N   1 
ATOM   4800 C  CA  . PHE B  1  279 ? -2.487  -20.307 67.606 1.00 41.50  ? 292 PHE B CA  1 
ATOM   4801 C  C   . PHE B  1  279 ? -3.920  -20.832 67.563 1.00 46.90  ? 292 PHE B C   1 
ATOM   4802 O  O   . PHE B  1  279 ? -4.518  -20.816 66.493 1.00 43.81  ? 292 PHE B O   1 
ATOM   4803 C  CB  . PHE B  1  279 ? -1.509  -21.224 66.866 1.00 40.71  ? 292 PHE B CB  1 
ATOM   4804 C  CG  . PHE B  1  279 ? -0.265  -20.439 66.484 1.00 44.22  ? 292 PHE B CG  1 
ATOM   4805 C  CD1 . PHE B  1  279 ? -0.282  -19.608 65.373 1.00 49.22  ? 292 PHE B CD1 1 
ATOM   4806 C  CD2 . PHE B  1  279 ? 0.891   -20.486 67.259 1.00 47.10  ? 292 PHE B CD2 1 
ATOM   4807 C  CE1 . PHE B  1  279 ? 0.839   -18.870 65.018 1.00 51.20  ? 292 PHE B CE1 1 
ATOM   4808 C  CE2 . PHE B  1  279 ? 2.001   -19.738 66.905 1.00 48.51  ? 292 PHE B CE2 1 
ATOM   4809 C  CZ  . PHE B  1  279 ? 1.967   -18.920 65.797 1.00 48.17  ? 292 PHE B CZ  1 
ATOM   4810 N  N   . THR B  1  280 ? -4.492  -21.246 68.704 1.00 50.58  ? 293 THR B N   1 
ATOM   4811 C  CA  . THR B  1  280 ? -5.908  -21.593 68.732 1.00 53.31  ? 293 THR B CA  1 
ATOM   4812 C  C   . THR B  1  280 ? -6.709  -20.498 69.440 1.00 52.85  ? 293 THR B C   1 
ATOM   4813 O  O   . THR B  1  280 ? -7.902  -20.675 69.675 1.00 53.58  ? 293 THR B O   1 
ATOM   4814 C  CB  . THR B  1  280 ? -6.119  -22.962 69.386 1.00 50.28  ? 293 THR B CB  1 
ATOM   4815 O  OG1 . THR B  1  280 ? -5.641  -22.891 70.726 1.00 51.25  ? 293 THR B OG1 1 
ATOM   4816 C  CG2 . THR B  1  280 ? -5.365  -24.079 68.687 1.00 51.62  ? 293 THR B CG2 1 
ATOM   4817 N  N   . HIS B  1  281 ? -6.070  -19.365 69.764 1.00 47.11  ? 294 HIS B N   1 
ATOM   4818 C  CA  . HIS B  1  281 ? -6.747  -18.241 70.398 1.00 45.69  ? 294 HIS B CA  1 
ATOM   4819 C  C   . HIS B  1  281 ? -6.255  -16.928 69.787 1.00 44.42  ? 294 HIS B C   1 
ATOM   4820 O  O   . HIS B  1  281 ? -5.804  -16.041 70.508 1.00 45.42  ? 294 HIS B O   1 
ATOM   4821 C  CB  . HIS B  1  281 ? -6.537  -18.251 71.921 1.00 48.20  ? 294 HIS B CB  1 
ATOM   4822 C  CG  . HIS B  1  281 ? -7.061  -19.459 72.632 1.00 57.58  ? 294 HIS B CG  1 
ATOM   4823 N  ND1 . HIS B  1  281 ? -8.340  -19.496 73.153 1.00 60.71  ? 294 HIS B ND1 1 
ATOM   4824 C  CD2 . HIS B  1  281 ? -6.514  -20.657 72.906 1.00 58.74  ? 294 HIS B CD2 1 
ATOM   4825 C  CE1 . HIS B  1  281 ? -8.548  -20.671 73.727 1.00 61.29  ? 294 HIS B CE1 1 
ATOM   4826 N  NE2 . HIS B  1  281 ? -7.452  -21.390 73.590 1.00 65.69  ? 294 HIS B NE2 1 
ATOM   4827 N  N   . LEU B  1  282 ? -6.367  -16.802 68.460 1.00 43.10  ? 295 LEU B N   1 
ATOM   4828 C  CA  . LEU B  1  282 ? -5.758  -15.692 67.743 1.00 42.49  ? 295 LEU B CA  1 
ATOM   4829 C  C   . LEU B  1  282 ? -6.449  -14.371 68.050 1.00 42.79  ? 295 LEU B C   1 
ATOM   4830 O  O   . LEU B  1  282 ? -5.803  -13.319 68.045 1.00 40.60  ? 295 LEU B O   1 
ATOM   4831 C  CB  . LEU B  1  282 ? -5.753  -15.956 66.242 1.00 41.73  ? 295 LEU B CB  1 
ATOM   4832 C  CG  . LEU B  1  282 ? -4.743  -16.998 65.763 1.00 42.54  ? 295 LEU B CG  1 
ATOM   4833 C  CD1 . LEU B  1  282 ? -4.973  -17.324 64.301 1.00 43.95  ? 295 LEU B CD1 1 
ATOM   4834 C  CD2 . LEU B  1  282 ? -3.326  -16.484 66.004 1.00 43.43  ? 295 LEU B CD2 1 
ATOM   4835 N  N   . CYS B  1  283 ? -7.758  -14.417 68.323 1.00 42.24  ? 296 CYS B N   1 
ATOM   4836 C  CA  . CYS B  1  283 ? -8.499  -13.181 68.542 1.00 42.90  ? 296 CYS B CA  1 
ATOM   4837 C  C   . CYS B  1  283 ? -8.019  -12.475 69.809 1.00 40.43  ? 296 CYS B C   1 
ATOM   4838 O  O   . CYS B  1  283 ? -8.152  -11.266 69.917 1.00 44.43  ? 296 CYS B O   1 
ATOM   4839 C  CB  . CYS B  1  283 ? -10.007 -13.410 68.515 1.00 50.44  ? 296 CYS B CB  1 
ATOM   4840 S  SG  . CYS B  1  283 ? -10.657 -13.813 66.860 1.00 59.05  ? 296 CYS B SG  1 
ATOM   4841 N  N   . ARG B  1  284 ? -7.399  -13.202 70.735 1.00 40.49  ? 297 ARG B N   1 
ATOM   4842 C  CA  . ARG B  1  284 ? -6.803  -12.569 71.898 1.00 44.83  ? 297 ARG B CA  1 
ATOM   4843 C  C   . ARG B  1  284 ? -5.734  -11.567 71.483 1.00 43.79  ? 297 ARG B C   1 
ATOM   4844 O  O   . ARG B  1  284 ? -5.549  -10.565 72.169 1.00 42.88  ? 297 ARG B O   1 
ATOM   4845 C  CB  . ARG B  1  284 ? -6.150  -13.577 72.837 1.00 49.96  ? 297 ARG B CB  1 
ATOM   4846 C  CG  . ARG B  1  284 ? -7.149  -14.460 73.565 1.00 51.02  ? 297 ARG B CG  1 
ATOM   4847 C  CD  . ARG B  1  284 ? -6.390  -15.398 74.474 1.00 54.01  ? 297 ARG B CD  1 
ATOM   4848 N  NE  . ARG B  1  284 ? -7.282  -16.393 75.074 1.00 54.80  ? 297 ARG B NE  1 
ATOM   4849 C  CZ  . ARG B  1  284 ? -6.916  -17.335 75.924 1.00 60.55  ? 297 ARG B CZ  1 
ATOM   4850 N  NH1 . ARG B  1  284 ? -5.649  -17.474 76.284 1.00 59.96  ? 297 ARG B NH1 1 
ATOM   4851 N  NH2 . ARG B  1  284 ? -7.831  -18.147 76.413 1.00 60.25  ? 297 ARG B NH2 1 
ATOM   4852 N  N   . LEU B  1  285 ? -5.030  -11.849 70.377 1.00 40.61  ? 298 LEU B N   1 
ATOM   4853 C  CA  . LEU B  1  285 ? -4.007  -10.932 69.892 1.00 40.09  ? 298 LEU B CA  1 
ATOM   4854 C  C   . LEU B  1  285 ? -4.679  -9.619  69.489 1.00 36.73  ? 298 LEU B C   1 
ATOM   4855 O  O   . LEU B  1  285 ? -4.196  -8.537  69.831 1.00 36.37  ? 298 LEU B O   1 
ATOM   4856 C  CB  . LEU B  1  285 ? -3.190  -11.542 68.749 1.00 39.08  ? 298 LEU B CB  1 
ATOM   4857 C  CG  . LEU B  1  285 ? -2.013  -10.701 68.233 1.00 40.61  ? 298 LEU B CG  1 
ATOM   4858 C  CD1 . LEU B  1  285 ? -0.995  -11.574 67.533 1.00 42.35  ? 298 LEU B CD1 1 
ATOM   4859 C  CD2 . LEU B  1  285 ? -2.435  -9.606  67.279 1.00 41.24  ? 298 LEU B CD2 1 
ATOM   4860 N  N   . TYR B  1  286 ? -5.801  -9.722  68.763 1.00 38.43  ? 299 TYR B N   1 
ATOM   4861 C  CA  . TYR B  1  286 ? -6.532  -8.545  68.318 1.00 37.72  ? 299 TYR B CA  1 
ATOM   4862 C  C   . TYR B  1  286 ? -6.992  -7.723  69.528 1.00 35.69  ? 299 TYR B C   1 
ATOM   4863 O  O   . TYR B  1  286 ? -6.779  -6.524  69.575 1.00 37.07  ? 299 TYR B O   1 
ATOM   4864 C  CB  . TYR B  1  286 ? -7.682  -8.991  67.406 1.00 36.34  ? 299 TYR B CB  1 
ATOM   4865 C  CG  . TYR B  1  286 ? -8.666  -7.888  67.062 1.00 35.83  ? 299 TYR B CG  1 
ATOM   4866 C  CD1 . TYR B  1  286 ? -8.284  -6.812  66.279 1.00 33.71  ? 299 TYR B CD1 1 
ATOM   4867 C  CD2 . TYR B  1  286 ? -9.976  -7.916  67.533 1.00 37.28  ? 299 TYR B CD2 1 
ATOM   4868 C  CE1 . TYR B  1  286 ? -9.169  -5.797  65.959 1.00 35.24  ? 299 TYR B CE1 1 
ATOM   4869 C  CE2 . TYR B  1  286 ? -10.876 -6.913  67.209 1.00 36.10  ? 299 TYR B CE2 1 
ATOM   4870 C  CZ  . TYR B  1  286 ? -10.472 -5.850  66.428 1.00 36.40  ? 299 TYR B CZ  1 
ATOM   4871 O  OH  . TYR B  1  286 ? -11.355 -4.862  66.130 1.00 36.99  ? 299 TYR B OH  1 
ATOM   4872 N  N   . GLU B  1  287 ? -7.592  -8.377  70.518 1.00 36.45  ? 300 GLU B N   1 
ATOM   4873 C  CA  . GLU B  1  287 ? -8.126  -7.693  71.691 1.00 42.59  ? 300 GLU B CA  1 
ATOM   4874 C  C   . GLU B  1  287 ? -6.990  -7.046  72.475 1.00 38.22  ? 300 GLU B C   1 
ATOM   4875 O  O   . GLU B  1  287 ? -7.106  -5.890  72.894 1.00 38.06  ? 300 GLU B O   1 
ATOM   4876 C  CB  . GLU B  1  287 ? -8.912  -8.658  72.581 1.00 43.05  ? 300 GLU B CB  1 
ATOM   4877 C  CG  . GLU B  1  287 ? -10.194 -9.158  71.927 1.00 55.11  ? 300 GLU B CG  1 
ATOM   4878 C  CD  . GLU B  1  287 ? -10.821 -10.425 72.488 1.00 68.87  ? 300 GLU B CD  1 
ATOM   4879 O  OE1 . GLU B  1  287 ? -10.157 -11.256 73.156 1.00 71.62  ? 300 GLU B OE1 1 
ATOM   4880 O  OE2 . GLU B  1  287 ? -12.034 -10.568 72.226 1.00 82.26  ? 300 GLU B OE2 1 
ATOM   4881 N  N   . PHE B  1  288 ? -5.876  -7.775  72.615 1.00 38.32  ? 301 PHE B N   1 
ATOM   4882 C  CA  . PHE B  1  288 ? -4.724  -7.270  73.350 1.00 37.64  ? 301 PHE B CA  1 
ATOM   4883 C  C   . PHE B  1  288 ? -4.226  -5.978  72.715 1.00 35.66  ? 301 PHE B C   1 
ATOM   4884 O  O   . PHE B  1  288 ? -3.962  -4.994  73.404 1.00 37.77  ? 301 PHE B O   1 
ATOM   4885 C  CB  . PHE B  1  288 ? -3.607  -8.320  73.380 1.00 42.16  ? 301 PHE B CB  1 
ATOM   4886 C  CG  . PHE B  1  288 ? -2.398  -7.869  74.183 1.00 44.37  ? 301 PHE B CG  1 
ATOM   4887 C  CD1 . PHE B  1  288 ? -2.352  -8.062  75.561 1.00 41.43  ? 301 PHE B CD1 1 
ATOM   4888 C  CD2 . PHE B  1  288 ? -1.340  -7.202  73.565 1.00 45.46  ? 301 PHE B CD2 1 
ATOM   4889 C  CE1 . PHE B  1  288 ? -1.258  -7.625  76.297 1.00 45.92  ? 301 PHE B CE1 1 
ATOM   4890 C  CE2 . PHE B  1  288 ? -0.247  -6.770  74.308 1.00 45.14  ? 301 PHE B CE2 1 
ATOM   4891 C  CZ  . PHE B  1  288 ? -0.209  -6.975  75.670 1.00 44.03  ? 301 PHE B CZ  1 
ATOM   4892 N  N   . VAL B  1  289 ? -4.098  -5.984  71.379 1.00 36.63  ? 302 VAL B N   1 
ATOM   4893 C  CA  . VAL B  1  289 ? -3.536  -4.846  70.682 1.00 35.37  ? 302 VAL B CA  1 
ATOM   4894 C  C   . VAL B  1  289 ? -4.499  -3.664  70.749 1.00 35.39  ? 302 VAL B C   1 
ATOM   4895 O  O   . VAL B  1  289 ? -4.060  -2.524  70.845 1.00 35.16  ? 302 VAL B O   1 
ATOM   4896 C  CB  . VAL B  1  289 ? -3.159  -5.182  69.222 1.00 37.20  ? 302 VAL B CB  1 
ATOM   4897 C  CG1 . VAL B  1  289 ? -2.858  -3.928  68.422 1.00 37.46  ? 302 VAL B CG1 1 
ATOM   4898 C  CG2 . VAL B  1  289 ? -1.984  -6.149  69.149 1.00 37.26  ? 302 VAL B CG2 1 
ATOM   4899 N  N   . VAL B  1  290 ? -5.811  -3.909  70.666 1.00 35.62  ? 303 VAL B N   1 
ATOM   4900 C  CA  . VAL B  1  290 ? -6.763  -2.804  70.762 1.00 34.12  ? 303 VAL B CA  1 
ATOM   4901 C  C   . VAL B  1  290 ? -6.623  -2.122  72.129 1.00 33.05  ? 303 VAL B C   1 
ATOM   4902 O  O   . VAL B  1  290 ? -6.609  -0.885  72.214 1.00 35.73  ? 303 VAL B O   1 
ATOM   4903 C  CB  . VAL B  1  290 ? -8.193  -3.303  70.486 1.00 37.61  ? 303 VAL B CB  1 
ATOM   4904 C  CG1 . VAL B  1  290 ? -9.244  -2.296  70.901 1.00 38.72  ? 303 VAL B CG1 1 
ATOM   4905 C  CG2 . VAL B  1  290 ? -8.393  -3.729  69.031 1.00 37.31  ? 303 VAL B CG2 1 
ATOM   4906 N  N   . GLY B  1  291 ? -6.441  -2.931  73.182 1.00 35.36  ? 304 GLY B N   1 
ATOM   4907 C  CA  . GLY B  1  291 ? -6.145  -2.420  74.512 1.00 39.75  ? 304 GLY B CA  1 
ATOM   4908 C  C   . GLY B  1  291 ? -4.845  -1.613  74.543 1.00 44.75  ? 304 GLY B C   1 
ATOM   4909 O  O   . GLY B  1  291 ? -4.796  -0.527  75.120 1.00 42.38  ? 304 GLY B O   1 
ATOM   4910 N  N   . SER B  1  292 ? -3.791  -2.131  73.892 1.00 43.18  ? 305 SER B N   1 
ATOM   4911 C  CA  . SER B  1  292 ? -2.528  -1.410  73.845 1.00 38.01  ? 305 SER B CA  1 
ATOM   4912 C  C   . SER B  1  292 ? -2.712  -0.069  73.155 1.00 35.31  ? 305 SER B C   1 
ATOM   4913 O  O   . SER B  1  292 ? -2.118  0.921   73.579 1.00 38.91  ? 305 SER B O   1 
ATOM   4914 C  CB  . SER B  1  292 ? -1.429  -2.206  73.155 1.00 39.49  ? 305 SER B CB  1 
ATOM   4915 O  OG  . SER B  1  292 ? -1.309  -3.495  73.738 1.00 36.94  ? 305 SER B OG  1 
ATOM   4916 N  N   . VAL B  1  293 ? -3.505  -0.030  72.077 1.00 34.22  ? 306 VAL B N   1 
ATOM   4917 C  CA  . VAL B  1  293 ? -3.723  1.216   71.370 1.00 35.74  ? 306 VAL B CA  1 
ATOM   4918 C  C   . VAL B  1  293 ? -4.390  2.227   72.307 1.00 38.94  ? 306 VAL B C   1 
ATOM   4919 O  O   . VAL B  1  293 ? -4.083  3.420   72.272 1.00 37.14  ? 306 VAL B O   1 
ATOM   4920 C  CB  . VAL B  1  293 ? -4.541  1.021   70.082 1.00 37.74  ? 306 VAL B CB  1 
ATOM   4921 C  CG1 . VAL B  1  293 ? -4.963  2.344   69.473 1.00 39.43  ? 306 VAL B CG1 1 
ATOM   4922 C  CG2 . VAL B  1  293 ? -3.795  0.197   69.039 1.00 41.70  ? 306 VAL B CG2 1 
ATOM   4923 N  N   . GLN B  1  294 ? -5.319  1.757   73.143 1.00 38.25  ? 307 GLN B N   1 
ATOM   4924 C  CA  . GLN B  1  294 ? -6.016  2.665   74.046 1.00 42.46  ? 307 GLN B CA  1 
ATOM   4925 C  C   . GLN B  1  294 ? -5.062  3.227   75.097 1.00 43.78  ? 307 GLN B C   1 
ATOM   4926 O  O   . GLN B  1  294 ? -5.223  4.364   75.501 1.00 43.99  ? 307 GLN B O   1 
ATOM   4927 C  CB  . GLN B  1  294 ? -7.194  1.969   74.708 1.00 40.22  ? 307 GLN B CB  1 
ATOM   4928 C  CG  . GLN B  1  294 ? -8.291  1.606   73.722 1.00 43.65  ? 307 GLN B CG  1 
ATOM   4929 C  CD  . GLN B  1  294 ? -9.363  0.781   74.377 1.00 49.35  ? 307 GLN B CD  1 
ATOM   4930 O  OE1 . GLN B  1  294 ? -9.315  -0.456  74.391 1.00 50.60  ? 307 GLN B OE1 1 
ATOM   4931 N  NE2 . GLN B  1  294 ? -10.269 1.509   74.999 1.00 49.76  ? 307 GLN B NE2 1 
ATOM   4932 N  N   . GLU B  1  295 ? -4.059  2.439   75.514 1.00 44.82  ? 308 GLU B N   1 
ATOM   4933 C  CA  . GLU B  1  295 ? -3.050  2.913   76.456 1.00 43.77  ? 308 GLU B CA  1 
ATOM   4934 C  C   . GLU B  1  295 ? -2.178  3.994   75.823 1.00 45.94  ? 308 GLU B C   1 
ATOM   4935 O  O   . GLU B  1  295 ? -1.815  4.944   76.507 1.00 43.90  ? 308 GLU B O   1 
ATOM   4936 C  CB  . GLU B  1  295 ? -2.160  1.799   76.997 1.00 50.01  ? 308 GLU B CB  1 
ATOM   4937 C  CG  . GLU B  1  295 ? -2.914  0.807   77.879 1.00 56.59  ? 308 GLU B CG  1 
ATOM   4938 C  CD  . GLU B  1  295 ? -2.152  -0.461  78.232 1.00 65.94  ? 308 GLU B CD  1 
ATOM   4939 O  OE1 . GLU B  1  295 ? -0.996  -0.647  77.782 1.00 75.98  ? 308 GLU B OE1 1 
ATOM   4940 O  OE2 . GLU B  1  295 ? -2.739  -1.273  78.978 1.00 68.80  ? 308 GLU B OE2 1 
ATOM   4941 N  N   . LEU B  1  296 ? -1.851  3.868   74.525 1.00 44.63  ? 309 LEU B N   1 
ATOM   4942 C  CA  . LEU B  1  296 ? -1.103  4.900   73.822 1.00 42.19  ? 309 LEU B CA  1 
ATOM   4943 C  C   . LEU B  1  296 ? -1.947  6.151   73.603 1.00 40.94  ? 309 LEU B C   1 
ATOM   4944 O  O   . LEU B  1  296 ? -1.401  7.254   73.546 1.00 40.61  ? 309 LEU B O   1 
ATOM   4945 C  CB  . LEU B  1  296 ? -0.593  4.394   72.472 1.00 43.39  ? 309 LEU B CB  1 
ATOM   4946 C  CG  . LEU B  1  296 ? 0.409   3.239   72.516 1.00 45.65  ? 309 LEU B CG  1 
ATOM   4947 C  CD1 . LEU B  1  296 ? 0.675   2.740   71.103 1.00 45.79  ? 309 LEU B CD1 1 
ATOM   4948 C  CD2 . LEU B  1  296 ? 1.710   3.670   73.192 1.00 44.21  ? 309 LEU B CD2 1 
ATOM   4949 N  N   . TYR B  1  297 ? -3.246  5.964   73.357 1.00 41.58  ? 310 TYR B N   1 
ATOM   4950 C  CA  . TYR B  1  297 ? -4.120  7.054   72.949 1.00 43.52  ? 310 TYR B CA  1 
ATOM   4951 C  C   . TYR B  1  297 ? -5.381  7.037   73.817 1.00 51.51  ? 310 TYR B C   1 
ATOM   4952 O  O   . TYR B  1  297 ? -6.432  6.595   73.364 1.00 44.33  ? 310 TYR B O   1 
ATOM   4953 C  CB  . TYR B  1  297 ? -4.490  6.925   71.470 1.00 45.98  ? 310 TYR B CB  1 
ATOM   4954 C  CG  . TYR B  1  297 ? -3.326  7.035   70.500 1.00 46.16  ? 310 TYR B CG  1 
ATOM   4955 C  CD1 . TYR B  1  297 ? -2.833  8.272   70.126 1.00 44.44  ? 310 TYR B CD1 1 
ATOM   4956 C  CD2 . TYR B  1  297 ? -2.717  5.903   69.969 1.00 44.00  ? 310 TYR B CD2 1 
ATOM   4957 C  CE1 . TYR B  1  297 ? -1.761  8.384   69.260 1.00 45.92  ? 310 TYR B CE1 1 
ATOM   4958 C  CE2 . TYR B  1  297 ? -1.642  6.004   69.092 1.00 44.73  ? 310 TYR B CE2 1 
ATOM   4959 C  CZ  . TYR B  1  297 ? -1.174  7.250   68.724 1.00 44.99  ? 310 TYR B CZ  1 
ATOM   4960 O  OH  . TYR B  1  297 ? -0.139  7.409   67.851 1.00 43.51  ? 310 TYR B OH  1 
ATOM   4961 N  N   . PRO B  1  298 ? -5.315  7.432   75.111 1.00 49.14  ? 311 PRO B N   1 
ATOM   4962 C  CA  . PRO B  1  298 ? -6.488  7.325   75.990 1.00 49.40  ? 311 PRO B CA  1 
ATOM   4963 C  C   . PRO B  1  298 ? -7.655  8.247   75.652 1.00 48.87  ? 311 PRO B C   1 
ATOM   4964 O  O   . PRO B  1  298 ? -8.805  7.862   75.818 1.00 56.65  ? 311 PRO B O   1 
ATOM   4965 C  CB  . PRO B  1  298 ? -5.968  7.558   77.406 1.00 51.37  ? 311 PRO B CB  1 
ATOM   4966 C  CG  . PRO B  1  298 ? -4.573  8.151   77.226 1.00 53.41  ? 311 PRO B CG  1 
ATOM   4967 C  CD  . PRO B  1  298 ? -4.094  7.877   75.798 1.00 49.95  ? 311 PRO B CD  1 
ATOM   4968 N  N   . ASN B  1  299 ? -7.372  9.439   75.121 1.00 49.51  ? 312 ASN B N   1 
ATOM   4969 C  CA  . ASN B  1  299 ? -8.413  10.419  74.873 1.00 52.12  ? 312 ASN B CA  1 
ATOM   4970 C  C   . ASN B  1  299 ? -8.037  11.270  73.670 1.00 54.15  ? 312 ASN B C   1 
ATOM   4971 O  O   . ASN B  1  299 ? -7.865  12.483  73.791 1.00 62.73  ? 312 ASN B O   1 
ATOM   4972 C  CB  . ASN B  1  299 ? -8.655  11.321  76.082 1.00 55.91  ? 312 ASN B CB  1 
ATOM   4973 C  CG  . ASN B  1  299 ? -9.034  10.561  77.328 1.00 62.96  ? 312 ASN B CG  1 
ATOM   4974 O  OD1 . ASN B  1  299 ? -8.288  10.564  78.316 1.00 71.98  ? 312 ASN B OD1 1 
ATOM   4975 N  ND2 . ASN B  1  299 ? -10.182 9.897   77.294 1.00 63.14  ? 312 ASN B ND2 1 
ATOM   4976 N  N   . PRO B  1  300 ? -7.968  10.680  72.451 1.00 49.77  ? 313 PRO B N   1 
ATOM   4977 C  CA  . PRO B  1  300 ? -7.644  11.454  71.261 1.00 49.40  ? 313 PRO B CA  1 
ATOM   4978 C  C   . PRO B  1  300 ? -8.836  12.298  70.810 1.00 50.78  ? 313 PRO B C   1 
ATOM   4979 O  O   . PRO B  1  300 ? -9.997  11.962  71.076 1.00 46.80  ? 313 PRO B O   1 
ATOM   4980 C  CB  . PRO B  1  300 ? -7.287  10.331  70.274 1.00 49.17  ? 313 PRO B CB  1 
ATOM   4981 C  CG  . PRO B  1  300 ? -8.218  9.190   70.641 1.00 44.43  ? 313 PRO B CG  1 
ATOM   4982 C  CD  . PRO B  1  300 ? -8.264  9.269   72.145 1.00 47.01  ? 313 PRO B CD  1 
ATOM   4983 N  N   . THR B  1  301 ? -8.530  13.380  70.094 1.00 55.00  ? 314 THR B N   1 
ATOM   4984 C  CA  . THR B  1  301 ? -9.551  14.228  69.506 1.00 60.28  ? 314 THR B CA  1 
ATOM   4985 C  C   . THR B  1  301 ? -9.126  14.563  68.085 1.00 57.90  ? 314 THR B C   1 
ATOM   4986 O  O   . THR B  1  301 ? -8.020  14.235  67.685 1.00 58.23  ? 314 THR B O   1 
ATOM   4987 C  CB  . THR B  1  301 ? -9.729  15.489  70.367 1.00 63.78  ? 314 THR B CB  1 
ATOM   4988 O  OG1 . THR B  1  301 ? -8.469  16.147  70.470 1.00 65.80  ? 314 THR B OG1 1 
ATOM   4989 C  CG2 . THR B  1  301 ? -10.187 15.184  71.782 1.00 63.42  ? 314 THR B CG2 1 
ATOM   4990 N  N   . GLY B  1  302 ? -10.020 15.223  67.348 1.00 54.75  ? 315 GLY B N   1 
ATOM   4991 C  CA  . GLY B  1  302 ? -9.719  15.759  66.030 1.00 60.17  ? 315 GLY B CA  1 
ATOM   4992 C  C   . GLY B  1  302 ? -9.335  14.672  65.025 1.00 60.34  ? 315 GLY B C   1 
ATOM   4993 O  O   . GLY B  1  302 ? -9.893  13.567  65.032 1.00 50.84  ? 315 GLY B O   1 
ATOM   4994 N  N   . ILE B  1  303 ? -8.361  15.022  64.168 1.00 65.45  ? 316 ILE B N   1 
ATOM   4995 C  CA  . ILE B  1  303 ? -7.890  14.160  63.090 1.00 64.01  ? 316 ILE B CA  1 
ATOM   4996 C  C   . ILE B  1  303 ? -7.265  12.896  63.681 1.00 52.05  ? 316 ILE B C   1 
ATOM   4997 O  O   . ILE B  1  303 ? -7.454  11.825  63.132 1.00 52.76  ? 316 ILE B O   1 
ATOM   4998 C  CB  . ILE B  1  303 ? -6.921  14.909  62.152 1.00 69.87  ? 316 ILE B CB  1 
ATOM   4999 C  CG1 . ILE B  1  303 ? -7.546  16.194  61.605 1.00 91.29  ? 316 ILE B CG1 1 
ATOM   5000 C  CG2 . ILE B  1  303 ? -6.473  14.022  60.994 1.00 69.15  ? 316 ILE B CG2 1 
ATOM   5001 C  CD1 . ILE B  1  303 ? -6.541  17.201  61.075 1.00 99.30  ? 316 ILE B CD1 1 
ATOM   5002 N  N   . LEU B  1  304 ? -6.560  13.000  64.806 1.00 45.38  ? 317 LEU B N   1 
ATOM   5003 C  CA  . LEU B  1  304 ? -5.967  11.837  65.449 1.00 48.21  ? 317 LEU B CA  1 
ATOM   5004 C  C   . LEU B  1  304 ? -7.036  10.802  65.799 1.00 50.65  ? 317 LEU B C   1 
ATOM   5005 O  O   . LEU B  1  304 ? -6.872  9.619   65.521 1.00 44.32  ? 317 LEU B O   1 
ATOM   5006 C  CB  . LEU B  1  304 ? -5.170  12.260  66.684 1.00 44.11  ? 317 LEU B CB  1 
ATOM   5007 C  CG  . LEU B  1  304 ? -4.551  11.128  67.507 1.00 50.06  ? 317 LEU B CG  1 
ATOM   5008 C  CD1 . LEU B  1  304 ? -3.635  10.285  66.637 1.00 50.95  ? 317 LEU B CD1 1 
ATOM   5009 C  CD2 . LEU B  1  304 ? -3.799  11.700  68.699 1.00 50.70  ? 317 LEU B CD2 1 
ATOM   5010 N  N   . ARG B  1  305 ? -8.144  11.247  66.400 1.00 50.63  ? 318 ARG B N   1 
ATOM   5011 C  CA  A ARG B  1  305 ? -9.226  10.352  66.768 0.50 49.92  ? 318 ARG B CA  1 
ATOM   5012 C  CA  B ARG B  1  305 ? -9.221  10.343  66.769 0.50 47.86  ? 318 ARG B CA  1 
ATOM   5013 C  C   . ARG B  1  305 ? -9.787  9.692   65.507 1.00 46.23  ? 318 ARG B C   1 
ATOM   5014 O  O   . ARG B  1  305 ? -10.007 8.475   65.459 1.00 45.74  ? 318 ARG B O   1 
ATOM   5015 C  CB  A ARG B  1  305 ? -10.331 11.109  67.526 0.50 52.29  ? 318 ARG B CB  1 
ATOM   5016 C  CB  B ARG B  1  305 ? -10.333 11.053  67.561 0.50 47.17  ? 318 ARG B CB  1 
ATOM   5017 C  CG  A ARG B  1  305 ? -11.490 10.174  67.878 0.50 53.72  ? 318 ARG B CG  1 
ATOM   5018 C  CG  B ARG B  1  305 ? -11.564 10.171  67.772 0.50 46.01  ? 318 ARG B CG  1 
ATOM   5019 C  CD  A ARG B  1  305 ? -12.792 10.876  68.328 0.50 55.13  ? 318 ARG B CD  1 
ATOM   5020 C  CD  B ARG B  1  305 ? -12.664 10.674  68.724 0.50 43.64  ? 318 ARG B CD  1 
ATOM   5021 N  NE  A ARG B  1  305 ? -13.972 9.994   68.418 0.50 51.67  ? 318 ARG B NE  1 
ATOM   5022 N  NE  B ARG B  1  305 ? -12.283 10.556  70.132 0.50 40.60  ? 318 ARG B NE  1 
ATOM   5023 C  CZ  A ARG B  1  305 ? -14.985 9.935   67.535 0.50 45.70  ? 318 ARG B CZ  1 
ATOM   5024 C  CZ  B ARG B  1  305 ? -12.746 9.671   70.997 0.50 35.21  ? 318 ARG B CZ  1 
ATOM   5025 N  NH1 A ARG B  1  305 ? -14.978 10.640  66.421 0.50 50.49  ? 318 ARG B NH1 1 
ATOM   5026 N  NH1 B ARG B  1  305 ? -12.139 9.543   72.150 0.50 34.78  ? 318 ARG B NH1 1 
ATOM   5027 N  NH2 A ARG B  1  305 ? -16.024 9.160   67.763 0.50 45.68  ? 318 ARG B NH2 1 
ATOM   5028 N  NH2 B ARG B  1  305 ? -13.730 8.860   70.697 0.50 34.47  ? 318 ARG B NH2 1 
ATOM   5029 N  N   . ARG B  1  306 ? -10.049 10.518  64.497 1.00 42.06  ? 319 ARG B N   1 
ATOM   5030 C  CA  . ARG B  1  306 ? -10.632 10.045  63.252 1.00 49.00  ? 319 ARG B CA  1 
ATOM   5031 C  C   . ARG B  1  306 ? -9.720  8.999   62.597 1.00 45.41  ? 319 ARG B C   1 
ATOM   5032 O  O   . ARG B  1  306 ? -10.186 7.961   62.138 1.00 41.88  ? 319 ARG B O   1 
ATOM   5033 C  CB  . ARG B  1  306 ? -10.838 11.261  62.348 1.00 59.69  ? 319 ARG B CB  1 
ATOM   5034 C  CG  . ARG B  1  306 ? -11.854 11.159  61.220 1.00 77.23  ? 319 ARG B CG  1 
ATOM   5035 C  CD  . ARG B  1  306 ? -11.793 12.411  60.335 1.00 89.00  ? 319 ARG B CD  1 
ATOM   5036 N  NE  . ARG B  1  306 ? -10.542 12.458  59.564 1.00 108.95 ? 319 ARG B NE  1 
ATOM   5037 C  CZ  . ARG B  1  306 ? -10.032 13.491  58.892 1.00 118.27 ? 319 ARG B CZ  1 
ATOM   5038 N  NH1 . ARG B  1  306 ? -10.676 14.646  58.854 1.00 120.43 ? 319 ARG B NH1 1 
ATOM   5039 N  NH2 . ARG B  1  306 ? -8.871  13.353  58.263 1.00 115.07 ? 319 ARG B NH2 1 
ATOM   5040 N  N   . ASN B  1  307 ? -8.416  9.280   62.551 1.00 44.26  ? 320 ASN B N   1 
ATOM   5041 C  CA  . ASN B  1  307 ? -7.463  8.403   61.882 1.00 43.41  ? 320 ASN B CA  1 
ATOM   5042 C  C   . ASN B  1  307 ? -7.269  7.122   62.678 1.00 39.57  ? 320 ASN B C   1 
ATOM   5043 O  O   . ASN B  1  307 ? -7.049  6.077   62.075 1.00 43.03  ? 320 ASN B O   1 
ATOM   5044 C  CB  . ASN B  1  307 ? -6.159  9.128   61.563 1.00 40.22  ? 320 ASN B CB  1 
ATOM   5045 C  CG  . ASN B  1  307 ? -6.331  10.075  60.398 1.00 43.82  ? 320 ASN B CG  1 
ATOM   5046 O  OD1 . ASN B  1  307 ? -7.451  10.227  59.899 1.00 44.86  ? 320 ASN B OD1 1 
ATOM   5047 N  ND2 . ASN B  1  307 ? -5.254  10.731  59.971 1.00 46.34  ? 320 ASN B ND2 1 
ATOM   5048 N  N   . LEU B  1  308 ? -7.388  7.180   64.010 1.00 38.52  ? 321 LEU B N   1 
ATOM   5049 C  CA  . LEU B  1  308 ? -7.346  5.969   64.815 1.00 41.56  ? 321 LEU B CA  1 
ATOM   5050 C  C   . LEU B  1  308 ? -8.510  5.054   64.457 1.00 41.93  ? 321 LEU B C   1 
ATOM   5051 O  O   . LEU B  1  308 ? -8.343  3.839   64.344 1.00 41.43  ? 321 LEU B O   1 
ATOM   5052 C  CB  . LEU B  1  308 ? -7.370  6.273   66.308 1.00 44.42  ? 321 LEU B CB  1 
ATOM   5053 C  CG  . LEU B  1  308 ? -6.012  6.522   66.957 1.00 46.98  ? 321 LEU B CG  1 
ATOM   5054 C  CD1 . LEU B  1  308 ? -6.187  7.290   68.258 1.00 46.79  ? 321 LEU B CD1 1 
ATOM   5055 C  CD2 . LEU B  1  308 ? -5.312  5.210   67.191 1.00 45.63  ? 321 LEU B CD2 1 
ATOM   5056 N  N   . ILE B  1  309 ? -9.707  5.634   64.345 1.00 40.52  ? 322 ILE B N   1 
ATOM   5057 C  CA  . ILE B  1  309 ? -10.895 4.854   64.063 1.00 37.84  ? 322 ILE B CA  1 
ATOM   5058 C  C   . ILE B  1  309 ? -10.729 4.153   62.711 1.00 38.20  ? 322 ILE B C   1 
ATOM   5059 O  O   . ILE B  1  309 ? -11.007 2.956   62.563 1.00 39.07  ? 322 ILE B O   1 
ATOM   5060 C  CB  . ILE B  1  309 ? -12.146 5.755   64.129 1.00 40.46  ? 322 ILE B CB  1 
ATOM   5061 C  CG1 . ILE B  1  309 ? -12.440 6.179   65.567 1.00 42.85  ? 322 ILE B CG1 1 
ATOM   5062 C  CG2 . ILE B  1  309 ? -13.339 5.045   63.503 1.00 40.97  ? 322 ILE B CG2 1 
ATOM   5063 C  CD1 . ILE B  1  309 ? -13.463 7.297   65.705 1.00 48.65  ? 322 ILE B CD1 1 
ATOM   5064 N  N   . LYS B  1  310 ? -10.259 4.904   61.718 1.00 38.42  ? 323 LYS B N   1 
ATOM   5065 C  CA  . LYS B  1  310 ? -10.093 4.363   60.375 1.00 42.35  ? 323 LYS B CA  1 
ATOM   5066 C  C   . LYS B  1  310 ? -9.033  3.252   60.339 1.00 39.34  ? 323 LYS B C   1 
ATOM   5067 O  O   . LYS B  1  310 ? -9.272  2.196   59.770 1.00 37.60  ? 323 LYS B O   1 
ATOM   5068 C  CB  . LYS B  1  310 ? -9.729  5.495   59.415 1.00 45.25  ? 323 LYS B CB  1 
ATOM   5069 C  CG  . LYS B  1  310 ? -10.879 6.409   59.094 1.00 52.39  ? 323 LYS B CG  1 
ATOM   5070 C  CD  . LYS B  1  310 ? -10.457 7.607   58.254 1.00 57.53  ? 323 LYS B CD  1 
ATOM   5071 C  CE  . LYS B  1  310 ? -11.611 8.233   57.542 1.00 63.69  ? 323 LYS B CE  1 
ATOM   5072 N  NZ  . LYS B  1  310 ? -11.185 9.501   56.957 1.00 66.30  ? 323 LYS B NZ  1 
ATOM   5073 N  N   . ASN B  1  311 ? -7.875  3.489   60.966 1.00 38.62  ? 324 ASN B N   1 
ATOM   5074 C  CA  . ASN B  1  311 ? -6.781  2.527   60.957 1.00 35.91  ? 324 ASN B CA  1 
ATOM   5075 C  C   . ASN B  1  311 ? -7.173  1.269   61.719 1.00 37.38  ? 324 ASN B C   1 
ATOM   5076 O  O   . ASN B  1  311 ? -6.839  0.170   61.313 1.00 34.80  ? 324 ASN B O   1 
ATOM   5077 C  CB  . ASN B  1  311 ? -5.494  3.142   61.482 1.00 36.85  ? 324 ASN B CB  1 
ATOM   5078 C  CG  . ASN B  1  311 ? -4.790  3.930   60.404 1.00 41.02  ? 324 ASN B CG  1 
ATOM   5079 O  OD1 . ASN B  1  311 ? -4.135  3.343   59.529 1.00 42.02  ? 324 ASN B OD1 1 
ATOM   5080 N  ND2 . ASN B  1  311 ? -4.907  5.249   60.450 1.00 41.91  ? 324 ASN B ND2 1 
ATOM   5081 N  N   . LEU B  1  312 ? -7.930  1.405   62.806 1.00 36.70  ? 325 LEU B N   1 
ATOM   5082 C  CA  . LEU B  1  312 ? -8.377  0.236   63.538 1.00 35.87  ? 325 LEU B CA  1 
ATOM   5083 C  C   . LEU B  1  312 ? -9.282  -0.613  62.655 1.00 33.07  ? 325 LEU B C   1 
ATOM   5084 O  O   . LEU B  1  312 ? -9.183  -1.837  62.675 1.00 36.81  ? 325 LEU B O   1 
ATOM   5085 C  CB  . LEU B  1  312 ? -9.077  0.651   64.832 1.00 38.81  ? 325 LEU B CB  1 
ATOM   5086 C  CG  . LEU B  1  312 ? -8.155  1.034   65.984 1.00 37.42  ? 325 LEU B CG  1 
ATOM   5087 C  CD1 . LEU B  1  312 ? -8.935  1.812   67.026 1.00 41.65  ? 325 LEU B CD1 1 
ATOM   5088 C  CD2 . LEU B  1  312 ? -7.527  -0.189  66.595 1.00 39.38  ? 325 LEU B CD2 1 
ATOM   5089 N  N   . HIS B  1  313 ? -10.173 0.049   61.909 1.00 37.08  ? 326 HIS B N   1 
ATOM   5090 C  CA  . HIS B  1  313 ? -11.051 -0.632  60.975 1.00 38.72  ? 326 HIS B CA  1 
ATOM   5091 C  C   . HIS B  1  313 ? -10.229 -1.328  59.880 1.00 36.83  ? 326 HIS B C   1 
ATOM   5092 O  O   . HIS B  1  313 ? -10.459 -2.495  59.579 1.00 35.67  ? 326 HIS B O   1 
ATOM   5093 C  CB  . HIS B  1  313 ? -12.124 0.315   60.405 1.00 38.20  ? 326 HIS B CB  1 
ATOM   5094 C  CG  . HIS B  1  313 ? -13.029 -0.420  59.474 1.00 39.86  ? 326 HIS B CG  1 
ATOM   5095 N  ND1 . HIS B  1  313 ? -13.832 -1.455  59.920 1.00 41.24  ? 326 HIS B ND1 1 
ATOM   5096 C  CD2 . HIS B  1  313 ? -13.171 -0.373  58.141 1.00 40.38  ? 326 HIS B CD2 1 
ATOM   5097 C  CE1 . HIS B  1  313 ? -14.466 -1.984  58.886 1.00 44.71  ? 326 HIS B CE1 1 
ATOM   5098 N  NE2 . HIS B  1  313 ? -14.082 -1.336  57.793 1.00 42.68  ? 326 HIS B NE2 1 
ATOM   5099 N  N   . TYR B  1  314 ? -9.271  -0.615  59.280 1.00 37.57  ? 327 TYR B N   1 
ATOM   5100 C  CA  . TYR B  1  314 ? -8.448  -1.202  58.223 1.00 38.32  ? 327 TYR B CA  1 
ATOM   5101 C  C   . TYR B  1  314 ? -7.758  -2.458  58.742 1.00 36.57  ? 327 TYR B C   1 
ATOM   5102 O  O   . TYR B  1  314 ? -7.767  -3.498  58.078 1.00 36.30  ? 327 TYR B O   1 
ATOM   5103 C  CB  . TYR B  1  314 ? -7.395  -0.216  57.731 1.00 40.51  ? 327 TYR B CB  1 
ATOM   5104 C  CG  . TYR B  1  314 ? -7.942  1.051   57.096 1.00 40.84  ? 327 TYR B CG  1 
ATOM   5105 C  CD1 . TYR B  1  314 ? -9.225  1.120   56.558 1.00 44.55  ? 327 TYR B CD1 1 
ATOM   5106 C  CD2 . TYR B  1  314 ? -7.150  2.182   57.023 1.00 44.12  ? 327 TYR B CD2 1 
ATOM   5107 C  CE1 . TYR B  1  314 ? -9.699  2.285   55.969 1.00 40.65  ? 327 TYR B CE1 1 
ATOM   5108 C  CE2 . TYR B  1  314 ? -7.610  3.350   56.435 1.00 45.33  ? 327 TYR B CE2 1 
ATOM   5109 C  CZ  . TYR B  1  314 ? -8.893  3.409   55.922 1.00 45.24  ? 327 TYR B CZ  1 
ATOM   5110 O  OH  . TYR B  1  314 ? -9.286  4.577   55.324 1.00 44.98  ? 327 TYR B OH  1 
ATOM   5111 N  N   . TRP B  1  315 ? -7.219  -2.378  59.962 1.00 35.21  ? 328 TRP B N   1 
ATOM   5112 C  CA  . TRP B  1  315 ? -6.528  -3.510  60.545 1.00 34.22  ? 328 TRP B CA  1 
ATOM   5113 C  C   . TRP B  1  315 ? -7.482  -4.690  60.684 1.00 35.23  ? 328 TRP B C   1 
ATOM   5114 O  O   . TRP B  1  315 ? -7.154  -5.824  60.310 1.00 33.98  ? 328 TRP B O   1 
ATOM   5115 C  CB  . TRP B  1  315 ? -5.884  -3.142  61.887 1.00 32.96  ? 328 TRP B CB  1 
ATOM   5116 C  CG  . TRP B  1  315 ? -4.946  -4.198  62.400 1.00 33.83  ? 328 TRP B CG  1 
ATOM   5117 C  CD1 . TRP B  1  315 ? -3.974  -4.852  61.694 1.00 35.39  ? 328 TRP B CD1 1 
ATOM   5118 C  CD2 . TRP B  1  315 ? -4.911  -4.745  63.731 1.00 35.23  ? 328 TRP B CD2 1 
ATOM   5119 N  NE1 . TRP B  1  315 ? -3.344  -5.774  62.483 1.00 34.44  ? 328 TRP B NE1 1 
ATOM   5120 C  CE2 . TRP B  1  315 ? -3.887  -5.722  63.742 1.00 34.95  ? 328 TRP B CE2 1 
ATOM   5121 C  CE3 . TRP B  1  315 ? -5.616  -4.490  64.915 1.00 34.47  ? 328 TRP B CE3 1 
ATOM   5122 C  CZ2 . TRP B  1  315 ? -3.572  -6.449  64.882 1.00 34.40  ? 328 TRP B CZ2 1 
ATOM   5123 C  CZ3 . TRP B  1  315 ? -5.292  -5.202  66.048 1.00 34.52  ? 328 TRP B CZ3 1 
ATOM   5124 C  CH2 . TRP B  1  315 ? -4.282  -6.169  66.032 1.00 37.08  ? 328 TRP B CH2 1 
ATOM   5125 N  N   . TRP B  1  316 ? -8.677  -4.408  61.209 1.00 35.91  ? 329 TRP B N   1 
ATOM   5126 C  CA  . TRP B  1  316 ? -9.669  -5.444  61.392 1.00 32.56  ? 329 TRP B CA  1 
ATOM   5127 C  C   . TRP B  1  316 ? -10.024 -6.124  60.071 1.00 29.16  ? 329 TRP B C   1 
ATOM   5128 O  O   . TRP B  1  316 ? -10.241 -7.329  60.069 1.00 34.17  ? 329 TRP B O   1 
ATOM   5129 C  CB  . TRP B  1  316 ? -10.915 -4.888  62.098 1.00 37.26  ? 329 TRP B CB  1 
ATOM   5130 C  CG  . TRP B  1  316 ? -12.012 -5.913  62.169 1.00 34.30  ? 329 TRP B CG  1 
ATOM   5131 C  CD1 . TRP B  1  316 ? -12.157 -6.892  63.093 1.00 36.55  ? 329 TRP B CD1 1 
ATOM   5132 C  CD2 . TRP B  1  316 ? -13.039 -6.125  61.182 1.00 36.23  ? 329 TRP B CD2 1 
ATOM   5133 N  NE1 . TRP B  1  316 ? -13.235 -7.669  62.788 1.00 40.61  ? 329 TRP B NE1 1 
ATOM   5134 C  CE2 . TRP B  1  316 ? -13.799 -7.221  61.626 1.00 36.87  ? 329 TRP B CE2 1 
ATOM   5135 C  CE3 . TRP B  1  316 ? -13.403 -5.477  59.994 1.00 40.54  ? 329 TRP B CE3 1 
ATOM   5136 C  CZ2 . TRP B  1  316 ? -14.901 -7.700  60.920 1.00 41.23  ? 329 TRP B CZ2 1 
ATOM   5137 C  CZ3 . TRP B  1  316 ? -14.499 -5.953  59.295 1.00 43.47  ? 329 TRP B CZ3 1 
ATOM   5138 C  CH2 . TRP B  1  316 ? -15.229 -7.055  59.751 1.00 39.62  ? 329 TRP B CH2 1 
ATOM   5139 N  N   . THR B  1  317 ? -10.053 -5.397  58.951 1.00 33.42  ? 330 THR B N   1 
ATOM   5140 C  CA  . THR B  1  317 ? -10.401 -6.014  57.677 1.00 37.47  ? 330 THR B CA  1 
ATOM   5141 C  C   . THR B  1  317 ? -9.431  -7.153  57.371 1.00 37.60  ? 330 THR B C   1 
ATOM   5142 O  O   . THR B  1  317 ? -9.851  -8.183  56.860 1.00 37.25  ? 330 THR B O   1 
ATOM   5143 C  CB  . THR B  1  317 ? -10.475 -5.053  56.489 1.00 40.45  ? 330 THR B CB  1 
ATOM   5144 O  OG1 . THR B  1  317 ? -9.183  -4.533  56.192 1.00 38.85  ? 330 THR B OG1 1 
ATOM   5145 C  CG2 . THR B  1  317 ? -11.492 -3.943  56.689 1.00 42.98  ? 330 THR B CG2 1 
ATOM   5146 N  N   . GLY B  1  318 ? -8.149  -6.987  57.694 1.00 37.47  ? 331 GLY B N   1 
ATOM   5147 C  CA  . GLY B  1  318 ? -7.210  -8.082  57.496 1.00 37.70  ? 331 GLY B CA  1 
ATOM   5148 C  C   . GLY B  1  318 ? -7.303  -9.135  58.600 1.00 35.43  ? 331 GLY B C   1 
ATOM   5149 O  O   . GLY B  1  318 ? -7.244  -10.338 58.333 1.00 36.23  ? 331 GLY B O   1 
ATOM   5150 N  N   . VAL B  1  319 ? -7.398  -8.683  59.853 1.00 33.93  ? 332 VAL B N   1 
ATOM   5151 C  CA  . VAL B  1  319 ? -7.456  -9.599  60.985 1.00 34.05  ? 332 VAL B CA  1 
ATOM   5152 C  C   . VAL B  1  319 ? -8.638  -10.552 60.838 1.00 32.98  ? 332 VAL B C   1 
ATOM   5153 O  O   . VAL B  1  319 ? -8.524  -11.743 61.127 1.00 34.71  ? 332 VAL B O   1 
ATOM   5154 C  CB  . VAL B  1  319 ? -7.537  -8.807  62.301 1.00 36.53  ? 332 VAL B CB  1 
ATOM   5155 C  CG1 . VAL B  1  319 ? -8.022  -9.654  63.478 1.00 37.61  ? 332 VAL B CG1 1 
ATOM   5156 C  CG2 . VAL B  1  319 ? -6.204  -8.166  62.635 1.00 37.72  ? 332 VAL B CG2 1 
ATOM   5157 N  N   . ASN B  1  320 ? -9.788  -10.011 60.433 1.00 35.02  ? 333 ASN B N   1 
ATOM   5158 C  CA  . ASN B  1  320 ? -11.010 -10.801 60.367 1.00 36.25  ? 333 ASN B CA  1 
ATOM   5159 C  C   . ASN B  1  320 ? -10.815 -12.021 59.471 1.00 39.37  ? 333 ASN B C   1 
ATOM   5160 O  O   . ASN B  1  320 ? -11.255 -13.112 59.810 1.00 37.11  ? 333 ASN B O   1 
ATOM   5161 C  CB  . ASN B  1  320 ? -12.187 -9.975  59.874 1.00 38.81  ? 333 ASN B CB  1 
ATOM   5162 C  CG  . ASN B  1  320 ? -13.487 -10.703 60.099 1.00 41.24  ? 333 ASN B CG  1 
ATOM   5163 O  OD1 . ASN B  1  320 ? -13.745 -11.183 61.205 1.00 43.59  ? 333 ASN B OD1 1 
ATOM   5164 N  ND2 . ASN B  1  320 ? -14.299 -10.830 59.071 1.00 38.78  ? 333 ASN B ND2 1 
ATOM   5165 N  N   . VAL B  1  321 ? -10.097 -11.843 58.352 1.00 43.28  ? 334 VAL B N   1 
ATOM   5166 C  CA  . VAL B  1  321 ? -9.815  -12.954 57.456 1.00 40.06  ? 334 VAL B CA  1 
ATOM   5167 C  C   . VAL B  1  321 ? -8.670  -13.795 58.016 1.00 39.75  ? 334 VAL B C   1 
ATOM   5168 O  O   . VAL B  1  321 ? -8.802  -14.998 58.169 1.00 40.26  ? 334 VAL B O   1 
ATOM   5169 C  CB  . VAL B  1  321 ? -9.519  -12.516 56.010 1.00 43.53  ? 334 VAL B CB  1 
ATOM   5170 C  CG1 . VAL B  1  321 ? -9.359  -13.738 55.108 1.00 47.89  ? 334 VAL B CG1 1 
ATOM   5171 C  CG2 . VAL B  1  321 ? -10.593 -11.583 55.455 1.00 42.23  ? 334 VAL B CG2 1 
ATOM   5172 N  N   . ALA B  1  322 ? -7.536  -13.176 58.343 1.00 41.09  ? 335 ALA B N   1 
ATOM   5173 C  CA  . ALA B  1  322 ? -6.355  -13.945 58.709 1.00 41.56  ? 335 ALA B CA  1 
ATOM   5174 C  C   . ALA B  1  322 ? -6.577  -14.784 59.967 1.00 43.81  ? 335 ALA B C   1 
ATOM   5175 O  O   . ALA B  1  322 ? -5.976  -15.852 60.107 1.00 44.52  ? 335 ALA B O   1 
ATOM   5176 C  CB  . ALA B  1  322 ? -5.166  -13.032 58.882 1.00 43.68  ? 335 ALA B CB  1 
ATOM   5177 N  N   . PHE B  1  323 ? -7.409  -14.299 60.901 1.00 42.38  ? 336 PHE B N   1 
ATOM   5178 C  CA  . PHE B  1  323 ? -7.570  -14.976 62.178 1.00 42.83  ? 336 PHE B CA  1 
ATOM   5179 C  C   . PHE B  1  323 ? -8.839  -15.821 62.194 1.00 49.16  ? 336 PHE B C   1 
ATOM   5180 O  O   . PHE B  1  323 ? -9.165  -16.400 63.218 1.00 50.10  ? 336 PHE B O   1 
ATOM   5181 C  CB  . PHE B  1  323 ? -7.616  -13.987 63.343 1.00 43.60  ? 336 PHE B CB  1 
ATOM   5182 C  CG  . PHE B  1  323 ? -6.319  -13.268 63.679 1.00 44.31  ? 336 PHE B CG  1 
ATOM   5183 C  CD1 . PHE B  1  323 ? -5.164  -13.428 62.911 1.00 45.70  ? 336 PHE B CD1 1 
ATOM   5184 C  CD2 . PHE B  1  323 ? -6.270  -12.391 64.754 1.00 42.45  ? 336 PHE B CD2 1 
ATOM   5185 C  CE1 . PHE B  1  323 ? -3.999  -12.740 63.227 1.00 45.34  ? 336 PHE B CE1 1 
ATOM   5186 C  CE2 . PHE B  1  323 ? -5.106  -11.710 65.066 1.00 44.00  ? 336 PHE B CE2 1 
ATOM   5187 C  CZ  . PHE B  1  323 ? -3.966  -11.892 64.307 1.00 46.16  ? 336 PHE B CZ  1 
ATOM   5188 N  N   . GLY B  1  324 ? -9.568  -15.865 61.080 1.00 51.72  ? 337 GLY B N   1 
ATOM   5189 C  CA  . GLY B  1  324 ? -10.725 -16.737 60.967 1.00 54.90  ? 337 GLY B CA  1 
ATOM   5190 C  C   . GLY B  1  324 ? -11.946 -16.198 61.709 1.00 51.31  ? 337 GLY B C   1 
ATOM   5191 O  O   . GLY B  1  324 ? -12.769 -16.984 62.157 1.00 53.46  ? 337 GLY B O   1 
ATOM   5192 N  N   . GLY B  1  325 ? -12.073 -14.869 61.800 1.00 48.26  ? 338 GLY B N   1 
ATOM   5193 C  CA  . GLY B  1  325 ? -13.272 -14.221 62.319 1.00 47.86  ? 338 GLY B CA  1 
ATOM   5194 C  C   . GLY B  1  325 ? -13.058 -13.687 63.735 1.00 45.30  ? 338 GLY B C   1 
ATOM   5195 O  O   . GLY B  1  325 ? -12.829 -14.468 64.650 1.00 42.61  ? 338 GLY B O   1 
ATOM   5196 N  N   . CYS B  1  326 ? -13.072 -12.356 63.889 1.00 43.44  ? 339 CYS B N   1 
ATOM   5197 C  CA  . CYS B  1  326 ? -12.969 -11.706 65.187 1.00 46.39  ? 339 CYS B CA  1 
ATOM   5198 C  C   . CYS B  1  326 ? -14.021 -10.609 65.220 1.00 46.15  ? 339 CYS B C   1 
ATOM   5199 O  O   . CYS B  1  326 ? -14.202 -9.897  64.227 1.00 40.78  ? 339 CYS B O   1 
ATOM   5200 C  CB  . CYS B  1  326 ? -11.608 -11.054 65.448 1.00 48.41  ? 339 CYS B CB  1 
ATOM   5201 S  SG  . CYS B  1  326 ? -10.208 -12.202 65.547 1.00 61.76  ? 339 CYS B SG  1 
ATOM   5202 N  N   . ASP B  1  327 ? -14.703 -10.476 66.360 1.00 47.06  ? 340 ASP B N   1 
ATOM   5203 C  CA  . ASP B  1  327 ? -15.688 -9.416  66.520 1.00 44.42  ? 340 ASP B CA  1 
ATOM   5204 C  C   . ASP B  1  327 ? -14.950 -8.082  66.551 1.00 40.78  ? 340 ASP B C   1 
ATOM   5205 O  O   . ASP B  1  327 ? -14.067 -7.889  67.396 1.00 41.68  ? 340 ASP B O   1 
ATOM   5206 C  CB  . ASP B  1  327 ? -16.480 -9.544  67.816 1.00 50.35  ? 340 ASP B CB  1 
ATOM   5207 C  CG  . ASP B  1  327 ? -17.203 -10.859 68.070 1.00 56.48  ? 340 ASP B CG  1 
ATOM   5208 O  OD1 . ASP B  1  327 ? -17.441 -11.597 67.092 1.00 54.35  ? 340 ASP B OD1 1 
ATOM   5209 O  OD2 . ASP B  1  327 ? -17.488 -11.133 69.257 1.00 60.33  ? 340 ASP B OD2 1 
ATOM   5210 N  N   . GLU B  1  328 ? -15.328 -7.168  65.651 1.00 37.63  ? 341 GLU B N   1 
ATOM   5211 C  CA  . GLU B  1  328 ? -14.690 -5.871  65.574 1.00 37.59  ? 341 GLU B CA  1 
ATOM   5212 C  C   . GLU B  1  328 ? -14.967 -5.081  66.846 1.00 42.62  ? 341 GLU B C   1 
ATOM   5213 O  O   . GLU B  1  328 ? -16.093 -5.085  67.353 1.00 39.46  ? 341 GLU B O   1 
ATOM   5214 C  CB  . GLU B  1  328 ? -15.177 -5.098  64.356 1.00 38.79  ? 341 GLU B CB  1 
ATOM   5215 C  CG  . GLU B  1  328 ? -14.366 -3.828  64.114 1.00 41.24  ? 341 GLU B CG  1 
ATOM   5216 C  CD  . GLU B  1  328 ? -14.633 -3.160  62.778 1.00 39.13  ? 341 GLU B CD  1 
ATOM   5217 O  OE1 . GLU B  1  328 ? -15.551 -3.610  62.075 1.00 44.45  ? 341 GLU B OE1 1 
ATOM   5218 O  OE2 . GLU B  1  328 ? -13.935 -2.191  62.454 1.00 42.96  ? 341 GLU B OE2 1 
ATOM   5219 N  N   . LEU B  1  329 ? -13.917 -4.412  67.347 1.00 40.22  ? 342 LEU B N   1 
ATOM   5220 C  CA  . LEU B  1  329 ? -14.038 -3.526  68.490 1.00 41.58  ? 342 LEU B CA  1 
ATOM   5221 C  C   . LEU B  1  329 ? -13.970 -2.082  68.001 1.00 40.03  ? 342 LEU B C   1 
ATOM   5222 O  O   . LEU B  1  329 ? -13.278 -1.769  67.031 1.00 43.81  ? 342 LEU B O   1 
ATOM   5223 C  CB  . LEU B  1  329 ? -12.947 -3.844  69.514 1.00 39.70  ? 342 LEU B CB  1 
ATOM   5224 C  CG  . LEU B  1  329 ? -12.965 -5.266  70.091 1.00 45.25  ? 342 LEU B CG  1 
ATOM   5225 C  CD1 . LEU B  1  329 ? -11.758 -5.514  70.966 1.00 43.88  ? 342 LEU B CD1 1 
ATOM   5226 C  CD2 . LEU B  1  329 ? -14.238 -5.634  70.851 1.00 45.91  ? 342 LEU B CD2 1 
ATOM   5227 N  N   . PHE B  1  330 ? -14.686 -1.201  68.699 1.00 37.45  ? 343 PHE B N   1 
ATOM   5228 C  CA  . PHE B  1  330 ? -14.767 0.212   68.360 1.00 36.94  ? 343 PHE B CA  1 
ATOM   5229 C  C   . PHE B  1  330 ? -14.464 1.023   69.620 1.00 44.79  ? 343 PHE B C   1 
ATOM   5230 O  O   . PHE B  1  330 ? -15.348 1.651   70.216 1.00 45.42  ? 343 PHE B O   1 
ATOM   5231 C  CB  . PHE B  1  330 ? -16.140 0.577   67.799 1.00 38.84  ? 343 PHE B CB  1 
ATOM   5232 C  CG  . PHE B  1  330 ? -16.571 -0.293  66.634 1.00 36.67  ? 343 PHE B CG  1 
ATOM   5233 C  CD1 . PHE B  1  330 ? -16.133 -0.003  65.353 1.00 40.68  ? 343 PHE B CD1 1 
ATOM   5234 C  CD2 . PHE B  1  330 ? -17.395 -1.395  66.823 1.00 41.57  ? 343 PHE B CD2 1 
ATOM   5235 C  CE1 . PHE B  1  330 ? -16.572 -0.760  64.274 1.00 40.25  ? 343 PHE B CE1 1 
ATOM   5236 C  CE2 . PHE B  1  330 ? -17.767 -2.192  65.757 1.00 46.36  ? 343 PHE B CE2 1 
ATOM   5237 C  CZ  . PHE B  1  330 ? -17.360 -1.874  64.486 1.00 43.55  ? 343 PHE B CZ  1 
ATOM   5238 N  N   . PRO B  1  331 ? -13.190 1.041   70.069 1.00 43.52  ? 344 PRO B N   1 
ATOM   5239 C  CA  . PRO B  1  331 ? -12.840 1.707   71.323 1.00 42.76  ? 344 PRO B CA  1 
ATOM   5240 C  C   . PRO B  1  331 ? -13.104 3.207   71.338 1.00 41.00  ? 344 PRO B C   1 
ATOM   5241 O  O   . PRO B  1  331 ? -13.185 3.792   72.409 1.00 40.94  ? 344 PRO B O   1 
ATOM   5242 C  CB  . PRO B  1  331 ? -11.346 1.372   71.499 1.00 45.81  ? 344 PRO B CB  1 
ATOM   5243 C  CG  . PRO B  1  331 ? -10.871 1.108   70.089 1.00 47.63  ? 344 PRO B CG  1 
ATOM   5244 C  CD  . PRO B  1  331 ? -12.035 0.390   69.421 1.00 45.27  ? 344 PRO B CD  1 
ATOM   5245 N  N   . TYR B  1  332 ? -13.250 3.820   70.166 1.00 37.98  ? 345 TYR B N   1 
ATOM   5246 C  CA  . TYR B  1  332 ? -13.490 5.251   70.075 1.00 39.51  ? 345 TYR B CA  1 
ATOM   5247 C  C   . TYR B  1  332 ? -14.824 5.559   69.392 1.00 41.00  ? 345 TYR B C   1 
ATOM   5248 O  O   . TYR B  1  332 ? -15.019 6.675   68.908 1.00 42.34  ? 345 TYR B O   1 
ATOM   5249 C  CB  . TYR B  1  332 ? -12.331 5.889   69.310 1.00 40.91  ? 345 TYR B CB  1 
ATOM   5250 C  CG  . TYR B  1  332 ? -10.977 5.581   69.918 1.00 42.56  ? 345 TYR B CG  1 
ATOM   5251 C  CD1 . TYR B  1  332 ? -10.617 6.125   71.138 1.00 42.19  ? 345 TYR B CD1 1 
ATOM   5252 C  CD2 . TYR B  1  332 ? -10.059 4.764   69.262 1.00 41.88  ? 345 TYR B CD2 1 
ATOM   5253 C  CE1 . TYR B  1  332 ? -9.371  5.884   71.693 1.00 45.90  ? 345 TYR B CE1 1 
ATOM   5254 C  CE2 . TYR B  1  332 ? -8.832  4.469   69.833 1.00 42.96  ? 345 TYR B CE2 1 
ATOM   5255 C  CZ  . TYR B  1  332 ? -8.476  5.045   71.039 1.00 46.63  ? 345 TYR B CZ  1 
ATOM   5256 O  OH  . TYR B  1  332 ? -7.248  4.766   71.556 1.00 41.05  ? 345 TYR B OH  1 
ATOM   5257 N  N   . GLY B  1  333 ? -15.727 4.571   69.349 1.00 42.47  ? 346 GLY B N   1 
ATOM   5258 C  CA  . GLY B  1  333 ? -16.973 4.707   68.617 1.00 46.99  ? 346 GLY B CA  1 
ATOM   5259 C  C   . GLY B  1  333 ? -16.726 4.636   67.111 1.00 53.97  ? 346 GLY B C   1 
ATOM   5260 O  O   . GLY B  1  333 ? -15.731 4.059   66.667 1.00 52.88  ? 346 GLY B O   1 
ATOM   5261 N  N   . GLN B  1  334 ? -17.651 5.242   66.345 1.00 61.67  ? 347 GLN B N   1 
ATOM   5262 C  CA  A GLN B  1  334 ? -17.602 5.231   64.885 0.50 64.53  ? 347 GLN B CA  1 
ATOM   5263 C  CA  B GLN B  1  334 ? -17.639 5.237   64.890 0.50 67.87  ? 347 GLN B CA  1 
ATOM   5264 C  C   . GLN B  1  334 ? -17.511 6.662   64.354 1.00 68.77  ? 347 GLN B C   1 
ATOM   5265 O  O   . GLN B  1  334 ? -17.515 7.620   65.124 1.00 71.74  ? 347 GLN B O   1 
ATOM   5266 C  CB  A GLN B  1  334 ? -18.705 4.350   64.286 0.50 62.61  ? 347 GLN B CB  1 
ATOM   5267 C  CB  B GLN B  1  334 ? -18.923 4.622   64.339 0.50 70.82  ? 347 GLN B CB  1 
ATOM   5268 C  CG  A GLN B  1  334 ? -18.312 2.881   64.430 0.50 61.58  ? 347 GLN B CG  1 
ATOM   5269 C  CG  B GLN B  1  334 ? -18.839 3.122   64.087 0.50 76.40  ? 347 GLN B CG  1 
ATOM   5270 C  CD  A GLN B  1  334 ? -19.231 1.852   63.810 0.50 55.49  ? 347 GLN B CD  1 
ATOM   5271 C  CD  B GLN B  1  334 ? -19.580 2.309   65.121 0.50 80.66  ? 347 GLN B CD  1 
ATOM   5272 O  OE1 A GLN B  1  334 ? -19.236 1.623   62.597 0.50 55.63  ? 347 GLN B OE1 1 
ATOM   5273 O  OE1 B GLN B  1  334 ? -20.674 1.798   64.857 0.50 83.76  ? 347 GLN B OE1 1 
ATOM   5274 N  NE2 A GLN B  1  334 ? -19.910 1.112   64.670 0.50 53.17  ? 347 GLN B NE2 1 
ATOM   5275 N  NE2 B GLN B  1  334 ? -19.003 2.189   66.307 0.50 87.96  ? 347 GLN B NE2 1 
ATOM   5276 N  N   . LEU B  1  335 ? -17.333 6.776   63.030 1.00 72.43  ? 348 LEU B N   1 
ATOM   5277 C  CA  . LEU B  1  335 ? -17.215 8.063   62.362 1.00 80.57  ? 348 LEU B CA  1 
ATOM   5278 C  C   . LEU B  1  335 ? -18.608 8.694   62.217 1.00 80.57  ? 348 LEU B C   1 
ATOM   5279 O  O   . LEU B  1  335 ? -19.580 7.915   62.149 1.00 83.39  ? 348 LEU B O   1 
ATOM   5280 C  CB  . LEU B  1  335 ? -16.510 7.873   61.018 1.00 86.79  ? 348 LEU B CB  1 
ATOM   5281 C  CG  . LEU B  1  335 ? -15.005 7.582   61.102 1.00 90.65  ? 348 LEU B CG  1 
ATOM   5282 C  CD1 . LEU B  1  335 ? -14.397 7.429   59.723 1.00 91.29  ? 348 LEU B CD1 1 
ATOM   5283 C  CD2 . LEU B  1  335 ? -14.228 8.632   61.893 1.00 91.15  ? 348 LEU B CD2 1 
ATOM   5284 N  N   . GLN C  1  1   ? 4.980   -17.354 26.991 1.00 136.38 ? 14  GLN C N   1 
ATOM   5285 C  CA  . GLN C  1  1   ? 5.565   -17.098 25.645 1.00 133.38 ? 14  GLN C CA  1 
ATOM   5286 C  C   . GLN C  1  1   ? 5.018   -15.772 25.110 1.00 125.14 ? 14  GLN C C   1 
ATOM   5287 O  O   . GLN C  1  1   ? 4.652   -14.915 25.910 1.00 129.58 ? 14  GLN C O   1 
ATOM   5288 C  CB  . GLN C  1  1   ? 5.253   -18.298 24.753 1.00 132.72 ? 14  GLN C CB  1 
ATOM   5289 C  CG  . GLN C  1  1   ? 6.085   -18.346 23.477 1.00 134.72 ? 14  GLN C CG  1 
ATOM   5290 C  CD  . GLN C  1  1   ? 5.794   -19.547 22.608 1.00 137.11 ? 14  GLN C CD  1 
ATOM   5291 O  OE1 . GLN C  1  1   ? 5.116   -20.498 23.013 1.00 139.84 ? 14  GLN C OE1 1 
ATOM   5292 N  NE2 . GLN C  1  1   ? 6.315   -19.511 21.391 1.00 138.99 ? 14  GLN C NE2 1 
ATOM   5293 N  N   . GLY C  1  2   ? 4.988   -15.593 23.781 1.00 105.14 ? 15  GLY C N   1 
ATOM   5294 C  CA  . GLY C  1  2   ? 4.326   -14.459 23.158 1.00 82.92  ? 15  GLY C CA  1 
ATOM   5295 C  C   . GLY C  1  2   ? 4.083   -14.666 21.662 1.00 72.36  ? 15  GLY C C   1 
ATOM   5296 O  O   . GLY C  1  2   ? 4.119   -15.783 21.162 1.00 69.81  ? 15  GLY C O   1 
ATOM   5297 N  N   . VAL C  1  3   ? 3.840   -13.552 20.963 1.00 62.69  ? 16  VAL C N   1 
ATOM   5298 C  CA  . VAL C  1  3   ? 3.419   -13.540 19.571 1.00 59.24  ? 16  VAL C CA  1 
ATOM   5299 C  C   . VAL C  1  3   ? 4.548   -12.999 18.696 1.00 58.37  ? 16  VAL C C   1 
ATOM   5300 O  O   . VAL C  1  3   ? 5.369   -12.204 19.151 1.00 48.41  ? 16  VAL C O   1 
ATOM   5301 C  CB  . VAL C  1  3   ? 2.152   -12.662 19.513 1.00 63.11  ? 16  VAL C CB  1 
ATOM   5302 C  CG1 . VAL C  1  3   ? 1.769   -12.223 18.105 1.00 69.02  ? 16  VAL C CG1 1 
ATOM   5303 C  CG2 . VAL C  1  3   ? 0.985   -13.357 20.204 1.00 66.51  ? 16  VAL C CG2 1 
ATOM   5304 N  N   . ASP C  1  4   ? 4.555   -13.405 17.419 1.00 52.41  ? 17  ASP C N   1 
ATOM   5305 C  CA  . ASP C  1  4   ? 5.419   -12.827 16.400 1.00 52.62  ? 17  ASP C CA  1 
ATOM   5306 C  C   . ASP C  1  4   ? 4.619   -11.800 15.590 1.00 50.34  ? 17  ASP C C   1 
ATOM   5307 O  O   . ASP C  1  4   ? 3.768   -12.179 14.796 1.00 49.06  ? 17  ASP C O   1 
ATOM   5308 C  CB  . ASP C  1  4   ? 5.990   -13.936 15.532 1.00 58.56  ? 17  ASP C CB  1 
ATOM   5309 C  CG  . ASP C  1  4   ? 7.232   -13.582 14.730 1.00 67.51  ? 17  ASP C CG  1 
ATOM   5310 O  OD1 . ASP C  1  4   ? 7.670   -12.415 14.793 1.00 72.50  ? 17  ASP C OD1 1 
ATOM   5311 O  OD2 . ASP C  1  4   ? 7.764   -14.484 14.057 1.00 77.25  ? 17  ASP C OD2 1 
ATOM   5312 N  N   . PRO C  1  5   ? 4.824   -10.473 15.778 1.00 44.95  ? 18  PRO C N   1 
ATOM   5313 C  CA  . PRO C  1  5   ? 3.885   -9.474  15.255 1.00 43.60  ? 18  PRO C CA  1 
ATOM   5314 C  C   . PRO C  1  5   ? 4.050   -9.239  13.756 1.00 41.83  ? 18  PRO C C   1 
ATOM   5315 O  O   . PRO C  1  5   ? 5.154   -8.974  13.319 1.00 37.57  ? 18  PRO C O   1 
ATOM   5316 C  CB  . PRO C  1  5   ? 4.195   -8.198  16.038 1.00 44.37  ? 18  PRO C CB  1 
ATOM   5317 C  CG  . PRO C  1  5   ? 5.605   -8.404  16.584 1.00 45.97  ? 18  PRO C CG  1 
ATOM   5318 C  CD  . PRO C  1  5   ? 5.957   -9.879  16.501 1.00 44.88  ? 18  PRO C CD  1 
ATOM   5319 N  N   . PRO C  1  6   ? 2.975   -9.306  12.940 1.00 39.19  ? 19  PRO C N   1 
ATOM   5320 C  CA  . PRO C  1  6   ? 3.092   -9.182  11.490 1.00 43.11  ? 19  PRO C CA  1 
ATOM   5321 C  C   . PRO C  1  6   ? 3.253   -7.723  11.091 1.00 39.68  ? 19  PRO C C   1 
ATOM   5322 O  O   . PRO C  1  6   ? 2.921   -6.832  11.868 1.00 36.34  ? 19  PRO C O   1 
ATOM   5323 C  CB  . PRO C  1  6   ? 1.760   -9.772  10.987 1.00 45.50  ? 19  PRO C CB  1 
ATOM   5324 C  CG  . PRO C  1  6   ? 0.780   -9.399  12.066 1.00 44.37  ? 19  PRO C CG  1 
ATOM   5325 C  CD  . PRO C  1  6   ? 1.582   -9.511  13.371 1.00 44.96  ? 19  PRO C CD  1 
ATOM   5326 N  N   . PRO C  1  7   ? 3.770   -7.434  9.881  1.00 44.26  ? 20  PRO C N   1 
ATOM   5327 C  CA  . PRO C  1  7   ? 3.828   -6.066  9.383  1.00 40.91  ? 20  PRO C CA  1 
ATOM   5328 C  C   . PRO C  1  7   ? 2.428   -5.477  9.262  1.00 33.14  ? 20  PRO C C   1 
ATOM   5329 O  O   . PRO C  1  7   ? 1.451   -6.194  9.182  1.00 30.97  ? 20  PRO C O   1 
ATOM   5330 C  CB  . PRO C  1  7   ? 4.566   -6.156  8.034  1.00 45.43  ? 20  PRO C CB  1 
ATOM   5331 C  CG  . PRO C  1  7   ? 4.463   -7.615  7.656  1.00 50.23  ? 20  PRO C CG  1 
ATOM   5332 C  CD  . PRO C  1  7   ? 4.379   -8.398  8.952  1.00 51.21  ? 20  PRO C CD  1 
ATOM   5333 N  N   . PRO C  1  8   ? 2.278   -4.140  9.332  1.00 30.10  ? 21  PRO C N   1 
ATOM   5334 C  CA  . PRO C  1  8   ? 0.961   -3.523  9.266  1.00 30.34  ? 21  PRO C CA  1 
ATOM   5335 C  C   . PRO C  1  8   ? 0.324   -3.764  7.899  1.00 32.00  ? 21  PRO C C   1 
ATOM   5336 O  O   . PRO C  1  8   ? 1.020   -3.881  6.883  1.00 29.76  ? 21  PRO C O   1 
ATOM   5337 C  CB  . PRO C  1  8   ? 1.242   -2.065  9.489  1.00 31.08  ? 21  PRO C CB  1 
ATOM   5338 C  CG  . PRO C  1  8   ? 2.672   -1.896  9.080  1.00 34.67  ? 21  PRO C CG  1 
ATOM   5339 C  CD  . PRO C  1  8   ? 3.359   -3.167  9.462  1.00 34.17  ? 21  PRO C CD  1 
ATOM   5340 N  N   . PRO C  1  9   ? -1.012  -3.849  7.835  1.00 33.06  ? 22  PRO C N   1 
ATOM   5341 C  CA  . PRO C  1  9   ? -1.710  -3.852  6.554  1.00 33.99  ? 22  PRO C CA  1 
ATOM   5342 C  C   . PRO C  1  9   ? -1.311  -2.632  5.741  1.00 30.70  ? 22  PRO C C   1 
ATOM   5343 O  O   . PRO C  1  9   ? -0.978  -1.595  6.300  1.00 30.64  ? 22  PRO C O   1 
ATOM   5344 C  CB  . PRO C  1  9   ? -3.193  -3.806  6.962  1.00 35.70  ? 22  PRO C CB  1 
ATOM   5345 C  CG  . PRO C  1  9   ? -3.199  -4.410  8.336  1.00 37.80  ? 22  PRO C CG  1 
ATOM   5346 C  CD  . PRO C  1  9   ? -1.918  -3.952  8.982  1.00 35.26  ? 22  PRO C CD  1 
ATOM   5347 N  N   . GLY C  1  10  ? -1.383  -2.782  4.415  1.00 30.70  ? 23  GLY C N   1 
ATOM   5348 C  CA  . GLY C  1  10  ? -1.378  -1.666  3.496  1.00 29.49  ? 23  GLY C CA  1 
ATOM   5349 C  C   . GLY C  1  10  ? -2.770  -1.061  3.345  1.00 31.08  ? 23  GLY C C   1 
ATOM   5350 O  O   . GLY C  1  10  ? -3.708  -1.431  4.047  1.00 28.63  ? 23  GLY C O   1 
ATOM   5351 N  N   . PRO C  1  11  ? -2.924  -0.087  2.424  1.00 30.42  ? 24  PRO C N   1 
ATOM   5352 C  CA  . PRO C  1  11  ? -4.207  0.571   2.171  1.00 30.78  ? 24  PRO C CA  1 
ATOM   5353 C  C   . PRO C  1  11  ? -5.302  -0.436  1.858  1.00 30.85  ? 24  PRO C C   1 
ATOM   5354 O  O   . PRO C  1  11  ? -5.019  -1.532  1.384  1.00 30.52  ? 24  PRO C O   1 
ATOM   5355 C  CB  . PRO C  1  11  ? -3.914  1.492   0.979  1.00 30.92  ? 24  PRO C CB  1 
ATOM   5356 C  CG  . PRO C  1  11  ? -2.429  1.714   1.044  1.00 31.31  ? 24  PRO C CG  1 
ATOM   5357 C  CD  . PRO C  1  11  ? -1.865  0.392   1.526  1.00 32.59  ? 24  PRO C CD  1 
ATOM   5358 N  N   . PRO C  1  12  ? -6.589  -0.115  2.089  1.00 30.33  ? 25  PRO C N   1 
ATOM   5359 C  CA  . PRO C  1  12  ? -7.652  -1.048  1.714  1.00 32.77  ? 25  PRO C CA  1 
ATOM   5360 C  C   . PRO C  1  12  ? -7.695  -1.184  0.184  1.00 34.16  ? 25  PRO C C   1 
ATOM   5361 O  O   . PRO C  1  12  ? -7.333  -0.235  -0.530 1.00 31.30  ? 25  PRO C O   1 
ATOM   5362 C  CB  . PRO C  1  12  ? -8.913  -0.395  2.299  1.00 32.63  ? 25  PRO C CB  1 
ATOM   5363 C  CG  . PRO C  1  12  ? -8.600  1.086   2.337  1.00 32.70  ? 25  PRO C CG  1 
ATOM   5364 C  CD  . PRO C  1  12  ? -7.085  1.195   2.542  1.00 31.74  ? 25  PRO C CD  1 
ATOM   5365 N  N   . SER C  1  13  ? -8.108  -2.374  -0.284 1.00 34.19  ? 26  SER C N   1 
ATOM   5366 C  CA  A SER C  1  13  ? -8.233  -2.667  -1.706 0.50 36.27  ? 26  SER C CA  1 
ATOM   5367 C  CA  B SER C  1  13  ? -8.250  -2.684  -1.701 0.50 38.77  ? 26  SER C CA  1 
ATOM   5368 C  C   . SER C  1  13  ? -9.142  -1.650  -2.389 1.00 34.27  ? 26  SER C C   1 
ATOM   5369 O  O   . SER C  1  13  ? -8.859  -1.197  -3.491 1.00 31.95  ? 26  SER C O   1 
ATOM   5370 C  CB  A SER C  1  13  ? -8.760  -4.067  -1.919 0.50 35.30  ? 26  SER C CB  1 
ATOM   5371 C  CB  B SER C  1  13  ? -8.805  -4.092  -1.853 0.50 40.89  ? 26  SER C CB  1 
ATOM   5372 O  OG  A SER C  1  13  ? -7.760  -5.005  -1.563 0.50 35.64  ? 26  SER C OG  1 
ATOM   5373 O  OG  B SER C  1  13  ? -9.084  -4.400  -3.209 0.50 49.45  ? 26  SER C OG  1 
ATOM   5374 N  N   . PHE C  1  14  ? -10.236 -1.297  -1.720 1.00 32.69  ? 27  PHE C N   1 
ATOM   5375 C  CA  . PHE C  1  14  ? -11.182 -0.318  -2.226 1.00 31.60  ? 27  PHE C CA  1 
ATOM   5376 C  C   . PHE C  1  14  ? -11.117 0.918   -1.346 1.00 32.19  ? 27  PHE C C   1 
ATOM   5377 O  O   . PHE C  1  14  ? -11.322 0.804   -0.134 1.00 31.61  ? 27  PHE C O   1 
ATOM   5378 C  CB  . PHE C  1  14  ? -12.575 -0.967  -2.247 1.00 33.51  ? 27  PHE C CB  1 
ATOM   5379 C  CG  . PHE C  1  14  ? -13.656 0.004   -2.689 1.00 35.15  ? 27  PHE C CG  1 
ATOM   5380 C  CD1 . PHE C  1  14  ? -13.776 0.409   -4.015 1.00 37.61  ? 27  PHE C CD1 1 
ATOM   5381 C  CD2 . PHE C  1  14  ? -14.554 0.506   -1.764 1.00 39.40  ? 27  PHE C CD2 1 
ATOM   5382 C  CE1 . PHE C  1  14  ? -14.754 1.320   -4.391 1.00 38.38  ? 27  PHE C CE1 1 
ATOM   5383 C  CE2 . PHE C  1  14  ? -15.545 1.401   -2.143 1.00 39.88  ? 27  PHE C CE2 1 
ATOM   5384 C  CZ  . PHE C  1  14  ? -15.641 1.819   -3.451 1.00 39.03  ? 27  PHE C CZ  1 
ATOM   5385 N  N   . THR C  1  15  ? -10.892 2.094   -1.951 1.00 30.43  ? 28  THR C N   1 
ATOM   5386 C  CA  . THR C  1  15  ? -10.745 3.337   -1.210 1.00 31.13  ? 28  THR C CA  1 
ATOM   5387 C  C   . THR C  1  15  ? -11.853 4.341   -1.501 1.00 30.87  ? 28  THR C C   1 
ATOM   5388 O  O   . THR C  1  15  ? -11.715 5.507   -1.152 1.00 29.73  ? 28  THR C O   1 
ATOM   5389 C  CB  . THR C  1  15  ? -9.384  3.961   -1.533 1.00 35.73  ? 28  THR C CB  1 
ATOM   5390 O  OG1 . THR C  1  15  ? -9.410  4.480   -2.861 1.00 34.66  ? 28  THR C OG1 1 
ATOM   5391 C  CG2 . THR C  1  15  ? -8.226  2.999   -1.324 1.00 36.97  ? 28  THR C CG2 1 
ATOM   5392 N  N   . GLY C  1  16  ? -12.951 3.920   -2.120 1.00 32.01  ? 29  GLY C N   1 
ATOM   5393 C  CA  . GLY C  1  16  ? -14.079 4.816   -2.355 1.00 31.98  ? 29  GLY C CA  1 
ATOM   5394 C  C   . GLY C  1  16  ? -15.051 4.840   -1.171 1.00 37.50  ? 29  GLY C C   1 
ATOM   5395 O  O   . GLY C  1  16  ? -14.817 4.191   -0.150 1.00 32.96  ? 29  GLY C O   1 
ATOM   5396 N  N   . THR C  1  17  ? -16.153 5.587   -1.313 1.00 38.87  ? 30  THR C N   1 
ATOM   5397 C  CA  . THR C  1  17  ? -17.160 5.651   -0.261 1.00 41.08  ? 30  THR C CA  1 
ATOM   5398 C  C   . THR C  1  17  ? -17.907 4.326   -0.224 1.00 41.95  ? 30  THR C C   1 
ATOM   5399 O  O   . THR C  1  17  ? -17.920 3.578   -1.203 1.00 40.52  ? 30  THR C O   1 
ATOM   5400 C  CB  . THR C  1  17  ? -18.123 6.828   -0.438 1.00 43.91  ? 30  THR C CB  1 
ATOM   5401 O  OG1 . THR C  1  17  ? -18.850 6.878   0.795  1.00 43.63  ? 30  THR C OG1 1 
ATOM   5402 C  CG2 . THR C  1  17  ? -19.055 6.642   -1.628 1.00 40.59  ? 30  THR C CG2 1 
ATOM   5403 N  N   . LYS C  1  18  ? -18.480 4.040   0.943  1.00 39.19  ? 31  LYS C N   1 
ATOM   5404 C  CA  . LYS C  1  18  ? -19.389 2.922   1.104  1.00 40.83  ? 31  LYS C CA  1 
ATOM   5405 C  C   . LYS C  1  18  ? -20.130 3.083   2.424  1.00 40.89  ? 31  LYS C C   1 
ATOM   5406 O  O   . LYS C  1  18  ? -19.695 3.848   3.280  1.00 39.16  ? 31  LYS C O   1 
ATOM   5407 C  CB  . LYS C  1  18  ? -18.690 1.561   1.103  1.00 42.80  ? 31  LYS C CB  1 
ATOM   5408 C  CG  . LYS C  1  18  ? -17.672 1.314   2.210  1.00 43.92  ? 31  LYS C CG  1 
ATOM   5409 C  CD  . LYS C  1  18  ? -17.075 -0.081  2.047  1.00 51.02  ? 31  LYS C CD  1 
ATOM   5410 C  CE  . LYS C  1  18  ? -17.499 -1.089  3.063  1.00 56.35  ? 31  LYS C CE  1 
ATOM   5411 N  NZ  . LYS C  1  18  ? -16.747 -2.322  2.836  1.00 63.08  ? 31  LYS C NZ  1 
ATOM   5412 N  N   . LEU C  1  19  ? -21.235 2.344   2.561  1.00 43.06  ? 32  LEU C N   1 
ATOM   5413 C  CA  . LEU C  1  19  ? -21.999 2.288   3.791  1.00 43.03  ? 32  LEU C CA  1 
ATOM   5414 C  C   . LEU C  1  19  ? -21.171 1.524   4.814  1.00 40.09  ? 32  LEU C C   1 
ATOM   5415 O  O   . LEU C  1  19  ? -20.819 0.370   4.580  1.00 40.97  ? 32  LEU C O   1 
ATOM   5416 C  CB  . LEU C  1  19  ? -23.343 1.589   3.582  1.00 41.73  ? 32  LEU C CB  1 
ATOM   5417 C  CG  . LEU C  1  19  ? -24.144 1.320   4.861  1.00 41.93  ? 32  LEU C CG  1 
ATOM   5418 C  CD1 . LEU C  1  19  ? -24.642 2.632   5.417  1.00 41.57  ? 32  LEU C CD1 1 
ATOM   5419 C  CD2 . LEU C  1  19  ? -25.287 0.349   4.628  1.00 46.85  ? 32  LEU C CD2 1 
ATOM   5420 N  N   . VAL C  1  20  ? -20.900 2.149   5.962  1.00 38.52  ? 33  VAL C N   1 
ATOM   5421 C  CA  . VAL C  1  20  ? -20.116 1.458   6.974  1.00 39.88  ? 33  VAL C CA  1 
ATOM   5422 C  C   . VAL C  1  20  ? -20.991 1.099   8.170  1.00 39.00  ? 33  VAL C C   1 
ATOM   5423 O  O   . VAL C  1  20  ? -20.661 0.172   8.911  1.00 36.56  ? 33  VAL C O   1 
ATOM   5424 C  CB  . VAL C  1  20  ? -18.864 2.246   7.401  1.00 41.77  ? 33  VAL C CB  1 
ATOM   5425 C  CG1 . VAL C  1  20  ? -17.904 2.441   6.232  1.00 38.99  ? 33  VAL C CG1 1 
ATOM   5426 C  CG2 . VAL C  1  20  ? -19.200 3.575   8.039  1.00 40.70  ? 33  VAL C CG2 1 
ATOM   5427 N  N   . ASN C  1  21  ? -22.081 1.847   8.363  1.00 41.35  ? 34  ASN C N   1 
ATOM   5428 C  CA  . ASN C  1  21  ? -23.057 1.504   9.383  1.00 40.45  ? 34  ASN C CA  1 
ATOM   5429 C  C   . ASN C  1  21  ? -24.029 0.486   8.805  1.00 44.06  ? 34  ASN C C   1 
ATOM   5430 O  O   . ASN C  1  21  ? -25.147 0.842   8.480  1.00 47.45  ? 34  ASN C O   1 
ATOM   5431 C  CB  . ASN C  1  21  ? -23.771 2.761   9.866  1.00 38.12  ? 34  ASN C CB  1 
ATOM   5432 C  CG  . ASN C  1  21  ? -24.645 2.493   11.066 1.00 38.60  ? 34  ASN C CG  1 
ATOM   5433 O  OD1 . ASN C  1  21  ? -24.762 1.361   11.557 1.00 40.79  ? 34  ASN C OD1 1 
ATOM   5434 N  ND2 . ASN C  1  21  ? -25.248 3.553   11.565 1.00 39.11  ? 34  ASN C ND2 1 
ATOM   5435 N  N   . ASP C  1  22  ? -23.594 -0.766  8.680  1.00 46.35  ? 35  ASP C N   1 
ATOM   5436 C  CA  . ASP C  1  22  ? -24.285 -1.755  7.862  1.00 50.16  ? 35  ASP C CA  1 
ATOM   5437 C  C   . ASP C  1  22  ? -24.701 -2.932  8.743  1.00 52.06  ? 35  ASP C C   1 
ATOM   5438 O  O   . ASP C  1  22  ? -24.411 -2.952  9.937  1.00 47.60  ? 35  ASP C O   1 
ATOM   5439 C  CB  . ASP C  1  22  ? -23.428 -2.166  6.668  1.00 50.63  ? 35  ASP C CB  1 
ATOM   5440 C  CG  . ASP C  1  22  ? -22.102 -2.850  6.997  1.00 56.81  ? 35  ASP C CG  1 
ATOM   5441 O  OD1 . ASP C  1  22  ? -21.801 -3.006  8.195  1.00 56.89  ? 35  ASP C OD1 1 
ATOM   5442 O  OD2 . ASP C  1  22  ? -21.368 -3.233  6.064  1.00 53.93  ? 35  ASP C OD2 1 
ATOM   5443 N  N   . ALA C  1  23  ? -25.324 -3.937  8.126  1.00 50.86  ? 36  ALA C N   1 
ATOM   5444 C  CA  . ALA C  1  23  ? -25.950 -5.031  8.851  1.00 56.03  ? 36  ALA C CA  1 
ATOM   5445 C  C   . ALA C  1  23  ? -24.905 -5.838  9.608  1.00 52.68  ? 36  ALA C C   1 
ATOM   5446 O  O   . ALA C  1  23  ? -25.184 -6.358  10.683 1.00 48.46  ? 36  ALA C O   1 
ATOM   5447 C  CB  . ALA C  1  23  ? -26.733 -5.918  7.899  1.00 56.33  ? 36  ALA C CB  1 
ATOM   5448 N  N   . ASP C  1  24  ? -23.704 -5.933  9.042  1.00 54.34  ? 37  ASP C N   1 
ATOM   5449 C  CA  . ASP C  1  24  ? -22.647 -6.729  9.642  1.00 52.78  ? 37  ASP C CA  1 
ATOM   5450 C  C   . ASP C  1  24  ? -21.974 -6.002  10.811 1.00 42.40  ? 37  ASP C C   1 
ATOM   5451 O  O   . ASP C  1  24  ? -21.238 -6.638  11.546 1.00 44.00  ? 37  ASP C O   1 
ATOM   5452 C  CB  . ASP C  1  24  ? -21.592 -7.109  8.618  1.00 62.37  ? 37  ASP C CB  1 
ATOM   5453 C  CG  . ASP C  1  24  ? -22.063 -7.983  7.469  1.00 71.97  ? 37  ASP C CG  1 
ATOM   5454 O  OD1 . ASP C  1  24  ? -22.470 -9.119  7.761  1.00 75.14  ? 37  ASP C OD1 1 
ATOM   5455 O  OD2 . ASP C  1  24  ? -22.009 -7.516  6.306  1.00 86.39  ? 37  ASP C OD2 1 
ATOM   5456 N  N   . HIS C  1  25  ? -22.200 -4.686  10.956 1.00 38.40  ? 38  HIS C N   1 
ATOM   5457 C  CA  . HIS C  1  25  ? -21.503 -3.863  11.934 1.00 40.62  ? 38  HIS C CA  1 
ATOM   5458 C  C   . HIS C  1  25  ? -22.518 -3.047  12.727 1.00 39.29  ? 38  HIS C C   1 
ATOM   5459 O  O   . HIS C  1  25  ? -22.529 -1.810  12.681 1.00 39.44  ? 38  HIS C O   1 
ATOM   5460 C  CB  . HIS C  1  25  ? -20.458 -2.984  11.242 1.00 42.11  ? 38  HIS C CB  1 
ATOM   5461 C  CG  . HIS C  1  25  ? -19.380 -3.775  10.579 1.00 42.96  ? 38  HIS C CG  1 
ATOM   5462 N  ND1 . HIS C  1  25  ? -19.399 -4.056  9.227  1.00 44.63  ? 38  HIS C ND1 1 
ATOM   5463 C  CD2 . HIS C  1  25  ? -18.268 -4.373  11.077 1.00 45.93  ? 38  HIS C CD2 1 
ATOM   5464 C  CE1 . HIS C  1  25  ? -18.329 -4.792  8.929  1.00 47.40  ? 38  HIS C CE1 1 
ATOM   5465 N  NE2 . HIS C  1  25  ? -17.630 -5.001  10.041 1.00 45.15  ? 38  HIS C NE2 1 
ATOM   5466 N  N   . PRO C  1  26  ? -23.436 -3.721  13.464 1.00 37.56  ? 39  PRO C N   1 
ATOM   5467 C  CA  . PRO C  1  26  ? -24.441 -3.006  14.248 1.00 38.95  ? 39  PRO C CA  1 
ATOM   5468 C  C   . PRO C  1  26  ? -23.814 -2.403  15.499 1.00 40.46  ? 39  PRO C C   1 
ATOM   5469 O  O   . PRO C  1  26  ? -22.957 -3.026  16.116 1.00 42.60  ? 39  PRO C O   1 
ATOM   5470 C  CB  . PRO C  1  26  ? -25.442 -4.116  14.603 1.00 38.32  ? 39  PRO C CB  1 
ATOM   5471 C  CG  . PRO C  1  26  ? -24.574 -5.356  14.708 1.00 40.75  ? 39  PRO C CG  1 
ATOM   5472 C  CD  . PRO C  1  26  ? -23.535 -5.183  13.592 1.00 39.09  ? 39  PRO C CD  1 
ATOM   5473 N  N   . TRP C  1  27  ? -24.253 -1.199  15.860 1.00 37.97  ? 40  TRP C N   1 
ATOM   5474 C  CA  . TRP C  1  27  ? -23.977 -0.685  17.182 1.00 41.20  ? 40  TRP C CA  1 
ATOM   5475 C  C   . TRP C  1  27  ? -24.560 -1.623  18.232 1.00 44.70  ? 40  TRP C C   1 
ATOM   5476 O  O   . TRP C  1  27  ? -25.683 -2.089  18.087 1.00 39.55  ? 40  TRP C O   1 
ATOM   5477 C  CB  . TRP C  1  27  ? -24.546 0.718   17.349 1.00 39.84  ? 40  TRP C CB  1 
ATOM   5478 C  CG  . TRP C  1  27  ? -24.165 1.346   18.658 1.00 47.84  ? 40  TRP C CG  1 
ATOM   5479 C  CD1 . TRP C  1  27  ? -23.088 2.129   18.914 1.00 45.57  ? 40  TRP C CD1 1 
ATOM   5480 C  CD2 . TRP C  1  27  ? -24.907 1.279   19.891 1.00 52.05  ? 40  TRP C CD2 1 
ATOM   5481 N  NE1 . TRP C  1  27  ? -23.099 2.561   20.207 1.00 46.92  ? 40  TRP C NE1 1 
ATOM   5482 C  CE2 . TRP C  1  27  ? -24.195 2.052   20.837 1.00 50.93  ? 40  TRP C CE2 1 
ATOM   5483 C  CE3 . TRP C  1  27  ? -26.086 0.649   20.287 1.00 48.40  ? 40  TRP C CE3 1 
ATOM   5484 C  CZ2 . TRP C  1  27  ? -24.624 2.220   22.149 1.00 49.32  ? 40  TRP C CZ2 1 
ATOM   5485 C  CZ3 . TRP C  1  27  ? -26.501 0.795   21.594 1.00 49.76  ? 40  TRP C CZ3 1 
ATOM   5486 C  CH2 . TRP C  1  27  ? -25.781 1.564   22.508 1.00 48.02  ? 40  TRP C CH2 1 
ATOM   5487 N  N   . GLN C  1  28  ? -23.781 -1.896  19.283 1.00 42.60  ? 41  GLN C N   1 
ATOM   5488 C  CA  . GLN C  1  28  ? -24.272 -2.632  20.431 1.00 42.07  ? 41  GLN C CA  1 
ATOM   5489 C  C   . GLN C  1  28  ? -23.779 -1.967  21.708 1.00 46.21  ? 41  GLN C C   1 
ATOM   5490 O  O   . GLN C  1  28  ? -22.706 -1.357  21.736 1.00 40.65  ? 41  GLN C O   1 
ATOM   5491 C  CB  . GLN C  1  28  ? -23.823 -4.084  20.395 1.00 43.02  ? 41  GLN C CB  1 
ATOM   5492 C  CG  . GLN C  1  28  ? -24.346 -4.852  19.193 1.00 42.76  ? 41  GLN C CG  1 
ATOM   5493 C  CD  . GLN C  1  28  ? -23.821 -6.267  19.124 1.00 46.15  ? 41  GLN C CD  1 
ATOM   5494 O  OE1 . GLN C  1  28  ? -22.984 -6.702  19.928 1.00 50.97  ? 41  GLN C OE1 1 
ATOM   5495 N  NE2 . GLN C  1  28  ? -24.299 -6.996  18.129 1.00 44.89  ? 41  GLN C NE2 1 
ATOM   5496 N  N   . PRO C  1  29  ? -24.590 -2.023  22.785 1.00 47.53  ? 42  PRO C N   1 
ATOM   5497 C  CA  . PRO C  1  29  ? -24.233 -1.342  24.025 1.00 46.92  ? 42  PRO C CA  1 
ATOM   5498 C  C   . PRO C  1  29  ? -23.049 -2.021  24.693 1.00 37.91  ? 42  PRO C C   1 
ATOM   5499 O  O   . PRO C  1  29  ? -22.789 -3.210  24.454 1.00 39.71  ? 42  PRO C O   1 
ATOM   5500 C  CB  . PRO C  1  29  ? -25.513 -1.352  24.882 1.00 49.66  ? 42  PRO C CB  1 
ATOM   5501 C  CG  . PRO C  1  29  ? -26.369 -2.446  24.273 1.00 53.56  ? 42  PRO C CG  1 
ATOM   5502 C  CD  . PRO C  1  29  ? -25.911 -2.673  22.827 1.00 52.02  ? 42  PRO C CD  1 
ATOM   5503 N  N   . LEU C  1  30  ? -22.361 -1.246  25.529 1.00 36.48  ? 43  LEU C N   1 
ATOM   5504 C  CA  . LEU C  1  30  ? -21.217 -1.735  26.282 1.00 39.16  ? 43  LEU C CA  1 
ATOM   5505 C  C   . LEU C  1  30  ? -21.671 -2.800  27.266 1.00 42.29  ? 43  LEU C C   1 
ATOM   5506 O  O   . LEU C  1  30  ? -22.745 -2.673  27.866 1.00 43.86  ? 43  LEU C O   1 
ATOM   5507 C  CB  . LEU C  1  30  ? -20.565 -0.575  27.025 1.00 38.81  ? 43  LEU C CB  1 
ATOM   5508 C  CG  . LEU C  1  30  ? -20.049 0.574   26.159 1.00 47.17  ? 43  LEU C CG  1 
ATOM   5509 C  CD1 . LEU C  1  30  ? -19.580 1.741   26.998 1.00 47.81  ? 43  LEU C CD1 1 
ATOM   5510 C  CD2 . LEU C  1  30  ? -18.940 -0.003  25.284 1.00 46.33  ? 43  LEU C CD2 1 
ATOM   5511 N  N   . ARG C  1  31  ? -20.856 -3.852  27.373 1.00 40.09  ? 44  ARG C N   1 
ATOM   5512 C  CA  . ARG C  1  31  ? -21.019 -4.881  28.377 1.00 41.09  ? 44  ARG C CA  1 
ATOM   5513 C  C   . ARG C  1  31  ? -19.985 -4.619  29.470 1.00 42.79  ? 44  ARG C C   1 
ATOM   5514 O  O   . ARG C  1  31  ? -18.975 -3.938  29.248 1.00 41.26  ? 44  ARG C O   1 
ATOM   5515 C  CB  . ARG C  1  31  ? -20.816 -6.280  27.793 1.00 42.98  ? 44  ARG C CB  1 
ATOM   5516 C  CG  . ARG C  1  31  ? -21.673 -6.665  26.595 1.00 50.55  ? 44  ARG C CG  1 
ATOM   5517 C  CD  . ARG C  1  31  ? -21.060 -7.837  25.827 1.00 55.63  ? 44  ARG C CD  1 
ATOM   5518 N  NE  . ARG C  1  31  ? -19.716 -7.478  25.346 1.00 73.13  ? 44  ARG C NE  1 
ATOM   5519 C  CZ  . ARG C  1  31  ? -18.885 -8.208  24.587 1.00 74.81  ? 44  ARG C CZ  1 
ATOM   5520 N  NH1 . ARG C  1  31  ? -19.288 -9.347  24.046 1.00 82.75  ? 44  ARG C NH1 1 
ATOM   5521 N  NH2 . ARG C  1  31  ? -17.652 -7.790  24.342 1.00 72.64  ? 44  ARG C NH2 1 
ATOM   5522 N  N   . GLU C  1  32  ? -20.238 -5.176  30.659 1.00 40.69  ? 45  GLU C N   1 
ATOM   5523 C  CA  . GLU C  1  32  ? -19.249 -5.199  31.729 1.00 45.16  ? 45  GLU C CA  1 
ATOM   5524 C  C   . GLU C  1  32  ? -17.933 -5.740  31.160 1.00 42.25  ? 45  GLU C C   1 
ATOM   5525 O  O   . GLU C  1  32  ? -17.918 -6.782  30.498 1.00 40.78  ? 45  GLU C O   1 
ATOM   5526 C  CB  . GLU C  1  32  ? -19.742 -6.096  32.874 1.00 45.31  ? 45  GLU C CB  1 
ATOM   5527 C  CG  . GLU C  1  32  ? -18.813 -6.145  34.089 1.00 48.47  ? 45  GLU C CG  1 
ATOM   5528 C  CD  . GLU C  1  32  ? -18.563 -4.805  34.763 1.00 52.22  ? 45  GLU C CD  1 
ATOM   5529 O  OE1 . GLU C  1  32  ? -19.528 -4.020  34.868 1.00 52.77  ? 45  GLU C OE1 1 
ATOM   5530 O  OE2 . GLU C  1  32  ? -17.425 -4.547  35.217 1.00 59.76  ? 45  GLU C OE2 1 
ATOM   5531 N  N   . GLY C  1  33  ? -16.833 -5.028  31.416 1.00 46.40  ? 46  GLY C N   1 
ATOM   5532 C  CA  . GLY C  1  33  ? -15.524 -5.489  30.975 1.00 48.51  ? 46  GLY C CA  1 
ATOM   5533 C  C   . GLY C  1  33  ? -15.078 -4.887  29.639 1.00 48.57  ? 46  GLY C C   1 
ATOM   5534 O  O   . GLY C  1  33  ? -13.880 -4.854  29.366 1.00 46.38  ? 46  GLY C O   1 
ATOM   5535 N  N   . ASP C  1  34  ? -16.017 -4.364  28.842 1.00 44.83  ? 47  ASP C N   1 
ATOM   5536 C  CA  . ASP C  1  34  ? -15.668 -3.691  27.592 1.00 48.03  ? 47  ASP C CA  1 
ATOM   5537 C  C   . ASP C  1  34  ? -14.931 -2.388  27.898 1.00 45.75  ? 47  ASP C C   1 
ATOM   5538 O  O   . ASP C  1  34  ? -15.334 -1.638  28.779 1.00 38.37  ? 47  ASP C O   1 
ATOM   5539 C  CB  . ASP C  1  34  ? -16.894 -3.393  26.745 1.00 44.51  ? 47  ASP C CB  1 
ATOM   5540 C  CG  . ASP C  1  34  ? -17.564 -4.591  26.090 1.00 46.23  ? 47  ASP C CG  1 
ATOM   5541 O  OD1 . ASP C  1  34  ? -16.917 -5.680  26.034 1.00 45.64  ? 47  ASP C OD1 1 
ATOM   5542 O  OD2 . ASP C  1  34  ? -18.717 -4.413  25.618 1.00 47.09  ? 47  ASP C OD2 1 
ATOM   5543 N  N   . ILE C  1  35  ? -13.848 -2.119  27.150 1.00 44.87  ? 48  ILE C N   1 
ATOM   5544 C  CA  . ILE C  1  35  ? -13.023 -0.941  27.377 1.00 36.92  ? 48  ILE C CA  1 
ATOM   5545 C  C   . ILE C  1  35  ? -13.237 0.088   26.277 1.00 36.56  ? 48  ILE C C   1 
ATOM   5546 O  O   . ILE C  1  35  ? -13.257 -0.234  25.088 1.00 38.98  ? 48  ILE C O   1 
ATOM   5547 C  CB  . ILE C  1  35  ? -11.552 -1.373  27.508 1.00 42.36  ? 48  ILE C CB  1 
ATOM   5548 C  CG1 . ILE C  1  35  ? -11.357 -2.155  28.833 1.00 49.96  ? 48  ILE C CG1 1 
ATOM   5549 C  CG2 . ILE C  1  35  ? -10.604 -0.172  27.434 1.00 38.93  ? 48  ILE C CG2 1 
ATOM   5550 C  CD1 . ILE C  1  35  ? -10.408 -3.324  28.727 1.00 58.73  ? 48  ILE C CD1 1 
ATOM   5551 N  N   . ARG C  1  36  ? -13.366 1.345   26.691 1.00 34.16  ? 49  ARG C N   1 
ATOM   5552 C  CA  . ARG C  1  36  ? -13.441 2.474   25.783 1.00 36.02  ? 49  ARG C CA  1 
ATOM   5553 C  C   . ARG C  1  36  ? -12.532 3.544   26.369 1.00 38.63  ? 49  ARG C C   1 
ATOM   5554 O  O   . ARG C  1  36  ? -12.201 3.474   27.541 1.00 34.77  ? 49  ARG C O   1 
ATOM   5555 C  CB  . ARG C  1  36  ? -14.876 3.011   25.640 1.00 39.87  ? 49  ARG C CB  1 
ATOM   5556 C  CG  . ARG C  1  36  ? -15.831 2.004   25.022 1.00 39.02  ? 49  ARG C CG  1 
ATOM   5557 C  CD  . ARG C  1  36  ? -15.532 1.738   23.567 1.00 38.78  ? 49  ARG C CD  1 
ATOM   5558 N  NE  . ARG C  1  36  ? -16.455 0.803   22.917 1.00 36.81  ? 49  ARG C NE  1 
ATOM   5559 C  CZ  . ARG C  1  36  ? -16.414 -0.512  23.002 1.00 36.80  ? 49  ARG C CZ  1 
ATOM   5560 N  NH1 . ARG C  1  36  ? -15.436 -1.137  23.636 1.00 38.99  ? 49  ARG C NH1 1 
ATOM   5561 N  NH2 . ARG C  1  36  ? -17.363 -1.228  22.440 1.00 42.23  ? 49  ARG C NH2 1 
ATOM   5562 N  N   . GLY C  1  37  ? -12.133 4.525   25.554 1.00 39.70  ? 50  GLY C N   1 
ATOM   5563 C  CA  . GLY C  1  37  ? -11.132 5.474   25.988 1.00 37.89  ? 50  GLY C CA  1 
ATOM   5564 C  C   . GLY C  1  37  ? -11.311 6.844   25.367 1.00 35.70  ? 50  GLY C C   1 
ATOM   5565 O  O   . GLY C  1  37  ? -12.428 7.274   25.095 1.00 34.24  ? 50  GLY C O   1 
ATOM   5566 N  N   . PRO C  1  38  ? -10.194 7.568   25.146 1.00 32.73  ? 51  PRO C N   1 
ATOM   5567 C  CA  . PRO C  1  38  ? -10.240 8.968   24.753 1.00 32.05  ? 51  PRO C CA  1 
ATOM   5568 C  C   . PRO C  1  38  ? -10.431 9.228   23.268 1.00 34.80  ? 51  PRO C C   1 
ATOM   5569 O  O   . PRO C  1  38  ? -10.599 10.381  22.865 1.00 32.76  ? 51  PRO C O   1 
ATOM   5570 C  CB  . PRO C  1  38  ? -8.878  9.433   25.227 1.00 32.26  ? 51  PRO C CB  1 
ATOM   5571 C  CG  . PRO C  1  38  ? -7.995  8.278   24.922 1.00 32.31  ? 51  PRO C CG  1 
ATOM   5572 C  CD  . PRO C  1  38  ? -8.821  7.071   25.296 1.00 34.85  ? 51  PRO C CD  1 
ATOM   5573 N  N   . CYS C  1  39  ? -10.403 8.158   22.467 1.00 37.29  ? 52  CYS C N   1 
ATOM   5574 C  CA  . CYS C  1  39  ? -10.519 8.319   21.020 1.00 35.96  ? 52  CYS C CA  1 
ATOM   5575 C  C   . CYS C  1  39  ? -11.928 7.964   20.553 1.00 30.97  ? 52  CYS C C   1 
ATOM   5576 O  O   . CYS C  1  39  ? -12.322 6.797   20.594 1.00 32.99  ? 52  CYS C O   1 
ATOM   5577 C  CB  . CYS C  1  39  ? -9.583  7.397   20.250 1.00 32.91  ? 52  CYS C CB  1 
ATOM   5578 S  SG  . CYS C  1  39  ? -9.731  7.663   18.464 1.00 36.77  ? 52  CYS C SG  1 
ATOM   5579 N  N   . PRO C  1  40  ? -12.708 8.932   20.045 1.00 32.22  ? 53  PRO C N   1 
ATOM   5580 C  CA  . PRO C  1  40  ? -14.050 8.653   19.530 1.00 36.76  ? 53  PRO C CA  1 
ATOM   5581 C  C   . PRO C  1  40  ? -14.049 7.778   18.278 1.00 36.09  ? 53  PRO C C   1 
ATOM   5582 O  O   . PRO C  1  40  ? -14.994 7.024   18.050 1.00 34.31  ? 53  PRO C O   1 
ATOM   5583 C  CB  . PRO C  1  40  ? -14.604 10.045  19.260 1.00 34.42  ? 53  PRO C CB  1 
ATOM   5584 C  CG  . PRO C  1  40  ? -13.412 10.900  18.977 1.00 32.24  ? 53  PRO C CG  1 
ATOM   5585 C  CD  . PRO C  1  40  ? -12.324 10.337  19.871 1.00 32.47  ? 53  PRO C CD  1 
ATOM   5586 N  N   . GLY C  1  41  ? -12.960 7.840   17.489 1.00 36.84  ? 54  GLY C N   1 
ATOM   5587 C  CA  . GLY C  1  41  ? -12.855 6.984   16.318 1.00 30.08  ? 54  GLY C CA  1 
ATOM   5588 C  C   . GLY C  1  41  ? -12.777 5.519   16.704 1.00 31.39  ? 54  GLY C C   1 
ATOM   5589 O  O   . GLY C  1  41  ? -13.590 4.712   16.266 1.00 31.95  ? 54  GLY C O   1 
ATOM   5590 N  N   . LEU C  1  42  ? -11.792 5.169   17.540 1.00 30.43  ? 55  LEU C N   1 
ATOM   5591 C  CA  . LEU C  1  42  ? -11.633 3.791   17.970 1.00 28.97  ? 55  LEU C CA  1 
ATOM   5592 C  C   . LEU C  1  42  ? -12.850 3.331   18.778 1.00 27.09  ? 55  LEU C C   1 
ATOM   5593 O  O   . LEU C  1  42  ? -13.250 2.178   18.673 1.00 30.75  ? 55  LEU C O   1 
ATOM   5594 C  CB  . LEU C  1  42  ? -10.337 3.633   18.754 1.00 31.78  ? 55  LEU C CB  1 
ATOM   5595 C  CG  . LEU C  1  42  ? -9.057  4.000   17.995 1.00 36.11  ? 55  LEU C CG  1 
ATOM   5596 C  CD1 . LEU C  1  42  ? -7.861  3.817   18.935 1.00 39.80  ? 55  LEU C CD1 1 
ATOM   5597 C  CD2 . LEU C  1  42  ? -8.896  3.131   16.747 1.00 37.05  ? 55  LEU C CD2 1 
ATOM   5598 N  N   . ASN C  1  43  ? -13.391 4.208   19.620 1.00 30.48  ? 56  ASN C N   1 
ATOM   5599 C  CA  . ASN C  1  43  ? -14.565 3.864   20.414 1.00 33.17  ? 56  ASN C CA  1 
ATOM   5600 C  C   . ASN C  1  43  ? -15.721 3.440   19.493 1.00 34.22  ? 56  ASN C C   1 
ATOM   5601 O  O   . ASN C  1  43  ? -16.356 2.408   19.728 1.00 36.97  ? 56  ASN C O   1 
ATOM   5602 C  CB  . ASN C  1  43  ? -15.009 5.017   21.308 1.00 33.55  ? 56  ASN C CB  1 
ATOM   5603 C  CG  . ASN C  1  43  ? -14.068 5.303   22.460 1.00 37.80  ? 56  ASN C CG  1 
ATOM   5604 O  OD1 . ASN C  1  43  ? -13.233 4.465   22.850 1.00 31.32  ? 56  ASN C OD1 1 
ATOM   5605 N  ND2 . ASN C  1  43  ? -14.227 6.482   23.043 1.00 38.30  ? 56  ASN C ND2 1 
ATOM   5606 N  N   . THR C  1  44  ? -15.989 4.236   18.447 1.00 37.12  ? 57  THR C N   1 
ATOM   5607 C  CA  . THR C  1  44  ? -17.068 3.929   17.500 1.00 33.78  ? 57  THR C CA  1 
ATOM   5608 C  C   . THR C  1  44  ? -16.796 2.624   16.761 1.00 38.37  ? 57  THR C C   1 
ATOM   5609 O  O   . THR C  1  44  ? -17.698 1.800   16.596 1.00 33.70  ? 57  THR C O   1 
ATOM   5610 C  CB  . THR C  1  44  ? -17.279 5.103   16.553 1.00 38.87  ? 57  THR C CB  1 
ATOM   5611 O  OG1 . THR C  1  44  ? -17.570 6.218   17.389 1.00 33.06  ? 57  THR C OG1 1 
ATOM   5612 C  CG2 . THR C  1  44  ? -18.410 4.869   15.559 1.00 41.15  ? 57  THR C CG2 1 
ATOM   5613 N  N   . LEU C  1  45  ? -15.545 2.401   16.343 1.00 35.62  ? 58  LEU C N   1 
ATOM   5614 C  CA  . LEU C  1  45  ? -15.202 1.171   15.647 1.00 31.40  ? 58  LEU C CA  1 
ATOM   5615 C  C   . LEU C  1  45  ? -15.433 -0.037  16.544 1.00 31.94  ? 58  LEU C C   1 
ATOM   5616 O  O   . LEU C  1  45  ? -15.918 -1.078  16.098 1.00 35.17  ? 58  LEU C O   1 
ATOM   5617 C  CB  . LEU C  1  45  ? -13.755 1.256   15.158 1.00 31.92  ? 58  LEU C CB  1 
ATOM   5618 C  CG  . LEU C  1  45  ? -13.511 2.330   14.093 1.00 34.22  ? 58  LEU C CG  1 
ATOM   5619 C  CD1 . LEU C  1  45  ? -12.039 2.610   13.869 1.00 33.41  ? 58  LEU C CD1 1 
ATOM   5620 C  CD2 . LEU C  1  45  ? -14.198 1.946   12.783 1.00 32.25  ? 58  LEU C CD2 1 
ATOM   5621 N  N   . ALA C  1  46  ? -15.070 0.074   17.829 1.00 32.46  ? 59  ALA C N   1 
ATOM   5622 C  CA  . ALA C  1  46  ? -15.273 -1.040  18.744 1.00 33.67  ? 59  ALA C CA  1 
ATOM   5623 C  C   . ALA C  1  46  ? -16.772 -1.305  18.934 1.00 32.05  ? 59  ALA C C   1 
ATOM   5624 O  O   . ALA C  1  46  ? -17.220 -2.448  18.950 1.00 35.22  ? 59  ALA C O   1 
ATOM   5625 C  CB  . ALA C  1  46  ? -14.588 -0.774  20.069 1.00 34.38  ? 59  ALA C CB  1 
ATOM   5626 N  N   . SER C  1  47  ? -17.547 -0.239  19.081 1.00 32.91  ? 60  SER C N   1 
ATOM   5627 C  CA  . SER C  1  47  ? -18.962 -0.374  19.404 1.00 39.88  ? 60  SER C CA  1 
ATOM   5628 C  C   . SER C  1  47  ? -19.797 -0.826  18.193 1.00 44.55  ? 60  SER C C   1 
ATOM   5629 O  O   . SER C  1  47  ? -20.949 -1.237  18.370 1.00 41.00  ? 60  SER C O   1 
ATOM   5630 C  CB  . SER C  1  47  ? -19.478 0.895   20.030 1.00 36.71  ? 60  SER C CB  1 
ATOM   5631 O  OG  . SER C  1  47  ? -19.050 0.985   21.384 1.00 38.91  ? 60  SER C OG  1 
ATOM   5632 N  N   . HIS C  1  48  ? -19.201 -0.803  16.984 1.00 38.41  ? 61  HIS C N   1 
ATOM   5633 C  CA  . HIS C  1  48  ? -19.829 -1.358  15.787 1.00 38.17  ? 61  HIS C CA  1 
ATOM   5634 C  C   . HIS C  1  48  ? -19.196 -2.677  15.353 1.00 38.70  ? 61  HIS C C   1 
ATOM   5635 O  O   . HIS C  1  48  ? -19.571 -3.213  14.315 1.00 40.25  ? 61  HIS C O   1 
ATOM   5636 C  CB  . HIS C  1  48  ? -19.814 -0.360  14.633 1.00 36.42  ? 61  HIS C CB  1 
ATOM   5637 C  CG  . HIS C  1  48  ? -20.831 0.716   14.753 1.00 36.74  ? 61  HIS C CG  1 
ATOM   5638 N  ND1 . HIS C  1  48  ? -22.043 0.627   14.093 1.00 37.08  ? 61  HIS C ND1 1 
ATOM   5639 C  CD2 . HIS C  1  48  ? -20.839 1.891   15.399 1.00 36.09  ? 61  HIS C CD2 1 
ATOM   5640 C  CE1 . HIS C  1  48  ? -22.747 1.728   14.360 1.00 34.77  ? 61  HIS C CE1 1 
ATOM   5641 N  NE2 . HIS C  1  48  ? -22.048 2.507   15.161 1.00 34.92  ? 61  HIS C NE2 1 
ATOM   5642 N  N   . GLY C  1  49  ? -18.215 -3.180  16.112 1.00 32.29  ? 62  GLY C N   1 
ATOM   5643 C  CA  . GLY C  1  49  ? -17.611 -4.468  15.818 1.00 34.38  ? 62  GLY C CA  1 
ATOM   5644 C  C   . GLY C  1  49  ? -16.596 -4.419  14.671 1.00 29.99  ? 62  GLY C C   1 
ATOM   5645 O  O   . GLY C  1  49  ? -16.198 -5.468  14.190 1.00 34.89  ? 62  GLY C O   1 
ATOM   5646 N  N   . TYR C  1  50  ? -16.152 -3.230  14.253 1.00 34.89  ? 63  TYR C N   1 
ATOM   5647 C  CA  . TYR C  1  50  ? -14.993 -3.118  13.369 1.00 36.11  ? 63  TYR C CA  1 
ATOM   5648 C  C   . TYR C  1  50  ? -13.728 -3.525  14.132 1.00 38.93  ? 63  TYR C C   1 
ATOM   5649 O  O   . TYR C  1  50  ? -12.816 -4.102  13.546 1.00 41.50  ? 63  TYR C O   1 
ATOM   5650 C  CB  . TYR C  1  50  ? -14.871 -1.714  12.765 1.00 35.75  ? 63  TYR C CB  1 
ATOM   5651 C  CG  . TYR C  1  50  ? -15.804 -1.467  11.590 1.00 40.57  ? 63  TYR C CG  1 
ATOM   5652 C  CD1 . TYR C  1  50  ? -15.470 -1.889  10.309 1.00 43.18  ? 63  TYR C CD1 1 
ATOM   5653 C  CD2 . TYR C  1  50  ? -17.034 -0.847  11.757 1.00 40.83  ? 63  TYR C CD2 1 
ATOM   5654 C  CE1 . TYR C  1  50  ? -16.321 -1.697  9.230  1.00 43.29  ? 63  TYR C CE1 1 
ATOM   5655 C  CE2 . TYR C  1  50  ? -17.897 -0.645  10.689 1.00 41.08  ? 63  TYR C CE2 1 
ATOM   5656 C  CZ  . TYR C  1  50  ? -17.546 -1.081  9.424  1.00 42.67  ? 63  TYR C CZ  1 
ATOM   5657 O  OH  . TYR C  1  50  ? -18.411 -0.891  8.388  1.00 43.91  ? 63  TYR C OH  1 
ATOM   5658 N  N   . LEU C  1  51  ? -13.654 -3.164  15.419 1.00 39.19  ? 64  LEU C N   1 
ATOM   5659 C  CA  . LEU C  1  51  ? -12.678 -3.700  16.365 1.00 41.37  ? 64  LEU C CA  1 
ATOM   5660 C  C   . LEU C  1  51  ? -13.368 -4.722  17.258 1.00 42.42  ? 64  LEU C C   1 
ATOM   5661 O  O   . LEU C  1  51  ? -14.591 -4.716  17.343 1.00 44.49  ? 64  LEU C O   1 
ATOM   5662 C  CB  . LEU C  1  51  ? -12.101 -2.576  17.230 1.00 40.65  ? 64  LEU C CB  1 
ATOM   5663 C  CG  . LEU C  1  51  ? -11.186 -1.582  16.514 1.00 40.78  ? 64  LEU C CG  1 
ATOM   5664 C  CD1 . LEU C  1  51  ? -10.861 -0.384  17.347 1.00 41.77  ? 64  LEU C CD1 1 
ATOM   5665 C  CD2 . LEU C  1  51  ? -9.925  -2.284  16.117 1.00 41.21  ? 64  LEU C CD2 1 
ATOM   5666 N  N   . PRO C  1  52  ? -12.618 -5.592  17.972 1.00 43.82  ? 65  PRO C N   1 
ATOM   5667 C  CA  . PRO C  1  52  ? -13.196 -6.391  19.055 1.00 43.99  ? 65  PRO C CA  1 
ATOM   5668 C  C   . PRO C  1  52  ? -14.004 -5.475  19.965 1.00 42.31  ? 65  PRO C C   1 
ATOM   5669 O  O   . PRO C  1  52  ? -13.547 -4.387  20.314 1.00 38.33  ? 65  PRO C O   1 
ATOM   5670 C  CB  . PRO C  1  52  ? -11.962 -6.986  19.755 1.00 43.51  ? 65  PRO C CB  1 
ATOM   5671 C  CG  . PRO C  1  52  ? -10.937 -7.088  18.637 1.00 41.70  ? 65  PRO C CG  1 
ATOM   5672 C  CD  . PRO C  1  52  ? -11.175 -5.838  17.801 1.00 39.42  ? 65  PRO C CD  1 
ATOM   5673 N  N   . ARG C  1  53  ? -15.227 -5.897  20.308 1.00 38.91  ? 66  ARG C N   1 
ATOM   5674 C  CA  . ARG C  1  53  ? -16.145 -5.036  21.044 1.00 39.08  ? 66  ARG C CA  1 
ATOM   5675 C  C   . ARG C  1  53  ? -15.660 -4.796  22.478 1.00 36.14  ? 66  ARG C C   1 
ATOM   5676 O  O   . ARG C  1  53  ? -16.110 -3.852  23.123 1.00 45.00  ? 66  ARG C O   1 
ATOM   5677 C  CB  . ARG C  1  53  ? -17.559 -5.634  21.014 1.00 41.13  ? 66  ARG C CB  1 
ATOM   5678 C  CG  . ARG C  1  53  ? -18.137 -5.670  19.605 1.00 42.54  ? 66  ARG C CG  1 
ATOM   5679 C  CD  . ARG C  1  53  ? -19.558 -6.196  19.546 1.00 46.26  ? 66  ARG C CD  1 
ATOM   5680 N  NE  . ARG C  1  53  ? -20.081 -6.179  18.173 1.00 43.19  ? 66  ARG C NE  1 
ATOM   5681 C  CZ  . ARG C  1  53  ? -20.760 -5.176  17.641 1.00 37.74  ? 66  ARG C CZ  1 
ATOM   5682 N  NH1 . ARG C  1  53  ? -20.943 -4.048  18.298 1.00 36.03  ? 66  ARG C NH1 1 
ATOM   5683 N  NH2 . ARG C  1  53  ? -21.246 -5.291  16.417 1.00 43.83  ? 66  ARG C NH2 1 
ATOM   5684 N  N   . ASP C  1  54  ? -14.711 -5.603  22.965 1.00 39.60  ? 67  ASP C N   1 
ATOM   5685 C  CA  . ASP C  1  54  ? -14.164 -5.379  24.297 1.00 41.90  ? 67  ASP C CA  1 
ATOM   5686 C  C   . ASP C  1  54  ? -13.086 -4.290  24.313 1.00 41.77  ? 67  ASP C C   1 
ATOM   5687 O  O   . ASP C  1  54  ? -12.589 -3.952  25.383 1.00 42.49  ? 67  ASP C O   1 
ATOM   5688 C  CB  . ASP C  1  54  ? -13.673 -6.678  24.902 1.00 42.54  ? 67  ASP C CB  1 
ATOM   5689 C  CG  . ASP C  1  54  ? -12.449 -7.330  24.263 1.00 50.95  ? 67  ASP C CG  1 
ATOM   5690 O  OD1 . ASP C  1  54  ? -11.885 -6.770  23.276 1.00 53.54  ? 67  ASP C OD1 1 
ATOM   5691 O  OD2 . ASP C  1  54  ? -12.044 -8.383  24.792 1.00 48.60  ? 67  ASP C OD2 1 
ATOM   5692 N  N   . GLY C  1  55  ? -12.727 -3.730  23.148 1.00 39.18  ? 68  GLY C N   1 
ATOM   5693 C  CA  . GLY C  1  55  ? -11.852 -2.562  23.110 1.00 35.80  ? 68  GLY C CA  1 
ATOM   5694 C  C   . GLY C  1  55  ? -10.369 -2.888  23.319 1.00 35.36  ? 68  GLY C C   1 
ATOM   5695 O  O   . GLY C  1  55  ? -9.568  -2.018  23.643 1.00 41.03  ? 68  GLY C O   1 
ATOM   5696 N  N   . VAL C  1  56  ? -9.990  -4.142  23.102 1.00 37.09  ? 69  VAL C N   1 
ATOM   5697 C  CA  . VAL C  1  56  ? -8.597  -4.555  23.111 1.00 39.32  ? 69  VAL C CA  1 
ATOM   5698 C  C   . VAL C  1  56  ? -8.309  -5.207  21.765 1.00 38.66  ? 69  VAL C C   1 
ATOM   5699 O  O   . VAL C  1  56  ? -9.081  -6.050  21.320 1.00 36.81  ? 69  VAL C O   1 
ATOM   5700 C  CB  . VAL C  1  56  ? -8.328  -5.518  24.282 1.00 41.17  ? 69  VAL C CB  1 
ATOM   5701 C  CG1 . VAL C  1  56  ? -6.930  -6.128  24.233 1.00 44.68  ? 69  VAL C CG1 1 
ATOM   5702 C  CG2 . VAL C  1  56  ? -8.549  -4.813  25.617 1.00 45.30  ? 69  VAL C CG2 1 
ATOM   5703 N  N   . ALA C  1  57  ? -7.216  -4.794  21.110 1.00 37.49  ? 70  ALA C N   1 
ATOM   5704 C  CA  . ALA C  1  57  ? -6.976  -5.185  19.732 1.00 34.64  ? 70  ALA C CA  1 
ATOM   5705 C  C   . ALA C  1  57  ? -5.480  -5.223  19.423 1.00 32.95  ? 70  ALA C C   1 
ATOM   5706 O  O   . ALA C  1  57  ? -4.686  -4.583  20.100 1.00 34.57  ? 70  ALA C O   1 
ATOM   5707 C  CB  . ALA C  1  57  ? -7.699  -4.210  18.816 1.00 33.64  ? 70  ALA C CB  1 
ATOM   5708 N  N   . THR C  1  58  ? -5.127  -5.930  18.344 1.00 32.40  ? 71  THR C N   1 
ATOM   5709 C  CA  . THR C  1  58  ? -3.778  -5.900  17.802 1.00 31.04  ? 71  THR C CA  1 
ATOM   5710 C  C   . THR C  1  58  ? -3.617  -4.625  16.983 1.00 31.65  ? 71  THR C C   1 
ATOM   5711 O  O   . THR C  1  58  ? -4.597  -4.035  16.517 1.00 33.94  ? 71  THR C O   1 
ATOM   5712 C  CB  . THR C  1  58  ? -3.470  -7.123  16.941 1.00 31.80  ? 71  THR C CB  1 
ATOM   5713 O  OG1 . THR C  1  58  ? -4.241  -6.945  15.751 1.00 32.86  ? 71  THR C OG1 1 
ATOM   5714 C  CG2 . THR C  1  58  ? -3.769  -8.434  17.650 1.00 31.32  ? 71  THR C CG2 1 
ATOM   5715 N  N   . PRO C  1  59  ? -2.370  -4.143  16.805 1.00 31.21  ? 72  PRO C N   1 
ATOM   5716 C  CA  . PRO C  1  59  ? -2.122  -3.021  15.901 1.00 29.51  ? 72  PRO C CA  1 
ATOM   5717 C  C   . PRO C  1  59  ? -2.720  -3.219  14.510 1.00 27.33  ? 72  PRO C C   1 
ATOM   5718 O  O   . PRO C  1  59  ? -3.301  -2.295  13.963 1.00 26.33  ? 72  PRO C O   1 
ATOM   5719 C  CB  . PRO C  1  59  ? -0.584  -2.980  15.875 1.00 29.39  ? 72  PRO C CB  1 
ATOM   5720 C  CG  . PRO C  1  59  ? -0.209  -3.431  17.258 1.00 33.82  ? 72  PRO C CG  1 
ATOM   5721 C  CD  . PRO C  1  59  ? -1.164  -4.586  17.530 1.00 31.97  ? 72  PRO C CD  1 
ATOM   5722 N  N   . ALA C  1  60  ? -2.574  -4.425  13.968 1.00 28.62  ? 73  ALA C N   1 
ATOM   5723 C  CA  . ALA C  1  60  ? -3.074  -4.737  12.643 1.00 33.11  ? 73  ALA C CA  1 
ATOM   5724 C  C   . ALA C  1  60  ? -4.591  -4.585  12.613 1.00 34.92  ? 73  ALA C C   1 
ATOM   5725 O  O   . ALA C  1  60  ? -5.104  -4.009  11.658 1.00 31.16  ? 73  ALA C O   1 
ATOM   5726 C  CB  . ALA C  1  60  ? -2.657  -6.130  12.212 1.00 32.88  ? 73  ALA C CB  1 
ATOM   5727 N  N   . GLN C  1  61  ? -5.290  -5.074  13.650 1.00 32.15  ? 74  GLN C N   1 
ATOM   5728 C  CA  . GLN C  1  61  ? -6.735  -4.913  13.719 1.00 33.21  ? 74  GLN C CA  1 
ATOM   5729 C  C   . GLN C  1  61  ? -7.135  -3.442  13.729 1.00 30.84  ? 74  GLN C C   1 
ATOM   5730 O  O   . GLN C  1  61  ? -8.107  -3.065  13.092 1.00 33.82  ? 74  GLN C O   1 
ATOM   5731 C  CB  . GLN C  1  61  ? -7.325  -5.612  14.940 1.00 33.69  ? 74  GLN C CB  1 
ATOM   5732 C  CG  . GLN C  1  61  ? -7.303  -7.126  14.808 1.00 34.70  ? 74  GLN C CG  1 
ATOM   5733 C  CD  . GLN C  1  61  ? -7.728  -7.805  16.094 1.00 39.57  ? 74  GLN C CD  1 
ATOM   5734 O  OE1 . GLN C  1  61  ? -7.386  -7.382  17.203 1.00 37.00  ? 74  GLN C OE1 1 
ATOM   5735 N  NE2 . GLN C  1  61  ? -8.528  -8.842  15.949 1.00 42.19  ? 74  GLN C NE2 1 
ATOM   5736 N  N   . ILE C  1  62  ? -6.385  -2.610  14.451 1.00 29.45  ? 75  ILE C N   1 
ATOM   5737 C  CA  . ILE C  1  62  ? -6.709  -1.192  14.554 1.00 30.55  ? 75  ILE C CA  1 
ATOM   5738 C  C   . ILE C  1  62  ? -6.551  -0.524  13.185 1.00 30.86  ? 75  ILE C C   1 
ATOM   5739 O  O   . ILE C  1  62  ? -7.402  0.262   12.772 1.00 32.50  ? 75  ILE C O   1 
ATOM   5740 C  CB  . ILE C  1  62  ? -5.861  -0.527  15.657 1.00 29.92  ? 75  ILE C CB  1 
ATOM   5741 C  CG1 . ILE C  1  62  ? -6.292  -1.034  17.031 1.00 30.90  ? 75  ILE C CG1 1 
ATOM   5742 C  CG2 . ILE C  1  62  ? -5.925  0.995   15.565 1.00 31.32  ? 75  ILE C CG2 1 
ATOM   5743 C  CD1 . ILE C  1  62  ? -5.312  -0.743  18.160 1.00 30.70  ? 75  ILE C CD1 1 
ATOM   5744 N  N   . ILE C  1  63  ? -5.441  -0.818  12.497 1.00 30.73  ? 76  ILE C N   1 
ATOM   5745 C  CA  . ILE C  1  63  ? -5.177  -0.193  11.216 1.00 31.49  ? 76  ILE C CA  1 
ATOM   5746 C  C   . ILE C  1  63  ? -6.293  -0.563  10.237 1.00 30.39  ? 76  ILE C C   1 
ATOM   5747 O  O   . ILE C  1  63  ? -6.853  0.320   9.614  1.00 27.16  ? 76  ILE C O   1 
ATOM   5748 C  CB  . ILE C  1  63  ? -3.780  -0.566  10.710 1.00 31.40  ? 76  ILE C CB  1 
ATOM   5749 C  CG1 . ILE C  1  63  ? -2.723  0.163   11.550 1.00 32.48  ? 76  ILE C CG1 1 
ATOM   5750 C  CG2 . ILE C  1  63  ? -3.626  -0.249  9.222  1.00 30.31  ? 76  ILE C CG2 1 
ATOM   5751 C  CD1 . ILE C  1  63  ? -1.406  -0.553  11.582 1.00 36.88  ? 76  ILE C CD1 1 
ATOM   5752 N  N   . THR C  1  64  ? -6.656  -1.850  10.162 1.00 29.92  ? 77  THR C N   1 
ATOM   5753 C  CA  A THR C  1  64  ? -7.668  -2.288  9.220  0.50 30.13  ? 77  THR C CA  1 
ATOM   5754 C  CA  B THR C  1  64  ? -7.667  -2.281  9.204  0.50 32.37  ? 77  THR C CA  1 
ATOM   5755 C  C   . THR C  1  64  ? -9.021  -1.672  9.581  1.00 31.79  ? 77  THR C C   1 
ATOM   5756 O  O   . THR C  1  64  ? -9.756  -1.238  8.701  1.00 32.93  ? 77  THR C O   1 
ATOM   5757 C  CB  A THR C  1  64  ? -7.718  -3.811  9.191  0.50 29.30  ? 77  THR C CB  1 
ATOM   5758 C  CB  B THR C  1  64  ? -7.696  -3.802  9.013  0.50 36.09  ? 77  THR C CB  1 
ATOM   5759 O  OG1 A THR C  1  64  ? -8.026  -4.097  10.552 0.50 43.40  ? 77  THR C OG1 1 
ATOM   5760 O  OG1 B THR C  1  64  ? -9.020  -4.221  8.656  0.50 36.02  ? 77  THR C OG1 1 
ATOM   5761 C  CG2 A THR C  1  64  ? -6.411  -4.456  8.806  0.50 22.57  ? 77  THR C CG2 1 
ATOM   5762 C  CG2 B THR C  1  64  ? -7.351  -4.591  10.256 0.50 42.03  ? 77  THR C CG2 1 
ATOM   5763 N  N   . ALA C  1  65  ? -9.333  -1.563  10.887 1.00 31.77  ? 78  ALA C N   1 
ATOM   5764 C  CA  . ALA C  1  65  ? -10.614 -1.010  11.316 1.00 29.59  ? 78  ALA C CA  1 
ATOM   5765 C  C   . ALA C  1  65  ? -10.731 0.470   10.963 1.00 31.49  ? 78  ALA C C   1 
ATOM   5766 O  O   . ALA C  1  65  ? -11.787 0.910   10.505 1.00 29.91  ? 78  ALA C O   1 
ATOM   5767 C  CB  . ALA C  1  65  ? -10.829 -1.222  12.801 1.00 30.77  ? 78  ALA C CB  1 
ATOM   5768 N  N   . THR C  1  66  ? -9.662  1.247   11.163 1.00 27.19  ? 79  THR C N   1 
ATOM   5769 C  CA  . THR C  1  66  ? -9.727  2.673   10.861 1.00 29.30  ? 79  THR C CA  1 
ATOM   5770 C  C   . THR C  1  66  ? -9.858  2.881   9.345  1.00 27.68  ? 79  THR C C   1 
ATOM   5771 O  O   . THR C  1  66  ? -10.505 3.822   8.909  1.00 27.89  ? 79  THR C O   1 
ATOM   5772 C  CB  . THR C  1  66  ? -8.531  3.450   11.420 1.00 30.01  ? 79  THR C CB  1 
ATOM   5773 O  OG1 . THR C  1  66  ? -7.332  2.947   10.857 1.00 29.29  ? 79  THR C OG1 1 
ATOM   5774 C  CG2 . THR C  1  66  ? -8.434  3.346   12.935 1.00 33.28  ? 79  THR C CG2 1 
ATOM   5775 N  N   . GLN C  1  67  ? -9.218  2.028   8.546  1.00 28.87  ? 80  GLN C N   1 
ATOM   5776 C  CA  . GLN C  1  67  ? -9.349  2.086   7.090  1.00 29.14  ? 80  GLN C CA  1 
ATOM   5777 C  C   . GLN C  1  67  ? -10.755 1.666   6.650  1.00 29.74  ? 80  GLN C C   1 
ATOM   5778 O  O   . GLN C  1  67  ? -11.398 2.388   5.910  1.00 31.66  ? 80  GLN C O   1 
ATOM   5779 C  CB  . GLN C  1  67  ? -8.270  1.214   6.469  1.00 27.48  ? 80  GLN C CB  1 
ATOM   5780 C  CG  . GLN C  1  67  ? -6.885  1.796   6.703  1.00 28.61  ? 80  GLN C CG  1 
ATOM   5781 C  CD  . GLN C  1  67  ? -5.743  1.025   6.091  1.00 29.31  ? 80  GLN C CD  1 
ATOM   5782 O  OE1 . GLN C  1  67  ? -4.660  1.583   5.962  1.00 32.96  ? 80  GLN C OE1 1 
ATOM   5783 N  NE2 . GLN C  1  67  ? -5.929  -0.244  5.740  1.00 30.69  ? 80  GLN C NE2 1 
ATOM   5784 N  N   . GLU C  1  68  ? -11.236 0.511   7.116  1.00 29.90  ? 81  GLU C N   1 
ATOM   5785 C  CA  . GLU C  1  68  ? -12.517 -0.007  6.668  1.00 33.48  ? 81  GLU C CA  1 
ATOM   5786 C  C   . GLU C  1  68  ? -13.659 0.906   7.113  1.00 37.17  ? 81  GLU C C   1 
ATOM   5787 O  O   . GLU C  1  68  ? -14.547 1.208   6.319  1.00 34.70  ? 81  GLU C O   1 
ATOM   5788 C  CB  . GLU C  1  68  ? -12.787 -1.403  7.220  1.00 37.70  ? 81  GLU C CB  1 
ATOM   5789 C  CG  . GLU C  1  68  ? -11.872 -2.497  6.691  1.00 44.11  ? 81  GLU C CG  1 
ATOM   5790 C  CD  . GLU C  1  68  ? -11.870 -2.668  5.179  1.00 54.78  ? 81  GLU C CD  1 
ATOM   5791 O  OE1 . GLU C  1  68  ? -10.772 -2.966  4.639  1.00 47.74  ? 81  GLU C OE1 1 
ATOM   5792 O  OE2 . GLU C  1  68  ? -12.952 -2.513  4.552  1.00 54.44  ? 81  GLU C OE2 1 
ATOM   5793 N  N   . GLY C  1  69  ? -13.602 1.399   8.363  1.00 34.90  ? 82  GLY C N   1 
ATOM   5794 C  CA  . GLY C  1  69  ? -14.698 2.148   8.953  1.00 31.28  ? 82  GLY C CA  1 
ATOM   5795 C  C   . GLY C  1  69  ? -14.733 3.615   8.570  1.00 31.11  ? 82  GLY C C   1 
ATOM   5796 O  O   . GLY C  1  69  ? -15.817 4.181   8.428  1.00 34.76  ? 82  GLY C O   1 
ATOM   5797 N  N   . PHE C  1  70  ? -13.560 4.244   8.421  1.00 30.39  ? 83  PHE C N   1 
ATOM   5798 C  CA  . PHE C  1  70  ? -13.507 5.685   8.197  1.00 29.00  ? 83  PHE C CA  1 
ATOM   5799 C  C   . PHE C  1  70  ? -12.666 6.094   6.988  1.00 28.15  ? 83  PHE C C   1 
ATOM   5800 O  O   . PHE C  1  70  ? -12.571 7.284   6.699  1.00 29.25  ? 83  PHE C O   1 
ATOM   5801 C  CB  . PHE C  1  70  ? -12.902 6.388   9.411  1.00 32.68  ? 83  PHE C CB  1 
ATOM   5802 C  CG  . PHE C  1  70  ? -13.845 6.480   10.598 1.00 36.20  ? 83  PHE C CG  1 
ATOM   5803 C  CD1 . PHE C  1  70  ? -14.912 7.372   10.585 1.00 36.79  ? 83  PHE C CD1 1 
ATOM   5804 C  CD2 . PHE C  1  70  ? -13.644 5.703   11.728 1.00 37.49  ? 83  PHE C CD2 1 
ATOM   5805 C  CE1 . PHE C  1  70  ? -15.762 7.476   11.675 1.00 36.83  ? 83  PHE C CE1 1 
ATOM   5806 C  CE2 . PHE C  1  70  ? -14.489 5.814   12.820 1.00 37.67  ? 83  PHE C CE2 1 
ATOM   5807 C  CZ  . PHE C  1  70  ? -15.546 6.697   12.786 1.00 36.98  ? 83  PHE C CZ  1 
ATOM   5808 N  N   . ASN C  1  71  ? -11.987 5.142   6.338  1.00 29.33  ? 84  ASN C N   1 
ATOM   5809 C  CA  . ASN C  1  71  ? -11.055 5.463   5.264  1.00 31.82  ? 84  ASN C CA  1 
ATOM   5810 C  C   . ASN C  1  71  ? -9.905  6.316   5.800  1.00 29.69  ? 84  ASN C C   1 
ATOM   5811 O  O   . ASN C  1  71  ? -9.431  7.243   5.144  1.00 28.74  ? 84  ASN C O   1 
ATOM   5812 C  CB  . ASN C  1  71  ? -11.770 6.137   4.090  1.00 32.40  ? 84  ASN C CB  1 
ATOM   5813 C  CG  . ASN C  1  71  ? -11.260 5.666   2.745  1.00 34.33  ? 84  ASN C CG  1 
ATOM   5814 O  OD1 . ASN C  1  71  ? -10.215 5.006   2.646  1.00 32.83  ? 84  ASN C OD1 1 
ATOM   5815 N  ND2 . ASN C  1  71  ? -11.993 5.995   1.696  1.00 32.12  ? 84  ASN C ND2 1 
ATOM   5816 N  N   . PHE C  1  72  ? -9.473  6.033   7.035  1.00 30.12  ? 85  PHE C N   1 
ATOM   5817 C  CA  . PHE C  1  72  ? -8.283  6.688   7.551  1.00 29.27  ? 85  PHE C CA  1 
ATOM   5818 C  C   . PHE C  1  72  ? -7.110  6.287   6.656  1.00 25.87  ? 85  PHE C C   1 
ATOM   5819 O  O   . PHE C  1  72  ? -6.969  5.111   6.333  1.00 24.93  ? 85  PHE C O   1 
ATOM   5820 C  CB  . PHE C  1  72  ? -8.081  6.277   9.016  1.00 28.44  ? 85  PHE C CB  1 
ATOM   5821 C  CG  . PHE C  1  72  ? -7.203  7.206   9.840  1.00 29.68  ? 85  PHE C CG  1 
ATOM   5822 C  CD1 . PHE C  1  72  ? -7.355  8.581   9.773  1.00 32.25  ? 85  PHE C CD1 1 
ATOM   5823 C  CD2 . PHE C  1  72  ? -6.244  6.698   10.711 1.00 32.19  ? 85  PHE C CD2 1 
ATOM   5824 C  CE1 . PHE C  1  72  ? -6.569  9.419   10.556 1.00 34.33  ? 85  PHE C CE1 1 
ATOM   5825 C  CE2 . PHE C  1  72  ? -5.462  7.544   11.482 1.00 32.24  ? 85  PHE C CE2 1 
ATOM   5826 C  CZ  . PHE C  1  72  ? -5.608  8.895   11.395 1.00 30.84  ? 85  PHE C CZ  1 
ATOM   5827 N  N   . GLU C  1  73  ? -6.281  7.247   6.271  1.00 29.00  ? 86  GLU C N   1 
ATOM   5828 C  CA  . GLU C  1  73  ? -5.164  6.988   5.361  1.00 31.89  ? 86  GLU C CA  1 
ATOM   5829 C  C   . GLU C  1  73  ? -4.140  6.069   6.030  1.00 30.70  ? 86  GLU C C   1 
ATOM   5830 O  O   . GLU C  1  73  ? -3.848  6.203   7.207  1.00 28.32  ? 86  GLU C O   1 
ATOM   5831 C  CB  . GLU C  1  73  ? -4.588  8.330   4.901  1.00 33.78  ? 86  GLU C CB  1 
ATOM   5832 C  CG  . GLU C  1  73  ? -3.552  8.208   3.782  1.00 36.69  ? 86  GLU C CG  1 
ATOM   5833 C  CD  . GLU C  1  73  ? -2.133  7.847   4.212  1.00 40.13  ? 86  GLU C CD  1 
ATOM   5834 O  OE1 . GLU C  1  73  ? -1.434  7.010   3.566  1.00 38.86  ? 86  GLU C OE1 1 
ATOM   5835 O  OE2 . GLU C  1  73  ? -1.729  8.405   5.251  1.00 38.07  ? 86  GLU C OE2 1 
ATOM   5836 N  N   . ASN C  1  74  ? -3.567  5.158   5.251  1.00 28.97  ? 87  ASN C N   1 
ATOM   5837 C  CA  . ASN C  1  74  ? -2.765  4.037   5.722  1.00 29.57  ? 87  ASN C CA  1 
ATOM   5838 C  C   . ASN C  1  74  ? -1.577  4.487   6.584  1.00 30.44  ? 87  ASN C C   1 
ATOM   5839 O  O   . ASN C  1  74  ? -1.384  3.966   7.666  1.00 30.19  ? 87  ASN C O   1 
ATOM   5840 C  CB  . ASN C  1  74  ? -2.324  3.195   4.532  1.00 27.72  ? 87  ASN C CB  1 
ATOM   5841 C  CG  . ASN C  1  74  ? -1.449  2.031   4.905  1.00 26.23  ? 87  ASN C CG  1 
ATOM   5842 O  OD1 . ASN C  1  74  ? -0.289  1.971   4.480  1.00 28.92  ? 87  ASN C OD1 1 
ATOM   5843 N  ND2 . ASN C  1  74  ? -1.986  1.099   5.666  1.00 27.04  ? 87  ASN C ND2 1 
ATOM   5844 N  N   . ASN C  1  75  ? -0.778  5.439   6.111  1.00 29.68  ? 88  ASN C N   1 
ATOM   5845 C  CA  . ASN C  1  75  ? 0.390   5.873   6.857  1.00 32.83  ? 88  ASN C CA  1 
ATOM   5846 C  C   . ASN C  1  75  ? -0.013  6.663   8.099  1.00 32.33  ? 88  ASN C C   1 
ATOM   5847 O  O   . ASN C  1  75  ? 0.643   6.543   9.117  1.00 30.27  ? 88  ASN C O   1 
ATOM   5848 C  CB  . ASN C  1  75  ? 1.391   6.587   5.964  1.00 31.22  ? 88  ASN C CB  1 
ATOM   5849 C  CG  . ASN C  1  75  ? 2.177   5.569   5.154  1.00 33.91  ? 88  ASN C CG  1 
ATOM   5850 O  OD1 . ASN C  1  75  ? 2.641   4.539   5.668  1.00 32.70  ? 88  ASN C OD1 1 
ATOM   5851 N  ND2 . ASN C  1  75  ? 2.266   5.786   3.860  1.00 33.31  ? 88  ASN C ND2 1 
ATOM   5852 N  N   . ALA C  1  76  ? -1.078  7.453   8.025  1.00 29.28  ? 89  ALA C N   1 
ATOM   5853 C  CA  . ALA C  1  76  ? -1.610  8.124   9.205  1.00 31.61  ? 89  ALA C CA  1 
ATOM   5854 C  C   . ALA C  1  76  ? -2.045  7.096   10.249 1.00 30.67  ? 89  ALA C C   1 
ATOM   5855 O  O   . ALA C  1  76  ? -1.797  7.282   11.446 1.00 31.80  ? 89  ALA C O   1 
ATOM   5856 C  CB  . ALA C  1  76  ? -2.739  9.057   8.831  1.00 32.10  ? 89  ALA C CB  1 
ATOM   5857 N  N   . ALA C  1  77  ? -2.664  6.001   9.795  1.00 28.45  ? 90  ALA C N   1 
ATOM   5858 C  CA  . ALA C  1  77  ? -3.075  4.924   10.690 1.00 29.07  ? 90  ALA C CA  1 
ATOM   5859 C  C   . ALA C  1  77  ? -1.856  4.255   11.321 1.00 27.55  ? 90  ALA C C   1 
ATOM   5860 O  O   . ALA C  1  77  ? -1.856  3.952   12.515 1.00 28.34  ? 90  ALA C O   1 
ATOM   5861 C  CB  . ALA C  1  77  ? -3.921  3.906   9.960  1.00 29.05  ? 90  ALA C CB  1 
ATOM   5862 N  N   . ILE C  1  78  ? -0.817  4.022   10.522 1.00 27.21  ? 91  ILE C N   1 
ATOM   5863 C  CA  . ILE C  1  78  ? 0.395   3.374   11.010 1.00 28.49  ? 91  ILE C CA  1 
ATOM   5864 C  C   . ILE C  1  78  ? 1.089   4.270   12.031 1.00 26.81  ? 91  ILE C C   1 
ATOM   5865 O  O   . ILE C  1  78  ? 1.473   3.797   13.100 1.00 27.45  ? 91  ILE C O   1 
ATOM   5866 C  CB  . ILE C  1  78  ? 1.295   2.962   9.834  1.00 29.06  ? 91  ILE C CB  1 
ATOM   5867 C  CG1 . ILE C  1  78  ? 0.674   1.775   9.109  1.00 29.41  ? 91  ILE C CG1 1 
ATOM   5868 C  CG2 . ILE C  1  78  ? 2.715   2.627   10.284 1.00 28.64  ? 91  ILE C CG2 1 
ATOM   5869 C  CD1 . ILE C  1  78  ? 1.286   1.488   7.745  1.00 31.56  ? 91  ILE C CD1 1 
ATOM   5870 N  N   . VAL C  1  79  ? 1.178   5.572   11.745 1.00 25.45  ? 92  VAL C N   1 
ATOM   5871 C  CA  . VAL C  1  79  ? 1.822   6.501   12.658 1.00 29.26  ? 92  VAL C CA  1 
ATOM   5872 C  C   . VAL C  1  79  ? 1.099   6.534   14.005 1.00 32.21  ? 92  VAL C C   1 
ATOM   5873 O  O   . VAL C  1  79  ? 1.755   6.441   15.043 1.00 30.66  ? 92  VAL C O   1 
ATOM   5874 C  CB  . VAL C  1  79  ? 1.969   7.908   12.058 1.00 28.84  ? 92  VAL C CB  1 
ATOM   5875 C  CG1 . VAL C  1  79  ? 2.417   8.923   13.095 1.00 30.60  ? 92  VAL C CG1 1 
ATOM   5876 C  CG2 . VAL C  1  79  ? 2.956   7.916   10.899 1.00 30.38  ? 92  VAL C CG2 1 
ATOM   5877 N  N   . ALA C  1  80  ? -0.236  6.672   13.995 1.00 28.70  ? 93  ALA C N   1 
ATOM   5878 C  CA  . ALA C  1  80  ? -0.994  6.729   15.232 1.00 28.90  ? 93  ALA C CA  1 
ATOM   5879 C  C   . ALA C  1  80  ? -0.943  5.395   15.974 1.00 30.03  ? 93  ALA C C   1 
ATOM   5880 O  O   . ALA C  1  80  ? -0.755  5.368   17.185 1.00 30.63  ? 93  ALA C O   1 
ATOM   5881 C  CB  . ALA C  1  80  ? -2.430  7.138   14.969 1.00 32.21  ? 93  ALA C CB  1 
ATOM   5882 N  N   . THR C  1  81  ? -1.094  4.281   15.257 1.00 28.59  ? 94  THR C N   1 
ATOM   5883 C  CA  . THR C  1  81  ? -1.330  2.998   15.906 1.00 26.92  ? 94  THR C CA  1 
ATOM   5884 C  C   . THR C  1  81  ? -0.063  2.513   16.613 1.00 31.60  ? 94  THR C C   1 
ATOM   5885 O  O   . THR C  1  81  ? -0.136  2.082   17.758 1.00 29.40  ? 94  THR C O   1 
ATOM   5886 C  CB  . THR C  1  81  ? -1.832  1.959   14.913 1.00 27.12  ? 94  THR C CB  1 
ATOM   5887 O  OG1 . THR C  1  81  ? -3.106  2.370   14.422 1.00 25.85  ? 94  THR C OG1 1 
ATOM   5888 C  CG2 . THR C  1  81  ? -1.954  0.579   15.540 1.00 28.77  ? 94  THR C CG2 1 
ATOM   5889 N  N   . TYR C  1  82  ? 1.089   2.557   15.934 1.00 29.84  ? 95  TYR C N   1 
ATOM   5890 C  CA  . TYR C  1  82  ? 2.311   2.030   16.519 1.00 29.14  ? 95  TYR C CA  1 
ATOM   5891 C  C   . TYR C  1  82  ? 2.867   3.000   17.564 1.00 29.35  ? 95  TYR C C   1 
ATOM   5892 O  O   . TYR C  1  82  ? 3.540   2.566   18.488 1.00 31.94  ? 95  TYR C O   1 
ATOM   5893 C  CB  . TYR C  1  82  ? 3.323   1.622   15.443 1.00 28.34  ? 95  TYR C CB  1 
ATOM   5894 C  CG  . TYR C  1  82  ? 2.867   0.392   14.686 1.00 29.21  ? 95  TYR C CG  1 
ATOM   5895 C  CD1 . TYR C  1  82  ? 2.991   -0.878  15.236 1.00 30.46  ? 95  TYR C CD1 1 
ATOM   5896 C  CD2 . TYR C  1  82  ? 2.241   0.500   13.447 1.00 33.85  ? 95  TYR C CD2 1 
ATOM   5897 C  CE1 . TYR C  1  82  ? 2.554   -2.006  14.564 1.00 27.30  ? 95  TYR C CE1 1 
ATOM   5898 C  CE2 . TYR C  1  82  ? 1.786   -0.619  12.775 1.00 33.46  ? 95  TYR C CE2 1 
ATOM   5899 C  CZ  . TYR C  1  82  ? 1.940   -1.874  13.328 1.00 33.39  ? 95  TYR C CZ  1 
ATOM   5900 O  OH  . TYR C  1  82  ? 1.495   -2.978  12.654 1.00 34.17  ? 95  TYR C OH  1 
ATOM   5901 N  N   . LEU C  1  83  ? 2.585   4.292   17.444 1.00 30.59  ? 96  LEU C N   1 
ATOM   5902 C  CA  . LEU C  1  83  ? 2.910   5.229   18.508 1.00 32.46  ? 96  LEU C CA  1 
ATOM   5903 C  C   . LEU C  1  83  ? 2.156   4.800   19.769 1.00 35.30  ? 96  LEU C C   1 
ATOM   5904 O  O   . LEU C  1  83  ? 2.733   4.668   20.836 1.00 32.75  ? 96  LEU C O   1 
ATOM   5905 C  CB  . LEU C  1  83  ? 2.548   6.647   18.074 1.00 32.60  ? 96  LEU C CB  1 
ATOM   5906 C  CG  . LEU C  1  83  ? 2.575   7.741   19.142 1.00 36.02  ? 96  LEU C CG  1 
ATOM   5907 C  CD1 . LEU C  1  83  ? 3.971   7.928   19.655 1.00 37.60  ? 96  LEU C CD1 1 
ATOM   5908 C  CD2 . LEU C  1  83  ? 2.056   9.042   18.582 1.00 37.36  ? 96  LEU C CD2 1 
ATOM   5909 N  N   . GLY C  1  84  ? 0.854   4.572   19.636 1.00 30.54  ? 97  GLY C N   1 
ATOM   5910 C  CA  . GLY C  1  84  ? 0.040   4.139   20.760 1.00 31.97  ? 97  GLY C CA  1 
ATOM   5911 C  C   . GLY C  1  84  ? 0.504   2.793   21.308 1.00 31.46  ? 97  GLY C C   1 
ATOM   5912 O  O   . GLY C  1  84  ? 0.577   2.610   22.518 1.00 30.69  ? 97  GLY C O   1 
ATOM   5913 N  N   . HIS C  1  85  ? 0.832   1.853   20.415 1.00 27.66  ? 98  HIS C N   1 
ATOM   5914 C  CA  . HIS C  1  85  ? 1.247   0.527   20.844 1.00 26.58  ? 98  HIS C CA  1 
ATOM   5915 C  C   . HIS C  1  85  ? 2.622   0.540   21.534 1.00 30.06  ? 98  HIS C C   1 
ATOM   5916 O  O   . HIS C  1  85  ? 2.796   -0.069  22.585 1.00 28.83  ? 98  HIS C O   1 
ATOM   5917 C  CB  . HIS C  1  85  ? 1.240   -0.417  19.652 1.00 26.72  ? 98  HIS C CB  1 
ATOM   5918 C  CG  . HIS C  1  85  ? 1.475   -1.827  20.015 1.00 28.14  ? 98  HIS C CG  1 
ATOM   5919 N  ND1 . HIS C  1  85  ? 0.693   -2.472  20.944 1.00 29.76  ? 98  HIS C ND1 1 
ATOM   5920 C  CD2 . HIS C  1  85  ? 2.343   -2.736  19.545 1.00 30.15  ? 98  HIS C CD2 1 
ATOM   5921 C  CE1 . HIS C  1  85  ? 1.101   -3.734  21.035 1.00 30.70  ? 98  HIS C CE1 1 
ATOM   5922 N  NE2 . HIS C  1  85  ? 2.121   -3.910  20.217 1.00 30.99  ? 98  HIS C NE2 1 
ATOM   5923 N  N   . LEU C  1  86  ? 3.618   1.210   20.944 1.00 29.23  ? 99  LEU C N   1 
ATOM   5924 C  CA  . LEU C  1  86  ? 4.958   1.251   21.525 1.00 30.82  ? 99  LEU C CA  1 
ATOM   5925 C  C   . LEU C  1  86  ? 4.920   1.815   22.954 1.00 29.23  ? 99  LEU C C   1 
ATOM   5926 O  O   . LEU C  1  86  ? 5.548   1.270   23.846 1.00 33.00  ? 99  LEU C O   1 
ATOM   5927 C  CB  . LEU C  1  86  ? 5.867   2.085   20.625 1.00 28.29  ? 99  LEU C CB  1 
ATOM   5928 C  CG  . LEU C  1  86  ? 6.379   1.377   19.369 1.00 28.17  ? 99  LEU C CG  1 
ATOM   5929 C  CD1 . LEU C  1  86  ? 6.959   2.374   18.407 1.00 28.80  ? 99  LEU C CD1 1 
ATOM   5930 C  CD2 . LEU C  1  86  ? 7.422   0.326   19.715 1.00 31.16  ? 99  LEU C CD2 1 
ATOM   5931 N  N   . LEU C  1  87  ? 4.153   2.891   23.157 1.00 31.38  ? 100 LEU C N   1 
ATOM   5932 C  CA  . LEU C  1  87  ? 4.092   3.592   24.430 1.00 32.23  ? 100 LEU C CA  1 
ATOM   5933 C  C   . LEU C  1  87  ? 3.124   2.931   25.407 1.00 33.39  ? 100 LEU C C   1 
ATOM   5934 O  O   . LEU C  1  87  ? 3.377   2.976   26.610 1.00 32.92  ? 100 LEU C O   1 
ATOM   5935 C  CB  . LEU C  1  87  ? 3.683   5.037   24.196 1.00 30.37  ? 100 LEU C CB  1 
ATOM   5936 C  CG  . LEU C  1  87  ? 4.670   5.896   23.408 1.00 32.71  ? 100 LEU C CG  1 
ATOM   5937 C  CD1 . LEU C  1  87  ? 4.077   7.272   23.186 1.00 33.48  ? 100 LEU C CD1 1 
ATOM   5938 C  CD2 . LEU C  1  87  ? 6.028   6.007   24.079 1.00 38.40  ? 100 LEU C CD2 1 
ATOM   5939 N  N   . ASN C  1  88  ? 2.024   2.347   24.906 1.00 29.03  ? 101 ASN C N   1 
ATOM   5940 C  CA  . ASN C  1  88  ? 0.901   2.008   25.768 1.00 31.71  ? 101 ASN C CA  1 
ATOM   5941 C  C   . ASN C  1  88  ? 0.397   0.580   25.587 1.00 31.72  ? 101 ASN C C   1 
ATOM   5942 O  O   . ASN C  1  88  ? -0.533  0.176   26.292 1.00 31.08  ? 101 ASN C O   1 
ATOM   5943 C  CB  . ASN C  1  88  ? -0.311  2.902   25.550 1.00 31.61  ? 101 ASN C CB  1 
ATOM   5944 C  CG  . ASN C  1  88  ? -0.012  4.356   25.786 1.00 32.94  ? 101 ASN C CG  1 
ATOM   5945 O  OD1 . ASN C  1  88  ? 0.633   4.704   26.771 1.00 35.10  ? 101 ASN C OD1 1 
ATOM   5946 N  ND2 . ASN C  1  88  ? -0.476  5.233   24.911 1.00 35.47  ? 101 ASN C ND2 1 
ATOM   5947 N  N   . GLY C  1  89  ? 0.996   -0.200  24.688 1.00 29.97  ? 102 GLY C N   1 
ATOM   5948 C  CA  . GLY C  1  89  ? 0.533   -1.559  24.456 1.00 27.93  ? 102 GLY C CA  1 
ATOM   5949 C  C   . GLY C  1  89  ? 1.488   -2.604  25.024 1.00 29.94  ? 102 GLY C C   1 
ATOM   5950 O  O   . GLY C  1  89  ? 2.585   -2.293  25.485 1.00 32.54  ? 102 GLY C O   1 
ATOM   5951 N  N   . ASN C  1  90  ? 1.062   -3.858  24.926 1.00 29.24  ? 103 ASN C N   1 
ATOM   5952 C  CA  . ASN C  1  90  ? 1.871   -4.986  25.331 1.00 32.19  ? 103 ASN C CA  1 
ATOM   5953 C  C   . ASN C  1  90  ? 2.539   -5.576  24.093 1.00 34.53  ? 103 ASN C C   1 
ATOM   5954 O  O   . ASN C  1  90  ? 1.881   -6.200  23.264 1.00 32.77  ? 103 ASN C O   1 
ATOM   5955 C  CB  . ASN C  1  90  ? 1.013   -6.014  26.060 1.00 33.86  ? 103 ASN C CB  1 
ATOM   5956 C  CG  . ASN C  1  90  ? 1.852   -7.080  26.716 1.00 37.69  ? 103 ASN C CG  1 
ATOM   5957 O  OD1 . ASN C  1  90  ? 2.759   -7.636  26.077 1.00 36.00  ? 103 ASN C OD1 1 
ATOM   5958 N  ND2 . ASN C  1  90  ? 1.565   -7.359  27.987 1.00 42.76  ? 103 ASN C ND2 1 
ATOM   5959 N  N   . LEU C  1  91  ? 3.861   -5.410  24.009 1.00 32.23  ? 104 LEU C N   1 
ATOM   5960 C  CA  . LEU C  1  91  ? 4.605   -5.752  22.812 1.00 35.57  ? 104 LEU C CA  1 
ATOM   5961 C  C   . LEU C  1  91  ? 4.770   -7.257  22.666 1.00 35.20  ? 104 LEU C C   1 
ATOM   5962 O  O   . LEU C  1  91  ? 4.929   -7.753  21.550 1.00 37.03  ? 104 LEU C O   1 
ATOM   5963 C  CB  . LEU C  1  91  ? 5.936   -5.009  22.867 1.00 38.19  ? 104 LEU C CB  1 
ATOM   5964 C  CG  . LEU C  1  91  ? 5.772   -3.485  22.851 1.00 44.49  ? 104 LEU C CG  1 
ATOM   5965 C  CD1 . LEU C  1  91  ? 7.066   -2.799  23.080 1.00 47.87  ? 104 LEU C CD1 1 
ATOM   5966 C  CD2 . LEU C  1  91  ? 5.192   -3.006  21.530 1.00 49.42  ? 104 LEU C CD2 1 
ATOM   5967 N  N   . VAL C  1  92  ? 4.694   -7.987  23.785 1.00 33.81  ? 105 VAL C N   1 
ATOM   5968 C  CA  . VAL C  1  92  ? 4.866   -9.429  23.769 1.00 35.94  ? 105 VAL C CA  1 
ATOM   5969 C  C   . VAL C  1  92  ? 3.579   -10.124 23.327 1.00 34.85  ? 105 VAL C C   1 
ATOM   5970 O  O   . VAL C  1  92  ? 3.642   -11.045 22.525 1.00 39.23  ? 105 VAL C O   1 
ATOM   5971 C  CB  . VAL C  1  92  ? 5.379   -9.921  25.132 1.00 40.12  ? 105 VAL C CB  1 
ATOM   5972 C  CG1 . VAL C  1  92  ? 5.355   -11.440 25.227 1.00 40.35  ? 105 VAL C CG1 1 
ATOM   5973 C  CG2 . VAL C  1  92  ? 6.793   -9.386  25.375 1.00 40.83  ? 105 VAL C CG2 1 
ATOM   5974 N  N   . THR C  1  93  ? 2.419   -9.694  23.831 1.00 36.23  ? 106 THR C N   1 
ATOM   5975 C  CA  . THR C  1  93  ? 1.154   -10.294 23.426 1.00 39.23  ? 106 THR C CA  1 
ATOM   5976 C  C   . THR C  1  93  ? 0.593   -9.614  22.171 1.00 42.57  ? 106 THR C C   1 
ATOM   5977 O  O   . THR C  1  93  ? -0.368  -10.120 21.595 1.00 39.88  ? 106 THR C O   1 
ATOM   5978 C  CB  . THR C  1  93  ? 0.130   -10.214 24.556 1.00 40.68  ? 106 THR C CB  1 
ATOM   5979 O  OG1 . THR C  1  93  ? -0.090  -8.816  24.744 1.00 38.94  ? 106 THR C OG1 1 
ATOM   5980 C  CG2 . THR C  1  93  ? 0.612   -10.904 25.826 1.00 47.29  ? 106 THR C CG2 1 
ATOM   5981 N  N   . ASP C  1  94  ? 1.160   -8.457  21.789 1.00 37.30  ? 107 ASP C N   1 
ATOM   5982 C  CA  . ASP C  1  94  ? 0.716   -7.694  20.627 1.00 36.24  ? 107 ASP C CA  1 
ATOM   5983 C  C   . ASP C  1  94  ? -0.705  -7.160  20.802 1.00 38.25  ? 107 ASP C C   1 
ATOM   5984 O  O   . ASP C  1  94  ? -1.479  -7.131  19.844 1.00 40.46  ? 107 ASP C O   1 
ATOM   5985 C  CB  . ASP C  1  94  ? 0.870   -8.497  19.342 1.00 35.80  ? 107 ASP C CB  1 
ATOM   5986 C  CG  . ASP C  1  94  ? 0.950   -7.670  18.058 1.00 37.83  ? 107 ASP C CG  1 
ATOM   5987 O  OD1 . ASP C  1  94  ? 1.639   -6.629  18.083 1.00 36.81  ? 107 ASP C OD1 1 
ATOM   5988 O  OD2 . ASP C  1  94  ? 0.326   -8.081  17.041 1.00 36.72  ? 107 ASP C OD2 1 
ATOM   5989 N  N   . LEU C  1  95  ? -1.054  -6.722  22.020 1.00 34.85  ? 108 LEU C N   1 
ATOM   5990 C  CA  . LEU C  1  95  ? -2.386  -6.201  22.291 1.00 32.81  ? 108 LEU C CA  1 
ATOM   5991 C  C   . LEU C  1  95  ? -2.289  -4.803  22.895 1.00 32.95  ? 108 LEU C C   1 
ATOM   5992 O  O   . LEU C  1  95  ? -1.432  -4.537  23.733 1.00 35.35  ? 108 LEU C O   1 
ATOM   5993 C  CB  . LEU C  1  95  ? -3.139  -7.159  23.214 1.00 34.44  ? 108 LEU C CB  1 
ATOM   5994 C  CG  . LEU C  1  95  ? -3.403  -8.565  22.668 1.00 36.57  ? 108 LEU C CG  1 
ATOM   5995 C  CD1 . LEU C  1  95  ? -3.830  -9.503  23.793 1.00 41.28  ? 108 LEU C CD1 1 
ATOM   5996 C  CD2 . LEU C  1  95  ? -4.474  -8.525  21.564 1.00 37.89  ? 108 LEU C CD2 1 
ATOM   5997 N  N   . LEU C  1  96  ? -3.201  -3.928  22.467 1.00 31.75  ? 109 LEU C N   1 
ATOM   5998 C  CA  . LEU C  1  96  ? -3.326  -2.575  22.970 1.00 31.94  ? 109 LEU C CA  1 
ATOM   5999 C  C   . LEU C  1  96  ? -4.764  -2.336  23.445 1.00 38.22  ? 109 LEU C C   1 
ATOM   6000 O  O   . LEU C  1  96  ? -5.727  -2.614  22.720 1.00 35.99  ? 109 LEU C O   1 
ATOM   6001 C  CB  . LEU C  1  96  ? -2.958  -1.613  21.853 1.00 32.13  ? 109 LEU C CB  1 
ATOM   6002 C  CG  . LEU C  1  96  ? -3.272  -0.129  22.086 1.00 32.08  ? 109 LEU C CG  1 
ATOM   6003 C  CD1 . LEU C  1  96  ? -2.483  0.440   23.263 1.00 37.07  ? 109 LEU C CD1 1 
ATOM   6004 C  CD2 . LEU C  1  96  ? -2.985  0.693   20.860 1.00 32.06  ? 109 LEU C CD2 1 
ATOM   6005 N  N   . SER C  1  97  ? -4.891  -1.795  24.668 1.00 33.68  ? 110 SER C N   1 
ATOM   6006 C  CA  . SER C  1  97  ? -6.172  -1.325  25.165 1.00 35.01  ? 110 SER C CA  1 
ATOM   6007 C  C   . SER C  1  97  ? -6.452  0.063   24.620 1.00 34.04  ? 110 SER C C   1 
ATOM   6008 O  O   . SER C  1  97  ? -5.584  0.925   24.714 1.00 34.43  ? 110 SER C O   1 
ATOM   6009 C  CB  . SER C  1  97  ? -6.200  -1.321  26.677 1.00 36.26  ? 110 SER C CB  1 
ATOM   6010 O  OG  . SER C  1  97  ? -7.301  -0.558  27.158 1.00 38.15  ? 110 SER C OG  1 
ATOM   6011 N  N   . ILE C  1  98  ? -7.668  0.297   24.085 1.00 30.98  ? 111 ILE C N   1 
ATOM   6012 C  CA  . ILE C  1  98  ? -7.987  1.618   23.563 1.00 29.79  ? 111 ILE C CA  1 
ATOM   6013 C  C   . ILE C  1  98  ? -8.397  2.550   24.693 1.00 33.86  ? 111 ILE C C   1 
ATOM   6014 O  O   . ILE C  1  98  ? -8.724  3.710   24.445 1.00 38.32  ? 111 ILE C O   1 
ATOM   6015 C  CB  . ILE C  1  98  ? -9.064  1.567   22.462 1.00 35.20  ? 111 ILE C CB  1 
ATOM   6016 C  CG1 . ILE C  1  98  ? -10.470 1.194   23.005 1.00 36.97  ? 111 ILE C CG1 1 
ATOM   6017 C  CG2 . ILE C  1  98  ? -8.625  0.633   21.342 1.00 34.39  ? 111 ILE C CG2 1 
ATOM   6018 C  CD1 . ILE C  1  98  ? -11.569 1.216   21.953 1.00 37.76  ? 111 ILE C CD1 1 
ATOM   6019 N  N   . GLY C  1  99  ? -8.419  2.024   25.925 1.00 38.93  ? 112 GLY C N   1 
ATOM   6020 C  CA  . GLY C  1  99  ? -8.716  2.822   27.100 1.00 42.98  ? 112 GLY C CA  1 
ATOM   6021 C  C   . GLY C  1  99  ? -7.661  2.596   28.182 1.00 45.49  ? 112 GLY C C   1 
ATOM   6022 O  O   . GLY C  1  99  ? -6.489  2.937   27.988 1.00 36.30  ? 112 GLY C O   1 
ATOM   6023 N  N   . GLY C  1  100 ? -8.103  2.044   29.319 1.00 43.68  ? 113 GLY C N   1 
ATOM   6024 C  CA  . GLY C  1  100 ? -7.263  1.905   30.502 1.00 43.30  ? 113 GLY C CA  1 
ATOM   6025 C  C   . GLY C  1  100 ? -6.725  0.484   30.659 1.00 40.40  ? 113 GLY C C   1 
ATOM   6026 O  O   . GLY C  1  100 ? -6.844  -0.343  29.764 1.00 39.47  ? 113 GLY C O   1 
ATOM   6027 N  N   . ALA C  1  101 ? -6.163  0.197   31.837 1.00 41.29  ? 114 ALA C N   1 
ATOM   6028 C  CA  . ALA C  1  101 ? -5.466  -1.055  32.085 1.00 38.67  ? 114 ALA C CA  1 
ATOM   6029 C  C   . ALA C  1  101 ? -6.455  -2.204  32.155 1.00 41.71  ? 114 ALA C C   1 
ATOM   6030 O  O   . ALA C  1  101 ? -7.591  -2.037  32.593 1.00 45.78  ? 114 ALA C O   1 
ATOM   6031 C  CB  . ALA C  1  101 ? -4.666  -0.958  33.374 1.00 45.74  ? 114 ALA C CB  1 
ATOM   6032 N  N   . THR C  1  102 ? -6.009  -3.384  31.734 1.00 41.15  ? 115 THR C N   1 
ATOM   6033 C  CA  . THR C  1  102 ? -6.897  -4.522  31.702 1.00 45.52  ? 115 THR C CA  1 
ATOM   6034 C  C   . THR C  1  102 ? -6.058  -5.780  31.666 1.00 51.77  ? 115 THR C C   1 
ATOM   6035 O  O   . THR C  1  102 ? -5.028  -5.808  31.001 1.00 52.54  ? 115 THR C O   1 
ATOM   6036 C  CB  . THR C  1  102 ? -7.825  -4.433  30.484 1.00 57.72  ? 115 THR C CB  1 
ATOM   6037 O  OG1 . THR C  1  102 ? -8.551  -5.661  30.469 1.00 53.37  ? 115 THR C OG1 1 
ATOM   6038 C  CG2 . THR C  1  102 ? -7.070  -4.240  29.177 1.00 54.37  ? 115 THR C CG2 1 
ATOM   6039 N  N   . PRO C  1  103 ? -6.487  -6.862  32.352 1.00 52.31  ? 116 PRO C N   1 
ATOM   6040 C  CA  . PRO C  1  103 ? -5.827  -8.162  32.213 1.00 53.13  ? 116 PRO C CA  1 
ATOM   6041 C  C   . PRO C  1  103 ? -5.894  -8.710  30.787 1.00 43.35  ? 116 PRO C C   1 
ATOM   6042 O  O   . PRO C  1  103 ? -5.132  -9.602  30.432 1.00 49.28  ? 116 PRO C O   1 
ATOM   6043 C  CB  . PRO C  1  103 ? -6.571  -9.080  33.230 1.00 55.83  ? 116 PRO C CB  1 
ATOM   6044 C  CG  . PRO C  1  103 ? -7.892  -8.367  33.514 1.00 55.82  ? 116 PRO C CG  1 
ATOM   6045 C  CD  . PRO C  1  103 ? -7.607  -6.877  33.307 1.00 53.33  ? 116 PRO C CD  1 
ATOM   6046 N  N   . LYS C  1  104 ? -6.818  -8.194  29.976 1.00 46.99  ? 117 LYS C N   1 
ATOM   6047 C  CA  . LYS C  1  104 ? -7.016  -8.680  28.618 1.00 52.45  ? 117 LYS C CA  1 
ATOM   6048 C  C   . LYS C  1  104 ? -5.770  -8.476  27.746 1.00 49.18  ? 117 LYS C C   1 
ATOM   6049 O  O   . LYS C  1  104 ? -5.631  -9.172  26.744 1.00 50.25  ? 117 LYS C O   1 
ATOM   6050 C  CB  . LYS C  1  104 ? -8.213  -7.998  27.951 1.00 54.38  ? 117 LYS C CB  1 
ATOM   6051 C  CG  . LYS C  1  104 ? -9.591  -8.280  28.531 1.00 58.82  ? 117 LYS C CG  1 
ATOM   6052 C  CD  . LYS C  1  104 ? -10.612 -7.230  28.089 1.00 65.25  ? 117 LYS C CD  1 
ATOM   6053 C  CE  . LYS C  1  104 ? -12.003 -7.435  28.609 1.00 71.36  ? 117 LYS C CE  1 
ATOM   6054 N  NZ  . LYS C  1  104 ? -12.568 -8.678  28.067 1.00 73.65  ? 117 LYS C NZ  1 
ATOM   6055 N  N   . THR C  1  105 ? -4.864  -7.551  28.118 1.00 46.49  ? 118 THR C N   1 
ATOM   6056 C  CA  . THR C  1  105 ? -3.653  -7.344  27.334 1.00 48.58  ? 118 THR C CA  1 
ATOM   6057 C  C   . THR C  1  105 ? -2.573  -8.342  27.728 1.00 51.53  ? 118 THR C C   1 
ATOM   6058 O  O   . THR C  1  105 ? -1.541  -8.391  27.078 1.00 49.08  ? 118 THR C O   1 
ATOM   6059 C  CB  . THR C  1  105 ? -3.138  -5.906  27.400 1.00 43.62  ? 118 THR C CB  1 
ATOM   6060 O  OG1 . THR C  1  105 ? -2.927  -5.482  28.739 1.00 43.41  ? 118 THR C OG1 1 
ATOM   6061 C  CG2 . THR C  1  105 ? -4.097  -4.924  26.753 1.00 40.77  ? 118 THR C CG2 1 
ATOM   6062 N  N   . GLY C  1  106 ? -2.806  -9.133  28.780 1.00 54.02  ? 119 GLY C N   1 
ATOM   6063 C  CA  . GLY C  1  106 ? -1.878  -10.176 29.189 1.00 50.63  ? 119 GLY C CA  1 
ATOM   6064 C  C   . GLY C  1  106 ? -0.967  -9.728  30.333 1.00 49.53  ? 119 GLY C C   1 
ATOM   6065 O  O   . GLY C  1  106 ? -1.123  -8.634  30.874 1.00 52.44  ? 119 GLY C O   1 
ATOM   6066 N  N   . PRO C  1  107 ? 0.019   -10.567 30.731 1.00 51.76  ? 120 PRO C N   1 
ATOM   6067 C  CA  . PRO C  1  107 ? 0.948   -10.234 31.816 1.00 54.22  ? 120 PRO C CA  1 
ATOM   6068 C  C   . PRO C  1  107 ? 1.616   -8.878  31.629 1.00 55.06  ? 120 PRO C C   1 
ATOM   6069 O  O   . PRO C  1  107 ? 2.133   -8.598  30.558 1.00 60.08  ? 120 PRO C O   1 
ATOM   6070 C  CB  . PRO C  1  107 ? 1.984   -11.371 31.781 1.00 54.85  ? 120 PRO C CB  1 
ATOM   6071 C  CG  . PRO C  1  107 ? 1.252   -12.530 31.135 1.00 59.52  ? 120 PRO C CG  1 
ATOM   6072 C  CD  . PRO C  1  107 ? 0.266   -11.901 30.160 1.00 55.74  ? 120 PRO C CD  1 
ATOM   6073 N  N   . PRO C  1  108 ? 1.660   -8.013  32.663 1.00 57.21  ? 121 PRO C N   1 
ATOM   6074 C  CA  . PRO C  1  108 ? 2.288   -6.699  32.537 1.00 57.98  ? 121 PRO C CA  1 
ATOM   6075 C  C   . PRO C  1  108 ? 3.758   -6.774  32.127 1.00 55.85  ? 121 PRO C C   1 
ATOM   6076 O  O   . PRO C  1  108 ? 4.461   -7.729  32.456 1.00 51.45  ? 121 PRO C O   1 
ATOM   6077 C  CB  . PRO C  1  108 ? 2.098   -6.020  33.912 1.00 58.30  ? 121 PRO C CB  1 
ATOM   6078 C  CG  . PRO C  1  108 ? 1.709   -7.149  34.865 1.00 63.80  ? 121 PRO C CG  1 
ATOM   6079 C  CD  . PRO C  1  108 ? 1.107   -8.258  34.005 1.00 63.18  ? 121 PRO C CD  1 
ATOM   6080 N  N   . PRO C  1  109 ? 4.251   -5.784  31.352 1.00 49.54  ? 122 PRO C N   1 
ATOM   6081 C  CA  . PRO C  1  109 ? 5.665   -5.710  31.001 1.00 46.00  ? 122 PRO C CA  1 
ATOM   6082 C  C   . PRO C  1  109 ? 6.481   -5.281  32.214 1.00 46.69  ? 122 PRO C C   1 
ATOM   6083 O  O   . PRO C  1  109 ? 5.922   -4.773  33.179 1.00 48.05  ? 122 PRO C O   1 
ATOM   6084 C  CB  . PRO C  1  109 ? 5.698   -4.652  29.887 1.00 43.49  ? 122 PRO C CB  1 
ATOM   6085 C  CG  . PRO C  1  109 ? 4.545   -3.759  30.207 1.00 44.05  ? 122 PRO C CG  1 
ATOM   6086 C  CD  . PRO C  1  109 ? 3.477   -4.675  30.791 1.00 43.37  ? 122 PRO C CD  1 
ATOM   6087 N  N   . PRO C  1  110 ? 7.822   -5.438  32.185 1.00 46.08  ? 123 PRO C N   1 
ATOM   6088 C  CA  . PRO C  1  110 ? 8.692   -4.860  33.213 1.00 47.98  ? 123 PRO C CA  1 
ATOM   6089 C  C   . PRO C  1  110 ? 8.629   -3.334  33.279 1.00 45.81  ? 123 PRO C C   1 
ATOM   6090 O  O   . PRO C  1  110 ? 8.740   -2.649  32.269 1.00 39.94  ? 123 PRO C O   1 
ATOM   6091 C  CB  . PRO C  1  110 ? 10.100  -5.392  32.854 1.00 48.56  ? 123 PRO C CB  1 
ATOM   6092 C  CG  . PRO C  1  110 ? 9.991   -5.840  31.405 1.00 52.11  ? 123 PRO C CG  1 
ATOM   6093 C  CD  . PRO C  1  110 ? 8.550   -6.239  31.194 1.00 50.02  ? 123 PRO C CD  1 
ATOM   6094 N  N   . PRO C  1  111 ? 8.422   -2.749  34.483 1.00 48.05  ? 124 PRO C N   1 
ATOM   6095 C  CA  . PRO C  1  111 ? 8.408   -1.298  34.642 1.00 44.74  ? 124 PRO C CA  1 
ATOM   6096 C  C   . PRO C  1  111 ? 9.744   -0.729  34.192 1.00 40.24  ? 124 PRO C C   1 
ATOM   6097 O  O   . PRO C  1  111 ? 10.743  -1.430  34.200 1.00 38.87  ? 124 PRO C O   1 
ATOM   6098 C  CB  . PRO C  1  111 ? 8.134   -1.073  36.144 1.00 52.36  ? 124 PRO C CB  1 
ATOM   6099 C  CG  . PRO C  1  111 ? 8.540   -2.382  36.786 1.00 50.36  ? 124 PRO C CG  1 
ATOM   6100 C  CD  . PRO C  1  111 ? 8.156   -3.443  35.757 1.00 51.19  ? 124 PRO C CD  1 
ATOM   6101 N  N   . PRO C  1  112 ? 9.821   0.556   33.785 1.00 35.94  ? 125 PRO C N   1 
ATOM   6102 C  CA  . PRO C  1  112 ? 8.685   1.492   33.815 1.00 40.16  ? 125 PRO C CA  1 
ATOM   6103 C  C   . PRO C  1  112 ? 7.648   1.398   32.683 1.00 41.08  ? 125 PRO C C   1 
ATOM   6104 O  O   . PRO C  1  112 ? 6.712   2.191   32.623 1.00 38.10  ? 125 PRO C O   1 
ATOM   6105 C  CB  . PRO C  1  112 ? 9.382   2.851   33.815 1.00 40.20  ? 125 PRO C CB  1 
ATOM   6106 C  CG  . PRO C  1  112 ? 10.682  2.614   33.098 1.00 41.98  ? 125 PRO C CG  1 
ATOM   6107 C  CD  . PRO C  1  112 ? 11.054  1.165   33.301 1.00 38.52  ? 125 PRO C CD  1 
ATOM   6108 N  N   . ALA C  1  113 ? 7.788   0.388   31.816 1.00 39.09  ? 126 ALA C N   1 
ATOM   6109 C  CA  . ALA C  1  113 ? 6.751   0.084   30.836 1.00 40.81  ? 126 ALA C CA  1 
ATOM   6110 C  C   . ALA C  1  113 ? 5.501   -0.405  31.570 1.00 46.19  ? 126 ALA C C   1 
ATOM   6111 O  O   . ALA C  1  113 ? 5.611   -0.943  32.670 1.00 43.53  ? 126 ALA C O   1 
ATOM   6112 C  CB  . ALA C  1  113 ? 7.255   -0.941  29.851 1.00 35.25  ? 126 ALA C CB  1 
ATOM   6113 N  N   . HIS C  1  114 ? 4.323   -0.223  30.957 1.00 40.38  ? 127 HIS C N   1 
ATOM   6114 C  CA  . HIS C  1  114 ? 3.056   -0.367  31.673 1.00 38.24  ? 127 HIS C CA  1 
ATOM   6115 C  C   . HIS C  1  114 ? 1.975   -1.071  30.851 1.00 41.57  ? 127 HIS C C   1 
ATOM   6116 O  O   . HIS C  1  114 ? 1.165   -1.815  31.412 1.00 37.89  ? 127 HIS C O   1 
ATOM   6117 C  CB  . HIS C  1  114 ? 2.598   0.995   32.193 1.00 40.09  ? 127 HIS C CB  1 
ATOM   6118 C  CG  . HIS C  1  114 ? 2.655   2.074   31.164 1.00 42.43  ? 127 HIS C CG  1 
ATOM   6119 N  ND1 . HIS C  1  114 ? 1.671   2.182   30.208 1.00 36.46  ? 127 HIS C ND1 1 
ATOM   6120 C  CD2 . HIS C  1  114 ? 3.538   3.068   30.924 1.00 42.55  ? 127 HIS C CD2 1 
ATOM   6121 C  CE1 . HIS C  1  114 ? 1.949   3.219   29.435 1.00 36.49  ? 127 HIS C CE1 1 
ATOM   6122 N  NE2 . HIS C  1  114 ? 3.091   3.765   29.831 1.00 38.02  ? 127 HIS C NE2 1 
ATOM   6123 N  N   . ALA C  1  115 ? 1.956   -0.879  29.518 1.00 37.86  ? 128 ALA C N   1 
ATOM   6124 C  CA  . ALA C  1  115 ? 0.870   -1.397  28.692 1.00 33.00  ? 128 ALA C CA  1 
ATOM   6125 C  C   . ALA C  1  115 ? -0.484  -0.981  29.269 1.00 32.83  ? 128 ALA C C   1 
ATOM   6126 O  O   . ALA C  1  115 ? -1.441  -1.753  29.256 1.00 36.46  ? 128 ALA C O   1 
ATOM   6127 C  CB  . ALA C  1  115 ? 0.984   -2.897  28.546 1.00 34.08  ? 128 ALA C CB  1 
ATOM   6128 N  N   . GLY C  1  116 ? -0.551  0.284   29.686 1.00 33.14  ? 129 GLY C N   1 
ATOM   6129 C  CA  . GLY C  1  116 ? -1.693  0.807   30.414 1.00 39.57  ? 129 GLY C CA  1 
ATOM   6130 C  C   . GLY C  1  116 ? -2.797  1.367   29.510 1.00 41.26  ? 129 GLY C C   1 
ATOM   6131 O  O   . GLY C  1  116 ? -3.801  1.875   30.006 1.00 37.86  ? 129 GLY C O   1 
ATOM   6132 N  N   . GLY C  1  117 ? -2.591  1.340   28.185 1.00 36.97  ? 130 GLY C N   1 
ATOM   6133 C  CA  . GLY C  1  117 ? -3.626  1.736   27.248 1.00 34.17  ? 130 GLY C CA  1 
ATOM   6134 C  C   . GLY C  1  117 ? -3.556  3.218   26.886 1.00 31.71  ? 130 GLY C C   1 
ATOM   6135 O  O   . GLY C  1  117 ? -2.763  3.981   27.434 1.00 31.15  ? 130 GLY C O   1 
ATOM   6136 N  N   . LEU C  1  118 ? -4.413  3.612   25.934 1.00 31.25  ? 131 LEU C N   1 
ATOM   6137 C  CA  . LEU C  1  118 ? -4.436  4.972   25.413 1.00 29.91  ? 131 LEU C CA  1 
ATOM   6138 C  C   . LEU C  1  118 ? -4.778  6.018   26.470 1.00 32.42  ? 131 LEU C C   1 
ATOM   6139 O  O   . LEU C  1  118 ? -4.511  7.197   26.241 1.00 33.74  ? 131 LEU C O   1 
ATOM   6140 C  CB  . LEU C  1  118 ? -5.419  5.038   24.240 1.00 31.98  ? 131 LEU C CB  1 
ATOM   6141 C  CG  . LEU C  1  118 ? -5.049  4.204   23.006 1.00 33.19  ? 131 LEU C CG  1 
ATOM   6142 C  CD1 . LEU C  1  118 ? -6.056  4.417   21.884 1.00 34.22  ? 131 LEU C CD1 1 
ATOM   6143 C  CD2 . LEU C  1  118 ? -3.644  4.552   22.502 1.00 32.30  ? 131 LEU C CD2 1 
ATOM   6144 N  N   . ASN C  1  119 ? -5.411  5.610   27.592 1.00 36.46  ? 132 ASN C N   1 
ATOM   6145 C  CA  . ASN C  1  119 ? -5.713  6.528   28.682 1.00 41.60  ? 132 ASN C CA  1 
ATOM   6146 C  C   . ASN C  1  119 ? -4.457  7.132   29.321 1.00 42.89  ? 132 ASN C C   1 
ATOM   6147 O  O   . ASN C  1  119 ? -4.543  8.197   29.928 1.00 44.62  ? 132 ASN C O   1 
ATOM   6148 C  CB  . ASN C  1  119 ? -6.530  5.859   29.787 1.00 43.93  ? 132 ASN C CB  1 
ATOM   6149 C  CG  . ASN C  1  119 ? -7.981  5.650   29.406 1.00 47.88  ? 132 ASN C CG  1 
ATOM   6150 O  OD1 . ASN C  1  119 ? -8.401  5.967   28.288 1.00 43.61  ? 132 ASN C OD1 1 
ATOM   6151 N  ND2 . ASN C  1  119 ? -8.777  5.121   30.321 1.00 46.47  ? 132 ASN C ND2 1 
ATOM   6152 N  N   . VAL C  1  120 ? -3.297  6.478   29.193 1.00 41.02  ? 133 VAL C N   1 
ATOM   6153 C  CA  . VAL C  1  120 ? -2.082  6.960   29.852 1.00 41.32  ? 133 VAL C CA  1 
ATOM   6154 C  C   . VAL C  1  120 ? -1.701  8.357   29.354 1.00 36.73  ? 133 VAL C C   1 
ATOM   6155 O  O   . VAL C  1  120 ? -1.514  8.591   28.165 1.00 40.18  ? 133 VAL C O   1 
ATOM   6156 C  CB  . VAL C  1  120 ? -0.911  5.970   29.694 1.00 39.11  ? 133 VAL C CB  1 
ATOM   6157 C  CG1 . VAL C  1  120 ? 0.397   6.539   30.253 1.00 44.76  ? 133 VAL C CG1 1 
ATOM   6158 C  CG2 . VAL C  1  120 ? -1.239  4.634   30.339 1.00 39.61  ? 133 VAL C CG2 1 
ATOM   6159 N  N   . HIS C  1  121 ? -1.506  9.278   30.303 1.00 39.09  ? 134 HIS C N   1 
ATOM   6160 C  CA  . HIS C  1  121 ? -1.284  10.692  30.029 1.00 38.54  ? 134 HIS C CA  1 
ATOM   6161 C  C   . HIS C  1  121 ? 0.204   11.030  29.908 1.00 42.59  ? 134 HIS C C   1 
ATOM   6162 O  O   . HIS C  1  121 ? 1.030   10.442  30.585 1.00 42.43  ? 134 HIS C O   1 
ATOM   6163 C  CB  . HIS C  1  121 ? -1.882  11.512  31.180 1.00 42.34  ? 134 HIS C CB  1 
ATOM   6164 C  CG  . HIS C  1  121 ? -1.572  12.972  31.132 1.00 42.22  ? 134 HIS C CG  1 
ATOM   6165 N  ND1 . HIS C  1  121 ? -2.166  13.816  30.216 1.00 48.21  ? 134 HIS C ND1 1 
ATOM   6166 C  CD2 . HIS C  1  121 ? -0.728  13.724  31.846 1.00 42.26  ? 134 HIS C CD2 1 
ATOM   6167 C  CE1 . HIS C  1  121 ? -1.701  15.045  30.389 1.00 49.27  ? 134 HIS C CE1 1 
ATOM   6168 N  NE2 . HIS C  1  121 ? -0.825  15.016  31.375 1.00 47.87  ? 134 HIS C NE2 1 
ATOM   6169 N  N   . GLY C  1  122 ? 0.546   12.013  29.069 1.00 47.37  ? 135 GLY C N   1 
ATOM   6170 C  CA  . GLY C  1  122 ? 1.811   12.716  29.208 1.00 48.50  ? 135 GLY C CA  1 
ATOM   6171 C  C   . GLY C  1  122 ? 2.748   12.607  28.003 1.00 51.12  ? 135 GLY C C   1 
ATOM   6172 O  O   . GLY C  1  122 ? 3.516   13.538  27.771 1.00 48.93  ? 135 GLY C O   1 
ATOM   6173 N  N   . THR C  1  123 ? 2.745   11.487  27.263 1.00 47.63  ? 136 THR C N   1 
ATOM   6174 C  CA  A THR C  1  123 ? 3.608   11.344  26.096 0.50 52.46  ? 136 THR C CA  1 
ATOM   6175 C  CA  B THR C  1  123 ? 3.613   11.384  26.093 0.50 51.19  ? 136 THR C CA  1 
ATOM   6176 C  C   . THR C  1  123 ? 2.771   11.231  24.818 1.00 48.78  ? 136 THR C C   1 
ATOM   6177 O  O   . THR C  1  123 ? 3.160   11.773  23.796 1.00 50.78  ? 136 THR C O   1 
ATOM   6178 C  CB  A THR C  1  123 ? 4.542   10.148  26.282 0.50 55.80  ? 136 THR C CB  1 
ATOM   6179 C  CB  B THR C  1  123 ? 4.670   10.290  26.291 0.50 53.50  ? 136 THR C CB  1 
ATOM   6180 O  OG1 A THR C  1  123 ? 3.680   9.039   26.517 0.50 68.92  ? 136 THR C OG1 1 
ATOM   6181 O  OG1 B THR C  1  123 ? 5.563   10.224  25.179 0.50 50.67  ? 136 THR C OG1 1 
ATOM   6182 C  CG2 A THR C  1  123 ? 5.507   10.353  27.435 0.50 53.87  ? 136 THR C CG2 1 
ATOM   6183 C  CG2 B THR C  1  123 ? 4.065   8.913   26.461 0.50 59.24  ? 136 THR C CG2 1 
ATOM   6184 N  N   . PHE C  1  124 ? 1.625   10.522  24.865 1.00 46.95  ? 137 PHE C N   1 
ATOM   6185 C  CA  . PHE C  1  124 ? 0.664   10.520  23.754 1.00 42.63  ? 137 PHE C CA  1 
ATOM   6186 C  C   . PHE C  1  124 ? -0.584  11.337  24.140 1.00 42.74  ? 137 PHE C C   1 
ATOM   6187 O  O   . PHE C  1  124 ? -0.656  12.517  23.798 1.00 44.40  ? 137 PHE C O   1 
ATOM   6188 C  CB  . PHE C  1  124 ? 0.376   9.096   23.268 1.00 40.18  ? 137 PHE C CB  1 
ATOM   6189 C  CG  . PHE C  1  124 ? -0.425  8.945   21.972 1.00 40.49  ? 137 PHE C CG  1 
ATOM   6190 C  CD1 . PHE C  1  124 ? -0.831  10.039  21.211 1.00 44.60  ? 137 PHE C CD1 1 
ATOM   6191 C  CD2 . PHE C  1  124 ? -0.742  7.683   21.491 1.00 42.84  ? 137 PHE C CD2 1 
ATOM   6192 C  CE1 . PHE C  1  124 ? -1.546  9.870   20.027 1.00 45.02  ? 137 PHE C CE1 1 
ATOM   6193 C  CE2 . PHE C  1  124 ? -1.435  7.516   20.294 1.00 40.38  ? 137 PHE C CE2 1 
ATOM   6194 C  CZ  . PHE C  1  124 ? -1.846  8.611   19.573 1.00 40.43  ? 137 PHE C CZ  1 
ATOM   6195 N  N   . GLU C  1  125 ? -1.563  10.736  24.844 1.00 44.23  ? 138 GLU C N   1 
ATOM   6196 C  CA  . GLU C  1  125 ? -2.733  11.474  25.329 1.00 43.79  ? 138 GLU C CA  1 
ATOM   6197 C  C   . GLU C  1  125 ? -2.283  12.772  26.010 1.00 43.69  ? 138 GLU C C   1 
ATOM   6198 O  O   . GLU C  1  125 ? -1.307  12.786  26.759 1.00 41.98  ? 138 GLU C O   1 
ATOM   6199 C  CB  . GLU C  1  125 ? -3.578  10.616  26.274 1.00 45.63  ? 138 GLU C CB  1 
ATOM   6200 C  CG  . GLU C  1  125 ? -4.907  11.229  26.717 1.00 48.37  ? 138 GLU C CG  1 
ATOM   6201 C  CD  . GLU C  1  125 ? -4.821  12.403  27.684 1.00 50.80  ? 138 GLU C CD  1 
ATOM   6202 O  OE1 . GLU C  1  125 ? -3.972  12.308  28.600 1.00 48.74  ? 138 GLU C OE1 1 
ATOM   6203 O  OE2 . GLU C  1  125 ? -5.582  13.399  27.518 1.00 43.15  ? 138 GLU C OE2 1 
ATOM   6204 N  N   . GLY C  1  126 ? -2.996  13.872  25.740 1.00 44.33  ? 139 GLY C N   1 
ATOM   6205 C  CA  . GLY C  1  126 ? -2.682  15.147  26.352 1.00 43.48  ? 139 GLY C CA  1 
ATOM   6206 C  C   . GLY C  1  126 ? -3.865  16.115  26.383 1.00 46.16  ? 139 GLY C C   1 
ATOM   6207 O  O   . GLY C  1  126 ? -5.042  15.752  26.209 1.00 42.86  ? 139 GLY C O   1 
ATOM   6208 N  N   . ASP C  1  127 ? -3.499  17.386  26.564 1.00 44.40  ? 140 ASP C N   1 
ATOM   6209 C  CA  . ASP C  1  127 ? -4.404  18.397  27.081 1.00 49.81  ? 140 ASP C CA  1 
ATOM   6210 C  C   . ASP C  1  127 ? -5.087  19.149  25.943 1.00 51.72  ? 140 ASP C C   1 
ATOM   6211 O  O   . ASP C  1  127 ? -4.678  19.071  24.783 1.00 46.16  ? 140 ASP C O   1 
ATOM   6212 C  CB  . ASP C  1  127 ? -3.644  19.351  27.994 1.00 48.18  ? 140 ASP C CB  1 
ATOM   6213 C  CG  . ASP C  1  127 ? -3.003  18.733  29.229 1.00 46.47  ? 140 ASP C CG  1 
ATOM   6214 O  OD1 . ASP C  1  127 ? -3.590  17.775  29.786 1.00 46.73  ? 140 ASP C OD1 1 
ATOM   6215 O  OD2 . ASP C  1  127 ? -1.920  19.220  29.635 1.00 51.07  ? 140 ASP C OD2 1 
ATOM   6216 N  N   . ALA C  1  128 ? -6.120  19.915  26.317 1.00 47.88  ? 141 ALA C N   1 
ATOM   6217 C  CA  . ALA C  1  128 ? -6.833  20.811  25.419 1.00 47.45  ? 141 ALA C CA  1 
ATOM   6218 C  C   . ALA C  1  128 ? -7.584  20.030  24.334 1.00 44.55  ? 141 ALA C C   1 
ATOM   6219 O  O   . ALA C  1  128 ? -7.684  20.462  23.196 1.00 48.36  ? 141 ALA C O   1 
ATOM   6220 C  CB  . ALA C  1  128 ? -5.876  21.848  24.853 1.00 44.36  ? 141 ALA C CB  1 
ATOM   6221 N  N   . GLY C  1  129 ? -8.172  18.900  24.703 1.00 50.26  ? 142 GLY C N   1 
ATOM   6222 C  CA  . GLY C  1  129 ? -9.057  18.178  23.802 1.00 54.35  ? 142 GLY C CA  1 
ATOM   6223 C  C   . GLY C  1  129 ? -10.396 18.899  23.641 1.00 59.54  ? 142 GLY C C   1 
ATOM   6224 O  O   . GLY C  1  129 ? -10.703 19.817  24.394 1.00 54.14  ? 142 GLY C O   1 
ATOM   6225 N  N   . MET C  1  130 ? -11.196 18.443  22.669 1.00 55.05  ? 143 MET C N   1 
ATOM   6226 C  CA  . MET C  1  130 ? -12.452 19.083  22.319 1.00 52.83  ? 143 MET C CA  1 
ATOM   6227 C  C   . MET C  1  130 ? -13.579 18.616  23.237 1.00 52.57  ? 143 MET C C   1 
ATOM   6228 O  O   . MET C  1  130 ? -14.384 19.428  23.682 1.00 54.50  ? 143 MET C O   1 
ATOM   6229 C  CB  . MET C  1  130 ? -12.839 18.763  20.869 1.00 53.82  ? 143 MET C CB  1 
ATOM   6230 C  CG  . MET C  1  130 ? -12.001 19.485  19.819 1.00 54.58  ? 143 MET C CG  1 
ATOM   6231 S  SD  . MET C  1  130 ? -12.336 18.890  18.142 1.00 58.13  ? 143 MET C SD  1 
ATOM   6232 C  CE  . MET C  1  130 ? -11.737 17.202  18.255 1.00 45.01  ? 143 MET C CE  1 
ATOM   6233 N  N   . THR C  1  131 ? -13.674 17.300  23.478 1.00 49.18  ? 144 THR C N   1 
ATOM   6234 C  CA  . THR C  1  131 ? -14.775 16.742  24.248 1.00 50.40  ? 144 THR C CA  1 
ATOM   6235 C  C   . THR C  1  131 ? -14.289 15.994  25.489 1.00 44.66  ? 144 THR C C   1 
ATOM   6236 O  O   . THR C  1  131 ? -15.118 15.419  26.202 1.00 48.36  ? 144 THR C O   1 
ATOM   6237 C  CB  . THR C  1  131 ? -15.633 15.826  23.374 1.00 50.94  ? 144 THR C CB  1 
ATOM   6238 O  OG1 . THR C  1  131 ? -14.911 14.618  23.124 1.00 45.32  ? 144 THR C OG1 1 
ATOM   6239 C  CG2 . THR C  1  131 ? -16.060 16.521  22.092 1.00 55.39  ? 144 THR C CG2 1 
ATOM   6240 N  N   . ARG C  1  132 ? -12.968 15.980  25.717 1.00 45.55  ? 145 ARG C N   1 
ATOM   6241 C  CA  . ARG C  1  132 ? -12.377 15.361  26.895 1.00 47.34  ? 145 ARG C CA  1 
ATOM   6242 C  C   . ARG C  1  132 ? -11.632 16.429  27.699 1.00 47.45  ? 145 ARG C C   1 
ATOM   6243 O  O   . ARG C  1  132 ? -10.972 17.272  27.107 1.00 42.94  ? 145 ARG C O   1 
ATOM   6244 C  CB  . ARG C  1  132 ? -11.411 14.232  26.517 1.00 44.17  ? 145 ARG C CB  1 
ATOM   6245 C  CG  . ARG C  1  132 ? -12.062 12.854  26.452 1.00 50.36  ? 145 ARG C CG  1 
ATOM   6246 C  CD  . ARG C  1  132 ? -12.996 12.695  25.251 1.00 46.05  ? 145 ARG C CD  1 
ATOM   6247 N  NE  . ARG C  1  132 ? -13.678 11.400  25.334 1.00 46.43  ? 145 ARG C NE  1 
ATOM   6248 C  CZ  . ARG C  1  132 ? -14.740 11.031  24.626 1.00 44.59  ? 145 ARG C CZ  1 
ATOM   6249 N  NH1 . ARG C  1  132 ? -15.320 11.881  23.793 1.00 42.98  ? 145 ARG C NH1 1 
ATOM   6250 N  NH2 . ARG C  1  132 ? -15.217 9.813   24.781 1.00 46.70  ? 145 ARG C NH2 1 
ATOM   6251 N  N   . ALA C  1  133 ? -11.706 16.339  29.039 1.00 44.94  ? 146 ALA C N   1 
ATOM   6252 C  CA  . ALA C  1  133 ? -11.031 17.279  29.925 1.00 51.14  ? 146 ALA C CA  1 
ATOM   6253 C  C   . ALA C  1  133 ? -9.583  16.853  30.177 1.00 48.19  ? 146 ALA C C   1 
ATOM   6254 O  O   . ALA C  1  133 ? -9.268  15.670  30.114 1.00 44.61  ? 146 ALA C O   1 
ATOM   6255 N  N   . ASP C  1  134 ? -8.719  17.834  30.488 1.00 51.04  ? 147 ASP C N   1 
ATOM   6256 C  CA  . ASP C  1  134 ? -7.325  17.591  30.831 1.00 53.34  ? 147 ASP C CA  1 
ATOM   6257 C  C   . ASP C  1  134 ? -7.237  16.648  32.024 1.00 54.39  ? 147 ASP C C   1 
ATOM   6258 O  O   . ASP C  1  134 ? -8.075  16.695  32.927 1.00 50.60  ? 147 ASP C O   1 
ATOM   6259 C  CB  . ASP C  1  134 ? -6.575  18.869  31.165 1.00 48.02  ? 147 ASP C CB  1 
ATOM   6260 C  CG  . ASP C  1  134 ? -6.470  19.873  30.034 1.00 53.86  ? 147 ASP C CG  1 
ATOM   6261 O  OD1 . ASP C  1  134 ? -7.082  19.611  28.966 1.00 53.46  ? 147 ASP C OD1 1 
ATOM   6262 O  OD2 . ASP C  1  134 ? -5.773  20.902  30.232 1.00 50.52  ? 147 ASP C OD2 1 
ATOM   6263 N  N   . GLU C  1  135 ? -6.199  15.803  31.999 1.00 47.27  ? 148 GLU C N   1 
ATOM   6264 C  CA  . GLU C  1  135 ? -5.976  14.783  33.008 1.00 48.18  ? 148 GLU C CA  1 
ATOM   6265 C  C   . GLU C  1  135 ? -5.889  15.396  34.410 1.00 47.36  ? 148 GLU C C   1 
ATOM   6266 O  O   . GLU C  1  135 ? -6.271  14.751  35.377 1.00 44.21  ? 148 GLU C O   1 
ATOM   6267 C  CB  . GLU C  1  135 ? -4.678  14.032  32.702 1.00 46.56  ? 148 GLU C CB  1 
ATOM   6268 C  CG  . GLU C  1  135 ? -4.493  12.806  33.592 1.00 51.16  ? 148 GLU C CG  1 
ATOM   6269 C  CD  . GLU C  1  135 ? -3.660  13.025  34.848 1.00 58.38  ? 148 GLU C CD  1 
ATOM   6270 O  OE1 . GLU C  1  135 ? -3.183  14.155  35.114 1.00 59.07  ? 148 GLU C OE1 1 
ATOM   6271 O  OE2 . GLU C  1  135 ? -3.481  12.015  35.560 1.00 67.42  ? 148 GLU C OE2 1 
ATOM   6272 N  N   . PHE C  1  136 ? -5.377  16.626  34.509 1.00 49.38  ? 149 PHE C N   1 
ATOM   6273 C  CA  . PHE C  1  136 ? -5.229  17.311  35.782 1.00 59.97  ? 149 PHE C CA  1 
ATOM   6274 C  C   . PHE C  1  136 ? -6.559  17.353  36.536 1.00 56.88  ? 149 PHE C C   1 
ATOM   6275 O  O   . PHE C  1  136 ? -6.557  17.207  37.751 1.00 57.52  ? 149 PHE C O   1 
ATOM   6276 C  CB  . PHE C  1  136 ? -4.685  18.731  35.606 1.00 65.31  ? 149 PHE C CB  1 
ATOM   6277 C  CG  . PHE C  1  136 ? -4.559  19.475  36.929 1.00 73.87  ? 149 PHE C CG  1 
ATOM   6278 C  CD1 . PHE C  1  136 ? -3.569  19.134  37.851 1.00 79.62  ? 149 PHE C CD1 1 
ATOM   6279 C  CD2 . PHE C  1  136 ? -5.434  20.507  37.254 1.00 75.22  ? 149 PHE C CD2 1 
ATOM   6280 C  CE1 . PHE C  1  136 ? -3.470  19.806  39.067 1.00 81.17  ? 149 PHE C CE1 1 
ATOM   6281 C  CE2 . PHE C  1  136 ? -5.319  21.181  38.465 1.00 81.42  ? 149 PHE C CE2 1 
ATOM   6282 C  CZ  . PHE C  1  136 ? -4.324  20.843  39.357 1.00 79.85  ? 149 PHE C CZ  1 
ATOM   6283 N  N   . PHE C  1  137 ? -7.683  17.504  35.823 1.00 51.23  ? 150 PHE C N   1 
ATOM   6284 C  CA  . PHE C  1  137 ? -8.976  17.667  36.469 1.00 48.42  ? 150 PHE C CA  1 
ATOM   6285 C  C   . PHE C  1  137 ? -9.608  16.320  36.827 1.00 52.11  ? 150 PHE C C   1 
ATOM   6286 O  O   . PHE C  1  137 ? -10.727 16.299  37.340 1.00 57.67  ? 150 PHE C O   1 
ATOM   6287 C  CB  . PHE C  1  137 ? -9.915  18.479  35.575 1.00 49.40  ? 150 PHE C CB  1 
ATOM   6288 C  CG  . PHE C  1  137 ? -9.339  19.813  35.125 1.00 52.23  ? 150 PHE C CG  1 
ATOM   6289 C  CD1 . PHE C  1  137 ? -8.836  20.732  36.037 1.00 58.38  ? 150 PHE C CD1 1 
ATOM   6290 C  CD2 . PHE C  1  137 ? -9.279  20.126  33.775 1.00 55.79  ? 150 PHE C CD2 1 
ATOM   6291 C  CE1 . PHE C  1  137 ? -8.286  21.923  35.607 1.00 57.66  ? 150 PHE C CE1 1 
ATOM   6292 C  CE2 . PHE C  1  137 ? -8.760  21.338  33.350 1.00 55.77  ? 150 PHE C CE2 1 
ATOM   6293 C  CZ  . PHE C  1  137 ? -8.264  22.231  34.270 1.00 61.55  ? 150 PHE C CZ  1 
ATOM   6294 N  N   . GLY C  1  138 ? -8.949  15.195  36.519 1.00 50.73  ? 151 GLY C N   1 
ATOM   6295 C  CA  . GLY C  1  138 ? -9.323  13.921  37.113 1.00 48.15  ? 151 GLY C CA  1 
ATOM   6296 C  C   . GLY C  1  138 ? -9.803  12.855  36.127 1.00 53.64  ? 151 GLY C C   1 
ATOM   6297 O  O   . GLY C  1  138 ? -9.809  11.675  36.483 1.00 51.63  ? 151 GLY C O   1 
ATOM   6298 N  N   . ASP C  1  139 ? -10.208 13.233  34.903 1.00 55.10  ? 152 ASP C N   1 
ATOM   6299 C  CA  . ASP C  1  139 ? -10.755 12.250  33.971 1.00 57.33  ? 152 ASP C CA  1 
ATOM   6300 C  C   . ASP C  1  139 ? -10.466 12.664  32.530 1.00 55.68  ? 152 ASP C C   1 
ATOM   6301 O  O   . ASP C  1  139 ? -11.126 13.555  31.999 1.00 54.15  ? 152 ASP C O   1 
ATOM   6302 C  CB  . ASP C  1  139 ? -12.238 12.011  34.198 1.00 59.78  ? 152 ASP C CB  1 
ATOM   6303 C  CG  . ASP C  1  139 ? -12.910 11.032  33.238 1.00 66.99  ? 152 ASP C CG  1 
ATOM   6304 O  OD1 . ASP C  1  139 ? -12.262 10.607  32.251 1.00 66.27  ? 152 ASP C OD1 1 
ATOM   6305 O  OD2 . ASP C  1  139 ? -14.085 10.713  33.479 1.00 70.53  ? 152 ASP C OD2 1 
ATOM   6306 N  N   . ASN C  1  140 ? -9.491  11.981  31.908 1.00 50.78  ? 153 ASN C N   1 
ATOM   6307 C  CA  . ASN C  1  140 ? -8.994  12.394  30.604 1.00 47.65  ? 153 ASN C CA  1 
ATOM   6308 C  C   . ASN C  1  140 ? -9.656  11.600  29.481 1.00 45.82  ? 153 ASN C C   1 
ATOM   6309 O  O   . ASN C  1  140 ? -9.275  11.779  28.326 1.00 47.78  ? 153 ASN C O   1 
ATOM   6310 C  CB  . ASN C  1  140 ? -7.474  12.270  30.496 1.00 45.83  ? 153 ASN C CB  1 
ATOM   6311 C  CG  . ASN C  1  140 ? -6.980  10.845  30.564 1.00 43.06  ? 153 ASN C CG  1 
ATOM   6312 O  OD1 . ASN C  1  140 ? -7.741  9.921   30.870 1.00 48.77  ? 153 ASN C OD1 1 
ATOM   6313 N  ND2 . ASN C  1  140 ? -5.692  10.643  30.321 1.00 47.88  ? 153 ASN C ND2 1 
ATOM   6314 N  N   . HIS C  1  141 ? -10.627 10.729  29.806 1.00 44.80  ? 154 HIS C N   1 
ATOM   6315 C  CA  . HIS C  1  141 ? -11.106 9.747   28.845 1.00 52.95  ? 154 HIS C CA  1 
ATOM   6316 C  C   . HIS C  1  141 ? -12.606 9.868   28.572 1.00 56.55  ? 154 HIS C C   1 
ATOM   6317 O  O   . HIS C  1  141 ? -13.040 9.612   27.443 1.00 53.49  ? 154 HIS C O   1 
ATOM   6318 C  CB  . HIS C  1  141 ? -10.649 8.339   29.249 1.00 56.33  ? 154 HIS C CB  1 
ATOM   6319 C  CG  . HIS C  1  141 ? -11.053 7.941   30.617 1.00 60.56  ? 154 HIS C CG  1 
ATOM   6320 N  ND1 . HIS C  1  141 ? -12.273 7.343   30.845 1.00 66.94  ? 154 HIS C ND1 1 
ATOM   6321 C  CD2 . HIS C  1  141 ? -10.447 8.052   31.803 1.00 60.92  ? 154 HIS C CD2 1 
ATOM   6322 C  CE1 . HIS C  1  141 ? -12.392 7.096   32.141 1.00 67.95  ? 154 HIS C CE1 1 
ATOM   6323 N  NE2 . HIS C  1  141 ? -11.294 7.511   32.737 1.00 64.48  ? 154 HIS C NE2 1 
ATOM   6324 N  N   . SER C  1  142 ? -13.394 10.223  29.596 1.00 53.04  ? 155 SER C N   1 
ATOM   6325 C  CA  . SER C  1  142 ? -14.836 10.282  29.450 1.00 51.61  ? 155 SER C CA  1 
ATOM   6326 C  C   . SER C  1  142 ? -15.236 11.494  28.623 1.00 45.04  ? 155 SER C C   1 
ATOM   6327 O  O   . SER C  1  142 ? -14.624 12.559  28.697 1.00 43.70  ? 155 SER C O   1 
ATOM   6328 C  CB  . SER C  1  142 ? -15.530 10.333  30.788 1.00 56.20  ? 155 SER C CB  1 
ATOM   6329 O  OG  . SER C  1  142 ? -15.223 9.179   31.556 1.00 55.18  ? 155 SER C OG  1 
ATOM   6330 N  N   . PHE C  1  143 ? -16.324 11.320  27.872 1.00 48.23  ? 156 PHE C N   1 
ATOM   6331 C  CA  . PHE C  1  143 ? -17.003 12.447  27.262 1.00 51.91  ? 156 PHE C CA  1 
ATOM   6332 C  C   . PHE C  1  143 ? -17.417 13.437  28.348 1.00 52.17  ? 156 PHE C C   1 
ATOM   6333 O  O   . PHE C  1  143 ? -17.892 13.031  29.407 1.00 52.51  ? 156 PHE C O   1 
ATOM   6334 C  CB  . PHE C  1  143 ? -18.215 11.919  26.498 1.00 51.33  ? 156 PHE C CB  1 
ATOM   6335 C  CG  . PHE C  1  143 ? -19.088 13.018  25.918 1.00 54.14  ? 156 PHE C CG  1 
ATOM   6336 C  CD1 . PHE C  1  143 ? -18.825 13.557  24.665 1.00 50.47  ? 156 PHE C CD1 1 
ATOM   6337 C  CD2 . PHE C  1  143 ? -20.195 13.486  26.633 1.00 57.18  ? 156 PHE C CD2 1 
ATOM   6338 C  CE1 . PHE C  1  143 ? -19.667 14.522  24.137 1.00 55.54  ? 156 PHE C CE1 1 
ATOM   6339 C  CE2 . PHE C  1  143 ? -21.020 14.459  26.103 1.00 56.41  ? 156 PHE C CE2 1 
ATOM   6340 C  CZ  . PHE C  1  143 ? -20.759 14.965  24.858 1.00 54.91  ? 156 PHE C CZ  1 
ATOM   6341 N  N   . ASN C  1  144 ? -17.241 14.726  28.059 1.00 50.17  ? 157 ASN C N   1 
ATOM   6342 C  CA  . ASN C  1  144 ? -17.532 15.772  29.012 1.00 53.38  ? 157 ASN C CA  1 
ATOM   6343 C  C   . ASN C  1  144 ? -18.545 16.730  28.394 1.00 57.55  ? 157 ASN C C   1 
ATOM   6344 O  O   . ASN C  1  144 ? -18.211 17.439  27.455 1.00 50.10  ? 157 ASN C O   1 
ATOM   6345 C  CB  . ASN C  1  144 ? -16.260 16.489  29.423 1.00 63.45  ? 157 ASN C CB  1 
ATOM   6346 C  CG  . ASN C  1  144 ? -16.485 17.426  30.585 1.00 72.47  ? 157 ASN C CG  1 
ATOM   6347 O  OD1 . ASN C  1  144 ? -17.558 17.472  31.195 1.00 91.68  ? 157 ASN C OD1 1 
ATOM   6348 N  ND2 . ASN C  1  144 ? -15.439 18.142  30.949 1.00 84.02  ? 157 ASN C ND2 1 
ATOM   6349 N  N   . GLN C  1  145 ? -19.768 16.752  28.945 1.00 61.32  ? 158 GLN C N   1 
ATOM   6350 C  CA  . GLN C  1  145 ? -20.889 17.494  28.388 1.00 63.05  ? 158 GLN C CA  1 
ATOM   6351 C  C   . GLN C  1  145 ? -20.609 18.998  28.364 1.00 54.88  ? 158 GLN C C   1 
ATOM   6352 O  O   . GLN C  1  145 ? -21.019 19.669  27.418 1.00 63.30  ? 158 GLN C O   1 
ATOM   6353 C  CB  . GLN C  1  145 ? -22.169 17.190  29.176 1.00 65.95  ? 158 GLN C CB  1 
ATOM   6354 C  CG  . GLN C  1  145 ? -23.438 17.853  28.633 1.00 62.04  ? 158 GLN C CG  1 
ATOM   6355 C  CD  . GLN C  1  145 ? -23.815 17.409  27.236 1.00 59.68  ? 158 GLN C CD  1 
ATOM   6356 O  OE1 . GLN C  1  145 ? -23.920 16.214  26.946 1.00 61.88  ? 158 GLN C OE1 1 
ATOM   6357 N  NE2 . GLN C  1  145 ? -24.048 18.359  26.342 1.00 61.08  ? 158 GLN C NE2 1 
ATOM   6358 N  N   . THR C  1  146 ? -19.922 19.522  29.388 1.00 58.46  ? 159 THR C N   1 
ATOM   6359 C  CA  . THR C  1  146 ? -19.596 20.943  29.445 1.00 58.90  ? 159 THR C CA  1 
ATOM   6360 C  C   . THR C  1  146 ? -18.762 21.326  28.226 1.00 57.35  ? 159 THR C C   1 
ATOM   6361 O  O   . THR C  1  146 ? -18.998 22.353  27.593 1.00 56.59  ? 159 THR C O   1 
ATOM   6362 C  CB  . THR C  1  146 ? -18.844 21.298  30.730 1.00 63.32  ? 159 THR C CB  1 
ATOM   6363 O  OG1 . THR C  1  146 ? -19.584 20.779  31.833 1.00 67.41  ? 159 THR C OG1 1 
ATOM   6364 C  CG2 . THR C  1  146 ? -18.650 22.799  30.880 1.00 59.48  ? 159 THR C CG2 1 
ATOM   6365 N  N   . LEU C  1  147 ? -17.761 20.495  27.909 1.00 61.20  ? 160 LEU C N   1 
ATOM   6366 C  CA  . LEU C  1  147 ? -16.905 20.772  26.769 1.00 57.98  ? 160 LEU C CA  1 
ATOM   6367 C  C   . LEU C  1  147 ? -17.675 20.606  25.460 1.00 48.74  ? 160 LEU C C   1 
ATOM   6368 O  O   . LEU C  1  147 ? -17.458 21.350  24.510 1.00 47.60  ? 160 LEU C O   1 
ATOM   6369 C  CB  . LEU C  1  147 ? -15.673 19.875  26.842 1.00 58.80  ? 160 LEU C CB  1 
ATOM   6370 C  CG  . LEU C  1  147 ? -14.653 20.279  27.912 1.00 60.06  ? 160 LEU C CG  1 
ATOM   6371 C  CD1 . LEU C  1  147 ? -13.491 19.289  27.930 1.00 57.91  ? 160 LEU C CD1 1 
ATOM   6372 C  CD2 . LEU C  1  147 ? -14.154 21.698  27.678 1.00 53.52  ? 160 LEU C CD2 1 
ATOM   6373 N  N   . PHE C  1  148 ? -18.580 19.633  25.408 1.00 51.67  ? 161 PHE C N   1 
ATOM   6374 C  CA  . PHE C  1  148 ? -19.390 19.449  24.217 1.00 55.47  ? 161 PHE C CA  1 
ATOM   6375 C  C   . PHE C  1  148 ? -20.299 20.663  24.024 1.00 61.60  ? 161 PHE C C   1 
ATOM   6376 O  O   . PHE C  1  148 ? -20.537 21.060  22.886 1.00 57.03  ? 161 PHE C O   1 
ATOM   6377 C  CB  . PHE C  1  148 ? -20.185 18.143  24.243 1.00 58.85  ? 161 PHE C CB  1 
ATOM   6378 C  CG  . PHE C  1  148 ? -20.920 17.917  22.931 1.00 67.26  ? 161 PHE C CG  1 
ATOM   6379 C  CD1 . PHE C  1  148 ? -20.222 17.541  21.785 1.00 70.27  ? 161 PHE C CD1 1 
ATOM   6380 C  CD2 . PHE C  1  148 ? -22.291 18.132  22.833 1.00 65.57  ? 161 PHE C CD2 1 
ATOM   6381 C  CE1 . PHE C  1  148 ? -20.883 17.347  20.587 1.00 72.93  ? 161 PHE C CE1 1 
ATOM   6382 C  CE2 . PHE C  1  148 ? -22.947 17.923  21.627 1.00 66.06  ? 161 PHE C CE2 1 
ATOM   6383 C  CZ  . PHE C  1  148 ? -22.241 17.533  20.506 1.00 70.30  ? 161 PHE C CZ  1 
ATOM   6384 N  N   . ASP C  1  149 ? -20.780 21.262  25.127 1.00 63.91  ? 162 ASP C N   1 
ATOM   6385 C  CA  . ASP C  1  149 ? -21.590 22.476  25.054 1.00 59.89  ? 162 ASP C CA  1 
ATOM   6386 C  C   . ASP C  1  149 ? -20.802 23.613  24.409 1.00 50.60  ? 162 ASP C C   1 
ATOM   6387 O  O   . ASP C  1  149 ? -21.368 24.401  23.660 1.00 55.67  ? 162 ASP C O   1 
ATOM   6388 C  CB  . ASP C  1  149 ? -22.129 22.891  26.419 1.00 61.65  ? 162 ASP C CB  1 
ATOM   6389 C  CG  . ASP C  1  149 ? -23.170 21.964  27.031 1.00 68.02  ? 162 ASP C CG  1 
ATOM   6390 O  OD1 . ASP C  1  149 ? -23.813 21.216  26.263 1.00 64.59  ? 162 ASP C OD1 1 
ATOM   6391 O  OD2 . ASP C  1  149 ? -23.312 21.970  28.275 1.00 74.46  ? 162 ASP C OD2 1 
ATOM   6392 N  N   . LYS C  1  150 ? -19.500 23.702  24.703 1.00 55.41  ? 163 LYS C N   1 
ATOM   6393 C  CA  . LYS C  1  150 ? -18.632 24.706  24.089 1.00 58.29  ? 163 LYS C CA  1 
ATOM   6394 C  C   . LYS C  1  150 ? -18.455 24.420  22.594 1.00 61.80  ? 163 LYS C C   1 
ATOM   6395 O  O   . LYS C  1  150 ? -18.461 25.337  21.777 1.00 59.40  ? 163 LYS C O   1 
ATOM   6396 C  CB  . LYS C  1  150 ? -17.284 24.740  24.817 1.00 58.46  ? 163 LYS C CB  1 
ATOM   6397 C  CG  . LYS C  1  150 ? -16.304 25.803  24.343 1.00 58.49  ? 163 LYS C CG  1 
ATOM   6398 C  CD  . LYS C  1  150 ? -15.053 25.871  25.220 1.00 59.36  ? 163 LYS C CD  1 
ATOM   6399 C  CE  . LYS C  1  150 ? -13.941 26.705  24.669 1.00 61.44  ? 163 LYS C CE  1 
ATOM   6400 N  NZ  . LYS C  1  150 ? -13.896 28.099  25.104 1.00 67.43  ? 163 LYS C NZ  1 
ATOM   6401 N  N   . PHE C  1  151 ? -18.309 23.140  22.236 1.00 62.96  ? 164 PHE C N   1 
ATOM   6402 C  CA  . PHE C  1  151 ? -18.225 22.723  20.844 1.00 64.29  ? 164 PHE C CA  1 
ATOM   6403 C  C   . PHE C  1  151 ? -19.459 23.210  20.082 1.00 62.07  ? 164 PHE C C   1 
ATOM   6404 O  O   . PHE C  1  151 ? -19.344 23.753  18.980 1.00 57.44  ? 164 PHE C O   1 
ATOM   6405 C  CB  . PHE C  1  151 ? -18.080 21.194  20.843 1.00 63.24  ? 164 PHE C CB  1 
ATOM   6406 C  CG  . PHE C  1  151 ? -17.955 20.526  19.482 1.00 65.15  ? 164 PHE C CG  1 
ATOM   6407 C  CD1 . PHE C  1  151 ? -16.709 20.373  18.887 1.00 64.11  ? 164 PHE C CD1 1 
ATOM   6408 C  CD2 . PHE C  1  151 ? -19.074 20.020  18.821 1.00 65.55  ? 164 PHE C CD2 1 
ATOM   6409 C  CE1 . PHE C  1  151 ? -16.591 19.769  17.647 1.00 67.42  ? 164 PHE C CE1 1 
ATOM   6410 C  CE2 . PHE C  1  151 ? -18.950 19.418  17.579 1.00 65.99  ? 164 PHE C CE2 1 
ATOM   6411 C  CZ  . PHE C  1  151 ? -17.711 19.297  16.993 1.00 65.28  ? 164 PHE C CZ  1 
ATOM   6412 N  N   . VAL C  1  152 ? -20.642 22.992  20.677 1.00 60.31  ? 165 VAL C N   1 
ATOM   6413 C  CA  . VAL C  1  152 ? -21.901 23.432  20.089 1.00 60.61  ? 165 VAL C CA  1 
ATOM   6414 C  C   . VAL C  1  152 ? -21.915 24.955  19.994 1.00 58.63  ? 165 VAL C C   1 
ATOM   6415 O  O   . VAL C  1  152 ? -22.297 25.506  18.964 1.00 57.92  ? 165 VAL C O   1 
ATOM   6416 C  CB  . VAL C  1  152 ? -23.117 22.918  20.883 1.00 68.22  ? 165 VAL C CB  1 
ATOM   6417 C  CG1 . VAL C  1  152 ? -24.427 23.560  20.438 1.00 66.99  ? 165 VAL C CG1 1 
ATOM   6418 C  CG2 . VAL C  1  152 ? -23.241 21.402  20.801 1.00 72.91  ? 165 VAL C CG2 1 
ATOM   6419 N  N   . ASP C  1  153 ? -21.517 25.623  21.081 1.00 64.16  ? 166 ASP C N   1 
ATOM   6420 C  CA  . ASP C  1  153 ? -21.515 27.075  21.108 1.00 71.06  ? 166 ASP C CA  1 
ATOM   6421 C  C   . ASP C  1  153 ? -20.632 27.632  19.994 1.00 63.53  ? 166 ASP C C   1 
ATOM   6422 O  O   . ASP C  1  153 ? -21.056 28.511  19.248 1.00 68.40  ? 166 ASP C O   1 
ATOM   6423 C  CB  . ASP C  1  153 ? -21.138 27.607  22.484 1.00 77.29  ? 166 ASP C CB  1 
ATOM   6424 C  CG  . ASP C  1  153 ? -21.342 29.107  22.646 1.00 82.16  ? 166 ASP C CG  1 
ATOM   6425 O  OD1 . ASP C  1  153 ? -22.452 29.593  22.327 1.00 82.02  ? 166 ASP C OD1 1 
ATOM   6426 O  OD2 . ASP C  1  153 ? -20.390 29.782  23.084 1.00 87.48  ? 166 ASP C OD2 1 
ATOM   6427 N  N   . PHE C  1  154 ? -19.407 27.111  19.861 1.00 63.78  ? 167 PHE C N   1 
ATOM   6428 C  CA  . PHE C  1  154 ? -18.495 27.587  18.829 1.00 60.28  ? 167 PHE C CA  1 
ATOM   6429 C  C   . PHE C  1  154 ? -19.032 27.252  17.437 1.00 57.10  ? 167 PHE C C   1 
ATOM   6430 O  O   . PHE C  1  154 ? -18.829 28.025  16.509 1.00 51.12  ? 167 PHE C O   1 
ATOM   6431 C  CB  . PHE C  1  154 ? -17.082 27.040  19.037 1.00 60.75  ? 167 PHE C CB  1 
ATOM   6432 C  CG  . PHE C  1  154 ? -16.253 27.921  19.953 1.00 62.16  ? 167 PHE C CG  1 
ATOM   6433 C  CD1 . PHE C  1  154 ? -16.624 28.087  21.279 1.00 63.82  ? 167 PHE C CD1 1 
ATOM   6434 C  CD2 . PHE C  1  154 ? -15.099 28.559  19.498 1.00 63.30  ? 167 PHE C CD2 1 
ATOM   6435 C  CE1 . PHE C  1  154 ? -15.876 28.893  22.128 1.00 66.87  ? 167 PHE C CE1 1 
ATOM   6436 C  CE2 . PHE C  1  154 ? -14.351 29.361  20.355 1.00 64.75  ? 167 PHE C CE2 1 
ATOM   6437 C  CZ  . PHE C  1  154 ? -14.744 29.533  21.664 1.00 65.32  ? 167 PHE C CZ  1 
ATOM   6438 N  N   . SER C  1  155 ? -19.711 26.112  17.287 1.00 58.18  ? 168 SER C N   1 
ATOM   6439 C  CA  . SER C  1  155 ? -20.326 25.769  16.014 1.00 66.55  ? 168 SER C CA  1 
ATOM   6440 C  C   . SER C  1  155 ? -21.449 26.758  15.674 1.00 68.44  ? 168 SER C C   1 
ATOM   6441 O  O   . SER C  1  155 ? -21.622 27.137  14.518 1.00 63.45  ? 168 SER C O   1 
ATOM   6442 C  CB  . SER C  1  155 ? -20.829 24.346  16.017 1.00 70.32  ? 168 SER C CB  1 
ATOM   6443 O  OG  . SER C  1  155 ? -19.773 23.418  16.244 1.00 71.55  ? 168 SER C OG  1 
ATOM   6444 N  N   . ASN C  1  156 ? -22.227 27.182  16.680 1.00 65.52  ? 169 ASN C N   1 
ATOM   6445 C  CA  . ASN C  1  156 ? -23.273 28.175  16.454 1.00 65.45  ? 169 ASN C CA  1 
ATOM   6446 C  C   . ASN C  1  156 ? -22.652 29.519  16.084 1.00 58.41  ? 169 ASN C C   1 
ATOM   6447 O  O   . ASN C  1  156 ? -23.141 30.201  15.196 1.00 63.67  ? 169 ASN C O   1 
ATOM   6448 C  CB  . ASN C  1  156 ? -24.193 28.301  17.662 1.00 57.01  ? 169 ASN C CB  1 
ATOM   6449 C  CG  . ASN C  1  156 ? -25.096 27.092  17.817 1.00 62.67  ? 169 ASN C CG  1 
ATOM   6450 O  OD1 . ASN C  1  156 ? -25.411 26.389  16.846 1.00 64.96  ? 169 ASN C OD1 1 
ATOM   6451 N  ND2 . ASN C  1  156 ? -25.582 26.843  19.021 1.00 60.50  ? 169 ASN C ND2 1 
ATOM   6452 N  N   . ARG C  1  157 ? -21.566 29.887  16.761 1.00 63.22  ? 170 ARG C N   1 
ATOM   6453 C  CA  . ARG C  1  157 ? -20.985 31.217  16.639 1.00 68.22  ? 170 ARG C CA  1 
ATOM   6454 C  C   . ARG C  1  157 ? -20.212 31.375  15.332 1.00 66.05  ? 170 ARG C C   1 
ATOM   6455 O  O   . ARG C  1  157 ? -20.161 32.472  14.796 1.00 64.33  ? 170 ARG C O   1 
ATOM   6456 C  CB  . ARG C  1  157 ? -20.072 31.522  17.832 1.00 72.81  ? 170 ARG C CB  1 
ATOM   6457 C  CG  . ARG C  1  157 ? -19.836 33.010  18.074 1.00 78.64  ? 170 ARG C CG  1 
ATOM   6458 C  CD  . ARG C  1  157 ? -18.752 33.323  19.091 1.00 74.38  ? 170 ARG C CD  1 
ATOM   6459 N  NE  . ARG C  1  157 ? -18.854 32.495  20.301 1.00 77.98  ? 170 ARG C NE  1 
ATOM   6460 C  CZ  . ARG C  1  157 ? -17.950 32.393  21.274 1.00 71.87  ? 170 ARG C CZ  1 
ATOM   6461 N  NH1 . ARG C  1  157 ? -16.815 33.070  21.232 1.00 67.86  ? 170 ARG C NH1 1 
ATOM   6462 N  NH2 . ARG C  1  157 ? -18.193 31.601  22.301 1.00 67.58  ? 170 ARG C NH2 1 
ATOM   6463 N  N   . TYR C  1  158 ? -19.584 30.299  14.833 1.00 71.91  ? 171 TYR C N   1 
ATOM   6464 C  CA  . TYR C  1  158 ? -18.652 30.425  13.720 1.00 68.84  ? 171 TYR C CA  1 
ATOM   6465 C  C   . TYR C  1  158 ? -18.981 29.520  12.533 1.00 64.92  ? 171 TYR C C   1 
ATOM   6466 O  O   . TYR C  1  158 ? -18.364 29.672  11.481 1.00 63.48  ? 171 TYR C O   1 
ATOM   6467 C  CB  . TYR C  1  158 ? -17.243 30.104  14.217 1.00 76.00  ? 171 TYR C CB  1 
ATOM   6468 C  CG  . TYR C  1  158 ? -16.735 31.092  15.249 1.00 79.99  ? 171 TYR C CG  1 
ATOM   6469 C  CD1 . TYR C  1  158 ? -16.399 32.384  14.874 1.00 81.50  ? 171 TYR C CD1 1 
ATOM   6470 C  CD2 . TYR C  1  158 ? -16.573 30.728  16.579 1.00 80.62  ? 171 TYR C CD2 1 
ATOM   6471 C  CE1 . TYR C  1  158 ? -15.915 33.299  15.797 1.00 82.91  ? 171 TYR C CE1 1 
ATOM   6472 C  CE2 . TYR C  1  158 ? -16.094 31.630  17.516 1.00 84.91  ? 171 TYR C CE2 1 
ATOM   6473 C  CZ  . TYR C  1  158 ? -15.767 32.921  17.122 1.00 83.26  ? 171 TYR C CZ  1 
ATOM   6474 O  OH  . TYR C  1  158 ? -15.291 33.813  18.038 1.00 83.79  ? 171 TYR C OH  1 
ATOM   6475 N  N   . GLY C  1  159 ? -19.925 28.581  12.684 1.00 64.19  ? 172 GLY C N   1 
ATOM   6476 C  CA  . GLY C  1  159 ? -20.166 27.610  11.629 1.00 63.23  ? 172 GLY C CA  1 
ATOM   6477 C  C   . GLY C  1  159 ? -21.637 27.466  11.249 1.00 62.90  ? 172 GLY C C   1 
ATOM   6478 O  O   . GLY C  1  159 ? -22.007 26.475  10.624 1.00 56.44  ? 172 GLY C O   1 
ATOM   6479 N  N   . GLY C  1  160 ? -22.478 28.445  11.612 1.00 63.94  ? 173 GLY C N   1 
ATOM   6480 C  CA  . GLY C  1  160 ? -23.887 28.408  11.252 1.00 54.20  ? 173 GLY C CA  1 
ATOM   6481 C  C   . GLY C  1  160 ? -24.620 27.237  11.904 1.00 55.51  ? 173 GLY C C   1 
ATOM   6482 O  O   . GLY C  1  160 ? -25.635 26.778  11.375 1.00 60.70  ? 173 GLY C O   1 
ATOM   6483 N  N   . GLY C  1  161 ? -24.097 26.761  13.045 1.00 52.36  ? 174 GLY C N   1 
ATOM   6484 C  CA  . GLY C  1  161 ? -24.683 25.638  13.771 1.00 54.69  ? 174 GLY C CA  1 
ATOM   6485 C  C   . GLY C  1  161 ? -24.046 24.290  13.420 1.00 54.48  ? 174 GLY C C   1 
ATOM   6486 O  O   . GLY C  1  161 ? -24.521 23.240  13.865 1.00 53.26  ? 174 GLY C O   1 
ATOM   6487 N  N   . PHE C  1  162 ? -22.999 24.332  12.590 1.00 62.23  ? 175 PHE C N   1 
ATOM   6488 C  CA  . PHE C  1  162 ? -22.262 23.150  12.171 1.00 64.01  ? 175 PHE C CA  1 
ATOM   6489 C  C   . PHE C  1  162 ? -20.783 23.338  12.500 1.00 64.23  ? 175 PHE C C   1 
ATOM   6490 O  O   . PHE C  1  162 ? -20.303 24.460  12.628 1.00 58.96  ? 175 PHE C O   1 
ATOM   6491 C  CB  . PHE C  1  162 ? -22.435 22.930  10.668 1.00 64.73  ? 175 PHE C CB  1 
ATOM   6492 C  CG  . PHE C  1  162 ? -23.862 22.671  10.217 1.00 68.31  ? 175 PHE C CG  1 
ATOM   6493 C  CD1 . PHE C  1  162 ? -24.346 21.372  10.161 1.00 72.98  ? 175 PHE C CD1 1 
ATOM   6494 C  CD2 . PHE C  1  162 ? -24.711 23.707  9.836  1.00 71.83  ? 175 PHE C CD2 1 
ATOM   6495 C  CE1 . PHE C  1  162 ? -25.635 21.104  9.727  1.00 73.91  ? 175 PHE C CE1 1 
ATOM   6496 C  CE2 . PHE C  1  162 ? -26.006 23.436  9.411  1.00 75.70  ? 175 PHE C CE2 1 
ATOM   6497 C  CZ  . PHE C  1  162 ? -26.471 22.135  9.371  1.00 74.58  ? 175 PHE C CZ  1 
ATOM   6498 N  N   . TYR C  1  163 ? -20.057 22.221  12.630 1.00 63.28  ? 176 TYR C N   1 
ATOM   6499 C  CA  . TYR C  1  163 ? -18.617 22.275  12.824 1.00 58.23  ? 176 TYR C CA  1 
ATOM   6500 C  C   . TYR C  1  163 ? -17.955 22.249  11.453 1.00 55.11  ? 176 TYR C C   1 
ATOM   6501 O  O   . TYR C  1  163 ? -18.139 21.304  10.692 1.00 56.06  ? 176 TYR C O   1 
ATOM   6502 C  CB  . TYR C  1  163 ? -18.137 21.097  13.673 1.00 59.83  ? 176 TYR C CB  1 
ATOM   6503 C  CG  . TYR C  1  163 ? -16.666 21.119  14.065 1.00 58.40  ? 176 TYR C CG  1 
ATOM   6504 C  CD1 . TYR C  1  163 ? -16.231 21.860  15.155 1.00 54.14  ? 176 TYR C CD1 1 
ATOM   6505 C  CD2 . TYR C  1  163 ? -15.721 20.366  13.376 1.00 54.26  ? 176 TYR C CD2 1 
ATOM   6506 C  CE1 . TYR C  1  163 ? -14.900 21.857  15.544 1.00 55.59  ? 176 TYR C CE1 1 
ATOM   6507 C  CE2 . TYR C  1  163 ? -14.386 20.360  13.748 1.00 54.09  ? 176 TYR C CE2 1 
ATOM   6508 C  CZ  . TYR C  1  163 ? -13.979 21.081  14.857 1.00 53.73  ? 176 TYR C CZ  1 
ATOM   6509 O  OH  . TYR C  1  163 ? -12.668 21.088  15.233 1.00 49.99  ? 176 TYR C OH  1 
ATOM   6510 N  N   . ASN C  1  164 ? -17.188 23.292  11.147 1.00 50.66  ? 177 ASN C N   1 
ATOM   6511 C  CA  . ASN C  1  164 ? -16.441 23.349  9.906  1.00 53.20  ? 177 ASN C CA  1 
ATOM   6512 C  C   . ASN C  1  164 ? -15.044 23.880  10.214 1.00 53.46  ? 177 ASN C C   1 
ATOM   6513 O  O   . ASN C  1  164 ? -14.711 24.093  11.383 1.00 54.20  ? 177 ASN C O   1 
ATOM   6514 C  CB  . ASN C  1  164 ? -17.231 24.119  8.855  1.00 61.53  ? 177 ASN C CB  1 
ATOM   6515 C  CG  . ASN C  1  164 ? -17.206 25.623  9.029  1.00 65.36  ? 177 ASN C CG  1 
ATOM   6516 O  OD1 . ASN C  1  164 ? -16.560 26.156  9.946  1.00 60.87  ? 177 ASN C OD1 1 
ATOM   6517 N  ND2 . ASN C  1  164 ? -17.887 26.318  8.126  1.00 73.11  ? 177 ASN C ND2 1 
ATOM   6518 N  N   . LEU C  1  165 ? -14.238 24.101  9.168  1.00 52.03  ? 178 LEU C N   1 
ATOM   6519 C  CA  . LEU C  1  165 ? -12.837 24.446  9.350  1.00 60.57  ? 178 LEU C CA  1 
ATOM   6520 C  C   . LEU C  1  165 ? -12.692 25.734  10.167 1.00 62.48  ? 178 LEU C C   1 
ATOM   6521 O  O   . LEU C  1  165 ? -11.755 25.862  10.954 1.00 58.90  ? 178 LEU C O   1 
ATOM   6522 C  CB  . LEU C  1  165 ? -12.153 24.538  7.987  1.00 63.00  ? 178 LEU C CB  1 
ATOM   6523 C  CG  . LEU C  1  165 ? -10.645 24.824  8.008  1.00 74.09  ? 178 LEU C CG  1 
ATOM   6524 C  CD1 . LEU C  1  165 ? -9.853  23.652  8.574  1.00 73.78  ? 178 LEU C CD1 1 
ATOM   6525 C  CD2 . LEU C  1  165 ? -10.114 25.254  6.653  1.00 78.31  ? 178 LEU C CD2 1 
ATOM   6526 N  N   . THR C  1  166 ? -13.606 26.700  9.981  1.00 65.23  ? 179 THR C N   1 
ATOM   6527 C  CA  . THR C  1  166 ? -13.505 27.970  10.688 1.00 63.18  ? 179 THR C CA  1 
ATOM   6528 C  C   . THR C  1  166 ? -13.724 27.736  12.184 1.00 49.79  ? 179 THR C C   1 
ATOM   6529 O  O   . THR C  1  166 ? -12.991 28.252  13.014 1.00 54.57  ? 179 THR C O   1 
ATOM   6530 C  CB  . THR C  1  166 ? -14.497 28.991  10.125 1.00 70.13  ? 179 THR C CB  1 
ATOM   6531 O  OG1 . THR C  1  166 ? -14.441 28.940  8.699  1.00 69.68  ? 179 THR C OG1 1 
ATOM   6532 C  CG2 . THR C  1  166 ? -14.143 30.392  10.594 1.00 69.25  ? 179 THR C CG2 1 
ATOM   6533 N  N   . VAL C  1  167 ? -14.711 26.914  12.520 1.00 49.04  ? 180 VAL C N   1 
ATOM   6534 C  CA  . VAL C  1  167 ? -14.983 26.566  13.909 1.00 54.89  ? 180 VAL C CA  1 
ATOM   6535 C  C   . VAL C  1  167 ? -13.751 25.902  14.529 1.00 60.87  ? 180 VAL C C   1 
ATOM   6536 O  O   . VAL C  1  167 ? -13.368 26.231  15.651 1.00 57.60  ? 180 VAL C O   1 
ATOM   6537 C  CB  . VAL C  1  167 ? -16.217 25.656  14.053 1.00 54.73  ? 180 VAL C CB  1 
ATOM   6538 C  CG1 . VAL C  1  167 ? -16.575 25.426  15.517 1.00 56.11  ? 180 VAL C CG1 1 
ATOM   6539 C  CG2 . VAL C  1  167 ? -17.437 26.192  13.313 1.00 58.28  ? 180 VAL C CG2 1 
ATOM   6540 N  N   . ALA C  1  168 ? -13.128 24.974  13.786 1.00 63.23  ? 181 ALA C N   1 
ATOM   6541 C  CA  . ALA C  1  168 ? -11.968 24.228  14.265 1.00 58.41  ? 181 ALA C CA  1 
ATOM   6542 C  C   . ALA C  1  168 ? -10.851 25.164  14.707 1.00 54.10  ? 181 ALA C C   1 
ATOM   6543 O  O   . ALA C  1  168 ? -10.284 24.990  15.782 1.00 54.61  ? 181 ALA C O   1 
ATOM   6544 C  CB  . ALA C  1  168 ? -11.469 23.278  13.196 1.00 58.55  ? 181 ALA C CB  1 
ATOM   6545 N  N   . GLY C  1  169 ? -10.553 26.164  13.878 1.00 54.51  ? 182 GLY C N   1 
ATOM   6546 C  CA  . GLY C  1  169 ? -9.515  27.130  14.202 1.00 59.99  ? 182 GLY C CA  1 
ATOM   6547 C  C   . GLY C  1  169 ? -9.819  27.856  15.512 1.00 65.22  ? 182 GLY C C   1 
ATOM   6548 O  O   . GLY C  1  169 ? -8.938  28.023  16.344 1.00 67.72  ? 182 GLY C O   1 
ATOM   6549 N  N   . GLU C  1  170 ? -11.073 28.282  15.686 1.00 63.18  ? 183 GLU C N   1 
ATOM   6550 C  CA  . GLU C  1  170 ? -11.463 29.065  16.848 1.00 62.29  ? 183 GLU C CA  1 
ATOM   6551 C  C   . GLU C  1  170 ? -11.486 28.171  18.086 1.00 57.98  ? 183 GLU C C   1 
ATOM   6552 O  O   . GLU C  1  170 ? -11.008 28.564  19.139 1.00 58.14  ? 183 GLU C O   1 
ATOM   6553 C  CB  . GLU C  1  170 ? -12.822 29.746  16.642 1.00 66.86  ? 183 GLU C CB  1 
ATOM   6554 C  CG  . GLU C  1  170 ? -12.854 30.777  15.517 1.00 69.53  ? 183 GLU C CG  1 
ATOM   6555 C  CD  . GLU C  1  170 ? -11.812 31.872  15.622 1.00 70.09  ? 183 GLU C CD  1 
ATOM   6556 O  OE1 . GLU C  1  170 ? -11.518 32.268  16.756 1.00 73.80  ? 183 GLU C OE1 1 
ATOM   6557 O  OE2 . GLU C  1  170 ? -11.269 32.296  14.587 1.00 80.72  ? 183 GLU C OE2 1 
ATOM   6558 N  N   . LEU C  1  171 ? -12.040 26.962  17.970 1.00 58.30  ? 184 LEU C N   1 
ATOM   6559 C  CA  . LEU C  1  171 ? -12.210 26.112  19.140 1.00 55.64  ? 184 LEU C CA  1 
ATOM   6560 C  C   . LEU C  1  171 ? -10.849 25.646  19.660 1.00 54.41  ? 184 LEU C C   1 
ATOM   6561 O  O   . LEU C  1  171 ? -10.619 25.642  20.864 1.00 57.55  ? 184 LEU C O   1 
ATOM   6562 C  CB  . LEU C  1  171 ? -13.123 24.930  18.831 1.00 57.88  ? 184 LEU C CB  1 
ATOM   6563 C  CG  . LEU C  1  171 ? -13.438 24.010  20.015 1.00 58.72  ? 184 LEU C CG  1 
ATOM   6564 C  CD1 . LEU C  1  171 ? -14.121 24.741  21.161 1.00 61.79  ? 184 LEU C CD1 1 
ATOM   6565 C  CD2 . LEU C  1  171 ? -14.308 22.837  19.612 1.00 59.72  ? 184 LEU C CD2 1 
ATOM   6566 N  N   . ARG C  1  172 ? -9.946  25.277  18.748 1.00 52.76  ? 185 ARG C N   1 
ATOM   6567 C  CA  . ARG C  1  172 ? -8.623  24.792  19.126 1.00 58.64  ? 185 ARG C CA  1 
ATOM   6568 C  C   . ARG C  1  172 ? -7.918  25.832  19.998 1.00 61.56  ? 185 ARG C C   1 
ATOM   6569 O  O   . ARG C  1  172 ? -7.393  25.509  21.062 1.00 55.64  ? 185 ARG C O   1 
ATOM   6570 C  CB  . ARG C  1  172 ? -7.839  24.435  17.855 1.00 51.77  ? 185 ARG C CB  1 
ATOM   6571 C  CG  . ARG C  1  172 ? -6.324  24.317  17.939 1.00 52.09  ? 185 ARG C CG  1 
ATOM   6572 C  CD  . ARG C  1  172 ? -5.790  23.429  19.033 1.00 52.40  ? 185 ARG C CD  1 
ATOM   6573 N  NE  . ARG C  1  172 ? -6.420  22.108  19.099 1.00 54.43  ? 185 ARG C NE  1 
ATOM   6574 C  CZ  . ARG C  1  172 ? -6.894  21.544  20.203 1.00 59.73  ? 185 ARG C CZ  1 
ATOM   6575 N  NH1 . ARG C  1  172 ? -6.906  22.218  21.340 1.00 63.90  ? 185 ARG C NH1 1 
ATOM   6576 N  NH2 . ARG C  1  172 ? -7.371  20.307  20.171 1.00 59.62  ? 185 ARG C NH2 1 
ATOM   6577 N  N   . TYR C  1  173 ? -7.912  27.083  19.536 1.00 63.69  ? 186 TYR C N   1 
ATOM   6578 C  CA  . TYR C  1  173 ? -7.236  28.158  20.243 1.00 64.90  ? 186 TYR C CA  1 
ATOM   6579 C  C   . TYR C  1  173 ? -7.888  28.387  21.606 1.00 61.83  ? 186 TYR C C   1 
ATOM   6580 O  O   . TYR C  1  173 ? -7.208  28.496  22.620 1.00 62.58  ? 186 TYR C O   1 
ATOM   6581 C  CB  . TYR C  1  173 ? -7.269  29.417  19.378 1.00 65.33  ? 186 TYR C CB  1 
ATOM   6582 C  CG  . TYR C  1  173 ? -6.523  30.588  19.990 1.00 77.47  ? 186 TYR C CG  1 
ATOM   6583 C  CD1 . TYR C  1  173 ? -5.143  30.540  20.149 1.00 80.66  ? 186 TYR C CD1 1 
ATOM   6584 C  CD2 . TYR C  1  173 ? -7.190  31.741  20.389 1.00 83.32  ? 186 TYR C CD2 1 
ATOM   6585 C  CE1 . TYR C  1  173 ? -4.436  31.616  20.657 1.00 81.78  ? 186 TYR C CE1 1 
ATOM   6586 C  CE2 . TYR C  1  173 ? -6.495  32.820  20.922 1.00 83.01  ? 186 TYR C CE2 1 
ATOM   6587 C  CZ  . TYR C  1  173 ? -5.117  32.760  21.039 1.00 82.74  ? 186 TYR C CZ  1 
ATOM   6588 O  OH  . TYR C  1  173 ? -4.427  33.802  21.573 1.00 82.13  ? 186 TYR C OH  1 
ATOM   6589 N  N   . SER C  1  174 ? -9.218  28.434  21.628 1.00 60.49  ? 187 SER C N   1 
ATOM   6590 C  CA  . SER C  1  174 ? -9.941  28.735  22.851 1.00 63.39  ? 187 SER C CA  1 
ATOM   6591 C  C   . SER C  1  174 ? -9.697  27.642  23.891 1.00 64.86  ? 187 SER C C   1 
ATOM   6592 O  O   . SER C  1  174 ? -9.580  27.929  25.084 1.00 56.84  ? 187 SER C O   1 
ATOM   6593 C  CB  . SER C  1  174 ? -11.417 28.936  22.580 1.00 64.73  ? 187 SER C CB  1 
ATOM   6594 O  OG  . SER C  1  174 ? -12.111 29.149  23.798 1.00 60.92  ? 187 SER C OG  1 
ATOM   6595 N  N   . ARG C  1  175 ? -9.574  26.387  23.436 1.00 59.83  ? 188 ARG C N   1 
ATOM   6596 C  CA  . ARG C  1  175 ? -9.330  25.281  24.350 1.00 55.87  ? 188 ARG C CA  1 
ATOM   6597 C  C   . ARG C  1  175 ? -7.922  25.374  24.936 1.00 53.78  ? 188 ARG C C   1 
ATOM   6598 O  O   . ARG C  1  175 ? -7.725  25.067  26.110 1.00 59.84  ? 188 ARG C O   1 
ATOM   6599 C  CB  . ARG C  1  175 ? -9.613  23.920  23.702 1.00 54.88  ? 188 ARG C CB  1 
ATOM   6600 C  CG  . ARG C  1  175 ? -11.094 23.692  23.421 1.00 54.80  ? 188 ARG C CG  1 
ATOM   6601 C  CD  . ARG C  1  175 ? -11.933 23.483  24.672 1.00 55.87  ? 188 ARG C CD  1 
ATOM   6602 N  NE  . ARG C  1  175 ? -11.473 22.283  25.376 1.00 59.73  ? 188 ARG C NE  1 
ATOM   6603 C  CZ  . ARG C  1  175 ? -10.876 22.220  26.564 1.00 63.58  ? 188 ARG C CZ  1 
ATOM   6604 N  NH1 . ARG C  1  175 ? -10.800 23.275  27.359 1.00 62.14  ? 188 ARG C NH1 1 
ATOM   6605 N  NH2 . ARG C  1  175 ? -10.356 21.075  26.955 1.00 61.84  ? 188 ARG C NH2 1 
ATOM   6606 N  N   . ILE C  1  176 ? -6.946  25.793  24.127 1.00 53.94  ? 189 ILE C N   1 
ATOM   6607 C  CA  . ILE C  1  176 ? -5.602  26.052  24.627 1.00 58.82  ? 189 ILE C CA  1 
ATOM   6608 C  C   . ILE C  1  176 ? -5.675  27.098  25.748 1.00 62.32  ? 189 ILE C C   1 
ATOM   6609 O  O   . ILE C  1  176 ? -5.099  26.913  26.823 1.00 57.28  ? 189 ILE C O   1 
ATOM   6610 C  CB  . ILE C  1  176 ? -4.664  26.471  23.474 1.00 53.16  ? 189 ILE C CB  1 
ATOM   6611 C  CG1 . ILE C  1  176 ? -4.403  25.297  22.505 1.00 53.11  ? 189 ILE C CG1 1 
ATOM   6612 C  CG2 . ILE C  1  176 ? -3.350  27.058  23.998 1.00 55.44  ? 189 ILE C CG2 1 
ATOM   6613 C  CD1 . ILE C  1  176 ? -3.761  25.708  21.192 1.00 51.63  ? 189 ILE C CD1 1 
ATOM   6614 N  N   . GLN C  1  177 ? -6.408  28.191  25.507 1.00 68.14  ? 190 GLN C N   1 
ATOM   6615 C  CA  . GLN C  1  177 ? -6.543  29.263  26.489 1.00 64.23  ? 190 GLN C CA  1 
ATOM   6616 C  C   . GLN C  1  177 ? -7.196  28.765  27.778 1.00 57.99  ? 190 GLN C C   1 
ATOM   6617 O  O   . GLN C  1  177 ? -6.723  29.105  28.861 1.00 66.71  ? 190 GLN C O   1 
ATOM   6618 C  CB  . GLN C  1  177 ? -7.301  30.463  25.921 1.00 68.27  ? 190 GLN C CB  1 
ATOM   6619 C  CG  . GLN C  1  177 ? -6.601  31.148  24.752 1.00 65.00  ? 190 GLN C CG  1 
ATOM   6620 C  CD  . GLN C  1  177 ? -5.195  31.620  25.069 1.00 67.53  ? 190 GLN C CD  1 
ATOM   6621 O  OE1 . GLN C  1  177 ? -4.830  31.844  26.230 1.00 75.04  ? 190 GLN C OE1 1 
ATOM   6622 N  NE2 . GLN C  1  177 ? -4.383  31.785  24.034 1.00 69.25  ? 190 GLN C NE2 1 
ATOM   6623 N  N   . ASP C  1  178 ? -8.253  27.945  27.674 1.00 55.01  ? 191 ASP C N   1 
ATOM   6624 C  CA  . ASP C  1  178 ? -8.880  27.364  28.855 1.00 59.21  ? 191 ASP C CA  1 
ATOM   6625 C  C   . ASP C  1  178 ? -7.841  26.631  29.705 1.00 66.27  ? 191 ASP C C   1 
ATOM   6626 O  O   . ASP C  1  178 ? -7.810  26.794  30.929 1.00 57.95  ? 191 ASP C O   1 
ATOM   6627 C  CB  . ASP C  1  178 ? -9.991  26.379  28.528 1.00 61.84  ? 191 ASP C CB  1 
ATOM   6628 C  CG  . ASP C  1  178 ? -11.220 26.926  27.808 1.00 67.74  ? 191 ASP C CG  1 
ATOM   6629 O  OD1 . ASP C  1  178 ? -11.392 28.166  27.784 1.00 78.82  ? 191 ASP C OD1 1 
ATOM   6630 O  OD2 . ASP C  1  178 ? -11.995 26.104  27.250 1.00 65.15  ? 191 ASP C OD2 1 
ATOM   6631 N  N   . SER C  1  179 ? -7.012  25.802  29.059 1.00 58.29  ? 192 SER C N   1 
ATOM   6632 C  CA  . SER C  1  179 ? -6.025  25.009  29.778 1.00 59.06  ? 192 SER C CA  1 
ATOM   6633 C  C   . SER C  1  179 ? -4.929  25.893  30.388 1.00 57.95  ? 192 SER C C   1 
ATOM   6634 O  O   . SER C  1  179 ? -4.469  25.629  31.496 1.00 57.01  ? 192 SER C O   1 
ATOM   6635 C  CB  . SER C  1  179 ? -5.435  23.912  28.880 1.00 57.53  ? 192 SER C CB  1 
ATOM   6636 O  OG  . SER C  1  179 ? -6.336  22.820  28.734 1.00 57.14  ? 192 SER C OG  1 
ATOM   6637 N  N   . ILE C  1  180 ? -4.489  26.935  29.671 1.00 56.58  ? 193 ILE C N   1 
ATOM   6638 C  CA  . ILE C  1  180 ? -3.490  27.845  30.222 1.00 62.63  ? 193 ILE C CA  1 
ATOM   6639 C  C   . ILE C  1  180 ? -4.019  28.440  31.529 1.00 68.70  ? 193 ILE C C   1 
ATOM   6640 O  O   . ILE C  1  180 ? -3.322  28.451  32.540 1.00 67.05  ? 193 ILE C O   1 
ATOM   6641 C  CB  . ILE C  1  180 ? -3.116  28.949  29.218 1.00 61.31  ? 193 ILE C CB  1 
ATOM   6642 C  CG1 . ILE C  1  180 ? -2.273  28.393  28.075 1.00 60.31  ? 193 ILE C CG1 1 
ATOM   6643 C  CG2 . ILE C  1  180 ? -2.399  30.106  29.921 1.00 61.27  ? 193 ILE C CG2 1 
ATOM   6644 C  CD1 . ILE C  1  180 ? -2.042  29.366  26.936 1.00 59.40  ? 193 ILE C CD1 1 
ATOM   6645 N  N   . ALA C  1  181 ? -5.276  28.899  31.491 1.00 71.51  ? 194 ALA C N   1 
ATOM   6646 C  CA  . ALA C  1  181 ? -5.878  29.642  32.582 1.00 70.06  ? 194 ALA C CA  1 
ATOM   6647 C  C   . ALA C  1  181 ? -6.203  28.751  33.776 1.00 67.30  ? 194 ALA C C   1 
ATOM   6648 O  O   . ALA C  1  181 ? -6.254  29.255  34.891 1.00 70.17  ? 194 ALA C O   1 
ATOM   6649 C  CB  . ALA C  1  181 ? -7.121  30.353  32.089 1.00 71.03  ? 194 ALA C CB  1 
ATOM   6650 N  N   . THR C  1  182 ? -6.422  27.443  33.574 1.00 65.21  ? 195 THR C N   1 
ATOM   6651 C  CA  . THR C  1  182 ? -7.012  26.638  34.635 1.00 66.34  ? 195 THR C CA  1 
ATOM   6652 C  C   . THR C  1  182 ? -6.167  25.418  35.004 1.00 69.21  ? 195 THR C C   1 
ATOM   6653 O  O   . THR C  1  182 ? -6.451  24.768  36.008 1.00 61.77  ? 195 THR C O   1 
ATOM   6654 C  CB  . THR C  1  182 ? -8.427  26.209  34.241 1.00 75.15  ? 195 THR C CB  1 
ATOM   6655 O  OG1 . THR C  1  182 ? -8.324  25.371  33.092 1.00 77.01  ? 195 THR C OG1 1 
ATOM   6656 C  CG2 . THR C  1  182 ? -9.341  27.384  33.936 1.00 77.00  ? 195 THR C CG2 1 
ATOM   6657 N  N   . ASN C  1  183 ? -5.174  25.059  34.188 1.00 70.06  ? 196 ASN C N   1 
ATOM   6658 C  CA  . ASN C  1  183 ? -4.448  23.819  34.412 1.00 66.30  ? 196 ASN C CA  1 
ATOM   6659 C  C   . ASN C  1  183 ? -2.987  24.163  34.649 1.00 61.48  ? 196 ASN C C   1 
ATOM   6660 O  O   . ASN C  1  183 ? -2.269  24.490  33.709 1.00 56.15  ? 196 ASN C O   1 
ATOM   6661 C  CB  . ASN C  1  183 ? -4.603  22.842  33.249 1.00 70.17  ? 196 ASN C CB  1 
ATOM   6662 C  CG  . ASN C  1  183 ? -3.858  21.541  33.452 1.00 68.28  ? 196 ASN C CG  1 
ATOM   6663 O  OD1 . ASN C  1  183 ? -3.191  21.349  34.479 1.00 67.94  ? 196 ASN C OD1 1 
ATOM   6664 N  ND2 . ASN C  1  183 ? -3.959  20.637  32.483 1.00 64.33  ? 196 ASN C ND2 1 
ATOM   6665 N  N   . PRO C  1  184 ? -2.503  24.105  35.907 1.00 62.83  ? 197 PRO C N   1 
ATOM   6666 C  CA  . PRO C  1  184 ? -1.118  24.475  36.192 1.00 64.95  ? 197 PRO C CA  1 
ATOM   6667 C  C   . PRO C  1  184 ? -0.089  23.492  35.628 1.00 68.42  ? 197 PRO C C   1 
ATOM   6668 O  O   . PRO C  1  184 ? 1.085   23.832  35.525 1.00 66.13  ? 197 PRO C O   1 
ATOM   6669 C  CB  . PRO C  1  184 ? -1.111  24.533  37.729 1.00 63.46  ? 197 PRO C CB  1 
ATOM   6670 C  CG  . PRO C  1  184 ? -2.145  23.515  38.141 1.00 64.90  ? 197 PRO C CG  1 
ATOM   6671 C  CD  . PRO C  1  184 ? -3.241  23.642  37.096 1.00 63.90  ? 197 PRO C CD  1 
ATOM   6672 N  N   . GLU C  1  185 ? -0.541  22.278  35.264 1.00 67.98  ? 198 GLU C N   1 
ATOM   6673 C  CA  . GLU C  1  185 ? 0.314   21.248  34.687 1.00 67.59  ? 198 GLU C CA  1 
ATOM   6674 C  C   . GLU C  1  185 ? 0.137   21.154  33.165 1.00 63.73  ? 198 GLU C C   1 
ATOM   6675 O  O   . GLU C  1  185 ? 0.616   20.210  32.551 1.00 58.46  ? 198 GLU C O   1 
ATOM   6676 C  CB  . GLU C  1  185 ? -0.007  19.894  35.326 1.00 67.43  ? 198 GLU C CB  1 
ATOM   6677 C  CG  . GLU C  1  185 ? 0.302   19.818  36.820 1.00 68.04  ? 198 GLU C CG  1 
ATOM   6678 C  CD  . GLU C  1  185 ? -0.082  18.486  37.450 1.00 78.21  ? 198 GLU C CD  1 
ATOM   6679 O  OE1 . GLU C  1  185 ? -0.552  17.584  36.722 1.00 76.39  ? 198 GLU C OE1 1 
ATOM   6680 O  OE2 . GLU C  1  185 ? 0.046   18.345  38.685 1.00 80.30  ? 198 GLU C OE2 1 
ATOM   6681 N  N   . PHE C  1  186 ? -0.524  22.139  32.550 1.00 61.38  ? 199 PHE C N   1 
ATOM   6682 C  CA  . PHE C  1  186 ? -0.781  22.146  31.118 1.00 60.58  ? 199 PHE C CA  1 
ATOM   6683 C  C   . PHE C  1  186 ? 0.510   22.006  30.314 1.00 61.25  ? 199 PHE C C   1 
ATOM   6684 O  O   . PHE C  1  186 ? 1.428   22.807  30.465 1.00 57.16  ? 199 PHE C O   1 
ATOM   6685 C  CB  . PHE C  1  186 ? -1.443  23.459  30.701 1.00 56.22  ? 199 PHE C CB  1 
ATOM   6686 C  CG  . PHE C  1  186 ? -1.735  23.617  29.214 1.00 54.75  ? 199 PHE C CG  1 
ATOM   6687 C  CD1 . PHE C  1  186 ? -2.291  22.576  28.475 1.00 53.37  ? 199 PHE C CD1 1 
ATOM   6688 C  CD2 . PHE C  1  186 ? -1.439  24.806  28.553 1.00 51.08  ? 199 PHE C CD2 1 
ATOM   6689 C  CE1 . PHE C  1  186 ? -2.563  22.733  27.125 1.00 48.87  ? 199 PHE C CE1 1 
ATOM   6690 C  CE2 . PHE C  1  186 ? -1.709  24.960  27.201 1.00 51.23  ? 199 PHE C CE2 1 
ATOM   6691 C  CZ  . PHE C  1  186 ? -2.267  23.920  26.487 1.00 54.26  ? 199 PHE C CZ  1 
ATOM   6692 N  N   . GLN C  1  187 ? 0.530   20.999  29.424 1.00 61.64  ? 200 GLN C N   1 
ATOM   6693 C  CA  . GLN C  1  187 ? 1.623   20.761  28.493 1.00 56.98  ? 200 GLN C CA  1 
ATOM   6694 C  C   . GLN C  1  187 ? 1.048   20.713  27.083 1.00 53.50  ? 200 GLN C C   1 
ATOM   6695 O  O   . GLN C  1  187 ? -0.015  20.133  26.869 1.00 53.04  ? 200 GLN C O   1 
ATOM   6696 C  CB  . GLN C  1  187 ? 2.294   19.420  28.809 1.00 61.36  ? 200 GLN C CB  1 
ATOM   6697 C  CG  . GLN C  1  187 ? 3.109   19.413  30.099 1.00 66.55  ? 200 GLN C CG  1 
ATOM   6698 C  CD  . GLN C  1  187 ? 4.372   20.238  29.971 1.00 68.82  ? 200 GLN C CD  1 
ATOM   6699 O  OE1 . GLN C  1  187 ? 5.313   19.862  29.261 1.00 69.98  ? 200 GLN C OE1 1 
ATOM   6700 N  NE2 . GLN C  1  187 ? 4.380   21.401  30.606 1.00 70.20  ? 200 GLN C NE2 1 
ATOM   6701 N  N   . PHE C  1  188 ? 1.756   21.316  26.130 1.00 47.54  ? 201 PHE C N   1 
ATOM   6702 C  CA  . PHE C  1  188 ? 1.304   21.347  24.750 1.00 48.11  ? 201 PHE C CA  1 
ATOM   6703 C  C   . PHE C  1  188 ? 2.521   21.325  23.834 1.00 47.55  ? 201 PHE C C   1 
ATOM   6704 O  O   . PHE C  1  188 ? 2.774   22.267  23.097 1.00 50.62  ? 201 PHE C O   1 
ATOM   6705 C  CB  . PHE C  1  188 ? 0.413   22.571  24.546 1.00 47.03  ? 201 PHE C CB  1 
ATOM   6706 C  CG  . PHE C  1  188 ? -0.538  22.465  23.364 1.00 44.53  ? 201 PHE C CG  1 
ATOM   6707 C  CD1 . PHE C  1  188 ? -1.619  21.602  23.405 1.00 47.44  ? 201 PHE C CD1 1 
ATOM   6708 C  CD2 . PHE C  1  188 ? -0.380  23.266  22.246 1.00 45.13  ? 201 PHE C CD2 1 
ATOM   6709 C  CE1 . PHE C  1  188 ? -2.510  21.533  22.349 1.00 47.77  ? 201 PHE C CE1 1 
ATOM   6710 C  CE2 . PHE C  1  188 ? -1.272  23.192  21.195 1.00 44.22  ? 201 PHE C CE2 1 
ATOM   6711 C  CZ  . PHE C  1  188 ? -2.332  22.328  21.250 1.00 43.37  ? 201 PHE C CZ  1 
ATOM   6712 N  N   . LYS C  1  189 ? 3.267   20.220  23.878 1.00 47.89  ? 202 LYS C N   1 
ATOM   6713 C  CA  . LYS C  1  189 ? 4.499   20.106  23.116 1.00 49.23  ? 202 LYS C CA  1 
ATOM   6714 C  C   . LYS C  1  189 ? 4.688   18.670  22.608 1.00 43.83  ? 202 LYS C C   1 
ATOM   6715 O  O   . LYS C  1  189 ? 3.906   17.773  22.927 1.00 45.81  ? 202 LYS C O   1 
ATOM   6716 C  CB  . LYS C  1  189 ? 5.642   20.559  24.034 1.00 52.63  ? 202 LYS C CB  1 
ATOM   6717 C  CG  . LYS C  1  189 ? 5.820   19.700  25.279 1.00 56.02  ? 202 LYS C CG  1 
ATOM   6718 C  CD  . LYS C  1  189 ? 7.180   19.929  25.926 1.00 61.19  ? 202 LYS C CD  1 
ATOM   6719 C  CE  . LYS C  1  189 ? 7.232   21.128  26.796 1.00 64.67  ? 202 LYS C CE  1 
ATOM   6720 N  NZ  . LYS C  1  189 ? 7.300   20.679  28.186 1.00 71.13  ? 202 LYS C NZ  1 
ATOM   6721 N  N   . ASN C  1  190 ? 5.736   18.475  21.804 1.00 44.34  ? 203 ASN C N   1 
ATOM   6722 C  CA  . ASN C  1  190 ? 6.104   17.170  21.275 1.00 44.46  ? 203 ASN C CA  1 
ATOM   6723 C  C   . ASN C  1  190 ? 4.888   16.475  20.648 1.00 37.75  ? 203 ASN C C   1 
ATOM   6724 O  O   . ASN C  1  190 ? 4.257   17.032  19.763 1.00 40.05  ? 203 ASN C O   1 
ATOM   6725 C  CB  . ASN C  1  190 ? 6.841   16.395  22.356 1.00 48.55  ? 203 ASN C CB  1 
ATOM   6726 C  CG  . ASN C  1  190 ? 8.165   17.044  22.685 1.00 54.12  ? 203 ASN C CG  1 
ATOM   6727 O  OD1 . ASN C  1  190 ? 8.926   17.387  21.771 1.00 57.00  ? 203 ASN C OD1 1 
ATOM   6728 N  ND2 . ASN C  1  190 ? 8.447   17.211  23.967 1.00 51.99  ? 203 ASN C ND2 1 
ATOM   6729 N  N   . VAL C  1  191 ? 4.547   15.263  21.085 1.00 36.87  ? 204 VAL C N   1 
ATOM   6730 C  CA  . VAL C  1  191 ? 3.505   14.511  20.404 1.00 40.79  ? 204 VAL C CA  1 
ATOM   6731 C  C   . VAL C  1  191 ? 2.201   15.310  20.421 1.00 42.59  ? 204 VAL C C   1 
ATOM   6732 O  O   . VAL C  1  191 ? 1.538   15.448  19.394 1.00 42.76  ? 204 VAL C O   1 
ATOM   6733 C  CB  . VAL C  1  191 ? 3.280   13.115  21.010 1.00 41.74  ? 204 VAL C CB  1 
ATOM   6734 C  CG1 . VAL C  1  191 ? 2.065   12.424  20.391 1.00 40.38  ? 204 VAL C CG1 1 
ATOM   6735 C  CG2 . VAL C  1  191 ? 4.524   12.238  20.901 1.00 40.52  ? 204 VAL C CG2 1 
ATOM   6736 N  N   . ARG C  1  192 ? 1.824   15.827  21.595 1.00 40.92  ? 205 ARG C N   1 
ATOM   6737 C  CA  . ARG C  1  192 ? 0.517   16.445  21.743 1.00 41.81  ? 205 ARG C CA  1 
ATOM   6738 C  C   . ARG C  1  192 ? 0.354   17.637  20.803 1.00 40.32  ? 205 ARG C C   1 
ATOM   6739 O  O   . ARG C  1  192 ? -0.726  17.865  20.267 1.00 41.94  ? 205 ARG C O   1 
ATOM   6740 C  CB  . ARG C  1  192 ? 0.266   16.898  23.188 1.00 45.54  ? 205 ARG C CB  1 
ATOM   6741 C  CG  . ARG C  1  192 ? -1.129  17.478  23.393 1.00 47.81  ? 205 ARG C CG  1 
ATOM   6742 C  CD  . ARG C  1  192 ? -2.224  16.569  22.852 1.00 49.77  ? 205 ARG C CD  1 
ATOM   6743 N  NE  . ARG C  1  192 ? -3.567  17.124  23.053 1.00 49.24  ? 205 ARG C NE  1 
ATOM   6744 C  CZ  . ARG C  1  192 ? -4.651  16.796  22.353 1.00 51.23  ? 205 ARG C CZ  1 
ATOM   6745 N  NH1 . ARG C  1  192 ? -4.576  15.881  21.392 1.00 46.92  ? 205 ARG C NH1 1 
ATOM   6746 N  NH2 . ARG C  1  192 ? -5.812  17.394  22.613 1.00 47.69  ? 205 ARG C NH2 1 
ATOM   6747 N  N   . PHE C  1  193 ? 1.420   18.415  20.620 1.00 42.71  ? 206 PHE C N   1 
ATOM   6748 C  CA  . PHE C  1  193 ? 1.338   19.614  19.808 1.00 43.67  ? 206 PHE C CA  1 
ATOM   6749 C  C   . PHE C  1  193 ? 0.955   19.227  18.383 1.00 47.99  ? 206 PHE C C   1 
ATOM   6750 O  O   . PHE C  1  193 ? 0.162   19.918  17.744 1.00 44.19  ? 206 PHE C O   1 
ATOM   6751 C  CB  . PHE C  1  193 ? 2.648   20.404  19.841 1.00 40.90  ? 206 PHE C CB  1 
ATOM   6752 C  CG  . PHE C  1  193 ? 2.605   21.634  18.954 1.00 44.75  ? 206 PHE C CG  1 
ATOM   6753 C  CD1 . PHE C  1  193 ? 1.950   22.784  19.376 1.00 47.10  ? 206 PHE C CD1 1 
ATOM   6754 C  CD2 . PHE C  1  193 ? 3.213   21.630  17.707 1.00 45.59  ? 206 PHE C CD2 1 
ATOM   6755 C  CE1 . PHE C  1  193 ? 1.900   23.899  18.564 1.00 47.95  ? 206 PHE C CE1 1 
ATOM   6756 C  CE2 . PHE C  1  193 ? 3.152   22.745  16.891 1.00 49.67  ? 206 PHE C CE2 1 
ATOM   6757 C  CZ  . PHE C  1  193 ? 2.487   23.876  17.318 1.00 49.48  ? 206 PHE C CZ  1 
ATOM   6758 N  N   . ILE C  1  194 ? 1.499   18.104  17.897 1.00 46.21  ? 207 ILE C N   1 
ATOM   6759 C  CA  . ILE C  1  194 ? 1.234   17.681  16.534 1.00 41.86  ? 207 ILE C CA  1 
ATOM   6760 C  C   . ILE C  1  194 ? -0.168  17.072  16.442 1.00 39.49  ? 207 ILE C C   1 
ATOM   6761 O  O   . ILE C  1  194 ? -0.942  17.464  15.570 1.00 44.41  ? 207 ILE C O   1 
ATOM   6762 C  CB  . ILE C  1  194 ? 2.349   16.756  16.029 1.00 43.26  ? 207 ILE C CB  1 
ATOM   6763 C  CG1 . ILE C  1  194 ? 3.719   17.455  16.043 1.00 48.25  ? 207 ILE C CG1 1 
ATOM   6764 C  CG2 . ILE C  1  194 ? 2.018   16.210  14.645 1.00 46.20  ? 207 ILE C CG2 1 
ATOM   6765 C  CD1 . ILE C  1  194 ? 3.830   18.713  15.205 1.00 51.20  ? 207 ILE C CD1 1 
ATOM   6766 N  N   . THR C  1  195 ? -0.523  16.168  17.363 1.00 39.15  ? 208 THR C N   1 
ATOM   6767 C  CA  . THR C  1  195 ? -1.784  15.436  17.271 1.00 42.46  ? 208 THR C CA  1 
ATOM   6768 C  C   . THR C  1  195 ? -2.979  16.352  17.530 1.00 44.69  ? 208 THR C C   1 
ATOM   6769 O  O   . THR C  1  195 ? -4.065  16.085  17.026 1.00 41.16  ? 208 THR C O   1 
ATOM   6770 C  CB  . THR C  1  195 ? -1.813  14.234  18.218 1.00 45.39  ? 208 THR C CB  1 
ATOM   6771 O  OG1 . THR C  1  195 ? -1.767  14.714  19.563 1.00 48.60  ? 208 THR C OG1 1 
ATOM   6772 C  CG2 . THR C  1  195 ? -0.672  13.271  17.943 1.00 45.26  ? 208 THR C CG2 1 
ATOM   6773 N  N   . ALA C  1  196 ? -2.795  17.438  18.285 1.00 45.32  ? 209 ALA C N   1 
ATOM   6774 C  CA  . ALA C  1  196 ? -3.915  18.290  18.664 1.00 46.64  ? 209 ALA C CA  1 
ATOM   6775 C  C   . ALA C  1  196 ? -4.485  19.048  17.472 1.00 47.05  ? 209 ALA C C   1 
ATOM   6776 O  O   . ALA C  1  196 ? -5.652  19.426  17.516 1.00 50.42  ? 209 ALA C O   1 
ATOM   6777 C  CB  . ALA C  1  196 ? -3.511  19.275  19.743 1.00 51.75  ? 209 ALA C CB  1 
ATOM   6778 N  N   . TYR C  1  197 ? -3.675  19.315  16.439 1.00 42.11  ? 210 TYR C N   1 
ATOM   6779 C  CA  . TYR C  1  197 ? -4.167  20.040  15.277 1.00 45.68  ? 210 TYR C CA  1 
ATOM   6780 C  C   . TYR C  1  197 ? -4.914  19.063  14.370 1.00 48.14  ? 210 TYR C C   1 
ATOM   6781 O  O   . TYR C  1  197 ? -6.029  19.351  13.930 1.00 49.84  ? 210 TYR C O   1 
ATOM   6782 C  CB  . TYR C  1  197 ? -3.037  20.865  14.652 1.00 50.03  ? 210 TYR C CB  1 
ATOM   6783 C  CG  . TYR C  1  197 ? -2.786  22.102  15.502 1.00 56.90  ? 210 TYR C CG  1 
ATOM   6784 C  CD1 . TYR C  1  197 ? -3.543  23.266  15.331 1.00 59.59  ? 210 TYR C CD1 1 
ATOM   6785 C  CD2 . TYR C  1  197 ? -1.875  22.062  16.545 1.00 55.96  ? 210 TYR C CD2 1 
ATOM   6786 C  CE1 . TYR C  1  197 ? -3.366  24.364  16.156 1.00 59.83  ? 210 TYR C CE1 1 
ATOM   6787 C  CE2 . TYR C  1  197 ? -1.693  23.153  17.375 1.00 61.75  ? 210 TYR C CE2 1 
ATOM   6788 C  CZ  . TYR C  1  197 ? -2.441  24.303  17.185 1.00 60.71  ? 210 TYR C CZ  1 
ATOM   6789 O  OH  . TYR C  1  197 ? -2.245  25.367  18.010 1.00 64.10  ? 210 TYR C OH  1 
ATOM   6790 N  N   . GLY C  1  198 ? -4.327  17.888  14.131 1.00 43.57  ? 211 GLY C N   1 
ATOM   6791 C  CA  . GLY C  1  198 ? -4.983  16.883  13.313 1.00 41.17  ? 211 GLY C CA  1 
ATOM   6792 C  C   . GLY C  1  198 ? -6.336  16.464  13.880 1.00 39.78  ? 211 GLY C C   1 
ATOM   6793 O  O   . GLY C  1  198 ? -7.288  16.301  13.130 1.00 42.95  ? 211 GLY C O   1 
ATOM   6794 N  N   . GLU C  1  199 ? -6.440  16.293  15.198 1.00 39.26  ? 212 GLU C N   1 
ATOM   6795 C  CA  A GLU C  1  199 ? -7.674  15.811  15.796 0.50 40.57  ? 212 GLU C CA  1 
ATOM   6796 C  CA  B GLU C  1  199 ? -7.664  15.835  15.838 0.50 42.76  ? 212 GLU C CA  1 
ATOM   6797 C  C   . GLU C  1  199 ? -8.812  16.801  15.541 1.00 40.49  ? 212 GLU C C   1 
ATOM   6798 O  O   . GLU C  1  199 ? -9.970  16.396  15.504 1.00 41.88  ? 212 GLU C O   1 
ATOM   6799 C  CB  A GLU C  1  199 ? -7.471  15.424  17.262 0.50 39.65  ? 212 GLU C CB  1 
ATOM   6800 C  CB  B GLU C  1  199 ? -7.499  15.635  17.352 0.50 44.99  ? 212 GLU C CB  1 
ATOM   6801 C  CG  A GLU C  1  199 ? -6.733  14.097  17.425 0.50 38.90  ? 212 GLU C CG  1 
ATOM   6802 C  CG  B GLU C  1  199 ? -7.678  16.898  18.197 0.50 48.00  ? 212 GLU C CG  1 
ATOM   6803 C  CD  A GLU C  1  199 ? -6.111  13.953  18.800 0.50 39.61  ? 212 GLU C CD  1 
ATOM   6804 C  CD  B GLU C  1  199 ? -7.531  16.724  19.702 0.50 46.59  ? 212 GLU C CD  1 
ATOM   6805 O  OE1 A GLU C  1  199 ? -6.467  14.756  19.684 0.50 39.64  ? 212 GLU C OE1 1 
ATOM   6806 O  OE1 B GLU C  1  199 ? -7.153  15.624  20.139 0.50 43.80  ? 212 GLU C OE1 1 
ATOM   6807 O  OE2 A GLU C  1  199 ? -5.263  13.068  18.989 0.50 38.03  ? 212 GLU C OE2 1 
ATOM   6808 O  OE2 B GLU C  1  199 ? -7.808  17.684  20.444 0.50 46.05  ? 212 GLU C OE2 1 
ATOM   6809 N  N   . THR C  1  200 ? -8.499  18.087  15.335 1.00 39.85  ? 213 THR C N   1 
ATOM   6810 C  CA  . THR C  1  200 ? -9.567  19.074  15.178 1.00 49.08  ? 213 THR C CA  1 
ATOM   6811 C  C   . THR C  1  200 ? -10.135 19.066  13.759 1.00 50.75  ? 213 THR C C   1 
ATOM   6812 O  O   . THR C  1  200 ? -11.230 19.587  13.560 1.00 44.72  ? 213 THR C O   1 
ATOM   6813 C  CB  . THR C  1  200 ? -9.129  20.489  15.567 1.00 52.28  ? 213 THR C CB  1 
ATOM   6814 O  OG1 . THR C  1  200 ? -8.276  21.010  14.555 1.00 52.16  ? 213 THR C OG1 1 
ATOM   6815 C  CG2 . THR C  1  200 ? -8.440  20.521  16.915 1.00 53.20  ? 213 THR C CG2 1 
ATOM   6816 N  N   . VAL C  1  201 ? -9.426  18.464  12.786 1.00 50.13  ? 214 VAL C N   1 
ATOM   6817 C  CA  . VAL C  1  201 ? -9.960  18.351  11.433 1.00 45.24  ? 214 VAL C CA  1 
ATOM   6818 C  C   . VAL C  1  201 ? -10.510 16.954  11.149 1.00 42.69  ? 214 VAL C C   1 
ATOM   6819 O  O   . VAL C  1  201 ? -11.293 16.791  10.218 1.00 44.06  ? 214 VAL C O   1 
ATOM   6820 C  CB  . VAL C  1  201 ? -8.952  18.780  10.357 1.00 45.50  ? 214 VAL C CB  1 
ATOM   6821 C  CG1 . VAL C  1  201 ? -8.618  20.254  10.512 1.00 45.41  ? 214 VAL C CG1 1 
ATOM   6822 C  CG2 . VAL C  1  201 ? -7.685  17.928  10.348 1.00 42.16  ? 214 VAL C CG2 1 
ATOM   6823 N  N   . PHE C  1  202 ? -10.157 15.949  11.956 1.00 39.06  ? 215 PHE C N   1 
ATOM   6824 C  CA  . PHE C  1  202 ? -10.710 14.624  11.737 1.00 42.22  ? 215 PHE C CA  1 
ATOM   6825 C  C   . PHE C  1  202 ? -12.242 14.660  11.699 1.00 44.85  ? 215 PHE C C   1 
ATOM   6826 O  O   . PHE C  1  202 ? -12.849 13.936  10.912 1.00 42.41  ? 215 PHE C O   1 
ATOM   6827 C  CB  . PHE C  1  202 ? -10.248 13.593  12.771 1.00 41.58  ? 215 PHE C CB  1 
ATOM   6828 C  CG  . PHE C  1  202 ? -8.769  13.237  12.736 1.00 39.56  ? 215 PHE C CG  1 
ATOM   6829 C  CD1 . PHE C  1  202 ? -7.949  13.592  11.672 1.00 36.69  ? 215 PHE C CD1 1 
ATOM   6830 C  CD2 . PHE C  1  202 ? -8.204  12.531  13.789 1.00 38.09  ? 215 PHE C CD2 1 
ATOM   6831 C  CE1 . PHE C  1  202 ? -6.598  13.268  11.674 1.00 38.76  ? 215 PHE C CE1 1 
ATOM   6832 C  CE2 . PHE C  1  202 ? -6.861  12.195  13.781 1.00 42.00  ? 215 PHE C CE2 1 
ATOM   6833 C  CZ  . PHE C  1  202 ? -6.056  12.569  12.735 1.00 42.28  ? 215 PHE C CZ  1 
ATOM   6834 N  N   . PRO C  1  203 ? -12.957 15.431  12.542 1.00 43.67  ? 216 PRO C N   1 
ATOM   6835 C  CA  . PRO C  1  203 ? -14.418 15.464  12.453 1.00 43.70  ? 216 PRO C CA  1 
ATOM   6836 C  C   . PRO C  1  203 ? -14.921 15.941  11.090 1.00 43.26  ? 216 PRO C C   1 
ATOM   6837 O  O   . PRO C  1  203 ? -15.961 15.491  10.638 1.00 49.96  ? 216 PRO C O   1 
ATOM   6838 C  CB  . PRO C  1  203 ? -14.848 16.394  13.603 1.00 43.51  ? 216 PRO C CB  1 
ATOM   6839 C  CG  . PRO C  1  203 ? -13.679 16.365  14.561 1.00 43.46  ? 216 PRO C CG  1 
ATOM   6840 C  CD  . PRO C  1  203 ? -12.447 16.237  13.653 1.00 45.60  ? 216 PRO C CD  1 
ATOM   6841 N  N   . ILE C  1  204 ? -14.184 16.841  10.440 1.00 39.97  ? 217 ILE C N   1 
ATOM   6842 C  CA  . ILE C  1  204 ? -14.559 17.330  9.124  1.00 42.44  ? 217 ILE C CA  1 
ATOM   6843 C  C   . ILE C  1  204 ? -14.227 16.283  8.060  1.00 43.43  ? 217 ILE C C   1 
ATOM   6844 O  O   . ILE C  1  204 ? -15.051 15.988  7.205  1.00 41.35  ? 217 ILE C O   1 
ATOM   6845 C  CB  . ILE C  1  204 ? -13.865 18.667  8.823  1.00 44.73  ? 217 ILE C CB  1 
ATOM   6846 C  CG1 . ILE C  1  204 ? -14.219 19.722  9.891  1.00 49.82  ? 217 ILE C CG1 1 
ATOM   6847 C  CG2 . ILE C  1  204 ? -14.198 19.140  7.408  1.00 46.23  ? 217 ILE C CG2 1 
ATOM   6848 C  CD1 . ILE C  1  204 ? -13.295 20.922  9.903  1.00 51.21  ? 217 ILE C CD1 1 
ATOM   6849 N  N   . ASN C  1  205 ? -13.011 15.729  8.106  1.00 40.24  ? 218 ASN C N   1 
ATOM   6850 C  CA  . ASN C  1  205 ? -12.519 14.885  7.026  1.00 38.08  ? 218 ASN C CA  1 
ATOM   6851 C  C   . ASN C  1  205 ? -13.113 13.490  7.111  1.00 36.72  ? 218 ASN C C   1 
ATOM   6852 O  O   . ASN C  1  205 ? -13.274 12.855  6.076  1.00 38.69  ? 218 ASN C O   1 
ATOM   6853 C  CB  . ASN C  1  205 ? -10.997 14.815  7.017  1.00 38.11  ? 218 ASN C CB  1 
ATOM   6854 C  CG  . ASN C  1  205 ? -10.397 16.185  6.818  1.00 39.35  ? 218 ASN C CG  1 
ATOM   6855 O  OD1 . ASN C  1  205 ? -11.040 17.057  6.223  1.00 42.73  ? 218 ASN C OD1 1 
ATOM   6856 N  ND2 . ASN C  1  205 ? -9.189  16.408  7.312  1.00 39.72  ? 218 ASN C ND2 1 
ATOM   6857 N  N   . LEU C  1  206 ? -13.417 13.013  8.333  1.00 34.03  ? 219 LEU C N   1 
ATOM   6858 C  CA  . LEU C  1  206 ? -13.766 11.618  8.533  1.00 33.00  ? 219 LEU C CA  1 
ATOM   6859 C  C   . LEU C  1  206 ? -15.163 11.415  9.120  1.00 34.56  ? 219 LEU C C   1 
ATOM   6860 O  O   . LEU C  1  206 ? -15.732 10.340  8.936  1.00 35.62  ? 219 LEU C O   1 
ATOM   6861 C  CB  . LEU C  1  206 ? -12.695 10.975  9.407  1.00 34.47  ? 219 LEU C CB  1 
ATOM   6862 C  CG  . LEU C  1  206 ? -11.269 11.058  8.849  1.00 38.31  ? 219 LEU C CG  1 
ATOM   6863 C  CD1 . LEU C  1  206 ? -10.238 10.701  9.879  1.00 38.13  ? 219 LEU C CD1 1 
ATOM   6864 C  CD2 . LEU C  1  206 ? -11.106 10.164  7.637  1.00 39.08  ? 219 LEU C CD2 1 
ATOM   6865 N  N   . PHE C  1  207 ? -15.705 12.385  9.871  1.00 40.97  ? 220 PHE C N   1 
ATOM   6866 C  CA  . PHE C  1  207 ? -17.009 12.185  10.504 1.00 38.73  ? 220 PHE C CA  1 
ATOM   6867 C  C   . PHE C  1  207 ? -18.145 12.736  9.638  1.00 40.62  ? 220 PHE C C   1 
ATOM   6868 O  O   . PHE C  1  207 ? -19.301 12.391  9.861  1.00 40.22  ? 220 PHE C O   1 
ATOM   6869 C  CB  . PHE C  1  207 ? -17.153 12.825  11.886 1.00 41.74  ? 220 PHE C CB  1 
ATOM   6870 C  CG  . PHE C  1  207 ? -16.272 12.242  12.979 1.00 44.03  ? 220 PHE C CG  1 
ATOM   6871 C  CD1 . PHE C  1  207 ? -15.608 11.028  12.813 1.00 42.21  ? 220 PHE C CD1 1 
ATOM   6872 C  CD2 . PHE C  1  207 ? -16.135 12.909  14.191 1.00 46.11  ? 220 PHE C CD2 1 
ATOM   6873 C  CE1 . PHE C  1  207 ? -14.813 10.512  13.828 1.00 42.06  ? 220 PHE C CE1 1 
ATOM   6874 C  CE2 . PHE C  1  207 ? -15.313 12.408  15.190 1.00 43.97  ? 220 PHE C CE2 1 
ATOM   6875 C  CZ  . PHE C  1  207 ? -14.665 11.204  15.016 1.00 42.57  ? 220 PHE C CZ  1 
ATOM   6876 N  N   . VAL C  1  208 ? -17.815 13.584  8.668  1.00 39.48  ? 221 VAL C N   1 
ATOM   6877 C  CA  . VAL C  1  208 ? -18.780 14.032  7.677  1.00 43.80  ? 221 VAL C CA  1 
ATOM   6878 C  C   . VAL C  1  208 ? -18.925 12.948  6.621  1.00 43.85  ? 221 VAL C C   1 
ATOM   6879 O  O   . VAL C  1  208 ? -17.937 12.394  6.143  1.00 41.71  ? 221 VAL C O   1 
ATOM   6880 C  CB  . VAL C  1  208 ? -18.347 15.364  7.051  1.00 42.92  ? 221 VAL C CB  1 
ATOM   6881 C  CG1 . VAL C  1  208 ? -19.270 15.791  5.917  1.00 50.56  ? 221 VAL C CG1 1 
ATOM   6882 C  CG2 . VAL C  1  208 ? -18.262 16.448  8.111  1.00 44.32  ? 221 VAL C CG2 1 
ATOM   6883 N  N   . ASP C  1  209 ? -20.177 12.688  6.251  1.00 42.90  ? 222 ASP C N   1 
ATOM   6884 C  CA  . ASP C  1  209 ? -20.531 11.626  5.332  1.00 45.18  ? 222 ASP C CA  1 
ATOM   6885 C  C   . ASP C  1  209 ? -19.770 11.805  4.019  1.00 41.66  ? 222 ASP C C   1 
ATOM   6886 O  O   . ASP C  1  209 ? -19.653 12.916  3.519  1.00 39.90  ? 222 ASP C O   1 
ATOM   6887 C  CB  . ASP C  1  209 ? -22.038 11.596  5.144  1.00 44.34  ? 222 ASP C CB  1 
ATOM   6888 C  CG  . ASP C  1  209 ? -22.532 10.398  4.360  1.00 45.61  ? 222 ASP C CG  1 
ATOM   6889 O  OD1 . ASP C  1  209 ? -22.268 10.370  3.132  1.00 46.42  ? 222 ASP C OD1 1 
ATOM   6890 O  OD2 . ASP C  1  209 ? -23.111 9.481   4.984  1.00 41.29  ? 222 ASP C OD2 1 
ATOM   6891 N  N   . GLY C  1  210 ? -19.279 10.694  3.462  1.00 39.24  ? 223 GLY C N   1 
ATOM   6892 C  CA  . GLY C  1  210 ? -18.439 10.738  2.268  1.00 44.53  ? 223 GLY C CA  1 
ATOM   6893 C  C   . GLY C  1  210 ? -19.210 11.125  0.996  1.00 46.55  ? 223 GLY C C   1 
ATOM   6894 O  O   . GLY C  1  210 ? -18.601 11.443  -0.015 1.00 45.45  ? 223 GLY C O   1 
ATOM   6895 N  N   . ARG C  1  211 ? -20.551 11.092  1.035  1.00 45.87  ? 224 ARG C N   1 
ATOM   6896 C  CA  . ARG C  1  211 ? -21.368 11.549  -0.080 1.00 43.56  ? 224 ARG C CA  1 
ATOM   6897 C  C   . ARG C  1  211 ? -21.447 13.072  -0.114 1.00 45.65  ? 224 ARG C C   1 
ATOM   6898 O  O   . ARG C  1  211 ? -21.902 13.622  -1.106 1.00 49.10  ? 224 ARG C O   1 
ATOM   6899 C  CB  . ARG C  1  211 ? -22.776 10.956  -0.032 1.00 41.78  ? 224 ARG C CB  1 
ATOM   6900 C  CG  . ARG C  1  211 ? -22.767 9.455   -0.263 1.00 42.64  ? 224 ARG C CG  1 
ATOM   6901 C  CD  . ARG C  1  211 ? -24.066 8.805   0.144  1.00 48.88  ? 224 ARG C CD  1 
ATOM   6902 N  NE  . ARG C  1  211 ? -24.301 8.949   1.587  1.00 50.58  ? 224 ARG C NE  1 
ATOM   6903 C  CZ  . ARG C  1  211 ? -25.317 8.405   2.257  1.00 53.07  ? 224 ARG C CZ  1 
ATOM   6904 N  NH1 . ARG C  1  211 ? -26.235 7.698   1.629  1.00 50.49  ? 224 ARG C NH1 1 
ATOM   6905 N  NH2 . ARG C  1  211 ? -25.414 8.566   3.565  1.00 54.94  ? 224 ARG C NH2 1 
ATOM   6906 N  N   . VAL C  1  212 ? -20.990 13.754  0.939  1.00 44.51  ? 225 VAL C N   1 
ATOM   6907 C  CA  . VAL C  1  212 ? -20.975 15.206  0.946  1.00 50.12  ? 225 VAL C CA  1 
ATOM   6908 C  C   . VAL C  1  212 ? -19.662 15.690  0.330  1.00 57.48  ? 225 VAL C C   1 
ATOM   6909 O  O   . VAL C  1  212 ? -18.603 15.554  0.937  1.00 57.89  ? 225 VAL C O   1 
ATOM   6910 C  CB  . VAL C  1  212 ? -21.153 15.747  2.378  1.00 50.61  ? 225 VAL C CB  1 
ATOM   6911 C  CG1 . VAL C  1  212 ? -21.040 17.269  2.447  1.00 49.99  ? 225 VAL C CG1 1 
ATOM   6912 C  CG2 . VAL C  1  212 ? -22.456 15.261  2.999  1.00 51.32  ? 225 VAL C CG2 1 
ATOM   6913 N  N   . THR C  1  213 ? -19.755 16.293  -0.864 1.00 64.16  ? 226 THR C N   1 
ATOM   6914 C  CA  . THR C  1  213 ? -18.588 16.643  -1.661 1.00 69.69  ? 226 THR C CA  1 
ATOM   6915 C  C   . THR C  1  213 ? -18.211 18.111  -1.462 1.00 72.48  ? 226 THR C C   1 
ATOM   6916 O  O   . THR C  1  213 ? -17.047 18.473  -1.606 1.00 72.73  ? 226 THR C O   1 
ATOM   6917 C  CB  . THR C  1  213 ? -18.877 16.333  -3.132 1.00 74.59  ? 226 THR C CB  1 
ATOM   6918 O  OG1 . THR C  1  213 ? -20.032 17.069  -3.528 1.00 72.31  ? 226 THR C OG1 1 
ATOM   6919 C  CG2 . THR C  1  213 ? -19.157 14.861  -3.387 1.00 72.07  ? 226 THR C CG2 1 
ATOM   6920 N  N   . THR C  1  214 ? -19.191 18.952  -1.116 1.00 75.68  ? 227 THR C N   1 
ATOM   6921 C  CA  . THR C  1  214 ? -18.982 20.388  -1.056 1.00 75.84  ? 227 THR C CA  1 
ATOM   6922 C  C   . THR C  1  214 ? -19.382 20.916  0.325  1.00 76.99  ? 227 THR C C   1 
ATOM   6923 O  O   . THR C  1  214 ? -20.386 20.478  0.904  1.00 70.27  ? 227 THR C O   1 
ATOM   6924 C  CB  . THR C  1  214 ? -19.788 21.033  -2.186 1.00 78.17  ? 227 THR C CB  1 
ATOM   6925 O  OG1 . THR C  1  214 ? -19.365 22.391  -2.148 1.00 84.67  ? 227 THR C OG1 1 
ATOM   6926 C  CG2 . THR C  1  214 ? -21.296 20.903  -2.019 1.00 75.28  ? 227 THR C CG2 1 
ATOM   6927 N  N   . ASP C  1  215 ? -18.599 21.877  0.842  1.00 76.95  ? 228 ASP C N   1 
ATOM   6928 C  CA  . ASP C  1  215 ? -18.962 22.597  2.053  1.00 79.87  ? 228 ASP C CA  1 
ATOM   6929 C  C   . ASP C  1  215 ? -19.124 21.581  3.183  1.00 72.08  ? 228 ASP C C   1 
ATOM   6930 O  O   . ASP C  1  215 ? -20.198 21.443  3.767  1.00 75.62  ? 228 ASP C O   1 
ATOM   6931 C  CB  . ASP C  1  215 ? -20.196 23.458  1.799  1.00 91.09  ? 228 ASP C CB  1 
ATOM   6932 C  CG  . ASP C  1  215 ? -20.753 24.252  2.977  1.00 94.90  ? 228 ASP C CG  1 
ATOM   6933 O  OD1 . ASP C  1  215 ? -20.048 24.352  4.002  1.00 101.60 ? 228 ASP C OD1 1 
ATOM   6934 O  OD2 . ASP C  1  215 ? -21.909 24.711  2.882  1.00 92.59  ? 228 ASP C OD2 1 
ATOM   6935 N  N   . ARG C  1  216 ? -18.050 20.845  3.462  1.00 64.19  ? 229 ARG C N   1 
ATOM   6936 C  CA  . ARG C  1  216 ? -18.120 19.745  4.409  1.00 59.84  ? 229 ARG C CA  1 
ATOM   6937 C  C   . ARG C  1  216 ? -18.223 20.313  5.825  1.00 49.15  ? 229 ARG C C   1 
ATOM   6938 O  O   . ARG C  1  216 ? -17.432 21.156  6.228  1.00 52.68  ? 229 ARG C O   1 
ATOM   6939 C  CB  . ARG C  1  216 ? -16.941 18.789  4.183  1.00 58.50  ? 229 ARG C CB  1 
ATOM   6940 C  CG  . ARG C  1  216 ? -17.100 17.958  2.918  1.00 58.05  ? 229 ARG C CG  1 
ATOM   6941 C  CD  . ARG C  1  216 ? -15.865 17.134  2.576  1.00 55.41  ? 229 ARG C CD  1 
ATOM   6942 N  NE  . ARG C  1  216 ? -15.560 16.123  3.594  1.00 51.20  ? 229 ARG C NE  1 
ATOM   6943 C  CZ  . ARG C  1  216 ? -16.203 14.974  3.797  1.00 53.62  ? 229 ARG C CZ  1 
ATOM   6944 N  NH1 . ARG C  1  216 ? -17.146 14.546  2.964  1.00 49.64  ? 229 ARG C NH1 1 
ATOM   6945 N  NH2 . ARG C  1  216 ? -15.877 14.228  4.841  1.00 58.82  ? 229 ARG C NH2 1 
ATOM   6946 N  N   . LYS C  1  217 ? -19.233 19.857  6.564  1.00 52.69  ? 230 LYS C N   1 
ATOM   6947 C  CA  . LYS C  1  217 ? -19.522 20.387  7.884  1.00 53.03  ? 230 LYS C CA  1 
ATOM   6948 C  C   . LYS C  1  217 ? -20.281 19.331  8.678  1.00 48.53  ? 230 LYS C C   1 
ATOM   6949 O  O   . LYS C  1  217 ? -21.064 18.577  8.110  1.00 50.69  ? 230 LYS C O   1 
ATOM   6950 C  CB  . LYS C  1  217 ? -20.345 21.666  7.715  1.00 62.09  ? 230 LYS C CB  1 
ATOM   6951 C  CG  . LYS C  1  217 ? -21.732 21.449  7.128  1.00 64.73  ? 230 LYS C CG  1 
ATOM   6952 C  CD  . LYS C  1  217 ? -22.487 22.733  6.784  1.00 70.40  ? 230 LYS C CD  1 
ATOM   6953 C  CE  . LYS C  1  217 ? -23.904 22.439  6.408  1.00 69.59  ? 230 LYS C CE  1 
ATOM   6954 N  NZ  . LYS C  1  217 ? -24.558 23.631  5.872  1.00 71.17  ? 230 LYS C NZ  1 
ATOM   6955 N  N   . LEU C  1  218 ? -20.057 19.285  9.994  1.00 49.13  ? 231 LEU C N   1 
ATOM   6956 C  CA  . LEU C  1  218 ? -20.618 18.230  10.823 1.00 55.85  ? 231 LEU C CA  1 
ATOM   6957 C  C   . LEU C  1  218 ? -21.777 18.776  11.663 1.00 55.93  ? 231 LEU C C   1 
ATOM   6958 O  O   . LEU C  1  218 ? -21.613 19.764  12.366 1.00 57.12  ? 231 LEU C O   1 
ATOM   6959 C  CB  . LEU C  1  218 ? -19.494 17.685  11.701 1.00 49.10  ? 231 LEU C CB  1 
ATOM   6960 C  CG  . LEU C  1  218 ? -19.857 16.489  12.587 1.00 51.44  ? 231 LEU C CG  1 
ATOM   6961 C  CD1 . LEU C  1  218 ? -20.169 15.245  11.767 1.00 52.65  ? 231 LEU C CD1 1 
ATOM   6962 C  CD2 . LEU C  1  218 ? -18.736 16.219  13.572 1.00 51.49  ? 231 LEU C CD2 1 
ATOM   6963 N  N   . SER C  1  219 ? -22.921 18.084  11.638 1.00 55.68  ? 232 SER C N   1 
ATOM   6964 C  CA  . SER C  1  219 ? -24.061 18.454  12.464 1.00 54.27  ? 232 SER C CA  1 
ATOM   6965 C  C   . SER C  1  219 ? -23.801 18.090  13.928 1.00 60.71  ? 232 SER C C   1 
ATOM   6966 O  O   . SER C  1  219 ? -22.997 17.208  14.222 1.00 57.38  ? 232 SER C O   1 
ATOM   6967 C  CB  . SER C  1  219 ? -25.324 17.799  11.976 1.00 49.93  ? 232 SER C CB  1 
ATOM   6968 O  OG  . SER C  1  219 ? -25.386 16.432  12.360 1.00 52.71  ? 232 SER C OG  1 
ATOM   6969 N  N   . MET C  1  220 ? -24.515 18.752  14.845 1.00 51.09  ? 233 MET C N   1 
ATOM   6970 C  CA  . MET C  1  220 ? -24.316 18.520  16.262 1.00 51.05  ? 233 MET C CA  1 
ATOM   6971 C  C   . MET C  1  220 ? -24.876 17.155  16.653 1.00 55.75  ? 233 MET C C   1 
ATOM   6972 O  O   . MET C  1  220 ? -24.369 16.524  17.580 1.00 59.35  ? 233 MET C O   1 
ATOM   6973 C  CB  . MET C  1  220 ? -24.963 19.638  17.091 1.00 57.08  ? 233 MET C CB  1 
ATOM   6974 C  CG  . MET C  1  220 ? -24.354 21.020  16.883 1.00 55.61  ? 233 MET C CG  1 
ATOM   6975 S  SD  . MET C  1  220 ? -22.574 21.062  17.187 1.00 62.10  ? 233 MET C SD  1 
ATOM   6976 C  CE  . MET C  1  220 ? -21.928 20.958  15.509 1.00 63.77  ? 233 MET C CE  1 
ATOM   6977 N  N   . GLU C  1  221 ? -25.902 16.691  15.932 1.00 49.79  ? 234 GLU C N   1 
ATOM   6978 C  CA  . GLU C  1  221 ? -26.480 15.375  16.164 1.00 57.23  ? 234 GLU C CA  1 
ATOM   6979 C  C   . GLU C  1  221 ? -25.440 14.295  15.864 1.00 51.35  ? 234 GLU C C   1 
ATOM   6980 O  O   . GLU C  1  221 ? -25.284 13.350  16.631 1.00 50.41  ? 234 GLU C O   1 
ATOM   6981 C  CB  . GLU C  1  221 ? -27.719 15.141  15.291 1.00 63.48  ? 234 GLU C CB  1 
ATOM   6982 C  CG  . GLU C  1  221 ? -28.904 16.052  15.610 1.00 79.89  ? 234 GLU C CG  1 
ATOM   6983 C  CD  . GLU C  1  221 ? -28.870 17.519  15.171 1.00 89.36  ? 234 GLU C CD  1 
ATOM   6984 O  OE1 . GLU C  1  221 ? -27.963 17.990  14.426 1.00 79.17  ? 234 GLU C OE1 1 
ATOM   6985 O  OE2 . GLU C  1  221 ? -29.795 18.218  15.637 1.00 103.26 ? 234 GLU C OE2 1 
ATOM   6986 N  N   . ASP C  1  222 ? -24.767 14.421  14.722 1.00 47.66  ? 235 ASP C N   1 
ATOM   6987 C  CA  . ASP C  1  222 ? -23.748 13.471  14.301 1.00 54.91  ? 235 ASP C CA  1 
ATOM   6988 C  C   . ASP C  1  222 ? -22.547 13.537  15.247 1.00 47.50  ? 235 ASP C C   1 
ATOM   6989 O  O   . ASP C  1  222 ? -22.020 12.502  15.637 1.00 45.81  ? 235 ASP C O   1 
ATOM   6990 C  CB  . ASP C  1  222 ? -23.369 13.695  12.846 1.00 54.70  ? 235 ASP C CB  1 
ATOM   6991 C  CG  . ASP C  1  222 ? -24.458 13.367  11.831 1.00 60.13  ? 235 ASP C CG  1 
ATOM   6992 O  OD1 . ASP C  1  222 ? -25.482 12.751  12.238 1.00 62.82  ? 235 ASP C OD1 1 
ATOM   6993 O  OD2 . ASP C  1  222 ? -24.317 13.820  10.674 1.00 55.19  ? 235 ASP C OD2 1 
ATOM   6994 N  N   . ALA C  1  223 ? -22.139 14.748  15.619 1.00 43.83  ? 236 ALA C N   1 
ATOM   6995 C  CA  . ALA C  1  223 ? -21.069 14.927  16.586 1.00 50.14  ? 236 ALA C CA  1 
ATOM   6996 C  C   . ALA C  1  223 ? -21.387 14.211  17.899 1.00 56.52  ? 236 ALA C C   1 
ATOM   6997 O  O   . ALA C  1  223 ? -20.545 13.478  18.416 1.00 53.50  ? 236 ALA C O   1 
ATOM   6998 C  CB  . ALA C  1  223 ? -20.799 16.398  16.804 1.00 50.02  ? 236 ALA C CB  1 
ATOM   6999 N  N   . ALA C  1  224 ? -22.600 14.393  18.439 1.00 49.25  ? 237 ALA C N   1 
ATOM   7000 C  CA  . ALA C  1  224 ? -22.918 13.795  19.728 1.00 50.90  ? 237 ALA C CA  1 
ATOM   7001 C  C   . ALA C  1  224 ? -22.916 12.280  19.607 1.00 49.61  ? 237 ALA C C   1 
ATOM   7002 O  O   . ALA C  1  224 ? -22.431 11.565  20.483 1.00 47.68  ? 237 ALA C O   1 
ATOM   7003 C  CB  . ALA C  1  224 ? -24.271 14.275  20.236 1.00 54.61  ? 237 ALA C CB  1 
ATOM   7004 N  N   . SER C  1  225 ? -23.487 11.803  18.500 1.00 45.48  ? 238 SER C N   1 
ATOM   7005 C  CA  . SER C  1  225 ? -23.587 10.380  18.244 1.00 45.85  ? 238 SER C CA  1 
ATOM   7006 C  C   . SER C  1  225 ? -22.203 9.726   18.328 1.00 41.10  ? 238 SER C C   1 
ATOM   7007 O  O   . SER C  1  225 ? -22.057 8.686   18.953 1.00 39.55  ? 238 SER C O   1 
ATOM   7008 C  CB  . SER C  1  225 ? -24.257 10.163  16.895 1.00 44.15  ? 238 SER C CB  1 
ATOM   7009 O  OG  . SER C  1  225 ? -24.442 8.784   16.645 1.00 42.05  ? 238 SER C OG  1 
ATOM   7010 N  N   . ILE C  1  226 ? -21.187 10.347  17.729 1.00 42.28  ? 239 ILE C N   1 
ATOM   7011 C  CA  . ILE C  1  226 ? -19.853 9.762   17.652 1.00 43.14  ? 239 ILE C CA  1 
ATOM   7012 C  C   . ILE C  1  226 ? -19.072 10.026  18.942 1.00 41.52  ? 239 ILE C C   1 
ATOM   7013 O  O   . ILE C  1  226 ? -18.574 9.082   19.556 1.00 43.11  ? 239 ILE C O   1 
ATOM   7014 C  CB  . ILE C  1  226 ? -19.109 10.270  16.403 1.00 44.99  ? 239 ILE C CB  1 
ATOM   7015 C  CG1 . ILE C  1  226 ? -19.788 9.748   15.132 1.00 46.29  ? 239 ILE C CG1 1 
ATOM   7016 C  CG2 . ILE C  1  226 ? -17.630 9.874   16.440 1.00 44.18  ? 239 ILE C CG2 1 
ATOM   7017 C  CD1 . ILE C  1  226 ? -19.407 10.514  13.879 1.00 45.00  ? 239 ILE C CD1 1 
ATOM   7018 N  N   . PHE C  1  227 ? -18.980 11.295  19.350 1.00 39.79  ? 240 PHE C N   1 
ATOM   7019 C  CA  . PHE C  1  227 ? -18.181 11.691  20.501 1.00 46.22  ? 240 PHE C CA  1 
ATOM   7020 C  C   . PHE C  1  227 ? -18.740 11.141  21.814 1.00 48.24  ? 240 PHE C C   1 
ATOM   7021 O  O   . PHE C  1  227 ? -17.967 10.798  22.708 1.00 45.43  ? 240 PHE C O   1 
ATOM   7022 C  CB  . PHE C  1  227 ? -18.095 13.212  20.597 1.00 44.15  ? 240 PHE C CB  1 
ATOM   7023 C  CG  . PHE C  1  227 ? -17.148 13.901  19.630 1.00 45.86  ? 240 PHE C CG  1 
ATOM   7024 C  CD1 . PHE C  1  227 ? -15.771 13.872  19.841 1.00 48.41  ? 240 PHE C CD1 1 
ATOM   7025 C  CD2 . PHE C  1  227 ? -17.627 14.667  18.580 1.00 50.31  ? 240 PHE C CD2 1 
ATOM   7026 C  CE1 . PHE C  1  227 ? -14.907 14.555  18.997 1.00 47.00  ? 240 PHE C CE1 1 
ATOM   7027 C  CE2 . PHE C  1  227 ? -16.759 15.342  17.738 1.00 52.69  ? 240 PHE C CE2 1 
ATOM   7028 C  CZ  . PHE C  1  227 ? -15.402 15.294  17.950 1.00 51.09  ? 240 PHE C CZ  1 
ATOM   7029 N  N   . ARG C  1  228 ? -20.074 11.091  21.953 1.00 47.16  ? 241 ARG C N   1 
ATOM   7030 C  CA  . ARG C  1  228 ? -20.672 10.644  23.200 1.00 42.75  ? 241 ARG C CA  1 
ATOM   7031 C  C   . ARG C  1  228 ? -21.053 9.180   23.081 1.00 45.28  ? 241 ARG C C   1 
ATOM   7032 O  O   . ARG C  1  228 ? -20.636 8.362   23.897 1.00 38.51  ? 241 ARG C O   1 
ATOM   7033 C  CB  . ARG C  1  228 ? -21.887 11.481  23.621 1.00 50.76  ? 241 ARG C CB  1 
ATOM   7034 C  CG  . ARG C  1  228 ? -22.487 11.084  24.967 1.00 55.69  ? 241 ARG C CG  1 
ATOM   7035 C  CD  . ARG C  1  228 ? -23.612 12.037  25.366 1.00 61.27  ? 241 ARG C CD  1 
ATOM   7036 N  NE  . ARG C  1  228 ? -24.823 11.670  24.621 1.00 63.55  ? 241 ARG C NE  1 
ATOM   7037 C  CZ  . ARG C  1  228 ? -25.587 12.438  23.847 1.00 69.19  ? 241 ARG C CZ  1 
ATOM   7038 N  NH1 . ARG C  1  228 ? -25.319 13.724  23.677 1.00 64.52  ? 241 ARG C NH1 1 
ATOM   7039 N  NH2 . ARG C  1  228 ? -26.634 11.894  23.248 1.00 69.45  ? 241 ARG C NH2 1 
ATOM   7040 N  N   . ASP C  1  229 ? -21.839 8.827   22.054 1.00 42.35  ? 242 ASP C N   1 
ATOM   7041 C  CA  . ASP C  1  229 ? -22.483 7.524   22.045 1.00 44.46  ? 242 ASP C CA  1 
ATOM   7042 C  C   . ASP C  1  229 ? -21.682 6.453   21.315 1.00 41.91  ? 242 ASP C C   1 
ATOM   7043 O  O   . ASP C  1  229 ? -22.048 5.281   21.375 1.00 39.10  ? 242 ASP C O   1 
ATOM   7044 C  CB  . ASP C  1  229 ? -23.911 7.663   21.541 1.00 53.73  ? 242 ASP C CB  1 
ATOM   7045 C  CG  . ASP C  1  229 ? -24.810 8.405   22.530 1.00 56.00  ? 242 ASP C CG  1 
ATOM   7046 O  OD1 . ASP C  1  229 ? -24.714 8.045   23.727 1.00 53.49  ? 242 ASP C OD1 1 
ATOM   7047 O  OD2 . ASP C  1  229 ? -25.525 9.362   22.117 1.00 64.01  ? 242 ASP C OD2 1 
ATOM   7048 N  N   . MET C  1  230 ? -20.578 6.836   20.659 1.00 43.30  ? 243 MET C N   1 
ATOM   7049 C  CA  A MET C  1  230 ? -19.714 5.882   19.980 0.50 40.13  ? 243 MET C CA  1 
ATOM   7050 C  CA  B MET C  1  230 ? -19.716 5.884   19.981 0.50 42.05  ? 243 MET C CA  1 
ATOM   7051 C  C   . MET C  1  230 ? -20.493 5.185   18.866 1.00 37.22  ? 243 MET C C   1 
ATOM   7052 O  O   . MET C  1  230 ? -20.341 3.968   18.662 1.00 37.63  ? 243 MET C O   1 
ATOM   7053 C  CB  A MET C  1  230 ? -19.175 4.836   20.957 0.50 39.39  ? 243 MET C CB  1 
ATOM   7054 C  CB  B MET C  1  230 ? -19.197 4.828   20.964 0.50 44.26  ? 243 MET C CB  1 
ATOM   7055 C  CG  A MET C  1  230 ? -18.563 5.424   22.217 0.50 40.17  ? 243 MET C CG  1 
ATOM   7056 C  CG  B MET C  1  230 ? -18.579 5.390   22.226 0.50 47.92  ? 243 MET C CG  1 
ATOM   7057 S  SD  A MET C  1  230 ? -18.136 4.142   23.405 0.50 36.50  ? 243 MET C SD  1 
ATOM   7058 S  SD  B MET C  1  230 ? -18.199 4.014   23.321 0.50 49.44  ? 243 MET C SD  1 
ATOM   7059 C  CE  A MET C  1  230 ? -17.808 5.153   24.861 0.50 36.57  ? 243 MET C CE  1 
ATOM   7060 C  CE  B MET C  1  230 ? -19.843 3.667   23.955 0.50 57.51  ? 243 MET C CE  1 
ATOM   7061 N  N   . ARG C  1  231 ? -21.317 5.962   18.152 1.00 39.38  ? 244 ARG C N   1 
ATOM   7062 C  CA  A ARG C  1  231 ? -22.268 5.424   17.193 0.50 40.56  ? 244 ARG C CA  1 
ATOM   7063 C  CA  B ARG C  1  231 ? -22.249 5.408   17.187 0.50 37.93  ? 244 ARG C CA  1 
ATOM   7064 C  C   . ARG C  1  231 ? -22.183 6.213   15.893 1.00 36.41  ? 244 ARG C C   1 
ATOM   7065 O  O   . ARG C  1  231 ? -22.249 7.450   15.890 1.00 34.42  ? 244 ARG C O   1 
ATOM   7066 C  CB  A ARG C  1  231 ? -23.694 5.499   17.761 0.50 45.63  ? 244 ARG C CB  1 
ATOM   7067 C  CB  B ARG C  1  231 ? -23.658 5.354   17.795 0.50 38.76  ? 244 ARG C CB  1 
ATOM   7068 C  CG  A ARG C  1  231 ? -24.790 4.846   16.938 0.50 49.26  ? 244 ARG C CG  1 
ATOM   7069 C  CG  B ARG C  1  231 ? -24.695 4.658   16.924 0.50 38.20  ? 244 ARG C CG  1 
ATOM   7070 C  CD  A ARG C  1  231 ? -26.116 5.135   17.657 0.50 55.16  ? 244 ARG C CD  1 
ATOM   7071 C  CD  B ARG C  1  231 ? -25.950 4.291   17.717 0.50 39.84  ? 244 ARG C CD  1 
ATOM   7072 N  NE  A ARG C  1  231 ? -27.097 4.046   17.565 0.50 57.96  ? 244 ARG C NE  1 
ATOM   7073 N  NE  B ARG C  1  231 ? -26.509 5.443   18.438 0.50 37.72  ? 244 ARG C NE  1 
ATOM   7074 C  CZ  A ARG C  1  231 ? -27.685 3.454   18.604 0.50 57.92  ? 244 ARG C CZ  1 
ATOM   7075 C  CZ  B ARG C  1  231 ? -26.828 5.491   19.734 0.50 38.84  ? 244 ARG C CZ  1 
ATOM   7076 N  NH1 A ARG C  1  231 ? -27.494 3.903   19.837 0.50 61.12  ? 244 ARG C NH1 1 
ATOM   7077 N  NH1 B ARG C  1  231 ? -26.720 4.431   20.525 0.50 37.45  ? 244 ARG C NH1 1 
ATOM   7078 N  NH2 A ARG C  1  231 ? -28.466 2.411   18.397 0.50 49.58  ? 244 ARG C NH2 1 
ATOM   7079 N  NH2 B ARG C  1  231 ? -27.283 6.618   20.241 0.50 35.24  ? 244 ARG C NH2 1 
ATOM   7080 N  N   . PHE C  1  232 ? -22.031 5.488   14.784 1.00 39.04  ? 245 PHE C N   1 
ATOM   7081 C  CA  . PHE C  1  232 ? -22.129 6.108   13.471 1.00 41.10  ? 245 PHE C CA  1 
ATOM   7082 C  C   . PHE C  1  232 ? -23.508 6.737   13.286 1.00 41.08  ? 245 PHE C C   1 
ATOM   7083 O  O   . PHE C  1  232 ? -24.512 6.168   13.702 1.00 39.24  ? 245 PHE C O   1 
ATOM   7084 C  CB  . PHE C  1  232 ? -21.957 5.059   12.371 1.00 39.03  ? 245 PHE C CB  1 
ATOM   7085 C  CG  . PHE C  1  232 ? -20.532 4.563   12.174 1.00 37.26  ? 245 PHE C CG  1 
ATOM   7086 C  CD1 . PHE C  1  232 ? -19.539 5.434   11.751 1.00 37.87  ? 245 PHE C CD1 1 
ATOM   7087 C  CD2 . PHE C  1  232 ? -20.219 3.213   12.328 1.00 40.20  ? 245 PHE C CD2 1 
ATOM   7088 C  CE1 . PHE C  1  232 ? -18.259 4.964   11.538 1.00 36.61  ? 245 PHE C CE1 1 
ATOM   7089 C  CE2 . PHE C  1  232 ? -18.938 2.746   12.091 1.00 39.26  ? 245 PHE C CE2 1 
ATOM   7090 C  CZ  . PHE C  1  232 ? -17.963 3.617   11.700 1.00 36.52  ? 245 PHE C CZ  1 
ATOM   7091 N  N   . PRO C  1  233 ? -23.617 7.891   12.606 1.00 43.48  ? 246 PRO C N   1 
ATOM   7092 C  CA  . PRO C  1  233 ? -24.914 8.353   12.103 1.00 47.63  ? 246 PRO C CA  1 
ATOM   7093 C  C   . PRO C  1  233 ? -25.618 7.261   11.307 1.00 49.37  ? 246 PRO C C   1 
ATOM   7094 O  O   . PRO C  1  233 ? -24.979 6.387   10.717 1.00 43.16  ? 246 PRO C O   1 
ATOM   7095 C  CB  . PRO C  1  233 ? -24.553 9.573   11.242 1.00 46.75  ? 246 PRO C CB  1 
ATOM   7096 C  CG  . PRO C  1  233 ? -23.257 10.080  11.868 1.00 45.75  ? 246 PRO C CG  1 
ATOM   7097 C  CD  . PRO C  1  233 ? -22.517 8.821   12.302 1.00 44.49  ? 246 PRO C CD  1 
ATOM   7098 N  N   . ASP C  1  234 ? -26.952 7.294   11.310 1.00 51.06  ? 247 ASP C N   1 
ATOM   7099 C  CA  . ASP C  1  234 ? -27.738 6.380   10.490 1.00 51.62  ? 247 ASP C CA  1 
ATOM   7100 C  C   . ASP C  1  234 ? -27.264 6.484   9.038  1.00 40.50  ? 247 ASP C C   1 
ATOM   7101 O  O   . ASP C  1  234 ? -27.024 7.585   8.554  1.00 38.52  ? 247 ASP C O   1 
ATOM   7102 C  CB  . ASP C  1  234 ? -29.232 6.691   10.549 1.00 59.96  ? 247 ASP C CB  1 
ATOM   7103 C  CG  . ASP C  1  234 ? -29.867 6.594   11.928 1.00 69.26  ? 247 ASP C CG  1 
ATOM   7104 O  OD1 . ASP C  1  234 ? -29.488 5.652   12.643 1.00 71.57  ? 247 ASP C OD1 1 
ATOM   7105 O  OD2 . ASP C  1  234 ? -30.708 7.464   12.277 1.00 73.42  ? 247 ASP C OD2 1 
ATOM   7106 N  N   . ASP C  1  235 ? -27.094 5.328   8.380  1.00 37.27  ? 248 ASP C N   1 
ATOM   7107 C  CA  . ASP C  1  235 ? -26.758 5.278   6.957  1.00 46.94  ? 248 ASP C CA  1 
ATOM   7108 C  C   . ASP C  1  235 ? -25.389 5.917   6.667  1.00 47.01  ? 248 ASP C C   1 
ATOM   7109 O  O   . ASP C  1  235 ? -25.140 6.366   5.549  1.00 43.12  ? 248 ASP C O   1 
ATOM   7110 C  CB  . ASP C  1  235 ? -27.840 5.931   6.099  1.00 46.43  ? 248 ASP C CB  1 
ATOM   7111 C  CG  . ASP C  1  235 ? -27.716 5.680   4.600  1.00 46.70  ? 248 ASP C CG  1 
ATOM   7112 O  OD1 . ASP C  1  235 ? -27.553 4.506   4.226  1.00 41.63  ? 248 ASP C OD1 1 
ATOM   7113 O  OD2 . ASP C  1  235 ? -27.769 6.659   3.822  1.00 44.15  ? 248 ASP C OD2 1 
ATOM   7114 N  N   . PHE C  1  236 ? -24.479 5.939   7.654  1.00 39.67  ? 249 PHE C N   1 
ATOM   7115 C  CA  . PHE C  1  236 ? -23.226 6.660   7.476  1.00 40.32  ? 249 PHE C CA  1 
ATOM   7116 C  C   . PHE C  1  236 ? -22.369 6.020   6.380  1.00 32.87  ? 249 PHE C C   1 
ATOM   7117 O  O   . PHE C  1  236 ? -22.114 4.808   6.411  1.00 34.29  ? 249 PHE C O   1 
ATOM   7118 C  CB  . PHE C  1  236 ? -22.401 6.671   8.764  1.00 39.00  ? 249 PHE C CB  1 
ATOM   7119 C  CG  . PHE C  1  236 ? -21.156 7.536   8.645  1.00 35.66  ? 249 PHE C CG  1 
ATOM   7120 C  CD1 . PHE C  1  236 ? -21.271 8.913   8.574  1.00 36.90  ? 249 PHE C CD1 1 
ATOM   7121 C  CD2 . PHE C  1  236 ? -19.884 6.974   8.647  1.00 39.90  ? 249 PHE C CD2 1 
ATOM   7122 C  CE1 . PHE C  1  236 ? -20.150 9.706   8.490  1.00 39.89  ? 249 PHE C CE1 1 
ATOM   7123 C  CE2 . PHE C  1  236 ? -18.759 7.783   8.554  1.00 36.16  ? 249 PHE C CE2 1 
ATOM   7124 C  CZ  . PHE C  1  236 ? -18.892 9.150   8.482  1.00 37.06  ? 249 PHE C CZ  1 
ATOM   7125 N  N   . HIS C  1  237 ? -21.910 6.860   5.447  1.00 36.57  ? 250 HIS C N   1 
ATOM   7126 C  CA  . HIS C  1  237 ? -20.947 6.460   4.430  1.00 36.69  ? 250 HIS C CA  1 
ATOM   7127 C  C   . HIS C  1  237 ? -19.621 7.145   4.725  1.00 33.96  ? 250 HIS C C   1 
ATOM   7128 O  O   . HIS C  1  237 ? -19.576 8.360   4.891  1.00 35.29  ? 250 HIS C O   1 
ATOM   7129 C  CB  . HIS C  1  237 ? -21.405 6.868   3.020  1.00 39.78  ? 250 HIS C CB  1 
ATOM   7130 C  CG  . HIS C  1  237 ? -22.538 6.060   2.488  1.00 46.21  ? 250 HIS C CG  1 
ATOM   7131 N  ND1 . HIS C  1  237 ? -23.687 5.814   3.212  1.00 49.07  ? 250 HIS C ND1 1 
ATOM   7132 C  CD2 . HIS C  1  237 ? -22.696 5.430   1.305  1.00 49.44  ? 250 HIS C CD2 1 
ATOM   7133 C  CE1 . HIS C  1  237 ? -24.499 5.046   2.493  1.00 52.23  ? 250 HIS C CE1 1 
ATOM   7134 N  NE2 . HIS C  1  237 ? -23.912 4.788   1.336  1.00 52.45  ? 250 HIS C NE2 1 
ATOM   7135 N  N   . ARG C  1  238 ? -18.540 6.362   4.746  1.00 35.15  ? 251 ARG C N   1 
ATOM   7136 C  CA  . ARG C  1  238 ? -17.211 6.887   5.034  1.00 33.55  ? 251 ARG C CA  1 
ATOM   7137 C  C   . ARG C  1  238 ? -16.751 7.814   3.912  1.00 35.80  ? 251 ARG C C   1 
ATOM   7138 O  O   . ARG C  1  238 ? -17.307 7.787   2.811  1.00 35.06  ? 251 ARG C O   1 
ATOM   7139 C  CB  . ARG C  1  238 ? -16.215 5.732   5.174  1.00 34.45  ? 251 ARG C CB  1 
ATOM   7140 C  CG  . ARG C  1  238 ? -15.958 4.978   3.883  1.00 34.17  ? 251 ARG C CG  1 
ATOM   7141 C  CD  . ARG C  1  238 ? -14.979 3.831   4.047  1.00 36.05  ? 251 ARG C CD  1 
ATOM   7142 N  NE  . ARG C  1  238 ? -14.472 3.451   2.727  1.00 35.53  ? 251 ARG C NE  1 
ATOM   7143 C  CZ  . ARG C  1  238 ? -13.756 2.393   2.454  1.00 37.27  ? 251 ARG C CZ  1 
ATOM   7144 N  NH1 . ARG C  1  238 ? -13.455 1.521   3.402  1.00 40.56  ? 251 ARG C NH1 1 
ATOM   7145 N  NH2 . ARG C  1  238 ? -13.407 2.172   1.190  1.00 37.51  ? 251 ARG C NH2 1 
ATOM   7146 N  N   . SER C  1  239 ? -15.719 8.606   4.218  1.00 34.36  ? 252 SER C N   1 
ATOM   7147 C  CA  . SER C  1  239 ? -14.995 9.437   3.270  1.00 35.25  ? 252 SER C CA  1 
ATOM   7148 C  C   . SER C  1  239 ? -14.779 8.686   1.956  1.00 33.63  ? 252 SER C C   1 
ATOM   7149 O  O   . SER C  1  239 ? -14.478 7.491   1.967  1.00 31.79  ? 252 SER C O   1 
ATOM   7150 C  CB  . SER C  1  239 ? -13.658 9.858   3.838  1.00 34.57  ? 252 SER C CB  1 
ATOM   7151 O  OG  . SER C  1  239 ? -12.885 10.577  2.888  1.00 34.65  ? 252 SER C OG  1 
ATOM   7152 N  N   . ALA C  1  240 ? -14.925 9.425   0.849  1.00 35.58  ? 253 ALA C N   1 
ATOM   7153 C  CA  . ALA C  1  240 ? -14.804 8.899   -0.499 1.00 37.20  ? 253 ALA C CA  1 
ATOM   7154 C  C   . ALA C  1  240 ? -13.340 8.706   -0.888 1.00 35.35  ? 253 ALA C C   1 
ATOM   7155 O  O   . ALA C  1  240 ? -13.094 8.141   -1.942 1.00 35.34  ? 253 ALA C O   1 
ATOM   7156 C  CB  . ALA C  1  240 ? -15.496 9.830   -1.488 1.00 38.39  ? 253 ALA C CB  1 
ATOM   7157 N  N   . VAL C  1  241 ? -12.403 9.241   -0.097 1.00 36.15  ? 254 VAL C N   1 
ATOM   7158 C  CA  . VAL C  1  241 ? -10.968 9.102   -0.316 1.00 35.70  ? 254 VAL C CA  1 
ATOM   7159 C  C   . VAL C  1  241 ? -10.282 8.846   1.029  1.00 34.90  ? 254 VAL C C   1 
ATOM   7160 O  O   . VAL C  1  241 ? -10.765 9.294   2.073  1.00 33.55  ? 254 VAL C O   1 
ATOM   7161 C  CB  . VAL C  1  241 ? -10.338 10.343  -0.966 1.00 42.12  ? 254 VAL C CB  1 
ATOM   7162 C  CG1 . VAL C  1  241 ? -10.819 10.553  -2.384 1.00 52.52  ? 254 VAL C CG1 1 
ATOM   7163 C  CG2 . VAL C  1  241 ? -10.590 11.598  -0.150 1.00 41.85  ? 254 VAL C CG2 1 
ATOM   7164 N  N   . PRO C  1  242 ? -9.125  8.148   1.051  1.00 34.21  ? 255 PRO C N   1 
ATOM   7165 C  CA  . PRO C  1  242 ? -8.301  8.063   2.261  1.00 31.77  ? 255 PRO C CA  1 
ATOM   7166 C  C   . PRO C  1  242 ? -8.034  9.476   2.746  1.00 33.41  ? 255 PRO C C   1 
ATOM   7167 O  O   . PRO C  1  242 ? -7.775  10.369  1.950  1.00 31.37  ? 255 PRO C O   1 
ATOM   7168 C  CB  . PRO C  1  242 ? -7.019  7.363   1.786  1.00 33.19  ? 255 PRO C CB  1 
ATOM   7169 C  CG  . PRO C  1  242 ? -7.509  6.496   0.656  1.00 34.77  ? 255 PRO C CG  1 
ATOM   7170 C  CD  . PRO C  1  242 ? -8.539  7.389   -0.062 1.00 31.72  ? 255 PRO C CD  1 
ATOM   7171 N  N   . ALA C  1  243 ? -8.156  9.693   4.059  1.00 34.69  ? 256 ALA C N   1 
ATOM   7172 C  CA  . ALA C  1  243 ? -7.976  11.034  4.578  1.00 34.59  ? 256 ALA C CA  1 
ATOM   7173 C  C   . ALA C  1  243 ? -7.447  10.963  6.001  1.00 32.67  ? 256 ALA C C   1 
ATOM   7174 O  O   . ALA C  1  243 ? -7.525  9.921   6.645  1.00 30.90  ? 256 ALA C O   1 
ATOM   7175 C  CB  . ALA C  1  243 ? -9.283  11.797  4.489  1.00 38.42  ? 256 ALA C CB  1 
ATOM   7176 N  N   . SER C  1  244 ? -6.963  12.113  6.463  1.00 32.04  ? 257 SER C N   1 
ATOM   7177 C  CA  . SER C  1  244 ? -6.425  12.257  7.798  1.00 35.32  ? 257 SER C CA  1 
ATOM   7178 C  C   . SER C  1  244 ? -6.506  13.728  8.197  1.00 34.94  ? 257 SER C C   1 
ATOM   7179 O  O   . SER C  1  244 ? -7.585  14.211  8.514  1.00 35.70  ? 257 SER C O   1 
ATOM   7180 C  CB  . SER C  1  244 ? -5.029  11.667  7.889  1.00 32.52  ? 257 SER C CB  1 
ATOM   7181 O  OG  . SER C  1  244 ? -4.164  12.281  6.956  1.00 34.21  ? 257 SER C OG  1 
ATOM   7182 N  N   . ASN C  1  245 ? -5.385  14.444  8.113  1.00 37.57  ? 258 ASN C N   1 
ATOM   7183 C  CA  . ASN C  1  245 ? -5.253  15.740  8.753  1.00 39.05  ? 258 ASN C CA  1 
ATOM   7184 C  C   . ASN C  1  245 ? -5.257  16.889  7.748  1.00 40.67  ? 258 ASN C C   1 
ATOM   7185 O  O   . ASN C  1  245 ? -4.694  17.940  8.031  1.00 42.78  ? 258 ASN C O   1 
ATOM   7186 C  CB  . ASN C  1  245 ? -3.984  15.796  9.589  1.00 39.98  ? 258 ASN C CB  1 
ATOM   7187 C  CG  . ASN C  1  245 ? -2.749  15.720  8.733  1.00 41.59  ? 258 ASN C CG  1 
ATOM   7188 O  OD1 . ASN C  1  245 ? -2.815  15.334  7.570  1.00 41.15  ? 258 ASN C OD1 1 
ATOM   7189 N  ND2 . ASN C  1  245 ? -1.614  16.076  9.296  1.00 49.07  ? 258 ASN C ND2 1 
ATOM   7190 N  N   . GLU C  1  246 ? -5.919  16.718  6.598  1.00 42.14  ? 259 GLU C N   1 
ATOM   7191 C  CA  . GLU C  1  246 ? -6.074  17.807  5.642  1.00 45.88  ? 259 GLU C CA  1 
ATOM   7192 C  C   . GLU C  1  246 ? -6.741  19.008  6.330  1.00 43.78  ? 259 GLU C C   1 
ATOM   7193 O  O   . GLU C  1  246 ? -7.783  18.874  6.956  1.00 42.33  ? 259 GLU C O   1 
ATOM   7194 C  CB  . GLU C  1  246 ? -6.871  17.387  4.401  1.00 47.42  ? 259 GLU C CB  1 
ATOM   7195 C  CG  . GLU C  1  246 ? -6.170  16.332  3.542  1.00 49.95  ? 259 GLU C CG  1 
ATOM   7196 C  CD  . GLU C  1  246 ? -6.307  14.884  4.009  1.00 50.13  ? 259 GLU C CD  1 
ATOM   7197 O  OE1 . GLU C  1  246 ? -6.883  14.640  5.099  1.00 44.34  ? 259 GLU C OE1 1 
ATOM   7198 O  OE2 . GLU C  1  246 ? -5.857  13.988  3.266  1.00 42.10  ? 259 GLU C OE2 1 
ATOM   7199 N  N   . GLY C  1  247 ? -6.107  20.180  6.214  1.00 45.75  ? 260 GLY C N   1 
ATOM   7200 C  CA  . GLY C  1  247 ? -6.632  21.425  6.749  1.00 49.77  ? 260 GLY C CA  1 
ATOM   7201 C  C   . GLY C  1  247 ? -6.027  21.797  8.104  1.00 50.55  ? 260 GLY C C   1 
ATOM   7202 O  O   . GLY C  1  247 ? -6.263  22.899  8.587  1.00 48.18  ? 260 GLY C O   1 
ATOM   7203 N  N   . ALA C  1  248 ? -5.250  20.895  8.720  1.00 45.87  ? 261 ALA C N   1 
ATOM   7204 C  CA  . ALA C  1  248 ? -4.686  21.164  10.035 1.00 49.21  ? 261 ALA C CA  1 
ATOM   7205 C  C   . ALA C  1  248 ? -3.770  22.387  9.998  1.00 46.34  ? 261 ALA C C   1 
ATOM   7206 O  O   . ALA C  1  248 ? -3.701  23.130  10.974 1.00 48.98  ? 261 ALA C O   1 
ATOM   7207 C  CB  . ALA C  1  248 ? -3.937  19.952  10.554 1.00 48.88  ? 261 ALA C CB  1 
ATOM   7208 N  N   . ASP C  1  249 ? -3.054  22.566  8.886  1.00 45.92  ? 262 ASP C N   1 
ATOM   7209 C  CA  . ASP C  1  249 ? -2.198  23.724  8.672  1.00 55.94  ? 262 ASP C CA  1 
ATOM   7210 C  C   . ASP C  1  249 ? -3.001  25.027  8.788  1.00 60.38  ? 262 ASP C C   1 
ATOM   7211 O  O   . ASP C  1  249 ? -2.515  26.005  9.347  1.00 64.69  ? 262 ASP C O   1 
ATOM   7212 C  CB  . ASP C  1  249 ? -1.484  23.640  7.329  1.00 58.69  ? 262 ASP C CB  1 
ATOM   7213 C  CG  . ASP C  1  249 ? -2.360  23.412  6.098  1.00 63.51  ? 262 ASP C CG  1 
ATOM   7214 O  OD1 . ASP C  1  249 ? -3.554  23.063  6.251  1.00 65.02  ? 262 ASP C OD1 1 
ATOM   7215 O  OD2 . ASP C  1  249 ? -1.842  23.587  4.975  1.00 70.32  ? 262 ASP C OD2 1 
ATOM   7216 N  N   . GLN C  1  250 ? -4.231  25.039  8.261  1.00 56.39  ? 263 GLN C N   1 
ATOM   7217 C  CA  . GLN C  1  250 ? -5.059  26.232  8.287  1.00 60.71  ? 263 GLN C CA  1 
ATOM   7218 C  C   . GLN C  1  250 ? -5.569  26.512  9.697  1.00 60.46  ? 263 GLN C C   1 
ATOM   7219 O  O   . GLN C  1  250 ? -5.790  27.666  10.046 1.00 63.91  ? 263 GLN C O   1 
ATOM   7220 C  CB  . GLN C  1  250 ? -6.248  26.088  7.343  1.00 60.81  ? 263 GLN C CB  1 
ATOM   7221 C  CG  . GLN C  1  250 ? -5.855  26.052  5.875  1.00 61.90  ? 263 GLN C CG  1 
ATOM   7222 C  CD  . GLN C  1  250 ? -7.042  25.845  4.959  1.00 68.38  ? 263 GLN C CD  1 
ATOM   7223 O  OE1 . GLN C  1  250 ? -8.126  26.417  5.127  1.00 68.44  ? 263 GLN C OE1 1 
ATOM   7224 N  NE2 . GLN C  1  250 ? -6.837  25.009  3.956  1.00 73.50  ? 263 GLN C NE2 1 
ATOM   7225 N  N   . VAL C  1  251 ? -5.774  25.457  10.492 1.00 57.54  ? 264 VAL C N   1 
ATOM   7226 C  CA  . VAL C  1  251 ? -6.234  25.607  11.861 1.00 62.19  ? 264 VAL C CA  1 
ATOM   7227 C  C   . VAL C  1  251 ? -5.152  26.319  12.671 1.00 59.90  ? 264 VAL C C   1 
ATOM   7228 O  O   . VAL C  1  251 ? -5.460  27.238  13.427 1.00 62.90  ? 264 VAL C O   1 
ATOM   7229 C  CB  . VAL C  1  251 ? -6.635  24.248  12.479 1.00 63.97  ? 264 VAL C CB  1 
ATOM   7230 C  CG1 . VAL C  1  251 ? -6.836  24.312  13.993 1.00 65.02  ? 264 VAL C CG1 1 
ATOM   7231 C  CG2 . VAL C  1  251 ? -7.889  23.693  11.813 1.00 62.02  ? 264 VAL C CG2 1 
ATOM   7232 N  N   . LEU C  1  252 ? -3.894  25.898  12.493 1.00 57.10  ? 265 LEU C N   1 
ATOM   7233 C  CA  . LEU C  1  252 ? -2.761  26.545  13.134 1.00 58.75  ? 265 LEU C CA  1 
ATOM   7234 C  C   . LEU C  1  252 ? -2.621  27.988  12.645 1.00 60.65  ? 265 LEU C C   1 
ATOM   7235 O  O   . LEU C  1  252 ? -2.404  28.882  13.453 1.00 62.34  ? 265 LEU C O   1 
ATOM   7236 C  CB  . LEU C  1  252 ? -1.473  25.764  12.886 1.00 58.05  ? 265 LEU C CB  1 
ATOM   7237 C  CG  . LEU C  1  252 ? -0.205  26.322  13.534 1.00 57.07  ? 265 LEU C CG  1 
ATOM   7238 C  CD1 . LEU C  1  252 ? -0.348  26.230  15.031 1.00 57.32  ? 265 LEU C CD1 1 
ATOM   7239 C  CD2 . LEU C  1  252 ? 1.026   25.568  13.074 1.00 60.64  ? 265 LEU C CD2 1 
ATOM   7240 N  N   . ALA C  1  253 ? -2.740  28.214  11.331 1.00 66.64  ? 266 ALA C N   1 
ATOM   7241 C  CA  . ALA C  1  253 ? -2.536  29.535  10.747 1.00 70.42  ? 266 ALA C CA  1 
ATOM   7242 C  C   . ALA C  1  253 ? -3.563  30.555  11.264 1.00 69.59  ? 266 ALA C C   1 
ATOM   7243 O  O   . ALA C  1  253 ? -3.251  31.731  11.392 1.00 68.31  ? 266 ALA C O   1 
ATOM   7244 C  CB  . ALA C  1  253 ? -2.569  29.431  9.236  1.00 67.70  ? 266 ALA C CB  1 
ATOM   7245 N  N   . ALA C  1  254 ? -4.784  30.110  11.579 1.00 67.94  ? 267 ALA C N   1 
ATOM   7246 C  CA  . ALA C  1  254 ? -5.826  30.988  12.096 1.00 69.96  ? 267 ALA C CA  1 
ATOM   7247 C  C   . ALA C  1  254 ? -5.441  31.597  13.446 1.00 77.69  ? 267 ALA C C   1 
ATOM   7248 O  O   . ALA C  1  254 ? -5.892  32.692  13.771 1.00 78.46  ? 267 ALA C O   1 
ATOM   7249 C  CB  . ALA C  1  254 ? -7.131  30.230  12.212 1.00 64.47  ? 267 ALA C CB  1 
ATOM   7250 N  N   . HIS C  1  255 ? -4.663  30.865  14.255 1.00 72.52  ? 268 HIS C N   1 
ATOM   7251 C  CA  . HIS C  1  255 ? -4.173  31.363  15.532 1.00 71.75  ? 268 HIS C CA  1 
ATOM   7252 C  C   . HIS C  1  255 ? -2.795  30.765  15.813 1.00 68.53  ? 268 HIS C C   1 
ATOM   7253 O  O   . HIS C  1  255 ? -2.679  29.790  16.560 1.00 71.03  ? 268 HIS C O   1 
ATOM   7254 C  CB  . HIS C  1  255 ? -5.151  31.043  16.670 1.00 77.83  ? 268 HIS C CB  1 
ATOM   7255 C  CG  . HIS C  1  255 ? -6.414  31.838  16.664 1.00 84.29  ? 268 HIS C CG  1 
ATOM   7256 N  ND1 . HIS C  1  255 ? -6.482  33.146  17.101 1.00 83.54  ? 268 HIS C ND1 1 
ATOM   7257 C  CD2 . HIS C  1  255 ? -7.656  31.505  16.281 1.00 84.51  ? 268 HIS C CD2 1 
ATOM   7258 C  CE1 . HIS C  1  255 ? -7.729  33.579  16.982 1.00 83.90  ? 268 HIS C CE1 1 
ATOM   7259 N  NE2 . HIS C  1  255 ? -8.459  32.598  16.490 1.00 84.35  ? 268 HIS C NE2 1 
ATOM   7260 N  N   . PRO C  1  256 ? -1.722  31.315  15.195 1.00 58.05  ? 269 PRO C N   1 
ATOM   7261 C  CA  . PRO C  1  256 ? -0.368  30.785  15.336 1.00 57.26  ? 269 PRO C CA  1 
ATOM   7262 C  C   . PRO C  1  256 ? -0.027  30.504  16.791 1.00 62.75  ? 269 PRO C C   1 
ATOM   7263 O  O   . PRO C  1  256 ? -0.363  31.293  17.673 1.00 66.55  ? 269 PRO C O   1 
ATOM   7264 C  CB  . PRO C  1  256 ? 0.515   31.869  14.724 1.00 54.77  ? 269 PRO C CB  1 
ATOM   7265 C  CG  . PRO C  1  256 ? -0.368  32.453  13.654 1.00 56.58  ? 269 PRO C CG  1 
ATOM   7266 C  CD  . PRO C  1  256 ? -1.761  32.467  14.285 1.00 59.61  ? 269 PRO C CD  1 
ATOM   7267 N  N   . TRP C  1  257 ? 0.609   29.353  17.018 1.00 60.72  ? 270 TRP C N   1 
ATOM   7268 C  CA  . TRP C  1  257 ? 0.882   28.901  18.366 1.00 60.06  ? 270 TRP C CA  1 
ATOM   7269 C  C   . TRP C  1  257 ? 2.147   28.057  18.377 1.00 61.87  ? 270 TRP C C   1 
ATOM   7270 O  O   . TRP C  1  257 ? 2.453   27.367  17.411 1.00 58.62  ? 270 TRP C O   1 
ATOM   7271 C  CB  . TRP C  1  257 ? -0.313  28.127  18.931 1.00 64.26  ? 270 TRP C CB  1 
ATOM   7272 C  CG  . TRP C  1  257 ? -0.203  27.947  20.416 1.00 69.52  ? 270 TRP C CG  1 
ATOM   7273 C  CD1 . TRP C  1  257 ? 0.200   26.832  21.085 1.00 70.51  ? 270 TRP C CD1 1 
ATOM   7274 C  CD2 . TRP C  1  257 ? -0.411  28.968  21.410 1.00 73.87  ? 270 TRP C CD2 1 
ATOM   7275 N  NE1 . TRP C  1  257 ? 0.208   27.071  22.430 1.00 70.74  ? 270 TRP C NE1 1 
ATOM   7276 C  CE2 . TRP C  1  257 ? -0.156  28.371  22.660 1.00 72.40  ? 270 TRP C CE2 1 
ATOM   7277 C  CE3 . TRP C  1  257 ? -0.803  30.311  21.364 1.00 74.47  ? 270 TRP C CE3 1 
ATOM   7278 C  CZ2 . TRP C  1  257 ? -0.273  29.080  23.851 1.00 78.27  ? 270 TRP C CZ2 1 
ATOM   7279 C  CZ3 . TRP C  1  257 ? -0.927  31.009  22.543 1.00 75.78  ? 270 TRP C CZ3 1 
ATOM   7280 C  CH2 . TRP C  1  257 ? -0.660  30.400  23.769 1.00 77.84  ? 270 TRP C CH2 1 
ATOM   7281 N  N   . VAL C  1  258 ? 2.861   28.126  19.498 1.00 63.11  ? 271 VAL C N   1 
ATOM   7282 C  CA  . VAL C  1  258 ? 4.182   27.544  19.606 1.00 65.01  ? 271 VAL C CA  1 
ATOM   7283 C  C   . VAL C  1  258 ? 4.138   26.515  20.728 1.00 60.23  ? 271 VAL C C   1 
ATOM   7284 O  O   . VAL C  1  258 ? 3.530   26.756  21.776 1.00 60.81  ? 271 VAL C O   1 
ATOM   7285 C  CB  . VAL C  1  258 ? 5.239   28.638  19.854 1.00 70.28  ? 271 VAL C CB  1 
ATOM   7286 C  CG1 . VAL C  1  258 ? 6.631   28.052  20.009 1.00 75.60  ? 271 VAL C CG1 1 
ATOM   7287 C  CG2 . VAL C  1  258 ? 5.256   29.676  18.739 1.00 67.37  ? 271 VAL C CG2 1 
ATOM   7288 N  N   . PRO C  1  259 ? 4.771   25.335  20.545 1.00 56.47  ? 272 PRO C N   1 
ATOM   7289 C  CA  . PRO C  1  259 ? 4.768   24.312  21.583 1.00 56.97  ? 272 PRO C CA  1 
ATOM   7290 C  C   . PRO C  1  259 ? 5.380   24.843  22.875 1.00 55.17  ? 272 PRO C C   1 
ATOM   7291 O  O   . PRO C  1  259 ? 6.287   25.662  22.841 1.00 51.60  ? 272 PRO C O   1 
ATOM   7292 C  CB  . PRO C  1  259 ? 5.593   23.158  20.954 1.00 58.50  ? 272 PRO C CB  1 
ATOM   7293 C  CG  . PRO C  1  259 ? 6.410   23.828  19.872 1.00 55.46  ? 272 PRO C CG  1 
ATOM   7294 C  CD  . PRO C  1  259 ? 5.508   24.915  19.342 1.00 57.14  ? 272 PRO C CD  1 
ATOM   7295 N  N   . GLY C  1  260 ? 4.863   24.355  24.003 1.00 57.61  ? 273 GLY C N   1 
ATOM   7296 C  CA  . GLY C  1  260 ? 5.328   24.772  25.313 1.00 57.81  ? 273 GLY C CA  1 
ATOM   7297 C  C   . GLY C  1  260 ? 4.415   24.213  26.398 1.00 63.46  ? 273 GLY C C   1 
ATOM   7298 O  O   . GLY C  1  260 ? 3.835   23.133  26.231 1.00 58.23  ? 273 GLY C O   1 
ATOM   7299 N  N   . GLY C  1  261 ? 4.297   24.967  27.499 1.00 59.58  ? 274 GLY C N   1 
ATOM   7300 C  CA  . GLY C  1  261 ? 3.486   24.569  28.636 1.00 61.00  ? 274 GLY C CA  1 
ATOM   7301 C  C   . GLY C  1  261 ? 3.529   25.632  29.735 1.00 63.19  ? 274 GLY C C   1 
ATOM   7302 O  O   . GLY C  1  261 ? 4.333   26.564  29.679 1.00 58.45  ? 274 GLY C O   1 
ATOM   7303 N  N   . ASN C  1  262 ? 2.629   25.493  30.712 1.00 63.72  ? 275 ASN C N   1 
ATOM   7304 C  CA  . ASN C  1  262 ? 2.686   26.281  31.934 1.00 63.20  ? 275 ASN C CA  1 
ATOM   7305 C  C   . ASN C  1  262 ? 3.886   25.821  32.755 1.00 67.91  ? 275 ASN C C   1 
ATOM   7306 O  O   . ASN C  1  262 ? 3.990   24.637  33.068 1.00 67.85  ? 275 ASN C O   1 
ATOM   7307 C  CB  . ASN C  1  262 ? 1.422   26.125  32.772 1.00 60.19  ? 275 ASN C CB  1 
ATOM   7308 C  CG  . ASN C  1  262 ? 0.302   27.056  32.366 1.00 58.41  ? 275 ASN C CG  1 
ATOM   7309 O  OD1 . ASN C  1  262 ? 0.541   28.115  31.770 1.00 51.40  ? 275 ASN C OD1 1 
ATOM   7310 N  ND2 . ASN C  1  262 ? -0.927  26.685  32.709 1.00 58.69  ? 275 ASN C ND2 1 
ATOM   7311 N  N   . ALA C  1  263 ? 4.779   26.753  33.114 1.00 69.89  ? 276 ALA C N   1 
ATOM   7312 C  CA  . ALA C  1  263 ? 5.952   26.414  33.915 1.00 73.15  ? 276 ALA C CA  1 
ATOM   7313 C  C   . ALA C  1  263 ? 5.654   26.535  35.413 1.00 75.06  ? 276 ALA C C   1 
ATOM   7314 O  O   . ALA C  1  263 ? 4.783   27.303  35.823 1.00 70.64  ? 276 ALA C O   1 
ATOM   7315 C  CB  . ALA C  1  263 ? 7.123   27.286  33.516 1.00 70.99  ? 276 ALA C CB  1 
ATOM   7316 N  N   . ASP C  1  264 ? 6.368   25.725  36.209 1.00 80.41  ? 277 ASP C N   1 
ATOM   7317 C  CA  . ASP C  1  264 ? 6.488   25.884  37.651 1.00 85.19  ? 277 ASP C CA  1 
ATOM   7318 C  C   . ASP C  1  264 ? 5.136   25.751  38.345 1.00 86.73  ? 277 ASP C C   1 
ATOM   7319 O  O   . ASP C  1  264 ? 4.885   26.434  39.333 1.00 91.69  ? 277 ASP C O   1 
ATOM   7320 C  CB  . ASP C  1  264 ? 7.178   27.193  38.011 1.00 89.59  ? 277 ASP C CB  1 
ATOM   7321 C  CG  . ASP C  1  264 ? 8.561   27.389  37.403 1.00 96.07  ? 277 ASP C CG  1 
ATOM   7322 O  OD1 . ASP C  1  264 ? 9.393   26.464  37.542 1.00 100.66 ? 277 ASP C OD1 1 
ATOM   7323 O  OD2 . ASP C  1  264 ? 8.807   28.469  36.819 1.00 92.41  ? 277 ASP C OD2 1 
ATOM   7324 N  N   . ASN C  1  265 ? 4.277   24.866  37.827 1.00 79.42  ? 278 ASN C N   1 
ATOM   7325 C  CA  . ASN C  1  265 ? 3.040   24.494  38.494 1.00 74.62  ? 278 ASN C CA  1 
ATOM   7326 C  C   . ASN C  1  265 ? 2.177   25.735  38.742 1.00 71.31  ? 278 ASN C C   1 
ATOM   7327 O  O   . ASN C  1  265 ? 1.534   25.852  39.782 1.00 68.98  ? 278 ASN C O   1 
ATOM   7328 C  CB  . ASN C  1  265 ? 3.375   23.679  39.736 1.00 74.37  ? 278 ASN C CB  1 
ATOM   7329 C  CG  . ASN C  1  265 ? 2.196   22.910  40.275 1.00 79.64  ? 278 ASN C CG  1 
ATOM   7330 O  OD1 . ASN C  1  265 ? 1.453   22.289  39.507 1.00 82.73  ? 278 ASN C OD1 1 
ATOM   7331 N  ND2 . ASN C  1  265 ? 2.007   22.940  41.586 1.00 86.76  ? 278 ASN C ND2 1 
ATOM   7332 N  N   . GLN C  1  266 ? 2.139   26.641  37.762 1.00 74.91  ? 279 GLN C N   1 
ATOM   7333 C  CA  . GLN C  1  266 ? 1.330   27.846  37.850 1.00 79.16  ? 279 GLN C CA  1 
ATOM   7334 C  C   . GLN C  1  266 ? 0.497   28.031  36.586 1.00 75.17  ? 279 GLN C C   1 
ATOM   7335 O  O   . GLN C  1  266 ? 0.968   27.770  35.482 1.00 82.68  ? 279 GLN C O   1 
ATOM   7336 C  CB  . GLN C  1  266 ? 2.214   29.083  37.983 1.00 82.62  ? 279 GLN C CB  1 
ATOM   7337 C  CG  . GLN C  1  266 ? 2.863   29.266  39.350 1.00 88.76  ? 279 GLN C CG  1 
ATOM   7338 C  CD  . GLN C  1  266 ? 3.979   30.292  39.308 1.00 86.37  ? 279 GLN C CD  1 
ATOM   7339 O  OE1 . GLN C  1  266 ? 3.883   31.304  38.606 1.00 82.36  ? 279 GLN C OE1 1 
ATOM   7340 N  NE2 . GLN C  1  266 ? 5.082   30.005  39.988 1.00 88.52  ? 279 GLN C NE2 1 
ATOM   7341 N  N   . VAL C  1  267 ? -0.728  28.535  36.757 1.00 66.22  ? 280 VAL C N   1 
ATOM   7342 C  CA  . VAL C  1  267 ? -1.570  28.912  35.633 1.00 64.72  ? 280 VAL C CA  1 
ATOM   7343 C  C   . VAL C  1  267 ? -1.068  30.226  35.035 1.00 62.00  ? 280 VAL C C   1 
ATOM   7344 O  O   . VAL C  1  267 ? -0.198  30.879  35.602 1.00 65.16  ? 280 VAL C O   1 
ATOM   7345 C  CB  . VAL C  1  267 ? -3.051  28.991  36.051 1.00 67.24  ? 280 VAL C CB  1 
ATOM   7346 C  CG1 . VAL C  1  267 ? -3.562  27.630  36.506 1.00 68.79  ? 280 VAL C CG1 1 
ATOM   7347 C  CG2 . VAL C  1  267 ? -3.318  30.047  37.128 1.00 67.44  ? 280 VAL C CG2 1 
ATOM   7348 N  N   . ASN C  1  268 ? -1.605  30.561  33.859 1.00 63.47  ? 281 ASN C N   1 
ATOM   7349 C  CA  . ASN C  1  268 ? -1.247  31.748  33.094 1.00 72.16  ? 281 ASN C CA  1 
ATOM   7350 C  C   . ASN C  1  268 ? 0.260   31.974  33.080 1.00 71.84  ? 281 ASN C C   1 
ATOM   7351 O  O   . ASN C  1  268 ? 0.721   33.097  33.244 1.00 80.21  ? 281 ASN C O   1 
ATOM   7352 C  CB  . ASN C  1  268 ? -1.988  32.980  33.599 1.00 72.96  ? 281 ASN C CB  1 
ATOM   7353 C  CG  . ASN C  1  268 ? -3.480  32.811  33.450 1.00 75.47  ? 281 ASN C CG  1 
ATOM   7354 O  OD1 . ASN C  1  268 ? -3.995  32.733  32.329 1.00 74.39  ? 281 ASN C OD1 1 
ATOM   7355 N  ND2 . ASN C  1  268 ? -4.189  32.733  34.565 1.00 81.45  ? 281 ASN C ND2 1 
ATOM   7356 N  N   . ASN C  1  269 ? 1.018   30.912  32.811 1.00 72.10  ? 282 ASN C N   1 
ATOM   7357 C  CA  . ASN C  1  269 ? 2.467   30.988  32.860 1.00 72.07  ? 282 ASN C CA  1 
ATOM   7358 C  C   . ASN C  1  269 ? 3.053   30.138  31.730 1.00 72.80  ? 282 ASN C C   1 
ATOM   7359 O  O   . ASN C  1  269 ? 3.909   29.286  31.959 1.00 67.86  ? 282 ASN C O   1 
ATOM   7360 C  CB  . ASN C  1  269 ? 2.937   30.631  34.266 1.00 67.48  ? 282 ASN C CB  1 
ATOM   7361 C  CG  . ASN C  1  269 ? 4.408   30.893  34.467 1.00 61.40  ? 282 ASN C CG  1 
ATOM   7362 O  OD1 . ASN C  1  269 ? 4.968   31.851  33.925 1.00 60.25  ? 282 ASN C OD1 1 
ATOM   7363 N  ND2 . ASN C  1  269 ? 5.062   30.017  35.205 1.00 61.11  ? 282 ASN C ND2 1 
ATOM   7364 N  N   . TYR C  1  270 ? 2.608   30.411  30.497 1.00 72.04  ? 283 TYR C N   1 
ATOM   7365 C  CA  . TYR C  1  270 ? 2.950   29.580  29.354 1.00 72.10  ? 283 TYR C CA  1 
ATOM   7366 C  C   . TYR C  1  270 ? 4.313   29.983  28.794 1.00 71.21  ? 283 TYR C C   1 
ATOM   7367 O  O   . TYR C  1  270 ? 4.473   31.108  28.335 1.00 69.85  ? 283 TYR C O   1 
ATOM   7368 C  CB  . TYR C  1  270 ? 1.882   29.692  28.261 1.00 70.19  ? 283 TYR C CB  1 
ATOM   7369 C  CG  . TYR C  1  270 ? 2.033   28.685  27.125 1.00 70.08  ? 283 TYR C CG  1 
ATOM   7370 C  CD1 . TYR C  1  270 ? 1.480   27.408  27.218 1.00 76.38  ? 283 TYR C CD1 1 
ATOM   7371 C  CD2 . TYR C  1  270 ? 2.721   29.002  25.958 1.00 69.95  ? 283 TYR C CD2 1 
ATOM   7372 C  CE1 . TYR C  1  270 ? 1.613   26.481  26.193 1.00 72.90  ? 283 TYR C CE1 1 
ATOM   7373 C  CE2 . TYR C  1  270 ? 2.861   28.083  24.926 1.00 72.74  ? 283 TYR C CE2 1 
ATOM   7374 C  CZ  . TYR C  1  270 ? 2.305   26.819  25.043 1.00 69.67  ? 283 TYR C CZ  1 
ATOM   7375 O  OH  . TYR C  1  270 ? 2.413   25.921  24.020 1.00 65.53  ? 283 TYR C OH  1 
ATOM   7376 N  N   . VAL C  1  271 ? 5.254   29.025  28.780 1.00 75.41  ? 284 VAL C N   1 
ATOM   7377 C  CA  . VAL C  1  271 ? 6.600   29.226  28.265 1.00 74.92  ? 284 VAL C CA  1 
ATOM   7378 C  C   . VAL C  1  271 ? 6.824   28.330  27.045 1.00 74.85  ? 284 VAL C C   1 
ATOM   7379 O  O   . VAL C  1  271 ? 6.597   27.125  27.114 1.00 69.30  ? 284 VAL C O   1 
ATOM   7380 C  CB  . VAL C  1  271 ? 7.646   28.906  29.349 1.00 80.83  ? 284 VAL C CB  1 
ATOM   7381 C  CG1 . VAL C  1  271 ? 9.066   29.092  28.819 1.00 80.32  ? 284 VAL C CG1 1 
ATOM   7382 C  CG2 . VAL C  1  271 ? 7.431   29.719  30.623 1.00 82.64  ? 284 VAL C CG2 1 
ATOM   7383 N  N   . GLU C  1  272 ? 7.342   28.932  25.959 1.00 69.57  ? 285 GLU C N   1 
ATOM   7384 C  CA  A GLU C  1  272 ? 7.633   28.216  24.730 0.50 65.14  ? 285 GLU C CA  1 
ATOM   7385 C  CA  B GLU C  1  272 ? 7.668   28.243  24.717 0.50 69.91  ? 285 GLU C CA  1 
ATOM   7386 C  C   . GLU C  1  272 ? 8.773   27.225  24.970 1.00 68.33  ? 285 GLU C C   1 
ATOM   7387 O  O   . GLU C  1  272 ? 9.648   27.467  25.791 1.00 63.56  ? 285 GLU C O   1 
ATOM   7388 C  CB  A GLU C  1  272 ? 7.901   29.244  23.628 0.50 60.20  ? 285 GLU C CB  1 
ATOM   7389 C  CB  B GLU C  1  272 ? 8.171   29.198  23.627 0.50 71.79  ? 285 GLU C CB  1 
ATOM   7390 C  CG  A GLU C  1  272 ? 6.699   30.168  23.394 0.50 54.73  ? 285 GLU C CG  1 
ATOM   7391 C  CG  B GLU C  1  272 ? 9.042   28.529  22.561 0.50 72.88  ? 285 GLU C CG  1 
ATOM   7392 C  CD  A GLU C  1  272 ? 6.845   31.437  22.568 0.50 51.79  ? 285 GLU C CD  1 
ATOM   7393 C  CD  B GLU C  1  272 ? 9.489   29.391  21.391 0.50 71.33  ? 285 GLU C CD  1 
ATOM   7394 O  OE1 A GLU C  1  272 ? 7.941   31.744  22.068 0.50 48.37  ? 285 GLU C OE1 1 
ATOM   7395 O  OE1 B GLU C  1  272 ? 8.913   30.476  21.182 0.50 68.58  ? 285 GLU C OE1 1 
ATOM   7396 O  OE2 A GLU C  1  272 ? 5.815   32.135  22.436 0.50 50.62  ? 285 GLU C OE2 1 
ATOM   7397 O  OE2 B GLU C  1  272 ? 10.434  28.971  20.689 0.50 74.37  ? 285 GLU C OE2 1 
ATOM   7398 N  N   . ASP C  1  273 ? 8.718   26.089  24.251 1.00 72.14  ? 286 ASP C N   1 
ATOM   7399 C  CA  . ASP C  1  273 ? 9.795   25.104  24.234 1.00 67.26  ? 286 ASP C CA  1 
ATOM   7400 C  C   . ASP C  1  273 ? 10.385  25.045  22.826 1.00 70.91  ? 286 ASP C C   1 
ATOM   7401 O  O   . ASP C  1  273 ? 9.781   24.455  21.932 1.00 70.95  ? 286 ASP C O   1 
ATOM   7402 C  CB  . ASP C  1  273 ? 9.340   23.721  24.678 1.00 65.50  ? 286 ASP C CB  1 
ATOM   7403 C  CG  . ASP C  1  273 ? 10.413  22.638  24.620 1.00 66.70  ? 286 ASP C CG  1 
ATOM   7404 O  OD1 . ASP C  1  273 ? 11.555  22.944  24.219 1.00 70.18  ? 286 ASP C OD1 1 
ATOM   7405 O  OD2 . ASP C  1  273 ? 10.111  21.488  24.984 1.00 65.67  ? 286 ASP C OD2 1 
ATOM   7406 N  N   . PRO C  1  274 ? 11.584  25.627  22.591 1.00 75.09  ? 287 PRO C N   1 
ATOM   7407 C  CA  . PRO C  1  274 ? 12.172  25.676  21.246 1.00 73.07  ? 287 PRO C CA  1 
ATOM   7408 C  C   . PRO C  1  274 ? 12.700  24.340  20.715 1.00 66.41  ? 287 PRO C C   1 
ATOM   7409 O  O   . PRO C  1  274 ? 12.922  24.207  19.512 1.00 60.32  ? 287 PRO C O   1 
ATOM   7410 C  CB  . PRO C  1  274 ? 13.309  26.705  21.419 1.00 73.84  ? 287 PRO C CB  1 
ATOM   7411 C  CG  . PRO C  1  274 ? 13.747  26.517  22.861 1.00 75.15  ? 287 PRO C CG  1 
ATOM   7412 C  CD  . PRO C  1  274 ? 12.450  26.239  23.613 1.00 77.34  ? 287 PRO C CD  1 
ATOM   7413 N  N   . ASP C  1  275 ? 12.910  23.367  21.619 1.00 61.37  ? 288 ASP C N   1 
ATOM   7414 C  CA  . ASP C  1  275 ? 13.418  22.047  21.267 1.00 65.13  ? 288 ASP C CA  1 
ATOM   7415 C  C   . ASP C  1  275 ? 12.308  21.081  20.824 1.00 58.55  ? 288 ASP C C   1 
ATOM   7416 O  O   . ASP C  1  275 ? 12.606  20.003  20.323 1.00 52.72  ? 288 ASP C O   1 
ATOM   7417 C  CB  . ASP C  1  275 ? 14.194  21.454  22.431 1.00 66.44  ? 288 ASP C CB  1 
ATOM   7418 C  CG  . ASP C  1  275 ? 15.496  22.173  22.769 1.00 73.66  ? 288 ASP C CG  1 
ATOM   7419 O  OD1 . ASP C  1  275 ? 15.864  23.116  22.042 1.00 72.48  ? 288 ASP C OD1 1 
ATOM   7420 O  OD2 . ASP C  1  275 ? 16.140  21.789  23.761 1.00 70.75  ? 288 ASP C OD2 1 
ATOM   7421 N  N   . SER C  1  276 ? 11.038  21.453  21.027 1.00 54.93  ? 289 SER C N   1 
ATOM   7422 C  CA  . SER C  1  276 ? 9.907   20.598  20.704 1.00 53.18  ? 289 SER C CA  1 
ATOM   7423 C  C   . SER C  1  276 ? 9.782   20.419  19.195 1.00 53.64  ? 289 SER C C   1 
ATOM   7424 O  O   . SER C  1  276 ? 10.127  21.292  18.411 1.00 52.51  ? 289 SER C O   1 
ATOM   7425 C  CB  . SER C  1  276 ? 8.616   21.153  21.283 1.00 59.33  ? 289 SER C CB  1 
ATOM   7426 O  OG  . SER C  1  276 ? 7.460   20.542  20.712 1.00 54.85  ? 289 SER C OG  1 
ATOM   7427 N  N   . ALA C  1  277 ? 9.230   19.275  18.791 1.00 52.63  ? 290 ALA C N   1 
ATOM   7428 C  CA  . ALA C  1  277 ? 8.717   19.126  17.445 1.00 48.49  ? 290 ALA C CA  1 
ATOM   7429 C  C   . ALA C  1  277 ? 7.702   20.229  17.159 1.00 45.25  ? 290 ALA C C   1 
ATOM   7430 O  O   . ALA C  1  277 ? 7.055   20.746  18.067 1.00 45.37  ? 290 ALA C O   1 
ATOM   7431 C  CB  . ALA C  1  277 ? 8.096   17.761  17.283 1.00 48.09  ? 290 ALA C CB  1 
ATOM   7432 N  N   . ASP C  1  278 ? 7.594   20.573  15.880 1.00 42.15  ? 291 ASP C N   1 
ATOM   7433 C  CA  . ASP C  1  278 ? 6.525   21.405  15.355 1.00 49.34  ? 291 ASP C CA  1 
ATOM   7434 C  C   . ASP C  1  278 ? 6.312   20.969  13.907 1.00 46.43  ? 291 ASP C C   1 
ATOM   7435 O  O   . ASP C  1  278 ? 6.937   20.008  13.455 1.00 50.69  ? 291 ASP C O   1 
ATOM   7436 C  CB  . ASP C  1  278 ? 6.829   22.887  15.553 1.00 53.83  ? 291 ASP C CB  1 
ATOM   7437 C  CG  . ASP C  1  278 ? 8.016   23.442  14.774 1.00 55.55  ? 291 ASP C CG  1 
ATOM   7438 O  OD1 . ASP C  1  278 ? 8.333   22.895  13.704 1.00 57.69  ? 291 ASP C OD1 1 
ATOM   7439 O  OD2 . ASP C  1  278 ? 8.623   24.427  15.243 1.00 67.29  ? 291 ASP C OD2 1 
ATOM   7440 N  N   . PHE C  1  279 ? 5.474   21.702  13.168 1.00 45.03  ? 292 PHE C N   1 
ATOM   7441 C  CA  . PHE C  1  279 ? 5.042   21.244  11.862 1.00 45.11  ? 292 PHE C CA  1 
ATOM   7442 C  C   . PHE C  1  279 ? 6.134   21.382  10.804 1.00 48.81  ? 292 PHE C C   1 
ATOM   7443 O  O   . PHE C  1  279 ? 6.015   20.757  9.752  1.00 52.34  ? 292 PHE C O   1 
ATOM   7444 C  CB  . PHE C  1  279 ? 3.720   21.902  11.468 1.00 44.11  ? 292 PHE C CB  1 
ATOM   7445 C  CG  . PHE C  1  279 ? 2.575   21.264  12.236 1.00 48.61  ? 292 PHE C CG  1 
ATOM   7446 C  CD1 . PHE C  1  279 ? 2.068   20.024  11.842 1.00 45.20  ? 292 PHE C CD1 1 
ATOM   7447 C  CD2 . PHE C  1  279 ? 2.057   21.864  13.382 1.00 46.21  ? 292 PHE C CD2 1 
ATOM   7448 C  CE1 . PHE C  1  279 ? 1.041   19.422  12.553 1.00 49.17  ? 292 PHE C CE1 1 
ATOM   7449 C  CE2 . PHE C  1  279 ? 1.028   21.259  14.089 1.00 49.29  ? 292 PHE C CE2 1 
ATOM   7450 C  CZ  . PHE C  1  279 ? 0.530   20.035  13.680 1.00 54.74  ? 292 PHE C CZ  1 
ATOM   7451 N  N   . THR C  1  280 ? 7.207   22.130  11.073 1.00 52.24  ? 293 THR C N   1 
ATOM   7452 C  CA  . THR C  1  280 ? 8.341   22.155  10.154 1.00 52.20  ? 293 THR C CA  1 
ATOM   7453 C  C   . THR C  1  280 ? 9.517   21.368  10.734 1.00 50.03  ? 293 THR C C   1 
ATOM   7454 O  O   . THR C  1  280 ? 10.599  21.373  10.156 1.00 51.18  ? 293 THR C O   1 
ATOM   7455 C  CB  . THR C  1  280 ? 8.744   23.597  9.823  1.00 62.11  ? 293 THR C CB  1 
ATOM   7456 O  OG1 . THR C  1  280 ? 9.118   24.242  11.036 1.00 63.29  ? 293 THR C OG1 1 
ATOM   7457 C  CG2 . THR C  1  280 ? 7.616   24.409  9.211  1.00 63.25  ? 293 THR C CG2 1 
ATOM   7458 N  N   . HIS C  1  281 ? 9.312   20.671  11.862 1.00 50.10  ? 294 HIS C N   1 
ATOM   7459 C  CA  . HIS C  1  281 ? 10.363  19.866  12.473 1.00 50.73  ? 294 HIS C CA  1 
ATOM   7460 C  C   . HIS C  1  281 ? 9.768   18.549  12.967 1.00 48.79  ? 294 HIS C C   1 
ATOM   7461 O  O   . HIS C  1  281 ? 9.902   18.197  14.135 1.00 43.99  ? 294 HIS C O   1 
ATOM   7462 C  CB  . HIS C  1  281 ? 11.050  20.622  13.621 1.00 53.58  ? 294 HIS C CB  1 
ATOM   7463 C  CG  . HIS C  1  281 ? 11.754  21.871  13.213 1.00 56.79  ? 294 HIS C CG  1 
ATOM   7464 N  ND1 . HIS C  1  281 ? 13.086  21.870  12.856 1.00 64.08  ? 294 HIS C ND1 1 
ATOM   7465 C  CD2 . HIS C  1  281 ? 11.340  23.143  13.102 1.00 59.70  ? 294 HIS C CD2 1 
ATOM   7466 C  CE1 . HIS C  1  281 ? 13.456  23.100  12.526 1.00 66.15  ? 294 HIS C CE1 1 
ATOM   7467 N  NE2 . HIS C  1  281 ? 12.410  23.889  12.672 1.00 67.35  ? 294 HIS C NE2 1 
ATOM   7468 N  N   . LEU C  1  282 ? 9.155   17.804  12.045 1.00 48.92  ? 295 LEU C N   1 
ATOM   7469 C  CA  . LEU C  1  282 ? 8.402   16.613  12.389 1.00 43.27  ? 295 LEU C CA  1 
ATOM   7470 C  C   . LEU C  1  282 ? 9.326   15.491  12.849 1.00 42.25  ? 295 LEU C C   1 
ATOM   7471 O  O   . LEU C  1  282 ? 8.923   14.690  13.683 1.00 39.69  ? 295 LEU C O   1 
ATOM   7472 C  CB  . LEU C  1  282 ? 7.537   16.170  11.214 1.00 41.73  ? 295 LEU C CB  1 
ATOM   7473 C  CG  . LEU C  1  282 ? 6.308   17.037  10.946 1.00 42.53  ? 295 LEU C CG  1 
ATOM   7474 C  CD1 . LEU C  1  282 ? 5.604   16.632  9.665  1.00 43.95  ? 295 LEU C CD1 1 
ATOM   7475 C  CD2 . LEU C  1  282 ? 5.350   16.959  12.114 1.00 45.56  ? 295 LEU C CD2 1 
ATOM   7476 N  N   . CYS C  1  283 ? 10.547  15.427  12.319 1.00 40.72  ? 296 CYS C N   1 
ATOM   7477 C  CA  . CYS C  1  283 ? 11.436  14.324  12.657 1.00 42.08  ? 296 CYS C CA  1 
ATOM   7478 C  C   . CYS C  1  283 ? 11.839  14.385  14.129 1.00 41.27  ? 296 CYS C C   1 
ATOM   7479 O  O   . CYS C  1  283 ? 12.167  13.352  14.717 1.00 40.16  ? 296 CYS C O   1 
ATOM   7480 C  CB  . CYS C  1  283 ? 12.643  14.224  11.726 1.00 46.54  ? 296 CYS C CB  1 
ATOM   7481 S  SG  . CYS C  1  283 ? 12.226  13.692  10.034 1.00 55.48  ? 296 CYS C SG  1 
ATOM   7482 N  N   . ARG C  1  284 ? 11.754  15.569  14.750 1.00 41.25  ? 297 ARG C N   1 
ATOM   7483 C  CA  . ARG C  1  284 ? 11.979  15.661  16.185 1.00 43.25  ? 297 ARG C CA  1 
ATOM   7484 C  C   . ARG C  1  284 ? 10.989  14.788  16.945 1.00 39.57  ? 297 ARG C C   1 
ATOM   7485 O  O   . ARG C  1  284 ? 11.325  14.263  17.999 1.00 39.39  ? 297 ARG C O   1 
ATOM   7486 C  CB  . ARG C  1  284 ? 11.799  17.082  16.725 1.00 50.71  ? 297 ARG C CB  1 
ATOM   7487 C  CG  . ARG C  1  284 ? 12.919  18.010  16.289 1.00 52.85  ? 297 ARG C CG  1 
ATOM   7488 C  CD  . ARG C  1  284 ? 12.665  19.381  16.869 1.00 55.92  ? 297 ARG C CD  1 
ATOM   7489 N  NE  . ARG C  1  284 ? 13.614  20.350  16.318 1.00 60.35  ? 297 ARG C NE  1 
ATOM   7490 C  CZ  . ARG C  1  284 ? 13.675  21.634  16.639 1.00 63.62  ? 297 ARG C CZ  1 
ATOM   7491 N  NH1 . ARG C  1  284 ? 12.825  22.152  17.512 1.00 60.15  ? 297 ARG C NH1 1 
ATOM   7492 N  NH2 . ARG C  1  284 ? 14.602  22.384  16.066 1.00 65.35  ? 297 ARG C NH2 1 
ATOM   7493 N  N   . LEU C  1  285 ? 9.763   14.663  16.420 1.00 40.24  ? 298 LEU C N   1 
ATOM   7494 C  CA  . LEU C  1  285 ? 8.752   13.847  17.070 1.00 38.79  ? 298 LEU C CA  1 
ATOM   7495 C  C   . LEU C  1  285 ? 9.204   12.394  17.052 1.00 36.86  ? 298 LEU C C   1 
ATOM   7496 O  O   . LEU C  1  285 ? 9.098   11.711  18.067 1.00 34.71  ? 298 LEU C O   1 
ATOM   7497 C  CB  . LEU C  1  285 ? 7.375   14.043  16.445 1.00 38.89  ? 298 LEU C CB  1 
ATOM   7498 C  CG  . LEU C  1  285 ? 6.211   13.357  17.161 1.00 40.42  ? 298 LEU C CG  1 
ATOM   7499 C  CD1 . LEU C  1  285 ? 4.898   14.018  16.840 1.00 43.03  ? 298 LEU C CD1 1 
ATOM   7500 C  CD2 . LEU C  1  285 ? 6.096   11.891  16.790 1.00 45.85  ? 298 LEU C CD2 1 
ATOM   7501 N  N   . TYR C  1  286 ? 9.719   11.937  15.906 1.00 35.47  ? 299 TYR C N   1 
ATOM   7502 C  CA  . TYR C  1  286 ? 10.202  10.575  15.766 1.00 34.15  ? 299 TYR C CA  1 
ATOM   7503 C  C   . TYR C  1  286 ? 11.317  10.312  16.784 1.00 35.69  ? 299 TYR C C   1 
ATOM   7504 O  O   . TYR C  1  286 ? 11.270  9.326   17.521 1.00 33.87  ? 299 TYR C O   1 
ATOM   7505 C  CB  . TYR C  1  286 ? 10.631  10.303  14.317 1.00 31.40  ? 299 TYR C CB  1 
ATOM   7506 C  CG  . TYR C  1  286 ? 11.338  8.970   14.112 1.00 29.00  ? 299 TYR C CG  1 
ATOM   7507 C  CD1 . TYR C  1  286 ? 10.671  7.767   14.294 1.00 30.39  ? 299 TYR C CD1 1 
ATOM   7508 C  CD2 . TYR C  1  286 ? 12.687  8.915   13.794 1.00 29.76  ? 299 TYR C CD2 1 
ATOM   7509 C  CE1 . TYR C  1  286 ? 11.309  6.547   14.137 1.00 28.41  ? 299 TYR C CE1 1 
ATOM   7510 C  CE2 . TYR C  1  286 ? 13.339  7.707   13.641 1.00 30.56  ? 299 TYR C CE2 1 
ATOM   7511 C  CZ  . TYR C  1  286 ? 12.652  6.522   13.826 1.00 30.95  ? 299 TYR C CZ  1 
ATOM   7512 O  OH  . TYR C  1  286 ? 13.299  5.334   13.660 1.00 30.38  ? 299 TYR C OH  1 
ATOM   7513 N  N   . GLU C  1  287 ? 12.307  11.210  16.841 1.00 37.64  ? 300 GLU C N   1 
ATOM   7514 C  CA  . GLU C  1  287 ? 13.448  11.021  17.729 1.00 40.48  ? 300 GLU C CA  1 
ATOM   7515 C  C   . GLU C  1  287 ? 12.989  11.048  19.186 1.00 34.93  ? 300 GLU C C   1 
ATOM   7516 O  O   . GLU C  1  287 ? 13.414  10.223  19.976 1.00 36.31  ? 300 GLU C O   1 
ATOM   7517 C  CB  . GLU C  1  287 ? 14.508  12.092  17.466 1.00 47.69  ? 300 GLU C CB  1 
ATOM   7518 C  CG  . GLU C  1  287 ? 15.169  11.988  16.093 1.00 56.35  ? 300 GLU C CG  1 
ATOM   7519 C  CD  . GLU C  1  287 ? 15.571  13.302  15.420 1.00 69.51  ? 300 GLU C CD  1 
ATOM   7520 O  OE1 . GLU C  1  287 ? 15.592  14.377  16.059 1.00 78.13  ? 300 GLU C OE1 1 
ATOM   7521 O  OE2 . GLU C  1  287 ? 15.812  13.250  14.199 1.00 77.37  ? 300 GLU C OE2 1 
ATOM   7522 N  N   . PHE C  1  288 ? 12.089  11.979  19.516 1.00 34.99  ? 301 PHE C N   1 
ATOM   7523 C  CA  . PHE C  1  288 ? 11.565  12.105  20.866 1.00 37.12  ? 301 PHE C CA  1 
ATOM   7524 C  C   . PHE C  1  288 ? 10.904  10.800  21.304 1.00 37.84  ? 301 PHE C C   1 
ATOM   7525 O  O   . PHE C  1  288 ? 11.142  10.312  22.398 1.00 35.93  ? 301 PHE C O   1 
ATOM   7526 C  CB  . PHE C  1  288 ? 10.568  13.265  20.969 1.00 42.56  ? 301 PHE C CB  1 
ATOM   7527 C  CG  . PHE C  1  288 ? 10.025  13.450  22.381 1.00 44.28  ? 301 PHE C CG  1 
ATOM   7528 C  CD1 . PHE C  1  288 ? 10.711  14.230  23.311 1.00 47.36  ? 301 PHE C CD1 1 
ATOM   7529 C  CD2 . PHE C  1  288 ? 8.857   12.809  22.789 1.00 46.80  ? 301 PHE C CD2 1 
ATOM   7530 C  CE1 . PHE C  1  288 ? 10.222  14.378  24.609 1.00 49.99  ? 301 PHE C CE1 1 
ATOM   7531 C  CE2 . PHE C  1  288 ? 8.382   12.952  24.094 1.00 49.20  ? 301 PHE C CE2 1 
ATOM   7532 C  CZ  . PHE C  1  288 ? 9.054   13.749  24.994 1.00 45.23  ? 301 PHE C CZ  1 
ATOM   7533 N  N   . VAL C  1  289 ? 10.062  10.225  20.437 1.00 33.05  ? 302 VAL C N   1 
ATOM   7534 C  CA  . VAL C  1  289 ? 9.318   9.036   20.809 1.00 31.90  ? 302 VAL C CA  1 
ATOM   7535 C  C   . VAL C  1  289 ? 10.257  7.837   20.928 1.00 28.86  ? 302 VAL C C   1 
ATOM   7536 O  O   . VAL C  1  289 ? 10.054  6.975   21.789 1.00 29.93  ? 302 VAL C O   1 
ATOM   7537 C  CB  . VAL C  1  289 ? 8.161   8.749   19.837 1.00 32.27  ? 302 VAL C CB  1 
ATOM   7538 C  CG1 . VAL C  1  289 ? 7.599   7.354   20.051 1.00 33.09  ? 302 VAL C CG1 1 
ATOM   7539 C  CG2 . VAL C  1  289 ? 7.062   9.792   19.935 1.00 33.09  ? 302 VAL C CG2 1 
ATOM   7540 N  N   . VAL C  1  290 ? 11.274  7.743   20.062 1.00 29.20  ? 303 VAL C N   1 
ATOM   7541 C  CA  . VAL C  1  290 ? 12.219  6.647   20.189 1.00 31.89  ? 303 VAL C CA  1 
ATOM   7542 C  C   . VAL C  1  290 ? 12.935  6.731   21.548 1.00 30.88  ? 303 VAL C C   1 
ATOM   7543 O  O   . VAL C  1  290 ? 13.114  5.715   22.224 1.00 28.29  ? 303 VAL C O   1 
ATOM   7544 C  CB  . VAL C  1  290 ? 13.199  6.609   19.000 1.00 35.02  ? 303 VAL C CB  1 
ATOM   7545 C  CG1 . VAL C  1  290 ? 14.356  5.649   19.246 1.00 36.94  ? 303 VAL C CG1 1 
ATOM   7546 C  CG2 . VAL C  1  290 ? 12.478  6.240   17.705 1.00 34.86  ? 303 VAL C CG2 1 
ATOM   7547 N  N   . GLY C  1  291 ? 13.280  7.951   21.965 1.00 30.31  ? 304 GLY C N   1 
ATOM   7548 C  CA  . GLY C  1  291 ? 13.817  8.206   23.304 1.00 35.45  ? 304 GLY C CA  1 
ATOM   7549 C  C   . GLY C  1  291 ? 12.853  7.766   24.402 1.00 34.28  ? 304 GLY C C   1 
ATOM   7550 O  O   . GLY C  1  291 ? 13.249  7.091   25.357 1.00 35.23  ? 304 GLY C O   1 
ATOM   7551 N  N   . SER C  1  292 ? 11.562  8.092   24.231 1.00 34.33  ? 305 SER C N   1 
ATOM   7552 C  CA  . SER C  1  292 ? 10.569  7.688   25.217 1.00 33.79  ? 305 SER C CA  1 
ATOM   7553 C  C   . SER C  1  292 ? 10.505  6.164   25.320 1.00 34.55  ? 305 SER C C   1 
ATOM   7554 O  O   . SER C  1  292 ? 10.391  5.613   26.423 1.00 32.74  ? 305 SER C O   1 
ATOM   7555 C  CB  . SER C  1  292 ? 9.214   8.265   24.926 1.00 33.24  ? 305 SER C CB  1 
ATOM   7556 O  OG  . SER C  1  292 ? 9.287   9.668   24.726 1.00 35.44  ? 305 SER C OG  1 
ATOM   7557 N  N   . VAL C  1  293 ? 10.569  5.479   24.176 1.00 31.03  ? 306 VAL C N   1 
ATOM   7558 C  CA  . VAL C  1  293 ? 10.508  4.026   24.188 1.00 29.03  ? 306 VAL C CA  1 
ATOM   7559 C  C   . VAL C  1  293 ? 11.722  3.460   24.935 1.00 29.23  ? 306 VAL C C   1 
ATOM   7560 O  O   . VAL C  1  293 ? 11.604  2.474   25.657 1.00 29.61  ? 306 VAL C O   1 
ATOM   7561 C  CB  . VAL C  1  293 ? 10.411  3.456   22.764 1.00 31.05  ? 306 VAL C CB  1 
ATOM   7562 C  CG1 . VAL C  1  293 ? 10.601  1.938   22.741 1.00 31.76  ? 306 VAL C CG1 1 
ATOM   7563 C  CG2 . VAL C  1  293 ? 9.083   3.844   22.114 1.00 34.09  ? 306 VAL C CG2 1 
ATOM   7564 N  N   . GLN C  1  294 ? 12.891  4.087   24.770 1.00 33.12  ? 307 GLN C N   1 
ATOM   7565 C  CA  . GLN C  1  294 ? 14.090  3.605   25.444 1.00 37.02  ? 307 GLN C CA  1 
ATOM   7566 C  C   . GLN C  1  294 ? 13.965  3.761   26.965 1.00 35.80  ? 307 GLN C C   1 
ATOM   7567 O  O   . GLN C  1  294 ? 14.482  2.920   27.711 1.00 35.30  ? 307 GLN C O   1 
ATOM   7568 C  CB  . GLN C  1  294 ? 15.335  4.338   24.951 1.00 40.36  ? 307 GLN C CB  1 
ATOM   7569 C  CG  . GLN C  1  294 ? 15.726  4.006   23.519 1.00 43.65  ? 307 GLN C CG  1 
ATOM   7570 C  CD  . GLN C  1  294 ? 16.836  4.900   22.993 1.00 44.25  ? 307 GLN C CD  1 
ATOM   7571 O  OE1 . GLN C  1  294 ? 16.617  6.018   22.520 1.00 47.25  ? 307 GLN C OE1 1 
ATOM   7572 N  NE2 . GLN C  1  294 ? 18.057  4.412   23.038 1.00 44.38  ? 307 GLN C NE2 1 
ATOM   7573 N  N   . GLU C  1  295 ? 13.263  4.808   27.419 1.00 38.07  ? 308 GLU C N   1 
ATOM   7574 C  CA  . GLU C  1  295 ? 13.042  5.012   28.848 1.00 40.27  ? 308 GLU C CA  1 
ATOM   7575 C  C   . GLU C  1  295 ? 12.116  3.943   29.406 1.00 39.01  ? 308 GLU C C   1 
ATOM   7576 O  O   . GLU C  1  295 ? 12.350  3.483   30.522 1.00 34.85  ? 308 GLU C O   1 
ATOM   7577 C  CB  . GLU C  1  295 ? 12.489  6.391   29.193 1.00 44.53  ? 308 GLU C CB  1 
ATOM   7578 C  CG  . GLU C  1  295 ? 13.484  7.516   28.922 1.00 49.29  ? 308 GLU C CG  1 
ATOM   7579 C  CD  . GLU C  1  295 ? 12.896  8.923   29.009 1.00 62.10  ? 308 GLU C CD  1 
ATOM   7580 O  OE1 . GLU C  1  295 ? 11.676  9.080   29.250 1.00 73.57  ? 308 GLU C OE1 1 
ATOM   7581 O  OE2 . GLU C  1  295 ? 13.663  9.892   28.846 1.00 72.56  ? 308 GLU C OE2 1 
ATOM   7582 N  N   . LEU C  1  296 ? 11.097  3.530   28.626 1.00 30.69  ? 309 LEU C N   1 
ATOM   7583 C  CA  . LEU C  1  296 ? 10.203  2.459   29.034 1.00 29.14  ? 309 LEU C CA  1 
ATOM   7584 C  C   . LEU C  1  296 ? 10.915  1.113   29.038 1.00 29.70  ? 309 LEU C C   1 
ATOM   7585 O  O   . LEU C  1  296 ? 10.568  0.242   29.845 1.00 34.20  ? 309 LEU C O   1 
ATOM   7586 C  CB  . LEU C  1  296 ? 8.961   2.373   28.142 1.00 30.69  ? 309 LEU C CB  1 
ATOM   7587 C  CG  . LEU C  1  296 ? 8.056   3.600   28.107 1.00 32.46  ? 309 LEU C CG  1 
ATOM   7588 C  CD1 . LEU C  1  296 ? 6.938   3.391   27.098 1.00 36.35  ? 309 LEU C CD1 1 
ATOM   7589 C  CD2 . LEU C  1  296 ? 7.446   3.950   29.472 1.00 35.71  ? 309 LEU C CD2 1 
ATOM   7590 N  N   . TYR C  1  297 ? 11.839  0.918   28.083 1.00 31.61  ? 310 TYR C N   1 
ATOM   7591 C  CA  . TYR C  1  297 ? 12.461  -0.379  27.855 1.00 31.06  ? 310 TYR C CA  1 
ATOM   7592 C  C   . TYR C  1  297 ? 13.981  -0.194  27.793 1.00 34.57  ? 310 TYR C C   1 
ATOM   7593 O  O   . TYR C  1  297 ? 14.577  -0.162  26.707 1.00 32.33  ? 310 TYR C O   1 
ATOM   7594 C  CB  . TYR C  1  297 ? 11.935  -1.042  26.578 1.00 32.86  ? 310 TYR C CB  1 
ATOM   7595 C  CG  . TYR C  1  297 ? 10.444  -1.354  26.596 1.00 30.57  ? 310 TYR C CG  1 
ATOM   7596 C  CD1 . TYR C  1  297 ? 9.956   -2.496  27.216 1.00 32.47  ? 310 TYR C CD1 1 
ATOM   7597 C  CD2 . TYR C  1  297 ? 9.526   -0.495  26.007 1.00 32.43  ? 310 TYR C CD2 1 
ATOM   7598 C  CE1 . TYR C  1  297 ? 8.604   -2.790  27.233 1.00 32.05  ? 310 TYR C CE1 1 
ATOM   7599 C  CE2 . TYR C  1  297 ? 8.167   -0.770  26.010 1.00 30.75  ? 310 TYR C CE2 1 
ATOM   7600 C  CZ  . TYR C  1  297 ? 7.704   -1.917  26.634 1.00 32.47  ? 310 TYR C CZ  1 
ATOM   7601 O  OH  . TYR C  1  297 ? 6.366   -2.171  26.686 1.00 31.35  ? 310 TYR C OH  1 
ATOM   7602 N  N   . PRO C  1  298 ? 14.643  0.000   28.956 1.00 34.94  ? 311 PRO C N   1 
ATOM   7603 C  CA  . PRO C  1  298 ? 16.070  0.320   29.004 1.00 32.40  ? 311 PRO C CA  1 
ATOM   7604 C  C   . PRO C  1  298 ? 17.012  -0.744  28.458 1.00 27.23  ? 311 PRO C C   1 
ATOM   7605 O  O   . PRO C  1  298 ? 18.056  -0.391  27.931 1.00 29.84  ? 311 PRO C O   1 
ATOM   7606 C  CB  . PRO C  1  298 ? 16.387  0.548   30.504 1.00 37.09  ? 311 PRO C CB  1 
ATOM   7607 C  CG  . PRO C  1  298 ? 15.060  0.652   31.187 1.00 41.87  ? 311 PRO C CG  1 
ATOM   7608 C  CD  . PRO C  1  298 ? 14.018  0.024   30.282 1.00 37.59  ? 311 PRO C CD  1 
ATOM   7609 N  N   . ASN C  1  299 ? 16.699  -2.024  28.664 1.00 29.31  ? 312 ASN C N   1 
ATOM   7610 C  CA  . ASN C  1  299 ? 17.640  -3.073  28.316 1.00 32.12  ? 312 ASN C CA  1 
ATOM   7611 C  C   . ASN C  1  299 ? 16.916  -4.377  28.032 1.00 35.32  ? 312 ASN C C   1 
ATOM   7612 O  O   . ASN C  1  299 ? 17.176  -5.379  28.697 1.00 33.75  ? 312 ASN C O   1 
ATOM   7613 C  CB  . ASN C  1  299 ? 18.667  -3.232  29.439 1.00 34.12  ? 312 ASN C CB  1 
ATOM   7614 C  CG  . ASN C  1  299 ? 19.786  -4.179  29.090 1.00 33.65  ? 312 ASN C CG  1 
ATOM   7615 O  OD1 . ASN C  1  299 ? 20.035  -5.107  29.858 1.00 32.87  ? 312 ASN C OD1 1 
ATOM   7616 N  ND2 . ASN C  1  299 ? 20.456  -3.980  27.960 1.00 32.07  ? 312 ASN C ND2 1 
ATOM   7617 N  N   . PRO C  1  300 ? 16.038  -4.435  26.998 1.00 33.85  ? 313 PRO C N   1 
ATOM   7618 C  CA  . PRO C  1  300 ? 15.268  -5.647  26.726 1.00 33.49  ? 313 PRO C CA  1 
ATOM   7619 C  C   . PRO C  1  300 ? 16.114  -6.729  26.065 1.00 31.57  ? 313 PRO C C   1 
ATOM   7620 O  O   . PRO C  1  300 ? 17.084  -6.430  25.373 1.00 34.30  ? 313 PRO C O   1 
ATOM   7621 C  CB  . PRO C  1  300 ? 14.132  -5.125  25.789 1.00 33.69  ? 313 PRO C CB  1 
ATOM   7622 C  CG  . PRO C  1  300 ? 14.831  -4.036  25.016 1.00 33.20  ? 313 PRO C CG  1 
ATOM   7623 C  CD  . PRO C  1  300 ? 15.788  -3.362  26.022 1.00 33.47  ? 313 PRO C CD  1 
ATOM   7624 N  N   . THR C  1  301 ? 15.701  -7.981  26.264 1.00 32.25  ? 314 THR C N   1 
ATOM   7625 C  CA  . THR C  1  301 ? 16.290  -9.119  25.588 1.00 35.84  ? 314 THR C CA  1 
ATOM   7626 C  C   . THR C  1  301 ? 15.157  -10.035 25.126 1.00 34.70  ? 314 THR C C   1 
ATOM   7627 O  O   . THR C  1  301 ? 13.988  -9.772  25.421 1.00 37.54  ? 314 THR C O   1 
ATOM   7628 C  CB  . THR C  1  301 ? 17.272  -9.827  26.531 1.00 45.36  ? 314 THR C CB  1 
ATOM   7629 O  OG1 . THR C  1  301 ? 16.554  -10.238 27.688 1.00 47.58  ? 314 THR C OG1 1 
ATOM   7630 C  CG2 . THR C  1  301 ? 18.414  -8.931  26.982 1.00 45.36  ? 314 THR C CG2 1 
ATOM   7631 N  N   . GLY C  1  302 ? 15.517  -11.099 24.394 1.00 33.87  ? 315 GLY C N   1 
ATOM   7632 C  CA  . GLY C  1  302 ? 14.572  -12.146 24.030 1.00 39.21  ? 315 GLY C CA  1 
ATOM   7633 C  C   . GLY C  1  302 ? 13.439  -11.634 23.133 1.00 38.67  ? 315 GLY C C   1 
ATOM   7634 O  O   . GLY C  1  302 ? 13.658  -10.782 22.278 1.00 36.77  ? 315 GLY C O   1 
ATOM   7635 N  N   . ILE C  1  303 ? 12.235  -12.168 23.350 1.00 38.37  ? 316 ILE C N   1 
ATOM   7636 C  CA  . ILE C  1  303 ? 11.057  -11.869 22.541 1.00 41.43  ? 316 ILE C CA  1 
ATOM   7637 C  C   . ILE C  1  303 ? 10.692  -10.394 22.687 1.00 38.22  ? 316 ILE C C   1 
ATOM   7638 O  O   . ILE C  1  303 ? 10.304  -9.762  21.708 1.00 35.76  ? 316 ILE C O   1 
ATOM   7639 C  CB  . ILE C  1  303 ? 9.882   -12.805 22.899 1.00 49.41  ? 316 ILE C CB  1 
ATOM   7640 C  CG1 . ILE C  1  303 ? 10.288  -14.280 22.716 1.00 66.76  ? 316 ILE C CG1 1 
ATOM   7641 C  CG2 . ILE C  1  303 ? 8.632   -12.501 22.073 1.00 48.42  ? 316 ILE C CG2 1 
ATOM   7642 C  CD1 . ILE C  1  303 ? 9.471   -15.272 23.531 1.00 79.27  ? 316 ILE C CD1 1 
ATOM   7643 N  N   . LEU C  1  304 ? 10.852  -9.824  23.892 1.00 34.93  ? 317 LEU C N   1 
ATOM   7644 C  CA  . LEU C  1  304 ? 10.522  -8.419  24.084 1.00 33.73  ? 317 LEU C CA  1 
ATOM   7645 C  C   . LEU C  1  304 ? 11.408  -7.546  23.187 1.00 34.81  ? 317 LEU C C   1 
ATOM   7646 O  O   . LEU C  1  304 ? 10.917  -6.635  22.514 1.00 31.27  ? 317 LEU C O   1 
ATOM   7647 C  CB  . LEU C  1  304 ? 10.609  -8.023  25.554 1.00 35.60  ? 317 LEU C CB  1 
ATOM   7648 C  CG  . LEU C  1  304 ? 10.390  -6.539  25.859 1.00 37.42  ? 317 LEU C CG  1 
ATOM   7649 C  CD1 . LEU C  1  304 ? 9.022   -6.041  25.374 1.00 37.05  ? 317 LEU C CD1 1 
ATOM   7650 C  CD2 . LEU C  1  304 ? 10.544  -6.263  27.357 1.00 40.36  ? 317 LEU C CD2 1 
ATOM   7651 N  N   . ARG C  1  305 ? 12.718  -7.831  23.147 1.00 32.33  ? 318 ARG C N   1 
ATOM   7652 C  CA  A ARG C  1  305 ? 13.622  -7.072  22.296 0.50 32.27  ? 318 ARG C CA  1 
ATOM   7653 C  CA  B ARG C  1  305 ? 13.641  -7.098  22.293 0.50 35.03  ? 318 ARG C CA  1 
ATOM   7654 C  C   . ARG C  1  305 ? 13.219  -7.235  20.831 1.00 31.49  ? 318 ARG C C   1 
ATOM   7655 O  O   . ARG C  1  305 ? 13.181  -6.263  20.104 1.00 27.80  ? 318 ARG C O   1 
ATOM   7656 C  CB  A ARG C  1  305 ? 15.077  -7.514  22.482 0.50 28.18  ? 318 ARG C CB  1 
ATOM   7657 C  CB  B ARG C  1  305 ? 15.078  -7.611  22.444 0.50 34.69  ? 318 ARG C CB  1 
ATOM   7658 C  CG  A ARG C  1  305 ? 16.076  -7.003  21.460 0.50 26.68  ? 318 ARG C CG  1 
ATOM   7659 C  CG  B ARG C  1  305 ? 16.146  -6.778  21.745 0.50 37.34  ? 318 ARG C CG  1 
ATOM   7660 C  CD  A ARG C  1  305 ? 17.427  -7.691  21.583 0.50 24.86  ? 318 ARG C CD  1 
ATOM   7661 C  CD  B ARG C  1  305 ? 17.555  -7.348  21.936 0.50 37.91  ? 318 ARG C CD  1 
ATOM   7662 N  NE  A ARG C  1  305 ? 18.314  -7.183  20.539 0.50 20.89  ? 318 ARG C NE  1 
ATOM   7663 N  NE  B ARG C  1  305 ? 18.609  -6.415  21.520 0.50 38.76  ? 318 ARG C NE  1 
ATOM   7664 C  CZ  A ARG C  1  305 ? 18.449  -7.741  19.384 0.50 18.27  ? 318 ARG C CZ  1 
ATOM   7665 C  CZ  B ARG C  1  305 ? 19.043  -5.379  22.232 0.50 31.64  ? 318 ARG C CZ  1 
ATOM   7666 N  NH1 A ARG C  1  305 ? 17.875  -8.906  19.188 0.50 17.39  ? 318 ARG C NH1 1 
ATOM   7667 N  NH1 B ARG C  1  305 ? 18.747  -5.191  23.529 0.50 40.66  ? 318 ARG C NH1 1 
ATOM   7668 N  NH2 A ARG C  1  305 ? 19.156  -7.126  18.463 0.50 17.22  ? 318 ARG C NH2 1 
ATOM   7669 N  NH2 B ARG C  1  305 ? 19.763  -4.501  21.627 0.50 24.62  ? 318 ARG C NH2 1 
ATOM   7670 N  N   . ARG C  1  306 ? 12.946  -8.464  20.414 1.00 31.22  ? 319 ARG C N   1 
ATOM   7671 C  CA  . ARG C  1  306 ? 12.589  -8.754  19.033 1.00 36.98  ? 319 ARG C CA  1 
ATOM   7672 C  C   . ARG C  1  306 ? 11.335  -7.973  18.640 1.00 32.67  ? 319 ARG C C   1 
ATOM   7673 O  O   . ARG C  1  306 ? 11.304  -7.360  17.576 1.00 32.14  ? 319 ARG C O   1 
ATOM   7674 C  CB  . ARG C  1  306 ? 12.364  -10.259 18.875 1.00 39.65  ? 319 ARG C CB  1 
ATOM   7675 C  CG  . ARG C  1  306 ? 12.178  -10.731 17.440 1.00 51.41  ? 319 ARG C CG  1 
ATOM   7676 C  CD  . ARG C  1  306 ? 11.530  -12.125 17.343 1.00 55.20  ? 319 ARG C CD  1 
ATOM   7677 N  NE  . ARG C  1  306 ? 10.136  -12.099 17.814 1.00 65.19  ? 319 ARG C NE  1 
ATOM   7678 C  CZ  . ARG C  1  306 ? 9.344   -13.151 18.012 1.00 72.26  ? 319 ARG C CZ  1 
ATOM   7679 N  NH1 . ARG C  1  306 ? 9.761   -14.377 17.752 1.00 75.47  ? 319 ARG C NH1 1 
ATOM   7680 N  NH2 . ARG C  1  306 ? 8.131   -12.974 18.487 1.00 74.11  ? 319 ARG C NH2 1 
ATOM   7681 N  N   . ASN C  1  307 ? 10.317  -7.992  19.503 1.00 30.94  ? 320 ASN C N   1 
ATOM   7682 C  CA  . ASN C  1  307 ? 9.049   -7.347  19.187 1.00 31.38  ? 320 ASN C CA  1 
ATOM   7683 C  C   . ASN C  1  307 ? 9.186   -5.825  19.216 1.00 31.03  ? 320 ASN C C   1 
ATOM   7684 O  O   . ASN C  1  307 ? 8.526   -5.115  18.447 1.00 31.08  ? 320 ASN C O   1 
ATOM   7685 C  CB  . ASN C  1  307 ? 7.928   -7.871  20.069 1.00 31.24  ? 320 ASN C CB  1 
ATOM   7686 C  CG  . ASN C  1  307 ? 7.544   -9.281  19.709 1.00 32.97  ? 320 ASN C CG  1 
ATOM   7687 O  OD1 . ASN C  1  307 ? 8.190   -9.901  18.865 1.00 34.47  ? 320 ASN C OD1 1 
ATOM   7688 N  ND2 . ASN C  1  307 ? 6.491   -9.798  20.312 1.00 35.47  ? 320 ASN C ND2 1 
ATOM   7689 N  N   . LEU C  1  308 ? 10.084  -5.306  20.057 1.00 28.41  ? 321 LEU C N   1 
ATOM   7690 C  CA  . LEU C  1  308 ? 10.375  -3.874  20.045 1.00 29.74  ? 321 LEU C CA  1 
ATOM   7691 C  C   . LEU C  1  308 ? 11.001  -3.474  18.712 1.00 27.98  ? 321 LEU C C   1 
ATOM   7692 O  O   . LEU C  1  308 ? 10.652  -2.444  18.149 1.00 29.05  ? 321 LEU C O   1 
ATOM   7693 C  CB  . LEU C  1  308 ? 11.283  -3.454  21.197 1.00 31.00  ? 321 LEU C CB  1 
ATOM   7694 C  CG  . LEU C  1  308 ? 10.555  -3.136  22.506 1.00 33.27  ? 321 LEU C CG  1 
ATOM   7695 C  CD1 . LEU C  1  308 ? 11.523  -3.260  23.694 1.00 35.27  ? 321 LEU C CD1 1 
ATOM   7696 C  CD2 . LEU C  1  308 ? 9.949   -1.722  22.409 1.00 34.45  ? 321 LEU C CD2 1 
ATOM   7697 N  N   . ILE C  1  309 ? 11.973  -4.253  18.256 1.00 27.85  ? 322 ILE C N   1 
ATOM   7698 C  CA  . ILE C  1  309 ? 12.686  -3.933  17.021 1.00 29.13  ? 322 ILE C CA  1 
ATOM   7699 C  C   . ILE C  1  309 ? 11.677  -3.906  15.860 1.00 26.36  ? 322 ILE C C   1 
ATOM   7700 O  O   . ILE C  1  309 ? 11.675  -2.988  15.040 1.00 29.90  ? 322 ILE C O   1 
ATOM   7701 C  CB  . ILE C  1  309 ? 13.823  -4.939  16.770 1.00 28.38  ? 322 ILE C CB  1 
ATOM   7702 C  CG1 . ILE C  1  309 ? 14.959  -4.748  17.753 1.00 32.08  ? 322 ILE C CG1 1 
ATOM   7703 C  CG2 . ILE C  1  309 ? 14.327  -4.875  15.326 1.00 31.47  ? 322 ILE C CG2 1 
ATOM   7704 C  CD1 . ILE C  1  309 ? 15.946  -5.901  17.805 1.00 29.82  ? 322 ILE C CD1 1 
ATOM   7705 N  N   . LYS C  1  310 ? 10.802  -4.905  15.816 1.00 29.82  ? 323 LYS C N   1 
ATOM   7706 C  CA  . LYS C  1  310 ? 9.810   -5.001  14.755 1.00 31.38  ? 323 LYS C CA  1 
ATOM   7707 C  C   . LYS C  1  310 ? 8.841   -3.827  14.777 1.00 30.07  ? 323 LYS C C   1 
ATOM   7708 O  O   . LYS C  1  310 ? 8.625   -3.189  13.738 1.00 30.94  ? 323 LYS C O   1 
ATOM   7709 C  CB  . LYS C  1  310 ? 9.103   -6.344  14.854 1.00 32.84  ? 323 LYS C CB  1 
ATOM   7710 C  CG  . LYS C  1  310 ? 9.957   -7.455  14.306 1.00 34.35  ? 323 LYS C CG  1 
ATOM   7711 C  CD  . LYS C  1  310 ? 9.353   -8.831  14.514 1.00 44.45  ? 323 LYS C CD  1 
ATOM   7712 C  CE  . LYS C  1  310 ? 10.145  -9.850  13.774 1.00 53.99  ? 323 LYS C CE  1 
ATOM   7713 N  NZ  . LYS C  1  310 ? 9.547   -11.166 13.984 1.00 62.76  ? 323 LYS C NZ  1 
ATOM   7714 N  N   . ASN C  1  311 ? 8.286   -3.529  15.954 1.00 26.40  ? 324 ASN C N   1 
ATOM   7715 C  CA  . ASN C  1  311 ? 7.289   -2.478  16.081 1.00 26.17  ? 324 ASN C CA  1 
ATOM   7716 C  C   . ASN C  1  311 ? 7.897   -1.117  15.767 1.00 26.60  ? 324 ASN C C   1 
ATOM   7717 O  O   . ASN C  1  311 ? 7.264   -0.281  15.121 1.00 28.91  ? 324 ASN C O   1 
ATOM   7718 C  CB  . ASN C  1  311 ? 6.596   -2.531  17.436 1.00 28.49  ? 324 ASN C CB  1 
ATOM   7719 C  CG  . ASN C  1  311 ? 5.501   -3.564  17.460 1.00 29.72  ? 324 ASN C CG  1 
ATOM   7720 O  OD1 . ASN C  1  311 ? 4.400   -3.308  16.958 1.00 32.96  ? 324 ASN C OD1 1 
ATOM   7721 N  ND2 . ASN C  1  311 ? 5.774   -4.720  18.032 1.00 31.35  ? 324 ASN C ND2 1 
ATOM   7722 N  N   . LEU C  1  312 ? 9.147   -0.902  16.183 1.00 25.07  ? 325 LEU C N   1 
ATOM   7723 C  CA  . LEU C  1  312 ? 9.820   0.358   15.888 1.00 25.46  ? 325 LEU C CA  1 
ATOM   7724 C  C   . LEU C  1  312 ? 9.971   0.524   14.378 1.00 26.30  ? 325 LEU C C   1 
ATOM   7725 O  O   . LEU C  1  312 ? 9.787   1.620   13.845 1.00 26.63  ? 325 LEU C O   1 
ATOM   7726 C  CB  . LEU C  1  312 ? 11.181  0.406   16.588 1.00 25.64  ? 325 LEU C CB  1 
ATOM   7727 C  CG  . LEU C  1  312 ? 11.132  0.749   18.079 1.00 27.73  ? 325 LEU C CG  1 
ATOM   7728 C  CD1 . LEU C  1  312 ? 12.439  0.402   18.734 1.00 30.52  ? 325 LEU C CD1 1 
ATOM   7729 C  CD2 . LEU C  1  312 ? 10.842  2.229   18.275 1.00 28.91  ? 325 LEU C CD2 1 
ATOM   7730 N  N   . HIS C  1  313 ? 10.345  -0.561  13.702 1.00 27.79  ? 326 HIS C N   1 
ATOM   7731 C  CA  . HIS C  1  313 ? 10.494  -0.533  12.250 1.00 27.87  ? 326 HIS C CA  1 
ATOM   7732 C  C   . HIS C  1  313 ? 9.139   -0.273  11.578 1.00 27.20  ? 326 HIS C C   1 
ATOM   7733 O  O   . HIS C  1  313 ? 9.052   0.574   10.691 1.00 28.04  ? 326 HIS C O   1 
ATOM   7734 C  CB  . HIS C  1  313 ? 11.182  -1.795  11.729 1.00 30.33  ? 326 HIS C CB  1 
ATOM   7735 C  CG  . HIS C  1  313 ? 11.361  -1.740  10.257 1.00 33.19  ? 326 HIS C CG  1 
ATOM   7736 N  ND1 . HIS C  1  313 ? 12.181  -0.796  9.679  1.00 32.48  ? 326 HIS C ND1 1 
ATOM   7737 C  CD2 . HIS C  1  313 ? 10.735  -2.382  9.242  1.00 36.33  ? 326 HIS C CD2 1 
ATOM   7738 C  CE1 . HIS C  1  313 ? 12.103  -0.923  8.360  1.00 37.75  ? 326 HIS C CE1 1 
ATOM   7739 N  NE2 . HIS C  1  313 ? 11.230  -1.873  8.068  1.00 32.35  ? 326 HIS C NE2 1 
ATOM   7740 N  N   . TYR C  1  314 ? 8.084   -0.965  12.014 1.00 28.55  ? 327 TYR C N   1 
ATOM   7741 C  CA  . TYR C  1  314 ? 6.758   -0.749  11.446 1.00 28.89  ? 327 TYR C CA  1 
ATOM   7742 C  C   . TYR C  1  314 ? 6.367   0.719   11.568 1.00 30.39  ? 327 TYR C C   1 
ATOM   7743 O  O   . TYR C  1  314 ? 5.903   1.328   10.598 1.00 25.72  ? 327 TYR C O   1 
ATOM   7744 C  CB  . TYR C  1  314 ? 5.701   -1.609  12.139 1.00 30.67  ? 327 TYR C CB  1 
ATOM   7745 C  CG  . TYR C  1  314 ? 5.925   -3.104  12.033 1.00 28.85  ? 327 TYR C CG  1 
ATOM   7746 C  CD1 . TYR C  1  314 ? 6.702   -3.658  11.021 1.00 31.24  ? 327 TYR C CD1 1 
ATOM   7747 C  CD2 . TYR C  1  314 ? 5.368   -3.963  12.969 1.00 31.25  ? 327 TYR C CD2 1 
ATOM   7748 C  CE1 . TYR C  1  314 ? 6.923   -5.027  10.946 1.00 33.33  ? 327 TYR C CE1 1 
ATOM   7749 C  CE2 . TYR C  1  314 ? 5.561   -5.330  12.888 1.00 28.84  ? 327 TYR C CE2 1 
ATOM   7750 C  CZ  . TYR C  1  314 ? 6.354   -5.860  11.892 1.00 31.75  ? 327 TYR C CZ  1 
ATOM   7751 O  OH  . TYR C  1  314 ? 6.520   -7.222  11.853 1.00 32.43  ? 327 TYR C OH  1 
ATOM   7752 N  N   . TRP C  1  315 ? 6.614   1.298   12.749 1.00 27.76  ? 328 TRP C N   1 
ATOM   7753 C  CA  . TRP C  1  315 ? 6.276   2.687   12.987 1.00 28.61  ? 328 TRP C CA  1 
ATOM   7754 C  C   . TRP C  1  315 ? 7.036   3.584   12.006 1.00 28.41  ? 328 TRP C C   1 
ATOM   7755 O  O   . TRP C  1  315 ? 6.463   4.484   11.388 1.00 29.09  ? 328 TRP C O   1 
ATOM   7756 C  CB  . TRP C  1  315 ? 6.539   3.086   14.447 1.00 28.09  ? 328 TRP C CB  1 
ATOM   7757 C  CG  . TRP C  1  315 ? 5.961   4.431   14.789 1.00 27.75  ? 328 TRP C CG  1 
ATOM   7758 C  CD1 . TRP C  1  315 ? 4.690   4.852   14.534 1.00 30.31  ? 328 TRP C CD1 1 
ATOM   7759 C  CD2 . TRP C  1  315 ? 6.629   5.541   15.420 1.00 30.36  ? 328 TRP C CD2 1 
ATOM   7760 N  NE1 . TRP C  1  315 ? 4.525   6.147   14.939 1.00 31.76  ? 328 TRP C NE1 1 
ATOM   7761 C  CE2 . TRP C  1  315 ? 5.693   6.595   15.492 1.00 31.97  ? 328 TRP C CE2 1 
ATOM   7762 C  CE3 . TRP C  1  315 ? 7.917   5.734   15.939 1.00 32.41  ? 328 TRP C CE3 1 
ATOM   7763 C  CZ2 . TRP C  1  315 ? 5.997   7.820   16.071 1.00 34.58  ? 328 TRP C CZ2 1 
ATOM   7764 C  CZ3 . TRP C  1  315 ? 8.223   6.948   16.495 1.00 32.12  ? 328 TRP C CZ3 1 
ATOM   7765 C  CH2 . TRP C  1  315 ? 7.284   7.981   16.543 1.00 34.99  ? 328 TRP C CH2 1 
ATOM   7766 N  N   . TRP C  1  316 ? 8.332   3.330   11.864 1.00 26.54  ? 329 TRP C N   1 
ATOM   7767 C  CA  . TRP C  1  316 ? 9.161   4.107   10.967 1.00 27.92  ? 329 TRP C CA  1 
ATOM   7768 C  C   . TRP C  1  316 ? 8.624   4.058   9.528  1.00 26.63  ? 329 TRP C C   1 
ATOM   7769 O  O   . TRP C  1  316 ? 8.677   5.062   8.823  1.00 27.45  ? 329 TRP C O   1 
ATOM   7770 C  CB  . TRP C  1  316 ? 10.633  3.683   11.044 1.00 29.68  ? 329 TRP C CB  1 
ATOM   7771 C  CG  . TRP C  1  316 ? 11.459  4.407   10.013 1.00 30.30  ? 329 TRP C CG  1 
ATOM   7772 C  CD1 . TRP C  1  316 ? 11.993  5.658   10.102 1.00 29.52  ? 329 TRP C CD1 1 
ATOM   7773 C  CD2 . TRP C  1  316 ? 11.721  3.957   8.670  1.00 28.87  ? 329 TRP C CD2 1 
ATOM   7774 N  NE1 . TRP C  1  316 ? 12.592  5.997   8.922  1.00 31.36  ? 329 TRP C NE1 1 
ATOM   7775 C  CE2 . TRP C  1  316 ? 12.426  4.987   8.018  1.00 30.50  ? 329 TRP C CE2 1 
ATOM   7776 C  CE3 . TRP C  1  316 ? 11.417  2.793   7.963  1.00 30.24  ? 329 TRP C CE3 1 
ATOM   7777 C  CZ2 . TRP C  1  316 ? 12.844  4.887   6.690  1.00 30.56  ? 329 TRP C CZ2 1 
ATOM   7778 C  CZ3 . TRP C  1  316 ? 11.815  2.700   6.647  1.00 31.66  ? 329 TRP C CZ3 1 
ATOM   7779 C  CH2 . TRP C  1  316 ? 12.495  3.745   6.019  1.00 29.27  ? 329 TRP C CH2 1 
ATOM   7780 N  N   . THR C  1  317 ? 8.095   2.910   9.078  1.00 26.56  ? 330 THR C N   1 
ATOM   7781 C  CA  . THR C  1  317 ? 7.586   2.821   7.710  1.00 28.13  ? 330 THR C CA  1 
ATOM   7782 C  C   . THR C  1  317 ? 6.494   3.867   7.491  1.00 28.65  ? 330 THR C C   1 
ATOM   7783 O  O   . THR C  1  317 ? 6.424   4.468   6.422  1.00 32.51  ? 330 THR C O   1 
ATOM   7784 C  CB  . THR C  1  317 ? 7.077   1.441   7.299  1.00 27.50  ? 330 THR C CB  1 
ATOM   7785 O  OG1 . THR C  1  317 ? 5.890   1.113   8.019  1.00 26.84  ? 330 THR C OG1 1 
ATOM   7786 C  CG2 . THR C  1  317 ? 8.131   0.352   7.429  1.00 29.75  ? 330 THR C CG2 1 
ATOM   7787 N  N   . GLY C  1  318 ? 5.652   4.112   8.501  1.00 28.34  ? 331 GLY C N   1 
ATOM   7788 C  CA  . GLY C  1  318 ? 4.650   5.162   8.403  1.00 28.33  ? 331 GLY C CA  1 
ATOM   7789 C  C   . GLY C  1  318 ? 5.249   6.559   8.543  1.00 29.08  ? 331 GLY C C   1 
ATOM   7790 O  O   . GLY C  1  318 ? 4.898   7.477   7.802  1.00 29.32  ? 331 GLY C O   1 
ATOM   7791 N  N   . VAL C  1  319 ? 6.142   6.727   9.522  1.00 29.60  ? 332 VAL C N   1 
ATOM   7792 C  CA  . VAL C  1  319 ? 6.735   8.025   9.790  1.00 30.43  ? 332 VAL C CA  1 
ATOM   7793 C  C   . VAL C  1  319 ? 7.482   8.520   8.549  1.00 29.61  ? 332 VAL C C   1 
ATOM   7794 O  O   . VAL C  1  319 ? 7.421   9.692   8.205  1.00 31.28  ? 332 VAL C O   1 
ATOM   7795 C  CB  . VAL C  1  319 ? 7.668   7.904   11.013 1.00 31.65  ? 332 VAL C CB  1 
ATOM   7796 C  CG1 . VAL C  1  319 ? 8.663   9.056   11.088 1.00 33.82  ? 332 VAL C CG1 1 
ATOM   7797 C  CG2 . VAL C  1  319 ? 6.886   7.743   12.311 1.00 33.94  ? 332 VAL C CG2 1 
ATOM   7798 N  N   . ASN C  1  320 ? 8.218   7.625   7.894  1.00 29.79  ? 333 ASN C N   1 
ATOM   7799 C  CA  . ASN C  1  320 ? 9.063   8.024   6.778  1.00 30.18  ? 333 ASN C CA  1 
ATOM   7800 C  C   . ASN C  1  320 ? 8.243   8.714   5.689  1.00 31.52  ? 333 ASN C C   1 
ATOM   7801 O  O   . ASN C  1  320 ? 8.660   9.727   5.125  1.00 34.03  ? 333 ASN C O   1 
ATOM   7802 C  CB  . ASN C  1  320 ? 9.827   6.845   6.198  1.00 30.74  ? 333 ASN C CB  1 
ATOM   7803 C  CG  . ASN C  1  320 ? 10.907  7.331   5.261  1.00 33.52  ? 333 ASN C CG  1 
ATOM   7804 O  OD1 . ASN C  1  320 ? 11.701  8.208   5.633  1.00 33.01  ? 333 ASN C OD1 1 
ATOM   7805 N  ND2 . ASN C  1  320 ? 10.927  6.788   4.047  1.00 31.81  ? 333 ASN C ND2 1 
ATOM   7806 N  N   . VAL C  1  321 ? 7.040   8.195   5.440  1.00 29.85  ? 334 VAL C N   1 
ATOM   7807 C  CA  . VAL C  1  321 ? 6.161   8.775   4.444  1.00 30.54  ? 334 VAL C CA  1 
ATOM   7808 C  C   . VAL C  1  321 ? 5.441   9.978   5.046  1.00 34.56  ? 334 VAL C C   1 
ATOM   7809 O  O   . VAL C  1  321 ? 5.498   11.069  4.486  1.00 36.83  ? 334 VAL C O   1 
ATOM   7810 C  CB  . VAL C  1  321 ? 5.177   7.757   3.840  1.00 32.32  ? 334 VAL C CB  1 
ATOM   7811 C  CG1 . VAL C  1  321 ? 4.358   8.405   2.734  1.00 35.26  ? 334 VAL C CG1 1 
ATOM   7812 C  CG2 . VAL C  1  321 ? 5.910   6.528   3.301  1.00 32.18  ? 334 VAL C CG2 1 
ATOM   7813 N  N   . ALA C  1  322 ? 4.792   9.811   6.200  1.00 33.44  ? 335 ALA C N   1 
ATOM   7814 C  CA  . ALA C  1  322 ? 3.937   10.870  6.725  1.00 35.33  ? 335 ALA C CA  1 
ATOM   7815 C  C   . ALA C  1  322 ? 4.728   12.133  7.062  1.00 36.97  ? 335 ALA C C   1 
ATOM   7816 O  O   . ALA C  1  322 ? 4.182   13.226  6.989  1.00 37.77  ? 335 ALA C O   1 
ATOM   7817 C  CB  . ALA C  1  322 ? 3.177   10.383  7.940  1.00 36.19  ? 335 ALA C CB  1 
ATOM   7818 N  N   . PHE C  1  323 ? 5.990   11.992  7.470  1.00 33.99  ? 336 PHE C N   1 
ATOM   7819 C  CA  . PHE C  1  323 ? 6.761   13.132  7.932  1.00 37.56  ? 336 PHE C CA  1 
ATOM   7820 C  C   . PHE C  1  323 ? 7.708   13.623  6.845  1.00 38.30  ? 336 PHE C C   1 
ATOM   7821 O  O   . PHE C  1  323 ? 8.508   14.505  7.115  1.00 40.94  ? 336 PHE C O   1 
ATOM   7822 C  CB  . PHE C  1  323 ? 7.607   12.797  9.170  1.00 38.94  ? 336 PHE C CB  1 
ATOM   7823 C  CG  . PHE C  1  323 ? 6.842   12.560  10.464 1.00 38.69  ? 336 PHE C CG  1 
ATOM   7824 C  CD1 . PHE C  1  323 ? 5.450   12.559  10.505 1.00 42.30  ? 336 PHE C CD1 1 
ATOM   7825 C  CD2 . PHE C  1  323 ? 7.537   12.301  11.639 1.00 39.07  ? 336 PHE C CD2 1 
ATOM   7826 C  CE1 . PHE C  1  323 ? 4.774   12.302  11.688 1.00 42.44  ? 336 PHE C CE1 1 
ATOM   7827 C  CE2 . PHE C  1  323 ? 6.861   12.053  12.822 1.00 39.41  ? 336 PHE C CE2 1 
ATOM   7828 C  CZ  . PHE C  1  323 ? 5.475   12.039  12.842 1.00 42.90  ? 336 PHE C CZ  1 
ATOM   7829 N  N   . GLY C  1  324 ? 7.673   13.012  5.660  1.00 40.25  ? 337 GLY C N   1 
ATOM   7830 C  CA  . GLY C  1  324 ? 8.451   13.514  4.540  1.00 39.84  ? 337 GLY C CA  1 
ATOM   7831 C  C   . GLY C  1  324 ? 9.933   13.156  4.638  1.00 43.69  ? 337 GLY C C   1 
ATOM   7832 O  O   . GLY C  1  324 ? 10.762  13.893  4.120  1.00 42.82  ? 337 GLY C O   1 
ATOM   7833 N  N   . GLY C  1  325 ? 10.255  12.013  5.259  1.00 39.84  ? 338 GLY C N   1 
ATOM   7834 C  CA  . GLY C  1  325 ? 11.601  11.456  5.260  1.00 39.79  ? 338 GLY C CA  1 
ATOM   7835 C  C   . GLY C  1  325 ? 12.304  11.673  6.600  1.00 41.34  ? 338 GLY C C   1 
ATOM   7836 O  O   . GLY C  1  325 ? 12.525  12.811  6.983  1.00 41.51  ? 338 GLY C O   1 
ATOM   7837 N  N   . CYS C  1  326 ? 12.571  10.581  7.330  1.00 38.21  ? 339 CYS C N   1 
ATOM   7838 C  CA  . CYS C  1  326 ? 13.302  10.626  8.587  1.00 41.15  ? 339 CYS C CA  1 
ATOM   7839 C  C   . CYS C  1  326 ? 14.279  9.461   8.573  1.00 39.65  ? 339 CYS C C   1 
ATOM   7840 O  O   . CYS C  1  326 ? 13.933  8.370   8.131  1.00 37.22  ? 339 CYS C O   1 
ATOM   7841 C  CB  . CYS C  1  326 ? 12.421  10.483  9.844  1.00 44.70  ? 339 CYS C CB  1 
ATOM   7842 S  SG  . CYS C  1  326 ? 11.223  11.827  10.106 1.00 56.11  ? 339 CYS C SG  1 
ATOM   7843 N  N   . ASP C  1  327 ? 15.503  9.693   9.046  1.00 36.71  ? 340 ASP C N   1 
ATOM   7844 C  CA  . ASP C  1  327 ? 16.479  8.623   9.152  1.00 37.92  ? 340 ASP C CA  1 
ATOM   7845 C  C   . ASP C  1  327 ? 16.053  7.687   10.277 1.00 36.76  ? 340 ASP C C   1 
ATOM   7846 O  O   . ASP C  1  327 ? 15.823  8.109   11.399 1.00 36.37  ? 340 ASP C O   1 
ATOM   7847 C  CB  . ASP C  1  327 ? 17.880  9.166   9.395  1.00 41.91  ? 340 ASP C CB  1 
ATOM   7848 C  CG  . ASP C  1  327 ? 18.550  9.826   8.187  1.00 50.88  ? 340 ASP C CG  1 
ATOM   7849 O  OD1 . ASP C  1  327 ? 17.887  10.082  7.163  1.00 50.70  ? 340 ASP C OD1 1 
ATOM   7850 O  OD2 . ASP C  1  327 ? 19.765  10.039  8.237  1.00 52.70  ? 340 ASP C OD2 1 
ATOM   7851 N  N   . GLU C  1  328 ? 15.988  6.399   9.968  1.00 35.08  ? 341 GLU C N   1 
ATOM   7852 C  CA  . GLU C  1  328 ? 15.557  5.409   10.934 1.00 33.94  ? 341 GLU C CA  1 
ATOM   7853 C  C   . GLU C  1  328 ? 16.614  5.268   12.032 1.00 36.47  ? 341 GLU C C   1 
ATOM   7854 O  O   . GLU C  1  328 ? 17.799  5.258   11.743 1.00 32.44  ? 341 GLU C O   1 
ATOM   7855 C  CB  . GLU C  1  328 ? 15.357  4.076   10.213 1.00 34.20  ? 341 GLU C CB  1 
ATOM   7856 C  CG  . GLU C  1  328 ? 14.718  3.029   11.116 1.00 32.08  ? 341 GLU C CG  1 
ATOM   7857 C  CD  . GLU C  1  328 ? 14.269  1.773   10.424 1.00 37.38  ? 341 GLU C CD  1 
ATOM   7858 O  OE1 . GLU C  1  328 ? 14.552  1.679   9.212  1.00 36.24  ? 341 GLU C OE1 1 
ATOM   7859 O  OE2 . GLU C  1  328 ? 13.656  0.905   11.108 1.00 38.24  ? 341 GLU C OE2 1 
ATOM   7860 N  N   . LEU C  1  329 ? 16.157  5.109   13.277 1.00 33.09  ? 342 LEU C N   1 
ATOM   7861 C  CA  . LEU C  1  329 ? 17.007  4.836   14.425 1.00 35.21  ? 342 LEU C CA  1 
ATOM   7862 C  C   . LEU C  1  329 ? 16.886  3.365   14.815 1.00 32.38  ? 342 LEU C C   1 
ATOM   7863 O  O   . LEU C  1  329 ? 15.829  2.752   14.633 1.00 34.11  ? 342 LEU C O   1 
ATOM   7864 C  CB  . LEU C  1  329 ? 16.593  5.747   15.584 1.00 33.62  ? 342 LEU C CB  1 
ATOM   7865 C  CG  . LEU C  1  329 ? 16.831  7.244   15.383 1.00 41.15  ? 342 LEU C CG  1 
ATOM   7866 C  CD1 . LEU C  1  329 ? 16.139  8.036   16.459 1.00 45.90  ? 342 LEU C CD1 1 
ATOM   7867 C  CD2 . LEU C  1  329 ? 18.319  7.543   15.403 1.00 41.73  ? 342 LEU C CD2 1 
ATOM   7868 N  N   . PHE C  1  330 ? 17.979  2.813   15.364 1.00 29.54  ? 343 PHE C N   1 
ATOM   7869 C  CA  . PHE C  1  330 ? 18.066  1.412   15.717 1.00 29.61  ? 343 PHE C CA  1 
ATOM   7870 C  C   . PHE C  1  330 ? 18.499  1.269   17.171 1.00 35.96  ? 343 PHE C C   1 
ATOM   7871 O  O   . PHE C  1  330 ? 19.577  0.729   17.444 1.00 36.43  ? 343 PHE C O   1 
ATOM   7872 C  CB  . PHE C  1  330 ? 19.025  0.695   14.757 1.00 34.64  ? 343 PHE C CB  1 
ATOM   7873 C  CG  . PHE C  1  330 ? 18.577  0.786   13.303 1.00 39.15  ? 343 PHE C CG  1 
ATOM   7874 C  CD1 . PHE C  1  330 ? 17.510  0.013   12.825 1.00 40.16  ? 343 PHE C CD1 1 
ATOM   7875 C  CD2 . PHE C  1  330 ? 19.180  1.690   12.438 1.00 38.19  ? 343 PHE C CD2 1 
ATOM   7876 C  CE1 . PHE C  1  330 ? 17.075  0.137   11.515 1.00 41.89  ? 343 PHE C CE1 1 
ATOM   7877 C  CE2 . PHE C  1  330 ? 18.747  1.794   11.113 1.00 43.12  ? 343 PHE C CE2 1 
ATOM   7878 C  CZ  . PHE C  1  330 ? 17.689  1.024   10.661 1.00 41.99  ? 343 PHE C CZ  1 
ATOM   7879 N  N   . PRO C  1  331 ? 17.657  1.672   18.151 1.00 36.81  ? 344 PRO C N   1 
ATOM   7880 C  CA  . PRO C  1  331 ? 18.075  1.654   19.561 1.00 32.11  ? 344 PRO C CA  1 
ATOM   7881 C  C   . PRO C  1  331 ? 18.419  0.263   20.089 1.00 30.47  ? 344 PRO C C   1 
ATOM   7882 O  O   . PRO C  1  331 ? 19.160  0.155   21.063 1.00 32.88  ? 344 PRO C O   1 
ATOM   7883 C  CB  . PRO C  1  331 ? 16.881  2.287   20.308 1.00 32.82  ? 344 PRO C CB  1 
ATOM   7884 C  CG  . PRO C  1  331 ? 15.684  1.992   19.401 1.00 32.21  ? 344 PRO C CG  1 
ATOM   7885 C  CD  . PRO C  1  331 ? 16.277  2.161   17.976 1.00 34.91  ? 344 PRO C CD  1 
ATOM   7886 N  N   . TYR C  1  332 ? 17.895  -0.791  19.446 1.00 29.44  ? 345 TYR C N   1 
ATOM   7887 C  CA  . TYR C  1  332 ? 18.117  -2.155  19.890 1.00 29.50  ? 345 TYR C CA  1 
ATOM   7888 C  C   . TYR C  1  332 ? 18.815  -2.987  18.819 1.00 28.21  ? 345 TYR C C   1 
ATOM   7889 O  O   . TYR C  1  332 ? 18.850  -4.217  18.920 1.00 31.04  ? 345 TYR C O   1 
ATOM   7890 C  CB  . TYR C  1  332 ? 16.809  -2.796  20.343 1.00 31.77  ? 345 TYR C CB  1 
ATOM   7891 C  CG  . TYR C  1  332 ? 16.085  -1.952  21.378 1.00 32.93  ? 345 TYR C CG  1 
ATOM   7892 C  CD1 . TYR C  1  332 ? 16.594  -1.756  22.662 1.00 34.40  ? 345 TYR C CD1 1 
ATOM   7893 C  CD2 . TYR C  1  332 ? 14.864  -1.381  21.080 1.00 32.64  ? 345 TYR C CD2 1 
ATOM   7894 C  CE1 . TYR C  1  332 ? 15.937  -0.948  23.582 1.00 34.77  ? 345 TYR C CE1 1 
ATOM   7895 C  CE2 . TYR C  1  332 ? 14.186  -0.594  21.997 1.00 32.98  ? 345 TYR C CE2 1 
ATOM   7896 C  CZ  . TYR C  1  332 ? 14.706  -0.400  23.266 1.00 35.97  ? 345 TYR C CZ  1 
ATOM   7897 O  OH  . TYR C  1  332 ? 14.006  0.390   24.132 1.00 33.68  ? 345 TYR C OH  1 
ATOM   7898 N  N   . GLY C  1  333 ? 19.431  -2.317  17.838 1.00 29.26  ? 346 GLY C N   1 
ATOM   7899 C  CA  . GLY C  1  333 ? 20.107  -3.008  16.746 1.00 33.63  ? 346 GLY C CA  1 
ATOM   7900 C  C   . GLY C  1  333 ? 19.109  -3.646  15.776 1.00 34.80  ? 346 GLY C C   1 
ATOM   7901 O  O   . GLY C  1  333 ? 18.006  -3.140  15.622 1.00 34.57  ? 346 GLY C O   1 
ATOM   7902 N  N   . GLN C  1  334 ? 19.489  -4.788  15.198 1.00 38.97  ? 347 GLN C N   1 
ATOM   7903 C  CA  . GLN C  1  334 ? 18.727  -5.458  14.155 1.00 42.00  ? 347 GLN C CA  1 
ATOM   7904 C  C   . GLN C  1  334 ? 18.403  -6.869  14.619 1.00 39.39  ? 347 GLN C C   1 
ATOM   7905 O  O   . GLN C  1  334 ? 19.013  -7.365  15.568 1.00 35.55  ? 347 GLN C O   1 
ATOM   7906 C  CB  . GLN C  1  334 ? 19.540  -5.560  12.860 1.00 49.55  ? 347 GLN C CB  1 
ATOM   7907 C  CG  . GLN C  1  334 ? 20.359  -4.330  12.476 1.00 57.63  ? 347 GLN C CG  1 
ATOM   7908 C  CD  . GLN C  1  334 ? 19.532  -3.222  11.864 1.00 61.58  ? 347 GLN C CD  1 
ATOM   7909 O  OE1 . GLN C  1  334 ? 18.401  -3.442  11.418 1.00 68.54  ? 347 GLN C OE1 1 
ATOM   7910 N  NE2 . GLN C  1  334 ? 20.107  -2.027  11.813 1.00 61.98  ? 347 GLN C NE2 1 
ATOM   7911 N  N   . LEU C  1  335 ? 17.453  -7.520  13.927 1.00 36.84  ? 348 LEU C N   1 
ATOM   7912 C  CA  . LEU C  1  335 ? 17.052  -8.881  14.255 1.00 41.79  ? 348 LEU C CA  1 
ATOM   7913 C  C   . LEU C  1  335 ? 18.213  -9.875  14.013 1.00 46.82  ? 348 LEU C C   1 
ATOM   7914 O  O   . LEU C  1  335 ? 19.019  -9.588  13.086 1.00 50.10  ? 348 LEU C O   1 
ATOM   7915 C  CB  . LEU C  1  335 ? 15.825  -9.276  13.438 1.00 43.85  ? 348 LEU C CB  1 
ATOM   7916 C  CG  . LEU C  1  335 ? 14.542  -8.496  13.728 1.00 47.57  ? 348 LEU C CG  1 
ATOM   7917 C  CD1 . LEU C  1  335 ? 13.461  -8.849  12.709 1.00 53.15  ? 348 LEU C CD1 1 
ATOM   7918 C  CD2 . LEU C  1  335 ? 14.095  -8.795  15.159 1.00 46.86  ? 348 LEU C CD2 1 
HETATM 7919 C  C1  . NAG D  2  .   ? 28.761  12.658  34.448 1.00 59.44  ? 1   NAG G C1  1 
HETATM 7920 C  C2  . NAG D  2  .   ? 28.889  14.076  35.022 1.00 61.75  ? 1   NAG G C2  1 
HETATM 7921 C  C3  . NAG D  2  .   ? 28.405  15.107  33.986 1.00 59.93  ? 1   NAG G C3  1 
HETATM 7922 C  C4  . NAG D  2  .   ? 28.961  14.851  32.585 1.00 62.29  ? 1   NAG G C4  1 
HETATM 7923 C  C5  . NAG D  2  .   ? 28.743  13.394  32.198 1.00 67.92  ? 1   NAG G C5  1 
HETATM 7924 C  C6  . NAG D  2  .   ? 29.291  13.028  30.833 1.00 65.64  ? 1   NAG G C6  1 
HETATM 7925 C  C7  . NAG D  2  .   ? 28.145  13.518  37.366 1.00 83.35  ? 1   NAG G C7  1 
HETATM 7926 C  C8  . NAG D  2  .   ? 28.341  14.203  38.703 1.00 80.82  ? 1   NAG G C8  1 
HETATM 7927 N  N2  . NAG D  2  .   ? 28.210  14.321  36.291 1.00 68.43  ? 1   NAG G N2  1 
HETATM 7928 O  O3  . NAG D  2  .   ? 28.757  16.419  34.395 1.00 62.31  ? 1   NAG G O3  1 
HETATM 7929 O  O4  . NAG D  2  .   ? 28.281  15.627  31.602 1.00 63.72  ? 1   NAG G O4  1 
HETATM 7930 O  O5  . NAG D  2  .   ? 29.423  12.597  33.184 1.00 57.94  ? 1   NAG G O5  1 
HETATM 7931 O  O6  . NAG D  2  .   ? 30.711  13.319  30.717 1.00 58.49  ? 1   NAG G O6  1 
HETATM 7932 O  O7  . NAG D  2  .   ? 27.879  12.282  37.274 1.00 113.39 ? 1   NAG G O7  1 
HETATM 7933 C  C1  . NAG D  2  .   ? 28.975  16.409  30.681 1.00 57.56  ? 2   NAG G C1  1 
HETATM 7934 C  C2  . NAG D  2  .   ? 28.139  16.680  29.437 1.00 53.97  ? 2   NAG G C2  1 
HETATM 7935 C  C3  . NAG D  2  .   ? 28.890  17.628  28.510 1.00 61.84  ? 2   NAG G C3  1 
HETATM 7936 C  C4  . NAG D  2  .   ? 29.313  18.891  29.252 1.00 64.90  ? 2   NAG G C4  1 
HETATM 7937 C  C5  . NAG D  2  .   ? 30.081  18.523  30.518 1.00 61.55  ? 2   NAG G C5  1 
HETATM 7938 C  C6  . NAG D  2  .   ? 30.383  19.725  31.377 1.00 60.75  ? 2   NAG G C6  1 
HETATM 7939 C  C7  . NAG D  2  .   ? 26.621  14.865  28.792 1.00 55.29  ? 2   NAG G C7  1 
HETATM 7940 C  C8  . NAG D  2  .   ? 26.407  13.681  27.898 1.00 55.37  ? 2   NAG G C8  1 
HETATM 7941 N  N2  . NAG D  2  .   ? 27.790  15.505  28.666 1.00 52.09  ? 2   NAG G N2  1 
HETATM 7942 O  O3  . NAG D  2  .   ? 28.044  17.898  27.398 1.00 60.54  ? 2   NAG G O3  1 
HETATM 7943 O  O4  . NAG D  2  .   ? 30.186  19.687  28.438 1.00 73.37  ? 2   NAG G O4  1 
HETATM 7944 O  O5  . NAG D  2  .   ? 29.287  17.637  31.326 1.00 56.71  ? 2   NAG G O5  1 
HETATM 7945 O  O6  . NAG D  2  .   ? 29.168  20.313  31.797 1.00 60.30  ? 2   NAG G O6  1 
HETATM 7946 O  O7  . NAG D  2  .   ? 25.770  15.223  29.600 1.00 51.83  ? 2   NAG G O7  1 
HETATM 7947 C  C1  . BMA D  2  .   ? 29.680  20.833  27.827 1.00 80.66  ? 3   BMA G C1  1 
HETATM 7948 C  C2  . BMA D  2  .   ? 30.851  21.757  27.502 1.00 81.14  ? 3   BMA G C2  1 
HETATM 7949 C  C3  . BMA D  2  .   ? 30.361  22.956  26.684 1.00 89.48  ? 3   BMA G C3  1 
HETATM 7950 C  C4  . BMA D  2  .   ? 29.543  22.524  25.481 1.00 92.13  ? 3   BMA G C4  1 
HETATM 7951 C  C5  . BMA D  2  .   ? 28.438  21.535  25.855 1.00 92.20  ? 3   BMA G C5  1 
HETATM 7952 C  C6  . BMA D  2  .   ? 27.813  20.906  24.627 1.00 94.39  ? 3   BMA G C6  1 
HETATM 7953 O  O2  . BMA D  2  .   ? 31.902  21.023  26.872 1.00 65.86  ? 3   BMA G O2  1 
HETATM 7954 O  O3  . BMA D  2  .   ? 31.466  23.735  26.226 1.00 86.94  ? 3   BMA G O3  1 
HETATM 7955 O  O4  . BMA D  2  .   ? 28.943  23.690  24.903 1.00 96.92  ? 3   BMA G O4  1 
HETATM 7956 O  O5  . BMA D  2  .   ? 28.972  20.449  26.648 1.00 80.21  ? 3   BMA G O5  1 
HETATM 7957 O  O6  . BMA D  2  .   ? 26.780  19.977  24.962 1.00 100.78 ? 3   BMA G O6  1 
HETATM 7958 C  C1  . MAN D  2  .   ? 31.643  24.995  26.800 1.00 85.00  ? 4   MAN G C1  1 
HETATM 7959 C  C2  . MAN D  2  .   ? 32.149  25.856  25.653 1.00 87.33  ? 4   MAN G C2  1 
HETATM 7960 C  C3  . MAN D  2  .   ? 33.581  25.387  25.247 1.00 83.64  ? 4   MAN G C3  1 
HETATM 7961 C  C4  . MAN D  2  .   ? 34.530  25.310  26.452 1.00 83.77  ? 4   MAN G C4  1 
HETATM 7962 C  C5  . MAN D  2  .   ? 33.899  24.474  27.581 1.00 81.19  ? 4   MAN G C5  1 
HETATM 7963 C  C6  . MAN D  2  .   ? 34.724  24.447  28.860 1.00 75.57  ? 4   MAN G C6  1 
HETATM 7964 O  O2  . MAN D  2  .   ? 31.998  27.237  25.996 1.00 78.03  ? 4   MAN G O2  1 
HETATM 7965 O  O3  . MAN D  2  .   ? 34.131  26.235  24.227 1.00 83.61  ? 4   MAN G O3  1 
HETATM 7966 O  O4  . MAN D  2  .   ? 35.775  24.705  26.069 1.00 72.42  ? 4   MAN G O4  1 
HETATM 7967 O  O5  . MAN D  2  .   ? 32.574  24.996  27.906 1.00 82.18  ? 4   MAN G O5  1 
HETATM 7968 O  O6  . MAN D  2  .   ? 35.022  25.733  29.399 1.00 68.87  ? 4   MAN G O6  1 
HETATM 7969 C  C1  . MAN D  2  .   ? 25.965  19.559  23.896 1.00 105.77 ? 5   MAN G C1  1 
HETATM 7970 C  C2  . MAN D  2  .   ? 24.704  18.930  24.494 1.00 103.79 ? 5   MAN G C2  1 
HETATM 7971 C  C3  . MAN D  2  .   ? 24.975  17.558  25.109 1.00 99.62  ? 5   MAN G C3  1 
HETATM 7972 C  C4  . MAN D  2  .   ? 25.610  16.650  24.070 1.00 100.91 ? 5   MAN G C4  1 
HETATM 7973 C  C5  . MAN D  2  .   ? 26.894  17.281  23.505 1.00 104.82 ? 5   MAN G C5  1 
HETATM 7974 C  C6  . MAN D  2  .   ? 27.455  16.470  22.353 1.00 92.87  ? 5   MAN G C6  1 
HETATM 7975 O  O2  . MAN D  2  .   ? 23.704  18.839  23.484 1.00 105.61 ? 5   MAN G O2  1 
HETATM 7976 O  O3  . MAN D  2  .   ? 23.770  16.976  25.616 1.00 86.14  ? 5   MAN G O3  1 
HETATM 7977 O  O4  . MAN D  2  .   ? 25.933  15.389  24.652 1.00 104.66 ? 5   MAN G O4  1 
HETATM 7978 O  O5  . MAN D  2  .   ? 26.644  18.637  23.003 1.00 111.75 ? 5   MAN G O5  1 
HETATM 7979 O  O6  . MAN D  2  .   ? 28.657  17.043  21.821 1.00 85.84  ? 5   MAN G O6  1 
HETATM 7980 C  C1  . NAG E  3  .   ? 27.934  -8.810  19.736 1.00 37.98  ? 1   NAG I C1  1 
HETATM 7981 C  C2  . NAG E  3  .   ? 28.582  -9.802  18.770 1.00 35.66  ? 1   NAG I C2  1 
HETATM 7982 C  C3  . NAG E  3  .   ? 27.935  -9.697  17.396 1.00 38.04  ? 1   NAG I C3  1 
HETATM 7983 C  C4  . NAG E  3  .   ? 26.426  -9.835  17.529 1.00 40.36  ? 1   NAG I C4  1 
HETATM 7984 C  C5  . NAG E  3  .   ? 25.898  -8.799  18.524 1.00 40.61  ? 1   NAG I C5  1 
HETATM 7985 C  C6  . NAG E  3  .   ? 24.405  -8.895  18.748 1.00 37.46  ? 1   NAG I C6  1 
HETATM 7986 C  C7  . NAG E  3  .   ? 30.879  -10.585 19.042 1.00 39.49  ? 1   NAG I C7  1 
HETATM 7987 C  C8  . NAG E  3  .   ? 32.331  -10.317 18.791 1.00 40.77  ? 1   NAG I C8  1 
HETATM 7988 N  N2  . NAG E  3  .   ? 30.017  -9.657  18.621 1.00 39.01  ? 1   NAG I N2  1 
HETATM 7989 O  O3  . NAG E  3  .   ? 28.489  -10.714 16.574 1.00 36.55  ? 1   NAG I O3  1 
HETATM 7990 O  O4  . NAG E  3  .   ? 25.809  -9.604  16.269 1.00 41.23  ? 1   NAG I O4  1 
HETATM 7991 O  O5  . NAG E  3  .   ? 26.531  -9.043  19.792 1.00 38.81  ? 1   NAG I O5  1 
HETATM 7992 O  O6  . NAG E  3  .   ? 24.084  -10.140 19.367 1.00 36.54  ? 1   NAG I O6  1 
HETATM 7993 O  O7  . NAG E  3  .   ? 30.501  -11.607 19.603 1.00 38.44  ? 1   NAG I O7  1 
HETATM 7994 C  C1  . NAG E  3  .   ? 25.561  -10.710 15.461 1.00 46.14  ? 2   NAG I C1  1 
HETATM 7995 C  C2  . NAG E  3  .   ? 24.270  -10.515 14.672 1.00 46.85  ? 2   NAG I C2  1 
HETATM 7996 C  C3  . NAG E  3  .   ? 24.123  -11.629 13.638 1.00 55.34  ? 2   NAG I C3  1 
HETATM 7997 C  C4  . NAG E  3  .   ? 25.376  -11.725 12.775 1.00 59.33  ? 2   NAG I C4  1 
HETATM 7998 C  C5  . NAG E  3  .   ? 26.630  -11.861 13.640 1.00 60.84  ? 2   NAG I C5  1 
HETATM 7999 C  C6  . NAG E  3  .   ? 27.897  -11.764 12.820 1.00 56.94  ? 2   NAG I C6  1 
HETATM 8000 C  C7  . NAG E  3  .   ? 22.411  -9.386  15.836 1.00 44.64  ? 2   NAG I C7  1 
HETATM 8001 C  C8  . NAG E  3  .   ? 21.195  -9.587  16.690 1.00 47.78  ? 2   NAG I C8  1 
HETATM 8002 N  N2  . NAG E  3  .   ? 23.089  -10.491 15.507 1.00 43.33  ? 2   NAG I N2  1 
HETATM 8003 O  O3  . NAG E  3  .   ? 22.977  -11.381 12.830 1.00 47.61  ? 2   NAG I O3  1 
HETATM 8004 O  O4  . NAG E  3  .   ? 25.280  -12.859 11.903 1.00 62.32  ? 2   NAG I O4  1 
HETATM 8005 O  O5  . NAG E  3  .   ? 26.690  -10.783 14.597 1.00 46.99  ? 2   NAG I O5  1 
HETATM 8006 O  O6  . NAG E  3  .   ? 29.035  -11.795 13.658 1.00 72.02  ? 2   NAG I O6  1 
HETATM 8007 O  O7  . NAG E  3  .   ? 22.771  -8.270  15.482 1.00 41.64  ? 2   NAG I O7  1 
HETATM 8008 C  C1  . BMA E  3  .   ? 25.605  -12.542 10.584 1.00 71.02  ? 3   BMA I C1  1 
HETATM 8009 C  C2  . BMA E  3  .   ? 25.725  -13.825 9.775  1.00 73.38  ? 3   BMA I C2  1 
HETATM 8010 C  C3  . BMA E  3  .   ? 26.077  -13.483 8.326  1.00 84.88  ? 3   BMA I C3  1 
HETATM 8011 C  C4  . BMA E  3  .   ? 25.076  -12.490 7.756  1.00 82.03  ? 3   BMA I C4  1 
HETATM 8012 C  C5  . BMA E  3  .   ? 25.032  -11.247 8.652  1.00 80.26  ? 3   BMA I C5  1 
HETATM 8013 C  C6  . BMA E  3  .   ? 24.042  -10.193 8.203  1.00 81.92  ? 3   BMA I C6  1 
HETATM 8014 O  O2  . BMA E  3  .   ? 24.529  -14.584 9.913  1.00 63.11  ? 3   BMA I O2  1 
HETATM 8015 O  O3  . BMA E  3  .   ? 26.141  -14.668 7.528  1.00 99.50  ? 3   BMA I O3  1 
HETATM 8016 O  O4  . BMA E  3  .   ? 25.462  -12.121 6.431  1.00 75.98  ? 3   BMA I O4  1 
HETATM 8017 O  O5  . BMA E  3  .   ? 24.640  -11.684 9.973  1.00 75.13  ? 3   BMA I O5  1 
HETATM 8018 O  O6  . BMA E  3  .   ? 22.766  -10.778 7.956  1.00 91.08  ? 3   BMA I O6  1 
HETATM 8019 C  C1  . MAN E  3  .   ? 21.881  -10.079 7.117  1.00 101.22 ? 4   MAN I C1  1 
HETATM 8020 C  C2  . MAN E  3  .   ? 20.492  -10.546 7.522  1.00 97.15  ? 4   MAN I C2  1 
HETATM 8021 C  C3  . MAN E  3  .   ? 20.296  -12.025 7.172  1.00 98.12  ? 4   MAN I C3  1 
HETATM 8022 C  C4  . MAN E  3  .   ? 20.762  -12.391 5.764  1.00 104.70 ? 4   MAN I C4  1 
HETATM 8023 C  C5  . MAN E  3  .   ? 22.116  -11.776 5.414  1.00 115.30 ? 4   MAN I C5  1 
HETATM 8024 C  C6  . MAN E  3  .   ? 22.507  -11.940 3.949  1.00 124.59 ? 4   MAN I C6  1 
HETATM 8025 O  O2  . MAN E  3  .   ? 19.501  -9.689  6.963  1.00 91.18  ? 4   MAN I O2  1 
HETATM 8026 O  O3  . MAN E  3  .   ? 18.920  -12.348 7.293  1.00 93.08  ? 4   MAN I O3  1 
HETATM 8027 O  O4  . MAN E  3  .   ? 20.889  -13.807 5.688  1.00 101.65 ? 4   MAN I O4  1 
HETATM 8028 O  O5  . MAN E  3  .   ? 22.094  -10.355 5.728  1.00 111.47 ? 4   MAN I O5  1 
HETATM 8029 O  O6  . MAN E  3  .   ? 21.437  -11.627 3.014  1.00 145.24 ? 4   MAN I O6  1 
HETATM 8030 C  C1  . MAN E  3  .   ? 18.641  -13.597 7.843  1.00 95.93  ? 5   MAN I C1  1 
HETATM 8031 C  C2  . MAN E  3  .   ? 17.262  -13.985 7.382  1.00 99.20  ? 5   MAN I C2  1 
HETATM 8032 C  C3  . MAN E  3  .   ? 16.240  -12.956 7.850  1.00 98.31  ? 5   MAN I C3  1 
HETATM 8033 C  C4  . MAN E  3  .   ? 16.284  -12.843 9.370  1.00 93.76  ? 5   MAN I C4  1 
HETATM 8034 C  C5  . MAN E  3  .   ? 17.729  -12.592 9.851  1.00 95.19  ? 5   MAN I C5  1 
HETATM 8035 C  C6  . MAN E  3  .   ? 17.884  -12.691 11.351 1.00 91.01  ? 5   MAN I C6  1 
HETATM 8036 O  O2  . MAN E  3  .   ? 16.955  -15.283 7.883  1.00 96.79  ? 5   MAN I O2  1 
HETATM 8037 O  O3  . MAN E  3  .   ? 14.931  -13.319 7.394  1.00 102.28 ? 5   MAN I O3  1 
HETATM 8038 O  O4  . MAN E  3  .   ? 15.454  -11.763 9.799  1.00 75.17  ? 5   MAN I O4  1 
HETATM 8039 O  O5  . MAN E  3  .   ? 18.653  -13.563 9.275  1.00 95.04  ? 5   MAN I O5  1 
HETATM 8040 O  O6  . MAN E  3  .   ? 19.027  -11.951 11.765 1.00 80.43  ? 5   MAN I O6  1 
HETATM 8041 C  C1  . MAN E  3  .   ? 21.705  -11.910 1.661  1.00 145.15 ? 6   MAN I C1  1 
HETATM 8042 C  C2  . MAN E  3  .   ? 22.293  -10.655 1.020  1.00 149.18 ? 6   MAN I C2  1 
HETATM 8043 C  C3  . MAN E  3  .   ? 21.255  -9.541  0.826  1.00 145.37 ? 6   MAN I C3  1 
HETATM 8044 C  C4  . MAN E  3  .   ? 19.968  -10.058 0.193  1.00 135.91 ? 6   MAN I C4  1 
HETATM 8045 C  C5  . MAN E  3  .   ? 19.467  -11.319 0.902  1.00 131.09 ? 6   MAN I C5  1 
HETATM 8046 C  C6  . MAN E  3  .   ? 18.291  -11.957 0.195  1.00 125.43 ? 6   MAN I C6  1 
HETATM 8047 O  O2  . MAN E  3  .   ? 22.919  -11.000 -0.212 1.00 152.52 ? 6   MAN I O2  1 
HETATM 8048 O  O3  . MAN E  3  .   ? 21.811  -8.504  0.014  1.00 138.17 ? 6   MAN I O3  1 
HETATM 8049 O  O4  . MAN E  3  .   ? 18.960  -9.052  0.284  1.00 122.74 ? 6   MAN I O4  1 
HETATM 8050 O  O5  . MAN E  3  .   ? 20.516  -12.319 0.958  1.00 133.36 ? 6   MAN I O5  1 
HETATM 8051 O  O6  . MAN E  3  .   ? 17.381  -12.549 1.138  1.00 118.61 ? 6   MAN I O6  1 
HETATM 8052 C  C1  . MAN E  3  .   ? 27.374  -15.323 7.455  1.00 109.12 ? 7   MAN I C1  1 
HETATM 8053 C  C2  . MAN E  3  .   ? 27.503  -15.849 6.029  1.00 112.94 ? 7   MAN I C2  1 
HETATM 8054 C  C3  . MAN E  3  .   ? 26.526  -17.011 5.769  1.00 107.93 ? 7   MAN I C3  1 
HETATM 8055 C  C4  . MAN E  3  .   ? 26.464  -18.026 6.921  1.00 103.10 ? 7   MAN I C4  1 
HETATM 8056 C  C5  . MAN E  3  .   ? 26.419  -17.372 8.301  1.00 96.65  ? 7   MAN I C5  1 
HETATM 8057 C  C6  . MAN E  3  .   ? 26.593  -18.378 9.419  1.00 89.87  ? 7   MAN I C6  1 
HETATM 8058 O  O2  . MAN E  3  .   ? 28.864  -16.173 5.737  1.00 108.86 ? 7   MAN I O2  1 
HETATM 8059 O  O3  . MAN E  3  .   ? 26.901  -17.672 4.552  1.00 106.05 ? 7   MAN I O3  1 
HETATM 8060 O  O4  . MAN E  3  .   ? 25.276  -18.809 6.817  1.00 92.89  ? 7   MAN I O4  1 
HETATM 8061 O  O5  . MAN E  3  .   ? 27.480  -16.398 8.410  1.00 101.35 ? 7   MAN I O5  1 
HETATM 8062 O  O6  . MAN E  3  .   ? 27.684  -18.042 10.261 1.00 97.89  ? 7   MAN I O6  1 
HETATM 8063 C  C1  . NAG F  4  .   ? 24.681  -10.714 69.150 1.00 57.13  ? 1   NAG Z C1  1 
HETATM 8064 C  C2  . NAG F  4  .   ? 24.924  -9.823  70.354 1.00 64.06  ? 1   NAG Z C2  1 
HETATM 8065 C  C3  . NAG F  4  .   ? 25.825  -10.652 71.254 1.00 64.22  ? 1   NAG Z C3  1 
HETATM 8066 C  C4  . NAG F  4  .   ? 24.966  -11.763 71.834 1.00 64.40  ? 1   NAG Z C4  1 
HETATM 8067 C  C5  . NAG F  4  .   ? 24.325  -12.574 70.700 1.00 61.87  ? 1   NAG Z C5  1 
HETATM 8068 C  C6  . NAG F  4  .   ? 23.168  -13.436 71.186 1.00 58.12  ? 1   NAG Z C6  1 
HETATM 8069 C  C7  . NAG F  4  .   ? 26.431  -8.221  69.377 1.00 65.80  ? 1   NAG Z C7  1 
HETATM 8070 C  C8  . NAG F  4  .   ? 26.785  -6.774  69.201 1.00 62.44  ? 1   NAG Z C8  1 
HETATM 8071 N  N2  . NAG F  4  .   ? 25.384  -8.469  70.145 1.00 73.43  ? 1   NAG Z N2  1 
HETATM 8072 O  O3  . NAG F  4  .   ? 26.468  -9.901  72.265 1.00 62.02  ? 1   NAG Z O3  1 
HETATM 8073 O  O4  . NAG F  4  .   ? 25.812  -12.596 72.623 1.00 72.47  ? 1   NAG Z O4  1 
HETATM 8074 O  O5  . NAG F  4  .   ? 23.802  -11.735 69.639 1.00 57.78  ? 1   NAG Z O5  1 
HETATM 8075 O  O6  . NAG F  4  .   ? 22.200  -12.691 71.935 1.00 48.29  ? 1   NAG Z O6  1 
HETATM 8076 O  O7  . NAG F  4  .   ? 27.050  -9.142  68.852 1.00 65.19  ? 1   NAG Z O7  1 
HETATM 8077 C  C1  . NAG F  4  .   ? 25.329  -12.912 73.892 1.00 70.40  ? 2   NAG Z C1  1 
HETATM 8078 C  C2  . NAG F  4  .   ? 25.845  -14.252 74.389 1.00 67.46  ? 2   NAG Z C2  1 
HETATM 8079 C  C3  . NAG F  4  .   ? 25.220  -14.528 75.755 1.00 74.00  ? 2   NAG Z C3  1 
HETATM 8080 C  C4  . NAG F  4  .   ? 25.453  -13.358 76.712 1.00 77.24  ? 2   NAG Z C4  1 
HETATM 8081 C  C5  . NAG F  4  .   ? 24.996  -12.050 76.065 1.00 75.66  ? 2   NAG Z C5  1 
HETATM 8082 C  C6  . NAG F  4  .   ? 25.257  -10.801 76.888 1.00 69.90  ? 2   NAG Z C6  1 
HETATM 8083 C  C7  . NAG F  4  .   ? 26.482  -15.833 72.601 1.00 70.53  ? 2   NAG Z C7  1 
HETATM 8084 C  C8  . NAG F  4  .   ? 26.199  -17.199 72.050 1.00 69.77  ? 2   NAG Z C8  1 
HETATM 8085 N  N2  . NAG F  4  .   ? 25.581  -15.335 73.461 1.00 67.54  ? 2   NAG Z N2  1 
HETATM 8086 O  O3  . NAG F  4  .   ? 25.767  -15.738 76.265 1.00 70.73  ? 2   NAG Z O3  1 
HETATM 8087 O  O4  . NAG F  4  .   ? 24.714  -13.563 77.929 1.00 81.95  ? 2   NAG Z O4  1 
HETATM 8088 O  O5  . NAG F  4  .   ? 25.704  -11.900 74.821 1.00 64.22  ? 2   NAG Z O5  1 
HETATM 8089 O  O6  . NAG F  4  .   ? 26.521  -10.842 77.527 1.00 75.89  ? 2   NAG Z O6  1 
HETATM 8090 O  O7  . NAG F  4  .   ? 27.493  -15.213 72.285 1.00 71.32  ? 2   NAG Z O7  1 
HETATM 8091 C  C1  . BMA F  4  .   ? 25.431  -13.885 79.083 1.00 89.72  ? 3   BMA Z C1  1 
HETATM 8092 C  C2  . BMA F  4  .   ? 24.605  -13.594 80.347 1.00 89.65  ? 3   BMA Z C2  1 
HETATM 8093 C  C3  . BMA F  4  .   ? 25.354  -14.063 81.600 1.00 94.04  ? 3   BMA Z C3  1 
HETATM 8094 C  C4  . BMA F  4  .   ? 25.867  -15.500 81.448 1.00 93.74  ? 3   BMA Z C4  1 
HETATM 8095 C  C5  . BMA F  4  .   ? 26.680  -15.658 80.148 1.00 94.40  ? 3   BMA Z C5  1 
HETATM 8096 C  C6  . BMA F  4  .   ? 27.128  -17.083 79.877 1.00 92.26  ? 3   BMA Z C6  1 
HETATM 8097 O  O2  . BMA F  4  .   ? 23.300  -14.170 80.277 1.00 80.26  ? 3   BMA Z O2  1 
HETATM 8098 O  O3  . BMA F  4  .   ? 24.481  -13.962 82.741 1.00 85.33  ? 3   BMA Z O3  1 
HETATM 8099 O  O4  . BMA F  4  .   ? 26.685  -15.841 82.576 1.00 89.96  ? 3   BMA Z O4  1 
HETATM 8100 O  O5  . BMA F  4  .   ? 25.847  -15.264 79.033 1.00 90.75  ? 3   BMA Z O5  1 
HETATM 8101 O  O6  . BMA F  4  .   ? 28.253  -17.136 78.988 1.00 90.35  ? 3   BMA Z O6  1 
HETATM 8102 C  C1  . MAN F  4  .   ? 24.746  -12.946 83.668 1.00 79.12  ? 4   MAN Z C1  1 
HETATM 8103 C  C2  . MAN F  4  .   ? 24.153  -13.429 84.998 1.00 75.76  ? 4   MAN Z C2  1 
HETATM 8104 C  C3  . MAN F  4  .   ? 22.594  -13.447 84.915 1.00 69.06  ? 4   MAN Z C3  1 
HETATM 8105 C  C4  . MAN F  4  .   ? 22.081  -12.054 84.550 1.00 65.42  ? 4   MAN Z C4  1 
HETATM 8106 C  C5  . MAN F  4  .   ? 22.716  -11.603 83.228 1.00 66.20  ? 4   MAN Z C5  1 
HETATM 8107 C  C6  . MAN F  4  .   ? 22.340  -10.185 82.858 1.00 65.90  ? 4   MAN Z C6  1 
HETATM 8108 O  O2  . MAN F  4  .   ? 24.668  -12.631 86.073 1.00 66.73  ? 4   MAN Z O2  1 
HETATM 8109 O  O3  . MAN F  4  .   ? 21.982  -13.878 86.136 1.00 63.45  ? 4   MAN Z O3  1 
HETATM 8110 O  O4  . MAN F  4  .   ? 20.658  -12.064 84.413 1.00 62.88  ? 4   MAN Z O4  1 
HETATM 8111 O  O5  . MAN F  4  .   ? 24.197  -11.665 83.310 1.00 71.69  ? 4   MAN Z O5  1 
HETATM 8112 O  O6  . MAN F  4  .   ? 22.346  -9.329  84.014 1.00 65.79  ? 4   MAN Z O6  1 
HETATM 8113 C  C1  . NAG G  5  .   ? 15.724  -30.250 55.049 1.00 41.09  ? 1   NAG a C1  1 
HETATM 8114 C  C2  . NAG G  5  .   ? 14.580  -31.192 54.645 1.00 43.24  ? 1   NAG a C2  1 
HETATM 8115 C  C3  . NAG G  5  .   ? 14.892  -32.614 55.101 1.00 43.37  ? 1   NAG a C3  1 
HETATM 8116 C  C4  . NAG G  5  .   ? 16.252  -33.027 54.547 1.00 40.54  ? 1   NAG a C4  1 
HETATM 8117 C  C5  . NAG G  5  .   ? 17.317  -32.047 55.014 1.00 41.73  ? 1   NAG a C5  1 
HETATM 8118 C  C6  . NAG G  5  .   ? 18.687  -32.398 54.467 1.00 37.06  ? 1   NAG a C6  1 
HETATM 8119 C  C7  . NAG G  5  .   ? 12.282  -30.453 54.295 1.00 43.70  ? 1   NAG a C7  1 
HETATM 8120 C  C8  . NAG G  5  .   ? 10.936  -30.187 54.902 1.00 45.75  ? 1   NAG a C8  1 
HETATM 8121 N  N2  . NAG G  5  .   ? 13.273  -30.784 55.129 1.00 39.25  ? 1   NAG a N2  1 
HETATM 8122 O  O3  . NAG G  5  .   ? 13.852  -33.471 54.654 1.00 41.69  ? 1   NAG a O3  1 
HETATM 8123 O  O4  . NAG G  5  .   ? 16.627  -34.297 55.045 1.00 40.65  ? 1   NAG a O4  1 
HETATM 8124 O  O5  . NAG G  5  .   ? 16.968  -30.733 54.538 1.00 40.10  ? 1   NAG a O5  1 
HETATM 8125 O  O6  . NAG G  5  .   ? 18.712  -32.202 53.058 1.00 35.12  ? 1   NAG a O6  1 
HETATM 8126 O  O7  . NAG G  5  .   ? 12.464  -30.368 53.086 1.00 44.97  ? 1   NAG a O7  1 
HETATM 8127 C  C1  . NAG G  5  .   ? 16.351  -35.402 54.246 1.00 52.40  ? 2   NAG a C1  1 
HETATM 8128 C  C2  . NAG G  5  .   ? 17.403  -36.468 54.530 1.00 51.88  ? 2   NAG a C2  1 
HETATM 8129 C  C3  . NAG G  5  .   ? 17.009  -37.826 53.955 1.00 59.61  ? 2   NAG a C3  1 
HETATM 8130 C  C4  . NAG G  5  .   ? 15.566  -38.168 54.294 1.00 67.16  ? 2   NAG a C4  1 
HETATM 8131 C  C5  . NAG G  5  .   ? 14.650  -37.028 53.850 1.00 69.52  ? 2   NAG a C5  1 
HETATM 8132 C  C6  . NAG G  5  .   ? 13.184  -37.257 54.158 1.00 65.83  ? 2   NAG a C6  1 
HETATM 8133 C  C7  . NAG G  5  .   ? 19.726  -35.723 54.679 1.00 46.05  ? 2   NAG a C7  1 
HETATM 8134 C  C8  . NAG G  5  .   ? 20.950  -35.326 53.909 1.00 42.23  ? 2   NAG a C8  1 
HETATM 8135 N  N2  . NAG G  5  .   ? 18.668  -36.080 53.950 1.00 48.15  ? 2   NAG a N2  1 
HETATM 8136 O  O3  . NAG G  5  .   ? 17.890  -38.818 54.465 1.00 54.74  ? 2   NAG a O3  1 
HETATM 8137 O  O4  . NAG G  5  .   ? 15.233  -39.391 53.623 1.00 76.98  ? 2   NAG a O4  1 
HETATM 8138 O  O5  . NAG G  5  .   ? 15.039  -35.851 54.581 1.00 56.31  ? 2   NAG a O5  1 
HETATM 8139 O  O6  . NAG G  5  .   ? 13.003  -37.388 55.563 1.00 64.17  ? 2   NAG a O6  1 
HETATM 8140 O  O7  . NAG G  5  .   ? 19.682  -35.698 55.904 1.00 44.67  ? 2   NAG a O7  1 
HETATM 8141 C  C1  . BMA G  5  .   ? 14.781  -40.396 54.475 1.00 84.96  ? 3   BMA a C1  1 
HETATM 8142 C  C2  . BMA G  5  .   ? 14.058  -41.430 53.629 1.00 84.68  ? 3   BMA a C2  1 
HETATM 8143 C  C3  . BMA G  5  .   ? 13.427  -42.442 54.576 1.00 93.23  ? 3   BMA a C3  1 
HETATM 8144 C  C4  . BMA G  5  .   ? 14.521  -43.077 55.446 1.00 86.73  ? 3   BMA a C4  1 
HETATM 8145 C  C5  . BMA G  5  .   ? 15.288  -41.966 56.193 1.00 86.47  ? 3   BMA a C5  1 
HETATM 8146 C  C6  . BMA G  5  .   ? 16.455  -42.450 57.037 1.00 90.75  ? 3   BMA a C6  1 
HETATM 8147 O  O2  . BMA G  5  .   ? 14.959  -41.968 52.665 1.00 79.34  ? 3   BMA a O2  1 
HETATM 8148 O  O3  . BMA G  5  .   ? 12.576  -43.381 53.882 1.00 110.87 ? 3   BMA a O3  1 
HETATM 8149 O  O4  . BMA G  5  .   ? 13.964  -43.953 56.433 1.00 79.16  ? 3   BMA a O4  1 
HETATM 8150 O  O5  . BMA G  5  .   ? 15.813  -41.038 55.224 1.00 79.30  ? 3   BMA a O5  1 
HETATM 8151 O  O6  . BMA G  5  .   ? 17.336  -43.299 56.298 1.00 96.88  ? 3   BMA a O6  1 
HETATM 8152 C  C1  . MAN G  5  .   ? 18.437  -43.824 56.998 1.00 98.89  ? 4   MAN a C1  1 
HETATM 8153 C  C2  . MAN G  5  .   ? 19.533  -44.047 55.968 1.00 99.42  ? 4   MAN a C2  1 
HETATM 8154 C  C3  . MAN G  5  .   ? 19.115  -45.080 54.917 1.00 101.75 ? 4   MAN a C3  1 
HETATM 8155 C  C4  . MAN G  5  .   ? 18.476  -46.343 55.510 1.00 104.60 ? 4   MAN a C4  1 
HETATM 8156 C  C5  . MAN G  5  .   ? 17.667  -46.140 56.818 1.00 105.03 ? 4   MAN a C5  1 
HETATM 8157 C  C6  . MAN G  5  .   ? 17.688  -47.386 57.684 1.00 105.96 ? 4   MAN a C6  1 
HETATM 8158 O  O2  . MAN G  5  .   ? 20.748  -44.399 56.623 1.00 93.51  ? 4   MAN a O2  1 
HETATM 8159 O  O3  . MAN G  5  .   ? 20.272  -45.460 54.167 1.00 99.50  ? 4   MAN a O3  1 
HETATM 8160 O  O4  . MAN G  5  .   ? 17.581  -46.883 54.536 1.00 100.78 ? 4   MAN a O4  1 
HETATM 8161 O  O5  . MAN G  5  .   ? 18.171  -45.063 57.659 1.00 101.77 ? 4   MAN a O5  1 
HETATM 8162 O  O6  . MAN G  5  .   ? 16.646  -48.311 57.313 1.00 110.27 ? 4   MAN a O6  1 
HETATM 8163 C  C1  . MAN G  5  .   ? 20.215  -45.378 52.776 1.00 97.76  ? 5   MAN a C1  1 
HETATM 8164 C  C2  . MAN G  5  .   ? 21.351  -46.199 52.206 1.00 98.79  ? 5   MAN a C2  1 
HETATM 8165 C  C3  . MAN G  5  .   ? 22.713  -45.606 52.571 1.00 99.43  ? 5   MAN a C3  1 
HETATM 8166 C  C4  . MAN G  5  .   ? 22.799  -44.141 52.164 1.00 96.34  ? 5   MAN a C4  1 
HETATM 8167 C  C5  . MAN G  5  .   ? 21.581  -43.378 52.705 1.00 94.61  ? 5   MAN a C5  1 
HETATM 8168 C  C6  . MAN G  5  .   ? 21.493  -41.950 52.215 1.00 86.65  ? 5   MAN a C6  1 
HETATM 8169 O  O2  . MAN G  5  .   ? 21.189  -46.288 50.794 1.00 94.95  ? 5   MAN a O2  1 
HETATM 8170 O  O3  . MAN G  5  .   ? 23.756  -46.354 51.937 1.00 101.49 ? 5   MAN a O3  1 
HETATM 8171 O  O4  . MAN G  5  .   ? 24.004  -43.572 52.689 1.00 86.55  ? 5   MAN a O4  1 
HETATM 8172 O  O5  . MAN G  5  .   ? 20.346  -44.033 52.298 1.00 98.67  ? 5   MAN a O5  1 
HETATM 8173 O  O6  . MAN G  5  .   ? 20.756  -41.154 53.148 1.00 75.12  ? 5   MAN a O6  1 
HETATM 8174 C  C1  . MAN G  5  .   ? 12.892  -44.093 52.720 1.00 122.19 ? 6   MAN a C1  1 
HETATM 8175 C  C2  . MAN G  5  .   ? 12.633  -43.321 51.394 1.00 122.00 ? 6   MAN a C2  1 
HETATM 8176 C  C3  . MAN G  5  .   ? 11.195  -43.387 50.865 1.00 125.91 ? 6   MAN a C3  1 
HETATM 8177 C  C4  . MAN G  5  .   ? 10.620  -44.784 51.002 1.00 132.22 ? 6   MAN a C4  1 
HETATM 8178 C  C5  . MAN G  5  .   ? 10.723  -45.182 52.465 1.00 131.53 ? 6   MAN a C5  1 
HETATM 8179 C  C6  . MAN G  5  .   ? 10.043  -46.489 52.806 1.00 128.81 ? 6   MAN a C6  1 
HETATM 8180 O  O2  . MAN G  5  .   ? 13.526  -43.788 50.386 1.00 115.72 ? 6   MAN a O2  1 
HETATM 8181 O  O3  . MAN G  5  .   ? 11.168  -42.972 49.493 1.00 124.33 ? 6   MAN a O3  1 
HETATM 8182 O  O4  . MAN G  5  .   ? 9.259   -44.809 50.569 1.00 135.03 ? 6   MAN a O4  1 
HETATM 8183 O  O5  . MAN G  5  .   ? 12.129  -45.320 52.783 1.00 131.72 ? 6   MAN a O5  1 
HETATM 8184 O  O6  . MAN G  5  .   ? 9.061   -46.288 53.823 1.00 123.16 ? 6   MAN a O6  1 
HETATM 8185 C  C1  . NAG H  4  .   ? -15.431 19.128  32.015 1.00 83.64  ? 1   NAG q C1  1 
HETATM 8186 C  C2  . NAG H  4  .   ? -15.009 18.764  33.438 1.00 82.72  ? 1   NAG q C2  1 
HETATM 8187 C  C3  . NAG H  4  .   ? -15.116 20.008  34.312 1.00 83.92  ? 1   NAG q C3  1 
HETATM 8188 C  C4  . NAG H  4  .   ? -14.292 21.144  33.719 1.00 84.34  ? 1   NAG q C4  1 
HETATM 8189 C  C5  . NAG H  4  .   ? -14.623 21.365  32.243 1.00 81.19  ? 1   NAG q C5  1 
HETATM 8190 C  C6  . NAG H  4  .   ? -13.665 22.308  31.552 1.00 75.07  ? 1   NAG q C6  1 
HETATM 8191 C  C7  . NAG H  4  .   ? -16.941 17.537  34.357 1.00 77.48  ? 1   NAG q C7  1 
HETATM 8192 C  C8  . NAG H  4  .   ? -17.372 16.258  35.010 1.00 77.74  ? 1   NAG q C8  1 
HETATM 8193 N  N2  . NAG H  4  .   ? -15.641 17.638  34.096 1.00 79.97  ? 1   NAG q N2  1 
HETATM 8194 O  O3  . NAG H  4  .   ? -14.659 19.671  35.614 1.00 86.05  ? 1   NAG q O3  1 
HETATM 8195 O  O4  . NAG H  4  .   ? -14.594 22.334  34.437 1.00 84.78  ? 1   NAG q O4  1 
HETATM 8196 O  O5  . NAG H  4  .   ? -14.528 20.120  31.529 1.00 76.18  ? 1   NAG q O5  1 
HETATM 8197 O  O6  . NAG H  4  .   ? -12.330 21.790  31.612 1.00 68.80  ? 1   NAG q O6  1 
HETATM 8198 O  O7  . NAG H  4  .   ? -17.731 18.431  34.074 1.00 85.76  ? 1   NAG q O7  1 
HETATM 8199 C  C1  . NAG H  4  .   ? -13.524 23.052  34.920 1.00 89.17  ? 2   NAG q C1  1 
HETATM 8200 C  C2  . NAG H  4  .   ? -13.636 24.563  34.856 1.00 87.45  ? 2   NAG q C2  1 
HETATM 8201 C  C3  . NAG H  4  .   ? -12.320 25.181  35.307 1.00 92.94  ? 2   NAG q C3  1 
HETATM 8202 C  C4  . NAG H  4  .   ? -11.958 24.642  36.684 1.00 97.68  ? 2   NAG q C4  1 
HETATM 8203 C  C5  . NAG H  4  .   ? -11.773 23.133  36.578 1.00 98.46  ? 2   NAG q C5  1 
HETATM 8204 C  C6  . NAG H  4  .   ? -11.406 22.469  37.888 1.00 92.87  ? 2   NAG q C6  1 
HETATM 8205 C  C7  . NAG H  4  .   ? -15.267 25.411  33.207 1.00 87.62  ? 2   NAG q C7  1 
HETATM 8206 C  C8  . NAG H  4  .   ? -15.419 26.521  32.210 1.00 82.20  ? 2   NAG q C8  1 
HETATM 8207 N  N2  . NAG H  4  .   ? -14.013 25.103  33.563 1.00 84.76  ? 2   NAG q N2  1 
HETATM 8208 O  O3  . NAG H  4  .   ? -12.454 26.595  35.297 1.00 95.89  ? 2   NAG q O3  1 
HETATM 8209 O  O4  . NAG H  4  .   ? -10.756 25.251  37.164 1.00 106.87 ? 2   NAG q O4  1 
HETATM 8210 O  O5  . NAG H  4  .   ? -13.024 22.556  36.149 1.00 92.84  ? 2   NAG q O5  1 
HETATM 8211 O  O6  . NAG H  4  .   ? -12.486 22.525  38.810 1.00 89.04  ? 2   NAG q O6  1 
HETATM 8212 O  O7  . NAG H  4  .   ? -16.241 24.812  33.657 1.00 92.11  ? 2   NAG q O7  1 
HETATM 8213 C  C1  . BMA H  4  .   ? -10.924 26.277  38.092 1.00 124.21 ? 3   BMA q C1  1 
HETATM 8214 C  C2  . BMA H  4  .   ? -9.586  26.480  38.800 1.00 126.73 ? 3   BMA q C2  1 
HETATM 8215 C  C3  . BMA H  4  .   ? -9.493  27.812  39.554 1.00 129.75 ? 3   BMA q C3  1 
HETATM 8216 C  C4  . BMA H  4  .   ? -10.059 28.957  38.718 1.00 133.90 ? 3   BMA q C4  1 
HETATM 8217 C  C5  . BMA H  4  .   ? -11.474 28.600  38.289 1.00 132.94 ? 3   BMA q C5  1 
HETATM 8218 C  C6  . BMA H  4  .   ? -12.210 29.693  37.535 1.00 127.40 ? 3   BMA q C6  1 
HETATM 8219 O  O2  . BMA H  4  .   ? -8.523  26.337  37.861 1.00 113.87 ? 3   BMA q O2  1 
HETATM 8220 O  O3  . BMA H  4  .   ? -8.127  28.067  39.904 1.00 127.70 ? 3   BMA q O3  1 
HETATM 8221 O  O4  . BMA H  4  .   ? -10.075 30.172  39.476 1.00 136.87 ? 3   BMA q O4  1 
HETATM 8222 O  O5  . BMA H  4  .   ? -11.364 27.460  37.423 1.00 132.89 ? 3   BMA q O5  1 
HETATM 8223 O  O6  . BMA H  4  .   ? -11.521 30.101  36.354 1.00 123.20 ? 3   BMA q O6  1 
HETATM 8224 C  C1  . MAN H  4  .   ? -7.703  27.806  41.210 1.00 125.04 ? 4   MAN q C1  1 
HETATM 8225 C  C2  . MAN H  4  .   ? -6.635  28.852  41.541 1.00 119.29 ? 4   MAN q C2  1 
HETATM 8226 C  C3  . MAN H  4  .   ? -5.311  28.557  40.836 1.00 114.99 ? 4   MAN q C3  1 
HETATM 8227 C  C4  . MAN H  4  .   ? -4.862  27.120  41.102 1.00 115.70 ? 4   MAN q C4  1 
HETATM 8228 C  C5  . MAN H  4  .   ? -5.969  26.153  40.667 1.00 115.15 ? 4   MAN q C5  1 
HETATM 8229 C  C6  . MAN H  4  .   ? -5.647  24.688  40.913 1.00 104.73 ? 4   MAN q C6  1 
HETATM 8230 O  O2  . MAN H  4  .   ? -6.470  28.951  42.956 1.00 110.00 ? 4   MAN q O2  1 
HETATM 8231 O  O3  . MAN H  4  .   ? -4.323  29.499  41.272 1.00 111.54 ? 4   MAN q O3  1 
HETATM 8232 O  O4  . MAN H  4  .   ? -3.669  26.808  40.377 1.00 101.24 ? 4   MAN q O4  1 
HETATM 8233 O  O5  . MAN H  4  .   ? -7.195  26.462  41.392 1.00 124.31 ? 4   MAN q O5  1 
HETATM 8234 O  O6  . MAN H  4  .   ? -4.559  24.488  41.818 1.00 97.30  ? 4   MAN q O6  1 
HETATM 8235 C  C1  . NAG I  6  .   ? -17.983 27.771  8.115  1.00 78.62  ? 1   NAG s C1  1 
HETATM 8236 C  C2  . NAG I  6  .   ? -17.334 28.385  6.879  1.00 78.87  ? 1   NAG s C2  1 
HETATM 8237 C  C3  . NAG I  6  .   ? -17.477 29.904  6.880  1.00 81.90  ? 1   NAG s C3  1 
HETATM 8238 C  C4  . NAG I  6  .   ? -18.921 30.313  7.139  1.00 85.83  ? 1   NAG s C4  1 
HETATM 8239 C  C5  . NAG I  6  .   ? -19.381 29.665  8.439  1.00 86.34  ? 1   NAG s C5  1 
HETATM 8240 C  C6  . NAG I  6  .   ? -20.791 30.024  8.856  1.00 86.81  ? 1   NAG s C6  1 
HETATM 8241 C  C7  . NAG I  6  .   ? -15.414 27.409  5.742  1.00 83.83  ? 1   NAG s C7  1 
HETATM 8242 C  C8  . NAG I  6  .   ? -14.065 27.893  5.299  1.00 87.46  ? 1   NAG s C8  1 
HETATM 8243 N  N2  . NAG I  6  .   ? -15.938 28.015  6.805  1.00 79.20  ? 1   NAG s N2  1 
HETATM 8244 O  O3  . NAG I  6  .   ? -17.010 30.391  5.630  1.00 73.54  ? 1   NAG s O3  1 
HETATM 8245 O  O4  . NAG I  6  .   ? -19.025 31.730  7.245  1.00 103.88 ? 1   NAG s O4  1 
HETATM 8246 O  O5  . NAG I  6  .   ? -19.326 28.237  8.251  1.00 78.35  ? 1   NAG s O5  1 
HETATM 8247 O  O6  . NAG I  6  .   ? -21.769 29.417  8.011  1.00 83.20  ? 1   NAG s O6  1 
HETATM 8248 O  O7  . NAG I  6  .   ? -16.015 26.513  5.160  1.00 75.85  ? 1   NAG s O7  1 
HETATM 8249 C  C1  . NAG I  6  .   ? -19.643 32.367  6.170  1.00 123.22 ? 2   NAG s C1  1 
HETATM 8250 C  C2  . NAG I  6  .   ? -20.348 33.630  6.672  1.00 121.59 ? 2   NAG s C2  1 
HETATM 8251 C  C3  . NAG I  6  .   ? -20.499 34.725  5.613  1.00 130.52 ? 2   NAG s C3  1 
HETATM 8252 C  C4  . NAG I  6  .   ? -19.370 34.761  4.588  1.00 141.06 ? 2   NAG s C4  1 
HETATM 8253 C  C5  . NAG I  6  .   ? -19.152 33.351  4.066  1.00 137.59 ? 2   NAG s C5  1 
HETATM 8254 C  C6  . NAG I  6  .   ? -18.172 33.256  2.914  1.00 131.64 ? 2   NAG s C6  1 
HETATM 8255 C  C7  . NAG I  6  .   ? -22.170 33.542  8.368  1.00 112.51 ? 2   NAG s C7  1 
HETATM 8256 C  C8  . NAG I  6  .   ? -23.612 33.191  8.597  1.00 101.05 ? 2   NAG s C8  1 
HETATM 8257 N  N2  . NAG I  6  .   ? -21.677 33.285  7.148  1.00 120.26 ? 2   NAG s N2  1 
HETATM 8258 O  O3  . NAG I  6  .   ? -20.571 35.947  6.332  1.00 135.40 ? 2   NAG s O3  1 
HETATM 8259 O  O4  . NAG I  6  .   ? -19.687 35.604  3.469  1.00 158.02 ? 2   NAG s O4  1 
HETATM 8260 O  O5  . NAG I  6  .   ? -18.636 32.625  5.193  1.00 135.30 ? 2   NAG s O5  1 
HETATM 8261 O  O6  . NAG I  6  .   ? -17.079 32.394  3.201  1.00 133.89 ? 2   NAG s O6  1 
HETATM 8262 O  O7  . NAG I  6  .   ? -21.479 34.026  9.258  1.00 114.09 ? 2   NAG s O7  1 
HETATM 8263 C  C1  . BMA I  6  .   ? -20.008 36.948  3.648  1.00 164.31 ? 3   BMA s C1  1 
HETATM 8264 C  C2  . BMA I  6  .   ? -19.012 37.850  2.959  1.00 161.28 ? 3   BMA s C2  1 
HETATM 8265 C  C3  . BMA I  6  .   ? -19.362 39.288  3.278  1.00 160.06 ? 3   BMA s C3  1 
HETATM 8266 C  C4  . BMA I  6  .   ? -20.807 39.597  2.876  1.00 165.62 ? 3   BMA s C4  1 
HETATM 8267 C  C5  . BMA I  6  .   ? -21.792 38.548  3.434  1.00 161.68 ? 3   BMA s C5  1 
HETATM 8268 C  C6  . BMA I  6  .   ? -23.182 38.632  2.837  1.00 152.74 ? 3   BMA s C6  1 
HETATM 8269 O  O2  . BMA I  6  .   ? -18.993 37.607  1.554  1.00 160.59 ? 3   BMA s O2  1 
HETATM 8270 O  O3  . BMA I  6  .   ? -18.445 40.153  2.613  1.00 145.53 ? 3   BMA s O3  1 
HETATM 8271 O  O4  . BMA I  6  .   ? -21.178 40.887  3.379  1.00 167.17 ? 3   BMA s O4  1 
HETATM 8272 O  O5  . BMA I  6  .   ? -21.318 37.219  3.138  1.00 163.60 ? 3   BMA s O5  1 
HETATM 8273 O  O6  . BMA I  6  .   ? -23.730 39.945  2.913  1.00 149.07 ? 3   BMA s O6  1 
HETATM 8274 C  C1  A MYR J  7  .   ? 50.696  -6.554  25.611 0.50 102.67 ? 401 MYR A C1  1 
HETATM 8275 C  C1  B MYR J  7  .   ? 44.608  -1.663  34.012 0.50 73.80  ? 401 MYR A C1  1 
HETATM 8276 O  O1  A MYR J  7  .   ? 49.911  -6.748  24.655 0.50 104.83 ? 401 MYR A O1  1 
HETATM 8277 O  O1  B MYR J  7  .   ? 45.099  -2.694  34.522 0.50 63.14  ? 401 MYR A O1  1 
HETATM 8278 O  O2  A MYR J  7  .   ? 51.109  -7.465  26.358 0.50 95.40  ? 401 MYR A O2  1 
HETATM 8279 O  O2  B MYR J  7  .   ? 43.544  -1.130  34.414 0.50 69.49  ? 401 MYR A O2  1 
HETATM 8280 C  C2  A MYR J  7  .   ? 51.172  -5.133  25.875 0.50 100.75 ? 401 MYR A C2  1 
HETATM 8281 C  C2  B MYR J  7  .   ? 45.308  -1.066  32.800 0.50 76.09  ? 401 MYR A C2  1 
HETATM 8282 C  C3  A MYR J  7  .   ? 50.375  -4.068  25.189 0.50 96.81  ? 401 MYR A C3  1 
HETATM 8283 C  C3  B MYR J  7  .   ? 46.710  -0.572  33.019 0.50 77.38  ? 401 MYR A C3  1 
HETATM 8284 C  C4  A MYR J  7  .   ? 49.881  -3.015  26.158 0.50 93.85  ? 401 MYR A C4  1 
HETATM 8285 C  C4  B MYR J  7  .   ? 47.772  -1.550  32.526 0.50 78.29  ? 401 MYR A C4  1 
HETATM 8286 C  C5  A MYR J  7  .   ? 49.396  -3.585  27.461 0.50 90.31  ? 401 MYR A C5  1 
HETATM 8287 C  C5  B MYR J  7  .   ? 48.266  -1.315  31.119 0.50 80.57  ? 401 MYR A C5  1 
HETATM 8288 C  C6  A MYR J  7  .   ? 49.037  -2.555  28.501 0.50 91.08  ? 401 MYR A C6  1 
HETATM 8289 C  C6  B MYR J  7  .   ? 49.614  -0.630  31.034 0.50 79.38  ? 401 MYR A C6  1 
HETATM 8290 C  C7  A MYR J  7  .   ? 50.189  -1.748  29.042 0.50 90.47  ? 401 MYR A C7  1 
HETATM 8291 C  C7  B MYR J  7  .   ? 50.148  -0.488  29.630 0.50 76.68  ? 401 MYR A C7  1 
HETATM 8292 C  C8  A MYR J  7  .   ? 49.825  -0.945  30.264 0.50 87.66  ? 401 MYR A C8  1 
HETATM 8293 C  C8  B MYR J  7  .   ? 50.625  -1.782  29.014 0.50 77.45  ? 401 MYR A C8  1 
HETATM 8294 C  C9  A MYR J  7  .   ? 48.589  -1.458  30.966 0.50 87.21  ? 401 MYR A C9  1 
HETATM 8295 C  C9  B MYR J  7  .   ? 49.615  -2.487  28.128 0.50 74.45  ? 401 MYR A C9  1 
HETATM 8296 C  C10 A MYR J  7  .   ? 48.452  -1.026  32.402 0.50 83.04  ? 401 MYR A C10 1 
HETATM 8297 C  C10 B MYR J  7  .   ? 50.228  -3.408  27.100 0.50 70.37  ? 401 MYR A C10 1 
HETATM 8298 C  C11 A MYR J  7  .   ? 47.030  -0.719  32.826 0.50 85.91  ? 401 MYR A C11 1 
HETATM 8299 C  C11 B MYR J  7  .   ? 49.445  -3.549  25.814 0.50 72.64  ? 401 MYR A C11 1 
HETATM 8300 C  C12 A MYR J  7  .   ? 46.116  -1.922  32.893 0.50 87.21  ? 401 MYR A C12 1 
HETATM 8301 C  C12 B MYR J  7  .   ? 50.015  -4.598  24.899 0.50 75.87  ? 401 MYR A C12 1 
HETATM 8302 C  C13 A MYR J  7  .   ? 45.128  -1.875  34.035 0.50 87.69  ? 401 MYR A C13 1 
HETATM 8303 C  C13 B MYR J  7  .   ? 51.096  -5.406  25.585 0.50 80.85  ? 401 MYR A C13 1 
HETATM 8304 C  C14 A MYR J  7  .   ? 44.004  -0.874  33.845 0.50 87.82  ? 401 MYR A C14 1 
HETATM 8305 C  C14 B MYR J  7  .   ? 50.683  -6.790  26.042 0.50 81.48  ? 401 MYR A C14 1 
HETATM 8306 C  C1  . GOL K  8  .   ? 42.364  -3.123  56.731 1.00 56.00  ? 402 GOL A C1  1 
HETATM 8307 O  O1  . GOL K  8  .   ? 41.674  -2.472  55.664 1.00 40.95  ? 402 GOL A O1  1 
HETATM 8308 C  C2  . GOL K  8  .   ? 42.098  -4.611  56.684 1.00 57.26  ? 402 GOL A C2  1 
HETATM 8309 O  O2  . GOL K  8  .   ? 43.243  -5.328  56.206 1.00 60.43  ? 402 GOL A O2  1 
HETATM 8310 C  C3  . GOL K  8  .   ? 40.890  -4.893  55.825 1.00 49.78  ? 402 GOL A C3  1 
HETATM 8311 O  O3  . GOL K  8  .   ? 40.925  -6.170  55.217 1.00 51.02  ? 402 GOL A O3  1 
HETATM 8312 N  N1  . EPE L  9  .   ? 60.477  3.785   19.014 1.00 89.67  ? 403 EPE A N1  1 
HETATM 8313 C  C2  . EPE L  9  .   ? 60.935  4.941   19.804 1.00 84.60  ? 403 EPE A C2  1 
HETATM 8314 C  C3  . EPE L  9  .   ? 61.105  6.168   18.944 1.00 77.11  ? 403 EPE A C3  1 
HETATM 8315 N  N4  . EPE L  9  .   ? 62.083  5.926   17.888 1.00 79.65  ? 403 EPE A N4  1 
HETATM 8316 C  C5  . EPE L  9  .   ? 61.643  4.757   17.101 1.00 78.87  ? 403 EPE A C5  1 
HETATM 8317 C  C6  . EPE L  9  .   ? 61.482  3.535   17.967 1.00 82.46  ? 403 EPE A C6  1 
HETATM 8318 C  C7  . EPE L  9  .   ? 62.225  7.123   17.044 1.00 88.75  ? 403 EPE A C7  1 
HETATM 8319 C  C8  . EPE L  9  .   ? 61.159  7.276   15.973 1.00 88.53  ? 403 EPE A C8  1 
HETATM 8320 O  O8  . EPE L  9  .   ? 61.399  8.366   15.112 1.00 87.31  ? 403 EPE A O8  1 
HETATM 8321 C  C9  . EPE L  9  .   ? 60.203  2.591   19.888 1.00 92.50  ? 403 EPE A C9  1 
HETATM 8322 C  C10 . EPE L  9  .   ? 59.787  1.320   19.142 1.00 95.92  ? 403 EPE A C10 1 
HETATM 8323 S  S   . EPE L  9  .   ? 59.769  -0.179  20.100 1.00 104.31 ? 403 EPE A S   1 
HETATM 8324 O  O1S . EPE L  9  .   ? 58.706  -0.067  21.061 1.00 80.38  ? 403 EPE A O1S 1 
HETATM 8325 O  O2S . EPE L  9  .   ? 61.125  -0.424  20.533 1.00 91.26  ? 403 EPE A O2S 1 
HETATM 8326 O  O3S . EPE L  9  .   ? 59.293  -1.216  19.011 1.00 88.78  ? 403 EPE A O3S 1 
HETATM 8327 C  C1  . GOL M  8  .   ? 20.917  -2.189  35.287 1.00 69.59  ? 404 GOL A C1  1 
HETATM 8328 O  O1  . GOL M  8  .   ? 22.181  -1.872  34.705 1.00 62.08  ? 404 GOL A O1  1 
HETATM 8329 C  C2  . GOL M  8  .   ? 19.908  -2.762  34.307 1.00 67.73  ? 404 GOL A C2  1 
HETATM 8330 O  O2  . GOL M  8  .   ? 19.970  -4.190  34.325 1.00 72.21  ? 404 GOL A O2  1 
HETATM 8331 C  C3  . GOL M  8  .   ? 20.033  -2.241  32.886 1.00 62.21  ? 404 GOL A C3  1 
HETATM 8332 O  O3  . GOL M  8  .   ? 19.249  -1.066  32.671 1.00 64.31  ? 404 GOL A O3  1 
HETATM 8333 C  C1  . GOL N  8  .   ? 45.224  -7.248  21.869 1.00 59.97  ? 405 GOL A C1  1 
HETATM 8334 O  O1  . GOL N  8  .   ? 46.200  -7.510  22.872 1.00 74.87  ? 405 GOL A O1  1 
HETATM 8335 C  C2  . GOL N  8  .   ? 45.309  -8.250  20.740 1.00 65.07  ? 405 GOL A C2  1 
HETATM 8336 O  O2  . GOL N  8  .   ? 46.679  -8.428  20.370 1.00 72.93  ? 405 GOL A O2  1 
HETATM 8337 C  C3  . GOL N  8  .   ? 44.634  -9.583  21.022 1.00 58.22  ? 405 GOL A C3  1 
HETATM 8338 O  O3  . GOL N  8  .   ? 45.524  -10.540 21.587 1.00 70.79  ? 405 GOL A O3  1 
HETATM 8339 C  CHA . HEM O  10 .   ? 40.564  1.506   35.011 1.00 25.91  ? 406 HEM A CHA 1 
HETATM 8340 C  CHB . HEM O  10 .   ? 44.628  0.806   37.494 1.00 25.21  ? 406 HEM A CHB 1 
HETATM 8341 C  CHC . HEM O  10 .   ? 43.786  -3.995  37.484 1.00 26.87  ? 406 HEM A CHC 1 
HETATM 8342 C  CHD . HEM O  10 .   ? 39.613  -3.256  35.128 1.00 24.74  ? 406 HEM A CHD 1 
HETATM 8343 C  C1A . HEM O  10 .   ? 41.730  1.709   35.709 1.00 24.73  ? 406 HEM A C1A 1 
HETATM 8344 C  C2A . HEM O  10 .   ? 42.274  3.002   35.964 1.00 25.44  ? 406 HEM A C2A 1 
HETATM 8345 C  C3A . HEM O  10 .   ? 43.421  2.818   36.649 1.00 25.54  ? 406 HEM A C3A 1 
HETATM 8346 C  C4A . HEM O  10 .   ? 43.595  1.403   36.820 1.00 25.74  ? 406 HEM A C4A 1 
HETATM 8347 C  CMA . HEM O  10 .   ? 44.391  3.872   37.136 1.00 27.03  ? 406 HEM A CMA 1 
HETATM 8348 C  CAA . HEM O  10 .   ? 41.675  4.314   35.514 1.00 27.03  ? 406 HEM A CAA 1 
HETATM 8349 C  CBA . HEM O  10 .   ? 42.065  4.521   34.090 1.00 30.19  ? 406 HEM A CBA 1 
HETATM 8350 C  CGA . HEM O  10 .   ? 41.892  5.947   33.588 1.00 36.55  ? 406 HEM A CGA 1 
HETATM 8351 O  O1A . HEM O  10 .   ? 42.661  6.315   32.651 1.00 39.51  ? 406 HEM A O1A 1 
HETATM 8352 O  O2A . HEM O  10 .   ? 41.046  6.760   33.988 1.00 32.70  ? 406 HEM A O2A 1 
HETATM 8353 C  C1B . HEM O  10 .   ? 44.731  -0.563  37.659 1.00 26.99  ? 406 HEM A C1B 1 
HETATM 8354 C  C2B . HEM O  10 .   ? 45.853  -1.168  38.298 1.00 26.08  ? 406 HEM A C2B 1 
HETATM 8355 C  C3B . HEM O  10 .   ? 45.624  -2.520  38.323 1.00 27.99  ? 406 HEM A C3B 1 
HETATM 8356 C  C4B . HEM O  10 .   ? 44.353  -2.738  37.647 1.00 27.56  ? 406 HEM A C4B 1 
HETATM 8357 C  CMB . HEM O  10 .   ? 47.060  -0.545  38.936 1.00 26.29  ? 406 HEM A CMB 1 
HETATM 8358 C  CAB . HEM O  10 .   ? 46.620  -3.453  38.846 1.00 29.27  ? 406 HEM A CAB 1 
HETATM 8359 C  CBB . HEM O  10 .   ? 46.773  -4.661  38.336 1.00 35.55  ? 406 HEM A CBB 1 
HETATM 8360 C  C1C . HEM O  10 .   ? 42.569  -4.217  36.867 1.00 26.47  ? 406 HEM A C1C 1 
HETATM 8361 C  C2C . HEM O  10 .   ? 41.900  -5.479  36.766 1.00 26.25  ? 406 HEM A C2C 1 
HETATM 8362 C  C3C . HEM O  10 .   ? 40.731  -5.219  36.097 1.00 25.23  ? 406 HEM A C3C 1 
HETATM 8363 C  C4C . HEM O  10 .   ? 40.651  -3.835  35.815 1.00 25.88  ? 406 HEM A C4C 1 
HETATM 8364 C  CMC . HEM O  10 .   ? 42.420  -6.815  37.299 1.00 27.47  ? 406 HEM A CMC 1 
HETATM 8365 C  CAC . HEM O  10 .   ? 39.617  -6.084  35.729 1.00 29.62  ? 406 HEM A CAC 1 
HETATM 8366 C  CBC . HEM O  10 .   ? 39.305  -7.086  36.484 1.00 33.82  ? 406 HEM A CBC 1 
HETATM 8367 C  C1D . HEM O  10 .   ? 39.590  -1.873  34.881 1.00 25.39  ? 406 HEM A C1D 1 
HETATM 8368 C  C2D . HEM O  10 .   ? 38.551  -1.277  34.028 1.00 24.60  ? 406 HEM A C2D 1 
HETATM 8369 C  C3D . HEM O  10 .   ? 38.804  0.039   34.013 1.00 25.51  ? 406 HEM A C3D 1 
HETATM 8370 C  C4D . HEM O  10 .   ? 40.020  0.237   34.829 1.00 25.19  ? 406 HEM A C4D 1 
HETATM 8371 C  CMD . HEM O  10 .   ? 37.365  -1.967  33.355 1.00 24.20  ? 406 HEM A CMD 1 
HETATM 8372 C  CAD . HEM O  10 .   ? 37.969  1.086   33.275 1.00 25.41  ? 406 HEM A CAD 1 
HETATM 8373 C  CBD . HEM O  10 .   ? 36.921  1.772   34.159 1.00 26.49  ? 406 HEM A CBD 1 
HETATM 8374 C  CGD . HEM O  10 .   ? 36.084  2.754   33.311 1.00 28.36  ? 406 HEM A CGD 1 
HETATM 8375 O  O1D . HEM O  10 .   ? 36.546  3.315   32.291 1.00 26.90  ? 406 HEM A O1D 1 
HETATM 8376 O  O2D . HEM O  10 .   ? 34.865  2.918   33.549 1.00 28.87  ? 406 HEM A O2D 1 
HETATM 8377 N  NA  . HEM O  10 .   ? 42.525  0.772   36.297 1.00 23.88  ? 406 HEM A NA  1 
HETATM 8378 N  NB  . HEM O  10 .   ? 43.869  -1.511  37.277 1.00 24.33  ? 406 HEM A NB  1 
HETATM 8379 N  NC  . HEM O  10 .   ? 41.796  -3.253  36.302 1.00 24.41  ? 406 HEM A NC  1 
HETATM 8380 N  ND  . HEM O  10 .   ? 40.464  -0.936  35.345 1.00 22.99  ? 406 HEM A ND  1 
HETATM 8381 FE FE  . HEM O  10 .   ? 42.025  -1.197  36.461 1.00 24.86  ? 406 HEM A FE  1 
HETATM 8382 S  S   . SO4 P  11 .   ? 50.424  -19.391 44.479 1.00 97.18  ? 407 SO4 A S   1 
HETATM 8383 O  O1  . SO4 P  11 .   ? 51.311  -18.754 43.533 1.00 95.53  ? 407 SO4 A O1  1 
HETATM 8384 O  O2  . SO4 P  11 .   ? 49.073  -19.410 43.956 1.00 82.15  ? 407 SO4 A O2  1 
HETATM 8385 O  O3  . SO4 P  11 .   ? 50.870  -20.744 44.713 1.00 108.85 ? 407 SO4 A O3  1 
HETATM 8386 O  O4  . SO4 P  11 .   ? 50.446  -18.656 45.723 1.00 103.44 ? 407 SO4 A O4  1 
HETATM 8387 S  S   . SO4 Q  11 .   ? 28.946  1.233   49.993 1.00 63.20  ? 408 SO4 A S   1 
HETATM 8388 O  O1  . SO4 Q  11 .   ? 29.956  0.478   49.197 1.00 38.56  ? 408 SO4 A O1  1 
HETATM 8389 O  O2  . SO4 Q  11 .   ? 28.875  2.598   49.468 1.00 81.15  ? 408 SO4 A O2  1 
HETATM 8390 O  O3  . SO4 Q  11 .   ? 27.661  0.598   49.874 1.00 66.56  ? 408 SO4 A O3  1 
HETATM 8391 O  O4  . SO4 Q  11 .   ? 29.269  1.262   51.400 1.00 51.24  ? 408 SO4 A O4  1 
HETATM 8392 S  S   . SO4 R  11 .   ? 26.076  8.426   19.237 1.00 80.62  ? 409 SO4 A S   1 
HETATM 8393 O  O1  . SO4 R  11 .   ? 26.518  7.229   18.561 1.00 72.61  ? 409 SO4 A O1  1 
HETATM 8394 O  O2  . SO4 R  11 .   ? 24.990  9.035   18.506 1.00 75.69  ? 409 SO4 A O2  1 
HETATM 8395 O  O3  . SO4 R  11 .   ? 25.606  8.113   20.576 1.00 66.77  ? 409 SO4 A O3  1 
HETATM 8396 O  O4  . SO4 R  11 .   ? 27.195  9.322   19.315 1.00 72.11  ? 409 SO4 A O4  1 
HETATM 8397 S  S   . SO4 S  11 .   ? 32.256  3.703   60.078 1.00 99.66  ? 410 SO4 A S   1 
HETATM 8398 O  O1  . SO4 S  11 .   ? 31.316  2.675   60.454 1.00 111.06 ? 410 SO4 A O1  1 
HETATM 8399 O  O2  . SO4 S  11 .   ? 32.028  4.071   58.701 1.00 92.74  ? 410 SO4 A O2  1 
HETATM 8400 O  O3  . SO4 S  11 .   ? 32.065  4.867   60.914 1.00 112.51 ? 410 SO4 A O3  1 
HETATM 8401 O  O4  . SO4 S  11 .   ? 33.598  3.203   60.266 1.00 78.63  ? 410 SO4 A O4  1 
HETATM 8402 MG MG  . MG  T  12 .   ? 39.895  8.356   33.769 1.00 33.03  ? 411 MG  A MG  1 
HETATM 8403 C  C1  A MYR U  7  .   ? -1.780  -17.894 61.913 0.50 151.43 ? 401 MYR B C1  1 
HETATM 8404 C  C1  B MYR U  7  .   ? 5.772   -9.847  60.833 0.50 48.95  ? 401 MYR B C1  1 
HETATM 8405 O  O1  A MYR U  7  .   ? -0.940  -17.426 62.715 0.50 158.20 ? 401 MYR B O1  1 
HETATM 8406 O  O1  B MYR U  7  .   ? 6.332   -9.295  61.815 0.50 48.21  ? 401 MYR B O1  1 
HETATM 8407 O  O2  A MYR U  7  .   ? -2.044  -19.114 61.812 0.50 162.24 ? 401 MYR B O2  1 
HETATM 8408 O  O2  B MYR U  7  .   ? 6.001   -9.546  59.628 0.50 52.99  ? 401 MYR B O2  1 
HETATM 8409 C  C2  A MYR U  7  .   ? -2.516  -16.929 61.001 0.50 136.51 ? 401 MYR B C2  1 
HETATM 8410 C  C2  B MYR U  7  .   ? 4.832   -11.004 61.113 0.50 45.21  ? 401 MYR B C2  1 
HETATM 8411 C  C3  A MYR U  7  .   ? -2.372  -15.488 61.373 0.50 128.26 ? 401 MYR B C3  1 
HETATM 8412 C  C3  B MYR U  7  .   ? 3.442   -10.889 60.562 0.50 47.12  ? 401 MYR B C3  1 
HETATM 8413 C  C4  A MYR U  7  .   ? -1.008  -14.931 61.018 0.50 124.00 ? 401 MYR B C4  1 
HETATM 8414 C  C4  B MYR U  7  .   ? 2.592   -9.942  61.390 0.50 48.68  ? 401 MYR B C4  1 
HETATM 8415 C  C5  A MYR U  7  .   ? -0.452  -13.962 62.029 0.50 123.33 ? 401 MYR B C5  1 
HETATM 8416 C  C5  B MYR U  7  .   ? 1.315   -10.519 61.919 0.50 46.45  ? 401 MYR B C5  1 
HETATM 8417 C  C6  A MYR U  7  .   ? 0.994   -13.624 61.805 0.50 124.24 ? 401 MYR B C6  1 
HETATM 8418 C  C6  B MYR U  7  .   ? 1.507   -11.728 62.792 0.50 48.04  ? 401 MYR B C6  1 
HETATM 8419 C  C7  A MYR U  7  .   ? 1.535   -12.516 62.683 0.50 128.85 ? 401 MYR B C7  1 
HETATM 8420 C  C7  B MYR U  7  .   ? 0.912   -12.980 62.234 0.50 44.55  ? 401 MYR B C7  1 
HETATM 8421 C  C8  A MYR U  7  .   ? 0.972   -11.148 62.384 0.50 131.04 ? 401 MYR B C8  1 
HETATM 8422 C  C8  B MYR U  7  .   ? -0.546  -12.869 61.979 0.50 44.17  ? 401 MYR B C8  1 
HETATM 8423 C  C9  A MYR U  7  .   ? 1.998   -10.128 61.935 0.50 131.38 ? 401 MYR B C9  1 
HETATM 8424 C  C9  B MYR U  7  .   ? -1.121  -14.085 61.348 0.50 41.38  ? 401 MYR B C9  1 
HETATM 8425 C  C10 A MYR U  7  .   ? 3.239   -10.714 61.300 0.50 130.70 ? 401 MYR B C10 1 
HETATM 8426 C  C10 B MYR U  7  .   ? -0.942  -15.301 62.182 0.50 40.24  ? 401 MYR B C10 1 
HETATM 8427 C  C11 A MYR U  7  .   ? 4.414   -9.763  61.236 0.50 127.83 ? 401 MYR B C11 1 
HETATM 8428 C  C11 B MYR U  7  .   ? -1.657  -16.492 61.625 0.50 43.12  ? 401 MYR B C11 1 
HETATM 8429 C  C12 A MYR U  7  .   ? 5.303   -9.945  60.028 0.50 126.79 ? 401 MYR B C12 1 
HETATM 8430 C  C12 B MYR U  7  .   ? -1.484  -17.756 62.432 0.50 42.63  ? 401 MYR B C12 1 
HETATM 8431 C  C13 A MYR U  7  .   ? 6.778   -9.942  60.353 0.50 123.72 ? 401 MYR B C13 1 
HETATM 8432 C  C13 B MYR U  7  .   ? -2.228  -18.925 61.823 0.50 45.54  ? 401 MYR B C13 1 
HETATM 8433 C  C14 A MYR U  7  .   ? 7.067   -10.081 61.829 0.50 124.64 ? 401 MYR B C14 1 
HETATM 8434 C  C14 B MYR U  7  .   ? -2.177  -20.198 62.633 0.50 47.77  ? 401 MYR B C14 1 
HETATM 8435 N  N1  . EPE V  9  .   ? 25.042  0.224   56.027 1.00 80.42  ? 402 EPE B N1  1 
HETATM 8436 C  C2  . EPE V  9  .   ? 25.807  0.988   57.029 1.00 84.58  ? 402 EPE B C2  1 
HETATM 8437 C  C3  . EPE V  9  .   ? 25.718  0.377   58.406 1.00 94.68  ? 402 EPE B C3  1 
HETATM 8438 N  N4  . EPE V  9  .   ? 25.967  -1.086  58.406 1.00 92.89  ? 402 EPE B N4  1 
HETATM 8439 C  C5  . EPE V  9  .   ? 25.084  -1.776  57.434 1.00 87.42  ? 402 EPE B C5  1 
HETATM 8440 C  C6  . EPE V  9  .   ? 24.222  -0.809  56.659 1.00 81.24  ? 402 EPE B C6  1 
HETATM 8441 C  C7  . EPE V  9  .   ? 25.803  -1.661  59.751 1.00 84.72  ? 402 EPE B C7  1 
HETATM 8442 C  C8  . EPE V  9  .   ? 26.149  -0.746  60.909 1.00 87.15  ? 402 EPE B C8  1 
HETATM 8443 O  O8  . EPE V  9  .   ? 27.534  -0.475  60.964 1.00 88.35  ? 402 EPE B O8  1 
HETATM 8444 C  C9  . EPE V  9  .   ? 25.938  -0.361  55.050 1.00 76.84  ? 402 EPE B C9  1 
HETATM 8445 C  C10 . EPE V  9  .   ? 26.293  0.693   54.038 1.00 68.66  ? 402 EPE B C10 1 
HETATM 8446 S  S   . EPE V  9  .   ? 25.162  0.610   52.694 1.00 55.27  ? 402 EPE B S   1 
HETATM 8447 O  O1S . EPE V  9  .   ? 24.623  1.940   52.623 1.00 66.06  ? 402 EPE B O1S 1 
HETATM 8448 O  O2S . EPE V  9  .   ? 25.959  0.187   51.578 1.00 74.37  ? 402 EPE B O2S 1 
HETATM 8449 O  O3S . EPE V  9  .   ? 23.932  -0.448  52.855 1.00 41.84  ? 402 EPE B O3S 1 
HETATM 8450 C  C1  . GOL W  8  .   ? 12.644  6.680   46.766 1.00 73.03  ? 403 GOL B C1  1 
HETATM 8451 O  O1  . GOL W  8  .   ? 11.680  6.834   45.728 1.00 87.14  ? 403 GOL B O1  1 
HETATM 8452 C  C2  . GOL W  8  .   ? 12.799  7.953   47.574 1.00 69.09  ? 403 GOL B C2  1 
HETATM 8453 O  O2  . GOL W  8  .   ? 11.524  8.590   47.683 1.00 80.11  ? 403 GOL B O2  1 
HETATM 8454 C  C3  . GOL W  8  .   ? 13.380  7.715   48.954 1.00 70.35  ? 403 GOL B C3  1 
HETATM 8455 O  O3  . GOL W  8  .   ? 13.628  8.896   49.710 1.00 63.28  ? 403 GOL B O3  1 
HETATM 8456 N  N1  . EPE X  9  .   ? -10.453 -16.294 74.266 1.00 94.00  ? 404 EPE B N1  1 
HETATM 8457 C  C2  . EPE X  9  .   ? -11.126 -15.611 75.386 1.00 92.79  ? 404 EPE B C2  1 
HETATM 8458 C  C3  . EPE X  9  .   ? -10.961 -16.383 76.674 1.00 93.05  ? 404 EPE B C3  1 
HETATM 8459 N  N4  . EPE X  9  .   ? -11.675 -17.678 76.627 1.00 97.09  ? 404 EPE B N4  1 
HETATM 8460 C  C5  . EPE X  9  .   ? -11.909 -18.059 75.217 1.00 95.81  ? 404 EPE B C5  1 
HETATM 8461 C  C6  . EPE X  9  .   ? -10.712 -17.745 74.350 1.00 97.28  ? 404 EPE B C6  1 
HETATM 8462 C  C7  . EPE X  9  .   ? -11.010 -18.712 77.445 1.00 97.46  ? 404 EPE B C7  1 
HETATM 8463 C  C8  . EPE X  9  .   ? -11.132 -20.162 76.978 1.00 90.91  ? 404 EPE B C8  1 
HETATM 8464 O  O8  . EPE X  9  .   ? -10.142 -20.976 77.576 1.00 85.22  ? 404 EPE B O8  1 
HETATM 8465 C  C9  . EPE X  9  .   ? -10.817 -15.713 72.930 1.00 101.65 ? 404 EPE B C9  1 
HETATM 8466 C  C10 . EPE X  9  .   ? -9.862  -16.025 71.764 1.00 97.69  ? 404 EPE B C10 1 
HETATM 8467 S  S   . EPE X  9  .   ? -10.602 -16.872 70.386 1.00 105.07 ? 404 EPE B S   1 
HETATM 8468 O  O1S . EPE X  9  .   ? -11.844 -16.204 70.108 1.00 102.12 ? 404 EPE B O1S 1 
HETATM 8469 O  O2S . EPE X  9  .   ? -10.617 -18.266 70.735 1.00 113.92 ? 404 EPE B O2S 1 
HETATM 8470 O  O3S . EPE X  9  .   ? -9.676  -16.690 69.136 1.00 86.15  ? 404 EPE B O3S 1 
HETATM 8471 C  C1  . GOL Y  8  .   ? -0.138  -24.041 56.745 1.00 73.86  ? 405 GOL B C1  1 
HETATM 8472 O  O1  . GOL Y  8  .   ? 0.960   -24.909 57.024 1.00 71.34  ? 405 GOL B O1  1 
HETATM 8473 C  C2  . GOL Y  8  .   ? -0.059  -22.734 57.518 1.00 73.47  ? 405 GOL B C2  1 
HETATM 8474 O  O2  . GOL Y  8  .   ? -1.176  -21.897 57.192 1.00 70.08  ? 405 GOL B O2  1 
HETATM 8475 C  C3  . GOL Y  8  .   ? 0.024   -22.918 59.022 1.00 63.41  ? 405 GOL B C3  1 
HETATM 8476 O  O3  . GOL Y  8  .   ? 0.823   -21.916 59.646 1.00 58.35  ? 405 GOL B O3  1 
HETATM 8477 C  CHA . HEM Z  10 .   ? 10.903  -9.383  61.387 1.00 30.74  ? 406 HEM B CHA 1 
HETATM 8478 C  CHB . HEM Z  10 .   ? 7.608   -5.909  60.693 1.00 28.41  ? 406 HEM B CHB 1 
HETATM 8479 C  CHC . HEM Z  10 .   ? 6.791   -7.637  56.203 1.00 29.31  ? 406 HEM B CHC 1 
HETATM 8480 C  CHD . HEM Z  10 .   ? 10.286  -10.952 56.872 1.00 30.52  ? 406 HEM B CHD 1 
HETATM 8481 C  C1A . HEM Z  10 .   ? 10.090  -8.305  61.524 1.00 28.97  ? 406 HEM B C1A 1 
HETATM 8482 C  C2A . HEM Z  10 .   ? 10.046  -7.519  62.701 1.00 29.20  ? 406 HEM B C2A 1 
HETATM 8483 C  C3A . HEM Z  10 .   ? 9.102   -6.559  62.519 1.00 27.87  ? 406 HEM B C3A 1 
HETATM 8484 C  C4A . HEM Z  10 .   ? 8.579   -6.728  61.234 1.00 29.40  ? 406 HEM B C4A 1 
HETATM 8485 C  CMA . HEM Z  10 .   ? 8.692   -5.495  63.514 1.00 31.36  ? 406 HEM B CMA 1 
HETATM 8486 C  CAA . HEM Z  10 .   ? 10.847  -7.733  63.975 1.00 30.36  ? 406 HEM B CAA 1 
HETATM 8487 C  CBA . HEM Z  10 .   ? 10.125  -8.800  64.800 1.00 32.05  ? 406 HEM B CBA 1 
HETATM 8488 C  CGA . HEM Z  10 .   ? 10.682  -8.939  66.212 1.00 38.25  ? 406 HEM B CGA 1 
HETATM 8489 O  O1A . HEM Z  10 .   ? 9.841   -9.320  67.127 1.00 40.74  ? 406 HEM B O1A 1 
HETATM 8490 O  O2A . HEM Z  10 .   ? 11.892  -8.726  66.541 1.00 36.34  ? 406 HEM B O2A 1 
HETATM 8491 C  C1B . HEM Z  10 .   ? 7.093   -6.141  59.420 1.00 27.10  ? 406 HEM B C1B 1 
HETATM 8492 C  C2B . HEM Z  10 .   ? 6.043   -5.367  58.883 1.00 28.04  ? 406 HEM B C2B 1 
HETATM 8493 C  C3B . HEM Z  10 .   ? 5.826   -5.817  57.621 1.00 28.21  ? 406 HEM B C3B 1 
HETATM 8494 C  C4B . HEM Z  10 .   ? 6.737   -6.945  57.394 1.00 29.28  ? 406 HEM B C4B 1 
HETATM 8495 C  CMB . HEM Z  10 .   ? 5.292   -4.189  59.488 1.00 30.21  ? 406 HEM B CMB 1 
HETATM 8496 C  CAB . HEM Z  10 .   ? 4.745   -5.308  56.796 1.00 29.76  ? 406 HEM B CAB 1 
HETATM 8497 C  CBB . HEM Z  10 .   ? 4.099   -6.051  55.916 1.00 33.98  ? 406 HEM B CBB 1 
HETATM 8498 C  C1C . HEM Z  10 .   ? 7.680   -8.668  55.978 1.00 29.63  ? 406 HEM B C1C 1 
HETATM 8499 C  C2C . HEM Z  10 .   ? 7.880   -9.315  54.752 1.00 29.08  ? 406 HEM B C2C 1 
HETATM 8500 C  C3C . HEM Z  10 .   ? 8.848   -10.298 54.978 1.00 30.08  ? 406 HEM B C3C 1 
HETATM 8501 C  C4C . HEM Z  10 .   ? 9.289   -10.177 56.321 1.00 29.85  ? 406 HEM B C4C 1 
HETATM 8502 C  CMC . HEM Z  10 .   ? 7.125   -9.080  53.469 1.00 33.01  ? 406 HEM B CMC 1 
HETATM 8503 C  CAC . HEM Z  10 .   ? 9.500   -11.216 54.045 1.00 31.60  ? 406 HEM B CAC 1 
HETATM 8504 C  CBC . HEM Z  10 .   ? 9.670   -10.884 52.795 1.00 36.62  ? 406 HEM B CBC 1 
HETATM 8505 C  C1D . HEM Z  10 .   ? 10.694  -10.772 58.204 1.00 27.37  ? 406 HEM B C1D 1 
HETATM 8506 C  C2D . HEM Z  10 .   ? 11.646  -11.664 58.829 1.00 27.70  ? 406 HEM B C2D 1 
HETATM 8507 C  C3D . HEM Z  10 .   ? 11.821  -11.228 60.074 1.00 25.95  ? 406 HEM B C3D 1 
HETATM 8508 C  C4D . HEM Z  10 .   ? 10.961  -10.079 60.200 1.00 26.97  ? 406 HEM B C4D 1 
HETATM 8509 C  CMD . HEM Z  10 .   ? 12.317  -12.865 58.169 1.00 28.58  ? 406 HEM B CMD 1 
HETATM 8510 C  CAD . HEM Z  10 .   ? 12.722  -11.840 61.122 1.00 27.80  ? 406 HEM B CAD 1 
HETATM 8511 C  CBD . HEM Z  10 .   ? 14.130  -11.238 61.138 1.00 28.63  ? 406 HEM B CBD 1 
HETATM 8512 C  CGD . HEM Z  10 .   ? 14.985  -12.051 62.094 1.00 30.53  ? 406 HEM B CGD 1 
HETATM 8513 O  O1D . HEM Z  10 .   ? 14.570  -12.645 63.125 1.00 31.99  ? 406 HEM B O1D 1 
HETATM 8514 O  O2D . HEM Z  10 .   ? 16.183  -12.204 61.850 1.00 31.64  ? 406 HEM B O2D 1 
HETATM 8515 N  NA  . HEM Z  10 .   ? 9.213   -7.791  60.599 1.00 25.53  ? 406 HEM B NA  1 
HETATM 8516 N  NB  . HEM Z  10 .   ? 7.497   -7.048  58.504 1.00 28.99  ? 406 HEM B NB  1 
HETATM 8517 N  NC  . HEM Z  10 .   ? 8.568   -9.153  56.913 1.00 27.62  ? 406 HEM B NC  1 
HETATM 8518 N  ND  . HEM Z  10 .   ? 10.292  -9.839  59.058 1.00 27.85  ? 406 HEM B ND  1 
HETATM 8519 FE FE  . HEM Z  10 .   ? 9.066   -8.382  58.716 1.00 27.46  ? 406 HEM B FE  1 
HETATM 8520 S  S   . SO4 AA 11 .   ? 22.715  -26.323 70.356 1.00 78.88  ? 407 SO4 B S   1 
HETATM 8521 O  O1  . SO4 AA 11 .   ? 23.360  -25.350 69.498 1.00 69.80  ? 407 SO4 B O1  1 
HETATM 8522 O  O2  . SO4 AA 11 .   ? 23.120  -27.652 69.974 1.00 88.61  ? 407 SO4 B O2  1 
HETATM 8523 O  O3  . SO4 AA 11 .   ? 23.142  -26.068 71.707 1.00 87.55  ? 407 SO4 B O3  1 
HETATM 8524 O  O4  . SO4 AA 11 .   ? 21.266  -26.230 70.266 1.00 72.79  ? 407 SO4 B O4  1 
HETATM 8525 MG MG  . MG  BA 12 .   ? 13.450  -8.724  67.797 1.00 33.66  ? 408 MG  B MG  1 
HETATM 8526 C  C1  . MYR CA 7  .   ? 1.660   16.042  9.896  0.90 84.25  ? 401 MYR C C1  1 
HETATM 8527 O  O1  . MYR CA 7  .   ? 1.919   17.247  10.083 0.90 93.23  ? 401 MYR C O1  1 
HETATM 8528 O  O2  . MYR CA 7  .   ? 1.274   15.590  8.803  0.90 86.38  ? 401 MYR C O2  1 
HETATM 8529 C  C2  . MYR CA 7  .   ? 1.822   15.072  11.055 0.90 83.28  ? 401 MYR C C2  1 
HETATM 8530 C  C3  . MYR CA 7  .   ? 0.654   14.161  11.286 0.90 81.09  ? 401 MYR C C3  1 
HETATM 8531 C  C4  . MYR CA 7  .   ? 1.039   12.868  11.982 0.90 80.67  ? 401 MYR C C4  1 
HETATM 8532 C  C5  . MYR CA 7  .   ? 1.069   11.658  11.065 0.90 77.60  ? 401 MYR C C5  1 
HETATM 8533 C  C6  . MYR CA 7  .   ? -0.239  10.914  10.985 0.90 78.69  ? 401 MYR C C6  1 
HETATM 8534 C  C7  . MYR CA 7  .   ? -0.539  10.006  12.164 0.90 75.25  ? 401 MYR C C7  1 
HETATM 8535 C  C8  . MYR CA 7  .   ? -1.869  10.211  12.830 0.90 75.04  ? 401 MYR C C8  1 
HETATM 8536 C  C9  . MYR CA 7  .   ? -1.811  11.150  14.028 0.90 86.43  ? 401 MYR C C9  1 
HETATM 8537 C  C10 . MYR CA 7  .   ? -1.654  10.479  15.379 0.90 82.65  ? 401 MYR C C10 1 
HETATM 8538 C  C11 . MYR CA 7  .   ? -2.817  10.705  16.324 0.90 85.70  ? 401 MYR C C11 1 
HETATM 8539 C  C12 . MYR CA 7  .   ? -4.170  10.208  15.825 0.90 85.20  ? 401 MYR C C12 1 
HETATM 8540 C  C13 . MYR CA 7  .   ? -5.345  10.586  16.678 0.90 84.70  ? 401 MYR C C13 1 
HETATM 8541 C  C14 . MYR CA 7  .   ? -4.969  11.478  17.811 0.90 84.68  ? 401 MYR C C14 1 
HETATM 8542 C  C1  . GOL DA 8  .   ? -17.201 -10.084 20.262 1.00 77.48  ? 402 GOL C C1  1 
HETATM 8543 O  O1  . GOL DA 8  .   ? -18.526 -9.911  19.762 1.00 69.61  ? 402 GOL C O1  1 
HETATM 8544 C  C2  . GOL DA 8  .   ? -16.163 -9.730  19.213 1.00 70.89  ? 402 GOL C C2  1 
HETATM 8545 O  O2  . GOL DA 8  .   ? -16.006 -8.314  19.194 1.00 59.81  ? 402 GOL C O2  1 
HETATM 8546 C  C3  . GOL DA 8  .   ? -14.827 -10.417 19.440 1.00 77.73  ? 402 GOL C C3  1 
HETATM 8547 O  O3  . GOL DA 8  .   ? -13.870 -10.125 18.422 1.00 78.94  ? 402 GOL C O3  1 
HETATM 8548 C  CHA . HEM EA 10 .   ? -8.270  11.583  20.031 1.00 34.93  ? 403 HEM C CHA 1 
HETATM 8549 C  CHB . HEM EA 10 .   ? -5.542  7.604   19.486 1.00 32.11  ? 403 HEM C CHB 1 
HETATM 8550 C  CHC . HEM EA 10 .   ? -7.567  6.929   15.081 1.00 30.93  ? 403 HEM C CHC 1 
HETATM 8551 C  CHD . HEM EA 10 .   ? -10.472 10.753  15.819 1.00 33.41  ? 403 HEM C CHD 1 
HETATM 8552 C  C1A . HEM EA 10 .   ? -7.373  10.566  20.220 1.00 32.95  ? 403 HEM C C1A 1 
HETATM 8553 C  C2A . HEM EA 10 .   ? -6.601  10.412  21.400 1.00 35.53  ? 403 HEM C C2A 1 
HETATM 8554 C  C3A . HEM EA 10 .   ? -5.837  9.300   21.267 1.00 33.47  ? 403 HEM C C3A 1 
HETATM 8555 C  C4A . HEM EA 10 .   ? -6.117  8.749   19.991 1.00 34.20  ? 403 HEM C C4A 1 
HETATM 8556 C  CMA . HEM EA 10 .   ? -4.843  8.759   22.265 1.00 33.94  ? 403 HEM C CMA 1 
HETATM 8557 C  CAA . HEM EA 10 .   ? -6.586  11.321  22.587 1.00 37.48  ? 403 HEM C CAA 1 
HETATM 8558 C  CBA . HEM EA 10 .   ? -5.707  12.517  22.221 1.00 39.78  ? 403 HEM C CBA 1 
HETATM 8559 C  CGA . HEM EA 10 .   ? -5.395  13.346  23.478 1.00 45.12  ? 403 HEM C CGA 1 
HETATM 8560 O  O1A . HEM EA 10 .   ? -6.149  13.370  24.474 1.00 41.25  ? 403 HEM C O1A 1 
HETATM 8561 O  O2A . HEM EA 10 .   ? -4.315  14.007  23.555 1.00 44.42  ? 403 HEM C O2A 1 
HETATM 8562 C  C1B . HEM EA 10 .   ? -5.860  7.152   18.202 1.00 33.75  ? 403 HEM C C1B 1 
HETATM 8563 C  C2B . HEM EA 10 .   ? -5.196  6.028   17.648 1.00 29.81  ? 403 HEM C C2B 1 
HETATM 8564 C  C3B . HEM EA 10 .   ? -5.751  5.815   16.417 1.00 31.34  ? 403 HEM C C3B 1 
HETATM 8565 C  C4B . HEM EA 10 .   ? -6.753  6.879   16.208 1.00 30.73  ? 403 HEM C C4B 1 
HETATM 8566 C  CMB . HEM EA 10 .   ? -4.123  5.180   18.282 1.00 29.45  ? 403 HEM C CMB 1 
HETATM 8567 C  CAB . HEM EA 10 .   ? -5.277  4.770   15.509 1.00 34.54  ? 403 HEM C CAB 1 
HETATM 8568 C  CBB . HEM EA 10 .   ? -5.414  4.900   14.189 1.00 38.72  ? 403 HEM C CBB 1 
HETATM 8569 C  C1C . HEM EA 10 .   ? -8.562  7.870   14.919 1.00 31.00  ? 403 HEM C C1C 1 
HETATM 8570 C  C2C . HEM EA 10 .   ? -9.467  7.929   13.821 1.00 31.21  ? 403 HEM C C2C 1 
HETATM 8571 C  C3C . HEM EA 10 .   ? -10.270 9.048   14.055 1.00 30.95  ? 403 HEM C C3C 1 
HETATM 8572 C  C4C . HEM EA 10 .   ? -9.878  9.630   15.298 1.00 34.26  ? 403 HEM C C4C 1 
HETATM 8573 C  CMC . HEM EA 10 .   ? -9.562  6.965   12.648 1.00 32.06  ? 403 HEM C CMC 1 
HETATM 8574 C  CAC . HEM EA 10 .   ? -11.430 9.529   13.325 1.00 35.57  ? 403 HEM C CAC 1 
HETATM 8575 C  CBC . HEM EA 10 .   ? -12.138 8.694   12.561 1.00 39.05  ? 403 HEM C CBC 1 
HETATM 8576 C  C1D . HEM EA 10 .   ? -10.051 11.272  17.037 1.00 35.49  ? 403 HEM C C1D 1 
HETATM 8577 C  C2D . HEM EA 10 .   ? -10.576 12.532  17.536 1.00 33.55  ? 403 HEM C C2D 1 
HETATM 8578 C  C3D . HEM EA 10 .   ? -9.971  12.772  18.699 1.00 33.83  ? 403 HEM C C3D 1 
HETATM 8579 C  C4D . HEM EA 10 .   ? -9.062  11.647  18.908 1.00 33.82  ? 403 HEM C C4D 1 
HETATM 8580 C  CMD . HEM EA 10 .   ? -11.639 13.371  16.896 1.00 37.30  ? 403 HEM C CMD 1 
HETATM 8581 C  CAD . HEM EA 10 .   ? -10.208 13.974  19.618 1.00 36.12  ? 403 HEM C CAD 1 
HETATM 8582 C  CBD . HEM EA 10 .   ? -11.252 13.665  20.700 1.00 35.15  ? 403 HEM C CBD 1 
HETATM 8583 C  CGD . HEM EA 10 .   ? -11.523 14.959  21.456 1.00 40.06  ? 403 HEM C CGD 1 
HETATM 8584 O  O1D . HEM EA 10 .   ? -10.680 15.906  21.460 1.00 39.88  ? 403 HEM C O1D 1 
HETATM 8585 O  O2D . HEM EA 10 .   ? -12.638 15.101  22.029 1.00 40.66  ? 403 HEM C O2D 1 
HETATM 8586 N  NA  . HEM EA 10 .   ? -7.083  9.508   19.386 1.00 32.13  ? 403 HEM C NA  1 
HETATM 8587 N  NB  . HEM EA 10 .   ? -6.808  7.605   17.344 1.00 30.05  ? 403 HEM C NB  1 
HETATM 8588 N  NC  . HEM EA 10 .   ? -8.828  8.910   15.787 1.00 28.83  ? 403 HEM C NC  1 
HETATM 8589 N  ND  . HEM EA 10 .   ? -9.117  10.775  17.877 1.00 32.62  ? 403 HEM C ND  1 
HETATM 8590 FE FE  . HEM EA 10 .   ? -8.094  9.184   17.700 1.00 31.57  ? 403 HEM C FE  1 
HETATM 8591 S  S   . SO4 FA 11 .   ? -15.264 32.226  24.847 1.00 117.10 ? 404 SO4 C S   1 
HETATM 8592 O  O1  . SO4 FA 11 .   ? -13.858 31.968  25.035 1.00 111.80 ? 404 SO4 C O1  1 
HETATM 8593 O  O2  . SO4 FA 11 .   ? -15.483 32.725  23.509 1.00 104.10 ? 404 SO4 C O2  1 
HETATM 8594 O  O3  . SO4 FA 11 .   ? -16.003 31.000  25.050 1.00 105.27 ? 404 SO4 C O3  1 
HETATM 8595 O  O4  . SO4 FA 11 .   ? -15.708 33.215  25.796 1.00 117.31 ? 404 SO4 C O4  1 
HETATM 8596 S  S   . SO4 GA 11 .   ? 16.819  20.003  14.312 1.00 103.38 ? 405 SO4 C S   1 
HETATM 8597 O  O1  . SO4 GA 11 .   ? 17.752  19.258  13.503 1.00 89.14  ? 405 SO4 C O1  1 
HETATM 8598 O  O2  . SO4 GA 11 .   ? 15.643  19.198  14.536 1.00 91.68  ? 405 SO4 C O2  1 
HETATM 8599 O  O3  . SO4 GA 11 .   ? 17.440  20.326  15.580 1.00 94.94  ? 405 SO4 C O3  1 
HETATM 8600 O  O4  . SO4 GA 11 .   ? 16.443  21.224  13.629 1.00 98.03  ? 405 SO4 C O4  1 
HETATM 8601 MG MG  . MG  HA 12 .   ? -6.770  14.326  26.151 1.00 42.41  ? 406 MG  C MG  1 
HETATM 8602 O  O   . HOH IA 13 .   ? 36.200  -14.656 32.302 1.00 60.21  ? 501 HOH A O   1 
HETATM 8603 O  O   . HOH IA 13 .   ? 42.492  -9.718  18.757 1.00 48.41  ? 502 HOH A O   1 
HETATM 8604 O  O   . HOH IA 13 .   ? 27.761  -18.864 25.661 1.00 56.94  ? 503 HOH A O   1 
HETATM 8605 O  O   . HOH IA 13 .   ? 26.389  -13.541 35.891 1.00 53.69  ? 504 HOH A O   1 
HETATM 8606 O  O   . HOH IA 13 .   ? 18.703  -4.811  36.340 1.00 59.03  ? 505 HOH A O   1 
HETATM 8607 O  O   . HOH IA 13 .   ? 17.183  -8.975  33.589 1.00 52.93  ? 506 HOH A O   1 
HETATM 8608 O  O   . HOH IA 13 .   ? 25.677  -19.474 39.015 1.00 44.88  ? 507 HOH A O   1 
HETATM 8609 O  O   . HOH IA 13 .   ? 46.089  -1.430  54.024 1.00 41.86  ? 508 HOH A O   1 
HETATM 8610 O  O   . HOH IA 13 .   ? 56.159  -4.678  51.338 1.00 44.85  ? 509 HOH A O   1 
HETATM 8611 O  O   . HOH IA 13 .   ? 50.487  10.025  38.242 1.00 34.32  ? 510 HOH A O   1 
HETATM 8612 O  O   . HOH IA 13 .   ? 51.968  -15.465 32.845 1.00 37.10  ? 511 HOH A O   1 
HETATM 8613 O  O   . HOH IA 13 .   ? 68.758  -5.232  35.468 1.00 49.57  ? 512 HOH A O   1 
HETATM 8614 O  O   . HOH IA 13 .   ? 20.313  -10.266 22.686 1.00 36.60  ? 513 HOH A O   1 
HETATM 8615 O  O   . HOH IA 13 .   ? 25.921  8.601   23.032 1.00 50.83  ? 514 HOH A O   1 
HETATM 8616 O  O   . HOH IA 13 .   ? 38.977  6.230   12.583 1.00 49.86  ? 515 HOH A O   1 
HETATM 8617 O  O   . HOH IA 13 .   ? 38.072  -4.821  14.601 1.00 45.79  ? 516 HOH A O   1 
HETATM 8618 O  O   . HOH IA 13 .   ? 63.307  0.373   34.778 1.00 33.79  ? 517 HOH A O   1 
HETATM 8619 O  O   . HOH IA 13 .   ? 61.087  13.724  44.910 1.00 38.12  ? 518 HOH A O   1 
HETATM 8620 O  O   . HOH IA 13 .   ? 57.395  -2.860  45.648 1.00 31.45  ? 519 HOH A O   1 
HETATM 8621 O  O   . HOH IA 13 .   ? 65.510  8.235   31.490 1.00 51.37  ? 520 HOH A O   1 
HETATM 8622 O  O   . HOH IA 13 .   ? 39.131  7.573   35.471 1.00 25.66  ? 521 HOH A O   1 
HETATM 8623 O  O   . HOH IA 13 .   ? 50.962  -20.978 37.022 1.00 37.07  ? 522 HOH A O   1 
HETATM 8624 O  O   . HOH IA 13 .   ? 32.373  -7.285  15.742 1.00 53.60  ? 523 HOH A O   1 
HETATM 8625 O  O   . HOH IA 13 .   ? 23.858  1.226   43.370 1.00 27.33  ? 524 HOH A O   1 
HETATM 8626 O  O   . HOH IA 13 .   ? 46.779  7.773   38.131 1.00 26.45  ? 525 HOH A O   1 
HETATM 8627 O  O   . HOH IA 13 .   ? 61.542  18.105  47.352 1.00 37.25  ? 526 HOH A O   1 
HETATM 8628 O  O   . HOH IA 13 .   ? 56.219  -10.807 46.460 1.00 47.38  ? 527 HOH A O   1 
HETATM 8629 O  O   . HOH IA 13 .   ? 30.717  -14.853 54.588 1.00 48.87  ? 528 HOH A O   1 
HETATM 8630 O  O   . HOH IA 13 .   ? 22.782  -1.555  42.132 1.00 30.31  ? 529 HOH A O   1 
HETATM 8631 O  O   . HOH IA 13 .   ? 38.194  8.194   45.173 1.00 41.15  ? 530 HOH A O   1 
HETATM 8632 O  O   . HOH IA 13 .   ? 48.220  14.182  30.450 1.00 56.44  ? 531 HOH A O   1 
HETATM 8633 O  O   . HOH IA 13 .   ? 44.291  21.841  25.239 1.00 52.07  ? 532 HOH A O   1 
HETATM 8634 O  O   . HOH IA 13 .   ? 54.798  14.825  49.023 1.00 36.53  ? 533 HOH A O   1 
HETATM 8635 O  O   . HOH IA 13 .   ? 61.005  17.580  38.607 1.00 48.44  ? 534 HOH A O   1 
HETATM 8636 O  O   . HOH IA 13 .   ? 35.663  -10.262 16.869 1.00 54.24  ? 535 HOH A O   1 
HETATM 8637 O  O   . HOH IA 13 .   ? 52.242  8.535   51.818 1.00 29.30  ? 536 HOH A O   1 
HETATM 8638 O  O   . HOH IA 13 .   ? 27.053  -16.248 25.924 1.00 48.18  ? 537 HOH A O   1 
HETATM 8639 O  O   . HOH IA 13 .   ? 53.105  7.505   17.824 1.00 59.95  ? 538 HOH A O   1 
HETATM 8640 O  O   . HOH IA 13 .   ? 29.155  -22.486 43.051 1.00 47.78  ? 539 HOH A O   1 
HETATM 8641 O  O   . HOH IA 13 .   ? 48.591  10.435  36.560 1.00 37.63  ? 540 HOH A O   1 
HETATM 8642 O  O   . HOH IA 13 .   ? 38.961  7.135   32.475 1.00 39.21  ? 541 HOH A O   1 
HETATM 8643 O  O   . HOH IA 13 .   ? 40.488  15.829  31.718 1.00 31.30  ? 542 HOH A O   1 
HETATM 8644 O  O   . HOH IA 13 .   ? 58.175  0.223   47.312 1.00 28.47  ? 543 HOH A O   1 
HETATM 8645 O  O   . HOH IA 13 .   ? 23.261  -11.298 34.379 1.00 45.53  ? 544 HOH A O   1 
HETATM 8646 O  O   . HOH IA 13 .   ? 34.861  -1.911  54.093 1.00 30.31  ? 545 HOH A O   1 
HETATM 8647 O  O   . HOH IA 13 .   ? 44.652  -2.921  15.788 1.00 45.69  ? 546 HOH A O   1 
HETATM 8648 O  O   . HOH IA 13 .   ? 38.589  -17.541 47.149 1.00 35.78  ? 547 HOH A O   1 
HETATM 8649 O  O   . HOH IA 13 .   ? 46.551  -12.189 28.915 1.00 34.13  ? 548 HOH A O   1 
HETATM 8650 O  O   . HOH IA 13 .   ? 43.988  11.621  29.359 1.00 38.95  ? 549 HOH A O   1 
HETATM 8651 O  O   . HOH IA 13 .   ? 56.909  -5.546  45.352 1.00 30.11  ? 550 HOH A O   1 
HETATM 8652 O  O   . HOH IA 13 .   ? 35.098  -22.671 32.191 1.00 49.15  ? 551 HOH A O   1 
HETATM 8653 O  O   . HOH IA 13 .   ? 52.747  -7.506  50.701 1.00 35.90  ? 552 HOH A O   1 
HETATM 8654 O  O   . HOH IA 13 .   ? 30.493  -13.865 49.239 1.00 34.75  ? 553 HOH A O   1 
HETATM 8655 O  O   . HOH IA 13 .   ? 33.467  10.364  37.262 1.00 28.18  ? 554 HOH A O   1 
HETATM 8656 O  O   . HOH IA 13 .   ? 44.767  18.875  25.786 1.00 51.09  ? 555 HOH A O   1 
HETATM 8657 O  O   . HOH IA 13 .   ? 35.187  4.907   42.911 1.00 26.48  ? 556 HOH A O   1 
HETATM 8658 O  O   . HOH IA 13 .   ? 57.819  -12.694 39.779 1.00 46.74  ? 557 HOH A O   1 
HETATM 8659 O  O   . HOH IA 13 .   ? 24.732  -10.370 22.028 1.00 40.17  ? 558 HOH A O   1 
HETATM 8660 O  O   . HOH IA 13 .   ? 23.097  5.436   39.902 1.00 38.35  ? 559 HOH A O   1 
HETATM 8661 O  O   . HOH IA 13 .   ? 41.261  10.465  49.716 1.00 36.81  ? 560 HOH A O   1 
HETATM 8662 O  O   . HOH IA 13 .   ? 73.968  1.793   35.465 1.00 54.83  ? 561 HOH A O   1 
HETATM 8663 O  O   . HOH IA 13 .   ? 50.114  13.765  35.961 1.00 46.37  ? 562 HOH A O   1 
HETATM 8664 O  O   . HOH IA 13 .   ? 24.275  6.850   24.272 1.00 40.48  ? 563 HOH A O   1 
HETATM 8665 O  O   . HOH IA 13 .   ? 36.814  9.656   31.389 1.00 35.12  ? 564 HOH A O   1 
HETATM 8666 O  O   . HOH IA 13 .   ? 61.307  -10.359 32.614 1.00 54.74  ? 565 HOH A O   1 
HETATM 8667 O  O   . HOH IA 13 .   ? 58.158  -13.780 43.499 1.00 49.86  ? 566 HOH A O   1 
HETATM 8668 O  O   . HOH IA 13 .   ? 24.171  8.923   28.563 1.00 42.76  ? 567 HOH A O   1 
HETATM 8669 O  O   . HOH IA 13 .   ? 46.525  -9.946  48.073 1.00 32.47  ? 568 HOH A O   1 
HETATM 8670 O  O   . HOH IA 13 .   ? 45.278  5.174   32.129 1.00 38.21  ? 569 HOH A O   1 
HETATM 8671 O  O   . HOH IA 13 .   ? 50.969  -25.176 38.658 1.00 52.80  ? 570 HOH A O   1 
HETATM 8672 O  O   . HOH IA 13 .   ? 45.975  -1.908  26.341 1.00 47.88  ? 571 HOH A O   1 
HETATM 8673 O  O   . HOH IA 13 .   ? 68.756  10.324  36.855 1.00 37.34  ? 572 HOH A O   1 
HETATM 8674 O  O   . HOH IA 13 .   ? 55.740  13.077  32.571 1.00 50.65  ? 573 HOH A O   1 
HETATM 8675 O  O   . HOH IA 13 .   ? 55.674  7.537   43.756 1.00 27.93  ? 574 HOH A O   1 
HETATM 8676 O  O   . HOH IA 13 .   ? 64.387  15.285  37.560 1.00 39.71  ? 575 HOH A O   1 
HETATM 8677 O  O   . HOH IA 13 .   ? 51.794  -16.205 42.910 1.00 39.96  ? 576 HOH A O   1 
HETATM 8678 O  O   . HOH IA 13 .   ? 68.463  2.959   38.345 1.00 31.87  ? 577 HOH A O   1 
HETATM 8679 O  O   . HOH IA 13 .   ? 36.445  -20.432 46.384 1.00 37.02  ? 578 HOH A O   1 
HETATM 8680 O  O   . HOH IA 13 .   ? 43.981  -7.436  54.740 1.00 63.26  ? 579 HOH A O   1 
HETATM 8681 O  O   . HOH IA 13 .   ? 20.733  2.806   31.671 1.00 45.18  ? 580 HOH A O   1 
HETATM 8682 O  O   . HOH IA 13 .   ? 54.798  -14.363 34.296 1.00 44.44  ? 581 HOH A O   1 
HETATM 8683 O  O   . HOH IA 13 .   ? 32.826  -10.173 22.748 1.00 36.67  ? 582 HOH A O   1 
HETATM 8684 O  O   . HOH IA 13 .   ? 27.512  -11.360 21.815 1.00 51.21  ? 583 HOH A O   1 
HETATM 8685 O  O   . HOH IA 13 .   ? 41.945  7.086   54.604 1.00 37.10  ? 584 HOH A O   1 
HETATM 8686 O  O   . HOH IA 13 .   ? 43.791  -15.301 27.911 1.00 40.18  ? 585 HOH A O   1 
HETATM 8687 O  O   . HOH IA 13 .   ? 23.123  -5.308  39.231 1.00 39.21  ? 586 HOH A O   1 
HETATM 8688 O  O   . HOH IA 13 .   ? 33.140  -2.459  16.942 1.00 38.94  ? 587 HOH A O   1 
HETATM 8689 O  O   . HOH IA 13 .   ? 54.858  -0.315  55.252 1.00 48.89  ? 588 HOH A O   1 
HETATM 8690 O  O   . HOH IA 13 .   ? 39.323  3.871   18.515 1.00 35.54  ? 589 HOH A O   1 
HETATM 8691 O  O   . HOH IA 13 .   ? 42.230  -13.250 50.091 1.00 53.34  ? 590 HOH A O   1 
HETATM 8692 O  O   . HOH IA 13 .   ? 62.348  -10.307 30.610 1.00 57.01  ? 591 HOH A O   1 
HETATM 8693 O  O   . HOH IA 13 .   ? 48.042  -15.197 42.851 1.00 35.89  ? 592 HOH A O   1 
HETATM 8694 O  O   . HOH IA 13 .   ? 39.194  2.472   57.012 1.00 42.30  ? 593 HOH A O   1 
HETATM 8695 O  O   . HOH IA 13 .   ? 45.403  12.384  45.237 1.00 36.60  ? 594 HOH A O   1 
HETATM 8696 O  O   . HOH IA 13 .   ? 30.171  5.094   28.462 1.00 32.21  ? 595 HOH A O   1 
HETATM 8697 O  O   . HOH IA 13 .   ? 38.766  -14.959 29.908 1.00 33.41  ? 596 HOH A O   1 
HETATM 8698 O  O   . HOH IA 13 .   ? 70.441  4.027   48.193 1.00 41.26  ? 597 HOH A O   1 
HETATM 8699 O  O   . HOH IA 13 .   ? 65.656  -0.259  35.920 1.00 33.91  ? 598 HOH A O   1 
HETATM 8700 O  O   . HOH IA 13 .   ? 63.418  8.065   29.672 1.00 46.14  ? 599 HOH A O   1 
HETATM 8701 O  O   . HOH IA 13 .   ? 34.581  14.609  36.068 1.00 40.47  ? 600 HOH A O   1 
HETATM 8702 O  O   . HOH IA 13 .   ? 29.574  -12.128 34.895 1.00 37.39  ? 601 HOH A O   1 
HETATM 8703 O  O   . HOH IA 13 .   ? 46.793  -17.205 29.664 1.00 37.59  ? 602 HOH A O   1 
HETATM 8704 O  O   . HOH IA 13 .   ? 57.754  7.483   47.646 1.00 31.71  ? 603 HOH A O   1 
HETATM 8705 O  O   . HOH IA 13 .   ? 43.490  15.710  30.281 1.00 42.61  ? 604 HOH A O   1 
HETATM 8706 O  O   . HOH IA 13 .   ? 21.390  -1.094  37.484 1.00 42.05  ? 605 HOH A O   1 
HETATM 8707 O  O   . HOH IA 13 .   ? 26.461  -5.007  16.237 1.00 36.03  ? 606 HOH A O   1 
HETATM 8708 O  O   . HOH IA 13 .   ? 31.878  -1.579  49.478 1.00 25.31  ? 607 HOH A O   1 
HETATM 8709 O  O   . HOH IA 13 .   ? 21.278  9.349   30.803 1.00 61.39  ? 608 HOH A O   1 
HETATM 8710 O  O   . HOH IA 13 .   ? 46.644  -15.173 36.603 1.00 27.26  ? 609 HOH A O   1 
HETATM 8711 O  O   . HOH IA 13 .   ? 49.016  -3.609  53.149 1.00 34.66  ? 610 HOH A O   1 
HETATM 8712 O  O   . HOH IA 13 .   ? 34.471  -10.147 57.587 1.00 60.21  ? 611 HOH A O   1 
HETATM 8713 O  O   . HOH IA 13 .   ? 44.329  -11.557 47.573 1.00 32.66  ? 612 HOH A O   1 
HETATM 8714 O  O   . HOH IA 13 .   ? 37.411  1.866   18.798 1.00 35.21  ? 613 HOH A O   1 
HETATM 8715 O  O   . HOH IA 13 .   ? 20.678  3.820   28.803 1.00 41.07  ? 614 HOH A O   1 
HETATM 8716 O  O   . HOH IA 13 .   ? 37.891  -13.272 35.721 1.00 27.98  ? 615 HOH A O   1 
HETATM 8717 O  O   . HOH IA 13 .   ? 54.276  -2.163  53.541 1.00 48.55  ? 616 HOH A O   1 
HETATM 8718 O  O   . HOH IA 13 .   ? 48.287  8.915   50.095 1.00 33.39  ? 617 HOH A O   1 
HETATM 8719 O  O   . HOH IA 13 .   ? 68.213  -5.416  31.599 1.00 45.42  ? 618 HOH A O   1 
HETATM 8720 O  O   . HOH IA 13 .   ? 28.889  7.729   41.947 1.00 46.32  ? 619 HOH A O   1 
HETATM 8721 O  O   . HOH IA 13 .   ? 62.537  16.595  44.749 1.00 53.33  ? 620 HOH A O   1 
HETATM 8722 O  O   . HOH IA 13 .   ? 38.994  4.618   32.815 1.00 42.32  ? 621 HOH A O   1 
HETATM 8723 O  O   . HOH IA 13 .   ? 21.975  -5.962  43.309 1.00 49.15  ? 622 HOH A O   1 
HETATM 8724 O  O   . HOH IA 13 .   ? 49.343  6.037   47.123 1.00 28.50  ? 623 HOH A O   1 
HETATM 8725 O  O   . HOH IA 13 .   ? 48.836  -4.429  32.098 1.00 39.40  ? 624 HOH A O   1 
HETATM 8726 O  O   . HOH IA 13 .   ? 56.703  -12.710 37.434 1.00 36.54  ? 625 HOH A O   1 
HETATM 8727 O  O   . HOH IA 13 .   ? 30.289  11.161  20.461 1.00 45.65  ? 626 HOH A O   1 
HETATM 8728 O  O   . HOH IA 13 .   ? 31.154  4.578   17.532 1.00 39.55  ? 627 HOH A O   1 
HETATM 8729 O  O   . HOH IA 13 .   ? 47.555  4.366   16.562 1.00 46.28  ? 628 HOH A O   1 
HETATM 8730 O  O   . HOH IA 13 .   ? 19.225  1.763   23.336 1.00 31.16  ? 629 HOH A O   1 
HETATM 8731 O  O   . HOH IA 13 .   ? 33.011  -17.419 21.346 1.00 61.60  ? 630 HOH A O   1 
HETATM 8732 O  O   . HOH IA 13 .   ? 56.661  9.309   24.019 1.00 50.22  ? 631 HOH A O   1 
HETATM 8733 O  O   . HOH IA 13 .   ? 68.661  13.476  48.360 1.00 48.13  ? 632 HOH A O   1 
HETATM 8734 O  O   . HOH IA 13 .   ? 59.801  11.899  52.188 1.00 47.01  ? 633 HOH A O   1 
HETATM 8735 O  O   . HOH IA 13 .   ? 34.019  12.867  27.889 1.00 36.13  ? 634 HOH A O   1 
HETATM 8736 O  O   . HOH IA 13 .   ? 40.560  12.097  33.363 1.00 29.95  ? 635 HOH A O   1 
HETATM 8737 O  O   . HOH IA 13 .   ? 46.868  -20.754 42.942 1.00 35.94  ? 636 HOH A O   1 
HETATM 8738 O  O   . HOH IA 13 .   ? 29.007  11.364  27.059 1.00 44.51  ? 637 HOH A O   1 
HETATM 8739 O  O   . HOH IA 13 .   ? 46.041  -24.671 37.034 1.00 38.29  ? 638 HOH A O   1 
HETATM 8740 O  O   . HOH IA 13 .   ? 69.963  -1.935  29.496 1.00 50.37  ? 639 HOH A O   1 
HETATM 8741 O  O   . HOH IA 13 .   ? 29.014  -24.184 38.018 1.00 53.29  ? 640 HOH A O   1 
HETATM 8742 O  O   . HOH IA 13 .   ? 57.685  7.757   53.831 1.00 55.29  ? 641 HOH A O   1 
HETATM 8743 O  O   . HOH IA 13 .   ? 27.239  -11.384 32.439 1.00 29.88  ? 642 HOH A O   1 
HETATM 8744 O  O   . HOH IA 13 .   ? 20.344  5.747   21.291 1.00 46.38  ? 643 HOH A O   1 
HETATM 8745 O  O   . HOH IA 13 .   ? 44.622  -18.834 42.041 1.00 44.21  ? 644 HOH A O   1 
HETATM 8746 O  O   . HOH IA 13 .   ? 48.784  16.641  20.596 1.00 50.88  ? 645 HOH A O   1 
HETATM 8747 O  O   . HOH IA 13 .   ? 73.230  4.573   35.471 1.00 39.36  ? 646 HOH A O   1 
HETATM 8748 O  O   . HOH IA 13 .   ? 36.936  -13.280 26.715 1.00 38.40  ? 647 HOH A O   1 
HETATM 8749 O  O   . HOH IA 13 .   ? 27.930  -19.269 45.224 1.00 45.09  ? 648 HOH A O   1 
HETATM 8750 O  O   . HOH IA 13 .   ? 40.315  2.119   42.132 1.00 23.36  ? 649 HOH A O   1 
HETATM 8751 O  O   . HOH IA 13 .   ? 70.744  -2.734  40.473 1.00 54.92  ? 650 HOH A O   1 
HETATM 8752 O  O   . HOH IA 13 .   ? 64.521  1.842   26.700 1.00 47.39  ? 651 HOH A O   1 
HETATM 8753 O  O   . HOH IA 13 .   ? 67.115  14.713  38.081 1.00 39.23  ? 652 HOH A O   1 
HETATM 8754 O  O   . HOH IA 13 .   ? 51.305  9.345   30.116 1.00 36.95  ? 653 HOH A O   1 
HETATM 8755 O  O   . HOH IA 13 .   ? 43.912  -22.299 32.898 1.00 45.23  ? 654 HOH A O   1 
HETATM 8756 O  O   . HOH IA 13 .   ? 35.228  7.362   44.124 1.00 33.78  ? 655 HOH A O   1 
HETATM 8757 O  O   . HOH IA 13 .   ? 54.070  9.904   43.738 1.00 27.47  ? 656 HOH A O   1 
HETATM 8758 O  O   . HOH IA 13 .   ? 31.963  14.582  27.978 1.00 39.18  ? 657 HOH A O   1 
HETATM 8759 O  O   . HOH IA 13 .   ? 45.701  -4.047  55.751 1.00 53.61  ? 658 HOH A O   1 
HETATM 8760 O  O   . HOH IA 13 .   ? 28.801  -14.773 37.341 1.00 44.11  ? 659 HOH A O   1 
HETATM 8761 O  O   . HOH IA 13 .   ? 36.891  2.865   60.115 1.00 55.15  ? 660 HOH A O   1 
HETATM 8762 O  O   . HOH IA 13 .   ? 47.075  9.991   31.691 1.00 42.54  ? 661 HOH A O   1 
HETATM 8763 O  O   . HOH IA 13 .   ? 58.596  -5.653  52.469 1.00 56.09  ? 662 HOH A O   1 
HETATM 8764 O  O   . HOH IA 13 .   ? 37.954  -9.733  24.207 1.00 43.97  ? 663 HOH A O   1 
HETATM 8765 O  O   . HOH IA 13 .   ? 28.547  -0.396  46.839 1.00 36.29  ? 664 HOH A O   1 
HETATM 8766 O  O   . HOH IA 13 .   ? 21.918  1.074   36.077 1.00 46.16  ? 665 HOH A O   1 
HETATM 8767 O  O   . HOH IA 13 .   ? 29.599  10.852  39.150 1.00 41.80  ? 666 HOH A O   1 
HETATM 8768 O  O   . HOH IA 13 .   ? 29.331  3.920   43.038 1.00 41.30  ? 667 HOH A O   1 
HETATM 8769 O  O   . HOH IA 13 .   ? 38.102  5.090   35.478 1.00 28.03  ? 668 HOH A O   1 
HETATM 8770 O  O   . HOH IA 13 .   ? 57.641  -11.334 25.063 1.00 60.95  ? 669 HOH A O   1 
HETATM 8771 O  O   . HOH IA 13 .   ? 54.388  -6.682  22.691 1.00 54.70  ? 670 HOH A O   1 
HETATM 8772 O  O   . HOH IA 13 .   ? 65.683  -6.315  27.068 1.00 50.09  ? 671 HOH A O   1 
HETATM 8773 O  O   . HOH IA 13 .   ? 58.734  8.269   25.011 1.00 55.08  ? 672 HOH A O   1 
HETATM 8774 O  O   . HOH IA 13 .   ? 60.617  -10.010 25.508 1.00 56.60  ? 673 HOH A O   1 
HETATM 8775 O  O   . HOH IA 13 .   ? 55.143  -5.478  47.471 1.00 28.59  ? 674 HOH A O   1 
HETATM 8776 O  O   . HOH IA 13 .   ? 22.680  -11.842 22.793 1.00 43.25  ? 675 HOH A O   1 
HETATM 8777 O  O   . HOH IA 13 .   ? 22.252  -5.058  19.097 1.00 34.58  ? 676 HOH A O   1 
HETATM 8778 O  O   . HOH IA 13 .   ? 39.115  -24.316 34.845 1.00 39.36  ? 677 HOH A O   1 
HETATM 8779 O  O   . HOH IA 13 .   ? 38.443  9.892   33.471 1.00 36.57  ? 678 HOH A O   1 
HETATM 8780 O  O   . HOH IA 13 .   ? 66.632  0.120   38.447 1.00 35.99  ? 679 HOH A O   1 
HETATM 8781 O  O   . HOH IA 13 .   ? 35.525  -23.120 43.011 1.00 36.15  ? 680 HOH A O   1 
HETATM 8782 O  O   . HOH IA 13 .   ? 45.158  14.793  39.730 1.00 50.16  ? 681 HOH A O   1 
HETATM 8783 O  O   . HOH IA 13 .   ? 58.493  11.763  30.432 1.00 47.17  ? 682 HOH A O   1 
HETATM 8784 O  O   . HOH IA 13 .   ? 51.533  11.898  30.464 1.00 49.72  ? 683 HOH A O   1 
HETATM 8785 O  O   . HOH IA 13 .   ? 36.995  -18.132 30.967 1.00 40.08  ? 684 HOH A O   1 
HETATM 8786 O  O   . HOH IA 13 .   ? 73.034  1.095   46.477 1.00 48.85  ? 685 HOH A O   1 
HETATM 8787 O  O   . HOH IA 13 .   ? 22.676  -13.600 46.845 1.00 39.74  ? 686 HOH A O   1 
HETATM 8788 O  O   . HOH IA 13 .   ? 65.604  7.864   51.716 1.00 39.02  ? 687 HOH A O   1 
HETATM 8789 O  O   . HOH IA 13 .   ? 40.041  8.736   47.753 1.00 32.86  ? 688 HOH A O   1 
HETATM 8790 O  O   . HOH IA 13 .   ? 33.000  -24.051 41.801 1.00 51.11  ? 689 HOH A O   1 
HETATM 8791 O  O   . HOH IA 13 .   ? 20.511  -8.960  30.666 1.00 39.80  ? 690 HOH A O   1 
HETATM 8792 O  O   . HOH IA 13 .   ? 30.478  -10.172 56.202 1.00 35.13  ? 691 HOH A O   1 
HETATM 8793 O  O   . HOH IA 13 .   ? 49.122  -15.362 35.318 1.00 27.11  ? 692 HOH A O   1 
HETATM 8794 O  O   . HOH IA 13 .   ? 35.761  -7.115  57.902 1.00 51.62  ? 693 HOH A O   1 
HETATM 8795 O  O   . HOH IA 13 .   ? 23.826  -4.000  15.790 1.00 39.32  ? 694 HOH A O   1 
HETATM 8796 O  O   . HOH IA 13 .   ? 65.340  -9.948  38.038 1.00 62.43  ? 695 HOH A O   1 
HETATM 8797 O  O   . HOH IA 13 .   ? 32.129  2.288   42.019 1.00 30.92  ? 696 HOH A O   1 
HETATM 8798 O  O   . HOH IA 13 .   ? 43.298  12.839  46.677 1.00 40.23  ? 697 HOH A O   1 
HETATM 8799 O  O   . HOH IA 13 .   ? 29.271  -11.208 48.909 1.00 30.61  ? 698 HOH A O   1 
HETATM 8800 O  O   . HOH IA 13 .   ? 61.400  -4.797  55.207 1.00 42.31  ? 699 HOH A O   1 
HETATM 8801 O  O   . HOH IA 13 .   ? 31.387  12.105  37.147 1.00 34.36  ? 700 HOH A O   1 
HETATM 8802 O  O   . HOH IA 13 .   ? 62.786  13.399  33.139 1.00 40.96  ? 701 HOH A O   1 
HETATM 8803 O  O   . HOH IA 13 .   ? 34.549  -3.700  56.024 1.00 36.98  ? 702 HOH A O   1 
HETATM 8804 O  O   . HOH IA 13 .   ? 22.752  2.388   16.460 1.00 37.78  ? 703 HOH A O   1 
HETATM 8805 O  O   . HOH IA 13 .   ? 27.063  1.554   45.433 1.00 38.49  ? 704 HOH A O   1 
HETATM 8806 O  O   . HOH IA 13 .   ? 67.690  -4.599  29.104 1.00 46.04  ? 705 HOH A O   1 
HETATM 8807 O  O   . HOH IA 13 .   ? 52.438  11.896  38.862 1.00 43.47  ? 706 HOH A O   1 
HETATM 8808 O  O   . HOH IA 13 .   ? 45.546  -8.494  50.177 1.00 33.47  ? 707 HOH A O   1 
HETATM 8809 O  O   . HOH IA 13 .   ? 34.731  5.494   53.063 1.00 45.36  ? 708 HOH A O   1 
HETATM 8810 O  O   . HOH IA 13 .   ? 56.275  13.324  36.520 1.00 38.68  ? 709 HOH A O   1 
HETATM 8811 O  O   . HOH IA 13 .   ? 43.671  12.554  14.407 1.00 54.31  ? 710 HOH A O   1 
HETATM 8812 O  O   . HOH IA 13 .   ? 34.566  -3.874  52.040 1.00 27.63  ? 711 HOH A O   1 
HETATM 8813 O  O   . HOH IA 13 .   ? 31.279  5.767   42.714 1.00 36.52  ? 712 HOH A O   1 
HETATM 8814 O  O   . HOH IA 13 .   ? 39.025  -5.799  57.427 1.00 53.25  ? 713 HOH A O   1 
HETATM 8815 O  O   . HOH IA 13 .   ? 33.916  12.309  30.537 1.00 33.36  ? 714 HOH A O   1 
HETATM 8816 O  O   . HOH IA 13 .   ? 49.712  6.014   15.728 1.00 45.83  ? 715 HOH A O   1 
HETATM 8817 O  O   . HOH IA 13 .   ? 47.465  15.892  38.473 1.00 60.09  ? 716 HOH A O   1 
HETATM 8818 O  O   . HOH IA 13 .   ? 32.001  16.780  38.838 1.00 52.69  ? 717 HOH A O   1 
HETATM 8819 O  O   . HOH IA 13 .   ? 48.657  9.393   29.583 1.00 38.23  ? 718 HOH A O   1 
HETATM 8820 O  O   . HOH IA 13 .   ? 21.478  -14.412 26.505 1.00 59.39  ? 719 HOH A O   1 
HETATM 8821 O  O   . HOH IA 13 .   ? 37.815  6.969   48.399 1.00 32.49  ? 720 HOH A O   1 
HETATM 8822 O  O   . HOH IA 13 .   ? 42.201  17.602  32.543 1.00 41.60  ? 721 HOH A O   1 
HETATM 8823 O  O   . HOH IA 13 .   ? 41.415  13.363  41.150 1.00 50.13  ? 722 HOH A O   1 
HETATM 8824 O  O   . HOH IA 13 .   ? 49.815  -25.210 45.130 1.00 50.16  ? 723 HOH A O   1 
HETATM 8825 O  O   . HOH IA 13 .   ? 39.097  17.774  16.256 1.00 44.89  ? 724 HOH A O   1 
HETATM 8826 O  O   . HOH IA 13 .   ? 75.175  3.101   40.618 1.00 38.36  ? 725 HOH A O   1 
HETATM 8827 O  O   . HOH IA 13 .   ? 47.171  11.273  27.815 1.00 39.18  ? 726 HOH A O   1 
HETATM 8828 O  O   . HOH IA 13 .   ? 45.515  19.593  28.311 1.00 64.50  ? 727 HOH A O   1 
HETATM 8829 O  O   . HOH IA 13 .   ? 48.693  2.413   17.606 1.00 40.61  ? 728 HOH A O   1 
HETATM 8830 O  O   . HOH IA 13 .   ? 46.913  16.204  13.526 1.00 51.71  ? 729 HOH A O   1 
HETATM 8831 O  O   . HOH IA 13 .   ? 28.894  -13.822 32.563 1.00 45.18  ? 730 HOH A O   1 
HETATM 8832 O  O   . HOH IA 13 .   ? 38.812  14.347  40.210 1.00 40.18  ? 731 HOH A O   1 
HETATM 8833 O  O   . HOH IA 13 .   ? 58.436  -10.791 36.357 1.00 51.22  ? 732 HOH A O   1 
HETATM 8834 O  O   . HOH IA 13 .   ? 51.666  11.052  50.813 1.00 38.69  ? 733 HOH A O   1 
HETATM 8835 O  O   . HOH IA 13 .   ? 48.327  -10.480 25.907 1.00 62.52  ? 734 HOH A O   1 
HETATM 8836 O  O   . HOH IA 13 .   ? 26.948  -15.614 45.797 1.00 49.65  ? 735 HOH A O   1 
HETATM 8837 O  O   . HOH IA 13 .   ? 65.855  11.082  49.077 1.00 36.18  ? 736 HOH A O   1 
HETATM 8838 O  O   . HOH IA 13 .   ? 48.269  -7.225  28.716 1.00 51.13  ? 737 HOH A O   1 
HETATM 8839 O  O   . HOH IA 13 .   ? 48.727  13.256  28.019 1.00 55.24  ? 738 HOH A O   1 
HETATM 8840 O  O   . HOH IA 13 .   ? 31.951  -2.947  56.845 1.00 47.21  ? 739 HOH A O   1 
HETATM 8841 O  O   . HOH IA 13 .   ? 43.154  10.121  15.217 1.00 46.73  ? 740 HOH A O   1 
HETATM 8842 O  O   . HOH IA 13 .   ? 24.786  3.904   14.212 1.00 57.67  ? 741 HOH A O   1 
HETATM 8843 O  O   . HOH IA 13 .   ? 38.013  -9.147  55.856 1.00 55.85  ? 742 HOH A O   1 
HETATM 8844 O  O   . HOH IA 13 .   ? 33.828  0.097   40.968 1.00 28.58  ? 743 HOH A O   1 
HETATM 8845 O  O   . HOH IA 13 .   ? 55.100  -16.331 43.630 1.00 45.61  ? 744 HOH A O   1 
HETATM 8846 O  O   . HOH IA 13 .   ? 55.946  -2.163  20.023 1.00 49.07  ? 745 HOH A O   1 
HETATM 8847 O  O   . HOH IA 13 .   ? 64.139  -0.204  23.925 1.00 49.98  ? 746 HOH A O   1 
HETATM 8848 O  O   . HOH IA 13 .   ? 47.623  -5.608  54.960 1.00 44.75  ? 747 HOH A O   1 
HETATM 8849 O  O   . HOH IA 13 .   ? 68.805  -4.737  37.816 1.00 49.05  ? 748 HOH A O   1 
HETATM 8850 O  O   . HOH IA 13 .   ? 36.455  15.084  43.110 1.00 58.91  ? 749 HOH A O   1 
HETATM 8851 O  O   . HOH IA 13 .   ? 35.230  8.029   54.741 1.00 60.08  ? 750 HOH A O   1 
HETATM 8852 O  O   . HOH IA 13 .   ? 25.723  -13.268 47.210 1.00 50.42  ? 751 HOH A O   1 
HETATM 8853 O  O   . HOH IA 13 .   ? 57.592  15.687  52.339 1.00 42.93  ? 752 HOH A O   1 
HETATM 8854 O  O   . HOH IA 13 .   ? 45.048  -1.421  30.055 1.00 60.45  ? 753 HOH A O   1 
HETATM 8855 O  O   . HOH IA 13 .   ? 47.224  -26.514 38.990 1.00 44.32  ? 754 HOH A O   1 
HETATM 8856 O  O   . HOH IA 13 .   ? 67.582  6.468   54.291 1.00 44.46  ? 755 HOH A O   1 
HETATM 8857 O  O   . HOH IA 13 .   ? 43.112  -11.490 51.974 1.00 59.38  ? 756 HOH A O   1 
HETATM 8858 O  O   . HOH IA 13 .   ? 68.580  -7.152  39.156 1.00 66.72  ? 757 HOH A O   1 
HETATM 8859 O  O   . HOH IA 13 .   ? 66.107  15.574  46.768 1.00 41.46  ? 758 HOH A O   1 
HETATM 8860 O  O   . HOH IA 13 .   ? 50.903  -11.266 48.093 1.00 40.45  ? 759 HOH A O   1 
HETATM 8861 O  O   . HOH IA 13 .   ? 65.692  3.782   57.009 1.00 73.13  ? 760 HOH A O   1 
HETATM 8862 O  O   . HOH IA 13 .   ? 46.547  -4.314  21.985 1.00 54.48  ? 761 HOH A O   1 
HETATM 8863 O  O   . HOH IA 13 .   ? 40.956  12.723  45.100 1.00 48.33  ? 762 HOH A O   1 
HETATM 8864 O  O   . HOH IA 13 .   ? 48.994  -10.273 52.184 1.00 48.66  ? 763 HOH A O   1 
HETATM 8865 O  O   . HOH IA 13 .   ? 48.549  -11.158 49.541 1.00 37.39  ? 764 HOH A O   1 
HETATM 8866 O  O   . HOH IA 13 .   ? 58.683  8.178   50.080 1.00 41.77  ? 765 HOH A O   1 
HETATM 8867 O  O   . HOH IA 13 .   ? 42.458  -16.255 47.321 1.00 57.03  ? 766 HOH A O   1 
HETATM 8868 O  O   . HOH IA 13 .   ? 35.750  7.394   46.812 1.00 48.21  ? 767 HOH A O   1 
HETATM 8869 O  O   . HOH IA 13 .   ? 39.875  -11.677 21.599 1.00 58.66  ? 768 HOH A O   1 
HETATM 8870 O  O   . HOH IA 13 .   ? 42.300  -12.027 20.745 1.00 55.77  ? 769 HOH A O   1 
HETATM 8871 O  O   . HOH IA 13 .   ? 47.824  18.015  22.278 1.00 65.85  ? 770 HOH A O   1 
HETATM 8872 O  O   . HOH IA 13 .   ? 27.728  -18.146 34.869 1.00 55.08  ? 771 HOH A O   1 
HETATM 8873 O  O   . HOH IA 13 .   ? 48.729  11.461  50.947 1.00 39.72  ? 772 HOH A O   1 
HETATM 8874 O  O   . HOH IA 13 .   ? 23.150  7.401   26.490 1.00 40.94  ? 773 HOH A O   1 
HETATM 8875 O  O   . HOH IA 13 .   ? 57.952  1.789   56.536 1.00 54.77  ? 774 HOH A O   1 
HETATM 8876 O  O   . HOH IA 13 .   ? 20.162  2.330   38.170 1.00 45.44  ? 775 HOH A O   1 
HETATM 8877 O  O   . HOH IA 13 .   ? 52.718  8.360   59.116 1.00 49.72  ? 776 HOH A O   1 
HETATM 8878 O  O   . HOH IA 13 .   ? 44.238  -0.824  13.971 1.00 52.79  ? 777 HOH A O   1 
HETATM 8879 O  O   . HOH IA 13 .   ? 42.634  -6.549  14.758 1.00 53.21  ? 778 HOH A O   1 
HETATM 8880 O  O   . HOH IA 13 .   ? 62.841  7.665   55.097 1.00 60.94  ? 779 HOH A O   1 
HETATM 8881 O  O   . HOH IA 13 .   ? 54.015  12.016  36.767 1.00 35.58  ? 780 HOH A O   1 
HETATM 8882 O  O   . HOH IA 13 .   ? 63.911  12.916  45.291 1.00 48.17  ? 781 HOH A O   1 
HETATM 8883 O  O   . HOH IA 13 .   ? 38.094  10.425  46.493 1.00 56.72  ? 782 HOH A O   1 
HETATM 8884 O  O   . HOH IA 13 .   ? 45.685  -2.304  20.075 1.00 52.08  ? 783 HOH A O   1 
HETATM 8885 O  O   . HOH IA 13 .   ? 64.859  13.138  47.772 1.00 43.73  ? 784 HOH A O   1 
HETATM 8886 O  O   . HOH IA 13 .   ? 53.159  13.268  32.386 1.00 47.57  ? 785 HOH A O   1 
HETATM 8887 O  O   . HOH IA 13 .   ? 19.592  5.170   37.251 1.00 55.66  ? 786 HOH A O   1 
HETATM 8888 O  O   . HOH IA 13 .   ? 31.908  14.811  36.724 1.00 49.90  ? 787 HOH A O   1 
HETATM 8889 O  O   . HOH IA 13 .   ? 69.662  -3.147  49.116 1.00 60.23  ? 788 HOH A O   1 
HETATM 8890 O  O   . HOH IA 13 .   ? 31.641  -9.600  15.042 1.00 58.73  ? 789 HOH A O   1 
HETATM 8891 O  O   . HOH IA 13 .   ? 55.213  -7.080  49.660 1.00 49.60  ? 790 HOH A O   1 
HETATM 8892 O  O   . HOH IA 13 .   ? 28.680  -21.468 27.781 1.00 60.72  ? 791 HOH A O   1 
HETATM 8893 O  O   . HOH IA 13 .   ? 32.404  -6.925  59.492 1.00 59.39  ? 792 HOH A O   1 
HETATM 8894 O  O   . HOH IA 13 .   ? 51.451  14.429  38.855 1.00 50.65  ? 793 HOH A O   1 
HETATM 8895 O  O   . HOH IA 13 .   ? 25.006  -17.219 45.166 1.00 49.82  ? 794 HOH A O   1 
HETATM 8896 O  O   . HOH IA 13 .   ? 60.123  9.988   26.394 1.00 58.00  ? 795 HOH A O   1 
HETATM 8897 O  O   . HOH IA 13 .   ? 63.336  -9.105  39.977 1.00 53.13  ? 796 HOH A O   1 
HETATM 8898 O  O   . HOH IA 13 .   ? 31.817  -17.714 56.555 1.00 51.30  ? 797 HOH A O   1 
HETATM 8899 O  O   . HOH IA 13 .   ? 68.108  -2.607  39.116 1.00 52.81  ? 798 HOH A O   1 
HETATM 8900 O  O   . HOH IA 13 .   ? 22.629  -13.914 21.072 1.00 57.24  ? 799 HOH A O   1 
HETATM 8901 O  O   . HOH IA 13 .   ? 25.499  -17.450 37.318 1.00 47.32  ? 800 HOH A O   1 
HETATM 8902 O  O   . HOH IA 13 .   ? 27.028  -20.591 34.350 1.00 64.17  ? 801 HOH A O   1 
HETATM 8903 O  O   . HOH IA 13 .   ? 55.687  -13.913 45.963 1.00 57.28  ? 802 HOH A O   1 
HETATM 8904 O  O   . HOH IA 13 .   ? 52.834  -10.579 28.203 1.00 50.56  ? 803 HOH A O   1 
HETATM 8905 O  O   . HOH IA 13 .   ? 52.362  -9.935  49.614 1.00 52.82  ? 804 HOH A O   1 
HETATM 8906 O  O   . HOH IA 13 .   ? 21.186  -3.547  38.377 1.00 61.67  ? 805 HOH A O   1 
HETATM 8907 O  O   . HOH IA 13 .   ? 59.187  -12.750 33.161 1.00 65.68  ? 806 HOH A O   1 
HETATM 8908 O  O   . HOH IA 13 .   ? 67.260  -3.948  41.397 1.00 53.88  ? 807 HOH A O   1 
HETATM 8909 O  O   . HOH IA 13 .   ? 23.020  -15.769 40.319 1.00 48.26  ? 808 HOH A O   1 
HETATM 8910 O  O   . HOH IA 13 .   ? 72.987  8.512   51.542 1.00 52.42  ? 809 HOH A O   1 
HETATM 8911 O  O   . HOH IA 13 .   ? 60.443  -11.728 39.843 1.00 54.54  ? 810 HOH A O   1 
HETATM 8912 O  O   . HOH IA 13 .   ? 46.043  -21.643 31.071 1.00 54.55  ? 811 HOH A O   1 
HETATM 8913 O  O   . HOH IA 13 .   ? 33.407  3.469   44.383 1.00 33.59  ? 812 HOH A O   1 
HETATM 8914 O  O   . HOH IA 13 .   ? 68.674  18.469  44.062 1.00 48.80  ? 813 HOH A O   1 
HETATM 8915 O  O   . HOH IA 13 .   ? 28.872  -22.808 45.569 1.00 58.84  ? 814 HOH A O   1 
HETATM 8916 O  O   . HOH IA 13 .   ? 56.185  15.480  38.248 1.00 53.58  ? 815 HOH A O   1 
HETATM 8917 O  O   . HOH IA 13 .   ? 32.351  7.959   57.385 1.00 77.91  ? 816 HOH A O   1 
HETATM 8918 O  O   . HOH IA 13 .   ? 24.201  3.843   43.757 1.00 39.40  ? 817 HOH A O   1 
HETATM 8919 O  O   . HOH IA 13 .   ? 45.013  -5.051  13.962 1.00 56.03  ? 818 HOH A O   1 
HETATM 8920 O  O   . HOH IA 13 .   ? 42.240  7.668   57.210 1.00 42.10  ? 819 HOH A O   1 
HETATM 8921 O  O   . HOH IA 13 .   ? 40.684  -14.731 27.503 1.00 60.24  ? 820 HOH A O   1 
HETATM 8922 O  O   . HOH IA 13 .   ? 35.723  -13.543 24.226 1.00 52.63  ? 821 HOH A O   1 
HETATM 8923 O  O   . HOH IA 13 .   ? 35.261  10.278  47.241 1.00 57.28  ? 822 HOH A O   1 
HETATM 8924 O  O   . HOH IA 13 .   ? 29.699  14.039  26.899 1.00 47.54  ? 823 HOH A O   1 
HETATM 8925 O  O   . HOH IA 13 .   ? 57.346  -15.786 37.022 1.00 59.58  ? 824 HOH A O   1 
HETATM 8926 O  O   . HOH IA 13 .   ? 23.816  -17.579 42.970 1.00 51.05  ? 825 HOH A O   1 
HETATM 8927 O  O   . HOH IA 13 .   ? 30.801  5.374   52.930 1.00 55.74  ? 826 HOH A O   1 
HETATM 8928 O  O   . HOH IA 13 .   ? 26.340  -16.014 28.088 1.00 48.72  ? 827 HOH A O   1 
HETATM 8929 O  O   . HOH IA 13 .   ? 58.616  6.232   56.409 1.00 50.87  ? 828 HOH A O   1 
HETATM 8930 O  O   . HOH IA 13 .   ? 42.489  -20.271 48.211 1.00 58.35  ? 829 HOH A O   1 
HETATM 8931 O  O   . HOH IA 13 .   ? 43.639  -14.183 48.096 1.00 47.02  ? 830 HOH A O   1 
HETATM 8932 O  O   . HOH IA 13 .   ? 50.467  -4.955  29.914 1.00 57.58  ? 831 HOH A O   1 
HETATM 8933 O  O   . HOH IA 13 .   ? 44.251  6.781   58.902 1.00 52.77  ? 832 HOH A O   1 
HETATM 8934 O  O   . HOH IA 13 .   ? 38.735  -27.180 38.534 1.00 46.52  ? 833 HOH A O   1 
HETATM 8935 O  O   . HOH IA 13 .   ? 46.372  -2.902  28.775 1.00 46.24  ? 834 HOH A O   1 
HETATM 8936 O  O   . HOH IA 13 .   ? 50.007  -17.151 33.489 1.00 35.46  ? 835 HOH A O   1 
HETATM 8937 O  O   . HOH IA 13 .   ? 72.316  13.736  51.443 1.00 53.33  ? 836 HOH A O   1 
HETATM 8938 O  O   . HOH IA 13 .   ? 25.273  6.618   40.987 1.00 51.88  ? 837 HOH A O   1 
HETATM 8939 O  O   . HOH IA 13 .   ? 46.933  -5.227  30.044 1.00 43.35  ? 838 HOH A O   1 
HETATM 8940 O  O   . HOH IA 13 .   ? 63.541  -9.443  48.910 1.00 57.20  ? 839 HOH A O   1 
HETATM 8941 O  O   . HOH IA 13 .   ? 61.191  -12.251 37.137 1.00 55.72  ? 840 HOH A O   1 
HETATM 8942 O  O   . HOH IA 13 .   ? 62.573  -11.653 48.239 1.00 69.50  ? 841 HOH A O   1 
HETATM 8943 O  O   . HOH IA 13 .   ? 39.182  10.039  51.484 1.00 54.24  ? 842 HOH A O   1 
HETATM 8944 O  O   . HOH IA 13 .   ? 36.088  -11.140 22.830 1.00 46.04  ? 843 HOH A O   1 
HETATM 8945 O  O   . HOH IA 13 .   ? 46.841  -2.504  17.455 1.00 53.62  ? 844 HOH A O   1 
HETATM 8946 O  O   . HOH IA 13 .   ? 63.641  17.811  37.725 1.00 41.71  ? 845 HOH A O   1 
HETATM 8947 O  O   . HOH IA 13 .   ? 48.906  -17.622 31.127 1.00 44.58  ? 846 HOH A O   1 
HETATM 8948 O  O   . HOH IA 13 .   ? 61.113  9.536   51.353 1.00 49.31  ? 847 HOH A O   1 
HETATM 8949 O  O   . HOH IA 13 .   ? 27.085  5.610   42.490 1.00 44.37  ? 848 HOH A O   1 
HETATM 8950 O  O   . HOH IA 13 .   ? 63.951  10.688  51.086 1.00 48.99  ? 849 HOH A O   1 
HETATM 8951 O  O   . HOH IA 13 .   ? 50.232  -0.322  56.878 1.00 55.74  ? 850 HOH A O   1 
HETATM 8952 O  O   . HOH IA 13 .   ? 34.106  6.040   48.106 1.00 46.43  ? 851 HOH A O   1 
HETATM 8953 O  O   . HOH IA 13 .   ? 27.128  -15.827 33.692 1.00 47.63  ? 852 HOH A O   1 
HETATM 8954 O  O   . HOH IA 13 .   ? 50.872  -19.792 34.436 1.00 41.15  ? 853 HOH A O   1 
HETATM 8955 O  O   . HOH IA 13 .   ? 48.179  -0.700  15.838 1.00 54.60  ? 854 HOH A O   1 
HETATM 8956 O  O   . HOH IA 13 .   ? 61.848  -12.902 41.502 1.00 55.12  ? 855 HOH A O   1 
HETATM 8957 O  O   . HOH IA 13 .   ? 35.495  -11.881 20.151 1.00 57.60  ? 856 HOH A O   1 
HETATM 8958 O  O   . HOH IA 13 .   ? 32.485  4.552   46.672 1.00 37.96  ? 857 HOH A O   1 
HETATM 8959 O  O   . HOH IA 13 .   ? 27.707  -3.691  14.376 1.00 48.50  ? 858 HOH A O   1 
HETATM 8960 O  O   . HOH IA 13 .   ? 50.850  15.364  51.129 1.00 55.10  ? 859 HOH A O   1 
HETATM 8961 O  O   . HOH IA 13 .   ? 55.299  -10.295 49.148 1.00 50.61  ? 860 HOH A O   1 
HETATM 8962 O  O   . HOH IA 13 .   ? 63.646  13.670  51.951 1.00 47.30  ? 861 HOH A O   1 
HETATM 8963 O  O   . HOH IA 13 .   ? 32.210  -22.534 48.330 1.00 39.03  ? 862 HOH A O   1 
HETATM 8964 O  O   . HOH IA 13 .   ? 27.135  18.188  33.046 1.00 49.91  ? 863 HOH A O   1 
HETATM 8965 O  O   . HOH JA 13 .   ? 9.146   -17.749 46.801 1.00 58.10  ? 501 HOH B O   1 
HETATM 8966 O  O   . HOH JA 13 .   ? 22.763  -30.368 50.989 1.00 39.69  ? 502 HOH B O   1 
HETATM 8967 O  O   . HOH JA 13 .   ? -3.338  -14.336 55.307 1.00 53.57  ? 503 HOH B O   1 
HETATM 8968 O  O   . HOH JA 13 .   ? -9.788  -2.584  75.437 1.00 46.74  ? 504 HOH B O   1 
HETATM 8969 O  O   . HOH JA 13 .   ? -3.401  4.498   57.010 1.00 44.26  ? 505 HOH B O   1 
HETATM 8970 O  O   . HOH JA 13 .   ? 16.883  -29.772 46.588 1.00 55.21  ? 506 HOH B O   1 
HETATM 8971 O  O   . HOH JA 13 .   ? 18.102  -10.601 35.992 1.00 49.44  ? 507 HOH B O   1 
HETATM 8972 O  O   . HOH JA 13 .   ? 0.483   -20.909 61.906 1.00 57.09  ? 508 HOH B O   1 
HETATM 8973 O  O   . HOH JA 13 .   ? 7.148   -9.531  66.530 1.00 43.59  ? 509 HOH B O   1 
HETATM 8974 O  O   . HOH JA 13 .   ? -5.213  -10.410 42.660 1.00 53.26  ? 510 HOH B O   1 
HETATM 8975 O  O   . HOH JA 13 .   ? 1.371   -26.783 65.303 1.00 46.44  ? 511 HOH B O   1 
HETATM 8976 O  O   . HOH JA 13 .   ? 13.567  -10.593 66.933 1.00 37.02  ? 512 HOH B O   1 
HETATM 8977 O  O   . HOH JA 13 .   ? -5.475  -12.274 49.396 1.00 46.93  ? 513 HOH B O   1 
HETATM 8978 O  O   . HOH JA 13 .   ? -1.534  8.745   53.179 1.00 52.06  ? 514 HOH B O   1 
HETATM 8979 O  O   . HOH JA 13 .   ? 17.596  0.817   63.055 1.00 45.74  ? 515 HOH B O   1 
HETATM 8980 O  O   . HOH JA 13 .   ? 12.031  4.568   68.510 1.00 46.81  ? 516 HOH B O   1 
HETATM 8981 O  O   . HOH JA 13 .   ? 9.537   -10.478 73.381 1.00 39.51  ? 517 HOH B O   1 
HETATM 8982 O  O   . HOH JA 13 .   ? 7.058   10.654  66.591 1.00 49.34  ? 518 HOH B O   1 
HETATM 8983 O  O   . HOH JA 13 .   ? 21.920  8.968   58.619 1.00 54.62  ? 519 HOH B O   1 
HETATM 8984 O  O   . HOH JA 13 .   ? -3.124  -3.760  45.034 1.00 53.48  ? 520 HOH B O   1 
HETATM 8985 O  O   . HOH JA 13 .   ? -3.902  3.259   54.728 1.00 40.60  ? 521 HOH B O   1 
HETATM 8986 O  O   . HOH JA 13 .   ? 28.192  -7.459  54.141 1.00 27.66  ? 522 HOH B O   1 
HETATM 8987 O  O   . HOH JA 13 .   ? 9.438   8.854   64.170 1.00 45.79  ? 523 HOH B O   1 
HETATM 8988 O  O   . HOH JA 13 .   ? 19.708  5.939   47.262 1.00 48.71  ? 524 HOH B O   1 
HETATM 8989 O  O   . HOH JA 13 .   ? -0.355  -16.481 41.295 1.00 51.89  ? 525 HOH B O   1 
HETATM 8990 O  O   . HOH JA 13 .   ? 16.199  -11.482 69.218 1.00 31.37  ? 526 HOH B O   1 
HETATM 8991 O  O   . HOH JA 13 .   ? 20.609  -6.439  71.439 1.00 41.86  ? 527 HOH B O   1 
HETATM 8992 O  O   . HOH JA 13 .   ? 5.775   8.237   51.695 1.00 51.69  ? 528 HOH B O   1 
HETATM 8993 O  O   . HOH JA 13 .   ? -10.401 -2.691  65.065 1.00 36.75  ? 529 HOH B O   1 
HETATM 8994 O  O   . HOH JA 13 .   ? 1.278   -23.022 72.090 1.00 53.87  ? 530 HOH B O   1 
HETATM 8995 O  O   . HOH JA 13 .   ? 18.875  -16.839 37.662 1.00 50.15  ? 531 HOH B O   1 
HETATM 8996 O  O   . HOH JA 13 .   ? 26.933  -18.341 66.805 1.00 35.72  ? 532 HOH B O   1 
HETATM 8997 O  O   . HOH JA 13 .   ? -8.109  -3.574  50.794 1.00 52.52  ? 533 HOH B O   1 
HETATM 8998 O  O   . HOH JA 13 .   ? 11.670  -8.587  76.393 1.00 44.64  ? 534 HOH B O   1 
HETATM 8999 O  O   . HOH JA 13 .   ? 20.261  12.197  52.486 1.00 56.15  ? 535 HOH B O   1 
HETATM 9000 O  O   . HOH JA 13 .   ? -1.852  -17.467 47.618 1.00 45.90  ? 536 HOH B O   1 
HETATM 9001 O  O   . HOH JA 13 .   ? 29.324  -9.611  59.286 1.00 43.01  ? 537 HOH B O   1 
HETATM 9002 O  O   . HOH JA 13 .   ? 27.875  -9.783  51.967 1.00 27.36  ? 538 HOH B O   1 
HETATM 9003 O  O   . HOH JA 13 .   ? -1.604  9.866   73.291 1.00 46.20  ? 539 HOH B O   1 
HETATM 9004 O  O   . HOH JA 13 .   ? -6.888  -13.677 77.642 1.00 54.01  ? 540 HOH B O   1 
HETATM 9005 O  O   . HOH JA 13 .   ? 15.806  10.328  59.022 1.00 45.29  ? 541 HOH B O   1 
HETATM 9006 O  O   . HOH JA 13 .   ? -17.130 -2.241  60.453 1.00 46.43  ? 542 HOH B O   1 
HETATM 9007 O  O   . HOH JA 13 .   ? 17.499  -32.846 59.283 1.00 39.19  ? 543 HOH B O   1 
HETATM 9008 O  O   . HOH JA 13 .   ? 25.682  -13.259 49.823 1.00 37.84  ? 544 HOH B O   1 
HETATM 9009 O  O   . HOH JA 13 .   ? 0.938   -19.422 49.358 1.00 41.86  ? 545 HOH B O   1 
HETATM 9010 O  O   . HOH JA 13 .   ? -11.471 8.141   74.299 1.00 47.99  ? 546 HOH B O   1 
HETATM 9011 O  O   . HOH JA 13 .   ? -5.155  10.874  74.880 1.00 54.29  ? 547 HOH B O   1 
HETATM 9012 O  O   . HOH JA 13 .   ? 8.106   0.347   42.893 1.00 51.67  ? 548 HOH B O   1 
HETATM 9013 O  O   . HOH JA 13 .   ? 24.007  -3.106  52.763 1.00 41.57  ? 549 HOH B O   1 
HETATM 9014 O  O   . HOH JA 13 .   ? 17.110  -15.997 42.851 1.00 51.51  ? 550 HOH B O   1 
HETATM 9015 O  O   . HOH JA 13 .   ? -2.565  -19.130 75.731 1.00 53.09  ? 551 HOH B O   1 
HETATM 9016 O  O   . HOH JA 13 .   ? 6.625   -2.747  70.350 1.00 37.52  ? 552 HOH B O   1 
HETATM 9017 O  O   . HOH JA 13 .   ? 20.818  -7.089  66.969 1.00 31.52  ? 553 HOH B O   1 
HETATM 9018 O  O   . HOH JA 13 .   ? 1.128   5.133   66.920 1.00 39.62  ? 554 HOH B O   1 
HETATM 9019 O  O   . HOH JA 13 .   ? 15.723  -28.962 51.788 1.00 52.59  ? 555 HOH B O   1 
HETATM 9020 O  O   . HOH JA 13 .   ? 18.662  -29.666 51.974 1.00 40.51  ? 556 HOH B O   1 
HETATM 9021 O  O   . HOH JA 13 .   ? 16.509  -27.419 68.424 1.00 46.33  ? 557 HOH B O   1 
HETATM 9022 O  O   . HOH JA 13 .   ? 19.244  -17.360 44.101 1.00 51.64  ? 558 HOH B O   1 
HETATM 9023 O  O   . HOH JA 13 .   ? 22.599  5.852   47.674 1.00 50.58  ? 559 HOH B O   1 
HETATM 9024 O  O   . HOH JA 13 .   ? 17.448  10.236  53.666 1.00 54.88  ? 560 HOH B O   1 
HETATM 9025 O  O   . HOH JA 13 .   ? 11.434  -26.316 53.684 1.00 40.09  ? 561 HOH B O   1 
HETATM 9026 O  O   . HOH JA 13 .   ? 24.524  -12.434 38.177 1.00 44.06  ? 562 HOH B O   1 
HETATM 9027 O  O   . HOH JA 13 .   ? 8.934   -13.883 47.159 1.00 27.90  ? 563 HOH B O   1 
HETATM 9028 O  O   . HOH JA 13 .   ? 11.122  -31.875 59.160 1.00 58.31  ? 564 HOH B O   1 
HETATM 9029 O  O   . HOH JA 13 .   ? 18.779  -2.910  60.363 1.00 33.52  ? 565 HOH B O   1 
HETATM 9030 O  O   . HOH JA 13 .   ? 14.343  -7.643  66.303 1.00 32.21  ? 566 HOH B O   1 
HETATM 9031 O  O   . HOH JA 13 .   ? 28.458  -20.841 61.451 1.00 37.52  ? 567 HOH B O   1 
HETATM 9032 O  O   . HOH JA 13 .   ? 7.862   -2.793  67.121 1.00 34.99  ? 568 HOH B O   1 
HETATM 9033 O  O   . HOH JA 13 .   ? 15.541  -13.257 34.187 1.00 53.66  ? 569 HOH B O   1 
HETATM 9034 O  O   . HOH JA 13 .   ? 25.631  -4.512  47.770 1.00 44.53  ? 570 HOH B O   1 
HETATM 9035 O  O   . HOH JA 13 .   ? 12.778  -10.952 64.582 1.00 46.85  ? 571 HOH B O   1 
HETATM 9036 O  O   . HOH JA 13 .   ? -2.890  7.109   59.564 1.00 38.03  ? 572 HOH B O   1 
HETATM 9037 O  O   . HOH JA 13 .   ? 14.762  -8.200  75.572 1.00 36.45  ? 573 HOH B O   1 
HETATM 9038 O  O   . HOH JA 13 .   ? -13.362 2.901   67.261 1.00 38.86  ? 574 HOH B O   1 
HETATM 9039 O  O   . HOH JA 13 .   ? 23.979  -22.675 51.653 1.00 28.60  ? 575 HOH B O   1 
HETATM 9040 O  O   . HOH JA 13 .   ? 21.198  -0.088  51.163 1.00 29.74  ? 576 HOH B O   1 
HETATM 9041 O  O   . HOH JA 13 .   ? -12.539 13.324  65.530 1.00 58.64  ? 577 HOH B O   1 
HETATM 9042 O  O   . HOH JA 13 .   ? 18.419  -4.094  39.964 1.00 45.74  ? 578 HOH B O   1 
HETATM 9043 O  O   . HOH JA 13 .   ? 16.627  -17.019 46.654 1.00 40.16  ? 579 HOH B O   1 
HETATM 9044 O  O   . HOH JA 13 .   ? 6.108   -1.860  74.188 1.00 45.07  ? 580 HOH B O   1 
HETATM 9045 O  O   . HOH JA 13 .   ? 13.858  -7.727  71.677 1.00 33.16  ? 581 HOH B O   1 
HETATM 9046 O  O   . HOH JA 13 .   ? 12.277  -29.193 62.899 1.00 41.58  ? 582 HOH B O   1 
HETATM 9047 O  O   . HOH JA 13 .   ? 19.270  0.354   37.059 1.00 52.24  ? 583 HOH B O   1 
HETATM 9048 O  O   . HOH JA 13 .   ? 6.183   -19.357 47.891 1.00 37.96  ? 584 HOH B O   1 
HETATM 9049 O  O   . HOH JA 13 .   ? 6.979   5.715   62.880 1.00 35.10  ? 585 HOH B O   1 
HETATM 9050 O  O   . HOH JA 13 .   ? 10.182  -7.116  36.170 1.00 36.01  ? 586 HOH B O   1 
HETATM 9051 O  O   . HOH JA 13 .   ? 0.468   6.113   49.935 1.00 48.80  ? 587 HOH B O   1 
HETATM 9052 O  O   . HOH JA 13 .   ? 28.806  -18.664 59.596 1.00 47.85  ? 588 HOH B O   1 
HETATM 9053 O  O   . HOH JA 13 .   ? 25.214  -22.701 49.135 1.00 37.50  ? 589 HOH B O   1 
HETATM 9054 O  O   . HOH JA 13 .   ? 4.856   1.178   47.577 1.00 36.65  ? 590 HOH B O   1 
HETATM 9055 O  O   . HOH JA 13 .   ? 7.278   -23.128 54.509 1.00 46.10  ? 591 HOH B O   1 
HETATM 9056 O  O   . HOH JA 13 .   ? 9.018   -24.002 69.330 1.00 41.35  ? 592 HOH B O   1 
HETATM 9057 O  O   . HOH JA 13 .   ? 3.673   -31.729 67.918 1.00 52.44  ? 593 HOH B O   1 
HETATM 9058 O  O   . HOH JA 13 .   ? -9.453  -4.940  73.913 1.00 44.91  ? 594 HOH B O   1 
HETATM 9059 O  O   . HOH JA 13 .   ? -12.283 -8.392  55.634 1.00 47.53  ? 595 HOH B O   1 
HETATM 9060 O  O   . HOH JA 13 .   ? 10.201  -24.954 67.055 1.00 38.64  ? 596 HOH B O   1 
HETATM 9061 O  O   . HOH JA 13 .   ? 27.995  -27.310 65.559 1.00 45.89  ? 597 HOH B O   1 
HETATM 9062 O  O   . HOH JA 13 .   ? 14.430  -8.673  63.799 1.00 29.25  ? 598 HOH B O   1 
HETATM 9063 O  O   . HOH JA 13 .   ? 6.146   -0.565  45.663 1.00 37.37  ? 599 HOH B O   1 
HETATM 9064 O  O   . HOH JA 13 .   ? -12.510 -0.987  64.461 1.00 38.39  ? 600 HOH B O   1 
HETATM 9065 O  O   . HOH JA 13 .   ? 20.112  -17.681 64.762 1.00 29.26  ? 601 HOH B O   1 
HETATM 9066 O  O   . HOH JA 13 .   ? 9.254   -4.677  39.196 1.00 42.16  ? 602 HOH B O   1 
HETATM 9067 O  O   . HOH JA 13 .   ? 2.282   -0.575  73.171 1.00 43.31  ? 603 HOH B O   1 
HETATM 9068 O  O   . HOH JA 13 .   ? -7.893  -6.007  51.022 1.00 44.31  ? 604 HOH B O   1 
HETATM 9069 O  O   . HOH JA 13 .   ? 22.761  -19.341 46.186 1.00 50.77  ? 605 HOH B O   1 
HETATM 9070 O  O   . HOH JA 13 .   ? 14.578  5.499   67.777 1.00 49.34  ? 606 HOH B O   1 
HETATM 9071 O  O   . HOH JA 13 .   ? 7.461   -20.774 39.352 1.00 54.50  ? 607 HOH B O   1 
HETATM 9072 O  O   . HOH JA 13 .   ? 6.867   -19.819 44.048 1.00 45.49  ? 608 HOH B O   1 
HETATM 9073 O  O   . HOH JA 13 .   ? -0.017  9.246   65.801 1.00 46.99  ? 609 HOH B O   1 
HETATM 9074 O  O   . HOH JA 13 .   ? 20.325  -33.815 59.912 1.00 44.36  ? 610 HOH B O   1 
HETATM 9075 O  O   . HOH JA 13 .   ? -12.702 1.726   64.361 1.00 42.28  ? 611 HOH B O   1 
HETATM 9076 O  O   . HOH JA 13 .   ? 24.963  -9.141  39.122 1.00 37.75  ? 612 HOH B O   1 
HETATM 9077 O  O   . HOH JA 13 .   ? 2.351   -7.470  41.380 1.00 48.44  ? 613 HOH B O   1 
HETATM 9078 O  O   . HOH JA 13 .   ? 0.983   -10.968 58.867 1.00 45.12  ? 614 HOH B O   1 
HETATM 9079 O  O   . HOH JA 13 .   ? -0.389  -16.771 52.353 1.00 47.42  ? 615 HOH B O   1 
HETATM 9080 O  O   . HOH JA 13 .   ? 18.562  -19.776 47.859 1.00 33.94  ? 616 HOH B O   1 
HETATM 9081 O  O   . HOH JA 13 .   ? 22.792  -17.474 70.607 1.00 47.69  ? 617 HOH B O   1 
HETATM 9082 O  O   . HOH JA 13 .   ? 16.424  6.498   64.211 1.00 51.25  ? 618 HOH B O   1 
HETATM 9083 O  O   . HOH JA 13 .   ? 2.941   5.278   68.844 1.00 38.41  ? 619 HOH B O   1 
HETATM 9084 O  O   . HOH JA 13 .   ? 5.190   -0.771  70.042 1.00 43.76  ? 620 HOH B O   1 
HETATM 9085 O  O   . HOH JA 13 .   ? -12.776 -9.438  69.309 1.00 52.23  ? 621 HOH B O   1 
HETATM 9086 O  O   . HOH JA 13 .   ? 20.160  -29.883 49.933 1.00 38.81  ? 622 HOH B O   1 
HETATM 9087 O  O   . HOH JA 13 .   ? 0.436   -10.734 46.918 1.00 34.93  ? 623 HOH B O   1 
HETATM 9088 O  O   . HOH JA 13 .   ? 2.377   -8.092  72.505 1.00 35.84  ? 624 HOH B O   1 
HETATM 9089 O  O   . HOH JA 13 .   ? 6.349   11.586  64.313 1.00 42.96  ? 625 HOH B O   1 
HETATM 9090 O  O   . HOH JA 13 .   ? 19.418  4.818   49.726 1.00 40.37  ? 626 HOH B O   1 
HETATM 9091 O  O   . HOH JA 13 .   ? 22.100  -31.615 57.311 1.00 32.69  ? 627 HOH B O   1 
HETATM 9092 O  O   . HOH JA 13 .   ? 21.215  -14.709 73.942 1.00 40.76  ? 628 HOH B O   1 
HETATM 9093 O  O   . HOH JA 13 .   ? -13.987 -10.050 56.402 1.00 48.57  ? 629 HOH B O   1 
HETATM 9094 O  O   . HOH JA 13 .   ? 12.908  -2.822  59.196 1.00 29.10  ? 630 HOH B O   1 
HETATM 9095 O  O   . HOH JA 13 .   ? 6.709   2.900   47.774 1.00 42.12  ? 631 HOH B O   1 
HETATM 9096 O  O   . HOH JA 13 .   ? 18.862  -14.620 72.709 1.00 36.76  ? 632 HOH B O   1 
HETATM 9097 O  O   . HOH JA 13 .   ? -6.449  -10.632 74.821 1.00 61.01  ? 633 HOH B O   1 
HETATM 9098 O  O   . HOH JA 13 .   ? 19.815  -1.161  62.036 1.00 35.48  ? 634 HOH B O   1 
HETATM 9099 O  O   . HOH JA 13 .   ? 2.732   -16.771 62.603 1.00 45.41  ? 635 HOH B O   1 
HETATM 9100 O  O   . HOH JA 13 .   ? 25.260  -22.674 66.651 1.00 46.25  ? 636 HOH B O   1 
HETATM 9101 O  O   . HOH JA 13 .   ? 28.367  -14.211 53.735 1.00 40.82  ? 637 HOH B O   1 
HETATM 9102 O  O   . HOH JA 13 .   ? 3.967   -17.285 37.685 1.00 44.87  ? 638 HOH B O   1 
HETATM 9103 O  O   . HOH JA 13 .   ? -1.845  4.553   53.724 1.00 36.08  ? 639 HOH B O   1 
HETATM 9104 O  O   . HOH JA 13 .   ? 6.799   -7.755  71.696 1.00 43.00  ? 640 HOH B O   1 
HETATM 9105 O  O   . HOH JA 13 .   ? -2.201  6.114   79.073 1.00 53.06  ? 641 HOH B O   1 
HETATM 9106 O  O   . HOH JA 13 .   ? 4.058   1.073   71.864 1.00 51.82  ? 642 HOH B O   1 
HETATM 9107 O  O   . HOH JA 13 .   ? 7.576   -22.546 50.306 1.00 44.29  ? 643 HOH B O   1 
HETATM 9108 O  O   . HOH JA 13 .   ? -17.505 -5.686  62.119 1.00 44.01  ? 644 HOH B O   1 
HETATM 9109 O  O   . HOH JA 13 .   ? 16.556  3.990   62.864 1.00 39.66  ? 645 HOH B O   1 
HETATM 9110 O  O   . HOH JA 13 .   ? 24.849  -6.614  65.882 1.00 44.75  ? 646 HOH B O   1 
HETATM 9111 O  O   . HOH JA 13 .   ? -1.315  -11.835 78.238 1.00 48.59  ? 647 HOH B O   1 
HETATM 9112 O  O   . HOH JA 13 .   ? 15.181  -9.023  69.001 1.00 35.51  ? 648 HOH B O   1 
HETATM 9113 O  O   . HOH JA 13 .   ? 0.422   0.484   74.825 1.00 46.69  ? 649 HOH B O   1 
HETATM 9114 O  O   . HOH JA 13 .   ? 12.882  -21.889 82.613 1.00 50.16  ? 650 HOH B O   1 
HETATM 9115 O  O   . HOH JA 13 .   ? 14.469  11.135  48.122 1.00 62.73  ? 651 HOH B O   1 
HETATM 9116 O  O   . HOH JA 13 .   ? -4.028  -11.730 75.836 1.00 54.52  ? 652 HOH B O   1 
HETATM 9117 O  O   . HOH JA 13 .   ? 23.734  -4.783  58.018 1.00 48.28  ? 653 HOH B O   1 
HETATM 9118 O  O   . HOH JA 13 .   ? 23.160  -31.587 65.096 1.00 43.92  ? 654 HOH B O   1 
HETATM 9119 O  O   . HOH JA 13 .   ? 12.032  0.199   72.650 1.00 50.97  ? 655 HOH B O   1 
HETATM 9120 O  O   . HOH JA 13 .   ? 21.158  -28.162 45.775 1.00 55.61  ? 656 HOH B O   1 
HETATM 9121 O  O   . HOH JA 13 .   ? 28.187  -14.658 56.595 1.00 37.65  ? 657 HOH B O   1 
HETATM 9122 O  O   . HOH JA 13 .   ? -3.197  -4.754  76.185 1.00 55.98  ? 658 HOH B O   1 
HETATM 9123 O  O   . HOH JA 13 .   ? -16.493 4.298   61.783 1.00 58.29  ? 659 HOH B O   1 
HETATM 9124 O  O   . HOH JA 13 .   ? 4.966   -15.101 82.046 1.00 56.65  ? 660 HOH B O   1 
HETATM 9125 O  O   . HOH JA 13 .   ? 18.140  3.311   60.715 1.00 40.93  ? 661 HOH B O   1 
HETATM 9126 O  O   . HOH JA 13 .   ? 9.622   -11.197 34.956 1.00 45.61  ? 662 HOH B O   1 
HETATM 9127 O  O   . HOH JA 13 .   ? 0.406   -4.539  44.957 1.00 49.27  ? 663 HOH B O   1 
HETATM 9128 O  O   . HOH JA 13 .   ? 13.943  -6.342  77.099 1.00 44.70  ? 664 HOH B O   1 
HETATM 9129 O  O   . HOH JA 13 .   ? -6.353  -0.364  77.577 1.00 54.74  ? 665 HOH B O   1 
HETATM 9130 O  O   . HOH JA 13 .   ? 20.513  -5.623  57.573 1.00 32.02  ? 666 HOH B O   1 
HETATM 9131 O  O   . HOH JA 13 .   ? 23.239  -7.355  67.963 1.00 32.72  ? 667 HOH B O   1 
HETATM 9132 O  O   . HOH JA 13 .   ? 25.673  -4.401  54.372 1.00 40.43  ? 668 HOH B O   1 
HETATM 9133 O  O   . HOH JA 13 .   ? 4.777   -9.448  72.294 1.00 39.22  ? 669 HOH B O   1 
HETATM 9134 O  O   . HOH JA 13 .   ? 31.357  -15.423 60.671 1.00 48.79  ? 670 HOH B O   1 
HETATM 9135 O  O   . HOH JA 13 .   ? 11.859  4.114   43.542 1.00 54.64  ? 671 HOH B O   1 
HETATM 9136 O  O   . HOH JA 13 .   ? -17.198 -8.046  63.576 1.00 43.00  ? 672 HOH B O   1 
HETATM 9137 O  O   . HOH JA 13 .   ? 18.606  2.445   48.768 1.00 36.22  ? 673 HOH B O   1 
HETATM 9138 O  O   . HOH JA 13 .   ? 19.414  -12.432 71.385 1.00 36.69  ? 674 HOH B O   1 
HETATM 9139 O  O   . HOH JA 13 .   ? -2.295  -11.172 47.876 1.00 34.51  ? 675 HOH B O   1 
HETATM 9140 O  O   . HOH JA 13 .   ? -6.840  -18.480 61.117 1.00 51.05  ? 676 HOH B O   1 
HETATM 9141 O  O   . HOH JA 13 .   ? 12.017  -12.913 33.863 1.00 59.00  ? 677 HOH B O   1 
HETATM 9142 O  O   . HOH JA 13 .   ? 17.693  -1.627  70.606 1.00 46.54  ? 678 HOH B O   1 
HETATM 9143 O  O   . HOH JA 13 .   ? -11.249 15.146  61.704 1.00 59.46  ? 679 HOH B O   1 
HETATM 9144 O  O   . HOH JA 13 .   ? 5.090   -13.247 61.555 1.00 46.16  ? 680 HOH B O   1 
HETATM 9145 O  O   . HOH JA 13 .   ? -16.468 -10.314 62.374 1.00 52.17  ? 681 HOH B O   1 
HETATM 9146 O  O   . HOH JA 13 .   ? 20.379  -4.297  42.187 1.00 37.09  ? 682 HOH B O   1 
HETATM 9147 O  O   . HOH JA 13 .   ? 27.349  -10.434 47.271 1.00 52.68  ? 683 HOH B O   1 
HETATM 9148 O  O   . HOH JA 13 .   ? -1.978  -13.383 37.998 1.00 48.44  ? 684 HOH B O   1 
HETATM 9149 O  O   . HOH JA 13 .   ? 14.427  1.636   34.558 1.00 45.19  ? 685 HOH B O   1 
HETATM 9150 O  O   . HOH JA 13 .   ? 22.679  -4.239  60.273 1.00 39.90  ? 686 HOH B O   1 
HETATM 9151 O  O   . HOH JA 13 .   ? 29.860  -17.670 65.906 1.00 55.29  ? 687 HOH B O   1 
HETATM 9152 O  O   . HOH JA 13 .   ? -9.767  -11.727 51.598 1.00 60.31  ? 688 HOH B O   1 
HETATM 9153 O  O   . HOH JA 13 .   ? -0.462  -22.375 70.068 1.00 42.66  ? 689 HOH B O   1 
HETATM 9154 O  O   . HOH JA 13 .   ? -13.574 -15.326 67.448 1.00 63.91  ? 690 HOH B O   1 
HETATM 9155 O  O   . HOH JA 13 .   ? -6.188  -2.054  45.273 1.00 45.79  ? 691 HOH B O   1 
HETATM 9156 O  O   . HOH JA 13 .   ? -7.439  -10.248 49.902 1.00 49.25  ? 692 HOH B O   1 
HETATM 9157 O  O   . HOH JA 13 .   ? 6.609   -24.087 76.860 1.00 52.54  ? 693 HOH B O   1 
HETATM 9158 O  O   . HOH JA 13 .   ? 15.702  0.193   69.551 1.00 55.06  ? 694 HOH B O   1 
HETATM 9159 O  O   . HOH JA 13 .   ? 20.274  0.358   69.796 1.00 61.93  ? 695 HOH B O   1 
HETATM 9160 O  O   . HOH JA 13 .   ? 6.329   -10.988 74.199 1.00 37.39  ? 696 HOH B O   1 
HETATM 9161 O  O   . HOH JA 13 .   ? 24.554  -4.193  71.766 1.00 49.87  ? 697 HOH B O   1 
HETATM 9162 O  O   . HOH JA 13 .   ? 8.745   3.497   46.089 1.00 53.36  ? 698 HOH B O   1 
HETATM 9163 O  O   . HOH JA 13 .   ? -7.634  17.986  64.337 1.00 53.83  ? 699 HOH B O   1 
HETATM 9164 O  O   . HOH JA 13 .   ? 24.632  10.827  52.147 1.00 56.59  ? 700 HOH B O   1 
HETATM 9165 O  O   . HOH JA 13 .   ? 29.288  -21.804 47.684 1.00 59.30  ? 701 HOH B O   1 
HETATM 9166 O  O   . HOH JA 13 .   ? 0.003   -6.288  39.707 1.00 46.46  ? 702 HOH B O   1 
HETATM 9167 O  O   . HOH JA 13 .   ? 18.032  -6.569  56.352 1.00 30.62  ? 703 HOH B O   1 
HETATM 9168 O  O   . HOH JA 13 .   ? 21.293  3.006   40.512 1.00 44.99  ? 704 HOH B O   1 
HETATM 9169 O  O   . HOH JA 13 .   ? -2.171  -3.741  40.999 1.00 60.01  ? 705 HOH B O   1 
HETATM 9170 O  O   . HOH JA 13 .   ? 20.704  -33.049 67.555 1.00 58.21  ? 706 HOH B O   1 
HETATM 9171 O  O   . HOH JA 13 .   ? 11.907  -26.796 40.850 1.00 61.31  ? 707 HOH B O   1 
HETATM 9172 O  O   . HOH JA 13 .   ? 9.046   -32.519 70.304 1.00 66.08  ? 708 HOH B O   1 
HETATM 9173 O  O   . HOH JA 13 .   ? -13.819 -12.375 68.684 1.00 50.95  ? 709 HOH B O   1 
HETATM 9174 O  O   . HOH JA 13 .   ? -16.390 0.329   60.526 1.00 55.82  ? 710 HOH B O   1 
HETATM 9175 O  O   . HOH JA 13 .   ? -6.873  -5.541  40.557 1.00 63.69  ? 711 HOH B O   1 
HETATM 9176 O  O   . HOH JA 13 .   ? 8.637   -30.351 47.834 1.00 67.04  ? 712 HOH B O   1 
HETATM 9177 O  O   . HOH JA 13 .   ? 5.517   -9.379  76.414 1.00 54.37  ? 713 HOH B O   1 
HETATM 9178 O  O   . HOH JA 13 .   ? 16.292  -19.946 45.765 1.00 49.04  ? 714 HOH B O   1 
HETATM 9179 O  O   . HOH JA 13 .   ? -5.495  13.991  70.935 1.00 56.50  ? 715 HOH B O   1 
HETATM 9180 O  O   . HOH JA 13 .   ? -0.048  11.768  65.713 1.00 54.59  ? 716 HOH B O   1 
HETATM 9181 O  O   . HOH JA 13 .   ? 9.031   -27.850 49.231 1.00 60.19  ? 717 HOH B O   1 
HETATM 9182 O  O   . HOH JA 13 .   ? 7.846   0.631   39.029 1.00 58.99  ? 718 HOH B O   1 
HETATM 9183 O  O   . HOH JA 13 .   ? 13.876  -17.959 34.014 1.00 56.30  ? 719 HOH B O   1 
HETATM 9184 O  O   . HOH JA 13 .   ? -7.647  -19.241 66.660 1.00 55.00  ? 720 HOH B O   1 
HETATM 9185 O  O   . HOH JA 13 .   ? 20.809  -9.026  38.887 1.00 47.30  ? 721 HOH B O   1 
HETATM 9186 O  O   . HOH JA 13 .   ? 14.767  5.584   43.119 1.00 61.96  ? 722 HOH B O   1 
HETATM 9187 O  O   . HOH JA 13 .   ? 16.457  2.906   68.000 1.00 54.70  ? 723 HOH B O   1 
HETATM 9188 O  O   . HOH JA 13 .   ? -1.149  -2.124  45.206 1.00 49.23  ? 724 HOH B O   1 
HETATM 9189 O  O   . HOH JA 13 .   ? 19.887  1.304   61.194 1.00 49.76  ? 725 HOH B O   1 
HETATM 9190 O  O   . HOH JA 13 .   ? 7.769   -10.574 86.328 1.00 57.35  ? 726 HOH B O   1 
HETATM 9191 O  O   . HOH JA 13 .   ? 2.345   -25.924 71.120 1.00 63.59  ? 727 HOH B O   1 
HETATM 9192 O  O   . HOH JA 13 .   ? 27.008  -16.662 53.920 1.00 51.42  ? 728 HOH B O   1 
HETATM 9193 O  O   . HOH JA 13 .   ? 3.608   5.514   46.000 1.00 64.53  ? 729 HOH B O   1 
HETATM 9194 O  O   . HOH JA 13 .   ? 3.084   2.760   46.222 1.00 49.16  ? 730 HOH B O   1 
HETATM 9195 O  O   . HOH JA 13 .   ? 30.632  -12.786 56.656 1.00 40.05  ? 731 HOH B O   1 
HETATM 9196 O  O   . HOH JA 13 .   ? 1.496   -8.893  79.098 1.00 55.81  ? 732 HOH B O   1 
HETATM 9197 O  O   . HOH JA 13 .   ? 1.986   -27.809 67.973 1.00 54.50  ? 733 HOH B O   1 
HETATM 9198 O  O   . HOH JA 13 .   ? 6.293   -13.412 82.697 1.00 61.70  ? 734 HOH B O   1 
HETATM 9199 O  O   . HOH JA 13 .   ? 27.082  -20.977 65.967 1.00 35.96  ? 735 HOH B O   1 
HETATM 9200 O  O   . HOH JA 13 .   ? 28.094  -12.722 50.902 1.00 50.66  ? 736 HOH B O   1 
HETATM 9201 O  O   . HOH JA 13 .   ? 30.032  -10.359 65.739 1.00 63.91  ? 737 HOH B O   1 
HETATM 9202 O  O   . HOH JA 13 .   ? 20.441  -22.779 76.184 1.00 61.72  ? 738 HOH B O   1 
HETATM 9203 O  O   . HOH JA 13 .   ? 7.420   8.962   49.550 1.00 60.81  ? 739 HOH B O   1 
HETATM 9204 O  O   . HOH JA 13 .   ? -13.649 3.400   60.063 1.00 57.58  ? 740 HOH B O   1 
HETATM 9205 O  O   . HOH JA 13 .   ? 16.221  -19.938 40.606 1.00 56.35  ? 741 HOH B O   1 
HETATM 9206 O  O   . HOH JA 13 .   ? 18.942  -17.724 40.181 1.00 50.34  ? 742 HOH B O   1 
HETATM 9207 O  O   . HOH JA 13 .   ? 31.793  -12.803 59.285 1.00 55.71  ? 743 HOH B O   1 
HETATM 9208 O  O   . HOH JA 13 .   ? -17.961 -10.298 59.730 1.00 57.37  ? 744 HOH B O   1 
HETATM 9209 O  O   . HOH JA 13 .   ? 17.067  1.783   34.093 1.00 53.67  ? 745 HOH B O   1 
HETATM 9210 O  O   . HOH JA 13 .   ? 13.670  -5.213  33.809 1.00 51.58  ? 746 HOH B O   1 
HETATM 9211 O  O   . HOH JA 13 .   ? -14.526 -12.623 55.701 1.00 60.66  ? 747 HOH B O   1 
HETATM 9212 O  O   . HOH JA 13 .   ? 0.625   10.412  53.055 1.00 59.07  ? 748 HOH B O   1 
HETATM 9213 O  O   . HOH JA 13 .   ? 21.923  -0.637  58.168 1.00 41.68  ? 749 HOH B O   1 
HETATM 9214 O  O   . HOH JA 13 .   ? 4.383   -25.221 53.592 1.00 57.47  ? 750 HOH B O   1 
HETATM 9215 O  O   . HOH JA 13 .   ? 20.161  -2.834  57.913 1.00 46.50  ? 751 HOH B O   1 
HETATM 9216 O  O   . HOH JA 13 .   ? 28.810  -6.312  56.404 1.00 34.26  ? 752 HOH B O   1 
HETATM 9217 O  O   . HOH JA 13 .   ? 21.408  -10.906 36.889 1.00 58.93  ? 753 HOH B O   1 
HETATM 9218 O  O   . HOH JA 13 .   ? -14.865 2.076   62.194 1.00 46.41  ? 754 HOH B O   1 
HETATM 9219 O  O   . HOH JA 13 .   ? -9.417  -7.552  48.723 1.00 61.40  ? 755 HOH B O   1 
HETATM 9220 O  O   . HOH JA 13 .   ? 14.738  14.622  57.883 1.00 58.98  ? 756 HOH B O   1 
HETATM 9221 O  O   . HOH JA 13 .   ? -16.787 -8.811  56.441 1.00 62.33  ? 757 HOH B O   1 
HETATM 9222 O  O   . HOH JA 13 .   ? -1.242  -12.213 59.409 1.00 52.12  ? 758 HOH B O   1 
HETATM 9223 O  O   . HOH JA 13 .   ? 8.719   -4.282  77.535 1.00 61.16  ? 759 HOH B O   1 
HETATM 9224 O  O   . HOH JA 13 .   ? 31.760  -10.135 60.426 1.00 56.86  ? 760 HOH B O   1 
HETATM 9225 O  O   . HOH JA 13 .   ? 3.337   -14.125 61.029 1.00 55.46  ? 761 HOH B O   1 
HETATM 9226 O  O   . HOH JA 13 .   ? -7.840  -2.738  77.636 1.00 57.60  ? 762 HOH B O   1 
HETATM 9227 O  O   . HOH JA 13 .   ? 1.871   -13.665 58.380 1.00 43.95  ? 763 HOH B O   1 
HETATM 9228 O  O   . HOH JA 13 .   ? 16.469  13.097  58.934 1.00 51.29  ? 764 HOH B O   1 
HETATM 9229 O  O   . HOH JA 13 .   ? 7.869   -24.998 50.877 1.00 45.36  ? 765 HOH B O   1 
HETATM 9230 O  O   . HOH JA 13 .   ? 10.790  6.354   70.349 1.00 59.39  ? 766 HOH B O   1 
HETATM 9231 O  O   . HOH JA 13 .   ? 27.944  -7.499  60.096 1.00 47.73  ? 767 HOH B O   1 
HETATM 9232 O  O   . HOH JA 13 .   ? -11.913 -8.706  52.865 1.00 57.84  ? 768 HOH B O   1 
HETATM 9233 O  O   . HOH JA 13 .   ? -11.259 -6.750  74.547 1.00 51.94  ? 769 HOH B O   1 
HETATM 9234 O  O   . HOH JA 13 .   ? -4.079  -13.056 47.014 1.00 42.93  ? 770 HOH B O   1 
HETATM 9235 O  O   . HOH JA 13 .   ? 17.040  -24.992 45.110 1.00 50.10  ? 771 HOH B O   1 
HETATM 9236 O  O   . HOH JA 13 .   ? 17.326  -19.744 43.353 1.00 50.58  ? 772 HOH B O   1 
HETATM 9237 O  O   . HOH JA 13 .   ? 16.386  -33.656 61.151 1.00 52.80  ? 773 HOH B O   1 
HETATM 9238 O  O   . HOH JA 13 .   ? -3.805  -15.664 47.377 1.00 50.99  ? 774 HOH B O   1 
HETATM 9239 O  O   . HOH JA 13 .   ? 3.239   10.195  51.798 1.00 63.07  ? 775 HOH B O   1 
HETATM 9240 O  O   . HOH JA 13 .   ? 26.226  -5.917  59.181 1.00 43.48  ? 776 HOH B O   1 
HETATM 9241 O  O   . HOH JA 13 .   ? 8.543   -25.546 53.383 1.00 58.64  ? 777 HOH B O   1 
HETATM 9242 O  O   . HOH JA 13 .   ? 24.503  4.966   56.870 1.00 60.34  ? 778 HOH B O   1 
HETATM 9243 O  O   . HOH JA 13 .   ? 22.359  -22.930 45.683 1.00 57.98  ? 779 HOH B O   1 
HETATM 9244 O  O   . HOH JA 13 .   ? -5.488  -12.440 44.637 1.00 48.73  ? 780 HOH B O   1 
HETATM 9245 O  O   . HOH JA 13 .   ? 21.443  1.633   59.231 1.00 42.21  ? 781 HOH B O   1 
HETATM 9246 O  O   . HOH JA 13 .   ? -11.400 5.341   49.123 1.00 63.33  ? 782 HOH B O   1 
HETATM 9247 O  O   . HOH JA 13 .   ? 25.773  5.771   45.970 1.00 59.33  ? 783 HOH B O   1 
HETATM 9248 O  O   . HOH JA 13 .   ? -1.704  16.660  73.476 1.00 70.76  ? 784 HOH B O   1 
HETATM 9249 O  O   . HOH JA 13 .   ? 29.937  -5.533  60.668 1.00 61.23  ? 785 HOH B O   1 
HETATM 9250 O  O   . HOH JA 13 .   ? 13.248  -7.255  32.823 1.00 38.67  ? 786 HOH B O   1 
HETATM 9251 O  O   . HOH JA 13 .   ? 28.403  -19.250 74.569 1.00 57.45  ? 787 HOH B O   1 
HETATM 9252 O  O   . HOH KA 13 .   ? 1.377   13.775  7.448  1.00 65.40  ? 501 HOH C O   1 
HETATM 9253 O  O   . HOH KA 13 .   ? -23.286 15.761  10.001 1.00 46.08  ? 502 HOH C O   1 
HETATM 9254 O  O   . HOH KA 13 .   ? -11.023 29.439  12.520 1.00 50.22  ? 503 HOH C O   1 
HETATM 9255 O  O   . HOH KA 13 .   ? -0.679  -10.216 16.710 1.00 44.84  ? 504 HOH C O   1 
HETATM 9256 O  O   . HOH KA 13 .   ? -0.125  26.318  9.566  1.00 60.80  ? 505 HOH C O   1 
HETATM 9257 O  O   . HOH KA 13 .   ? -10.672 19.428  6.577  1.00 52.22  ? 506 HOH C O   1 
HETATM 9258 O  O   . HOH KA 13 .   ? 16.261  9.927   12.958 1.00 52.97  ? 507 HOH C O   1 
HETATM 9259 O  O   . HOH KA 13 .   ? -19.653 -2.183  36.468 1.00 52.05  ? 508 HOH C O   1 
HETATM 9260 O  O   . HOH KA 13 .   ? 4.514   -3.057  34.202 1.00 54.08  ? 509 HOH C O   1 
HETATM 9261 O  O   . HOH KA 13 .   ? -13.068 13.011  3.356  1.00 39.46  ? 510 HOH C O   1 
HETATM 9262 O  O   . HOH KA 13 .   ? -8.577  17.936  27.387 1.00 48.38  ? 511 HOH C O   1 
HETATM 9263 O  O   . HOH KA 13 .   ? -0.400  17.946  31.160 1.00 45.34  ? 512 HOH C O   1 
HETATM 9264 O  O   . HOH KA 13 .   ? 10.687  -2.313  30.726 1.00 39.58  ? 513 HOH C O   1 
HETATM 9265 O  O   . HOH KA 13 .   ? -16.915 -2.629  32.139 1.00 48.77  ? 514 HOH C O   1 
HETATM 9266 O  O   . HOH KA 13 .   ? 6.914   16.297  25.734 1.00 53.80  ? 515 HOH C O   1 
HETATM 9267 O  O   . HOH KA 13 .   ? 12.087  3.259   14.450 1.00 30.31  ? 516 HOH C O   1 
HETATM 9268 O  O   . HOH KA 13 .   ? 3.798   -6.402  19.412 1.00 30.82  ? 517 HOH C O   1 
HETATM 9269 O  O   . HOH KA 13 .   ? -21.390 -1.895  3.568  1.00 49.16  ? 518 HOH C O   1 
HETATM 9270 O  O   . HOH KA 13 .   ? -0.098  10.236  5.940  1.00 57.13  ? 519 HOH C O   1 
HETATM 9271 O  O   . HOH KA 13 .   ? -5.349  -3.396  4.036  1.00 41.20  ? 520 HOH C O   1 
HETATM 9272 O  O   . HOH KA 13 .   ? -25.522 -1.076  11.280 1.00 50.33  ? 521 HOH C O   1 
HETATM 9273 O  O   . HOH KA 13 .   ? 14.027  3.805   32.436 1.00 40.95  ? 522 HOH C O   1 
HETATM 9274 O  O   . HOH KA 13 .   ? -27.138 2.805   8.848  1.00 54.20  ? 523 HOH C O   1 
HETATM 9275 O  O   . HOH KA 13 .   ? 19.065  5.322   9.508  1.00 46.58  ? 524 HOH C O   1 
HETATM 9276 O  O   . HOH KA 13 .   ? 4.612   -0.636  25.598 1.00 30.41  ? 525 HOH C O   1 
HETATM 9277 O  O   . HOH KA 13 .   ? 1.570   -5.342  13.666 1.00 28.75  ? 526 HOH C O   1 
HETATM 9278 O  O   . HOH KA 13 .   ? -10.011 -8.282  22.366 1.00 47.92  ? 527 HOH C O   1 
HETATM 9279 O  O   . HOH KA 13 .   ? -0.760  17.658  26.934 1.00 52.64  ? 528 HOH C O   1 
HETATM 9280 O  O   . HOH KA 13 .   ? 0.837   9.176   27.256 1.00 50.31  ? 529 HOH C O   1 
HETATM 9281 O  O   . HOH KA 13 .   ? -20.594 -4.234  23.532 1.00 40.80  ? 530 HOH C O   1 
HETATM 9282 O  O   . HOH KA 13 .   ? -1.020  -6.953  8.979  1.00 48.95  ? 531 HOH C O   1 
HETATM 9283 O  O   . HOH KA 13 .   ? -16.681 23.267  -0.227 1.00 65.42  ? 532 HOH C O   1 
HETATM 9284 O  O   . HOH KA 13 .   ? -4.072  14.541  1.452  1.00 52.46  ? 533 HOH C O   1 
HETATM 9285 O  O   . HOH KA 13 .   ? -14.459 6.981   26.706 1.00 45.30  ? 534 HOH C O   1 
HETATM 9286 O  O   . HOH KA 13 .   ? -4.347  -9.122  14.309 1.00 43.76  ? 535 HOH C O   1 
HETATM 9287 O  O   . HOH KA 13 .   ? 4.102   19.565  8.419  1.00 53.24  ? 536 HOH C O   1 
HETATM 9288 O  O   . HOH KA 13 .   ? -18.661 -2.182  6.122  1.00 55.82  ? 537 HOH C O   1 
HETATM 9289 O  O   . HOH KA 13 .   ? 15.310  -0.671  8.333  1.00 41.96  ? 538 HOH C O   1 
HETATM 9290 O  O   . HOH KA 13 .   ? -3.529  -3.151  30.023 1.00 42.60  ? 539 HOH C O   1 
HETATM 9291 O  O   . HOH KA 13 .   ? -9.773  12.673  23.854 1.00 38.48  ? 540 HOH C O   1 
HETATM 9292 O  O   . HOH KA 13 .   ? 14.097  8.211   4.546  1.00 33.03  ? 541 HOH C O   1 
HETATM 9293 O  O   . HOH KA 13 .   ? -2.246  13.223  21.683 1.00 48.98  ? 542 HOH C O   1 
HETATM 9294 O  O   . HOH KA 13 .   ? -3.034  -3.164  0.775  1.00 38.47  ? 543 HOH C O   1 
HETATM 9295 O  O   . HOH KA 13 .   ? -21.283 0.826   22.787 1.00 37.13  ? 544 HOH C O   1 
HETATM 9296 O  O   . HOH KA 13 .   ? -3.777  2.874   32.454 1.00 42.76  ? 545 HOH C O   1 
HETATM 9297 O  O   . HOH KA 13 .   ? -1.831  7.796   25.663 1.00 34.63  ? 546 HOH C O   1 
HETATM 9298 O  O   . HOH KA 13 .   ? -7.504  15.570  25.043 1.00 52.06  ? 547 HOH C O   1 
HETATM 9299 O  O   . HOH KA 13 .   ? 2.155   6.852   27.037 1.00 41.83  ? 548 HOH C O   1 
HETATM 9300 O  O   . HOH KA 13 .   ? 2.650   -5.239  16.067 1.00 31.94  ? 549 HOH C O   1 
HETATM 9301 O  O   . HOH KA 13 .   ? -7.475  -10.481 25.361 1.00 58.52  ? 550 HOH C O   1 
HETATM 9302 O  O   . HOH KA 13 .   ? 7.441   3.244   4.298  1.00 30.51  ? 551 HOH C O   1 
HETATM 9303 O  O   . HOH KA 13 .   ? -1.847  5.921   1.178  1.00 36.17  ? 552 HOH C O   1 
HETATM 9304 O  O   . HOH KA 13 .   ? -8.202  13.027  26.126 1.00 45.57  ? 553 HOH C O   1 
HETATM 9305 O  O   . HOH KA 13 .   ? 15.892  2.775   7.185  1.00 39.65  ? 554 HOH C O   1 
HETATM 9306 O  O   . HOH KA 13 .   ? 12.611  -2.962  35.328 1.00 50.21  ? 555 HOH C O   1 
HETATM 9307 O  O   . HOH KA 13 .   ? -10.538 -2.087  -5.367 1.00 43.82  ? 556 HOH C O   1 
HETATM 9308 O  O   . HOH KA 13 .   ? -21.717 -6.391  22.261 1.00 48.10  ? 557 HOH C O   1 
HETATM 9309 O  O   . HOH KA 13 .   ? -4.702  11.783  4.384  1.00 42.53  ? 558 HOH C O   1 
HETATM 9310 O  O   . HOH KA 13 .   ? -12.972 14.178  30.163 1.00 45.20  ? 559 HOH C O   1 
HETATM 9311 O  O   . HOH KA 13 .   ? 0.884   8.155   2.869  1.00 41.23  ? 560 HOH C O   1 
HETATM 9312 O  O   . HOH KA 13 .   ? 1.870   0.395   4.707  1.00 30.46  ? 561 HOH C O   1 
HETATM 9313 O  O   . HOH KA 13 .   ? -5.145  -0.227  -2.083 1.00 48.50  ? 562 HOH C O   1 
HETATM 9314 O  O   . HOH KA 13 .   ? -14.349 6.511   29.358 1.00 56.14  ? 563 HOH C O   1 
HETATM 9315 O  O   . HOH KA 13 .   ? -18.651 11.255  -2.694 1.00 51.00  ? 564 HOH C O   1 
HETATM 9316 O  O   . HOH KA 13 .   ? -23.919 -5.599  23.942 1.00 41.25  ? 565 HOH C O   1 
HETATM 9317 O  O   . HOH KA 13 .   ? -13.184 17.164  4.318  1.00 45.69  ? 566 HOH C O   1 
HETATM 9318 O  O   . HOH KA 13 .   ? -14.891 22.053  23.356 1.00 47.50  ? 567 HOH C O   1 
HETATM 9319 O  O   . HOH KA 13 .   ? 16.689  3.968   28.850 1.00 40.69  ? 568 HOH C O   1 
HETATM 9320 O  O   . HOH KA 13 .   ? -10.119 20.103  30.082 1.00 53.81  ? 569 HOH C O   1 
HETATM 9321 O  O   . HOH KA 13 .   ? -23.701 -9.387  17.019 1.00 66.23  ? 570 HOH C O   1 
HETATM 9322 O  O   . HOH KA 13 .   ? 21.968  -7.014  29.726 1.00 29.96  ? 571 HOH C O   1 
HETATM 9323 O  O   . HOH KA 13 .   ? -2.639  -1.544  26.424 1.00 33.63  ? 572 HOH C O   1 
HETATM 9324 O  O   . HOH KA 13 .   ? -4.814  15.351  29.555 1.00 42.22  ? 573 HOH C O   1 
HETATM 9325 O  O   . HOH KA 13 .   ? 4.208   5.953   28.646 1.00 48.14  ? 574 HOH C O   1 
HETATM 9326 O  O   . HOH KA 13 .   ? -12.725 -1.075  2.238  1.00 40.93  ? 575 HOH C O   1 
HETATM 9327 O  O   . HOH KA 13 .   ? -14.988 8.538   6.994  1.00 33.50  ? 576 HOH C O   1 
HETATM 9328 O  O   . HOH KA 13 .   ? 18.723  2.266   27.905 1.00 45.65  ? 577 HOH C O   1 
HETATM 9329 O  O   . HOH KA 13 .   ? -0.455  -6.253  29.686 1.00 41.43  ? 578 HOH C O   1 
HETATM 9330 O  O   . HOH KA 13 .   ? -7.843  13.172  1.557  1.00 41.30  ? 579 HOH C O   1 
HETATM 9331 O  O   . HOH KA 13 .   ? -9.582  -0.151  32.445 1.00 58.71  ? 580 HOH C O   1 
HETATM 9332 O  O   . HOH KA 13 .   ? -9.836  -5.210  12.296 1.00 36.01  ? 581 HOH C O   1 
HETATM 9333 O  O   . HOH KA 13 .   ? 13.710  1.103   13.851 1.00 29.13  ? 582 HOH C O   1 
HETATM 9334 O  O   . HOH KA 13 .   ? -3.337  17.639  32.524 1.00 47.53  ? 583 HOH C O   1 
HETATM 9335 O  O   . HOH KA 13 .   ? -15.042 -5.653  34.393 1.00 65.37  ? 584 HOH C O   1 
HETATM 9336 O  O   . HOH KA 13 .   ? 22.017  0.025   16.364 1.00 31.89  ? 585 HOH C O   1 
HETATM 9337 O  O   . HOH KA 13 .   ? 1.009   13.848  25.689 1.00 49.54  ? 586 HOH C O   1 
HETATM 9338 O  O   . HOH KA 13 .   ? 2.452   -1.938  5.532  1.00 39.72  ? 587 HOH C O   1 
HETATM 9339 O  O   . HOH KA 13 .   ? -7.853  10.731  33.755 1.00 50.34  ? 588 HOH C O   1 
HETATM 9340 O  O   . HOH KA 13 .   ? 16.120  9.643   20.027 1.00 44.49  ? 589 HOH C O   1 
HETATM 9341 O  O   . HOH KA 13 .   ? 5.227   -1.399  7.057  1.00 42.47  ? 590 HOH C O   1 
HETATM 9342 O  O   . HOH KA 13 .   ? 3.029   -15.516 16.473 1.00 55.58  ? 591 HOH C O   1 
HETATM 9343 O  O   . HOH KA 13 .   ? -0.554  -6.744  14.778 1.00 32.30  ? 592 HOH C O   1 
HETATM 9344 O  O   . HOH KA 13 .   ? -12.138 -3.939  10.860 1.00 39.52  ? 593 HOH C O   1 
HETATM 9345 O  O   . HOH KA 13 .   ? 16.394  -1.260  16.875 1.00 29.76  ? 594 HOH C O   1 
HETATM 9346 O  O   . HOH KA 13 .   ? 13.463  15.373  19.379 1.00 51.80  ? 595 HOH C O   1 
HETATM 9347 O  O   . HOH KA 13 .   ? 15.998  -10.619 20.792 1.00 38.39  ? 596 HOH C O   1 
HETATM 9348 O  O   . HOH KA 13 .   ? -7.485  -9.323  19.188 1.00 45.81  ? 597 HOH C O   1 
HETATM 9349 O  O   . HOH KA 13 .   ? 15.820  7.813   26.124 1.00 45.12  ? 598 HOH C O   1 
HETATM 9350 O  O   . HOH KA 13 .   ? 21.924  -0.831  13.558 1.00 46.17  ? 599 HOH C O   1 
HETATM 9351 O  O   . HOH KA 13 .   ? -7.793  4.163   3.748  1.00 28.70  ? 600 HOH C O   1 
HETATM 9352 O  O   . HOH KA 13 .   ? -11.769 -4.147  -3.963 1.00 53.80  ? 601 HOH C O   1 
HETATM 9353 O  O   . HOH KA 13 .   ? -23.071 1.459   25.301 1.00 37.63  ? 602 HOH C O   1 
HETATM 9354 O  O   . HOH KA 13 .   ? 14.804  -3.469  30.151 1.00 41.43  ? 603 HOH C O   1 
HETATM 9355 O  O   . HOH KA 13 .   ? -7.450  15.738  27.665 1.00 50.10  ? 604 HOH C O   1 
HETATM 9356 O  O   . HOH KA 13 .   ? 1.003   2.678   2.081  1.00 32.30  ? 605 HOH C O   1 
HETATM 9357 O  O   . HOH KA 13 .   ? -9.017  22.556  29.552 1.00 41.95  ? 606 HOH C O   1 
HETATM 9358 O  O   . HOH KA 13 .   ? -25.644 12.266  8.737  1.00 59.80  ? 607 HOH C O   1 
HETATM 9359 O  O   . HOH KA 13 .   ? -10.411 5.357   22.903 1.00 33.87  ? 608 HOH C O   1 
HETATM 9360 O  O   . HOH KA 13 .   ? 4.008   0.679   28.131 1.00 34.08  ? 609 HOH C O   1 
HETATM 9361 O  O   . HOH KA 13 .   ? -1.467  16.444  12.987 1.00 57.83  ? 610 HOH C O   1 
HETATM 9362 O  O   . HOH KA 13 .   ? 1.232   -5.969  4.987  1.00 50.61  ? 611 HOH C O   1 
HETATM 9363 O  O   . HOH KA 13 .   ? -8.206  -2.161  5.515  1.00 42.32  ? 612 HOH C O   1 
HETATM 9364 O  O   . HOH KA 13 .   ? 3.954   2.033   5.729  1.00 33.03  ? 613 HOH C O   1 
HETATM 9365 O  O   . HOH KA 13 .   ? -9.456  1.417   -4.405 1.00 30.18  ? 614 HOH C O   1 
HETATM 9366 O  O   . HOH KA 13 .   ? 5.358   -4.809  26.368 1.00 35.51  ? 615 HOH C O   1 
HETATM 9367 O  O   . HOH KA 13 .   ? -26.981 4.782   13.972 1.00 48.35  ? 616 HOH C O   1 
HETATM 9368 O  O   . HOH KA 13 .   ? 14.020  -1.384  14.897 1.00 30.65  ? 617 HOH C O   1 
HETATM 9369 O  O   . HOH KA 13 .   ? -3.627  20.291  4.818  1.00 53.38  ? 618 HOH C O   1 
HETATM 9370 O  O   . HOH KA 13 .   ? 11.682  -11.166 26.369 1.00 44.36  ? 619 HOH C O   1 
HETATM 9371 O  O   . HOH KA 13 .   ? 17.988  -10.778 17.030 1.00 46.04  ? 620 HOH C O   1 
HETATM 9372 O  O   . HOH KA 13 .   ? 5.080   13.894  23.718 1.00 41.48  ? 621 HOH C O   1 
HETATM 9373 O  O   . HOH KA 13 .   ? -11.298 -2.776  0.512  1.00 35.59  ? 622 HOH C O   1 
HETATM 9374 O  O   . HOH KA 13 .   ? 3.712   9.457   30.169 1.00 52.92  ? 623 HOH C O   1 
HETATM 9375 O  O   . HOH KA 13 .   ? 18.273  -11.645 23.700 1.00 44.63  ? 624 HOH C O   1 
HETATM 9376 O  O   . HOH KA 13 .   ? -20.331 -2.863  21.023 1.00 38.04  ? 625 HOH C O   1 
HETATM 9377 O  O   . HOH KA 13 .   ? -26.898 -6.416  16.974 1.00 48.36  ? 626 HOH C O   1 
HETATM 9378 O  O   . HOH KA 13 .   ? 17.324  -8.001  29.942 1.00 54.07  ? 627 HOH C O   1 
HETATM 9379 O  O   . HOH KA 13 .   ? 16.225  -5.784  11.942 1.00 44.68  ? 628 HOH C O   1 
HETATM 9380 O  O   . HOH KA 13 .   ? -3.596  -11.749 31.659 1.00 55.63  ? 629 HOH C O   1 
HETATM 9381 O  O   . HOH KA 13 .   ? -0.065  -4.452  31.581 1.00 46.77  ? 630 HOH C O   1 
HETATM 9382 O  O   . HOH KA 13 .   ? 14.904  -12.646 27.532 1.00 58.28  ? 631 HOH C O   1 
HETATM 9383 O  O   . HOH KA 13 .   ? -19.384 -9.055  17.101 1.00 53.24  ? 632 HOH C O   1 
HETATM 9384 O  O   . HOH KA 13 .   ? -15.301 12.287  1.367  1.00 44.57  ? 633 HOH C O   1 
HETATM 9385 O  O   . HOH KA 13 .   ? -13.391 1.879   29.696 1.00 45.76  ? 634 HOH C O   1 
HETATM 9386 O  O   . HOH KA 13 .   ? 16.579  5.274   7.324  1.00 43.59  ? 635 HOH C O   1 
HETATM 9387 O  O   . HOH KA 13 .   ? 2.793   15.232  24.306 1.00 41.88  ? 636 HOH C O   1 
HETATM 9388 O  O   . HOH KA 13 .   ? -10.714 1.439   30.527 1.00 45.23  ? 637 HOH C O   1 
HETATM 9389 O  O   . HOH KA 13 .   ? -15.151 -2.336  0.366  1.00 52.18  ? 638 HOH C O   1 
HETATM 9390 O  O   . HOH KA 13 .   ? -5.052  4.322   2.852  1.00 27.10  ? 639 HOH C O   1 
HETATM 9391 O  O   . HOH KA 13 .   ? 20.465  4.035   16.359 1.00 42.15  ? 640 HOH C O   1 
HETATM 9392 O  O   . HOH KA 13 .   ? 8.995   7.157   28.507 1.00 40.91  ? 641 HOH C O   1 
HETATM 9393 O  O   . HOH KA 13 .   ? -22.318 0.886   0.233  1.00 51.09  ? 642 HOH C O   1 
HETATM 9394 O  O   . HOH KA 13 .   ? 13.738  -8.411  28.434 1.00 41.58  ? 643 HOH C O   1 
HETATM 9395 O  O   . HOH KA 13 .   ? 0.497   32.438  30.066 1.00 56.51  ? 644 HOH C O   1 
HETATM 9396 O  O   . HOH KA 13 .   ? 21.982  -5.821  16.415 1.00 32.65  ? 645 HOH C O   1 
HETATM 9397 O  O   . HOH KA 13 .   ? -14.875 -5.970  10.526 1.00 52.62  ? 646 HOH C O   1 
HETATM 9398 O  O   . HOH KA 13 .   ? 5.343   -7.097  27.457 1.00 43.37  ? 647 HOH C O   1 
HETATM 9399 O  O   . HOH KA 13 .   ? -25.213 2.982   -0.647 1.00 57.15  ? 648 HOH C O   1 
HETATM 9400 O  O   . HOH KA 13 .   ? -5.980  27.549  16.355 1.00 65.00  ? 649 HOH C O   1 
HETATM 9401 O  O   . HOH KA 13 .   ? 15.985  12.553  9.817  1.00 44.08  ? 650 HOH C O   1 
HETATM 9402 O  O   . HOH KA 13 .   ? 12.011  17.174  10.365 1.00 54.75  ? 651 HOH C O   1 
HETATM 9403 O  O   . HOH KA 13 .   ? -23.003 20.361  3.742  1.00 56.91  ? 652 HOH C O   1 
HETATM 9404 O  O   . HOH KA 13 .   ? -24.431 10.050  7.633  1.00 53.20  ? 653 HOH C O   1 
HETATM 9405 O  O   . HOH KA 13 .   ? -22.312 17.728  -1.660 1.00 62.70  ? 654 HOH C O   1 
HETATM 9406 O  O   . HOH KA 13 .   ? -16.344 6.661   -4.138 1.00 47.33  ? 655 HOH C O   1 
HETATM 9407 O  O   . HOH KA 13 .   ? 2.593   17.886  25.688 1.00 48.18  ? 656 HOH C O   1 
HETATM 9408 O  O   . HOH KA 13 .   ? 4.335   24.474  13.643 1.00 50.87  ? 657 HOH C O   1 
HETATM 9409 O  O   . HOH KA 13 .   ? 11.863  17.074  20.616 1.00 53.82  ? 658 HOH C O   1 
HETATM 9410 O  O   . HOH KA 13 .   ? -26.287 0.237   14.116 1.00 44.18  ? 659 HOH C O   1 
HETATM 9411 O  O   . HOH KA 13 .   ? 3.098   12.355  3.104  1.00 61.68  ? 660 HOH C O   1 
HETATM 9412 O  O   . HOH KA 13 .   ? 20.709  -12.003 13.918 1.00 46.63  ? 661 HOH C O   1 
HETATM 9413 O  O   . HOH KA 13 .   ? -26.735 10.818  14.273 1.00 56.33  ? 662 HOH C O   1 
HETATM 9414 O  O   . HOH KA 13 .   ? -14.696 -8.550  22.060 1.00 53.67  ? 663 HOH C O   1 
HETATM 9415 O  O   . HOH KA 13 .   ? -10.910 -6.412  14.285 1.00 46.59  ? 664 HOH C O   1 
HETATM 9416 O  O   . HOH KA 13 .   ? -13.636 -7.056  14.855 1.00 55.77  ? 665 HOH C O   1 
HETATM 9417 O  O   . HOH KA 13 .   ? -26.329 -3.690  5.216  1.00 55.61  ? 666 HOH C O   1 
HETATM 9418 O  O   . HOH KA 13 .   ? -16.653 8.134   21.807 1.00 35.79  ? 667 HOH C O   1 
HETATM 9419 O  O   . HOH KA 13 .   ? 18.604  -12.505 28.347 1.00 59.67  ? 668 HOH C O   1 
HETATM 9420 O  O   . HOH KA 13 .   ? 8.975   18.672  9.045  1.00 52.83  ? 669 HOH C O   1 
HETATM 9421 O  O   . HOH KA 13 .   ? -9.568  -4.405  2.128  1.00 49.98  ? 670 HOH C O   1 
HETATM 9422 O  O   . HOH KA 13 .   ? 3.621   3.671   1.980  1.00 28.70  ? 671 HOH C O   1 
HETATM 9423 O  O   . HOH KA 13 .   ? -6.355  2.668   33.769 1.00 50.42  ? 672 HOH C O   1 
HETATM 9424 O  O   . HOH KA 13 .   ? -9.697  -10.545 18.332 1.00 49.73  ? 673 HOH C O   1 
HETATM 9425 O  O   . HOH KA 13 .   ? 13.032  -2.738  32.453 1.00 42.77  ? 674 HOH C O   1 
HETATM 9426 O  O   . HOH KA 13 .   ? -1.743  8.146   33.272 1.00 52.57  ? 675 HOH C O   1 
HETATM 9427 O  O   . HOH KA 13 .   ? -2.521  20.065  6.973  1.00 61.22  ? 676 HOH C O   1 
HETATM 9428 O  O   . HOH KA 13 .   ? -19.411 -4.105  2.745  1.00 53.97  ? 677 HOH C O   1 
HETATM 9429 O  O   . HOH KA 13 .   ? 12.309  -14.477 25.630 1.00 55.33  ? 678 HOH C O   1 
HETATM 9430 O  O   . HOH KA 13 .   ? -2.397  -5.607  3.162  1.00 45.13  ? 679 HOH C O   1 
HETATM 9431 O  O   . HOH KA 13 .   ? 6.585   -15.915 19.045 1.00 58.34  ? 680 HOH C O   1 
HETATM 9432 O  O   . HOH KA 13 .   ? -26.599 7.053   -1.562 1.00 60.91  ? 681 HOH C O   1 
HETATM 9433 O  O   . HOH KA 13 .   ? -26.328 28.936  14.238 1.00 63.19  ? 682 HOH C O   1 
HETATM 9434 O  O   . HOH KA 13 .   ? 6.383   7.519   27.762 1.00 43.98  ? 683 HOH C O   1 
HETATM 9435 O  O   . HOH KA 13 .   ? -8.868  -9.718  12.740 1.00 52.76  ? 684 HOH C O   1 
HETATM 9436 O  O   . HOH KA 13 .   ? -8.914  -7.250  11.318 1.00 46.20  ? 685 HOH C O   1 
HETATM 9437 O  O   . HOH KA 13 .   ? -7.640  5.273   33.533 1.00 58.29  ? 686 HOH C O   1 
HETATM 9438 O  O   . HOH KA 13 .   ? -3.371  13.658  14.716 1.00 59.74  ? 687 HOH C O   1 
HETATM 9439 O  O   . HOH KA 13 .   ? -26.877 2.504   14.397 1.00 53.59  ? 688 HOH C O   1 
HETATM 9440 O  O   . HOH KA 13 .   ? -6.277  -7.042  10.152 1.00 47.99  ? 689 HOH C O   1 
HETATM 9441 O  O   . HOH KA 13 .   ? 7.129   -6.656  35.805 1.00 60.72  ? 690 HOH C O   1 
HETATM 9442 O  O   . HOH KA 13 .   ? 7.150   23.941  29.352 1.00 67.22  ? 691 HOH C O   1 
HETATM 9443 O  O   . HOH KA 13 .   ? -6.617  -4.502  6.118  1.00 43.56  ? 692 HOH C O   1 
HETATM 9444 O  O   . HOH KA 13 .   ? 16.143  -4.767  31.999 1.00 44.74  ? 693 HOH C O   1 
HETATM 9445 O  O   . HOH KA 13 .   ? 0.818   -4.514  2.273  1.00 48.88  ? 694 HOH C O   1 
HETATM 9446 O  O   . HOH KA 13 .   ? -19.557 4.267   -4.258 1.00 62.30  ? 695 HOH C O   1 
HETATM 9447 O  O   . HOH KA 13 .   ? 10.243  16.963  27.046 1.00 63.66  ? 696 HOH C O   1 
HETATM 9448 O  O   . HOH KA 13 .   ? -1.917  -8.970  13.940 1.00 42.55  ? 697 HOH C O   1 
HETATM 9449 O  O   . HOH KA 13 .   ? -0.796  12.266  8.221  1.00 66.03  ? 698 HOH C O   1 
HETATM 9450 O  O   . HOH KA 13 .   ? 13.352  17.732  12.174 1.00 55.24  ? 699 HOH C O   1 
HETATM 9451 O  O   . HOH KA 13 .   ? 4.452   6.870   31.325 1.00 58.10  ? 700 HOH C O   1 
HETATM 9452 O  O   . HOH KA 13 .   ? -25.110 12.784  3.486  1.00 65.82  ? 701 HOH C O   1 
HETATM 9453 O  O   . HOH KA 13 .   ? 19.371  4.970   18.649 1.00 53.53  ? 702 HOH C O   1 
HETATM 9454 O  O   . HOH KA 13 .   ? 7.957   -3.740  7.435  1.00 50.51  ? 703 HOH C O   1 
HETATM 9455 O  O   . HOH KA 13 .   ? 1.259   10.496  3.945  1.00 48.44  ? 704 HOH C O   1 
HETATM 9456 O  O   . HOH KA 13 .   ? 14.751  -2.550  12.558 1.00 61.27  ? 705 HOH C O   1 
HETATM 9457 O  O   . HOH KA 13 .   ? 13.068  -12.665 14.766 1.00 59.63  ? 706 HOH C O   1 
HETATM 9458 O  O   . HOH KA 13 .   ? 2.025   -0.026  2.026  1.00 31.40  ? 707 HOH C O   1 
HETATM 9459 O  O   . HOH KA 13 .   ? 2.472   5.677   33.221 1.00 56.69  ? 708 HOH C O   1 
HETATM 9460 O  O   . HOH KA 13 .   ? -22.349 5.494   -2.261 1.00 56.11  ? 709 HOH C O   1 
HETATM 9461 O  O   . HOH KA 13 .   ? 5.221   2.259   3.269  1.00 37.32  ? 710 HOH C O   1 
HETATM 9462 O  O   . HOH KA 13 .   ? -1.394  8.318   -0.301 1.00 40.46  ? 711 HOH C O   1 
HETATM 9463 O  O   . HOH KA 13 .   ? -12.875 -4.398  -1.035 1.00 54.91  ? 712 HOH C O   1 
HETATM 9464 O  O   . HOH KA 13 .   ? 19.854  -12.466 18.452 1.00 53.74  ? 713 HOH C O   1 
HETATM 9465 O  O   . HOH KA 13 .   ? 12.741  -5.324  11.785 1.00 55.27  ? 714 HOH C O   1 
HETATM 9466 O  O   . HOH KA 13 .   ? 12.570  -3.918  29.222 1.00 45.32  ? 715 HOH C O   1 
HETATM 9467 O  O   . HOH KA 13 .   ? -2.952  12.285  11.027 1.00 44.28  ? 716 HOH C O   1 
HETATM 9468 O  O   . HOH KA 13 .   ? 9.086   6.167   31.348 1.00 50.80  ? 717 HOH C O   1 
HETATM 9469 O  O   . HOH KA 13 .   ? 7.687   14.053  1.117  1.00 49.59  ? 718 HOH C O   1 
HETATM 9470 O  O   . HOH KA 13 .   ? 0.684   4.359   33.796 1.00 51.98  ? 719 HOH C O   1 
HETATM 9471 O  O   . HOH KA 13 .   ? -32.625 1.828   19.376 1.00 64.14  ? 720 HOH C O   1 
HETATM 9472 O  O   . HOH KA 13 .   ? -1.139  -2.369  -0.789 1.00 34.94  ? 721 HOH C O   1 
HETATM 9473 O  O   . HOH KA 13 .   ? 1.598   24.478  9.541  1.00 57.82  ? 722 HOH C O   1 
HETATM 9474 O  O   . HOH KA 13 .   ? -9.492  2.373   33.787 1.00 71.50  ? 723 HOH C O   1 
HETATM 9475 O  O   . HOH KA 13 .   ? -4.725  29.258  5.897  1.00 66.61  ? 724 HOH C O   1 
HETATM 9476 O  O   . HOH KA 13 .   ? 16.602  4.296   31.760 1.00 51.12  ? 725 HOH C O   1 
HETATM 9477 O  O   . HOH KA 13 .   ? 19.341  -13.254 25.812 1.00 54.58  ? 726 HOH C O   1 
HETATM 9478 O  O   . HOH KA 13 .   ? 17.656  -13.498 21.006 1.00 52.54  ? 727 HOH C O   1 
HETATM 9479 O  O   . HOH KA 13 .   ? -24.997 -3.363  3.117  1.00 60.83  ? 728 HOH C O   1 
HETATM 9480 O  O   . HOH KA 13 .   ? -4.325  5.107   0.370  1.00 34.23  ? 729 HOH C O   1 
HETATM 9481 O  O   . HOH KA 13 .   ? -20.790 -6.954  38.358 1.00 59.01  ? 730 HOH C O   1 
HETATM 9482 O  O   . HOH KA 13 .   ? -0.000  4.188   0.000  0.50 30.79  ? 731 HOH C O   1 
HETATM 9483 O  O   . HOH KA 13 .   ? 12.779  -6.644  30.117 1.00 54.98  ? 732 HOH C O   1 
HETATM 9484 O  O   . HOH KA 13 .   ? 11.658  -9.110  29.558 1.00 60.58  ? 733 HOH C O   1 
HETATM 9485 O  O   . HOH KA 13 .   ? 22.027  -12.768 10.579 1.00 53.41  ? 734 HOH C O   1 
HETATM 9486 O  O   . HOH KA 13 .   ? 1.208   12.028  14.998 1.00 59.06  ? 735 HOH C O   1 
HETATM 9487 O  O   . HOH KA 13 .   ? -9.007  17.607  1.517  1.00 57.92  ? 736 HOH C O   1 
HETATM 9488 O  O   . HOH KA 13 .   ? 8.424   -11.379 28.215 1.00 62.74  ? 737 HOH C O   1 
HETATM 9489 O  O   . HOH KA 13 .   ? 1.744   -15.104 33.486 1.00 66.71  ? 738 HOH C O   1 
# 
