data_9JN3
# 
_entry.id   9JN3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9JN3         pdb_00009jn3 10.2210/pdb9jn3/pdb 
WWPDB D_1300051696 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JN3 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 zhengyu.zhang@whu.edu.cn Zhengyu Zhang ? 'principal investigator/group leader' 0000-0001-5035-1229 
4 wqchen@whu.edu.cn        Wenqing Chen  ? 'principal investigator/group leader' 0000-0003-2557-8960 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, J.H.'    1 0009-0002-0143-1219 
'Wang, Z.Q.'  2 0009-0009-9222-0222 
'Zhang, Z.Y.' 3 0000-0001-5035-1229 
'Chen, W.Q.'  4 0000-0003-2557-8960 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1217 
_citation.page_last                 1229 
_citation.title                     
'Efficient Synthesis of Glycodiversified Nucleoside Analogues by a Thermophilic Promiscuous Glycosyltransferase' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06506 
_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 'Wang, Z.'  1  ? 
primary 'Li, J.'    2  ? 
primary 'Wang, X.'  3  ? 
primary 'Jin, B.'   4  ? 
primary 'Zhou, L.'  5  ? 
primary 'Zhao, Z.'  6  ? 
primary 'Gu, M.'    7  ? 
primary 'Song, X.'  8  ? 
primary 'Wang, J.'  9  ? 
primary 'Deng, Z.'  10 ? 
primary 'Wu, S.'    11 ? 
primary 'Zhang, Z.' 12 ? 
primary 'Chen, W.'  13 ? 
# 
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 'GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase'  34029.172 2   2.4.1.293 ? ? ? 
2 non-polymer syn "URIDINE-5'-DIPHOSPHATE-GLUCOSE"                                   566.302   2   ?         ? ? ? 
3 non-polymer syn '2-(6-AMINO-PURIN-9-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL' 267.241   2   ?         ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                    24.305    2   ?         ? ? ? 
5 water       nat water                                                              18.015    126 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'glycosyltransferase AvpGT' 
# 
_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       
;MLVSVIIPTYNRPERLAVALQSVQTLDFDSEQLEVIVVNDHGTPVDDVVEAAGRSLNVRLIDQPSQSGPSGARNAGLEVA
RGEYVAFLDDDDVFSPQHLSGTLPLLKGGADFVYVNINIARTRVTGTTIADAEVLVRLEFPYDRGLLDVTNHFAPSAVVC
RSPRSAGAFFDTALGVEEDWDFFLRLAHGHKYRVVHQPEVAIALHRIPGVESLTTPTSDDIAALKVYEDNWHLICERWPA
ATERAEQVRRFMPVMYQMAYASFEAGVPLDHHYYERTLQVLYRALGDPQPSPAQVEDELRAALEGR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLVSVIIPTYNRPERLAVALQSVQTLDFDSEQLEVIVVNDHGTPVDDVVEAAGRSLNVRLIDQPSQSGPSGARNAGLEVA
RGEYVAFLDDDDVFSPQHLSGTLPLLKGGADFVYVNINIARTRVTGTTIADAEVLVRLEFPYDRGLLDVTNHFAPSAVVC
RSPRSAGAFFDTALGVEEDWDFFLRLAHGHKYRVVHQPEVAIALHRIPGVESLTTPTSDDIAALKVYEDNWHLICERWPA
ATERAEQVRRFMPVMYQMAYASFEAGVPLDHHYYERTLQVLYRALGDPQPSPAQVEDELRAALEGR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "URIDINE-5'-DIPHOSPHATE-GLUCOSE"                                   UPG 
3 '2-(6-AMINO-PURIN-9-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL' RAB 
4 'MAGNESIUM ION'                                                    MG  
5 water                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LEU n 
1 3   VAL n 
1 4   SER n 
1 5   VAL n 
1 6   ILE n 
1 7   ILE n 
1 8   PRO n 
1 9   THR n 
1 10  TYR n 
1 11  ASN n 
1 12  ARG n 
1 13  PRO n 
1 14  GLU n 
1 15  ARG n 
1 16  LEU n 
1 17  ALA n 
1 18  VAL n 
1 19  ALA n 
1 20  LEU n 
1 21  GLN n 
1 22  SER n 
1 23  VAL n 
1 24  GLN n 
1 25  THR n 
1 26  LEU n 
1 27  ASP n 
1 28  PHE n 
1 29  ASP n 
1 30  SER n 
1 31  GLU n 
1 32  GLN n 
1 33  LEU n 
1 34  GLU n 
1 35  VAL n 
1 36  ILE n 
1 37  VAL n 
1 38  VAL n 
1 39  ASN n 
1 40  ASP n 
1 41  HIS n 
1 42  GLY n 
1 43  THR n 
1 44  PRO n 
1 45  VAL n 
1 46  ASP n 
1 47  ASP n 
1 48  VAL n 
1 49  VAL n 
1 50  GLU n 
1 51  ALA n 
1 52  ALA n 
1 53  GLY n 
1 54  ARG n 
1 55  SER n 
1 56  LEU n 
1 57  ASN n 
1 58  VAL n 
1 59  ARG n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  PRO n 
1 65  SER n 
1 66  GLN n 
1 67  SER n 
1 68  GLY n 
1 69  PRO n 
1 70  SER n 
1 71  GLY n 
1 72  ALA n 
1 73  ARG n 
1 74  ASN n 
1 75  ALA n 
1 76  GLY n 
1 77  LEU n 
1 78  GLU n 
1 79  VAL n 
1 80  ALA n 
1 81  ARG n 
1 82  GLY n 
1 83  GLU n 
1 84  TYR n 
1 85  VAL n 
1 86  ALA n 
1 87  PHE n 
1 88  LEU n 
1 89  ASP n 
1 90  ASP n 
1 91  ASP n 
1 92  ASP n 
1 93  VAL n 
1 94  PHE n 
1 95  SER n 
1 96  PRO n 
1 97  GLN n 
1 98  HIS n 
1 99  LEU n 
1 100 SER n 
1 101 GLY n 
1 102 THR n 
1 103 LEU n 
1 104 PRO n 
1 105 LEU n 
1 106 LEU n 
1 107 LYS n 
1 108 GLY n 
1 109 GLY n 
1 110 ALA n 
1 111 ASP n 
1 112 PHE n 
1 113 VAL n 
1 114 TYR n 
1 115 VAL n 
1 116 ASN n 
1 117 ILE n 
1 118 ASN n 
1 119 ILE n 
1 120 ALA n 
1 121 ARG n 
1 122 THR n 
1 123 ARG n 
1 124 VAL n 
1 125 THR n 
1 126 GLY n 
1 127 THR n 
1 128 THR n 
1 129 ILE n 
1 130 ALA n 
1 131 ASP n 
1 132 ALA n 
1 133 GLU n 
1 134 VAL n 
1 135 LEU n 
1 136 VAL n 
1 137 ARG n 
1 138 LEU n 
1 139 GLU n 
1 140 PHE n 
1 141 PRO n 
1 142 TYR n 
1 143 ASP n 
1 144 ARG n 
1 145 GLY n 
1 146 LEU n 
1 147 LEU n 
1 148 ASP n 
1 149 VAL n 
1 150 THR n 
1 151 ASN n 
1 152 HIS n 
1 153 PHE n 
1 154 ALA n 
1 155 PRO n 
1 156 SER n 
1 157 ALA n 
1 158 VAL n 
1 159 VAL n 
1 160 CYS n 
1 161 ARG n 
1 162 SER n 
1 163 PRO n 
1 164 ARG n 
1 165 SER n 
1 166 ALA n 
1 167 GLY n 
1 168 ALA n 
1 169 PHE n 
1 170 PHE n 
1 171 ASP n 
1 172 THR n 
1 173 ALA n 
1 174 LEU n 
1 175 GLY n 
1 176 VAL n 
1 177 GLU n 
1 178 GLU n 
1 179 ASP n 
1 180 TRP n 
1 181 ASP n 
1 182 PHE n 
1 183 PHE n 
1 184 LEU n 
1 185 ARG n 
1 186 LEU n 
1 187 ALA n 
1 188 HIS n 
1 189 GLY n 
1 190 HIS n 
1 191 LYS n 
1 192 TYR n 
1 193 ARG n 
1 194 VAL n 
1 195 VAL n 
1 196 HIS n 
1 197 GLN n 
1 198 PRO n 
1 199 GLU n 
1 200 VAL n 
1 201 ALA n 
1 202 ILE n 
1 203 ALA n 
1 204 LEU n 
1 205 HIS n 
1 206 ARG n 
1 207 ILE n 
1 208 PRO n 
1 209 GLY n 
1 210 VAL n 
1 211 GLU n 
1 212 SER n 
1 213 LEU n 
1 214 THR n 
1 215 THR n 
1 216 PRO n 
1 217 THR n 
1 218 SER n 
1 219 ASP n 
1 220 ASP n 
1 221 ILE n 
1 222 ALA n 
1 223 ALA n 
1 224 LEU n 
1 225 LYS n 
1 226 VAL n 
1 227 TYR n 
1 228 GLU n 
1 229 ASP n 
1 230 ASN n 
1 231 TRP n 
1 232 HIS n 
1 233 LEU n 
1 234 ILE n 
1 235 CYS n 
1 236 GLU n 
1 237 ARG n 
1 238 TRP n 
1 239 PRO n 
1 240 ALA n 
1 241 ALA n 
1 242 THR n 
1 243 GLU n 
1 244 ARG n 
1 245 ALA n 
1 246 GLU n 
1 247 GLN n 
1 248 VAL n 
1 249 ARG n 
1 250 ARG n 
1 251 PHE n 
1 252 MET n 
1 253 PRO n 
1 254 VAL n 
1 255 MET n 
1 256 TYR n 
1 257 GLN n 
1 258 MET n 
1 259 ALA n 
1 260 TYR n 
1 261 ALA n 
1 262 SER n 
1 263 PHE n 
1 264 GLU n 
1 265 ALA n 
1 266 GLY n 
1 267 VAL n 
1 268 PRO n 
1 269 LEU n 
1 270 ASP n 
1 271 HIS n 
1 272 HIS n 
1 273 TYR n 
1 274 TYR n 
1 275 GLU n 
1 276 ARG n 
1 277 THR n 
1 278 LEU n 
1 279 GLN n 
1 280 VAL n 
1 281 LEU n 
1 282 TYR n 
1 283 ARG n 
1 284 ALA n 
1 285 LEU n 
1 286 GLY n 
1 287 ASP n 
1 288 PRO n 
1 289 GLN n 
1 290 PRO n 
1 291 SER n 
1 292 PRO n 
1 293 ALA n 
1 294 GLN n 
1 295 VAL n 
1 296 GLU n 
1 297 ASP n 
1 298 GLU n 
1 299 LEU n 
1 300 ARG n 
1 301 ALA n 
1 302 ALA n 
1 303 LEU n 
1 304 GLU n 
1 305 GLY n 
1 306 ARG 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'pglI, APS67_002972' 
_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      'Streptomyces sp. AVP053U2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1737066 
_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               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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_
_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 
CYS 'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'      121.158 
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  
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 
MET 'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                    ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'        115.130 
RAB non-polymer         . '2-(6-AMINO-PURIN-9-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL' 9-BETA-D-ARABINOFURANOSYL-ADENINE 
'C10 H13 N5 O4'     267.241 
SER 'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'        105.093 
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 
UPG non-polymer         . "URIDINE-5'-DIPHOSPHATE-GLUCOSE"                                   
;URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
;
'C15 H24 N2 O17 P2' 566.302 
VAL 'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'       117.146 
# 
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   MET 1   1   1   MET MET A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  GLN 21  21  21  GLN GLN A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 TYR 142 142 142 TYR TYR A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 HIS 152 152 152 HIS HIS A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 TRP 180 180 180 TRP TRP A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 HIS 188 188 188 HIS HIS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 HIS 190 190 190 HIS HIS A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 ILE 207 207 ?   ?   ?   A . n 
A 1 208 PRO 208 208 ?   ?   ?   A . n 
A 1 209 GLY 209 209 ?   ?   ?   A . n 
A 1 210 VAL 210 210 ?   ?   ?   A . n 
A 1 211 GLU 211 211 ?   ?   ?   A . n 
A 1 212 SER 212 212 ?   ?   ?   A . n 
A 1 213 LEU 213 213 ?   ?   ?   A . n 
A 1 214 THR 214 214 ?   ?   ?   A . n 
A 1 215 THR 215 215 ?   ?   ?   A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 CYS 235 235 235 CYS CYS A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ARG 244 244 244 ARG ARG A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 GLN 247 247 247 GLN GLN A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 MET 258 258 258 MET MET A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 TYR 260 260 260 TYR TYR A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 PRO 268 268 268 PRO PRO A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 HIS 271 271 271 HIS HIS A . n 
A 1 272 HIS 272 272 272 HIS HIS A . n 
A 1 273 TYR 273 273 273 TYR TYR A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 ASP 287 287 287 ASP ASP A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 GLY 305 305 ?   ?   ?   A . n 
A 1 306 ARG 306 306 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   LEU 2   2   2   LEU LEU B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   ILE 7   7   7   ILE ILE B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   THR 9   9   9   THR THR B . n 
B 1 10  TYR 10  10  10  TYR TYR B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  ARG 12  12  12  ARG ARG B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  ARG 15  15  15  ARG ARG B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  GLN 21  21  21  GLN GLN B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  PHE 28  28  28  PHE PHE B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  GLN 32  32  32  GLN GLN B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  VAL 37  37  37  VAL VAL B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  ASN 39  39  39  ASN ASN B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  GLY 42  42  42  GLY GLY B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  ASN 57  57  57  ASN ASN B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  GLN 66  66  66  GLN GLN B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  PRO 69  69  69  PRO PRO B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  TYR 84  84  84  TYR TYR B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  ASP 91  91  91  ASP ASP B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 THR 102 102 102 THR THR B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 ILE 119 119 119 ILE ILE B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ARG 121 121 ?   ?   ?   B . n 
B 1 122 THR 122 122 ?   ?   ?   B . n 
B 1 123 ARG 123 123 ?   ?   ?   B . n 
B 1 124 VAL 124 124 ?   ?   ?   B . n 
B 1 125 THR 125 125 ?   ?   ?   B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 THR 127 127 127 THR THR B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 VAL 136 136 136 VAL VAL B . n 
B 1 137 ARG 137 137 137 ARG ARG B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 TYR 142 142 142 TYR TYR B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 HIS 152 152 152 HIS HIS B . n 
B 1 153 PHE 153 153 153 PHE PHE B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 ALA 157 157 157 ALA ALA B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 PRO 163 163 163 PRO PRO B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 PHE 169 169 169 PHE PHE B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 THR 172 172 172 THR THR B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 VAL 176 176 176 VAL VAL B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 TRP 180 180 180 TRP TRP B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 PHE 182 182 182 PHE PHE B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 LEU 186 186 186 LEU LEU B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 HIS 188 188 188 HIS HIS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 HIS 190 190 190 HIS HIS B . n 
B 1 191 LYS 191 191 191 LYS LYS B . n 
B 1 192 TYR 192 192 192 TYR TYR B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 GLN 197 197 197 GLN GLN B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 ALA 201 201 201 ALA ALA B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 HIS 205 205 205 HIS HIS B . n 
B 1 206 ARG 206 206 206 ARG ARG B . n 
B 1 207 ILE 207 207 207 ILE ILE B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 SER 212 212 212 SER SER B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 THR 215 215 215 THR THR B . n 
B 1 216 PRO 216 216 216 PRO PRO B . n 
B 1 217 THR 217 217 217 THR THR B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 ASP 219 219 219 ASP ASP B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 LYS 225 225 225 LYS LYS B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 TRP 231 231 231 TRP TRP B . n 
B 1 232 HIS 232 232 232 HIS HIS B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 CYS 235 235 235 CYS CYS B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 ARG 237 237 237 ARG ARG B . n 
B 1 238 TRP 238 238 238 TRP TRP B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ARG 244 244 244 ARG ARG B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 GLU 246 246 246 GLU GLU B . n 
B 1 247 GLN 247 247 247 GLN GLN B . n 
B 1 248 VAL 248 248 248 VAL VAL B . n 
B 1 249 ARG 249 249 249 ARG ARG B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 PHE 251 251 251 PHE PHE B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 PRO 253 253 253 PRO PRO B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 MET 255 255 255 MET MET B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 MET 258 258 258 MET MET B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 TYR 260 260 260 TYR TYR B . n 
B 1 261 ALA 261 261 261 ALA ALA B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 PHE 263 263 263 PHE PHE B . n 
B 1 264 GLU 264 264 264 GLU GLU B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 VAL 267 267 267 VAL VAL B . n 
B 1 268 PRO 268 268 268 PRO PRO B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 HIS 271 271 271 HIS HIS B . n 
B 1 272 HIS 272 272 272 HIS HIS B . n 
B 1 273 TYR 273 273 273 TYR TYR B . n 
B 1 274 TYR 274 274 274 TYR TYR B . n 
B 1 275 GLU 275 275 275 GLU GLU B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 LEU 281 281 281 LEU LEU B . n 
B 1 282 TYR 282 282 282 TYR TYR B . n 
B 1 283 ARG 283 283 283 ARG ARG B . n 
B 1 284 ALA 284 284 284 ALA ALA B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 GLY 286 286 286 GLY GLY B . n 
B 1 287 ASP 287 287 287 ASP ASP B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 SER 291 291 291 SER SER B . n 
B 1 292 PRO 292 292 292 PRO PRO B . n 
B 1 293 ALA 293 293 293 ALA ALA B . n 
B 1 294 GLN 294 294 294 GLN GLN B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 GLU 296 296 296 GLU GLU B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 ARG 300 300 300 ARG ARG B . n 
B 1 301 ALA 301 301 301 ALA ALA B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 LEU 303 303 303 LEU LEU B . n 
B 1 304 GLU 304 304 304 GLU GLU B . n 
B 1 305 GLY 305 305 ?   ?   ?   B . n 
B 1 306 ARG 306 306 ?   ?   ?   B . 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 RAB ? ? RAB ? ? 'SUBJECT OF INVESTIGATION' ? 
2 UPG ? ? UPG ? ? '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 
C 2 UPG 1  401 401 UPG DRG A . 
D 3 RAB 1  402 501 RAB Ara A . 
E 4 MG  1  403 2   MG  MG  A . 
F 2 UPG 1  401 401 UPG DRG B . 
G 3 RAB 1  402 501 RAB Ara B . 
H 4 MG  1  403 1   MG  MG  B . 
I 5 HOH 1  501 129 HOH HOH A . 
I 5 HOH 2  502 114 HOH HOH A . 
I 5 HOH 3  503 128 HOH HOH A . 
I 5 HOH 4  504 22  HOH HOH A . 
I 5 HOH 5  505 65  HOH HOH A . 
I 5 HOH 6  506 54  HOH HOH A . 
I 5 HOH 7  507 44  HOH HOH A . 
I 5 HOH 8  508 68  HOH HOH A . 
I 5 HOH 9  509 111 HOH HOH A . 
I 5 HOH 10 510 46  HOH HOH A . 
I 5 HOH 11 511 24  HOH HOH A . 
I 5 HOH 12 512 132 HOH HOH A . 
I 5 HOH 13 513 82  HOH HOH A . 
I 5 HOH 14 514 59  HOH HOH A . 
I 5 HOH 15 515 43  HOH HOH A . 
I 5 HOH 16 516 13  HOH HOH A . 
I 5 HOH 17 517 126 HOH HOH A . 
I 5 HOH 18 518 40  HOH HOH A . 
I 5 HOH 19 519 103 HOH HOH A . 
I 5 HOH 20 520 20  HOH HOH A . 
I 5 HOH 21 521 77  HOH HOH A . 
I 5 HOH 22 522 57  HOH HOH A . 
I 5 HOH 23 523 48  HOH HOH A . 
I 5 HOH 24 524 67  HOH HOH A . 
I 5 HOH 25 525 3   HOH HOH A . 
I 5 HOH 26 526 12  HOH HOH A . 
I 5 HOH 27 527 35  HOH HOH A . 
I 5 HOH 28 528 42  HOH HOH A . 
I 5 HOH 29 529 10  HOH HOH A . 
I 5 HOH 30 530 11  HOH HOH A . 
I 5 HOH 31 531 94  HOH HOH A . 
I 5 HOH 32 532 38  HOH HOH A . 
I 5 HOH 33 533 99  HOH HOH A . 
I 5 HOH 34 534 97  HOH HOH A . 
I 5 HOH 35 535 98  HOH HOH A . 
I 5 HOH 36 536 31  HOH HOH A . 
I 5 HOH 37 537 47  HOH HOH A . 
I 5 HOH 38 538 101 HOH HOH A . 
I 5 HOH 39 539 8   HOH HOH A . 
I 5 HOH 40 540 133 HOH HOH A . 
I 5 HOH 41 541 29  HOH HOH A . 
I 5 HOH 42 542 137 HOH HOH A . 
I 5 HOH 43 543 23  HOH HOH A . 
I 5 HOH 44 544 53  HOH HOH A . 
I 5 HOH 45 545 34  HOH HOH A . 
I 5 HOH 46 546 89  HOH HOH A . 
I 5 HOH 47 547 100 HOH HOH A . 
I 5 HOH 48 548 93  HOH HOH A . 
I 5 HOH 49 549 30  HOH HOH A . 
I 5 HOH 50 550 21  HOH HOH A . 
I 5 HOH 51 551 25  HOH HOH A . 
I 5 HOH 52 552 49  HOH HOH A . 
I 5 HOH 53 553 102 HOH HOH A . 
I 5 HOH 54 554 96  HOH HOH A . 
I 5 HOH 55 555 62  HOH HOH A . 
I 5 HOH 56 556 139 HOH HOH A . 
I 5 HOH 57 557 134 HOH HOH A . 
I 5 HOH 58 558 79  HOH HOH A . 
I 5 HOH 59 559 105 HOH HOH A . 
I 5 HOH 60 560 135 HOH HOH A . 
I 5 HOH 61 561 87  HOH HOH A . 
I 5 HOH 62 562 136 HOH HOH A . 
I 5 HOH 63 563 80  HOH HOH A . 
I 5 HOH 64 564 63  HOH HOH A . 
I 5 HOH 65 565 130 HOH HOH A . 
J 5 HOH 1  501 84  HOH HOH B . 
J 5 HOH 2  502 55  HOH HOH B . 
J 5 HOH 3  503 119 HOH HOH B . 
J 5 HOH 4  504 74  HOH HOH B . 
J 5 HOH 5  505 4   HOH HOH B . 
J 5 HOH 6  506 112 HOH HOH B . 
J 5 HOH 7  507 104 HOH HOH B . 
J 5 HOH 8  508 14  HOH HOH B . 
J 5 HOH 9  509 75  HOH HOH B . 
J 5 HOH 10 510 70  HOH HOH B . 
J 5 HOH 11 511 71  HOH HOH B . 
J 5 HOH 12 512 107 HOH HOH B . 
J 5 HOH 13 513 45  HOH HOH B . 
J 5 HOH 14 514 52  HOH HOH B . 
J 5 HOH 15 515 122 HOH HOH B . 
J 5 HOH 16 516 9   HOH HOH B . 
J 5 HOH 17 517 64  HOH HOH B . 
J 5 HOH 18 518 33  HOH HOH B . 
J 5 HOH 19 519 118 HOH HOH B . 
J 5 HOH 20 520 36  HOH HOH B . 
J 5 HOH 21 521 41  HOH HOH B . 
J 5 HOH 22 522 39  HOH HOH B . 
J 5 HOH 23 523 28  HOH HOH B . 
J 5 HOH 24 524 76  HOH HOH B . 
J 5 HOH 25 525 16  HOH HOH B . 
J 5 HOH 26 526 6   HOH HOH B . 
J 5 HOH 27 527 26  HOH HOH B . 
J 5 HOH 28 528 83  HOH HOH B . 
J 5 HOH 29 529 85  HOH HOH B . 
J 5 HOH 30 530 72  HOH HOH B . 
J 5 HOH 31 531 61  HOH HOH B . 
J 5 HOH 32 532 19  HOH HOH B . 
J 5 HOH 33 533 5   HOH HOH B . 
J 5 HOH 34 534 88  HOH HOH B . 
J 5 HOH 35 535 66  HOH HOH B . 
J 5 HOH 36 536 116 HOH HOH B . 
J 5 HOH 37 537 18  HOH HOH B . 
J 5 HOH 38 538 81  HOH HOH B . 
J 5 HOH 39 539 51  HOH HOH B . 
J 5 HOH 40 540 7   HOH HOH B . 
J 5 HOH 41 541 37  HOH HOH B . 
J 5 HOH 42 542 91  HOH HOH B . 
J 5 HOH 43 543 27  HOH HOH B . 
J 5 HOH 44 544 60  HOH HOH B . 
J 5 HOH 45 545 86  HOH HOH B . 
J 5 HOH 46 546 1   HOH HOH B . 
J 5 HOH 47 547 50  HOH HOH B . 
J 5 HOH 48 548 73  HOH HOH B . 
J 5 HOH 49 549 90  HOH HOH B . 
J 5 HOH 50 550 17  HOH HOH B . 
J 5 HOH 51 551 2   HOH HOH B . 
J 5 HOH 52 552 32  HOH HOH B . 
J 5 HOH 53 553 125 HOH HOH B . 
J 5 HOH 54 554 120 HOH HOH B . 
J 5 HOH 55 555 78  HOH HOH B . 
J 5 HOH 56 556 58  HOH HOH B . 
J 5 HOH 57 557 92  HOH HOH B . 
J 5 HOH 58 558 121 HOH HOH B . 
J 5 HOH 59 559 110 HOH HOH B . 
J 5 HOH 60 560 56  HOH HOH B . 
J 5 HOH 61 561 138 HOH HOH B . 
# 
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 GLU 31  ? CG  ? A GLU 31  CG  
2  1 Y 1 A GLU 31  ? CD  ? A GLU 31  CD  
3  1 Y 1 A GLU 31  ? OE1 ? A GLU 31  OE1 
4  1 Y 1 A GLU 31  ? OE2 ? A GLU 31  OE2 
5  1 Y 1 A ASP 47  ? CG  ? A ASP 47  CG  
6  1 Y 1 A ASP 47  ? OD1 ? A ASP 47  OD1 
7  1 Y 1 A ASP 47  ? OD2 ? A ASP 47  OD2 
8  1 Y 1 A GLU 50  ? CG  ? A GLU 50  CG  
9  1 Y 1 A GLU 50  ? CD  ? A GLU 50  CD  
10 1 Y 1 A GLU 50  ? OE1 ? A GLU 50  OE1 
11 1 Y 1 A GLU 50  ? OE2 ? A GLU 50  OE2 
12 1 Y 1 A ARG 54  ? CG  ? A ARG 54  CG  
13 1 Y 1 A ARG 54  ? CD  ? A ARG 54  CD  
14 1 Y 1 A ARG 54  ? NE  ? A ARG 54  NE  
15 1 Y 1 A ARG 54  ? CZ  ? A ARG 54  CZ  
16 1 Y 1 A ARG 54  ? NH1 ? A ARG 54  NH1 
17 1 Y 1 A ARG 54  ? NH2 ? A ARG 54  NH2 
18 1 Y 1 A ARG 121 ? CG  ? A ARG 121 CG  
19 1 Y 1 A ARG 121 ? CD  ? A ARG 121 CD  
20 1 Y 1 A ARG 121 ? NE  ? A ARG 121 NE  
21 1 Y 1 A ARG 121 ? CZ  ? A ARG 121 CZ  
22 1 Y 1 A ARG 121 ? NH1 ? A ARG 121 NH1 
23 1 Y 1 A ARG 121 ? NH2 ? A ARG 121 NH2 
24 1 Y 1 A ASP 131 ? CG  ? A ASP 131 CG  
25 1 Y 1 A ASP 131 ? OD1 ? A ASP 131 OD1 
26 1 Y 1 A ASP 131 ? OD2 ? A ASP 131 OD2 
27 1 Y 1 A GLU 133 ? CG  ? A GLU 133 CG  
28 1 Y 1 A GLU 133 ? CD  ? A GLU 133 CD  
29 1 Y 1 A GLU 133 ? OE1 ? A GLU 133 OE1 
30 1 Y 1 A GLU 133 ? OE2 ? A GLU 133 OE2 
31 1 Y 1 A LEU 135 ? CG  ? A LEU 135 CG  
32 1 Y 1 A LEU 135 ? CD1 ? A LEU 135 CD1 
33 1 Y 1 A LEU 135 ? CD2 ? A LEU 135 CD2 
34 1 Y 1 A HIS 205 ? CG  ? A HIS 205 CG  
35 1 Y 1 A HIS 205 ? ND1 ? A HIS 205 ND1 
36 1 Y 1 A HIS 205 ? CD2 ? A HIS 205 CD2 
37 1 Y 1 A HIS 205 ? CE1 ? A HIS 205 CE1 
38 1 Y 1 A HIS 205 ? NE2 ? A HIS 205 NE2 
39 1 Y 1 A VAL 226 ? CG1 ? A VAL 226 CG1 
40 1 Y 1 A VAL 226 ? CG2 ? A VAL 226 CG2 
41 1 Y 1 A HIS 271 ? CG  ? A HIS 271 CG  
42 1 Y 1 A HIS 271 ? ND1 ? A HIS 271 ND1 
43 1 Y 1 A HIS 271 ? CD2 ? A HIS 271 CD2 
44 1 Y 1 A HIS 271 ? CE1 ? A HIS 271 CE1 
45 1 Y 1 A HIS 271 ? NE2 ? A HIS 271 NE2 
46 1 Y 1 A ASP 287 ? CG  ? A ASP 287 CG  
47 1 Y 1 A ASP 287 ? OD1 ? A ASP 287 OD1 
48 1 Y 1 A ASP 287 ? OD2 ? A ASP 287 OD2 
49 1 Y 1 B ARG 54  ? CG  ? B ARG 54  CG  
50 1 Y 1 B ARG 54  ? CD  ? B ARG 54  CD  
51 1 Y 1 B ARG 54  ? NE  ? B ARG 54  NE  
52 1 Y 1 B ARG 54  ? CZ  ? B ARG 54  CZ  
53 1 Y 1 B ARG 54  ? NH1 ? B ARG 54  NH1 
54 1 Y 1 B ARG 54  ? NH2 ? B ARG 54  NH2 
55 1 Y 1 B GLU 133 ? CG  ? B GLU 133 CG  
56 1 Y 1 B GLU 133 ? CD  ? B GLU 133 CD  
57 1 Y 1 B GLU 133 ? OE1 ? B GLU 133 OE1 
58 1 Y 1 B GLU 133 ? OE2 ? B GLU 133 OE2 
59 1 Y 1 B VAL 134 ? CG1 ? B VAL 134 CG1 
60 1 Y 1 B VAL 134 ? CG2 ? B VAL 134 CG2 
61 1 Y 1 B LEU 135 ? CG  ? B LEU 135 CG  
62 1 Y 1 B LEU 135 ? CD1 ? B LEU 135 CD1 
63 1 Y 1 B LEU 135 ? CD2 ? B LEU 135 CD2 
64 1 Y 1 B ARG 250 ? CG  ? B ARG 250 CG  
65 1 Y 1 B ARG 250 ? CD  ? B ARG 250 CD  
66 1 Y 1 B ARG 250 ? NE  ? B ARG 250 NE  
67 1 Y 1 B ARG 250 ? CZ  ? B ARG 250 CZ  
68 1 Y 1 B ARG 250 ? NH1 ? B ARG 250 NH1 
69 1 Y 1 B ARG 250 ? NH2 ? B ARG 250 NH2 
70 1 Y 1 B HIS 271 ? CG  ? B HIS 271 CG  
71 1 Y 1 B HIS 271 ? ND1 ? B HIS 271 ND1 
72 1 Y 1 B HIS 271 ? CD2 ? B HIS 271 CD2 
73 1 Y 1 B HIS 271 ? CE1 ? B HIS 271 CE1 
74 1 Y 1 B HIS 271 ? NE2 ? B HIS 271 NE2 
75 1 Y 1 B GLN 294 ? CG  ? B GLN 294 CG  
76 1 Y 1 B GLN 294 ? CD  ? B GLN 294 CD  
77 1 Y 1 B GLN 294 ? OE1 ? B GLN 294 OE1 
78 1 Y 1 B GLN 294 ? NE2 ? B GLN 294 NE2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.12 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JN3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.302 
_cell.length_a_esd                 ? 
_cell.length_b                     95.114 
_cell.length_b_esd                 ? 
_cell.length_c                     70.988 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9JN3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9JN3 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.64 
_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    '20% (w/v) PEG 6000, 0.1 M Hepes, 0.2 M Calcium chloride dihydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-28 
_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                    ? 
_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   0.987 
_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                        'SSRF BEAMLINE BL17UM' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17UM 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JN3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               24.81 
_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                                     22081 
_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                           99.61 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.64 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.4 
_reflns_shell.d_res_low                                     2.486 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.34 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2187 
_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                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.816 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9JN3 
_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                            2.40 
_refine.ls_d_res_low                             24.81 
_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                     22068 
_refine.ls_number_reflns_R_free                  1094 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.71 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1845 
_refine.ls_R_factor_R_free                       0.2484 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1810 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      9JMA 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 27.74 
_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                             ? 
_refine.overall_SU_ML                            0.32 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        24.81 
_refine_hist.number_atoms_solvent             127 
_refine_hist.number_atoms_total               4825 
_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        4586 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         112 
_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' ? 0.011  ? 4812 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.251  ? 6593 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.339 ? 754  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065  ? 757  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 858  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 2.40 2.51  . . 137 2618 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2970 
'X-RAY DIFFRACTION' 2.51 2.64  . . 128 2611 100.00 . . . . 0.2220 . . . . . . . . . . . 0.3486 
'X-RAY DIFFRACTION' 2.64 2.81  . . 138 2614 100.00 . . . . 0.2172 . . . . . . . . . . . 0.2919 
'X-RAY DIFFRACTION' 2.81 3.02  . . 132 2602 100.00 . . . . 0.2061 . . . . . . . . . . . 0.3096 
'X-RAY DIFFRACTION' 3.02 3.33  . . 124 2658 100.00 . . . . 0.2012 . . . . . . . . . . . 0.2783 
'X-RAY DIFFRACTION' 3.33 3.81  . . 118 2613 100.00 . . . . 0.1779 . . . . . . . . . . . 0.2458 
'X-RAY DIFFRACTION' 3.81 4.79  . . 166 2617 99.00  . . . . 0.1537 . . . . . . . . . . . 0.2112 
'X-RAY DIFFRACTION' 4.79 24.81 . . 151 2641 100.00 . . . . 0.1646 . . . . . . . . . . . 0.2184 
# 
_struct.entry_id                     9JN3 
_struct.title                        'Crystal structure of AvpGT in complex with Ara-A' 
_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        9JN3 
_struct_keywords.text            'glycosyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1D2IE05_9ACTN 
_struct_ref.pdbx_db_accession          A0A1D2IE05 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLVSVIIPTYNRPERLAVALQSVQTLDFDSEQLEVIVVNDHGTPVDDVVEAAGRSLNVRLIDQPSQSGPSGARNAGLEVA
RGEYVAFLDDDDVFSPQHLSGTLPLLKGGADFVYVNINIARTRVTGTTIADAEVLVRLEFPYDRGLLDVTNHFAPSAVVC
RSPRSAGAFFDTALGVEEDWDFFLRLAHGHKYRVVHQPEVAIALHRIPGVESLTTPTSDDIAALKVYEDNWHLICERWPA
ATERAEQVRRFMPVMYQMAYASFEAGVPLDHHYYERTLQVLYRALGDPQPSPAQVEDELRAALEGR
;
_struct_ref.pdbx_align_begin           1 
# 
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 9JN3 A 1 ? 306 ? A0A1D2IE05 1 ? 306 ? 1 306 
2 1 9JN3 B 1 ? 306 ? A0A1D2IE05 1 ? 306 ? 1 306 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ARG A 12  ? THR A 25  ? ARG A 12  THR A 25  1 ? 14 
HELX_P HELX_P2  AA2 ASP A 29  ? GLU A 31  ? ASP A 29  GLU A 31  5 ? 3  
HELX_P HELX_P3  AA3 VAL A 45  ? GLY A 53  ? VAL A 45  GLY A 53  1 ? 9  
HELX_P HELX_P4  AA4 SER A 67  ? ALA A 80  ? SER A 67  ALA A 80  1 ? 14 
HELX_P HELX_P5  AA5 THR A 102 ? GLY A 108 ? THR A 102 GLY A 108 1 ? 7  
HELX_P HELX_P6  AA6 THR A 125 ? ALA A 132 ? THR A 125 ALA A 132 5 ? 8  
HELX_P HELX_P7  AA7 GLY A 145 ? THR A 150 ? GLY A 145 THR A 150 1 ? 6  
HELX_P HELX_P8  AA8 ALA A 154 ? SER A 156 ? ALA A 154 SER A 156 5 ? 3  
HELX_P HELX_P9  AA9 SER A 162 ? GLY A 167 ? SER A 162 GLY A 167 1 ? 6  
HELX_P HELX_P10 AB1 GLU A 177 ? HIS A 188 ? GLU A 177 HIS A 188 1 ? 12 
HELX_P HELX_P11 AB2 THR A 217 ? TRP A 238 ? THR A 217 TRP A 238 1 ? 22 
HELX_P HELX_P12 AB3 THR A 242 ? ARG A 249 ? THR A 242 ARG A 249 1 ? 8  
HELX_P HELX_P13 AB4 ARG A 250 ? ALA A 265 ? ARG A 250 ALA A 265 1 ? 16 
HELX_P HELX_P14 AB5 HIS A 272 ? LEU A 285 ? HIS A 272 LEU A 285 1 ? 14 
HELX_P HELX_P15 AB6 SER A 291 ? GLU A 304 ? SER A 291 GLU A 304 1 ? 14 
HELX_P HELX_P16 AB7 ARG B 12  ? THR B 25  ? ARG B 12  THR B 25  1 ? 14 
HELX_P HELX_P17 AB8 ASP B 29  ? GLU B 31  ? ASP B 29  GLU B 31  5 ? 3  
HELX_P HELX_P18 AB9 VAL B 45  ? GLY B 53  ? VAL B 45  GLY B 53  1 ? 9  
HELX_P HELX_P19 AC1 SER B 67  ? ALA B 80  ? SER B 67  ALA B 80  1 ? 14 
HELX_P HELX_P20 AC2 THR B 102 ? GLY B 108 ? THR B 102 GLY B 108 1 ? 7  
HELX_P HELX_P21 AC3 THR B 128 ? ALA B 132 ? THR B 128 ALA B 132 5 ? 5  
HELX_P HELX_P22 AC4 GLY B 145 ? THR B 150 ? GLY B 145 THR B 150 1 ? 6  
HELX_P HELX_P23 AC5 ALA B 154 ? SER B 156 ? ALA B 154 SER B 156 5 ? 3  
HELX_P HELX_P24 AC6 SER B 162 ? GLY B 167 ? SER B 162 GLY B 167 1 ? 6  
HELX_P HELX_P25 AC7 GLU B 177 ? GLY B 189 ? GLU B 177 GLY B 189 1 ? 13 
HELX_P HELX_P26 AC8 GLY B 209 ? THR B 214 ? GLY B 209 THR B 214 5 ? 6  
HELX_P HELX_P27 AC9 SER B 218 ? TRP B 238 ? SER B 218 TRP B 238 1 ? 21 
HELX_P HELX_P28 AD1 THR B 242 ? ARG B 249 ? THR B 242 ARG B 249 1 ? 8  
HELX_P HELX_P29 AD2 ARG B 250 ? ALA B 265 ? ARG B 250 ALA B 265 1 ? 16 
HELX_P HELX_P30 AD3 HIS B 272 ? LEU B 285 ? HIS B 272 LEU B 285 1 ? 14 
HELX_P HELX_P31 AD4 SER B 291 ? LEU B 303 ? SER B 291 LEU B 303 1 ? 13 
# 
_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 
metalc1  metalc ? ? A ASP 91 OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP 91  A MG  403 1_555 ? ? ? ? ? ? ? 2.661 ? ? 
metalc2  metalc ? ? A ASP 91 OD2 ? ? ? 1_555 E MG  . MG ? ? A ASP 91  A MG  403 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc3  metalc ? ? C UPG .  O2A ? ? ? 1_555 E MG  . MG ? ? A UPG 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc4  metalc ? ? C UPG .  O1B ? ? ? 1_555 E MG  . MG ? ? A UPG 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.194 ? ? 
metalc5  metalc ? ? E MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  403 A HOH 503 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc6  metalc ? ? E MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  403 A HOH 505 1_555 ? ? ? ? ? ? ? 2.243 ? ? 
metalc7  metalc ? ? B ASP 91 OD1 ? ? ? 1_555 H MG  . MG ? ? B ASP 91  B MG  403 1_555 ? ? ? ? ? ? ? 2.683 ? ? 
metalc8  metalc ? ? B ASP 91 OD2 ? ? ? 1_555 H MG  . MG ? ? B ASP 91  B MG  403 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
metalc9  metalc ? ? F UPG .  O2A ? ? ? 1_555 H MG  . MG ? ? B UPG 401 B MG  403 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
metalc10 metalc ? ? F UPG .  O1B ? ? ? 1_555 H MG  . MG ? ? B UPG 401 B MG  403 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? B MG  403 B HOH 506 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? B MG  403 B HOH 517 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 OD2 ? A ASP 91 ? A ASP 91  ? 1_555 51.9  ? 
2  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O2A ? C UPG .  ? A UPG 401 ? 1_555 83.4  ? 
3  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O2A ? C UPG .  ? A UPG 401 ? 1_555 86.4  ? 
4  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1B ? C UPG .  ? A UPG 401 ? 1_555 155.1 ? 
5  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1B ? C UPG .  ? A UPG 401 ? 1_555 141.8 ? 
6  O2A ? C UPG .  ? A UPG 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1B ? C UPG .  ? A UPG 401 ? 1_555 78.2  ? 
7  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 503 ? 1_555 127.5 ? 
8  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 503 ? 1_555 77.7  ? 
9  O2A ? C UPG .  ? A UPG 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 503 ? 1_555 79.4  ? 
10 O1B ? C UPG .  ? A UPG 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 503 ? 1_555 65.3  ? 
11 OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 505 ? 1_555 75.0  ? 
12 OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 505 ? 1_555 120.9 ? 
13 O2A ? C UPG .  ? A UPG 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 505 ? 1_555 114.0 ? 
14 O1B ? C UPG .  ? A UPG 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 505 ? 1_555 97.3  ? 
15 O   ? I HOH .  ? A HOH 503 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? I HOH .  ? A HOH 505 ? 1_555 156.4 ? 
16 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 52.5  ? 
17 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O2A ? F UPG .  ? B UPG 401 ? 1_555 88.1  ? 
18 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O2A ? F UPG .  ? B UPG 401 ? 1_555 89.6  ? 
19 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O1B ? F UPG .  ? B UPG 401 ? 1_555 160.7 ? 
20 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O1B ? F UPG .  ? B UPG 401 ? 1_555 134.4 ? 
21 O2A ? F UPG .  ? B UPG 401 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O1B ? F UPG .  ? B UPG 401 ? 1_555 74.8  ? 
22 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 506 ? 1_555 123.5 ? 
23 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 506 ? 1_555 73.5  ? 
24 O2A ? F UPG .  ? B UPG 401 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 506 ? 1_555 74.9  ? 
25 O1B ? F UPG .  ? B UPG 401 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 506 ? 1_555 61.1  ? 
26 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 517 ? 1_555 80.9  ? 
27 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 517 ? 1_555 130.2 ? 
28 O2A ? F UPG .  ? B UPG 401 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 517 ? 1_555 107.2 ? 
29 O1B ? F UPG .  ? B UPG 401 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 517 ? 1_555 95.4  ? 
30 O   ? J HOH .  ? B HOH 506 ? 1_555 MG ? H MG . ? B MG 403 ? 1_555 O   ? J HOH .  ? B HOH 517 ? 1_555 155.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? 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 58  ? ASP A 62  ? VAL A 58  ASP A 62  
AA1 2 LEU A 33  ? ASN A 39  ? LEU A 33  ASN A 39  
AA1 3 VAL A 3   ? THR A 9   ? VAL A 3   THR A 9   
AA1 4 TYR A 84  ? PHE A 87  ? TYR A 84  PHE A 87  
AA1 5 VAL A 158 ? ARG A 161 ? VAL A 158 ARG A 161 
AA1 6 PHE A 112 ? ALA A 120 ? PHE A 112 ALA A 120 
AA1 7 VAL A 134 ? LEU A 138 ? VAL A 134 LEU A 138 
AA2 1 VAL A 58  ? ASP A 62  ? VAL A 58  ASP A 62  
AA2 2 LEU A 33  ? ASN A 39  ? LEU A 33  ASN A 39  
AA2 3 VAL A 3   ? THR A 9   ? VAL A 3   THR A 9   
AA2 4 TYR A 84  ? PHE A 87  ? TYR A 84  PHE A 87  
AA2 5 VAL A 158 ? ARG A 161 ? VAL A 158 ARG A 161 
AA2 6 PHE A 112 ? ALA A 120 ? PHE A 112 ALA A 120 
AA2 7 VAL A 194 ? HIS A 205 ? VAL A 194 HIS A 205 
AA3 1 VAL B 58  ? ASP B 62  ? VAL B 58  ASP B 62  
AA3 2 LEU B 33  ? ASN B 39  ? LEU B 33  ASN B 39  
AA3 3 VAL B 3   ? THR B 9   ? VAL B 3   THR B 9   
AA3 4 TYR B 84  ? PHE B 87  ? TYR B 84  PHE B 87  
AA3 5 VAL B 158 ? ARG B 161 ? VAL B 158 ARG B 161 
AA3 6 PHE B 112 ? ILE B 119 ? PHE B 112 ILE B 119 
AA3 7 VAL B 136 ? LEU B 138 ? VAL B 136 LEU B 138 
AA4 1 VAL B 58  ? ASP B 62  ? VAL B 58  ASP B 62  
AA4 2 LEU B 33  ? ASN B 39  ? LEU B 33  ASN B 39  
AA4 3 VAL B 3   ? THR B 9   ? VAL B 3   THR B 9   
AA4 4 TYR B 84  ? PHE B 87  ? TYR B 84  PHE B 87  
AA4 5 VAL B 158 ? ARG B 161 ? VAL B 158 ARG B 161 
AA4 6 PHE B 112 ? ILE B 119 ? PHE B 112 ILE B 119 
AA4 7 VAL B 194 ? ALA B 203 ? VAL B 194 ALA B 203 
# 
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 O ARG A 59  ? O ARG A 59  N VAL A 37  ? N VAL A 37  
AA1 2 3 O ILE A 36  ? O ILE A 36  N VAL A 5   ? N VAL A 5   
AA1 3 4 N SER A 4   ? N SER A 4   O ALA A 86  ? O ALA A 86  
AA1 4 5 N VAL A 85  ? N VAL A 85  O CYS A 160 ? O CYS A 160 
AA1 5 6 O VAL A 159 ? O VAL A 159 N VAL A 113 ? N VAL A 113 
AA1 6 7 N ILE A 119 ? N ILE A 119 O VAL A 136 ? O VAL A 136 
AA2 1 2 O ARG A 59  ? O ARG A 59  N VAL A 37  ? N VAL A 37  
AA2 2 3 O ILE A 36  ? O ILE A 36  N VAL A 5   ? N VAL A 5   
AA2 3 4 N SER A 4   ? N SER A 4   O ALA A 86  ? O ALA A 86  
AA2 4 5 N VAL A 85  ? N VAL A 85  O CYS A 160 ? O CYS A 160 
AA2 5 6 O VAL A 159 ? O VAL A 159 N VAL A 113 ? N VAL A 113 
AA2 6 7 N ASN A 118 ? N ASN A 118 O LEU A 204 ? O LEU A 204 
AA3 1 2 O ILE B 61  ? O ILE B 61  N VAL B 37  ? N VAL B 37  
AA3 2 3 O VAL B 38  ? O VAL B 38  N THR B 9   ? N THR B 9   
AA3 3 4 N SER B 4   ? N SER B 4   O TYR B 84  ? O TYR B 84  
AA3 4 5 N VAL B 85  ? N VAL B 85  O CYS B 160 ? O CYS B 160 
AA3 5 6 O VAL B 159 ? O VAL B 159 N VAL B 113 ? N VAL B 113 
AA3 6 7 N ILE B 117 ? N ILE B 117 O LEU B 138 ? O LEU B 138 
AA4 1 2 O ILE B 61  ? O ILE B 61  N VAL B 37  ? N VAL B 37  
AA4 2 3 O VAL B 38  ? O VAL B 38  N THR B 9   ? N THR B 9   
AA4 3 4 N SER B 4   ? N SER B 4   O TYR B 84  ? O TYR B 84  
AA4 4 5 N VAL B 85  ? N VAL B 85  O CYS B 160 ? O CYS B 160 
AA4 5 6 O VAL B 159 ? O VAL B 159 N VAL B 113 ? N VAL B 113 
AA4 6 7 N TYR B 114 ? N TYR B 114 O GLN B 197 ? O GLN B 197 
# 
_pdbx_entry_details.entry_id                   9JN3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 TYR A 10  ? ? -160.06 104.08 
2  1 PHE A 112 ? ? -165.96 114.37 
3  1 ALA A 130 ? ? -77.76  35.40  
4  1 TYR A 142 ? ? -87.45  31.59  
5  1 SER A 162 ? ? -25.15  101.93 
6  1 THR A 217 ? ? -29.61  -53.36 
7  1 ASP A 270 ? ? -49.91  150.45 
8  1 HIS A 272 ? ? -114.92 60.81  
9  1 ASP A 287 ? ? -39.09  -75.53 
10 1 GLN B 32  ? ? -109.67 49.28  
11 1 ASP B 40  ? ? -82.48  43.57  
12 1 TYR B 142 ? ? -91.67  45.79  
13 1 PRO B 216 ? ? -45.09  92.85  
14 1 SER B 218 ? ? 72.81   -6.57  
15 1 SER B 262 ? ? -37.00  -38.32 
16 1 GLN B 289 ? ? -25.00  105.94 
17 1 LEU B 303 ? ? -67.14  1.19   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 207 ? A ILE 207 
2  1 Y 1 A PRO 208 ? A PRO 208 
3  1 Y 1 A GLY 209 ? A GLY 209 
4  1 Y 1 A VAL 210 ? A VAL 210 
5  1 Y 1 A GLU 211 ? A GLU 211 
6  1 Y 1 A SER 212 ? A SER 212 
7  1 Y 1 A LEU 213 ? A LEU 213 
8  1 Y 1 A THR 214 ? A THR 214 
9  1 Y 1 A THR 215 ? A THR 215 
10 1 Y 1 A GLY 305 ? A GLY 305 
11 1 Y 1 A ARG 306 ? A ARG 306 
12 1 Y 1 B ARG 121 ? B ARG 121 
13 1 Y 1 B THR 122 ? B THR 122 
14 1 Y 1 B ARG 123 ? B ARG 123 
15 1 Y 1 B VAL 124 ? B VAL 124 
16 1 Y 1 B THR 125 ? B THR 125 
17 1 Y 1 B GLY 305 ? B GLY 305 
18 1 Y 1 B ARG 306 ? B ARG 306 
# 
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  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
MG  MG     MG N N 250 
PHE N      N  N N 251 
PHE CA     C  N S 252 
PHE C      C  N N 253 
PHE O      O  N N 254 
PHE CB     C  N N 255 
PHE CG     C  Y N 256 
PHE CD1    C  Y N 257 
PHE CD2    C  Y N 258 
PHE CE1    C  Y N 259 
PHE CE2    C  Y N 260 
PHE CZ     C  Y N 261 
PHE OXT    O  N N 262 
PHE H      H  N N 263 
PHE H2     H  N N 264 
PHE HA     H  N N 265 
PHE HB2    H  N N 266 
PHE HB3    H  N N 267 
PHE HD1    H  N N 268 
PHE HD2    H  N N 269 
PHE HE1    H  N N 270 
PHE HE2    H  N N 271 
PHE HZ     H  N N 272 
PHE HXT    H  N N 273 
PRO N      N  N N 274 
PRO CA     C  N S 275 
PRO C      C  N N 276 
PRO O      O  N N 277 
PRO CB     C  N N 278 
PRO CG     C  N N 279 
PRO CD     C  N N 280 
PRO OXT    O  N N 281 
PRO H      H  N N 282 
PRO HA     H  N N 283 
PRO HB2    H  N N 284 
PRO HB3    H  N N 285 
PRO HG2    H  N N 286 
PRO HG3    H  N N 287 
PRO HD2    H  N N 288 
PRO HD3    H  N N 289 
PRO HXT    H  N N 290 
RAB "O5'"  O  N N 291 
RAB "C5'"  C  N N 292 
RAB "C4'"  C  N R 293 
RAB "O4'"  O  N N 294 
RAB "C1'"  C  N R 295 
RAB N9     N  Y N 296 
RAB C4     C  Y N 297 
RAB N3     N  Y N 298 
RAB C2     C  Y N 299 
RAB N1     N  Y N 300 
RAB C6     C  Y N 301 
RAB N6     N  N N 302 
RAB C5     C  Y N 303 
RAB N7     N  Y N 304 
RAB C8     C  Y N 305 
RAB "C2'"  C  N S 306 
RAB "O2'"  O  N N 307 
RAB "C3'"  C  N S 308 
RAB "O3'"  O  N N 309 
RAB "H5'"  H  N N 310 
RAB "H5'1" H  N N 311 
RAB "H5'2" H  N N 312 
RAB "H4'"  H  N N 313 
RAB "H1'"  H  N N 314 
RAB H2     H  N N 315 
RAB HN61   H  N N 316 
RAB HN62   H  N N 317 
RAB H8     H  N N 318 
RAB "H2'"  H  N N 319 
RAB H1     H  N N 320 
RAB "H3'"  H  N N 321 
RAB H3     H  N N 322 
SER N      N  N N 323 
SER CA     C  N S 324 
SER C      C  N N 325 
SER O      O  N N 326 
SER CB     C  N N 327 
SER OG     O  N N 328 
SER OXT    O  N N 329 
SER H      H  N N 330 
SER H2     H  N N 331 
SER HA     H  N N 332 
SER HB2    H  N N 333 
SER HB3    H  N N 334 
SER HG     H  N N 335 
SER HXT    H  N N 336 
THR N      N  N N 337 
THR CA     C  N S 338 
THR C      C  N N 339 
THR O      O  N N 340 
THR CB     C  N R 341 
THR OG1    O  N N 342 
THR CG2    C  N N 343 
THR OXT    O  N N 344 
THR H      H  N N 345 
THR H2     H  N N 346 
THR HA     H  N N 347 
THR HB     H  N N 348 
THR HG1    H  N N 349 
THR HG21   H  N N 350 
THR HG22   H  N N 351 
THR HG23   H  N N 352 
THR HXT    H  N N 353 
TRP N      N  N N 354 
TRP CA     C  N S 355 
TRP C      C  N N 356 
TRP O      O  N N 357 
TRP CB     C  N N 358 
TRP CG     C  Y N 359 
TRP CD1    C  Y N 360 
TRP CD2    C  Y N 361 
TRP NE1    N  Y N 362 
TRP CE2    C  Y N 363 
TRP CE3    C  Y N 364 
TRP CZ2    C  Y N 365 
TRP CZ3    C  Y N 366 
TRP CH2    C  Y N 367 
TRP OXT    O  N N 368 
TRP H      H  N N 369 
TRP H2     H  N N 370 
TRP HA     H  N N 371 
TRP HB2    H  N N 372 
TRP HB3    H  N N 373 
TRP HD1    H  N N 374 
TRP HE1    H  N N 375 
TRP HE3    H  N N 376 
TRP HZ2    H  N N 377 
TRP HZ3    H  N N 378 
TRP HH2    H  N N 379 
TRP HXT    H  N N 380 
TYR N      N  N N 381 
TYR CA     C  N S 382 
TYR C      C  N N 383 
TYR O      O  N N 384 
TYR CB     C  N N 385 
TYR CG     C  Y N 386 
TYR CD1    C  Y N 387 
TYR CD2    C  Y N 388 
TYR CE1    C  Y N 389 
TYR CE2    C  Y N 390 
TYR CZ     C  Y N 391 
TYR OH     O  N N 392 
TYR OXT    O  N N 393 
TYR H      H  N N 394 
TYR H2     H  N N 395 
TYR HA     H  N N 396 
TYR HB2    H  N N 397 
TYR HB3    H  N N 398 
TYR HD1    H  N N 399 
TYR HD2    H  N N 400 
TYR HE1    H  N N 401 
TYR HE2    H  N N 402 
TYR HH     H  N N 403 
TYR HXT    H  N N 404 
UPG N1     N  N N 405 
UPG C2     C  N N 406 
UPG N3     N  N N 407 
UPG C4     C  N N 408 
UPG C5     C  N N 409 
UPG C6     C  N N 410 
UPG O2     O  N N 411 
UPG O4     O  N N 412 
UPG C1C    C  N R 413 
UPG C2C    C  N R 414 
UPG O2C    O  N N 415 
UPG C3C    C  N S 416 
UPG C4C    C  N R 417 
UPG O4C    O  N N 418 
UPG O3C    O  N N 419 
UPG C5C    C  N N 420 
UPG O5C    O  N N 421 
UPG PA     P  N N 422 
UPG O1A    O  N N 423 
UPG O2A    O  N N 424 
UPG O3A    O  N N 425 
UPG PB     P  N N 426 
UPG O1B    O  N N 427 
UPG O2B    O  N N 428 
UPG O3B    O  N N 429 
UPG "C1'"  C  N R 430 
UPG "C2'"  C  N R 431 
UPG "C3'"  C  N S 432 
UPG "C4'"  C  N S 433 
UPG "C5'"  C  N R 434 
UPG "C6'"  C  N N 435 
UPG "O2'"  O  N N 436 
UPG "O3'"  O  N N 437 
UPG "O4'"  O  N N 438 
UPG "O5'"  O  N N 439 
UPG "O6'"  O  N N 440 
UPG HN3    H  N N 441 
UPG H5     H  N N 442 
UPG H6     H  N N 443 
UPG H1C    H  N N 444 
UPG H2C    H  N N 445 
UPG HO2C   H  N N 446 
UPG H3C    H  N N 447 
UPG H4C    H  N N 448 
UPG HO3C   H  N N 449 
UPG H5C1   H  N N 450 
UPG H5C2   H  N N 451 
UPG HOA2   H  N N 452 
UPG HOB2   H  N N 453 
UPG "H1'"  H  N N 454 
UPG "H2'"  H  N N 455 
UPG "H3'"  H  N N 456 
UPG "H4'"  H  N N 457 
UPG "H5'"  H  N N 458 
UPG "H6'1" H  N N 459 
UPG "H6'2" H  N N 460 
UPG "HO2'" H  N N 461 
UPG "HO3'" H  N N 462 
UPG "HO4'" H  N N 463 
UPG "HO6'" H  N N 464 
VAL N      N  N N 465 
VAL CA     C  N S 466 
VAL C      C  N N 467 
VAL O      O  N N 468 
VAL CB     C  N N 469 
VAL CG1    C  N N 470 
VAL CG2    C  N N 471 
VAL OXT    O  N N 472 
VAL H      H  N N 473 
VAL H2     H  N N 474 
VAL HA     H  N N 475 
VAL HB     H  N N 476 
VAL HG11   H  N N 477 
VAL HG12   H  N N 478 
VAL HG13   H  N N 479 
VAL HG21   H  N N 480 
VAL HG22   H  N N 481 
VAL HG23   H  N N 482 
VAL HXT    H  N N 483 
# 
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  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
RAB "O5'" "C5'"  sing N N 277 
RAB "O5'" "H5'"  sing N N 278 
RAB "C5'" "C4'"  sing N N 279 
RAB "C5'" "H5'1" sing N N 280 
RAB "C5'" "H5'2" sing N N 281 
RAB "C4'" "O4'"  sing N N 282 
RAB "C4'" "C3'"  sing N N 283 
RAB "C4'" "H4'"  sing N N 284 
RAB "O4'" "C1'"  sing N N 285 
RAB "C1'" N9     sing N N 286 
RAB "C1'" "C2'"  sing N N 287 
RAB "C1'" "H1'"  sing N N 288 
RAB N9    C4     sing Y N 289 
RAB N9    C8     sing Y N 290 
RAB C4    N3     doub Y N 291 
RAB C4    C5     sing Y N 292 
RAB N3    C2     sing Y N 293 
RAB C2    N1     doub Y N 294 
RAB C2    H2     sing N N 295 
RAB N1    C6     sing Y N 296 
RAB C6    N6     sing N N 297 
RAB C6    C5     doub Y N 298 
RAB N6    HN61   sing N N 299 
RAB N6    HN62   sing N N 300 
RAB C5    N7     sing Y N 301 
RAB N7    C8     doub Y N 302 
RAB C8    H8     sing N N 303 
RAB "C2'" "O2'"  sing N N 304 
RAB "C2'" "C3'"  sing N N 305 
RAB "C2'" "H2'"  sing N N 306 
RAB "O2'" H1     sing N N 307 
RAB "C3'" "O3'"  sing N N 308 
RAB "C3'" "H3'"  sing N N 309 
RAB "O3'" H3     sing N N 310 
SER N     CA     sing N N 311 
SER N     H      sing N N 312 
SER N     H2     sing N N 313 
SER CA    C      sing N N 314 
SER CA    CB     sing N N 315 
SER CA    HA     sing N N 316 
SER C     O      doub N N 317 
SER C     OXT    sing N N 318 
SER CB    OG     sing N N 319 
SER CB    HB2    sing N N 320 
SER CB    HB3    sing N N 321 
SER OG    HG     sing N N 322 
SER OXT   HXT    sing N N 323 
THR N     CA     sing N N 324 
THR N     H      sing N N 325 
THR N     H2     sing N N 326 
THR CA    C      sing N N 327 
THR CA    CB     sing N N 328 
THR CA    HA     sing N N 329 
THR C     O      doub N N 330 
THR C     OXT    sing N N 331 
THR CB    OG1    sing N N 332 
THR CB    CG2    sing N N 333 
THR CB    HB     sing N N 334 
THR OG1   HG1    sing N N 335 
THR CG2   HG21   sing N N 336 
THR CG2   HG22   sing N N 337 
THR CG2   HG23   sing N N 338 
THR OXT   HXT    sing N N 339 
TRP N     CA     sing N N 340 
TRP N     H      sing N N 341 
TRP N     H2     sing N N 342 
TRP CA    C      sing N N 343 
TRP CA    CB     sing N N 344 
TRP CA    HA     sing N N 345 
TRP C     O      doub N N 346 
TRP C     OXT    sing N N 347 
TRP CB    CG     sing N N 348 
TRP CB    HB2    sing N N 349 
TRP CB    HB3    sing N N 350 
TRP CG    CD1    doub Y N 351 
TRP CG    CD2    sing Y N 352 
TRP CD1   NE1    sing Y N 353 
TRP CD1   HD1    sing N N 354 
TRP CD2   CE2    doub Y N 355 
TRP CD2   CE3    sing Y N 356 
TRP NE1   CE2    sing Y N 357 
TRP NE1   HE1    sing N N 358 
TRP CE2   CZ2    sing Y N 359 
TRP CE3   CZ3    doub Y N 360 
TRP CE3   HE3    sing N N 361 
TRP CZ2   CH2    doub Y N 362 
TRP CZ2   HZ2    sing N N 363 
TRP CZ3   CH2    sing Y N 364 
TRP CZ3   HZ3    sing N N 365 
TRP CH2   HH2    sing N N 366 
TRP OXT   HXT    sing N N 367 
TYR N     CA     sing N N 368 
TYR N     H      sing N N 369 
TYR N     H2     sing N N 370 
TYR CA    C      sing N N 371 
TYR CA    CB     sing N N 372 
TYR CA    HA     sing N N 373 
TYR C     O      doub N N 374 
TYR C     OXT    sing N N 375 
TYR CB    CG     sing N N 376 
TYR CB    HB2    sing N N 377 
TYR CB    HB3    sing N N 378 
TYR CG    CD1    doub Y N 379 
TYR CG    CD2    sing Y N 380 
TYR CD1   CE1    sing Y N 381 
TYR CD1   HD1    sing N N 382 
TYR CD2   CE2    doub Y N 383 
TYR CD2   HD2    sing N N 384 
TYR CE1   CZ     doub Y N 385 
TYR CE1   HE1    sing N N 386 
TYR CE2   CZ     sing Y N 387 
TYR CE2   HE2    sing N N 388 
TYR CZ    OH     sing N N 389 
TYR OH    HH     sing N N 390 
TYR OXT   HXT    sing N N 391 
UPG N1    C2     sing N N 392 
UPG N1    C6     sing N N 393 
UPG N1    C1C    sing N N 394 
UPG C2    N3     sing N N 395 
UPG C2    O2     doub N N 396 
UPG N3    C4     sing N N 397 
UPG N3    HN3    sing N N 398 
UPG C4    C5     sing N N 399 
UPG C4    O4     doub N N 400 
UPG C5    C6     doub N N 401 
UPG C5    H5     sing N N 402 
UPG C6    H6     sing N N 403 
UPG C1C   C2C    sing N N 404 
UPG C1C   O4C    sing N N 405 
UPG C1C   H1C    sing N N 406 
UPG C2C   O2C    sing N N 407 
UPG C2C   C3C    sing N N 408 
UPG C2C   H2C    sing N N 409 
UPG O2C   HO2C   sing N N 410 
UPG C3C   C4C    sing N N 411 
UPG C3C   O3C    sing N N 412 
UPG C3C   H3C    sing N N 413 
UPG C4C   O4C    sing N N 414 
UPG C4C   C5C    sing N N 415 
UPG C4C   H4C    sing N N 416 
UPG O3C   HO3C   sing N N 417 
UPG C5C   O5C    sing N N 418 
UPG C5C   H5C1   sing N N 419 
UPG C5C   H5C2   sing N N 420 
UPG O5C   PA     sing N N 421 
UPG PA    O1A    doub N N 422 
UPG PA    O2A    sing N N 423 
UPG PA    O3A    sing N N 424 
UPG O2A   HOA2   sing N N 425 
UPG O3A   PB     sing N N 426 
UPG PB    O1B    doub N N 427 
UPG PB    O2B    sing N N 428 
UPG PB    O3B    sing N N 429 
UPG O2B   HOB2   sing N N 430 
UPG O3B   "C1'"  sing N N 431 
UPG "C1'" "C2'"  sing N N 432 
UPG "C1'" "O5'"  sing N N 433 
UPG "C1'" "H1'"  sing N N 434 
UPG "C2'" "C3'"  sing N N 435 
UPG "C2'" "O2'"  sing N N 436 
UPG "C2'" "H2'"  sing N N 437 
UPG "C3'" "C4'"  sing N N 438 
UPG "C3'" "O3'"  sing N N 439 
UPG "C3'" "H3'"  sing N N 440 
UPG "C4'" "C5'"  sing N N 441 
UPG "C4'" "O4'"  sing N N 442 
UPG "C4'" "H4'"  sing N N 443 
UPG "C5'" "C6'"  sing N N 444 
UPG "C5'" "O5'"  sing N N 445 
UPG "C5'" "H5'"  sing N N 446 
UPG "C6'" "O6'"  sing N N 447 
UPG "C6'" "H6'1" sing N N 448 
UPG "C6'" "H6'2" sing N N 449 
UPG "O2'" "HO2'" sing N N 450 
UPG "O3'" "HO3'" sing N N 451 
UPG "O4'" "HO4'" sing N N 452 
UPG "O6'" "HO6'" sing N N 453 
VAL N     CA     sing N N 454 
VAL N     H      sing N N 455 
VAL N     H2     sing N N 456 
VAL CA    C      sing N N 457 
VAL CA    CB     sing N N 458 
VAL CA    HA     sing N N 459 
VAL C     O      doub N N 460 
VAL C     OXT    sing N N 461 
VAL CB    CG1    sing N N 462 
VAL CB    CG2    sing N N 463 
VAL CB    HB     sing N N 464 
VAL CG1   HG11   sing N N 465 
VAL CG1   HG12   sing N N 466 
VAL CG1   HG13   sing N N 467 
VAL CG2   HG21   sing N N 468 
VAL CG2   HG22   sing N N 469 
VAL CG2   HG23   sing N N 470 
VAL OXT   HXT    sing N N 471 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32371303 
_pdbx_audit_support.ordinal                1 
# 
_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   9JMA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JN3 
_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]   0.023094 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004538 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010514 
_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]   0.014356 
_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  
MG 
N  
O  
P  
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     . MET A 1 1   ? 16.360  16.696  25.638  1.00 45.56  ?  1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 15.310  16.571  26.659  1.00 39.84  ?  1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 14.148  15.725  26.121  1.00 35.95  ?  1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 13.860  14.657  26.640  1.00 37.66  ?  1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 14.832  17.955  27.127  1.00 48.80  ?  1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 15.454  18.383  28.449  1.00 50.93  ?  1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 14.812  19.883  29.223  1.00 80.67  ?  1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 15.227  21.194  28.043  1.00 52.42  ?  1   MET A CE    1 
ATOM   9    N  N     . LEU A 1 2   ? 13.511  16.146  25.037  1.00 38.90  ?  2   LEU A N     1 
ATOM   10   C  CA    . LEU A 1 2   ? 12.420  15.324  24.520  1.00 36.23  ?  2   LEU A CA    1 
ATOM   11   C  C     . LEU A 1 2   ? 12.938  14.160  23.690  1.00 36.17  ?  2   LEU A C     1 
ATOM   12   O  O     . LEU A 1 2   ? 12.502  13.020  23.874  1.00 35.45  ?  2   LEU A O     1 
ATOM   13   C  CB    . LEU A 1 2   ? 11.455  16.173  23.700  1.00 39.42  ?  2   LEU A CB    1 
ATOM   14   C  CG    . LEU A 1 2   ? 10.210  15.431  23.244  1.00 38.71  ?  2   LEU A CG    1 
ATOM   15   C  CD1   . LEU A 1 2   ? 9.409   14.844  24.418  1.00 34.73  ?  2   LEU A CD1   1 
ATOM   16   C  CD2   . LEU A 1 2   ? 9.330   16.338  22.414  1.00 43.54  ?  2   LEU A CD2   1 
ATOM   17   N  N     . VAL A 1 3   ? 13.875  14.413  22.774  1.00 38.87  ?  3   VAL A N     1 
ATOM   18   C  CA    . VAL A 1 3   ? 14.292  13.390  21.824  1.00 33.45  ?  3   VAL A CA    1 
ATOM   19   C  C     . VAL A 1 3   ? 15.810  13.368  21.769  1.00 35.91  ?  3   VAL A C     1 
ATOM   20   O  O     . VAL A 1 3   ? 16.443  14.426  21.761  1.00 33.85  ?  3   VAL A O     1 
ATOM   21   C  CB    . VAL A 1 3   ? 13.728  13.651  20.410  1.00 34.81  ?  3   VAL A CB    1 
ATOM   22   C  CG1   . VAL A 1 3   ? 14.493  12.804  19.353  1.00 30.74  ?  3   VAL A CG1   1 
ATOM   23   C  CG2   . VAL A 1 3   ? 12.186  13.494  20.370  1.00 41.61  ?  3   VAL A CG2   1 
ATOM   24   N  N     . SER A 1 4   ? 16.387  12.161  21.721  1.00 29.30  ?  4   SER A N     1 
ATOM   25   C  CA    . SER A 1 4   ? 17.792  11.941  21.447  1.00 28.27  ?  4   SER A CA    1 
ATOM   26   C  C     . SER A 1 4   ? 17.911  11.163  20.142  1.00 33.51  ?  4   SER A C     1 
ATOM   27   O  O     . SER A 1 4   ? 17.344  10.069  20.007  1.00 30.28  ?  4   SER A O     1 
ATOM   28   C  CB    . SER A 1 4   ? 18.470  11.187  22.594  1.00 29.47  ?  4   SER A CB    1 
ATOM   29   O  OG    . SER A 1 4   ? 18.317  11.864  23.831  1.00 32.41  ?  4   SER A OG    1 
ATOM   30   N  N     . VAL A 1 5   ? 18.629  11.733  19.175  1.00 29.26  ?  5   VAL A N     1 
ATOM   31   C  CA    . VAL A 1 5   ? 18.949  11.031  17.947  1.00 28.23  ?  5   VAL A CA    1 
ATOM   32   C  C     . VAL A 1 5   ? 20.287  10.373  18.186  1.00 32.25  ?  5   VAL A C     1 
ATOM   33   O  O     . VAL A 1 5   ? 21.200  11.008  18.715  1.00 35.16  ?  5   VAL A O     1 
ATOM   34   C  CB    . VAL A 1 5   ? 19.003  11.979  16.734  1.00 31.71  ?  5   VAL A CB    1 
ATOM   35   C  CG1   . VAL A 1 5   ? 19.404  11.210  15.475  1.00 29.70  ?  5   VAL A CG1   1 
ATOM   36   C  CG2   . VAL A 1 5   ? 17.672  12.653  16.502  1.00 30.24  ?  5   VAL A CG2   1 
ATOM   37   N  N     . ILE A 1 6   ? 20.386  9.086   17.871  1.00 31.57  ?  6   ILE A N     1 
ATOM   38   C  CA    . ILE A 1 6   ? 21.614  8.328   18.042  1.00 30.10  ?  6   ILE A CA    1 
ATOM   39   C  C     . ILE A 1 6   ? 22.083  7.880   16.662  1.00 33.24  ?  6   ILE A C     1 
ATOM   40   O  O     . ILE A 1 6   ? 21.345  7.190   15.953  1.00 31.60  ?  6   ILE A O     1 
ATOM   41   C  CB    . ILE A 1 6   ? 21.399  7.141   18.985  1.00 34.91  ?  6   ILE A CB    1 
ATOM   42   C  CG1   . ILE A 1 6   ? 20.833  7.678   20.317  1.00 30.67  ?  6   ILE A CG1   1 
ATOM   43   C  CG2   . ILE A 1 6   ? 22.717  6.337   19.156  1.00 31.10  ?  6   ILE A CG2   1 
ATOM   44   C  CD1   . ILE A 1 6   ? 20.729  6.651   21.401  1.00 30.69  ?  6   ILE A CD1   1 
ATOM   45   N  N     . ILE A 1 7   ? 23.282  8.305   16.273  1.00 35.06  ?  7   ILE A N     1 
ATOM   46   C  CA    . ILE A 1 7   ? 23.871  7.993   14.973  1.00 34.63  ?  7   ILE A CA    1 
ATOM   47   C  C     . ILE A 1 7   ? 25.197  7.277   15.185  1.00 34.82  ?  7   ILE A C     1 
ATOM   48   O  O     . ILE A 1 7   ? 26.240  7.919   15.369  1.00 34.11  ?  7   ILE A O     1 
ATOM   49   C  CB    . ILE A 1 7   ? 24.069  9.254   14.115  1.00 36.70  ?  7   ILE A CB    1 
ATOM   50   C  CG1   . ILE A 1 7   ? 22.786  10.089  14.066  1.00 31.61  ?  7   ILE A CG1   1 
ATOM   51   C  CG2   . ILE A 1 7   ? 24.561  8.872   12.696  1.00 28.38  ?  7   ILE A CG2   1 
ATOM   52   C  CD1   . ILE A 1 7   ? 23.037  11.444  13.483  1.00 34.46  ?  7   ILE A CD1   1 
ATOM   53   N  N     . PRO A 1 8   ? 25.210  5.945   15.132  1.00 31.36  ?  8   PRO A N     1 
ATOM   54   C  CA    . PRO A 1 8   ? 26.480  5.210   15.031  1.00 34.24  ?  8   PRO A CA    1 
ATOM   55   C  C     . PRO A 1 8   ? 27.145  5.442   13.673  1.00 34.72  ?  8   PRO A C     1 
ATOM   56   O  O     . PRO A 1 8   ? 26.483  5.407   12.635  1.00 34.35  ?  8   PRO A O     1 
ATOM   57   C  CB    . PRO A 1 8   ? 26.042  3.745   15.185  1.00 34.25  ?  8   PRO A CB    1 
ATOM   58   C  CG    . PRO A 1 8   ? 24.669  3.716   14.532  1.00 29.96  ?  8   PRO A CG    1 
ATOM   59   C  CD    . PRO A 1 8   ? 24.047  5.084   14.847  1.00 29.73  ?  8   PRO A CD    1 
ATOM   60   N  N     . THR A 1 9   ? 28.466  5.680   13.668  1.00 36.91  ?  9   THR A N     1 
ATOM   61   C  CA    . THR A 1 9   ? 29.137  6.014   12.414  1.00 33.86  ?  9   THR A CA    1 
ATOM   62   C  C     . THR A 1 9   ? 30.493  5.335   12.306  1.00 41.52  ?  9   THR A C     1 
ATOM   63   O  O     . THR A 1 9   ? 31.177  5.108   13.312  1.00 45.72  ?  9   THR A O     1 
ATOM   64   C  CB    . THR A 1 9   ? 29.298  7.527   12.240  1.00 36.43  ?  9   THR A CB    1 
ATOM   65   O  OG1   . THR A 1 9   ? 29.511  7.814   10.849  1.00 36.28  ?  9   THR A OG1   1 
ATOM   66   C  CG2   . THR A 1 9   ? 30.445  8.054   13.082  1.00 33.42  ?  9   THR A CG2   1 
ATOM   67   N  N     . TYR A 1 10  ? 30.897  5.033   11.063  1.00 39.22  ?  10  TYR A N     1 
ATOM   68   C  CA    . TYR A 1 10  ? 32.132  4.271   10.851  1.00 42.00  ?  10  TYR A CA    1 
ATOM   69   C  C     . TYR A 1 10  ? 32.659  4.458   9.421   1.00 40.73  ?  10  TYR A C     1 
ATOM   70   O  O     . TYR A 1 10  ? 32.119  3.869   8.483   1.00 35.15  ?  10  TYR A O     1 
ATOM   71   C  CB    . TYR A 1 10  ? 31.892  2.804   11.166  1.00 42.77  ?  10  TYR A CB    1 
ATOM   72   C  CG    . TYR A 1 10  ? 33.135  1.983   11.054  1.00 44.02  ?  10  TYR A CG    1 
ATOM   73   C  CD1   . TYR A 1 10  ? 34.121  2.065   12.030  1.00 41.79  ?  10  TYR A CD1   1 
ATOM   74   C  CD2   . TYR A 1 10  ? 33.303  1.078   10.015  1.00 47.70  ?  10  TYR A CD2   1 
ATOM   75   C  CE1   . TYR A 1 10  ? 35.279  1.312   11.951  1.00 44.32  ?  10  TYR A CE1   1 
ATOM   76   C  CE2   . TYR A 1 10  ? 34.453  0.290   9.934   1.00 48.82  ?  10  TYR A CE2   1 
ATOM   77   C  CZ    . TYR A 1 10  ? 35.440  0.419   10.901  1.00 51.16  ?  10  TYR A CZ    1 
ATOM   78   O  OH    . TYR A 1 10  ? 36.586  -0.353  10.832  1.00 50.78  ?  10  TYR A OH    1 
ATOM   79   N  N     . ASN A 1 11  ? 33.714  5.271   9.278   1.00 40.38  ?  11  ASN A N     1 
ATOM   80   C  CA    . ASN A 1 11  ? 34.414  5.489   7.998   1.00 36.84  ?  11  ASN A CA    1 
ATOM   81   C  C     . ASN A 1 11  ? 33.483  5.969   6.903   1.00 38.21  ?  11  ASN A C     1 
ATOM   82   O  O     . ASN A 1 11  ? 33.650  5.597   5.749   1.00 41.17  ?  11  ASN A O     1 
ATOM   83   C  CB    . ASN A 1 11  ? 35.129  4.227   7.513   1.00 33.49  ?  11  ASN A CB    1 
ATOM   84   C  CG    . ASN A 1 11  ? 36.216  3.774   8.460   1.00 38.05  ?  11  ASN A CG    1 
ATOM   85   O  OD1   . ASN A 1 11  ? 36.542  4.456   9.415   1.00 42.07  ?  11  ASN A OD1   1 
ATOM   86   N  ND2   . ASN A 1 11  ? 36.758  2.602   8.215   1.00 42.27  ?  11  ASN A ND2   1 
ATOM   87   N  N     . ARG A 1 12  ? 32.449  6.730   7.248   1.00 40.34  ?  12  ARG A N     1 
ATOM   88   C  CA    . ARG A 1 12  ? 31.573  7.329   6.243   1.00 39.12  ?  12  ARG A CA    1 
ATOM   89   C  C     . ARG A 1 12  ? 31.344  8.807   6.529   1.00 35.53  ?  12  ARG A C     1 
ATOM   90   O  O     . ARG A 1 12  ? 30.218  9.286   6.464   1.00 37.93  ?  12  ARG A O     1 
ATOM   91   C  CB    . ARG A 1 12  ? 30.239  6.606   6.185   1.00 44.32  ?  12  ARG A CB    1 
ATOM   92   C  CG    . ARG A 1 12  ? 30.221  5.266   5.515   1.00 44.08  ?  12  ARG A CG    1 
ATOM   93   C  CD    . ARG A 1 12  ? 28.866  4.607   5.865   1.00 47.50  ?  12  ARG A CD    1 
ATOM   94   N  NE    . ARG A 1 12  ? 28.794  3.168   5.622   1.00 46.24  ?  12  ARG A NE    1 
ATOM   95   C  CZ    . ARG A 1 12  ? 27.787  2.396   6.016   1.00 45.72  ?  12  ARG A CZ    1 
ATOM   96   N  NH1   . ARG A 1 12  ? 26.783  2.882   6.733   1.00 41.60  ?  12  ARG A NH1   1 
ATOM   97   N  NH2   . ARG A 1 12  ? 27.796  1.105   5.698   1.00 40.78  ?  12  ARG A NH2   1 
ATOM   98   N  N     . PRO A 1 13  ? 32.409  9.578   6.746   1.00 40.37  ?  13  PRO A N     1 
ATOM   99   C  CA    . PRO A 1 13  ? 32.237  10.985  7.147   1.00 37.77  ?  13  PRO A CA    1 
ATOM   100  C  C     . PRO A 1 13  ? 31.253  11.757  6.291   1.00 41.30  ?  13  PRO A C     1 
ATOM   101  O  O     . PRO A 1 13  ? 30.620  12.711  6.767   1.00 38.86  ?  13  PRO A O     1 
ATOM   102  C  CB    . PRO A 1 13  ? 33.654  11.553  6.978   1.00 41.69  ?  13  PRO A CB    1 
ATOM   103  C  CG    . PRO A 1 13  ? 34.247  10.701  5.869   1.00 38.80  ?  13  PRO A CG    1 
ATOM   104  C  CD    . PRO A 1 13  ? 33.754  9.329   6.174   1.00 38.26  ?  13  PRO A CD    1 
ATOM   105  N  N     . GLU A 1 14  ? 31.122  11.377  5.023   1.00 41.36  ?  14  GLU A N     1 
ATOM   106  C  CA    . GLU A 1 14  ? 30.358  12.129  4.041   1.00 39.27  ?  14  GLU A CA    1 
ATOM   107  C  C     . GLU A 1 14  ? 28.896  11.699  3.999   1.00 41.87  ?  14  GLU A C     1 
ATOM   108  O  O     . GLU A 1 14  ? 28.006  12.536  3.803   1.00 43.21  ?  14  GLU A O     1 
ATOM   109  C  CB    . GLU A 1 14  ? 31.046  11.982  2.675   1.00 48.90  ?  14  GLU A CB    1 
ATOM   110  C  CG    . GLU A 1 14  ? 30.896  10.581  2.058   1.00 52.92  ?  14  GLU A CG    1 
ATOM   111  C  CD    . GLU A 1 14  ? 31.708  9.509   2.808   1.00 51.11  ?  14  GLU A CD    1 
ATOM   112  O  OE1   . GLU A 1 14  ? 32.869  9.799   3.196   1.00 59.26  ?  14  GLU A OE1   1 
ATOM   113  O  OE2   . GLU A 1 14  ? 31.183  8.387   3.006   1.00 53.71  ?  14  GLU A OE2   1 
ATOM   114  N  N     . ARG A 1 15  ? 28.612  10.422  4.206   1.00 43.55  ?  15  ARG A N     1 
ATOM   115  C  CA    . ARG A 1 15  ? 27.231  10.040  4.440   1.00 41.53  ?  15  ARG A CA    1 
ATOM   116  C  C     . ARG A 1 15  ? 26.741  10.586  5.777   1.00 38.32  ?  15  ARG A C     1 
ATOM   117  O  O     . ARG A 1 15  ? 25.633  11.121  5.866   1.00 39.98  ?  15  ARG A O     1 
ATOM   118  C  CB    . ARG A 1 15  ? 27.120  8.525   4.327   1.00 45.85  ?  15  ARG A CB    1 
ATOM   119  C  CG    . ARG A 1 15  ? 27.282  8.125   2.869   1.00 43.03  ?  15  ARG A CG    1 
ATOM   120  C  CD    . ARG A 1 15  ? 28.338  7.074   2.670   1.00 55.05  ?  15  ARG A CD    1 
ATOM   121  N  NE    . ARG A 1 15  ? 27.794  5.737   2.868   1.00 58.30  ?  15  ARG A NE    1 
ATOM   122  C  CZ    . ARG A 1 15  ? 27.069  5.083   1.966   1.00 67.55  ?  15  ARG A CZ    1 
ATOM   123  N  NH1   . ARG A 1 15  ? 26.826  5.603   0.761   1.00 63.77  ?  15  ARG A NH1   1 
ATOM   124  N  NH2   . ARG A 1 15  ? 26.550  3.892   2.288   1.00 63.99  ?  15  ARG A NH2   1 
ATOM   125  N  N     . LEU A 1 16  ? 27.590  10.550  6.808   1.00 37.20  ?  16  LEU A N     1 
ATOM   126  C  CA    . LEU A 1 16  ? 27.207  11.110  8.097   1.00 32.74  ?  16  LEU A CA    1 
ATOM   127  C  C     . LEU A 1 16  ? 26.807  12.571  7.975   1.00 38.89  ?  16  LEU A C     1 
ATOM   128  O  O     . LEU A 1 16  ? 25.920  13.035  8.712   1.00 41.29  ?  16  LEU A O     1 
ATOM   129  C  CB    . LEU A 1 16  ? 28.349  10.950  9.095   1.00 37.46  ?  16  LEU A CB    1 
ATOM   130  C  CG    . LEU A 1 16  ? 28.258  11.784  10.379  1.00 41.96  ?  16  LEU A CG    1 
ATOM   131  C  CD1   . LEU A 1 16  ? 27.081  11.315  11.276  1.00 31.55  ?  16  LEU A CD1   1 
ATOM   132  C  CD2   . LEU A 1 16  ? 29.598  11.836  11.154  1.00 33.24  ?  16  LEU A CD2   1 
ATOM   133  N  N     . ALA A 1 17  ? 27.437  13.315  7.057   1.00 38.12  ?  17  ALA A N     1 
ATOM   134  C  CA    . ALA A 1 17  ? 27.042  14.705  6.840   1.00 35.61  ?  17  ALA A CA    1 
ATOM   135  C  C     . ALA A 1 17  ? 25.607  14.804  6.329   1.00 35.19  ?  17  ALA A C     1 
ATOM   136  O  O     . ALA A 1 17  ? 24.872  15.724  6.691   1.00 33.87  ?  17  ALA A O     1 
ATOM   137  C  CB    . ALA A 1 17  ? 27.990  15.369  5.851   1.00 32.62  ?  17  ALA A CB    1 
ATOM   138  N  N     . VAL A 1 18  ? 25.214  13.889  5.445   1.00 37.10  ?  18  VAL A N     1 
ATOM   139  C  CA    . VAL A 1 18  ? 23.857  13.863  4.912   1.00 37.87  ?  18  VAL A CA    1 
ATOM   140  C  C     . VAL A 1 18  ? 22.847  13.533  6.017   1.00 38.62  ?  18  VAL A C     1 
ATOM   141  O  O     . VAL A 1 18  ? 21.802  14.191  6.139   1.00 31.14  ?  18  VAL A O     1 
ATOM   142  C  CB    . VAL A 1 18  ? 23.796  12.858  3.743   1.00 40.62  ?  18  VAL A CB    1 
ATOM   143  C  CG1   . VAL A 1 18  ? 22.448  12.862  3.050   1.00 38.80  ?  18  VAL A CG1   1 
ATOM   144  C  CG2   . VAL A 1 18  ? 24.893  13.167  2.733   1.00 37.97  ?  18  VAL A CG2   1 
ATOM   145  N  N     . ALA A 1 19  ? 23.157  12.528  6.854   1.00 40.23  ?  19  ALA A N     1 
ATOM   146  C  CA    . ALA A 1 19  ? 22.255  12.153  7.945   1.00 35.08  ?  19  ALA A CA    1 
ATOM   147  C  C     . ALA A 1 19  ? 22.067  13.303  8.934   1.00 37.47  ?  19  ALA A C     1 
ATOM   148  O  O     . ALA A 1 19  ? 20.936  13.586  9.374   1.00 36.74  ?  19  ALA A O     1 
ATOM   149  C  CB    . ALA A 1 19  ? 22.790  10.910  8.656   1.00 36.25  ?  19  ALA A CB    1 
ATOM   150  N  N     . LEU A 1 20  ? 23.158  13.988  9.294   1.00 36.08  ?  20  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 20  ? 23.026  15.088  10.246  1.00 35.09  ?  20  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 20  ? 22.158  16.190  9.664   1.00 38.17  ?  20  LEU A C     1 
ATOM   153  O  O     . LEU A 1 20  ? 21.196  16.648  10.305  1.00 38.15  ?  20  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 20  ? 24.396  15.618  10.654  1.00 28.63  ?  20  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 20  ? 25.025  14.779  11.777  1.00 38.53  ?  20  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 20  ? 26.546  14.932  11.889  1.00 38.29  ?  20  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 20  ? 24.391  15.051  13.110  1.00 31.39  ?  20  LEU A CD2   1 
ATOM   158  N  N     . GLN A 1 21  ? 22.438  16.573  8.414   1.00 37.58  ?  21  GLN A N     1 
ATOM   159  C  CA    . GLN A 1 21  ? 21.648  17.613  7.757   1.00 40.22  ?  21  GLN A CA    1 
ATOM   160  C  C     . GLN A 1 21  ? 20.176  17.233  7.706   1.00 36.59  ?  21  GLN A C     1 
ATOM   161  O  O     . GLN A 1 21  ? 19.310  18.101  7.765   1.00 37.45  ?  21  GLN A O     1 
ATOM   162  C  CB    . GLN A 1 21  ? 22.204  17.861  6.355   1.00 38.20  ?  21  GLN A CB    1 
ATOM   163  C  CG    . GLN A 1 21  ? 21.435  18.858  5.545   1.00 45.91  ?  21  GLN A CG    1 
ATOM   164  C  CD    . GLN A 1 21  ? 21.585  20.259  6.068   1.00 45.68  ?  21  GLN A CD    1 
ATOM   165  O  OE1   . GLN A 1 21  ? 22.524  20.563  6.788   1.00 50.78  ?  21  GLN A OE1   1 
ATOM   166  N  NE2   . GLN A 1 21  ? 20.660  21.124  5.703   1.00 50.50  ?  21  GLN A NE2   1 
ATOM   167  N  N     . SER A 1 22  ? 19.878  15.935  7.613   1.00 35.45  ?  22  SER A N     1 
ATOM   168  C  CA    . SER A 1 22  ? 18.497  15.488  7.670   1.00 36.72  ?  22  SER A CA    1 
ATOM   169  C  C     . SER A 1 22  ? 17.910  15.593  9.084   1.00 36.96  ?  22  SER A C     1 
ATOM   170  O  O     . SER A 1 22  ? 16.682  15.603  9.233   1.00 33.76  ?  22  SER A O     1 
ATOM   171  C  CB    . SER A 1 22  ? 18.400  14.056  7.140   1.00 32.23  ?  22  SER A CB    1 
ATOM   172  O  OG    . SER A 1 22  ? 18.500  13.139  8.204   1.00 32.78  ?  22  SER A OG    1 
ATOM   173  N  N     . VAL A 1 23  ? 18.747  15.668  10.122  1.00 34.57  ?  23  VAL A N     1 
ATOM   174  C  CA    . VAL A 1 23  ? 18.228  16.020  11.439  1.00 31.89  ?  23  VAL A CA    1 
ATOM   175  C  C     . VAL A 1 23  ? 17.950  17.512  11.505  1.00 37.49  ?  23  VAL A C     1 
ATOM   176  O  O     . VAL A 1 23  ? 16.948  17.945  12.090  1.00 35.02  ?  23  VAL A O     1 
ATOM   177  C  CB    . VAL A 1 23  ? 19.208  15.573  12.545  1.00 33.49  ?  23  VAL A CB    1 
ATOM   178  C  CG1   . VAL A 1 23  ? 18.693  15.940  13.918  1.00 30.83  ?  23  VAL A CG1   1 
ATOM   179  C  CG2   . VAL A 1 23  ? 19.499  14.071  12.464  1.00 30.96  ?  23  VAL A CG2   1 
ATOM   180  N  N     . GLN A 1 24  ? 18.831  18.317  10.888  1.00 40.88  ?  24  GLN A N     1 
ATOM   181  C  CA    . GLN A 1 24  ? 18.725  19.775  10.917  1.00 39.67  ?  24  GLN A CA    1 
ATOM   182  C  C     . GLN A 1 24  ? 17.528  20.289  10.142  1.00 41.05  ?  24  GLN A C     1 
ATOM   183  O  O     . GLN A 1 24  ? 17.078  21.408  10.400  1.00 46.47  ?  24  GLN A O     1 
ATOM   184  C  CB    . GLN A 1 24  ? 19.988  20.418  10.342  1.00 40.72  ?  24  GLN A CB    1 
ATOM   185  C  CG    . GLN A 1 24  ? 20.809  21.166  11.378  1.00 47.35  ?  24  GLN A CG    1 
ATOM   186  C  CD    . GLN A 1 24  ? 22.234  21.220  10.963  1.00 45.57  ?  24  GLN A CD    1 
ATOM   187  O  OE1   . GLN A 1 24  ? 22.577  20.701  9.917   1.00 53.67  ?  24  GLN A OE1   1 
ATOM   188  N  NE2   . GLN A 1 24  ? 23.086  21.795  11.785  1.00 52.99  ?  24  GLN A NE2   1 
ATOM   189  N  N     . THR A 1 25  ? 17.022  19.521  9.179   1.00 35.25  ?  25  THR A N     1 
ATOM   190  C  CA    . THR A 1 25  ? 15.807  19.889  8.478   1.00 38.03  ?  25  THR A CA    1 
ATOM   191  C  C     . THR A 1 25  ? 14.570  19.224  9.086   1.00 42.80  ?  25  THR A C     1 
ATOM   192  O  O     . THR A 1 25  ? 13.518  19.148  8.437   1.00 39.29  ?  25  THR A O     1 
ATOM   193  C  CB    . THR A 1 25  ? 15.946  19.568  6.988   1.00 43.64  ?  25  THR A CB    1 
ATOM   194  O  OG1   . THR A 1 25  ? 16.092  18.156  6.801   1.00 51.98  ?  25  THR A OG1   1 
ATOM   195  C  CG2   . THR A 1 25  ? 17.166  20.281  6.398   1.00 45.28  ?  25  THR A CG2   1 
ATOM   196  N  N     . LEU A 1 26  ? 14.676  18.725  10.312  1.00 38.17  ?  26  LEU A N     1 
ATOM   197  C  CA    . LEU A 1 26  ? 13.488  18.212  10.951  1.00 40.04  ?  26  LEU A CA    1 
ATOM   198  C  C     . LEU A 1 26  ? 12.554  19.374  11.214  1.00 43.99  ?  26  LEU A C     1 
ATOM   199  O  O     . LEU A 1 26  ? 12.993  20.474  11.563  1.00 48.57  ?  26  LEU A O     1 
ATOM   200  C  CB    . LEU A 1 26  ? 13.830  17.493  12.250  1.00 38.93  ?  26  LEU A CB    1 
ATOM   201  C  CG    . LEU A 1 26  ? 14.389  16.082  12.097  1.00 36.99  ?  26  LEU A CG    1 
ATOM   202  C  CD1   . LEU A 1 26  ? 14.704  15.567  13.463  1.00 37.94  ?  26  LEU A CD1   1 
ATOM   203  C  CD2   . LEU A 1 26  ? 13.422  15.203  11.338  1.00 29.67  ?  26  LEU A CD2   1 
ATOM   204  N  N     . ASP A 1 27  ? 11.271  19.138  10.985  1.00 40.17  ?  27  ASP A N     1 
ATOM   205  C  CA    . ASP A 1 27  ? 10.212  20.047  11.406  1.00 46.17  ?  27  ASP A CA    1 
ATOM   206  C  C     . ASP A 1 27  ? 9.985   19.803  12.902  1.00 51.64  ?  27  ASP A C     1 
ATOM   207  O  O     . ASP A 1 27  ? 9.086   19.067  13.324  1.00 48.44  ?  27  ASP A O     1 
ATOM   208  C  CB    . ASP A 1 27  ? 8.968   19.791  10.556  1.00 51.49  ?  27  ASP A CB    1 
ATOM   209  C  CG    . ASP A 1 27  ? 7.779   20.644  10.943  1.00 53.68  ?  27  ASP A CG    1 
ATOM   210  O  OD1   . ASP A 1 27  ? 7.967   21.821  11.319  1.00 58.56  ?  27  ASP A OD1   1 
ATOM   211  O  OD2   . ASP A 1 27  ? 6.643   20.124  10.835  1.00 61.19  ?  27  ASP A OD2   1 
ATOM   212  N  N     . PHE A 1 28  ? 10.852  20.400  13.720  1.00 50.66  ?  28  PHE A N     1 
ATOM   213  C  CA    . PHE A 1 28  ? 10.845  20.127  15.157  1.00 47.75  ?  28  PHE A CA    1 
ATOM   214  C  C     . PHE A 1 28  ? 11.583  21.252  15.881  1.00 43.34  ?  28  PHE A C     1 
ATOM   215  O  O     . PHE A 1 28  ? 12.405  21.949  15.295  1.00 48.21  ?  28  PHE A O     1 
ATOM   216  C  CB    . PHE A 1 28  ? 11.479  18.759  15.455  1.00 41.78  ?  28  PHE A CB    1 
ATOM   217  C  CG    . PHE A 1 28  ? 11.347  18.310  16.900  1.00 45.36  ?  28  PHE A CG    1 
ATOM   218  C  CD1   . PHE A 1 28  ? 10.155  17.778  17.374  1.00 40.43  ?  28  PHE A CD1   1 
ATOM   219  C  CD2   . PHE A 1 28  ? 12.425  18.402  17.775  1.00 42.11  ?  28  PHE A CD2   1 
ATOM   220  C  CE1   . PHE A 1 28  ? 10.044  17.380  18.695  1.00 43.15  ?  28  PHE A CE1   1 
ATOM   221  C  CE2   . PHE A 1 28  ? 12.324  17.999  19.099  1.00 44.22  ?  28  PHE A CE2   1 
ATOM   222  C  CZ    . PHE A 1 28  ? 11.133  17.493  19.565  1.00 44.76  ?  28  PHE A CZ    1 
ATOM   223  N  N     . ASP A 1 29  ? 11.172  21.530  17.115  1.00 51.02  ?  29  ASP A N     1 
ATOM   224  C  CA    . ASP A 1 29  ? 11.813  22.539  17.998  1.00 50.51  ?  29  ASP A CA    1 
ATOM   225  C  C     . ASP A 1 29  ? 13.126  21.945  18.491  1.00 52.02  ?  29  ASP A C     1 
ATOM   226  O  O     . ASP A 1 29  ? 13.091  21.116  19.379  1.00 52.97  ?  29  ASP A O     1 
ATOM   227  C  CB    . ASP A 1 29  ? 10.918  22.881  19.183  1.00 48.48  ?  29  ASP A CB    1 
ATOM   228  C  CG    . ASP A 1 29  ? 11.409  24.053  20.012  1.00 66.82  ?  29  ASP A CG    1 
ATOM   229  O  OD1   . ASP A 1 29  ? 12.468  24.621  19.673  1.00 64.31  ?  29  ASP A OD1   1 
ATOM   230  O  OD2   . ASP A 1 29  ? 10.714  24.399  20.976  1.00 65.49  ?  29  ASP A OD2   1 
ATOM   231  N  N     . SER A 1 30  ? 14.246  22.464  18.006  1.00 47.82  ?  30  SER A N     1 
ATOM   232  C  CA    . SER A 1 30  ? 15.589  21.900  18.277  1.00 47.13  ?  30  SER A CA    1 
ATOM   233  C  C     . SER A 1 30  ? 16.075  22.047  19.728  1.00 49.16  ?  30  SER A C     1 
ATOM   234  O  O     . SER A 1 30  ? 17.075  21.424  20.049  1.00 52.72  ?  30  SER A O     1 
ATOM   235  C  CB    . SER A 1 30  ? 16.579  22.370  17.245  1.00 54.39  ?  30  SER A CB    1 
ATOM   236  O  OG    . SER A 1 30  ? 17.393  23.415  17.738  1.00 63.22  ?  30  SER A OG    1 
ATOM   237  N  N     . GLU A 1 31  ? 15.408  22.844  20.560  1.00 49.41  ?  31  GLU A N     1 
ATOM   238  C  CA    . GLU A 1 31  ? 15.754  22.989  21.992  1.00 53.68  ?  31  GLU A CA    1 
ATOM   239  C  C     . GLU A 1 31  ? 15.320  21.728  22.747  1.00 48.59  ?  31  GLU A C     1 
ATOM   240  O  O     . GLU A 1 31  ? 15.820  21.522  23.849  1.00 50.37  ?  31  GLU A O     1 
ATOM   241  C  CB    . GLU A 1 31  ? 15.071  24.227  22.568  1.00 56.72  ?  31  GLU A CB    1 
ATOM   242  N  N     . GLN A 1 32  ? 14.422  20.930  22.169  1.00 41.82  ?  32  GLN A N     1 
ATOM   243  C  CA    . GLN A 1 32  ? 13.969  19.709  22.808  1.00 42.60  ?  32  GLN A CA    1 
ATOM   244  C  C     . GLN A 1 32  ? 14.762  18.485  22.379  1.00 44.17  ?  32  GLN A C     1 
ATOM   245  O  O     . GLN A 1 32  ? 14.486  17.382  22.864  1.00 44.20  ?  32  GLN A O     1 
ATOM   246  C  CB    . GLN A 1 32  ? 12.501  19.489  22.489  1.00 48.10  ?  32  GLN A CB    1 
ATOM   247  C  CG    . GLN A 1 32  ? 11.644  20.649  22.876  1.00 50.31  ?  32  GLN A CG    1 
ATOM   248  C  CD    . GLN A 1 32  ? 10.505  20.221  23.766  1.00 57.79  ?  32  GLN A CD    1 
ATOM   249  O  OE1   . GLN A 1 32  ? 9.366   20.104  23.304  1.00 58.04  ?  32  GLN A OE1   1 
ATOM   250  N  NE2   . GLN A 1 32  ? 10.799  19.984  25.057  1.00 56.40  ?  32  GLN A NE2   1 
ATOM   251  N  N     . LEU A 1 33  ? 15.740  18.659  21.500  1.00 40.02  ?  33  LEU A N     1 
ATOM   252  C  CA    . LEU A 1 33  ? 16.375  17.570  20.793  1.00 38.67  ?  33  LEU A CA    1 
ATOM   253  C  C     . LEU A 1 33  ? 17.878  17.588  21.011  1.00 40.31  ?  33  LEU A C     1 
ATOM   254  O  O     . LEU A 1 33  ? 18.501  18.659  21.020  1.00 38.72  ?  33  LEU A O     1 
ATOM   255  C  CB    . LEU A 1 33  ? 16.059  17.687  19.307  1.00 42.13  ?  33  LEU A CB    1 
ATOM   256  C  CG    . LEU A 1 33  ? 16.709  16.656  18.415  1.00 39.28  ?  33  LEU A CG    1 
ATOM   257  C  CD1   . LEU A 1 33  ? 15.652  15.951  17.649  1.00 38.41  ?  33  LEU A CD1   1 
ATOM   258  C  CD2   . LEU A 1 33  ? 17.570  17.362  17.460  1.00 38.50  ?  33  LEU A CD2   1 
ATOM   259  N  N     . GLU A 1 34  ? 18.463  16.398  21.175  1.00 35.37  ?  34  GLU A N     1 
ATOM   260  C  CA    . GLU A 1 34  ? 19.907  16.256  21.134  1.00 35.70  ?  34  GLU A CA    1 
ATOM   261  C  C     . GLU A 1 34  ? 20.290  15.202  20.112  1.00 43.02  ?  34  GLU A C     1 
ATOM   262  O  O     . GLU A 1 34  ? 19.518  14.287  19.811  1.00 41.20  ?  34  GLU A O     1 
ATOM   263  C  CB    . GLU A 1 34  ? 20.507  15.891  22.492  1.00 33.90  ?  34  GLU A CB    1 
ATOM   264  C  CG    . GLU A 1 34  ? 20.089  14.556  23.046  1.00 35.29  ?  34  GLU A CG    1 
ATOM   265  C  CD    . GLU A 1 34  ? 20.802  14.250  24.367  1.00 37.53  ?  34  GLU A CD    1 
ATOM   266  O  OE1   . GLU A 1 34  ? 21.556  15.126  24.832  1.00 45.46  ?  34  GLU A OE1   1 
ATOM   267  O  OE2   . GLU A 1 34  ? 20.652  13.142  24.933  1.00 39.40  ?  34  GLU A OE2   1 
ATOM   268  N  N     . VAL A 1 35  ? 21.502  15.331  19.584  1.00 35.17  ?  35  VAL A N     1 
ATOM   269  C  CA    . VAL A 1 35  ? 22.049  14.349  18.668  1.00 36.33  ?  35  VAL A CA    1 
ATOM   270  C  C     . VAL A 1 35  ? 23.301  13.738  19.285  1.00 34.97  ?  35  VAL A C     1 
ATOM   271  O  O     . VAL A 1 35  ? 24.186  14.457  19.753  1.00 33.48  ?  35  VAL A O     1 
ATOM   272  C  CB    . VAL A 1 35  ? 22.364  14.966  17.294  1.00 35.35  ?  35  VAL A CB    1 
ATOM   273  C  CG1   . VAL A 1 35  ? 22.939  13.878  16.365  1.00 30.51  ?  35  VAL A CG1   1 
ATOM   274  C  CG2   . VAL A 1 35  ? 21.092  15.598  16.704  1.00 34.69  ?  35  VAL A CG2   1 
ATOM   275  N  N     . ILE A 1 36  ? 23.392  12.417  19.250  1.00 31.52  ?  36  ILE A N     1 
ATOM   276  C  CA    . ILE A 1 36  ? 24.562  11.712  19.737  1.00 34.98  ?  36  ILE A CA    1 
ATOM   277  C  C     . ILE A 1 36  ? 25.144  10.930  18.582  1.00 31.79  ?  36  ILE A C     1 
ATOM   278  O  O     . ILE A 1 36  ? 24.514  9.989   18.080  1.00 34.69  ?  36  ILE A O     1 
ATOM   279  C  CB    . ILE A 1 36  ? 24.222  10.803  20.910  1.00 36.05  ?  36  ILE A CB    1 
ATOM   280  C  CG1   . ILE A 1 36  ? 23.647  11.683  22.032  1.00 32.48  ?  36  ILE A CG1   1 
ATOM   281  C  CG2   . ILE A 1 36  ? 25.453  10.047  21.327  1.00 29.78  ?  36  ILE A CG2   1 
ATOM   282  C  CD1   . ILE A 1 36  ? 22.735  10.978  22.922  1.00 31.64  ?  36  ILE A CD1   1 
ATOM   283  N  N     . VAL A 1 37  ? 26.314  11.356  18.126  1.00 27.80  ?  37  VAL A N     1 
ATOM   284  C  CA    . VAL A 1 37  ? 27.103  10.648  17.114  1.00 31.67  ?  37  VAL A CA    1 
ATOM   285  C  C     . VAL A 1 37  ? 28.103  9.756   17.837  1.00 32.36  ?  37  VAL A C     1 
ATOM   286  O  O     . VAL A 1 37  ? 28.754  10.194  18.792  1.00 34.77  ?  37  VAL A O     1 
ATOM   287  C  CB    . VAL A 1 37  ? 27.827  11.639  16.186  1.00 28.07  ?  37  VAL A CB    1 
ATOM   288  C  CG1   . VAL A 1 37  ? 28.677  10.901  15.152  1.00 31.31  ?  37  VAL A CG1   1 
ATOM   289  C  CG2   . VAL A 1 37  ? 26.833  12.566  15.502  1.00 29.50  ?  37  VAL A CG2   1 
ATOM   290  N  N     . VAL A 1 38  ? 28.207  8.509   17.412  1.00 31.17  ?  38  VAL A N     1 
ATOM   291  C  CA    . VAL A 1 38  ? 29.124  7.541   18.007  1.00 35.77  ?  38  VAL A CA    1 
ATOM   292  C  C     . VAL A 1 38  ? 30.055  7.011   16.914  1.00 38.69  ?  38  VAL A C     1 
ATOM   293  O  O     . VAL A 1 38  ? 29.645  6.182   16.089  1.00 36.59  ?  38  VAL A O     1 
ATOM   294  C  CB    . VAL A 1 38  ? 28.382  6.380   18.685  1.00 33.38  ?  38  VAL A CB    1 
ATOM   295  C  CG1   . VAL A 1 38  ? 29.409  5.363   19.223  1.00 29.96  ?  38  VAL A CG1   1 
ATOM   296  C  CG2   . VAL A 1 38  ? 27.369  6.904   19.805  1.00 29.78  ?  38  VAL A CG2   1 
ATOM   297  N  N     . ASN A 1 39  ? 31.307  7.473   16.918  1.00 37.06  ?  39  ASN A N     1 
ATOM   298  C  CA    . ASN A 1 39  ? 32.337  6.986   16.003  1.00 34.72  ?  39  ASN A CA    1 
ATOM   299  C  C     . ASN A 1 39  ? 32.828  5.622   16.490  1.00 35.90  ?  39  ASN A C     1 
ATOM   300  O  O     . ASN A 1 39  ? 33.431  5.515   17.564  1.00 39.42  ?  39  ASN A O     1 
ATOM   301  C  CB    . ASN A 1 39  ? 33.480  7.992   15.936  1.00 34.10  ?  39  ASN A CB    1 
ATOM   302  C  CG    . ASN A 1 39  ? 34.548  7.621   14.902  1.00 39.46  ?  39  ASN A CG    1 
ATOM   303  O  OD1   . ASN A 1 39  ? 34.642  6.476   14.440  1.00 35.76  ?  39  ASN A OD1   1 
ATOM   304  N  ND2   . ASN A 1 39  ? 35.361  8.601   14.543  1.00 39.02  ?  39  ASN A ND2   1 
ATOM   305  N  N     . ASP A 1 40  ? 32.568  4.570   15.720  1.00 32.90  ?  40  ASP A N     1 
ATOM   306  C  CA    . ASP A 1 40  ? 32.960  3.227   16.154  1.00 39.39  ?  40  ASP A CA    1 
ATOM   307  C  C     . ASP A 1 40  ? 34.444  2.928   15.830  1.00 40.29  ?  40  ASP A C     1 
ATOM   308  O  O     . ASP A 1 40  ? 34.769  1.926   15.186  1.00 36.71  ?  40  ASP A O     1 
ATOM   309  C  CB    . ASP A 1 40  ? 32.005  2.201   15.525  1.00 34.11  ?  40  ASP A CB    1 
ATOM   310  C  CG    . ASP A 1 40  ? 32.113  0.837   16.150  1.00 35.17  ?  40  ASP A CG    1 
ATOM   311  O  OD1   . ASP A 1 40  ? 32.580  0.743   17.301  1.00 41.11  ?  40  ASP A OD1   1 
ATOM   312  O  OD2   . ASP A 1 40  ? 31.744  -0.156  15.494  1.00 37.71  ?  40  ASP A OD2   1 
ATOM   313  N  N     . HIS A 1 41  ? 35.344  3.794   16.320  1.00 41.36  ?  41  HIS A N     1 
ATOM   314  C  CA    . HIS A 1 41  ? 36.800  3.715   16.117  1.00 45.43  ?  41  HIS A CA    1 
ATOM   315  C  C     . HIS A 1 41  ? 37.173  3.670   14.633  1.00 40.65  ?  41  HIS A C     1 
ATOM   316  O  O     . HIS A 1 41  ? 37.986  2.857   14.200  1.00 39.63  ?  41  HIS A O     1 
ATOM   317  C  CB    . HIS A 1 41  ? 37.422  2.528   16.876  1.00 40.36  ?  41  HIS A CB    1 
ATOM   318  C  CG    . HIS A 1 41  ? 38.825  2.783   17.347  1.00 44.80  ?  41  HIS A CG    1 
ATOM   319  N  ND1   . HIS A 1 41  ? 39.545  1.870   18.087  1.00 49.31  ?  41  HIS A ND1   1 
ATOM   320  C  CD2   . HIS A 1 41  ? 39.642  3.854   17.181  1.00 51.79  ?  41  HIS A CD2   1 
ATOM   321  C  CE1   . HIS A 1 41  ? 40.741  2.363   18.359  1.00 49.13  ?  41  HIS A CE1   1 
ATOM   322  N  NE2   . HIS A 1 41  ? 40.826  3.566   17.820  1.00 53.68  ?  41  HIS A NE2   1 
ATOM   323  N  N     . GLY A 1 42  ? 36.553  4.547   13.846  1.00 42.57  ?  42  GLY A N     1 
ATOM   324  C  CA    . GLY A 1 42  ? 36.922  4.764   12.473  1.00 34.86  ?  42  GLY A CA    1 
ATOM   325  C  C     . GLY A 1 42  ? 37.580  6.113   12.275  1.00 43.43  ?  42  GLY A C     1 
ATOM   326  O  O     . GLY A 1 42  ? 38.018  6.770   13.230  1.00 46.44  ?  42  GLY A O     1 
ATOM   327  N  N     . THR A 1 43  ? 37.656  6.533   11.017  1.00 42.25  ?  43  THR A N     1 
ATOM   328  C  CA    . THR A 1 43  ? 38.241  7.824   10.699  1.00 38.74  ?  43  THR A CA    1 
ATOM   329  C  C     . THR A 1 43  ? 37.525  8.911   11.495  1.00 45.86  ?  43  THR A C     1 
ATOM   330  O  O     . THR A 1 43  ? 36.303  8.841   11.699  1.00 43.89  ?  43  THR A O     1 
ATOM   331  C  CB    . THR A 1 43  ? 38.135  8.101   9.200   1.00 42.96  ?  43  THR A CB    1 
ATOM   332  O  OG1   . THR A 1 43  ? 36.895  8.743   8.904   1.00 45.13  ?  43  THR A OG1   1 
ATOM   333  C  CG2   . THR A 1 43  ? 38.123  6.808   8.448   1.00 46.50  ?  43  THR A CG2   1 
ATOM   334  N  N     . PRO A 1 44  ? 38.244  9.902   11.991  1.00 47.92  ?  44  PRO A N     1 
ATOM   335  C  CA    . PRO A 1 44  ? 37.607  10.876  12.875  1.00 44.95  ?  44  PRO A CA    1 
ATOM   336  C  C     . PRO A 1 44  ? 36.617  11.717  12.098  1.00 42.32  ?  44  PRO A C     1 
ATOM   337  O  O     . PRO A 1 44  ? 36.748  11.924  10.893  1.00 43.56  ?  44  PRO A O     1 
ATOM   338  C  CB    . PRO A 1 44  ? 38.781  11.713  13.409  1.00 47.53  ?  44  PRO A CB    1 
ATOM   339  C  CG    . PRO A 1 44  ? 40.055  10.952  12.953  1.00 43.95  ?  44  PRO A CG    1 
ATOM   340  C  CD    . PRO A 1 44  ? 39.653  10.229  11.715  1.00 43.33  ?  44  PRO A CD    1 
ATOM   341  N  N     . VAL A 1 45  ? 35.571  12.143  12.788  1.00 40.08  ?  45  VAL A N     1 
ATOM   342  C  CA    . VAL A 1 45  ? 34.535  12.908  12.120  1.00 38.10  ?  45  VAL A CA    1 
ATOM   343  C  C     . VAL A 1 45  ? 34.269  14.187  12.907  1.00 38.71  ?  45  VAL A C     1 
ATOM   344  O  O     . VAL A 1 45  ? 33.133  14.656  12.960  1.00 45.80  ?  45  VAL A O     1 
ATOM   345  C  CB    . VAL A 1 45  ? 33.265  12.045  11.941  1.00 51.37  ?  45  VAL A CB    1 
ATOM   346  C  CG1   . VAL A 1 45  ? 33.527  10.930  10.911  1.00 35.56  ?  45  VAL A CG1   1 
ATOM   347  C  CG2   . VAL A 1 45  ? 32.760  11.456  13.297  1.00 38.32  ?  45  VAL A CG2   1 
ATOM   348  N  N     . ASP A 1 46  ? 35.316  14.763  13.510  1.00 36.01  ?  46  ASP A N     1 
ATOM   349  C  CA    . ASP A 1 46  ? 35.163  15.940  14.365  1.00 39.45  ?  46  ASP A CA    1 
ATOM   350  C  C     . ASP A 1 46  ? 34.737  17.169  13.565  1.00 43.51  ?  46  ASP A C     1 
ATOM   351  O  O     . ASP A 1 46  ? 33.826  17.906  13.968  1.00 41.36  ?  46  ASP A O     1 
ATOM   352  C  CB    . ASP A 1 46  ? 36.472  16.218  15.091  1.00 42.84  ?  46  ASP A CB    1 
ATOM   353  C  CG    . ASP A 1 46  ? 36.794  15.179  16.128  1.00 54.52  ?  46  ASP A CG    1 
ATOM   354  O  OD1   . ASP A 1 46  ? 36.715  13.973  15.793  1.00 57.14  ?  46  ASP A OD1   1 
ATOM   355  O  OD2   . ASP A 1 46  ? 37.119  15.558  17.285  1.00 57.81  ?  46  ASP A OD2   1 
ATOM   356  N  N     . ASP A 1 47  ? 35.407  17.430  12.443  1.00 41.31  ?  47  ASP A N     1 
ATOM   357  C  CA    . ASP A 1 47  ? 35.033  18.596  11.652  1.00 48.48  ?  47  ASP A CA    1 
ATOM   358  C  C     . ASP A 1 47  ? 33.649  18.426  11.035  1.00 48.80  ?  47  ASP A C     1 
ATOM   359  O  O     . ASP A 1 47  ? 32.922  19.410  10.868  1.00 52.45  ?  47  ASP A O     1 
ATOM   360  C  CB    . ASP A 1 47  ? 36.085  18.877  10.572  1.00 47.15  ?  47  ASP A CB    1 
ATOM   361  N  N     . VAL A 1 48  ? 33.260  17.198  10.704  1.00 45.61  ?  48  VAL A N     1 
ATOM   362  C  CA    . VAL A 1 48  ? 31.920  16.968  10.182  1.00 43.75  ?  48  VAL A CA    1 
ATOM   363  C  C     . VAL A 1 48  ? 30.887  17.271  11.258  1.00 49.82  ?  48  VAL A C     1 
ATOM   364  O  O     . VAL A 1 48  ? 29.857  17.907  10.997  1.00 51.43  ?  48  VAL A O     1 
ATOM   365  C  CB    . VAL A 1 48  ? 31.800  15.516  9.661   1.00 46.78  ?  48  VAL A CB    1 
ATOM   366  C  CG1   . VAL A 1 48  ? 30.372  15.008  9.740   1.00 45.77  ?  48  VAL A CG1   1 
ATOM   367  C  CG2   . VAL A 1 48  ? 32.305  15.387  8.222   1.00 48.97  ?  48  VAL A CG2   1 
ATOM   368  N  N     . VAL A 1 49  ? 31.148  16.822  12.485  1.00 50.27  ?  49  VAL A N     1 
ATOM   369  C  CA    . VAL A 1 49  ? 30.220  17.036  13.593  1.00 50.97  ?  49  VAL A CA    1 
ATOM   370  C  C     . VAL A 1 49  ? 30.281  18.485  14.100  1.00 53.06  ?  49  VAL A C     1 
ATOM   371  O  O     . VAL A 1 49  ? 29.247  19.096  14.396  1.00 51.12  ?  49  VAL A O     1 
ATOM   372  C  CB    . VAL A 1 49  ? 30.514  16.021  14.717  1.00 46.07  ?  49  VAL A CB    1 
ATOM   373  C  CG1   . VAL A 1 49  ? 29.693  16.334  15.939  1.00 35.80  ?  49  VAL A CG1   1 
ATOM   374  C  CG2   . VAL A 1 49  ? 30.270  14.582  14.243  1.00 41.56  ?  49  VAL A CG2   1 
ATOM   375  N  N     . GLU A 1 50  ? 31.479  19.073  14.218  1.00 55.96  ?  50  GLU A N     1 
ATOM   376  C  CA    . GLU A 1 50  ? 31.524  20.458  14.687  1.00 55.43  ?  50  GLU A CA    1 
ATOM   377  C  C     . GLU A 1 50  ? 30.822  21.394  13.719  1.00 53.08  ?  50  GLU A C     1 
ATOM   378  O  O     . GLU A 1 50  ? 30.395  22.475  14.130  1.00 62.42  ?  50  GLU A O     1 
ATOM   379  C  CB    . GLU A 1 50  ? 32.960  20.927  14.922  1.00 56.11  ?  50  GLU A CB    1 
ATOM   380  N  N     . ALA A 1 51  ? 30.647  20.984  12.462  1.00 48.14  ?  51  ALA A N     1 
ATOM   381  C  CA    . ALA A 1 51  ? 29.904  21.804  11.516  1.00 50.49  ?  51  ALA A CA    1 
ATOM   382  C  C     . ALA A 1 51  ? 28.416  21.850  11.861  1.00 58.25  ?  51  ALA A C     1 
ATOM   383  O  O     . ALA A 1 51  ? 27.835  22.937  11.986  1.00 62.46  ?  51  ALA A O     1 
ATOM   384  C  CB    . ALA A 1 51  ? 30.107  21.286  10.099  1.00 51.94  ?  51  ALA A CB    1 
ATOM   385  N  N     . ALA A 1 52  ? 27.778  20.677  12.022  1.00 57.17  ?  52  ALA A N     1 
ATOM   386  C  CA    . ALA A 1 52  ? 26.331  20.647  12.263  1.00 52.77  ?  52  ALA A CA    1 
ATOM   387  C  C     . ALA A 1 52  ? 25.962  21.179  13.648  1.00 49.93  ?  52  ALA A C     1 
ATOM   388  O  O     . ALA A 1 52  ? 24.864  21.715  13.837  1.00 54.92  ?  52  ALA A O     1 
ATOM   389  C  CB    . ALA A 1 52  ? 25.796  19.231  12.054  1.00 44.96  ?  52  ALA A CB    1 
ATOM   390  N  N     . GLY A 1 53  ? 26.872  21.075  14.616  1.00 52.87  ?  53  GLY A N     1 
ATOM   391  C  CA    . GLY A 1 53  ? 26.638  21.564  15.966  1.00 49.90  ?  53  GLY A CA    1 
ATOM   392  C  C     . GLY A 1 53  ? 26.404  23.060  16.078  1.00 56.12  ?  53  GLY A C     1 
ATOM   393  O  O     . GLY A 1 53  ? 25.961  23.517  17.140  1.00 57.91  ?  53  GLY A O     1 
ATOM   394  N  N     . ARG A 1 54  ? 26.697  23.837  15.032  1.00 54.44  ?  54  ARG A N     1 
ATOM   395  C  CA    . ARG A 1 54  ? 26.352  25.248  15.094  1.00 60.87  ?  54  ARG A CA    1 
ATOM   396  C  C     . ARG A 1 54  ? 24.844  25.454  15.102  1.00 61.76  ?  54  ARG A C     1 
ATOM   397  O  O     . ARG A 1 54  ? 24.385  26.560  15.394  1.00 67.96  ?  54  ARG A O     1 
ATOM   398  C  CB    . ARG A 1 54  ? 26.994  26.008  13.922  1.00 61.86  ?  54  ARG A CB    1 
ATOM   399  N  N     . SER A 1 55  ? 24.066  24.424  14.790  1.00 59.18  ?  55  SER A N     1 
ATOM   400  C  CA    . SER A 1 55  ? 22.615  24.488  14.893  1.00 61.36  ?  55  SER A CA    1 
ATOM   401  C  C     . SER A 1 55  ? 22.035  23.475  15.879  1.00 55.53  ?  55  SER A C     1 
ATOM   402  O  O     . SER A 1 55  ? 21.110  23.808  16.621  1.00 57.29  ?  55  SER A O     1 
ATOM   403  C  CB    . SER A 1 55  ? 22.000  24.300  13.490  1.00 61.43  ?  55  SER A CB    1 
ATOM   404  O  OG    . SER A 1 55  ? 20.605  24.034  13.552  1.00 66.47  ?  55  SER A OG    1 
ATOM   405  N  N     . LEU A 1 56  ? 22.562  22.251  15.936  1.00 50.85  ?  56  LEU A N     1 
ATOM   406  C  CA    . LEU A 1 56  ? 22.005  21.205  16.790  1.00 51.02  ?  56  LEU A CA    1 
ATOM   407  C  C     . LEU A 1 56  ? 22.802  21.060  18.084  1.00 44.98  ?  56  LEU A C     1 
ATOM   408  O  O     . LEU A 1 56  ? 23.999  21.352  18.136  1.00 44.91  ?  56  LEU A O     1 
ATOM   409  C  CB    . LEU A 1 56  ? 21.981  19.848  16.071  1.00 44.66  ?  56  LEU A CB    1 
ATOM   410  C  CG    . LEU A 1 56  ? 21.489  19.618  14.646  1.00 44.46  ?  56  LEU A CG    1 
ATOM   411  C  CD1   . LEU A 1 56  ? 21.971  18.272  14.142  1.00 41.63  ?  56  LEU A CD1   1 
ATOM   412  C  CD2   . LEU A 1 56  ? 19.977  19.682  14.564  1.00 48.29  ?  56  LEU A CD2   1 
ATOM   413  N  N     . ASN A 1 57  ? 22.153  20.550  19.124  1.00 45.72  ?  57  ASN A N     1 
ATOM   414  C  CA    . ASN A 1 57  ? 22.861  20.238  20.391  1.00 40.54  ?  57  ASN A CA    1 
ATOM   415  C  C     . ASN A 1 57  ? 23.531  18.890  20.134  1.00 42.37  ?  57  ASN A C     1 
ATOM   416  O  O     . ASN A 1 57  ? 22.886  17.884  20.313  1.00 48.35  ?  57  ASN A O     1 
ATOM   417  C  CB    . ASN A 1 57  ? 21.915  20.264  21.586  1.00 41.30  ?  57  ASN A CB    1 
ATOM   418  C  CG    . ASN A 1 57  ? 22.524  19.739  22.868  1.00 51.03  ?  57  ASN A CG    1 
ATOM   419  O  OD1   . ASN A 1 57  ? 23.692  19.950  23.157  1.00 51.16  ?  57  ASN A OD1   1 
ATOM   420  N  ND2   . ASN A 1 57  ? 21.730  19.044  23.655  1.00 52.60  ?  57  ASN A ND2   1 
ATOM   421  N  N     . VAL A 1 58  ? 24.804  18.894  19.762  1.00 42.69  ?  58  VAL A N     1 
ATOM   422  C  CA    . VAL A 1 58  ? 25.439  17.641  19.282  1.00 38.28  ?  58  VAL A CA    1 
ATOM   423  C  C     . VAL A 1 58  ? 26.554  17.146  20.203  1.00 38.71  ?  58  VAL A C     1 
ATOM   424  O  O     . VAL A 1 58  ? 27.246  17.947  20.788  1.00 45.56  ?  58  VAL A O     1 
ATOM   425  C  CB    . VAL A 1 58  ? 25.833  17.826  17.808  1.00 39.98  ?  58  VAL A CB    1 
ATOM   426  C  CG1   . VAL A 1 58  ? 26.781  16.781  17.272  1.00 42.51  ?  58  VAL A CG1   1 
ATOM   427  C  CG2   . VAL A 1 58  ? 24.593  17.858  16.950  1.00 42.50  ?  58  VAL A CG2   1 
ATOM   428  N  N     . ARG A 1 59  ? 26.629  15.830  20.356  1.00 41.91  ?  59  ARG A N     1 
ATOM   429  C  CA    . ARG A 1 59  ? 27.629  15.136  21.191  1.00 42.56  ?  59  ARG A CA    1 
ATOM   430  C  C     . ARG A 1 59  ? 28.333  14.083  20.333  1.00 38.52  ?  59  ARG A C     1 
ATOM   431  O  O     . ARG A 1 59  ? 27.655  13.268  19.740  1.00 37.31  ?  59  ARG A O     1 
ATOM   432  C  CB    . ARG A 1 59  ? 26.892  14.427  22.329  1.00 45.35  ?  59  ARG A CB    1 
ATOM   433  C  CG    . ARG A 1 59  ? 27.433  14.724  23.715  1.00 51.39  ?  59  ARG A CG    1 
ATOM   434  C  CD    . ARG A 1 59  ? 26.741  13.980  24.837  1.00 55.53  ?  59  ARG A CD    1 
ATOM   435  N  NE    . ARG A 1 59  ? 27.652  12.984  25.381  1.00 63.70  ?  59  ARG A NE    1 
ATOM   436  C  CZ    . ARG A 1 59  ? 27.603  12.433  26.595  1.00 62.73  ?  59  ARG A CZ    1 
ATOM   437  N  NH1   . ARG A 1 59  ? 26.645  12.771  27.441  1.00 61.89  ?  59  ARG A NH1   1 
ATOM   438  N  NH2   . ARG A 1 59  ? 28.514  11.539  26.943  1.00 58.19  ?  59  ARG A NH2   1 
ATOM   439  N  N     . LEU A 1 60  ? 29.654  14.141  20.267  1.00 35.12  ?  60  LEU A N     1 
ATOM   440  C  CA    . LEU A 1 60  ? 30.487  13.156  19.574  1.00 32.35  ?  60  LEU A CA    1 
ATOM   441  C  C     . LEU A 1 60  ? 31.152  12.237  20.586  1.00 32.78  ?  60  LEU A C     1 
ATOM   442  O  O     . LEU A 1 60  ? 31.885  12.698  21.464  1.00 37.73  ?  60  LEU A O     1 
ATOM   443  C  CB    . LEU A 1 60  ? 31.549  13.796  18.683  1.00 33.31  ?  60  LEU A CB    1 
ATOM   444  C  CG    . LEU A 1 60  ? 32.538  12.727  18.179  1.00 34.03  ?  60  LEU A CG    1 
ATOM   445  C  CD1   . LEU A 1 60  ? 31.867  11.718  17.220  1.00 35.02  ?  60  LEU A CD1   1 
ATOM   446  C  CD2   . LEU A 1 60  ? 33.823  13.312  17.542  1.00 43.95  ?  60  LEU A CD2   1 
ATOM   447  N  N     . ILE A 1 61  ? 30.900  10.940  20.452  1.00 32.14  ?  61  ILE A N     1 
ATOM   448  C  CA    . ILE A 1 61  ? 31.433  9.926   21.344  1.00 30.29  ?  61  ILE A CA    1 
ATOM   449  C  C     . ILE A 1 61  ? 32.360  9.041   20.523  1.00 35.27  ?  61  ILE A C     1 
ATOM   450  O  O     . ILE A 1 61  ? 31.996  8.623   19.418  1.00 39.10  ?  61  ILE A O     1 
ATOM   451  C  CB    . ILE A 1 61  ? 30.297  9.120   22.003  1.00 30.70  ?  61  ILE A CB    1 
ATOM   452  C  CG1   . ILE A 1 61  ? 29.560  10.007  22.996  1.00 33.59  ?  61  ILE A CG1   1 
ATOM   453  C  CG2   . ILE A 1 61  ? 30.825  7.863   22.747  1.00 27.85  ?  61  ILE A CG2   1 
ATOM   454  C  CD1   . ILE A 1 61  ? 28.461  9.257   23.803  1.00 40.63  ?  61  ILE A CD1   1 
ATOM   455  N  N     . ASP A 1 62  ? 33.554  8.758   21.068  1.00 35.17  ?  62  ASP A N     1 
ATOM   456  C  CA    . ASP A 1 62  ? 34.629  8.022   20.401  1.00 35.83  ?  62  ASP A CA    1 
ATOM   457  C  C     . ASP A 1 62  ? 34.817  6.665   21.079  1.00 35.02  ?  62  ASP A C     1 
ATOM   458  O  O     . ASP A 1 62  ? 35.208  6.599   22.245  1.00 37.69  ?  62  ASP A O     1 
ATOM   459  C  CB    . ASP A 1 62  ? 35.936  8.815   20.457  1.00 45.12  ?  62  ASP A CB    1 
ATOM   460  C  CG    . ASP A 1 62  ? 36.261  9.569   19.158  1.00 50.80  ?  62  ASP A CG    1 
ATOM   461  O  OD1   . ASP A 1 62  ? 35.664  9.270   18.089  1.00 48.74  ?  62  ASP A OD1   1 
ATOM   462  O  OD2   . ASP A 1 62  ? 37.154  10.453  19.228  1.00 53.96  ?  62  ASP A OD2   1 
ATOM   463  N  N     . GLN A 1 63  ? 34.540  5.587   20.358  1.00 33.31  ?  63  GLN A N     1 
ATOM   464  C  CA    . GLN A 1 63  ? 34.608  4.265   20.959  1.00 35.69  ?  63  GLN A CA    1 
ATOM   465  C  C     . GLN A 1 63  ? 36.065  3.875   21.226  1.00 41.70  ?  63  GLN A C     1 
ATOM   466  O  O     . GLN A 1 63  ? 36.973  4.276   20.481  1.00 36.11  ?  63  GLN A O     1 
ATOM   467  C  CB    . GLN A 1 63  ? 33.957  3.226   20.046  1.00 33.91  ?  63  GLN A CB    1 
ATOM   468  C  CG    . GLN A 1 63  ? 32.464  3.318   19.978  1.00 40.52  ?  63  GLN A CG    1 
ATOM   469  C  CD    . GLN A 1 63  ? 31.837  3.181   21.351  1.00 38.02  ?  63  GLN A CD    1 
ATOM   470  O  OE1   . GLN A 1 63  ? 31.794  4.146   22.123  1.00 34.18  ?  63  GLN A OE1   1 
ATOM   471  N  NE2   . GLN A 1 63  ? 31.379  1.967   21.677  1.00 35.50  ?  63  GLN A NE2   1 
ATOM   472  N  N     . PRO A 1 64  ? 36.307  3.054   22.258  1.00 36.28  ?  64  PRO A N     1 
ATOM   473  C  CA    . PRO A 1 64  ? 37.681  2.609   22.527  1.00 36.71  ?  64  PRO A CA    1 
ATOM   474  C  C     . PRO A 1 64  ? 38.185  1.586   21.531  1.00 38.05  ?  64  PRO A C     1 
ATOM   475  O  O     . PRO A 1 64  ? 39.403  1.399   21.451  1.00 40.58  ?  64  PRO A O     1 
ATOM   476  C  CB    . PRO A 1 64  ? 37.591  2.008   23.935  1.00 36.17  ?  64  PRO A CB    1 
ATOM   477  C  CG    . PRO A 1 64  ? 36.174  1.419   23.996  1.00 29.56  ?  64  PRO A CG    1 
ATOM   478  C  CD    . PRO A 1 64  ? 35.314  2.343   23.096  1.00 34.75  ?  64  PRO A CD    1 
ATOM   479  N  N     . SER A 1 65  ? 37.293  0.925   20.788  1.00 36.47  ?  65  SER A N     1 
ATOM   480  C  CA    . SER A 1 65  ? 37.597  -0.083  19.768  1.00 41.43  ?  65  SER A CA    1 
ATOM   481  C  C     . SER A 1 65  ? 36.381  -0.238  18.867  1.00 43.89  ?  65  SER A C     1 
ATOM   482  O  O     . SER A 1 65  ? 35.267  0.161   19.224  1.00 44.57  ?  65  SER A O     1 
ATOM   483  C  CB    . SER A 1 65  ? 37.940  -1.445  20.382  1.00 44.35  ?  65  SER A CB    1 
ATOM   484  O  OG    . SER A 1 65  ? 36.786  -1.986  21.013  1.00 40.96  ?  65  SER A OG    1 
ATOM   485  N  N     . GLN A 1 66  ? 36.583  -0.860  17.713  1.00 42.28  ?  66  GLN A N     1 
ATOM   486  C  CA    . GLN A 1 66  ? 35.459  -1.064  16.806  1.00 44.80  ?  66  GLN A CA    1 
ATOM   487  C  C     . GLN A 1 66  ? 34.542  -2.129  17.394  1.00 47.85  ?  66  GLN A C     1 
ATOM   488  O  O     . GLN A 1 66  ? 34.918  -3.304  17.478  1.00 45.75  ?  66  GLN A O     1 
ATOM   489  C  CB    . GLN A 1 66  ? 35.933  -1.464  15.417  1.00 47.95  ?  66  GLN A CB    1 
ATOM   490  C  CG    . GLN A 1 66  ? 34.873  -1.187  14.368  1.00 48.25  ?  66  GLN A CG    1 
ATOM   491  C  CD    . GLN A 1 66  ? 34.905  -2.191  13.271  1.00 51.25  ?  66  GLN A CD    1 
ATOM   492  O  OE1   . GLN A 1 66  ? 35.648  -2.041  12.302  1.00 53.91  ?  66  GLN A OE1   1 
ATOM   493  N  NE2   . GLN A 1 66  ? 34.128  -3.256  13.426  1.00 55.31  ?  66  GLN A NE2   1 
ATOM   494  N  N     . SER A 1 67  ? 33.337  -1.719  17.802  1.00 42.69  ?  67  SER A N     1 
ATOM   495  C  CA    . SER A 1 67  ? 32.485  -2.535  18.663  1.00 42.94  ?  67  SER A CA    1 
ATOM   496  C  C     . SER A 1 67  ? 31.314  -3.176  17.932  1.00 42.73  ?  67  SER A C     1 
ATOM   497  O  O     . SER A 1 67  ? 30.563  -3.931  18.553  1.00 53.45  ?  67  SER A O     1 
ATOM   498  C  CB    . SER A 1 67  ? 31.946  -1.691  19.849  1.00 43.94  ?  67  SER A CB    1 
ATOM   499  O  OG    . SER A 1 67  ? 31.404  -0.400  19.497  1.00 34.03  ?  67  SER A OG    1 
ATOM   500  N  N     . GLY A 1 68  ? 31.123  -2.878  16.649  1.00 43.33  ?  68  GLY A N     1 
ATOM   501  C  CA    . GLY A 1 68  ? 29.932  -3.273  15.940  1.00 40.58  ?  68  GLY A CA    1 
ATOM   502  C  C     . GLY A 1 68  ? 28.818  -2.284  16.195  1.00 42.44  ?  68  GLY A C     1 
ATOM   503  O  O     . GLY A 1 68  ? 28.854  -1.541  17.179  1.00 43.87  ?  68  GLY A O     1 
ATOM   504  N  N     . PRO A 1 69  ? 27.810  -2.241  15.313  1.00 44.47  ?  69  PRO A N     1 
ATOM   505  C  CA    . PRO A 1 69  ? 26.667  -1.334  15.560  1.00 36.33  ?  69  PRO A CA    1 
ATOM   506  C  C     . PRO A 1 69  ? 25.998  -1.554  16.916  1.00 39.54  ?  69  PRO A C     1 
ATOM   507  O  O     . PRO A 1 69  ? 25.433  -0.606  17.472  1.00 32.22  ?  69  PRO A O     1 
ATOM   508  C  CB    . PRO A 1 69  ? 25.692  -1.622  14.400  1.00 40.23  ?  69  PRO A CB    1 
ATOM   509  C  CG    . PRO A 1 69  ? 26.355  -2.625  13.498  1.00 43.64  ?  69  PRO A CG    1 
ATOM   510  C  CD    . PRO A 1 69  ? 27.653  -3.090  14.113  1.00 43.44  ?  69  PRO A CD    1 
ATOM   511  N  N     . SER A 1 70  ? 26.046  -2.766  17.479  1.00 38.02  ?  70  SER A N     1 
ATOM   512  C  CA    . SER A 1 70  ? 25.518  -2.939  18.829  1.00 38.53  ?  70  SER A CA    1 
ATOM   513  C  C     . SER A 1 70  ? 26.263  -2.067  19.827  1.00 38.36  ?  70  SER A C     1 
ATOM   514  O  O     . SER A 1 70  ? 25.643  -1.302  20.575  1.00 39.52  ?  70  SER A O     1 
ATOM   515  C  CB    . SER A 1 70  ? 25.587  -4.393  19.266  1.00 33.16  ?  70  SER A CB    1 
ATOM   516  O  OG    . SER A 1 70  ? 24.621  -5.141  18.574  1.00 40.81  ?  70  SER A OG    1 
ATOM   517  N  N     . GLY A 1 71  ? 27.590  -2.184  19.871  1.00 34.91  ?  71  GLY A N     1 
ATOM   518  C  CA    . GLY A 1 71  ? 28.350  -1.436  20.858  1.00 31.78  ?  71  GLY A CA    1 
ATOM   519  C  C     . GLY A 1 71  ? 28.284  0.058   20.630  1.00 33.97  ?  71  GLY A C     1 
ATOM   520  O  O     . GLY A 1 71  ? 28.277  0.834   21.589  1.00 37.03  ?  71  GLY A O     1 
ATOM   521  N  N     . ALA A 1 72  ? 28.219  0.491   19.369  1.00 33.60  ?  72  ALA A N     1 
ATOM   522  C  CA    . ALA A 1 72  ? 28.151  1.930   19.114  1.00 34.36  ?  72  ALA A CA    1 
ATOM   523  C  C     . ALA A 1 72  ? 26.796  2.498   19.539  1.00 36.37  ?  72  ALA A C     1 
ATOM   524  O  O     . ALA A 1 72  ? 26.731  3.511   20.259  1.00 33.57  ?  72  ALA A O     1 
ATOM   525  C  CB    . ALA A 1 72  ? 28.430  2.229   17.644  1.00 30.80  ?  72  ALA A CB    1 
ATOM   526  N  N     . ARG A 1 73  ? 25.699  1.842   19.128  1.00 33.95  ?  73  ARG A N     1 
ATOM   527  C  CA    . ARG A 1 73  ? 24.359  2.290   19.529  1.00 32.55  ?  73  ARG A CA    1 
ATOM   528  C  C     . ARG A 1 73  ? 24.200  2.296   21.049  1.00 32.38  ?  73  ARG A C     1 
ATOM   529  O  O     . ARG A 1 73  ? 23.684  3.257   21.625  1.00 33.86  ?  73  ARG A O     1 
ATOM   530  C  CB    . ARG A 1 73  ? 23.304  1.404   18.887  1.00 28.22  ?  73  ARG A CB    1 
ATOM   531  C  CG    . ARG A 1 73  ? 23.097  1.739   17.435  1.00 30.23  ?  73  ARG A CG    1 
ATOM   532  C  CD    . ARG A 1 73  ? 21.864  1.083   16.932  1.00 29.04  ?  73  ARG A CD    1 
ATOM   533  N  NE    . ARG A 1 73  ? 21.877  1.060   15.486  1.00 29.69  ?  73  ARG A NE    1 
ATOM   534  C  CZ    . ARG A 1 73  ? 22.115  -0.043  14.787  1.00 37.11  ?  73  ARG A CZ    1 
ATOM   535  N  NH1   . ARG A 1 73  ? 22.293  -1.210  15.389  1.00 36.56  ?  73  ARG A NH1   1 
ATOM   536  N  NH2   . ARG A 1 73  ? 22.208  0.033   13.457  1.00 34.56  ?  73  ARG A NH2   1 
ATOM   537  N  N     . ASN A 1 74  ? 24.648  1.233   21.710  1.00 32.22  ?  74  ASN A N     1 
ATOM   538  C  CA    . ASN A 1 74  ? 24.618  1.173   23.169  1.00 31.65  ?  74  ASN A CA    1 
ATOM   539  C  C     . ASN A 1 74  ? 25.301  2.374   23.813  1.00 28.39  ?  74  ASN A C     1 
ATOM   540  O  O     . ASN A 1 74  ? 24.782  2.935   24.777  1.00 31.79  ?  74  ASN A O     1 
ATOM   541  C  CB    . ASN A 1 74  ? 25.270  -0.127  23.646  1.00 29.43  ?  74  ASN A CB    1 
ATOM   542  C  CG    . ASN A 1 74  ? 24.356  -1.307  23.471  1.00 34.13  ?  74  ASN A CG    1 
ATOM   543  O  OD1   . ASN A 1 74  ? 23.195  -1.132  23.086  1.00 34.86  ?  74  ASN A OD1   1 
ATOM   544  N  ND2   . ASN A 1 74  ? 24.856  -2.515  23.742  1.00 31.65  ?  74  ASN A ND2   1 
ATOM   545  N  N     . ALA A 1 75  ? 26.465  2.773   23.307  1.00 27.75  ?  75  ALA A N     1 
ATOM   546  C  CA    . ALA A 1 75  ? 27.125  3.959   23.828  1.00 30.76  ?  75  ALA A CA    1 
ATOM   547  C  C     . ALA A 1 75  ? 26.204  5.179   23.731  1.00 30.40  ?  75  ALA A C     1 
ATOM   548  O  O     . ALA A 1 75  ? 26.189  6.029   24.622  1.00 29.68  ?  75  ALA A O     1 
ATOM   549  C  CB    . ALA A 1 75  ? 28.465  4.181   23.081  1.00 27.73  ?  75  ALA A CB    1 
ATOM   550  N  N     . GLY A 1 76  ? 25.405  5.265   22.669  1.00 29.03  ?  76  GLY A N     1 
ATOM   551  C  CA    . GLY A 1 76  ? 24.431  6.331   22.587  1.00 26.95  ?  76  GLY A CA    1 
ATOM   552  C  C     . GLY A 1 76  ? 23.262  6.142   23.545  1.00 33.21  ?  76  GLY A C     1 
ATOM   553  O  O     . GLY A 1 76  ? 22.822  7.102   24.199  1.00 27.97  ?  76  GLY A O     1 
ATOM   554  N  N     . LEU A 1 77  ? 22.725  4.913   23.638  1.00 29.63  ?  77  LEU A N     1 
ATOM   555  C  CA    . LEU A 1 77  ? 21.612  4.703   24.558  1.00 24.91  ?  77  LEU A CA    1 
ATOM   556  C  C     . LEU A 1 77  ? 22.011  5.031   25.993  1.00 29.60  ?  77  LEU A C     1 
ATOM   557  O  O     . LEU A 1 77  ? 21.167  5.454   26.783  1.00 32.51  ?  77  LEU A O     1 
ATOM   558  C  CB    . LEU A 1 77  ? 21.096  3.272   24.460  1.00 29.07  ?  77  LEU A CB    1 
ATOM   559  C  CG    . LEU A 1 77  ? 20.533  2.781   23.118  1.00 28.50  ?  77  LEU A CG    1 
ATOM   560  C  CD1   . LEU A 1 77  ? 20.176  1.294   23.151  1.00 23.11  ?  77  LEU A CD1   1 
ATOM   561  C  CD2   . LEU A 1 77  ? 19.330  3.615   22.722  1.00 28.52  ?  77  LEU A CD2   1 
ATOM   562  N  N     . GLU A 1 78  ? 23.295  4.875   26.347  1.00 30.24  ?  78  GLU A N     1 
ATOM   563  C  CA    . GLU A 1 78  ? 23.709  5.066   27.739  1.00 32.49  ?  78  GLU A CA    1 
ATOM   564  C  C     . GLU A 1 78  ? 23.642  6.524   28.167  1.00 30.52  ?  78  GLU A C     1 
ATOM   565  O  O     . GLU A 1 78  ? 23.476  6.809   29.352  1.00 30.28  ?  78  GLU A O     1 
ATOM   566  C  CB    . GLU A 1 78  ? 25.138  4.562   27.965  1.00 33.47  ?  78  GLU A CB    1 
ATOM   567  C  CG    . GLU A 1 78  ? 25.326  3.075   27.883  1.00 35.43  ?  78  GLU A CG    1 
ATOM   568  C  CD    . GLU A 1 78  ? 24.861  2.359   29.136  1.00 38.72  ?  78  GLU A CD    1 
ATOM   569  O  OE1   . GLU A 1 78  ? 24.107  2.970   29.917  1.00 40.79  ?  78  GLU A OE1   1 
ATOM   570  O  OE2   . GLU A 1 78  ? 25.237  1.184   29.337  1.00 37.75  ?  78  GLU A OE2   1 
ATOM   571  N  N     . VAL A 1 79  ? 23.848  7.462   27.251  1.00 32.33  ?  79  VAL A N     1 
ATOM   572  C  CA    . VAL A 1 79  ? 23.891  8.869   27.627  1.00 30.86  ?  79  VAL A CA    1 
ATOM   573  C  C     . VAL A 1 79  ? 22.715  9.635   27.091  1.00 30.19  ?  79  VAL A C     1 
ATOM   574  O  O     . VAL A 1 79  ? 22.538  10.799  27.477  1.00 35.37  ?  79  VAL A O     1 
ATOM   575  C  CB    . VAL A 1 79  ? 25.209  9.555   27.193  1.00 32.92  ?  79  VAL A CB    1 
ATOM   576  C  CG1   . VAL A 1 79  ? 26.436  8.812   27.760  1.00 24.75  ?  79  VAL A CG1   1 
ATOM   577  C  CG2   . VAL A 1 79  ? 25.254  9.741   25.680  1.00 27.27  ?  79  VAL A CG2   1 
ATOM   578  N  N     . ALA A 1 80  ? 21.891  9.020   26.240  1.00 31.15  ?  80  ALA A N     1 
ATOM   579  C  CA    . ALA A 1 80  ? 20.711  9.683   25.685  1.00 33.89  ?  80  ALA A CA    1 
ATOM   580  C  C     . ALA A 1 80  ? 19.717  10.050  26.795  1.00 33.90  ?  80  ALA A C     1 
ATOM   581  O  O     . ALA A 1 80  ? 19.232  9.180   27.537  1.00 32.80  ?  80  ALA A O     1 
ATOM   582  C  CB    . ALA A 1 80  ? 20.047  8.791   24.631  1.00 30.75  ?  80  ALA A CB    1 
ATOM   583  N  N     . ARG A 1 81  ? 19.426  11.352  26.896  1.00 38.96  ?  81  ARG A N     1 
ATOM   584  C  CA    . ARG A 1 81  ? 18.606  11.929  27.959  1.00 40.37  ?  81  ARG A CA    1 
ATOM   585  C  C     . ARG A 1 81  ? 17.155  12.120  27.557  1.00 32.43  ?  81  ARG A C     1 
ATOM   586  O  O     . ARG A 1 81  ? 16.331  12.478  28.401  1.00 33.75  ?  81  ARG A O     1 
ATOM   587  C  CB    . ARG A 1 81  ? 19.179  13.287  28.388  1.00 36.57  ?  81  ARG A CB    1 
ATOM   588  C  CG    . ARG A 1 81  ? 20.387  13.179  29.331  1.00 40.54  ?  81  ARG A CG    1 
ATOM   589  C  CD    . ARG A 1 81  ? 20.988  14.558  29.511  1.00 42.18  ?  81  ARG A CD    1 
ATOM   590  N  NE    . ARG A 1 81  ? 21.165  15.196  28.212  1.00 43.18  ?  81  ARG A NE    1 
ATOM   591  C  CZ    . ARG A 1 81  ? 21.561  16.444  28.047  1.00 44.73  ?  81  ARG A CZ    1 
ATOM   592  N  NH1   . ARG A 1 81  ? 21.765  17.239  29.085  1.00 43.52  ?  81  ARG A NH1   1 
ATOM   593  N  NH2   . ARG A 1 81  ? 21.766  16.903  26.812  1.00 45.07  ?  81  ARG A NH2   1 
ATOM   594  N  N     . GLY A 1 82  ? 16.841  11.943  26.284  1.00 30.91  ?  82  GLY A N     1 
ATOM   595  C  CA    . GLY A 1 82  ? 15.488  12.130  25.850  1.00 31.26  ?  82  GLY A CA    1 
ATOM   596  C  C     . GLY A 1 82  ? 14.579  11.075  26.443  1.00 33.59  ?  82  GLY A C     1 
ATOM   597  O  O     . GLY A 1 82  ? 14.965  9.916   26.630  1.00 31.60  ?  82  GLY A O     1 
ATOM   598  N  N     . GLU A 1 83  ? 13.358  11.506  26.771  1.00 31.02  ?  83  GLU A N     1 
ATOM   599  C  CA    . GLU A 1 83  ? 12.283  10.572  27.027  1.00 30.94  ?  83  GLU A CA    1 
ATOM   600  C  C     . GLU A 1 83  ? 12.147  9.611   25.858  1.00 33.49  ?  83  GLU A C     1 
ATOM   601  O  O     . GLU A 1 83  ? 11.768  8.451   26.044  1.00 32.52  ?  83  GLU A O     1 
ATOM   602  C  CB    . GLU A 1 83  ? 10.974  11.329  27.247  1.00 30.60  ?  83  GLU A CB    1 
ATOM   603  C  CG    . GLU A 1 83  ? 9.758   10.410  27.312  1.00 26.56  ?  83  GLU A CG    1 
ATOM   604  C  CD    . GLU A 1 83  ? 8.492   11.109  27.842  1.00 32.95  ?  83  GLU A CD    1 
ATOM   605  O  OE1   . GLU A 1 83  ? 8.333   12.346  27.707  1.00 36.15  ?  83  GLU A OE1   1 
ATOM   606  O  OE2   . GLU A 1 83  ? 7.619   10.407  28.377  1.00 32.39  ?  83  GLU A OE2   1 
ATOM   607  N  N     . TYR A 1 84  ? 12.485  10.071  24.652  1.00 30.36  ?  84  TYR A N     1 
ATOM   608  C  CA    . TYR A 1 84  ? 12.370  9.260   23.455  1.00 32.66  ?  84  TYR A CA    1 
ATOM   609  C  C     . TYR A 1 84  ? 13.684  9.286   22.676  1.00 32.28  ?  84  TYR A C     1 
ATOM   610  O  O     . TYR A 1 84  ? 14.413  10.281  22.684  1.00 32.86  ?  84  TYR A O     1 
ATOM   611  C  CB    . TYR A 1 84  ? 11.192  9.756   22.605  1.00 27.12  ?  84  TYR A CB    1 
ATOM   612  C  CG    . TYR A 1 84  ? 9.862   9.772   23.347  1.00 32.34  ?  84  TYR A CG    1 
ATOM   613  C  CD1   . TYR A 1 84  ? 9.178   8.575   23.619  1.00 32.33  ?  84  TYR A CD1   1 
ATOM   614  C  CD2   . TYR A 1 84  ? 9.274   10.979  23.767  1.00 28.49  ?  84  TYR A CD2   1 
ATOM   615  C  CE1   . TYR A 1 84  ? 7.949   8.580   24.292  1.00 29.43  ?  84  TYR A CE1   1 
ATOM   616  C  CE2   . TYR A 1 84  ? 8.050   10.996  24.419  1.00 26.41  ?  84  TYR A CE2   1 
ATOM   617  C  CZ    . TYR A 1 84  ? 7.394   9.795   24.676  1.00 31.82  ?  84  TYR A CZ    1 
ATOM   618  O  OH    . TYR A 1 84  ? 6.192   9.791   25.343  1.00 32.03  ?  84  TYR A OH    1 
ATOM   619  N  N     . VAL A 1 85  ? 13.956  8.186   21.998  1.00 31.67  ?  85  VAL A N     1 
ATOM   620  C  CA    . VAL A 1 85  ? 15.203  7.975   21.226  1.00 27.55  ?  85  VAL A CA    1 
ATOM   621  C  C     . VAL A 1 85  ? 14.825  7.661   19.779  1.00 31.00  ?  85  VAL A C     1 
ATOM   622  O  O     . VAL A 1 85  ? 13.889  6.931   19.558  1.00 28.08  ?  85  VAL A O     1 
ATOM   623  C  CB    . VAL A 1 85  ? 16.016  6.849   21.891  1.00 25.98  ?  85  VAL A CB    1 
ATOM   624  C  CG1   . VAL A 1 85  ? 16.752  5.958   20.922  1.00 37.28  ?  85  VAL A CG1   1 
ATOM   625  C  CG2   . VAL A 1 85  ? 16.941  7.354   22.972  1.00 28.11  ?  85  VAL A CG2   1 
ATOM   626  N  N     . ALA A 1 86  ? 15.510  8.297   18.838  1.00 36.90  ?  86  ALA A N     1 
ATOM   627  C  CA    . ALA A 1 86  ? 15.336  8.051   17.404  1.00 29.78  ?  86  ALA A CA    1 
ATOM   628  C  C     . ALA A 1 86  ? 16.672  7.603   16.824  1.00 33.42  ?  86  ALA A C     1 
ATOM   629  O  O     . ALA A 1 86  ? 17.622  8.396   16.752  1.00 34.43  ?  86  ALA A O     1 
ATOM   630  C  CB    . ALA A 1 86  ? 14.841  9.300   16.679  1.00 30.40  ?  86  ALA A CB    1 
ATOM   631  N  N     . PHE A 1 87  ? 16.753  6.342   16.408  1.00 31.03  ?  87  PHE A N     1 
ATOM   632  C  CA    . PHE A 1 87  ? 17.967  5.855   15.767  1.00 30.57  ?  87  PHE A CA    1 
ATOM   633  C  C     . PHE A 1 87  ? 18.053  6.400   14.344  1.00 34.80  ?  87  PHE A C     1 
ATOM   634  O  O     . PHE A 1 87  ? 17.037  6.525   13.644  1.00 36.88  ?  87  PHE A O     1 
ATOM   635  C  CB    . PHE A 1 87  ? 17.971  4.328   15.746  1.00 28.25  ?  87  PHE A CB    1 
ATOM   636  C  CG    . PHE A 1 87  ? 17.787  3.717   17.093  1.00 30.84  ?  87  PHE A CG    1 
ATOM   637  C  CD1   . PHE A 1 87  ? 18.837  3.643   17.986  1.00 28.50  ?  87  PHE A CD1   1 
ATOM   638  C  CD2   . PHE A 1 87  ? 16.552  3.216   17.483  1.00 32.78  ?  87  PHE A CD2   1 
ATOM   639  C  CE1   . PHE A 1 87  ? 18.656  3.096   19.257  1.00 26.43  ?  87  PHE A CE1   1 
ATOM   640  C  CE2   . PHE A 1 87  ? 16.388  2.683   18.739  1.00 32.88  ?  87  PHE A CE2   1 
ATOM   641  C  CZ    . PHE A 1 87  ? 17.455  2.614   19.614  1.00 27.34  ?  87  PHE A CZ    1 
ATOM   642  N  N     . LEU A 1 88  ? 19.260  6.760   13.923  1.00 30.00  ?  88  LEU A N     1 
ATOM   643  C  CA    . LEU A 1 88  ? 19.516  7.087   12.514  1.00 35.95  ?  88  LEU A CA    1 
ATOM   644  C  C     . LEU A 1 88  ? 20.885  6.533   12.128  1.00 34.09  ?  88  LEU A C     1 
ATOM   645  O  O     . LEU A 1 88  ? 21.895  6.980   12.671  1.00 31.75  ?  88  LEU A O     1 
ATOM   646  C  CB    . LEU A 1 88  ? 19.449  8.593   12.254  1.00 32.51  ?  88  LEU A CB    1 
ATOM   647  C  CG    . LEU A 1 88  ? 19.865  9.036   10.841  1.00 33.21  ?  88  LEU A CG    1 
ATOM   648  C  CD1   . LEU A 1 88  ? 19.042  8.384   9.735   1.00 25.08  ?  88  LEU A CD1   1 
ATOM   649  C  CD2   . LEU A 1 88  ? 19.813  10.568  10.735  1.00 34.56  ?  88  LEU A CD2   1 
ATOM   650  N  N     . ASP A 1 89  ? 20.911  5.541   11.232  1.00 32.66  ?  89  ASP A N     1 
ATOM   651  C  CA    . ASP A 1 89  ? 22.153  5.064   10.630  1.00 34.61  ?  89  ASP A CA    1 
ATOM   652  C  C     . ASP A 1 89  ? 22.840  6.196   9.848   1.00 40.42  ?  89  ASP A C     1 
ATOM   653  O  O     . ASP A 1 89  ? 22.194  7.151   9.399   1.00 38.96  ?  89  ASP A O     1 
ATOM   654  C  CB    . ASP A 1 89  ? 21.872  3.892   9.698   1.00 33.08  ?  89  ASP A CB    1 
ATOM   655  C  CG    . ASP A 1 89  ? 21.587  2.569   10.445  1.00 40.34  ?  89  ASP A CG    1 
ATOM   656  O  OD1   . ASP A 1 89  ? 21.537  2.493   11.710  1.00 38.26  ?  89  ASP A OD1   1 
ATOM   657  O  OD2   . ASP A 1 89  ? 21.393  1.573   9.720   1.00 41.65  ?  89  ASP A OD2   1 
ATOM   658  N  N     . ASP A 1 90  ? 24.173  6.098   9.678   1.00 34.35  ?  90  ASP A N     1 
ATOM   659  C  CA    . ASP A 1 90  ? 24.832  7.223   9.023   1.00 36.34  ?  90  ASP A CA    1 
ATOM   660  C  C     . ASP A 1 90  ? 24.582  7.284   7.522   1.00 37.25  ?  90  ASP A C     1 
ATOM   661  O  O     . ASP A 1 90  ? 24.798  8.346   6.944   1.00 42.84  ?  90  ASP A O     1 
ATOM   662  C  CB    . ASP A 1 90  ? 26.348  7.266   9.317   1.00 35.38  ?  90  ASP A CB    1 
ATOM   663  C  CG    . ASP A 1 90  ? 27.122  6.103   8.720   1.00 41.79  ?  90  ASP A CG    1 
ATOM   664  O  OD1   . ASP A 1 90  ? 26.538  5.258   8.002   1.00 44.40  ?  90  ASP A OD1   1 
ATOM   665  O  OD2   . ASP A 1 90  ? 28.346  6.052   8.964   1.00 41.49  ?  90  ASP A OD2   1 
ATOM   666  N  N     . ASP A 1 91  ? 24.090  6.220   6.883   1.00 40.05  ?  91  ASP A N     1 
ATOM   667  C  CA    . ASP A 1 91  ? 23.814  6.237   5.445   1.00 42.33  ?  91  ASP A CA    1 
ATOM   668  C  C     . ASP A 1 91  ? 22.323  6.397   5.107   1.00 43.17  ?  91  ASP A C     1 
ATOM   669  O  O     . ASP A 1 91  ? 21.935  6.207   3.944   1.00 44.24  ?  91  ASP A O     1 
ATOM   670  C  CB    . ASP A 1 91  ? 24.391  4.976   4.759   1.00 44.36  ?  91  ASP A CB    1 
ATOM   671  C  CG    . ASP A 1 91  ? 23.833  3.632   5.338   1.00 48.82  ?  91  ASP A CG    1 
ATOM   672  O  OD1   . ASP A 1 91  ? 23.284  3.615   6.468   1.00 44.35  ?  91  ASP A OD1   1 
ATOM   673  O  OD2   . ASP A 1 91  ? 23.981  2.572   4.669   1.00 46.34  ?  91  ASP A OD2   1 
ATOM   674  N  N     . ASP A 1 92  ? 21.481  6.766   6.074   1.00 45.10  ?  92  ASP A N     1 
ATOM   675  C  CA    . ASP A 1 92  ? 20.050  6.956   5.835   1.00 37.97  ?  92  ASP A CA    1 
ATOM   676  C  C     . ASP A 1 92  ? 19.658  8.405   6.118   1.00 36.97  ?  92  ASP A C     1 
ATOM   677  O  O     . ASP A 1 92  ? 20.444  9.170   6.670   1.00 39.09  ?  92  ASP A O     1 
ATOM   678  C  CB    . ASP A 1 92  ? 19.230  5.986   6.688   1.00 36.05  ?  92  ASP A CB    1 
ATOM   679  C  CG    . ASP A 1 92  ? 19.560  4.526   6.397   1.00 39.87  ?  92  ASP A CG    1 
ATOM   680  O  OD1   . ASP A 1 92  ? 19.753  4.198   5.215   1.00 43.90  ?  92  ASP A OD1   1 
ATOM   681  O  OD2   . ASP A 1 92  ? 19.635  3.703   7.341   1.00 37.77  ?  92  ASP A OD2   1 
ATOM   682  N  N     . VAL A 1 93  ? 18.425  8.798   5.749   1.00 38.67  ?  93  VAL A N     1 
ATOM   683  C  CA    . VAL A 1 93  ? 17.940  10.165  5.969   1.00 34.15  ?  93  VAL A CA    1 
ATOM   684  C  C     . VAL A 1 93  ? 16.523  10.170  6.532   1.00 37.11  ?  93  VAL A C     1 
ATOM   685  O  O     . VAL A 1 93  ? 15.649  9.441   6.051   1.00 39.69  ?  93  VAL A O     1 
ATOM   686  C  CB    . VAL A 1 93  ? 17.951  11.004  4.679   1.00 35.49  ?  93  VAL A CB    1 
ATOM   687  C  CG1   . VAL A 1 93  ? 19.378  11.391  4.306   1.00 41.34  ?  93  VAL A CG1   1 
ATOM   688  C  CG2   . VAL A 1 93  ? 17.271  10.250  3.566   1.00 36.39  ?  93  VAL A CG2   1 
ATOM   689  N  N     . PHE A 1 94  ? 16.288  11.059  7.502   1.00 36.80  ?  94  PHE A N     1 
ATOM   690  C  CA    . PHE A 1 94  ? 14.947  11.355  8.007   1.00 37.52  ?  94  PHE A CA    1 
ATOM   691  C  C     . PHE A 1 94  ? 14.158  12.208  7.010   1.00 40.60  ?  94  PHE A C     1 
ATOM   692  O  O     . PHE A 1 94  ? 14.705  13.074  6.321   1.00 37.71  ?  94  PHE A O     1 
ATOM   693  C  CB    . PHE A 1 94  ? 15.030  12.144  9.321   1.00 30.00  ?  94  PHE A CB    1 
ATOM   694  C  CG    . PHE A 1 94  ? 15.463  11.342  10.512  1.00 32.69  ?  94  PHE A CG    1 
ATOM   695  C  CD1   . PHE A 1 94  ? 15.360  9.946   10.528  1.00 29.17  ?  94  PHE A CD1   1 
ATOM   696  C  CD2   . PHE A 1 94  ? 15.959  12.000  11.652  1.00 35.78  ?  94  PHE A CD2   1 
ATOM   697  C  CE1   . PHE A 1 94  ? 15.767  9.212   11.664  1.00 29.34  ?  94  PHE A CE1   1 
ATOM   698  C  CE2   . PHE A 1 94  ? 16.364  11.273  12.801  1.00 30.66  ?  94  PHE A CE2   1 
ATOM   699  C  CZ    . PHE A 1 94  ? 16.275  9.878   12.801  1.00 24.50  ?  94  PHE A CZ    1 
ATOM   700  N  N     . SER A 1 95  ? 12.862  12.003  6.973   1.00 33.35  ?  95  SER A N     1 
ATOM   701  C  CA    . SER A 1 95  ? 12.035  13.045  6.407   1.00 36.06  ?  95  SER A CA    1 
ATOM   702  C  C     . SER A 1 95  ? 11.783  14.124  7.466   1.00 35.92  ?  95  SER A C     1 
ATOM   703  O  O     . SER A 1 95  ? 11.972  13.889  8.662   1.00 35.19  ?  95  SER A O     1 
ATOM   704  C  CB    . SER A 1 95  ? 10.721  12.459  5.909   1.00 37.12  ?  95  SER A CB    1 
ATOM   705  O  OG    . SER A 1 95  ? 9.790   12.400  6.979   1.00 33.80  ?  95  SER A OG    1 
ATOM   706  N  N     . PRO A 1 96  ? 11.381  15.330  7.055   1.00 35.00  ?  96  PRO A N     1 
ATOM   707  C  CA    . PRO A 1 96  ? 11.152  16.398  8.049   1.00 36.61  ?  96  PRO A CA    1 
ATOM   708  C  C     . PRO A 1 96  ? 9.992   16.122  8.972   1.00 36.27  ?  96  PRO A C     1 
ATOM   709  O  O     . PRO A 1 96  ? 9.902   16.760  10.027  1.00 39.48  ?  96  PRO A O     1 
ATOM   710  C  CB    . PRO A 1 96  ? 10.883  17.649  7.193   1.00 38.42  ?  96  PRO A CB    1 
ATOM   711  C  CG    . PRO A 1 96  ? 11.378  17.321  5.829   1.00 43.14  ?  96  PRO A CG    1 
ATOM   712  C  CD    . PRO A 1 96  ? 11.251  15.818  5.669   1.00 39.54  ?  96  PRO A CD    1 
ATOM   713  N  N     . GLN A 1 97  ? 9.111   15.193  8.623   1.00 35.81  ?  97  GLN A N     1 
ATOM   714  C  CA    . GLN A 1 97  ? 8.015   14.764  9.487   1.00 38.03  ?  97  GLN A CA    1 
ATOM   715  C  C     . GLN A 1 97  ? 8.389   13.609  10.416  1.00 33.87  ?  97  GLN A C     1 
ATOM   716  O  O     . GLN A 1 97  ? 7.504   13.083  11.094  1.00 34.81  ?  97  GLN A O     1 
ATOM   717  C  CB    . GLN A 1 97  ? 6.801   14.369  8.638   1.00 31.63  ?  97  GLN A CB    1 
ATOM   718  C  CG    . GLN A 1 97  ? 6.153   15.546  7.857   1.00 36.29  ?  97  GLN A CG    1 
ATOM   719  C  CD    . GLN A 1 97  ? 6.917   15.940  6.577   1.00 42.50  ?  97  GLN A CD    1 
ATOM   720  O  OE1   . GLN A 1 97  ? 7.846   15.254  6.147   1.00 43.18  ?  97  GLN A OE1   1 
ATOM   721  N  NE2   . GLN A 1 97  ? 6.511   17.045  5.962   1.00 43.54  ?  97  GLN A NE2   1 
ATOM   722  N  N     . HIS A 1 98  ? 9.673   13.227  10.482  1.00 31.75  ?  98  HIS A N     1 
ATOM   723  C  CA    . HIS A 1 98  ? 10.066  12.024  11.224  1.00 33.22  ?  98  HIS A CA    1 
ATOM   724  C  C     . HIS A 1 98  ? 9.657   12.099  12.692  1.00 31.98  ?  98  HIS A C     1 
ATOM   725  O  O     . HIS A 1 98  ? 9.264   11.086  13.282  1.00 33.06  ?  98  HIS A O     1 
ATOM   726  C  CB    . HIS A 1 98  ? 11.580  11.788  11.123  1.00 31.03  ?  98  HIS A CB    1 
ATOM   727  C  CG    . HIS A 1 98  ? 12.007  10.416  11.554  1.00 25.68  ?  98  HIS A CG    1 
ATOM   728  N  ND1   . HIS A 1 98  ? 11.819  9.298   10.768  1.00 28.14  ?  98  HIS A ND1   1 
ATOM   729  C  CD2   . HIS A 1 98  ? 12.605  9.978   12.690  1.00 25.60  ?  98  HIS A CD2   1 
ATOM   730  C  CE1   . HIS A 1 98  ? 12.278  8.229   11.400  1.00 27.69  ?  98  HIS A CE1   1 
ATOM   731  N  NE2   . HIS A 1 98  ? 12.774  8.617   12.563  1.00 27.51  ?  98  HIS A NE2   1 
ATOM   732  N  N     . LEU A 1 99  ? 9.752   13.280  13.307  1.00 31.41  ?  99  LEU A N     1 
ATOM   733  C  CA    . LEU A 1 99  ? 9.372   13.434  14.704  1.00 32.19  ?  99  LEU A CA    1 
ATOM   734  C  C     . LEU A 1 99  ? 7.970   13.990  14.886  1.00 36.09  ?  99  LEU A C     1 
ATOM   735  O  O     . LEU A 1 99  ? 7.238   13.514  15.756  1.00 32.09  ?  99  LEU A O     1 
ATOM   736  C  CB    . LEU A 1 99  ? 10.358  14.327  15.444  1.00 31.05  ?  99  LEU A CB    1 
ATOM   737  C  CG    . LEU A 1 99  ? 11.759  13.736  15.512  1.00 38.16  ?  99  LEU A CG    1 
ATOM   738  C  CD1   . LEU A 1 99  ? 12.666  14.558  16.438  1.00 37.80  ?  99  LEU A CD1   1 
ATOM   739  C  CD2   . LEU A 1 99  ? 11.707  12.257  15.918  1.00 33.05  ?  99  LEU A CD2   1 
ATOM   740  N  N     . SER A 1 100 ? 7.573   14.992  14.101  1.00 36.66  ?  100 SER A N     1 
ATOM   741  C  CA    . SER A 1 100 ? 6.209   15.488  14.228  1.00 34.57  ?  100 SER A CA    1 
ATOM   742  C  C     . SER A 1 100 ? 5.210   14.409  13.852  1.00 38.69  ?  100 SER A C     1 
ATOM   743  O  O     . SER A 1 100 ? 4.052   14.460  14.281  1.00 34.66  ?  100 SER A O     1 
ATOM   744  C  CB    . SER A 1 100 ? 6.009   16.730  13.362  1.00 34.96  ?  100 SER A CB    1 
ATOM   745  O  OG    . SER A 1 100 ? 6.043   16.385  11.991  1.00 45.54  ?  100 SER A OG    1 
ATOM   746  N  N     . GLY A 1 101 ? 5.650   13.407  13.093  1.00 37.34  ?  101 GLY A N     1 
ATOM   747  C  CA    . GLY A 1 101 ? 4.767   12.322  12.739  1.00 37.89  ?  101 GLY A CA    1 
ATOM   748  C  C     . GLY A 1 101 ? 4.762   11.159  13.713  1.00 36.99  ?  101 GLY A C     1 
ATOM   749  O  O     . GLY A 1 101 ? 3.872   10.314  13.634  1.00 39.10  ?  101 GLY A O     1 
ATOM   750  N  N     . THR A 1 102 ? 5.742   11.071  14.613  1.00 35.29  ?  102 THR A N     1 
ATOM   751  C  CA    . THR A 1 102 ? 5.795   9.939   15.534  1.00 35.71  ?  102 THR A CA    1 
ATOM   752  C  C     . THR A 1 102 ? 5.534   10.313  16.984  1.00 31.34  ?  102 THR A C     1 
ATOM   753  O  O     . THR A 1 102 ? 4.863   9.554   17.694  1.00 31.44  ?  102 THR A O     1 
ATOM   754  C  CB    . THR A 1 102 ? 7.152   9.217   15.441  1.00 33.01  ?  102 THR A CB    1 
ATOM   755  O  OG1   . THR A 1 102 ? 8.205   10.126  15.769  1.00 31.94  ?  102 THR A OG1   1 
ATOM   756  C  CG2   . THR A 1 102 ? 7.359   8.637   14.058  1.00 29.45  ?  102 THR A CG2   1 
ATOM   757  N  N     . LEU A 1 103 ? 6.048   11.462  17.430  1.00 32.52  ?  103 LEU A N     1 
ATOM   758  C  CA    . LEU A 1 103 ? 5.913   11.857  18.831  1.00 32.85  ?  103 LEU A CA    1 
ATOM   759  C  C     . LEU A 1 103 ? 4.472   11.944  19.323  1.00 33.94  ?  103 LEU A C     1 
ATOM   760  O  O     . LEU A 1 103 ? 4.244   11.645  20.509  1.00 34.26  ?  103 LEU A O     1 
ATOM   761  C  CB    . LEU A 1 103 ? 6.622   13.193  19.059  1.00 30.18  ?  103 LEU A CB    1 
ATOM   762  C  CG    . LEU A 1 103 ? 8.116   13.070  19.307  1.00 38.96  ?  103 LEU A CG    1 
ATOM   763  C  CD1   . LEU A 1 103 ? 8.773   14.409  19.071  1.00 40.59  ?  103 LEU A CD1   1 
ATOM   764  C  CD2   . LEU A 1 103 ? 8.385   12.572  20.737  1.00 39.27  ?  103 LEU A CD2   1 
ATOM   765  N  N     . PRO A 1 104 ? 3.486   12.383  18.527  1.00 32.90  ?  104 PRO A N     1 
ATOM   766  C  CA    . PRO A 1 104 ? 2.103   12.334  19.028  1.00 34.90  ?  104 PRO A CA    1 
ATOM   767  C  C     . PRO A 1 104 ? 1.658   10.937  19.395  1.00 33.63  ?  104 PRO A C     1 
ATOM   768  O  O     . PRO A 1 104 ? 0.912   10.781  20.370  1.00 33.32  ?  104 PRO A O     1 
ATOM   769  C  CB    . PRO A 1 104 ? 1.278   12.914  17.867  1.00 35.79  ?  104 PRO A CB    1 
ATOM   770  C  CG    . PRO A 1 104 ? 2.260   13.869  17.190  1.00 32.61  ?  104 PRO A CG    1 
ATOM   771  C  CD    . PRO A 1 104 ? 3.583   13.149  17.262  1.00 35.02  ?  104 PRO A CD    1 
ATOM   772  N  N     . LEU A 1 105 ? 2.126   9.902   18.679  1.00 34.00  ?  105 LEU A N     1 
ATOM   773  C  CA    . LEU A 1 105 ? 1.723   8.551   19.057  1.00 31.46  ?  105 LEU A CA    1 
ATOM   774  C  C     . LEU A 1 105 ? 2.428   8.094   20.322  1.00 31.49  ?  105 LEU A C     1 
ATOM   775  O  O     . LEU A 1 105 ? 1.838   7.367   21.119  1.00 35.15  ?  105 LEU A O     1 
ATOM   776  C  CB    . LEU A 1 105 ? 1.978   7.575   17.914  1.00 36.03  ?  105 LEU A CB    1 
ATOM   777  C  CG    . LEU A 1 105 ? 1.020   7.733   16.735  1.00 34.53  ?  105 LEU A CG    1 
ATOM   778  C  CD1   . LEU A 1 105 ? 1.687   7.165   15.501  1.00 33.34  ?  105 LEU A CD1   1 
ATOM   779  C  CD2   . LEU A 1 105 ? -0.276  6.968   17.031  1.00 36.74  ?  105 LEU A CD2   1 
ATOM   780  N  N     . LEU A 1 106 ? 3.671   8.526   20.540  1.00 30.95  ?  106 LEU A N     1 
ATOM   781  C  CA    . LEU A 1 106 ? 4.386   8.124   21.743  1.00 33.08  ?  106 LEU A CA    1 
ATOM   782  C  C     . LEU A 1 106 ? 3.844   8.840   22.974  1.00 34.51  ?  106 LEU A C     1 
ATOM   783  O  O     . LEU A 1 106 ? 3.621   8.216   24.025  1.00 31.85  ?  106 LEU A O     1 
ATOM   784  C  CB    . LEU A 1 106 ? 5.879   8.380   21.557  1.00 31.10  ?  106 LEU A CB    1 
ATOM   785  C  CG    . LEU A 1 106 ? 6.467   7.468   20.466  1.00 30.25  ?  106 LEU A CG    1 
ATOM   786  C  CD1   . LEU A 1 106 ? 7.711   8.098   19.808  1.00 31.03  ?  106 LEU A CD1   1 
ATOM   787  C  CD2   . LEU A 1 106 ? 6.758   6.028   20.985  1.00 23.91  ?  106 LEU A CD2   1 
ATOM   788  N  N     . LYS A 1 107 ? 3.630   10.158  22.864  1.00 35.27  ?  107 LYS A N     1 
ATOM   789  C  CA    . LYS A 1 107 ? 3.050   10.901  23.974  1.00 33.31  ?  107 LYS A CA    1 
ATOM   790  C  C     . LYS A 1 107 ? 1.664   10.367  24.309  1.00 33.59  ?  107 LYS A C     1 
ATOM   791  O  O     . LYS A 1 107 ? 1.266   10.347  25.485  1.00 31.07  ?  107 LYS A O     1 
ATOM   792  C  CB    . LYS A 1 107 ? 2.983   12.408  23.649  1.00 36.39  ?  107 LYS A CB    1 
ATOM   793  C  CG    . LYS A 1 107 ? 4.328   13.134  23.273  1.00 42.16  ?  107 LYS A CG    1 
ATOM   794  C  CD    . LYS A 1 107 ? 4.146   14.710  23.241  1.00 46.23  ?  107 LYS A CD    1 
ATOM   795  C  CE    . LYS A 1 107 ? 4.886   15.435  22.095  1.00 52.58  ?  107 LYS A CE    1 
ATOM   796  N  NZ    . LYS A 1 107 ? 4.073   15.866  20.878  1.00 50.60  ?  107 LYS A NZ    1 
ATOM   797  N  N     . GLY A 1 108 ? 0.922   9.917   23.298  1.00 33.01  ?  108 GLY A N     1 
ATOM   798  C  CA    . GLY A 1 108 ? -0.404  9.361   23.508  1.00 22.83  ?  108 GLY A CA    1 
ATOM   799  C  C     . GLY A 1 108 ? -0.439  7.989   24.158  1.00 33.83  ?  108 GLY A C     1 
ATOM   800  O  O     . GLY A 1 108 ? -1.527  7.544   24.541  1.00 31.52  ?  108 GLY A O     1 
ATOM   801  N  N     . GLY A 1 109 ? 0.703   7.294   24.281  1.00 32.05  ?  109 GLY A N     1 
ATOM   802  C  CA    . GLY A 1 109 ? 0.691   5.981   24.926  1.00 33.35  ?  109 GLY A CA    1 
ATOM   803  C  C     . GLY A 1 109 ? 1.423   4.839   24.225  1.00 33.54  ?  109 GLY A C     1 
ATOM   804  O  O     . GLY A 1 109 ? 1.598   3.771   24.807  1.00 29.17  ?  109 GLY A O     1 
ATOM   805  N  N     . ALA A 1 110 ? 1.830   5.034   22.969  1.00 33.84  ?  110 ALA A N     1 
ATOM   806  C  CA    . ALA A 1 110 ? 2.760   4.110   22.334  1.00 32.22  ?  110 ALA A CA    1 
ATOM   807  C  C     . ALA A 1 110 ? 4.091   4.134   23.072  1.00 27.38  ?  110 ALA A C     1 
ATOM   808  O  O     . ALA A 1 110 ? 4.397   5.072   23.791  1.00 34.16  ?  110 ALA A O     1 
ATOM   809  C  CB    . ALA A 1 110 ? 2.978   4.486   20.870  1.00 36.45  ?  110 ALA A CB    1 
ATOM   810  N  N     . ASP A 1 111 ? 4.882   3.070   22.910  1.00 31.95  ?  111 ASP A N     1 
ATOM   811  C  CA    . ASP A 1 111 ? 6.265   3.046   23.398  1.00 29.71  ?  111 ASP A CA    1 
ATOM   812  C  C     . ASP A 1 111 ? 7.273   2.915   22.268  1.00 31.23  ?  111 ASP A C     1 
ATOM   813  O  O     . ASP A 1 111 ? 8.492   3.047   22.498  1.00 27.50  ?  111 ASP A O     1 
ATOM   814  C  CB    . ASP A 1 111 ? 6.475   1.892   24.397  1.00 26.50  ?  111 ASP A CB    1 
ATOM   815  C  CG    . ASP A 1 111 ? 5.459   1.922   25.578  1.00 32.49  ?  111 ASP A CG    1 
ATOM   816  O  OD1   . ASP A 1 111 ? 5.236   2.995   26.176  1.00 30.81  ?  111 ASP A OD1   1 
ATOM   817  O  OD2   . ASP A 1 111 ? 4.889   0.861   25.916  1.00 27.30  ?  111 ASP A OD2   1 
ATOM   818  N  N     . PHE A 1 112 ? 6.794   2.688   21.051  1.00 31.32  ?  112 PHE A N     1 
ATOM   819  C  CA    . PHE A 1 112 ? 7.627   2.211   19.965  1.00 29.63  ?  112 PHE A CA    1 
ATOM   820  C  C     . PHE A 1 112 ? 6.852   2.399   18.667  1.00 28.67  ?  112 PHE A C     1 
ATOM   821  O  O     . PHE A 1 112 ? 5.791   1.787   18.463  1.00 27.54  ?  112 PHE A O     1 
ATOM   822  C  CB    . PHE A 1 112 ? 7.983   0.745   20.227  1.00 29.73  ?  112 PHE A CB    1 
ATOM   823  C  CG    . PHE A 1 112 ? 8.995   0.165   19.287  1.00 31.13  ?  112 PHE A CG    1 
ATOM   824  C  CD1   . PHE A 1 112 ? 8.710   0.004   17.921  1.00 31.09  ?  112 PHE A CD1   1 
ATOM   825  C  CD2   . PHE A 1 112 ? 10.222  -0.293  19.779  1.00 30.49  ?  112 PHE A CD2   1 
ATOM   826  C  CE1   . PHE A 1 112 ? 9.665   -0.591  17.044  1.00 31.43  ?  112 PHE A CE1   1 
ATOM   827  C  CE2   . PHE A 1 112 ? 11.167  -0.878  18.920  1.00 39.29  ?  112 PHE A CE2   1 
ATOM   828  C  CZ    . PHE A 1 112 ? 10.886  -1.037  17.546  1.00 32.98  ?  112 PHE A CZ    1 
ATOM   829  N  N     . VAL A 1 113 ? 7.358   3.274   17.809  1.00 27.69  ?  113 VAL A N     1 
ATOM   830  C  CA    . VAL A 1 113 ? 6.778   3.555   16.503  1.00 30.39  ?  113 VAL A CA    1 
ATOM   831  C  C     . VAL A 1 113 ? 7.825   3.194   15.447  1.00 31.55  ?  113 VAL A C     1 
ATOM   832  O  O     . VAL A 1 113 ? 9.008   3.530   15.596  1.00 27.84  ?  113 VAL A O     1 
ATOM   833  C  CB    . VAL A 1 113 ? 6.359   5.037   16.402  1.00 30.51  ?  113 VAL A CB    1 
ATOM   834  C  CG1   . VAL A 1 113 ? 5.631   5.359   15.080  1.00 25.79  ?  113 VAL A CG1   1 
ATOM   835  C  CG2   . VAL A 1 113 ? 5.521   5.409   17.596  1.00 27.23  ?  113 VAL A CG2   1 
ATOM   836  N  N     . TYR A 1 114 ? 7.409   2.474   14.410  1.00 29.10  ?  114 TYR A N     1 
ATOM   837  C  CA    . TYR A 1 114 ? 8.214   2.370   13.205  1.00 32.56  ?  114 TYR A CA    1 
ATOM   838  C  C     . TYR A 1 114 ? 7.435   2.987   12.053  1.00 35.36  ?  114 TYR A C     1 
ATOM   839  O  O     . TYR A 1 114 ? 6.199   2.876   11.998  1.00 28.84  ?  114 TYR A O     1 
ATOM   840  C  CB    . TYR A 1 114 ? 8.614   0.921   12.885  1.00 30.97  ?  114 TYR A CB    1 
ATOM   841  C  CG    . TYR A 1 114 ? 7.472   -0.000  12.522  1.00 35.76  ?  114 TYR A CG    1 
ATOM   842  C  CD1   . TYR A 1 114 ? 6.632   -0.518  13.514  1.00 30.52  ?  114 TYR A CD1   1 
ATOM   843  C  CD2   . TYR A 1 114 ? 7.239   -0.371  11.190  1.00 33.77  ?  114 TYR A CD2   1 
ATOM   844  C  CE1   . TYR A 1 114 ? 5.609   -1.366  13.210  1.00 32.55  ?  114 TYR A CE1   1 
ATOM   845  C  CE2   . TYR A 1 114 ? 6.212   -1.229  10.870  1.00 32.30  ?  114 TYR A CE2   1 
ATOM   846  C  CZ    . TYR A 1 114 ? 5.382   -1.716  11.887  1.00 35.29  ?  114 TYR A CZ    1 
ATOM   847  O  OH    . TYR A 1 114 ? 4.333   -2.564  11.595  1.00 27.19  ?  114 TYR A OH    1 
ATOM   848  N  N     . VAL A 1 115 ? 8.162   3.657   11.139  1.00 32.50  ?  115 VAL A N     1 
ATOM   849  C  CA    . VAL A 1 115 ? 7.481   4.323   10.032  1.00 35.03  ?  115 VAL A CA    1 
ATOM   850  C  C     . VAL A 1 115 ? 7.735   3.536   8.759   1.00 31.94  ?  115 VAL A C     1 
ATOM   851  O  O     . VAL A 1 115 ? 8.330   2.461   8.801   1.00 32.27  ?  115 VAL A O     1 
ATOM   852  C  CB    . VAL A 1 115 ? 7.904   5.792   9.865   1.00 31.01  ?  115 VAL A CB    1 
ATOM   853  C  CG1   . VAL A 1 115 ? 7.520   6.588   11.101  1.00 30.01  ?  115 VAL A CG1   1 
ATOM   854  C  CG2   . VAL A 1 115 ? 9.373   5.876   9.565   1.00 28.76  ?  115 VAL A CG2   1 
ATOM   855  N  N     . ASN A 1 116 ? 7.224   4.030   7.641   1.00 33.41  ?  116 ASN A N     1 
ATOM   856  C  CA    . ASN A 1 116 ? 7.460   3.374   6.364   1.00 41.03  ?  116 ASN A CA    1 
ATOM   857  C  C     . ASN A 1 116 ? 8.928   3.535   5.958   1.00 38.10  ?  116 ASN A C     1 
ATOM   858  O  O     . ASN A 1 116 ? 9.596   4.490   6.359   1.00 33.62  ?  116 ASN A O     1 
ATOM   859  C  CB    . ASN A 1 116 ? 6.537   3.976   5.301   1.00 41.62  ?  116 ASN A CB    1 
ATOM   860  C  CG    . ASN A 1 116 ? 5.188   3.298   5.243   1.00 38.76  ?  116 ASN A CG    1 
ATOM   861  O  OD1   . ASN A 1 116 ? 4.949   2.295   5.910   1.00 40.19  ?  116 ASN A OD1   1 
ATOM   862  N  ND2   . ASN A 1 116 ? 4.302   3.842   4.441   1.00 41.83  ?  116 ASN A ND2   1 
ATOM   863  N  N     . ILE A 1 117 ? 9.428   2.584   5.166   1.00 37.62  ?  117 ILE A N     1 
ATOM   864  C  CA    . ILE A 1 117 ? 10.793  2.614   4.650   1.00 36.62  ?  117 ILE A CA    1 
ATOM   865  C  C     . ILE A 1 117 ? 10.757  2.580   3.124   1.00 40.19  ?  117 ILE A C     1 
ATOM   866  O  O     . ILE A 1 117 ? 10.142  1.688   2.531   1.00 41.32  ?  117 ILE A O     1 
ATOM   867  C  CB    . ILE A 1 117 ? 11.635  1.438   5.181   1.00 42.76  ?  117 ILE A CB    1 
ATOM   868  C  CG1   . ILE A 1 117 ? 11.975  1.624   6.671   1.00 39.43  ?  117 ILE A CG1   1 
ATOM   869  C  CG2   . ILE A 1 117 ? 12.900  1.264   4.327   1.00 36.08  ?  117 ILE A CG2   1 
ATOM   870  C  CD1   . ILE A 1 117 ? 12.283  0.309   7.437   1.00 31.46  ?  117 ILE A CD1   1 
ATOM   871  N  N     . ASN A 1 118 ? 11.439  3.527   2.489   1.00 39.64  ?  118 ASN A N     1 
ATOM   872  C  CA    . ASN A 1 118 ? 11.710  3.467   1.057   1.00 41.99  ?  118 ASN A CA    1 
ATOM   873  C  C     . ASN A 1 118 ? 13.124  2.917   0.843   1.00 42.86  ?  118 ASN A C     1 
ATOM   874  O  O     . ASN A 1 118 ? 14.111  3.527   1.279   1.00 39.67  ?  118 ASN A O     1 
ATOM   875  C  CB    . ASN A 1 118 ? 11.581  4.849   0.416   1.00 41.49  ?  118 ASN A CB    1 
ATOM   876  C  CG    . ASN A 1 118 ? 10.170  5.385   0.425   1.00 43.65  ?  118 ASN A CG    1 
ATOM   877  O  OD1   . ASN A 1 118 ? 9.227   4.713   0.017   1.00 46.30  ?  118 ASN A OD1   1 
ATOM   878  N  ND2   . ASN A 1 118 ? 10.021  6.618   0.871   1.00 42.44  ?  118 ASN A ND2   1 
ATOM   879  N  N     . ILE A 1 119 ? 13.239  1.780   0.168   1.00 43.33  ?  119 ILE A N     1 
ATOM   880  C  CA    . ILE A 1 119 ? 14.567  1.244   -0.120  1.00 43.56  ?  119 ILE A CA    1 
ATOM   881  C  C     . ILE A 1 119 ? 15.117  2.010   -1.315  1.00 44.73  ?  119 ILE A C     1 
ATOM   882  O  O     . ILE A 1 119 ? 14.669  1.822   -2.451  1.00 42.50  ?  119 ILE A O     1 
ATOM   883  C  CB    . ILE A 1 119 ? 14.544  -0.263  -0.378  1.00 47.01  ?  119 ILE A CB    1 
ATOM   884  C  CG1   . ILE A 1 119 ? 14.084  -1.009  0.879   1.00 47.77  ?  119 ILE A CG1   1 
ATOM   885  C  CG2   . ILE A 1 119 ? 15.908  -0.717  -0.780  1.00 45.23  ?  119 ILE A CG2   1 
ATOM   886  C  CD1   . ILE A 1 119 ? 14.931  -0.707  2.094   1.00 43.88  ?  119 ILE A CD1   1 
ATOM   887  N  N     . ALA A 1 120 ? 16.074  2.890   -1.046  1.00 42.88  ?  120 ALA A N     1 
ATOM   888  C  CA    . ALA A 1 120 ? 16.568  3.852   -2.018  1.00 52.43  ?  120 ALA A CA    1 
ATOM   889  C  C     . ALA A 1 120 ? 17.815  3.283   -2.686  1.00 54.08  ?  120 ALA A C     1 
ATOM   890  O  O     . ALA A 1 120 ? 18.810  2.951   -2.020  1.00 44.27  ?  120 ALA A O     1 
ATOM   891  C  CB    . ALA A 1 120 ? 16.856  5.205   -1.362  1.00 52.80  ?  120 ALA A CB    1 
ATOM   892  N  N     . ARG A 1 121 ? 17.723  3.124   -3.993  1.00 59.30  ?  121 ARG A N     1 
ATOM   893  C  CA    . ARG A 1 121 ? 18.818  2.671   -4.823  1.00 62.62  ?  121 ARG A CA    1 
ATOM   894  C  C     . ARG A 1 121 ? 19.604  3.840   -5.399  1.00 65.15  ?  121 ARG A C     1 
ATOM   895  O  O     . ARG A 1 121 ? 20.470  3.635   -6.253  1.00 74.54  ?  121 ARG A O     1 
ATOM   896  C  CB    . ARG A 1 121 ? 18.269  1.773   -5.936  1.00 62.13  ?  121 ARG A CB    1 
ATOM   897  N  N     . THR A 1 122 ? 19.292  5.063   -4.968  1.00 63.06  ?  122 THR A N     1 
ATOM   898  C  CA    . THR A 1 122 ? 20.054  6.266   -5.273  1.00 61.86  ?  122 THR A CA    1 
ATOM   899  C  C     . THR A 1 122 ? 20.245  7.060   -3.991  1.00 62.45  ?  122 THR A C     1 
ATOM   900  O  O     . THR A 1 122 ? 19.344  7.099   -3.152  1.00 63.30  ?  122 THR A O     1 
ATOM   901  C  CB    . THR A 1 122 ? 19.346  7.142   -6.309  1.00 66.64  ?  122 THR A CB    1 
ATOM   902  O  OG1   . THR A 1 122 ? 18.266  7.843   -5.675  1.00 68.37  ?  122 THR A OG1   1 
ATOM   903  C  CG2   . THR A 1 122 ? 18.826  6.308   -7.471  1.00 67.51  ?  122 THR A CG2   1 
ATOM   904  N  N     . ARG A 1 123 ? 21.411  7.688   -3.832  1.00 67.47  ?  123 ARG A N     1 
ATOM   905  C  CA    . ARG A 1 123 ? 21.638  8.528   -2.660  1.00 64.02  ?  123 ARG A CA    1 
ATOM   906  C  C     . ARG A 1 123 ? 20.709  9.741   -2.715  1.00 64.07  ?  123 ARG A C     1 
ATOM   907  O  O     . ARG A 1 123 ? 20.427  10.278  -3.791  1.00 59.21  ?  123 ARG A O     1 
ATOM   908  C  CB    . ARG A 1 123 ? 23.108  8.964   -2.573  1.00 58.05  ?  123 ARG A CB    1 
ATOM   909  C  CG    . ARG A 1 123 ? 23.916  8.232   -1.514  1.00 59.87  ?  123 ARG A CG    1 
ATOM   910  C  CD    . ARG A 1 123 ? 23.745  6.735   -1.731  1.00 68.91  ?  123 ARG A CD    1 
ATOM   911  N  NE    . ARG A 1 123 ? 24.139  5.906   -0.595  1.00 73.61  ?  123 ARG A NE    1 
ATOM   912  C  CZ    . ARG A 1 123 ? 23.792  4.630   -0.450  1.00 65.66  ?  123 ARG A CZ    1 
ATOM   913  N  NH1   . ARG A 1 123 ? 22.988  4.027   -1.313  1.00 59.68  ?  123 ARG A NH1   1 
ATOM   914  N  NH2   . ARG A 1 123 ? 24.242  3.946   0.600   1.00 64.87  ?  123 ARG A NH2   1 
ATOM   915  N  N     . VAL A 1 124 ? 20.201  10.154  -1.553  1.00 62.53  ?  124 VAL A N     1 
ATOM   916  C  CA    . VAL A 1 124 ? 19.256  11.257  -1.458  1.00 55.89  ?  124 VAL A CA    1 
ATOM   917  C  C     . VAL A 1 124 ? 19.579  12.083  -0.220  1.00 55.42  ?  124 VAL A C     1 
ATOM   918  O  O     . VAL A 1 124 ? 20.481  11.762  0.550   1.00 53.39  ?  124 VAL A O     1 
ATOM   919  C  CB    . VAL A 1 124 ? 17.794  10.772  -1.417  1.00 64.95  ?  124 VAL A CB    1 
ATOM   920  C  CG1   . VAL A 1 124 ? 17.315  10.497  -2.816  1.00 66.28  ?  124 VAL A CG1   1 
ATOM   921  C  CG2   . VAL A 1 124 ? 17.674  9.516   -0.556  1.00 57.80  ?  124 VAL A CG2   1 
ATOM   922  N  N     . THR A 1 125 ? 18.835  13.170  -0.049  1.00 60.26  ?  125 THR A N     1 
ATOM   923  C  CA    . THR A 1 125 ? 18.860  14.015  1.135   1.00 55.69  ?  125 THR A CA    1 
ATOM   924  C  C     . THR A 1 125 ? 17.494  13.976  1.828   1.00 53.68  ?  125 THR A C     1 
ATOM   925  O  O     . THR A 1 125 ? 16.539  13.352  1.344   1.00 52.05  ?  125 THR A O     1 
ATOM   926  C  CB    . THR A 1 125 ? 19.264  15.442  0.749   1.00 55.93  ?  125 THR A CB    1 
ATOM   927  O  OG1   . THR A 1 125 ? 18.110  16.174  0.318   1.00 57.96  ?  125 THR A OG1   1 
ATOM   928  C  CG2   . THR A 1 125 ? 20.275  15.385  -0.393  1.00 47.83  ?  125 THR A CG2   1 
ATOM   929  N  N     . GLY A 1 126 ? 17.419  14.639  2.989   1.00 53.22  ?  126 GLY A N     1 
ATOM   930  C  CA    . GLY A 1 126 ? 16.209  14.576  3.804   1.00 47.70  ?  126 GLY A CA    1 
ATOM   931  C  C     . GLY A 1 126 ? 14.982  15.204  3.153   1.00 53.84  ?  126 GLY A C     1 
ATOM   932  O  O     . GLY A 1 126 ? 13.864  14.669  3.263   1.00 49.37  ?  126 GLY A O     1 
ATOM   933  N  N     . THR A 1 127 ? 15.169  16.347  2.472   1.00 55.93  ?  127 THR A N     1 
ATOM   934  C  CA    . THR A 1 127 ? 14.118  17.103  1.787   1.00 56.61  ?  127 THR A CA    1 
ATOM   935  C  C     . THR A 1 127 ? 13.846  16.623  0.359   1.00 60.68  ?  127 THR A C     1 
ATOM   936  O  O     . THR A 1 127 ? 13.023  17.228  -0.343  1.00 67.86  ?  127 THR A O     1 
ATOM   937  C  CB    . THR A 1 127 ? 14.489  18.589  1.727   1.00 56.30  ?  127 THR A CB    1 
ATOM   938  O  OG1   . THR A 1 127 ? 15.697  18.721  0.969   1.00 64.57  ?  127 THR A OG1   1 
ATOM   939  C  CG2   . THR A 1 127 ? 14.686  19.186  3.119   1.00 54.79  ?  127 THR A CG2   1 
ATOM   940  N  N     . THR A 1 128 ? 14.531  15.576  -0.096  1.00 61.62  ?  128 THR A N     1 
ATOM   941  C  CA    . THR A 1 128 ? 14.432  15.081  -1.467  1.00 66.46  ?  128 THR A CA    1 
ATOM   942  C  C     . THR A 1 128 ? 14.281  13.560  -1.478  1.00 63.01  ?  128 THR A C     1 
ATOM   943  O  O     . THR A 1 128 ? 14.732  12.894  -2.419  1.00 64.28  ?  128 THR A O     1 
ATOM   944  C  CB    . THR A 1 128 ? 15.649  15.516  -2.309  1.00 66.04  ?  128 THR A CB    1 
ATOM   945  O  OG1   . THR A 1 128 ? 16.810  14.751  -1.947  1.00 65.84  ?  128 THR A OG1   1 
ATOM   946  C  CG2   . THR A 1 128 ? 15.968  17.014  -2.120  1.00 63.78  ?  128 THR A CG2   1 
ATOM   947  N  N     . ILE A 1 129 ? 13.685  13.001  -0.415  1.00 59.65  ?  129 ILE A N     1 
ATOM   948  C  CA    . ILE A 1 129 ? 13.407  11.565  -0.364  1.00 59.34  ?  129 ILE A CA    1 
ATOM   949  C  C     . ILE A 1 129 ? 12.568  11.152  -1.567  1.00 63.60  ?  129 ILE A C     1 
ATOM   950  O  O     . ILE A 1 129 ? 12.909  10.208  -2.286  1.00 56.84  ?  129 ILE A O     1 
ATOM   951  C  CB    . ILE A 1 129 ? 12.725  11.189  0.969   1.00 57.01  ?  129 ILE A CB    1 
ATOM   952  C  CG1   . ILE A 1 129 ? 13.774  10.827  2.026   1.00 54.20  ?  129 ILE A CG1   1 
ATOM   953  C  CG2   . ILE A 1 129 ? 11.787  10.015  0.798   1.00 51.86  ?  129 ILE A CG2   1 
ATOM   954  C  CD1   . ILE A 1 129 ? 13.217  10.671  3.416   1.00 45.79  ?  129 ILE A CD1   1 
ATOM   955  N  N     . ALA A 1 130 ? 11.480  11.887  -1.829  1.00 70.29  ?  130 ALA A N     1 
ATOM   956  C  CA    . ALA A 1 130 ? 10.590  11.617  -2.959  1.00 68.13  ?  130 ALA A CA    1 
ATOM   957  C  C     . ALA A 1 130 ? 11.152  12.109  -4.291  1.00 70.88  ?  130 ALA A C     1 
ATOM   958  O  O     . ALA A 1 130 ? 10.397  12.575  -5.151  1.00 73.78  ?  130 ALA A O     1 
ATOM   959  C  CB    . ALA A 1 130 ? 9.221   12.237  -2.690  1.00 71.74  ?  130 ALA A CB    1 
ATOM   960  N  N     . ASP A 1 131 ? 12.475  12.030  -4.482  1.00 69.31  ?  131 ASP A N     1 
ATOM   961  C  CA    . ASP A 1 131 ? 13.109  12.212  -5.787  1.00 70.61  ?  131 ASP A CA    1 
ATOM   962  C  C     . ASP A 1 131 ? 14.137  11.114  -6.041  1.00 72.44  ?  131 ASP A C     1 
ATOM   963  O  O     . ASP A 1 131 ? 15.131  11.344  -6.730  1.00 74.14  ?  131 ASP A O     1 
ATOM   964  C  CB    . ASP A 1 131 ? 13.763  13.593  -5.911  1.00 68.25  ?  131 ASP A CB    1 
ATOM   965  N  N     . ALA A 1 132 ? 13.905  9.911   -5.500  1.00 69.47  ?  132 ALA A N     1 
ATOM   966  C  CA    . ALA A 1 132 ? 14.851  8.807   -5.562  1.00 66.49  ?  132 ALA A CA    1 
ATOM   967  C  C     . ALA A 1 132 ? 14.266  7.644   -6.349  1.00 68.54  ?  132 ALA A C     1 
ATOM   968  O  O     . ALA A 1 132 ? 13.052  7.432   -6.356  1.00 65.46  ?  132 ALA A O     1 
ATOM   969  C  CB    . ALA A 1 132 ? 15.220  8.303   -4.166  1.00 63.12  ?  132 ALA A CB    1 
ATOM   970  N  N     . GLU A 1 133 ? 15.147  6.876   -6.994  1.00 73.57  ?  133 GLU A N     1 
ATOM   971  C  CA    . GLU A 1 133 ? 14.757  5.619   -7.636  1.00 72.68  ?  133 GLU A CA    1 
ATOM   972  C  C     . GLU A 1 133 ? 14.468  4.612   -6.528  1.00 68.08  ?  133 GLU A C     1 
ATOM   973  O  O     . GLU A 1 133 ? 15.380  4.001   -5.966  1.00 65.36  ?  133 GLU A O     1 
ATOM   974  C  CB    . GLU A 1 133 ? 15.844  5.120   -8.589  1.00 65.75  ?  133 GLU A CB    1 
ATOM   975  N  N     . VAL A 1 134 ? 13.195  4.457   -6.187  1.00 67.79  ?  134 VAL A N     1 
ATOM   976  C  CA    . VAL A 1 134 ? 12.806  3.659   -5.036  1.00 57.31  ?  134 VAL A CA    1 
ATOM   977  C  C     . VAL A 1 134 ? 12.640  2.228   -5.496  1.00 57.34  ?  134 VAL A C     1 
ATOM   978  O  O     . VAL A 1 134 ? 11.789  1.928   -6.339  1.00 62.20  ?  134 VAL A O     1 
ATOM   979  C  CB    . VAL A 1 134 ? 11.526  4.197   -4.388  1.00 60.20  ?  134 VAL A CB    1 
ATOM   980  C  CG1   . VAL A 1 134 ? 10.876  3.132   -3.510  1.00 55.44  ?  134 VAL A CG1   1 
ATOM   981  C  CG2   . VAL A 1 134 ? 11.877  5.433   -3.579  1.00 58.80  ?  134 VAL A CG2   1 
ATOM   982  N  N     . LEU A 1 135 ? 13.456  1.344   -4.940  1.00 56.69  ?  135 LEU A N     1 
ATOM   983  C  CA    . LEU A 1 135 ? 13.444  -0.038  -5.388  1.00 60.45  ?  135 LEU A CA    1 
ATOM   984  C  C     . LEU A 1 135 ? 12.311  -0.817  -4.726  1.00 57.23  ?  135 LEU A C     1 
ATOM   985  O  O     . LEU A 1 135 ? 11.518  -1.475  -5.411  1.00 62.22  ?  135 LEU A O     1 
ATOM   986  C  CB    . LEU A 1 135 ? 14.817  -0.670  -5.124  1.00 59.74  ?  135 LEU A CB    1 
ATOM   987  N  N     . VAL A 1 136 ? 12.204  -0.753  -3.394  1.00 56.26  ?  136 VAL A N     1 
ATOM   988  C  CA    . VAL A 1 136 ? 11.091  -1.375  -2.683  1.00 55.69  ?  136 VAL A CA    1 
ATOM   989  C  C     . VAL A 1 136 ? 10.652  -0.469  -1.533  1.00 50.96  ?  136 VAL A C     1 
ATOM   990  O  O     . VAL A 1 136 ? 11.382  0.422   -1.090  1.00 47.43  ?  136 VAL A O     1 
ATOM   991  C  CB    . VAL A 1 136 ? 11.418  -2.792  -2.140  1.00 54.39  ?  136 VAL A CB    1 
ATOM   992  C  CG1   . VAL A 1 136 ? 10.138  -3.567  -1.913  1.00 62.43  ?  136 VAL A CG1   1 
ATOM   993  C  CG2   . VAL A 1 136 ? 12.329  -3.563  -3.072  1.00 59.76  ?  136 VAL A CG2   1 
ATOM   994  N  N     . ARG A 1 137 ? 9.435   -0.713  -1.051  1.00 48.65  ?  137 ARG A N     1 
ATOM   995  C  CA    . ARG A 1 137 ? 8.867   0.003   0.088   1.00 48.73  ?  137 ARG A CA    1 
ATOM   996  C  C     . ARG A 1 137 ? 8.427   -1.014  1.126   1.00 45.35  ?  137 ARG A C     1 
ATOM   997  O  O     . ARG A 1 137 ? 7.561   -1.843  0.840   1.00 46.70  ?  137 ARG A O     1 
ATOM   998  C  CB    . ARG A 1 137 ? 7.673   0.859   -0.333  1.00 43.35  ?  137 ARG A CB    1 
ATOM   999  C  CG    . ARG A 1 137 ? 8.062   2.095   -1.095  1.00 52.71  ?  137 ARG A CG    1 
ATOM   1000 C  CD    . ARG A 1 137 ? 6.835   2.920   -1.415  1.00 57.81  ?  137 ARG A CD    1 
ATOM   1001 N  NE    . ARG A 1 137 ? 6.648   3.023   -2.853  1.00 60.36  ?  137 ARG A NE    1 
ATOM   1002 C  CZ    . ARG A 1 137 ? 7.080   4.033   -3.594  1.00 63.95  ?  137 ARG A CZ    1 
ATOM   1003 N  NH1   . ARG A 1 137 ? 7.728   5.061   -3.059  1.00 63.41  ?  137 ARG A NH1   1 
ATOM   1004 N  NH2   . ARG A 1 137 ? 6.847   4.020   -4.905  1.00 67.03  ?  137 ARG A NH2   1 
ATOM   1005 N  N     . LEU A 1 138 ? 8.999   -0.940  2.329   1.00 42.83  ?  138 LEU A N     1 
ATOM   1006 C  CA    . LEU A 1 138 ? 8.562   -1.774  3.452   1.00 44.01  ?  138 LEU A CA    1 
ATOM   1007 C  C     . LEU A 1 138 ? 7.478   -1.017  4.215   1.00 41.15  ?  138 LEU A C     1 
ATOM   1008 O  O     . LEU A 1 138 ? 7.753   0.012   4.842   1.00 45.65  ?  138 LEU A O     1 
ATOM   1009 C  CB    . LEU A 1 138 ? 9.732   -2.117  4.376   1.00 41.62  ?  138 LEU A CB    1 
ATOM   1010 C  CG    . LEU A 1 138 ? 10.988  -2.785  3.810   1.00 43.40  ?  138 LEU A CG    1 
ATOM   1011 C  CD1   . LEU A 1 138 ? 11.993  -3.020  4.923   1.00 38.88  ?  138 LEU A CD1   1 
ATOM   1012 C  CD2   . LEU A 1 138 ? 10.640  -4.073  3.143   1.00 40.50  ?  138 LEU A CD2   1 
ATOM   1013 N  N     . GLU A 1 139 ? 6.244   -1.509  4.158   1.00 36.33  ?  139 GLU A N     1 
ATOM   1014 C  CA    . GLU A 1 139 ? 5.147   -0.799  4.803   1.00 38.06  ?  139 GLU A CA    1 
ATOM   1015 C  C     . GLU A 1 139 ? 4.188   -1.743  5.528   1.00 35.70  ?  139 GLU A C     1 
ATOM   1016 O  O     . GLU A 1 139 ? 2.996   -1.456  5.607   1.00 37.78  ?  139 GLU A O     1 
ATOM   1017 C  CB    . GLU A 1 139 ? 4.345   0.040   3.794   1.00 38.64  ?  139 GLU A CB    1 
ATOM   1018 C  CG    . GLU A 1 139 ? 5.096   0.480   2.549   1.00 42.64  ?  139 GLU A CG    1 
ATOM   1019 C  CD    . GLU A 1 139 ? 4.241   1.306   1.577   1.00 51.76  ?  139 GLU A CD    1 
ATOM   1020 O  OE1   . GLU A 1 139 ? 3.005   1.032   1.485   1.00 52.03  ?  139 GLU A OE1   1 
ATOM   1021 O  OE2   . GLU A 1 139 ? 4.814   2.212   0.902   1.00 48.84  ?  139 GLU A OE2   1 
ATOM   1022 N  N     . PHE A 1 140 ? 4.673   -2.855  6.065   1.00 36.52  ?  140 PHE A N     1 
ATOM   1023 C  CA    . PHE A 1 140 ? 3.783   -3.871  6.641   1.00 37.14  ?  140 PHE A CA    1 
ATOM   1024 C  C     . PHE A 1 140 ? 3.165   -3.387  7.945   1.00 39.41  ?  140 PHE A C     1 
ATOM   1025 O  O     . PHE A 1 140 ? 3.902   -3.007  8.860   1.00 40.12  ?  140 PHE A O     1 
ATOM   1026 C  CB    . PHE A 1 140 ? 4.558   -5.147  6.887   1.00 35.23  ?  140 PHE A CB    1 
ATOM   1027 C  CG    . PHE A 1 140 ? 5.122   -5.744  5.642   1.00 33.11  ?  140 PHE A CG    1 
ATOM   1028 C  CD1   . PHE A 1 140 ? 4.310   -6.451  4.777   1.00 33.94  ?  140 PHE A CD1   1 
ATOM   1029 C  CD2   . PHE A 1 140 ? 6.466   -5.586  5.331   1.00 34.51  ?  140 PHE A CD2   1 
ATOM   1030 C  CE1   . PHE A 1 140 ? 4.816   -7.000  3.617   1.00 37.74  ?  140 PHE A CE1   1 
ATOM   1031 C  CE2   . PHE A 1 140 ? 6.994   -6.129  4.172   1.00 39.43  ?  140 PHE A CE2   1 
ATOM   1032 C  CZ    . PHE A 1 140 ? 6.168   -6.854  3.312   1.00 42.58  ?  140 PHE A CZ    1 
ATOM   1033 N  N     . PRO A 1 141 ? 1.843   -3.384  8.082   1.00 36.31  ?  141 PRO A N     1 
ATOM   1034 C  CA    . PRO A 1 141 ? 1.247   -3.032  9.372   1.00 31.65  ?  141 PRO A CA    1 
ATOM   1035 C  C     . PRO A 1 141 ? 1.534   -4.100  10.404  1.00 35.06  ?  141 PRO A C     1 
ATOM   1036 O  O     . PRO A 1 141 ? 1.937   -5.226  10.100  1.00 36.46  ?  141 PRO A O     1 
ATOM   1037 C  CB    . PRO A 1 141 ? -0.255  -2.947  9.085   1.00 36.49  ?  141 PRO A CB    1 
ATOM   1038 C  CG    . PRO A 1 141 ? -0.413  -3.229  7.620   1.00 40.06  ?  141 PRO A CG    1 
ATOM   1039 C  CD    . PRO A 1 141 ? 0.850   -3.808  7.092   1.00 39.49  ?  141 PRO A CD    1 
ATOM   1040 N  N     . TYR A 1 142 ? 1.312   -3.724  11.656  1.00 35.92  ?  142 TYR A N     1 
ATOM   1041 C  CA    . TYR A 1 142 ? 1.585   -4.586  12.797  1.00 36.64  ?  142 TYR A CA    1 
ATOM   1042 C  C     . TYR A 1 142 ? 0.406   -5.501  13.148  1.00 39.20  ?  142 TYR A C     1 
ATOM   1043 O  O     . TYR A 1 142 ? 0.201   -5.822  14.330  1.00 33.45  ?  142 TYR A O     1 
ATOM   1044 C  CB    . TYR A 1 142 ? 1.940   -3.723  14.007  1.00 33.82  ?  142 TYR A CB    1 
ATOM   1045 C  CG    . TYR A 1 142 ? 2.880   -4.396  14.948  1.00 34.39  ?  142 TYR A CG    1 
ATOM   1046 C  CD1   . TYR A 1 142 ? 4.159   -4.715  14.535  1.00 30.69  ?  142 TYR A CD1   1 
ATOM   1047 C  CD2   . TYR A 1 142 ? 2.487   -4.739  16.247  1.00 30.06  ?  142 TYR A CD2   1 
ATOM   1048 C  CE1   . TYR A 1 142 ? 5.031   -5.336  15.384  1.00 26.52  ?  142 TYR A CE1   1 
ATOM   1049 C  CE2   . TYR A 1 142 ? 3.359   -5.369  17.104  1.00 29.05  ?  142 TYR A CE2   1 
ATOM   1050 C  CZ    . TYR A 1 142 ? 4.641   -5.665  16.654  1.00 28.39  ?  142 TYR A CZ    1 
ATOM   1051 O  OH    . TYR A 1 142 ? 5.555   -6.284  17.478  1.00 33.85  ?  142 TYR A OH    1 
ATOM   1052 N  N     . ASP A 1 143 ? -0.390  -5.923  12.172  1.00 35.21  ?  143 ASP A N     1 
ATOM   1053 C  CA    . ASP A 1 143 ? -1.618  -6.609  12.541  1.00 38.95  ?  143 ASP A CA    1 
ATOM   1054 C  C     . ASP A 1 143 ? -1.456  -8.105  12.593  1.00 36.23  ?  143 ASP A C     1 
ATOM   1055 O  O     . ASP A 1 143 ? -2.373  -8.776  13.069  1.00 39.82  ?  143 ASP A O     1 
ATOM   1056 C  CB    . ASP A 1 143 ? -2.760  -6.277  11.575  1.00 32.74  ?  143 ASP A CB    1 
ATOM   1057 C  CG    . ASP A 1 143 ? -2.363  -6.436  10.121  1.00 41.80  ?  143 ASP A CG    1 
ATOM   1058 O  OD1   . ASP A 1 143 ? -1.171  -6.705  9.813   1.00 40.59  ?  143 ASP A OD1   1 
ATOM   1059 O  OD2   . ASP A 1 143 ? -3.256  -6.280  9.273   1.00 48.62  ?  143 ASP A OD2   1 
ATOM   1060 N  N     . ARG A 1 144 ? -0.302  -8.635  12.172  1.00 35.08  ?  144 ARG A N     1 
ATOM   1061 C  CA    . ARG A 1 144 ? -0.170  -10.073 11.966  1.00 36.02  ?  144 ARG A CA    1 
ATOM   1062 C  C     . ARG A 1 144 ? 0.996   -10.780 12.634  1.00 32.35  ?  144 ARG A C     1 
ATOM   1063 O  O     . ARG A 1 144 ? 1.170   -11.980 12.374  1.00 32.74  ?  144 ARG A O     1 
ATOM   1064 C  CB    . ARG A 1 144 ? -0.053  -10.377 10.478  1.00 37.42  ?  144 ARG A CB    1 
ATOM   1065 C  CG    . ARG A 1 144 ? -1.339  -10.647 9.840   1.00 39.16  ?  144 ARG A CG    1 
ATOM   1066 C  CD    . ARG A 1 144 ? -1.113  -10.637 8.384   1.00 39.59  ?  144 ARG A CD    1 
ATOM   1067 N  NE    . ARG A 1 144 ? -2.146  -9.829  7.772   1.00 39.99  ?  144 ARG A NE    1 
ATOM   1068 C  CZ    . ARG A 1 144 ? -2.603  -10.023 6.547   1.00 45.67  ?  144 ARG A CZ    1 
ATOM   1069 N  NH1   . ARG A 1 144 ? -2.067  -10.933 5.749   1.00 46.45  ?  144 ARG A NH1   1 
ATOM   1070 N  NH2   . ARG A 1 144 ? -3.620  -9.283  6.111   1.00 48.45  ?  144 ARG A NH2   1 
ATOM   1071 N  N     . GLY A 1 145 ? 1.825   -10.094 13.422  1.00 31.64  ?  145 GLY A N     1 
ATOM   1072 C  CA    . GLY A 1 145 ? 3.010   -10.755 13.976  1.00 36.14  ?  145 GLY A CA    1 
ATOM   1073 C  C     . GLY A 1 145 ? 4.135   -11.085 12.983  1.00 33.59  ?  145 GLY A C     1 
ATOM   1074 O  O     . GLY A 1 145 ? 4.945   -11.989 13.242  1.00 28.65  ?  145 GLY A O     1 
ATOM   1075 N  N     . LEU A 1 146 ? 4.192   -10.388 11.845  1.00 30.19  ?  146 LEU A N     1 
ATOM   1076 C  CA    . LEU A 1 146 ? 5.319   -10.523 10.916  1.00 37.81  ?  146 LEU A CA    1 
ATOM   1077 C  C     . LEU A 1 146 ? 6.659   -10.396 11.635  1.00 32.48  ?  146 LEU A C     1 
ATOM   1078 O  O     . LEU A 1 146 ? 7.556   -11.219 11.440  1.00 34.11  ?  146 LEU A O     1 
ATOM   1079 C  CB    . LEU A 1 146 ? 5.220   -9.469  9.805   1.00 36.49  ?  146 LEU A CB    1 
ATOM   1080 C  CG    . LEU A 1 146 ? 6.288   -9.593  8.707   1.00 36.57  ?  146 LEU A CG    1 
ATOM   1081 C  CD1   . LEU A 1 146 ? 6.231   -10.986 8.088   1.00 29.52  ?  146 LEU A CD1   1 
ATOM   1082 C  CD2   . LEU A 1 146 ? 6.116   -8.474  7.617   1.00 31.70  ?  146 LEU A CD2   1 
ATOM   1083 N  N     . LEU A 1 147 ? 6.798   -9.376  12.491  1.00 29.43  ?  147 LEU A N     1 
ATOM   1084 C  CA    . LEU A 1 147 ? 8.026   -9.190  13.249  1.00 30.95  ?  147 LEU A CA    1 
ATOM   1085 C  C     . LEU A 1 147 ? 8.409   -10.400 14.095  1.00 30.48  ?  147 LEU A C     1 
ATOM   1086 O  O     . LEU A 1 147 ? 9.573   -10.532 14.452  1.00 34.43  ?  147 LEU A O     1 
ATOM   1087 C  CB    . LEU A 1 147 ? 7.903   -7.970  14.136  1.00 29.40  ?  147 LEU A CB    1 
ATOM   1088 C  CG    . LEU A 1 147 ? 9.136   -7.589  14.939  1.00 27.24  ?  147 LEU A CG    1 
ATOM   1089 C  CD1   . LEU A 1 147 ? 10.185  -7.052  13.971  1.00 28.30  ?  147 LEU A CD1   1 
ATOM   1090 C  CD2   . LEU A 1 147 ? 8.722   -6.538  15.945  1.00 32.07  ?  147 LEU A CD2   1 
ATOM   1091 N  N     . ASP A 1 148 ? 7.470   -11.281 14.433  1.00 34.58  ?  148 ASP A N     1 
ATOM   1092 C  CA    . ASP A 1 148 ? 7.831   -12.514 15.123  1.00 33.38  ?  148 ASP A CA    1 
ATOM   1093 C  C     . ASP A 1 148 ? 8.476   -13.519 14.174  1.00 33.77  ?  148 ASP A C     1 
ATOM   1094 O  O     . ASP A 1 148 ? 9.233   -14.392 14.607  1.00 34.91  ?  148 ASP A O     1 
ATOM   1095 C  CB    . ASP A 1 148 ? 6.590   -13.140 15.778  1.00 32.30  ?  148 ASP A CB    1 
ATOM   1096 C  CG    . ASP A 1 148 ? 6.175   -12.414 17.060  1.00 41.67  ?  148 ASP A CG    1 
ATOM   1097 O  OD1   . ASP A 1 148 ? 6.898   -11.498 17.504  1.00 45.95  ?  148 ASP A OD1   1 
ATOM   1098 O  OD2   . ASP A 1 148 ? 5.121   -12.744 17.636  1.00 47.19  ?  148 ASP A OD2   1 
ATOM   1099 N  N     . VAL A 1 149 ? 8.163   -13.439 12.886  1.00 32.13  ?  149 VAL A N     1 
ATOM   1100 C  CA    . VAL A 1 149 ? 8.706   -14.381 11.922  1.00 35.54  ?  149 VAL A CA    1 
ATOM   1101 C  C     . VAL A 1 149 ? 10.150  -14.020 11.562  1.00 33.61  ?  149 VAL A C     1 
ATOM   1102 O  O     . VAL A 1 149 ? 11.050  -14.867 11.565  1.00 32.19  ?  149 VAL A O     1 
ATOM   1103 C  CB    . VAL A 1 149 ? 7.789   -14.414 10.683  1.00 36.44  ?  149 VAL A CB    1 
ATOM   1104 C  CG1   . VAL A 1 149 ? 8.292   -15.421 9.657   1.00 33.88  ?  149 VAL A CG1   1 
ATOM   1105 C  CG2   . VAL A 1 149 ? 6.355   -14.720 11.110  1.00 33.51  ?  149 VAL A CG2   1 
ATOM   1106 N  N     . THR A 1 150 ? 10.390  -12.753 11.269  1.00 32.49  ?  150 THR A N     1 
ATOM   1107 C  CA    . THR A 1 150 ? 11.704  -12.245 10.894  1.00 36.13  ?  150 THR A CA    1 
ATOM   1108 C  C     . THR A 1 150 ? 11.534  -10.736 10.848  1.00 34.18  ?  150 THR A C     1 
ATOM   1109 O  O     . THR A 1 150 ? 10.413  -10.217 10.956  1.00 36.03  ?  150 THR A O     1 
ATOM   1110 C  CB    . THR A 1 150 ? 12.186  -12.846 9.556   1.00 38.52  ?  150 THR A CB    1 
ATOM   1111 O  OG1   . THR A 1 150 ? 13.487  -12.364 9.210   1.00 38.40  ?  150 THR A OG1   1 
ATOM   1112 C  CG2   . THR A 1 150 ? 11.189  -12.534 8.430   1.00 31.33  ?  150 THR A CG2   1 
ATOM   1113 N  N     . ASN A 1 151 ? 12.644  -10.033 10.705  1.00 34.55  ?  151 ASN A N     1 
ATOM   1114 C  CA    . ASN A 1 151 ? 12.587  -8.582  10.785  1.00 35.96  ?  151 ASN A CA    1 
ATOM   1115 C  C     . ASN A 1 151 ? 11.958  -7.986  9.534   1.00 37.53  ?  151 ASN A C     1 
ATOM   1116 O  O     . ASN A 1 151 ? 12.151  -8.492  8.428   1.00 39.42  ?  151 ASN A O     1 
ATOM   1117 C  CB    . ASN A 1 151 ? 13.969  -7.984  10.998  1.00 29.56  ?  151 ASN A CB    1 
ATOM   1118 C  CG    . ASN A 1 151 ? 13.881  -6.575  11.453  1.00 34.41  ?  151 ASN A CG    1 
ATOM   1119 O  OD1   . ASN A 1 151 ? 12.767  -6.038  11.612  1.00 37.45  ?  151 ASN A OD1   1 
ATOM   1120 N  ND2   . ASN A 1 151 ? 15.012  -5.942  11.658  1.00 32.22  ?  151 ASN A ND2   1 
ATOM   1121 N  N     . HIS A 1 152 ? 11.172  -6.911  9.713   1.00 29.26  ?  152 HIS A N     1 
ATOM   1122 C  CA    . HIS A 1 152 ? 10.664  -6.194  8.555   1.00 30.47  ?  152 HIS A CA    1 
ATOM   1123 C  C     . HIS A 1 152 ? 10.864  -4.683  8.638   1.00 33.76  ?  152 HIS A C     1 
ATOM   1124 O  O     . HIS A 1 152 ? 10.239  -3.951  7.860   1.00 36.04  ?  152 HIS A O     1 
ATOM   1125 C  CB    . HIS A 1 152 ? 9.179   -6.530  8.279   1.00 32.91  ?  152 HIS A CB    1 
ATOM   1126 C  CG    . HIS A 1 152 ? 8.213   -6.226  9.402   1.00 35.53  ?  152 HIS A CG    1 
ATOM   1127 N  ND1   . HIS A 1 152 ? 7.421   -5.091  9.415   1.00 32.48  ?  152 HIS A ND1   1 
ATOM   1128 C  CD2   . HIS A 1 152 ? 7.831   -6.961  10.481  1.00 32.62  ?  152 HIS A CD2   1 
ATOM   1129 C  CE1   . HIS A 1 152 ? 6.628   -5.123  10.476  1.00 33.11  ?  152 HIS A CE1   1 
ATOM   1130 N  NE2   . HIS A 1 152 ? 6.857   -6.246  11.138  1.00 34.17  ?  152 HIS A NE2   1 
ATOM   1131 N  N     . PHE A 1 153 ? 11.695  -4.184  9.547   1.00 30.55  ?  153 PHE A N     1 
ATOM   1132 C  CA    . PHE A 1 153 ? 12.069  -2.772  9.446   1.00 35.39  ?  153 PHE A CA    1 
ATOM   1133 C  C     . PHE A 1 153 ? 13.510  -2.611  9.937   1.00 34.66  ?  153 PHE A C     1 
ATOM   1134 O  O     . PHE A 1 153 ? 14.271  -3.584  10.011  1.00 36.06  ?  153 PHE A O     1 
ATOM   1135 C  CB    . PHE A 1 153 ? 11.041  -1.847  10.149  1.00 31.86  ?  153 PHE A CB    1 
ATOM   1136 C  CG    . PHE A 1 153 ? 10.584  -2.306  11.505  1.00 31.86  ?  153 PHE A CG    1 
ATOM   1137 C  CD1   . PHE A 1 153 ? 11.289  -1.929  12.657  1.00 33.26  ?  153 PHE A CD1   1 
ATOM   1138 C  CD2   . PHE A 1 153 ? 9.404   -3.073  11.645  1.00 33.29  ?  153 PHE A CD2   1 
ATOM   1139 C  CE1   . PHE A 1 153 ? 10.850  -2.330  13.938  1.00 33.02  ?  153 PHE A CE1   1 
ATOM   1140 C  CE2   . PHE A 1 153 ? 8.947   -3.501  12.910  1.00 28.52  ?  153 PHE A CE2   1 
ATOM   1141 C  CZ    . PHE A 1 153 ? 9.664   -3.136  14.064  1.00 29.12  ?  153 PHE A CZ    1 
ATOM   1142 N  N     . ALA A 1 154 ? 13.895  -1.377  10.236  1.00 35.73  ?  154 ALA A N     1 
ATOM   1143 C  CA    . ALA A 1 154 ? 15.291  -1.013  10.402  1.00 33.79  ?  154 ALA A CA    1 
ATOM   1144 C  C     . ALA A 1 154 ? 15.375  0.124   11.404  1.00 31.29  ?  154 ALA A C     1 
ATOM   1145 O  O     . ALA A 1 154 ? 14.424  0.905   11.526  1.00 32.70  ?  154 ALA A O     1 
ATOM   1146 C  CB    . ALA A 1 154 ? 15.901  -0.588  9.069   1.00 34.44  ?  154 ALA A CB    1 
ATOM   1147 N  N     . PRO A 1 155 ? 16.481  0.237   12.140  1.00 31.79  ?  155 PRO A N     1 
ATOM   1148 C  CA    . PRO A 1 155 ? 16.479  1.171   13.287  1.00 29.63  ?  155 PRO A CA    1 
ATOM   1149 C  C     . PRO A 1 155 ? 16.270  2.613   12.883  1.00 34.69  ?  155 PRO A C     1 
ATOM   1150 O  O     . PRO A 1 155 ? 15.643  3.372   13.648  1.00 32.37  ?  155 PRO A O     1 
ATOM   1151 C  CB    . PRO A 1 155 ? 17.837  0.934   13.949  1.00 29.62  ?  155 PRO A CB    1 
ATOM   1152 C  CG    . PRO A 1 155 ? 18.162  -0.533  13.575  1.00 35.24  ?  155 PRO A CG    1 
ATOM   1153 C  CD    . PRO A 1 155 ? 17.610  -0.704  12.177  1.00 35.19  ?  155 PRO A CD    1 
ATOM   1154 N  N     . SER A 1 156 ? 16.715  3.004   11.682  1.00 30.88  ?  156 SER A N     1 
ATOM   1155 C  CA    . SER A 1 156 ? 16.394  4.348   11.200  1.00 35.51  ?  156 SER A CA    1 
ATOM   1156 C  C     . SER A 1 156 ? 14.888  4.583   11.121  1.00 32.24  ?  156 SER A C     1 
ATOM   1157 O  O     . SER A 1 156 ? 14.474  5.730   10.958  1.00 31.22  ?  156 SER A O     1 
ATOM   1158 C  CB    . SER A 1 156 ? 17.042  4.629   9.825   1.00 32.69  ?  156 SER A CB    1 
ATOM   1159 O  OG    . SER A 1 156 ? 18.458  4.382   9.813   1.00 37.68  ?  156 SER A OG    1 
ATOM   1160 N  N     . ALA A 1 157 ? 14.058  3.548   11.247  1.00 28.07  ?  157 ALA A N     1 
ATOM   1161 C  CA    . ALA A 1 157 ? 12.623  3.749   11.135  1.00 32.21  ?  157 ALA A CA    1 
ATOM   1162 C  C     . ALA A 1 157 ? 11.916  3.831   12.487  1.00 33.74  ?  157 ALA A C     1 
ATOM   1163 O  O     . ALA A 1 157 ? 10.684  3.966   12.526  1.00 33.04  ?  157 ALA A O     1 
ATOM   1164 C  CB    . ALA A 1 157 ? 11.997  2.636   10.288  1.00 29.56  ?  157 ALA A CB    1 
ATOM   1165 N  N     . VAL A 1 158 ? 12.662  3.789   13.584  1.00 31.90  ?  158 VAL A N     1 
ATOM   1166 C  CA    . VAL A 1 158 ? 12.127  3.483   14.899  1.00 29.84  ?  158 VAL A CA    1 
ATOM   1167 C  C     . VAL A 1 158 ? 12.334  4.701   15.786  1.00 35.06  ?  158 VAL A C     1 
ATOM   1168 O  O     . VAL A 1 158 ? 13.422  5.287   15.779  1.00 30.78  ?  158 VAL A O     1 
ATOM   1169 C  CB    . VAL A 1 158 ? 12.834  2.255   15.489  1.00 32.66  ?  158 VAL A CB    1 
ATOM   1170 C  CG1   . VAL A 1 158 ? 12.408  2.028   16.911  1.00 33.45  ?  158 VAL A CG1   1 
ATOM   1171 C  CG2   . VAL A 1 158 ? 12.597  1.028   14.611  1.00 34.28  ?  158 VAL A CG2   1 
ATOM   1172 N  N     . VAL A 1 159 ? 11.281  5.113   16.506  1.00 28.83  ?  159 VAL A N     1 
ATOM   1173 C  CA    . VAL A 1 159 ? 11.391  6.036   17.631  1.00 27.04  ?  159 VAL A CA    1 
ATOM   1174 C  C     . VAL A 1 159 ? 10.741  5.355   18.841  1.00 32.22  ?  159 VAL A C     1 
ATOM   1175 O  O     . VAL A 1 159 ? 9.641   4.802   18.728  1.00 31.67  ?  159 VAL A O     1 
ATOM   1176 C  CB    . VAL A 1 159 ? 10.742  7.409   17.326  1.00 30.88  ?  159 VAL A CB    1 
ATOM   1177 C  CG1   . VAL A 1 159 ? 11.097  8.438   18.407  1.00 26.43  ?  159 VAL A CG1   1 
ATOM   1178 C  CG2   . VAL A 1 159 ? 11.201  7.947   15.991  1.00 28.78  ?  159 VAL A CG2   1 
ATOM   1179 N  N     . CYS A 1 160 ? 11.412  5.375   19.994  1.00 29.97  ?  160 CYS A N     1 
ATOM   1180 C  CA    . CYS A 1 160 ? 10.896  4.570   21.091  1.00 31.92  ?  160 CYS A CA    1 
ATOM   1181 C  C     . CYS A 1 160 ? 11.269  5.174   22.443  1.00 32.32  ?  160 CYS A C     1 
ATOM   1182 O  O     . CYS A 1 160 ? 12.193  5.981   22.555  1.00 32.88  ?  160 CYS A O     1 
ATOM   1183 C  CB    . CYS A 1 160 ? 11.402  3.117   20.990  1.00 32.20  ?  160 CYS A CB    1 
ATOM   1184 S  SG    . CYS A 1 160 ? 13.196  2.914   21.225  1.00 38.23  ?  160 CYS A SG    1 
ATOM   1185 N  N     . ARG A 1 161 ? 10.516  4.769   23.464  1.00 34.44  ?  161 ARG A N     1 
ATOM   1186 C  CA    . ARG A 1 161 ? 10.774  5.168   24.848  1.00 35.84  ?  161 ARG A CA    1 
ATOM   1187 C  C     . ARG A 1 161 ? 12.197  4.798   25.273  1.00 32.71  ?  161 ARG A C     1 
ATOM   1188 O  O     . ARG A 1 161 ? 12.650  3.669   25.053  1.00 34.03  ?  161 ARG A O     1 
ATOM   1189 C  CB    . ARG A 1 161 ? 9.749   4.478   25.769  1.00 27.82  ?  161 ARG A CB    1 
ATOM   1190 C  CG    . ARG A 1 161 ? 9.142   5.372   26.809  1.00 34.79  ?  161 ARG A CG    1 
ATOM   1191 C  CD    . ARG A 1 161 ? 7.845   4.785   27.464  1.00 32.77  ?  161 ARG A CD    1 
ATOM   1192 N  NE    . ARG A 1 161 ? 6.635   5.282   26.819  1.00 29.45  ?  161 ARG A NE    1 
ATOM   1193 C  CZ    . ARG A 1 161 ? 6.238   6.544   26.854  1.00 28.70  ?  161 ARG A CZ    1 
ATOM   1194 N  NH1   . ARG A 1 161 ? 6.834   7.435   27.632  1.00 25.63  ?  161 ARG A NH1   1 
ATOM   1195 N  NH2   . ARG A 1 161 ? 5.254   6.933   26.049  1.00 27.29  ?  161 ARG A NH2   1 
ATOM   1196 N  N     . SER A 1 162 ? 12.890  5.750   25.914  1.00 35.53  ?  162 SER A N     1 
ATOM   1197 C  CA    . SER A 1 162 ? 14.238  5.653   26.489  1.00 33.13  ?  162 SER A CA    1 
ATOM   1198 C  C     . SER A 1 162 ? 14.628  4.218   26.860  1.00 32.49  ?  162 SER A C     1 
ATOM   1199 O  O     . SER A 1 162 ? 14.177  3.690   27.876  1.00 32.71  ?  162 SER A O     1 
ATOM   1200 C  CB    . SER A 1 162 ? 14.328  6.538   27.731  1.00 30.43  ?  162 SER A CB    1 
ATOM   1201 O  OG    . SER A 1 162 ? 15.465  6.240   28.512  1.00 34.40  ?  162 SER A OG    1 
ATOM   1202 N  N     . PRO A 1 163 ? 15.439  3.543   26.051  1.00 31.92  ?  163 PRO A N     1 
ATOM   1203 C  CA    . PRO A 1 163 ? 15.816  2.169   26.403  1.00 31.30  ?  163 PRO A CA    1 
ATOM   1204 C  C     . PRO A 1 163 ? 16.739  2.085   27.606  1.00 32.30  ?  163 PRO A C     1 
ATOM   1205 O  O     . PRO A 1 163 ? 16.733  1.048   28.291  1.00 33.48  ?  163 PRO A O     1 
ATOM   1206 C  CB    . PRO A 1 163 ? 16.476  1.650   25.121  1.00 30.56  ?  163 PRO A CB    1 
ATOM   1207 C  CG    . PRO A 1 163 ? 15.795  2.482   24.018  1.00 28.03  ?  163 PRO A CG    1 
ATOM   1208 C  CD    . PRO A 1 163 ? 15.639  3.834   24.618  1.00 28.63  ?  163 PRO A CD    1 
ATOM   1209 N  N     . ARG A 1 164 ? 17.493  3.136   27.930  1.00 28.41  ?  164 ARG A N     1 
ATOM   1210 C  CA    . ARG A 1 164 ? 18.329  3.039   29.121  1.00 28.04  ?  164 ARG A CA    1 
ATOM   1211 C  C     . ARG A 1 164 ? 17.462  2.944   30.367  1.00 31.82  ?  164 ARG A C     1 
ATOM   1212 O  O     . ARG A 1 164 ? 17.764  2.158   31.276  1.00 30.76  ?  164 ARG A O     1 
ATOM   1213 C  CB    . ARG A 1 164 ? 19.313  4.204   29.195  1.00 29.02  ?  164 ARG A CB    1 
ATOM   1214 C  CG    . ARG A 1 164 ? 18.789  5.490   29.810  1.00 32.11  ?  164 ARG A CG    1 
ATOM   1215 C  CD    . ARG A 1 164 ? 19.886  6.526   29.793  1.00 32.87  ?  164 ARG A CD    1 
ATOM   1216 N  NE    . ARG A 1 164 ? 19.499  7.807   30.362  1.00 38.37  ?  164 ARG A NE    1 
ATOM   1217 C  CZ    . ARG A 1 164 ? 20.352  8.789   30.629  1.00 36.67  ?  164 ARG A CZ    1 
ATOM   1218 N  NH1   . ARG A 1 164 ? 21.649  8.650   30.425  1.00 28.73  ?  164 ARG A NH1   1 
ATOM   1219 N  NH2   . ARG A 1 164 ? 19.888  9.940   31.106  1.00 32.67  ?  164 ARG A NH2   1 
ATOM   1220 N  N     . SER A 1 165 ? 16.322  3.648   30.369  1.00 28.15  ?  165 SER A N     1 
ATOM   1221 C  CA    . SER A 1 165 ? 15.402  3.596   31.511  1.00 36.45  ?  165 SER A CA    1 
ATOM   1222 C  C     . SER A 1 165 ? 14.775  2.220   31.669  1.00 28.20  ?  165 SER A C     1 
ATOM   1223 O  O     . SER A 1 165 ? 14.620  1.749   32.790  1.00 32.91  ?  165 SER A O     1 
ATOM   1224 C  CB    . SER A 1 165 ? 14.312  4.669   31.382  1.00 31.11  ?  165 SER A CB    1 
ATOM   1225 O  OG    . SER A 1 165 ? 14.920  5.969   31.407  1.00 39.33  ?  165 SER A OG    1 
ATOM   1226 N  N     . ALA A 1 166 ? 14.442  1.548   30.564  1.00 34.12  ?  166 ALA A N     1 
ATOM   1227 C  CA    . ALA A 1 166 ? 14.037  0.134   30.591  1.00 33.16  ?  166 ALA A CA    1 
ATOM   1228 C  C     . ALA A 1 166 ? 15.193  -0.829  30.858  1.00 31.98  ?  166 ALA A C     1 
ATOM   1229 O  O     . ALA A 1 166 ? 14.937  -2.001  31.127  1.00 34.70  ?  166 ALA A O     1 
ATOM   1230 C  CB    . ALA A 1 166 ? 13.380  -0.261  29.263  1.00 31.43  ?  166 ALA A CB    1 
ATOM   1231 N  N     . GLY A 1 167 ? 16.444  -0.374  30.779  1.00 35.30  ?  167 GLY A N     1 
ATOM   1232 C  CA    . GLY A 1 167 ? 17.586  -1.261  30.886  1.00 34.49  ?  167 GLY A CA    1 
ATOM   1233 C  C     . GLY A 1 167 ? 17.710  -2.217  29.731  1.00 32.32  ?  167 GLY A C     1 
ATOM   1234 O  O     . GLY A 1 167 ? 18.235  -3.313  29.900  1.00 38.83  ?  167 GLY A O     1 
ATOM   1235 N  N     . ALA A 1 168 ? 17.216  -1.833  28.559  1.00 34.52  ?  168 ALA A N     1 
ATOM   1236 C  CA    . ALA A 1 168 ? 17.201  -2.666  27.364  1.00 30.61  ?  168 ALA A CA    1 
ATOM   1237 C  C     . ALA A 1 168 ? 18.261  -2.168  26.384  1.00 33.49  ?  168 ALA A C     1 
ATOM   1238 O  O     . ALA A 1 168 ? 18.195  -1.018  25.925  1.00 29.31  ?  168 ALA A O     1 
ATOM   1239 C  CB    . ALA A 1 168 ? 15.821  -2.631  26.716  1.00 28.63  ?  168 ALA A CB    1 
ATOM   1240 N  N     . PHE A 1 169 ? 19.221  -3.037  26.036  1.00 32.29  ?  169 PHE A N     1 
ATOM   1241 C  CA    . PHE A 1 169 ? 20.314  -2.631  25.165  1.00 33.14  ?  169 PHE A CA    1 
ATOM   1242 C  C     . PHE A 1 169 ? 20.499  -3.627  24.017  1.00 33.04  ?  169 PHE A C     1 
ATOM   1243 O  O     . PHE A 1 169 ? 19.928  -4.723  23.991  1.00 32.82  ?  169 PHE A O     1 
ATOM   1244 C  CB    . PHE A 1 169 ? 21.620  -2.463  25.974  1.00 33.32  ?  169 PHE A CB    1 
ATOM   1245 C  CG    . PHE A 1 169 ? 21.590  -1.318  26.978  1.00 27.91  ?  169 PHE A CG    1 
ATOM   1246 C  CD1   . PHE A 1 169 ? 22.006  -0.041  26.614  1.00 28.90  ?  169 PHE A CD1   1 
ATOM   1247 C  CD2   . PHE A 1 169 ? 21.182  -1.540  28.289  1.00 33.18  ?  169 PHE A CD2   1 
ATOM   1248 C  CE1   . PHE A 1 169 ? 21.987  1.021   27.528  1.00 35.70  ?  169 PHE A CE1   1 
ATOM   1249 C  CE2   . PHE A 1 169 ? 21.133  -0.483  29.225  1.00 33.69  ?  169 PHE A CE2   1 
ATOM   1250 C  CZ    . PHE A 1 169 ? 21.539  0.798   28.846  1.00 34.73  ?  169 PHE A CZ    1 
ATOM   1251 N  N     . PHE A 1 170 ? 21.332  -3.232  23.054  1.00 36.13  ?  170 PHE A N     1 
ATOM   1252 C  CA    . PHE A 1 170 ? 21.704  -4.113  21.950  1.00 30.15  ?  170 PHE A CA    1 
ATOM   1253 C  C     . PHE A 1 170 ? 22.630  -5.230  22.428  1.00 29.69  ?  170 PHE A C     1 
ATOM   1254 O  O     . PHE A 1 170 ? 23.398  -5.055  23.368  1.00 26.77  ?  170 PHE A O     1 
ATOM   1255 C  CB    . PHE A 1 170 ? 22.365  -3.312  20.839  1.00 29.65  ?  170 PHE A CB    1 
ATOM   1256 C  CG    . PHE A 1 170 ? 21.401  -2.509  20.032  1.00 30.16  ?  170 PHE A CG    1 
ATOM   1257 C  CD1   . PHE A 1 170 ? 20.944  -1.285  20.502  1.00 28.96  ?  170 PHE A CD1   1 
ATOM   1258 C  CD2   . PHE A 1 170 ? 20.958  -2.963  18.797  1.00 28.95  ?  170 PHE A CD2   1 
ATOM   1259 C  CE1   . PHE A 1 170 ? 20.039  -0.545  19.763  1.00 26.29  ?  170 PHE A CE1   1 
ATOM   1260 C  CE2   . PHE A 1 170 ? 20.068  -2.221  18.054  1.00 28.12  ?  170 PHE A CE2   1 
ATOM   1261 C  CZ    . PHE A 1 170 ? 19.597  -1.014  18.551  1.00 26.92  ?  170 PHE A CZ    1 
ATOM   1262 N  N     . ASP A 1 171 ? 22.507  -6.411  21.797  1.00 29.93  ?  171 ASP A N     1 
ATOM   1263 C  CA    . ASP A 1 171 ? 23.378  -7.552  22.085  1.00 31.89  ?  171 ASP A CA    1 
ATOM   1264 C  C     . ASP A 1 171 ? 24.661  -7.410  21.261  1.00 34.44  ?  171 ASP A C     1 
ATOM   1265 O  O     . ASP A 1 171 ? 24.620  -7.380  20.028  1.00 34.35  ?  171 ASP A O     1 
ATOM   1266 C  CB    . ASP A 1 171 ? 22.635  -8.852  21.764  1.00 34.35  ?  171 ASP A CB    1 
ATOM   1267 C  CG    . ASP A 1 171 ? 23.429  -10.127 22.134  1.00 45.15  ?  171 ASP A CG    1 
ATOM   1268 O  OD1   . ASP A 1 171 ? 24.637  -10.042 22.481  1.00 44.22  ?  171 ASP A OD1   1 
ATOM   1269 O  OD2   . ASP A 1 171 ? 22.826  -11.235 22.075  1.00 43.19  ?  171 ASP A OD2   1 
ATOM   1270 N  N     . THR A 1 172 ? 25.797  -7.282  21.935  1.00 40.30  ?  172 THR A N     1 
ATOM   1271 C  CA    . THR A 1 172 ? 27.064  -7.112  21.233  1.00 36.35  ?  172 THR A CA    1 
ATOM   1272 C  C     . THR A 1 172 ? 27.637  -8.409  20.697  1.00 40.02  ?  172 THR A C     1 
ATOM   1273 O  O     . THR A 1 172 ? 28.667  -8.361  20.023  1.00 47.94  ?  172 THR A O     1 
ATOM   1274 C  CB    . THR A 1 172 ? 28.110  -6.465  22.134  1.00 38.63  ?  172 THR A CB    1 
ATOM   1275 O  OG1   . THR A 1 172 ? 28.442  -7.378  23.186  1.00 40.48  ?  172 THR A OG1   1 
ATOM   1276 C  CG2   . THR A 1 172 ? 27.604  -5.132  22.710  1.00 31.84  ?  172 THR A CG2   1 
ATOM   1277 N  N     . ALA A 1 173 ? 27.034  -9.555  20.983  1.00 38.53  ?  173 ALA A N     1 
ATOM   1278 C  CA    . ALA A 1 173 ? 27.440  -10.809 20.356  1.00 39.26  ?  173 ALA A CA    1 
ATOM   1279 C  C     . ALA A 1 173 ? 26.816  -11.018 18.980  1.00 45.72  ?  173 ALA A C     1 
ATOM   1280 O  O     . ALA A 1 173 ? 26.970  -12.105 18.414  1.00 51.91  ?  173 ALA A O     1 
ATOM   1281 C  CB    . ALA A 1 173 ? 27.077  -12.003 21.245  1.00 41.38  ?  173 ALA A CB    1 
ATOM   1282 N  N     . LEU A 1 174 ? 26.108  -10.032 18.430  1.00 40.01  ?  174 LEU A N     1 
ATOM   1283 C  CA    . LEU A 1 174 ? 25.478  -10.174 17.118  1.00 47.14  ?  174 LEU A CA    1 
ATOM   1284 C  C     . LEU A 1 174 ? 25.911  -9.026  16.216  1.00 44.46  ?  174 LEU A C     1 
ATOM   1285 O  O     . LEU A 1 174 ? 25.661  -7.861  16.539  1.00 44.22  ?  174 LEU A O     1 
ATOM   1286 C  CB    . LEU A 1 174 ? 23.943  -10.204 17.235  1.00 43.23  ?  174 LEU A CB    1 
ATOM   1287 C  CG    . LEU A 1 174 ? 23.288  -11.155 18.243  1.00 38.91  ?  174 LEU A CG    1 
ATOM   1288 C  CD1   . LEU A 1 174 ? 21.809  -10.782 18.456  1.00 33.37  ?  174 LEU A CD1   1 
ATOM   1289 C  CD2   . LEU A 1 174 ? 23.396  -12.600 17.766  1.00 40.95  ?  174 LEU A CD2   1 
ATOM   1290 N  N     . GLY A 1 175 ? 26.547  -9.352  15.084  1.00 45.73  ?  175 GLY A N     1 
ATOM   1291 C  CA    . GLY A 1 175 ? 26.973  -8.339  14.121  1.00 42.47  ?  175 GLY A CA    1 
ATOM   1292 C  C     . GLY A 1 175 ? 25.968  -8.082  13.008  1.00 48.95  ?  175 GLY A C     1 
ATOM   1293 O  O     . GLY A 1 175 ? 26.039  -7.052  12.313  1.00 48.66  ?  175 GLY A O     1 
ATOM   1294 N  N     . VAL A 1 176 ? 25.027  -9.026  12.825  1.00 44.80  ?  176 VAL A N     1 
ATOM   1295 C  CA    . VAL A 1 176 ? 23.899  -8.874  11.908  1.00 46.12  ?  176 VAL A CA    1 
ATOM   1296 C  C     . VAL A 1 176 ? 22.638  -9.304  12.629  1.00 43.21  ?  176 VAL A C     1 
ATOM   1297 O  O     . VAL A 1 176 ? 22.667  -10.176 13.509  1.00 38.64  ?  176 VAL A O     1 
ATOM   1298 C  CB    . VAL A 1 176 ? 24.041  -9.689  10.602  1.00 47.39  ?  176 VAL A CB    1 
ATOM   1299 C  CG1   . VAL A 1 176 ? 25.227  -9.205  9.789   1.00 50.78  ?  176 VAL A CG1   1 
ATOM   1300 C  CG2   . VAL A 1 176 ? 24.121  -11.213 10.896  1.00 43.86  ?  176 VAL A CG2   1 
ATOM   1301 N  N     . GLU A 1 177 ? 21.520  -8.718  12.205  1.00 42.58  ?  177 GLU A N     1 
ATOM   1302 C  CA    . GLU A 1 177 ? 20.230  -8.876  12.866  1.00 40.81  ?  177 GLU A CA    1 
ATOM   1303 C  C     . GLU A 1 177 ? 20.298  -8.510  14.348  1.00 39.46  ?  177 GLU A C     1 
ATOM   1304 O  O     . GLU A 1 177 ? 19.543  -9.065  15.141  1.00 35.89  ?  177 GLU A O     1 
ATOM   1305 C  CB    . GLU A 1 177 ? 19.689  -10.309 12.729  1.00 40.88  ?  177 GLU A CB    1 
ATOM   1306 C  CG    . GLU A 1 177 ? 19.082  -10.713 11.387  1.00 38.28  ?  177 GLU A CG    1 
ATOM   1307 C  CD    . GLU A 1 177 ? 19.080  -12.234 11.242  1.00 44.22  ?  177 GLU A CD    1 
ATOM   1308 O  OE1   . GLU A 1 177 ? 20.125  -12.782 10.829  1.00 43.14  ?  177 GLU A OE1   1 
ATOM   1309 O  OE2   . GLU A 1 177 ? 18.065  -12.892 11.587  1.00 42.15  ?  177 GLU A OE2   1 
ATOM   1310 N  N     . GLU A 1 178 ? 21.235  -7.641  14.768  1.00 37.93  ?  178 GLU A N     1 
ATOM   1311 C  CA    . GLU A 1 178 ? 21.196  -7.151  16.144  1.00 36.27  ?  178 GLU A CA    1 
ATOM   1312 C  C     . GLU A 1 178 ? 19.979  -6.249  16.382  1.00 35.31  ?  178 GLU A C     1 
ATOM   1313 O  O     . GLU A 1 178 ? 19.535  -6.088  17.527  1.00 28.47  ?  178 GLU A O     1 
ATOM   1314 C  CB    . GLU A 1 178 ? 22.509  -6.427  16.494  1.00 38.30  ?  178 GLU A CB    1 
ATOM   1315 C  CG    . GLU A 1 178 ? 22.694  -4.994  15.949  1.00 37.58  ?  178 GLU A CG    1 
ATOM   1316 C  CD    . GLU A 1 178 ? 22.812  -4.921  14.415  1.00 45.84  ?  178 GLU A CD    1 
ATOM   1317 O  OE1   . GLU A 1 178 ? 23.210  -5.945  13.789  1.00 48.17  ?  178 GLU A OE1   1 
ATOM   1318 O  OE2   . GLU A 1 178 ? 22.507  -3.836  13.839  1.00 45.14  ?  178 GLU A OE2   1 
ATOM   1319 N  N     . ASP A 1 179 ? 19.409  -5.701  15.315  1.00 33.89  ?  179 ASP A N     1 
ATOM   1320 C  CA    . ASP A 1 179 ? 18.221  -4.872  15.442  1.00 33.96  ?  179 ASP A CA    1 
ATOM   1321 C  C     . ASP A 1 179 ? 16.957  -5.721  15.662  1.00 34.53  ?  179 ASP A C     1 
ATOM   1322 O  O     . ASP A 1 179 ? 16.182  -5.461  16.597  1.00 31.73  ?  179 ASP A O     1 
ATOM   1323 C  CB    . ASP A 1 179 ? 18.100  -3.976  14.213  1.00 31.33  ?  179 ASP A CB    1 
ATOM   1324 C  CG    . ASP A 1 179 ? 18.128  -4.751  12.899  1.00 38.84  ?  179 ASP A CG    1 
ATOM   1325 O  OD1   . ASP A 1 179 ? 18.678  -5.873  12.842  1.00 42.03  ?  179 ASP A OD1   1 
ATOM   1326 O  OD2   . ASP A 1 179 ? 17.604  -4.212  11.896  1.00 41.94  ?  179 ASP A OD2   1 
ATOM   1327 N  N     . TRP A 1 180 ? 16.757  -6.760  14.836  1.00 32.94  ?  180 TRP A N     1 
ATOM   1328 C  CA    . TRP A 1 180 ? 15.686  -7.732  15.074  1.00 33.68  ?  180 TRP A CA    1 
ATOM   1329 C  C     . TRP A 1 180 ? 15.657  -8.200  16.530  1.00 33.39  ?  180 TRP A C     1 
ATOM   1330 O  O     . TRP A 1 180 ? 14.623  -8.086  17.206  1.00 32.95  ?  180 TRP A O     1 
ATOM   1331 C  CB    . TRP A 1 180 ? 15.816  -8.932  14.119  1.00 32.19  ?  180 TRP A CB    1 
ATOM   1332 C  CG    . TRP A 1 180 ? 14.519  -9.725  14.055  1.00 31.15  ?  180 TRP A CG    1 
ATOM   1333 C  CD1   . TRP A 1 180 ? 13.254  -9.213  14.020  1.00 31.77  ?  180 TRP A CD1   1 
ATOM   1334 C  CD2   . TRP A 1 180 ? 14.371  -11.156 14.087  1.00 35.64  ?  180 TRP A CD2   1 
ATOM   1335 N  NE1   . TRP A 1 180 ? 12.329  -10.230 13.993  1.00 35.58  ?  180 TRP A NE1   1 
ATOM   1336 C  CE2   . TRP A 1 180 ? 12.986  -11.433 14.038  1.00 35.97  ?  180 TRP A CE2   1 
ATOM   1337 C  CE3   . TRP A 1 180 ? 15.272  -12.226 14.141  1.00 34.26  ?  180 TRP A CE3   1 
ATOM   1338 C  CZ2   . TRP A 1 180 ? 12.479  -12.734 14.059  1.00 31.03  ?  180 TRP A CZ2   1 
ATOM   1339 C  CZ3   . TRP A 1 180 ? 14.764  -13.512 14.172  1.00 38.14  ?  180 TRP A CZ3   1 
ATOM   1340 C  CH2   . TRP A 1 180 ? 13.373  -13.753 14.131  1.00 33.32  ?  180 TRP A CH2   1 
ATOM   1341 N  N     . ASP A 1 181 ? 16.796  -8.700  17.037  1.00 27.87  ?  181 ASP A N     1 
ATOM   1342 C  CA    . ASP A 1 181 ? 16.903  -9.052  18.454  1.00 28.92  ?  181 ASP A CA    1 
ATOM   1343 C  C     . ASP A 1 181 ? 16.500  -7.905  19.396  1.00 34.08  ?  181 ASP A C     1 
ATOM   1344 O  O     . ASP A 1 181 ? 15.854  -8.138  20.424  1.00 29.89  ?  181 ASP A O     1 
ATOM   1345 C  CB    . ASP A 1 181 ? 18.317  -9.511  18.755  1.00 31.82  ?  181 ASP A CB    1 
ATOM   1346 C  CG    . ASP A 1 181 ? 18.486  -9.995  20.162  1.00 30.92  ?  181 ASP A CG    1 
ATOM   1347 O  OD1   . ASP A 1 181 ? 17.793  -10.948 20.552  1.00 37.06  ?  181 ASP A OD1   1 
ATOM   1348 O  OD2   . ASP A 1 181 ? 19.321  -9.426  20.885  1.00 34.20  ?  181 ASP A OD2   1 
ATOM   1349 N  N     . PHE A 1 182 ? 16.870  -6.661  19.066  1.00 32.93  ?  182 PHE A N     1 
ATOM   1350 C  CA    . PHE A 1 182 ? 16.567  -5.556  19.972  1.00 29.03  ?  182 PHE A CA    1 
ATOM   1351 C  C     . PHE A 1 182 ? 15.081  -5.234  19.962  1.00 31.58  ?  182 PHE A C     1 
ATOM   1352 O  O     . PHE A 1 182 ? 14.498  -4.942  21.010  1.00 28.71  ?  182 PHE A O     1 
ATOM   1353 C  CB    . PHE A 1 182 ? 17.367  -4.321  19.582  1.00 26.58  ?  182 PHE A CB    1 
ATOM   1354 C  CG    . PHE A 1 182 ? 17.177  -3.128  20.508  1.00 30.13  ?  182 PHE A CG    1 
ATOM   1355 C  CD1   . PHE A 1 182 ? 17.730  -3.124  21.778  1.00 30.32  ?  182 PHE A CD1   1 
ATOM   1356 C  CD2   . PHE A 1 182 ? 16.485  -1.993  20.080  1.00 25.70  ?  182 PHE A CD2   1 
ATOM   1357 C  CE1   . PHE A 1 182 ? 17.592  -2.043  22.613  1.00 32.36  ?  182 PHE A CE1   1 
ATOM   1358 C  CE2   . PHE A 1 182 ? 16.344  -0.899  20.908  1.00 27.02  ?  182 PHE A CE2   1 
ATOM   1359 C  CZ    . PHE A 1 182 ? 16.890  -0.927  22.184  1.00 26.52  ?  182 PHE A CZ    1 
ATOM   1360 N  N     . PHE A 1 183 ? 14.459  -5.285  18.784  1.00 31.58  ?  183 PHE A N     1 
ATOM   1361 C  CA    . PHE A 1 183 ? 13.048  -4.972  18.681  1.00 29.21  ?  183 PHE A CA    1 
ATOM   1362 C  C     . PHE A 1 183 ? 12.214  -5.964  19.496  1.00 30.27  ?  183 PHE A C     1 
ATOM   1363 O  O     . PHE A 1 183 ? 11.312  -5.561  20.241  1.00 31.22  ?  183 PHE A O     1 
ATOM   1364 C  CB    . PHE A 1 183 ? 12.628  -4.944  17.204  1.00 29.38  ?  183 PHE A CB    1 
ATOM   1365 C  CG    . PHE A 1 183 ? 13.373  -3.938  16.379  1.00 29.58  ?  183 PHE A CG    1 
ATOM   1366 C  CD1   . PHE A 1 183 ? 13.913  -2.803  16.962  1.00 32.82  ?  183 PHE A CD1   1 
ATOM   1367 C  CD2   . PHE A 1 183 ? 13.540  -4.128  15.003  1.00 32.77  ?  183 PHE A CD2   1 
ATOM   1368 C  CE1   . PHE A 1 183 ? 14.654  -1.882  16.188  1.00 30.98  ?  183 PHE A CE1   1 
ATOM   1369 C  CE2   . PHE A 1 183 ? 14.258  -3.217  14.230  1.00 29.83  ?  183 PHE A CE2   1 
ATOM   1370 C  CZ    . PHE A 1 183 ? 14.803  -2.089  14.812  1.00 28.43  ?  183 PHE A CZ    1 
ATOM   1371 N  N     . LEU A 1 184 ? 12.539  -7.257  19.407  1.00 27.18  ?  184 LEU A N     1 
ATOM   1372 C  CA    . LEU A 1 184 ? 11.894  -8.261  20.243  1.00 25.67  ?  184 LEU A CA    1 
ATOM   1373 C  C     . LEU A 1 184 ? 12.225  -8.074  21.717  1.00 29.63  ?  184 LEU A C     1 
ATOM   1374 O  O     . LEU A 1 184 ? 11.370  -8.355  22.571  1.00 31.85  ?  184 LEU A O     1 
ATOM   1375 C  CB    . LEU A 1 184 ? 12.299  -9.662  19.798  1.00 25.26  ?  184 LEU A CB    1 
ATOM   1376 C  CG    . LEU A 1 184 ? 12.058  -10.026 18.328  1.00 26.57  ?  184 LEU A CG    1 
ATOM   1377 C  CD1   . LEU A 1 184 ? 12.651  -11.368 18.067  1.00 34.90  ?  184 LEU A CD1   1 
ATOM   1378 C  CD2   . LEU A 1 184 ? 10.615  -10.076 17.973  1.00 29.19  ?  184 LEU A CD2   1 
ATOM   1379 N  N     . ARG A 1 185 ? 13.446  -7.608  22.043  1.00 26.53  ?  185 ARG A N     1 
ATOM   1380 C  CA    . ARG A 1 185 ? 13.768  -7.277  23.433  1.00 29.34  ?  185 ARG A CA    1 
ATOM   1381 C  C     . ARG A 1 185 ? 12.782  -6.242  23.990  1.00 31.93  ?  185 ARG A C     1 
ATOM   1382 O  O     . ARG A 1 185 ? 12.342  -6.344  25.144  1.00 27.45  ?  185 ARG A O     1 
ATOM   1383 C  CB    . ARG A 1 185 ? 15.215  -6.752  23.555  1.00 27.96  ?  185 ARG A CB    1 
ATOM   1384 C  CG    . ARG A 1 185 ? 15.682  -6.499  25.028  1.00 29.04  ?  185 ARG A CG    1 
ATOM   1385 C  CD    . ARG A 1 185 ? 17.207  -6.317  25.214  1.00 25.95  ?  185 ARG A CD    1 
ATOM   1386 N  NE    . ARG A 1 185 ? 17.875  -7.598  25.006  1.00 35.02  ?  185 ARG A NE    1 
ATOM   1387 C  CZ    . ARG A 1 185 ? 18.337  -8.029  23.835  1.00 34.43  ?  185 ARG A CZ    1 
ATOM   1388 N  NH1   . ARG A 1 185 ? 18.393  -7.231  22.773  1.00 32.59  ?  185 ARG A NH1   1 
ATOM   1389 N  NH2   . ARG A 1 185 ? 18.710  -9.305  23.715  1.00 35.88  ?  185 ARG A NH2   1 
ATOM   1390 N  N     . LEU A 1 186 ? 12.452  -5.222  23.186  1.00 30.89  ?  186 LEU A N     1 
ATOM   1391 C  CA    . LEU A 1 186 ? 11.556  -4.166  23.629  1.00 28.84  ?  186 LEU A CA    1 
ATOM   1392 C  C     . LEU A 1 186 ? 10.125  -4.680  23.681  1.00 31.30  ?  186 LEU A C     1 
ATOM   1393 O  O     . LEU A 1 186 ? 9.443   -4.568  24.713  1.00 32.62  ?  186 LEU A O     1 
ATOM   1394 C  CB    . LEU A 1 186 ? 11.669  -2.964  22.689  1.00 27.51  ?  186 LEU A CB    1 
ATOM   1395 C  CG    . LEU A 1 186 ? 12.970  -2.161  22.765  1.00 28.95  ?  186 LEU A CG    1 
ATOM   1396 C  CD1   . LEU A 1 186 ? 12.850  -0.728  22.193  1.00 31.53  ?  186 LEU A CD1   1 
ATOM   1397 C  CD2   . LEU A 1 186 ? 13.538  -2.123  24.189  1.00 26.93  ?  186 LEU A CD2   1 
ATOM   1398 N  N     . ALA A 1 187 ? 9.682   -5.316  22.590  1.00 32.79  ?  187 ALA A N     1 
ATOM   1399 C  CA    . ALA A 1 187 ? 8.270   -5.664  22.429  1.00 35.82  ?  187 ALA A CA    1 
ATOM   1400 C  C     . ALA A 1 187 ? 7.863   -6.810  23.348  1.00 34.18  ?  187 ALA A C     1 
ATOM   1401 O  O     . ALA A 1 187 ? 6.834   -6.740  24.026  1.00 35.39  ?  187 ALA A O     1 
ATOM   1402 C  CB    . ALA A 1 187 ? 7.991   -6.005  20.964  1.00 32.18  ?  187 ALA A CB    1 
ATOM   1403 N  N     . HIS A 1 188 ? 8.659   -7.872  23.383  1.00 31.43  ?  188 HIS A N     1 
ATOM   1404 C  CA    . HIS A 1 188 ? 8.351   -9.023  24.214  1.00 33.83  ?  188 HIS A CA    1 
ATOM   1405 C  C     . HIS A 1 188 ? 9.033   -8.892  25.569  1.00 35.37  ?  188 HIS A C     1 
ATOM   1406 O  O     . HIS A 1 188 ? 8.365   -8.913  26.611  1.00 33.46  ?  188 HIS A O     1 
ATOM   1407 C  CB    . HIS A 1 188 ? 8.792   -10.321 23.522  1.00 31.88  ?  188 HIS A CB    1 
ATOM   1408 C  CG    . HIS A 1 188 ? 8.107   -10.573 22.214  1.00 34.26  ?  188 HIS A CG    1 
ATOM   1409 N  ND1   . HIS A 1 188 ? 8.254   -11.752 21.507  1.00 37.18  ?  188 HIS A ND1   1 
ATOM   1410 C  CD2   . HIS A 1 188 ? 7.243   -9.815  21.499  1.00 36.40  ?  188 HIS A CD2   1 
ATOM   1411 C  CE1   . HIS A 1 188 ? 7.525   -11.701 20.404  1.00 34.26  ?  188 HIS A CE1   1 
ATOM   1412 N  NE2   . HIS A 1 188 ? 6.904   -10.534 20.373  1.00 41.23  ?  188 HIS A NE2   1 
ATOM   1413 N  N     . GLY A 1 189 ? 10.362  -8.751  25.564  1.00 30.24  ?  189 GLY A N     1 
ATOM   1414 C  CA    . GLY A 1 189 ? 11.102  -8.745  26.815  1.00 29.65  ?  189 GLY A CA    1 
ATOM   1415 C  C     . GLY A 1 189 ? 10.684  -7.630  27.759  1.00 35.40  ?  189 GLY A C     1 
ATOM   1416 O  O     . GLY A 1 189 ? 10.784  -7.778  28.979  1.00 32.16  ?  189 GLY A O     1 
ATOM   1417 N  N     . HIS A 1 190 ? 10.198  -6.508  27.215  1.00 32.10  ?  190 HIS A N     1 
ATOM   1418 C  CA    . HIS A 1 190 ? 9.864   -5.346  28.024  1.00 34.32  ?  190 HIS A CA    1 
ATOM   1419 C  C     . HIS A 1 190 ? 8.470   -4.817  27.703  1.00 38.04  ?  190 HIS A C     1 
ATOM   1420 O  O     . HIS A 1 190 ? 8.121   -3.720  28.140  1.00 32.92  ?  190 HIS A O     1 
ATOM   1421 C  CB    . HIS A 1 190 ? 10.927  -4.250  27.838  1.00 28.44  ?  190 HIS A CB    1 
ATOM   1422 C  CG    . HIS A 1 190 ? 12.240  -4.582  28.487  1.00 36.34  ?  190 HIS A CG    1 
ATOM   1423 N  ND1   . HIS A 1 190 ? 12.573  -4.156  29.756  1.00 35.50  ?  190 HIS A ND1   1 
ATOM   1424 C  CD2   . HIS A 1 190 ? 13.293  -5.320  28.052  1.00 34.10  ?  190 HIS A CD2   1 
ATOM   1425 C  CE1   . HIS A 1 190 ? 13.780  -4.603  30.068  1.00 33.78  ?  190 HIS A CE1   1 
ATOM   1426 N  NE2   . HIS A 1 190 ? 14.238  -5.309  29.051  1.00 34.51  ?  190 HIS A NE2   1 
ATOM   1427 N  N     . LYS A 1 191 ? 7.678   -5.563  26.938  1.00 37.35  ?  191 LYS A N     1 
ATOM   1428 C  CA    . LYS A 1 191 ? 6.263   -5.255  26.718  1.00 42.11  ?  191 LYS A CA    1 
ATOM   1429 C  C     . LYS A 1 191 ? 6.028   -3.874  26.086  1.00 37.78  ?  191 LYS A C     1 
ATOM   1430 O  O     . LYS A 1 191 ? 4.965   -3.274  26.289  1.00 39.58  ?  191 LYS A O     1 
ATOM   1431 C  CB    . LYS A 1 191 ? 5.468   -5.394  28.026  1.00 38.06  ?  191 LYS A CB    1 
ATOM   1432 C  CG    . LYS A 1 191 ? 5.910   -6.609  28.860  1.00 42.51  ?  191 LYS A CG    1 
ATOM   1433 C  CD    . LYS A 1 191 ? 5.112   -6.732  30.152  1.00 53.38  ?  191 LYS A CD    1 
ATOM   1434 C  CE    . LYS A 1 191 ? 4.455   -8.119  30.256  1.00 62.55  ?  191 LYS A CE    1 
ATOM   1435 N  NZ    . LYS A 1 191 ? 3.764   -8.369  31.567  1.00 61.09  ?  191 LYS A NZ    1 
ATOM   1436 N  N     . TYR A 1 192 ? 6.987   -3.348  25.317  1.00 31.07  ?  192 TYR A N     1 
ATOM   1437 C  CA    . TYR A 1 192 ? 6.739   -2.092  24.601  1.00 35.44  ?  192 TYR A CA    1 
ATOM   1438 C  C     . TYR A 1 192 ? 5.513   -2.208  23.686  1.00 32.65  ?  192 TYR A C     1 
ATOM   1439 O  O     . TYR A 1 192 ? 5.262   -3.241  23.048  1.00 31.19  ?  192 TYR A O     1 
ATOM   1440 C  CB    . TYR A 1 192 ? 7.957   -1.659  23.762  1.00 27.88  ?  192 TYR A CB    1 
ATOM   1441 C  CG    . TYR A 1 192 ? 8.988   -0.823  24.488  1.00 29.69  ?  192 TYR A CG    1 
ATOM   1442 C  CD1   . TYR A 1 192 ? 9.483   -1.226  25.716  1.00 30.19  ?  192 TYR A CD1   1 
ATOM   1443 C  CD2   . TYR A 1 192 ? 9.516   0.338   23.911  1.00 28.32  ?  192 TYR A CD2   1 
ATOM   1444 C  CE1   . TYR A 1 192 ? 10.438  -0.506  26.359  1.00 32.28  ?  192 TYR A CE1   1 
ATOM   1445 C  CE2   . TYR A 1 192 ? 10.479  1.068   24.553  1.00 28.57  ?  192 TYR A CE2   1 
ATOM   1446 C  CZ    . TYR A 1 192 ? 10.924  0.650   25.780  1.00 32.45  ?  192 TYR A CZ    1 
ATOM   1447 O  OH    . TYR A 1 192 ? 11.869  1.346   26.461  1.00 33.97  ?  192 TYR A OH    1 
ATOM   1448 N  N     . ARG A 1 193 ? 4.723   -1.149  23.665  1.00 32.08  ?  193 ARG A N     1 
ATOM   1449 C  CA    . ARG A 1 193 ? 3.522   -1.105  22.812  1.00 33.98  ?  193 ARG A CA    1 
ATOM   1450 C  C     . ARG A 1 193 ? 3.963   -0.645  21.431  1.00 32.35  ?  193 ARG A C     1 
ATOM   1451 O  O     . ARG A 1 193 ? 4.294   0.500   21.292  1.00 31.85  ?  193 ARG A O     1 
ATOM   1452 C  CB    . ARG A 1 193 ? 2.432   -0.250  23.450  1.00 32.39  ?  193 ARG A CB    1 
ATOM   1453 C  CG    . ARG A 1 193 ? 1.810   -0.907  24.667  1.00 34.69  ?  193 ARG A CG    1 
ATOM   1454 C  CD    . ARG A 1 193 ? 1.093   0.008   25.623  1.00 38.79  ?  193 ARG A CD    1 
ATOM   1455 N  NE    . ARG A 1 193 ? 0.301   -0.844  26.475  1.00 46.97  ?  193 ARG A NE    1 
ATOM   1456 C  CZ    . ARG A 1 193 ? -0.822  -0.510  27.082  1.00 46.93  ?  193 ARG A CZ    1 
ATOM   1457 N  NH1   . ARG A 1 193 ? -1.322  0.701   26.965  1.00 37.91  ?  193 ARG A NH1   1 
ATOM   1458 N  NH2   . ARG A 1 193 ? -1.439  -1.405  27.820  1.00 51.18  ?  193 ARG A NH2   1 
ATOM   1459 N  N     . VAL A 1 194 ? 3.972   -1.563  20.475  1.00 27.32  ?  194 VAL A N     1 
ATOM   1460 C  CA    . VAL A 1 194 ? 4.450   -1.253  19.107  1.00 31.19  ?  194 VAL A CA    1 
ATOM   1461 C  C     . VAL A 1 194 ? 3.304   -0.692  18.280  1.00 31.14  ?  194 VAL A C     1 
ATOM   1462 O  O     . VAL A 1 194 ? 2.235   -1.238  18.312  1.00 34.52  ?  194 VAL A O     1 
ATOM   1463 C  CB    . VAL A 1 194 ? 5.103   -2.471  18.431  1.00 34.59  ?  194 VAL A CB    1 
ATOM   1464 C  CG1   . VAL A 1 194 ? 5.617   -2.137  17.047  1.00 24.95  ?  194 VAL A CG1   1 
ATOM   1465 C  CG2   . VAL A 1 194 ? 6.210   -3.037  19.293  1.00 30.16  ?  194 VAL A CG2   1 
ATOM   1466 N  N     . VAL A 1 195 ? 3.588   0.368   17.555  1.00 31.25  ?  195 VAL A N     1 
ATOM   1467 C  CA    . VAL A 1 195 ? 2.566   1.015   16.706  1.00 32.15  ?  195 VAL A CA    1 
ATOM   1468 C  C     . VAL A 1 195 ? 3.226   1.370   15.381  1.00 33.05  ?  195 VAL A C     1 
ATOM   1469 O  O     . VAL A 1 195 ? 4.350   1.841   15.407  1.00 34.28  ?  195 VAL A O     1 
ATOM   1470 C  CB    . VAL A 1 195 ? 1.987   2.240   17.430  1.00 36.17  ?  195 VAL A CB    1 
ATOM   1471 C  CG1   . VAL A 1 195 ? 1.835   3.434   16.526  1.00 35.01  ?  195 VAL A CG1   1 
ATOM   1472 C  CG2   . VAL A 1 195 ? 0.686   1.926   18.124  1.00 31.62  ?  195 VAL A CG2   1 
ATOM   1473 N  N     . HIS A 1 196 ? 2.544   1.090   14.276  1.00 30.91  ?  196 HIS A N     1 
ATOM   1474 C  CA    . HIS A 1 196 ? 3.064   1.445   12.936  1.00 32.05  ?  196 HIS A CA    1 
ATOM   1475 C  C     . HIS A 1 196 ? 2.546   2.828   12.548  1.00 36.07  ?  196 HIS A C     1 
ATOM   1476 O  O     . HIS A 1 196 ? 1.409   3.127   12.820  1.00 33.93  ?  196 HIS A O     1 
ATOM   1477 C  CB    . HIS A 1 196 ? 2.710   0.389   11.894  1.00 33.65  ?  196 HIS A CB    1 
ATOM   1478 C  CG    . HIS A 1 196 ? 3.114   0.751   10.506  1.00 37.43  ?  196 HIS A CG    1 
ATOM   1479 N  ND1   . HIS A 1 196 ? 2.283   0.585   9.438   1.00 33.90  ?  196 HIS A ND1   1 
ATOM   1480 C  CD2   . HIS A 1 196 ? 4.260   1.239   10.007  1.00 35.36  ?  196 HIS A CD2   1 
ATOM   1481 C  CE1   . HIS A 1 196 ? 2.887   0.963   8.353   1.00 34.06  ?  196 HIS A CE1   1 
ATOM   1482 N  NE2   . HIS A 1 196 ? 4.091   1.370   8.678   1.00 41.78  ?  196 HIS A NE2   1 
ATOM   1483 N  N     . GLN A 1 197 ? 3.426   3.645   11.998  1.00 32.72  ?  197 GLN A N     1 
ATOM   1484 C  CA    . GLN A 1 197 ? 3.071   4.978   11.526  1.00 34.78  ?  197 GLN A CA    1 
ATOM   1485 C  C     . GLN A 1 197 ? 3.237   5.021   10.011  1.00 38.07  ?  197 GLN A C     1 
ATOM   1486 O  O     . GLN A 1 197 ? 4.326   5.329   9.502   1.00 36.19  ?  197 GLN A O     1 
ATOM   1487 C  CB    . GLN A 1 197 ? 3.938   6.047   12.196  1.00 33.35  ?  197 GLN A CB    1 
ATOM   1488 C  CG    . GLN A 1 197 ? 3.864   7.445   11.583  1.00 32.75  ?  197 GLN A CG    1 
ATOM   1489 C  CD    . GLN A 1 197 ? 2.430   7.968   11.329  1.00 40.02  ?  197 GLN A CD    1 
ATOM   1490 O  OE1   . GLN A 1 197 ? 1.660   7.400   10.544  1.00 39.03  ?  197 GLN A OE1   1 
ATOM   1491 N  NE2   . GLN A 1 197 ? 2.100   9.087   11.961  1.00 33.30  ?  197 GLN A NE2   1 
ATOM   1492 N  N     . PRO A 1 198 ? 2.194   4.721   9.239   1.00 39.88  ?  198 PRO A N     1 
ATOM   1493 C  CA    . PRO A 1 198 ? 2.358   4.615   7.786   1.00 35.91  ?  198 PRO A CA    1 
ATOM   1494 C  C     . PRO A 1 198 ? 2.369   5.944   7.054   1.00 39.20  ?  198 PRO A C     1 
ATOM   1495 O  O     . PRO A 1 198 ? 2.463   5.932   5.825   1.00 41.42  ?  198 PRO A O     1 
ATOM   1496 C  CB    . PRO A 1 198 ? 1.144   3.787   7.377   1.00 38.67  ?  198 PRO A CB    1 
ATOM   1497 C  CG    . PRO A 1 198 ? 0.080   4.254   8.376   1.00 35.64  ?  198 PRO A CG    1 
ATOM   1498 C  CD    . PRO A 1 198 ? 0.822   4.417   9.672   1.00 36.78  ?  198 PRO A CD    1 
ATOM   1499 N  N     . GLU A 1 199 ? 2.291   7.084   7.754   1.00 44.60  ?  199 GLU A N     1 
ATOM   1500 C  CA    . GLU A 1 199 ? 2.255   8.410   7.133   1.00 37.80  ?  199 GLU A CA    1 
ATOM   1501 C  C     . GLU A 1 199 ? 3.614   9.105   7.093   1.00 42.35  ?  199 GLU A C     1 
ATOM   1502 O  O     . GLU A 1 199 ? 3.696   10.273  6.685   1.00 39.76  ?  199 GLU A O     1 
ATOM   1503 C  CB    . GLU A 1 199 ? 1.255   9.300   7.862   1.00 40.27  ?  199 GLU A CB    1 
ATOM   1504 C  CG    . GLU A 1 199 ? -0.068  9.418   7.130   1.00 48.79  ?  199 GLU A CG    1 
ATOM   1505 C  CD    . GLU A 1 199 ? -1.239  9.491   8.074   1.00 49.13  ?  199 GLU A CD    1 
ATOM   1506 O  OE1   . GLU A 1 199 ? -1.134  10.200  9.102   1.00 46.30  ?  199 GLU A OE1   1 
ATOM   1507 O  OE2   . GLU A 1 199 ? -2.260  8.832   7.793   1.00 57.69  ?  199 GLU A OE2   1 
ATOM   1508 N  N     . VAL A 1 200 ? 4.679   8.414   7.483   1.00 39.05  ?  200 VAL A N     1 
ATOM   1509 C  CA    . VAL A 1 200 ? 6.021   8.970   7.529   1.00 34.37  ?  200 VAL A CA    1 
ATOM   1510 C  C     . VAL A 1 200 ? 6.930   7.971   6.840   1.00 37.75  ?  200 VAL A C     1 
ATOM   1511 O  O     . VAL A 1 200 ? 6.705   6.755   6.950   1.00 38.39  ?  200 VAL A O     1 
ATOM   1512 C  CB    . VAL A 1 200 ? 6.480   9.213   8.989   1.00 35.07  ?  200 VAL A CB    1 
ATOM   1513 C  CG1   . VAL A 1 200 ? 7.949   9.588   9.047   1.00 31.87  ?  200 VAL A CG1   1 
ATOM   1514 C  CG2   . VAL A 1 200 ? 5.624   10.232  9.654   1.00 28.19  ?  200 VAL A CG2   1 
ATOM   1515 N  N     . ALA A 1 201 ? 7.956   8.470   6.133   1.00 32.90  ?  201 ALA A N     1 
ATOM   1516 C  CA    . ALA A 1 201 ? 8.896   7.589   5.455   1.00 35.14  ?  201 ALA A CA    1 
ATOM   1517 C  C     . ALA A 1 201 ? 10.328  8.054   5.661   1.00 34.53  ?  201 ALA A C     1 
ATOM   1518 O  O     . ALA A 1 201 ? 10.611  9.257   5.681   1.00 37.58  ?  201 ALA A O     1 
ATOM   1519 C  CB    . ALA A 1 201 ? 8.602   7.493   3.945   1.00 38.21  ?  201 ALA A CB    1 
ATOM   1520 N  N     . ILE A 1 202 ? 11.220  7.081   5.814   1.00 36.04  ?  202 ILE A N     1 
ATOM   1521 C  CA    . ILE A 1 202 ? 12.648  7.291   5.679   1.00 38.27  ?  202 ILE A CA    1 
ATOM   1522 C  C     . ILE A 1 202 ? 13.091  6.759   4.329   1.00 38.66  ?  202 ILE A C     1 
ATOM   1523 O  O     . ILE A 1 202 ? 12.422  5.938   3.690   1.00 38.54  ?  202 ILE A O     1 
ATOM   1524 C  CB    . ILE A 1 202 ? 13.503  6.619   6.778   1.00 37.29  ?  202 ILE A CB    1 
ATOM   1525 C  CG1   . ILE A 1 202 ? 13.650  5.122   6.453   1.00 34.39  ?  202 ILE A CG1   1 
ATOM   1526 C  CG2   . ILE A 1 202 ? 12.971  6.952   8.161   1.00 38.34  ?  202 ILE A CG2   1 
ATOM   1527 C  CD1   . ILE A 1 202 ? 14.419  4.294   7.471   1.00 35.49  ?  202 ILE A CD1   1 
ATOM   1528 N  N     . ALA A 1 203 ? 14.258  7.220   3.906   1.00 40.80  ?  203 ALA A N     1 
ATOM   1529 C  CA    . ALA A 1 203 ? 14.974  6.635   2.787   1.00 39.99  ?  203 ALA A CA    1 
ATOM   1530 C  C     . ALA A 1 203 ? 16.080  5.774   3.373   1.00 42.92  ?  203 ALA A C     1 
ATOM   1531 O  O     . ALA A 1 203 ? 16.976  6.288   4.053   1.00 40.22  ?  203 ALA A O     1 
ATOM   1532 C  CB    . ALA A 1 203 ? 15.545  7.706   1.862   1.00 33.90  ?  203 ALA A CB    1 
ATOM   1533 N  N     . LEU A 1 204 ? 16.000  4.467   3.142   1.00 43.49  ?  204 LEU A N     1 
ATOM   1534 C  CA    . LEU A 1 204 ? 17.060  3.559   3.547   1.00 42.65  ?  204 LEU A CA    1 
ATOM   1535 C  C     . LEU A 1 204 ? 17.933  3.237   2.328   1.00 44.38  ?  204 LEU A C     1 
ATOM   1536 O  O     . LEU A 1 204 ? 17.457  2.688   1.326   1.00 42.26  ?  204 LEU A O     1 
ATOM   1537 C  CB    . LEU A 1 204 ? 16.475  2.316   4.216   1.00 41.53  ?  204 LEU A CB    1 
ATOM   1538 C  CG    . LEU A 1 204 ? 17.500  1.442   4.921   1.00 49.24  ?  204 LEU A CG    1 
ATOM   1539 C  CD1   . LEU A 1 204 ? 17.032  1.135   6.286   1.00 42.92  ?  204 LEU A CD1   1 
ATOM   1540 C  CD2   . LEU A 1 204 ? 17.640  0.133   4.183   1.00 54.00  ?  204 LEU A CD2   1 
ATOM   1541 N  N     . HIS A 1 205 ? 19.190  3.644   2.397   1.00 43.51  ?  205 HIS A N     1 
ATOM   1542 C  CA    . HIS A 1 205 ? 20.145  3.391   1.331   1.00 52.50  ?  205 HIS A CA    1 
ATOM   1543 C  C     . HIS A 1 205 ? 20.757  2.013   1.528   1.00 52.67  ?  205 HIS A C     1 
ATOM   1544 O  O     . HIS A 1 205 ? 21.305  1.724   2.600   1.00 54.63  ?  205 HIS A O     1 
ATOM   1545 C  CB    . HIS A 1 205 ? 21.223  4.464   1.334   1.00 53.89  ?  205 HIS A CB    1 
ATOM   1546 N  N     . ARG A 1 206 ? 20.637  1.164   0.508   1.00 54.65  ?  206 ARG A N     1 
ATOM   1547 C  CA    . ARG A 1 206 ? 21.241  -0.168  0.531   1.00 61.88  ?  206 ARG A CA    1 
ATOM   1548 C  C     . ARG A 1 206 ? 22.097  -0.417  -0.703  1.00 58.88  ?  206 ARG A C     1 
ATOM   1549 O  O     . ARG A 1 206 ? 21.582  -0.369  -1.819  1.00 58.65  ?  206 ARG A O     1 
ATOM   1550 C  CB    . ARG A 1 206 ? 20.169  -1.245  0.614   1.00 56.56  ?  206 ARG A CB    1 
ATOM   1551 C  CG    . ARG A 1 206 ? 19.569  -1.367  1.968   1.00 60.54  ?  206 ARG A CG    1 
ATOM   1552 C  CD    . ARG A 1 206 ? 20.351  -2.291  2.902   1.00 63.14  ?  206 ARG A CD    1 
ATOM   1553 N  NE    . ARG A 1 206 ? 19.448  -3.200  3.603   1.00 63.59  ?  206 ARG A NE    1 
ATOM   1554 C  CZ    . ARG A 1 206 ? 19.118  -3.095  4.887   1.00 69.08  ?  206 ARG A CZ    1 
ATOM   1555 N  NH1   . ARG A 1 206 ? 19.605  -2.124  5.654   1.00 63.69  ?  206 ARG A NH1   1 
ATOM   1556 N  NH2   . ARG A 1 206 ? 18.271  -3.983  5.416   1.00 72.59  ?  206 ARG A NH2   1 
ATOM   1557 N  N     . PRO A 1 216 ? 30.300  -14.274 -6.624  1.00 76.13  ?  216 PRO A N     1 
ATOM   1558 C  CA    . PRO A 1 216 ? 31.193  -14.267 -5.455  1.00 73.36  ?  216 PRO A CA    1 
ATOM   1559 C  C     . PRO A 1 216 ? 30.992  -15.500 -4.583  1.00 72.89  ?  216 PRO A C     1 
ATOM   1560 O  O     . PRO A 1 216 ? 31.551  -15.551 -3.492  1.00 69.20  ?  216 PRO A O     1 
ATOM   1561 C  CB    . PRO A 1 216 ? 30.766  -13.003 -4.685  1.00 69.94  ?  216 PRO A CB    1 
ATOM   1562 C  CG    . PRO A 1 216 ? 29.768  -12.291 -5.599  1.00 78.24  ?  216 PRO A CG    1 
ATOM   1563 C  CD    . PRO A 1 216 ? 29.155  -13.376 -6.426  1.00 68.70  ?  216 PRO A CD    1 
ATOM   1564 N  N     . THR A 1 217 ? 30.224  -16.474 -5.096  1.00 74.41  ?  217 THR A N     1 
ATOM   1565 C  CA    . THR A 1 217 ? 29.431  -17.445 -4.331  1.00 69.40  ?  217 THR A CA    1 
ATOM   1566 C  C     . THR A 1 217 ? 29.956  -17.831 -2.946  1.00 65.36  ?  217 THR A C     1 
ATOM   1567 O  O     . THR A 1 217 ? 29.221  -17.696 -1.970  1.00 66.52  ?  217 THR A O     1 
ATOM   1568 C  CB    . THR A 1 217 ? 29.219  -18.707 -5.163  1.00 66.39  ?  217 THR A CB    1 
ATOM   1569 O  OG1   . THR A 1 217 ? 30.441  -19.445 -5.218  1.00 61.31  ?  217 THR A OG1   1 
ATOM   1570 C  CG2   . THR A 1 217 ? 28.742  -18.341 -6.564  1.00 62.76  ?  217 THR A CG2   1 
ATOM   1571 N  N     . SER A 1 218 ? 31.212  -18.269 -2.822  1.00 63.49  ?  218 SER A N     1 
ATOM   1572 C  CA    . SER A 1 218 ? 31.774  -18.617 -1.490  1.00 61.09  ?  218 SER A CA    1 
ATOM   1573 C  C     . SER A 1 218 ? 31.612  -17.415 -0.562  1.00 60.83  ?  218 SER A C     1 
ATOM   1574 O  O     . SER A 1 218 ? 31.348  -17.624 0.604   1.00 61.74  ?  218 SER A O     1 
ATOM   1575 C  CB    . SER A 1 218 ? 33.199  -19.092 -1.567  1.00 66.46  ?  218 SER A CB    1 
ATOM   1576 O  OG    . SER A 1 218 ? 34.069  -18.075 -2.036  1.00 62.43  ?  218 SER A OG    1 
ATOM   1577 N  N     . ASP A 1 219 ? 31.673  -16.224 -1.126  1.00 67.85  ?  219 ASP A N     1 
ATOM   1578 C  CA    . ASP A 1 219 ? 31.478  -15.012 -0.311  1.00 65.17  ?  219 ASP A CA    1 
ATOM   1579 C  C     . ASP A 1 219 ? 30.058  -15.078 0.235   1.00 59.03  ?  219 ASP A C     1 
ATOM   1580 O  O     . ASP A 1 219 ? 29.891  -15.102 1.447   1.00 59.44  ?  219 ASP A O     1 
ATOM   1581 C  CB    . ASP A 1 219 ? 31.563  -13.791 -1.221  1.00 69.64  ?  219 ASP A CB    1 
ATOM   1582 C  CG    . ASP A 1 219 ? 32.892  -13.074 -1.170  1.00 71.66  ?  219 ASP A CG    1 
ATOM   1583 O  OD1   . ASP A 1 219 ? 33.466  -13.013 -0.076  1.00 69.89  ?  219 ASP A OD1   1 
ATOM   1584 O  OD2   . ASP A 1 219 ? 33.326  -12.571 -2.225  1.00 69.95  ?  219 ASP A OD2   1 
ATOM   1585 N  N     . ASP A 1 220 ? 29.090  -15.082 -0.689  1.00 59.26  ?  220 ASP A N     1 
ATOM   1586 C  CA    . ASP A 1 220 ? 27.627  -15.054 -0.414  1.00 60.26  ?  220 ASP A CA    1 
ATOM   1587 C  C     . ASP A 1 220 ? 27.170  -16.211 0.483   1.00 62.71  ?  220 ASP A C     1 
ATOM   1588 O  O     . ASP A 1 220 ? 26.405  -15.931 1.427   1.00 60.98  ?  220 ASP A O     1 
ATOM   1589 C  CB    . ASP A 1 220 ? 26.822  -15.013 -1.716  1.00 60.29  ?  220 ASP A CB    1 
ATOM   1590 C  CG    . ASP A 1 220 ? 27.655  -14.631 -2.928  1.00 67.98  ?  220 ASP A CG    1 
ATOM   1591 O  OD1   . ASP A 1 220 ? 27.189  -13.782 -3.714  1.00 68.38  ?  220 ASP A OD1   1 
ATOM   1592 O  OD2   . ASP A 1 220 ? 28.762  -15.185 -3.075  1.00 71.48  ?  220 ASP A OD2   1 
ATOM   1593 N  N     . ILE A 1 221 ? 27.589  -17.451 0.200   1.00 54.05  ?  221 ILE A N     1 
ATOM   1594 C  CA    . ILE A 1 221 ? 27.108  -18.553 1.005   1.00 54.91  ?  221 ILE A CA    1 
ATOM   1595 C  C     . ILE A 1 221 ? 27.491  -18.338 2.457   1.00 54.84  ?  221 ILE A C     1 
ATOM   1596 O  O     . ILE A 1 221 ? 26.661  -18.481 3.365   1.00 57.53  ?  221 ILE A O     1 
ATOM   1597 C  CB    . ILE A 1 221 ? 27.634  -19.888 0.479   1.00 55.02  ?  221 ILE A CB    1 
ATOM   1598 C  CG1   . ILE A 1 221 ? 27.348  -20.020 -1.017  1.00 59.69  ?  221 ILE A CG1   1 
ATOM   1599 C  CG2   . ILE A 1 221 ? 26.939  -20.974 1.227   1.00 50.82  ?  221 ILE A CG2   1 
ATOM   1600 C  CD1   . ILE A 1 221 ? 27.718  -21.392 -1.620  1.00 52.36  ?  221 ILE A CD1   1 
ATOM   1601 N  N     . ALA A 1 222 ? 28.743  -17.976 2.707   1.00 50.02  ?  222 ALA A N     1 
ATOM   1602 C  CA    . ALA A 1 222 ? 29.136  -17.783 4.096   1.00 55.97  ?  222 ALA A CA    1 
ATOM   1603 C  C     . ALA A 1 222 ? 28.439  -16.572 4.714   1.00 56.06  ?  222 ALA A C     1 
ATOM   1604 O  O     . ALA A 1 222 ? 28.284  -16.508 5.936   1.00 52.32  ?  222 ALA A O     1 
ATOM   1605 C  CB    . ALA A 1 222 ? 30.654  -17.655 4.205   1.00 50.62  ?  222 ALA A CB    1 
ATOM   1606 N  N     . ALA A 1 223 ? 28.009  -15.612 3.895   1.00 56.03  ?  223 ALA A N     1 
ATOM   1607 C  CA    . ALA A 1 223 ? 27.380  -14.411 4.432   1.00 56.19  ?  223 ALA A CA    1 
ATOM   1608 C  C     . ALA A 1 223 ? 25.972  -14.712 4.925   1.00 55.05  ?  223 ALA A C     1 
ATOM   1609 O  O     . ALA A 1 223 ? 25.631  -14.456 6.089   1.00 54.07  ?  223 ALA A O     1 
ATOM   1610 C  CB    . ALA A 1 223 ? 27.360  -13.322 3.356   1.00 52.43  ?  223 ALA A CB    1 
ATOM   1611 N  N     . LEU A 1 224 ? 25.146  -15.271 4.043   1.00 55.26  ?  224 LEU A N     1 
ATOM   1612 C  CA    . LEU A 1 224 ? 23.781  -15.640 4.389   1.00 58.03  ?  224 LEU A CA    1 
ATOM   1613 C  C     . LEU A 1 224 ? 23.736  -16.681 5.502   1.00 55.08  ?  224 LEU A C     1 
ATOM   1614 O  O     . LEU A 1 224 ? 22.743  -16.770 6.238   1.00 55.02  ?  224 LEU A O     1 
ATOM   1615 C  CB    . LEU A 1 224 ? 23.076  -16.145 3.127   1.00 57.19  ?  224 LEU A CB    1 
ATOM   1616 C  CG    . LEU A 1 224 ? 21.594  -16.464 3.248   1.00 63.87  ?  224 LEU A CG    1 
ATOM   1617 C  CD1   . LEU A 1 224 ? 20.811  -15.595 2.322   1.00 64.67  ?  224 LEU A CD1   1 
ATOM   1618 C  CD2   . LEU A 1 224 ? 21.361  -17.896 2.852   1.00 64.38  ?  224 LEU A CD2   1 
ATOM   1619 N  N     . LYS A 1 225 ? 24.800  -17.463 5.650   1.00 48.43  ?  225 LYS A N     1 
ATOM   1620 C  CA    . LYS A 1 225 ? 24.839  -18.462 6.714   1.00 54.57  ?  225 LYS A CA    1 
ATOM   1621 C  C     . LYS A 1 225 ? 24.920  -17.794 8.082   1.00 53.09  ?  225 LYS A C     1 
ATOM   1622 O  O     . LYS A 1 225 ? 24.335  -18.286 9.056   1.00 43.59  ?  225 LYS A O     1 
ATOM   1623 C  CB    . LYS A 1 225 ? 26.023  -19.415 6.500   1.00 49.65  ?  225 LYS A CB    1 
ATOM   1624 C  CG    . LYS A 1 225 ? 26.206  -20.456 7.575   1.00 51.44  ?  225 LYS A CG    1 
ATOM   1625 C  CD    . LYS A 1 225 ? 25.534  -21.766 7.185   1.00 62.10  ?  225 LYS A CD    1 
ATOM   1626 C  CE    . LYS A 1 225 ? 24.879  -22.445 8.396   1.00 65.85  ?  225 LYS A CE    1 
ATOM   1627 N  NZ    . LYS A 1 225 ? 23.433  -22.045 8.550   1.00 59.90  ?  225 LYS A NZ    1 
ATOM   1628 N  N     . VAL A 1 226 ? 25.650  -16.675 8.174   1.00 51.20  ?  226 VAL A N     1 
ATOM   1629 C  CA    . VAL A 1 226 ? 25.655  -15.892 9.407   1.00 53.16  ?  226 VAL A CA    1 
ATOM   1630 C  C     . VAL A 1 226 ? 24.247  -15.407 9.720   1.00 45.67  ?  226 VAL A C     1 
ATOM   1631 O  O     . VAL A 1 226 ? 23.841  -15.330 10.887  1.00 39.47  ?  226 VAL A O     1 
ATOM   1632 C  CB    . VAL A 1 226 ? 26.645  -14.716 9.293   1.00 53.18  ?  226 VAL A CB    1 
ATOM   1633 N  N     . TYR A 1 227 ? 23.475  -15.108 8.678   1.00 42.64  ?  227 TYR A N     1 
ATOM   1634 C  CA    . TYR A 1 227 ? 22.140  -14.576 8.876   1.00 44.21  ?  227 TYR A CA    1 
ATOM   1635 C  C     . TYR A 1 227 ? 21.187  -15.667 9.376   1.00 47.18  ?  227 TYR A C     1 
ATOM   1636 O  O     . TYR A 1 227 ? 20.549  -15.511 10.426  1.00 43.29  ?  227 TYR A O     1 
ATOM   1637 C  CB    . TYR A 1 227 ? 21.666  -13.919 7.570   1.00 50.46  ?  227 TYR A CB    1 
ATOM   1638 C  CG    . TYR A 1 227 ? 22.044  -12.423 7.457   1.00 53.89  ?  227 TYR A CG    1 
ATOM   1639 C  CD1   . TYR A 1 227 ? 21.347  -11.447 8.183   1.00 52.23  ?  227 TYR A CD1   1 
ATOM   1640 C  CD2   . TYR A 1 227 ? 23.104  -11.996 6.649   1.00 53.76  ?  227 TYR A CD2   1 
ATOM   1641 C  CE1   . TYR A 1 227 ? 21.677  -10.097 8.104   1.00 53.77  ?  227 TYR A CE1   1 
ATOM   1642 C  CE2   . TYR A 1 227 ? 23.451  -10.635 6.558   1.00 55.81  ?  227 TYR A CE2   1 
ATOM   1643 C  CZ    . TYR A 1 227 ? 22.733  -9.692  7.296   1.00 65.15  ?  227 TYR A CZ    1 
ATOM   1644 O  OH    . TYR A 1 227 ? 23.055  -8.351  7.233   1.00 60.80  ?  227 TYR A OH    1 
ATOM   1645 N  N     . GLU A 1 228 ? 21.114  -16.800 8.666   1.00 45.27  ?  228 GLU A N     1 
ATOM   1646 C  CA    . GLU A 1 228 ? 20.310  -17.926 9.136   1.00 45.47  ?  228 GLU A CA    1 
ATOM   1647 C  C     . GLU A 1 228 ? 20.674  -18.326 10.562  1.00 40.34  ?  228 GLU A C     1 
ATOM   1648 O  O     . GLU A 1 228 ? 19.788  -18.590 11.388  1.00 43.50  ?  228 GLU A O     1 
ATOM   1649 C  CB    . GLU A 1 228 ? 20.466  -19.124 8.194   1.00 55.69  ?  228 GLU A CB    1 
ATOM   1650 C  CG    . GLU A 1 228 ? 19.979  -20.475 8.771   1.00 56.84  ?  228 GLU A CG    1 
ATOM   1651 C  CD    . GLU A 1 228 ? 20.040  -21.630 7.761   1.00 62.97  ?  228 GLU A CD    1 
ATOM   1652 O  OE1   . GLU A 1 228 ? 21.149  -22.156 7.503   1.00 62.32  ?  228 GLU A OE1   1 
ATOM   1653 O  OE2   . GLU A 1 228 ? 18.970  -22.024 7.240   1.00 65.13  ?  228 GLU A OE2   1 
ATOM   1654 N  N     . ASP A 1 229 ? 21.957  -18.354 10.885  1.00 35.46  ?  229 ASP A N     1 
ATOM   1655 C  CA    . ASP A 1 229 ? 22.339  -18.843 12.206  1.00 44.13  ?  229 ASP A CA    1 
ATOM   1656 C  C     . ASP A 1 229 ? 21.968  -17.864 13.308  1.00 44.59  ?  229 ASP A C     1 
ATOM   1657 O  O     . ASP A 1 229 ? 21.623  -18.296 14.413  1.00 47.01  ?  229 ASP A O     1 
ATOM   1658 C  CB    . ASP A 1 229 ? 23.829  -19.138 12.270  1.00 47.18  ?  229 ASP A CB    1 
ATOM   1659 C  CG    . ASP A 1 229 ? 24.196  -20.409 11.520  1.00 56.17  ?  229 ASP A CG    1 
ATOM   1660 O  OD1   . ASP A 1 229 ? 23.293  -21.267 11.291  1.00 55.10  ?  229 ASP A OD1   1 
ATOM   1661 O  OD2   . ASP A 1 229 ? 25.388  -20.543 11.166  1.00 54.21  ?  229 ASP A OD2   1 
ATOM   1662 N  N     . ASN A 1 230 ? 22.040  -16.560 13.029  1.00 38.47  ?  230 ASN A N     1 
ATOM   1663 C  CA    . ASN A 1 230 ? 21.607  -15.550 13.990  1.00 40.24  ?  230 ASN A CA    1 
ATOM   1664 C  C     . ASN A 1 230 ? 20.081  -15.507 14.074  1.00 40.38  ?  230 ASN A C     1 
ATOM   1665 O  O     . ASN A 1 230 ? 19.516  -15.341 15.156  1.00 36.33  ?  230 ASN A O     1 
ATOM   1666 C  CB    . ASN A 1 230 ? 22.172  -14.176 13.596  1.00 41.30  ?  230 ASN A CB    1 
ATOM   1667 C  CG    . ASN A 1 230 ? 23.635  -13.964 14.061  1.00 41.97  ?  230 ASN A CG    1 
ATOM   1668 O  OD1   . ASN A 1 230 ? 24.291  -14.878 14.575  1.00 44.27  ?  230 ASN A OD1   1 
ATOM   1669 N  ND2   . ASN A 1 230 ? 24.124  -12.739 13.910  1.00 37.20  ?  230 ASN A ND2   1 
ATOM   1670 N  N     . TRP A 1 231 ? 19.408  -15.707 12.941  1.00 39.24  ?  231 TRP A N     1 
ATOM   1671 C  CA    . TRP A 1 231 ? 17.961  -15.838 12.928  1.00 37.25  ?  231 TRP A CA    1 
ATOM   1672 C  C     . TRP A 1 231 ? 17.473  -17.021 13.788  1.00 39.45  ?  231 TRP A C     1 
ATOM   1673 O  O     . TRP A 1 231 ? 16.459  -16.904 14.485  1.00 38.72  ?  231 TRP A O     1 
ATOM   1674 C  CB    . TRP A 1 231 ? 17.487  -15.964 11.475  1.00 39.24  ?  231 TRP A CB    1 
ATOM   1675 C  CG    . TRP A 1 231 ? 16.002  -16.089 11.377  1.00 42.77  ?  231 TRP A CG    1 
ATOM   1676 C  CD1   . TRP A 1 231 ? 15.096  -15.077 11.355  1.00 43.63  ?  231 TRP A CD1   1 
ATOM   1677 C  CD2   . TRP A 1 231 ? 15.252  -17.299 11.326  1.00 39.72  ?  231 TRP A CD2   1 
ATOM   1678 N  NE1   . TRP A 1 231 ? 13.824  -15.580 11.282  1.00 41.32  ?  231 TRP A NE1   1 
ATOM   1679 C  CE2   . TRP A 1 231 ? 13.895  -16.946 11.260  1.00 40.55  ?  231 TRP A CE2   1 
ATOM   1680 C  CE3   . TRP A 1 231 ? 15.599  -18.656 11.347  1.00 40.63  ?  231 TRP A CE3   1 
ATOM   1681 C  CZ2   . TRP A 1 231 ? 12.879  -17.895 11.207  1.00 41.49  ?  231 TRP A CZ2   1 
ATOM   1682 C  CZ3   . TRP A 1 231 ? 14.605  -19.591 11.284  1.00 40.12  ?  231 TRP A CZ3   1 
ATOM   1683 C  CH2   . TRP A 1 231 ? 13.251  -19.211 11.218  1.00 43.28  ?  231 TRP A CH2   1 
ATOM   1684 N  N     . HIS A 1 232 ? 18.154  -18.175 13.732  1.00 40.61  ?  232 HIS A N     1 
ATOM   1685 C  CA    . HIS A 1 232 ? 17.806  -19.288 14.614  1.00 36.93  ?  232 HIS A CA    1 
ATOM   1686 C  C     . HIS A 1 232 ? 18.029  -18.906 16.064  1.00 39.50  ?  232 HIS A C     1 
ATOM   1687 O  O     . HIS A 1 232 ? 17.187  -19.185 16.932  1.00 43.56  ?  232 HIS A O     1 
ATOM   1688 C  CB    . HIS A 1 232 ? 18.653  -20.525 14.311  1.00 36.64  ?  232 HIS A CB    1 
ATOM   1689 C  CG    . HIS A 1 232 ? 18.115  -21.406 13.226  1.00 42.54  ?  232 HIS A CG    1 
ATOM   1690 N  ND1   . HIS A 1 232 ? 18.578  -21.350 11.923  1.00 47.41  ?  232 HIS A ND1   1 
ATOM   1691 C  CD2   . HIS A 1 232 ? 17.214  -22.417 13.261  1.00 38.13  ?  232 HIS A CD2   1 
ATOM   1692 C  CE1   . HIS A 1 232 ? 17.960  -22.267 11.198  1.00 46.74  ?  232 HIS A CE1   1 
ATOM   1693 N  NE2   . HIS A 1 232 ? 17.127  -22.927 11.984  1.00 39.12  ?  232 HIS A NE2   1 
ATOM   1694 N  N     . LEU A 1 233 ? 19.190  -18.309 16.349  1.00 35.69  ?  233 LEU A N     1 
ATOM   1695 C  CA    . LEU A 1 233 ? 19.518  -17.894 17.707  1.00 39.45  ?  233 LEU A CA    1 
ATOM   1696 C  C     . LEU A 1 233 ? 18.412  -17.019 18.267  1.00 40.02  ?  233 LEU A C     1 
ATOM   1697 O  O     . LEU A 1 233 ? 17.895  -17.263 19.364  1.00 33.77  ?  233 LEU A O     1 
ATOM   1698 C  CB    . LEU A 1 233 ? 20.846  -17.127 17.707  1.00 41.15  ?  233 LEU A CB    1 
ATOM   1699 C  CG    . LEU A 1 233 ? 21.465  -16.720 19.050  1.00 45.02  ?  233 LEU A CG    1 
ATOM   1700 C  CD1   . LEU A 1 233 ? 21.693  -17.969 19.860  1.00 45.70  ?  233 LEU A CD1   1 
ATOM   1701 C  CD2   . LEU A 1 233 ? 22.792  -15.963 18.875  1.00 44.79  ?  233 LEU A CD2   1 
ATOM   1702 N  N     . ILE A 1 234 ? 18.022  -16.008 17.484  1.00 36.69  ?  234 ILE A N     1 
ATOM   1703 C  CA    . ILE A 1 234 ? 17.051  -15.030 17.928  1.00 34.29  ?  234 ILE A CA    1 
ATOM   1704 C  C     . ILE A 1 234 ? 15.678  -15.677 18.086  1.00 36.08  ?  234 ILE A C     1 
ATOM   1705 O  O     . ILE A 1 234 ? 15.002  -15.468 19.098  1.00 33.01  ?  234 ILE A O     1 
ATOM   1706 C  CB    . ILE A 1 234 ? 17.055  -13.839 16.957  1.00 31.84  ?  234 ILE A CB    1 
ATOM   1707 C  CG1   . ILE A 1 234 ? 18.428  -13.174 17.017  1.00 33.95  ?  234 ILE A CG1   1 
ATOM   1708 C  CG2   . ILE A 1 234 ? 16.042  -12.805 17.371  1.00 27.95  ?  234 ILE A CG2   1 
ATOM   1709 C  CD1   . ILE A 1 234 ? 18.685  -12.127 15.961  1.00 38.03  ?  234 ILE A CD1   1 
ATOM   1710 N  N     . CYS A 1 235 ? 15.270  -16.517 17.126  1.00 33.63  ?  235 CYS A N     1 
ATOM   1711 C  CA    . CYS A 1 235 ? 14.020  -17.251 17.290  1.00 35.40  ?  235 CYS A CA    1 
ATOM   1712 C  C     . CYS A 1 235 ? 13.988  -18.029 18.605  1.00 38.55  ?  235 CYS A C     1 
ATOM   1713 O  O     . CYS A 1 235 ? 12.971  -18.038 19.301  1.00 32.69  ?  235 CYS A O     1 
ATOM   1714 C  CB    . CYS A 1 235 ? 13.809  -18.214 16.137  1.00 29.25  ?  235 CYS A CB    1 
ATOM   1715 S  SG    . CYS A 1 235 ? 13.223  -17.467 14.652  1.00 34.77  ?  235 CYS A SG    1 
ATOM   1716 N  N     . GLU A 1 236 ? 15.093  -18.695 18.951  1.00 38.90  ?  236 GLU A N     1 
ATOM   1717 C  CA    . GLU A 1 236 ? 15.137  -19.541 20.140  1.00 39.07  ?  236 GLU A CA    1 
ATOM   1718 C  C     . GLU A 1 236 ? 15.052  -18.714 21.421  1.00 39.63  ?  236 GLU A C     1 
ATOM   1719 O  O     . GLU A 1 236 ? 14.467  -19.167 22.423  1.00 37.52  ?  236 GLU A O     1 
ATOM   1720 C  CB    . GLU A 1 236 ? 16.421  -20.380 20.115  1.00 39.49  ?  236 GLU A CB    1 
ATOM   1721 C  CG    . GLU A 1 236 ? 16.238  -21.851 19.743  1.00 56.63  ?  236 GLU A CG    1 
ATOM   1722 C  CD    . GLU A 1 236 ? 15.413  -22.635 20.775  1.00 60.07  ?  236 GLU A CD    1 
ATOM   1723 O  OE1   . GLU A 1 236 ? 14.386  -23.248 20.395  1.00 61.98  ?  236 GLU A OE1   1 
ATOM   1724 O  OE2   . GLU A 1 236 ? 15.785  -22.623 21.975  1.00 66.63  ?  236 GLU A OE2   1 
ATOM   1725 N  N     . ARG A 1 237 ? 15.605  -17.494 21.396  1.00 37.91  ?  237 ARG A N     1 
ATOM   1726 C  CA    . ARG A 1 237 ? 15.578  -16.598 22.556  1.00 30.95  ?  237 ARG A CA    1 
ATOM   1727 C  C     . ARG A 1 237 ? 14.196  -15.954 22.758  1.00 37.76  ?  237 ARG A C     1 
ATOM   1728 O  O     . ARG A 1 237 ? 13.830  -15.587 23.887  1.00 42.47  ?  237 ARG A O     1 
ATOM   1729 C  CB    . ARG A 1 237 ? 16.671  -15.549 22.355  1.00 35.74  ?  237 ARG A CB    1 
ATOM   1730 C  CG    . ARG A 1 237 ? 16.681  -14.355 23.317  1.00 41.59  ?  237 ARG A CG    1 
ATOM   1731 C  CD    . ARG A 1 237 ? 17.671  -13.264 22.876  1.00 31.72  ?  237 ARG A CD    1 
ATOM   1732 N  NE    . ARG A 1 237 ? 19.033  -13.630 23.226  1.00 43.08  ?  237 ARG A NE    1 
ATOM   1733 C  CZ    . ARG A 1 237 ? 20.129  -13.078 22.716  1.00 44.56  ?  237 ARG A CZ    1 
ATOM   1734 N  NH1   . ARG A 1 237 ? 20.071  -12.102 21.823  1.00 39.72  ?  237 ARG A NH1   1 
ATOM   1735 N  NH2   . ARG A 1 237 ? 21.314  -13.511 23.121  1.00 41.74  ?  237 ARG A NH2   1 
ATOM   1736 N  N     . TRP A 1 238 ? 13.408  -15.826 21.690  1.00 38.41  ?  238 TRP A N     1 
ATOM   1737 C  CA    . TRP A 1 238 ? 12.160  -15.067 21.715  1.00 31.74  ?  238 TRP A CA    1 
ATOM   1738 C  C     . TRP A 1 238 ? 11.089  -15.845 20.962  1.00 35.64  ?  238 TRP A C     1 
ATOM   1739 O  O     . TRP A 1 238 ? 10.872  -15.617 19.765  1.00 34.22  ?  238 TRP A O     1 
ATOM   1740 C  CB    . TRP A 1 238 ? 12.330  -13.680 21.088  1.00 32.83  ?  238 TRP A CB    1 
ATOM   1741 C  CG    . TRP A 1 238 ? 13.406  -12.772 21.684  1.00 33.18  ?  238 TRP A CG    1 
ATOM   1742 C  CD1   . TRP A 1 238 ? 14.566  -12.374 21.081  1.00 32.00  ?  238 TRP A CD1   1 
ATOM   1743 C  CD2   . TRP A 1 238 ? 13.368  -12.099 22.955  1.00 33.48  ?  238 TRP A CD2   1 
ATOM   1744 N  NE1   . TRP A 1 238 ? 15.263  -11.521 21.900  1.00 31.82  ?  238 TRP A NE1   1 
ATOM   1745 C  CE2   . TRP A 1 238 ? 14.559  -11.347 23.063  1.00 31.77  ?  238 TRP A CE2   1 
ATOM   1746 C  CE3   . TRP A 1 238 ? 12.456  -12.079 24.018  1.00 27.62  ?  238 TRP A CE3   1 
ATOM   1747 C  CZ2   . TRP A 1 238 ? 14.868  -10.603 24.198  1.00 30.87  ?  238 TRP A CZ2   1 
ATOM   1748 C  CZ3   . TRP A 1 238 ? 12.756  -11.346 25.124  1.00 29.85  ?  238 TRP A CZ3   1 
ATOM   1749 C  CH2   . TRP A 1 238 ? 13.945  -10.598 25.210  1.00 30.94  ?  238 TRP A CH2   1 
ATOM   1750 N  N     . PRO A 1 239 ? 10.371  -16.746 21.642  1.00 32.97  ?  239 PRO A N     1 
ATOM   1751 C  CA    . PRO A 1 239 ? 9.277   -17.473 20.985  1.00 32.84  ?  239 PRO A CA    1 
ATOM   1752 C  C     . PRO A 1 239 ? 8.244   -16.519 20.412  1.00 34.49  ?  239 PRO A C     1 
ATOM   1753 O  O     . PRO A 1 239 ? 8.008   -15.443 20.956  1.00 34.91  ?  239 PRO A O     1 
ATOM   1754 C  CB    . PRO A 1 239 ? 8.672   -18.319 22.123  1.00 33.63  ?  239 PRO A CB    1 
ATOM   1755 C  CG    . PRO A 1 239 ? 9.731   -18.397 23.155  1.00 33.39  ?  239 PRO A CG    1 
ATOM   1756 C  CD    . PRO A 1 239 ? 10.530  -17.126 23.057  1.00 29.82  ?  239 PRO A CD    1 
ATOM   1757 N  N     . ALA A 1 240 ? 7.619   -16.934 19.309  1.00 33.30  ?  240 ALA A N     1 
ATOM   1758 C  CA    . ALA A 1 240 ? 6.600   -16.132 18.659  1.00 34.20  ?  240 ALA A CA    1 
ATOM   1759 C  C     . ALA A 1 240 ? 5.379   -15.967 19.567  1.00 39.71  ?  240 ALA A C     1 
ATOM   1760 O  O     . ALA A 1 240 ? 5.026   -16.870 20.329  1.00 36.32  ?  240 ALA A O     1 
ATOM   1761 C  CB    . ALA A 1 240 ? 6.183   -16.794 17.355  1.00 35.12  ?  240 ALA A CB    1 
ATOM   1762 N  N     . ALA A 1 241 ? 4.707   -14.816 19.461  1.00 37.76  ?  241 ALA A N     1 
ATOM   1763 C  CA    . ALA A 1 241 ? 3.568   -14.505 20.339  1.00 38.47  ?  241 ALA A CA    1 
ATOM   1764 C  C     . ALA A 1 241 ? 2.205   -14.885 19.748  1.00 36.69  ?  241 ALA A C     1 
ATOM   1765 O  O     . ALA A 1 241 ? 1.177   -14.508 20.323  1.00 36.17  ?  241 ALA A O     1 
ATOM   1766 C  CB    . ALA A 1 241 ? 3.564   -13.013 20.736  1.00 28.56  ?  241 ALA A CB    1 
ATOM   1767 N  N     . THR A 1 242 ? 2.176   -15.603 18.617  1.00 37.44  ?  242 THR A N     1 
ATOM   1768 C  CA    . THR A 1 242 ? 0.984   -16.311 18.155  1.00 34.27  ?  242 THR A CA    1 
ATOM   1769 C  C     . THR A 1 242 ? 1.425   -17.640 17.555  1.00 42.02  ?  242 THR A C     1 
ATOM   1770 O  O     . THR A 1 242 ? 2.593   -17.823 17.176  1.00 39.93  ?  242 THR A O     1 
ATOM   1771 C  CB    . THR A 1 242 ? 0.154   -15.538 17.098  1.00 38.91  ?  242 THR A CB    1 
ATOM   1772 O  OG1   . THR A 1 242 ? 0.953   -15.309 15.920  1.00 39.58  ?  242 THR A OG1   1 
ATOM   1773 C  CG2   . THR A 1 242 ? -0.431  -14.205 17.647  1.00 31.22  ?  242 THR A CG2   1 
ATOM   1774 N  N     . GLU A 1 243 ? 0.468   -18.576 17.445  1.00 38.40  ?  243 GLU A N     1 
ATOM   1775 C  CA    . GLU A 1 243 ? 0.831   -19.883 16.900  1.00 37.30  ?  243 GLU A CA    1 
ATOM   1776 C  C     . GLU A 1 243 ? 1.092   -19.797 15.407  1.00 38.92  ?  243 GLU A C     1 
ATOM   1777 O  O     . GLU A 1 243 ? 2.014   -20.452 14.899  1.00 39.02  ?  243 GLU A O     1 
ATOM   1778 C  CB    . GLU A 1 243 ? -0.253  -20.939 17.164  1.00 38.95  ?  243 GLU A CB    1 
ATOM   1779 C  CG    . GLU A 1 243 ? 0.050   -22.240 16.428  1.00 39.57  ?  243 GLU A CG    1 
ATOM   1780 C  CD    . GLU A 1 243 ? -0.820  -23.404 16.807  1.00 54.24  ?  243 GLU A CD    1 
ATOM   1781 O  OE1   . GLU A 1 243 ? -1.772  -23.260 17.630  1.00 51.35  ?  243 GLU A OE1   1 
ATOM   1782 O  OE2   . GLU A 1 243 ? -0.516  -24.494 16.277  1.00 64.38  ?  243 GLU A OE2   1 
ATOM   1783 N  N     . ARG A 1 244 ? 0.278   -19.022 14.677  1.00 36.81  ?  244 ARG A N     1 
ATOM   1784 C  CA    . ARG A 1 244 ? 0.513   -18.918 13.242  1.00 41.40  ?  244 ARG A CA    1 
ATOM   1785 C  C     . ARG A 1 244 ? 1.941   -18.461 12.952  1.00 38.33  ?  244 ARG A C     1 
ATOM   1786 O  O     . ARG A 1 244 ? 2.656   -19.099 12.175  1.00 39.46  ?  244 ARG A O     1 
ATOM   1787 C  CB    . ARG A 1 244 ? -0.489  -17.994 12.561  1.00 33.76  ?  244 ARG A CB    1 
ATOM   1788 C  CG    . ARG A 1 244 ? -0.191  -17.942 11.037  1.00 46.63  ?  244 ARG A CG    1 
ATOM   1789 C  CD    . ARG A 1 244 ? -0.805  -19.127 10.241  1.00 47.79  ?  244 ARG A CD    1 
ATOM   1790 N  NE    . ARG A 1 244 ? -2.257  -19.022 10.305  1.00 55.20  ?  244 ARG A NE    1 
ATOM   1791 C  CZ    . ARG A 1 244 ? -3.004  -18.358 9.429   1.00 57.16  ?  244 ARG A CZ    1 
ATOM   1792 N  NH1   . ARG A 1 244 ? -2.505  -17.922 8.283   1.00 52.07  ?  244 ARG A NH1   1 
ATOM   1793 N  NH2   . ARG A 1 244 ? -4.278  -18.103 9.723   1.00 54.45  ?  244 ARG A NH2   1 
ATOM   1794 N  N     . ALA A 1 245 ? 2.391   -17.396 13.620  1.00 39.59  ?  245 ALA A N     1 
ATOM   1795 C  CA    . ALA A 1 245 ? 3.751   -16.899 13.404  1.00 38.35  ?  245 ALA A CA    1 
ATOM   1796 C  C     . ALA A 1 245 ? 4.786   -17.942 13.803  1.00 35.40  ?  245 ALA A C     1 
ATOM   1797 O  O     . ALA A 1 245 ? 5.831   -18.075 13.154  1.00 36.70  ?  245 ALA A O     1 
ATOM   1798 C  CB    . ALA A 1 245 ? 3.963   -15.598 14.178  1.00 26.69  ?  245 ALA A CB    1 
ATOM   1799 N  N     . GLU A 1 246 ? 4.508   -18.700 14.866  1.00 35.02  ?  246 GLU A N     1 
ATOM   1800 C  CA    . GLU A 1 246 ? 5.390   -19.805 15.215  1.00 37.40  ?  246 GLU A CA    1 
ATOM   1801 C  C     . GLU A 1 246 ? 5.419   -20.855 14.109  1.00 40.21  ?  246 GLU A C     1 
ATOM   1802 O  O     . GLU A 1 246 ? 6.481   -21.412 13.829  1.00 42.45  ?  246 GLU A O     1 
ATOM   1803 C  CB    . GLU A 1 246 ? 4.970   -20.391 16.566  1.00 39.33  ?  246 GLU A CB    1 
ATOM   1804 C  CG    . GLU A 1 246 ? 5.984   -21.353 17.196  1.00 49.23  ?  246 GLU A CG    1 
ATOM   1805 C  CD    . GLU A 1 246 ? 7.374   -20.731 17.373  1.00 46.97  ?  246 GLU A CD    1 
ATOM   1806 O  OE1   . GLU A 1 246 ? 7.584   -19.849 18.265  1.00 43.78  ?  246 GLU A OE1   1 
ATOM   1807 O  OE2   . GLU A 1 246 ? 8.254   -21.133 16.585  1.00 45.73  ?  246 GLU A OE2   1 
ATOM   1808 N  N     . GLN A 1 247 ? 4.288   -21.069 13.414  1.00 41.37  ?  247 GLN A N     1 
ATOM   1809 C  CA    . GLN A 1 247 ? 4.268   -21.960 12.251  1.00 43.91  ?  247 GLN A CA    1 
ATOM   1810 C  C     . GLN A 1 247 ? 4.997   -21.351 11.051  1.00 41.52  ?  247 GLN A C     1 
ATOM   1811 O  O     . GLN A 1 247 ? 5.670   -22.070 10.301  1.00 36.74  ?  247 GLN A O     1 
ATOM   1812 C  CB    . GLN A 1 247 ? 2.825   -22.305 11.844  1.00 41.38  ?  247 GLN A CB    1 
ATOM   1813 C  CG    . GLN A 1 247 ? 2.055   -23.204 12.802  1.00 47.49  ?  247 GLN A CG    1 
ATOM   1814 C  CD    . GLN A 1 247 ? 0.516   -23.149 12.574  1.00 60.35  ?  247 GLN A CD    1 
ATOM   1815 O  OE1   . GLN A 1 247 ? 0.024   -22.548 11.601  1.00 61.30  ?  247 GLN A OE1   1 
ATOM   1816 N  NE2   . GLN A 1 247 ? -0.238  -23.750 13.495  1.00 62.84  ?  247 GLN A NE2   1 
ATOM   1817 N  N     . VAL A 1 248 ? 4.835   -20.046 10.814  1.00 36.39  ?  248 VAL A N     1 
ATOM   1818 C  CA    . VAL A 1 248 ? 5.359   -19.462 9.576   1.00 39.13  ?  248 VAL A CA    1 
ATOM   1819 C  C     . VAL A 1 248 ? 6.883   -19.285 9.620   1.00 38.60  ?  248 VAL A C     1 
ATOM   1820 O  O     . VAL A 1 248 ? 7.519   -19.189 8.563   1.00 33.61  ?  248 VAL A O     1 
ATOM   1821 C  CB    . VAL A 1 248 ? 4.592   -18.166 9.269   1.00 38.45  ?  248 VAL A CB    1 
ATOM   1822 C  CG1   . VAL A 1 248 ? 5.163   -17.414 8.072   1.00 33.69  ?  248 VAL A CG1   1 
ATOM   1823 C  CG2   . VAL A 1 248 ? 3.115   -18.500 9.018   1.00 36.99  ?  248 VAL A CG2   1 
ATOM   1824 N  N     . ARG A 1 249 ? 7.487   -19.316 10.816  1.00 39.33  ?  249 ARG A N     1 
ATOM   1825 C  CA    . ARG A 1 249 ? 8.942   -19.399 10.930  1.00 38.25  ?  249 ARG A CA    1 
ATOM   1826 C  C     . ARG A 1 249 ? 9.512   -20.597 10.195  1.00 39.61  ?  249 ARG A C     1 
ATOM   1827 O  O     . ARG A 1 249 ? 10.661  -20.559 9.732   1.00 42.19  ?  249 ARG A O     1 
ATOM   1828 C  CB    . ARG A 1 249 ? 9.350   -19.481 12.393  1.00 34.61  ?  249 ARG A CB    1 
ATOM   1829 C  CG    . ARG A 1 249 ? 9.045   -18.247 13.188  1.00 36.94  ?  249 ARG A CG    1 
ATOM   1830 C  CD    . ARG A 1 249 ? 9.647   -18.398 14.557  1.00 34.56  ?  249 ARG A CD    1 
ATOM   1831 N  NE    . ARG A 1 249 ? 9.709   -17.126 15.265  1.00 32.01  ?  249 ARG A NE    1 
ATOM   1832 C  CZ    . ARG A 1 249 ? 10.092  -17.017 16.528  1.00 32.45  ?  249 ARG A CZ    1 
ATOM   1833 N  NH1   . ARG A 1 249 ? 10.471  -18.077 17.229  1.00 31.36  ?  249 ARG A NH1   1 
ATOM   1834 N  NH2   . ARG A 1 249 ? 10.101  -15.824 17.099  1.00 28.96  ?  249 ARG A NH2   1 
ATOM   1835 N  N     . ARG A 1 250 ? 8.729   -21.664 10.079  1.00 41.92  ?  250 ARG A N     1 
ATOM   1836 C  CA    . ARG A 1 250 ? 9.213   -22.880 9.439   1.00 46.22  ?  250 ARG A CA    1 
ATOM   1837 C  C     . ARG A 1 250 ? 9.556   -22.660 7.966   1.00 46.83  ?  250 ARG A C     1 
ATOM   1838 O  O     . ARG A 1 250 ? 10.382  -23.397 7.414   1.00 47.78  ?  250 ARG A O     1 
ATOM   1839 C  CB    . ARG A 1 250 ? 8.172   -23.988 9.586   1.00 40.00  ?  250 ARG A CB    1 
ATOM   1840 C  CG    . ARG A 1 250 ? 7.975   -24.489 11.029  1.00 46.94  ?  250 ARG A CG    1 
ATOM   1841 C  CD    . ARG A 1 250 ? 6.587   -25.108 11.193  1.00 58.61  ?  250 ARG A CD    1 
ATOM   1842 N  NE    . ARG A 1 250 ? 5.690   -24.560 10.175  1.00 62.14  ?  250 ARG A NE    1 
ATOM   1843 C  CZ    . ARG A 1 250 ? 4.509   -25.062 9.838   1.00 68.57  ?  250 ARG A CZ    1 
ATOM   1844 N  NH1   . ARG A 1 250 ? 4.015   -26.134 10.444  1.00 73.14  ?  250 ARG A NH1   1 
ATOM   1845 N  NH2   . ARG A 1 250 ? 3.806   -24.472 8.866   1.00 65.02  ?  250 ARG A NH2   1 
ATOM   1846 N  N     . PHE A 1 251 ? 8.924   -21.681 7.308   1.00 41.23  ?  251 PHE A N     1 
ATOM   1847 C  CA    . PHE A 1 251 ? 9.278   -21.376 5.927   1.00 48.37  ?  251 PHE A CA    1 
ATOM   1848 C  C     . PHE A 1 251 ? 10.591  -20.609 5.782   1.00 48.20  ?  251 PHE A C     1 
ATOM   1849 O  O     . PHE A 1 251 ? 11.066  -20.463 4.652   1.00 50.64  ?  251 PHE A O     1 
ATOM   1850 C  CB    . PHE A 1 251 ? 8.199   -20.544 5.225   1.00 46.19  ?  251 PHE A CB    1 
ATOM   1851 C  CG    . PHE A 1 251 ? 6.810   -21.098 5.329   1.00 51.46  ?  251 PHE A CG    1 
ATOM   1852 C  CD1   . PHE A 1 251 ? 6.377   -22.101 4.469   1.00 52.56  ?  251 PHE A CD1   1 
ATOM   1853 C  CD2   . PHE A 1 251 ? 5.909   -20.566 6.232   1.00 44.83  ?  251 PHE A CD2   1 
ATOM   1854 C  CE1   . PHE A 1 251 ? 5.082   -22.578 4.538   1.00 51.55  ?  251 PHE A CE1   1 
ATOM   1855 C  CE2   . PHE A 1 251 ? 4.609   -21.052 6.311   1.00 47.73  ?  251 PHE A CE2   1 
ATOM   1856 C  CZ    . PHE A 1 251 ? 4.197   -22.057 5.465   1.00 51.83  ?  251 PHE A CZ    1 
ATOM   1857 N  N     . MET A 1 252 ? 11.172  -20.078 6.864   1.00 46.53  ?  252 MET A N     1 
ATOM   1858 C  CA    . MET A 1 252 ? 12.433  -19.358 6.698   1.00 44.21  ?  252 MET A CA    1 
ATOM   1859 C  C     . MET A 1 252 ? 13.568  -20.304 6.336   1.00 46.48  ?  252 MET A C     1 
ATOM   1860 O  O     . MET A 1 252 ? 14.265  -20.039 5.345   1.00 43.37  ?  252 MET A O     1 
ATOM   1861 C  CB    . MET A 1 252 ? 12.741  -18.525 7.943   1.00 41.75  ?  252 MET A CB    1 
ATOM   1862 C  CG    . MET A 1 252 ? 12.005  -17.184 7.975   1.00 41.74  ?  252 MET A CG    1 
ATOM   1863 S  SD    . MET A 1 252 ? 12.832  -15.908 7.008   1.00 49.38  ?  252 MET A SD    1 
ATOM   1864 C  CE    . MET A 1 252 ? 11.898  -15.992 5.527   1.00 35.72  ?  252 MET A CE    1 
ATOM   1865 N  N     . PRO A 1 253 ? 13.818  -21.395 7.064   1.00 49.55  ?  253 PRO A N     1 
ATOM   1866 C  CA    . PRO A 1 253 ? 14.862  -22.335 6.599   1.00 49.39  ?  253 PRO A CA    1 
ATOM   1867 C  C     . PRO A 1 253 ? 14.609  -22.867 5.195   1.00 49.78  ?  253 PRO A C     1 
ATOM   1868 O  O     . PRO A 1 253 ? 15.564  -23.194 4.478   1.00 49.18  ?  253 PRO A O     1 
ATOM   1869 C  CB    . PRO A 1 253 ? 14.815  -23.459 7.644   1.00 43.41  ?  253 PRO A CB    1 
ATOM   1870 C  CG    . PRO A 1 253 ? 14.282  -22.787 8.874   1.00 48.59  ?  253 PRO A CG    1 
ATOM   1871 C  CD    . PRO A 1 253 ? 13.269  -21.787 8.374   1.00 45.69  ?  253 PRO A CD    1 
ATOM   1872 N  N     . VAL A 1 254 ? 13.341  -22.965 4.786   1.00 49.15  ?  254 VAL A N     1 
ATOM   1873 C  CA    . VAL A 1 254 ? 13.018  -23.315 3.405   1.00 50.61  ?  254 VAL A CA    1 
ATOM   1874 C  C     . VAL A 1 254 ? 13.567  -22.259 2.457   1.00 50.24  ?  254 VAL A C     1 
ATOM   1875 O  O     . VAL A 1 254 ? 14.223  -22.576 1.454   1.00 53.05  ?  254 VAL A O     1 
ATOM   1876 C  CB    . VAL A 1 254 ? 11.495  -23.488 3.242   1.00 51.39  ?  254 VAL A CB    1 
ATOM   1877 C  CG1   . VAL A 1 254 ? 11.076  -23.304 1.791   1.00 49.46  ?  254 VAL A CG1   1 
ATOM   1878 C  CG2   . VAL A 1 254 ? 11.044  -24.849 3.787   1.00 47.75  ?  254 VAL A CG2   1 
ATOM   1879 N  N     . MET A 1 255 ? 13.308  -20.985 2.767   1.00 45.26  ?  255 MET A N     1 
ATOM   1880 C  CA    . MET A 1 255 ? 13.826  -19.889 1.953   1.00 45.74  ?  255 MET A CA    1 
ATOM   1881 C  C     . MET A 1 255 ? 15.355  -19.883 1.922   1.00 49.22  ?  255 MET A C     1 
ATOM   1882 O  O     . MET A 1 255 ? 15.960  -19.667 0.867   1.00 49.24  ?  255 MET A O     1 
ATOM   1883 C  CB    . MET A 1 255 ? 13.283  -18.560 2.476   1.00 46.08  ?  255 MET A CB    1 
ATOM   1884 C  CG    . MET A 1 255 ? 13.704  -17.359 1.678   1.00 47.32  ?  255 MET A CG    1 
ATOM   1885 S  SD    . MET A 1 255 ? 15.174  -16.675 2.448   1.00 58.00  ?  255 MET A SD    1 
ATOM   1886 C  CE    . MET A 1 255 ? 14.591  -15.070 2.961   1.00 48.60  ?  255 MET A CE    1 
ATOM   1887 N  N     . TYR A 1 256 ? 15.998  -20.124 3.066   1.00 50.31  ?  256 TYR A N     1 
ATOM   1888 C  CA    . TYR A 1 256 ? 17.455  -20.229 3.086   1.00 52.85  ?  256 TYR A CA    1 
ATOM   1889 C  C     . TYR A 1 256 ? 17.938  -21.362 2.189   1.00 52.93  ?  256 TYR A C     1 
ATOM   1890 O  O     . TYR A 1 256 ? 18.818  -21.167 1.345   1.00 52.55  ?  256 TYR A O     1 
ATOM   1891 C  CB    . TYR A 1 256 ? 17.947  -20.436 4.514   1.00 50.36  ?  256 TYR A CB    1 
ATOM   1892 C  CG    . TYR A 1 256 ? 17.859  -19.189 5.348   1.00 56.49  ?  256 TYR A CG    1 
ATOM   1893 C  CD1   . TYR A 1 256 ? 18.154  -17.953 4.802   1.00 54.95  ?  256 TYR A CD1   1 
ATOM   1894 C  CD2   . TYR A 1 256 ? 17.449  -19.240 6.675   1.00 58.53  ?  256 TYR A CD2   1 
ATOM   1895 C  CE1   . TYR A 1 256 ? 18.062  -16.807 5.546   1.00 55.99  ?  256 TYR A CE1   1 
ATOM   1896 C  CE2   . TYR A 1 256 ? 17.356  -18.084 7.439   1.00 51.05  ?  256 TYR A CE2   1 
ATOM   1897 C  CZ    . TYR A 1 256 ? 17.676  -16.871 6.870   1.00 54.12  ?  256 TYR A CZ    1 
ATOM   1898 O  OH    . TYR A 1 256 ? 17.600  -15.709 7.611   1.00 49.04  ?  256 TYR A OH    1 
ATOM   1899 N  N     . GLN A 1 257 ? 17.379  -22.561 2.363   1.00 51.55  ?  257 GLN A N     1 
ATOM   1900 C  CA    . GLN A 1 257 ? 17.805  -23.686 1.542   1.00 57.07  ?  257 GLN A CA    1 
ATOM   1901 C  C     . GLN A 1 257 ? 17.775  -23.332 0.056   1.00 53.80  ?  257 GLN A C     1 
ATOM   1902 O  O     . GLN A 1 257 ? 18.731  -23.621 -0.673  1.00 55.94  ?  257 GLN A O     1 
ATOM   1903 C  CB    . GLN A 1 257 ? 16.945  -24.918 1.843   1.00 53.41  ?  257 GLN A CB    1 
ATOM   1904 C  CG    . GLN A 1 257 ? 17.465  -26.196 1.189   1.00 61.66  ?  257 GLN A CG    1 
ATOM   1905 C  CD    . GLN A 1 257 ? 16.343  -27.168 0.800   1.00 77.95  ?  257 GLN A CD    1 
ATOM   1906 O  OE1   . GLN A 1 257 ? 15.312  -26.751 0.260   1.00 78.39  ?  257 GLN A OE1   1 
ATOM   1907 N  NE2   . GLN A 1 257 ? 16.546  -28.469 1.063   1.00 75.53  ?  257 GLN A NE2   1 
ATOM   1908 N  N     . MET A 1 258 ? 16.714  -22.657 -0.401  1.00 51.40  ?  258 MET A N     1 
ATOM   1909 C  CA    . MET A 1 258 ? 16.643  -22.270 -1.812  1.00 48.43  ?  258 MET A CA    1 
ATOM   1910 C  C     . MET A 1 258 ? 17.715  -21.244 -2.165  1.00 51.25  ?  258 MET A C     1 
ATOM   1911 O  O     . MET A 1 258 ? 18.268  -21.270 -3.269  1.00 55.44  ?  258 MET A O     1 
ATOM   1912 C  CB    . MET A 1 258 ? 15.266  -21.701 -2.156  1.00 47.06  ?  258 MET A CB    1 
ATOM   1913 C  CG    . MET A 1 258 ? 14.148  -22.700 -2.304  1.00 50.05  ?  258 MET A CG    1 
ATOM   1914 S  SD    . MET A 1 258 ? 12.555  -21.989 -1.790  1.00 63.58  ?  258 MET A SD    1 
ATOM   1915 C  CE    . MET A 1 258 ? 12.147  -21.000 -3.186  1.00 49.14  ?  258 MET A CE    1 
ATOM   1916 N  N     . ALA A 1 259 ? 17.993  -20.310 -1.257  1.00 50.52  ?  259 ALA A N     1 
ATOM   1917 C  CA    . ALA A 1 259 ? 19.066  -19.354 -1.494  1.00 51.46  ?  259 ALA A CA    1 
ATOM   1918 C  C     . ALA A 1 259 ? 20.405  -20.069 -1.646  1.00 51.03  ?  259 ALA A C     1 
ATOM   1919 O  O     . ALA A 1 259 ? 21.162  -19.792 -2.578  1.00 49.54  ?  259 ALA A O     1 
ATOM   1920 C  CB    . ALA A 1 259 ? 19.119  -18.333 -0.356  1.00 51.25  ?  259 ALA A CB    1 
ATOM   1921 N  N     . TYR A 1 260 ? 20.710  -20.993 -0.734  1.00 49.75  ?  260 TYR A N     1 
ATOM   1922 C  CA    . TYR A 1 260 ? 21.960  -21.740 -0.820  1.00 53.52  ?  260 TYR A CA    1 
ATOM   1923 C  C     . TYR A 1 260 ? 22.045  -22.533 -2.111  1.00 55.08  ?  260 TYR A C     1 
ATOM   1924 O  O     . TYR A 1 260 ? 23.113  -22.615 -2.728  1.00 51.43  ?  260 TYR A O     1 
ATOM   1925 C  CB    . TYR A 1 260 ? 22.081  -22.704 0.351   1.00 60.25  ?  260 TYR A CB    1 
ATOM   1926 C  CG    . TYR A 1 260 ? 22.179  -22.057 1.703   1.00 59.57  ?  260 TYR A CG    1 
ATOM   1927 C  CD1   . TYR A 1 260 ? 23.061  -21.013 1.920   1.00 60.02  ?  260 TYR A CD1   1 
ATOM   1928 C  CD2   . TYR A 1 260 ? 21.416  -22.517 2.775   1.00 55.12  ?  260 TYR A CD2   1 
ATOM   1929 C  CE1   . TYR A 1 260 ? 23.182  -20.435 3.164   1.00 63.45  ?  260 TYR A CE1   1 
ATOM   1930 C  CE2   . TYR A 1 260 ? 21.519  -21.934 4.021   1.00 62.88  ?  260 TYR A CE2   1 
ATOM   1931 C  CZ    . TYR A 1 260 ? 22.402  -20.886 4.207   1.00 63.52  ?  260 TYR A CZ    1 
ATOM   1932 O  OH    . TYR A 1 260 ? 22.538  -20.291 5.436   1.00 63.24  ?  260 TYR A OH    1 
ATOM   1933 N  N     . ALA A 1 261 ? 20.933  -23.156 -2.509  1.00 54.40  ?  261 ALA A N     1 
ATOM   1934 C  CA    . ALA A 1 261 ? 20.906  -23.941 -3.737  1.00 56.20  ?  261 ALA A CA    1 
ATOM   1935 C  C     . ALA A 1 261 ? 21.294  -23.085 -4.929  1.00 52.23  ?  261 ALA A C     1 
ATOM   1936 O  O     . ALA A 1 261 ? 22.154  -23.465 -5.730  1.00 57.99  ?  261 ALA A O     1 
ATOM   1937 C  CB    . ALA A 1 261 ? 19.519  -24.548 -3.939  1.00 48.27  ?  261 ALA A CB    1 
ATOM   1938 N  N     . SER A 1 262 ? 20.679  -21.913 -5.047  1.00 50.77  ?  262 SER A N     1 
ATOM   1939 C  CA    . SER A 1 262 ? 21.022  -20.992 -6.126  1.00 55.24  ?  262 SER A CA    1 
ATOM   1940 C  C     . SER A 1 262 ? 22.489  -20.581 -6.056  1.00 56.67  ?  262 SER A C     1 
ATOM   1941 O  O     . SER A 1 262 ? 23.224  -20.699 -7.045  1.00 57.95  ?  262 SER A O     1 
ATOM   1942 C  CB    . SER A 1 262 ? 20.112  -19.772 -6.062  1.00 50.77  ?  262 SER A CB    1 
ATOM   1943 O  OG    . SER A 1 262 ? 20.113  -19.080 -7.293  1.00 63.62  ?  262 SER A OG    1 
ATOM   1944 N  N     . PHE A 1 263 ? 22.937  -20.112 -4.882  1.00 52.47  ?  263 PHE A N     1 
ATOM   1945 C  CA    . PHE A 1 263 ? 24.329  -19.701 -4.727  1.00 56.54  ?  263 PHE A CA    1 
ATOM   1946 C  C     . PHE A 1 263 ? 25.281  -20.800 -5.157  1.00 56.84  ?  263 PHE A C     1 
ATOM   1947 O  O     . PHE A 1 263 ? 26.346  -20.522 -5.714  1.00 56.60  ?  263 PHE A O     1 
ATOM   1948 C  CB    . PHE A 1 263 ? 24.642  -19.325 -3.284  1.00 52.42  ?  263 PHE A CB    1 
ATOM   1949 C  CG    . PHE A 1 263 ? 24.136  -17.987 -2.888  1.00 57.69  ?  263 PHE A CG    1 
ATOM   1950 C  CD1   . PHE A 1 263 ? 24.095  -17.617 -1.551  1.00 53.24  ?  263 PHE A CD1   1 
ATOM   1951 C  CD2   . PHE A 1 263 ? 23.645  -17.106 -3.851  1.00 57.16  ?  263 PHE A CD2   1 
ATOM   1952 C  CE1   . PHE A 1 263 ? 23.615  -16.366 -1.190  1.00 58.75  ?  263 PHE A CE1   1 
ATOM   1953 C  CE2   . PHE A 1 263 ? 23.150  -15.859 -3.500  1.00 52.72  ?  263 PHE A CE2   1 
ATOM   1954 C  CZ    . PHE A 1 263 ? 23.143  -15.484 -2.173  1.00 58.87  ?  263 PHE A CZ    1 
ATOM   1955 N  N     . GLU A 1 264 ? 24.938  -22.053 -4.862  1.00 59.29  ?  264 GLU A N     1 
ATOM   1956 C  CA    . GLU A 1 264 ? 25.858  -23.137 -5.172  1.00 59.39  ?  264 GLU A CA    1 
ATOM   1957 C  C     . GLU A 1 264 ? 25.876  -23.427 -6.656  1.00 58.79  ?  264 GLU A C     1 
ATOM   1958 O  O     . GLU A 1 264 ? 26.917  -23.806 -7.195  1.00 57.45  ?  264 GLU A O     1 
ATOM   1959 C  CB    . GLU A 1 264 ? 25.485  -24.390 -4.410  1.00 55.19  ?  264 GLU A CB    1 
ATOM   1960 C  CG    . GLU A 1 264 ? 26.387  -24.684 -3.252  1.00 59.15  ?  264 GLU A CG    1 
ATOM   1961 C  CD    . GLU A 1 264 ? 25.719  -25.646 -2.306  1.00 66.25  ?  264 GLU A CD    1 
ATOM   1962 O  OE1   . GLU A 1 264 ? 24.661  -26.207 -2.705  1.00 61.87  ?  264 GLU A OE1   1 
ATOM   1963 O  OE2   . GLU A 1 264 ? 26.242  -25.838 -1.180  1.00 69.73  ?  264 GLU A OE2   1 
ATOM   1964 N  N     . ALA A 1 265 ? 24.741  -23.256 -7.327  1.00 57.36  ?  265 ALA A N     1 
ATOM   1965 C  CA    . ALA A 1 265 ? 24.712  -23.367 -8.774  1.00 53.76  ?  265 ALA A CA    1 
ATOM   1966 C  C     . ALA A 1 265 ? 25.267  -22.130 -9.449  1.00 59.82  ?  265 ALA A C     1 
ATOM   1967 O  O     . ALA A 1 265 ? 25.220  -22.044 -10.680 1.00 66.60  ?  265 ALA A O     1 
ATOM   1968 C  CB    . ALA A 1 265 ? 23.285  -23.618 -9.254  1.00 55.70  ?  265 ALA A CB    1 
ATOM   1969 N  N     . GLY A 1 266 ? 25.769  -21.173 -8.677  1.00 61.99  ?  266 GLY A N     1 
ATOM   1970 C  CA    . GLY A 1 266 ? 26.206  -19.906 -9.239  1.00 60.52  ?  266 GLY A CA    1 
ATOM   1971 C  C     . GLY A 1 266 ? 25.114  -19.130 -9.943  1.00 62.31  ?  266 GLY A C     1 
ATOM   1972 O  O     . GLY A 1 266 ? 25.373  -18.519 -10.985 1.00 59.13  ?  266 GLY A O     1 
ATOM   1973 N  N     . VAL A 1 267 ? 23.901  -19.121 -9.399  1.00 64.67  ?  267 VAL A N     1 
ATOM   1974 C  CA    . VAL A 1 267 ? 22.780  -18.363 -9.954  1.00 64.50  ?  267 VAL A CA    1 
ATOM   1975 C  C     . VAL A 1 267 ? 22.458  -17.204 -9.005  1.00 64.27  ?  267 VAL A C     1 
ATOM   1976 O  O     . VAL A 1 267 ? 22.299  -17.437 -7.803  1.00 64.16  ?  267 VAL A O     1 
ATOM   1977 C  CB    . VAL A 1 267 ? 21.531  -19.239 -10.173 1.00 61.58  ?  267 VAL A CB    1 
ATOM   1978 C  CG1   . VAL A 1 267 ? 20.442  -18.479 -10.977 1.00 54.21  ?  267 VAL A CG1   1 
ATOM   1979 C  CG2   . VAL A 1 267 ? 21.912  -20.535 -10.846 1.00 60.75  ?  267 VAL A CG2   1 
ATOM   1980 N  N     . PRO A 1 268 ? 22.372  -15.973 -9.501  1.00 68.46  ?  268 PRO A N     1 
ATOM   1981 C  CA    . PRO A 1 268 ? 21.951  -14.850 -8.642  1.00 68.15  ?  268 PRO A CA    1 
ATOM   1982 C  C     . PRO A 1 268 ? 20.453  -14.851 -8.345  1.00 63.73  ?  268 PRO A C     1 
ATOM   1983 O  O     . PRO A 1 268 ? 19.624  -15.133 -9.216  1.00 63.17  ?  268 PRO A O     1 
ATOM   1984 C  CB    . PRO A 1 268 ? 22.334  -13.600 -9.452  1.00 63.21  ?  268 PRO A CB    1 
ATOM   1985 C  CG    . PRO A 1 268 ? 22.861  -14.061 -10.764 1.00 69.92  ?  268 PRO A CG    1 
ATOM   1986 C  CD    . PRO A 1 268 ? 22.996  -15.550 -10.769 1.00 69.06  ?  268 PRO A CD    1 
ATOM   1987 N  N     . LEU A 1 269 ? 20.120  -14.506 -7.096  1.00 57.44  ?  269 LEU A N     1 
ATOM   1988 C  CA    . LEU A 1 269 ? 18.750  -14.283 -6.650  1.00 59.70  ?  269 LEU A CA    1 
ATOM   1989 C  C     . LEU A 1 269 ? 18.281  -12.876 -7.009  1.00 59.45  ?  269 LEU A C     1 
ATOM   1990 O  O     . LEU A 1 269 ? 19.089  -11.971 -7.269  1.00 59.22  ?  269 LEU A O     1 
ATOM   1991 C  CB    . LEU A 1 269 ? 18.621  -14.480 -5.136  1.00 51.99  ?  269 LEU A CB    1 
ATOM   1992 C  CG    . LEU A 1 269 ? 19.349  -15.642 -4.467  1.00 55.20  ?  269 LEU A CG    1 
ATOM   1993 C  CD1   . LEU A 1 269 ? 19.341  -15.538 -2.953  1.00 51.11  ?  269 LEU A CD1   1 
ATOM   1994 C  CD2   . LEU A 1 269 ? 18.667  -16.907 -4.892  1.00 57.83  ?  269 LEU A CD2   1 
ATOM   1995 N  N     . ASP A 1 270 ? 16.951  -12.699 -7.014  1.00 57.36  ?  270 ASP A N     1 
ATOM   1996 C  CA    . ASP A 1 270 ? 16.355  -11.385 -7.253  1.00 61.38  ?  270 ASP A CA    1 
ATOM   1997 C  C     . ASP A 1 270 ? 17.007  -10.341 -6.351  1.00 60.85  ?  270 ASP A C     1 
ATOM   1998 O  O     . ASP A 1 270 ? 17.470  -10.645 -5.244  1.00 61.26  ?  270 ASP A O     1 
ATOM   1999 C  CB    . ASP A 1 270 ? 14.839  -11.432 -7.001  1.00 64.79  ?  270 ASP A CB    1 
ATOM   2000 C  CG    . ASP A 1 270 ? 14.085  -10.212 -7.566  1.00 75.36  ?  270 ASP A CG    1 
ATOM   2001 O  OD1   . ASP A 1 270 ? 13.416  -10.350 -8.626  1.00 77.77  ?  270 ASP A OD1   1 
ATOM   2002 O  OD2   . ASP A 1 270 ? 14.156  -9.114  -6.947  1.00 72.85  ?  270 ASP A OD2   1 
ATOM   2003 N  N     . HIS A 1 271 ? 17.042  -9.097  -6.838  1.00 61.31  ?  271 HIS A N     1 
ATOM   2004 C  CA    . HIS A 1 271 ? 17.768  -8.022  -6.161  1.00 65.38  ?  271 HIS A CA    1 
ATOM   2005 C  C     . HIS A 1 271 ? 17.351  -7.892  -4.695  1.00 64.95  ?  271 HIS A C     1 
ATOM   2006 O  O     . HIS A 1 271 ? 18.198  -7.850  -3.792  1.00 62.49  ?  271 HIS A O     1 
ATOM   2007 C  CB    . HIS A 1 271 ? 17.543  -6.702  -6.908  1.00 62.90  ?  271 HIS A CB    1 
ATOM   2008 N  N     . HIS A 1 272 ? 16.041  -7.834  -4.444  1.00 62.50  ?  272 HIS A N     1 
ATOM   2009 C  CA    . HIS A 1 272 ? 15.507  -7.707  -3.093  1.00 58.68  ?  272 HIS A CA    1 
ATOM   2010 C  C     . HIS A 1 272 ? 14.719  -8.954  -2.722  1.00 57.17  ?  272 HIS A C     1 
ATOM   2011 O  O     . HIS A 1 272 ? 13.517  -8.880  -2.459  1.00 54.24  ?  272 HIS A O     1 
ATOM   2012 C  CB    . HIS A 1 272 ? 14.615  -6.471  -2.990  1.00 60.45  ?  272 HIS A CB    1 
ATOM   2013 C  CG    . HIS A 1 272 ? 15.141  -5.277  -3.731  1.00 63.75  ?  272 HIS A CG    1 
ATOM   2014 N  ND1   . HIS A 1 272 ? 14.914  -5.074  -5.078  1.00 61.33  ?  272 HIS A ND1   1 
ATOM   2015 C  CD2   . HIS A 1 272 ? 15.860  -4.210  -3.304  1.00 57.82  ?  272 HIS A CD2   1 
ATOM   2016 C  CE1   . HIS A 1 272 ? 15.478  -3.939  -5.450  1.00 59.10  ?  272 HIS A CE1   1 
ATOM   2017 N  NE2   . HIS A 1 272 ? 16.059  -3.396  -4.394  1.00 57.27  ?  272 HIS A NE2   1 
ATOM   2018 N  N     . TYR A 1 273 ? 15.381  -10.111 -2.712  1.00 55.40  ?  273 TYR A N     1 
ATOM   2019 C  CA    . TYR A 1 273 ? 14.650  -11.352 -2.509  1.00 51.68  ?  273 TYR A CA    1 
ATOM   2020 C  C     . TYR A 1 273 ? 14.123  -11.470 -1.082  1.00 54.12  ?  273 TYR A C     1 
ATOM   2021 O  O     . TYR A 1 273 ? 13.043  -12.046 -0.867  1.00 48.37  ?  273 TYR A O     1 
ATOM   2022 C  CB    . TYR A 1 273 ? 15.530  -12.544 -2.864  1.00 47.37  ?  273 TYR A CB    1 
ATOM   2023 C  CG    . TYR A 1 273 ? 16.693  -12.777 -1.941  1.00 51.18  ?  273 TYR A CG    1 
ATOM   2024 C  CD1   . TYR A 1 273 ? 16.554  -13.556 -0.797  1.00 51.61  ?  273 TYR A CD1   1 
ATOM   2025 C  CD2   . TYR A 1 273 ? 17.948  -12.248 -2.231  1.00 49.38  ?  273 TYR A CD2   1 
ATOM   2026 C  CE1   . TYR A 1 273 ? 17.618  -13.789 0.040   1.00 51.77  ?  273 TYR A CE1   1 
ATOM   2027 C  CE2   . TYR A 1 273 ? 19.017  -12.466 -1.401  1.00 49.43  ?  273 TYR A CE2   1 
ATOM   2028 C  CZ    . TYR A 1 273 ? 18.849  -13.239 -0.263  1.00 58.40  ?  273 TYR A CZ    1 
ATOM   2029 O  OH    . TYR A 1 273 ? 19.919  -13.470 0.568   1.00 59.47  ?  273 TYR A OH    1 
ATOM   2030 N  N     . TYR A 1 274 ? 14.867  -10.942 -0.103  1.00 51.17  ?  274 TYR A N     1 
ATOM   2031 C  CA    . TYR A 1 274 ? 14.362  -10.887 1.265   1.00 50.66  ?  274 TYR A CA    1 
ATOM   2032 C  C     . TYR A 1 274 ? 13.075  -10.057 1.343   1.00 50.97  ?  274 TYR A C     1 
ATOM   2033 O  O     . TYR A 1 274 ? 12.068  -10.493 1.918   1.00 42.23  ?  274 TYR A O     1 
ATOM   2034 C  CB    . TYR A 1 274 ? 15.443  -10.319 2.188   1.00 54.15  ?  274 TYR A CB    1 
ATOM   2035 C  CG    . TYR A 1 274 ? 15.031  -10.278 3.636   1.00 51.66  ?  274 TYR A CG    1 
ATOM   2036 C  CD1   . TYR A 1 274 ? 14.366  -9.175  4.171   1.00 45.44  ?  274 TYR A CD1   1 
ATOM   2037 C  CD2   . TYR A 1 274 ? 15.282  -11.362 4.462   1.00 50.80  ?  274 TYR A CD2   1 
ATOM   2038 C  CE1   . TYR A 1 274 ? 13.989  -9.154  5.511   1.00 43.80  ?  274 TYR A CE1   1 
ATOM   2039 C  CE2   . TYR A 1 274 ? 14.906  -11.357 5.767   1.00 51.67  ?  274 TYR A CE2   1 
ATOM   2040 C  CZ    . TYR A 1 274 ? 14.259  -10.259 6.303   1.00 46.50  ?  274 TYR A CZ    1 
ATOM   2041 O  OH    . TYR A 1 274 ? 13.910  -10.316 7.630   1.00 42.72  ?  274 TYR A OH    1 
ATOM   2042 N  N     . GLU A 1 275 ? 13.084  -8.859  0.748   1.00 52.65  ?  275 GLU A N     1 
ATOM   2043 C  CA    . GLU A 1 275 ? 11.908  -7.998  0.813   1.00 48.35  ?  275 GLU A CA    1 
ATOM   2044 C  C     . GLU A 1 275 ? 10.753  -8.572  0.007   1.00 45.83  ?  275 GLU A C     1 
ATOM   2045 O  O     . GLU A 1 275 ? 9.593   -8.378  0.377   1.00 44.89  ?  275 GLU A O     1 
ATOM   2046 C  CB    . GLU A 1 275 ? 12.261  -6.590  0.333   1.00 52.21  ?  275 GLU A CB    1 
ATOM   2047 C  CG    . GLU A 1 275 ? 13.191  -5.803  1.285   1.00 54.12  ?  275 GLU A CG    1 
ATOM   2048 C  CD    . GLU A 1 275 ? 14.682  -6.214  1.217   1.00 60.44  ?  275 GLU A CD    1 
ATOM   2049 O  OE1   . GLU A 1 275 ? 15.175  -6.631  0.136   1.00 57.34  ?  275 GLU A OE1   1 
ATOM   2050 O  OE2   . GLU A 1 275 ? 15.371  -6.101  2.264   1.00 62.22  ?  275 GLU A OE2   1 
ATOM   2051 N  N     . ARG A 1 276 ? 11.030  -9.302  -1.080  1.00 47.60  ?  276 ARG A N     1 
ATOM   2052 C  CA    . ARG A 1 276 ? 9.930   -10.044 -1.699  1.00 48.57  ?  276 ARG A CA    1 
ATOM   2053 C  C     . ARG A 1 276 ? 9.465   -11.179 -0.793  1.00 46.07  ?  276 ARG A C     1 
ATOM   2054 O  O     . ARG A 1 276 ? 8.286   -11.564 -0.830  1.00 43.02  ?  276 ARG A O     1 
ATOM   2055 C  CB    . ARG A 1 276 ? 10.316  -10.614 -3.071  1.00 46.38  ?  276 ARG A CB    1 
ATOM   2056 C  CG    . ARG A 1 276 ? 11.139  -9.725  -3.985  1.00 56.42  ?  276 ARG A CG    1 
ATOM   2057 C  CD    . ARG A 1 276 ? 10.305  -8.926  -4.984  1.00 64.40  ?  276 ARG A CD    1 
ATOM   2058 N  NE    . ARG A 1 276 ? 11.172  -8.144  -5.869  1.00 68.11  ?  276 ARG A NE    1 
ATOM   2059 C  CZ    . ARG A 1 276 ? 11.183  -6.817  -5.951  1.00 65.93  ?  276 ARG A CZ    1 
ATOM   2060 N  NH1   . ARG A 1 276 ? 10.368  -6.066  -5.220  1.00 61.14  ?  276 ARG A NH1   1 
ATOM   2061 N  NH2   . ARG A 1 276 ? 12.048  -6.227  -6.776  1.00 68.85  ?  276 ARG A NH2   1 
ATOM   2062 N  N     . THR A 1 277 ? 10.381  -11.726 0.019   1.00 43.66  ?  277 THR A N     1 
ATOM   2063 C  CA    . THR A 1 277 ? 10.039  -12.835 0.902   1.00 45.95  ?  277 THR A CA    1 
ATOM   2064 C  C     . THR A 1 277 ? 9.079   -12.381 1.986   1.00 41.97  ?  277 THR A C     1 
ATOM   2065 O  O     . THR A 1 277 ? 8.100   -13.079 2.285   1.00 40.57  ?  277 THR A O     1 
ATOM   2066 C  CB    . THR A 1 277 ? 11.305  -13.436 1.514   1.00 41.05  ?  277 THR A CB    1 
ATOM   2067 O  OG1   . THR A 1 277 ? 12.091  -14.004 0.464   1.00 39.49  ?  277 THR A OG1   1 
ATOM   2068 C  CG2   . THR A 1 277 ? 10.944  -14.516 2.557   1.00 36.42  ?  277 THR A CG2   1 
ATOM   2069 N  N     . LEU A 1 278 ? 9.328   -11.195 2.551   1.00 37.43  ?  278 LEU A N     1 
ATOM   2070 C  CA    . LEU A 1 278 ? 8.444   -10.643 3.563   1.00 41.52  ?  278 LEU A CA    1 
ATOM   2071 C  C     . LEU A 1 278 ? 7.013   -10.569 3.058   1.00 42.23  ?  278 LEU A C     1 
ATOM   2072 O  O     . LEU A 1 278 ? 6.079   -10.918 3.784   1.00 38.78  ?  278 LEU A O     1 
ATOM   2073 C  CB    . LEU A 1 278 ? 8.948   -9.269  4.004   1.00 41.73  ?  278 LEU A CB    1 
ATOM   2074 C  CG    . LEU A 1 278 ? 10.233  -9.259  4.856   1.00 38.65  ?  278 LEU A CG    1 
ATOM   2075 C  CD1   . LEU A 1 278 ? 10.603  -7.831  5.138   1.00 41.00  ?  278 LEU A CD1   1 
ATOM   2076 C  CD2   . LEU A 1 278 ? 10.107  -10.021 6.187   1.00 36.56  ?  278 LEU A CD2   1 
ATOM   2077 N  N     . GLN A 1 279 ? 6.821   -10.177 1.793   1.00 44.54  ?  279 GLN A N     1 
ATOM   2078 C  CA    . GLN A 1 279 ? 5.463   -10.115 1.266   1.00 44.80  ?  279 GLN A CA    1 
ATOM   2079 C  C     . GLN A 1 279 ? 4.809   -11.496 1.216   1.00 41.35  ?  279 GLN A C     1 
ATOM   2080 O  O     . GLN A 1 279 ? 3.617   -11.628 1.491   1.00 41.08  ?  279 GLN A O     1 
ATOM   2081 C  CB    . GLN A 1 279 ? 5.459   -9.443  -0.104  1.00 44.26  ?  279 GLN A CB    1 
ATOM   2082 C  CG    . GLN A 1 279 ? 4.040   -9.206  -0.630  1.00 54.87  ?  279 GLN A CG    1 
ATOM   2083 C  CD    . GLN A 1 279 ? 3.293   -8.052  0.096   1.00 57.90  ?  279 GLN A CD    1 
ATOM   2084 O  OE1   . GLN A 1 279 ? 3.804   -6.923  0.209   1.00 54.74  ?  279 GLN A OE1   1 
ATOM   2085 N  NE2   . GLN A 1 279 ? 2.066   -8.342  0.571   1.00 58.23  ?  279 GLN A NE2   1 
ATOM   2086 N  N     . VAL A 1 280 ? 5.578   -12.543 0.913   1.00 47.91  ?  280 VAL A N     1 
ATOM   2087 C  CA    . VAL A 1 280 ? 5.038   -13.906 0.973   1.00 47.96  ?  280 VAL A CA    1 
ATOM   2088 C  C     . VAL A 1 280 ? 4.723   -14.299 2.417   1.00 41.33  ?  280 VAL A C     1 
ATOM   2089 O  O     . VAL A 1 280 ? 3.696   -14.928 2.705   1.00 41.21  ?  280 VAL A O     1 
ATOM   2090 C  CB    . VAL A 1 280 ? 6.019   -14.900 0.312   1.00 50.32  ?  280 VAL A CB    1 
ATOM   2091 C  CG1   . VAL A 1 280 ? 5.633   -16.357 0.607   1.00 39.61  ?  280 VAL A CG1   1 
ATOM   2092 C  CG2   . VAL A 1 280 ? 6.094   -14.651 -1.201  1.00 48.13  ?  280 VAL A CG2   1 
ATOM   2093 N  N     . LEU A 1 281 ? 5.595   -13.943 3.351   1.00 41.62  ?  281 LEU A N     1 
ATOM   2094 C  CA    . LEU A 1 281 ? 5.354   -14.365 4.722   1.00 40.63  ?  281 LEU A CA    1 
ATOM   2095 C  C     . LEU A 1 281 ? 4.155   -13.641 5.323   1.00 40.29  ?  281 LEU A C     1 
ATOM   2096 O  O     . LEU A 1 281 ? 3.370   -14.241 6.070   1.00 37.79  ?  281 LEU A O     1 
ATOM   2097 C  CB    . LEU A 1 281 ? 6.615   -14.151 5.546   1.00 43.68  ?  281 LEU A CB    1 
ATOM   2098 C  CG    . LEU A 1 281 ? 7.829   -14.963 5.099   1.00 36.91  ?  281 LEU A CG    1 
ATOM   2099 C  CD1   . LEU A 1 281 ? 8.964   -14.585 5.992   1.00 38.17  ?  281 LEU A CD1   1 
ATOM   2100 C  CD2   . LEU A 1 281 ? 7.568   -16.421 5.229   1.00 31.23  ?  281 LEU A CD2   1 
ATOM   2101 N  N     . TYR A 1 282 ? 3.977   -12.359 4.975   1.00 41.35  ?  282 TYR A N     1 
ATOM   2102 C  CA    . TYR A 1 282 ? 2.815   -11.614 5.451   1.00 39.81  ?  282 TYR A CA    1 
ATOM   2103 C  C     . TYR A 1 282 ? 1.507   -12.265 4.985   1.00 39.98  ?  282 TYR A C     1 
ATOM   2104 O  O     . TYR A 1 282 ? 0.620   -12.541 5.798   1.00 40.09  ?  282 TYR A O     1 
ATOM   2105 C  CB    . TYR A 1 282 ? 2.923   -10.145 4.996   1.00 40.61  ?  282 TYR A CB    1 
ATOM   2106 C  CG    . TYR A 1 282 ? 1.892   -9.219  5.641   1.00 37.56  ?  282 TYR A CG    1 
ATOM   2107 C  CD1   . TYR A 1 282 ? 1.998   -8.830  6.968   1.00 36.97  ?  282 TYR A CD1   1 
ATOM   2108 C  CD2   . TYR A 1 282 ? 0.816   -8.746  4.911   1.00 38.45  ?  282 TYR A CD2   1 
ATOM   2109 C  CE1   . TYR A 1 282 ? 1.048   -7.978  7.556   1.00 38.07  ?  282 TYR A CE1   1 
ATOM   2110 C  CE2   . TYR A 1 282 ? -0.129  -7.899  5.470   1.00 39.24  ?  282 TYR A CE2   1 
ATOM   2111 C  CZ    . TYR A 1 282 ? -0.016  -7.518  6.794   1.00 42.21  ?  282 TYR A CZ    1 
ATOM   2112 O  OH    . TYR A 1 282 ? -1.000  -6.695  7.334   1.00 41.13  ?  282 TYR A OH    1 
ATOM   2113 N  N     . ARG A 1 283 ? 1.362   -12.486 3.669   1.00 43.97  ?  283 ARG A N     1 
ATOM   2114 C  CA    . ARG A 1 283 ? 0.281   -13.299 3.102   1.00 45.90  ?  283 ARG A CA    1 
ATOM   2115 C  C     . ARG A 1 283 ? 0.010   -14.567 3.900   1.00 45.47  ?  283 ARG A C     1 
ATOM   2116 O  O     . ARG A 1 283 ? -1.136  -14.852 4.273   1.00 50.44  ?  283 ARG A O     1 
ATOM   2117 C  CB    . ARG A 1 283 ? 0.628   -13.711 1.667   1.00 43.83  ?  283 ARG A CB    1 
ATOM   2118 C  CG    . ARG A 1 283 ? -0.117  -12.994 0.576   1.00 50.81  ?  283 ARG A CG    1 
ATOM   2119 C  CD    . ARG A 1 283 ? 0.402   -13.454 -0.803  1.00 60.48  ?  283 ARG A CD    1 
ATOM   2120 N  NE    . ARG A 1 283 ? 1.297   -12.472 -1.414  1.00 57.39  ?  283 ARG A NE    1 
ATOM   2121 C  CZ    . ARG A 1 283 ? 2.453   -12.765 -2.000  1.00 61.85  ?  283 ARG A CZ    1 
ATOM   2122 N  NH1   . ARG A 1 283 ? 2.875   -14.015 -2.106  1.00 63.80  ?  283 ARG A NH1   1 
ATOM   2123 N  NH2   . ARG A 1 283 ? 3.210   -11.777 -2.487  1.00 59.07  ?  283 ARG A NH2   1 
ATOM   2124 N  N     . ALA A 1 284 ? 1.053   -15.361 4.154   1.00 36.54  ?  284 ALA A N     1 
ATOM   2125 C  CA    . ALA A 1 284 ? 0.848   -16.621 4.865   1.00 36.31  ?  284 ALA A CA    1 
ATOM   2126 C  C     . ALA A 1 284 ? 0.315   -16.429 6.280   1.00 40.13  ?  284 ALA A C     1 
ATOM   2127 O  O     . ALA A 1 284 ? -0.170  -17.389 6.882   1.00 41.12  ?  284 ALA A O     1 
ATOM   2128 C  CB    . ALA A 1 284 ? 2.157   -17.416 4.930   1.00 37.45  ?  284 ALA A CB    1 
ATOM   2129 N  N     . LEU A 1 285 ? 0.435   -15.240 6.850   1.00 38.84  ?  285 LEU A N     1 
ATOM   2130 C  CA    . LEU A 1 285 ? -0.048  -15.013 8.204   1.00 40.68  ?  285 LEU A CA    1 
ATOM   2131 C  C     . LEU A 1 285 ? -1.498  -14.537 8.246   1.00 42.66  ?  285 LEU A C     1 
ATOM   2132 O  O     . LEU A 1 285 ? -2.009  -14.241 9.327   1.00 42.96  ?  285 LEU A O     1 
ATOM   2133 C  CB    . LEU A 1 285 ? 0.855   -13.991 8.900   1.00 40.00  ?  285 LEU A CB    1 
ATOM   2134 C  CG    . LEU A 1 285 ? 2.262   -14.413 9.317   1.00 38.90  ?  285 LEU A CG    1 
ATOM   2135 C  CD1   . LEU A 1 285 ? 3.162   -13.186 9.385   1.00 36.48  ?  285 LEU A CD1   1 
ATOM   2136 C  CD2   . LEU A 1 285 ? 2.204   -15.108 10.666  1.00 32.95  ?  285 LEU A CD2   1 
ATOM   2137 N  N     . GLY A 1 286 ? -2.169  -14.451 7.099   1.00 46.49  ?  286 GLY A N     1 
ATOM   2138 C  CA    . GLY A 1 286 ? -3.391  -13.695 6.972   1.00 53.17  ?  286 GLY A CA    1 
ATOM   2139 C  C     . GLY A 1 286 ? -4.638  -14.550 6.800   1.00 56.12  ?  286 GLY A C     1 
ATOM   2140 O  O     . GLY A 1 286 ? -4.562  -15.767 6.629   1.00 51.28  ?  286 GLY A O     1 
ATOM   2141 N  N     . ASP A 1 287 ? -5.816  -13.835 6.795   1.00 66.56  ?  287 ASP A N     1 
ATOM   2142 C  CA    . ASP A 1 287 ? -7.199  -14.307 6.957   1.00 65.05  ?  287 ASP A CA    1 
ATOM   2143 C  C     . ASP A 1 287 ? -7.411  -15.641 6.230   1.00 65.04  ?  287 ASP A C     1 
ATOM   2144 O  O     . ASP A 1 287 ? -7.412  -16.674 6.923   1.00 69.58  ?  287 ASP A O     1 
ATOM   2145 C  CB    . ASP A 1 287 ? -8.202  -13.207 6.548   1.00 61.11  ?  287 ASP A CB    1 
ATOM   2146 N  N     . PRO A 1 288 ? -7.532  -15.726 4.895   1.00 65.21  ?  288 PRO A N     1 
ATOM   2147 C  CA    . PRO A 1 288 ? -7.504  -17.075 4.280   1.00 61.55  ?  288 PRO A CA    1 
ATOM   2148 C  C     . PRO A 1 288 ? -6.069  -17.574 4.161   1.00 56.83  ?  288 PRO A C     1 
ATOM   2149 O  O     . PRO A 1 288 ? -5.248  -16.982 3.455   1.00 54.38  ?  288 PRO A O     1 
ATOM   2150 C  CB    . PRO A 1 288 ? -8.146  -16.858 2.903   1.00 58.13  ?  288 PRO A CB    1 
ATOM   2151 C  CG    . PRO A 1 288 ? -7.718  -15.497 2.537   1.00 67.11  ?  288 PRO A CG    1 
ATOM   2152 C  CD    . PRO A 1 288 ? -7.650  -14.690 3.844   1.00 64.65  ?  288 PRO A CD    1 
ATOM   2153 N  N     . GLN A 1 289 ? -5.766  -18.662 4.871   1.00 56.98  ?  289 GLN A N     1 
ATOM   2154 C  CA    . GLN A 1 289 ? -4.443  -19.246 5.058   1.00 55.40  ?  289 GLN A CA    1 
ATOM   2155 C  C     . GLN A 1 289 ? -4.100  -20.159 3.894   1.00 52.44  ?  289 GLN A C     1 
ATOM   2156 O  O     . GLN A 1 289 ? -4.868  -21.079 3.600   1.00 54.21  ?  289 GLN A O     1 
ATOM   2157 C  CB    . GLN A 1 289 ? -4.378  -20.041 6.359   1.00 51.91  ?  289 GLN A CB    1 
ATOM   2158 C  CG    . GLN A 1 289 ? -3.030  -20.688 6.576   1.00 55.63  ?  289 GLN A CG    1 
ATOM   2159 C  CD    . GLN A 1 289 ? -3.041  -21.731 7.663   1.00 59.67  ?  289 GLN A CD    1 
ATOM   2160 O  OE1   . GLN A 1 289 ? -2.208  -21.711 8.572   1.00 58.81  ?  289 GLN A OE1   1 
ATOM   2161 N  NE2   . GLN A 1 289 ? -3.978  -22.666 7.571   1.00 66.45  ?  289 GLN A NE2   1 
ATOM   2162 N  N     . PRO A 1 290 ? -2.968  -19.939 3.219   1.00 57.93  ?  290 PRO A N     1 
ATOM   2163 C  CA    . PRO A 1 290 ? -2.556  -20.836 2.132   1.00 49.73  ?  290 PRO A CA    1 
ATOM   2164 C  C     . PRO A 1 290 ? -1.897  -22.110 2.643   1.00 52.94  ?  290 PRO A C     1 
ATOM   2165 O  O     . PRO A 1 290 ? -1.342  -22.173 3.744   1.00 51.48  ?  290 PRO A O     1 
ATOM   2166 C  CB    . PRO A 1 290 ? -1.563  -19.989 1.329   1.00 53.73  ?  290 PRO A CB    1 
ATOM   2167 C  CG    . PRO A 1 290 ? -0.980  -19.035 2.323   1.00 54.43  ?  290 PRO A CG    1 
ATOM   2168 C  CD    . PRO A 1 290 ? -2.114  -18.738 3.307   1.00 56.25  ?  290 PRO A CD    1 
ATOM   2169 N  N     . SER A 1 291 ? -1.966  -23.138 1.798   1.00 58.01  ?  291 SER A N     1 
ATOM   2170 C  CA    . SER A 1 291 ? -1.267  -24.397 2.043   1.00 56.17  ?  291 SER A CA    1 
ATOM   2171 C  C     . SER A 1 291 ? 0.250   -24.206 1.918   1.00 54.03  ?  291 SER A C     1 
ATOM   2172 O  O     . SER A 1 291 ? 0.708   -23.304 1.209   1.00 51.22  ?  291 SER A O     1 
ATOM   2173 C  CB    . SER A 1 291 ? -1.738  -25.460 1.046   1.00 51.42  ?  291 SER A CB    1 
ATOM   2174 O  OG    . SER A 1 291 ? -1.180  -25.226 -0.249  1.00 56.21  ?  291 SER A OG    1 
ATOM   2175 N  N     . PRO A 1 292 ? 1.050   -25.071 2.571   1.00 53.04  ?  292 PRO A N     1 
ATOM   2176 C  CA    . PRO A 1 292 ? 2.508   -24.871 2.555   1.00 57.13  ?  292 PRO A CA    1 
ATOM   2177 C  C     . PRO A 1 292 ? 3.108   -24.994 1.177   1.00 58.26  ?  292 PRO A C     1 
ATOM   2178 O  O     . PRO A 1 292 ? 4.082   -24.298 0.855   1.00 54.44  ?  292 PRO A O     1 
ATOM   2179 C  CB    . PRO A 1 292 ? 3.032   -25.982 3.480   1.00 62.46  ?  292 PRO A CB    1 
ATOM   2180 C  CG    . PRO A 1 292 ? 1.851   -26.519 4.182   1.00 59.08  ?  292 PRO A CG    1 
ATOM   2181 C  CD    . PRO A 1 292 ? 0.692   -26.310 3.276   1.00 59.57  ?  292 PRO A CD    1 
ATOM   2182 N  N     . ALA A 1 293 ? 2.559   -25.892 0.358   1.00 61.06  ?  293 ALA A N     1 
ATOM   2183 C  CA    . ALA A 1 293 ? 3.029   -26.016 -1.013  1.00 55.32  ?  293 ALA A CA    1 
ATOM   2184 C  C     . ALA A 1 293 ? 2.816   -24.722 -1.772  1.00 53.39  ?  293 ALA A C     1 
ATOM   2185 O  O     . ALA A 1 293 ? 3.621   -24.382 -2.647  1.00 56.81  ?  293 ALA A O     1 
ATOM   2186 C  CB    . ALA A 1 293 ? 2.326   -27.182 -1.712  1.00 53.01  ?  293 ALA A CB    1 
ATOM   2187 N  N     . GLN A 1 294 ? 1.764   -23.970 -1.422  1.00 54.12  ?  294 GLN A N     1 
ATOM   2188 C  CA    . GLN A 1 294 ? 1.490   -22.692 -2.083  1.00 57.23  ?  294 GLN A CA    1 
ATOM   2189 C  C     . GLN A 1 294 ? 2.512   -21.627 -1.687  1.00 57.18  ?  294 GLN A C     1 
ATOM   2190 O  O     . GLN A 1 294 ? 3.038   -20.906 -2.544  1.00 55.56  ?  294 GLN A O     1 
ATOM   2191 C  CB    . GLN A 1 294 ? 0.067   -22.232 -1.759  1.00 61.49  ?  294 GLN A CB    1 
ATOM   2192 C  CG    . GLN A 1 294 ? -0.248  -20.798 -2.207  1.00 66.36  ?  294 GLN A CG    1 
ATOM   2193 C  CD    . GLN A 1 294 ? -0.831  -20.699 -3.606  1.00 74.59  ?  294 GLN A CD    1 
ATOM   2194 O  OE1   . GLN A 1 294 ? -0.198  -20.151 -4.521  1.00 72.76  ?  294 GLN A OE1   1 
ATOM   2195 N  NE2   . GLN A 1 294 ? -2.063  -21.200 -3.776  1.00 81.55  ?  294 GLN A NE2   1 
ATOM   2196 N  N     . VAL A 1 295 ? 2.807   -21.517 -0.389  1.00 57.68  ?  295 VAL A N     1 
ATOM   2197 C  CA    . VAL A 1 295 ? 3.850   -20.600 0.073   1.00 54.63  ?  295 VAL A CA    1 
ATOM   2198 C  C     . VAL A 1 295 ? 5.174   -20.926 -0.606  1.00 52.90  ?  295 VAL A C     1 
ATOM   2199 O  O     . VAL A 1 295 ? 5.881   -20.037 -1.097  1.00 52.85  ?  295 VAL A O     1 
ATOM   2200 C  CB    . VAL A 1 295 ? 3.974   -20.669 1.607   1.00 50.56  ?  295 VAL A CB    1 
ATOM   2201 C  CG1   . VAL A 1 295 ? 4.978   -19.670 2.104   1.00 45.08  ?  295 VAL A CG1   1 
ATOM   2202 C  CG2   . VAL A 1 295 ? 2.624   -20.459 2.261   1.00 47.03  ?  295 VAL A CG2   1 
ATOM   2203 N  N     . GLU A 1 296 ? 5.519   -22.214 -0.652  1.00 53.93  ?  296 GLU A N     1 
ATOM   2204 C  CA    . GLU A 1 296 ? 6.766   -22.641 -1.279  1.00 57.57  ?  296 GLU A CA    1 
ATOM   2205 C  C     . GLU A 1 296 ? 6.864   -22.160 -2.724  1.00 59.26  ?  296 GLU A C     1 
ATOM   2206 O  O     . GLU A 1 296 ? 7.925   -21.690 -3.161  1.00 61.40  ?  296 GLU A O     1 
ATOM   2207 C  CB    . GLU A 1 296 ? 6.880   -24.159 -1.202  1.00 59.77  ?  296 GLU A CB    1 
ATOM   2208 C  CG    . GLU A 1 296 ? 8.000   -24.754 -2.030  1.00 66.19  ?  296 GLU A CG    1 
ATOM   2209 C  CD    . GLU A 1 296 ? 8.872   -25.691 -1.219  1.00 73.07  ?  296 GLU A CD    1 
ATOM   2210 O  OE1   . GLU A 1 296 ? 8.512   -25.949 -0.046  1.00 74.22  ?  296 GLU A OE1   1 
ATOM   2211 O  OE2   . GLU A 1 296 ? 9.913   -26.163 -1.752  1.00 80.31  ?  296 GLU A OE2   1 
ATOM   2212 N  N     . ASP A 1 297 ? 5.763   -22.248 -3.473  1.00 62.00  ?  297 ASP A N     1 
ATOM   2213 C  CA    . ASP A 1 297 ? 5.778   -21.793 -4.859  1.00 58.33  ?  297 ASP A CA    1 
ATOM   2214 C  C     . ASP A 1 297 ? 6.024   -20.291 -4.920  1.00 55.80  ?  297 ASP A C     1 
ATOM   2215 O  O     . ASP A 1 297 ? 6.714   -19.799 -5.821  1.00 60.11  ?  297 ASP A O     1 
ATOM   2216 C  CB    . ASP A 1 297 ? 4.449   -22.138 -5.541  1.00 62.91  ?  297 ASP A CB    1 
ATOM   2217 C  CG    . ASP A 1 297 ? 4.162   -23.651 -5.591  1.00 71.23  ?  297 ASP A CG    1 
ATOM   2218 O  OD1   . ASP A 1 297 ? 5.103   -24.499 -5.522  1.00 64.93  ?  297 ASP A OD1   1 
ATOM   2219 O  OD2   . ASP A 1 297 ? 2.952   -23.988 -5.693  1.00 73.08  ?  297 ASP A OD2   1 
ATOM   2220 N  N     . GLU A 1 298 ? 5.478   -19.545 -3.955  1.00 57.99  ?  298 GLU A N     1 
ATOM   2221 C  CA    . GLU A 1 298 ? 5.677   -18.102 -3.936  1.00 55.28  ?  298 GLU A CA    1 
ATOM   2222 C  C     . GLU A 1 298 ? 7.077   -17.730 -3.456  1.00 50.12  ?  298 GLU A C     1 
ATOM   2223 O  O     . GLU A 1 298 ? 7.679   -16.791 -3.976  1.00 53.03  ?  298 GLU A O     1 
ATOM   2224 C  CB    . GLU A 1 298 ? 4.606   -17.452 -3.074  1.00 57.03  ?  298 GLU A CB    1 
ATOM   2225 C  CG    . GLU A 1 298 ? 3.238   -17.492 -3.708  1.00 55.22  ?  298 GLU A CG    1 
ATOM   2226 C  CD    . GLU A 1 298 ? 2.189   -16.956 -2.789  1.00 64.37  ?  298 GLU A CD    1 
ATOM   2227 O  OE1   . GLU A 1 298 ? 2.546   -16.184 -1.878  1.00 68.90  ?  298 GLU A OE1   1 
ATOM   2228 O  OE2   . GLU A 1 298 ? 1.006   -17.298 -2.965  1.00 70.40  ?  298 GLU A OE2   1 
ATOM   2229 N  N     . LEU A 1 299 ? 7.610   -18.446 -2.468  1.00 51.19  ?  299 LEU A N     1 
ATOM   2230 C  CA    . LEU A 1 299 ? 9.009   -18.256 -2.113  1.00 51.35  ?  299 LEU A CA    1 
ATOM   2231 C  C     . LEU A 1 299 ? 9.910   -18.468 -3.320  1.00 56.74  ?  299 LEU A C     1 
ATOM   2232 O  O     . LEU A 1 299 ? 10.917  -17.772 -3.474  1.00 48.86  ?  299 LEU A O     1 
ATOM   2233 C  CB    . LEU A 1 299 ? 9.420   -19.204 -0.994  1.00 46.66  ?  299 LEU A CB    1 
ATOM   2234 C  CG    . LEU A 1 299 ? 8.877   -18.948 0.394   1.00 50.55  ?  299 LEU A CG    1 
ATOM   2235 C  CD1   . LEU A 1 299 ? 9.145   -20.152 1.284   1.00 47.31  ?  299 LEU A CD1   1 
ATOM   2236 C  CD2   . LEU A 1 299 ? 9.564   -17.714 0.930   1.00 51.41  ?  299 LEU A CD2   1 
ATOM   2237 N  N     . ARG A 1 300 ? 9.574   -19.437 -4.181  1.00 54.76  ?  300 ARG A N     1 
ATOM   2238 C  CA    . ARG A 1 300 ? 10.287  -19.560 -5.445  1.00 53.26  ?  300 ARG A CA    1 
ATOM   2239 C  C     . ARG A 1 300 ? 10.269  -18.250 -6.223  1.00 57.91  ?  300 ARG A C     1 
ATOM   2240 O  O     . ARG A 1 300 ? 11.321  -17.639 -6.471  1.00 61.84  ?  300 ARG A O     1 
ATOM   2241 C  CB    . ARG A 1 300 ? 9.701   -20.684 -6.291  1.00 62.23  ?  300 ARG A CB    1 
ATOM   2242 C  CG    . ARG A 1 300 ? 10.632  -21.072 -7.448  1.00 65.95  ?  300 ARG A CG    1 
ATOM   2243 C  CD    . ARG A 1 300 ? 11.442  -22.305 -7.098  1.00 65.34  ?  300 ARG A CD    1 
ATOM   2244 N  NE    . ARG A 1 300 ? 10.581  -23.284 -6.445  1.00 67.95  ?  300 ARG A NE    1 
ATOM   2245 C  CZ    . ARG A 1 300 ? 11.024  -24.332 -5.772  1.00 66.42  ?  300 ARG A CZ    1 
ATOM   2246 N  NH1   . ARG A 1 300 ? 12.322  -24.585 -5.668  1.00 57.07  ?  300 ARG A NH1   1 
ATOM   2247 N  NH2   . ARG A 1 300 ? 10.145  -25.135 -5.172  1.00 67.32  ?  300 ARG A NH2   1 
ATOM   2248 N  N     . ALA A 1 301 ? 9.077   -17.804 -6.627  1.00 56.58  ?  301 ALA A N     1 
ATOM   2249 C  CA    . ALA A 1 301 ? 8.995   -16.623 -7.481  1.00 57.47  ?  301 ALA A CA    1 
ATOM   2250 C  C     . ALA A 1 301 ? 9.717   -15.439 -6.857  1.00 53.43  ?  301 ALA A C     1 
ATOM   2251 O  O     . ALA A 1 301 ? 10.443  -14.707 -7.542  1.00 52.12  ?  301 ALA A O     1 
ATOM   2252 C  CB    . ALA A 1 301 ? 7.533   -16.284 -7.763  1.00 52.81  ?  301 ALA A CB    1 
ATOM   2253 N  N     . ALA A 1 302 ? 9.547   -15.252 -5.548  1.00 52.25  ?  302 ALA A N     1 
ATOM   2254 C  CA    . ALA A 1 302 ? 10.225  -14.153 -4.873  1.00 56.05  ?  302 ALA A CA    1 
ATOM   2255 C  C     . ALA A 1 302 ? 11.733  -14.239 -5.072  1.00 51.18  ?  302 ALA A C     1 
ATOM   2256 O  O     . ALA A 1 302 ? 12.393  -13.226 -5.317  1.00 53.87  ?  302 ALA A O     1 
ATOM   2257 C  CB    . ALA A 1 302 ? 9.863   -14.145 -3.383  1.00 45.85  ?  302 ALA A CB    1 
ATOM   2258 N  N     . LEU A 1 303 ? 12.290  -15.442 -5.014  1.00 50.62  ?  303 LEU A N     1 
ATOM   2259 C  CA    . LEU A 1 303 ? 13.733  -15.567 -5.133  1.00 56.84  ?  303 LEU A CA    1 
ATOM   2260 C  C     . LEU A 1 303 ? 14.214  -15.610 -6.588  1.00 63.28  ?  303 LEU A C     1 
ATOM   2261 O  O     . LEU A 1 303 ? 15.334  -15.158 -6.866  1.00 59.07  ?  303 LEU A O     1 
ATOM   2262 C  CB    . LEU A 1 303 ? 14.210  -16.787 -4.340  1.00 49.09  ?  303 LEU A CB    1 
ATOM   2263 C  CG    . LEU A 1 303 ? 14.832  -16.363 -2.995  1.00 47.64  ?  303 LEU A CG    1 
ATOM   2264 C  CD1   . LEU A 1 303 ? 13.898  -15.471 -2.224  1.00 49.51  ?  303 LEU A CD1   1 
ATOM   2265 C  CD2   . LEU A 1 303 ? 15.231  -17.509 -2.116  1.00 48.31  ?  303 LEU A CD2   1 
ATOM   2266 N  N     . GLU A 1 304 ? 13.395  -16.121 -7.519  1.00 67.65  ?  304 GLU A N     1 
ATOM   2267 C  CA    . GLU A 1 304 ? 13.648  -16.001 -8.967  1.00 64.57  ?  304 GLU A CA    1 
ATOM   2268 C  C     . GLU A 1 304 ? 13.094  -14.686 -9.508  1.00 68.15  ?  304 GLU A C     1 
ATOM   2269 O  O     . GLU A 1 304 ? 13.621  -13.607 -9.235  1.00 74.62  ?  304 GLU A O     1 
ATOM   2270 C  CB    . GLU A 1 304 ? 13.009  -17.154 -9.760  1.00 66.60  ?  304 GLU A CB    1 
ATOM   2271 C  CG    . GLU A 1 304 ? 13.401  -18.585 -9.353  1.00 70.91  ?  304 GLU A CG    1 
ATOM   2272 C  CD    . GLU A 1 304 ? 14.901  -18.798 -9.213  1.00 75.02  ?  304 GLU A CD    1 
ATOM   2273 O  OE1   . GLU A 1 304 ? 15.602  -18.968 -10.251 1.00 79.44  ?  304 GLU A OE1   1 
ATOM   2274 O  OE2   . GLU A 1 304 ? 15.373  -18.816 -8.049  1.00 73.62  ?  304 GLU A OE2   1 
ATOM   2275 N  N     . MET B 1 1   ? 17.776  22.497  -40.457 1.00 37.82  ?  1   MET B N     1 
ATOM   2276 C  CA    . MET B 1 1   ? 18.393  21.602  -41.460 1.00 38.81  ?  1   MET B CA    1 
ATOM   2277 C  C     . MET B 1 1   ? 18.651  20.156  -40.992 1.00 38.53  ?  1   MET B C     1 
ATOM   2278 O  O     . MET B 1 1   ? 18.186  19.212  -41.634 1.00 34.31  ?  1   MET B O     1 
ATOM   2279 C  CB    . MET B 1 1   ? 19.689  22.211  -41.992 1.00 41.80  ?  1   MET B CB    1 
ATOM   2280 C  CG    . MET B 1 1   ? 19.831  22.035  -43.510 1.00 51.03  ?  1   MET B CG    1 
ATOM   2281 S  SD    . MET B 1 1   ? 18.488  22.893  -44.414 1.00 74.31  ?  1   MET B SD    1 
ATOM   2282 C  CE    . MET B 1 1   ? 17.342  21.546  -44.748 1.00 47.31  ?  1   MET B CE    1 
ATOM   2283 N  N     . LEU B 1 2   ? 19.387  19.946  -39.899 1.00 32.90  ?  2   LEU B N     1 
ATOM   2284 C  CA    . LEU B 1 2   ? 19.522  18.566  -39.425 1.00 34.55  ?  2   LEU B CA    1 
ATOM   2285 C  C     . LEU B 1 2   ? 18.331  18.160  -38.550 1.00 34.96  ?  2   LEU B C     1 
ATOM   2286 O  O     . LEU B 1 2   ? 17.767  17.071  -38.723 1.00 35.09  ?  2   LEU B O     1 
ATOM   2287 C  CB    . LEU B 1 2   ? 20.829  18.385  -38.655 1.00 35.75  ?  2   LEU B CB    1 
ATOM   2288 C  CG    . LEU B 1 2   ? 21.090  16.967  -38.108 1.00 39.24  ?  2   LEU B CG    1 
ATOM   2289 C  CD1   . LEU B 1 2   ? 21.142  15.945  -39.220 1.00 33.59  ?  2   LEU B CD1   1 
ATOM   2290 C  CD2   . LEU B 1 2   ? 22.356  16.867  -37.267 1.00 41.10  ?  2   LEU B CD2   1 
ATOM   2291 N  N     . VAL B 1 3   ? 17.937  19.023  -37.602 1.00 30.15  ?  3   VAL B N     1 
ATOM   2292 C  CA    . VAL B 1 3   ? 16.815  18.774  -36.705 1.00 34.48  ?  3   VAL B CA    1 
ATOM   2293 C  C     . VAL B 1 3   ? 15.865  19.970  -36.696 1.00 31.47  ?  3   VAL B C     1 
ATOM   2294 O  O     . VAL B 1 3   ? 16.295  21.129  -36.734 1.00 29.78  ?  3   VAL B O     1 
ATOM   2295 C  CB    . VAL B 1 3   ? 17.275  18.480  -35.265 1.00 30.70  ?  3   VAL B CB    1 
ATOM   2296 C  CG1   . VAL B 1 3   ? 16.115  17.920  -34.493 1.00 30.18  ?  3   VAL B CG1   1 
ATOM   2297 C  CG2   . VAL B 1 3   ? 18.400  17.511  -35.249 1.00 35.80  ?  3   VAL B CG2   1 
ATOM   2298 N  N     . SER B 1 4   ? 14.577  19.671  -36.618 1.00 24.61  ?  4   SER B N     1 
ATOM   2299 C  CA    . SER B 1 4   ? 13.515  20.629  -36.378 1.00 30.89  ?  4   SER B CA    1 
ATOM   2300 C  C     . SER B 1 4   ? 12.871  20.223  -35.073 1.00 31.97  ?  4   SER B C     1 
ATOM   2301 O  O     . SER B 1 4   ? 12.460  19.068  -34.921 1.00 29.83  ?  4   SER B O     1 
ATOM   2302 C  CB    . SER B 1 4   ? 12.477  20.638  -37.510 1.00 32.25  ?  4   SER B CB    1 
ATOM   2303 O  OG    . SER B 1 4   ? 13.110  20.698  -38.797 1.00 33.11  ?  4   SER B OG    1 
ATOM   2304 N  N     . VAL B 1 5   ? 12.875  21.137  -34.111 1.00 31.01  ?  5   VAL B N     1 
ATOM   2305 C  CA    . VAL B 1 5   ? 12.113  20.980  -32.887 1.00 31.30  ?  5   VAL B CA    1 
ATOM   2306 C  C     . VAL B 1 5   ? 10.752  21.586  -33.139 1.00 34.84  ?  5   VAL B C     1 
ATOM   2307 O  O     . VAL B 1 5   ? 10.653  22.713  -33.658 1.00 33.23  ?  5   VAL B O     1 
ATOM   2308 C  CB    . VAL B 1 5   ? 12.806  21.650  -31.687 1.00 32.63  ?  5   VAL B CB    1 
ATOM   2309 C  CG1   . VAL B 1 5   ? 12.038  21.308  -30.411 1.00 29.15  ?  5   VAL B CG1   1 
ATOM   2310 C  CG2   . VAL B 1 5   ? 14.240  21.147  -31.549 1.00 30.83  ?  5   VAL B CG2   1 
ATOM   2311 N  N     . ILE B 1 6   ? 9.706   20.821  -32.824 1.00 30.19  ?  6   ILE B N     1 
ATOM   2312 C  CA    . ILE B 1 6   ? 8.334   21.257  -33.012 1.00 33.76  ?  6   ILE B CA    1 
ATOM   2313 C  C     . ILE B 1 6   ? 7.675   21.376  -31.641 1.00 32.89  ?  6   ILE B C     1 
ATOM   2314 O  O     . ILE B 1 6   ? 7.563   20.387  -30.895 1.00 32.12  ?  6   ILE B O     1 
ATOM   2315 C  CB    . ILE B 1 6   ? 7.555   20.321  -33.951 1.00 38.46  ?  6   ILE B CB    1 
ATOM   2316 C  CG1   . ILE B 1 6   ? 8.226   20.339  -35.321 1.00 32.32  ?  6   ILE B CG1   1 
ATOM   2317 C  CG2   . ILE B 1 6   ? 6.055   20.762  -34.065 1.00 30.19  ?  6   ILE B CG2   1 
ATOM   2318 C  CD1   . ILE B 1 6   ? 7.459   19.631  -36.400 1.00 34.58  ?  6   ILE B CD1   1 
ATOM   2319 N  N     . ILE B 1 7   ? 7.288   22.602  -31.310 1.00 29.56  ?  7   ILE B N     1 
ATOM   2320 C  CA    . ILE B 1 7   ? 6.679   22.951  -30.039 1.00 33.08  ?  7   ILE B CA    1 
ATOM   2321 C  C     . ILE B 1 7   ? 5.301   23.524  -30.329 1.00 37.59  ?  7   ILE B C     1 
ATOM   2322 O  O     . ILE B 1 7   ? 5.168   24.696  -30.701 1.00 37.13  ?  7   ILE B O     1 
ATOM   2323 C  CB    . ILE B 1 7   ? 7.538   23.960  -29.257 1.00 35.14  ?  7   ILE B CB    1 
ATOM   2324 C  CG1   . ILE B 1 7   ? 8.999   23.503  -29.181 1.00 28.45  ?  7   ILE B CG1   1 
ATOM   2325 C  CG2   . ILE B 1 7   ? 6.960   24.177  -27.854 1.00 27.21  ?  7   ILE B CG2   1 
ATOM   2326 C  CD1   . ILE B 1 7   ? 9.905   24.445  -28.349 1.00 27.21  ?  7   ILE B CD1   1 
ATOM   2327 N  N     . PRO B 1 8   ? 4.244   22.714  -30.190 1.00 35.28  ?  8   PRO B N     1 
ATOM   2328 C  CA    . PRO B 1 8   ? 2.892   23.282  -30.129 1.00 30.27  ?  8   PRO B CA    1 
ATOM   2329 C  C     . PRO B 1 8   ? 2.712   24.038  -28.820 1.00 33.21  ?  8   PRO B C     1 
ATOM   2330 O  O     . PRO B 1 8   ? 3.155   23.584  -27.761 1.00 32.63  ?  8   PRO B O     1 
ATOM   2331 C  CB    . PRO B 1 8   ? 1.996   22.047  -30.184 1.00 30.84  ?  8   PRO B CB    1 
ATOM   2332 C  CG    . PRO B 1 8   ? 2.803   21.000  -29.410 1.00 28.52  ?  8   PRO B CG    1 
ATOM   2333 C  CD    . PRO B 1 8   ? 4.263   21.279  -29.832 1.00 31.63  ?  8   PRO B CD    1 
ATOM   2334 N  N     . THR B 1 9   ? 2.044   25.195  -28.882 1.00 34.22  ?  9   THR B N     1 
ATOM   2335 C  CA    . THR B 1 9   ? 1.891   25.979  -27.665 1.00 32.88  ?  9   THR B CA    1 
ATOM   2336 C  C     . THR B 1 9   ? 0.489   26.582  -27.540 1.00 34.81  ?  9   THR B C     1 
ATOM   2337 O  O     . THR B 1 9   ? -0.106  27.037  -28.528 1.00 33.69  ?  9   THR B O     1 
ATOM   2338 C  CB    . THR B 1 9   ? 2.994   27.048  -27.599 1.00 30.32  ?  9   THR B CB    1 
ATOM   2339 O  OG1   . THR B 1 9   ? 3.075   27.569  -26.270 1.00 34.84  ?  9   THR B OG1   1 
ATOM   2340 C  CG2   . THR B 1 9   ? 2.749   28.170  -28.597 1.00 29.28  ?  9   THR B CG2   1 
ATOM   2341 N  N     . TYR B 1 10  ? -0.034  26.588  -26.304 1.00 31.13  ?  10  TYR B N     1 
ATOM   2342 C  CA    . TYR B 1 10  ? -1.429  26.973  -26.056 1.00 33.17  ?  10  TYR B CA    1 
ATOM   2343 C  C     . TYR B 1 10  ? -1.584  27.526  -24.633 1.00 31.95  ?  10  TYR B C     1 
ATOM   2344 O  O     . TYR B 1 10  ? -1.690  26.753  -23.678 1.00 34.58  ?  10  TYR B O     1 
ATOM   2345 C  CB    . TYR B 1 10  ? -2.361  25.787  -26.284 1.00 30.62  ?  10  TYR B CB    1 
ATOM   2346 C  CG    . TYR B 1 10  ? -3.809  26.193  -26.284 1.00 31.35  ?  10  TYR B CG    1 
ATOM   2347 C  CD1   . TYR B 1 10  ? -4.271  27.193  -27.131 1.00 33.57  ?  10  TYR B CD1   1 
ATOM   2348 C  CD2   . TYR B 1 10  ? -4.714  25.566  -25.451 1.00 34.47  ?  10  TYR B CD2   1 
ATOM   2349 C  CE1   . TYR B 1 10  ? -5.604  27.560  -27.130 1.00 33.47  ?  10  TYR B CE1   1 
ATOM   2350 C  CE2   . TYR B 1 10  ? -6.029  25.928  -25.439 1.00 33.94  ?  10  TYR B CE2   1 
ATOM   2351 C  CZ    . TYR B 1 10  ? -6.467  26.917  -26.273 1.00 34.18  ?  10  TYR B CZ    1 
ATOM   2352 O  OH    . TYR B 1 10  ? -7.792  27.250  -26.222 1.00 46.41  ?  10  TYR B OH    1 
ATOM   2353 N  N     . ASN B 1 11  ? -1.658  28.852  -24.514 1.00 28.14  ?  11  ASN B N     1 
ATOM   2354 C  CA    . ASN B 1 11  ? -1.948  29.552  -23.259 1.00 32.20  ?  11  ASN B CA    1 
ATOM   2355 C  C     . ASN B 1 11  ? -0.946  29.238  -22.155 1.00 32.60  ?  11  ASN B C     1 
ATOM   2356 O  O     . ASN B 1 11  ? -1.292  29.290  -20.967 1.00 32.09  ?  11  ASN B O     1 
ATOM   2357 C  CB    . ASN B 1 11  ? -3.385  29.261  -22.772 1.00 29.47  ?  11  ASN B CB    1 
ATOM   2358 C  CG    . ASN B 1 11  ? -4.414  29.992  -23.601 1.00 35.19  ?  11  ASN B CG    1 
ATOM   2359 O  OD1   . ASN B 1 11  ? -4.220  31.179  -23.942 1.00 36.57  ?  11  ASN B OD1   1 
ATOM   2360 N  ND2   . ASN B 1 11  ? -5.479  29.288  -23.995 1.00 34.10  ?  11  ASN B ND2   1 
ATOM   2361 N  N     . ARG B 1 12  ? 0.297   28.919  -22.508 1.00 29.12  ?  12  ARG B N     1 
ATOM   2362 C  CA    . ARG B 1 12  ? 1.360   28.732  -21.513 1.00 29.86  ?  12  ARG B CA    1 
ATOM   2363 C  C     . ARG B 1 12  ? 2.596   29.529  -21.912 1.00 35.73  ?  12  ARG B C     1 
ATOM   2364 O  O     . ARG B 1 12  ? 3.687   28.970  -22.088 1.00 36.62  ?  12  ARG B O     1 
ATOM   2365 C  CB    . ARG B 1 12  ? 1.707   27.247  -21.351 1.00 35.43  ?  12  ARG B CB    1 
ATOM   2366 C  CG    . ARG B 1 12  ? 0.539   26.306  -20.998 1.00 30.63  ?  12  ARG B CG    1 
ATOM   2367 C  CD    . ARG B 1 12  ? 1.073   24.942  -20.607 1.00 35.69  ?  12  ARG B CD    1 
ATOM   2368 N  NE    . ARG B 1 12  ? 0.044   23.942  -20.324 1.00 31.78  ?  12  ARG B NE    1 
ATOM   2369 C  CZ    . ARG B 1 12  ? -0.016  22.747  -20.901 1.00 32.45  ?  12  ARG B CZ    1 
ATOM   2370 N  NH1   . ARG B 1 12  ? 0.888   22.357  -21.797 1.00 34.02  ?  12  ARG B NH1   1 
ATOM   2371 N  NH2   . ARG B 1 12  ? -1.014  21.924  -20.589 1.00 34.35  ?  12  ARG B NH2   1 
ATOM   2372 N  N     . PRO B 1 13  ? 2.475   30.855  -22.045 1.00 41.29  ?  13  PRO B N     1 
ATOM   2373 C  CA    . PRO B 1 13  ? 3.650   31.621  -22.485 1.00 31.97  ?  13  PRO B CA    1 
ATOM   2374 C  C     . PRO B 1 13  ? 4.810   31.515  -21.525 1.00 33.53  ?  13  PRO B C     1 
ATOM   2375 O  O     . PRO B 1 13  ? 5.958   31.652  -21.957 1.00 33.68  ?  13  PRO B O     1 
ATOM   2376 C  CB    . PRO B 1 13  ? 3.127   33.063  -22.568 1.00 38.22  ?  13  PRO B CB    1 
ATOM   2377 C  CG    . PRO B 1 13  ? 1.975   33.099  -21.614 1.00 27.87  ?  13  PRO B CG    1 
ATOM   2378 C  CD    . PRO B 1 13  ? 1.343   31.742  -21.683 1.00 31.27  ?  13  PRO B CD    1 
ATOM   2379 N  N     . GLU B 1 14  ? 4.571   31.289  -20.231 1.00 32.19  ?  14  GLU B N     1 
ATOM   2380 C  CA    . GLU B 1 14  ? 5.735   31.287  -19.350 1.00 35.39  ?  14  GLU B CA    1 
ATOM   2381 C  C     . GLU B 1 14  ? 6.390   29.913  -19.330 1.00 37.44  ?  14  GLU B C     1 
ATOM   2382 O  O     . GLU B 1 14  ? 7.619   29.832  -19.217 1.00 38.80  ?  14  GLU B O     1 
ATOM   2383 C  CB    . GLU B 1 14  ? 5.381   31.775  -17.933 1.00 34.99  ?  14  GLU B CB    1 
ATOM   2384 C  CG    . GLU B 1 14  ? 4.198   32.823  -17.886 1.00 42.47  ?  14  GLU B CG    1 
ATOM   2385 C  CD    . GLU B 1 14  ? 4.216   33.807  -16.694 1.00 45.94  ?  14  GLU B CD    1 
ATOM   2386 O  OE1   . GLU B 1 14  ? 5.277   33.989  -16.060 1.00 56.80  ?  14  GLU B OE1   1 
ATOM   2387 O  OE2   . GLU B 1 14  ? 3.155   34.421  -16.398 1.00 51.08  ?  14  GLU B OE2   1 
ATOM   2388 N  N     . ARG B 1 15  ? 5.615   28.830  -19.507 1.00 33.65  ?  15  ARG B N     1 
ATOM   2389 C  CA    . ARG B 1 15  ? 6.267   27.530  -19.657 1.00 37.58  ?  15  ARG B CA    1 
ATOM   2390 C  C     . ARG B 1 15  ? 6.975   27.413  -21.002 1.00 36.15  ?  15  ARG B C     1 
ATOM   2391 O  O     . ARG B 1 15  ? 8.031   26.784  -21.080 1.00 32.94  ?  15  ARG B O     1 
ATOM   2392 C  CB    . ARG B 1 15  ? 5.262   26.389  -19.479 1.00 37.64  ?  15  ARG B CB    1 
ATOM   2393 C  CG    . ARG B 1 15  ? 4.400   26.535  -18.242 1.00 38.63  ?  15  ARG B CG    1 
ATOM   2394 C  CD    . ARG B 1 15  ? 5.186   26.364  -16.952 1.00 40.42  ?  15  ARG B CD    1 
ATOM   2395 N  NE    . ARG B 1 15  ? 4.402   26.906  -15.840 1.00 57.99  ?  15  ARG B NE    1 
ATOM   2396 C  CZ    . ARG B 1 15  ? 3.662   26.192  -14.986 1.00 61.95  ?  15  ARG B CZ    1 
ATOM   2397 N  NH1   . ARG B 1 15  ? 3.681   24.858  -14.980 1.00 60.29  ?  15  ARG B NH1   1 
ATOM   2398 N  NH2   . ARG B 1 15  ? 2.869   26.831  -14.125 1.00 51.12  ?  15  ARG B NH2   1 
ATOM   2399 N  N     . LEU B 1 16  ? 6.415   28.028  -22.056 1.00 35.75  ?  16  LEU B N     1 
ATOM   2400 C  CA    . LEU B 1 16  ? 7.057   28.038  -23.363 1.00 33.55  ?  16  LEU B CA    1 
ATOM   2401 C  C     . LEU B 1 16  ? 8.462   28.659  -23.305 1.00 37.64  ?  16  LEU B C     1 
ATOM   2402 O  O     . LEU B 1 16  ? 9.393   28.195  -23.982 1.00 34.59  ?  16  LEU B O     1 
ATOM   2403 C  CB    . LEU B 1 16  ? 6.188   28.801  -24.359 1.00 31.62  ?  16  LEU B CB    1 
ATOM   2404 C  CG    . LEU B 1 16  ? 6.952   29.191  -25.634 1.00 28.62  ?  16  LEU B CG    1 
ATOM   2405 C  CD1   . LEU B 1 16  ? 7.289   27.926  -26.413 1.00 33.42  ?  16  LEU B CD1   1 
ATOM   2406 C  CD2   . LEU B 1 16  ? 6.108   30.057  -26.468 1.00 28.45  ?  16  LEU B CD2   1 
ATOM   2407 N  N     . ALA B 1 17  ? 8.633   29.711  -22.508 1.00 37.76  ?  17  ALA B N     1 
ATOM   2408 C  CA    . ALA B 1 17  ? 9.952   30.319  -22.409 1.00 38.30  ?  17  ALA B CA    1 
ATOM   2409 C  C     . ALA B 1 17  ? 10.954  29.349  -21.806 1.00 39.99  ?  17  ALA B C     1 
ATOM   2410 O  O     . ALA B 1 17  ? 12.136  29.362  -22.189 1.00 38.14  ?  17  ALA B O     1 
ATOM   2411 C  CB    . ALA B 1 17  ? 9.879   31.609  -21.595 1.00 36.43  ?  17  ALA B CB    1 
ATOM   2412 N  N     . VAL B 1 18  ? 10.493  28.480  -20.895 1.00 36.88  ?  18  VAL B N     1 
ATOM   2413 C  CA    . VAL B 1 18  ? 11.367  27.479  -20.293 1.00 38.00  ?  18  VAL B CA    1 
ATOM   2414 C  C     . VAL B 1 18  ? 11.699  26.391  -21.301 1.00 41.97  ?  18  VAL B C     1 
ATOM   2415 O  O     . VAL B 1 18  ? 12.840  25.905  -21.362 1.00 42.30  ?  18  VAL B O     1 
ATOM   2416 C  CB    . VAL B 1 18  ? 10.719  26.889  -19.025 1.00 37.34  ?  18  VAL B CB    1 
ATOM   2417 C  CG1   . VAL B 1 18  ? 11.602  25.784  -18.429 1.00 32.46  ?  18  VAL B CG1   1 
ATOM   2418 C  CG2   . VAL B 1 18  ? 10.516  27.966  -18.011 1.00 31.67  ?  18  VAL B CG2   1 
ATOM   2419 N  N     . ALA B 1 19  ? 10.713  25.981  -22.105 1.00 41.20  ?  19  ALA B N     1 
ATOM   2420 C  CA    . ALA B 1 19  ? 10.975  24.941  -23.097 1.00 40.41  ?  19  ALA B CA    1 
ATOM   2421 C  C     . ALA B 1 19  ? 11.985  25.432  -24.131 1.00 39.22  ?  19  ALA B C     1 
ATOM   2422 O  O     . ALA B 1 19  ? 12.899  24.697  -24.535 1.00 37.00  ?  19  ALA B O     1 
ATOM   2423 C  CB    . ALA B 1 19  ? 9.665   24.522  -23.762 1.00 33.21  ?  19  ALA B CB    1 
ATOM   2424 N  N     . LEU B 1 20  ? 11.832  26.683  -24.556 1.00 37.95  ?  20  LEU B N     1 
ATOM   2425 C  CA    . LEU B 1 20  ? 12.769  27.299  -25.481 1.00 35.57  ?  20  LEU B CA    1 
ATOM   2426 C  C     . LEU B 1 20  ? 14.173  27.362  -24.904 1.00 39.82  ?  20  LEU B C     1 
ATOM   2427 O  O     . LEU B 1 20  ? 15.158  27.166  -25.631 1.00 38.74  ?  20  LEU B O     1 
ATOM   2428 C  CB    . LEU B 1 20  ? 12.282  28.703  -25.813 1.00 37.90  ?  20  LEU B CB    1 
ATOM   2429 C  CG    . LEU B 1 20  ? 11.120  28.697  -26.779 1.00 36.35  ?  20  LEU B CG    1 
ATOM   2430 C  CD1   . LEU B 1 20  ? 10.764  30.122  -27.118 1.00 35.02  ?  20  LEU B CD1   1 
ATOM   2431 C  CD2   . LEU B 1 20  ? 11.477  27.877  -28.008 1.00 33.44  ?  20  LEU B CD2   1 
ATOM   2432 N  N     . GLN B 1 21  ? 14.293  27.691  -23.612 1.00 39.89  ?  21  GLN B N     1 
ATOM   2433 C  CA    . GLN B 1 21  ? 15.625  27.778  -23.033 1.00 41.36  ?  21  GLN B CA    1 
ATOM   2434 C  C     . GLN B 1 21  ? 16.290  26.412  -22.990 1.00 44.41  ?  21  GLN B C     1 
ATOM   2435 O  O     . GLN B 1 21  ? 17.480  26.296  -23.295 1.00 46.50  ?  21  GLN B O     1 
ATOM   2436 C  CB    . GLN B 1 21  ? 15.592  28.398  -21.642 1.00 41.93  ?  21  GLN B CB    1 
ATOM   2437 C  CG    . GLN B 1 21  ? 16.998  28.651  -21.048 1.00 50.64  ?  21  GLN B CG    1 
ATOM   2438 C  CD    . GLN B 1 21  ? 17.907  29.609  -21.899 1.00 62.91  ?  21  GLN B CD    1 
ATOM   2439 O  OE1   . GLN B 1 21  ? 19.063  29.883  -21.529 1.00 57.08  ?  21  GLN B OE1   1 
ATOM   2440 N  NE2   . GLN B 1 21  ? 17.355  30.167  -22.988 1.00 57.49  ?  21  GLN B NE2   1 
ATOM   2441 N  N     . SER B 1 22  ? 15.534  25.360  -22.648 1.00 41.71  ?  22  SER B N     1 
ATOM   2442 C  CA    . SER B 1 22  ? 16.083  24.011  -22.689 1.00 37.19  ?  22  SER B CA    1 
ATOM   2443 C  C     . SER B 1 22  ? 16.505  23.619  -24.103 1.00 38.82  ?  22  SER B C     1 
ATOM   2444 O  O     . SER B 1 22  ? 17.375  22.761  -24.267 1.00 36.14  ?  22  SER B O     1 
ATOM   2445 C  CB    . SER B 1 22  ? 15.069  23.002  -22.150 1.00 36.91  ?  22  SER B CB    1 
ATOM   2446 O  OG    . SER B 1 22  ? 14.197  22.544  -23.176 1.00 32.50  ?  22  SER B OG    1 
ATOM   2447 N  N     . VAL B 1 23  ? 15.877  24.194  -25.130 1.00 37.46  ?  23  VAL B N     1 
ATOM   2448 C  CA    . VAL B 1 23  ? 16.403  24.042  -26.480 1.00 36.73  ?  23  VAL B CA    1 
ATOM   2449 C  C     . VAL B 1 23  ? 17.693  24.839  -26.631 1.00 40.44  ?  23  VAL B C     1 
ATOM   2450 O  O     . VAL B 1 23  ? 18.665  24.374  -27.244 1.00 38.34  ?  23  VAL B O     1 
ATOM   2451 C  CB    . VAL B 1 23  ? 15.371  24.489  -27.524 1.00 36.78  ?  23  VAL B CB    1 
ATOM   2452 C  CG1   . VAL B 1 23  ? 16.020  24.511  -28.932 1.00 32.60  ?  23  VAL B CG1   1 
ATOM   2453 C  CG2   . VAL B 1 23  ? 14.158  23.611  -27.472 1.00 32.58  ?  23  VAL B CG2   1 
ATOM   2454 N  N     . GLN B 1 24  ? 17.717  26.060  -26.094 1.00 38.27  ?  24  GLN B N     1 
ATOM   2455 C  CA    . GLN B 1 24  ? 18.908  26.884  -26.215 1.00 38.86  ?  24  GLN B CA    1 
ATOM   2456 C  C     . GLN B 1 24  ? 20.065  26.320  -25.403 1.00 42.34  ?  24  GLN B C     1 
ATOM   2457 O  O     . GLN B 1 24  ? 21.223  26.511  -25.781 1.00 44.35  ?  24  GLN B O     1 
ATOM   2458 C  CB    . GLN B 1 24  ? 18.587  28.325  -25.812 1.00 49.22  ?  24  GLN B CB    1 
ATOM   2459 C  CG    . GLN B 1 24  ? 19.795  29.253  -25.646 1.00 53.39  ?  24  GLN B CG    1 
ATOM   2460 C  CD    . GLN B 1 24  ? 19.405  30.571  -24.964 1.00 63.83  ?  24  GLN B CD    1 
ATOM   2461 O  OE1   . GLN B 1 24  ? 20.053  31.012  -23.996 1.00 56.59  ?  24  GLN B OE1   1 
ATOM   2462 N  NE2   . GLN B 1 24  ? 18.331  31.205  -25.470 1.00 61.54  ?  24  GLN B NE2   1 
ATOM   2463 N  N     . THR B 1 25  ? 19.792  25.605  -24.307 1.00 40.05  ?  25  THR B N     1 
ATOM   2464 C  CA    . THR B 1 25  ? 20.861  24.990  -23.529 1.00 39.34  ?  25  THR B CA    1 
ATOM   2465 C  C     . THR B 1 25  ? 21.147  23.561  -23.983 1.00 45.42  ?  25  THR B C     1 
ATOM   2466 O  O     . THR B 1 25  ? 21.760  22.791  -23.230 1.00 43.71  ?  25  THR B O     1 
ATOM   2467 C  CB    . THR B 1 25  ? 20.540  25.026  -22.022 1.00 45.33  ?  25  THR B CB    1 
ATOM   2468 O  OG1   . THR B 1 25  ? 19.365  24.259  -21.739 1.00 45.04  ?  25  THR B OG1   1 
ATOM   2469 C  CG2   . THR B 1 25  ? 20.332  26.486  -21.517 1.00 41.55  ?  25  THR B CG2   1 
ATOM   2470 N  N     . LEU B 1 26  ? 20.715  23.193  -25.197 1.00 40.74  ?  26  LEU B N     1 
ATOM   2471 C  CA    . LEU B 1 26  ? 21.069  21.893  -25.750 1.00 42.54  ?  26  LEU B CA    1 
ATOM   2472 C  C     . LEU B 1 26  ? 22.570  21.822  -25.939 1.00 45.97  ?  26  LEU B C     1 
ATOM   2473 O  O     . LEU B 1 26  ? 23.197  22.768  -26.421 1.00 46.49  ?  26  LEU B O     1 
ATOM   2474 C  CB    . LEU B 1 26  ? 20.387  21.652  -27.098 1.00 36.33  ?  26  LEU B CB    1 
ATOM   2475 C  CG    . LEU B 1 26  ? 18.962  21.117  -27.078 1.00 37.26  ?  26  LEU B CG    1 
ATOM   2476 C  CD1   . LEU B 1 26  ? 18.482  20.812  -28.499 1.00 34.05  ?  26  LEU B CD1   1 
ATOM   2477 C  CD2   . LEU B 1 26  ? 18.927  19.921  -26.199 1.00 38.66  ?  26  LEU B CD2   1 
ATOM   2478 N  N     . ASP B 1 27  ? 23.166  20.690  -25.536 1.00 47.22  ?  27  ASP B N     1 
ATOM   2479 C  CA    . ASP B 1 27  ? 24.609  20.413  -25.797 1.00 42.95  ?  27  ASP B CA    1 
ATOM   2480 C  C     . ASP B 1 27  ? 24.616  19.888  -27.235 1.00 46.02  ?  27  ASP B C     1 
ATOM   2481 O  O     . ASP B 1 27  ? 24.585  18.651  -27.414 1.00 43.64  ?  27  ASP B O     1 
ATOM   2482 C  CB    . ASP B 1 27  ? 25.179  19.404  -24.797 1.00 44.34  ?  27  ASP B CB    1 
ATOM   2483 C  CG    . ASP B 1 27  ? 26.674  19.181  -24.951 1.00 55.35  ?  27  ASP B CG    1 
ATOM   2484 O  OD1   . ASP B 1 27  ? 27.265  19.789  -25.865 1.00 53.27  ?  27  ASP B OD1   1 
ATOM   2485 O  OD2   . ASP B 1 27  ? 27.234  18.402  -24.155 1.00 63.03  ?  27  ASP B OD2   1 
ATOM   2486 N  N     . PHE B 1 28  ? 24.715  20.813  -28.196 1.00 47.02  ?  28  PHE B N     1 
ATOM   2487 C  CA    . PHE B 1 28  ? 24.432  20.545  -29.601 1.00 44.08  ?  28  PHE B CA    1 
ATOM   2488 C  C     . PHE B 1 28  ? 24.726  21.797  -30.423 1.00 48.37  ?  28  PHE B C     1 
ATOM   2489 O  O     . PHE B 1 28  ? 24.618  22.920  -29.916 1.00 52.69  ?  28  PHE B O     1 
ATOM   2490 C  CB    . PHE B 1 28  ? 22.973  20.117  -29.771 1.00 43.16  ?  28  PHE B CB    1 
ATOM   2491 C  CG    . PHE B 1 28  ? 22.585  19.847  -31.172 1.00 37.97  ?  28  PHE B CG    1 
ATOM   2492 C  CD1   . PHE B 1 28  ? 22.733  18.584  -31.701 1.00 35.08  ?  28  PHE B CD1   1 
ATOM   2493 C  CD2   . PHE B 1 28  ? 22.050  20.855  -31.956 1.00 46.07  ?  28  PHE B CD2   1 
ATOM   2494 C  CE1   . PHE B 1 28  ? 22.377  18.330  -32.984 1.00 38.56  ?  28  PHE B CE1   1 
ATOM   2495 C  CE2   . PHE B 1 28  ? 21.688  20.608  -33.257 1.00 44.48  ?  28  PHE B CE2   1 
ATOM   2496 C  CZ    . PHE B 1 28  ? 21.856  19.342  -33.771 1.00 39.95  ?  28  PHE B CZ    1 
ATOM   2497 N  N     . ASP B 1 29  ? 25.082  21.593  -31.698 1.00 47.65  ?  29  ASP B N     1 
ATOM   2498 C  CA    . ASP B 1 29  ? 25.500  22.683  -32.591 1.00 54.33  ?  29  ASP B CA    1 
ATOM   2499 C  C     . ASP B 1 29  ? 24.270  23.359  -33.171 1.00 55.29  ?  29  ASP B C     1 
ATOM   2500 O  O     . ASP B 1 29  ? 23.689  22.885  -34.151 1.00 51.76  ?  29  ASP B O     1 
ATOM   2501 C  CB    . ASP B 1 29  ? 26.410  22.171  -33.705 1.00 60.19  ?  29  ASP B CB    1 
ATOM   2502 C  CG    . ASP B 1 29  ? 26.995  23.300  -34.573 1.00 65.89  ?  29  ASP B CG    1 
ATOM   2503 O  OD1   . ASP B 1 29  ? 28.010  23.032  -35.254 1.00 75.77  ?  29  ASP B OD1   1 
ATOM   2504 O  OD2   . ASP B 1 29  ? 26.454  24.432  -34.609 1.00 63.98  ?  29  ASP B OD2   1 
ATOM   2505 N  N     . SER B 1 30  ? 23.925  24.517  -32.601 1.00 53.42  ?  30  SER B N     1 
ATOM   2506 C  CA    . SER B 1 30  ? 22.664  25.175  -32.903 1.00 55.19  ?  30  SER B CA    1 
ATOM   2507 C  C     . SER B 1 30  ? 22.571  25.629  -34.356 1.00 53.34  ?  30  SER B C     1 
ATOM   2508 O  O     . SER B 1 30  ? 21.481  26.011  -34.793 1.00 57.35  ?  30  SER B O     1 
ATOM   2509 C  CB    . SER B 1 30  ? 22.444  26.349  -31.917 1.00 59.58  ?  30  SER B CB    1 
ATOM   2510 O  OG    . SER B 1 30  ? 23.414  27.389  -32.032 1.00 59.48  ?  30  SER B OG    1 
ATOM   2511 N  N     . GLU B 1 31  ? 23.651  25.548  -35.131 1.00 54.64  ?  31  GLU B N     1 
ATOM   2512 C  CA    . GLU B 1 31  ? 23.580  26.010  -36.515 1.00 57.38  ?  31  GLU B CA    1 
ATOM   2513 C  C     . GLU B 1 31  ? 22.776  25.074  -37.413 1.00 52.35  ?  31  GLU B C     1 
ATOM   2514 O  O     . GLU B 1 31  ? 22.307  25.500  -38.474 1.00 48.29  ?  31  GLU B O     1 
ATOM   2515 C  CB    . GLU B 1 31  ? 24.983  26.179  -37.081 1.00 59.69  ?  31  GLU B CB    1 
ATOM   2516 C  CG    . GLU B 1 31  ? 25.497  27.596  -37.008 1.00 70.47  ?  31  GLU B CG    1 
ATOM   2517 C  CD    . GLU B 1 31  ? 27.010  27.645  -36.964 1.00 84.48  ?  31  GLU B CD    1 
ATOM   2518 O  OE1   . GLU B 1 31  ? 27.629  27.987  -38.000 1.00 87.97  ?  31  GLU B OE1   1 
ATOM   2519 O  OE2   . GLU B 1 31  ? 27.578  27.311  -35.897 1.00 89.28  ?  31  GLU B OE2   1 
ATOM   2520 N  N     . GLN B 1 32  ? 22.685  23.802  -37.019 1.00 46.73  ?  32  GLN B N     1 
ATOM   2521 C  CA    . GLN B 1 32  ? 21.908  22.799  -37.793 1.00 46.69  ?  32  GLN B CA    1 
ATOM   2522 C  C     . GLN B 1 32  ? 20.665  22.452  -36.972 1.00 42.43  ?  32  GLN B C     1 
ATOM   2523 O  O     . GLN B 1 32  ? 20.389  21.250  -36.787 1.00 30.28  ?  32  GLN B O     1 
ATOM   2524 C  CB    . GLN B 1 32  ? 22.757  21.556  -38.064 1.00 40.92  ?  32  GLN B CB    1 
ATOM   2525 C  CG    . GLN B 1 32  ? 23.940  21.407  -37.118 1.00 48.28  ?  32  GLN B CG    1 
ATOM   2526 C  CD    . GLN B 1 32  ? 24.731  20.150  -37.387 1.00 58.61  ?  32  GLN B CD    1 
ATOM   2527 O  OE1   . GLN B 1 32  ? 24.720  19.611  -38.492 1.00 58.86  ?  32  GLN B OE1   1 
ATOM   2528 N  NE2   . GLN B 1 32  ? 25.429  19.671  -36.370 1.00 59.86  ?  32  GLN B NE2   1 
ATOM   2529 N  N     . LEU B 1 33  ? 19.951  23.480  -36.502 1.00 43.74  ?  33  LEU B N     1 
ATOM   2530 C  CA    . LEU B 1 33  ? 18.781  23.263  -35.663 1.00 41.65  ?  33  LEU B CA    1 
ATOM   2531 C  C     . LEU B 1 33  ? 17.814  24.415  -35.879 1.00 38.40  ?  33  LEU B C     1 
ATOM   2532 O  O     . LEU B 1 33  ? 18.211  25.586  -35.850 1.00 38.11  ?  33  LEU B O     1 
ATOM   2533 C  CB    . LEU B 1 33  ? 19.202  23.129  -34.197 1.00 42.43  ?  33  LEU B CB    1 
ATOM   2534 C  CG    . LEU B 1 33  ? 18.258  23.132  -32.998 1.00 41.87  ?  33  LEU B CG    1 
ATOM   2535 C  CD1   . LEU B 1 33  ? 18.986  22.557  -31.801 1.00 41.19  ?  33  LEU B CD1   1 
ATOM   2536 C  CD2   . LEU B 1 33  ? 17.795  24.548  -32.655 1.00 32.95  ?  33  LEU B CD2   1 
ATOM   2537 N  N     . GLU B 1 34  ? 16.561  24.074  -36.149 1.00 36.25  ?  34  GLU B N     1 
ATOM   2538 C  CA    . GLU B 1 34  ? 15.487  25.045  -36.279 1.00 37.82  ?  34  GLU B CA    1 
ATOM   2539 C  C     . GLU B 1 34  ? 14.413  24.671  -35.272 1.00 33.49  ?  34  GLU B C     1 
ATOM   2540 O  O     . GLU B 1 34  ? 14.175  23.492  -35.036 1.00 36.11  ?  34  GLU B O     1 
ATOM   2541 C  CB    . GLU B 1 34  ? 14.925  25.066  -37.707 1.00 34.94  ?  34  GLU B CB    1 
ATOM   2542 C  CG    . GLU B 1 34  ? 13.695  24.191  -37.914 1.00 40.48  ?  34  GLU B CG    1 
ATOM   2543 C  CD    . GLU B 1 34  ? 13.261  24.106  -39.369 1.00 42.21  ?  34  GLU B CD    1 
ATOM   2544 O  OE1   . GLU B 1 34  ? 13.330  25.141  -40.066 1.00 41.20  ?  34  GLU B OE1   1 
ATOM   2545 O  OE2   . GLU B 1 34  ? 12.839  23.003  -39.815 1.00 43.77  ?  34  GLU B OE2   1 
ATOM   2546 N  N     . VAL B 1 35  ? 13.822  25.674  -34.634 1.00 35.53  ?  35  VAL B N     1 
ATOM   2547 C  CA    . VAL B 1 35  ? 12.679  25.516  -33.748 1.00 33.69  ?  35  VAL B CA    1 
ATOM   2548 C  C     . VAL B 1 35  ? 11.452  26.055  -34.468 1.00 36.47  ?  35  VAL B C     1 
ATOM   2549 O  O     . VAL B 1 35  ? 11.508  27.105  -35.119 1.00 37.79  ?  35  VAL B O     1 
ATOM   2550 C  CB    . VAL B 1 35  ? 12.870  26.260  -32.413 1.00 32.93  ?  35  VAL B CB    1 
ATOM   2551 C  CG1   . VAL B 1 35  ? 11.659  26.021  -31.501 1.00 28.36  ?  35  VAL B CG1   1 
ATOM   2552 C  CG2   . VAL B 1 35  ? 14.158  25.847  -31.733 1.00 29.79  ?  35  VAL B CG2   1 
ATOM   2553 N  N     . ILE B 1 36  ? 10.338  25.357  -34.348 1.00 32.66  ?  36  ILE B N     1 
ATOM   2554 C  CA    . ILE B 1 36  ? 9.093   25.872  -34.882 1.00 35.93  ?  36  ILE B CA    1 
ATOM   2555 C  C     . ILE B 1 36  ? 8.080   25.832  -33.761 1.00 35.12  ?  36  ILE B C     1 
ATOM   2556 O  O     . ILE B 1 36  ? 7.725   24.751  -33.277 1.00 36.23  ?  36  ILE B O     1 
ATOM   2557 C  CB    . ILE B 1 36  ? 8.591   25.099  -36.100 1.00 33.50  ?  36  ILE B CB    1 
ATOM   2558 C  CG1   . ILE B 1 36  ? 9.545   25.293  -37.250 1.00 30.98  ?  36  ILE B CG1   1 
ATOM   2559 C  CG2   . ILE B 1 36  ? 7.214   25.586  -36.481 1.00 34.97  ?  36  ILE B CG2   1 
ATOM   2560 C  CD1   . ILE B 1 36  ? 9.700   24.053  -38.099 1.00 38.74  ?  36  ILE B CD1   1 
ATOM   2561 N  N     . VAL B 1 37  ? 7.654   27.011  -33.327 1.00 35.71  ?  37  VAL B N     1 
ATOM   2562 C  CA    . VAL B 1 37  ? 6.628   27.201  -32.317 1.00 35.84  ?  37  VAL B CA    1 
ATOM   2563 C  C     . VAL B 1 37  ? 5.307   27.436  -33.035 1.00 35.47  ?  37  VAL B C     1 
ATOM   2564 O  O     . VAL B 1 37  ? 5.245   28.270  -33.946 1.00 35.32  ?  37  VAL B O     1 
ATOM   2565 C  CB    . VAL B 1 37  ? 6.970   28.397  -31.410 1.00 36.51  ?  37  VAL B CB    1 
ATOM   2566 C  CG1   . VAL B 1 37  ? 5.849   28.605  -30.368 1.00 32.29  ?  37  VAL B CG1   1 
ATOM   2567 C  CG2   . VAL B 1 37  ? 8.351   28.217  -30.757 1.00 28.67  ?  37  VAL B CG2   1 
ATOM   2568 N  N     . VAL B 1 38  ? 4.258   26.715  -32.634 1.00 29.67  ?  38  VAL B N     1 
ATOM   2569 C  CA    . VAL B 1 38  ? 2.946   26.815  -33.271 1.00 33.55  ?  38  VAL B CA    1 
ATOM   2570 C  C     . VAL B 1 38  ? 1.946   27.199  -32.187 1.00 36.67  ?  38  VAL B C     1 
ATOM   2571 O  O     . VAL B 1 38  ? 1.552   26.347  -31.377 1.00 35.64  ?  38  VAL B O     1 
ATOM   2572 C  CB    . VAL B 1 38  ? 2.522   25.509  -33.957 1.00 36.10  ?  38  VAL B CB    1 
ATOM   2573 C  CG1   . VAL B 1 38  ? 1.204   25.699  -34.696 1.00 33.88  ?  38  VAL B CG1   1 
ATOM   2574 C  CG2   . VAL B 1 38  ? 3.591   25.023  -34.906 1.00 36.89  ?  38  VAL B CG2   1 
ATOM   2575 N  N     . ASN B 1 39  ? 1.534   28.473  -32.165 1.00 34.83  ?  39  ASN B N     1 
ATOM   2576 C  CA    . ASN B 1 39  ? 0.520   28.951  -31.231 1.00 29.93  ?  39  ASN B CA    1 
ATOM   2577 C  C     . ASN B 1 39  ? -0.833  28.500  -31.728 1.00 34.49  ?  39  ASN B C     1 
ATOM   2578 O  O     . ASN B 1 39  ? -1.267  28.933  -32.799 1.00 40.51  ?  39  ASN B O     1 
ATOM   2579 C  CB    . ASN B 1 39  ? 0.547   30.464  -31.120 1.00 32.03  ?  39  ASN B CB    1 
ATOM   2580 C  CG    . ASN B 1 39  ? -0.469  31.017  -30.091 1.00 40.63  ?  39  ASN B CG    1 
ATOM   2581 O  OD1   . ASN B 1 39  ? -1.027  30.273  -29.257 1.00 34.43  ?  39  ASN B OD1   1 
ATOM   2582 N  ND2   . ASN B 1 39  ? -0.678  32.349  -30.127 1.00 36.10  ?  39  ASN B ND2   1 
ATOM   2583 N  N     . ASP B 1 40  ? -1.489  27.628  -30.965 1.00 29.89  ?  40  ASP B N     1 
ATOM   2584 C  CA    . ASP B 1 40  ? -2.770  27.058  -31.365 1.00 35.98  ?  40  ASP B CA    1 
ATOM   2585 C  C     . ASP B 1 40  ? -3.938  27.978  -31.051 1.00 35.90  ?  40  ASP B C     1 
ATOM   2586 O  O     . ASP B 1 40  ? -4.959  27.553  -30.513 1.00 33.67  ?  40  ASP B O     1 
ATOM   2587 C  CB    . ASP B 1 40  ? -2.962  25.704  -30.689 1.00 32.65  ?  40  ASP B CB    1 
ATOM   2588 C  CG    . ASP B 1 40  ? -4.049  24.896  -31.346 1.00 36.92  ?  40  ASP B CG    1 
ATOM   2589 O  OD1   . ASP B 1 40  ? -4.198  25.031  -32.582 1.00 40.67  ?  40  ASP B OD1   1 
ATOM   2590 O  OD2   . ASP B 1 40  ? -4.771  24.147  -30.644 1.00 38.64  ?  40  ASP B OD2   1 
ATOM   2591 N  N     . HIS B 1 41  ? -3.767  29.256  -31.338 1.00 35.58  ?  41  HIS B N     1 
ATOM   2592 C  CA    . HIS B 1 41  ? -4.799  30.269  -31.218 1.00 30.23  ?  41  HIS B CA    1 
ATOM   2593 C  C     . HIS B 1 41  ? -5.171  30.530  -29.769 1.00 34.95  ?  41  HIS B C     1 
ATOM   2594 O  O     . HIS B 1 41  ? -6.337  30.709  -29.422 1.00 41.95  ?  41  HIS B O     1 
ATOM   2595 C  CB    . HIS B 1 41  ? -6.019  29.919  -32.036 1.00 36.70  ?  41  HIS B CB    1 
ATOM   2596 C  CG    . HIS B 1 41  ? -6.848  31.106  -32.344 1.00 42.09  ?  41  HIS B CG    1 
ATOM   2597 N  ND1   . HIS B 1 41  ? -6.367  32.158  -33.086 1.00 38.65  ?  41  HIS B ND1   1 
ATOM   2598 C  CD2   . HIS B 1 41  ? -8.093  31.454  -31.945 1.00 34.89  ?  41  HIS B CD2   1 
ATOM   2599 C  CE1   . HIS B 1 41  ? -7.300  33.084  -33.181 1.00 35.49  ?  41  HIS B CE1   1 
ATOM   2600 N  NE2   . HIS B 1 41  ? -8.356  32.681  -32.498 1.00 42.36  ?  41  HIS B NE2   1 
ATOM   2601 N  N     . GLY B 1 42  ? -4.167  30.522  -28.910 1.00 34.57  ?  42  GLY B N     1 
ATOM   2602 C  CA    . GLY B 1 42  ? -4.284  31.001  -27.571 1.00 34.80  ?  42  GLY B CA    1 
ATOM   2603 C  C     . GLY B 1 42  ? -3.556  32.313  -27.425 1.00 32.68  ?  42  GLY B C     1 
ATOM   2604 O  O     . GLY B 1 42  ? -3.199  32.961  -28.414 1.00 32.95  ?  42  GLY B O     1 
ATOM   2605 N  N     . THR B 1 43  ? -3.294  32.682  -26.184 1.00 36.18  ?  43  THR B N     1 
ATOM   2606 C  CA    . THR B 1 43  ? -2.708  33.981  -25.889 1.00 34.76  ?  43  THR B CA    1 
ATOM   2607 C  C     . THR B 1 43  ? -1.445  34.209  -26.723 1.00 34.99  ?  43  THR B C     1 
ATOM   2608 O  O     . THR B 1 43  ? -0.715  33.260  -27.026 1.00 33.42  ?  43  THR B O     1 
ATOM   2609 C  CB    . THR B 1 43  ? -2.417  34.105  -24.388 1.00 34.74  ?  43  THR B CB    1 
ATOM   2610 O  OG1   . THR B 1 43  ? -2.087  35.467  -24.079 1.00 37.78  ?  43  THR B OG1   1 
ATOM   2611 C  CG2   . THR B 1 43  ? -1.251  33.204  -23.972 1.00 34.16  ?  43  THR B CG2   1 
ATOM   2612 N  N     . PRO B 1 44  ? -1.178  35.457  -27.124 1.00 39.68  ?  44  PRO B N     1 
ATOM   2613 C  CA    . PRO B 1 44  ? -0.035  35.736  -28.009 1.00 32.64  ?  44  PRO B CA    1 
ATOM   2614 C  C     . PRO B 1 44  ? 1.307   35.440  -27.353 1.00 36.41  ?  44  PRO B C     1 
ATOM   2615 O  O     . PRO B 1 44  ? 1.512   35.709  -26.176 1.00 39.03  ?  44  PRO B O     1 
ATOM   2616 C  CB    . PRO B 1 44  ? -0.197  37.230  -28.321 1.00 37.32  ?  44  PRO B CB    1 
ATOM   2617 C  CG    . PRO B 1 44  ? -1.718  37.471  -28.125 1.00 37.41  ?  44  PRO B CG    1 
ATOM   2618 C  CD    . PRO B 1 44  ? -2.038  36.646  -26.929 1.00 33.29  ?  44  PRO B CD    1 
ATOM   2619 N  N     . VAL B 1 45  ? 2.228   34.856  -28.130 1.00 37.10  ?  45  VAL B N     1 
ATOM   2620 C  CA    . VAL B 1 45  ? 3.517   34.442  -27.583 1.00 36.88  ?  45  VAL B CA    1 
ATOM   2621 C  C     . VAL B 1 45  ? 4.646   35.049  -28.414 1.00 42.91  ?  45  VAL B C     1 
ATOM   2622 O  O     . VAL B 1 45  ? 5.785   34.575  -28.366 1.00 41.84  ?  45  VAL B O     1 
ATOM   2623 C  CB    . VAL B 1 45  ? 3.654   32.903  -27.515 1.00 35.30  ?  45  VAL B CB    1 
ATOM   2624 C  CG1   . VAL B 1 45  ? 2.526   32.281  -26.736 1.00 37.94  ?  45  VAL B CG1   1 
ATOM   2625 C  CG2   . VAL B 1 45  ? 3.669   32.296  -28.892 1.00 38.81  ?  45  VAL B CG2   1 
ATOM   2626 N  N     . ASP B 1 46  ? 4.346   36.107  -29.171 1.00 36.99  ?  46  ASP B N     1 
ATOM   2627 C  CA    . ASP B 1 46  ? 5.358   36.692  -30.039 1.00 45.23  ?  46  ASP B CA    1 
ATOM   2628 C  C     . ASP B 1 46  ? 6.565   37.162  -29.241 1.00 46.78  ?  46  ASP B C     1 
ATOM   2629 O  O     . ASP B 1 46  ? 7.710   36.920  -29.634 1.00 44.34  ?  46  ASP B O     1 
ATOM   2630 C  CB    . ASP B 1 46  ? 4.766   37.849  -30.836 1.00 40.70  ?  46  ASP B CB    1 
ATOM   2631 C  CG    . ASP B 1 46  ? 3.662   37.406  -31.766 1.00 47.67  ?  46  ASP B CG    1 
ATOM   2632 O  OD1   . ASP B 1 46  ? 2.617   36.932  -31.255 1.00 51.88  ?  46  ASP B OD1   1 
ATOM   2633 O  OD2   . ASP B 1 46  ? 3.826   37.537  -33.005 1.00 51.42  ?  46  ASP B OD2   1 
ATOM   2634 N  N     . ASP B 1 47  ? 6.326   37.818  -28.110 1.00 44.59  ?  47  ASP B N     1 
ATOM   2635 C  CA    . ASP B 1 47  ? 7.424   38.377  -27.326 1.00 48.19  ?  47  ASP B CA    1 
ATOM   2636 C  C     . ASP B 1 47  ? 8.351   37.283  -26.797 1.00 43.63  ?  47  ASP B C     1 
ATOM   2637 O  O     . ASP B 1 47  ? 9.576   37.373  -26.951 1.00 48.15  ?  47  ASP B O     1 
ATOM   2638 C  CB    . ASP B 1 47  ? 6.849   39.221  -26.185 1.00 54.40  ?  47  ASP B CB    1 
ATOM   2639 C  CG    . ASP B 1 47  ? 6.352   40.598  -26.665 1.00 61.33  ?  47  ASP B CG    1 
ATOM   2640 O  OD1   . ASP B 1 47  ? 6.288   40.847  -27.909 1.00 56.95  ?  47  ASP B OD1   1 
ATOM   2641 O  OD2   . ASP B 1 47  ? 5.970   41.411  -25.789 1.00 61.50  ?  47  ASP B OD2   1 
ATOM   2642 N  N     . VAL B 1 48  ? 7.788   36.258  -26.151 1.00 41.83  ?  48  VAL B N     1 
ATOM   2643 C  CA    . VAL B 1 48  ? 8.539   35.086  -25.710 1.00 40.66  ?  48  VAL B CA    1 
ATOM   2644 C  C     . VAL B 1 48  ? 9.489   34.617  -26.821 1.00 44.76  ?  48  VAL B C     1 
ATOM   2645 O  O     . VAL B 1 48  ? 10.682  34.387  -26.589 1.00 37.83  ?  48  VAL B O     1 
ATOM   2646 C  CB    . VAL B 1 48  ? 7.571   33.966  -25.291 1.00 37.67  ?  48  VAL B CB    1 
ATOM   2647 C  CG1   . VAL B 1 48  ? 8.337   32.752  -24.777 1.00 36.99  ?  48  VAL B CG1   1 
ATOM   2648 C  CG2   . VAL B 1 48  ? 6.630   34.462  -24.216 1.00 38.97  ?  48  VAL B CG2   1 
ATOM   2649 N  N     . VAL B 1 49  ? 8.974   34.543  -28.045 1.00 37.18  ?  49  VAL B N     1 
ATOM   2650 C  CA    . VAL B 1 49  ? 9.706   33.941  -29.134 1.00 37.84  ?  49  VAL B CA    1 
ATOM   2651 C  C     . VAL B 1 49  ? 10.829  34.852  -29.625 1.00 45.86  ?  49  VAL B C     1 
ATOM   2652 O  O     . VAL B 1 49  ? 11.965  34.390  -29.805 1.00 44.65  ?  49  VAL B O     1 
ATOM   2653 C  CB    . VAL B 1 49  ? 8.715   33.566  -30.243 1.00 41.07  ?  49  VAL B CB    1 
ATOM   2654 C  CG1   . VAL B 1 49  ? 9.451   33.070  -31.460 1.00 44.27  ?  49  VAL B CG1   1 
ATOM   2655 C  CG2   . VAL B 1 49  ? 7.786   32.488  -29.726 1.00 42.82  ?  49  VAL B CG2   1 
ATOM   2656 N  N     . GLU B 1 50  ? 10.553  36.153  -29.829 1.00 44.94  ?  50  GLU B N     1 
ATOM   2657 C  CA    . GLU B 1 50  ? 11.591  37.059  -30.333 1.00 47.71  ?  50  GLU B CA    1 
ATOM   2658 C  C     . GLU B 1 50  ? 12.793  37.063  -29.395 1.00 50.72  ?  50  GLU B C     1 
ATOM   2659 O  O     . GLU B 1 50  ? 13.953  36.997  -29.839 1.00 51.59  ?  50  GLU B O     1 
ATOM   2660 C  CB    . GLU B 1 50  ? 11.061  38.488  -30.490 1.00 51.16  ?  50  GLU B CB    1 
ATOM   2661 C  CG    . GLU B 1 50  ? 9.815   38.730  -31.359 1.00 53.73  ?  50  GLU B CG    1 
ATOM   2662 C  CD    . GLU B 1 50  ? 9.198   40.139  -31.099 1.00 56.79  ?  50  GLU B CD    1 
ATOM   2663 O  OE1   . GLU B 1 50  ? 9.733   41.151  -31.608 1.00 58.66  ?  50  GLU B OE1   1 
ATOM   2664 O  OE2   . GLU B 1 50  ? 8.197   40.242  -30.345 1.00 60.52  ?  50  GLU B OE2   1 
ATOM   2665 N  N     . ALA B 1 51  ? 12.514  37.096  -28.087 1.00 46.49  ?  51  ALA B N     1 
ATOM   2666 C  CA    . ALA B 1 51  ? 13.544  37.022  -27.060 1.00 44.19  ?  51  ALA B CA    1 
ATOM   2667 C  C     . ALA B 1 51  ? 14.424  35.782  -27.232 1.00 46.63  ?  51  ALA B C     1 
ATOM   2668 O  O     . ALA B 1 51  ? 15.653  35.887  -27.335 1.00 54.56  ?  51  ALA B O     1 
ATOM   2669 C  CB    . ALA B 1 51  ? 12.874  37.047  -25.686 1.00 43.52  ?  51  ALA B CB    1 
ATOM   2670 N  N     . ALA B 1 52  ? 13.818  34.595  -27.308 1.00 41.42  ?  52  ALA B N     1 
ATOM   2671 C  CA    . ALA B 1 52  ? 14.628  33.402  -27.538 1.00 44.08  ?  52  ALA B CA    1 
ATOM   2672 C  C     . ALA B 1 52  ? 15.265  33.408  -28.919 1.00 47.48  ?  52  ALA B C     1 
ATOM   2673 O  O     . ALA B 1 52  ? 16.378  32.890  -29.091 1.00 50.28  ?  52  ALA B O     1 
ATOM   2674 C  CB    . ALA B 1 52  ? 13.790  32.143  -27.359 1.00 44.96  ?  52  ALA B CB    1 
ATOM   2675 N  N     . GLY B 1 53  ? 14.581  33.984  -29.905 1.00 46.73  ?  53  GLY B N     1 
ATOM   2676 C  CA    . GLY B 1 53  ? 15.027  33.986  -31.288 1.00 54.93  ?  53  GLY B CA    1 
ATOM   2677 C  C     . GLY B 1 53  ? 16.251  34.826  -31.563 1.00 56.78  ?  53  GLY B C     1 
ATOM   2678 O  O     . GLY B 1 53  ? 16.714  34.880  -32.712 1.00 53.14  ?  53  GLY B O     1 
ATOM   2679 N  N     . ARG B 1 54  ? 16.736  35.535  -30.540 1.00 60.60  ?  54  ARG B N     1 
ATOM   2680 C  CA    . ARG B 1 54  ? 18.062  36.132  -30.598 1.00 62.34  ?  54  ARG B CA    1 
ATOM   2681 C  C     . ARG B 1 54  ? 19.121  35.043  -30.719 1.00 59.41  ?  54  ARG B C     1 
ATOM   2682 O  O     . ARG B 1 54  ? 19.908  35.021  -31.673 1.00 61.14  ?  54  ARG B O     1 
ATOM   2683 C  CB    . ARG B 1 54  ? 18.286  36.999  -29.353 1.00 58.18  ?  54  ARG B CB    1 
ATOM   2684 N  N     . SER B 1 55  ? 19.123  34.108  -29.762 1.00 59.17  ?  55  SER B N     1 
ATOM   2685 C  CA    . SER B 1 55  ? 20.032  32.965  -29.784 1.00 58.70  ?  55  SER B CA    1 
ATOM   2686 C  C     . SER B 1 55  ? 19.650  31.954  -30.869 1.00 64.24  ?  55  SER B C     1 
ATOM   2687 O  O     . SER B 1 55  ? 20.430  31.703  -31.801 1.00 64.98  ?  55  SER B O     1 
ATOM   2688 C  CB    . SER B 1 55  ? 20.037  32.285  -28.414 1.00 59.69  ?  55  SER B CB    1 
ATOM   2689 O  OG    . SER B 1 55  ? 20.603  33.117  -27.421 1.00 66.41  ?  55  SER B OG    1 
ATOM   2690 N  N     . LEU B 1 56  ? 18.454  31.354  -30.757 1.00 56.06  ?  56  LEU B N     1 
ATOM   2691 C  CA    . LEU B 1 56  ? 18.030  30.264  -31.626 1.00 45.83  ?  56  LEU B CA    1 
ATOM   2692 C  C     . LEU B 1 56  ? 17.433  30.762  -32.940 1.00 45.06  ?  56  LEU B C     1 
ATOM   2693 O  O     . LEU B 1 56  ? 16.997  31.906  -33.085 1.00 49.70  ?  56  LEU B O     1 
ATOM   2694 C  CB    . LEU B 1 56  ? 16.986  29.378  -30.946 1.00 45.66  ?  56  LEU B CB    1 
ATOM   2695 C  CG    . LEU B 1 56  ? 17.168  28.863  -29.528 1.00 44.39  ?  56  LEU B CG    1 
ATOM   2696 C  CD1   . LEU B 1 56  ? 15.787  28.564  -28.920 1.00 43.75  ?  56  LEU B CD1   1 
ATOM   2697 C  CD2   . LEU B 1 56  ? 18.013  27.634  -29.583 1.00 38.52  ?  56  LEU B CD2   1 
ATOM   2698 N  N     . ASN B 1 57  ? 17.410  29.850  -33.897 1.00 44.86  ?  57  ASN B N     1 
ATOM   2699 C  CA    . ASN B 1 57  ? 16.718  29.932  -35.181 1.00 42.43  ?  57  ASN B CA    1 
ATOM   2700 C  C     . ASN B 1 57  ? 15.258  29.496  -34.937 1.00 44.75  ?  57  ASN B C     1 
ATOM   2701 O  O     . ASN B 1 57  ? 14.921  28.309  -35.022 1.00 41.46  ?  57  ASN B O     1 
ATOM   2702 C  CB    . ASN B 1 57  ? 17.450  29.009  -36.154 1.00 39.05  ?  57  ASN B CB    1 
ATOM   2703 C  CG    . ASN B 1 57  ? 16.828  28.935  -37.540 1.00 45.72  ?  57  ASN B CG    1 
ATOM   2704 O  OD1   . ASN B 1 57  ? 15.660  29.240  -37.753 1.00 52.39  ?  57  ASN B OD1   1 
ATOM   2705 N  ND2   . ASN B 1 57  ? 17.595  28.393  -38.476 1.00 49.58  ?  57  ASN B ND2   1 
ATOM   2706 N  N     . VAL B 1 58  ? 14.369  30.443  -34.616 1.00 42.62  ?  58  VAL B N     1 
ATOM   2707 C  CA    . VAL B 1 58  ? 12.998  30.121  -34.217 1.00 40.05  ?  58  VAL B CA    1 
ATOM   2708 C  C     . VAL B 1 58  ? 12.020  30.771  -35.177 1.00 41.81  ?  58  VAL B C     1 
ATOM   2709 O  O     . VAL B 1 58  ? 12.080  31.985  -35.397 1.00 48.51  ?  58  VAL B O     1 
ATOM   2710 C  CB    . VAL B 1 58  ? 12.655  30.580  -32.790 1.00 40.36  ?  58  VAL B CB    1 
ATOM   2711 C  CG1   . VAL B 1 58  ? 11.480  29.764  -32.278 1.00 37.56  ?  58  VAL B CG1   1 
ATOM   2712 C  CG2   . VAL B 1 58  ? 13.825  30.497  -31.856 1.00 49.08  ?  58  VAL B CG2   1 
ATOM   2713 N  N     . ARG B 1 59  ? 11.072  29.978  -35.673 1.00 38.87  ?  59  ARG B N     1 
ATOM   2714 C  CA    . ARG B 1 59  ? 9.945   30.431  -36.478 1.00 35.70  ?  59  ARG B CA    1 
ATOM   2715 C  C     . ARG B 1 59  ? 8.659   30.328  -35.658 1.00 38.16  ?  59  ARG B C     1 
ATOM   2716 O  O     . ARG B 1 59  ? 8.454   29.357  -34.917 1.00 36.60  ?  59  ARG B O     1 
ATOM   2717 C  CB    . ARG B 1 59  ? 9.835   29.566  -37.735 1.00 38.60  ?  59  ARG B CB    1 
ATOM   2718 C  CG    . ARG B 1 59  ? 8.905   30.094  -38.760 1.00 44.62  ?  59  ARG B CG    1 
ATOM   2719 C  CD    . ARG B 1 59  ? 8.513   29.039  -39.793 1.00 47.05  ?  59  ARG B CD    1 
ATOM   2720 N  NE    . ARG B 1 59  ? 7.466   29.558  -40.674 1.00 46.56  ?  59  ARG B NE    1 
ATOM   2721 C  CZ    . ARG B 1 59  ? 7.284   29.212  -41.944 1.00 45.37  ?  59  ARG B CZ    1 
ATOM   2722 N  NH1   . ARG B 1 59  ? 8.046   28.303  -42.531 1.00 47.40  ?  59  ARG B NH1   1 
ATOM   2723 N  NH2   . ARG B 1 59  ? 6.310   29.795  -42.644 1.00 50.77  ?  59  ARG B NH2   1 
ATOM   2724 N  N     . LEU B 1 60  ? 7.777   31.305  -35.785 1.00 41.51  ?  60  LEU B N     1 
ATOM   2725 C  CA    . LEU B 1 60  ? 6.506   31.264  -35.065 1.00 35.39  ?  60  LEU B CA    1 
ATOM   2726 C  C     . LEU B 1 60  ? 5.373   31.170  -36.075 1.00 37.35  ?  60  LEU B C     1 
ATOM   2727 O  O     . LEU B 1 60  ? 5.288   31.991  -36.991 1.00 35.36  ?  60  LEU B O     1 
ATOM   2728 C  CB    . LEU B 1 60  ? 6.325   32.491  -34.163 1.00 33.67  ?  60  LEU B CB    1 
ATOM   2729 C  CG    . LEU B 1 60  ? 4.935   32.744  -33.502 1.00 37.38  ?  60  LEU B CG    1 
ATOM   2730 C  CD1   . LEU B 1 60  ? 4.549   31.643  -32.535 1.00 33.08  ?  60  LEU B CD1   1 
ATOM   2731 C  CD2   . LEU B 1 60  ? 4.864   34.117  -32.788 1.00 35.64  ?  60  LEU B CD2   1 
ATOM   2732 N  N     . ILE B 1 61  ? 4.512   30.169  -35.921 1.00 38.05  ?  61  ILE B N     1 
ATOM   2733 C  CA    . ILE B 1 61  ? 3.295   30.053  -36.726 1.00 39.34  ?  61  ILE B CA    1 
ATOM   2734 C  C     . ILE B 1 61  ? 2.091   30.268  -35.814 1.00 39.27  ?  61  ILE B C     1 
ATOM   2735 O  O     . ILE B 1 61  ? 1.894   29.524  -34.838 1.00 35.33  ?  61  ILE B O     1 
ATOM   2736 C  CB    . ILE B 1 61  ? 3.177   28.695  -37.439 1.00 38.93  ?  61  ILE B CB    1 
ATOM   2737 C  CG1   . ILE B 1 61  ? 4.190   28.532  -38.565 1.00 40.40  ?  61  ILE B CG1   1 
ATOM   2738 C  CG2   . ILE B 1 61  ? 1.722   28.444  -37.913 1.00 36.28  ?  61  ILE B CG2   1 
ATOM   2739 C  CD1   . ILE B 1 61  ? 4.307   27.098  -38.980 1.00 41.75  ?  61  ILE B CD1   1 
ATOM   2740 N  N     . ASP B 1 62  ? 1.277   31.267  -36.156 1.00 39.50  ?  62  ASP B N     1 
ATOM   2741 C  CA    . ASP B 1 62  ? 0.027   31.548  -35.457 1.00 40.60  ?  62  ASP B CA    1 
ATOM   2742 C  C     . ASP B 1 62  ? -1.108  30.780  -36.124 1.00 39.36  ?  62  ASP B C     1 
ATOM   2743 O  O     . ASP B 1 62  ? -1.418  31.020  -37.291 1.00 43.47  ?  62  ASP B O     1 
ATOM   2744 C  CB    . ASP B 1 62  ? -0.261  33.048  -35.521 1.00 46.87  ?  62  ASP B CB    1 
ATOM   2745 C  CG    . ASP B 1 62  ? 0.424   33.841  -34.417 1.00 52.64  ?  62  ASP B CG    1 
ATOM   2746 O  OD1   . ASP B 1 62  ? 0.696   33.282  -33.320 1.00 47.00  ?  62  ASP B OD1   1 
ATOM   2747 O  OD2   . ASP B 1 62  ? 0.730   35.034  -34.676 1.00 60.17  ?  62  ASP B OD2   1 
ATOM   2748 N  N     . GLN B 1 63  ? -1.738  29.885  -35.401 1.00 42.41  ?  63  GLN B N     1 
ATOM   2749 C  CA    . GLN B 1 63  ? -2.895  29.195  -35.962 1.00 39.47  ?  63  GLN B CA    1 
ATOM   2750 C  C     . GLN B 1 63  ? -4.087  30.149  -36.070 1.00 44.05  ?  63  GLN B C     1 
ATOM   2751 O  O     . GLN B 1 63  ? -4.370  30.891  -35.121 1.00 42.16  ?  63  GLN B O     1 
ATOM   2752 C  CB    . GLN B 1 63  ? -3.255  27.987  -35.099 1.00 41.66  ?  63  GLN B CB    1 
ATOM   2753 C  CG    . GLN B 1 63  ? -2.281  26.808  -35.200 1.00 36.17  ?  63  GLN B CG    1 
ATOM   2754 C  CD    . GLN B 1 63  ? -2.311  26.141  -36.580 1.00 37.29  ?  63  GLN B CD    1 
ATOM   2755 O  OE1   . GLN B 1 63  ? -1.718  26.641  -37.543 1.00 41.96  ?  63  GLN B OE1   1 
ATOM   2756 N  NE2   . GLN B 1 63  ? -2.993  25.004  -36.675 1.00 35.33  ?  63  GLN B NE2   1 
ATOM   2757 N  N     . PRO B 1 64  ? -4.783  30.185  -37.213 1.00 45.04  ?  64  PRO B N     1 
ATOM   2758 C  CA    . PRO B 1 64  ? -6.029  30.977  -37.314 1.00 42.63  ?  64  PRO B CA    1 
ATOM   2759 C  C     . PRO B 1 64  ? -7.094  30.595  -36.315 1.00 44.13  ?  64  PRO B C     1 
ATOM   2760 O  O     . PRO B 1 64  ? -7.905  31.446  -35.933 1.00 50.58  ?  64  PRO B O     1 
ATOM   2761 C  CB    . PRO B 1 64  ? -6.525  30.701  -38.746 1.00 46.37  ?  64  PRO B CB    1 
ATOM   2762 C  CG    . PRO B 1 64  ? -5.617  29.638  -39.313 1.00 43.11  ?  64  PRO B CG    1 
ATOM   2763 C  CD    . PRO B 1 64  ? -4.316  29.725  -38.528 1.00 44.64  ?  64  PRO B CD    1 
ATOM   2764 N  N     . SER B 1 65  ? -7.145  29.341  -35.891 1.00 45.96  ?  65  SER B N     1 
ATOM   2765 C  CA    . SER B 1 65  ? -8.032  28.988  -34.796 1.00 44.52  ?  65  SER B CA    1 
ATOM   2766 C  C     . SER B 1 65  ? -7.518  27.730  -34.126 1.00 40.54  ?  65  SER B C     1 
ATOM   2767 O  O     . SER B 1 65  ? -6.724  26.978  -34.691 1.00 43.58  ?  65  SER B O     1 
ATOM   2768 C  CB    . SER B 1 65  ? -9.476  28.794  -35.261 1.00 45.97  ?  65  SER B CB    1 
ATOM   2769 O  OG    . SER B 1 65  ? -9.585  27.790  -36.248 1.00 47.87  ?  65  SER B OG    1 
ATOM   2770 N  N     . GLN B 1 66  ? -8.011  27.516  -32.914 1.00 43.66  ?  66  GLN B N     1 
ATOM   2771 C  CA    . GLN B 1 66  ? -7.581  26.413  -32.072 1.00 44.44  ?  66  GLN B CA    1 
ATOM   2772 C  C     . GLN B 1 66  ? -7.888  25.098  -32.758 1.00 45.39  ?  66  GLN B C     1 
ATOM   2773 O  O     . GLN B 1 66  ? -9.048  24.815  -33.067 1.00 44.54  ?  66  GLN B O     1 
ATOM   2774 C  CB    . GLN B 1 66  ? -8.287  26.497  -30.718 1.00 38.97  ?  66  GLN B CB    1 
ATOM   2775 C  CG    . GLN B 1 66  ? -7.769  25.533  -29.701 1.00 39.49  ?  66  GLN B CG    1 
ATOM   2776 C  CD    . GLN B 1 66  ? -8.873  24.753  -29.081 1.00 51.00  ?  66  GLN B CD    1 
ATOM   2777 O  OE1   . GLN B 1 66  ? -9.730  25.326  -28.396 1.00 51.92  ?  66  GLN B OE1   1 
ATOM   2778 N  NE2   . GLN B 1 66  ? -8.896  23.435  -29.327 1.00 48.61  ?  66  GLN B NE2   1 
ATOM   2779 N  N     . SER B 1 67  ? -6.846  24.304  -33.032 1.00 43.04  ?  67  SER B N     1 
ATOM   2780 C  CA    . SER B 1 67  ? -7.038  23.027  -33.716 1.00 42.34  ?  67  SER B CA    1 
ATOM   2781 C  C     . SER B 1 67  ? -6.563  21.821  -32.910 1.00 40.64  ?  67  SER B C     1 
ATOM   2782 O  O     . SER B 1 67  ? -6.495  20.722  -33.464 1.00 45.47  ?  67  SER B O     1 
ATOM   2783 C  CB    . SER B 1 67  ? -6.338  23.051  -35.076 1.00 40.07  ?  67  SER B CB    1 
ATOM   2784 O  OG    . SER B 1 67  ? -5.107  23.761  -34.986 1.00 47.89  ?  67  SER B OG    1 
ATOM   2785 N  N     . GLY B 1 68  ? -6.214  21.989  -31.632 1.00 40.73  ?  68  GLY B N     1 
ATOM   2786 C  CA    . GLY B 1 68  ? -5.710  20.894  -30.830 1.00 33.63  ?  68  GLY B CA    1 
ATOM   2787 C  C     . GLY B 1 68  ? -4.267  20.514  -31.129 1.00 35.71  ?  68  GLY B C     1 
ATOM   2788 O  O     . GLY B 1 68  ? -3.728  20.821  -32.200 1.00 40.67  ?  68  GLY B O     1 
ATOM   2789 N  N     . PRO B 1 69  ? -3.628  19.802  -30.185 1.00 32.16  ?  69  PRO B N     1 
ATOM   2790 C  CA    . PRO B 1 69  ? -2.215  19.414  -30.362 1.00 36.41  ?  69  PRO B CA    1 
ATOM   2791 C  C     . PRO B 1 69  ? -1.895  18.763  -31.697 1.00 35.96  ?  69  PRO B C     1 
ATOM   2792 O  O     . PRO B 1 69  ? -0.802  18.990  -32.238 1.00 34.77  ?  69  PRO B O     1 
ATOM   2793 C  CB    . PRO B 1 69  ? -1.970  18.431  -29.203 1.00 37.92  ?  69  PRO B CB    1 
ATOM   2794 C  CG    . PRO B 1 69  ? -3.404  18.088  -28.654 1.00 33.40  ?  69  PRO B CG    1 
ATOM   2795 C  CD    . PRO B 1 69  ? -4.200  19.292  -28.923 1.00 34.26  ?  69  PRO B CD    1 
ATOM   2796 N  N     . SER B 1 70  ? -2.804  17.944  -32.229 1.00 35.32  ?  70  SER B N     1 
ATOM   2797 C  CA    . SER B 1 70  ? -2.566  17.310  -33.523 1.00 33.17  ?  70  SER B CA    1 
ATOM   2798 C  C     . SER B 1 70  ? -2.419  18.351  -34.617 1.00 33.28  ?  70  SER B C     1 
ATOM   2799 O  O     . SER B 1 70  ? -1.455  18.318  -35.384 1.00 36.35  ?  70  SER B O     1 
ATOM   2800 C  CB    . SER B 1 70  ? -3.701  16.338  -33.859 1.00 29.24  ?  70  SER B CB    1 
ATOM   2801 O  OG    . SER B 1 70  ? -3.577  15.172  -33.082 1.00 28.04  ?  70  SER B OG    1 
ATOM   2802 N  N     . GLY B 1 71  ? -3.355  19.305  -34.692 1.00 35.60  ?  71  GLY B N     1 
ATOM   2803 C  CA    . GLY B 1 71  ? -3.274  20.319  -35.728 1.00 33.81  ?  71  GLY B CA    1 
ATOM   2804 C  C     . GLY B 1 71  ? -2.123  21.282  -35.524 1.00 33.90  ?  71  GLY B C     1 
ATOM   2805 O  O     . GLY B 1 71  ? -1.553  21.790  -36.498 1.00 32.89  ?  71  GLY B O     1 
ATOM   2806 N  N     . ALA B 1 72  ? -1.765  21.554  -34.264 1.00 31.88  ?  72  ALA B N     1 
ATOM   2807 C  CA    . ALA B 1 72  ? -0.645  22.453  -34.013 1.00 35.52  ?  72  ALA B CA    1 
ATOM   2808 C  C     . ALA B 1 72  ? 0.668   21.813  -34.459 1.00 33.90  ?  72  ALA B C     1 
ATOM   2809 O  O     . ALA B 1 72  ? 1.459   22.426  -35.184 1.00 28.24  ?  72  ALA B O     1 
ATOM   2810 C  CB    . ALA B 1 72  ? -0.602  22.835  -32.542 1.00 33.89  ?  72  ALA B CB    1 
ATOM   2811 N  N     . ARG B 1 73  ? 0.890   20.554  -34.075 1.00 38.51  ?  73  ARG B N     1 
ATOM   2812 C  CA    . ARG B 1 73  ? 2.084   19.850  -34.524 1.00 37.38  ?  73  ARG B CA    1 
ATOM   2813 C  C     . ARG B 1 73  ? 2.087   19.705  -36.031 1.00 32.98  ?  73  ARG B C     1 
ATOM   2814 O  O     . ARG B 1 73  ? 3.115   19.916  -36.680 1.00 34.95  ?  73  ARG B O     1 
ATOM   2815 C  CB    . ARG B 1 73  ? 2.152   18.485  -33.860 1.00 30.75  ?  73  ARG B CB    1 
ATOM   2816 C  CG    . ARG B 1 73  ? 2.306   18.572  -32.370 1.00 28.35  ?  73  ARG B CG    1 
ATOM   2817 C  CD    . ARG B 1 73  ? 2.756   17.232  -31.849 1.00 31.74  ?  73  ARG B CD    1 
ATOM   2818 N  NE    . ARG B 1 73  ? 2.748   17.188  -30.408 1.00 28.57  ?  73  ARG B NE    1 
ATOM   2819 C  CZ    . ARG B 1 73  ? 1.804   16.571  -29.712 1.00 34.96  ?  73  ARG B CZ    1 
ATOM   2820 N  NH1   . ARG B 1 73  ? 0.859   15.861  -30.311 1.00 32.23  ?  73  ARG B NH1   1 
ATOM   2821 N  NH2   . ARG B 1 73  ? 1.801   16.682  -28.389 1.00 27.04  ?  73  ARG B NH2   1 
ATOM   2822 N  N     . ASN B 1 74  ? 0.945   19.345  -36.611 1.00 30.34  ?  74  ASN B N     1 
ATOM   2823 C  CA    . ASN B 1 74  ? 0.911   19.208  -38.059 1.00 32.63  ?  74  ASN B CA    1 
ATOM   2824 C  C     . ASN B 1 74  ? 1.354   20.492  -38.731 1.00 35.03  ?  74  ASN B C     1 
ATOM   2825 O  O     . ASN B 1 74  ? 2.080   20.449  -39.733 1.00 36.53  ?  74  ASN B O     1 
ATOM   2826 C  CB    . ASN B 1 74  ? -0.482  18.792  -38.518 1.00 32.11  ?  74  ASN B CB    1 
ATOM   2827 C  CG    . ASN B 1 74  ? -0.781  17.333  -38.164 1.00 37.34  ?  74  ASN B CG    1 
ATOM   2828 O  OD1   . ASN B 1 74  ? 0.155   16.563  -37.883 1.00 30.48  ?  74  ASN B OD1   1 
ATOM   2829 N  ND2   . ASN B 1 74  ? -2.084  16.955  -38.125 1.00 32.62  ?  74  ASN B ND2   1 
ATOM   2830 N  N     . ALA B 1 75  ? 0.954   21.644  -38.174 1.00 31.39  ?  75  ALA B N     1 
ATOM   2831 C  CA    . ALA B 1 75  ? 1.400   22.932  -38.713 1.00 36.70  ?  75  ALA B CA    1 
ATOM   2832 C  C     . ALA B 1 75  ? 2.921   23.041  -38.703 1.00 33.73  ?  75  ALA B C     1 
ATOM   2833 O  O     . ALA B 1 75  ? 3.511   23.578  -39.644 1.00 32.46  ?  75  ALA B O     1 
ATOM   2834 C  CB    . ALA B 1 75  ? 0.766   24.082  -37.929 1.00 36.05  ?  75  ALA B CB    1 
ATOM   2835 N  N     . GLY B 1 76  ? 3.577   22.512  -37.663 1.00 31.81  ?  76  GLY B N     1 
ATOM   2836 C  CA    . GLY B 1 76  ? 5.028   22.487  -37.658 1.00 30.67  ?  76  GLY B CA    1 
ATOM   2837 C  C     . GLY B 1 76  ? 5.599   21.463  -38.632 1.00 37.38  ?  76  GLY B C     1 
ATOM   2838 O  O     . GLY B 1 76  ? 6.559   21.742  -39.365 1.00 32.21  ?  76  GLY B O     1 
ATOM   2839 N  N     . LEU B 1 77  ? 5.023   20.255  -38.644 1.00 32.72  ?  77  LEU B N     1 
ATOM   2840 C  CA    . LEU B 1 77  ? 5.496   19.219  -39.554 1.00 30.24  ?  77  LEU B CA    1 
ATOM   2841 C  C     . LEU B 1 77  ? 5.451   19.667  -41.004 1.00 32.28  ?  77  LEU B C     1 
ATOM   2842 O  O     . LEU B 1 77  ? 6.282   19.234  -41.806 1.00 34.80  ?  77  LEU B O     1 
ATOM   2843 C  CB    . LEU B 1 77  ? 4.661   17.955  -39.382 1.00 30.72  ?  77  LEU B CB    1 
ATOM   2844 C  CG    . LEU B 1 77  ? 4.951   17.187  -38.101 1.00 36.04  ?  77  LEU B CG    1 
ATOM   2845 C  CD1   . LEU B 1 77  ? 3.902   16.075  -37.911 1.00 33.79  ?  77  LEU B CD1   1 
ATOM   2846 C  CD2   . LEU B 1 77  ? 6.380   16.644  -38.133 1.00 29.32  ?  77  LEU B CD2   1 
ATOM   2847 N  N     . GLU B 1 78  ? 4.500   20.520  -41.370 1.00 36.14  ?  78  GLU B N     1 
ATOM   2848 C  CA    . GLU B 1 78  ? 4.399   20.906  -42.771 1.00 36.17  ?  78  GLU B CA    1 
ATOM   2849 C  C     . GLU B 1 78  ? 5.548   21.796  -43.208 1.00 32.69  ?  78  GLU B C     1 
ATOM   2850 O  O     . GLU B 1 78  ? 5.850   21.839  -44.401 1.00 31.83  ?  78  GLU B O     1 
ATOM   2851 C  CB    . GLU B 1 78  ? 3.069   21.608  -43.060 1.00 37.08  ?  78  GLU B CB    1 
ATOM   2852 C  CG    . GLU B 1 78  ? 1.897   20.671  -42.922 1.00 43.51  ?  78  GLU B CG    1 
ATOM   2853 C  CD    . GLU B 1 78  ? 0.553   21.373  -42.948 1.00 54.26  ?  78  GLU B CD    1 
ATOM   2854 O  OE1   . GLU B 1 78  ? -0.445  20.757  -43.415 1.00 59.30  ?  78  GLU B OE1   1 
ATOM   2855 O  OE2   . GLU B 1 78  ? 0.501   22.560  -42.544 1.00 63.73  ?  78  GLU B OE2   1 
ATOM   2856 N  N     . VAL B 1 79  ? 6.176   22.540  -42.297 1.00 33.83  ?  79  VAL B N     1 
ATOM   2857 C  CA    . VAL B 1 79  ? 7.230   23.475  -42.710 1.00 36.25  ?  79  VAL B CA    1 
ATOM   2858 C  C     . VAL B 1 79  ? 8.620   23.047  -42.243 1.00 35.89  ?  79  VAL B C     1 
ATOM   2859 O  O     . VAL B 1 79  ? 9.623   23.608  -42.725 1.00 34.58  ?  79  VAL B O     1 
ATOM   2860 C  CB    . VAL B 1 79  ? 6.918   24.927  -42.267 1.00 36.03  ?  79  VAL B CB    1 
ATOM   2861 C  CG1   . VAL B 1 79  ? 5.463   25.284  -42.600 1.00 33.84  ?  79  VAL B CG1   1 
ATOM   2862 C  CG2   . VAL B 1 79  ? 7.207   25.156  -40.780 1.00 33.63  ?  79  VAL B CG2   1 
ATOM   2863 N  N     . ALA B 1 80  ? 8.708   22.035  -41.374 1.00 33.84  ?  80  ALA B N     1 
ATOM   2864 C  CA    . ALA B 1 80  ? 9.976   21.537  -40.857 1.00 35.09  ?  80  ALA B CA    1 
ATOM   2865 C  C     . ALA B 1 80  ? 10.928  21.127  -41.986 1.00 39.86  ?  80  ALA B C     1 
ATOM   2866 O  O     . ALA B 1 80  ? 10.569  20.342  -42.873 1.00 31.98  ?  80  ALA B O     1 
ATOM   2867 C  CB    . ALA B 1 80  ? 9.709   20.357  -39.922 1.00 28.34  ?  80  ALA B CB    1 
ATOM   2868 N  N     . ARG B 1 81  ? 12.160  21.666  -41.936 1.00 40.05  ?  81  ARG B N     1 
ATOM   2869 C  CA    . ARG B 1 81  ? 13.173  21.433  -42.964 1.00 37.99  ?  81  ARG B CA    1 
ATOM   2870 C  C     . ARG B 1 81  ? 14.192  20.376  -42.577 1.00 40.78  ?  81  ARG B C     1 
ATOM   2871 O  O     . ARG B 1 81  ? 15.035  20.028  -43.406 1.00 38.88  ?  81  ARG B O     1 
ATOM   2872 C  CB    . ARG B 1 81  ? 13.946  22.724  -43.300 1.00 37.33  ?  81  ARG B CB    1 
ATOM   2873 C  CG    . ARG B 1 81  ? 13.128  23.971  -43.595 1.00 44.49  ?  81  ARG B CG    1 
ATOM   2874 C  CD    . ARG B 1 81  ? 13.853  24.937  -44.539 1.00 54.55  ?  81  ARG B CD    1 
ATOM   2875 N  NE    . ARG B 1 81  ? 13.514  24.720  -45.950 1.00 72.45  ?  81  ARG B NE    1 
ATOM   2876 C  CZ    . ARG B 1 81  ? 14.168  23.932  -46.806 1.00 68.94  ?  81  ARG B CZ    1 
ATOM   2877 N  NH1   . ARG B 1 81  ? 15.278  23.295  -46.460 1.00 60.87  ?  81  ARG B NH1   1 
ATOM   2878 N  NH2   . ARG B 1 81  ? 13.701  23.791  -48.049 1.00 62.20  ?  81  ARG B NH2   1 
ATOM   2879 N  N     . GLY B 1 82  ? 14.168  19.892  -41.345 1.00 35.68  ?  82  GLY B N     1 
ATOM   2880 C  CA    . GLY B 1 82  ? 15.231  19.031  -40.884 1.00 34.01  ?  82  GLY B CA    1 
ATOM   2881 C  C     . GLY B 1 82  ? 15.038  17.562  -41.235 1.00 32.66  ?  82  GLY B C     1 
ATOM   2882 O  O     . GLY B 1 82  ? 13.944  17.043  -41.482 1.00 31.62  ?  82  GLY B O     1 
ATOM   2883 N  N     . GLU B 1 83  ? 16.152  16.846  -41.248 1.00 31.16  ?  83  GLU B N     1 
ATOM   2884 C  CA    . GLU B 1 83  ? 16.037  15.421  -41.484 1.00 32.11  ?  83  GLU B CA    1 
ATOM   2885 C  C     . GLU B 1 83  ? 15.312  14.746  -40.324 1.00 32.65  ?  83  GLU B C     1 
ATOM   2886 O  O     . GLU B 1 83  ? 14.600  13.754  -40.521 1.00 30.33  ?  83  GLU B O     1 
ATOM   2887 C  CB    . GLU B 1 83  ? 17.427  14.800  -41.707 1.00 30.52  ?  83  GLU B CB    1 
ATOM   2888 C  CG    . GLU B 1 83  ? 17.385  13.422  -42.348 1.00 33.61  ?  83  GLU B CG    1 
ATOM   2889 C  CD    . GLU B 1 83  ? 18.759  12.834  -42.554 1.00 37.88  ?  83  GLU B CD    1 
ATOM   2890 O  OE1   . GLU B 1 83  ? 19.746  13.590  -42.370 1.00 38.27  ?  83  GLU B OE1   1 
ATOM   2891 O  OE2   . GLU B 1 83  ? 18.843  11.624  -42.913 1.00 35.38  ?  83  GLU B OE2   1 
ATOM   2892 N  N     . TYR B 1 84  ? 15.510  15.252  -39.114 1.00 28.94  ?  84  TYR B N     1 
ATOM   2893 C  CA    . TYR B 1 84  ? 14.954  14.646  -37.925 1.00 27.61  ?  84  TYR B CA    1 
ATOM   2894 C  C     . TYR B 1 84  ? 14.107  15.676  -37.187 1.00 28.04  ?  84  TYR B C     1 
ATOM   2895 O  O     . TYR B 1 84  ? 14.373  16.871  -37.246 1.00 29.13  ?  84  TYR B O     1 
ATOM   2896 C  CB    . TYR B 1 84  ? 16.095  14.073  -37.072 1.00 27.29  ?  84  TYR B CB    1 
ATOM   2897 C  CG    . TYR B 1 84  ? 16.906  13.059  -37.888 1.00 31.53  ?  84  TYR B CG    1 
ATOM   2898 C  CD1   . TYR B 1 84  ? 16.386  11.778  -38.171 1.00 30.66  ?  84  TYR B CD1   1 
ATOM   2899 C  CD2   . TYR B 1 84  ? 18.143  13.403  -38.440 1.00 32.04  ?  84  TYR B CD2   1 
ATOM   2900 C  CE1   . TYR B 1 84  ? 17.096  10.866  -38.921 1.00 30.81  ?  84  TYR B CE1   1 
ATOM   2901 C  CE2   . TYR B 1 84  ? 18.868  12.499  -39.212 1.00 30.82  ?  84  TYR B CE2   1 
ATOM   2902 C  CZ    . TYR B 1 84  ? 18.348  11.243  -39.453 1.00 33.24  ?  84  TYR B CZ    1 
ATOM   2903 O  OH    . TYR B 1 84  ? 19.059  10.374  -40.220 1.00 24.42  ?  84  TYR B OH    1 
ATOM   2904 N  N     . VAL B 1 85  ? 13.053  15.199  -36.537 1.00 27.47  ?  85  VAL B N     1 
ATOM   2905 C  CA    . VAL B 1 85  ? 12.131  16.030  -35.786 1.00 27.72  ?  85  VAL B CA    1 
ATOM   2906 C  C     . VAL B 1 85  ? 12.147  15.578  -34.332 1.00 26.04  ?  85  VAL B C     1 
ATOM   2907 O  O     . VAL B 1 85  ? 12.058  14.383  -34.042 1.00 26.07  ?  85  VAL B O     1 
ATOM   2908 C  CB    . VAL B 1 85  ? 10.725  15.959  -36.390 1.00 29.96  ?  85  VAL B CB    1 
ATOM   2909 C  CG1   . VAL B 1 85  ? 9.719   16.444  -35.404 1.00 24.82  ?  85  VAL B CG1   1 
ATOM   2910 C  CG2   . VAL B 1 85  ? 10.697  16.775  -37.694 1.00 27.47  ?  85  VAL B CG2   1 
ATOM   2911 N  N     . ALA B 1 86  ? 12.349  16.519  -33.428 1.00 26.88  ?  86  ALA B N     1 
ATOM   2912 C  CA    . ALA B 1 86  ? 12.231  16.254  -32.001 1.00 26.61  ?  86  ALA B CA    1 
ATOM   2913 C  C     . ALA B 1 86  ? 11.031  17.060  -31.493 1.00 32.20  ?  86  ALA B C     1 
ATOM   2914 O  O     . ALA B 1 86  ? 11.055  18.298  -31.518 1.00 35.90  ?  86  ALA B O     1 
ATOM   2915 C  CB    . ALA B 1 86  ? 13.524  16.623  -31.266 1.00 26.98  ?  86  ALA B CB    1 
ATOM   2916 N  N     . PHE B 1 87  ? 9.974   16.366  -31.056 1.00 27.79  ?  87  PHE B N     1 
ATOM   2917 C  CA    . PHE B 1 87  ? 8.826   17.036  -30.463 1.00 29.34  ?  87  PHE B CA    1 
ATOM   2918 C  C     . PHE B 1 87  ? 9.132   17.476  -29.042 1.00 27.49  ?  87  PHE B C     1 
ATOM   2919 O  O     . PHE B 1 87  ? 9.734   16.732  -28.266 1.00 29.14  ?  87  PHE B O     1 
ATOM   2920 C  CB    . PHE B 1 87  ? 7.601   16.120  -30.462 1.00 25.51  ?  87  PHE B CB    1 
ATOM   2921 C  CG    . PHE B 1 87  ? 7.206   15.669  -31.826 1.00 30.07  ?  87  PHE B CG    1 
ATOM   2922 C  CD1   . PHE B 1 87  ? 6.524   16.532  -32.688 1.00 30.05  ?  87  PHE B CD1   1 
ATOM   2923 C  CD2   . PHE B 1 87  ? 7.531   14.393  -32.270 1.00 26.60  ?  87  PHE B CD2   1 
ATOM   2924 C  CE1   . PHE B 1 87  ? 6.169   16.131  -33.978 1.00 29.77  ?  87  PHE B CE1   1 
ATOM   2925 C  CE2   . PHE B 1 87  ? 7.175   13.976  -33.551 1.00 22.24  ?  87  PHE B CE2   1 
ATOM   2926 C  CZ    . PHE B 1 87  ? 6.503   14.841  -34.412 1.00 26.70  ?  87  PHE B CZ    1 
ATOM   2927 N  N     . LEU B 1 88  ? 8.682   18.684  -28.698 1.00 28.05  ?  88  LEU B N     1 
ATOM   2928 C  CA    . LEU B 1 88  ? 8.689   19.147  -27.318 1.00 28.00  ?  88  LEU B CA    1 
ATOM   2929 C  C     . LEU B 1 88  ? 7.371   19.870  -27.010 1.00 31.76  ?  88  LEU B C     1 
ATOM   2930 O  O     . LEU B 1 88  ? 7.068   20.898  -27.620 1.00 29.86  ?  88  LEU B O     1 
ATOM   2931 C  CB    . LEU B 1 88  ? 9.897   20.055  -27.081 1.00 27.01  ?  88  LEU B CB    1 
ATOM   2932 C  CG    . LEU B 1 88  ? 10.057  20.582  -25.655 1.00 31.67  ?  88  LEU B CG    1 
ATOM   2933 C  CD1   . LEU B 1 88  ? 10.384  19.469  -24.685 1.00 29.19  ?  88  LEU B CD1   1 
ATOM   2934 C  CD2   . LEU B 1 88  ? 11.122  21.662  -25.616 1.00 31.77  ?  88  LEU B CD2   1 
ATOM   2935 N  N     . ASP B 1 89  ? 6.571   19.328  -26.088 1.00 32.44  ?  89  ASP B N     1 
ATOM   2936 C  CA    . ASP B 1 89  ? 5.407   20.057  -25.588 1.00 33.56  ?  89  ASP B CA    1 
ATOM   2937 C  C     . ASP B 1 89  ? 5.845   21.265  -24.760 1.00 34.58  ?  89  ASP B C     1 
ATOM   2938 O  O     . ASP B 1 89  ? 6.902   21.250  -24.111 1.00 34.66  ?  89  ASP B O     1 
ATOM   2939 C  CB    . ASP B 1 89  ? 4.527   19.173  -24.699 1.00 33.41  ?  89  ASP B CB    1 
ATOM   2940 C  CG    . ASP B 1 89  ? 3.940   17.970  -25.432 1.00 37.36  ?  89  ASP B CG    1 
ATOM   2941 O  OD1   . ASP B 1 89  ? 3.838   17.977  -26.696 1.00 33.26  ?  89  ASP B OD1   1 
ATOM   2942 O  OD2   . ASP B 1 89  ? 3.560   17.003  -24.713 1.00 31.63  ?  89  ASP B OD2   1 
ATOM   2943 N  N     . ASP B 1 90  ? 4.993   22.301  -24.736 1.00 30.27  ?  90  ASP B N     1 
ATOM   2944 C  CA    . ASP B 1 90  ? 5.405   23.566  -24.116 1.00 33.19  ?  90  ASP B CA    1 
ATOM   2945 C  C     . ASP B 1 90  ? 5.598   23.491  -22.601 1.00 34.62  ?  90  ASP B C     1 
ATOM   2946 O  O     . ASP B 1 90  ? 6.251   24.369  -22.041 1.00 40.16  ?  90  ASP B O     1 
ATOM   2947 C  CB    . ASP B 1 90  ? 4.432   24.706  -24.443 1.00 30.25  ?  90  ASP B CB    1 
ATOM   2948 C  CG    . ASP B 1 90  ? 2.988   24.442  -24.009 1.00 31.79  ?  90  ASP B CG    1 
ATOM   2949 O  OD1   . ASP B 1 90  ? 2.692   23.566  -23.155 1.00 28.60  ?  90  ASP B OD1   1 
ATOM   2950 O  OD2   . ASP B 1 90  ? 2.128   25.164  -24.550 1.00 34.17  ?  90  ASP B OD2   1 
ATOM   2951 N  N     . ASP B 1 91  ? 5.085   22.477  -21.916 1.00 34.43  ?  91  ASP B N     1 
ATOM   2952 C  CA    . ASP B 1 91  ? 5.299   22.371  -20.478 1.00 36.26  ?  91  ASP B CA    1 
ATOM   2953 C  C     . ASP B 1 91  ? 6.399   21.375  -20.117 1.00 36.65  ?  91  ASP B C     1 
ATOM   2954 O  O     . ASP B 1 91  ? 6.552   21.046  -18.937 1.00 36.65  ?  91  ASP B O     1 
ATOM   2955 C  CB    . ASP B 1 91  ? 3.978   21.999  -19.768 1.00 33.29  ?  91  ASP B CB    1 
ATOM   2956 C  CG    . ASP B 1 91  ? 3.357   20.731  -20.324 1.00 37.09  ?  91  ASP B CG    1 
ATOM   2957 O  OD1   . ASP B 1 91  ? 3.833   20.224  -21.375 1.00 35.97  ?  91  ASP B OD1   1 
ATOM   2958 O  OD2   . ASP B 1 91  ? 2.408   20.223  -19.707 1.00 35.02  ?  91  ASP B OD2   1 
ATOM   2959 N  N     . ASP B 1 92  ? 7.170   20.886  -21.096 1.00 38.85  ?  92  ASP B N     1 
ATOM   2960 C  CA    . ASP B 1 92  ? 8.217   19.891  -20.850 1.00 38.12  ?  92  ASP B CA    1 
ATOM   2961 C  C     . ASP B 1 92  ? 9.579   20.487  -21.154 1.00 34.64  ?  92  ASP B C     1 
ATOM   2962 O  O     . ASP B 1 92  ? 9.694   21.607  -21.635 1.00 37.96  ?  92  ASP B O     1 
ATOM   2963 C  CB    . ASP B 1 92  ? 7.988   18.620  -21.675 1.00 36.82  ?  92  ASP B CB    1 
ATOM   2964 C  CG    . ASP B 1 92  ? 6.722   17.873  -21.261 1.00 37.38  ?  92  ASP B CG    1 
ATOM   2965 O  OD1   . ASP B 1 92  ? 6.434   17.851  -20.052 1.00 41.99  ?  92  ASP B OD1   1 
ATOM   2966 O  OD2   . ASP B 1 92  ? 6.018   17.317  -22.139 1.00 34.16  ?  92  ASP B OD2   1 
ATOM   2967 N  N     . VAL B 1 93  ? 10.624  19.704  -20.907 1.00 40.88  ?  93  VAL B N     1 
ATOM   2968 C  CA    . VAL B 1 93  ? 11.985  20.230  -20.924 1.00 38.02  ?  93  VAL B CA    1 
ATOM   2969 C  C     . VAL B 1 93  ? 12.952  19.140  -21.387 1.00 39.75  ?  93  VAL B C     1 
ATOM   2970 O  O     . VAL B 1 93  ? 12.871  17.995  -20.931 1.00 40.82  ?  93  VAL B O     1 
ATOM   2971 C  CB    . VAL B 1 93  ? 12.333  20.809  -19.531 1.00 43.16  ?  93  VAL B CB    1 
ATOM   2972 C  CG1   . VAL B 1 93  ? 13.725  21.243  -19.461 1.00 49.78  ?  93  VAL B CG1   1 
ATOM   2973 C  CG2   . VAL B 1 93  ? 11.467  22.019  -19.253 1.00 38.68  ?  93  VAL B CG2   1 
ATOM   2974 N  N     . PHE B 1 94  ? 13.844  19.510  -22.331 1.00 41.50  ?  94  PHE B N     1 
ATOM   2975 C  CA    . PHE B 1 94  ? 14.914  18.650  -22.844 1.00 38.37  ?  94  PHE B CA    1 
ATOM   2976 C  C     . PHE B 1 94  ? 16.110  18.644  -21.891 1.00 42.32  ?  94  PHE B C     1 
ATOM   2977 O  O     . PHE B 1 94  ? 16.551  19.693  -21.414 1.00 46.22  ?  94  PHE B O     1 
ATOM   2978 C  CB    . PHE B 1 94  ? 15.425  19.160  -24.197 1.00 37.98  ?  94  PHE B CB    1 
ATOM   2979 C  CG    . PHE B 1 94  ? 14.537  18.873  -25.399 1.00 34.65  ?  94  PHE B CG    1 
ATOM   2980 C  CD1   . PHE B 1 94  ? 13.537  17.932  -25.368 1.00 34.18  ?  94  PHE B CD1   1 
ATOM   2981 C  CD2   . PHE B 1 94  ? 14.757  19.559  -26.588 1.00 34.70  ?  94  PHE B CD2   1 
ATOM   2982 C  CE1   . PHE B 1 94  ? 12.769  17.691  -26.491 1.00 34.62  ?  94  PHE B CE1   1 
ATOM   2983 C  CE2   . PHE B 1 94  ? 13.995  19.324  -27.709 1.00 31.71  ?  94  PHE B CE2   1 
ATOM   2984 C  CZ    . PHE B 1 94  ? 12.989  18.391  -27.661 1.00 28.36  ?  94  PHE B CZ    1 
ATOM   2985 N  N     . SER B 1 95  ? 16.684  17.478  -21.661 1.00 41.65  ?  95  SER B N     1 
ATOM   2986 C  CA    . SER B 1 95  ? 17.994  17.453  -21.032 1.00 41.80  ?  95  SER B CA    1 
ATOM   2987 C  C     . SER B 1 95  ? 19.047  17.888  -22.056 1.00 41.16  ?  95  SER B C     1 
ATOM   2988 O  O     . SER B 1 95  ? 18.787  17.883  -23.261 1.00 36.54  ?  95  SER B O     1 
ATOM   2989 C  CB    . SER B 1 95  ? 18.291  16.065  -20.465 1.00 39.60  ?  95  SER B CB    1 
ATOM   2990 O  OG    . SER B 1 95  ? 18.733  15.190  -21.465 1.00 38.73  ?  95  SER B OG    1 
ATOM   2991 N  N     . PRO B 1 96  ? 20.212  18.360  -21.603 1.00 44.81  ?  96  PRO B N     1 
ATOM   2992 C  CA    . PRO B 1 96  ? 21.225  18.823  -22.569 1.00 42.41  ?  96  PRO B CA    1 
ATOM   2993 C  C     . PRO B 1 96  ? 21.675  17.744  -23.559 1.00 42.44  ?  96  PRO B C     1 
ATOM   2994 O  O     . PRO B 1 96  ? 22.137  18.107  -24.645 1.00 41.97  ?  96  PRO B O     1 
ATOM   2995 C  CB    . PRO B 1 96  ? 22.387  19.292  -21.680 1.00 44.09  ?  96  PRO B CB    1 
ATOM   2996 C  CG    . PRO B 1 96  ? 21.815  19.532  -20.341 1.00 40.04  ?  96  PRO B CG    1 
ATOM   2997 C  CD    . PRO B 1 96  ? 20.568  18.692  -20.209 1.00 46.81  ?  96  PRO B CD    1 
ATOM   2998 N  N     . GLN B 1 97  ? 21.500  16.446  -23.250 1.00 42.03  ?  97  GLN B N     1 
ATOM   2999 C  CA    . GLN B 1 97  ? 21.882  15.339  -24.127 1.00 43.54  ?  97  GLN B CA    1 
ATOM   3000 C  C     . GLN B 1 97  ? 20.775  14.889  -25.070 1.00 42.90  ?  97  GLN B C     1 
ATOM   3001 O  O     . GLN B 1 97  ? 20.920  13.839  -25.714 1.00 39.89  ?  97  GLN B O     1 
ATOM   3002 C  CB    . GLN B 1 97  ? 22.322  14.122  -23.309 1.00 38.16  ?  97  GLN B CB    1 
ATOM   3003 C  CG    . GLN B 1 97  ? 23.638  14.303  -22.609 1.00 40.04  ?  97  GLN B CG    1 
ATOM   3004 C  CD    . GLN B 1 97  ? 23.535  15.360  -21.545 1.00 53.16  ?  97  GLN B CD    1 
ATOM   3005 O  OE1   . GLN B 1 97  ? 22.428  15.658  -21.055 1.00 51.16  ?  97  GLN B OE1   1 
ATOM   3006 N  NE2   . GLN B 1 97  ? 24.666  15.968  -21.195 1.00 52.37  ?  97  GLN B NE2   1 
ATOM   3007 N  N     . HIS B 1 98  ? 19.669  15.627  -25.154 1.00 43.34  ?  98  HIS B N     1 
ATOM   3008 C  CA    . HIS B 1 98  ? 18.488  15.085  -25.825 1.00 43.45  ?  98  HIS B CA    1 
ATOM   3009 C  C     . HIS B 1 98  ? 18.804  14.729  -27.272 1.00 40.94  ?  98  HIS B C     1 
ATOM   3010 O  O     . HIS B 1 98  ? 18.441  13.641  -27.743 1.00 35.95  ?  98  HIS B O     1 
ATOM   3011 C  CB    . HIS B 1 98  ? 17.321  16.074  -25.743 1.00 34.95  ?  98  HIS B CB    1 
ATOM   3012 C  CG    . HIS B 1 98  ? 15.988  15.452  -26.023 1.00 39.02  ?  98  HIS B CG    1 
ATOM   3013 N  ND1   . HIS B 1 98  ? 15.286  14.731  -25.075 1.00 35.82  ?  98  HIS B ND1   1 
ATOM   3014 C  CD2   . HIS B 1 98  ? 15.220  15.448  -27.143 1.00 37.13  ?  98  HIS B CD2   1 
ATOM   3015 C  CE1   . HIS B 1 98  ? 14.154  14.303  -25.603 1.00 33.35  ?  98  HIS B CE1   1 
ATOM   3016 N  NE2   . HIS B 1 98  ? 14.088  14.721  -26.854 1.00 32.09  ?  98  HIS B NE2   1 
ATOM   3017 N  N     . LEU B 1 99  ? 19.506  15.635  -27.983 1.00 31.98  ?  99  LEU B N     1 
ATOM   3018 C  CA    . LEU B 1 99  ? 19.889  15.405  -29.376 1.00 35.26  ?  99  LEU B CA    1 
ATOM   3019 C  C     . LEU B 1 99  ? 21.158  14.564  -29.471 1.00 35.60  ?  99  LEU B C     1 
ATOM   3020 O  O     . LEU B 1 99  ? 21.182  13.551  -30.175 1.00 39.11  ?  99  LEU B O     1 
ATOM   3021 C  CB    . LEU B 1 99  ? 20.083  16.741  -30.117 1.00 31.81  ?  99  LEU B CB    1 
ATOM   3022 C  CG    . LEU B 1 99  ? 18.829  17.592  -30.351 1.00 37.99  ?  99  LEU B CG    1 
ATOM   3023 C  CD1   . LEU B 1 99  ? 18.972  18.423  -31.612 1.00 31.79  ?  99  LEU B CD1   1 
ATOM   3024 C  CD2   . LEU B 1 99  ? 17.564  16.701  -30.427 1.00 32.88  ?  99  LEU B CD2   1 
ATOM   3025 N  N     . SER B 1 100 ? 22.215  14.960  -28.757 1.00 36.43  ?  100 SER B N     1 
ATOM   3026 C  CA    . SER B 1 100 ? 23.499  14.275  -28.870 1.00 35.55  ?  100 SER B CA    1 
ATOM   3027 C  C     . SER B 1 100 ? 23.408  12.797  -28.511 1.00 35.50  ?  100 SER B C     1 
ATOM   3028 O  O     . SER B 1 100 ? 24.220  12.015  -29.007 1.00 34.30  ?  100 SER B O     1 
ATOM   3029 C  CB    . SER B 1 100 ? 24.551  14.976  -28.010 1.00 33.23  ?  100 SER B CB    1 
ATOM   3030 O  OG    . SER B 1 100 ? 24.296  14.836  -26.632 1.00 46.28  ?  100 SER B OG    1 
ATOM   3031 N  N     . GLY B 1 101 ? 22.392  12.386  -27.730 1.00 34.29  ?  101 GLY B N     1 
ATOM   3032 C  CA    . GLY B 1 101 ? 22.175  10.988  -27.385 1.00 31.60  ?  101 GLY B CA    1 
ATOM   3033 C  C     . GLY B 1 101 ? 21.249  10.175  -28.295 1.00 36.90  ?  101 GLY B C     1 
ATOM   3034 O  O     . GLY B 1 101 ? 21.119  8.962   -28.092 1.00 35.01  ?  101 GLY B O     1 
ATOM   3035 N  N     . THR B 1 102 ? 20.598  10.801  -29.289 1.00 36.51  ?  102 THR B N     1 
ATOM   3036 C  CA    . THR B 1 102 ? 19.615  10.130  -30.142 1.00 33.53  ?  102 THR B CA    1 
ATOM   3037 C  C     . THR B 1 102 ? 19.932  10.283  -31.629 1.00 33.54  ?  102 THR B C     1 
ATOM   3038 O  O     . THR B 1 102 ? 19.623  9.405   -32.449 1.00 28.77  ?  102 THR B O     1 
ATOM   3039 C  CB    . THR B 1 102 ? 18.222  10.693  -29.871 1.00 33.78  ?  102 THR B CB    1 
ATOM   3040 O  OG1   . THR B 1 102 ? 18.173  12.065  -30.307 1.00 34.25  ?  102 THR B OG1   1 
ATOM   3041 C  CG2   . THR B 1 102 ? 17.919  10.633  -28.382 1.00 34.18  ?  102 THR B CG2   1 
ATOM   3042 N  N     . LEU B 1 103 ? 20.530  11.413  -31.986 1.00 32.94  ?  103 LEU B N     1 
ATOM   3043 C  CA    . LEU B 1 103 ? 20.907  11.622  -33.383 1.00 35.32  ?  103 LEU B CA    1 
ATOM   3044 C  C     . LEU B 1 103 ? 21.870  10.567  -33.917 1.00 37.26  ?  103 LEU B C     1 
ATOM   3045 O  O     . LEU B 1 103 ? 21.695  10.146  -35.078 1.00 36.73  ?  103 LEU B O     1 
ATOM   3046 C  CB    . LEU B 1 103 ? 21.475  13.033  -33.559 1.00 32.38  ?  103 LEU B CB    1 
ATOM   3047 C  CG    . LEU B 1 103 ? 20.476  14.148  -33.948 1.00 31.07  ?  103 LEU B CG    1 
ATOM   3048 C  CD1   . LEU B 1 103 ? 21.315  15.396  -34.266 1.00 38.59  ?  103 LEU B CD1   1 
ATOM   3049 C  CD2   . LEU B 1 103 ? 19.634  13.808  -35.185 1.00 28.26  ?  103 LEU B CD2   1 
ATOM   3050 N  N     . PRO B 1 104 ? 22.859  10.074  -33.157 1.00 37.22  ?  104 PRO B N     1 
ATOM   3051 C  CA    . PRO B 1 104 ? 23.711  9.019   -33.718 1.00 32.95  ?  104 PRO B CA    1 
ATOM   3052 C  C     . PRO B 1 104 ? 22.943  7.754   -34.011 1.00 32.68  ?  104 PRO B C     1 
ATOM   3053 O  O     . PRO B 1 104 ? 23.255  7.057   -34.990 1.00 35.98  ?  104 PRO B O     1 
ATOM   3054 C  CB    . PRO B 1 104 ? 24.772  8.798   -32.627 1.00 30.21  ?  104 PRO B CB    1 
ATOM   3055 C  CG    . PRO B 1 104 ? 24.765  10.053  -31.815 1.00 28.66  ?  104 PRO B CG    1 
ATOM   3056 C  CD    . PRO B 1 104 ? 23.308  10.441  -31.795 1.00 38.36  ?  104 PRO B CD    1 
ATOM   3057 N  N     . LEU B 1 105 ? 21.940  7.430   -33.199 1.00 32.01  ?  105 LEU B N     1 
ATOM   3058 C  CA    . LEU B 1 105 ? 21.195  6.224   -33.495 1.00 29.47  ?  105 LEU B CA    1 
ATOM   3059 C  C     . LEU B 1 105 ? 20.364  6.418   -34.762 1.00 34.11  ?  105 LEU B C     1 
ATOM   3060 O  O     . LEU B 1 105 ? 20.205  5.469   -35.556 1.00 29.05  ?  105 LEU B O     1 
ATOM   3061 C  CB    . LEU B 1 105 ? 20.326  5.828   -32.299 1.00 31.81  ?  105 LEU B CB    1 
ATOM   3062 C  CG    . LEU B 1 105 ? 20.898  5.472   -30.916 1.00 38.28  ?  105 LEU B CG    1 
ATOM   3063 C  CD1   . LEU B 1 105 ? 19.732  5.344   -29.861 1.00 32.37  ?  105 LEU B CD1   1 
ATOM   3064 C  CD2   . LEU B 1 105 ? 21.710  4.191   -30.941 1.00 32.52  ?  105 LEU B CD2   1 
ATOM   3065 N  N     . LEU B 1 106 ? 19.858  7.648   -34.992 1.00 34.65  ?  106 LEU B N     1 
ATOM   3066 C  CA    . LEU B 1 106 ? 19.047  7.887   -36.189 1.00 31.61  ?  106 LEU B CA    1 
ATOM   3067 C  C     . LEU B 1 106 ? 19.926  8.000   -37.426 1.00 29.09  ?  106 LEU B C     1 
ATOM   3068 O  O     . LEU B 1 106 ? 19.602  7.436   -38.476 1.00 30.84  ?  106 LEU B O     1 
ATOM   3069 C  CB    . LEU B 1 106 ? 18.168  9.134   -36.030 1.00 28.68  ?  106 LEU B CB    1 
ATOM   3070 C  CG    . LEU B 1 106 ? 17.121  9.032   -34.892 1.00 33.54  ?  106 LEU B CG    1 
ATOM   3071 C  CD1   . LEU B 1 106 ? 16.951  10.386  -34.229 1.00 31.74  ?  106 LEU B CD1   1 
ATOM   3072 C  CD2   . LEU B 1 106 ? 15.749  8.445   -35.337 1.00 25.75  ?  106 LEU B CD2   1 
ATOM   3073 N  N     . LYS B 1 107 ? 21.040  8.714   -37.333 1.00 34.68  ?  107 LYS B N     1 
ATOM   3074 C  CA    . LYS B 1 107 ? 21.981  8.716   -38.458 1.00 36.43  ?  107 LYS B CA    1 
ATOM   3075 C  C     . LYS B 1 107 ? 22.441  7.291   -38.775 1.00 33.29  ?  107 LYS B C     1 
ATOM   3076 O  O     . LYS B 1 107 ? 22.542  6.913   -39.947 1.00 30.26  ?  107 LYS B O     1 
ATOM   3077 C  CB    . LYS B 1 107 ? 23.182  9.622   -38.154 1.00 33.15  ?  107 LYS B CB    1 
ATOM   3078 C  CG    . LYS B 1 107 ? 22.869  11.111  -38.155 1.00 33.00  ?  107 LYS B CG    1 
ATOM   3079 C  CD    . LYS B 1 107 ? 23.889  11.889  -37.304 1.00 38.18  ?  107 LYS B CD    1 
ATOM   3080 C  CE    . LYS B 1 107 ? 24.768  12.781  -38.178 1.00 41.00  ?  107 LYS B CE    1 
ATOM   3081 N  NZ    . LYS B 1 107 ? 25.003  14.141  -37.584 1.00 43.91  ?  107 LYS B NZ    1 
ATOM   3082 N  N     . GLY B 1 108 ? 22.629  6.464   -37.740 1.00 27.77  ?  108 GLY B N     1 
ATOM   3083 C  CA    . GLY B 1 108 ? 23.066  5.087   -37.925 1.00 28.12  ?  108 GLY B CA    1 
ATOM   3084 C  C     . GLY B 1 108 ? 22.052  4.149   -38.565 1.00 28.67  ?  108 GLY B C     1 
ATOM   3085 O  O     . GLY B 1 108 ? 22.424  3.033   -38.925 1.00 28.48  ?  108 GLY B O     1 
ATOM   3086 N  N     . GLY B 1 109 ? 20.794  4.539   -38.720 1.00 33.03  ?  109 GLY B N     1 
ATOM   3087 C  CA    . GLY B 1 109 ? 19.880  3.579   -39.342 1.00 33.98  ?  109 GLY B CA    1 
ATOM   3088 C  C     . GLY B 1 109 ? 18.520  3.394   -38.685 1.00 29.67  ?  109 GLY B C     1 
ATOM   3089 O  O     . GLY B 1 109 ? 17.588  2.872   -39.312 1.00 29.53  ?  109 GLY B O     1 
ATOM   3090 N  N     . ALA B 1 110 ? 18.392  3.828   -37.435 1.00 28.18  ?  110 ALA B N     1 
ATOM   3091 C  CA    . ALA B 1 110 ? 17.081  3.869   -36.793 1.00 34.06  ?  110 ALA B CA    1 
ATOM   3092 C  C     . ALA B 1 110 ? 16.200  4.923   -37.465 1.00 29.36  ?  110 ALA B C     1 
ATOM   3093 O  O     . ALA B 1 110 ? 16.690  5.837   -38.132 1.00 28.87  ?  110 ALA B O     1 
ATOM   3094 C  CB    . ALA B 1 110 ? 17.216  4.172   -35.301 1.00 24.70  ?  110 ALA B CB    1 
ATOM   3095 N  N     . ASP B 1 111 ? 14.874  4.758   -37.317 1.00 29.79  ?  111 ASP B N     1 
ATOM   3096 C  CA    . ASP B 1 111 ? 13.918  5.772   -37.755 1.00 29.05  ?  111 ASP B CA    1 
ATOM   3097 C  C     . ASP B 1 111 ? 13.191  6.458   -36.618 1.00 26.43  ?  111 ASP B C     1 
ATOM   3098 O  O     . ASP B 1 111 ? 12.612  7.512   -36.842 1.00 27.98  ?  111 ASP B O     1 
ATOM   3099 C  CB    . ASP B 1 111 ? 12.878  5.193   -38.711 1.00 25.54  ?  111 ASP B CB    1 
ATOM   3100 C  CG    . ASP B 1 111 ? 13.512  4.438   -39.867 1.00 32.28  ?  111 ASP B CG    1 
ATOM   3101 O  OD1   . ASP B 1 111 ? 14.383  4.987   -40.548 1.00 29.81  ?  111 ASP B OD1   1 
ATOM   3102 O  OD2   . ASP B 1 111 ? 13.157  3.259   -40.076 1.00 38.07  ?  111 ASP B OD2   1 
ATOM   3103 N  N     . PHE B 1 112 ? 13.255  5.925   -35.410 1.00 28.54  ?  112 PHE B N     1 
ATOM   3104 C  CA    . PHE B 1 112 ? 12.429  6.381   -34.298 1.00 27.76  ?  112 PHE B CA    1 
ATOM   3105 C  C     . PHE B 1 112 ? 13.173  6.033   -33.014 1.00 31.47  ?  112 PHE B C     1 
ATOM   3106 O  O     . PHE B 1 112 ? 13.453  4.849   -32.773 1.00 33.68  ?  112 PHE B O     1 
ATOM   3107 C  CB    . PHE B 1 112 ? 11.083  5.661   -34.390 1.00 31.73  ?  112 PHE B CB    1 
ATOM   3108 C  CG    . PHE B 1 112 ? 9.974   6.234   -33.529 1.00 33.08  ?  112 PHE B CG    1 
ATOM   3109 C  CD1   . PHE B 1 112 ? 9.904   5.961   -32.175 1.00 32.90  ?  112 PHE B CD1   1 
ATOM   3110 C  CD2   . PHE B 1 112 ? 8.946   6.982   -34.109 1.00 32.17  ?  112 PHE B CD2   1 
ATOM   3111 C  CE1   . PHE B 1 112 ? 8.838   6.478   -31.395 1.00 29.98  ?  112 PHE B CE1   1 
ATOM   3112 C  CE2   . PHE B 1 112 ? 7.916   7.507   -33.352 1.00 30.05  ?  112 PHE B CE2   1 
ATOM   3113 C  CZ    . PHE B 1 112 ? 7.850   7.237   -31.992 1.00 30.30  ?  112 PHE B CZ    1 
ATOM   3114 N  N     . VAL B 1 113 ? 13.553  7.043   -32.229 1.00 27.43  ?  113 VAL B N     1 
ATOM   3115 C  CA    . VAL B 1 113 ? 14.128  6.856   -30.898 1.00 29.89  ?  113 VAL B CA    1 
ATOM   3116 C  C     . VAL B 1 113 ? 13.167  7.426   -29.859 1.00 32.77  ?  113 VAL B C     1 
ATOM   3117 O  O     . VAL B 1 113 ? 12.672  8.550   -30.020 1.00 35.47  ?  113 VAL B O     1 
ATOM   3118 C  CB    . VAL B 1 113 ? 15.499  7.546   -30.762 1.00 28.51  ?  113 VAL B CB    1 
ATOM   3119 C  CG1   . VAL B 1 113 ? 16.084  7.354   -29.343 1.00 28.40  ?  113 VAL B CG1   1 
ATOM   3120 C  CG2   . VAL B 1 113 ? 16.449  6.971   -31.751 1.00 34.37  ?  113 VAL B CG2   1 
ATOM   3121 N  N     . TYR B 1 114 ? 12.931  6.684   -28.780 1.00 24.74  ?  114 TYR B N     1 
ATOM   3122 C  CA    . TYR B 1 114 ? 12.303  7.266   -27.601 1.00 32.74  ?  114 TYR B CA    1 
ATOM   3123 C  C     . TYR B 1 114 ? 13.262  7.105   -26.425 1.00 35.21  ?  114 TYR B C     1 
ATOM   3124 O  O     . TYR B 1 114 ? 13.991  6.118   -26.347 1.00 32.22  ?  114 TYR B O     1 
ATOM   3125 C  CB    . TYR B 1 114 ? 10.877  6.658   -27.305 1.00 30.39  ?  114 TYR B CB    1 
ATOM   3126 C  CG    . TYR B 1 114 ? 10.855  5.199   -26.948 1.00 33.41  ?  114 TYR B CG    1 
ATOM   3127 C  CD1   . TYR B 1 114 ? 10.806  4.200   -27.944 1.00 32.34  ?  114 TYR B CD1   1 
ATOM   3128 C  CD2   . TYR B 1 114 ? 10.889  4.804   -25.613 1.00 30.89  ?  114 TYR B CD2   1 
ATOM   3129 C  CE1   . TYR B 1 114 ? 10.796  2.827   -27.611 1.00 28.90  ?  114 TYR B CE1   1 
ATOM   3130 C  CE2   . TYR B 1 114 ? 10.887  3.452   -25.270 1.00 32.34  ?  114 TYR B CE2   1 
ATOM   3131 C  CZ    . TYR B 1 114 ? 10.857  2.465   -26.260 1.00 34.57  ?  114 TYR B CZ    1 
ATOM   3132 O  OH    . TYR B 1 114 ? 10.855  1.137   -25.865 1.00 31.30  ?  114 TYR B OH    1 
ATOM   3133 N  N     . VAL B 1 115 ? 13.302  8.104   -25.538 1.00 36.42  ?  115 VAL B N     1 
ATOM   3134 C  CA    . VAL B 1 115 ? 14.221  8.107   -24.396 1.00 34.64  ?  115 VAL B CA    1 
ATOM   3135 C  C     . VAL B 1 115 ? 13.453  7.756   -23.123 1.00 36.48  ?  115 VAL B C     1 
ATOM   3136 O  O     . VAL B 1 115 ? 12.248  7.496   -23.168 1.00 38.36  ?  115 VAL B O     1 
ATOM   3137 C  CB    . VAL B 1 115 ? 14.950  9.465   -24.254 1.00 37.88  ?  115 VAL B CB    1 
ATOM   3138 C  CG1   . VAL B 1 115 ? 15.808  9.747   -25.504 1.00 34.77  ?  115 VAL B CG1   1 
ATOM   3139 C  CG2   . VAL B 1 115 ? 13.964  10.624  -23.990 1.00 32.17  ?  115 VAL B CG2   1 
ATOM   3140 N  N     . ASN B 1 116 ? 14.142  7.733   -21.985 1.00 37.35  ?  116 ASN B N     1 
ATOM   3141 C  CA    . ASN B 1 116 ? 13.499  7.484   -20.700 1.00 36.99  ?  116 ASN B CA    1 
ATOM   3142 C  C     . ASN B 1 116 ? 12.685  8.698   -20.243 1.00 40.76  ?  116 ASN B C     1 
ATOM   3143 O  O     . ASN B 1 116 ? 12.933  9.844   -20.642 1.00 35.57  ?  116 ASN B O     1 
ATOM   3144 C  CB    . ASN B 1 116 ? 14.542  7.132   -19.640 1.00 38.00  ?  116 ASN B CB    1 
ATOM   3145 C  CG    . ASN B 1 116 ? 15.003  5.704   -19.745 1.00 43.17  ?  116 ASN B CG    1 
ATOM   3146 O  OD1   . ASN B 1 116 ? 14.542  4.954   -20.616 1.00 41.11  ?  116 ASN B OD1   1 
ATOM   3147 N  ND2   . ASN B 1 116 ? 15.904  5.302   -18.848 1.00 46.76  ?  116 ASN B ND2   1 
ATOM   3148 N  N     . ILE B 1 117 ? 11.692  8.432   -19.388 1.00 45.07  ?  117 ILE B N     1 
ATOM   3149 C  CA    . ILE B 1 117 ? 10.774  9.467   -18.921 1.00 47.40  ?  117 ILE B CA    1 
ATOM   3150 C  C     . ILE B 1 117 ? 10.753  9.526   -17.400 1.00 47.19  ?  117 ILE B C     1 
ATOM   3151 O  O     . ILE B 1 117 ? 10.534  8.506   -16.739 1.00 45.18  ?  117 ILE B O     1 
ATOM   3152 C  CB    . ILE B 1 117 ? 9.349   9.260   -19.462 1.00 45.00  ?  117 ILE B CB    1 
ATOM   3153 C  CG1   . ILE B 1 117 ? 9.405   9.014   -20.975 1.00 41.44  ?  117 ILE B CG1   1 
ATOM   3154 C  CG2   . ILE B 1 117 ? 8.452   10.436  -19.040 1.00 47.89  ?  117 ILE B CG2   1 
ATOM   3155 C  CD1   . ILE B 1 117 ? 8.082   9.094   -21.711 1.00 36.39  ?  117 ILE B CD1   1 
ATOM   3156 N  N     . ASN B 1 118 ? 10.990  10.724  -16.854 1.00 46.62  ?  118 ASN B N     1 
ATOM   3157 C  CA    . ASN B 1 118 ? 10.634  11.071  -15.478 1.00 51.41  ?  118 ASN B CA    1 
ATOM   3158 C  C     . ASN B 1 118 ? 9.354   11.903  -15.502 1.00 55.00  ?  118 ASN B C     1 
ATOM   3159 O  O     . ASN B 1 118 ? 9.351   13.045  -15.992 1.00 47.87  ?  118 ASN B O     1 
ATOM   3160 C  CB    . ASN B 1 118 ? 11.735  11.868  -14.781 1.00 49.75  ?  118 ASN B CB    1 
ATOM   3161 C  CG    . ASN B 1 118 ? 13.141  11.312  -15.019 1.00 53.47  ?  118 ASN B CG    1 
ATOM   3162 O  OD1   . ASN B 1 118 ? 13.352  10.102  -15.071 1.00 49.10  ?  118 ASN B OD1   1 
ATOM   3163 N  ND2   . ASN B 1 118 ? 14.113  12.219  -15.174 1.00 54.93  ?  118 ASN B ND2   1 
ATOM   3164 N  N     . ILE B 1 119 ? 8.278   11.343  -14.954 1.00 61.29  ?  119 ILE B N     1 
ATOM   3165 C  CA    . ILE B 1 119 ? 7.044   12.090  -14.687 1.00 60.96  ?  119 ILE B CA    1 
ATOM   3166 C  C     . ILE B 1 119 ? 7.252   12.921  -13.426 1.00 63.60  ?  119 ILE B C     1 
ATOM   3167 O  O     . ILE B 1 119 ? 7.103   12.408  -12.312 1.00 60.78  ?  119 ILE B O     1 
ATOM   3168 C  CB    . ILE B 1 119 ? 5.845   11.162  -14.533 1.00 59.63  ?  119 ILE B CB    1 
ATOM   3169 C  CG1   . ILE B 1 119 ? 5.742   10.205  -15.718 1.00 54.88  ?  119 ILE B CG1   1 
ATOM   3170 C  CG2   . ILE B 1 119 ? 4.602   11.968  -14.319 1.00 64.87  ?  119 ILE B CG2   1 
ATOM   3171 C  CD1   . ILE B 1 119 ? 4.457   9.395   -15.716 1.00 55.73  ?  119 ILE B CD1   1 
ATOM   3172 N  N     . ALA B 1 120 ? 7.583   14.203  -13.590 1.00 59.16  ?  120 ALA B N     1 
ATOM   3173 C  CA    . ALA B 1 120 ? 7.671   15.123  -12.449 1.00 67.14  ?  120 ALA B CA    1 
ATOM   3174 C  C     . ALA B 1 120 ? 6.377   15.951  -12.282 1.00 65.34  ?  120 ALA B C     1 
ATOM   3175 O  O     . ALA B 1 120 ? 6.298   16.892  -11.485 1.00 62.95  ?  120 ALA B O     1 
ATOM   3176 C  CB    . ALA B 1 120 ? 8.877   16.032  -12.603 1.00 61.64  ?  120 ALA B CB    1 
ATOM   3177 N  N     . GLY B 1 126 ? 15.588  22.756  -17.797 1.00 53.58  ?  126 GLY B N     1 
ATOM   3178 C  CA    . GLY B 1 126 ? 16.509  22.341  -18.856 1.00 61.73  ?  126 GLY B CA    1 
ATOM   3179 C  C     . GLY B 1 126 ? 17.882  21.843  -18.402 1.00 67.34  ?  126 GLY B C     1 
ATOM   3180 O  O     . GLY B 1 126 ? 18.292  20.715  -18.719 1.00 62.49  ?  126 GLY B O     1 
ATOM   3181 N  N     . THR B 1 127 ? 18.595  22.707  -17.666 1.00 70.05  ?  127 THR B N     1 
ATOM   3182 C  CA    . THR B 1 127 ? 19.882  22.357  -17.073 1.00 69.45  ?  127 THR B CA    1 
ATOM   3183 C  C     . THR B 1 127 ? 19.727  21.562  -15.778 1.00 73.68  ?  127 THR B C     1 
ATOM   3184 O  O     . THR B 1 127 ? 20.614  20.767  -15.438 1.00 75.67  ?  127 THR B O     1 
ATOM   3185 C  CB    . THR B 1 127 ? 20.701  23.634  -16.818 1.00 72.24  ?  127 THR B CB    1 
ATOM   3186 O  OG1   . THR B 1 127 ? 20.381  24.192  -15.530 1.00 74.68  ?  127 THR B OG1   1 
ATOM   3187 C  CG2   . THR B 1 127 ? 20.411  24.676  -17.886 1.00 69.30  ?  127 THR B CG2   1 
ATOM   3188 N  N     . THR B 1 128 ? 18.603  21.737  -15.072 1.00 75.93  ?  128 THR B N     1 
ATOM   3189 C  CA    . THR B 1 128 ? 18.406  21.241  -13.710 1.00 77.34  ?  128 THR B CA    1 
ATOM   3190 C  C     . THR B 1 128 ? 17.362  20.126  -13.621 1.00 73.81  ?  128 THR B C     1 
ATOM   3191 O  O     . THR B 1 128 ? 16.615  20.053  -12.647 1.00 78.59  ?  128 THR B O     1 
ATOM   3192 C  CB    . THR B 1 128 ? 18.001  22.388  -12.775 1.00 80.91  ?  128 THR B CB    1 
ATOM   3193 O  OG1   . THR B 1 128 ? 16.738  22.936  -13.184 1.00 75.68  ?  128 THR B OG1   1 
ATOM   3194 C  CG2   . THR B 1 128 ? 19.044  23.511  -12.791 1.00 76.94  ?  128 THR B CG2   1 
ATOM   3195 N  N     . ILE B 1 129 ? 17.303  19.227  -14.613 1.00 74.23  ?  129 ILE B N     1 
ATOM   3196 C  CA    . ILE B 1 129 ? 16.301  18.151  -14.586 1.00 76.91  ?  129 ILE B CA    1 
ATOM   3197 C  C     . ILE B 1 129 ? 16.445  17.248  -13.360 1.00 83.12  ?  129 ILE B C     1 
ATOM   3198 O  O     . ILE B 1 129 ? 15.437  16.763  -12.817 1.00 85.17  ?  129 ILE B O     1 
ATOM   3199 C  CB    . ILE B 1 129 ? 16.341  17.325  -15.893 1.00 71.02  ?  129 ILE B CB    1 
ATOM   3200 C  CG1   . ILE B 1 129 ? 15.596  18.058  -17.006 1.00 64.02  ?  129 ILE B CG1   1 
ATOM   3201 C  CG2   . ILE B 1 129 ? 15.791  15.893  -15.706 1.00 66.11  ?  129 ILE B CG2   1 
ATOM   3202 C  CD1   . ILE B 1 129 ? 15.579  17.301  -18.298 1.00 57.35  ?  129 ILE B CD1   1 
ATOM   3203 N  N     . ALA B 1 130 ? 17.679  16.996  -12.904 1.00 84.86  ?  130 ALA B N     1 
ATOM   3204 C  CA    . ALA B 1 130 ? 17.868  16.136  -11.738 1.00 84.56  ?  130 ALA B CA    1 
ATOM   3205 C  C     . ALA B 1 130 ? 17.170  16.703  -10.504 1.00 87.19  ?  130 ALA B C     1 
ATOM   3206 O  O     . ALA B 1 130 ? 16.703  15.935  -9.651  1.00 89.01  ?  130 ALA B O     1 
ATOM   3207 C  CB    . ALA B 1 130 ? 19.360  15.924  -11.465 1.00 78.18  ?  130 ALA B CB    1 
ATOM   3208 N  N     . ASP B 1 131 ? 17.056  18.038  -10.412 1.00 83.11  ?  131 ASP B N     1 
ATOM   3209 C  CA    . ASP B 1 131 ? 16.383  18.681  -9.284  1.00 82.91  ?  131 ASP B CA    1 
ATOM   3210 C  C     . ASP B 1 131 ? 14.896  18.326  -9.196  1.00 87.88  ?  131 ASP B C     1 
ATOM   3211 O  O     . ASP B 1 131 ? 14.277  18.564  -8.150  1.00 90.85  ?  131 ASP B O     1 
ATOM   3212 C  CB    . ASP B 1 131 ? 16.524  20.209  -9.374  1.00 83.14  ?  131 ASP B CB    1 
ATOM   3213 C  CG    . ASP B 1 131 ? 17.896  20.722  -8.924  1.00 79.03  ?  131 ASP B CG    1 
ATOM   3214 O  OD1   . ASP B 1 131 ? 18.701  19.934  -8.376  1.00 67.64  ?  131 ASP B OD1   1 
ATOM   3215 O  OD2   . ASP B 1 131 ? 18.150  21.938  -9.107  1.00 75.90  ?  131 ASP B OD2   1 
ATOM   3216 N  N     . ALA B 1 132 ? 14.304  17.781  -10.261 1.00 88.07  ?  132 ALA B N     1 
ATOM   3217 C  CA    . ALA B 1 132 ? 12.879  17.465  -10.248 1.00 84.88  ?  132 ALA B CA    1 
ATOM   3218 C  C     . ALA B 1 132 ? 12.590  16.322  -9.280  1.00 84.17  ?  132 ALA B C     1 
ATOM   3219 O  O     . ALA B 1 132 ? 13.356  15.359  -9.179  1.00 87.65  ?  132 ALA B O     1 
ATOM   3220 C  CB    . ALA B 1 132 ? 12.393  17.099  -11.656 1.00 76.40  ?  132 ALA B CB    1 
ATOM   3221 N  N     . GLU B 1 133 ? 11.491  16.448  -8.541  1.00 74.91  ?  133 GLU B N     1 
ATOM   3222 C  CA    . GLU B 1 133 ? 10.953  15.317  -7.805  1.00 75.61  ?  133 GLU B CA    1 
ATOM   3223 C  C     . GLU B 1 133 ? 10.129  14.451  -8.757  1.00 75.45  ?  133 GLU B C     1 
ATOM   3224 O  O     . GLU B 1 133 ? 9.379   14.964  -9.596  1.00 74.13  ?  133 GLU B O     1 
ATOM   3225 C  CB    . GLU B 1 133 ? 10.105  15.800  -6.623  1.00 75.58  ?  133 GLU B CB    1 
ATOM   3226 N  N     . VAL B 1 134 ? 10.292  13.131  -8.644  1.00 75.68  ?  134 VAL B N     1 
ATOM   3227 C  CA    . VAL B 1 134 ? 9.665   12.185  -9.568  1.00 72.86  ?  134 VAL B CA    1 
ATOM   3228 C  C     . VAL B 1 134 ? 9.474   10.827  -8.890  1.00 73.09  ?  134 VAL B C     1 
ATOM   3229 O  O     . VAL B 1 134 ? 10.418  10.265  -8.323  1.00 75.50  ?  134 VAL B O     1 
ATOM   3230 C  CB    . VAL B 1 134 ? 10.505  12.049  -10.856 1.00 69.82  ?  134 VAL B CB    1 
ATOM   3231 N  N     . LEU B 1 135 ? 8.257   10.279  -8.941  1.00 70.69  ?  135 LEU B N     1 
ATOM   3232 C  CA    . LEU B 1 135 ? 7.981   8.978   -8.345  1.00 65.90  ?  135 LEU B CA    1 
ATOM   3233 C  C     . LEU B 1 135 ? 7.685   7.908   -9.384  1.00 66.46  ?  135 LEU B C     1 
ATOM   3234 O  O     . LEU B 1 135 ? 7.467   6.749   -9.015  1.00 71.76  ?  135 LEU B O     1 
ATOM   3235 C  CB    . LEU B 1 135 ? 6.819   9.072   -7.345  1.00 66.81  ?  135 LEU B CB    1 
ATOM   3236 N  N     . VAL B 1 136 ? 7.693   8.251   -10.671 1.00 65.35  ?  136 VAL B N     1 
ATOM   3237 C  CA    . VAL B 1 136 ? 7.492   7.272   -11.738 1.00 65.97  ?  136 VAL B CA    1 
ATOM   3238 C  C     . VAL B 1 136 ? 8.467   7.536   -12.875 1.00 57.02  ?  136 VAL B C     1 
ATOM   3239 O  O     . VAL B 1 136 ? 8.590   8.668   -13.359 1.00 49.94  ?  136 VAL B O     1 
ATOM   3240 C  CB    . VAL B 1 136 ? 6.042   7.269   -12.257 1.00 63.52  ?  136 VAL B CB    1 
ATOM   3241 C  CG1   . VAL B 1 136 ? 5.198   6.426   -11.356 1.00 66.62  ?  136 VAL B CG1   1 
ATOM   3242 C  CG2   . VAL B 1 136 ? 5.491   8.684   -12.267 1.00 63.63  ?  136 VAL B CG2   1 
ATOM   3243 N  N     . ARG B 1 137 ? 9.150   6.479   -13.302 1.00 57.38  ?  137 ARG B N     1 
ATOM   3244 C  CA    . ARG B 1 137 ? 10.041  6.503   -14.449 1.00 55.53  ?  137 ARG B CA    1 
ATOM   3245 C  C     . ARG B 1 137 ? 9.517   5.520   -15.484 1.00 52.33  ?  137 ARG B C     1 
ATOM   3246 O  O     . ARG B 1 137 ? 9.281   4.354   -15.159 1.00 54.92  ?  137 ARG B O     1 
ATOM   3247 C  CB    . ARG B 1 137 ? 11.463  6.118   -14.039 1.00 59.52  ?  137 ARG B CB    1 
ATOM   3248 C  CG    . ARG B 1 137 ? 12.279  7.249   -13.420 1.00 62.78  ?  137 ARG B CG    1 
ATOM   3249 C  CD    . ARG B 1 137 ? 13.415  6.697   -12.552 1.00 65.96  ?  137 ARG B CD    1 
ATOM   3250 N  NE    . ARG B 1 137 ? 12.869  6.058   -11.363 1.00 72.84  ?  137 ARG B NE    1 
ATOM   3251 C  CZ    . ARG B 1 137 ? 12.509  6.711   -10.265 1.00 75.21  ?  137 ARG B CZ    1 
ATOM   3252 N  NH1   . ARG B 1 137 ? 12.750  8.009   -10.124 1.00 71.75  ?  137 ARG B NH1   1 
ATOM   3253 N  NH2   . ARG B 1 137 ? 11.886  6.047   -9.286  1.00 70.50  ?  137 ARG B NH2   1 
ATOM   3254 N  N     . LEU B 1 138 ? 9.330   5.980   -16.719 1.00 46.12  ?  138 LEU B N     1 
ATOM   3255 C  CA    . LEU B 1 138 ? 8.980   5.102   -17.840 1.00 43.53  ?  138 LEU B CA    1 
ATOM   3256 C  C     . LEU B 1 138 ? 10.267  4.776   -18.611 1.00 41.24  ?  138 LEU B C     1 
ATOM   3257 O  O     . LEU B 1 138 ? 10.857  5.665   -19.243 1.00 42.40  ?  138 LEU B O     1 
ATOM   3258 C  CB    . LEU B 1 138 ? 7.926   5.754   -18.740 1.00 37.28  ?  138 LEU B CB    1 
ATOM   3259 C  CG    . LEU B 1 138 ? 6.590   6.254   -18.111 1.00 44.96  ?  138 LEU B CG    1 
ATOM   3260 C  CD1   . LEU B 1 138 ? 6.133   7.640   -18.620 1.00 38.86  ?  138 LEU B CD1   1 
ATOM   3261 C  CD2   . LEU B 1 138 ? 5.494   5.297   -18.350 1.00 36.84  ?  138 LEU B CD2   1 
ATOM   3262 N  N     . GLU B 1 139 ? 10.727  3.502   -18.531 1.00 40.75  ?  139 GLU B N     1 
ATOM   3263 C  CA    . GLU B 1 139 ? 12.005  3.094   -19.122 1.00 42.93  ?  139 GLU B CA    1 
ATOM   3264 C  C     . GLU B 1 139 ? 11.916  1.731   -19.827 1.00 42.07  ?  139 GLU B C     1 
ATOM   3265 O  O     . GLU B 1 139 ? 12.930  1.038   -19.969 1.00 42.89  ?  139 GLU B O     1 
ATOM   3266 C  CB    . GLU B 1 139 ? 13.140  3.062   -18.062 1.00 43.03  ?  139 GLU B CB    1 
ATOM   3267 C  CG    . GLU B 1 139 ? 12.909  3.962   -16.817 1.00 47.05  ?  139 GLU B CG    1 
ATOM   3268 C  CD    . GLU B 1 139 ? 14.166  4.253   -15.976 1.00 56.37  ?  139 GLU B CD    1 
ATOM   3269 O  OE1   . GLU B 1 139 ? 14.959  3.317   -15.719 1.00 63.00  ?  139 GLU B OE1   1 
ATOM   3270 O  OE2   . GLU B 1 139 ? 14.354  5.428   -15.552 1.00 53.50  ?  139 GLU B OE2   1 
ATOM   3271 N  N     . PHE B 1 140 ? 10.737  1.350   -20.308 1.00 42.37  ?  140 PHE B N     1 
ATOM   3272 C  CA    . PHE B 1 140 ? 10.519  0.049   -20.954 1.00 41.92  ?  140 PHE B CA    1 
ATOM   3273 C  C     . PHE B 1 140 ? 11.357  -0.136  -22.219 1.00 42.95  ?  140 PHE B C     1 
ATOM   3274 O  O     . PHE B 1 140 ? 11.237  0.664   -23.155 1.00 43.57  ?  140 PHE B O     1 
ATOM   3275 C  CB    . PHE B 1 140 ? 9.043   -0.105  -21.314 1.00 36.93  ?  140 PHE B CB    1 
ATOM   3276 C  CG    . PHE B 1 140 ? 8.137   -0.085  -20.116 1.00 40.90  ?  140 PHE B CG    1 
ATOM   3277 C  CD1   . PHE B 1 140 ? 8.184   -1.109  -19.182 1.00 41.48  ?  140 PHE B CD1   1 
ATOM   3278 C  CD2   . PHE B 1 140 ? 7.254   0.962   -19.918 1.00 39.93  ?  140 PHE B CD2   1 
ATOM   3279 C  CE1   . PHE B 1 140 ? 7.371   -1.084  -18.073 1.00 45.47  ?  140 PHE B CE1   1 
ATOM   3280 C  CE2   . PHE B 1 140 ? 6.439   0.998   -18.828 1.00 40.50  ?  140 PHE B CE2   1 
ATOM   3281 C  CZ    . PHE B 1 140 ? 6.491   -0.025  -17.895 1.00 46.79  ?  140 PHE B CZ    1 
ATOM   3282 N  N     . PRO B 1 141 ? 12.169  -1.182  -22.312 1.00 42.21  ?  141 PRO B N     1 
ATOM   3283 C  CA    . PRO B 1 141 ? 12.808  -1.496  -23.599 1.00 43.87  ?  141 PRO B CA    1 
ATOM   3284 C  C     . PRO B 1 141 ? 11.770  -1.888  -24.649 1.00 42.05  ?  141 PRO B C     1 
ATOM   3285 O  O     . PRO B 1 141 ? 10.631  -2.249  -24.342 1.00 42.10  ?  141 PRO B O     1 
ATOM   3286 C  CB    . PRO B 1 141 ? 13.737  -2.669  -23.263 1.00 43.38  ?  141 PRO B CB    1 
ATOM   3287 C  CG    . PRO B 1 141 ? 13.700  -2.786  -21.741 1.00 45.70  ?  141 PRO B CG    1 
ATOM   3288 C  CD    . PRO B 1 141 ? 12.429  -2.198  -21.289 1.00 39.66  ?  141 PRO B CD    1 
ATOM   3289 N  N     . TYR B 1 142 ? 12.175  -1.803  -25.913 1.00 40.88  ?  142 TYR B N     1 
ATOM   3290 C  CA    . TYR B 1 142 ? 11.253  -2.073  -27.021 1.00 39.08  ?  142 TYR B CA    1 
ATOM   3291 C  C     . TYR B 1 142 ? 11.294  -3.534  -27.451 1.00 43.55  ?  142 TYR B C     1 
ATOM   3292 O  O     . TYR B 1 142 ? 11.367  -3.836  -28.647 1.00 45.13  ?  142 TYR B O     1 
ATOM   3293 C  CB    . TYR B 1 142 ? 11.583  -1.168  -28.201 1.00 34.35  ?  142 TYR B CB    1 
ATOM   3294 C  CG    . TYR B 1 142 ? 10.482  -1.061  -29.222 1.00 34.34  ?  142 TYR B CG    1 
ATOM   3295 C  CD1   . TYR B 1 142 ? 9.316   -0.370  -28.935 1.00 28.96  ?  142 TYR B CD1   1 
ATOM   3296 C  CD2   . TYR B 1 142 ? 10.620  -1.623  -30.488 1.00 35.59  ?  142 TYR B CD2   1 
ATOM   3297 C  CE1   . TYR B 1 142 ? 8.337   -0.246  -29.870 1.00 24.96  ?  142 TYR B CE1   1 
ATOM   3298 C  CE2   . TYR B 1 142 ? 9.621   -1.523  -31.427 1.00 33.20  ?  142 TYR B CE2   1 
ATOM   3299 C  CZ    . TYR B 1 142 ? 8.473   -0.834  -31.105 1.00 32.56  ?  142 TYR B CZ    1 
ATOM   3300 O  OH    . TYR B 1 142 ? 7.454   -0.702  -32.041 1.00 34.40  ?  142 TYR B OH    1 
ATOM   3301 N  N     . ASP B 1 143 ? 11.265  -4.476  -26.512 1.00 40.34  ?  143 ASP B N     1 
ATOM   3302 C  CA    . ASP B 1 143 ? 11.528  -5.853  -26.909 1.00 44.46  ?  143 ASP B CA    1 
ATOM   3303 C  C     . ASP B 1 143 ? 10.333  -6.774  -26.715 1.00 43.43  ?  143 ASP B C     1 
ATOM   3304 O  O     . ASP B 1 143 ? 10.472  -7.983  -26.897 1.00 44.96  ?  143 ASP B O     1 
ATOM   3305 C  CB    . ASP B 1 143 ? 12.755  -6.400  -26.172 1.00 39.96  ?  143 ASP B CB    1 
ATOM   3306 C  CG    . ASP B 1 143 ? 12.529  -6.559  -24.679 1.00 46.46  ?  143 ASP B CG    1 
ATOM   3307 O  OD1   . ASP B 1 143 ? 11.837  -5.715  -24.068 1.00 44.50  ?  143 ASP B OD1   1 
ATOM   3308 O  OD2   . ASP B 1 143 ? 13.057  -7.537  -24.110 1.00 51.26  ?  143 ASP B OD2   1 
ATOM   3309 N  N     . ARG B 1 144 ? 9.165   -6.249  -26.360 1.00 44.44  ?  144 ARG B N     1 
ATOM   3310 C  CA    . ARG B 1 144 ? 8.036   -7.127  -26.074 1.00 39.14  ?  144 ARG B CA    1 
ATOM   3311 C  C     . ARG B 1 144 ? 6.734   -6.728  -26.754 1.00 37.82  ?  144 ARG B C     1 
ATOM   3312 O  O     . ARG B 1 144 ? 5.752   -7.458  -26.615 1.00 37.80  ?  144 ARG B O     1 
ATOM   3313 C  CB    . ARG B 1 144 ? 7.807   -7.225  -24.562 1.00 38.35  ?  144 ARG B CB    1 
ATOM   3314 C  CG    . ARG B 1 144 ? 8.620   -8.322  -23.882 1.00 45.78  ?  144 ARG B CG    1 
ATOM   3315 C  CD    . ARG B 1 144 ? 8.586   -8.167  -22.379 1.00 41.89  ?  144 ARG B CD    1 
ATOM   3316 N  NE    . ARG B 1 144 ? 9.835   -8.544  -21.727 1.00 47.68  ?  144 ARG B NE    1 
ATOM   3317 C  CZ    . ARG B 1 144 ? 9.896   -9.075  -20.512 1.00 50.66  ?  144 ARG B CZ    1 
ATOM   3318 N  NH1   . ARG B 1 144 ? 8.800   -9.304  -19.809 1.00 54.10  ?  144 ARG B NH1   1 
ATOM   3319 N  NH2   . ARG B 1 144 ? 11.084  -9.378  -19.988 1.00 47.92  ?  144 ARG B NH2   1 
ATOM   3320 N  N     . GLY B 1 145 ? 6.698   -5.621  -27.506 1.00 36.01  ?  145 GLY B N     1 
ATOM   3321 C  CA    . GLY B 1 145 ? 5.455   -5.211  -28.140 1.00 39.19  ?  145 GLY B CA    1 
ATOM   3322 C  C     . GLY B 1 145 ? 4.489   -4.453  -27.240 1.00 37.23  ?  145 GLY B C     1 
ATOM   3323 O  O     . GLY B 1 145 ? 3.293   -4.383  -27.553 1.00 32.34  ?  145 GLY B O     1 
ATOM   3324 N  N     . LEU B 1 146 ? 4.983   -3.870  -26.139 1.00 30.58  ?  146 LEU B N     1 
ATOM   3325 C  CA    . LEU B 1 146 ? 4.114   -3.143  -25.236 1.00 29.64  ?  146 LEU B CA    1 
ATOM   3326 C  C     . LEU B 1 146 ? 3.403   -2.023  -25.967 1.00 32.85  ?  146 LEU B C     1 
ATOM   3327 O  O     . LEU B 1 146 ? 2.224   -1.749  -25.705 1.00 32.77  ?  146 LEU B O     1 
ATOM   3328 C  CB    . LEU B 1 146 ? 4.914   -2.600  -24.045 1.00 32.75  ?  146 LEU B CB    1 
ATOM   3329 C  CG    . LEU B 1 146 ? 4.100   -1.819  -22.982 1.00 30.26  ?  146 LEU B CG    1 
ATOM   3330 C  CD1   . LEU B 1 146 ? 3.084   -2.725  -22.326 1.00 34.82  ?  146 LEU B CD1   1 
ATOM   3331 C  CD2   . LEU B 1 146 ? 5.019   -1.204  -21.915 1.00 33.65  ?  146 LEU B CD2   1 
ATOM   3332 N  N     . LEU B 1 147 ? 4.100   -1.374  -26.900 1.00 33.48  ?  147 LEU B N     1 
ATOM   3333 C  CA    . LEU B 1 147 ? 3.499   -0.283  -27.656 1.00 32.79  ?  147 LEU B CA    1 
ATOM   3334 C  C     . LEU B 1 147 ? 2.259   -0.753  -28.398 1.00 37.11  ?  147 LEU B C     1 
ATOM   3335 O  O     . LEU B 1 147 ? 1.345   0.054   -28.645 1.00 34.55  ?  147 LEU B O     1 
ATOM   3336 C  CB    . LEU B 1 147 ? 4.505   0.310   -28.639 1.00 27.80  ?  147 LEU B CB    1 
ATOM   3337 C  CG    . LEU B 1 147 ? 3.986   1.559   -29.360 1.00 30.04  ?  147 LEU B CG    1 
ATOM   3338 C  CD1   . LEU B 1 147 ? 3.677   2.633   -28.334 1.00 29.71  ?  147 LEU B CD1   1 
ATOM   3339 C  CD2   . LEU B 1 147 ? 5.027   2.073   -30.325 1.00 30.04  ?  147 LEU B CD2   1 
ATOM   3340 N  N     . ASP B 1 148 ? 2.206   -2.058  -28.737 1.00 29.79  ?  148 ASP B N     1 
ATOM   3341 C  CA    . ASP B 1 148 ? 1.056   -2.643  -29.404 1.00 33.69  ?  148 ASP B CA    1 
ATOM   3342 C  C     . ASP B 1 148 ? -0.143  -2.793  -28.459 1.00 38.91  ?  148 ASP B C     1 
ATOM   3343 O  O     . ASP B 1 148 ? -1.287  -2.916  -28.924 1.00 33.67  ?  148 ASP B O     1 
ATOM   3344 C  CB    . ASP B 1 148 ? 1.448   -3.999  -29.984 1.00 32.08  ?  148 ASP B CB    1 
ATOM   3345 C  CG    . ASP B 1 148 ? 1.718   -3.940  -31.470 1.00 44.89  ?  148 ASP B CG    1 
ATOM   3346 O  OD1   . ASP B 1 148 ? 2.061   -2.847  -31.958 1.00 44.57  ?  148 ASP B OD1   1 
ATOM   3347 O  OD2   . ASP B 1 148 ? 1.615   -4.984  -32.160 1.00 48.93  ?  148 ASP B OD2   1 
ATOM   3348 N  N     . VAL B 1 149 ? 0.102   -2.794  -27.152 1.00 32.39  ?  149 VAL B N     1 
ATOM   3349 C  CA    . VAL B 1 149 ? -0.950  -3.006  -26.180 1.00 37.98  ?  149 VAL B CA    1 
ATOM   3350 C  C     . VAL B 1 149 ? -1.606  -1.692  -25.797 1.00 34.08  ?  149 VAL B C     1 
ATOM   3351 O  O     . VAL B 1 149 ? -2.834  -1.586  -25.765 1.00 32.95  ?  149 VAL B O     1 
ATOM   3352 C  CB    . VAL B 1 149 ? -0.368  -3.723  -24.952 1.00 34.49  ?  149 VAL B CB    1 
ATOM   3353 C  CG1   . VAL B 1 149 ? -1.459  -3.933  -23.930 1.00 38.42  ?  149 VAL B CG1   1 
ATOM   3354 C  CG2   . VAL B 1 149 ? 0.239   -5.027  -25.377 1.00 35.77  ?  149 VAL B CG2   1 
ATOM   3355 N  N     . THR B 1 150 ? -0.782  -0.672  -25.593 1.00 34.40  ?  150 THR B N     1 
ATOM   3356 C  CA    . THR B 1 150 ? -1.209  0.614   -25.072 1.00 37.49  ?  150 THR B CA    1 
ATOM   3357 C  C     . THR B 1 150 ? 0.027   1.504   -25.069 1.00 32.41  ?  150 THR B C     1 
ATOM   3358 O  O     . THR B 1 150 ? 1.143   0.990   -24.991 1.00 36.12  ?  150 THR B O     1 
ATOM   3359 C  CB    . THR B 1 150 ? -1.830  0.429   -23.673 1.00 39.07  ?  150 THR B CB    1 
ATOM   3360 O  OG1   . THR B 1 150 ? -2.568  1.598   -23.284 1.00 38.91  ?  150 THR B OG1   1 
ATOM   3361 C  CG2   . THR B 1 150 ? -0.741  0.098   -22.647 1.00 34.60  ?  150 THR B CG2   1 
ATOM   3362 N  N     . ASN B 1 151 ? -0.140  2.815   -25.192 1.00 33.78  ?  151 ASN B N     1 
ATOM   3363 C  CA    . ASN B 1 151 ? 1.009   3.705   -25.312 1.00 37.13  ?  151 ASN B CA    1 
ATOM   3364 C  C     . ASN B 1 151 ? 1.899   3.645   -24.066 1.00 34.43  ?  151 ASN B C     1 
ATOM   3365 O  O     . ASN B 1 151 ? 1.424   3.434   -22.950 1.00 34.12  ?  151 ASN B O     1 
ATOM   3366 C  CB    . ASN B 1 151 ? 0.546   5.139   -25.552 1.00 31.81  ?  151 ASN B CB    1 
ATOM   3367 C  CG    . ASN B 1 151 ? 1.621   5.969   -26.202 1.00 35.75  ?  151 ASN B CG    1 
ATOM   3368 O  OD1   . ASN B 1 151 ? 2.759   5.511   -26.322 1.00 36.88  ?  151 ASN B OD1   1 
ATOM   3369 N  ND2   . ASN B 1 151 ? 1.293   7.204   -26.594 1.00 35.78  ?  151 ASN B ND2   1 
ATOM   3370 N  N     . HIS B 1 152 ? 3.221   3.823   -24.263 1.00 30.53  ?  152 HIS B N     1 
ATOM   3371 C  CA    . HIS B 1 152 ? 4.091   3.846   -23.091 1.00 32.77  ?  152 HIS B CA    1 
ATOM   3372 C  C     . HIS B 1 152 ? 5.154   4.938   -23.175 1.00 32.43  ?  152 HIS B C     1 
ATOM   3373 O  O     . HIS B 1 152 ? 6.107   4.914   -22.392 1.00 31.23  ?  152 HIS B O     1 
ATOM   3374 C  CB    . HIS B 1 152 ? 4.728   2.458   -22.788 1.00 34.68  ?  152 HIS B CB    1 
ATOM   3375 C  CG    . HIS B 1 152 ? 5.742   1.954   -23.785 1.00 35.68  ?  152 HIS B CG    1 
ATOM   3376 N  ND1   . HIS B 1 152 ? 7.107   2.093   -23.601 1.00 37.53  ?  152 HIS B ND1   1 
ATOM   3377 C  CD2   . HIS B 1 152 ? 5.596   1.210   -24.912 1.00 36.02  ?  152 HIS B CD2   1 
ATOM   3378 C  CE1   . HIS B 1 152 ? 7.752   1.507   -24.599 1.00 32.12  ?  152 HIS B CE1   1 
ATOM   3379 N  NE2   . HIS B 1 152 ? 6.859   0.952   -25.401 1.00 32.10  ?  152 HIS B NE2   1 
ATOM   3380 N  N     . PHE B 1 153 ? 4.981   5.921   -24.056 1.00 28.84  ?  153 PHE B N     1 
ATOM   3381 C  CA    . PHE B 1 153 ? 5.780   7.149   -23.998 1.00 30.60  ?  153 PHE B CA    1 
ATOM   3382 C  C     . PHE B 1 153 ? 4.964   8.283   -24.620 1.00 36.96  ?  153 PHE B C     1 
ATOM   3383 O  O     . PHE B 1 153 ? 3.760   8.141   -24.855 1.00 42.06  ?  153 PHE B O     1 
ATOM   3384 C  CB    . PHE B 1 153 ? 7.160   6.980   -24.656 1.00 31.27  ?  153 PHE B CB    1 
ATOM   3385 C  CG    . PHE B 1 153 ? 7.156   6.228   -25.953 1.00 27.59  ?  153 PHE B CG    1 
ATOM   3386 C  CD1   . PHE B 1 153 ? 6.895   6.876   -27.140 1.00 29.68  ?  153 PHE B CD1   1 
ATOM   3387 C  CD2   . PHE B 1 153 ? 7.488   4.870   -25.989 1.00 34.30  ?  153 PHE B CD2   1 
ATOM   3388 C  CE1   . PHE B 1 153 ? 6.930   6.185   -28.357 1.00 31.46  ?  153 PHE B CE1   1 
ATOM   3389 C  CE2   . PHE B 1 153 ? 7.525   4.165   -27.194 1.00 31.17  ?  153 PHE B CE2   1 
ATOM   3390 C  CZ    . PHE B 1 153 ? 7.226   4.828   -28.385 1.00 27.85  ?  153 PHE B CZ    1 
ATOM   3391 N  N     . ALA B 1 154 ? 5.617   9.405   -24.912 1.00 35.75  ?  154 ALA B N     1 
ATOM   3392 C  CA    . ALA B 1 154 ? 4.911   10.620  -25.299 1.00 31.93  ?  154 ALA B CA    1 
ATOM   3393 C  C     . ALA B 1 154 ? 5.802   11.422  -26.234 1.00 31.83  ?  154 ALA B C     1 
ATOM   3394 O  O     . ALA B 1 154 ? 7.011   11.162  -26.315 1.00 29.91  ?  154 ALA B O     1 
ATOM   3395 C  CB    . ALA B 1 154 ? 4.526   11.438  -24.062 1.00 31.52  ?  154 ALA B CB    1 
ATOM   3396 N  N     . PRO B 1 155 ? 5.232   12.396  -26.974 1.00 34.87  ?  155 PRO B N     1 
ATOM   3397 C  CA    . PRO B 1 155 ? 6.036   13.093  -28.010 1.00 31.90  ?  155 PRO B CA    1 
ATOM   3398 C  C     . PRO B 1 155 ? 7.322   13.736  -27.514 1.00 33.29  ?  155 PRO B C     1 
ATOM   3399 O  O     . PRO B 1 155 ? 8.327   13.700  -28.249 1.00 30.70  ?  155 PRO B O     1 
ATOM   3400 C  CB    . PRO B 1 155 ? 5.061   14.144  -28.561 1.00 31.59  ?  155 PRO B CB    1 
ATOM   3401 C  CG    . PRO B 1 155 ? 3.702   13.494  -28.395 1.00 31.30  ?  155 PRO B CG    1 
ATOM   3402 C  CD    . PRO B 1 155 ? 3.790   12.714  -27.095 1.00 31.21  ?  155 PRO B CD    1 
ATOM   3403 N  N     . SER B 1 156 ? 7.342   14.326  -26.307 1.00 28.21  ?  156 SER B N     1 
ATOM   3404 C  CA    . SER B 1 156 ? 8.569   15.003  -25.875 1.00 30.26  ?  156 SER B CA    1 
ATOM   3405 C  C     . SER B 1 156 ? 9.752   14.053  -25.697 1.00 31.25  ?  156 SER B C     1 
ATOM   3406 O  O     . SER B 1 156 ? 10.888  14.526  -25.602 1.00 30.30  ?  156 SER B O     1 
ATOM   3407 C  CB    . SER B 1 156 ? 8.338   15.780  -24.573 1.00 32.15  ?  156 SER B CB    1 
ATOM   3408 O  OG    . SER B 1 156 ? 7.130   16.534  -24.643 1.00 36.33  ?  156 SER B OG    1 
ATOM   3409 N  N     . ALA B 1 157 ? 9.526   12.740  -25.675 1.00 30.30  ?  157 ALA B N     1 
ATOM   3410 C  CA    . ALA B 1 157 ? 10.596  11.765  -25.535 1.00 31.60  ?  157 ALA B CA    1 
ATOM   3411 C  C     . ALA B 1 157 ? 11.069  11.202  -26.877 1.00 33.81  ?  157 ALA B C     1 
ATOM   3412 O  O     . ALA B 1 157 ? 11.843  10.241  -26.902 1.00 35.11  ?  157 ALA B O     1 
ATOM   3413 C  CB    . ALA B 1 157 ? 10.151  10.627  -24.611 1.00 28.45  ?  157 ALA B CB    1 
ATOM   3414 N  N     . VAL B 1 158 ? 10.651  11.791  -27.990 1.00 33.44  ?  158 VAL B N     1 
ATOM   3415 C  CA    . VAL B 1 158 ? 10.742  11.134  -29.283 1.00 32.39  ?  158 VAL B CA    1 
ATOM   3416 C  C     . VAL B 1 158 ? 11.511  12.030  -30.255 1.00 33.50  ?  158 VAL B C     1 
ATOM   3417 O  O     . VAL B 1 158 ? 11.148  13.196  -30.452 1.00 29.41  ?  158 VAL B O     1 
ATOM   3418 C  CB    . VAL B 1 158 ? 9.340   10.786  -29.818 1.00 32.55  ?  158 VAL B CB    1 
ATOM   3419 C  CG1   . VAL B 1 158 ? 9.378   10.420  -31.284 1.00 34.58  ?  158 VAL B CG1   1 
ATOM   3420 C  CG2   . VAL B 1 158 ? 8.778   9.632   -29.036 1.00 30.15  ?  158 VAL B CG2   1 
ATOM   3421 N  N     . VAL B 1 159 ? 12.587  11.487  -30.832 1.00 27.62  ?  159 VAL B N     1 
ATOM   3422 C  CA    . VAL B 1 159 ? 13.287  12.052  -31.985 1.00 31.31  ?  159 VAL B CA    1 
ATOM   3423 C  C     . VAL B 1 159 ? 13.208  11.030  -33.119 1.00 30.21  ?  159 VAL B C     1 
ATOM   3424 O  O     . VAL B 1 159 ? 13.545  9.852   -32.933 1.00 27.32  ?  159 VAL B O     1 
ATOM   3425 C  CB    . VAL B 1 159 ? 14.759  12.417  -31.668 1.00 32.29  ?  159 VAL B CB    1 
ATOM   3426 C  CG1   . VAL B 1 159 ? 15.376  13.220  -32.792 1.00 25.26  ?  159 VAL B CG1   1 
ATOM   3427 C  CG2   . VAL B 1 159 ? 14.843  13.228  -30.388 1.00 27.15  ?  159 VAL B CG2   1 
ATOM   3428 N  N     . CYS B 1 160 ? 12.768  11.480  -34.292 1.00 31.26  ?  160 CYS B N     1 
ATOM   3429 C  CA    . CYS B 1 160 ? 12.425  10.529  -35.337 1.00 28.89  ?  160 CYS B CA    1 
ATOM   3430 C  C     . CYS B 1 160 ? 12.747  11.103  -36.706 1.00 28.29  ?  160 CYS B C     1 
ATOM   3431 O  O     . CYS B 1 160 ? 12.812  12.323  -36.902 1.00 29.52  ?  160 CYS B O     1 
ATOM   3432 C  CB    . CYS B 1 160 ? 10.937  10.142  -35.270 1.00 29.42  ?  160 CYS B CB    1 
ATOM   3433 S  SG    . CYS B 1 160 ? 9.768   11.522  -35.593 1.00 31.46  ?  160 CYS B SG    1 
ATOM   3434 N  N     . ARG B 1 161 ? 12.967  10.183  -37.644 1.00 31.19  ?  161 ARG B N     1 
ATOM   3435 C  CA    . ARG B 1 161 ? 13.094  10.518  -39.059 1.00 32.43  ?  161 ARG B CA    1 
ATOM   3436 C  C     . ARG B 1 161 ? 11.866  11.311  -39.495 1.00 30.91  ?  161 ARG B C     1 
ATOM   3437 O  O     . ARG B 1 161 ? 10.727  10.867  -39.315 1.00 32.91  ?  161 ARG B O     1 
ATOM   3438 C  CB    . ARG B 1 161 ? 13.263  9.228   -39.893 1.00 25.34  ?  161 ARG B CB    1 
ATOM   3439 C  CG    . ARG B 1 161 ? 13.655  9.431   -41.374 1.00 29.48  ?  161 ARG B CG    1 
ATOM   3440 C  CD    . ARG B 1 161 ? 14.179  8.126   -42.035 1.00 31.78  ?  161 ARG B CD    1 
ATOM   3441 N  NE    . ARG B 1 161 ? 15.325  7.584   -41.309 1.00 28.68  ?  161 ARG B NE    1 
ATOM   3442 C  CZ    . ARG B 1 161 ? 16.543  8.114   -41.296 1.00 29.21  ?  161 ARG B CZ    1 
ATOM   3443 N  NH1   . ARG B 1 161 ? 16.856  9.157   -42.055 1.00 26.93  ?  161 ARG B NH1   1 
ATOM   3444 N  NH2   . ARG B 1 161 ? 17.466  7.604   -40.475 1.00 27.17  ?  161 ARG B NH2   1 
ATOM   3445 N  N     . SER B 1 162 ? 12.099  12.491  -40.042 1.00 33.50  ?  162 SER B N     1 
ATOM   3446 C  CA    . SER B 1 162 ? 11.054  13.493  -40.258 1.00 33.00  ?  162 SER B CA    1 
ATOM   3447 C  C     . SER B 1 162 ? 9.747   12.933  -40.807 1.00 33.69  ?  162 SER B C     1 
ATOM   3448 O  O     . SER B 1 162 ? 9.737   12.388  -41.922 1.00 36.02  ?  162 SER B O     1 
ATOM   3449 C  CB    . SER B 1 162 ? 11.534  14.560  -41.237 1.00 29.99  ?  162 SER B CB    1 
ATOM   3450 O  OG    . SER B 1 162 ? 10.757  15.738  -41.080 1.00 37.77  ?  162 SER B OG    1 
ATOM   3451 N  N     . PRO B 1 163 ? 8.616   13.088  -40.099 1.00 33.69  ?  163 PRO B N     1 
ATOM   3452 C  CA    . PRO B 1 163 ? 7.359   12.543  -40.637 1.00 30.04  ?  163 PRO B CA    1 
ATOM   3453 C  C     . PRO B 1 163 ? 6.899   13.270  -41.866 1.00 33.97  ?  163 PRO B C     1 
ATOM   3454 O  O     . PRO B 1 163 ? 6.196   12.668  -42.694 1.00 34.49  ?  163 PRO B O     1 
ATOM   3455 C  CB    . PRO B 1 163 ? 6.366   12.677  -39.472 1.00 32.77  ?  163 PRO B CB    1 
ATOM   3456 C  CG    . PRO B 1 163 ? 7.227   12.774  -38.249 1.00 31.69  ?  163 PRO B CG    1 
ATOM   3457 C  CD    . PRO B 1 163 ? 8.481   13.509  -38.693 1.00 30.46  ?  163 PRO B CD    1 
ATOM   3458 N  N     . ARG B 1 164 ? 7.320   14.525  -42.043 1.00 33.70  ?  164 ARG B N     1 
ATOM   3459 C  CA    . ARG B 1 164 ? 7.046   15.248  -43.286 1.00 34.96  ?  164 ARG B CA    1 
ATOM   3460 C  C     . ARG B 1 164 ? 7.565   14.502  -44.505 1.00 34.42  ?  164 ARG B C     1 
ATOM   3461 O  O     . ARG B 1 164 ? 6.934   14.518  -45.564 1.00 36.24  ?  164 ARG B O     1 
ATOM   3462 C  CB    . ARG B 1 164 ? 7.681   16.633  -43.236 1.00 33.32  ?  164 ARG B CB    1 
ATOM   3463 C  CG    . ARG B 1 164 ? 7.401   17.404  -44.444 1.00 28.21  ?  164 ARG B CG    1 
ATOM   3464 C  CD    . ARG B 1 164 ? 8.285   18.605  -44.496 1.00 34.63  ?  164 ARG B CD    1 
ATOM   3465 N  NE    . ARG B 1 164 ? 7.981   19.418  -45.668 1.00 37.68  ?  164 ARG B NE    1 
ATOM   3466 C  CZ    . ARG B 1 164 ? 8.394   20.664  -45.846 1.00 33.93  ?  164 ARG B CZ    1 
ATOM   3467 N  NH1   . ARG B 1 164 ? 9.117   21.296  -44.930 1.00 35.33  ?  164 ARG B NH1   1 
ATOM   3468 N  NH2   . ARG B 1 164 ? 8.064   21.294  -46.967 1.00 32.35  ?  164 ARG B NH2   1 
ATOM   3469 N  N     . SER B 1 165 ? 8.722   13.852  -44.379 1.00 33.40  ?  165 SER B N     1 
ATOM   3470 C  CA    . SER B 1 165 ? 9.281   13.097  -45.500 1.00 35.16  ?  165 SER B CA    1 
ATOM   3471 C  C     . SER B 1 165 ? 8.366   11.961  -45.949 1.00 36.22  ?  165 SER B C     1 
ATOM   3472 O  O     . SER B 1 165 ? 8.272   11.672  -47.147 1.00 41.08  ?  165 SER B O     1 
ATOM   3473 C  CB    . SER B 1 165 ? 10.631  12.530  -45.116 1.00 35.47  ?  165 SER B CB    1 
ATOM   3474 O  OG    . SER B 1 165 ? 11.427  12.458  -46.270 1.00 57.64  ?  165 SER B OG    1 
ATOM   3475 N  N     . ALA B 1 166 ? 7.701   11.296  -44.998 1.00 33.12  ?  166 ALA B N     1 
ATOM   3476 C  CA    . ALA B 1 166 ? 6.768   10.207  -45.270 1.00 34.41  ?  166 ALA B CA    1 
ATOM   3477 C  C     . ALA B 1 166 ? 5.345   10.685  -45.514 1.00 30.75  ?  166 ALA B C     1 
ATOM   3478 O  O     . ALA B 1 166 ? 4.532   9.898   -46.005 1.00 29.53  ?  166 ALA B O     1 
ATOM   3479 C  CB    . ALA B 1 166 ? 6.756   9.197   -44.104 1.00 27.19  ?  166 ALA B CB    1 
ATOM   3480 N  N     . GLY B 1 167 ? 5.045   11.950  -45.222 1.00 27.72  ?  167 GLY B N     1 
ATOM   3481 C  CA    . GLY B 1 167 ? 3.686   12.447  -45.296 1.00 32.17  ?  167 GLY B CA    1 
ATOM   3482 C  C     . GLY B 1 167 ? 2.815   11.961  -44.155 1.00 36.46  ?  167 GLY B C     1 
ATOM   3483 O  O     . GLY B 1 167 ? 1.617   11.782  -44.337 1.00 39.18  ?  167 GLY B O     1 
ATOM   3484 N  N     . ALA B 1 168 ? 3.410   11.715  -42.989 1.00 37.27  ?  168 ALA B N     1 
ATOM   3485 C  CA    . ALA B 1 168 ? 2.735   11.189  -41.816 1.00 29.92  ?  168 ALA B CA    1 
ATOM   3486 C  C     . ALA B 1 168 ? 2.405   12.341  -40.891 1.00 34.29  ?  168 ALA B C     1 
ATOM   3487 O  O     . ALA B 1 168 ? 3.298   13.118  -40.524 1.00 37.89  ?  168 ALA B O     1 
ATOM   3488 C  CB    . ALA B 1 168 ? 3.624   10.185  -41.083 1.00 34.84  ?  168 ALA B CB    1 
ATOM   3489 N  N     . PHE B 1 169 ? 1.130   12.461  -40.531 1.00 32.24  ?  169 PHE B N     1 
ATOM   3490 C  CA    . PHE B 1 169 ? 0.716   13.532  -39.648 1.00 34.05  ?  169 PHE B CA    1 
ATOM   3491 C  C     . PHE B 1 169 ? -0.258  12.993  -38.601 1.00 37.82  ?  169 PHE B C     1 
ATOM   3492 O  O     . PHE B 1 169 ? -0.803  11.886  -38.720 1.00 33.12  ?  169 PHE B O     1 
ATOM   3493 C  CB    . PHE B 1 169 ? 0.069   14.708  -40.406 1.00 38.39  ?  169 PHE B CB    1 
ATOM   3494 C  CG    . PHE B 1 169 ? 1.012   15.486  -41.364 1.00 38.24  ?  169 PHE B CG    1 
ATOM   3495 C  CD1   . PHE B 1 169 ? 1.488   14.937  -42.563 1.00 44.71  ?  169 PHE B CD1   1 
ATOM   3496 C  CD2   . PHE B 1 169 ? 1.380   16.776  -41.062 1.00 35.36  ?  169 PHE B CD2   1 
ATOM   3497 C  CE1   . PHE B 1 169 ? 2.304   15.664  -43.423 1.00 44.91  ?  169 PHE B CE1   1 
ATOM   3498 C  CE2   . PHE B 1 169 ? 2.193   17.484  -41.895 1.00 38.38  ?  169 PHE B CE2   1 
ATOM   3499 C  CZ    . PHE B 1 169 ? 2.662   16.929  -43.081 1.00 44.56  ?  169 PHE B CZ    1 
ATOM   3500 N  N     . PHE B 1 170 ? -0.437  13.780  -37.545 1.00 32.88  ?  170 PHE B N     1 
ATOM   3501 C  CA    . PHE B 1 170 ? -1.340  13.386  -36.483 1.00 32.61  ?  170 PHE B CA    1 
ATOM   3502 C  C     . PHE B 1 170 ? -2.769  13.469  -36.984 1.00 33.39  ?  170 PHE B C     1 
ATOM   3503 O  O     . PHE B 1 170 ? -3.092  14.282  -37.849 1.00 32.63  ?  170 PHE B O     1 
ATOM   3504 C  CB    . PHE B 1 170 ? -1.166  14.280  -35.252 1.00 31.76  ?  170 PHE B CB    1 
ATOM   3505 C  CG    . PHE B 1 170 ? 0.170   14.124  -34.559 1.00 30.57  ?  170 PHE B CG    1 
ATOM   3506 C  CD1   . PHE B 1 170 ? 1.315   14.725  -35.074 1.00 29.06  ?  170 PHE B CD1   1 
ATOM   3507 C  CD2   . PHE B 1 170 ? 0.279   13.389  -33.383 1.00 28.08  ?  170 PHE B CD2   1 
ATOM   3508 C  CE1   . PHE B 1 170 ? 2.545   14.592  -34.406 1.00 29.60  ?  170 PHE B CE1   1 
ATOM   3509 C  CE2   . PHE B 1 170 ? 1.493   13.250  -32.725 1.00 24.08  ?  170 PHE B CE2   1 
ATOM   3510 C  CZ    . PHE B 1 170 ? 2.623   13.852  -33.231 1.00 25.25  ?  170 PHE B CZ    1 
ATOM   3511 N  N     . ASP B 1 171 ? -3.622  12.599  -36.435 1.00 32.84  ?  171 ASP B N     1 
ATOM   3512 C  CA    . ASP B 1 171 ? -5.040  12.578  -36.752 1.00 29.97  ?  171 ASP B CA    1 
ATOM   3513 C  C     . ASP B 1 171 ? -5.717  13.672  -35.954 1.00 36.60  ?  171 ASP B C     1 
ATOM   3514 O  O     . ASP B 1 171 ? -5.736  13.625  -34.718 1.00 36.45  ?  171 ASP B O     1 
ATOM   3515 C  CB    . ASP B 1 171 ? -5.624  11.215  -36.405 1.00 33.20  ?  171 ASP B CB    1 
ATOM   3516 C  CG    . ASP B 1 171 ? -7.086  11.061  -36.804 1.00 38.70  ?  171 ASP B CG    1 
ATOM   3517 O  OD1   . ASP B 1 171 ? -7.615  11.801  -37.666 1.00 41.68  ?  171 ASP B OD1   1 
ATOM   3518 O  OD2   . ASP B 1 171 ? -7.723  10.163  -36.231 1.00 38.48  ?  171 ASP B OD2   1 
ATOM   3519 N  N     . THR B 1 172 ? -6.271  14.660  -36.647 1.00 37.40  ?  172 THR B N     1 
ATOM   3520 C  CA    . THR B 1 172 ? -6.958  15.726  -35.929 1.00 33.01  ?  172 THR B CA    1 
ATOM   3521 C  C     . THR B 1 172 ? -8.277  15.264  -35.323 1.00 40.28  ?  172 THR B C     1 
ATOM   3522 O  O     . THR B 1 172 ? -8.826  15.971  -34.471 1.00 39.98  ?  172 THR B O     1 
ATOM   3523 C  CB    . THR B 1 172 ? -7.180  16.911  -36.854 1.00 34.71  ?  172 THR B CB    1 
ATOM   3524 O  OG1   . THR B 1 172 ? -7.956  16.491  -37.973 1.00 38.34  ?  172 THR B OG1   1 
ATOM   3525 C  CG2   . THR B 1 172 ? -5.830  17.458  -37.361 1.00 30.15  ?  172 THR B CG2   1 
ATOM   3526 N  N     . ALA B 1 173 ? -8.791  14.089  -35.715 1.00 41.82  ?  173 ALA B N     1 
ATOM   3527 C  CA    . ALA B 1 173 ? -10.012 13.585  -35.099 1.00 36.10  ?  173 ALA B CA    1 
ATOM   3528 C  C     . ALA B 1 173 ? -9.774  13.063  -33.699 1.00 38.26  ?  173 ALA B C     1 
ATOM   3529 O  O     . ALA B 1 173 ? -10.752 12.813  -32.992 1.00 41.46  ?  173 ALA B O     1 
ATOM   3530 C  CB    . ALA B 1 173 ? -10.644 12.462  -35.926 1.00 38.18  ?  173 ALA B CB    1 
ATOM   3531 N  N     . LEU B 1 174 ? -8.518  12.880  -33.289 1.00 37.33  ?  174 LEU B N     1 
ATOM   3532 C  CA    . LEU B 1 174 ? -8.192  12.378  -31.954 1.00 40.95  ?  174 LEU B CA    1 
ATOM   3533 C  C     . LEU B 1 174 ? -7.690  13.522  -31.083 1.00 43.56  ?  174 LEU B C     1 
ATOM   3534 O  O     . LEU B 1 174 ? -6.755  14.247  -31.463 1.00 48.36  ?  174 LEU B O     1 
ATOM   3535 C  CB    . LEU B 1 174 ? -7.141  11.271  -32.008 1.00 35.14  ?  174 LEU B CB    1 
ATOM   3536 C  CG    . LEU B 1 174 ? -7.595  9.917   -32.537 1.00 39.48  ?  174 LEU B CG    1 
ATOM   3537 C  CD1   . LEU B 1 174 ? -6.371  9.007   -32.658 1.00 34.39  ?  174 LEU B CD1   1 
ATOM   3538 C  CD2   . LEU B 1 174 ? -8.629  9.304   -31.618 1.00 35.88  ?  174 LEU B CD2   1 
ATOM   3539 N  N     . GLY B 1 175 ? -8.306  13.679  -29.921 1.00 37.38  ?  175 GLY B N     1 
ATOM   3540 C  CA    . GLY B 1 175 ? -7.905  14.735  -29.020 1.00 43.77  ?  175 GLY B CA    1 
ATOM   3541 C  C     . GLY B 1 175 ? -7.105  14.191  -27.863 1.00 47.25  ?  175 GLY B C     1 
ATOM   3542 O  O     . GLY B 1 175 ? -6.305  14.920  -27.267 1.00 50.25  ?  175 GLY B O     1 
ATOM   3543 N  N     . VAL B 1 176 ? -7.331  12.916  -27.525 1.00 45.72  ?  176 VAL B N     1 
ATOM   3544 C  CA    . VAL B 1 176 ? -6.458  12.184  -26.621 1.00 41.32  ?  176 VAL B CA    1 
ATOM   3545 C  C     . VAL B 1 176 ? -5.979  10.914  -27.310 1.00 40.56  ?  176 VAL B C     1 
ATOM   3546 O  O     . VAL B 1 176 ? -6.661  10.352  -28.178 1.00 41.74  ?  176 VAL B O     1 
ATOM   3547 C  CB    . VAL B 1 176 ? -7.156  11.849  -25.289 1.00 43.61  ?  176 VAL B CB    1 
ATOM   3548 C  CG1   . VAL B 1 176 ? -7.642  13.126  -24.635 1.00 43.85  ?  176 VAL B CG1   1 
ATOM   3549 C  CG2   . VAL B 1 176 ? -8.290  10.889  -25.530 1.00 39.84  ?  176 VAL B CG2   1 
ATOM   3550 N  N     . GLU B 1 177 ? -4.786  10.466  -26.912 1.00 35.24  ?  177 GLU B N     1 
ATOM   3551 C  CA    . GLU B 1 177 ? -4.095  9.330   -27.517 1.00 38.63  ?  177 GLU B CA    1 
ATOM   3552 C  C     . GLU B 1 177 ? -3.783  9.528   -29.000 1.00 36.96  ?  177 GLU B C     1 
ATOM   3553 O  O     . GLU B 1 177 ? -3.523  8.557   -29.716 1.00 34.25  ?  177 GLU B O     1 
ATOM   3554 C  CB    . GLU B 1 177 ? -4.889  8.042   -27.329 1.00 39.44  ?  177 GLU B CB    1 
ATOM   3555 C  CG    . GLU B 1 177 ? -4.771  7.486   -25.944 1.00 36.34  ?  177 GLU B CG    1 
ATOM   3556 C  CD    . GLU B 1 177 ? -5.870  6.498   -25.672 1.00 43.38  ?  177 GLU B CD    1 
ATOM   3557 O  OE1   . GLU B 1 177 ? -5.647  5.287   -25.963 1.00 39.62  ?  177 GLU B OE1   1 
ATOM   3558 O  OE2   . GLU B 1 177 ? -6.953  6.945   -25.187 1.00 39.98  ?  177 GLU B OE2   1 
ATOM   3559 N  N     . GLU B 1 178 ? -3.807  10.770  -29.483 1.00 36.03  ?  178 GLU B N     1 
ATOM   3560 C  CA    . GLU B 1 178 ? -3.402  11.021  -30.858 1.00 36.12  ?  178 GLU B CA    1 
ATOM   3561 C  C     . GLU B 1 178 ? -1.927  10.674  -31.058 1.00 35.58  ?  178 GLU B C     1 
ATOM   3562 O  O     . GLU B 1 178 ? -1.505  10.352  -32.183 1.00 27.86  ?  178 GLU B O     1 
ATOM   3563 C  CB    . GLU B 1 178 ? -3.683  12.486  -31.246 1.00 33.54  ?  178 GLU B CB    1 
ATOM   3564 C  CG    . GLU B 1 178 ? -2.687  13.507  -30.662 1.00 36.23  ?  178 GLU B CG    1 
ATOM   3565 C  CD    . GLU B 1 178 ? -2.799  13.678  -29.124 1.00 42.77  ?  178 GLU B CD    1 
ATOM   3566 O  OE1   . GLU B 1 178 ? -1.863  14.250  -28.509 1.00 45.06  ?  178 GLU B OE1   1 
ATOM   3567 O  OE2   . GLU B 1 178 ? -3.816  13.261  -28.527 1.00 42.87  ?  178 GLU B OE2   1 
ATOM   3568 N  N     . ASP B 1 179 ? -1.127  10.723  -29.987 1.00 26.92  ?  179 ASP B N     1 
ATOM   3569 C  CA    . ASP B 1 179 ? 0.255   10.292  -30.152 1.00 34.63  ?  179 ASP B CA    1 
ATOM   3570 C  C     . ASP B 1 179 ? 0.329   8.778   -30.296 1.00 32.62  ?  179 ASP B C     1 
ATOM   3571 O  O     . ASP B 1 179 ? 1.111   8.269   -31.095 1.00 34.72  ?  179 ASP B O     1 
ATOM   3572 C  CB    . ASP B 1 179 ? 1.116   10.772  -28.992 1.00 35.12  ?  179 ASP B CB    1 
ATOM   3573 C  CG    . ASP B 1 179 ? 0.571   10.344  -27.666 1.00 36.36  ?  179 ASP B CG    1 
ATOM   3574 O  OD1   . ASP B 1 179 ? -0.670  10.251  -27.573 1.00 37.91  ?  179 ASP B OD1   1 
ATOM   3575 O  OD2   . ASP B 1 179 ? 1.368   10.114  -26.716 1.00 41.06  ?  179 ASP B OD2   1 
ATOM   3576 N  N     . TRP B 1 180 ? -0.514  8.036   -29.580 1.00 32.34  ?  180 TRP B N     1 
ATOM   3577 C  CA    . TRP B 1 180 ? -0.453  6.586   -29.718 1.00 35.74  ?  180 TRP B CA    1 
ATOM   3578 C  C     . TRP B 1 180 ? -0.762  6.159   -31.157 1.00 32.54  ?  180 TRP B C     1 
ATOM   3579 O  O     . TRP B 1 180 ? -0.018  5.374   -31.753 1.00 27.95  ?  180 TRP B O     1 
ATOM   3580 C  CB    . TRP B 1 180 ? -1.387  5.921   -28.716 1.00 30.75  ?  180 TRP B CB    1 
ATOM   3581 C  CG    . TRP B 1 180 ? -1.150  4.434   -28.623 1.00 36.45  ?  180 TRP B CG    1 
ATOM   3582 C  CD1   . TRP B 1 180 ? 0.051   3.808   -28.605 1.00 33.28  ?  180 TRP B CD1   1 
ATOM   3583 C  CD2   . TRP B 1 180 ? -2.145  3.403   -28.557 1.00 34.05  ?  180 TRP B CD2   1 
ATOM   3584 N  NE1   . TRP B 1 180 ? -0.121  2.461   -28.535 1.00 34.39  ?  180 TRP B NE1   1 
ATOM   3585 C  CE2   . TRP B 1 180 ? -1.460  2.177   -28.493 1.00 35.25  ?  180 TRP B CE2   1 
ATOM   3586 C  CE3   . TRP B 1 180 ? -3.547  3.404   -28.529 1.00 33.31  ?  180 TRP B CE3   1 
ATOM   3587 C  CZ2   . TRP B 1 180 ? -2.122  0.944   -28.410 1.00 34.22  ?  180 TRP B CZ2   1 
ATOM   3588 C  CZ3   . TRP B 1 180 ? -4.211  2.190   -28.461 1.00 33.19  ?  180 TRP B CZ3   1 
ATOM   3589 C  CH2   . TRP B 1 180 ? -3.499  0.972   -28.391 1.00 35.19  ?  180 TRP B CH2   1 
ATOM   3590 N  N     . ASP B 1 181 ? -1.823  6.724   -31.749 1.00 35.30  ?  181 ASP B N     1 
ATOM   3591 C  CA    . ASP B 1 181 ? -2.142  6.466   -33.159 1.00 34.87  ?  181 ASP B CA    1 
ATOM   3592 C  C     . ASP B 1 181 ? -0.990  6.857   -34.075 1.00 31.68  ?  181 ASP B C     1 
ATOM   3593 O  O     . ASP B 1 181 ? -0.715  6.165   -35.060 1.00 30.65  ?  181 ASP B O     1 
ATOM   3594 C  CB    . ASP B 1 181 ? -3.412  7.220   -33.564 1.00 30.23  ?  181 ASP B CB    1 
ATOM   3595 C  CG    . ASP B 1 181 ? -3.706  7.140   -35.044 1.00 33.70  ?  181 ASP B CG    1 
ATOM   3596 O  OD1   . ASP B 1 181 ? -4.194  6.074   -35.494 1.00 33.30  ?  181 ASP B OD1   1 
ATOM   3597 O  OD2   . ASP B 1 181 ? -3.476  8.150   -35.748 1.00 32.31  ?  181 ASP B OD2   1 
ATOM   3598 N  N     . PHE B 1 182 ? -0.315  7.965   -33.764 1.00 27.61  ?  182 PHE B N     1 
ATOM   3599 C  CA    . PHE B 1 182 ? 0.803   8.414   -34.576 1.00 29.57  ?  182 PHE B CA    1 
ATOM   3600 C  C     . PHE B 1 182 ? 1.971   7.437   -34.504 1.00 30.29  ?  182 PHE B C     1 
ATOM   3601 O  O     . PHE B 1 182 ? 2.519   7.049   -35.544 1.00 28.31  ?  182 PHE B O     1 
ATOM   3602 C  CB    . PHE B 1 182 ? 1.256   9.801   -34.131 1.00 26.78  ?  182 PHE B CB    1 
ATOM   3603 C  CG    . PHE B 1 182 ? 2.193   10.440  -35.082 1.00 29.20  ?  182 PHE B CG    1 
ATOM   3604 C  CD1   . PHE B 1 182 ? 1.777   10.764  -36.359 1.00 28.93  ?  182 PHE B CD1   1 
ATOM   3605 C  CD2   . PHE B 1 182 ? 3.498   10.720  -34.711 1.00 30.77  ?  182 PHE B CD2   1 
ATOM   3606 C  CE1   . PHE B 1 182 ? 2.645   11.373  -37.246 1.00 32.40  ?  182 PHE B CE1   1 
ATOM   3607 C  CE2   . PHE B 1 182 ? 4.373   11.341  -35.585 1.00 30.02  ?  182 PHE B CE2   1 
ATOM   3608 C  CZ    . PHE B 1 182 ? 3.954   11.665  -36.857 1.00 34.02  ?  182 PHE B CZ    1 
ATOM   3609 N  N     . PHE B 1 183 ? 2.381   7.071   -33.271 1.00 27.03  ?  183 PHE B N     1 
ATOM   3610 C  CA    . PHE B 1 183 ? 3.489   6.145   -33.057 1.00 30.73  ?  183 PHE B CA    1 
ATOM   3611 C  C     . PHE B 1 183 ? 3.247   4.812   -33.759 1.00 30.51  ?  183 PHE B C     1 
ATOM   3612 O  O     . PHE B 1 183 ? 4.140   4.295   -34.444 1.00 30.34  ?  183 PHE B O     1 
ATOM   3613 C  CB    . PHE B 1 183 ? 3.710   5.925   -31.556 1.00 30.23  ?  183 PHE B CB    1 
ATOM   3614 C  CG    . PHE B 1 183 ? 4.046   7.184   -30.797 1.00 28.38  ?  183 PHE B CG    1 
ATOM   3615 C  CD1   . PHE B 1 183 ? 4.493   8.314   -31.458 1.00 30.10  ?  183 PHE B CD1   1 
ATOM   3616 C  CD2   . PHE B 1 183 ? 3.915   7.230   -29.421 1.00 28.47  ?  183 PHE B CD2   1 
ATOM   3617 C  CE1   . PHE B 1 183 ? 4.810   9.471   -30.754 1.00 32.90  ?  183 PHE B CE1   1 
ATOM   3618 C  CE2   . PHE B 1 183 ? 4.201   8.383   -28.704 1.00 31.89  ?  183 PHE B CE2   1 
ATOM   3619 C  CZ    . PHE B 1 183 ? 4.649   9.512   -29.358 1.00 29.44  ?  183 PHE B CZ    1 
ATOM   3620 N  N     . LEU B 1 184 ? 2.037   4.259   -33.620 1.00 29.31  ?  184 LEU B N     1 
ATOM   3621 C  CA    . LEU B 1 184 ? 1.675   3.018   -34.300 1.00 27.72  ?  184 LEU B CA    1 
ATOM   3622 C  C     . LEU B 1 184 ? 1.660   3.179   -35.818 1.00 28.78  ?  184 LEU B C     1 
ATOM   3623 O  O     . LEU B 1 184 ? 2.041   2.258   -36.540 1.00 35.48  ?  184 LEU B O     1 
ATOM   3624 C  CB    . LEU B 1 184 ? 0.304   2.531   -33.809 1.00 30.96  ?  184 LEU B CB    1 
ATOM   3625 C  CG    . LEU B 1 184 ? 0.161   1.968   -32.382 1.00 29.07  ?  184 LEU B CG    1 
ATOM   3626 C  CD1   . LEU B 1 184 ? -1.310  1.666   -32.059 1.00 30.88  ?  184 LEU B CD1   1 
ATOM   3627 C  CD2   . LEU B 1 184 ? 0.987   0.722   -32.176 1.00 29.87  ?  184 LEU B CD2   1 
ATOM   3628 N  N     . ARG B 1 185 ? 1.198   4.316   -36.335 1.00 30.80  ?  185 ARG B N     1 
ATOM   3629 C  CA    . ARG B 1 185 ? 1.196   4.493   -37.786 1.00 33.89  ?  185 ARG B CA    1 
ATOM   3630 C  C     . ARG B 1 185 ? 2.626   4.576   -38.345 1.00 32.98  ?  185 ARG B C     1 
ATOM   3631 O  O     . ARG B 1 185 ? 2.906   4.050   -39.426 1.00 28.46  ?  185 ARG B O     1 
ATOM   3632 C  CB    . ARG B 1 185 ? 0.395   5.734   -38.169 1.00 31.23  ?  185 ARG B CB    1 
ATOM   3633 C  CG    . ARG B 1 185 ? 0.290   5.987   -39.702 1.00 29.94  ?  185 ARG B CG    1 
ATOM   3634 C  CD    . ARG B 1 185 ? -1.113  6.500   -40.086 1.00 34.77  ?  185 ARG B CD    1 
ATOM   3635 N  NE    . ARG B 1 185 ? -1.624  7.438   -39.086 1.00 32.27  ?  185 ARG B NE    1 
ATOM   3636 C  CZ    . ARG B 1 185 ? -1.134  8.660   -38.907 1.00 30.23  ?  185 ARG B CZ    1 
ATOM   3637 N  NH1   . ARG B 1 185 ? -0.241  9.176   -39.750 1.00 26.36  ?  185 ARG B NH1   1 
ATOM   3638 N  NH2   . ARG B 1 185 ? -1.538  9.377   -37.851 1.00 31.08  ?  185 ARG B NH2   1 
ATOM   3639 N  N     . LEU B 1 186 ? 3.541   5.230   -37.632 1.00 29.48  ?  186 LEU B N     1 
ATOM   3640 C  CA    . LEU B 1 186 ? 4.913   5.275   -38.116 1.00 32.85  ?  186 LEU B CA    1 
ATOM   3641 C  C     . LEU B 1 186 ? 5.536   3.887   -38.076 1.00 32.06  ?  186 LEU B C     1 
ATOM   3642 O  O     . LEU B 1 186 ? 6.168   3.455   -39.044 1.00 31.25  ?  186 LEU B O     1 
ATOM   3643 C  CB    . LEU B 1 186 ? 5.748   6.257   -37.285 1.00 28.07  ?  186 LEU B CB    1 
ATOM   3644 C  CG    . LEU B 1 186 ? 5.525   7.751   -37.493 1.00 31.96  ?  186 LEU B CG    1 
ATOM   3645 C  CD1   . LEU B 1 186 ? 6.431   8.580   -36.572 1.00 27.11  ?  186 LEU B CD1   1 
ATOM   3646 C  CD2   . LEU B 1 186 ? 5.743   8.112   -38.957 1.00 27.06  ?  186 LEU B CD2   1 
ATOM   3647 N  N     . ALA B 1 187 ? 5.359   3.173   -36.967 1.00 30.40  ?  187 ALA B N     1 
ATOM   3648 C  CA    . ALA B 1 187 ? 6.082   1.922   -36.793 1.00 33.83  ?  187 ALA B CA    1 
ATOM   3649 C  C     . ALA B 1 187 ? 5.528   0.820   -37.690 1.00 34.02  ?  187 ALA B C     1 
ATOM   3650 O  O     . ALA B 1 187 ? 6.287   -0.005  -38.215 1.00 41.76  ?  187 ALA B O     1 
ATOM   3651 C  CB    . ALA B 1 187 ? 6.050   1.505   -35.325 1.00 24.90  ?  187 ALA B CB    1 
ATOM   3652 N  N     . HIS B 1 188 ? 4.219   0.795   -37.894 1.00 33.12  ?  188 HIS B N     1 
ATOM   3653 C  CA    . HIS B 1 188 ? 3.581   -0.271  -38.658 1.00 32.11  ?  188 HIS B CA    1 
ATOM   3654 C  C     . HIS B 1 188 ? 3.300   0.144   -40.088 1.00 33.86  ?  188 HIS B C     1 
ATOM   3655 O  O     . HIS B 1 188 ? 3.694   -0.558  -41.006 1.00 37.04  ?  188 HIS B O     1 
ATOM   3656 C  CB    . HIS B 1 188 ? 2.268   -0.703  -37.989 1.00 32.83  ?  188 HIS B CB    1 
ATOM   3657 C  CG    . HIS B 1 188 ? 2.464   -1.338  -36.654 1.00 37.40  ?  188 HIS B CG    1 
ATOM   3658 N  ND1   . HIS B 1 188 ? 3.621   -2.014  -36.318 1.00 43.05  ?  188 HIS B ND1   1 
ATOM   3659 C  CD2   . HIS B 1 188 ? 1.655   -1.422  -35.577 1.00 38.99  ?  188 HIS B CD2   1 
ATOM   3660 C  CE1   . HIS B 1 188 ? 3.518   -2.468  -35.083 1.00 39.84  ?  188 HIS B CE1   1 
ATOM   3661 N  NE2   . HIS B 1 188 ? 2.331   -2.129  -34.615 1.00 39.60  ?  188 HIS B NE2   1 
ATOM   3662 N  N     . GLY B 1 189 ? 2.612   1.271   -40.291 1.00 31.93  ?  189 GLY B N     1 
ATOM   3663 C  CA    . GLY B 1 189 ? 2.312   1.700   -41.644 1.00 30.25  ?  189 GLY B CA    1 
ATOM   3664 C  C     . GLY B 1 189 ? 3.542   2.156   -42.411 1.00 31.53  ?  189 GLY B C     1 
ATOM   3665 O  O     . GLY B 1 189 ? 3.665   1.903   -43.612 1.00 32.42  ?  189 GLY B O     1 
ATOM   3666 N  N     . HIS B 1 190 ? 4.474   2.813   -41.737 1.00 31.21  ?  190 HIS B N     1 
ATOM   3667 C  CA    . HIS B 1 190 ? 5.664   3.280   -42.418 1.00 33.01  ?  190 HIS B CA    1 
ATOM   3668 C  C     . HIS B 1 190 ? 6.893   2.432   -42.125 1.00 34.43  ?  190 HIS B C     1 
ATOM   3669 O  O     . HIS B 1 190 ? 7.962   2.711   -42.676 1.00 34.49  ?  190 HIS B O     1 
ATOM   3670 C  CB    . HIS B 1 190 ? 5.885   4.758   -42.075 1.00 33.54  ?  190 HIS B CB    1 
ATOM   3671 C  CG    . HIS B 1 190 ? 4.822   5.633   -42.656 1.00 31.09  ?  190 HIS B CG    1 
ATOM   3672 N  ND1   . HIS B 1 190 ? 4.880   6.111   -43.946 1.00 28.74  ?  190 HIS B ND1   1 
ATOM   3673 C  CD2   . HIS B 1 190 ? 3.615   6.014   -42.169 1.00 31.83  ?  190 HIS B CD2   1 
ATOM   3674 C  CE1   . HIS B 1 190 ? 3.780   6.793   -44.213 1.00 31.34  ?  190 HIS B CE1   1 
ATOM   3675 N  NE2   . HIS B 1 190 ? 2.999   6.759   -43.147 1.00 34.54  ?  190 HIS B NE2   1 
ATOM   3676 N  N     . LYS B 1 191 ? 6.765   1.399   -41.288 1.00 33.82  ?  191 LYS B N     1 
ATOM   3677 C  CA    . LYS B 1 191 ? 7.881   0.499   -40.985 1.00 38.01  ?  191 LYS B CA    1 
ATOM   3678 C  C     . LYS B 1 191 ? 9.038   1.245   -40.341 1.00 34.31  ?  191 LYS B C     1 
ATOM   3679 O  O     . LYS B 1 191 ? 10.201  0.935   -40.589 1.00 38.89  ?  191 LYS B O     1 
ATOM   3680 C  CB    . LYS B 1 191 ? 8.392   -0.233  -42.244 1.00 32.73  ?  191 LYS B CB    1 
ATOM   3681 C  CG    . LYS B 1 191 ? 7.423   -1.156  -42.908 1.00 30.42  ?  191 LYS B CG    1 
ATOM   3682 C  CD    . LYS B 1 191 ? 6.545   -1.779  -41.867 1.00 44.08  ?  191 LYS B CD    1 
ATOM   3683 C  CE    . LYS B 1 191 ? 5.353   -2.495  -42.426 1.00 47.21  ?  191 LYS B CE    1 
ATOM   3684 N  NZ    . LYS B 1 191 ? 5.281   -3.798  -41.719 1.00 60.57  ?  191 LYS B NZ    1 
ATOM   3685 N  N     . TYR B 1 192 ? 8.755   2.265   -39.552 1.00 33.98  ?  192 TYR B N     1 
ATOM   3686 C  CA    . TYR B 1 192 ? 9.835   2.973   -38.877 1.00 32.20  ?  192 TYR B CA    1 
ATOM   3687 C  C     . TYR B 1 192 ? 10.521  2.038   -37.893 1.00 29.84  ?  192 TYR B C     1 
ATOM   3688 O  O     . TYR B 1 192 ? 9.854   1.369   -37.093 1.00 34.27  ?  192 TYR B O     1 
ATOM   3689 C  CB    . TYR B 1 192 ? 9.284   4.195   -38.141 1.00 32.42  ?  192 TYR B CB    1 
ATOM   3690 C  CG    . TYR B 1 192 ? 9.370   5.464   -38.923 1.00 29.97  ?  192 TYR B CG    1 
ATOM   3691 C  CD1   . TYR B 1 192 ? 9.094   5.481   -40.275 1.00 27.54  ?  192 TYR B CD1   1 
ATOM   3692 C  CD2   . TYR B 1 192 ? 9.691   6.667   -38.298 1.00 32.78  ?  192 TYR B CD2   1 
ATOM   3693 C  CE1   . TYR B 1 192 ? 9.193   6.648   -40.994 1.00 31.03  ?  192 TYR B CE1   1 
ATOM   3694 C  CE2   . TYR B 1 192 ? 9.791   7.837   -39.015 1.00 27.64  ?  192 TYR B CE2   1 
ATOM   3695 C  CZ    . TYR B 1 192 ? 9.533   7.822   -40.354 1.00 30.07  ?  192 TYR B CZ    1 
ATOM   3696 O  OH    . TYR B 1 192 ? 9.625   8.982   -41.074 1.00 34.49  ?  192 TYR B OH    1 
ATOM   3697 N  N     . ARG B 1 193 ? 11.849  2.017   -37.926 1.00 31.24  ?  193 ARG B N     1 
ATOM   3698 C  CA    . ARG B 1 193 ? 12.644  1.172   -37.033 1.00 29.45  ?  193 ARG B CA    1 
ATOM   3699 C  C     . ARG B 1 193 ? 12.845  1.876   -35.690 1.00 32.49  ?  193 ARG B C     1 
ATOM   3700 O  O     . ARG B 1 193 ? 13.397  2.990   -35.619 1.00 29.81  ?  193 ARG B O     1 
ATOM   3701 C  CB    . ARG B 1 193 ? 13.964  0.833   -37.694 1.00 28.73  ?  193 ARG B CB    1 
ATOM   3702 C  CG    . ARG B 1 193 ? 13.742  0.110   -38.984 1.00 36.17  ?  193 ARG B CG    1 
ATOM   3703 C  CD    . ARG B 1 193 ? 14.977  0.021   -39.829 1.00 37.24  ?  193 ARG B CD    1 
ATOM   3704 N  NE    . ARG B 1 193 ? 15.110  1.228   -40.642 1.00 42.95  ?  193 ARG B NE    1 
ATOM   3705 C  CZ    . ARG B 1 193 ? 16.171  1.514   -41.386 1.00 39.32  ?  193 ARG B CZ    1 
ATOM   3706 N  NH1   . ARG B 1 193 ? 17.189  0.657   -41.499 1.00 37.39  ?  193 ARG B NH1   1 
ATOM   3707 N  NH2   . ARG B 1 193 ? 16.225  2.690   -42.010 1.00 32.62  ?  193 ARG B NH2   1 
ATOM   3708 N  N     . VAL B 1 194 ? 12.348  1.247   -34.639 1.00 30.82  ?  194 VAL B N     1 
ATOM   3709 C  CA    . VAL B 1 194 ? 12.209  1.866   -33.339 1.00 26.33  ?  194 VAL B CA    1 
ATOM   3710 C  C     . VAL B 1 194 ? 13.321  1.378   -32.424 1.00 30.83  ?  194 VAL B C     1 
ATOM   3711 O  O     . VAL B 1 194 ? 13.684  0.196   -32.437 1.00 30.18  ?  194 VAL B O     1 
ATOM   3712 C  CB    . VAL B 1 194 ? 10.826  1.544   -32.758 1.00 33.96  ?  194 VAL B CB    1 
ATOM   3713 C  CG1   . VAL B 1 194 ? 10.778  1.912   -31.262 1.00 28.34  ?  194 VAL B CG1   1 
ATOM   3714 C  CG2   . VAL B 1 194 ? 9.737   2.229   -33.602 1.00 31.16  ?  194 VAL B CG2   1 
ATOM   3715 N  N     . VAL B 1 195 ? 13.845  2.284   -31.607 1.00 30.61  ?  195 VAL B N     1 
ATOM   3716 C  CA    . VAL B 1 195 ? 14.975  1.999   -30.738 1.00 34.77  ?  195 VAL B CA    1 
ATOM   3717 C  C     . VAL B 1 195 ? 14.777  2.764   -29.432 1.00 33.94  ?  195 VAL B C     1 
ATOM   3718 O  O     . VAL B 1 195 ? 14.450  3.954   -29.450 1.00 32.79  ?  195 VAL B O     1 
ATOM   3719 C  CB    . VAL B 1 195 ? 16.309  2.387   -31.425 1.00 33.96  ?  195 VAL B CB    1 
ATOM   3720 C  CG1   . VAL B 1 195 ? 17.420  2.633   -30.400 1.00 35.16  ?  195 VAL B CG1   1 
ATOM   3721 C  CG2   . VAL B 1 195 ? 16.734  1.306   -32.374 1.00 32.52  ?  195 VAL B CG2   1 
ATOM   3722 N  N     . HIS B 1 196 ? 14.984  2.087   -28.306 1.00 37.25  ?  196 HIS B N     1 
ATOM   3723 C  CA    . HIS B 1 196 ? 14.949  2.722   -26.993 1.00 34.15  ?  196 HIS B CA    1 
ATOM   3724 C  C     . HIS B 1 196 ? 16.324  3.296   -26.680 1.00 34.29  ?  196 HIS B C     1 
ATOM   3725 O  O     . HIS B 1 196 ? 17.334  2.607   -26.798 1.00 34.72  ?  196 HIS B O     1 
ATOM   3726 C  CB    . HIS B 1 196 ? 14.514  1.713   -25.921 1.00 31.80  ?  196 HIS B CB    1 
ATOM   3727 C  CG    . HIS B 1 196 ? 14.372  2.300   -24.542 1.00 40.81  ?  196 HIS B CG    1 
ATOM   3728 N  ND1   . HIS B 1 196 ? 14.761  1.627   -23.402 1.00 37.49  ?  196 HIS B ND1   1 
ATOM   3729 C  CD2   . HIS B 1 196 ? 13.891  3.498   -24.121 1.00 36.66  ?  196 HIS B CD2   1 
ATOM   3730 C  CE1   . HIS B 1 196 ? 14.538  2.387   -22.345 1.00 30.99  ?  196 HIS B CE1   1 
ATOM   3731 N  NE2   . HIS B 1 196 ? 14.020  3.530   -22.756 1.00 33.02  ?  196 HIS B NE2   1 
ATOM   3732 N  N     . GLN B 1 197 ? 16.376  4.565   -26.308 1.00 33.53  ?  197 GLN B N     1 
ATOM   3733 C  CA    . GLN B 1 197 ? 17.644  5.130   -25.857 1.00 37.97  ?  197 GLN B CA    1 
ATOM   3734 C  C     . GLN B 1 197 ? 17.551  5.329   -24.351 1.00 40.07  ?  197 GLN B C     1 
ATOM   3735 O  O     . GLN B 1 197 ? 17.107  6.383   -23.884 1.00 42.60  ?  197 GLN B O     1 
ATOM   3736 C  CB    . GLN B 1 197 ? 17.970  6.448   -26.567 1.00 35.49  ?  197 GLN B CB    1 
ATOM   3737 C  CG    . GLN B 1 197 ? 19.125  7.280   -25.956 1.00 36.64  ?  197 GLN B CG    1 
ATOM   3738 C  CD    . GLN B 1 197 ? 20.426  6.506   -25.831 1.00 39.44  ?  197 GLN B CD    1 
ATOM   3739 O  OE1   . GLN B 1 197 ? 20.502  5.522   -25.101 1.00 39.99  ?  197 GLN B OE1   1 
ATOM   3740 N  NE2   . GLN B 1 197 ? 21.461  6.948   -26.556 1.00 36.86  ?  197 GLN B NE2   1 
ATOM   3741 N  N     . PRO B 1 198 ? 17.946  4.348   -23.539 1.00 40.60  ?  198 PRO B N     1 
ATOM   3742 C  CA    . PRO B 1 198 ? 17.823  4.529   -22.082 1.00 39.41  ?  198 PRO B CA    1 
ATOM   3743 C  C     . PRO B 1 198 ? 18.871  5.456   -21.506 1.00 37.43  ?  198 PRO B C     1 
ATOM   3744 O  O     . PRO B 1 198 ? 18.737  5.856   -20.350 1.00 39.52  ?  198 PRO B O     1 
ATOM   3745 C  CB    . PRO B 1 198 ? 17.990  3.104   -21.533 1.00 39.10  ?  198 PRO B CB    1 
ATOM   3746 C  CG    . PRO B 1 198 ? 18.954  2.462   -22.537 1.00 41.27  ?  198 PRO B CG    1 
ATOM   3747 C  CD    . PRO B 1 198 ? 18.598  3.077   -23.907 1.00 34.72  ?  198 PRO B CD    1 
ATOM   3748 N  N     . GLU B 1 199 ? 19.920  5.782   -22.246 1.00 41.81  ?  199 GLU B N     1 
ATOM   3749 C  CA    . GLU B 1 199 ? 20.953  6.694   -21.753 1.00 36.18  ?  199 GLU B CA    1 
ATOM   3750 C  C     . GLU B 1 199 ? 20.489  8.134   -21.712 1.00 42.17  ?  199 GLU B C     1 
ATOM   3751 O  O     . GLU B 1 199 ? 21.364  8.997   -21.448 1.00 38.86  ?  199 GLU B O     1 
ATOM   3752 C  CB    . GLU B 1 199 ? 22.225  6.631   -22.613 1.00 41.77  ?  199 GLU B CB    1 
ATOM   3753 C  CG    . GLU B 1 199 ? 23.048  5.346   -22.631 1.00 38.22  ?  199 GLU B CG    1 
ATOM   3754 C  CD    . GLU B 1 199 ? 24.238  5.450   -23.610 1.00 53.90  ?  199 GLU B CD    1 
ATOM   3755 O  OE1   . GLU B 1 199 ? 24.963  4.443   -23.811 1.00 62.77  ?  199 GLU B OE1   1 
ATOM   3756 O  OE2   . GLU B 1 199 ? 24.440  6.541   -24.194 1.00 51.55  ?  199 GLU B OE2   1 
ATOM   3757 N  N     . VAL B 1 200 ? 19.221  8.469   -21.992 1.00 39.52  ?  200 VAL B N     1 
ATOM   3758 C  CA    . VAL B 1 200 ? 18.767  9.855   -21.986 1.00 37.07  ?  200 VAL B CA    1 
ATOM   3759 C  C     . VAL B 1 200 ? 17.387  9.905   -21.347 1.00 37.99  ?  200 VAL B C     1 
ATOM   3760 O  O     . VAL B 1 200 ? 16.602  8.954   -21.449 1.00 38.96  ?  200 VAL B O     1 
ATOM   3761 C  CB    . VAL B 1 200 ? 18.766  10.457  -23.418 1.00 36.41  ?  200 VAL B CB    1 
ATOM   3762 C  CG1   . VAL B 1 200 ? 17.919  11.742  -23.512 1.00 36.28  ?  200 VAL B CG1   1 
ATOM   3763 C  CG2   . VAL B 1 200 ? 20.178  10.759  -23.837 1.00 34.42  ?  200 VAL B CG2   1 
ATOM   3764 N  N     . ALA B 1 201 ? 17.093  11.017  -20.668 1.00 39.28  ?  201 ALA B N     1 
ATOM   3765 C  CA    . ALA B 1 201 ? 15.800  11.178  -20.002 1.00 46.18  ?  201 ALA B CA    1 
ATOM   3766 C  C     . ALA B 1 201 ? 15.293  12.603  -20.185 1.00 43.46  ?  201 ALA B C     1 
ATOM   3767 O  O     . ALA B 1 201 ? 16.080  13.535  -20.361 1.00 36.21  ?  201 ALA B O     1 
ATOM   3768 C  CB    . ALA B 1 201 ? 15.879  10.839  -18.501 1.00 36.74  ?  201 ALA B CB    1 
ATOM   3769 N  N     . ILE B 1 202 ? 13.964  12.754  -20.168 1.00 40.96  ?  202 ILE B N     1 
ATOM   3770 C  CA    . ILE B 1 202 ? 13.315  14.054  -20.112 1.00 44.93  ?  202 ILE B CA    1 
ATOM   3771 C  C     . ILE B 1 202 ? 12.558  14.157  -18.799 1.00 49.03  ?  202 ILE B C     1 
ATOM   3772 O  O     . ILE B 1 202 ? 12.232  13.156  -18.165 1.00 50.20  ?  202 ILE B O     1 
ATOM   3773 C  CB    . ILE B 1 202 ? 12.334  14.281  -21.263 1.00 38.19  ?  202 ILE B CB    1 
ATOM   3774 C  CG1   . ILE B 1 202 ? 11.469  13.051  -21.364 1.00 41.92  ?  202 ILE B CG1   1 
ATOM   3775 C  CG2   . ILE B 1 202 ? 13.040  14.427  -22.537 1.00 46.00  ?  202 ILE B CG2   1 
ATOM   3776 C  CD1   . ILE B 1 202 ? 10.164  13.333  -21.999 1.00 48.97  ?  202 ILE B CD1   1 
ATOM   3777 N  N     . ALA B 1 203 ? 12.253  15.394  -18.415 1.00 51.06  ?  203 ALA B N     1 
ATOM   3778 C  CA    . ALA B 1 203 ? 11.248  15.678  -17.395 1.00 56.69  ?  203 ALA B CA    1 
ATOM   3779 C  C     . ALA B 1 203 ? 9.915   15.910  -18.107 1.00 52.73  ?  203 ALA B C     1 
ATOM   3780 O  O     . ALA B 1 203 ? 9.761   16.907  -18.834 1.00 47.13  ?  203 ALA B O     1 
ATOM   3781 C  CB    . ALA B 1 203 ? 11.648  16.896  -16.556 1.00 52.10  ?  203 ALA B CB    1 
ATOM   3782 N  N     . LEU B 1 204 ? 8.956   14.992  -17.905 1.00 49.41  ?  204 LEU B N     1 
ATOM   3783 C  CA    . LEU B 1 204 ? 7.595   15.125  -18.434 1.00 47.97  ?  204 LEU B CA    1 
ATOM   3784 C  C     . LEU B 1 204 ? 6.694   15.685  -17.331 1.00 60.24  ?  204 LEU B C     1 
ATOM   3785 O  O     . LEU B 1 204 ? 6.104   14.940  -16.531 1.00 55.59  ?  204 LEU B O     1 
ATOM   3786 C  CB    . LEU B 1 204 ? 7.046   13.803  -18.947 1.00 47.15  ?  204 LEU B CB    1 
ATOM   3787 C  CG    . LEU B 1 204 ? 5.666   14.108  -19.535 1.00 50.76  ?  204 LEU B CG    1 
ATOM   3788 C  CD1   . LEU B 1 204 ? 5.761   14.339  -21.037 1.00 39.18  ?  204 LEU B CD1   1 
ATOM   3789 C  CD2   . LEU B 1 204 ? 4.566   13.093  -19.188 1.00 41.90  ?  204 LEU B CD2   1 
ATOM   3790 N  N     . HIS B 1 205 ? 6.560   17.019  -17.324 1.00 58.65  ?  205 HIS B N     1 
ATOM   3791 C  CA    . HIS B 1 205 ? 5.871   17.710  -16.243 1.00 61.20  ?  205 HIS B CA    1 
ATOM   3792 C  C     . HIS B 1 205 ? 4.407   17.311  -16.177 1.00 62.49  ?  205 HIS B C     1 
ATOM   3793 O  O     . HIS B 1 205 ? 3.639   17.518  -17.128 1.00 52.44  ?  205 HIS B O     1 
ATOM   3794 C  CB    . HIS B 1 205 ? 6.040   19.213  -16.396 1.00 56.73  ?  205 HIS B CB    1 
ATOM   3795 C  CG    . HIS B 1 205 ? 7.368   19.694  -15.901 1.00 61.90  ?  205 HIS B CG    1 
ATOM   3796 N  ND1   . HIS B 1 205 ? 8.060   19.038  -14.905 1.00 63.26  ?  205 HIS B ND1   1 
ATOM   3797 C  CD2   . HIS B 1 205 ? 8.175   20.699  -16.319 1.00 64.30  ?  205 HIS B CD2   1 
ATOM   3798 C  CE1   . HIS B 1 205 ? 9.215   19.648  -14.697 1.00 65.41  ?  205 HIS B CE1   1 
ATOM   3799 N  NE2   . HIS B 1 205 ? 9.311   20.660  -15.542 1.00 62.66  ?  205 HIS B NE2   1 
ATOM   3800 N  N     . ARG B 1 206 ? 4.078   16.663  -15.062 1.00 66.00  ?  206 ARG B N     1 
ATOM   3801 C  CA    . ARG B 1 206 ? 2.735   16.277  -14.653 1.00 74.34  ?  206 ARG B CA    1 
ATOM   3802 C  C     . ARG B 1 206 ? 2.517   16.894  -13.268 1.00 79.13  ?  206 ARG B C     1 
ATOM   3803 O  O     . ARG B 1 206 ? 2.547   16.223  -12.229 1.00 79.62  ?  206 ARG B O     1 
ATOM   3804 C  CB    . ARG B 1 206 ? 2.592   14.726  -14.660 1.00 70.97  ?  206 ARG B CB    1 
ATOM   3805 C  CG    . ARG B 1 206 ? 1.163   14.185  -14.560 1.00 77.10  ?  206 ARG B CG    1 
ATOM   3806 C  CD    . ARG B 1 206 ? 0.804   13.773  -13.126 1.00 75.15  ?  206 ARG B CD    1 
ATOM   3807 N  NE    . ARG B 1 206 ? -0.620  13.481  -12.979 1.00 79.09  ?  206 ARG B NE    1 
ATOM   3808 C  CZ    . ARG B 1 206 ? -1.127  12.534  -12.194 1.00 82.91  ?  206 ARG B CZ    1 
ATOM   3809 N  NH1   . ARG B 1 206 ? -0.351  11.773  -11.432 1.00 81.99  ?  206 ARG B NH1   1 
ATOM   3810 N  NH2   . ARG B 1 206 ? -2.445  12.337  -12.182 1.00 71.18  ?  206 ARG B NH2   1 
ATOM   3811 N  N     . ILE B 1 207 ? 2.350   18.210  -13.262 1.00 84.04  ?  207 ILE B N     1 
ATOM   3812 C  CA    . ILE B 1 207 ? 2.425   19.011  -12.034 1.00 86.52  ?  207 ILE B CA    1 
ATOM   3813 C  C     . ILE B 1 207 ? 1.168   18.780  -11.202 1.00 89.80  ?  207 ILE B C     1 
ATOM   3814 O  O     . ILE B 1 207 ? 0.054   18.745  -11.764 1.00 88.62  ?  207 ILE B O     1 
ATOM   3815 C  CB    . ILE B 1 207 ? 2.608   20.496  -12.387 1.00 84.95  ?  207 ILE B CB    1 
ATOM   3816 C  CG1   . ILE B 1 207 ? 3.871   20.690  -13.258 1.00 72.29  ?  207 ILE B CG1   1 
ATOM   3817 C  CG2   . ILE B 1 207 ? 2.652   21.362  -11.127 1.00 81.40  ?  207 ILE B CG2   1 
ATOM   3818 C  CD1   . ILE B 1 207 ? 3.583   20.969  -14.750 1.00 58.43  ?  207 ILE B CD1   1 
ATOM   3819 N  N     . PRO B 1 208 ? 1.285   18.591  -9.867  1.00 91.01  ?  208 PRO B N     1 
ATOM   3820 C  CA    . PRO B 1 208 ? 0.101   18.249  -9.057  1.00 92.80  ?  208 PRO B CA    1 
ATOM   3821 C  C     . PRO B 1 208 ? -0.564  19.437  -8.365  1.00 86.46  ?  208 PRO B C     1 
ATOM   3822 O  O     . PRO B 1 208 ? 0.087   20.402  -7.947  1.00 87.55  ?  208 PRO B O     1 
ATOM   3823 C  CB    . PRO B 1 208 ? 0.659   17.251  -8.024  1.00 88.64  ?  208 PRO B CB    1 
ATOM   3824 C  CG    . PRO B 1 208 ? 2.160   17.106  -8.339  1.00 88.91  ?  208 PRO B CG    1 
ATOM   3825 C  CD    . PRO B 1 208 ? 2.531   18.324  -9.131  1.00 90.12  ?  208 PRO B CD    1 
ATOM   3826 N  N     . GLY B 1 209 ? -1.871  19.362  -8.226  1.00 83.39  ?  209 GLY B N     1 
ATOM   3827 C  CA    . GLY B 1 209 ? -2.639  20.404  -7.557  1.00 83.19  ?  209 GLY B CA    1 
ATOM   3828 C  C     . GLY B 1 209 ? -3.845  19.827  -6.864  1.00 86.68  ?  209 GLY B C     1 
ATOM   3829 O  O     . GLY B 1 209 ? -3.772  18.745  -6.263  1.00 87.27  ?  209 GLY B O     1 
ATOM   3830 N  N     . VAL B 1 210 ? -4.972  20.547  -6.944  1.00 89.61  ?  210 VAL B N     1 
ATOM   3831 C  CA    . VAL B 1 210 ? -6.205  20.128  -6.279  1.00 84.36  ?  210 VAL B CA    1 
ATOM   3832 C  C     . VAL B 1 210 ? -7.016  19.140  -7.107  1.00 90.42  ?  210 VAL B C     1 
ATOM   3833 O  O     . VAL B 1 210 ? -7.925  18.493  -6.562  1.00 96.23  ?  210 VAL B O     1 
ATOM   3834 C  CB    . VAL B 1 210 ? -6.970  21.405  -5.872  1.00 76.73  ?  210 VAL B CB    1 
ATOM   3835 C  CG1   . VAL B 1 210 ? -8.458  21.176  -5.705  1.00 77.79  ?  210 VAL B CG1   1 
ATOM   3836 C  CG2   . VAL B 1 210 ? -6.414  21.877  -4.550  1.00 76.18  ?  210 VAL B CG2   1 
ATOM   3837 N  N     . GLU B 1 211 ? -6.683  18.954  -8.391  1.00 91.82  ?  211 GLU B N     1 
ATOM   3838 C  CA    . GLU B 1 211 ? -7.288  17.864  -9.155  1.00 97.84  ?  211 GLU B CA    1 
ATOM   3839 C  C     . GLU B 1 211 ? -7.111  16.523  -8.433  1.00 99.92  ?  211 GLU B C     1 
ATOM   3840 O  O     . GLU B 1 211 ? -8.035  15.695  -8.399  1.00 100.36 ?  211 GLU B O     1 
ATOM   3841 C  CB    . GLU B 1 211 ? -6.696  17.819  -10.577 1.00 97.95  ?  211 GLU B CB    1 
ATOM   3842 C  CG    . GLU B 1 211 ? -7.729  17.498  -11.688 1.00 96.98  ?  211 GLU B CG    1 
ATOM   3843 C  CD    . GLU B 1 211 ? -7.122  17.232  -13.080 1.00 95.19  ?  211 GLU B CD    1 
ATOM   3844 O  OE1   . GLU B 1 211 ? -5.977  16.711  -13.189 1.00 89.96  ?  211 GLU B OE1   1 
ATOM   3845 O  OE2   . GLU B 1 211 ? -7.828  17.524  -14.073 1.00 84.24  ?  211 GLU B OE2   1 
ATOM   3846 N  N     . SER B 1 212 ? -5.942  16.313  -7.812  1.00 99.35  ?  212 SER B N     1 
ATOM   3847 C  CA    . SER B 1 212 ? -5.633  15.108  -7.047  1.00 97.02  ?  212 SER B CA    1 
ATOM   3848 C  C     . SER B 1 212 ? -5.953  15.239  -5.554  1.00 99.39  ?  212 SER B C     1 
ATOM   3849 O  O     . SER B 1 212 ? -5.763  14.272  -4.806  1.00 99.75  ?  212 SER B O     1 
ATOM   3850 C  CB    . SER B 1 212 ? -4.157  14.726  -7.258  1.00 95.02  ?  212 SER B CB    1 
ATOM   3851 O  OG    . SER B 1 212 ? -3.321  15.867  -7.397  1.00 91.64  ?  212 SER B OG    1 
ATOM   3852 N  N     . LEU B 1 213 ? -6.435  16.406  -5.112  1.00 102.00 ?  213 LEU B N     1 
ATOM   3853 C  CA    . LEU B 1 213 ? -6.958  16.634  -3.766  1.00 98.50  ?  213 LEU B CA    1 
ATOM   3854 C  C     . LEU B 1 213 ? -8.485  16.596  -3.732  1.00 101.60 ?  213 LEU B C     1 
ATOM   3855 O  O     . LEU B 1 213 ? -9.087  16.953  -2.709  1.00 101.04 ?  213 LEU B O     1 
ATOM   3856 C  CB    . LEU B 1 213 ? -6.444  17.976  -3.219  1.00 92.53  ?  213 LEU B CB    1 
ATOM   3857 C  CG    . LEU B 1 213 ? -6.190  18.169  -1.721  1.00 87.90  ?  213 LEU B CG    1 
ATOM   3858 C  CD1   . LEU B 1 213 ? -5.163  17.181  -1.200  1.00 87.27  ?  213 LEU B CD1   1 
ATOM   3859 C  CD2   . LEU B 1 213 ? -5.716  19.592  -1.480  1.00 77.18  ?  213 LEU B CD2   1 
ATOM   3860 N  N     . THR B 1 214 ? -9.116  16.209  -4.846  1.00 100.42 ?  214 THR B N     1 
ATOM   3861 C  CA    . THR B 1 214 ? -10.534 15.889  -4.912  1.00 98.69  ?  214 THR B CA    1 
ATOM   3862 C  C     . THR B 1 214 ? -10.676 14.389  -5.135  1.00 98.18  ?  214 THR B C     1 
ATOM   3863 O  O     . THR B 1 214 ? -9.937  13.800  -5.931  1.00 96.16  ?  214 THR B O     1 
ATOM   3864 C  CB    . THR B 1 214 ? -11.258 16.665  -6.033  1.00 98.75  ?  214 THR B CB    1 
ATOM   3865 O  OG1   . THR B 1 214 ? -10.614 16.441  -7.299  1.00 94.22  ?  214 THR B OG1   1 
ATOM   3866 C  CG2   . THR B 1 214 ? -11.302 18.163  -5.726  1.00 91.40  ?  214 THR B CG2   1 
ATOM   3867 N  N     . THR B 1 215 ? -11.609 13.778  -4.408  1.00 99.63  ?  215 THR B N     1 
ATOM   3868 C  CA    . THR B 1 215 ? -11.886 12.349  -4.509  1.00 95.70  ?  215 THR B CA    1 
ATOM   3869 C  C     . THR B 1 215 ? -12.749 12.070  -5.743  1.00 92.23  ?  215 THR B C     1 
ATOM   3870 O  O     . THR B 1 215 ? -13.290 12.998  -6.352  1.00 89.07  ?  215 THR B O     1 
ATOM   3871 C  CB    . THR B 1 215 ? -12.545 11.879  -3.212  1.00 96.31  ?  215 THR B CB    1 
ATOM   3872 O  OG1   . THR B 1 215 ? -13.655 12.730  -2.901  1.00 99.97  ?  215 THR B OG1   1 
ATOM   3873 C  CG2   . THR B 1 215 ? -11.542 11.921  -2.064  1.00 93.61  ?  215 THR B CG2   1 
ATOM   3874 N  N     . PRO B 1 216 ? -12.879 10.774  -6.158  1.00 87.79  ?  216 PRO B N     1 
ATOM   3875 C  CA    . PRO B 1 216 ? -13.565 10.435  -7.424  1.00 83.20  ?  216 PRO B CA    1 
ATOM   3876 C  C     . PRO B 1 216 ? -14.885 11.135  -7.712  1.00 80.92  ?  216 PRO B C     1 
ATOM   3877 O  O     . PRO B 1 216 ? -15.959 10.591  -7.429  1.00 80.97  ?  216 PRO B O     1 
ATOM   3878 C  CB    . PRO B 1 216 ? -13.788 8.928   -7.283  1.00 84.40  ?  216 PRO B CB    1 
ATOM   3879 C  CG    . PRO B 1 216 ? -12.588 8.474   -6.510  1.00 84.90  ?  216 PRO B CG    1 
ATOM   3880 C  CD    . PRO B 1 216 ? -12.184 9.604   -5.594  1.00 86.78  ?  216 PRO B CD    1 
ATOM   3881 N  N     . THR B 1 217 ? -14.792 12.251  -8.428  1.00 84.18  ?  217 THR B N     1 
ATOM   3882 C  CA    . THR B 1 217 ? -15.934 13.165  -8.692  1.00 82.75  ?  217 THR B CA    1 
ATOM   3883 C  C     . THR B 1 217 ? -17.061 12.616  -9.574  1.00 81.22  ?  217 THR B C     1 
ATOM   3884 O  O     . THR B 1 217 ? -18.113 13.259  -9.476  1.00 78.74  ?  217 THR B O     1 
ATOM   3885 C  CB    . THR B 1 217 ? -15.446 14.509  -9.234  1.00 76.17  ?  217 THR B CB    1 
ATOM   3886 O  OG1   . THR B 1 217 ? -15.394 14.386  -10.651 1.00 75.56  ?  217 THR B OG1   1 
ATOM   3887 C  CG2   . THR B 1 217 ? -14.076 14.869  -8.722  1.00 78.76  ?  217 THR B CG2   1 
ATOM   3888 N  N     . SER B 1 218 ? -16.960 11.418  -10.162 1.00 83.22  ?  218 SER B N     1 
ATOM   3889 C  CA    . SER B 1 218 ? -17.945 10.808  -11.114 1.00 77.11  ?  218 SER B CA    1 
ATOM   3890 C  C     . SER B 1 218 ? -17.879 11.504  -12.468 1.00 77.64  ?  218 SER B C     1 
ATOM   3891 O  O     . SER B 1 218 ? -18.573 11.066  -13.390 1.00 75.23  ?  218 SER B O     1 
ATOM   3892 C  CB    . SER B 1 218 ? -19.361 10.584  -10.665 1.00 67.14  ?  218 SER B CB    1 
ATOM   3893 O  OG    . SER B 1 218 ? -20.233 10.602  -11.792 1.00 60.28  ?  218 SER B OG    1 
ATOM   3894 N  N     . ASP B 1 219 ? -17.101 12.578  -12.547 1.00 76.75  ?  219 ASP B N     1 
ATOM   3895 C  CA    . ASP B 1 219 ? -16.763 13.155  -13.873 1.00 80.37  ?  219 ASP B CA    1 
ATOM   3896 C  C     . ASP B 1 219 ? -15.648 12.255  -14.431 1.00 75.95  ?  219 ASP B C     1 
ATOM   3897 O  O     . ASP B 1 219 ? -15.516 12.165  -15.654 1.00 70.04  ?  219 ASP B O     1 
ATOM   3898 C  CB    . ASP B 1 219 ? -16.235 14.582  -13.753 1.00 85.32  ?  219 ASP B CB    1 
ATOM   3899 C  CG    . ASP B 1 219 ? -17.290 15.591  -13.355 1.00 87.06  ?  219 ASP B CG    1 
ATOM   3900 O  OD1   . ASP B 1 219 ? -18.462 15.185  -13.230 1.00 88.95  ?  219 ASP B OD1   1 
ATOM   3901 O  OD2   . ASP B 1 219 ? -16.925 16.771  -13.171 1.00 82.04  ?  219 ASP B OD2   1 
ATOM   3902 N  N     . ASP B 1 220 ? -14.863 11.671  -13.516 1.00 72.13  ?  220 ASP B N     1 
ATOM   3903 C  CA    . ASP B 1 220 ? -13.782 10.689  -13.715 1.00 69.45  ?  220 ASP B CA    1 
ATOM   3904 C  C     . ASP B 1 220 ? -14.280 9.531   -14.584 1.00 65.90  ?  220 ASP B C     1 
ATOM   3905 O  O     . ASP B 1 220 ? -13.545 9.214   -15.500 1.00 69.47  ?  220 ASP B O     1 
ATOM   3906 C  CB    . ASP B 1 220 ? -13.228 10.241  -12.364 1.00 71.81  ?  220 ASP B CB    1 
ATOM   3907 C  CG    . ASP B 1 220 ? -12.533 11.337  -11.573 1.00 75.66  ?  220 ASP B CG    1 
ATOM   3908 O  OD1   . ASP B 1 220 ? -13.222 12.242  -11.111 1.00 80.02  ?  220 ASP B OD1   1 
ATOM   3909 O  OD2   . ASP B 1 220 ? -11.306 11.256  -11.406 1.00 73.77  ?  220 ASP B OD2   1 
ATOM   3910 N  N     . ILE B 1 221 ? -15.440 8.914   -14.322 1.00 66.92  ?  221 ILE B N     1 
ATOM   3911 C  CA    . ILE B 1 221 ? -15.816 7.833   -15.227 1.00 66.06  ?  221 ILE B CA    1 
ATOM   3912 C  C     . ILE B 1 221 ? -15.974 8.361   -16.646 1.00 62.06  ?  221 ILE B C     1 
ATOM   3913 O  O     . ILE B 1 221 ? -15.487 7.751   -17.602 1.00 56.57  ?  221 ILE B O     1 
ATOM   3914 C  CB    . ILE B 1 221 ? -17.094 7.126   -14.745 1.00 64.11  ?  221 ILE B CB    1 
ATOM   3915 C  CG1   . ILE B 1 221 ? -16.745 6.058   -13.710 1.00 68.35  ?  221 ILE B CG1   1 
ATOM   3916 C  CG2   . ILE B 1 221 ? -17.826 6.490   -15.927 1.00 55.32  ?  221 ILE B CG2   1 
ATOM   3917 C  CD1   . ILE B 1 221 ? -17.780 5.940   -12.615 1.00 71.01  ?  221 ILE B CD1   1 
ATOM   3918 N  N     . ALA B 1 222 ? -16.640 9.512   -16.803 1.00 65.42  ?  222 ALA B N     1 
ATOM   3919 C  CA    . ALA B 1 222 ? -16.859 10.075  -18.134 1.00 60.73  ?  222 ALA B CA    1 
ATOM   3920 C  C     . ALA B 1 222 ? -15.551 10.344  -18.859 1.00 58.21  ?  222 ALA B C     1 
ATOM   3921 O  O     . ALA B 1 222 ? -15.502 10.247  -20.091 1.00 57.35  ?  222 ALA B O     1 
ATOM   3922 C  CB    . ALA B 1 222 ? -17.674 11.363  -18.043 1.00 60.27  ?  222 ALA B CB    1 
ATOM   3923 N  N     . ALA B 1 223 ? -14.482 10.663  -18.116 1.00 61.04  ?  223 ALA B N     1 
ATOM   3924 C  CA    . ALA B 1 223 ? -13.193 11.014  -18.721 1.00 62.63  ?  223 ALA B CA    1 
ATOM   3925 C  C     . ALA B 1 223 ? -12.342 9.786   -19.070 1.00 55.48  ?  223 ALA B C     1 
ATOM   3926 O  O     . ALA B 1 223 ? -11.757 9.727   -20.152 1.00 53.43  ?  223 ALA B O     1 
ATOM   3927 C  CB    . ALA B 1 223 ? -12.425 11.950  -17.790 1.00 59.07  ?  223 ALA B CB    1 
ATOM   3928 N  N     . LEU B 1 224 ? -12.231 8.818   -18.154 1.00 50.64  ?  224 LEU B N     1 
ATOM   3929 C  CA    . LEU B 1 224 ? -11.602 7.543   -18.482 1.00 53.06  ?  224 LEU B CA    1 
ATOM   3930 C  C     . LEU B 1 224 ? -12.251 6.873   -19.684 1.00 55.53  ?  224 LEU B C     1 
ATOM   3931 O  O     . LEU B 1 224 ? -11.551 6.286   -20.515 1.00 54.22  ?  224 LEU B O     1 
ATOM   3932 C  CB    . LEU B 1 224 ? -11.648 6.596   -17.289 1.00 54.79  ?  224 LEU B CB    1 
ATOM   3933 C  CG    . LEU B 1 224 ? -10.458 5.645   -17.176 1.00 58.21  ?  224 LEU B CG    1 
ATOM   3934 C  CD1   . LEU B 1 224 ? -9.143  6.288   -17.626 1.00 56.16  ?  224 LEU B CD1   1 
ATOM   3935 C  CD2   . LEU B 1 224 ? -10.364 5.123   -15.756 1.00 54.91  ?  224 LEU B CD2   1 
ATOM   3936 N  N     . LYS B 1 225 ? -13.587 6.923   -19.783 1.00 55.21  ?  225 LYS B N     1 
ATOM   3937 C  CA    . LYS B 1 225 ? -14.255 6.242   -20.887 1.00 53.46  ?  225 LYS B CA    1 
ATOM   3938 C  C     . LYS B 1 225 ? -13.839 6.831   -22.224 1.00 52.64  ?  225 LYS B C     1 
ATOM   3939 O  O     . LYS B 1 225 ? -13.881 6.128   -23.242 1.00 47.70  ?  225 LYS B O     1 
ATOM   3940 C  CB    . LYS B 1 225 ? -15.775 6.308   -20.735 1.00 50.83  ?  225 LYS B CB    1 
ATOM   3941 C  CG    . LYS B 1 225 ? -16.375 5.182   -19.892 1.00 59.97  ?  225 LYS B CG    1 
ATOM   3942 C  CD    . LYS B 1 225 ? -16.921 4.016   -20.757 1.00 60.31  ?  225 LYS B CD    1 
ATOM   3943 C  CE    . LYS B 1 225 ? -17.595 2.937   -19.862 1.00 64.56  ?  225 LYS B CE    1 
ATOM   3944 N  NZ    . LYS B 1 225 ? -17.477 1.507   -20.348 1.00 64.31  ?  225 LYS B NZ    1 
ATOM   3945 N  N     . VAL B 1 226 ? -13.459 8.120   -22.230 1.00 48.73  ?  226 VAL B N     1 
ATOM   3946 C  CA    . VAL B 1 226 ? -12.811 8.753   -23.379 1.00 51.45  ?  226 VAL B CA    1 
ATOM   3947 C  C     . VAL B 1 226 ? -11.475 8.085   -23.701 1.00 50.93  ?  226 VAL B C     1 
ATOM   3948 O  O     . VAL B 1 226 ? -11.123 7.895   -24.870 1.00 47.39  ?  226 VAL B O     1 
ATOM   3949 C  CB    . VAL B 1 226 ? -12.611 10.256  -23.110 1.00 57.90  ?  226 VAL B CB    1 
ATOM   3950 C  CG1   . VAL B 1 226 ? -11.904 10.942  -24.277 1.00 44.75  ?  226 VAL B CG1   1 
ATOM   3951 C  CG2   . VAL B 1 226 ? -13.935 10.920  -22.800 1.00 66.12  ?  226 VAL B CG2   1 
ATOM   3952 N  N     . TYR B 1 227 ? -10.682 7.770   -22.687 1.00 50.22  ?  227 TYR B N     1 
ATOM   3953 C  CA    . TYR B 1 227 ? -9.432  7.096   -23.000 1.00 45.43  ?  227 TYR B CA    1 
ATOM   3954 C  C     . TYR B 1 227 ? -9.689  5.697   -23.510 1.00 45.17  ?  227 TYR B C     1 
ATOM   3955 O  O     . TYR B 1 227 ? -9.030  5.244   -24.458 1.00 45.84  ?  227 TYR B O     1 
ATOM   3956 C  CB    . TYR B 1 227 ? -8.524  7.056   -21.783 1.00 49.34  ?  227 TYR B CB    1 
ATOM   3957 C  CG    . TYR B 1 227 ? -7.773  8.333   -21.681 1.00 49.68  ?  227 TYR B CG    1 
ATOM   3958 C  CD1   . TYR B 1 227 ? -6.579  8.507   -22.358 1.00 42.42  ?  227 TYR B CD1   1 
ATOM   3959 C  CD2   . TYR B 1 227 ? -8.300  9.399   -20.968 1.00 49.58  ?  227 TYR B CD2   1 
ATOM   3960 C  CE1   . TYR B 1 227 ? -5.919  9.696   -22.278 1.00 51.53  ?  227 TYR B CE1   1 
ATOM   3961 C  CE2   . TYR B 1 227 ? -7.644  10.580  -20.881 1.00 46.64  ?  227 TYR B CE2   1 
ATOM   3962 C  CZ    . TYR B 1 227 ? -6.463  10.724  -21.528 1.00 51.19  ?  227 TYR B CZ    1 
ATOM   3963 O  OH    . TYR B 1 227 ? -5.825  11.914  -21.439 1.00 58.57  ?  227 TYR B OH    1 
ATOM   3964 N  N     . GLU B 1 228 ? -10.629 4.988   -22.883 1.00 44.10  ?  228 GLU B N     1 
ATOM   3965 C  CA    . GLU B 1 228 ? -10.927 3.639   -23.332 1.00 43.01  ?  228 GLU B CA    1 
ATOM   3966 C  C     . GLU B 1 228 ? -11.566 3.649   -24.715 1.00 40.18  ?  228 GLU B C     1 
ATOM   3967 O  O     . GLU B 1 228 ? -11.299 2.765   -25.523 1.00 41.95  ?  228 GLU B O     1 
ATOM   3968 C  CB    . GLU B 1 228 ? -11.827 2.911   -22.334 1.00 36.77  ?  228 GLU B CB    1 
ATOM   3969 C  CG    . GLU B 1 228 ? -12.270 1.593   -22.936 1.00 41.62  ?  228 GLU B CG    1 
ATOM   3970 C  CD    . GLU B 1 228 ? -13.124 0.750   -22.027 1.00 49.46  ?  228 GLU B CD    1 
ATOM   3971 O  OE1   . GLU B 1 228 ? -13.859 1.324   -21.198 1.00 48.86  ?  228 GLU B OE1   1 
ATOM   3972 O  OE2   . GLU B 1 228 ? -13.067 -0.493  -22.153 1.00 51.66  ?  228 GLU B OE2   1 
ATOM   3973 N  N     . ASP B 1 229 ? -12.429 4.620   -25.007 1.00 40.41  ?  229 ASP B N     1 
ATOM   3974 C  CA    . ASP B 1 229 ? -13.080 4.629   -26.311 1.00 39.60  ?  229 ASP B CA    1 
ATOM   3975 C  C     . ASP B 1 229 ? -12.063 4.856   -27.429 1.00 42.47  ?  229 ASP B C     1 
ATOM   3976 O  O     . ASP B 1 229 ? -12.073 4.151   -28.441 1.00 47.75  ?  229 ASP B O     1 
ATOM   3977 C  CB    . ASP B 1 229 ? -14.183 5.688   -26.353 1.00 42.85  ?  229 ASP B CB    1 
ATOM   3978 C  CG    . ASP B 1 229 ? -15.450 5.295   -25.535 1.00 47.81  ?  229 ASP B CG    1 
ATOM   3979 O  OD1   . ASP B 1 229 ? -15.615 4.134   -25.077 1.00 45.09  ?  229 ASP B OD1   1 
ATOM   3980 O  OD2   . ASP B 1 229 ? -16.289 6.192   -25.334 1.00 47.44  ?  229 ASP B OD2   1 
ATOM   3981 N  N     . ASN B 1 230 ? -11.168 5.838   -27.259 1.00 43.27  ?  230 ASN B N     1 
ATOM   3982 C  CA    . ASN B 1 230 ? -10.122 6.088   -28.250 1.00 42.25  ?  230 ASN B CA    1 
ATOM   3983 C  C     . ASN B 1 230 ? -9.154  4.914   -28.340 1.00 38.90  ?  230 ASN B C     1 
ATOM   3984 O  O     . ASN B 1 230 ? -8.702  4.560   -29.438 1.00 31.62  ?  230 ASN B O     1 
ATOM   3985 C  CB    . ASN B 1 230 ? -9.380  7.385   -27.914 1.00 41.04  ?  230 ASN B CB    1 
ATOM   3986 C  CG    . ASN B 1 230 ? -10.147 8.623   -28.370 1.00 47.32  ?  230 ASN B CG    1 
ATOM   3987 O  OD1   . ASN B 1 230 ? -11.339 8.548   -28.705 1.00 47.54  ?  230 ASN B OD1   1 
ATOM   3988 N  ND2   . ASN B 1 230 ? -9.469  9.764   -28.391 1.00 45.60  ?  230 ASN B ND2   1 
ATOM   3989 N  N     . TRP B 1 231 ? -8.838  4.296   -27.192 1.00 38.13  ?  231 TRP B N     1 
ATOM   3990 C  CA    . TRP B 1 231 ? -8.003  3.101   -27.179 1.00 37.26  ?  231 TRP B CA    1 
ATOM   3991 C  C     . TRP B 1 231 ? -8.618  1.995   -28.026 1.00 36.96  ?  231 TRP B C     1 
ATOM   3992 O  O     . TRP B 1 231 ? -7.908  1.257   -28.713 1.00 36.58  ?  231 TRP B O     1 
ATOM   3993 C  CB    . TRP B 1 231 ? -7.768  2.632   -25.735 1.00 40.00  ?  231 TRP B CB    1 
ATOM   3994 C  CG    . TRP B 1 231 ? -6.894  1.393   -25.661 1.00 38.51  ?  231 TRP B CG    1 
ATOM   3995 C  CD1   . TRP B 1 231 ? -5.519  1.343   -25.646 1.00 36.86  ?  231 TRP B CD1   1 
ATOM   3996 C  CD2   . TRP B 1 231 ? -7.345  0.038   -25.604 1.00 39.11  ?  231 TRP B CD2   1 
ATOM   3997 N  NE1   . TRP B 1 231 ? -5.088  0.033   -25.603 1.00 36.52  ?  231 TRP B NE1   1 
ATOM   3998 C  CE2   . TRP B 1 231 ? -6.188  -0.790  -25.578 1.00 38.38  ?  231 TRP B CE2   1 
ATOM   3999 C  CE3   . TRP B 1 231 ? -8.615  -0.562  -25.584 1.00 37.00  ?  231 TRP B CE3   1 
ATOM   4000 C  CZ2   . TRP B 1 231 ? -6.268  -2.187  -25.538 1.00 31.58  ?  231 TRP B CZ2   1 
ATOM   4001 C  CZ3   . TRP B 1 231 ? -8.692  -1.946  -25.529 1.00 36.14  ?  231 TRP B CZ3   1 
ATOM   4002 C  CH2   . TRP B 1 231 ? -7.523  -2.744  -25.492 1.00 34.07  ?  231 TRP B CH2   1 
ATOM   4003 N  N     . HIS B 1 232 ? -9.938  1.870   -28.006 1.00 39.53  ?  232 HIS B N     1 
ATOM   4004 C  CA    . HIS B 1 232 ? -10.599 0.899   -28.869 1.00 42.75  ?  232 HIS B CA    1 
ATOM   4005 C  C     . HIS B 1 232 ? -10.490 1.291   -30.346 1.00 36.62  ?  232 HIS B C     1 
ATOM   4006 O  O     . HIS B 1 232 ? -10.153 0.456   -31.185 1.00 38.83  ?  232 HIS B O     1 
ATOM   4007 C  CB    . HIS B 1 232 ? -12.071 0.744   -28.453 1.00 39.77  ?  232 HIS B CB    1 
ATOM   4008 C  CG    . HIS B 1 232 ? -12.300 -0.342  -27.450 1.00 45.71  ?  232 HIS B CG    1 
ATOM   4009 N  ND1   . HIS B 1 232 ? -12.148 -1.679  -27.756 1.00 47.99  ?  232 HIS B ND1   1 
ATOM   4010 C  CD2   . HIS B 1 232 ? -12.678 -0.291  -26.146 1.00 52.01  ?  232 HIS B CD2   1 
ATOM   4011 C  CE1   . HIS B 1 232 ? -12.410 -2.405  -26.680 1.00 55.77  ?  232 HIS B CE1   1 
ATOM   4012 N  NE2   . HIS B 1 232 ? -12.736 -1.588  -25.690 1.00 53.13  ?  232 HIS B NE2   1 
ATOM   4013 N  N     . LEU B 1 233 ? -10.829 2.540   -30.680 1.00 32.49  ?  233 LEU B N     1 
ATOM   4014 C  CA    . LEU B 1 233 ? -10.704 3.041   -32.049 1.00 38.93  ?  233 LEU B CA    1 
ATOM   4015 C  C     . LEU B 1 233 ? -9.346  2.723   -32.636 1.00 33.87  ?  233 LEU B C     1 
ATOM   4016 O  O     . LEU B 1 233 ? -9.231  2.317   -33.796 1.00 34.49  ?  233 LEU B O     1 
ATOM   4017 C  CB    . LEU B 1 233 ? -10.895 4.569   -32.106 1.00 39.01  ?  233 LEU B CB    1 
ATOM   4018 C  CG    . LEU B 1 233 ? -12.226 5.302   -32.019 1.00 47.63  ?  233 LEU B CG    1 
ATOM   4019 C  CD1   . LEU B 1 233 ? -12.158 6.454   -31.019 1.00 53.18  ?  233 LEU B CD1   1 
ATOM   4020 C  CD2   . LEU B 1 233 ? -12.568 5.852   -33.407 1.00 49.48  ?  233 LEU B CD2   1 
ATOM   4021 N  N     . ILE B 1 234 ? -8.298  2.976   -31.865 1.00 31.53  ?  234 ILE B N     1 
ATOM   4022 C  CA    . ILE B 1 234 ? -6.959  2.865   -32.415 1.00 35.88  ?  234 ILE B CA    1 
ATOM   4023 C  C     . ILE B 1 234 ? -6.593  1.392   -32.564 1.00 37.06  ?  234 ILE B C     1 
ATOM   4024 O  O     . ILE B 1 234 ? -5.982  0.992   -33.567 1.00 36.10  ?  234 ILE B O     1 
ATOM   4025 C  CB    . ILE B 1 234 ? -5.968  3.668   -31.547 1.00 32.31  ?  234 ILE B CB    1 
ATOM   4026 C  CG1   . ILE B 1 234 ? -6.259  5.169   -31.695 1.00 33.12  ?  234 ILE B CG1   1 
ATOM   4027 C  CG2   . ILE B 1 234 ? -4.572  3.412   -31.962 1.00 30.08  ?  234 ILE B CG2   1 
ATOM   4028 C  CD1   . ILE B 1 234 ? -5.882  6.004   -30.501 1.00 31.92  ?  234 ILE B CD1   1 
ATOM   4029 N  N     . CYS B 1 235 ? -7.059  0.548   -31.624 1.00 35.54  ?  235 CYS B N     1 
ATOM   4030 C  CA    . CYS B 1 235 ? -6.819  -0.894  -31.699 1.00 35.02  ?  235 CYS B CA    1 
ATOM   4031 C  C     . CYS B 1 235 ? -7.421  -1.499  -32.958 1.00 36.34  ?  235 CYS B C     1 
ATOM   4032 O  O     . CYS B 1 235 ? -6.890  -2.484  -33.489 1.00 39.47  ?  235 CYS B O     1 
ATOM   4033 C  CB    . CYS B 1 235 ? -7.397  -1.596  -30.471 1.00 31.23  ?  235 CYS B CB    1 
ATOM   4034 S  SG    . CYS B 1 235 ? -6.418  -1.544  -28.927 1.00 35.85  ?  235 CYS B SG    1 
ATOM   4035 N  N     . GLU B 1 236 ? -8.551  -0.947  -33.422 1.00 38.14  ?  236 GLU B N     1 
ATOM   4036 C  CA    . GLU B 1 236 ? -9.181  -1.373  -34.668 1.00 37.95  ?  236 GLU B CA    1 
ATOM   4037 C  C     . GLU B 1 236 ? -8.545  -0.731  -35.883 1.00 39.92  ?  236 GLU B C     1 
ATOM   4038 O  O     . GLU B 1 236 ? -8.715  -1.250  -36.984 1.00 41.05  ?  236 GLU B O     1 
ATOM   4039 C  CB    . GLU B 1 236 ? -10.685 -1.047  -34.671 1.00 41.42  ?  236 GLU B CB    1 
ATOM   4040 C  CG    . GLU B 1 236 ? -11.511 -1.891  -33.678 1.00 51.15  ?  236 GLU B CG    1 
ATOM   4041 C  CD    . GLU B 1 236 ? -12.852 -2.413  -34.230 1.00 64.84  ?  236 GLU B CD    1 
ATOM   4042 O  OE1   . GLU B 1 236 ? -12.881 -2.913  -35.378 1.00 57.00  ?  236 GLU B OE1   1 
ATOM   4043 O  OE2   . GLU B 1 236 ? -13.875 -2.354  -33.493 1.00 73.48  ?  236 GLU B OE2   1 
ATOM   4044 N  N     . ARG B 1 237 ? -7.857  0.410   -35.718 1.00 39.05  ?  237 ARG B N     1 
ATOM   4045 C  CA    . ARG B 1 237 ? -7.021  0.910   -36.798 1.00 36.29  ?  237 ARG B CA    1 
ATOM   4046 C  C     . ARG B 1 237 ? -5.741  0.106   -36.922 1.00 37.85  ?  237 ARG B C     1 
ATOM   4047 O  O     . ARG B 1 237 ? -5.184  0.031   -38.016 1.00 36.29  ?  237 ARG B O     1 
ATOM   4048 C  CB    . ARG B 1 237 ? -6.638  2.372   -36.592 1.00 37.22  ?  237 ARG B CB    1 
ATOM   4049 C  CG    . ARG B 1 237 ? -7.793  3.329   -36.419 1.00 36.48  ?  237 ARG B CG    1 
ATOM   4050 C  CD    . ARG B 1 237 ? -7.294  4.738   -36.667 1.00 35.90  ?  237 ARG B CD    1 
ATOM   4051 N  NE    . ARG B 1 237 ? -8.354  5.721   -36.518 1.00 40.56  ?  237 ARG B NE    1 
ATOM   4052 C  CZ    . ARG B 1 237 ? -8.140  6.970   -36.143 1.00 35.44  ?  237 ARG B CZ    1 
ATOM   4053 N  NH1   . ARG B 1 237 ? -6.917  7.413   -35.910 1.00 34.08  ?  237 ARG B NH1   1 
ATOM   4054 N  NH2   . ARG B 1 237 ? -9.173  7.790   -36.005 1.00 32.21  ?  237 ARG B NH2   1 
ATOM   4055 N  N     . TRP B 1 238 ? -5.254  -0.475  -35.819 1.00 37.91  ?  238 TRP B N     1 
ATOM   4056 C  CA    . TRP B 1 238 ? -3.918  -1.073  -35.763 1.00 34.66  ?  238 TRP B CA    1 
ATOM   4057 C  C     . TRP B 1 238 ? -3.942  -2.389  -34.985 1.00 36.48  ?  238 TRP B C     1 
ATOM   4058 O  O     . TRP B 1 238 ? -3.668  -2.417  -33.779 1.00 34.39  ?  238 TRP B O     1 
ATOM   4059 C  CB    . TRP B 1 238 ? -2.915  -0.094  -35.142 1.00 35.32  ?  238 TRP B CB    1 
ATOM   4060 C  CG    . TRP B 1 238 ? -2.759  1.159   -35.947 1.00 36.40  ?  238 TRP B CG    1 
ATOM   4061 C  CD1   . TRP B 1 238 ? -3.197  2.395   -35.621 1.00 30.82  ?  238 TRP B CD1   1 
ATOM   4062 C  CD2   . TRP B 1 238 ? -2.147  1.271   -37.249 1.00 33.49  ?  238 TRP B CD2   1 
ATOM   4063 N  NE1   . TRP B 1 238 ? -2.882  3.287   -36.631 1.00 34.13  ?  238 TRP B NE1   1 
ATOM   4064 C  CE2   . TRP B 1 238 ? -2.246  2.613   -37.643 1.00 33.83  ?  238 TRP B CE2   1 
ATOM   4065 C  CE3   . TRP B 1 238 ? -1.527  0.363   -38.108 1.00 31.59  ?  238 TRP B CE3   1 
ATOM   4066 C  CZ2   . TRP B 1 238 ? -1.732  3.078   -38.869 1.00 36.93  ?  238 TRP B CZ2   1 
ATOM   4067 C  CZ3   . TRP B 1 238 ? -1.022  0.823   -39.328 1.00 37.03  ?  238 TRP B CZ3   1 
ATOM   4068 C  CH2   . TRP B 1 238 ? -1.127  2.161   -39.694 1.00 32.65  ?  238 TRP B CH2   1 
ATOM   4069 N  N     . PRO B 1 239 ? -4.243  -3.505  -35.655 1.00 40.52  ?  239 PRO B N     1 
ATOM   4070 C  CA    . PRO B 1 239 ? -4.164  -4.824  -34.987 1.00 37.75  ?  239 PRO B CA    1 
ATOM   4071 C  C     . PRO B 1 239 ? -2.747  -5.124  -34.519 1.00 40.46  ?  239 PRO B C     1 
ATOM   4072 O  O     . PRO B 1 239 ? -1.774  -4.739  -35.169 1.00 40.70  ?  239 PRO B O     1 
ATOM   4073 C  CB    . PRO B 1 239 ? -4.609  -5.810  -36.077 1.00 38.61  ?  239 PRO B CB    1 
ATOM   4074 C  CG    . PRO B 1 239 ? -5.278  -4.956  -37.176 1.00 41.39  ?  239 PRO B CG    1 
ATOM   4075 C  CD    . PRO B 1 239 ? -4.606  -3.600  -37.085 1.00 38.99  ?  239 PRO B CD    1 
ATOM   4076 N  N     . ALA B 1 240 ? -2.625  -5.794  -33.369 1.00 37.56  ?  240 ALA B N     1 
ATOM   4077 C  CA    . ALA B 1 240 ? -1.297  -6.047  -32.808 1.00 39.01  ?  240 ALA B CA    1 
ATOM   4078 C  C     . ALA B 1 240 ? -0.428  -6.838  -33.781 1.00 44.72  ?  240 ALA B C     1 
ATOM   4079 O  O     . ALA B 1 240 ? -0.915  -7.705  -34.512 1.00 39.94  ?  240 ALA B O     1 
ATOM   4080 C  CB    . ALA B 1 240 ? -1.379  -6.810  -31.488 1.00 41.79  ?  240 ALA B CB    1 
ATOM   4081 N  N     . ALA B 1 241 ? 0.876   -6.534  -33.779 1.00 42.64  ?  241 ALA B N     1 
ATOM   4082 C  CA    . ALA B 1 241 ? 1.782   -7.199  -34.713 1.00 49.78  ?  241 ALA B CA    1 
ATOM   4083 C  C     . ALA B 1 241 ? 2.058   -8.651  -34.319 1.00 49.21  ?  241 ALA B C     1 
ATOM   4084 O  O     . ALA B 1 241 ? 2.394   -9.454  -35.192 1.00 55.17  ?  241 ALA B O     1 
ATOM   4085 C  CB    . ALA B 1 241 ? 3.095   -6.411  -34.840 1.00 47.27  ?  241 ALA B CB    1 
ATOM   4086 N  N     . THR B 1 242 ? 1.930   -9.012  -33.033 1.00 41.89  ?  242 THR B N     1 
ATOM   4087 C  CA    . THR B 1 242 ? 2.120   -10.378 -32.577 1.00 33.61  ?  242 THR B CA    1 
ATOM   4088 C  C     . THR B 1 242 ? 0.868   -10.903 -31.877 1.00 49.12  ?  242 THR B C     1 
ATOM   4089 O  O     . THR B 1 242 ? 0.038   -10.135 -31.364 1.00 42.90  ?  242 THR B O     1 
ATOM   4090 C  CB    . THR B 1 242 ? 3.295   -10.512 -31.606 1.00 41.94  ?  242 THR B CB    1 
ATOM   4091 O  OG1   . THR B 1 242 ? 2.942   -9.950  -30.338 1.00 45.81  ?  242 THR B OG1   1 
ATOM   4092 C  CG2   . THR B 1 242 ? 4.564   -9.840  -32.142 1.00 43.16  ?  242 THR B CG2   1 
ATOM   4093 N  N     . GLU B 1 243 ? 0.770   -12.246 -31.847 1.00 49.84  ?  243 GLU B N     1 
ATOM   4094 C  CA    . GLU B 1 243 ? -0.351  -12.925 -31.199 1.00 43.42  ?  243 GLU B CA    1 
ATOM   4095 C  C     . GLU B 1 243 ? -0.382  -12.607 -29.714 1.00 44.81  ?  243 GLU B C     1 
ATOM   4096 O  O     . GLU B 1 243 ? -1.439  -12.291 -29.141 1.00 42.49  ?  243 GLU B O     1 
ATOM   4097 C  CB    . GLU B 1 243 ? -0.225  -14.439 -31.428 1.00 43.65  ?  243 GLU B CB    1 
ATOM   4098 C  CG    . GLU B 1 243 ? -1.499  -15.258 -31.189 1.00 43.66  ?  243 GLU B CG    1 
ATOM   4099 C  CD    . GLU B 1 243 ? -2.689  -14.818 -32.051 1.00 50.00  ?  243 GLU B CD    1 
ATOM   4100 O  OE1   . GLU B 1 243 ? -2.497  -14.460 -33.241 1.00 51.12  ?  243 GLU B OE1   1 
ATOM   4101 O  OE2   . GLU B 1 243 ? -3.830  -14.831 -31.533 1.00 59.31  ?  243 GLU B OE2   1 
ATOM   4102 N  N     . ARG B 1 244 ? 0.787   -12.664 -29.088 1.00 42.64  ?  244 ARG B N     1 
ATOM   4103 C  CA    . ARG B 1 244 ? 0.920   -12.366 -27.674 1.00 45.54  ?  244 ARG B CA    1 
ATOM   4104 C  C     . ARG B 1 244 ? 0.337   -11.003 -27.328 1.00 47.77  ?  244 ARG B C     1 
ATOM   4105 O  O     . ARG B 1 244 ? -0.431  -10.873 -26.365 1.00 44.70  ?  244 ARG B O     1 
ATOM   4106 C  CB    . ARG B 1 244 ? 2.395   -12.426 -27.311 1.00 47.91  ?  244 ARG B CB    1 
ATOM   4107 C  CG    . ARG B 1 244 ? 2.661   -12.382 -25.851 1.00 52.84  ?  244 ARG B CG    1 
ATOM   4108 C  CD    . ARG B 1 244 ? 1.744   -13.264 -25.027 1.00 55.40  ?  244 ARG B CD    1 
ATOM   4109 N  NE    . ARG B 1 244 ? 2.420   -13.421 -23.749 1.00 65.34  ?  244 ARG B NE    1 
ATOM   4110 C  CZ    . ARG B 1 244 ? 3.466   -14.219 -23.557 1.00 69.18  ?  244 ARG B CZ    1 
ATOM   4111 N  NH1   . ARG B 1 244 ? 3.836   -15.113 -24.470 1.00 74.44  ?  244 ARG B NH1   1 
ATOM   4112 N  NH2   . ARG B 1 244 ? 4.183   -14.091 -22.439 1.00 65.12  ?  244 ARG B NH2   1 
ATOM   4113 N  N     . ALA B 1 245 ? 0.699   -9.963  -28.103 1.00 42.41  ?  245 ALA B N     1 
ATOM   4114 C  CA    . ALA B 1 245 ? 0.199   -8.625  -27.798 1.00 44.38  ?  245 ALA B CA    1 
ATOM   4115 C  C     . ALA B 1 245 ? -1.293  -8.527  -28.084 1.00 43.94  ?  245 ALA B C     1 
ATOM   4116 O  O     . ALA B 1 245 ? -2.032  -7.888  -27.322 1.00 43.59  ?  245 ALA B O     1 
ATOM   4117 C  CB    . ALA B 1 245 ? 0.987   -7.558  -28.564 1.00 41.17  ?  245 ALA B CB    1 
ATOM   4118 N  N     . GLU B 1 246 ? -1.765  -9.175  -29.158 1.00 42.48  ?  246 GLU B N     1 
ATOM   4119 C  CA    . GLU B 1 246 ? -3.209  -9.291  -29.338 1.00 43.68  ?  246 GLU B CA    1 
ATOM   4120 C  C     . GLU B 1 246 ? -3.853  -9.933  -28.116 1.00 45.40  ?  246 GLU B C     1 
ATOM   4121 O  O     . GLU B 1 246 ? -4.945  -9.534  -27.705 1.00 44.66  ?  246 GLU B O     1 
ATOM   4122 C  CB    . GLU B 1 246 ? -3.543  -10.080 -30.611 1.00 39.52  ?  246 GLU B CB    1 
ATOM   4123 C  CG    . GLU B 1 246 ? -4.880  -9.679  -31.321 1.00 43.78  ?  246 GLU B CG    1 
ATOM   4124 C  CD    . GLU B 1 246 ? -4.926  -8.213  -31.930 1.00 57.95  ?  246 GLU B CD    1 
ATOM   4125 O  OE1   . GLU B 1 246 ? -4.875  -7.204  -31.178 1.00 54.86  ?  246 GLU B OE1   1 
ATOM   4126 O  OE2   . GLU B 1 246 ? -5.040  -8.057  -33.179 1.00 56.60  ?  246 GLU B OE2   1 
ATOM   4127 N  N     . GLN B 1 247 ? -3.166  -10.879 -27.479 1.00 47.90  ?  247 GLN B N     1 
ATOM   4128 C  CA    . GLN B 1 247 ? -3.730  -11.499 -26.288 1.00 47.38  ?  247 GLN B CA    1 
ATOM   4129 C  C     . GLN B 1 247 ? -3.732  -10.537 -25.110 1.00 41.58  ?  247 GLN B C     1 
ATOM   4130 O  O     . GLN B 1 247 ? -4.750  -10.386 -24.438 1.00 41.48  ?  247 GLN B O     1 
ATOM   4131 C  CB    . GLN B 1 247 ? -2.966  -12.767 -25.952 1.00 44.96  ?  247 GLN B CB    1 
ATOM   4132 C  CG    . GLN B 1 247 ? -3.444  -13.964 -26.711 1.00 48.49  ?  247 GLN B CG    1 
ATOM   4133 C  CD    . GLN B 1 247 ? -2.505  -15.155 -26.503 1.00 60.89  ?  247 GLN B CD    1 
ATOM   4134 O  OE1   . GLN B 1 247 ? -1.624  -15.129 -25.623 1.00 56.68  ?  247 GLN B OE1   1 
ATOM   4135 N  NE2   . GLN B 1 247 ? -2.683  -16.202 -27.315 1.00 64.12  ?  247 GLN B NE2   1 
ATOM   4136 N  N     . VAL B 1 248 ? -2.611  -9.853  -24.862 1.00 41.90  ?  248 VAL B N     1 
ATOM   4137 C  CA    . VAL B 1 248 ? -2.501  -8.983  -23.690 1.00 43.22  ?  248 VAL B CA    1 
ATOM   4138 C  C     . VAL B 1 248 ? -3.384  -7.724  -23.794 1.00 48.98  ?  248 VAL B C     1 
ATOM   4139 O  O     . VAL B 1 248 ? -3.691  -7.089  -22.764 1.00 41.80  ?  248 VAL B O     1 
ATOM   4140 C  CB    . VAL B 1 248 ? -1.006  -8.672  -23.460 1.00 43.06  ?  248 VAL B CB    1 
ATOM   4141 C  CG1   . VAL B 1 248 ? -0.798  -7.471  -22.575 1.00 43.78  ?  248 VAL B CG1   1 
ATOM   4142 C  CG2   . VAL B 1 248 ? -0.318  -9.889  -22.820 1.00 44.44  ?  248 VAL B CG2   1 
ATOM   4143 N  N     . ARG B 1 249 ? -3.854  -7.374  -25.005 1.00 45.38  ?  249 ARG B N     1 
ATOM   4144 C  CA    . ARG B 1 249 ? -4.799  -6.265  -25.133 1.00 42.29  ?  249 ARG B CA    1 
ATOM   4145 C  C     . ARG B 1 249 ? -6.085  -6.516  -24.333 1.00 41.68  ?  249 ARG B C     1 
ATOM   4146 O  O     . ARG B 1 249 ? -6.730  -5.560  -23.885 1.00 45.16  ?  249 ARG B O     1 
ATOM   4147 C  CB    . ARG B 1 249 ? -5.123  -6.008  -26.609 1.00 39.96  ?  249 ARG B CB    1 
ATOM   4148 C  CG    . ARG B 1 249 ? -4.061  -5.186  -27.399 1.00 40.42  ?  249 ARG B CG    1 
ATOM   4149 C  CD    . ARG B 1 249 ? -4.508  -4.988  -28.863 1.00 34.69  ?  249 ARG B CD    1 
ATOM   4150 N  NE    . ARG B 1 249 ? -3.643  -4.079  -29.604 1.00 38.22  ?  249 ARG B NE    1 
ATOM   4151 C  CZ    . ARG B 1 249 ? -3.948  -3.531  -30.777 1.00 38.07  ?  249 ARG B CZ    1 
ATOM   4152 N  NH1   . ARG B 1 249 ? -5.119  -3.743  -31.365 1.00 36.23  ?  249 ARG B NH1   1 
ATOM   4153 N  NH2   . ARG B 1 249 ? -3.065  -2.736  -31.369 1.00 34.48  ?  249 ARG B NH2   1 
ATOM   4154 N  N     . ARG B 1 250 ? -6.459  -7.780  -24.117 1.00 41.36  ?  250 ARG B N     1 
ATOM   4155 C  CA    . ARG B 1 250 ? -7.718  -8.095  -23.432 1.00 44.35  ?  250 ARG B CA    1 
ATOM   4156 C  C     . ARG B 1 250 ? -7.736  -7.628  -21.984 1.00 43.04  ?  250 ARG B C     1 
ATOM   4157 O  O     . ARG B 1 250 ? -8.807  -7.547  -21.386 1.00 50.06  ?  250 ARG B O     1 
ATOM   4158 C  CB    . ARG B 1 250 ? -7.983  -9.602  -23.489 1.00 40.60  ?  250 ARG B CB    1 
ATOM   4159 N  N     . PHE B 1 251 ? -6.577  -7.333  -21.403 1.00 46.63  ?  251 PHE B N     1 
ATOM   4160 C  CA    . PHE B 1 251 ? -6.517  -6.873  -20.025 1.00 45.36  ?  251 PHE B CA    1 
ATOM   4161 C  C     . PHE B 1 251 ? -6.810  -5.382  -19.903 1.00 48.55  ?  251 PHE B C     1 
ATOM   4162 O  O     . PHE B 1 251 ? -7.134  -4.910  -18.806 1.00 50.45  ?  251 PHE B O     1 
ATOM   4163 C  CB    . PHE B 1 251 ? -5.137  -7.205  -19.437 1.00 41.18  ?  251 PHE B CB    1 
ATOM   4164 C  CG    . PHE B 1 251 ? -4.922  -8.681  -19.193 1.00 47.23  ?  251 PHE B CG    1 
ATOM   4165 C  CD1   . PHE B 1 251 ? -5.714  -9.371  -18.274 1.00 50.16  ?  251 PHE B CD1   1 
ATOM   4166 C  CD2   . PHE B 1 251 ? -3.944  -9.383  -19.881 1.00 44.35  ?  251 PHE B CD2   1 
ATOM   4167 C  CE1   . PHE B 1 251 ? -5.524  -10.721 -18.052 1.00 53.39  ?  251 PHE B CE1   1 
ATOM   4168 C  CE2   . PHE B 1 251 ? -3.749  -10.736 -19.668 1.00 47.80  ?  251 PHE B CE2   1 
ATOM   4169 C  CZ    . PHE B 1 251 ? -4.540  -11.409 -18.744 1.00 54.05  ?  251 PHE B CZ    1 
ATOM   4170 N  N     . MET B 1 252 ? -6.712  -4.638  -21.001 1.00 44.55  ?  252 MET B N     1 
ATOM   4171 C  CA    . MET B 1 252 ? -6.959  -3.199  -20.946 1.00 47.75  ?  252 MET B CA    1 
ATOM   4172 C  C     . MET B 1 252 ? -8.406  -2.880  -20.563 1.00 48.90  ?  252 MET B C     1 
ATOM   4173 O  O     . MET B 1 252 ? -8.613  -2.001  -19.710 1.00 46.33  ?  252 MET B O     1 
ATOM   4174 C  CB    . MET B 1 252 ? -6.578  -2.570  -22.293 1.00 41.05  ?  252 MET B CB    1 
ATOM   4175 C  CG    . MET B 1 252 ? -5.161  -2.013  -22.440 1.00 39.22  ?  252 MET B CG    1 
ATOM   4176 S  SD    . MET B 1 252 ? -4.368  -1.407  -20.955 1.00 39.92  ?  252 MET B SD    1 
ATOM   4177 C  CE    . MET B 1 252 ? -5.011  0.266   -20.955 1.00 38.67  ?  252 MET B CE    1 
ATOM   4178 N  N     . PRO B 1 253 ? -9.438  -3.514  -21.143 1.00 46.60  ?  253 PRO B N     1 
ATOM   4179 C  CA    . PRO B 1 253 ? -10.799 -3.266  -20.638 1.00 47.90  ?  253 PRO B CA    1 
ATOM   4180 C  C     . PRO B 1 253 ? -11.005 -3.805  -19.232 1.00 50.47  ?  253 PRO B C     1 
ATOM   4181 O  O     . PRO B 1 253 ? -11.786 -3.228  -18.465 1.00 48.87  ?  253 PRO B O     1 
ATOM   4182 C  CB    . PRO B 1 253 ? -11.696 -3.980  -21.661 1.00 45.32  ?  253 PRO B CB    1 
ATOM   4183 C  CG    . PRO B 1 253 ? -10.808 -4.207  -22.870 1.00 46.82  ?  253 PRO B CG    1 
ATOM   4184 C  CD    . PRO B 1 253 ? -9.453  -4.423  -22.308 1.00 40.73  ?  253 PRO B CD    1 
ATOM   4185 N  N     . VAL B 1 254 ? -10.314 -4.888  -18.868 1.00 49.06  ?  254 VAL B N     1 
ATOM   4186 C  CA    . VAL B 1 254 ? -10.344 -5.358  -17.488 1.00 45.10  ?  254 VAL B CA    1 
ATOM   4187 C  C     . VAL B 1 254 ? -9.814  -4.281  -16.560 1.00 49.23  ?  254 VAL B C     1 
ATOM   4188 O  O     . VAL B 1 254 ? -10.427 -3.963  -15.535 1.00 52.53  ?  254 VAL B O     1 
ATOM   4189 C  CB    . VAL B 1 254 ? -9.554  -6.670  -17.340 1.00 49.95  ?  254 VAL B CB    1 
ATOM   4190 C  CG1   . VAL B 1 254 ? -9.526  -7.120  -15.872 1.00 46.98  ?  254 VAL B CG1   1 
ATOM   4191 C  CG2   . VAL B 1 254 ? -10.150 -7.761  -18.235 1.00 49.09  ?  254 VAL B CG2   1 
ATOM   4192 N  N     . MET B 1 255 ? -8.674  -3.690  -16.909 1.00 50.88  ?  255 MET B N     1 
ATOM   4193 C  CA    . MET B 1 255 ? -8.163  -2.573  -16.120 1.00 54.76  ?  255 MET B CA    1 
ATOM   4194 C  C     . MET B 1 255 ? -9.185  -1.438  -16.010 1.00 54.59  ?  255 MET B C     1 
ATOM   4195 O  O     . MET B 1 255 ? -9.429  -0.922  -14.912 1.00 54.23  ?  255 MET B O     1 
ATOM   4196 C  CB    . MET B 1 255 ? -6.850  -2.058  -16.710 1.00 47.08  ?  255 MET B CB    1 
ATOM   4197 C  CG    . MET B 1 255 ? -6.256  -0.961  -15.862 1.00 52.72  ?  255 MET B CG    1 
ATOM   4198 S  SD    . MET B 1 255 ? -6.684  0.686   -16.460 1.00 58.32  ?  255 MET B SD    1 
ATOM   4199 C  CE    . MET B 1 255 ? -5.230  1.105   -17.400 1.00 50.06  ?  255 MET B CE    1 
ATOM   4200 N  N     . TYR B 1 256 ? -9.769  -1.016  -17.144 1.00 51.74  ?  256 TYR B N     1 
ATOM   4201 C  CA    . TYR B 1 256 ? -10.690 0.122   -17.142 1.00 52.66  ?  256 TYR B CA    1 
ATOM   4202 C  C     . TYR B 1 256 ? -11.912 -0.171  -16.273 1.00 55.02  ?  256 TYR B C     1 
ATOM   4203 O  O     . TYR B 1 256 ? -12.341 0.664   -15.469 1.00 53.80  ?  256 TYR B O     1 
ATOM   4204 C  CB    . TYR B 1 256 ? -11.137 0.459   -18.577 1.00 50.70  ?  256 TYR B CB    1 
ATOM   4205 C  CG    . TYR B 1 256 ? -10.146 1.209   -19.468 1.00 47.29  ?  256 TYR B CG    1 
ATOM   4206 C  CD1   . TYR B 1 256 ? -9.833  2.534   -19.238 1.00 44.92  ?  256 TYR B CD1   1 
ATOM   4207 C  CD2   . TYR B 1 256 ? -9.570  0.588   -20.577 1.00 49.51  ?  256 TYR B CD2   1 
ATOM   4208 C  CE1   . TYR B 1 256 ? -8.958  3.214   -20.057 1.00 50.71  ?  256 TYR B CE1   1 
ATOM   4209 C  CE2   . TYR B 1 256 ? -8.669  1.256   -21.403 1.00 43.24  ?  256 TYR B CE2   1 
ATOM   4210 C  CZ    . TYR B 1 256 ? -8.366  2.565   -21.141 1.00 47.63  ?  256 TYR B CZ    1 
ATOM   4211 O  OH    . TYR B 1 256 ? -7.486  3.234   -21.963 1.00 44.20  ?  256 TYR B OH    1 
ATOM   4212 N  N     . GLN B 1 257 ? -12.492 -1.363  -16.435 1.00 53.16  ?  257 GLN B N     1 
ATOM   4213 C  CA    . GLN B 1 257 ? -13.709 -1.711  -15.712 1.00 56.44  ?  257 GLN B CA    1 
ATOM   4214 C  C     . GLN B 1 257 ? -13.445 -1.827  -14.216 1.00 56.79  ?  257 GLN B C     1 
ATOM   4215 O  O     . GLN B 1 257 ? -14.329 -1.529  -13.397 1.00 55.26  ?  257 GLN B O     1 
ATOM   4216 C  CB    . GLN B 1 257 ? -14.300 -3.002  -16.293 1.00 59.16  ?  257 GLN B CB    1 
ATOM   4217 C  CG    . GLN B 1 257 ? -15.837 -3.021  -16.305 1.00 66.08  ?  257 GLN B CG    1 
ATOM   4218 C  CD    . GLN B 1 257 ? -16.476 -2.333  -17.527 1.00 67.70  ?  257 GLN B CD    1 
ATOM   4219 O  OE1   . GLN B 1 257 ? -15.929 -2.330  -18.633 1.00 69.87  ?  257 GLN B OE1   1 
ATOM   4220 N  NE2   . GLN B 1 257 ? -17.634 -1.717  -17.305 1.00 66.43  ?  257 GLN B NE2   1 
ATOM   4221 N  N     . MET B 1 258 ? -12.224 -2.210  -13.849 1.00 49.46  ?  258 MET B N     1 
ATOM   4222 C  CA    . MET B 1 258 ? -11.803 -2.122  -12.458 1.00 50.76  ?  258 MET B CA    1 
ATOM   4223 C  C     . MET B 1 258 ? -11.766 -0.673  -12.012 1.00 57.73  ?  258 MET B C     1 
ATOM   4224 O  O     . MET B 1 258 ? -12.184 -0.342  -10.896 1.00 63.66  ?  258 MET B O     1 
ATOM   4225 C  CB    . MET B 1 258 ? -10.425 -2.762  -12.302 1.00 55.23  ?  258 MET B CB    1 
ATOM   4226 C  CG    . MET B 1 258 ? -10.463 -4.285  -12.275 1.00 53.99  ?  258 MET B CG    1 
ATOM   4227 S  SD    . MET B 1 258 ? -8.910  -5.027  -11.773 1.00 54.69  ?  258 MET B SD    1 
ATOM   4228 C  CE    . MET B 1 258 ? -7.851  -3.591  -11.643 1.00 62.66  ?  258 MET B CE    1 
ATOM   4229 N  N     . ALA B 1 259 ? -11.301 0.209   -12.897 1.00 56.29  ?  259 ALA B N     1 
ATOM   4230 C  CA    . ALA B 1 259 ? -11.161 1.618   -12.571 1.00 58.99  ?  259 ALA B CA    1 
ATOM   4231 C  C     . ALA B 1 259 ? -12.520 2.298   -12.400 1.00 61.56  ?  259 ALA B C     1 
ATOM   4232 O  O     . ALA B 1 259 ? -12.707 3.083   -11.465 1.00 60.36  ?  259 ALA B O     1 
ATOM   4233 C  CB    . ALA B 1 259 ? -10.328 2.296   -13.657 1.00 55.15  ?  259 ALA B CB    1 
ATOM   4234 N  N     . TYR B 1 260 ? -13.481 2.020   -13.288 1.00 61.36  ?  260 TYR B N     1 
ATOM   4235 C  CA    . TYR B 1 260 ? -14.800 2.632   -13.140 1.00 63.21  ?  260 TYR B CA    1 
ATOM   4236 C  C     . TYR B 1 260 ? -15.473 2.181   -11.856 1.00 64.50  ?  260 TYR B C     1 
ATOM   4237 O  O     . TYR B 1 260 ? -16.069 2.999   -11.149 1.00 64.54  ?  260 TYR B O     1 
ATOM   4238 C  CB    . TYR B 1 260 ? -15.704 2.310   -14.332 1.00 63.96  ?  260 TYR B CB    1 
ATOM   4239 C  CG    . TYR B 1 260 ? -15.087 2.565   -15.682 1.00 62.72  ?  260 TYR B CG    1 
ATOM   4240 C  CD1   . TYR B 1 260 ? -14.415 3.744   -15.944 1.00 60.69  ?  260 TYR B CD1   1 
ATOM   4241 C  CD2   . TYR B 1 260 ? -15.207 1.635   -16.700 1.00 59.59  ?  260 TYR B CD2   1 
ATOM   4242 C  CE1   . TYR B 1 260 ? -13.856 3.974   -17.176 1.00 61.13  ?  260 TYR B CE1   1 
ATOM   4243 C  CE2   . TYR B 1 260 ? -14.662 1.850   -17.926 1.00 55.31  ?  260 TYR B CE2   1 
ATOM   4244 C  CZ    . TYR B 1 260 ? -13.982 3.017   -18.168 1.00 59.56  ?  260 TYR B CZ    1 
ATOM   4245 O  OH    . TYR B 1 260 ? -13.425 3.241   -19.411 1.00 58.11  ?  260 TYR B OH    1 
ATOM   4246 N  N     . ALA B 1 261 ? -15.408 0.877   -11.557 1.00 66.09  ?  261 ALA B N     1 
ATOM   4247 C  CA    . ALA B 1 261 ? -15.917 0.316   -10.313 1.00 56.61  ?  261 ALA B CA    1 
ATOM   4248 C  C     . ALA B 1 261 ? -15.393 1.108   -9.120  1.00 65.43  ?  261 ALA B C     1 
ATOM   4249 O  O     . ALA B 1 261 ? -16.165 1.772   -8.417  1.00 70.45  ?  261 ALA B O     1 
ATOM   4250 C  CB    . ALA B 1 261 ? -15.529 -1.154  -10.198 1.00 50.67  ?  261 ALA B CB    1 
ATOM   4251 N  N     . SER B 1 262 ? -14.080 1.074   -8.908  1.00 67.79  ?  262 SER B N     1 
ATOM   4252 C  CA    . SER B 1 262 ? -13.411 1.949   -7.950  1.00 68.98  ?  262 SER B CA    1 
ATOM   4253 C  C     . SER B 1 262 ? -14.015 3.351   -7.908  1.00 72.61  ?  262 SER B C     1 
ATOM   4254 O  O     . SER B 1 262 ? -14.154 3.934   -6.830  1.00 77.69  ?  262 SER B O     1 
ATOM   4255 C  CB    . SER B 1 262 ? -11.922 2.044   -8.287  1.00 67.56  ?  262 SER B CB    1 
ATOM   4256 O  OG    . SER B 1 262 ? -11.130 2.235   -7.131  1.00 70.61  ?  262 SER B OG    1 
ATOM   4257 N  N     . PHE B 1 263 ? -14.408 3.886   -9.070  1.00 72.78  ?  263 PHE B N     1 
ATOM   4258 C  CA    . PHE B 1 263 ? -14.911 5.255   -9.145  1.00 70.35  ?  263 PHE B CA    1 
ATOM   4259 C  C     . PHE B 1 263 ? -16.338 5.369   -8.626  1.00 74.50  ?  263 PHE B C     1 
ATOM   4260 O  O     . PHE B 1 263 ? -16.650 6.279   -7.847  1.00 75.81  ?  263 PHE B O     1 
ATOM   4261 C  CB    . PHE B 1 263 ? -14.836 5.765   -10.580 1.00 68.38  ?  263 PHE B CB    1 
ATOM   4262 C  CG    . PHE B 1 263 ? -13.517 6.370   -10.928 1.00 71.64  ?  263 PHE B CG    1 
ATOM   4263 C  CD1   . PHE B 1 263 ? -12.651 6.789   -9.930  1.00 74.65  ?  263 PHE B CD1   1 
ATOM   4264 C  CD2   . PHE B 1 263 ? -13.132 6.517   -12.247 1.00 69.79  ?  263 PHE B CD2   1 
ATOM   4265 C  CE1   . PHE B 1 263 ? -11.426 7.355   -10.244 1.00 71.56  ?  263 PHE B CE1   1 
ATOM   4266 C  CE2   . PHE B 1 263 ? -11.903 7.080   -12.567 1.00 66.79  ?  263 PHE B CE2   1 
ATOM   4267 C  CZ    . PHE B 1 263 ? -11.055 7.501   -11.567 1.00 65.35  ?  263 PHE B CZ    1 
ATOM   4268 N  N     . GLU B 1 264 ? -17.231 4.480   -9.069  1.00 70.96  ?  264 GLU B N     1 
ATOM   4269 C  CA    . GLU B 1 264 ? -18.612 4.582   -8.623  1.00 69.83  ?  264 GLU B CA    1 
ATOM   4270 C  C     . GLU B 1 264 ? -18.700 4.445   -7.105  1.00 75.63  ?  264 GLU B C     1 
ATOM   4271 O  O     . GLU B 1 264 ? -19.518 5.118   -6.464  1.00 77.51  ?  264 GLU B O     1 
ATOM   4272 C  CB    . GLU B 1 264 ? -19.476 3.535   -9.336  1.00 73.46  ?  264 GLU B CB    1 
ATOM   4273 C  CG    . GLU B 1 264 ? -19.989 3.961   -10.741 1.00 80.92  ?  264 GLU B CG    1 
ATOM   4274 C  CD    . GLU B 1 264 ? -21.129 5.017   -10.739 1.00 81.11  ?  264 GLU B CD    1 
ATOM   4275 O  OE1   . GLU B 1 264 ? -20.846 6.239   -10.650 1.00 71.05  ?  264 GLU B OE1   1 
ATOM   4276 O  OE2   . GLU B 1 264 ? -22.313 4.619   -10.860 1.00 82.83  ?  264 GLU B OE2   1 
ATOM   4277 N  N     . ALA B 1 265 ? -17.827 3.624   -6.511  1.00 77.04  ?  265 ALA B N     1 
ATOM   4278 C  CA    . ALA B 1 265 ? -17.700 3.463   -5.065  1.00 73.89  ?  265 ALA B CA    1 
ATOM   4279 C  C     . ALA B 1 265 ? -16.968 4.619   -4.387  1.00 72.90  ?  265 ALA B C     1 
ATOM   4280 O  O     . ALA B 1 265 ? -16.831 4.603   -3.163  1.00 71.63  ?  265 ALA B O     1 
ATOM   4281 C  CB    . ALA B 1 265 ? -16.979 2.148   -4.749  1.00 68.79  ?  265 ALA B CB    1 
ATOM   4282 N  N     . GLY B 1 266 ? -16.485 5.608   -5.130  1.00 76.17  ?  266 GLY B N     1 
ATOM   4283 C  CA    . GLY B 1 266 ? -15.765 6.712   -4.535  1.00 76.20  ?  266 GLY B CA    1 
ATOM   4284 C  C     . GLY B 1 266 ? -14.334 6.426   -4.116  1.00 83.95  ?  266 GLY B C     1 
ATOM   4285 O  O     . GLY B 1 266 ? -13.659 7.349   -3.633  1.00 86.23  ?  266 GLY B O     1 
ATOM   4286 N  N     . VAL B 1 267 ? -13.836 5.199   -4.287  1.00 80.29  ?  267 VAL B N     1 
ATOM   4287 C  CA    . VAL B 1 267 ? -12.475 4.855   -3.854  1.00 81.27  ?  267 VAL B CA    1 
ATOM   4288 C  C     . VAL B 1 267 ? -11.428 5.394   -4.826  1.00 83.51  ?  267 VAL B C     1 
ATOM   4289 O  O     . VAL B 1 267 ? -11.365 4.951   -5.987  1.00 80.07  ?  267 VAL B O     1 
ATOM   4290 C  CB    . VAL B 1 267 ? -12.298 3.339   -3.684  1.00 76.91  ?  267 VAL B CB    1 
ATOM   4291 C  CG1   . VAL B 1 267 ? -11.034 3.053   -2.881  1.00 75.18  ?  267 VAL B CG1   1 
ATOM   4292 C  CG2   . VAL B 1 267 ? -13.528 2.730   -3.025  1.00 70.01  ?  267 VAL B CG2   1 
ATOM   4293 N  N     . PRO B 1 268 ? -10.574 6.326   -4.394  1.00 84.39  ?  268 PRO B N     1 
ATOM   4294 C  CA    . PRO B 1 268 ? -9.583  6.902   -5.315  1.00 81.60  ?  268 PRO B CA    1 
ATOM   4295 C  C     . PRO B 1 268 ? -8.498  5.891   -5.655  1.00 79.58  ?  268 PRO B C     1 
ATOM   4296 O  O     . PRO B 1 268 ? -7.899  5.275   -4.767  1.00 72.78  ?  268 PRO B O     1 
ATOM   4297 C  CB    . PRO B 1 268 ? -9.018  8.104   -4.540  1.00 85.55  ?  268 PRO B CB    1 
ATOM   4298 C  CG    . PRO B 1 268 ? -9.915  8.275   -3.313  1.00 85.14  ?  268 PRO B CG    1 
ATOM   4299 C  CD    . PRO B 1 268 ? -10.502 6.924   -3.048  1.00 85.45  ?  268 PRO B CD    1 
ATOM   4300 N  N     . LEU B 1 269 ? -8.272  5.715   -6.960  1.00 78.33  ?  269 LEU B N     1 
ATOM   4301 C  CA    . LEU B 1 269 ? -7.182  4.891   -7.468  1.00 68.64  ?  269 LEU B CA    1 
ATOM   4302 C  C     . LEU B 1 269 ? -5.847  5.505   -7.090  1.00 64.44  ?  269 LEU B C     1 
ATOM   4303 O  O     . LEU B 1 269 ? -5.742  6.716   -6.886  1.00 68.03  ?  269 LEU B O     1 
ATOM   4304 C  CB    . LEU B 1 269 ? -7.277  4.791   -8.989  1.00 69.16  ?  269 LEU B CB    1 
ATOM   4305 C  CG    . LEU B 1 269 ? -8.600  4.221   -9.497  1.00 71.99  ?  269 LEU B CG    1 
ATOM   4306 C  CD1   . LEU B 1 269 ? -8.858  4.625   -10.947 1.00 63.87  ?  269 LEU B CD1   1 
ATOM   4307 C  CD2   . LEU B 1 269 ? -8.582  2.709   -9.330  1.00 65.31  ?  269 LEU B CD2   1 
ATOM   4308 N  N     . ASP B 1 270 ? -4.814  4.669   -6.994  1.00 66.99  ?  270 ASP B N     1 
ATOM   4309 C  CA    . ASP B 1 270 ? -3.481  5.243   -6.905  1.00 67.97  ?  270 ASP B CA    1 
ATOM   4310 C  C     . ASP B 1 270 ? -3.272  6.166   -8.094  1.00 64.55  ?  270 ASP B C     1 
ATOM   4311 O  O     . ASP B 1 270 ? -3.749  5.897   -9.203  1.00 59.53  ?  270 ASP B O     1 
ATOM   4312 C  CB    . ASP B 1 270 ? -2.384  4.189   -6.894  1.00 67.49  ?  270 ASP B CB    1 
ATOM   4313 C  CG    . ASP B 1 270 ? -1.020  4.798   -7.203  1.00 73.81  ?  270 ASP B CG    1 
ATOM   4314 O  OD1   . ASP B 1 270 ? -0.761  5.961   -6.799  1.00 76.15  ?  270 ASP B OD1   1 
ATOM   4315 O  OD2   . ASP B 1 270 ? -0.221  4.150   -7.893  1.00 68.04  ?  270 ASP B OD2   1 
ATOM   4316 N  N     . HIS B 1 271 ? -2.554  7.262   -7.849  1.00 62.84  ?  271 HIS B N     1 
ATOM   4317 C  CA    . HIS B 1 271 ? -2.479  8.335   -8.824  1.00 67.36  ?  271 HIS B CA    1 
ATOM   4318 C  C     . HIS B 1 271 ? -1.663  7.940   -10.050 1.00 69.23  ?  271 HIS B C     1 
ATOM   4319 O  O     . HIS B 1 271 ? -1.816  8.554   -11.113 1.00 72.60  ?  271 HIS B O     1 
ATOM   4320 C  CB    . HIS B 1 271 ? -1.911  9.591   -8.155  1.00 68.99  ?  271 HIS B CB    1 
ATOM   4321 N  N     . HIS B 1 272 ? -0.824  6.921   -9.948  1.00 67.17  ?  272 HIS B N     1 
ATOM   4322 C  CA    . HIS B 1 272 ? -0.094  6.434   -11.108 1.00 66.58  ?  272 HIS B CA    1 
ATOM   4323 C  C     . HIS B 1 272 ? -0.542  5.025   -11.464 1.00 61.91  ?  272 HIS B C     1 
ATOM   4324 O  O     . HIS B 1 272 ? 0.266   4.157   -11.803 1.00 63.43  ?  272 HIS B O     1 
ATOM   4325 C  CB    . HIS B 1 272 ? 1.409   6.521   -10.865 1.00 64.87  ?  272 HIS B CB    1 
ATOM   4326 C  CG    . HIS B 1 272 ? 1.898   7.932   -10.739 1.00 72.19  ?  272 HIS B CG    1 
ATOM   4327 N  ND1   . HIS B 1 272 ? 2.662   8.369   -9.676  1.00 75.77  ?  272 HIS B ND1   1 
ATOM   4328 C  CD2   . HIS B 1 272 ? 1.705   9.016   -11.533 1.00 76.67  ?  272 HIS B CD2   1 
ATOM   4329 C  CE1   . HIS B 1 272 ? 2.931   9.657   -9.829  1.00 74.75  ?  272 HIS B CE1   1 
ATOM   4330 N  NE2   . HIS B 1 272 ? 2.360   10.074  -10.946 1.00 77.83  ?  272 HIS B NE2   1 
ATOM   4331 N  N     . TYR B 1 273 ? -1.854  4.795   -11.405 1.00 56.26  ?  273 TYR B N     1 
ATOM   4332 C  CA    . TYR B 1 273 ? -2.373  3.464   -11.691 1.00 59.67  ?  273 TYR B CA    1 
ATOM   4333 C  C     . TYR B 1 273 ? -2.105  3.060   -13.136 1.00 56.11  ?  273 TYR B C     1 
ATOM   4334 O  O     . TYR B 1 273 ? -1.952  1.866   -13.428 1.00 52.05  ?  273 TYR B O     1 
ATOM   4335 C  CB    . TYR B 1 273 ? -3.876  3.403   -11.391 1.00 57.58  ?  273 TYR B CB    1 
ATOM   4336 C  CG    . TYR B 1 273 ? -4.704  4.118   -12.424 1.00 55.10  ?  273 TYR B CG    1 
ATOM   4337 C  CD1   . TYR B 1 273 ? -4.848  5.498   -12.378 1.00 59.78  ?  273 TYR B CD1   1 
ATOM   4338 C  CD2   . TYR B 1 273 ? -5.299  3.422   -13.476 1.00 50.48  ?  273 TYR B CD2   1 
ATOM   4339 C  CE1   . TYR B 1 273 ? -5.580  6.167   -13.329 1.00 59.19  ?  273 TYR B CE1   1 
ATOM   4340 C  CE2   . TYR B 1 273 ? -6.024  4.084   -14.442 1.00 55.78  ?  273 TYR B CE2   1 
ATOM   4341 C  CZ    . TYR B 1 273 ? -6.167  5.464   -14.357 1.00 60.35  ?  273 TYR B CZ    1 
ATOM   4342 O  OH    . TYR B 1 273 ? -6.895  6.150   -15.307 1.00 62.18  ?  273 TYR B OH    1 
ATOM   4343 N  N     . TYR B 1 274 ? -2.070  4.026   -14.055 1.00 50.90  ?  274 TYR B N     1 
ATOM   4344 C  CA    . TYR B 1 274 ? -1.817  3.668   -15.442 1.00 53.57  ?  274 TYR B CA    1 
ATOM   4345 C  C     . TYR B 1 274 ? -0.389  3.164   -15.602 1.00 49.17  ?  274 TYR B C     1 
ATOM   4346 O  O     . TYR B 1 274 ? -0.150  2.081   -16.144 1.00 46.92  ?  274 TYR B O     1 
ATOM   4347 C  CB    . TYR B 1 274 ? -2.085  4.862   -16.366 1.00 50.19  ?  274 TYR B CB    1 
ATOM   4348 C  CG    . TYR B 1 274 ? -1.809  4.560   -17.837 1.00 49.64  ?  274 TYR B CG    1 
ATOM   4349 C  CD1   . TYR B 1 274 ? -2.714  3.822   -18.597 1.00 48.50  ?  274 TYR B CD1   1 
ATOM   4350 C  CD2   . TYR B 1 274 ? -0.639  4.993   -18.449 1.00 48.67  ?  274 TYR B CD2   1 
ATOM   4351 C  CE1   . TYR B 1 274 ? -2.477  3.537   -19.915 1.00 47.05  ?  274 TYR B CE1   1 
ATOM   4352 C  CE2   . TYR B 1 274 ? -0.386  4.717   -19.776 1.00 50.00  ?  274 TYR B CE2   1 
ATOM   4353 C  CZ    . TYR B 1 274 ? -1.309  3.984   -20.516 1.00 49.56  ?  274 TYR B CZ    1 
ATOM   4354 O  OH    . TYR B 1 274 ? -1.054  3.710   -21.852 1.00 37.24  ?  274 TYR B OH    1 
ATOM   4355 N  N     . GLU B 1 275 ? 0.569   3.932   -15.116 1.00 48.71  ?  275 GLU B N     1 
ATOM   4356 C  CA    . GLU B 1 275 ? 1.961   3.548   -15.244 1.00 47.55  ?  275 GLU B CA    1 
ATOM   4357 C  C     . GLU B 1 275 ? 2.268   2.287   -14.437 1.00 48.93  ?  275 GLU B C     1 
ATOM   4358 O  O     . GLU B 1 275 ? 3.216   1.555   -14.765 1.00 49.58  ?  275 GLU B O     1 
ATOM   4359 C  CB    . GLU B 1 275 ? 2.824   4.753   -14.842 1.00 54.64  ?  275 GLU B CB    1 
ATOM   4360 C  CG    . GLU B 1 275 ? 2.620   6.038   -15.754 1.00 51.78  ?  275 GLU B CG    1 
ATOM   4361 C  CD    . GLU B 1 275 ? 1.490   7.016   -15.282 1.00 66.22  ?  275 GLU B CD    1 
ATOM   4362 O  OE1   . GLU B 1 275 ? 0.722   6.698   -14.327 1.00 59.85  ?  275 GLU B OE1   1 
ATOM   4363 O  OE2   . GLU B 1 275 ? 1.377   8.123   -15.876 1.00 65.39  ?  275 GLU B OE2   1 
ATOM   4364 N  N     . ARG B 1 276 ? 1.457   1.981   -13.425 1.00 50.17  ?  276 ARG B N     1 
ATOM   4365 C  CA    . ARG B 1 276 ? 1.592   0.684   -12.779 1.00 52.13  ?  276 ARG B CA    1 
ATOM   4366 C  C     . ARG B 1 276 ? 1.046   -0.441  -13.651 1.00 48.19  ?  276 ARG B C     1 
ATOM   4367 O  O     . ARG B 1 276 ? 1.595   -1.551  -13.655 1.00 42.83  ?  276 ARG B O     1 
ATOM   4368 C  CB    . ARG B 1 276 ? 0.897   0.705   -11.423 1.00 54.42  ?  276 ARG B CB    1 
ATOM   4369 C  CG    . ARG B 1 276 ? 1.566   1.624   -10.419 1.00 56.04  ?  276 ARG B CG    1 
ATOM   4370 C  CD    . ARG B 1 276 ? 0.688   1.752   -9.191  1.00 64.95  ?  276 ARG B CD    1 
ATOM   4371 N  NE    . ARG B 1 276 ? 1.120   0.905   -8.081  1.00 67.58  ?  276 ARG B NE    1 
ATOM   4372 C  CZ    . ARG B 1 276 ? 0.807   1.102   -6.807  1.00 75.35  ?  276 ARG B CZ    1 
ATOM   4373 N  NH1   . ARG B 1 276 ? 0.006   2.090   -6.431  1.00 79.10  ?  276 ARG B NH1   1 
ATOM   4374 N  NH2   . ARG B 1 276 ? 1.298   0.276   -5.885  1.00 83.37  ?  276 ARG B NH2   1 
ATOM   4375 N  N     . THR B 1 277 ? -0.016  -0.166  -14.404 1.00 44.85  ?  277 THR B N     1 
ATOM   4376 C  CA    . THR B 1 277 ? -0.536  -1.156  -15.334 1.00 43.62  ?  277 THR B CA    1 
ATOM   4377 C  C     . THR B 1 277 ? 0.492   -1.513  -16.408 1.00 44.79  ?  277 THR B C     1 
ATOM   4378 O  O     . THR B 1 277 ? 0.633   -2.691  -16.767 1.00 47.12  ?  277 THR B O     1 
ATOM   4379 C  CB    . THR B 1 277 ? -1.823  -0.625  -15.947 1.00 42.62  ?  277 THR B CB    1 
ATOM   4380 O  OG1   . THR B 1 277 ? -2.708  -0.289  -14.878 1.00 50.19  ?  277 THR B OG1   1 
ATOM   4381 C  CG2   . THR B 1 277 ? -2.489  -1.671  -16.833 1.00 43.22  ?  277 THR B CG2   1 
ATOM   4382 N  N     . LEU B 1 278 ? 1.255   -0.521  -16.859 1.00 39.72  ?  278 LEU B N     1 
ATOM   4383 C  CA    . LEU B 1 278 ? 2.294   -0.729  -17.896 1.00 40.38  ?  278 LEU B CA    1 
ATOM   4384 C  C     . LEU B 1 278 ? 3.284   -1.801  -17.430 1.00 45.40  ?  278 LEU B C     1 
ATOM   4385 O  O     . LEU B 1 278 ? 3.603   -2.675  -18.212 1.00 43.84  ?  278 LEU B O     1 
ATOM   4386 C  CB    . LEU B 1 278 ? 2.990   0.601   -18.183 1.00 38.32  ?  278 LEU B CB    1 
ATOM   4387 C  CG    . LEU B 1 278 ? 2.184   1.608   -18.992 1.00 38.04  ?  278 LEU B CG    1 
ATOM   4388 C  CD1   . LEU B 1 278 ? 3.016   2.813   -19.310 1.00 39.00  ?  278 LEU B CD1   1 
ATOM   4389 C  CD2   . LEU B 1 278 ? 1.666   1.004   -20.278 1.00 36.38  ?  278 LEU B CD2   1 
ATOM   4390 N  N     . GLN B 1 279 ? 3.728   -1.725  -16.181 1.00 45.77  ?  279 GLN B N     1 
ATOM   4391 C  CA    . GLN B 1 279 ? 4.667   -2.718  -15.613 1.00 46.92  ?  279 GLN B CA    1 
ATOM   4392 C  C     . GLN B 1 279 ? 4.007   -4.099  -15.605 1.00 49.01  ?  279 GLN B C     1 
ATOM   4393 O  O     . GLN B 1 279 ? 4.703   -5.066  -15.849 1.00 48.07  ?  279 GLN B O     1 
ATOM   4394 C  CB    . GLN B 1 279 ? 5.072   -2.318  -14.193 1.00 46.85  ?  279 GLN B CB    1 
ATOM   4395 C  CG    . GLN B 1 279 ? 6.337   -1.488  -14.101 1.00 47.92  ?  279 GLN B CG    1 
ATOM   4396 C  CD    . GLN B 1 279 ? 7.562   -2.260  -14.524 1.00 65.26  ?  279 GLN B CD    1 
ATOM   4397 O  OE1   . GLN B 1 279 ? 7.539   -3.476  -14.674 1.00 63.48  ?  279 GLN B OE1   1 
ATOM   4398 N  NE2   . GLN B 1 279 ? 8.660   -1.552  -14.718 1.00 64.68  ?  279 GLN B NE2   1 
ATOM   4399 N  N     . VAL B 1 280 ? 2.709   -4.166  -15.331 1.00 40.63  ?  280 VAL B N     1 
ATOM   4400 C  CA    . VAL B 1 280 ? 1.989   -5.469  -15.261 1.00 45.95  ?  280 VAL B CA    1 
ATOM   4401 C  C     . VAL B 1 280 ? 1.913   -6.077  -16.657 1.00 44.23  ?  280 VAL B C     1 
ATOM   4402 O  O     . VAL B 1 280 ? 2.231   -7.249  -16.803 1.00 41.80  ?  280 VAL B O     1 
ATOM   4403 C  CB    . VAL B 1 280 ? 0.575   -5.295  -14.678 1.00 48.05  ?  280 VAL B CB    1 
ATOM   4404 C  CG1   . VAL B 1 280 ? -0.257  -6.555  -14.813 1.00 51.11  ?  280 VAL B CG1   1 
ATOM   4405 C  CG2   . VAL B 1 280 ? 0.592   -4.805  -13.249 1.00 44.92  ?  280 VAL B CG2   1 
ATOM   4406 N  N     . LEU B 1 281 ? 1.494   -5.268  -17.624 1.00 44.26  ?  281 LEU B N     1 
ATOM   4407 C  CA    . LEU B 1 281 ? 1.314   -5.688  -19.032 1.00 46.26  ?  281 LEU B CA    1 
ATOM   4408 C  C     . LEU B 1 281 ? 2.655   -6.094  -19.635 1.00 44.29  ?  281 LEU B C     1 
ATOM   4409 O  O     . LEU B 1 281 ? 2.672   -6.991  -20.445 1.00 46.00  ?  281 LEU B O     1 
ATOM   4410 C  CB    . LEU B 1 281 ? 0.683   -4.522  -19.784 1.00 45.53  ?  281 LEU B CB    1 
ATOM   4411 C  CG    . LEU B 1 281 ? -0.713  -4.164  -19.295 1.00 43.96  ?  281 LEU B CG    1 
ATOM   4412 C  CD1   . LEU B 1 281 ? -1.281  -3.010  -20.080 1.00 41.51  ?  281 LEU B CD1   1 
ATOM   4413 C  CD2   . LEU B 1 281 ? -1.625  -5.364  -19.378 1.00 37.45  ?  281 LEU B CD2   1 
ATOM   4414 N  N     . TYR B 1 282 ? 3.730   -5.439  -19.231 1.00 39.88  ?  282 TYR B N     1 
ATOM   4415 C  CA    . TYR B 1 282 ? 5.038   -5.819  -19.742 1.00 41.68  ?  282 TYR B CA    1 
ATOM   4416 C  C     . TYR B 1 282 ? 5.375   -7.254  -19.353 1.00 42.65  ?  282 TYR B C     1 
ATOM   4417 O  O     . TYR B 1 282 ? 5.799   -8.048  -20.200 1.00 40.52  ?  282 TYR B O     1 
ATOM   4418 C  CB    . TYR B 1 282 ? 6.087   -4.837  -19.222 1.00 34.48  ?  282 TYR B CB    1 
ATOM   4419 C  CG    . TYR B 1 282 ? 7.431   -4.948  -19.850 1.00 39.21  ?  282 TYR B CG    1 
ATOM   4420 C  CD1   . TYR B 1 282 ? 7.666   -4.450  -21.141 1.00 43.14  ?  282 TYR B CD1   1 
ATOM   4421 C  CD2   . TYR B 1 282 ? 8.493   -5.528  -19.168 1.00 41.49  ?  282 TYR B CD2   1 
ATOM   4422 C  CE1   . TYR B 1 282 ? 8.916   -4.517  -21.736 1.00 39.85  ?  282 TYR B CE1   1 
ATOM   4423 C  CE2   . TYR B 1 282 ? 9.775   -5.611  -19.767 1.00 47.44  ?  282 TYR B CE2   1 
ATOM   4424 C  CZ    . TYR B 1 282 ? 9.971   -5.104  -21.045 1.00 44.85  ?  282 TYR B CZ    1 
ATOM   4425 O  OH    . TYR B 1 282 ? 11.215  -5.173  -21.628 1.00 44.88  ?  282 TYR B OH    1 
ATOM   4426 N  N     . ARG B 1 283 ? 5.178   -7.599  -18.065 1.00 43.20  ?  283 ARG B N     1 
ATOM   4427 C  CA    . ARG B 1 283 ? 5.308   -8.987  -17.608 1.00 48.27  ?  283 ARG B CA    1 
ATOM   4428 C  C     . ARG B 1 283 ? 4.334   -9.907  -18.327 1.00 43.56  ?  283 ARG B C     1 
ATOM   4429 O  O     . ARG B 1 283 ? 4.661   -11.065 -18.609 1.00 49.60  ?  283 ARG B O     1 
ATOM   4430 C  CB    . ARG B 1 283 ? 5.049   -9.136  -16.103 1.00 42.95  ?  283 ARG B CB    1 
ATOM   4431 C  CG    . ARG B 1 283 ? 5.945   -8.439  -15.149 1.00 48.10  ?  283 ARG B CG    1 
ATOM   4432 C  CD    . ARG B 1 283 ? 5.456   -8.685  -13.707 1.00 55.14  ?  283 ARG B CD    1 
ATOM   4433 N  NE    . ARG B 1 283 ? 4.955   -7.480  -13.045 1.00 58.86  ?  283 ARG B NE    1 
ATOM   4434 C  CZ    . ARG B 1 283 ? 5.698   -6.436  -12.690 1.00 60.94  ?  283 ARG B CZ    1 
ATOM   4435 N  NH1   . ARG B 1 283 ? 7.005   -6.392  -12.938 1.00 59.96  ?  283 ARG B NH1   1 
ATOM   4436 N  NH2   . ARG B 1 283 ? 5.118   -5.405  -12.076 1.00 60.30  ?  283 ARG B NH2   1 
ATOM   4437 N  N     . ALA B 1 284 ? 3.111   -9.439  -18.570 1.00 41.99  ?  284 ALA B N     1 
ATOM   4438 C  CA    . ALA B 1 284 ? 2.132   -10.302 -19.222 1.00 46.07  ?  284 ALA B CA    1 
ATOM   4439 C  C     . ALA B 1 284 ? 2.647   -10.777 -20.566 1.00 48.74  ?  284 ALA B C     1 
ATOM   4440 O  O     . ALA B 1 284 ? 2.270   -11.862 -21.027 1.00 55.93  ?  284 ALA B O     1 
ATOM   4441 C  CB    . ALA B 1 284 ? 0.798   -9.574  -19.387 1.00 45.87  ?  284 ALA B CB    1 
ATOM   4442 N  N     . LEU B 1 285 ? 3.521   -9.980  -21.191 1.00 49.73  ?  285 LEU B N     1 
ATOM   4443 C  CA    . LEU B 1 285 ? 4.182   -10.269 -22.458 1.00 50.22  ?  285 LEU B CA    1 
ATOM   4444 C  C     . LEU B 1 285 ? 5.515   -10.982 -22.282 1.00 48.89  ?  285 LEU B C     1 
ATOM   4445 O  O     . LEU B 1 285 ? 6.168   -11.284 -23.277 1.00 49.00  ?  285 LEU B O     1 
ATOM   4446 C  CB    . LEU B 1 285 ? 4.408   -8.963  -23.232 1.00 48.52  ?  285 LEU B CB    1 
ATOM   4447 C  CG    . LEU B 1 285 ? 3.143   -8.171  -23.568 1.00 45.10  ?  285 LEU B CG    1 
ATOM   4448 C  CD1   . LEU B 1 285 ? 3.391   -6.655  -23.467 1.00 36.11  ?  285 LEU B CD1   1 
ATOM   4449 C  CD2   . LEU B 1 285 ? 2.678   -8.567  -24.946 1.00 34.84  ?  285 LEU B CD2   1 
ATOM   4450 N  N     . GLY B 1 286 ? 5.933   -11.241 -21.043 1.00 51.93  ?  286 GLY B N     1 
ATOM   4451 C  CA    . GLY B 1 286 ? 7.222   -11.835 -20.791 1.00 54.71  ?  286 GLY B CA    1 
ATOM   4452 C  C     . GLY B 1 286 ? 7.204   -13.352 -20.880 1.00 66.26  ?  286 GLY B C     1 
ATOM   4453 O  O     . GLY B 1 286 ? 6.141   -13.982 -20.880 1.00 62.45  ?  286 GLY B O     1 
ATOM   4454 N  N     . ASP B 1 287 ? 8.428   -13.920 -20.929 1.00 70.64  ?  287 ASP B N     1 
ATOM   4455 C  CA    . ASP B 1 287 ? 8.631   -15.298 -21.354 1.00 73.75  ?  287 ASP B CA    1 
ATOM   4456 C  C     . ASP B 1 287 ? 7.846   -16.289 -20.494 1.00 79.40  ?  287 ASP B C     1 
ATOM   4457 O  O     . ASP B 1 287 ? 7.003   -17.014 -21.038 1.00 82.08  ?  287 ASP B O     1 
ATOM   4458 C  CB    . ASP B 1 287 ? 10.132  -15.619 -21.388 1.00 83.78  ?  287 ASP B CB    1 
ATOM   4459 C  CG    . ASP B 1 287 ? 10.707  -15.638 -22.806 1.00 88.72  ?  287 ASP B CG    1 
ATOM   4460 O  OD1   . ASP B 1 287 ? 9.944   -15.925 -23.763 1.00 90.43  ?  287 ASP B OD1   1 
ATOM   4461 O  OD2   . ASP B 1 287 ? 11.917  -15.344 -22.970 1.00 82.63  ?  287 ASP B OD2   1 
ATOM   4462 N  N     . PRO B 1 288 ? 8.052   -16.349 -19.154 1.00 78.67  ?  288 PRO B N     1 
ATOM   4463 C  CA    . PRO B 1 288 ? 7.127   -17.231 -18.406 1.00 70.33  ?  288 PRO B CA    1 
ATOM   4464 C  C     . PRO B 1 288 ? 5.774   -16.541 -18.263 1.00 70.51  ?  288 PRO B C     1 
ATOM   4465 O  O     . PRO B 1 288 ? 5.470   -15.891 -17.274 1.00 76.31  ?  288 PRO B O     1 
ATOM   4466 C  CB    . PRO B 1 288 ? 7.848   -17.423 -17.068 1.00 70.49  ?  288 PRO B CB    1 
ATOM   4467 C  CG    . PRO B 1 288 ? 8.588   -16.126 -16.855 1.00 74.21  ?  288 PRO B CG    1 
ATOM   4468 C  CD    . PRO B 1 288 ? 8.968   -15.619 -18.251 1.00 72.12  ?  288 PRO B CD    1 
ATOM   4469 N  N     . GLN B 1 289 ? 4.967   -16.647 -19.321 1.00 66.52  ?  289 GLN B N     1 
ATOM   4470 C  CA    . GLN B 1 289 ? 3.544   -16.300 -19.372 1.00 67.23  ?  289 GLN B CA    1 
ATOM   4471 C  C     . GLN B 1 289 ? 2.769   -16.332 -18.053 1.00 64.16  ?  289 GLN B C     1 
ATOM   4472 O  O     . GLN B 1 289 ? 2.449   -17.423 -17.583 1.00 62.90  ?  289 GLN B O     1 
ATOM   4473 C  CB    . GLN B 1 289 ? 2.855   -17.273 -20.328 1.00 71.38  ?  289 GLN B CB    1 
ATOM   4474 C  CG    . GLN B 1 289 ? 2.744   -16.845 -21.745 1.00 69.06  ?  289 GLN B CG    1 
ATOM   4475 C  CD    . GLN B 1 289 ? 1.291   -16.702 -22.131 1.00 69.97  ?  289 GLN B CD    1 
ATOM   4476 O  OE1   . GLN B 1 289 ? 0.545   -17.687 -22.119 1.00 72.07  ?  289 GLN B OE1   1 
ATOM   4477 N  NE2   . GLN B 1 289 ? 0.864   -15.477 -22.441 1.00 73.38  ?  289 GLN B NE2   1 
ATOM   4478 N  N     . PRO B 1 290 ? 2.415   -15.194 -17.445 1.00 68.73  ?  290 PRO B N     1 
ATOM   4479 C  CA    . PRO B 1 290 ? 1.486   -15.245 -16.305 1.00 63.05  ?  290 PRO B CA    1 
ATOM   4480 C  C     . PRO B 1 290 ? 0.067   -15.582 -16.741 1.00 64.54  ?  290 PRO B C     1 
ATOM   4481 O  O     . PRO B 1 290 ? -0.427  -15.114 -17.771 1.00 65.93  ?  290 PRO B O     1 
ATOM   4482 C  CB    . PRO B 1 290 ? 1.566   -13.832 -15.712 1.00 62.35  ?  290 PRO B CB    1 
ATOM   4483 C  CG    . PRO B 1 290 ? 2.087   -12.992 -16.841 1.00 63.64  ?  290 PRO B CG    1 
ATOM   4484 C  CD    . PRO B 1 290 ? 3.095   -13.885 -17.511 1.00 60.13  ?  290 PRO B CD    1 
ATOM   4485 N  N     . SER B 1 291 ? -0.589  -16.392 -15.916 1.00 65.46  ?  291 SER B N     1 
ATOM   4486 C  CA    . SER B 1 291 ? -1.955  -16.813 -16.154 1.00 61.99  ?  291 SER B CA    1 
ATOM   4487 C  C     . SER B 1 291 ? -2.920  -15.632 -16.116 1.00 63.56  ?  291 SER B C     1 
ATOM   4488 O  O     . SER B 1 291 ? -2.642  -14.606 -15.489 1.00 62.20  ?  291 SER B O     1 
ATOM   4489 C  CB    . SER B 1 291 ? -2.379  -17.814 -15.087 1.00 66.56  ?  291 SER B CB    1 
ATOM   4490 O  OG    . SER B 1 291 ? -2.733  -17.116 -13.895 1.00 59.97  ?  291 SER B OG    1 
ATOM   4491 N  N     . PRO B 1 292 ? -4.080  -15.774 -16.767 1.00 64.64  ?  292 PRO B N     1 
ATOM   4492 C  CA    . PRO B 1 292 ? -5.142  -14.765 -16.619 1.00 65.79  ?  292 PRO B CA    1 
ATOM   4493 C  C     . PRO B 1 292 ? -5.449  -14.367 -15.186 1.00 68.22  ?  292 PRO B C     1 
ATOM   4494 O  O     . PRO B 1 292 ? -5.767  -13.199 -14.937 1.00 65.56  ?  292 PRO B O     1 
ATOM   4495 C  CB    . PRO B 1 292 ? -6.340  -15.453 -17.275 1.00 62.37  ?  292 PRO B CB    1 
ATOM   4496 C  CG    . PRO B 1 292 ? -5.710  -16.216 -18.407 1.00 61.47  ?  292 PRO B CG    1 
ATOM   4497 C  CD    . PRO B 1 292 ? -4.349  -16.675 -17.904 1.00 63.19  ?  292 PRO B CD    1 
ATOM   4498 N  N     . ALA B 1 293 ? -5.353  -15.295 -14.234 1.00 66.37  ?  293 ALA B N     1 
ATOM   4499 C  CA    . ALA B 1 293 ? -5.675  -14.963 -12.850 1.00 67.99  ?  293 ALA B CA    1 
ATOM   4500 C  C     . ALA B 1 293 ? -4.530  -14.229 -12.159 1.00 68.68  ?  293 ALA B C     1 
ATOM   4501 O  O     . ALA B 1 293 ? -4.770  -13.346 -11.324 1.00 69.17  ?  293 ALA B O     1 
ATOM   4502 C  CB    . ALA B 1 293 ? -6.044  -16.230 -12.077 1.00 68.44  ?  293 ALA B CB    1 
ATOM   4503 N  N     . GLN B 1 294 ? -3.282  -14.586 -12.472 1.00 64.97  ?  294 GLN B N     1 
ATOM   4504 C  CA    . GLN B 1 294 ? -2.150  -13.874 -11.886 1.00 67.26  ?  294 GLN B CA    1 
ATOM   4505 C  C     . GLN B 1 294 ? -2.041  -12.451 -12.417 1.00 68.38  ?  294 GLN B C     1 
ATOM   4506 O  O     . GLN B 1 294 ? -1.491  -11.580 -11.729 1.00 68.05  ?  294 GLN B O     1 
ATOM   4507 C  CB    . GLN B 1 294 ? -0.841  -14.637 -12.142 1.00 66.82  ?  294 GLN B CB    1 
ATOM   4508 N  N     . VAL B 1 295 ? -2.565  -12.185 -13.611 1.00 67.71  ?  295 VAL B N     1 
ATOM   4509 C  CA    . VAL B 1 295 ? -2.429  -10.854 -14.182 1.00 64.25  ?  295 VAL B CA    1 
ATOM   4510 C  C     . VAL B 1 295 ? -3.572  -9.950  -13.749 1.00 64.53  ?  295 VAL B C     1 
ATOM   4511 O  O     . VAL B 1 295 ? -3.336  -8.806  -13.350 1.00 64.07  ?  295 VAL B O     1 
ATOM   4512 C  CB    . VAL B 1 295 ? -2.319  -10.937 -15.712 1.00 62.24  ?  295 VAL B CB    1 
ATOM   4513 C  CG1   . VAL B 1 295 ? -2.708  -9.598  -16.342 1.00 61.81  ?  295 VAL B CG1   1 
ATOM   4514 C  CG2   . VAL B 1 295 ? -0.909  -11.337 -16.100 1.00 63.01  ?  295 VAL B CG2   1 
ATOM   4515 N  N     . GLU B 1 296 ? -4.823  -10.435 -13.799 1.00 64.50  ?  296 GLU B N     1 
ATOM   4516 C  CA    . GLU B 1 296 ? -5.933  -9.638  -13.264 1.00 67.90  ?  296 GLU B CA    1 
ATOM   4517 C  C     . GLU B 1 296 ? -5.723  -9.320  -11.782 1.00 64.60  ?  296 GLU B C     1 
ATOM   4518 O  O     . GLU B 1 296 ? -6.101  -8.240  -11.315 1.00 62.00  ?  296 GLU B O     1 
ATOM   4519 C  CB    . GLU B 1 296 ? -7.281  -10.355 -13.495 1.00 67.18  ?  296 GLU B CB    1 
ATOM   4520 C  CG    . GLU B 1 296 ? -7.474  -10.886 -14.938 1.00 68.58  ?  296 GLU B CG    1 
ATOM   4521 C  CD    . GLU B 1 296 ? -8.898  -11.317 -15.270 1.00 72.39  ?  296 GLU B CD    1 
ATOM   4522 O  OE1   . GLU B 1 296 ? -9.840  -10.755 -14.684 1.00 78.51  ?  296 GLU B OE1   1 
ATOM   4523 O  OE2   . GLU B 1 296 ? -9.080  -12.228 -16.115 1.00 76.30  ?  296 GLU B OE2   1 
ATOM   4524 N  N     . ASP B 1 297 ? -5.082  -10.230 -11.043 1.00 67.65  ?  297 ASP B N     1 
ATOM   4525 C  CA    . ASP B 1 297 ? -4.709  -9.955  -9.661  1.00 66.43  ?  297 ASP B CA    1 
ATOM   4526 C  C     . ASP B 1 297 ? -3.613  -8.888  -9.582  1.00 68.80  ?  297 ASP B C     1 
ATOM   4527 O  O     . ASP B 1 297 ? -3.681  -7.983  -8.740  1.00 67.50  ?  297 ASP B O     1 
ATOM   4528 C  CB    . ASP B 1 297 ? -4.264  -11.257 -8.981  1.00 71.68  ?  297 ASP B CB    1 
ATOM   4529 C  CG    . ASP B 1 297 ? -5.421  -11.998 -8.258  1.00 80.73  ?  297 ASP B CG    1 
ATOM   4530 O  OD1   . ASP B 1 297 ? -6.590  -11.993 -8.743  1.00 74.30  ?  297 ASP B OD1   1 
ATOM   4531 O  OD2   . ASP B 1 297 ? -5.141  -12.603 -7.191  1.00 84.20  ?  297 ASP B OD2   1 
ATOM   4532 N  N     . GLU B 1 298 ? -2.596  -8.975  -10.456 1.00 71.16  ?  298 GLU B N     1 
ATOM   4533 C  CA    . GLU B 1 298 ? -1.529  -7.969  -10.504 1.00 65.62  ?  298 GLU B CA    1 
ATOM   4534 C  C     . GLU B 1 298 ? -2.068  -6.574  -10.827 1.00 59.93  ?  298 GLU B C     1 
ATOM   4535 O  O     . GLU B 1 298 ? -1.518  -5.564  -10.355 1.00 51.86  ?  298 GLU B O     1 
ATOM   4536 C  CB    . GLU B 1 298 ? -0.482  -8.372  -11.550 1.00 64.78  ?  298 GLU B CB    1 
ATOM   4537 C  CG    . GLU B 1 298 ? 0.696   -9.188  -11.062 1.00 60.64  ?  298 GLU B CG    1 
ATOM   4538 C  CD    . GLU B 1 298 ? 1.831   -9.161  -12.071 1.00 66.95  ?  298 GLU B CD    1 
ATOM   4539 O  OE1   . GLU B 1 298 ? 1.778   -9.990  -13.012 1.00 73.65  ?  298 GLU B OE1   1 
ATOM   4540 O  OE2   . GLU B 1 298 ? 2.744   -8.295  -11.950 1.00 55.98  ?  298 GLU B OE2   1 
ATOM   4541 N  N     . LEU B 1 299 ? -3.124  -6.508  -11.645 1.00 55.10  ?  299 LEU B N     1 
ATOM   4542 C  CA    . LEU B 1 299 ? -3.758  -5.236  -11.980 1.00 59.91  ?  299 LEU B CA    1 
ATOM   4543 C  C     . LEU B 1 299 ? -4.446  -4.628  -10.768 1.00 59.24  ?  299 LEU B C     1 
ATOM   4544 O  O     . LEU B 1 299 ? -4.306  -3.430  -10.494 1.00 61.23  ?  299 LEU B O     1 
ATOM   4545 C  CB    . LEU B 1 299 ? -4.774  -5.445  -13.100 1.00 60.08  ?  299 LEU B CB    1 
ATOM   4546 C  CG    . LEU B 1 299 ? -4.270  -5.716  -14.513 1.00 59.41  ?  299 LEU B CG    1 
ATOM   4547 C  CD1   . LEU B 1 299 ? -5.454  -5.984  -15.448 1.00 55.08  ?  299 LEU B CD1   1 
ATOM   4548 C  CD2   . LEU B 1 299 ? -3.452  -4.540  -14.997 1.00 55.19  ?  299 LEU B CD2   1 
ATOM   4549 N  N     . ARG B 1 300 ? -5.229  -5.439  -10.053 1.00 62.08  ?  300 ARG B N     1 
ATOM   4550 C  CA    . ARG B 1 300 ? -5.903  -4.967  -8.850  1.00 66.30  ?  300 ARG B CA    1 
ATOM   4551 C  C     . ARG B 1 300 ? -4.924  -4.246  -7.927  1.00 66.17  ?  300 ARG B C     1 
ATOM   4552 O  O     . ARG B 1 300 ? -5.219  -3.149  -7.437  1.00 68.31  ?  300 ARG B O     1 
ATOM   4553 C  CB    . ARG B 1 300 ? -6.588  -6.153  -8.149  1.00 66.94  ?  300 ARG B CB    1 
ATOM   4554 C  CG    . ARG B 1 300 ? -6.816  -5.987  -6.641  1.00 75.72  ?  300 ARG B CG    1 
ATOM   4555 C  CD    . ARG B 1 300 ? -7.527  -7.188  -5.940  1.00 78.60  ?  300 ARG B CD    1 
ATOM   4556 N  NE    . ARG B 1 300 ? -8.519  -7.895  -6.750  1.00 75.90  ?  300 ARG B NE    1 
ATOM   4557 C  CZ    . ARG B 1 300 ? -8.281  -8.994  -7.450  1.00 72.27  ?  300 ARG B CZ    1 
ATOM   4558 N  NH1   . ARG B 1 300 ? -7.098  -9.578  -7.429  1.00 76.68  ?  300 ARG B NH1   1 
ATOM   4559 N  NH2   . ARG B 1 300 ? -9.256  -9.521  -8.184  1.00 75.39  ?  300 ARG B NH2   1 
ATOM   4560 N  N     . ALA B 1 301 ? -3.728  -4.814  -7.725  1.00 60.36  ?  301 ALA B N     1 
ATOM   4561 C  CA    . ALA B 1 301 ? -2.732  -4.151  -6.886  1.00 60.95  ?  301 ALA B CA    1 
ATOM   4562 C  C     . ALA B 1 301 ? -2.168  -2.908  -7.552  1.00 64.49  ?  301 ALA B C     1 
ATOM   4563 O  O     . ALA B 1 301 ? -1.731  -1.978  -6.863  1.00 65.86  ?  301 ALA B O     1 
ATOM   4564 C  CB    . ALA B 1 301 ? -1.597  -5.112  -6.550  1.00 62.15  ?  301 ALA B CB    1 
ATOM   4565 N  N     . ALA B 1 302 ? -2.122  -2.895  -8.885  1.00 66.08  ?  302 ALA B N     1 
ATOM   4566 C  CA    . ALA B 1 302 ? -1.625  -1.722  -9.585  1.00 64.02  ?  302 ALA B CA    1 
ATOM   4567 C  C     . ALA B 1 302 ? -2.491  -0.511  -9.272  1.00 65.75  ?  302 ALA B C     1 
ATOM   4568 O  O     . ALA B 1 302 ? -1.996  0.503   -8.776  1.00 67.89  ?  302 ALA B O     1 
ATOM   4569 C  CB    . ALA B 1 302 ? -1.567  -1.989  -11.089 1.00 56.46  ?  302 ALA B CB    1 
ATOM   4570 N  N     . LEU B 1 303 ? -3.803  -0.620  -9.493  1.00 65.98  ?  303 LEU B N     1 
ATOM   4571 C  CA    . LEU B 1 303 ? -4.682  0.532   -9.295  1.00 64.64  ?  303 LEU B CA    1 
ATOM   4572 C  C     . LEU B 1 303 ? -4.799  0.968   -7.830  1.00 71.16  ?  303 LEU B C     1 
ATOM   4573 O  O     . LEU B 1 303 ? -5.543  1.914   -7.545  1.00 71.84  ?  303 LEU B O     1 
ATOM   4574 C  CB    . LEU B 1 303 ? -6.070  0.242   -9.866  1.00 61.56  ?  303 LEU B CB    1 
ATOM   4575 C  CG    . LEU B 1 303 ? -6.204  -0.334  -11.274 1.00 59.26  ?  303 LEU B CG    1 
ATOM   4576 C  CD1   . LEU B 1 303 ? -7.551  0.042   -11.889 1.00 59.20  ?  303 LEU B CD1   1 
ATOM   4577 C  CD2   . LEU B 1 303 ? -5.097  0.166   -12.140 1.00 54.84  ?  303 LEU B CD2   1 
ATOM   4578 N  N     . GLU B 1 304 ? -4.101  0.305   -6.906  1.00 76.51  ?  304 GLU B N     1 
ATOM   4579 C  CA    . GLU B 1 304 ? -3.946  0.768   -5.523  1.00 73.75  ?  304 GLU B CA    1 
ATOM   4580 C  C     . GLU B 1 304 ? -2.468  0.722   -5.113  1.00 75.03  ?  304 GLU B C     1 
ATOM   4581 O  O     . GLU B 1 304 ? -2.131  0.666   -3.933  1.00 81.01  ?  304 GLU B O     1 
ATOM   4582 C  CB    . GLU B 1 304 ? -4.800  -0.074  -4.586  1.00 62.32  ?  304 GLU B CB    1 
ATOM   4583 C  CG    . GLU B 1 304 ? -6.230  -0.171  -5.069  1.00 72.30  ?  304 GLU B CG    1 
ATOM   4584 C  CD    . GLU B 1 304 ? -6.745  -1.602  -5.125  1.00 79.14  ?  304 GLU B CD    1 
ATOM   4585 O  OE1   . GLU B 1 304 ? -6.094  -2.505  -4.542  1.00 75.83  ?  304 GLU B OE1   1 
ATOM   4586 O  OE2   . GLU B 1 304 ? -7.809  -1.816  -5.756  1.00 77.98  ?  304 GLU B OE2   1 
HETATM 4587 N  N1    . UPG C 2 .   ? 28.316  0.874   11.978  1.00 41.90  ?  401 UPG A N1    1 
HETATM 4588 C  C2    . UPG C 2 .   ? 29.008  0.938   13.185  1.00 42.15  ?  401 UPG A C2    1 
HETATM 4589 N  N3    . UPG C 2 .   ? 30.030  0.029   13.317  1.00 39.47  ?  401 UPG A N3    1 
HETATM 4590 C  C4    . UPG C 2 .   ? 30.413  -0.930  12.400  1.00 41.52  ?  401 UPG A C4    1 
HETATM 4591 C  C5    . UPG C 2 .   ? 29.640  -0.951  11.188  1.00 34.31  ?  401 UPG A C5    1 
HETATM 4592 C  C6    . UPG C 2 .   ? 28.640  -0.071  11.025  1.00 38.59  ?  401 UPG A C6    1 
HETATM 4593 O  O2    . UPG C 2 .   ? 28.764  1.749   14.060  1.00 40.24  ?  401 UPG A O2    1 
HETATM 4594 O  O4    . UPG C 2 .   ? 31.348  -1.685  12.678  1.00 45.10  ?  401 UPG A O4    1 
HETATM 4595 C  C1C   . UPG C 2 .   ? 27.166  1.785   11.762  1.00 38.42  ?  401 UPG A C1C   1 
HETATM 4596 C  C2C   . UPG C 2 .   ? 27.009  2.320   10.344  1.00 40.77  ?  401 UPG A C2C   1 
HETATM 4597 O  O2C   . UPG C 2 .   ? 27.846  3.445   10.140  1.00 43.98  ?  401 UPG A O2C   1 
HETATM 4598 C  C3C   . UPG C 2 .   ? 25.517  2.667   10.357  1.00 36.01  ?  401 UPG A C3C   1 
HETATM 4599 C  C4C   . UPG C 2 .   ? 24.947  1.420   11.035  1.00 40.00  ?  401 UPG A C4C   1 
HETATM 4600 O  O4C   . UPG C 2 .   ? 25.984  1.025   11.966  1.00 43.62  ?  401 UPG A O4C   1 
HETATM 4601 O  O3C   . UPG C 2 .   ? 25.291  3.813   11.162  1.00 37.79  ?  401 UPG A O3C   1 
HETATM 4602 C  C5C   . UPG C 2 .   ? 24.568  0.282   10.113  1.00 41.92  ?  401 UPG A C5C   1 
HETATM 4603 O  O5C   . UPG C 2 .   ? 25.717  -0.149  9.316   1.00 50.27  ?  401 UPG A O5C   1 
HETATM 4604 P  PA    . UPG C 2 .   ? 25.440  -0.505  7.779   1.00 43.86  ?  401 UPG A PA    1 
HETATM 4605 O  O1A   . UPG C 2 .   ? 26.622  -1.175  7.185   1.00 55.38  -1 401 UPG A O1A   1 
HETATM 4606 O  O2A   . UPG C 2 .   ? 24.774  0.655   7.132   1.00 41.27  ?  401 UPG A O2A   1 
HETATM 4607 O  O3A   . UPG C 2 .   ? 24.276  -1.560  8.022   1.00 54.80  ?  401 UPG A O3A   1 
HETATM 4608 P  PB    . UPG C 2 .   ? 23.244  -2.211  6.998   1.00 50.73  ?  401 UPG A PB    1 
HETATM 4609 O  O1B   . UPG C 2 .   ? 22.579  -1.073  6.322   1.00 49.21  ?  401 UPG A O1B   1 
HETATM 4610 O  O2B   . UPG C 2 .   ? 23.920  -3.251  6.185   1.00 64.75  -1 401 UPG A O2B   1 
HETATM 4611 O  O3B   . UPG C 2 .   ? 22.279  -2.910  8.051   1.00 58.22  ?  401 UPG A O3B   1 
HETATM 4612 C  "C1'" . UPG C 2 .   ? 22.868  -3.671  9.068   1.00 67.00  ?  401 UPG A "C1'" 1 
HETATM 4613 C  "C2'" . UPG C 2 .   ? 22.380  -5.128  9.090   1.00 63.59  ?  401 UPG A "C2'" 1 
HETATM 4614 C  "C3'" . UPG C 2 .   ? 20.956  -5.331  9.602   1.00 64.25  ?  401 UPG A "C3'" 1 
HETATM 4615 C  "C4'" . UPG C 2 .   ? 20.386  -4.202  10.463  1.00 57.59  ?  401 UPG A "C4'" 1 
HETATM 4616 C  "C5'" . UPG C 2 .   ? 21.041  -2.854  10.173  1.00 62.62  ?  401 UPG A "C5'" 1 
HETATM 4617 C  "C6'" . UPG C 2 .   ? 20.675  -1.688  11.054  1.00 54.65  ?  401 UPG A "C6'" 1 
HETATM 4618 O  "O2'" . UPG C 2 .   ? 22.448  -5.677  7.778   1.00 65.34  ?  401 UPG A "O2'" 1 
HETATM 4619 O  "O3'" . UPG C 2 .   ? 21.011  -6.541  10.365  1.00 63.44  ?  401 UPG A "O3'" 1 
HETATM 4620 O  "O4'" . UPG C 2 .   ? 19.023  -4.026  10.086  1.00 58.32  ?  401 UPG A "O4'" 1 
HETATM 4621 O  "O5'" . UPG C 2 .   ? 22.470  -2.981  10.247  1.00 63.70  ?  401 UPG A "O5'" 1 
HETATM 4622 O  "O6'" . UPG C 2 .   ? 21.347  -0.583  10.460  1.00 52.65  ?  401 UPG A "O6'" 1 
HETATM 4623 O  "O5'" . RAB D 3 .   ? 18.594  -7.158  3.771   1.00 66.79  ?  402 RAB A "O5'" 1 
HETATM 4624 C  "C5'" . RAB D 3 .   ? 18.942  -8.448  4.253   1.00 68.50  ?  402 RAB A "C5'" 1 
HETATM 4625 C  "C4'" . RAB D 3 .   ? 20.372  -8.927  4.085   1.00 67.37  ?  402 RAB A "C4'" 1 
HETATM 4626 O  "O4'" . RAB D 3 .   ? 20.648  -9.906  5.108   1.00 66.30  ?  402 RAB A "O4'" 1 
HETATM 4627 C  "C1'" . RAB D 3 .   ? 20.330  -11.202 4.594   1.00 66.02  ?  402 RAB A "C1'" 1 
HETATM 4628 N  N9    . RAB D 3 .   ? 19.332  -11.857 5.450   1.00 63.20  ?  402 RAB A N9    1 
HETATM 4629 C  C4    . RAB D 3 .   ? 18.565  -11.323 6.465   1.00 57.64  ?  402 RAB A C4    1 
HETATM 4630 N  N3    . RAB D 3 .   ? 18.507  -10.045 6.882   1.00 55.08  ?  402 RAB A N3    1 
HETATM 4631 C  C2    . RAB D 3 .   ? 17.649  -9.904  7.887   1.00 56.76  ?  402 RAB A C2    1 
HETATM 4632 N  N1    . RAB D 3 .   ? 16.892  -10.830 8.485   1.00 53.03  ?  402 RAB A N1    1 
HETATM 4633 C  C6    . RAB D 3 .   ? 16.966  -12.111 8.049   1.00 50.75  ?  402 RAB A C6    1 
HETATM 4634 N  N6    . RAB D 3 .   ? 16.229  -13.044 8.651   1.00 52.44  ?  402 RAB A N6    1 
HETATM 4635 C  C5    . RAB D 3 .   ? 17.845  -12.383 6.988   1.00 56.05  ?  402 RAB A C5    1 
HETATM 4636 N  N7    . RAB D 3 .   ? 18.150  -13.562 6.321   1.00 58.59  ?  402 RAB A N7    1 
HETATM 4637 C  C8    . RAB D 3 .   ? 19.037  -13.197 5.426   1.00 61.26  ?  402 RAB A C8    1 
HETATM 4638 C  "C2'" . RAB D 3 .   ? 20.058  -11.067 3.092   1.00 65.29  ?  402 RAB A "C2'" 1 
HETATM 4639 O  "O2'" . RAB D 3 .   ? 18.675  -11.161 2.815   1.00 65.67  ?  402 RAB A "O2'" 1 
HETATM 4640 C  "C3'" . RAB D 3 .   ? 20.700  -9.703  2.805   1.00 68.64  ?  402 RAB A "C3'" 1 
HETATM 4641 O  "O3'" . RAB D 3 .   ? 22.108  -9.903  2.773   1.00 59.48  ?  402 RAB A "O3'" 1 
HETATM 4642 MG MG    . MG  E 4 .   ? 22.751  1.072   5.892   1.00 33.49  ?  403 MG  A MG    1 
HETATM 4643 N  N1    . UPG F 2 .   ? -1.684  22.077  -27.095 1.00 35.99  ?  401 UPG B N1    1 
HETATM 4644 C  C2    . UPG F 2 .   ? -2.078  22.624  -28.305 1.00 33.42  ?  401 UPG B C2    1 
HETATM 4645 N  N3    . UPG F 2 .   ? -3.429  22.852  -28.424 1.00 32.03  ?  401 UPG B N3    1 
HETATM 4646 C  C4    . UPG F 2 .   ? -4.401  22.556  -27.479 1.00 33.76  ?  401 UPG B C4    1 
HETATM 4647 C  C5    . UPG F 2 .   ? -3.919  21.956  -26.269 1.00 30.11  ?  401 UPG B C5    1 
HETATM 4648 C  C6    . UPG F 2 .   ? -2.602  21.741  -26.120 1.00 35.17  ?  401 UPG B C6    1 
HETATM 4649 O  O2    . UPG F 2 .   ? -1.280  22.940  -29.171 1.00 36.05  ?  401 UPG B O2    1 
HETATM 4650 O  O4    . UPG F 2 .   ? -5.577  22.799  -27.722 1.00 34.73  ?  401 UPG B O4    1 
HETATM 4651 C  C1C   . UPG F 2 .   ? -0.257  21.776  -26.889 1.00 33.11  ?  401 UPG B C1C   1 
HETATM 4652 C  C2C   . UPG F 2 .   ? 0.241   22.128  -25.490 1.00 34.26  ?  401 UPG B C2C   1 
HETATM 4653 O  O2C   . UPG F 2 .   ? 0.512   23.515  -25.443 1.00 30.28  ?  401 UPG B O2C   1 
HETATM 4654 C  C3C   . UPG F 2 .   ? 1.462   21.205  -25.406 1.00 30.11  ?  401 UPG B C3C   1 
HETATM 4655 C  C4C   . UPG F 2 .   ? 0.870   19.921  -25.996 1.00 35.38  ?  401 UPG B C4C   1 
HETATM 4656 O  O4C   . UPG F 2 .   ? -0.146  20.366  -26.932 1.00 34.64  ?  401 UPG B O4C   1 
HETATM 4657 O  O3C   . UPG F 2 .   ? 2.494   21.665  -26.266 1.00 35.35  ?  401 UPG B O3C   1 
HETATM 4658 C  C5C   . UPG F 2 .   ? 0.283   18.930  -25.019 1.00 32.49  ?  401 UPG B C5C   1 
HETATM 4659 O  O5C   . UPG F 2 .   ? -0.836  19.473  -24.272 1.00 32.75  ?  401 UPG B O5C   1 
HETATM 4660 P  PA    . UPG F 2 .   ? -0.845  19.059  -22.725 1.00 38.44  ?  401 UPG B PA    1 
HETATM 4661 O  O1A   . UPG F 2 .   ? -2.049  19.613  -22.048 1.00 36.25  -1 401 UPG B O1A   1 
HETATM 4662 O  O2A   . UPG F 2 .   ? 0.492   19.381  -22.144 1.00 31.21  ?  401 UPG B O2A   1 
HETATM 4663 O  O3A   . UPG F 2 .   ? -0.862  17.446  -22.859 1.00 39.60  ?  401 UPG B O3A   1 
HETATM 4664 P  PB    . UPG F 2 .   ? -0.674  16.409  -21.662 1.00 38.18  ?  401 UPG B PB    1 
HETATM 4665 O  O1B   . UPG F 2 .   ? 0.401   16.968  -20.807 1.00 39.84  -1 401 UPG B O1B   1 
HETATM 4666 O  O2B   . UPG F 2 .   ? -1.992  16.084  -21.076 1.00 52.13  ?  401 UPG B O2B   1 
HETATM 4667 O  O3B   . UPG F 2 .   ? 0.090   15.053  -21.984 1.00 49.67  ?  401 UPG B O3B   1 
HETATM 4668 C  "C1'" . UPG F 2 .   ? -0.023  14.355  -23.173 1.00 52.95  ?  401 UPG B "C1'" 1 
HETATM 4669 C  "C2'" . UPG F 2 .   ? 0.011   12.830  -23.029 1.00 49.45  ?  401 UPG B "C2'" 1 
HETATM 4670 C  "C3'" . UPG F 2 .   ? 0.276   12.281  -24.427 1.00 42.10  ?  401 UPG B "C3'" 1 
HETATM 4671 C  "C4'" . UPG F 2 .   ? 0.041   13.364  -25.469 1.00 40.20  ?  401 UPG B "C4'" 1 
HETATM 4672 C  "C5'" . UPG F 2 .   ? 1.056   14.466  -25.212 1.00 40.79  ?  401 UPG B "C5'" 1 
HETATM 4673 C  "C6'" . UPG F 2 .   ? 0.606   15.743  -25.858 1.00 42.21  ?  401 UPG B "C6'" 1 
HETATM 4674 O  "O2'" . UPG F 2 .   ? 0.961   12.414  -22.049 1.00 51.65  ?  401 UPG B "O2'" 1 
HETATM 4675 O  "O3'" . UPG F 2 .   ? -0.602  11.200  -24.723 1.00 44.50  ?  401 UPG B "O3'" 1 
HETATM 4676 O  "O4'" . UPG F 2 .   ? 0.377   13.054  -26.818 1.00 41.72  ?  401 UPG B "O4'" 1 
HETATM 4677 O  "O5'" . UPG F 2 .   ? 1.174   14.757  -23.820 1.00 47.19  ?  401 UPG B "O5'" 1 
HETATM 4678 O  "O6'" . UPG F 2 .   ? 1.835   16.367  -26.196 1.00 43.77  ?  401 UPG B "O6'" 1 
HETATM 4679 O  "O5'" . RAB G 3 .   ? -2.495  8.191   -15.207 1.00 71.90  ?  402 RAB B "O5'" 1 
HETATM 4680 C  "C5'" . RAB G 3 .   ? -2.105  9.141   -16.191 1.00 69.36  ?  402 RAB B "C5'" 1 
HETATM 4681 C  "C4'" . RAB G 3 .   ? -3.046  9.336   -17.363 1.00 65.89  ?  402 RAB B "C4'" 1 
HETATM 4682 O  "O4'" . RAB G 3 .   ? -3.323  8.074   -18.004 1.00 66.01  ?  402 RAB B "O4'" 1 
HETATM 4683 C  "C1'" . RAB G 3 .   ? -4.343  8.451   -18.922 1.00 60.91  ?  402 RAB B "C1'" 1 
HETATM 4684 N  N9    . RAB G 3 .   ? -4.785  7.261   -19.650 1.00 55.53  ?  402 RAB B N9    1 
HETATM 4685 C  C4    . RAB G 3 .   ? -4.117  6.832   -20.766 1.00 51.50  ?  402 RAB B C4    1 
HETATM 4686 N  N3    . RAB G 3 .   ? -3.037  7.400   -21.318 1.00 53.49  ?  402 RAB B N3    1 
HETATM 4687 C  C2    . RAB G 3 .   ? -2.647  6.718   -22.388 1.00 52.53  ?  402 RAB B C2    1 
HETATM 4688 N  N1    . RAB G 3 .   ? -3.182  5.620   -22.931 1.00 47.97  ?  402 RAB B N1    1 
HETATM 4689 C  C6    . RAB G 3 .   ? -4.266  5.060   -22.350 1.00 47.76  ?  402 RAB B C6    1 
HETATM 4690 N  N6    . RAB G 3 .   ? -4.774  3.950   -22.891 1.00 48.24  ?  402 RAB B N6    1 
HETATM 4691 C  C5    . RAB G 3 .   ? -4.773  5.697   -21.199 1.00 52.55  ?  402 RAB B C5    1 
HETATM 4692 N  N7    . RAB G 3 .   ? -5.848  5.411   -20.365 1.00 54.32  ?  402 RAB B N7    1 
HETATM 4693 C  C8    . RAB G 3 .   ? -5.805  6.362   -19.461 1.00 53.84  ?  402 RAB B C8    1 
HETATM 4694 C  "C2'" . RAB G 3 .   ? -5.353  9.247   -18.095 1.00 61.34  ?  402 RAB B "C2'" 1 
HETATM 4695 O  "O2'" . RAB G 3 .   ? -6.203  8.351   -17.411 1.00 58.91  ?  402 RAB B "O2'" 1 
HETATM 4696 C  "C3'" . RAB G 3 .   ? -4.426  9.959   -17.094 1.00 71.37  ?  402 RAB B "C3'" 1 
HETATM 4697 O  "O3'" . RAB G 3 .   ? -4.367  11.372  -17.265 1.00 74.60  ?  402 RAB B "O3'" 1 
HETATM 4698 MG MG    . MG  H 4 .   ? 2.064   18.325  -20.694 1.00 25.18  ?  403 MG  B MG    1 
HETATM 4699 O  O     . HOH I 5 .   ? 4.935   16.552  18.853  1.00 49.29  ?  501 HOH A O     1 
HETATM 4700 O  O     . HOH I 5 .   ? -0.043  2.671   26.720  1.00 37.82  ?  502 HOH A O     1 
HETATM 4701 O  O     . HOH I 5 .   ? 23.837  -0.250  4.471   1.00 54.06  ?  503 HOH A O     1 
HETATM 4702 O  O     . HOH I 5 .   ? 21.251  3.012   14.037  1.00 33.99  ?  504 HOH A O     1 
HETATM 4703 O  O     . HOH I 5 .   ? 21.030  1.755   7.158   1.00 40.50  ?  505 HOH A O     1 
HETATM 4704 O  O     . HOH I 5 .   ? 18.142  17.812  24.469  1.00 28.25  ?  506 HOH A O     1 
HETATM 4705 O  O     . HOH I 5 .   ? 4.226   -5.447  23.252  1.00 38.07  ?  507 HOH A O     1 
HETATM 4706 O  O     . HOH I 5 .   ? 20.454  15.115  4.295   1.00 42.37  ?  508 HOH A O     1 
HETATM 4707 O  O     . HOH I 5 .   ? 5.742   -19.478 19.932  1.00 40.15  ?  509 HOH A O     1 
HETATM 4708 O  O     . HOH I 5 .   ? 9.801   16.175  12.509  1.00 37.34  ?  510 HOH A O     1 
HETATM 4709 O  O     . HOH I 5 .   ? 10.726  -20.793 17.160  1.00 38.05  ?  511 HOH A O     1 
HETATM 4710 O  O     . HOH I 5 .   ? 22.031  4.631   -3.621  1.00 58.27  ?  512 HOH A O     1 
HETATM 4711 O  O     . HOH I 5 .   ? 16.919  8.259   26.840  1.00 31.07  ?  513 HOH A O     1 
HETATM 4712 O  O     . HOH I 5 .   ? 16.450  7.862   30.567  1.00 32.79  ?  514 HOH A O     1 
HETATM 4713 O  O     . HOH I 5 .   ? 36.869  5.729   24.011  1.00 35.47  ?  515 HOH A O     1 
HETATM 4714 O  O     . HOH I 5 .   ? 29.562  0.549   23.804  1.00 32.71  ?  516 HOH A O     1 
HETATM 4715 O  O     . HOH I 5 .   ? 14.210  7.193   14.177  1.00 28.81  ?  517 HOH A O     1 
HETATM 4716 O  O     . HOH I 5 .   ? 7.396   -3.190  7.646   1.00 31.58  ?  518 HOH A O     1 
HETATM 4717 O  O     . HOH I 5 .   ? 11.334  -2.914  31.676  1.00 38.23  ?  519 HOH A O     1 
HETATM 4718 O  O     . HOH I 5 .   ? 2.289   -7.570  11.191  1.00 34.27  ?  520 HOH A O     1 
HETATM 4719 O  O     . HOH I 5 .   ? 7.647   11.574  5.733   1.00 39.49  ?  521 HOH A O     1 
HETATM 4720 O  O     . HOH I 5 .   ? 36.012  11.464  15.576  1.00 39.56  ?  522 HOH A O     1 
HETATM 4721 O  O     . HOH I 5 .   ? 22.228  -20.542 15.635  1.00 40.09  ?  523 HOH A O     1 
HETATM 4722 O  O     . HOH I 5 .   ? -0.033  -1.499  16.904  1.00 34.95  ?  524 HOH A O     1 
HETATM 4723 O  O     . HOH I 5 .   ? 10.996  10.164  8.194   1.00 28.99  ?  525 HOH A O     1 
HETATM 4724 O  O     . HOH I 5 .   ? 7.725   0.080   7.561   1.00 30.23  ?  526 HOH A O     1 
HETATM 4725 O  O     . HOH I 5 .   ? 34.060  6.888   11.450  1.00 41.05  ?  527 HOH A O     1 
HETATM 4726 O  O     . HOH I 5 .   ? 22.985  9.458   5.230   1.00 39.16  ?  528 HOH A O     1 
HETATM 4727 O  O     . HOH I 5 .   ? 14.760  15.632  7.289   1.00 33.27  ?  529 HOH A O     1 
HETATM 4728 O  O     . HOH I 5 .   ? 20.549  -7.103  20.001  1.00 29.41  ?  530 HOH A O     1 
HETATM 4729 O  O     . HOH I 5 .   ? -7.325  -22.272 3.918   1.00 47.77  ?  531 HOH A O     1 
HETATM 4730 O  O     . HOH I 5 .   ? 19.477  20.204  18.572  1.00 42.18  ?  532 HOH A O     1 
HETATM 4731 O  O     . HOH I 5 .   ? 6.327   4.482   1.330   1.00 48.46  ?  533 HOH A O     1 
HETATM 4732 O  O     . HOH I 5 .   ? 2.087   -2.742  27.654  1.00 46.79  ?  534 HOH A O     1 
HETATM 4733 O  O     . HOH I 5 .   ? 15.605  -4.956  5.051   1.00 43.11  ?  535 HOH A O     1 
HETATM 4734 O  O     . HOH I 5 .   ? 16.775  -6.580  28.649  1.00 37.53  ?  536 HOH A O     1 
HETATM 4735 O  O     . HOH I 5 .   ? 2.824   -4.154  20.968  1.00 36.47  ?  537 HOH A O     1 
HETATM 4736 O  O     . HOH I 5 .   ? -0.568  0.718   9.808   1.00 37.98  ?  538 HOH A O     1 
HETATM 4737 O  O     . HOH I 5 .   ? 18.301  5.446   26.400  1.00 27.97  ?  539 HOH A O     1 
HETATM 4738 O  O     . HOH I 5 .   ? 4.575   -8.870  16.635  1.00 44.95  ?  540 HOH A O     1 
HETATM 4739 O  O     . HOH I 5 .   ? 19.832  -5.359  27.649  1.00 34.60  ?  541 HOH A O     1 
HETATM 4740 O  O     . HOH I 5 .   ? 0.199   -20.491 7.510   1.00 55.05  ?  542 HOH A O     1 
HETATM 4741 O  O     . HOH I 5 .   ? 41.133  1.756   23.762  1.00 39.84  ?  543 HOH A O     1 
HETATM 4742 O  O     . HOH I 5 .   ? 3.289   15.709  11.138  1.00 46.36  ?  544 HOH A O     1 
HETATM 4743 O  O     . HOH I 5 .   ? 17.342  -7.741  10.958  1.00 44.44  ?  545 HOH A O     1 
HETATM 4744 O  O     . HOH I 5 .   ? 41.173  -0.180  19.638  1.00 48.02  ?  546 HOH A O     1 
HETATM 4745 O  O     . HOH I 5 .   ? 4.233   -10.195 19.077  1.00 47.77  ?  547 HOH A O     1 
HETATM 4746 O  O     . HOH I 5 .   ? 3.807   -1.233  -0.331  1.00 53.00  ?  548 HOH A O     1 
HETATM 4747 O  O     . HOH I 5 .   ? 4.590   -7.340  12.819  1.00 33.50  ?  549 HOH A O     1 
HETATM 4748 O  O     . HOH I 5 .   ? -0.242  -0.088  14.357  1.00 27.44  ?  550 HOH A O     1 
HETATM 4749 O  O     . HOH I 5 .   ? 26.372  -0.418  27.012  1.00 36.98  ?  551 HOH A O     1 
HETATM 4750 O  O     . HOH I 5 .   ? -0.552  -1.369  12.227  1.00 34.92  ?  552 HOH A O     1 
HETATM 4751 O  O     . HOH I 5 .   ? 2.568   -4.739  24.954  1.00 36.38  ?  553 HOH A O     1 
HETATM 4752 O  O     . HOH I 5 .   ? 33.619  -12.139 -5.462  1.00 69.82  ?  554 HOH A O     1 
HETATM 4753 O  O     . HOH I 5 .   ? 16.594  9.971   31.472  1.00 41.70  ?  555 HOH A O     1 
HETATM 4754 O  O     . HOH I 5 .   ? 19.610  6.922   1.523   1.00 45.73  ?  556 HOH A O     1 
HETATM 4755 O  O     . HOH I 5 .   ? 18.099  -10.905 26.816  1.00 31.53  ?  557 HOH A O     1 
HETATM 4756 O  O     . HOH I 5 .   ? 43.007  1.768   21.539  1.00 34.15  ?  558 HOH A O     1 
HETATM 4757 O  O     . HOH I 5 .   ? 6.906   18.836  20.928  1.00 49.62  ?  559 HOH A O     1 
HETATM 4758 O  O     . HOH I 5 .   ? 29.332  -10.834 -2.856  1.00 60.32  ?  560 HOH A O     1 
HETATM 4759 O  O     . HOH I 5 .   ? 28.535  1.332   26.226  1.00 37.17  ?  561 HOH A O     1 
HETATM 4760 O  O     . HOH I 5 .   ? 34.106  -15.037 -7.263  1.00 58.13  ?  562 HOH A O     1 
HETATM 4761 O  O     . HOH I 5 .   ? 22.124  -5.032  29.301  1.00 42.48  ?  563 HOH A O     1 
HETATM 4762 O  O     . HOH I 5 .   ? 24.684  -3.468  -1.516  1.00 58.38  ?  564 HOH A O     1 
HETATM 4763 O  O     . HOH I 5 .   ? 2.409   20.045  18.572  1.00 44.89  ?  565 HOH A O     1 
HETATM 4764 O  O     . HOH J 5 .   ? 9.349   12.142  -49.041 1.00 43.94  ?  501 HOH B O     1 
HETATM 4765 O  O     . HOH J 5 .   ? 18.355  24.565  -39.838 1.00 33.62  ?  502 HOH B O     1 
HETATM 4766 O  O     . HOH J 5 .   ? -13.456 -1.841  -29.616 1.00 52.17  ?  503 HOH B O     1 
HETATM 4767 O  O     . HOH J 5 .   ? -6.456  26.227  -36.852 1.00 46.91  ?  504 HOH B O     1 
HETATM 4768 O  O     . HOH J 5 .   ? 11.397  17.743  -42.041 1.00 31.40  ?  505 HOH B O     1 
HETATM 4769 O  O     . HOH J 5 .   ? 0.148   18.738  -19.338 1.00 42.03  ?  506 HOH B O     1 
HETATM 4770 O  O     . HOH J 5 .   ? 14.680  7.722   -15.779 1.00 50.90  ?  507 HOH B O     1 
HETATM 4771 O  O     . HOH J 5 .   ? -0.686  30.489  -26.936 1.00 28.44  ?  508 HOH B O     1 
HETATM 4772 O  O     . HOH J 5 .   ? 7.326   -1.653  -34.210 1.00 39.69  ?  509 HOH B O     1 
HETATM 4773 O  O     . HOH J 5 .   ? -2.781  22.140  -38.567 1.00 39.38  ?  510 HOH B O     1 
HETATM 4774 O  O     . HOH J 5 .   ? -10.537 12.934  -29.148 1.00 41.86  ?  511 HOH B O     1 
HETATM 4775 O  O     . HOH J 5 .   ? 3.200   35.234  -14.050 1.00 41.54  ?  512 HOH B O     1 
HETATM 4776 O  O     . HOH J 5 .   ? 11.583  33.827  -24.338 1.00 42.95  ?  513 HOH B O     1 
HETATM 4777 O  O     . HOH J 5 .   ? 11.021  34.212  -35.858 1.00 43.52  ?  514 HOH B O     1 
HETATM 4778 O  O     . HOH J 5 .   ? 18.093  33.895  -34.572 1.00 48.07  ?  515 HOH B O     1 
HETATM 4779 O  O     . HOH J 5 .   ? 1.165   34.297  -31.055 1.00 40.70  ?  516 HOH B O     1 
HETATM 4780 O  O     . HOH J 5 .   ? 3.511   17.019  -22.056 1.00 34.43  ?  517 HOH B O     1 
HETATM 4781 O  O     . HOH J 5 .   ? 8.588   -3.533  -25.152 1.00 41.76  ?  518 HOH B O     1 
HETATM 4782 O  O     . HOH J 5 .   ? -3.684  6.272   -38.122 1.00 38.04  ?  519 HOH B O     1 
HETATM 4783 O  O     . HOH J 5 .   ? 4.562   14.651  -24.544 1.00 36.72  ?  520 HOH B O     1 
HETATM 4784 O  O     . HOH J 5 .   ? 17.782  24.976  -19.814 1.00 42.82  ?  521 HOH B O     1 
HETATM 4785 O  O     . HOH J 5 .   ? 22.045  17.575  -27.190 1.00 37.06  ?  522 HOH B O     1 
HETATM 4786 O  O     . HOH J 5 .   ? 2.396   25.066  -41.475 1.00 35.35  ?  523 HOH B O     1 
HETATM 4787 O  O     . HOH J 5 .   ? -18.615 13.257  -6.915  1.00 57.36  ?  524 HOH B O     1 
HETATM 4788 O  O     . HOH J 5 .   ? 4.873   18.194  -29.098 1.00 28.83  ?  525 HOH B O     1 
HETATM 4789 O  O     . HOH J 5 .   ? 16.361  14.786  -22.680 1.00 38.39  ?  526 HOH B O     1 
HETATM 4790 O  O     . HOH J 5 .   ? 14.566  -1.767  -30.867 1.00 36.50  ?  527 HOH B O     1 
HETATM 4791 O  O     . HOH J 5 .   ? 11.979  15.017  -28.682 1.00 29.41  ?  528 HOH B O     1 
HETATM 4792 O  O     . HOH J 5 .   ? 2.396   4.085   -44.530 1.00 35.26  ?  529 HOH B O     1 
HETATM 4793 O  O     . HOH J 5 .   ? 18.742  21.670  -22.144 1.00 41.44  ?  530 HOH B O     1 
HETATM 4794 O  O     . HOH J 5 .   ? -5.804  33.201  -23.065 1.00 33.50  ?  531 HOH B O     1 
HETATM 4795 O  O     . HOH J 5 .   ? -7.235  -5.446  -31.308 1.00 37.54  ?  532 HOH B O     1 
HETATM 4796 O  O     . HOH J 5 .   ? 1.387   29.726  -24.900 1.00 32.75  ?  533 HOH B O     1 
HETATM 4797 O  O     . HOH J 5 .   ? 8.579   3.884   -21.732 1.00 36.99  ?  534 HOH B O     1 
HETATM 4798 O  O     . HOH J 5 .   ? -2.653  10.570  -34.709 1.00 31.10  ?  535 HOH B O     1 
HETATM 4799 O  O     . HOH J 5 .   ? -2.667  4.017   -25.188 1.00 41.16  ?  536 HOH B O     1 
HETATM 4800 O  O     . HOH J 5 .   ? 8.389   23.954  -20.271 1.00 31.99  ?  537 HOH B O     1 
HETATM 4801 O  O     . HOH J 5 .   ? 25.759  7.320   -36.291 1.00 43.49  ?  538 HOH B O     1 
HETATM 4802 O  O     . HOH J 5 .   ? 14.131  12.999  -43.227 1.00 31.66  ?  539 HOH B O     1 
HETATM 4803 O  O     . HOH J 5 .   ? 16.290  -0.757  -23.744 1.00 29.56  ?  540 HOH B O     1 
HETATM 4804 O  O     . HOH J 5 .   ? 8.186   -3.756  -29.074 1.00 42.42  ?  541 HOH B O     1 
HETATM 4805 O  O     . HOH J 5 .   ? 3.183   -7.131  -30.956 1.00 43.19  ?  542 HOH B O     1 
HETATM 4806 O  O     . HOH J 5 .   ? 15.702  -0.723  -28.443 1.00 33.54  ?  543 HOH B O     1 
HETATM 4807 O  O     . HOH J 5 .   ? 15.391  30.869  -25.019 1.00 42.02  ?  544 HOH B O     1 
HETATM 4808 O  O     . HOH J 5 .   ? 10.074  1.024   -17.123 1.00 43.26  ?  545 HOH B O     1 
HETATM 4809 O  O     . HOH J 5 .   ? 2.621   29.794  -18.629 1.00 19.89  ?  546 HOH B O     1 
HETATM 4810 O  O     . HOH J 5 .   ? -3.019  27.210  -19.813 1.00 32.80  ?  547 HOH B O     1 
HETATM 4811 O  O     . HOH J 5 .   ? 13.525  31.540  -23.616 1.00 39.90  ?  548 HOH B O     1 
HETATM 4812 O  O     . HOH J 5 .   ? 25.391  7.562   -40.377 1.00 34.59  ?  549 HOH B O     1 
HETATM 4813 O  O     . HOH J 5 .   ? 7.056   -1.632  -26.877 1.00 28.43  ?  550 HOH B O     1 
HETATM 4814 O  O     . HOH J 5 .   ? 0.589   8.506   -42.774 1.00 13.10  ?  551 HOH B O     1 
HETATM 4815 O  O     . HOH J 5 .   ? 14.835  25.345  -19.184 1.00 36.81  ?  552 HOH B O     1 
HETATM 4816 O  O     . HOH J 5 .   ? 27.736  20.690  -38.032 1.00 42.05  ?  553 HOH B O     1 
HETATM 4817 O  O     . HOH J 5 .   ? -11.162 4.623   -36.230 1.00 38.50  ?  554 HOH B O     1 
HETATM 4818 O  O     . HOH J 5 .   ? 15.250  -1.729  -26.095 1.00 36.38  ?  555 HOH B O     1 
HETATM 4819 O  O     . HOH J 5 .   ? 17.083  2.178   -17.871 1.00 37.91  ?  556 HOH B O     1 
HETATM 4820 O  O     . HOH J 5 .   ? 10.697  -1.477  -35.194 1.00 37.29  ?  557 HOH B O     1 
HETATM 4821 O  O     . HOH J 5 .   ? 3.652   -13.803 -30.138 1.00 39.53  ?  558 HOH B O     1 
HETATM 4822 O  O     . HOH J 5 .   ? 18.002  21.719  -47.700 1.00 49.75  ?  559 HOH B O     1 
HETATM 4823 O  O     . HOH J 5 .   ? -6.446  34.449  -25.373 1.00 40.07  ?  560 HOH B O     1 
HETATM 4824 O  O     . HOH J 5 .   ? -14.305 17.507  -7.348  1.00 70.84  ?  561 HOH B O     1 
# 
