data_9JMA
# 
_entry.id   9JMA 
# 
_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   9JMA         pdb_00009jma 10.2210/pdb9jma/pdb 
WWPDB D_1300051664 ?            ?                   
# 
_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                        9JMA 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-20 
_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"                                          404.161   2   ?         ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                                   24.305    2   ?         ? ? ? 
4 water       nat water                                                             18.015    388 ?         ? ? ? 
# 
_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" UDP 
3 'MAGNESIUM ION'          MG  
4 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 
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 
UDP 'RNA linking'       . "URIDINE-5'-DIPHOSPHATE" ? 'C9 H14 N2 O12 P2' 404.161 
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 207 207 207 ILE ILE A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 THR 215 215 215 THR THR 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 305 305 305 GLY GLY A . n 
A 1 306 ARG 306 306 306 ARG ARG 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 121 121 121 ARG ARG B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 THR 125 125 125 THR THR 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 305 305 305 GLY GLY B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UDP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UDP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 UDP 1   401 401 UDP UDP A . 
D 3 MG  1   402 1   MG  MG  A . 
E 2 UDP 1   401 401 UDP UDP B . 
F 3 MG  1   402 2   MG  MG  B . 
G 4 HOH 1   501 134 HOH HOH A . 
G 4 HOH 2   502 324 HOH HOH A . 
G 4 HOH 3   503 148 HOH HOH A . 
G 4 HOH 4   504 132 HOH HOH A . 
G 4 HOH 5   505 69  HOH HOH A . 
G 4 HOH 6   506 149 HOH HOH A . 
G 4 HOH 7   507 15  HOH HOH A . 
G 4 HOH 8   508 360 HOH HOH A . 
G 4 HOH 9   509 235 HOH HOH A . 
G 4 HOH 10  510 269 HOH HOH A . 
G 4 HOH 11  511 182 HOH HOH A . 
G 4 HOH 12  512 256 HOH HOH A . 
G 4 HOH 13  513 53  HOH HOH A . 
G 4 HOH 14  514 88  HOH HOH A . 
G 4 HOH 15  515 23  HOH HOH A . 
G 4 HOH 16  516 198 HOH HOH A . 
G 4 HOH 17  517 162 HOH HOH A . 
G 4 HOH 18  518 18  HOH HOH A . 
G 4 HOH 19  519 318 HOH HOH A . 
G 4 HOH 20  520 387 HOH HOH A . 
G 4 HOH 21  521 207 HOH HOH A . 
G 4 HOH 22  522 32  HOH HOH A . 
G 4 HOH 23  523 275 HOH HOH A . 
G 4 HOH 24  524 217 HOH HOH A . 
G 4 HOH 25  525 403 HOH HOH A . 
G 4 HOH 26  526 25  HOH HOH A . 
G 4 HOH 27  527 248 HOH HOH A . 
G 4 HOH 28  528 95  HOH HOH A . 
G 4 HOH 29  529 220 HOH HOH A . 
G 4 HOH 30  530 197 HOH HOH A . 
G 4 HOH 31  531 202 HOH HOH A . 
G 4 HOH 32  532 271 HOH HOH A . 
G 4 HOH 33  533 91  HOH HOH A . 
G 4 HOH 34  534 363 HOH HOH A . 
G 4 HOH 35  535 160 HOH HOH A . 
G 4 HOH 36  536 70  HOH HOH A . 
G 4 HOH 37  537 59  HOH HOH A . 
G 4 HOH 38  538 208 HOH HOH A . 
G 4 HOH 39  539 49  HOH HOH A . 
G 4 HOH 40  540 323 HOH HOH A . 
G 4 HOH 41  541 342 HOH HOH A . 
G 4 HOH 42  542 101 HOH HOH A . 
G 4 HOH 43  543 226 HOH HOH A . 
G 4 HOH 44  544 67  HOH HOH A . 
G 4 HOH 45  545 109 HOH HOH A . 
G 4 HOH 46  546 72  HOH HOH A . 
G 4 HOH 47  547 99  HOH HOH A . 
G 4 HOH 48  548 251 HOH HOH A . 
G 4 HOH 49  549 110 HOH HOH A . 
G 4 HOH 50  550 58  HOH HOH A . 
G 4 HOH 51  551 147 HOH HOH A . 
G 4 HOH 52  552 174 HOH HOH A . 
G 4 HOH 53  553 57  HOH HOH A . 
G 4 HOH 54  554 151 HOH HOH A . 
G 4 HOH 55  555 266 HOH HOH A . 
G 4 HOH 56  556 320 HOH HOH A . 
G 4 HOH 57  557 61  HOH HOH A . 
G 4 HOH 58  558 221 HOH HOH A . 
G 4 HOH 59  559 119 HOH HOH A . 
G 4 HOH 60  560 2   HOH HOH A . 
G 4 HOH 61  561 146 HOH HOH A . 
G 4 HOH 62  562 136 HOH HOH A . 
G 4 HOH 63  563 73  HOH HOH A . 
G 4 HOH 64  564 60  HOH HOH A . 
G 4 HOH 65  565 124 HOH HOH A . 
G 4 HOH 66  566 13  HOH HOH A . 
G 4 HOH 67  567 4   HOH HOH A . 
G 4 HOH 68  568 117 HOH HOH A . 
G 4 HOH 69  569 30  HOH HOH A . 
G 4 HOH 70  570 230 HOH HOH A . 
G 4 HOH 71  571 233 HOH HOH A . 
G 4 HOH 72  572 6   HOH HOH A . 
G 4 HOH 73  573 78  HOH HOH A . 
G 4 HOH 74  574 129 HOH HOH A . 
G 4 HOH 75  575 118 HOH HOH A . 
G 4 HOH 76  576 325 HOH HOH A . 
G 4 HOH 77  577 231 HOH HOH A . 
G 4 HOH 78  578 65  HOH HOH A . 
G 4 HOH 79  579 26  HOH HOH A . 
G 4 HOH 80  580 307 HOH HOH A . 
G 4 HOH 81  581 7   HOH HOH A . 
G 4 HOH 82  582 85  HOH HOH A . 
G 4 HOH 83  583 122 HOH HOH A . 
G 4 HOH 84  584 336 HOH HOH A . 
G 4 HOH 85  585 206 HOH HOH A . 
G 4 HOH 86  586 33  HOH HOH A . 
G 4 HOH 87  587 250 HOH HOH A . 
G 4 HOH 88  588 322 HOH HOH A . 
G 4 HOH 89  589 28  HOH HOH A . 
G 4 HOH 90  590 193 HOH HOH A . 
G 4 HOH 91  591 34  HOH HOH A . 
G 4 HOH 92  592 281 HOH HOH A . 
G 4 HOH 93  593 127 HOH HOH A . 
G 4 HOH 94  594 346 HOH HOH A . 
G 4 HOH 95  595 121 HOH HOH A . 
G 4 HOH 96  596 158 HOH HOH A . 
G 4 HOH 97  597 326 HOH HOH A . 
G 4 HOH 98  598 21  HOH HOH A . 
G 4 HOH 99  599 223 HOH HOH A . 
G 4 HOH 100 600 204 HOH HOH A . 
G 4 HOH 101 601 298 HOH HOH A . 
G 4 HOH 102 602 276 HOH HOH A . 
G 4 HOH 103 603 397 HOH HOH A . 
G 4 HOH 104 604 62  HOH HOH A . 
G 4 HOH 105 605 259 HOH HOH A . 
G 4 HOH 106 606 31  HOH HOH A . 
G 4 HOH 107 607 236 HOH HOH A . 
G 4 HOH 108 608 289 HOH HOH A . 
G 4 HOH 109 609 176 HOH HOH A . 
G 4 HOH 110 610 357 HOH HOH A . 
G 4 HOH 111 611 37  HOH HOH A . 
G 4 HOH 112 612 14  HOH HOH A . 
G 4 HOH 113 613 40  HOH HOH A . 
G 4 HOH 114 614 98  HOH HOH A . 
G 4 HOH 115 615 212 HOH HOH A . 
G 4 HOH 116 616 228 HOH HOH A . 
G 4 HOH 117 617 157 HOH HOH A . 
G 4 HOH 118 618 243 HOH HOH A . 
G 4 HOH 119 619 295 HOH HOH A . 
G 4 HOH 120 620 199 HOH HOH A . 
G 4 HOH 121 621 41  HOH HOH A . 
G 4 HOH 122 622 283 HOH HOH A . 
G 4 HOH 123 623 107 HOH HOH A . 
G 4 HOH 124 624 376 HOH HOH A . 
G 4 HOH 125 625 272 HOH HOH A . 
G 4 HOH 126 626 225 HOH HOH A . 
G 4 HOH 127 627 393 HOH HOH A . 
G 4 HOH 128 628 97  HOH HOH A . 
G 4 HOH 129 629 9   HOH HOH A . 
G 4 HOH 130 630 137 HOH HOH A . 
G 4 HOH 131 631 179 HOH HOH A . 
G 4 HOH 132 632 366 HOH HOH A . 
G 4 HOH 133 633 191 HOH HOH A . 
G 4 HOH 134 634 263 HOH HOH A . 
G 4 HOH 135 635 103 HOH HOH A . 
G 4 HOH 136 636 242 HOH HOH A . 
G 4 HOH 137 637 338 HOH HOH A . 
G 4 HOH 138 638 258 HOH HOH A . 
G 4 HOH 139 639 180 HOH HOH A . 
G 4 HOH 140 640 22  HOH HOH A . 
G 4 HOH 141 641 108 HOH HOH A . 
G 4 HOH 142 642 334 HOH HOH A . 
G 4 HOH 143 643 177 HOH HOH A . 
G 4 HOH 144 644 291 HOH HOH A . 
G 4 HOH 145 645 143 HOH HOH A . 
G 4 HOH 146 646 273 HOH HOH A . 
G 4 HOH 147 647 332 HOH HOH A . 
G 4 HOH 148 648 192 HOH HOH A . 
G 4 HOH 149 649 234 HOH HOH A . 
G 4 HOH 150 650 142 HOH HOH A . 
G 4 HOH 151 651 331 HOH HOH A . 
G 4 HOH 152 652 352 HOH HOH A . 
G 4 HOH 153 653 178 HOH HOH A . 
G 4 HOH 154 654 284 HOH HOH A . 
G 4 HOH 155 655 368 HOH HOH A . 
G 4 HOH 156 656 305 HOH HOH A . 
G 4 HOH 157 657 105 HOH HOH A . 
G 4 HOH 158 658 184 HOH HOH A . 
G 4 HOH 159 659 316 HOH HOH A . 
G 4 HOH 160 660 361 HOH HOH A . 
G 4 HOH 161 661 375 HOH HOH A . 
G 4 HOH 162 662 55  HOH HOH A . 
G 4 HOH 163 663 365 HOH HOH A . 
G 4 HOH 164 664 396 HOH HOH A . 
G 4 HOH 165 665 364 HOH HOH A . 
G 4 HOH 166 666 374 HOH HOH A . 
G 4 HOH 167 667 381 HOH HOH A . 
G 4 HOH 168 668 232 HOH HOH A . 
G 4 HOH 169 669 339 HOH HOH A . 
G 4 HOH 170 670 215 HOH HOH A . 
G 4 HOH 171 671 300 HOH HOH A . 
G 4 HOH 172 672 171 HOH HOH A . 
G 4 HOH 173 673 299 HOH HOH A . 
G 4 HOH 174 674 359 HOH HOH A . 
G 4 HOH 175 675 173 HOH HOH A . 
G 4 HOH 176 676 188 HOH HOH A . 
G 4 HOH 177 677 187 HOH HOH A . 
G 4 HOH 178 678 405 HOH HOH A . 
G 4 HOH 179 679 321 HOH HOH A . 
G 4 HOH 180 680 287 HOH HOH A . 
G 4 HOH 181 681 306 HOH HOH A . 
G 4 HOH 182 682 131 HOH HOH A . 
G 4 HOH 183 683 392 HOH HOH A . 
G 4 HOH 184 684 383 HOH HOH A . 
G 4 HOH 185 685 172 HOH HOH A . 
G 4 HOH 186 686 252 HOH HOH A . 
G 4 HOH 187 687 261 HOH HOH A . 
G 4 HOH 188 688 370 HOH HOH A . 
G 4 HOH 189 689 257 HOH HOH A . 
G 4 HOH 190 690 378 HOH HOH A . 
G 4 HOH 191 691 239 HOH HOH A . 
G 4 HOH 192 692 349 HOH HOH A . 
G 4 HOH 193 693 209 HOH HOH A . 
G 4 HOH 194 694 106 HOH HOH A . 
G 4 HOH 195 695 310 HOH HOH A . 
G 4 HOH 196 696 280 HOH HOH A . 
G 4 HOH 197 697 268 HOH HOH A . 
G 4 HOH 198 698 159 HOH HOH A . 
G 4 HOH 199 699 145 HOH HOH A . 
G 4 HOH 200 700 313 HOH HOH A . 
G 4 HOH 201 701 29  HOH HOH A . 
G 4 HOH 202 702 301 HOH HOH A . 
G 4 HOH 203 703 116 HOH HOH A . 
G 4 HOH 204 704 371 HOH HOH A . 
G 4 HOH 205 705 264 HOH HOH A . 
G 4 HOH 206 706 302 HOH HOH A . 
G 4 HOH 207 707 219 HOH HOH A . 
G 4 HOH 208 708 154 HOH HOH A . 
G 4 HOH 209 709 350 HOH HOH A . 
G 4 HOH 210 710 245 HOH HOH A . 
G 4 HOH 211 711 358 HOH HOH A . 
G 4 HOH 212 712 128 HOH HOH A . 
G 4 HOH 213 713 139 HOH HOH A . 
H 4 HOH 1   501 353 HOH HOH B . 
H 4 HOH 2   502 328 HOH HOH B . 
H 4 HOH 3   503 379 HOH HOH B . 
H 4 HOH 4   504 169 HOH HOH B . 
H 4 HOH 5   505 389 HOH HOH B . 
H 4 HOH 6   506 77  HOH HOH B . 
H 4 HOH 7   507 94  HOH HOH B . 
H 4 HOH 8   508 294 HOH HOH B . 
H 4 HOH 9   509 222 HOH HOH B . 
H 4 HOH 10  510 343 HOH HOH B . 
H 4 HOH 11  511 144 HOH HOH B . 
H 4 HOH 12  512 279 HOH HOH B . 
H 4 HOH 13  513 11  HOH HOH B . 
H 4 HOH 14  514 82  HOH HOH B . 
H 4 HOH 15  515 46  HOH HOH B . 
H 4 HOH 16  516 311 HOH HOH B . 
H 4 HOH 17  517 214 HOH HOH B . 
H 4 HOH 18  518 293 HOH HOH B . 
H 4 HOH 19  519 406 HOH HOH B . 
H 4 HOH 20  520 130 HOH HOH B . 
H 4 HOH 21  521 1   HOH HOH B . 
H 4 HOH 22  522 140 HOH HOH B . 
H 4 HOH 23  523 80  HOH HOH B . 
H 4 HOH 24  524 64  HOH HOH B . 
H 4 HOH 25  525 163 HOH HOH B . 
H 4 HOH 26  526 3   HOH HOH B . 
H 4 HOH 27  527 12  HOH HOH B . 
H 4 HOH 28  528 238 HOH HOH B . 
H 4 HOH 29  529 254 HOH HOH B . 
H 4 HOH 30  530 104 HOH HOH B . 
H 4 HOH 31  531 165 HOH HOH B . 
H 4 HOH 32  532 240 HOH HOH B . 
H 4 HOH 33  533 42  HOH HOH B . 
H 4 HOH 34  534 249 HOH HOH B . 
H 4 HOH 35  535 290 HOH HOH B . 
H 4 HOH 36  536 10  HOH HOH B . 
H 4 HOH 37  537 286 HOH HOH B . 
H 4 HOH 38  538 333 HOH HOH B . 
H 4 HOH 39  539 79  HOH HOH B . 
H 4 HOH 40  540 39  HOH HOH B . 
H 4 HOH 41  541 96  HOH HOH B . 
H 4 HOH 42  542 20  HOH HOH B . 
H 4 HOH 43  543 401 HOH HOH B . 
H 4 HOH 44  544 90  HOH HOH B . 
H 4 HOH 45  545 155 HOH HOH B . 
H 4 HOH 46  546 337 HOH HOH B . 
H 4 HOH 47  547 52  HOH HOH B . 
H 4 HOH 48  548 189 HOH HOH B . 
H 4 HOH 49  549 83  HOH HOH B . 
H 4 HOH 50  550 170 HOH HOH B . 
H 4 HOH 51  551 262 HOH HOH B . 
H 4 HOH 52  552 183 HOH HOH B . 
H 4 HOH 53  553 100 HOH HOH B . 
H 4 HOH 54  554 35  HOH HOH B . 
H 4 HOH 55  555 68  HOH HOH B . 
H 4 HOH 56  556 75  HOH HOH B . 
H 4 HOH 57  557 166 HOH HOH B . 
H 4 HOH 58  558 201 HOH HOH B . 
H 4 HOH 59  559 51  HOH HOH B . 
H 4 HOH 60  560 38  HOH HOH B . 
H 4 HOH 61  561 152 HOH HOH B . 
H 4 HOH 62  562 175 HOH HOH B . 
H 4 HOH 63  563 5   HOH HOH B . 
H 4 HOH 64  564 244 HOH HOH B . 
H 4 HOH 65  565 153 HOH HOH B . 
H 4 HOH 66  566 8   HOH HOH B . 
H 4 HOH 67  567 227 HOH HOH B . 
H 4 HOH 68  568 327 HOH HOH B . 
H 4 HOH 69  569 66  HOH HOH B . 
H 4 HOH 70  570 87  HOH HOH B . 
H 4 HOH 71  571 36  HOH HOH B . 
H 4 HOH 72  572 309 HOH HOH B . 
H 4 HOH 73  573 63  HOH HOH B . 
H 4 HOH 74  574 17  HOH HOH B . 
H 4 HOH 75  575 195 HOH HOH B . 
H 4 HOH 76  576 278 HOH HOH B . 
H 4 HOH 77  577 112 HOH HOH B . 
H 4 HOH 78  578 50  HOH HOH B . 
H 4 HOH 79  579 44  HOH HOH B . 
H 4 HOH 80  580 56  HOH HOH B . 
H 4 HOH 81  581 126 HOH HOH B . 
H 4 HOH 82  582 133 HOH HOH B . 
H 4 HOH 83  583 224 HOH HOH B . 
H 4 HOH 84  584 84  HOH HOH B . 
H 4 HOH 85  585 120 HOH HOH B . 
H 4 HOH 86  586 93  HOH HOH B . 
H 4 HOH 87  587 47  HOH HOH B . 
H 4 HOH 88  588 92  HOH HOH B . 
H 4 HOH 89  589 48  HOH HOH B . 
H 4 HOH 90  590 24  HOH HOH B . 
H 4 HOH 91  591 27  HOH HOH B . 
H 4 HOH 92  592 296 HOH HOH B . 
H 4 HOH 93  593 399 HOH HOH B . 
H 4 HOH 94  594 81  HOH HOH B . 
H 4 HOH 95  595 45  HOH HOH B . 
H 4 HOH 96  596 150 HOH HOH B . 
H 4 HOH 97  597 186 HOH HOH B . 
H 4 HOH 98  598 19  HOH HOH B . 
H 4 HOH 99  599 123 HOH HOH B . 
H 4 HOH 100 600 125 HOH HOH B . 
H 4 HOH 101 601 114 HOH HOH B . 
H 4 HOH 102 602 390 HOH HOH B . 
H 4 HOH 103 603 347 HOH HOH B . 
H 4 HOH 104 604 113 HOH HOH B . 
H 4 HOH 105 605 317 HOH HOH B . 
H 4 HOH 106 606 369 HOH HOH B . 
H 4 HOH 107 607 43  HOH HOH B . 
H 4 HOH 108 608 86  HOH HOH B . 
H 4 HOH 109 609 354 HOH HOH B . 
H 4 HOH 110 610 16  HOH HOH B . 
H 4 HOH 111 611 247 HOH HOH B . 
H 4 HOH 112 612 216 HOH HOH B . 
H 4 HOH 113 613 388 HOH HOH B . 
H 4 HOH 114 614 54  HOH HOH B . 
H 4 HOH 115 615 319 HOH HOH B . 
H 4 HOH 116 616 265 HOH HOH B . 
H 4 HOH 117 617 102 HOH HOH B . 
H 4 HOH 118 618 213 HOH HOH B . 
H 4 HOH 119 619 402 HOH HOH B . 
H 4 HOH 120 620 167 HOH HOH B . 
H 4 HOH 121 621 161 HOH HOH B . 
H 4 HOH 122 622 181 HOH HOH B . 
H 4 HOH 123 623 168 HOH HOH B . 
H 4 HOH 124 624 400 HOH HOH B . 
H 4 HOH 125 625 329 HOH HOH B . 
H 4 HOH 126 626 89  HOH HOH B . 
H 4 HOH 127 627 345 HOH HOH B . 
H 4 HOH 128 628 274 HOH HOH B . 
H 4 HOH 129 629 260 HOH HOH B . 
H 4 HOH 130 630 71  HOH HOH B . 
H 4 HOH 131 631 76  HOH HOH B . 
H 4 HOH 132 632 205 HOH HOH B . 
H 4 HOH 133 633 115 HOH HOH B . 
H 4 HOH 134 634 372 HOH HOH B . 
H 4 HOH 135 635 74  HOH HOH B . 
H 4 HOH 136 636 288 HOH HOH B . 
H 4 HOH 137 637 285 HOH HOH B . 
H 4 HOH 138 638 308 HOH HOH B . 
H 4 HOH 139 639 377 HOH HOH B . 
H 4 HOH 140 640 312 HOH HOH B . 
H 4 HOH 141 641 253 HOH HOH B . 
H 4 HOH 142 642 373 HOH HOH B . 
H 4 HOH 143 643 185 HOH HOH B . 
H 4 HOH 144 644 362 HOH HOH B . 
H 4 HOH 145 645 351 HOH HOH B . 
H 4 HOH 146 646 395 HOH HOH B . 
H 4 HOH 147 647 292 HOH HOH B . 
H 4 HOH 148 648 340 HOH HOH B . 
H 4 HOH 149 649 194 HOH HOH B . 
H 4 HOH 150 650 246 HOH HOH B . 
H 4 HOH 151 651 356 HOH HOH B . 
H 4 HOH 152 652 382 HOH HOH B . 
H 4 HOH 153 653 200 HOH HOH B . 
H 4 HOH 154 654 203 HOH HOH B . 
H 4 HOH 155 655 341 HOH HOH B . 
H 4 HOH 156 656 255 HOH HOH B . 
H 4 HOH 157 657 348 HOH HOH B . 
H 4 HOH 158 658 138 HOH HOH B . 
H 4 HOH 159 659 241 HOH HOH B . 
H 4 HOH 160 660 386 HOH HOH B . 
H 4 HOH 161 661 355 HOH HOH B . 
H 4 HOH 162 662 267 HOH HOH B . 
H 4 HOH 163 663 344 HOH HOH B . 
H 4 HOH 164 664 270 HOH HOH B . 
H 4 HOH 165 665 277 HOH HOH B . 
H 4 HOH 166 666 211 HOH HOH B . 
H 4 HOH 167 667 210 HOH HOH B . 
H 4 HOH 168 668 156 HOH HOH B . 
H 4 HOH 169 669 196 HOH HOH B . 
H 4 HOH 170 670 367 HOH HOH B . 
H 4 HOH 171 671 164 HOH HOH B . 
H 4 HOH 172 672 391 HOH HOH B . 
H 4 HOH 173 673 335 HOH HOH B . 
H 4 HOH 174 674 394 HOH HOH B . 
H 4 HOH 175 675 297 HOH HOH B . 
# 
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                   97.16 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JMA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.362 
_cell.length_a_esd                 ? 
_cell.length_b                     95.144 
_cell.length_b_esd                 ? 
_cell.length_c                     70.484 
_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                         9JMA 
_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                   9JMA 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.97 
_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              7.0 
_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 
# 
_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 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-02 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JMA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               42.09 
_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                                     32146 
_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                           99.74 
_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                          5.07 
_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                                   0.955 
_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                                    2.2 
_reflns_shell.d_res_low                                     2.279 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.01 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3202 
_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                                  0.823 
_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                                 9JMA 
_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                            2.20 
_refine.ls_d_res_low                             42.09 
_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                     32146 
_refine.ls_number_reflns_R_free                  1594 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1976 
_refine.ls_R_factor_R_free                       0.2446 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1950 
_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                          1.38 
_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                      ? 
_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                 28.21 
_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                            0.28 
_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                       2.20 
_refine_hist.d_res_low                        42.09 
_refine_hist.number_atoms_solvent             391 
_refine_hist.number_atoms_total               5243 
_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        4800 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_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' ? 0.008 ? 4966 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.910 ? 6790 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.653 ? 700  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052 ? 766  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 896  ? 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' 2.20 2.27  . . 155 2759 100.00 . . . . 0.2625 . . . . . . . . . . . 0.3531 
'X-RAY DIFFRACTION' 2.27 2.35  . . 146 2732 100.00 . . . . 0.2362 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 2.35 2.45  . . 152 2764 100.00 . . . . 0.2208 . . . . . . . . . . . 0.3396 
'X-RAY DIFFRACTION' 2.45 2.56  . . 139 2781 100.00 . . . . 0.2223 . . . . . . . . . . . 0.3031 
'X-RAY DIFFRACTION' 2.56 2.69  . . 128 2788 100.00 . . . . 0.2102 . . . . . . . . . . . 0.3377 
'X-RAY DIFFRACTION' 2.69 2.86  . . 151 2763 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 2.86 3.08  . . 145 2762 100.00 . . . . 0.1864 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 3.08 3.39  . . 149 2789 100.00 . . . . 0.1800 . . . . . . . . . . . 0.2257 
'X-RAY DIFFRACTION' 3.39 3.88  . . 150 2765 100.00 . . . . 0.1828 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 3.88 4.89  . . 146 2805 100.00 . . . . 0.1666 . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 4.89 42.09 . . 133 2844 100.00 . . . . 0.1847 . . . . . . . . . . . 0.1867 
# 
_struct.entry_id                     9JMA 
_struct.title                        'Crystal structure of glycosyltransferase AvpGT' 
_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        9JMA 
_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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 9JMA A 1 ? 306 ? A0A1D2IE05 1 ? 306 ? 1 306 
2 1 9JMA 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,G 
2 1 B,E,F,H 
# 
_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 109 ? THR A 102 GLY A 109 1 ? 8  
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 250 ? THR A 242 ARG A 250 1 ? 9  
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 ? GLY A 305 ? SER A 291 GLY A 305 1 ? 15 
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  ? ARG B 54  ? VAL B 45  ARG B 54  1 ? 10 
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 GLU B 177 ? HIS B 188 ? GLU B 177 HIS B 188 1 ? 12 
HELX_P HELX_P25 AC7 GLY B 209 ? THR B 214 ? GLY B 209 THR B 214 5 ? 6  
HELX_P HELX_P26 AC8 SER B 218 ? TRP B 238 ? SER B 218 TRP B 238 1 ? 21 
HELX_P HELX_P27 AC9 THR B 242 ? ARG B 249 ? THR B 242 ARG B 249 1 ? 8  
HELX_P HELX_P28 AD1 ARG B 250 ? ALA B 265 ? ARG B 250 ALA B 265 1 ? 16 
HELX_P HELX_P29 AD2 HIS B 272 ? ALA B 284 ? HIS B 272 ALA B 284 1 ? 13 
HELX_P HELX_P30 AD3 SER B 291 ? GLU B 304 ? SER B 291 GLU B 304 1 ? 14 
# 
_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 D MG  . MG ? ? A ASP 91  A MG  402 1_555 ? ? ? ? ? ? ? 2.628 ? ? 
metalc2  metalc ? ? A ASP 91 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 91  A MG  402 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc3  metalc ? ? C UDP .  O2A ? ? ? 1_555 D MG  . MG ? ? A UDP 401 A MG  402 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc4  metalc ? ? C UDP .  O3B ? ? ? 1_555 D MG  . MG ? ? A UDP 401 A MG  402 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc5  metalc ? ? D MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  402 A HOH 540 1_555 ? ? ? ? ? ? ? 2.549 ? ? 
metalc6  metalc ? ? D MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  402 A HOH 629 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc7  metalc ? ? B ASP 91 OD1 ? ? ? 1_555 F MG  . MG ? ? B ASP 91  B MG  402 1_555 ? ? ? ? ? ? ? 2.678 ? ? 
metalc8  metalc ? ? B ASP 91 OD2 ? ? ? 1_555 F MG  . MG ? ? B ASP 91  B MG  402 1_555 ? ? ? ? ? ? ? 2.187 ? ? 
metalc9  metalc ? ? E UDP .  O1A ? ? ? 1_555 F MG  . MG ? ? B UDP 401 B MG  402 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc10 metalc ? ? E UDP .  O1B ? ? ? 1_555 F MG  . MG ? ? B UDP 401 B MG  402 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc11 metalc ? ? F MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? B MG  402 B HOH 533 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc12 metalc ? ? F MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? B MG  402 B HOH 574 1_555 ? ? ? ? ? ? ? 2.411 ? ? 
metalc13 metalc ? ? F MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? B MG  402 B HOH 608 1_555 ? ? ? ? ? ? ? 2.748 ? ? 
# 
_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 ? D MG . ? A MG 402 ? 1_555 OD2 ? A ASP 91 ? A ASP 91  ? 1_555 52.1  ? 
2  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O2A ? C UDP .  ? A UDP 401 ? 1_555 91.8  ? 
3  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O2A ? C UDP .  ? A UDP 401 ? 1_555 89.0  ? 
4  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O3B ? C UDP .  ? A UDP 401 ? 1_555 155.6 ? 
5  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O3B ? C UDP .  ? A UDP 401 ? 1_555 150.5 ? 
6  O2A ? C UDP .  ? A UDP 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O3B ? C UDP .  ? A UDP 401 ? 1_555 82.1  ? 
7  OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 540 ? 1_555 84.4  ? 
8  OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 540 ? 1_555 135.7 ? 
9  O2A ? C UDP .  ? A UDP 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 540 ? 1_555 101.5 ? 
10 O3B ? C UDP .  ? A UDP 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 540 ? 1_555 73.8  ? 
11 OD1 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 629 ? 1_555 89.8  ? 
12 OD2 ? A ASP 91 ? A ASP 91  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 629 ? 1_555 89.3  ? 
13 O2A ? C UDP .  ? A UDP 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 629 ? 1_555 176.2 ? 
14 O3B ? C UDP .  ? A UDP 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 629 ? 1_555 97.9  ? 
15 O   ? G HOH .  ? A HOH 540 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .  ? A HOH 629 ? 1_555 82.1  ? 
16 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 52.3  ? 
17 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O1A ? E UDP .  ? B UDP 401 ? 1_555 85.8  ? 
18 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O1A ? E UDP .  ? B UDP 401 ? 1_555 87.0  ? 
19 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O1B ? E UDP .  ? B UDP 401 ? 1_555 154.4 ? 
20 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O1B ? E UDP .  ? B UDP 401 ? 1_555 147.8 ? 
21 O1A ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O1B ? E UDP .  ? B UDP 401 ? 1_555 81.4  ? 
22 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 533 ? 1_555 79.1  ? 
23 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 533 ? 1_555 129.9 ? 
24 O1A ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 533 ? 1_555 102.8 ? 
25 O1B ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 533 ? 1_555 82.2  ? 
26 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 574 ? 1_555 87.0  ? 
27 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 574 ? 1_555 81.4  ? 
28 O1A ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 574 ? 1_555 168.4 ? 
29 O1B ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 574 ? 1_555 108.6 ? 
30 O   ? H HOH .  ? B HOH 533 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 574 ? 1_555 84.7  ? 
31 OD1 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 133.0 ? 
32 OD2 ? B ASP 91 ? B ASP 91  ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 81.1  ? 
33 O1A ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 86.0  ? 
34 O1B ? E UDP .  ? B UDP 401 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 68.2  ? 
35 O   ? H HOH .  ? B HOH 533 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 147.6 ? 
36 O   ? H HOH .  ? B HOH 574 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? H HOH .  ? B HOH 608 ? 1_555 92.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 7 ? 
AA3 ? 8 ? 
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 ? parallel      
AA1 7 8 ? 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 ? anti-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 ? parallel      
AA3 7 8 ? 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 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 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 194 ? HIS A 205 ? VAL A 194 HIS A 205 
AA1 8 ASP A 92  ? VAL A 93  ? ASP A 92  VAL A 93  
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 134 ? LEU A 138 ? VAL A 134 LEU A 138 
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 ? ALA B 120 ? PHE B 112 ALA B 120 
AA3 7 VAL B 194 ? HIS B 205 ? VAL B 194 HIS B 205 
AA3 8 ASP B 92  ? VAL B 93  ? ASP B 92  VAL B 93  
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 ? ALA B 120 ? PHE B 112 ALA B 120 
AA4 7 VAL B 134 ? LEU B 138 ? VAL B 134 LEU B 138 
# 
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 ILE A 61  ? O ILE A 61  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 ASN A 118 ? N ASN A 118 O LEU A 204 ? O LEU A 204 
AA1 7 8 O ALA A 203 ? O ALA A 203 N VAL A 93  ? N VAL A 93  
AA2 1 2 O ILE A 61  ? O ILE A 61  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 ILE A 117 ? N ILE A 117 O LEU A 138 ? O LEU A 138 
AA3 1 2 O ILE B 61  ? O ILE B 61  N VAL B 37  ? N VAL B 37  
AA3 2 3 O ILE B 36  ? O ILE B 36  N VAL B 5   ? N VAL B 5   
AA3 3 4 N SER B 4   ? N SER B 4   O ALA B 86  ? O ALA B 86  
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 ASN B 118 ? N ASN B 118 O LEU B 204 ? O LEU B 204 
AA3 7 8 O ALA B 203 ? O ALA B 203 N VAL B 93  ? N VAL B 93  
AA4 1 2 O ILE B 61  ? O ILE B 61  N VAL B 37  ? N VAL B 37  
AA4 2 3 O ILE B 36  ? O ILE B 36  N VAL B 5   ? N VAL B 5   
AA4 3 4 N SER B 4   ? N SER B 4   O ALA B 86  ? O ALA B 86  
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 ILE B 117 ? N ILE B 117 O LEU B 138 ? O LEU B 138 
# 
_pdbx_entry_details.entry_id                   9JMA 
_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 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              14 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              14 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              14 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.61 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            12.21 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 40  ? ? -83.30  48.97   
2  1 TYR A 142 ? ? -102.57 42.19   
3  1 SER A 162 ? ? -29.13  109.93  
4  1 THR A 214 ? ? -97.00  -135.56 
5  1 ASP A 287 ? ? 45.53   -124.02 
6  1 ASP B 40  ? ? -82.91  48.83   
7  1 GLU B 139 ? ? -146.83 35.21   
8  1 PRO B 141 ? ? -59.18  171.77  
9  1 SER B 162 ? ? -39.50  117.54  
10 1 GLU B 177 ? ? 59.46   15.96   
11 1 THR B 217 ? ? -87.43  -149.88 
12 1 ASP B 287 ? ? 49.29   -144.30 
13 1 GLU B 304 ? ? -74.31  -93.34  
# 
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 
SER N      N  N N 291 
SER CA     C  N S 292 
SER C      C  N N 293 
SER O      O  N N 294 
SER CB     C  N N 295 
SER OG     O  N N 296 
SER OXT    O  N N 297 
SER H      H  N N 298 
SER H2     H  N N 299 
SER HA     H  N N 300 
SER HB2    H  N N 301 
SER HB3    H  N N 302 
SER HG     H  N N 303 
SER HXT    H  N N 304 
THR N      N  N N 305 
THR CA     C  N S 306 
THR C      C  N N 307 
THR O      O  N N 308 
THR CB     C  N R 309 
THR OG1    O  N N 310 
THR CG2    C  N N 311 
THR OXT    O  N N 312 
THR H      H  N N 313 
THR H2     H  N N 314 
THR HA     H  N N 315 
THR HB     H  N N 316 
THR HG1    H  N N 317 
THR HG21   H  N N 318 
THR HG22   H  N N 319 
THR HG23   H  N N 320 
THR HXT    H  N N 321 
TRP N      N  N N 322 
TRP CA     C  N S 323 
TRP C      C  N N 324 
TRP O      O  N N 325 
TRP CB     C  N N 326 
TRP CG     C  Y N 327 
TRP CD1    C  Y N 328 
TRP CD2    C  Y N 329 
TRP NE1    N  Y N 330 
TRP CE2    C  Y N 331 
TRP CE3    C  Y N 332 
TRP CZ2    C  Y N 333 
TRP CZ3    C  Y N 334 
TRP CH2    C  Y N 335 
TRP OXT    O  N N 336 
TRP H      H  N N 337 
TRP H2     H  N N 338 
TRP HA     H  N N 339 
TRP HB2    H  N N 340 
TRP HB3    H  N N 341 
TRP HD1    H  N N 342 
TRP HE1    H  N N 343 
TRP HE3    H  N N 344 
TRP HZ2    H  N N 345 
TRP HZ3    H  N N 346 
TRP HH2    H  N N 347 
TRP HXT    H  N N 348 
TYR N      N  N N 349 
TYR CA     C  N S 350 
TYR C      C  N N 351 
TYR O      O  N N 352 
TYR CB     C  N N 353 
TYR CG     C  Y N 354 
TYR CD1    C  Y N 355 
TYR CD2    C  Y N 356 
TYR CE1    C  Y N 357 
TYR CE2    C  Y N 358 
TYR CZ     C  Y N 359 
TYR OH     O  N N 360 
TYR OXT    O  N N 361 
TYR H      H  N N 362 
TYR H2     H  N N 363 
TYR HA     H  N N 364 
TYR HB2    H  N N 365 
TYR HB3    H  N N 366 
TYR HD1    H  N N 367 
TYR HD2    H  N N 368 
TYR HE1    H  N N 369 
TYR HE2    H  N N 370 
TYR HH     H  N N 371 
TYR HXT    H  N N 372 
UDP N1     N  N N 373 
UDP C2     C  N N 374 
UDP N3     N  N N 375 
UDP C4     C  N N 376 
UDP C5     C  N N 377 
UDP C6     C  N N 378 
UDP O2     O  N N 379 
UDP O4     O  N N 380 
UDP "C1'"  C  N R 381 
UDP "C2'"  C  N R 382 
UDP "O2'"  O  N N 383 
UDP "C3'"  C  N S 384 
UDP "C4'"  C  N R 385 
UDP "O4'"  O  N N 386 
UDP "O3'"  O  N N 387 
UDP "C5'"  C  N N 388 
UDP "O5'"  O  N N 389 
UDP PA     P  N N 390 
UDP O1A    O  N N 391 
UDP O2A    O  N N 392 
UDP O3A    O  N N 393 
UDP PB     P  N N 394 
UDP O1B    O  N N 395 
UDP O2B    O  N N 396 
UDP O3B    O  N N 397 
UDP HN3    H  N N 398 
UDP H5     H  N N 399 
UDP H6     H  N N 400 
UDP "H1'"  H  N N 401 
UDP "H2'"  H  N N 402 
UDP "HO2'" H  N N 403 
UDP "H3'"  H  N N 404 
UDP "H4'"  H  N N 405 
UDP "HO3'" H  N N 406 
UDP "H5'1" H  N N 407 
UDP "H5'2" H  N N 408 
UDP HOA2   H  N N 409 
UDP HOB2   H  N N 410 
UDP HOB3   H  N N 411 
VAL N      N  N N 412 
VAL CA     C  N S 413 
VAL C      C  N N 414 
VAL O      O  N N 415 
VAL CB     C  N N 416 
VAL CG1    C  N N 417 
VAL CG2    C  N N 418 
VAL OXT    O  N N 419 
VAL H      H  N N 420 
VAL H2     H  N N 421 
VAL HA     H  N N 422 
VAL HB     H  N N 423 
VAL HG11   H  N N 424 
VAL HG12   H  N N 425 
VAL HG13   H  N N 426 
VAL HG21   H  N N 427 
VAL HG22   H  N N 428 
VAL HG23   H  N N 429 
VAL HXT    H  N N 430 
# 
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 
SER N     CA     sing N N 277 
SER N     H      sing N N 278 
SER N     H2     sing N N 279 
SER CA    C      sing N N 280 
SER CA    CB     sing N N 281 
SER CA    HA     sing N N 282 
SER C     O      doub N N 283 
SER C     OXT    sing N N 284 
SER CB    OG     sing N N 285 
SER CB    HB2    sing N N 286 
SER CB    HB3    sing N N 287 
SER OG    HG     sing N N 288 
SER OXT   HXT    sing N N 289 
THR N     CA     sing N N 290 
THR N     H      sing N N 291 
THR N     H2     sing N N 292 
THR CA    C      sing N N 293 
THR CA    CB     sing N N 294 
THR CA    HA     sing N N 295 
THR C     O      doub N N 296 
THR C     OXT    sing N N 297 
THR CB    OG1    sing N N 298 
THR CB    CG2    sing N N 299 
THR CB    HB     sing N N 300 
THR OG1   HG1    sing N N 301 
THR CG2   HG21   sing N N 302 
THR CG2   HG22   sing N N 303 
THR CG2   HG23   sing N N 304 
THR OXT   HXT    sing N N 305 
TRP N     CA     sing N N 306 
TRP N     H      sing N N 307 
TRP N     H2     sing N N 308 
TRP CA    C      sing N N 309 
TRP CA    CB     sing N N 310 
TRP CA    HA     sing N N 311 
TRP C     O      doub N N 312 
TRP C     OXT    sing N N 313 
TRP CB    CG     sing N N 314 
TRP CB    HB2    sing N N 315 
TRP CB    HB3    sing N N 316 
TRP CG    CD1    doub Y N 317 
TRP CG    CD2    sing Y N 318 
TRP CD1   NE1    sing Y N 319 
TRP CD1   HD1    sing N N 320 
TRP CD2   CE2    doub Y N 321 
TRP CD2   CE3    sing Y N 322 
TRP NE1   CE2    sing Y N 323 
TRP NE1   HE1    sing N N 324 
TRP CE2   CZ2    sing Y N 325 
TRP CE3   CZ3    doub Y N 326 
TRP CE3   HE3    sing N N 327 
TRP CZ2   CH2    doub Y N 328 
TRP CZ2   HZ2    sing N N 329 
TRP CZ3   CH2    sing Y N 330 
TRP CZ3   HZ3    sing N N 331 
TRP CH2   HH2    sing N N 332 
TRP OXT   HXT    sing N N 333 
TYR N     CA     sing N N 334 
TYR N     H      sing N N 335 
TYR N     H2     sing N N 336 
TYR CA    C      sing N N 337 
TYR CA    CB     sing N N 338 
TYR CA    HA     sing N N 339 
TYR C     O      doub N N 340 
TYR C     OXT    sing N N 341 
TYR CB    CG     sing N N 342 
TYR CB    HB2    sing N N 343 
TYR CB    HB3    sing N N 344 
TYR CG    CD1    doub Y N 345 
TYR CG    CD2    sing Y N 346 
TYR CD1   CE1    sing Y N 347 
TYR CD1   HD1    sing N N 348 
TYR CD2   CE2    doub Y N 349 
TYR CD2   HD2    sing N N 350 
TYR CE1   CZ     doub Y N 351 
TYR CE1   HE1    sing N N 352 
TYR CE2   CZ     sing Y N 353 
TYR CE2   HE2    sing N N 354 
TYR CZ    OH     sing N N 355 
TYR OH    HH     sing N N 356 
TYR OXT   HXT    sing N N 357 
UDP N1    C2     sing N N 358 
UDP N1    C6     sing N N 359 
UDP N1    "C1'"  sing N N 360 
UDP C2    N3     sing N N 361 
UDP C2    O2     doub N N 362 
UDP N3    C4     sing N N 363 
UDP N3    HN3    sing N N 364 
UDP C4    C5     sing N N 365 
UDP C4    O4     doub N N 366 
UDP C5    C6     doub N N 367 
UDP C5    H5     sing N N 368 
UDP C6    H6     sing N N 369 
UDP "C1'" "C2'"  sing N N 370 
UDP "C1'" "O4'"  sing N N 371 
UDP "C1'" "H1'"  sing N N 372 
UDP "C2'" "O2'"  sing N N 373 
UDP "C2'" "C3'"  sing N N 374 
UDP "C2'" "H2'"  sing N N 375 
UDP "O2'" "HO2'" sing N N 376 
UDP "C3'" "C4'"  sing N N 377 
UDP "C3'" "O3'"  sing N N 378 
UDP "C3'" "H3'"  sing N N 379 
UDP "C4'" "O4'"  sing N N 380 
UDP "C4'" "C5'"  sing N N 381 
UDP "C4'" "H4'"  sing N N 382 
UDP "O3'" "HO3'" sing N N 383 
UDP "C5'" "O5'"  sing N N 384 
UDP "C5'" "H5'1" sing N N 385 
UDP "C5'" "H5'2" sing N N 386 
UDP "O5'" PA     sing N N 387 
UDP PA    O1A    doub N N 388 
UDP PA    O2A    sing N N 389 
UDP PA    O3A    sing N N 390 
UDP O2A   HOA2   sing N N 391 
UDP O3A   PB     sing N N 392 
UDP PB    O1B    doub N N 393 
UDP PB    O2B    sing N N 394 
UDP PB    O3B    sing N N 395 
UDP O2B   HOB2   sing N N 396 
UDP O3B   HOB3   sing N N 397 
VAL N     CA     sing N N 398 
VAL N     H      sing N N 399 
VAL N     H2     sing N N 400 
VAL CA    C      sing N N 401 
VAL CA    CB     sing N N 402 
VAL CA    HA     sing N N 403 
VAL C     O      doub N N 404 
VAL C     OXT    sing N N 405 
VAL CB    CG1    sing N N 406 
VAL CB    CG2    sing N N 407 
VAL CB    HB     sing N N 408 
VAL CG1   HG11   sing N N 409 
VAL CG1   HG12   sing N N 410 
VAL CG1   HG13   sing N N 411 
VAL CG2   HG21   sing N N 412 
VAL CG2   HG22   sing N N 413 
VAL CG2   HG23   sing N N 414 
VAL OXT   HXT    sing N N 415 
# 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JMA 
_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]   0.020677 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002596 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010510 
_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]   0.014299 
_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   ? 18.039  17.373  25.907  1.00 29.65  ?  1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 17.216  16.744  26.914  1.00 22.12  ?  1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 16.130  15.904  26.263  1.00 17.83  ?  1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 15.843  14.819  26.751  1.00 22.56  ?  1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 16.602  17.785  27.860  1.00 21.45  ?  1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 16.756  17.389  29.313  1.00 36.54  ?  1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 16.120  18.569  30.509  1.00 66.08  ?  1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 17.654  19.081  31.296  1.00 35.07  ?  1   MET A CE    1 
ATOM   9    N  N     . LEU A 1 2   ? 15.537  16.381  25.162  1.00 13.10  ?  2   LEU A N     1 
ATOM   10   C  CA    . LEU A 1 2   ? 14.491  15.600  24.503  1.00 13.89  ?  2   LEU A CA    1 
ATOM   11   C  C     . LEU A 1 2   ? 15.064  14.479  23.625  1.00 17.35  ?  2   LEU A C     1 
ATOM   12   O  O     . LEU A 1 2   ? 14.673  13.317  23.771  1.00 16.68  ?  2   LEU A O     1 
ATOM   13   C  CB    . LEU A 1 2   ? 13.580  16.513  23.687  1.00 13.56  ?  2   LEU A CB    1 
ATOM   14   C  CG    . LEU A 1 2   ? 12.335  15.805  23.133  1.00 19.91  ?  2   LEU A CG    1 
ATOM   15   C  CD1   . LEU A 1 2   ? 11.507  15.160  24.260  1.00 18.65  ?  2   LEU A CD1   1 
ATOM   16   C  CD2   . LEU A 1 2   ? 11.456  16.748  22.302  1.00 15.98  ?  2   LEU A CD2   1 
ATOM   17   N  N     . VAL A 1 3   ? 15.990  14.792  22.715  1.00 12.80  ?  3   VAL A N     1 
ATOM   18   C  CA    . VAL A 1 3   ? 16.518  13.807  21.776  1.00 16.51  ?  3   VAL A CA    1 
ATOM   19   C  C     . VAL A 1 3   ? 18.040  13.856  21.747  1.00 17.48  ?  3   VAL A C     1 
ATOM   20   O  O     . VAL A 1 3   ? 18.635  14.932  21.614  1.00 16.87  ?  3   VAL A O     1 
ATOM   21   C  CB    . VAL A 1 3   ? 15.976  14.005  20.348  1.00 15.49  ?  3   VAL A CB    1 
ATOM   22   C  CG1   . VAL A 1 3   ? 16.499  12.917  19.471  1.00 16.96  ?  3   VAL A CG1   1 
ATOM   23   C  CG2   . VAL A 1 3   ? 14.459  13.952  20.340  1.00 19.29  ?  3   VAL A CG2   1 
ATOM   24   N  N     . SER A 1 4   ? 18.663  12.680  21.811  1.00 16.44  ?  4   SER A N     1 
ATOM   25   C  CA    . SER A 1 4   ? 20.078  12.496  21.515  1.00 18.51  ?  4   SER A CA    1 
ATOM   26   C  C     . SER A 1 4   ? 20.210  11.694  20.231  1.00 16.99  ?  4   SER A C     1 
ATOM   27   O  O     . SER A 1 4   ? 19.563  10.655  20.076  1.00 18.92  ?  4   SER A O     1 
ATOM   28   C  CB    . SER A 1 4   ? 20.802  11.757  22.646  1.00 18.71  ?  4   SER A CB    1 
ATOM   29   O  OG    . SER A 1 4   ? 20.722  12.460  23.872  1.00 19.20  ?  4   SER A OG    1 
ATOM   30   N  N     . VAL A 1 5   ? 21.052  12.154  19.323  1.00 15.10  ?  5   VAL A N     1 
ATOM   31   C  CA    . VAL A 1 5   ? 21.368  11.392  18.123  1.00 15.58  ?  5   VAL A CA    1 
ATOM   32   C  C     . VAL A 1 5   ? 22.724  10.740  18.325  1.00 16.89  ?  5   VAL A C     1 
ATOM   33   O  O     . VAL A 1 5   ? 23.669  11.390  18.800  1.00 16.28  ?  5   VAL A O     1 
ATOM   34   C  CB    . VAL A 1 5   ? 21.347  12.280  16.872  1.00 17.03  ?  5   VAL A CB    1 
ATOM   35   C  CG1   . VAL A 1 5   ? 21.760  11.484  15.619  1.00 12.92  ?  5   VAL A CG1   1 
ATOM   36   C  CG2   . VAL A 1 5   ? 19.967  12.866  16.708  1.00 16.25  ?  5   VAL A CG2   1 
ATOM   37   N  N     . ILE A 1 6   ? 22.814  9.447   18.007  1.00 12.92  ?  6   ILE A N     1 
ATOM   38   C  CA    . ILE A 1 6   ? 24.026  8.664   18.224  1.00 11.85  ?  6   ILE A CA    1 
ATOM   39   C  C     . ILE A 1 6   ? 24.556  8.230   16.859  1.00 14.93  ?  6   ILE A C     1 
ATOM   40   O  O     . ILE A 1 6   ? 23.937  7.396   16.176  1.00 12.45  ?  6   ILE A O     1 
ATOM   41   C  CB    . ILE A 1 6   ? 23.773  7.450   19.122  1.00 15.03  ?  6   ILE A CB    1 
ATOM   42   C  CG1   . ILE A 1 6   ? 23.163  7.886   20.456  1.00 17.35  ?  6   ILE A CG1   1 
ATOM   43   C  CG2   . ILE A 1 6   ? 25.063  6.690   19.352  1.00 17.79  ?  6   ILE A CG2   1 
ATOM   44   C  CD1   . ILE A 1 6   ? 23.437  6.912   21.571  1.00 16.81  ?  6   ILE A CD1   1 
ATOM   45   N  N     . ILE A 1 7   ? 25.702  8.767   16.482  1.00 14.84  ?  7   ILE A N     1 
ATOM   46   C  CA    . ILE A 1 7   ? 26.347  8.457   15.205  1.00 10.43  ?  7   ILE A CA    1 
ATOM   47   C  C     . ILE A 1 7   ? 27.666  7.774   15.497  1.00 13.41  ?  7   ILE A C     1 
ATOM   48   O  O     . ILE A 1 7   ? 28.644  8.423   15.880  1.00 11.97  ?  7   ILE A O     1 
ATOM   49   C  CB    . ILE A 1 7   ? 26.552  9.727   14.367  1.00 11.89  ?  7   ILE A CB    1 
ATOM   50   C  CG1   . ILE A 1 7   ? 25.214  10.453  14.182  1.00 9.58   ?  7   ILE A CG1   1 
ATOM   51   C  CG2   . ILE A 1 7   ? 27.178  9.372   12.993  1.00 8.88   ?  7   ILE A CG2   1 
ATOM   52   C  CD1   . ILE A 1 7   ? 25.346  11.795  13.551  1.00 10.40  ?  7   ILE A CD1   1 
ATOM   53   N  N     . PRO A 1 8   ? 27.736  6.445   15.362  1.00 9.84   ?  8   PRO A N     1 
ATOM   54   C  CA    . PRO A 1 8   ? 29.034  5.775   15.345  1.00 18.85  ?  8   PRO A CA    1 
ATOM   55   C  C     . PRO A 1 8   ? 29.665  5.874   13.956  1.00 14.36  ?  8   PRO A C     1 
ATOM   56   O  O     . PRO A 1 8   ? 28.989  5.769   12.926  1.00 13.31  ?  8   PRO A O     1 
ATOM   57   C  CB    . PRO A 1 8   ? 28.684  4.325   15.720  1.00 13.34  ?  8   PRO A CB    1 
ATOM   58   C  CG    . PRO A 1 8   ? 27.313  4.121   15.157  1.00 15.77  ?  8   PRO A CG    1 
ATOM   59   C  CD    . PRO A 1 8   ? 26.629  5.493   15.137  1.00 12.62  ?  8   PRO A CD    1 
ATOM   60   N  N     . THR A 1 9   ? 30.977  6.073   13.923  1.00 14.01  ?  9   THR A N     1 
ATOM   61   C  CA    . THR A 1 9   ? 31.617  6.320   12.636  1.00 19.17  ?  9   THR A CA    1 
ATOM   62   C  C     . THR A 1 9   ? 32.999  5.684   12.619  1.00 20.08  ?  9   THR A C     1 
ATOM   63   O  O     . THR A 1 9   ? 33.701  5.685   13.633  1.00 24.42  ?  9   THR A O     1 
ATOM   64   C  CB    . THR A 1 9   ? 31.675  7.836   12.344  1.00 16.62  ?  9   THR A CB    1 
ATOM   65   O  OG1   . THR A 1 9   ? 32.205  8.076   11.031  1.00 21.35  ?  9   THR A OG1   1 
ATOM   66   C  CG2   . THR A 1 9   ? 32.514  8.570   13.394  1.00 16.66  ?  9   THR A CG2   1 
ATOM   67   N  N     . TYR A 1 10  ? 33.379  5.125   11.472  1.00 16.08  ?  10  TYR A N     1 
ATOM   68   C  CA    . TYR A 1 10  ? 34.642  4.386   11.363  1.00 24.69  ?  10  TYR A CA    1 
ATOM   69   C  C     . TYR A 1 10  ? 35.206  4.565   9.955   1.00 18.05  ?  10  TYR A C     1 
ATOM   70   O  O     . TYR A 1 10  ? 34.709  3.941   9.016   1.00 18.53  ?  10  TYR A O     1 
ATOM   71   C  CB    . TYR A 1 10  ? 34.440  2.909   11.669  1.00 20.95  ?  10  TYR A CB    1 
ATOM   72   C  CG    . TYR A 1 10  ? 35.727  2.146   11.613  1.00 22.47  ?  10  TYR A CG    1 
ATOM   73   C  CD1   . TYR A 1 10  ? 36.704  2.343   12.581  1.00 22.62  ?  10  TYR A CD1   1 
ATOM   74   C  CD2   . TYR A 1 10  ? 35.982  1.246   10.586  1.00 26.51  ?  10  TYR A CD2   1 
ATOM   75   C  CE1   . TYR A 1 10  ? 37.898  1.657   12.546  1.00 28.90  ?  10  TYR A CE1   1 
ATOM   76   C  CE2   . TYR A 1 10  ? 37.186  0.539   10.533  1.00 29.38  ?  10  TYR A CE2   1 
ATOM   77   C  CZ    . TYR A 1 10  ? 38.140  0.757   11.517  1.00 35.50  ?  10  TYR A CZ    1 
ATOM   78   O  OH    . TYR A 1 10  ? 39.331  0.073   11.491  1.00 37.37  ?  10  TYR A OH    1 
ATOM   79   N  N     . ASN A 1 11  ? 36.241  5.401   9.823   1.00 21.73  ?  11  ASN A N     1 
ATOM   80   C  CA    . ASN A 1 11  ? 36.922  5.643   8.533   1.00 22.14  ?  11  ASN A CA    1 
ATOM   81   C  C     . ASN A 1 11  ? 35.942  5.995   7.423   1.00 21.46  ?  11  ASN A C     1 
ATOM   82   O  O     . ASN A 1 11  ? 36.038  5.489   6.306   1.00 19.06  ?  11  ASN A O     1 
ATOM   83   C  CB    . ASN A 1 11  ? 37.765  4.444   8.100   1.00 18.44  ?  11  ASN A CB    1 
ATOM   84   C  CG    . ASN A 1 11  ? 38.851  4.100   9.095   1.00 23.94  ?  11  ASN A CG    1 
ATOM   85   O  OD1   . ASN A 1 11  ? 39.258  4.934   9.902   1.00 23.51  ?  11  ASN A OD1   1 
ATOM   86   N  ND2   . ASN A 1 11  ? 39.316  2.859   9.052   1.00 27.97  ?  11  ASN A ND2   1 
ATOM   87   N  N     . ARG A 1 12  ? 34.971  6.850   7.731   1.00 23.37  ?  12  ARG A N     1 
ATOM   88   C  CA    . ARG A 1 12  ? 34.055  7.381   6.720   1.00 23.88  ?  12  ARG A CA    1 
ATOM   89   C  C     . ARG A 1 12  ? 33.856  8.882   6.939   1.00 26.06  ?  12  ARG A C     1 
ATOM   90   O  O     . ARG A 1 12  ? 32.728  9.368   7.044   1.00 24.58  ?  12  ARG A O     1 
ATOM   91   C  CB    . ARG A 1 12  ? 32.723  6.633   6.758   1.00 21.76  ?  12  ARG A CB    1 
ATOM   92   C  CG    . ARG A 1 12  ? 32.783  5.172   6.334   1.00 24.94  ?  12  ARG A CG    1 
ATOM   93   C  CD    . ARG A 1 12  ? 31.361  4.587   6.254   1.00 19.82  ?  12  ARG A CD    1 
ATOM   94   N  NE    . ARG A 1 12  ? 31.354  3.137   6.095   1.00 19.90  ?  12  ARG A NE    1 
ATOM   95   C  CZ    . ARG A 1 12  ? 30.388  2.329   6.514   1.00 20.73  ?  12  ARG A CZ    1 
ATOM   96   N  NH1   . ARG A 1 12  ? 29.317  2.792   7.134   1.00 23.93  ?  12  ARG A NH1   1 
ATOM   97   N  NH2   . ARG A 1 12  ? 30.491  1.025   6.294   1.00 24.33  ?  12  ARG A NH2   1 
ATOM   98   N  N     . PRO A 1 13  ? 34.949  9.655   6.988   1.00 29.65  ?  13  PRO A N     1 
ATOM   99   C  CA    . PRO A 1 13  ? 34.784  11.083  7.325   1.00 25.26  ?  13  PRO A CA    1 
ATOM   100  C  C     . PRO A 1 13  ? 33.911  11.833  6.331   1.00 24.00  ?  13  PRO A C     1 
ATOM   101  O  O     . PRO A 1 13  ? 33.135  12.709  6.725   1.00 23.16  ?  13  PRO A O     1 
ATOM   102  C  CB    . PRO A 1 13  ? 36.230  11.599  7.345   1.00 31.01  ?  13  PRO A CB    1 
ATOM   103  C  CG    . PRO A 1 13  ? 36.967  10.683  6.401   1.00 28.89  ?  13  PRO A CG    1 
ATOM   104  C  CD    . PRO A 1 13  ? 36.331  9.335   6.568   1.00 24.28  ?  13  PRO A CD    1 
ATOM   105  N  N     . GLU A 1 14  ? 33.986  11.491  5.049   1.00 25.46  ?  14  GLU A N     1 
ATOM   106  C  CA    . GLU A 1 14  ? 33.144  12.155  4.060   1.00 24.38  ?  14  GLU A CA    1 
ATOM   107  C  C     . GLU A 1 14  ? 31.668  11.829  4.285   1.00 22.48  ?  14  GLU A C     1 
ATOM   108  O  O     . GLU A 1 14  ? 30.805  12.715  4.236   1.00 18.46  ?  14  GLU A O     1 
ATOM   109  C  CB    . GLU A 1 14  ? 33.580  11.758  2.641   1.00 26.60  ?  14  GLU A CB    1 
ATOM   110  C  CG    . GLU A 1 14  ? 33.531  10.239  2.281   1.00 38.96  ?  14  GLU A CG    1 
ATOM   111  C  CD    . GLU A 1 14  ? 34.338  9.301   3.207   1.00 33.47  ?  14  GLU A CD    1 
ATOM   112  O  OE1   . GLU A 1 14  ? 35.511  9.586   3.539   1.00 41.42  ?  14  GLU A OE1   1 
ATOM   113  O  OE2   . GLU A 1 14  ? 33.774  8.274   3.618   1.00 26.87  ?  14  GLU A OE2   1 
ATOM   114  N  N     . ARG A 1 15  ? 31.355  10.559  4.536   1.00 20.28  ?  15  ARG A N     1 
ATOM   115  C  CA    . ARG A 1 15  ? 29.954  10.197  4.680   1.00 22.44  ?  15  ARG A CA    1 
ATOM   116  C  C     . ARG A 1 15  ? 29.398  10.679  6.014   1.00 18.70  ?  15  ARG A C     1 
ATOM   117  O  O     . ARG A 1 15  ? 28.230  11.062  6.085   1.00 18.24  ?  15  ARG A O     1 
ATOM   118  C  CB    . ARG A 1 15  ? 29.784  8.689   4.498   1.00 23.90  ?  15  ARG A CB    1 
ATOM   119  C  CG    . ARG A 1 15  ? 29.748  8.288   3.022   1.00 25.03  ?  15  ARG A CG    1 
ATOM   120  C  CD    . ARG A 1 15  ? 29.948  6.803   2.853   1.00 37.25  ?  15  ARG A CD    1 
ATOM   121  N  NE    . ARG A 1 15  ? 30.909  6.498   1.799   1.00 47.59  ?  15  ARG A NE    1 
ATOM   122  C  CZ    . ARG A 1 15  ? 31.252  5.271   1.433   1.00 44.02  ?  15  ARG A CZ    1 
ATOM   123  N  NH1   . ARG A 1 15  ? 30.729  4.204   2.016   1.00 37.04  ?  15  ARG A NH1   1 
ATOM   124  N  NH2   . ARG A 1 15  ? 32.140  5.112   0.456   1.00 39.82  ?  15  ARG A NH2   1 
ATOM   125  N  N     . LEU A 1 16  ? 30.234  10.707  7.056   1.00 18.61  ?  16  LEU A N     1 
ATOM   126  C  CA    . LEU A 1 16  ? 29.846  11.294  8.329   1.00 16.43  ?  16  LEU A CA    1 
ATOM   127  C  C     . LEU A 1 16  ? 29.351  12.715  8.153   1.00 19.63  ?  16  LEU A C     1 
ATOM   128  O  O     . LEU A 1 16  ? 28.379  13.125  8.797   1.00 18.27  ?  16  LEU A O     1 
ATOM   129  C  CB    . LEU A 1 16  ? 31.027  11.274  9.300   1.00 16.96  ?  16  LEU A CB    1 
ATOM   130  C  CG    . LEU A 1 16  ? 30.781  12.074  10.576  1.00 19.75  ?  16  LEU A CG    1 
ATOM   131  C  CD1   . LEU A 1 16  ? 29.678  11.399  11.434  1.00 15.30  ?  16  LEU A CD1   1 
ATOM   132  C  CD2   . LEU A 1 16  ? 32.072  12.221  11.372  1.00 22.11  ?  16  LEU A CD2   1 
ATOM   133  N  N     . ALA A 1 17  ? 30.008  13.493  7.283   1.00 13.68  ?  17  ALA A N     1 
ATOM   134  C  CA    . ALA A 1 17  ? 29.569  14.869  7.083   1.00 14.94  ?  17  ALA A CA    1 
ATOM   135  C  C     . ALA A 1 17  ? 28.196  14.922  6.417   1.00 15.90  ?  17  ALA A C     1 
ATOM   136  O  O     . ALA A 1 17  ? 27.388  15.800  6.732   1.00 20.27  ?  17  ALA A O     1 
ATOM   137  C  CB    . ALA A 1 17  ? 30.610  15.642  6.270   1.00 22.65  ?  17  ALA A CB    1 
ATOM   138  N  N     . VAL A 1 18  ? 27.892  13.982  5.516   1.00 17.27  ?  18  VAL A N     1 
ATOM   139  C  CA    . VAL A 1 18  ? 26.547  13.943  4.949   1.00 12.16  ?  18  VAL A CA    1 
ATOM   140  C  C     . VAL A 1 18  ? 25.523  13.579  6.025   1.00 19.27  ?  18  VAL A C     1 
ATOM   141  O  O     . VAL A 1 18  ? 24.441  14.176  6.095   1.00 13.44  ?  18  VAL A O     1 
ATOM   142  C  CB    . VAL A 1 18  ? 26.476  12.973  3.761   1.00 17.11  ?  18  VAL A CB    1 
ATOM   143  C  CG1   . VAL A 1 18  ? 25.090  13.042  3.124   1.00 15.10  ?  18  VAL A CG1   1 
ATOM   144  C  CG2   . VAL A 1 18  ? 27.581  13.281  2.720   1.00 18.17  ?  18  VAL A CG2   1 
ATOM   145  N  N     . ALA A 1 19  ? 25.846  12.603  6.882   1.00 16.61  ?  19  ALA A N     1 
ATOM   146  C  CA    . ALA A 1 19  ? 24.918  12.223  7.952   1.00 23.07  ?  19  ALA A CA    1 
ATOM   147  C  C     . ALA A 1 19  ? 24.653  13.392  8.897   1.00 16.14  ?  19  ALA A C     1 
ATOM   148  O  O     . ALA A 1 19  ? 23.499  13.671  9.242   1.00 18.29  ?  19  ALA A O     1 
ATOM   149  C  CB    . ALA A 1 19  ? 25.454  11.011  8.722   1.00 14.22  ?  19  ALA A CB    1 
ATOM   150  N  N     . LEU A 1 20  ? 25.714  14.102  9.311   1.00 23.44  ?  20  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 20  ? 25.564  15.235  10.229  1.00 19.12  ?  20  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 20  ? 24.783  16.378  9.595   1.00 17.01  ?  20  LEU A C     1 
ATOM   153  O  O     . LEU A 1 20  ? 24.023  17.069  10.282  1.00 23.79  ?  20  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 20  ? 26.930  15.743  10.687  1.00 18.65  ?  20  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 20  ? 27.679  14.962  11.780  1.00 23.48  ?  20  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 20  ? 29.101  15.500  11.936  1.00 24.67  ?  20  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 20  ? 26.965  15.049  13.103  1.00 22.53  ?  20  LEU A CD2   1 
ATOM   158  N  N     . GLN A 1 21  ? 24.966  16.620  8.302   1.00 16.58  ?  21  GLN A N     1 
ATOM   159  C  CA    . GLN A 1 21  ? 24.172  17.671  7.670   1.00 21.46  ?  21  GLN A CA    1 
ATOM   160  C  C     . GLN A 1 21  ? 22.691  17.294  7.653   1.00 20.34  ?  21  GLN A C     1 
ATOM   161  O  O     . GLN A 1 21  ? 21.822  18.170  7.771   1.00 20.95  ?  21  GLN A O     1 
ATOM   162  C  CB    . GLN A 1 21  ? 24.696  17.958  6.265   1.00 17.70  ?  21  GLN A CB    1 
ATOM   163  C  CG    . GLN A 1 21  ? 23.861  18.923  5.431   1.00 19.53  ?  21  GLN A CG    1 
ATOM   164  C  CD    . GLN A 1 21  ? 24.111  20.400  5.745   1.00 25.31  ?  21  GLN A CD    1 
ATOM   165  O  OE1   . GLN A 1 21  ? 25.011  20.756  6.513   1.00 25.84  ?  21  GLN A OE1   1 
ATOM   166  N  NE2   . GLN A 1 21  ? 23.309  21.264  5.140   1.00 21.09  ?  21  GLN A NE2   1 
ATOM   167  N  N     . SER A 1 22  ? 22.387  15.999  7.570   1.00 15.06  ?  22  SER A N     1 
ATOM   168  C  CA    . SER A 1 22  ? 21.002  15.566  7.619   1.00 16.68  ?  22  SER A CA    1 
ATOM   169  C  C     . SER A 1 22  ? 20.406  15.748  9.024   1.00 15.13  ?  22  SER A C     1 
ATOM   170  O  O     . SER A 1 22  ? 19.184  15.847  9.160   1.00 12.69  ?  22  SER A O     1 
ATOM   171  C  CB    . SER A 1 22  ? 20.902  14.121  7.110   1.00 15.58  ?  22  SER A CB    1 
ATOM   172  O  OG    . SER A 1 22  ? 21.011  13.163  8.151   1.00 14.39  ?  22  SER A OG    1 
ATOM   173  N  N     . VAL A 1 23  ? 21.245  15.857  10.057  1.00 13.18  ?  23  VAL A N     1 
ATOM   174  C  CA    . VAL A 1 23  ? 20.767  16.312  11.355  1.00 15.62  ?  23  VAL A CA    1 
ATOM   175  C  C     . VAL A 1 23  ? 20.558  17.825  11.350  1.00 20.62  ?  23  VAL A C     1 
ATOM   176  O  O     . VAL A 1 23  ? 19.622  18.341  11.985  1.00 18.58  ?  23  VAL A O     1 
ATOM   177  C  CB    . VAL A 1 23  ? 21.745  15.865  12.460  1.00 19.77  ?  23  VAL A CB    1 
ATOM   178  C  CG1   . VAL A 1 23  ? 21.297  16.383  13.829  1.00 15.49  ?  23  VAL A CG1   1 
ATOM   179  C  CG2   . VAL A 1 23  ? 21.860  14.335  12.488  1.00 13.13  ?  23  VAL A CG2   1 
ATOM   180  N  N     . GLN A 1 24  ? 21.395  18.562  10.612  1.00 16.64  ?  24  GLN A N     1 
ATOM   181  C  CA    . GLN A 1 24  ? 21.263  20.016  10.625  1.00 19.07  ?  24  GLN A CA    1 
ATOM   182  C  C     . GLN A 1 24  ? 19.996  20.461  9.910   1.00 16.09  ?  24  GLN A C     1 
ATOM   183  O  O     . GLN A 1 24  ? 19.435  21.515  10.233  1.00 23.63  ?  24  GLN A O     1 
ATOM   184  C  CB    . GLN A 1 24  ? 22.514  20.663  10.018  1.00 21.52  ?  24  GLN A CB    1 
ATOM   185  C  CG    . GLN A 1 24  ? 23.744  20.157  10.725  1.00 25.47  ?  24  GLN A CG    1 
ATOM   186  C  CD    . GLN A 1 24  ? 24.938  21.036  10.607  1.00 29.84  ?  24  GLN A CD    1 
ATOM   187  O  OE1   . GLN A 1 24  ? 24.925  22.158  11.093  1.00 39.69  ?  24  GLN A OE1   1 
ATOM   188  N  NE2   . GLN A 1 24  ? 26.008  20.519  10.007  1.00 33.36  ?  24  GLN A NE2   1 
ATOM   189  N  N     . THR A 1 25  ? 19.499  19.655  8.979   1.00 15.53  ?  25  THR A N     1 
ATOM   190  C  CA    . THR A 1 25  ? 18.262  19.966  8.280   1.00 16.18  ?  25  THR A CA    1 
ATOM   191  C  C     . THR A 1 25  ? 17.055  19.229  8.872   1.00 18.05  ?  25  THR A C     1 
ATOM   192  O  O     . THR A 1 25  ? 16.014  19.119  8.217   1.00 17.74  ?  25  THR A O     1 
ATOM   193  C  CB    . THR A 1 25  ? 18.425  19.673  6.791   1.00 19.67  ?  25  THR A CB    1 
ATOM   194  O  OG1   . THR A 1 25  ? 18.676  18.276  6.599   1.00 14.91  ?  25  THR A OG1   1 
ATOM   195  C  CG2   . THR A 1 25  ? 19.621  20.469  6.237   1.00 19.13  ?  25  THR A CG2   1 
ATOM   196  N  N     . LEU A 1 26  ? 17.166  18.741  10.104  1.00 14.40  ?  26  LEU A N     1 
ATOM   197  C  CA    . LEU A 1 26  ? 15.973  18.336  10.837  1.00 22.24  ?  26  LEU A CA    1 
ATOM   198  C  C     . LEU A 1 26  ? 15.102  19.550  11.149  1.00 22.20  ?  26  LEU A C     1 
ATOM   199  O  O     . LEU A 1 26  ? 15.590  20.557  11.672  1.00 25.77  ?  26  LEU A O     1 
ATOM   200  C  CB    . LEU A 1 26  ? 16.360  17.649  12.142  1.00 21.63  ?  26  LEU A CB    1 
ATOM   201  C  CG    . LEU A 1 26  ? 16.732  16.176  12.070  1.00 18.66  ?  26  LEU A CG    1 
ATOM   202  C  CD1   . LEU A 1 26  ? 17.200  15.699  13.436  1.00 15.07  ?  26  LEU A CD1   1 
ATOM   203  C  CD2   . LEU A 1 26  ? 15.562  15.372  11.554  1.00 15.31  ?  26  LEU A CD2   1 
ATOM   204  N  N     . ASP A 1 27  ? 13.807  19.457  10.846  1.00 22.53  ?  27  ASP A N     1 
ATOM   205  C  CA    . ASP A 1 27  ? 12.864  20.430  11.401  1.00 30.08  ?  27  ASP A CA    1 
ATOM   206  C  C     . ASP A 1 27  ? 12.703  20.178  12.896  1.00 25.00  ?  27  ASP A C     1 
ATOM   207  O  O     . ASP A 1 27  ? 11.853  19.380  13.295  1.00 27.04  ?  27  ASP A O     1 
ATOM   208  C  CB    . ASP A 1 27  ? 11.499  20.345  10.711  1.00 29.15  ?  27  ASP A CB    1 
ATOM   209  C  CG    . ASP A 1 27  ? 10.514  21.406  11.203  1.00 41.91  ?  27  ASP A CG    1 
ATOM   210  O  OD1   . ASP A 1 27  ? 10.864  22.216  12.095  1.00 37.66  ?  27  ASP A OD1   1 
ATOM   211  O  OD2   . ASP A 1 27  ? 9.375   21.433  10.685  1.00 49.70  ?  27  ASP A OD2   1 
ATOM   212  N  N     . PHE A 1 28  ? 13.503  20.843  13.727  1.00 30.28  ?  28  PHE A N     1 
ATOM   213  C  CA    . PHE A 1 28  ? 13.486  20.558  15.156  1.00 28.45  ?  28  PHE A CA    1 
ATOM   214  C  C     . PHE A 1 28  ? 14.133  21.702  15.927  1.00 27.10  ?  28  PHE A C     1 
ATOM   215  O  O     . PHE A 1 28  ? 15.065  22.343  15.443  1.00 32.67  ?  28  PHE A O     1 
ATOM   216  C  CB    . PHE A 1 28  ? 14.209  19.244  15.454  1.00 19.94  ?  28  PHE A CB    1 
ATOM   217  C  CG    . PHE A 1 28  ? 13.884  18.674  16.788  1.00 20.30  ?  28  PHE A CG    1 
ATOM   218  C  CD1   . PHE A 1 28  ? 12.623  18.182  17.047  1.00 20.34  ?  28  PHE A CD1   1 
ATOM   219  C  CD2   . PHE A 1 28  ? 14.832  18.649  17.794  1.00 21.31  ?  28  PHE A CD2   1 
ATOM   220  C  CE1   . PHE A 1 28  ? 12.312  17.661  18.278  1.00 19.33  ?  28  PHE A CE1   1 
ATOM   221  C  CE2   . PHE A 1 28  ? 14.527  18.138  19.039  1.00 20.75  ?  28  PHE A CE2   1 
ATOM   222  C  CZ    . PHE A 1 28  ? 13.267  17.634  19.277  1.00 21.97  ?  28  PHE A CZ    1 
ATOM   223  N  N     . ASP A 1 29  ? 13.635  21.941  17.138  1.00 28.75  ?  29  ASP A N     1 
ATOM   224  C  CA    . ASP A 1 29  ? 14.265  22.906  18.037  1.00 35.96  ?  29  ASP A CA    1 
ATOM   225  C  C     . ASP A 1 29  ? 15.597  22.337  18.520  1.00 31.65  ?  29  ASP A C     1 
ATOM   226  O  O     . ASP A 1 29  ? 15.627  21.445  19.376  1.00 30.07  ?  29  ASP A O     1 
ATOM   227  C  CB    . ASP A 1 29  ? 13.353  23.234  19.219  1.00 29.52  ?  29  ASP A CB    1 
ATOM   228  C  CG    . ASP A 1 29  ? 13.990  24.241  20.202  1.00 40.84  ?  29  ASP A CG    1 
ATOM   229  O  OD1   . ASP A 1 29  ? 13.475  24.415  21.333  1.00 40.87  ?  29  ASP A OD1   1 
ATOM   230  O  OD2   . ASP A 1 29  ? 15.008  24.873  19.841  1.00 44.91  ?  29  ASP A OD2   1 
ATOM   231  N  N     . SER A 1 30  ? 16.698  22.873  17.990  1.00 30.45  ?  30  SER A N     1 
ATOM   232  C  CA    . SER A 1 30  ? 18.040  22.422  18.341  1.00 29.52  ?  30  SER A CA    1 
ATOM   233  C  C     . SER A 1 30  ? 18.376  22.614  19.818  1.00 22.61  ?  30  SER A C     1 
ATOM   234  O  O     . SER A 1 30  ? 19.356  22.033  20.294  1.00 25.10  ?  30  SER A O     1 
ATOM   235  C  CB    . SER A 1 30  ? 19.064  23.143  17.455  1.00 34.27  ?  30  SER A CB    1 
ATOM   236  O  OG    . SER A 1 30  ? 18.734  24.521  17.302  1.00 36.78  ?  30  SER A OG    1 
ATOM   237  N  N     . GLU A 1 31  ? 17.600  23.401  20.557  1.00 28.63  ?  31  GLU A N     1 
ATOM   238  C  CA    . GLU A 1 31  ? 17.814  23.498  21.997  1.00 27.30  ?  31  GLU A CA    1 
ATOM   239  C  C     . GLU A 1 31  ? 17.553  22.164  22.691  1.00 28.54  ?  31  GLU A C     1 
ATOM   240  O  O     . GLU A 1 31  ? 18.150  21.873  23.733  1.00 25.67  ?  31  GLU A O     1 
ATOM   241  C  CB    . GLU A 1 31  ? 16.912  24.591  22.571  1.00 32.14  ?  31  GLU A CB    1 
ATOM   242  C  CG    . GLU A 1 31  ? 17.535  25.418  23.690  1.00 45.85  ?  31  GLU A CG    1 
ATOM   243  C  CD    . GLU A 1 31  ? 18.244  26.674  23.182  1.00 56.39  ?  31  GLU A CD    1 
ATOM   244  O  OE1   . GLU A 1 31  ? 17.656  27.401  22.347  1.00 61.95  ?  31  GLU A OE1   1 
ATOM   245  O  OE2   . GLU A 1 31  ? 19.375  26.950  23.645  1.00 57.75  ?  31  GLU A OE2   1 
ATOM   246  N  N     . GLN A 1 32  ? 16.675  21.338  22.128  1.00 23.52  ?  32  GLN A N     1 
ATOM   247  C  CA    . GLN A 1 32  ? 16.304  20.058  22.711  1.00 26.52  ?  32  GLN A CA    1 
ATOM   248  C  C     . GLN A 1 32  ? 17.053  18.875  22.102  1.00 25.51  ?  32  GLN A C     1 
ATOM   249  O  O     . GLN A 1 32  ? 16.704  17.727  22.383  1.00 20.12  ?  32  GLN A O     1 
ATOM   250  C  CB    . GLN A 1 32  ? 14.802  19.851  22.553  1.00 27.59  ?  32  GLN A CB    1 
ATOM   251  C  CG    . GLN A 1 32  ? 13.991  21.005  23.063  1.00 33.86  ?  32  GLN A CG    1 
ATOM   252  C  CD    . GLN A 1 32  ? 13.559  20.765  24.478  1.00 40.16  ?  32  GLN A CD    1 
ATOM   253  O  OE1   . GLN A 1 32  ? 14.261  20.091  25.238  1.00 38.56  ?  32  GLN A OE1   1 
ATOM   254  N  NE2   . GLN A 1 32  ? 12.401  21.310  24.853  1.00 44.83  ?  32  GLN A NE2   1 
ATOM   255  N  N     . LEU A 1 33  ? 18.066  19.125  21.280  1.00 23.25  ?  33  LEU A N     1 
ATOM   256  C  CA    . LEU A 1 33  ? 18.750  18.077  20.541  1.00 23.43  ?  33  LEU A CA    1 
ATOM   257  C  C     . LEU A 1 33  ? 20.234  18.086  20.868  1.00 23.70  ?  33  LEU A C     1 
ATOM   258  O  O     . LEU A 1 33  ? 20.870  19.144  20.823  1.00 20.36  ?  33  LEU A O     1 
ATOM   259  C  CB    . LEU A 1 33  ? 18.552  18.265  19.034  1.00 25.47  ?  33  LEU A CB    1 
ATOM   260  C  CG    . LEU A 1 33  ? 19.321  17.236  18.198  1.00 27.26  ?  33  LEU A CG    1 
ATOM   261  C  CD1   . LEU A 1 33  ? 18.595  15.916  18.251  1.00 19.71  ?  33  LEU A CD1   1 
ATOM   262  C  CD2   . LEU A 1 33  ? 19.536  17.683  16.752  1.00 22.46  ?  33  LEU A CD2   1 
ATOM   263  N  N     . GLU A 1 34  ? 20.784  16.907  21.177  1.00 27.03  ?  34  GLU A N     1 
ATOM   264  C  CA    . GLU A 1 34  ? 22.228  16.705  21.261  1.00 23.42  ?  34  GLU A CA    1 
ATOM   265  C  C     . GLU A 1 34  ? 22.633  15.604  20.300  1.00 22.17  ?  34  GLU A C     1 
ATOM   266  O  O     . GLU A 1 34  ? 21.908  14.615  20.128  1.00 21.06  ?  34  GLU A O     1 
ATOM   267  C  CB    . GLU A 1 34  ? 22.703  16.343  22.684  1.00 23.63  ?  34  GLU A CB    1 
ATOM   268  C  CG    . GLU A 1 34  ? 22.402  14.911  23.117  1.00 22.37  ?  34  GLU A CG    1 
ATOM   269  C  CD    . GLU A 1 34  ? 23.138  14.477  24.396  1.00 29.35  ?  34  GLU A CD    1 
ATOM   270  O  OE1   . GLU A 1 34  ? 24.014  15.226  24.880  1.00 31.19  ?  34  GLU A OE1   1 
ATOM   271  O  OE2   . GLU A 1 34  ? 22.838  13.380  24.930  1.00 28.69  ?  34  GLU A OE2   1 
ATOM   272  N  N     . VAL A 1 35  ? 23.789  15.791  19.668  1.00 23.27  ?  35  VAL A N     1 
ATOM   273  C  CA    . VAL A 1 35  ? 24.385  14.817  18.762  1.00 15.21  ?  35  VAL A CA    1 
ATOM   274  C  C     . VAL A 1 35  ? 25.633  14.259  19.426  1.00 16.72  ?  35  VAL A C     1 
ATOM   275  O  O     . VAL A 1 35  ? 26.505  15.020  19.867  1.00 15.01  ?  35  VAL A O     1 
ATOM   276  C  CB    . VAL A 1 35  ? 24.739  15.451  17.408  1.00 18.67  ?  35  VAL A CB    1 
ATOM   277  C  CG1   . VAL A 1 35  ? 25.261  14.373  16.424  1.00 16.15  ?  35  VAL A CG1   1 
ATOM   278  C  CG2   . VAL A 1 35  ? 23.545  16.216  16.851  1.00 20.73  ?  35  VAL A CG2   1 
ATOM   279  N  N     . ILE A 1 36  ? 25.735  12.935  19.476  1.00 16.09  ?  36  ILE A N     1 
ATOM   280  C  CA    . ILE A 1 36  ? 26.925  12.271  19.995  1.00 16.24  ?  36  ILE A CA    1 
ATOM   281  C  C     . ILE A 1 36  ? 27.549  11.464  18.862  1.00 16.20  ?  36  ILE A C     1 
ATOM   282  O  O     . ILE A 1 36  ? 27.000  10.431  18.447  1.00 16.88  ?  36  ILE A O     1 
ATOM   283  C  CB    . ILE A 1 36  ? 26.602  11.382  21.199  1.00 14.41  ?  36  ILE A CB    1 
ATOM   284  C  CG1   . ILE A 1 36  ? 26.074  12.238  22.351  1.00 16.59  ?  36  ILE A CG1   1 
ATOM   285  C  CG2   . ILE A 1 36  ? 27.842  10.611  21.642  1.00 16.12  ?  36  ILE A CG2   1 
ATOM   286  C  CD1   . ILE A 1 36  ? 25.051  11.526  23.186  1.00 23.19  ?  36  ILE A CD1   1 
ATOM   287  N  N     . VAL A 1 37  ? 28.705  11.913  18.377  1.00 16.33  ?  37  VAL A N     1 
ATOM   288  C  CA    . VAL A 1 37  ? 29.471  11.197  17.353  1.00 12.77  ?  37  VAL A CA    1 
ATOM   289  C  C     . VAL A 1 37  ? 30.524  10.328  18.036  1.00 14.29  ?  37  VAL A C     1 
ATOM   290  O  O     . VAL A 1 37  ? 31.296  10.812  18.880  1.00 18.06  ?  37  VAL A O     1 
ATOM   291  C  CB    . VAL A 1 37  ? 30.120  12.181  16.366  1.00 11.91  ?  37  VAL A CB    1 
ATOM   292  C  CG1   . VAL A 1 37  ? 30.975  11.413  15.343  1.00 11.04  ?  37  VAL A CG1   1 
ATOM   293  C  CG2   . VAL A 1 37  ? 29.053  12.986  15.673  1.00 9.37   ?  37  VAL A CG2   1 
ATOM   294  N  N     . VAL A 1 38  ? 30.566  9.047   17.686  1.00 13.22  ?  38  VAL A N     1 
ATOM   295  C  CA    . VAL A 1 38  ? 31.475  8.102   18.334  1.00 14.89  ?  38  VAL A CA    1 
ATOM   296  C  C     . VAL A 1 38  ? 32.425  7.566   17.268  1.00 16.15  ?  38  VAL A C     1 
ATOM   297  O  O     . VAL A 1 38  ? 32.054  6.713   16.445  1.00 14.78  ?  38  VAL A O     1 
ATOM   298  C  CB    . VAL A 1 38  ? 30.736  6.964   19.053  1.00 15.25  ?  38  VAL A CB    1 
ATOM   299  C  CG1   . VAL A 1 38  ? 31.717  6.056   19.794  1.00 10.39  ?  38  VAL A CG1   1 
ATOM   300  C  CG2   . VAL A 1 38  ? 29.718  7.534   20.050  1.00 14.30  ?  38  VAL A CG2   1 
ATOM   301  N  N     . ASN A 1 39  ? 33.663  8.052   17.299  1.00 19.36  ?  39  ASN A N     1 
ATOM   302  C  CA    . ASN A 1 39  ? 34.718  7.561   16.419  1.00 17.53  ?  39  ASN A CA    1 
ATOM   303  C  C     . ASN A 1 39  ? 35.209  6.218   16.944  1.00 19.09  ?  39  ASN A C     1 
ATOM   304  O  O     . ASN A 1 39  ? 35.741  6.135   18.058  1.00 18.80  ?  39  ASN A O     1 
ATOM   305  C  CB    . ASN A 1 39  ? 35.854  8.572   16.360  1.00 17.60  ?  39  ASN A CB    1 
ATOM   306  C  CG    . ASN A 1 39  ? 36.927  8.190   15.367  1.00 21.80  ?  39  ASN A CG    1 
ATOM   307  O  OD1   . ASN A 1 39  ? 36.780  7.231   14.616  1.00 24.71  ?  39  ASN A OD1   1 
ATOM   308  N  ND2   . ASN A 1 39  ? 38.018  8.942   15.359  1.00 21.94  ?  39  ASN A ND2   1 
ATOM   309  N  N     . ASP A 1 40  ? 35.019  5.163   16.157  1.00 20.41  ?  40  ASP A N     1 
ATOM   310  C  CA    . ASP A 1 40  ? 35.418  3.829   16.598  1.00 19.61  ?  40  ASP A CA    1 
ATOM   311  C  C     . ASP A 1 40  ? 36.908  3.594   16.333  1.00 24.59  ?  40  ASP A C     1 
ATOM   312  O  O     . ASP A 1 40  ? 37.296  2.558   15.783  1.00 26.32  ?  40  ASP A O     1 
ATOM   313  C  CB    . ASP A 1 40  ? 34.549  2.772   15.911  1.00 19.17  ?  40  ASP A CB    1 
ATOM   314  C  CG    . ASP A 1 40  ? 34.636  1.420   16.581  1.00 19.00  ?  40  ASP A CG    1 
ATOM   315  O  OD1   . ASP A 1 40  ? 35.033  1.361   17.760  1.00 21.70  ?  40  ASP A OD1   1 
ATOM   316  O  OD2   . ASP A 1 40  ? 34.326  0.413   15.921  1.00 20.77  ?  40  ASP A OD2   1 
ATOM   317  N  N     . HIS A 1 41  ? 37.745  4.553   16.742  1.00 22.54  ?  41  HIS A N     1 
ATOM   318  C  CA    . HIS A 1 41  ? 39.203  4.486   16.610  1.00 26.76  ?  41  HIS A CA    1 
ATOM   319  C  C     . HIS A 1 41  ? 39.639  4.325   15.150  1.00 24.84  ?  41  HIS A C     1 
ATOM   320  O  O     . HIS A 1 41  ? 40.536  3.547   14.826  1.00 30.89  ?  41  HIS A O     1 
ATOM   321  C  CB    . HIS A 1 41  ? 39.801  3.385   17.491  1.00 31.26  ?  41  HIS A CB    1 
ATOM   322  C  CG    . HIS A 1 41  ? 41.277  3.543   17.716  1.00 42.26  ?  41  HIS A CG    1 
ATOM   323  N  ND1   . HIS A 1 41  ? 41.796  4.348   18.712  1.00 37.64  ?  41  HIS A ND1   1 
ATOM   324  C  CD2   . HIS A 1 41  ? 42.343  3.006   17.073  1.00 36.42  ?  41  HIS A CD2   1 
ATOM   325  C  CE1   . HIS A 1 41  ? 43.117  4.302   18.666  1.00 37.43  ?  41  HIS A CE1   1 
ATOM   326  N  NE2   . HIS A 1 41  ? 43.474  3.497   17.680  1.00 38.96  ?  41  HIS A NE2   1 
ATOM   327  N  N     . GLY A 1 42  ? 38.975  5.053   14.263  1.00 20.49  ?  42  GLY A N     1 
ATOM   328  C  CA    . GLY A 1 42  ? 39.401  5.226   12.900  1.00 29.67  ?  42  GLY A CA    1 
ATOM   329  C  C     . GLY A 1 42  ? 40.041  6.582   12.704  1.00 26.91  ?  42  GLY A C     1 
ATOM   330  O  O     . GLY A 1 42  ? 40.449  7.247   13.664  1.00 27.95  ?  42  GLY A O     1 
ATOM   331  N  N     . THR A 1 43  ? 40.111  7.012   11.444  1.00 22.61  ?  43  THR A N     1 
ATOM   332  C  CA    . THR A 1 43  ? 40.810  8.246   11.128  1.00 22.75  ?  43  THR A CA    1 
ATOM   333  C  C     . THR A 1 43  ? 40.044  9.444   11.681  1.00 26.84  ?  43  THR A C     1 
ATOM   334  O  O     . THR A 1 43  ? 38.810  9.427   11.739  1.00 29.22  ?  43  THR A O     1 
ATOM   335  C  CB    . THR A 1 43  ? 40.994  8.390   9.621   1.00 24.66  ?  43  THR A CB    1 
ATOM   336  O  OG1   . THR A 1 43  ? 39.713  8.471   8.988   1.00 30.95  ?  43  THR A OG1   1 
ATOM   337  C  CG2   . THR A 1 43  ? 41.738  7.186   9.074   1.00 28.12  ?  43  THR A CG2   1 
ATOM   338  N  N     . PRO A 1 44  ? 40.757  10.503  12.080  1.00 32.51  ?  44  PRO A N     1 
ATOM   339  C  CA    . PRO A 1 44  ? 40.132  11.558  12.894  1.00 25.89  ?  44  PRO A CA    1 
ATOM   340  C  C     . PRO A 1 44  ? 38.939  12.206  12.208  1.00 24.98  ?  44  PRO A C     1 
ATOM   341  O  O     . PRO A 1 44  ? 38.833  12.225  10.984  1.00 18.62  ?  44  PRO A O     1 
ATOM   342  C  CB    . PRO A 1 44  ? 41.272  12.564  13.103  1.00 25.56  ?  44  PRO A CB    1 
ATOM   343  C  CG    . PRO A 1 44  ? 42.537  11.768  12.880  1.00 25.44  ?  44  PRO A CG    1 
ATOM   344  C  CD    . PRO A 1 44  ? 42.189  10.765  11.822  1.00 25.22  ?  44  PRO A CD    1 
ATOM   345  N  N     . VAL A 1 45  ? 38.011  12.720  13.025  1.00 28.95  ?  45  VAL A N     1 
ATOM   346  C  CA    . VAL A 1 45  ? 36.784  13.331  12.514  1.00 23.02  ?  45  VAL A CA    1 
ATOM   347  C  C     . VAL A 1 45  ? 36.545  14.666  13.208  1.00 30.41  ?  45  VAL A C     1 
ATOM   348  O  O     . VAL A 1 45  ? 35.468  15.263  13.086  1.00 29.50  ?  45  VAL A O     1 
ATOM   349  C  CB    . VAL A 1 45  ? 35.575  12.393  12.702  1.00 27.60  ?  45  VAL A CB    1 
ATOM   350  C  CG1   . VAL A 1 45  ? 35.700  11.170  11.814  1.00 26.66  ?  45  VAL A CG1   1 
ATOM   351  C  CG2   . VAL A 1 45  ? 35.451  11.978  14.155  1.00 20.14  ?  45  VAL A CG2   1 
ATOM   352  N  N     . ASP A 1 46  ? 37.549  15.145  13.942  1.00 35.54  ?  46  ASP A N     1 
ATOM   353  C  CA    . ASP A 1 46  ? 37.375  16.354  14.738  1.00 32.71  ?  46  ASP A CA    1 
ATOM   354  C  C     . ASP A 1 46  ? 36.966  17.541  13.870  1.00 38.80  ?  46  ASP A C     1 
ATOM   355  O  O     . ASP A 1 46  ? 36.136  18.360  14.284  1.00 37.75  ?  46  ASP A O     1 
ATOM   356  C  CB    . ASP A 1 46  ? 38.662  16.665  15.503  1.00 37.85  ?  46  ASP A CB    1 
ATOM   357  C  CG    . ASP A 1 46  ? 39.247  15.443  16.198  1.00 40.37  ?  46  ASP A CG    1 
ATOM   358  O  OD1   . ASP A 1 46  ? 39.869  14.592  15.513  1.00 41.69  ?  46  ASP A OD1   1 
ATOM   359  O  OD2   . ASP A 1 46  ? 39.099  15.343  17.434  1.00 44.72  ?  46  ASP A OD2   1 
ATOM   360  N  N     . ASP A 1 47  ? 37.517  17.639  12.657  1.00 34.04  ?  47  ASP A N     1 
ATOM   361  C  CA    . ASP A 1 47  ? 37.197  18.760  11.776  1.00 37.01  ?  47  ASP A CA    1 
ATOM   362  C  C     . ASP A 1 47  ? 35.758  18.684  11.274  1.00 36.47  ?  47  ASP A C     1 
ATOM   363  O  O     . ASP A 1 47  ? 35.046  19.696  11.247  1.00 36.42  ?  47  ASP A O     1 
ATOM   364  C  CB    . ASP A 1 47  ? 38.173  18.790  10.599  1.00 35.89  ?  47  ASP A CB    1 
ATOM   365  C  CG    . ASP A 1 47  ? 39.614  18.616  11.040  1.00 51.30  ?  47  ASP A CG    1 
ATOM   366  O  OD1   . ASP A 1 47  ? 40.213  19.601  11.534  1.00 48.94  ?  47  ASP A OD1   1 
ATOM   367  O  OD2   . ASP A 1 47  ? 40.131  17.478  10.937  1.00 55.66  ?  47  ASP A OD2   1 
ATOM   368  N  N     . VAL A 1 48  ? 35.325  17.496  10.843  1.00 34.41  ?  48  VAL A N     1 
ATOM   369  C  CA    . VAL A 1 48  ? 33.929  17.288  10.457  1.00 31.08  ?  48  VAL A CA    1 
ATOM   370  C  C     . VAL A 1 48  ? 33.003  17.698  11.594  1.00 31.80  ?  48  VAL A C     1 
ATOM   371  O  O     . VAL A 1 48  ? 32.055  18.468  11.405  1.00 28.81  ?  48  VAL A O     1 
ATOM   372  C  CB    . VAL A 1 48  ? 33.702  15.817  10.054  1.00 31.09  ?  48  VAL A CB    1 
ATOM   373  C  CG1   . VAL A 1 48  ? 32.292  15.618  9.522   1.00 27.74  ?  48  VAL A CG1   1 
ATOM   374  C  CG2   . VAL A 1 48  ? 34.727  15.387  9.011   1.00 29.12  ?  48  VAL A CG2   1 
ATOM   375  N  N     . VAL A 1 49  ? 33.291  17.206  12.803  1.00 36.74  ?  49  VAL A N     1 
ATOM   376  C  CA    . VAL A 1 49  ? 32.414  17.426  13.948  1.00 32.60  ?  49  VAL A CA    1 
ATOM   377  C  C     . VAL A 1 49  ? 32.495  18.871  14.419  1.00 35.28  ?  49  VAL A C     1 
ATOM   378  O  O     . VAL A 1 49  ? 31.496  19.446  14.866  1.00 30.54  ?  49  VAL A O     1 
ATOM   379  C  CB    . VAL A 1 49  ? 32.767  16.440  15.075  1.00 28.67  ?  49  VAL A CB    1 
ATOM   380  C  CG1   . VAL A 1 49  ? 31.943  16.743  16.322  1.00 30.52  ?  49  VAL A CG1   1 
ATOM   381  C  CG2   . VAL A 1 49  ? 32.554  15.009  14.608  1.00 22.50  ?  49  VAL A CG2   1 
ATOM   382  N  N     . GLU A 1 50  ? 33.687  19.474  14.345  1.00 36.96  ?  50  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 50  ? 33.823  20.899  14.631  1.00 36.27  ?  50  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 50  ? 32.915  21.725  13.727  1.00 33.28  ?  50  GLU A C     1 
ATOM   385  O  O     . GLU A 1 50  ? 32.294  22.697  14.174  1.00 41.56  ?  50  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 50  ? 35.286  21.335  14.466  1.00 35.30  ?  50  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 50  ? 36.090  21.412  15.777  1.00 44.28  ?  50  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 50  ? 37.592  21.075  15.627  1.00 55.61  ?  50  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 50  ? 38.150  21.150  14.498  1.00 41.41  ?  50  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 50  ? 38.218  20.733  16.663  1.00 57.55  ?  50  GLU A OE2   1 
ATOM   391  N  N     . ALA A 1 51  ? 32.821  21.349  12.452  1.00 32.91  ?  51  ALA A N     1 
ATOM   392  C  CA    . ALA A 1 51  ? 32.007  22.112  11.513  1.00 32.92  ?  51  ALA A CA    1 
ATOM   393  C  C     . ALA A 1 51  ? 30.529  22.030  11.875  1.00 37.43  ?  51  ALA A C     1 
ATOM   394  O  O     . ALA A 1 51  ? 29.842  23.057  11.950  1.00 33.48  ?  51  ALA A O     1 
ATOM   395  C  CB    . ALA A 1 51  ? 32.251  21.618  10.086  1.00 24.15  ?  51  ALA A CB    1 
ATOM   396  N  N     . ALA A 1 52  ? 30.021  20.811  12.114  1.00 37.17  ?  52  ALA A N     1 
ATOM   397  C  CA    . ALA A 1 52  ? 28.617  20.642  12.481  1.00 30.47  ?  52  ALA A CA    1 
ATOM   398  C  C     . ALA A 1 52  ? 28.281  21.372  13.774  1.00 31.94  ?  52  ALA A C     1 
ATOM   399  O  O     . ALA A 1 52  ? 27.141  21.814  13.961  1.00 24.54  ?  52  ALA A O     1 
ATOM   400  C  CB    . ALA A 1 52  ? 28.282  19.160  12.617  1.00 28.26  ?  52  ALA A CB    1 
ATOM   401  N  N     . GLY A 1 53  ? 29.259  21.520  14.668  1.00 33.02  ?  53  GLY A N     1 
ATOM   402  C  CA    . GLY A 1 53  ? 29.022  22.187  15.934  1.00 28.33  ?  53  GLY A CA    1 
ATOM   403  C  C     . GLY A 1 53  ? 28.662  23.650  15.800  1.00 39.42  ?  53  GLY A C     1 
ATOM   404  O  O     . GLY A 1 53  ? 28.180  24.244  16.769  1.00 35.86  ?  53  GLY A O     1 
ATOM   405  N  N     . ARG A 1 54  ? 28.892  24.249  14.621  1.00 41.63  ?  54  ARG A N     1 
ATOM   406  C  CA    . ARG A 1 54  ? 28.462  25.630  14.398  1.00 47.96  ?  54  ARG A CA    1 
ATOM   407  C  C     . ARG A 1 54  ? 26.958  25.784  14.586  1.00 45.68  ?  54  ARG A C     1 
ATOM   408  O  O     . ARG A 1 54  ? 26.487  26.847  15.008  1.00 49.76  ?  54  ARG A O     1 
ATOM   409  C  CB    . ARG A 1 54  ? 28.863  26.101  12.995  1.00 46.67  ?  54  ARG A CB    1 
ATOM   410  C  CG    . ARG A 1 54  ? 30.345  25.933  12.634  1.00 48.95  ?  54  ARG A CG    1 
ATOM   411  C  CD    . ARG A 1 54  ? 31.259  26.763  13.522  1.00 53.74  ?  54  ARG A CD    1 
ATOM   412  N  NE    . ARG A 1 54  ? 31.533  28.081  12.958  1.00 62.22  ?  54  ARG A NE    1 
ATOM   413  C  CZ    . ARG A 1 54  ? 30.826  29.173  13.224  1.00 63.49  ?  54  ARG A CZ    1 
ATOM   414  N  NH1   . ARG A 1 54  ? 29.785  29.143  14.045  1.00 59.31  ?  54  ARG A NH1   1 
ATOM   415  N  NH2   . ARG A 1 54  ? 31.172  30.326  12.655  1.00 57.97  ?  54  ARG A NH2   1 
ATOM   416  N  N     . SER A 1 55  ? 26.193  24.736  14.289  1.00 38.51  ?  55  SER A N     1 
ATOM   417  C  CA    . SER A 1 55  ? 24.747  24.780  14.372  1.00 41.46  ?  55  SER A CA    1 
ATOM   418  C  C     . SER A 1 55  ? 24.150  23.784  15.356  1.00 40.71  ?  55  SER A C     1 
ATOM   419  O  O     . SER A 1 55  ? 23.005  23.982  15.779  1.00 45.07  ?  55  SER A O     1 
ATOM   420  C  CB    . SER A 1 55  ? 24.133  24.533  12.985  1.00 41.68  ?  55  SER A CB    1 
ATOM   421  O  OG    . SER A 1 55  ? 22.898  23.841  13.091  1.00 51.80  ?  55  SER A OG    1 
ATOM   422  N  N     . LEU A 1 56  ? 24.881  22.741  15.739  1.00 30.90  ?  56  LEU A N     1 
ATOM   423  C  CA    . LEU A 1 56  ? 24.362  21.679  16.583  1.00 28.48  ?  56  LEU A CA    1 
ATOM   424  C  C     . LEU A 1 56  ? 25.168  21.586  17.873  1.00 33.05  ?  56  LEU A C     1 
ATOM   425  O  O     . LEU A 1 56  ? 26.347  21.949  17.923  1.00 28.44  ?  56  LEU A O     1 
ATOM   426  C  CB    . LEU A 1 56  ? 24.429  20.320  15.879  1.00 29.06  ?  56  LEU A CB    1 
ATOM   427  C  CG    . LEU A 1 56  ? 23.479  19.978  14.739  1.00 28.63  ?  56  LEU A CG    1 
ATOM   428  C  CD1   . LEU A 1 56  ? 24.059  18.809  13.953  1.00 20.47  ?  56  LEU A CD1   1 
ATOM   429  C  CD2   . LEU A 1 56  ? 22.095  19.676  15.250  1.00 31.82  ?  56  LEU A CD2   1 
ATOM   430  N  N     . ASN A 1 57  ? 24.520  21.070  18.919  1.00 26.99  ?  57  ASN A N     1 
ATOM   431  C  CA    . ASN A 1 57  ? 25.189  20.687  20.161  1.00 25.09  ?  57  ASN A CA    1 
ATOM   432  C  C     . ASN A 1 57  ? 25.778  19.290  19.981  1.00 23.12  ?  57  ASN A C     1 
ATOM   433  O  O     . ASN A 1 57  ? 25.118  18.280  20.231  1.00 19.24  ?  57  ASN A O     1 
ATOM   434  C  CB    . ASN A 1 57  ? 24.208  20.736  21.330  1.00 27.78  ?  57  ASN A CB    1 
ATOM   435  C  CG    . ASN A 1 57  ? 23.322  21.982  21.299  1.00 41.75  ?  57  ASN A CG    1 
ATOM   436  O  OD1   . ASN A 1 57  ? 23.757  23.057  20.861  1.00 45.64  ?  57  ASN A OD1   1 
ATOM   437  N  ND2   . ASN A 1 57  ? 22.080  21.847  21.783  1.00 39.19  ?  57  ASN A ND2   1 
ATOM   438  N  N     . VAL A 1 58  ? 27.038  19.231  19.546  1.00 20.62  ?  58  VAL A N     1 
ATOM   439  C  CA    . VAL A 1 58  ? 27.693  17.989  19.123  1.00 21.55  ?  58  VAL A CA    1 
ATOM   440  C  C     . VAL A 1 58  ? 28.775  17.634  20.140  1.00 22.73  ?  58  VAL A C     1 
ATOM   441  O  O     . VAL A 1 58  ? 29.442  18.519  20.688  1.00 28.79  ?  58  VAL A O     1 
ATOM   442  C  CB    . VAL A 1 58  ? 28.304  18.117  17.704  1.00 24.50  ?  58  VAL A CB    1 
ATOM   443  C  CG1   . VAL A 1 58  ? 28.485  16.750  17.027  1.00 19.52  ?  58  VAL A CG1   1 
ATOM   444  C  CG2   . VAL A 1 58  ? 27.464  19.010  16.827  1.00 26.41  ?  58  VAL A CG2   1 
ATOM   445  N  N     . ARG A 1 59  ? 28.945  16.340  20.397  1.00 21.58  ?  59  ARG A N     1 
ATOM   446  C  CA    . ARG A 1 59  ? 30.008  15.845  21.263  1.00 21.49  ?  59  ARG A CA    1 
ATOM   447  C  C     . ARG A 1 59  ? 30.727  14.688  20.590  1.00 22.04  ?  59  ARG A C     1 
ATOM   448  O  O     . ARG A 1 59  ? 30.086  13.731  20.147  1.00 18.49  ?  59  ARG A O     1 
ATOM   449  C  CB    . ARG A 1 59  ? 29.463  15.376  22.596  1.00 21.26  ?  59  ARG A CB    1 
ATOM   450  C  CG    . ARG A 1 59  ? 30.562  14.983  23.551  1.00 34.10  ?  59  ARG A CG    1 
ATOM   451  C  CD    . ARG A 1 59  ? 30.000  14.581  24.894  1.00 36.71  ?  59  ARG A CD    1 
ATOM   452  N  NE    . ARG A 1 59  ? 30.654  13.385  25.413  1.00 41.29  ?  59  ARG A NE    1 
ATOM   453  C  CZ    . ARG A 1 59  ? 30.349  12.830  26.576  1.00 39.09  ?  59  ARG A CZ    1 
ATOM   454  N  NH1   . ARG A 1 59  ? 29.406  13.340  27.355  1.00 45.13  ?  59  ARG A NH1   1 
ATOM   455  N  NH2   . ARG A 1 59  ? 31.016  11.747  26.977  1.00 38.25  ?  59  ARG A NH2   1 
ATOM   456  N  N     . LEU A 1 60  ? 32.053  14.756  20.543  1.00 24.00  ?  60  LEU A N     1 
ATOM   457  C  CA    . LEU A 1 60  ? 32.858  13.708  19.930  1.00 24.87  ?  60  LEU A CA    1 
ATOM   458  C  C     . LEU A 1 60  ? 33.453  12.814  21.009  1.00 25.89  ?  60  LEU A C     1 
ATOM   459  O  O     . LEU A 1 60  ? 34.059  13.308  21.965  1.00 26.78  ?  60  LEU A O     1 
ATOM   460  C  CB    . LEU A 1 60  ? 33.970  14.303  19.064  1.00 22.94  ?  60  LEU A CB    1 
ATOM   461  C  CG    . LEU A 1 60  ? 34.909  13.255  18.444  1.00 25.57  ?  60  LEU A CG    1 
ATOM   462  C  CD1   . LEU A 1 60  ? 34.142  12.346  17.508  1.00 16.17  ?  60  LEU A CD1   1 
ATOM   463  C  CD2   . LEU A 1 60  ? 36.056  13.934  17.697  1.00 30.50  ?  60  LEU A CD2   1 
ATOM   464  N  N     . ILE A 1 61  ? 33.272  11.503  20.854  1.00 18.91  ?  61  ILE A N     1 
ATOM   465  C  CA    . ILE A 1 61  ? 33.880  10.501  21.716  1.00 17.64  ?  61  ILE A CA    1 
ATOM   466  C  C     . ILE A 1 61  ? 34.844  9.693   20.865  1.00 23.51  ?  61  ILE A C     1 
ATOM   467  O  O     . ILE A 1 61  ? 34.435  9.072   19.878  1.00 22.85  ?  61  ILE A O     1 
ATOM   468  C  CB    . ILE A 1 61  ? 32.836  9.565   22.341  1.00 22.48  ?  61  ILE A CB    1 
ATOM   469  C  CG1   . ILE A 1 61  ? 31.939  10.278  23.357  1.00 25.38  ?  61  ILE A CG1   1 
ATOM   470  C  CG2   . ILE A 1 61  ? 33.528  8.357   22.973  1.00 19.82  ?  61  ILE A CG2   1 
ATOM   471  C  CD1   . ILE A 1 61  ? 30.913  9.314   24.016  1.00 18.81  ?  61  ILE A CD1   1 
ATOM   472  N  N     . ASP A 1 62  ? 36.111  9.670   21.251  1.00 24.75  ?  62  ASP A N     1 
ATOM   473  C  CA    . ASP A 1 62  ? 37.123  8.901   20.539  1.00 24.74  ?  62  ASP A CA    1 
ATOM   474  C  C     . ASP A 1 62  ? 37.331  7.585   21.277  1.00 25.48  ?  62  ASP A C     1 
ATOM   475  O  O     . ASP A 1 62  ? 37.780  7.574   22.428  1.00 30.41  ?  62  ASP A O     1 
ATOM   476  C  CB    . ASP A 1 62  ? 38.426  9.684   20.424  1.00 25.15  ?  62  ASP A CB    1 
ATOM   477  C  CG    . ASP A 1 62  ? 38.328  10.826  19.443  1.00 34.60  ?  62  ASP A CG    1 
ATOM   478  O  OD1   . ASP A 1 62  ? 38.231  10.564  18.218  1.00 33.00  ?  62  ASP A OD1   1 
ATOM   479  O  OD2   . ASP A 1 62  ? 38.310  11.994  19.906  1.00 48.40  ?  62  ASP A OD2   1 
ATOM   480  N  N     . GLN A 1 63  ? 36.979  6.482   20.622  1.00 24.69  ?  63  GLN A N     1 
ATOM   481  C  CA    . GLN A 1 63  ? 37.237  5.170   21.194  1.00 36.01  ?  63  GLN A CA    1 
ATOM   482  C  C     . GLN A 1 63  ? 38.742  4.907   21.193  1.00 31.35  ?  63  GLN A C     1 
ATOM   483  O  O     . GLN A 1 63  ? 39.423  5.215   20.208  1.00 24.16  ?  63  GLN A O     1 
ATOM   484  C  CB    . GLN A 1 63  ? 36.519  4.066   20.408  1.00 26.95  ?  63  GLN A CB    1 
ATOM   485  C  CG    . GLN A 1 63  ? 35.010  4.120   20.433  1.00 18.46  ?  63  GLN A CG    1 
ATOM   486  C  CD    . GLN A 1 63  ? 34.460  4.042   21.824  1.00 32.83  ?  63  GLN A CD    1 
ATOM   487  O  OE1   . GLN A 1 63  ? 34.312  5.068   22.498  1.00 36.21  ?  63  GLN A OE1   1 
ATOM   488  N  NE2   . GLN A 1 63  ? 34.148  2.817   22.279  1.00 29.97  ?  63  GLN A NE2   1 
ATOM   489  N  N     . PRO A 1 64  ? 39.287  4.360   22.285  1.00 32.27  ?  64  PRO A N     1 
ATOM   490  C  CA    . PRO A 1 64  ? 40.720  4.042   22.329  1.00 27.38  ?  64  PRO A CA    1 
ATOM   491  C  C     . PRO A 1 64  ? 41.082  2.752   21.616  1.00 32.01  ?  64  PRO A C     1 
ATOM   492  O  O     . PRO A 1 64  ? 42.271  2.428   21.516  1.00 33.08  ?  64  PRO A O     1 
ATOM   493  C  CB    . PRO A 1 64  ? 41.004  3.944   23.834  1.00 30.34  ?  64  PRO A CB    1 
ATOM   494  C  CG    . PRO A 1 64  ? 39.692  3.573   24.457  1.00 24.01  ?  64  PRO A CG    1 
ATOM   495  C  CD    . PRO A 1 64  ? 38.602  4.117   23.572  1.00 23.53  ?  64  PRO A CD    1 
ATOM   496  N  N     . SER A 1 65  ? 40.093  2.015   21.125  1.00 29.95  ?  65  SER A N     1 
ATOM   497  C  CA    . SER A 1 65  ? 40.338  0.837   20.309  1.00 33.21  ?  65  SER A CA    1 
ATOM   498  C  C     . SER A 1 65  ? 39.098  0.592   19.466  1.00 32.68  ?  65  SER A C     1 
ATOM   499  O  O     . SER A 1 65  ? 38.016  1.110   19.758  1.00 25.42  ?  65  SER A O     1 
ATOM   500  C  CB    . SER A 1 65  ? 40.667  -0.385  21.163  1.00 30.32  ?  65  SER A CB    1 
ATOM   501  O  OG    . SER A 1 65  ? 39.514  -0.826  21.859  1.00 43.47  ?  65  SER A OG    1 
ATOM   502  N  N     . GLN A 1 66  ? 39.274  -0.187  18.399  1.00 31.44  ?  66  GLN A N     1 
ATOM   503  C  CA    . GLN A 1 66  ? 38.155  -0.520  17.530  1.00 27.04  ?  66  GLN A CA    1 
ATOM   504  C  C     . GLN A 1 66  ? 37.356  -1.636  18.182  1.00 34.32  ?  66  GLN A C     1 
ATOM   505  O  O     . GLN A 1 66  ? 37.838  -2.767  18.308  1.00 42.87  ?  66  GLN A O     1 
ATOM   506  C  CB    . GLN A 1 66  ? 38.622  -0.922  16.141  1.00 25.19  ?  66  GLN A CB    1 
ATOM   507  C  CG    . GLN A 1 66  ? 37.532  -0.704  15.138  1.00 29.42  ?  66  GLN A CG    1 
ATOM   508  C  CD    . GLN A 1 66  ? 37.547  -1.715  14.028  1.00 35.59  ?  66  GLN A CD    1 
ATOM   509  O  OE1   . GLN A 1 66  ? 38.379  -1.647  13.123  1.00 42.70  ?  66  GLN A OE1   1 
ATOM   510  N  NE2   . GLN A 1 66  ? 36.613  -2.661  14.077  1.00 43.72  ?  66  GLN A NE2   1 
ATOM   511  N  N     . SER A 1 67  ? 36.132  -1.313  18.598  1.00 23.99  ?  67  SER A N     1 
ATOM   512  C  CA    . SER A 1 67  ? 35.286  -2.229  19.338  1.00 26.07  ?  67  SER A CA    1 
ATOM   513  C  C     . SER A 1 67  ? 34.131  -2.784  18.518  1.00 25.67  ?  67  SER A C     1 
ATOM   514  O  O     . SER A 1 67  ? 33.484  -3.733  18.962  1.00 34.15  ?  67  SER A O     1 
ATOM   515  C  CB    . SER A 1 67  ? 34.730  -1.518  20.585  1.00 30.26  ?  67  SER A CB    1 
ATOM   516  O  OG    . SER A 1 67  ? 34.277  -0.207  20.258  1.00 28.42  ?  67  SER A OG    1 
ATOM   517  N  N     . GLY A 1 68  ? 33.838  -2.214  17.355  1.00 25.23  ?  68  GLY A N     1 
ATOM   518  C  CA    . GLY A 1 68  ? 32.705  -2.647  16.577  1.00 20.21  ?  68  GLY A CA    1 
ATOM   519  C  C     . GLY A 1 68  ? 31.537  -1.691  16.701  1.00 22.52  ?  68  GLY A C     1 
ATOM   520  O  O     . GLY A 1 68  ? 31.502  -0.812  17.576  1.00 19.28  ?  68  GLY A O     1 
ATOM   521  N  N     . PRO A 1 69  ? 30.545  -1.851  15.824  1.00 20.38  ?  69  PRO A N     1 
ATOM   522  C  CA    . PRO A 1 69  ? 29.359  -0.982  15.905  1.00 18.08  ?  69  PRO A CA    1 
ATOM   523  C  C     . PRO A 1 69  ? 28.586  -1.157  17.206  1.00 22.98  ?  69  PRO A C     1 
ATOM   524  O  O     . PRO A 1 69  ? 27.964  -0.194  17.686  1.00 20.24  ?  69  PRO A O     1 
ATOM   525  C  CB    . PRO A 1 69  ? 28.537  -1.396  14.676  1.00 18.31  ?  69  PRO A CB    1 
ATOM   526  C  CG    . PRO A 1 69  ? 29.026  -2.782  14.320  1.00 19.47  ?  69  PRO A CG    1 
ATOM   527  C  CD    . PRO A 1 69  ? 30.446  -2.869  14.764  1.00 18.60  ?  69  PRO A CD    1 
ATOM   528  N  N     . SER A 1 70  ? 28.620  -2.354  17.801  1.00 16.88  ?  70  SER A N     1 
ATOM   529  C  CA    . SER A 1 70  ? 28.016  -2.542  19.118  1.00 20.47  ?  70  SER A CA    1 
ATOM   530  C  C     . SER A 1 70  ? 28.731  -1.705  20.171  1.00 21.94  ?  70  SER A C     1 
ATOM   531  O  O     . SER A 1 70  ? 28.100  -0.922  20.890  1.00 20.90  ?  70  SER A O     1 
ATOM   532  C  CB    . SER A 1 70  ? 28.043  -4.019  19.495  1.00 20.30  ?  70  SER A CB    1 
ATOM   533  O  OG    . SER A 1 70  ? 27.105  -4.739  18.711  1.00 19.85  ?  70  SER A OG    1 
ATOM   534  N  N     . GLY A 1 71  ? 30.056  -1.844  20.266  1.00 19.70  ?  71  GLY A N     1 
ATOM   535  C  CA    . GLY A 1 71  ? 30.795  -1.093  21.269  1.00 21.59  ?  71  GLY A CA    1 
ATOM   536  C  C     . GLY A 1 71  ? 30.636  0.408   21.121  1.00 21.57  ?  71  GLY A C     1 
ATOM   537  O  O     . GLY A 1 71  ? 30.494  1.131   22.115  1.00 22.71  ?  71  GLY A O     1 
ATOM   538  N  N     . ALA A 1 72  ? 30.635  0.896   19.881  1.00 18.99  ?  72  ALA A N     1 
ATOM   539  C  CA    . ALA A 1 72  ? 30.619  2.340   19.653  1.00 16.39  ?  72  ALA A CA    1 
ATOM   540  C  C     . ALA A 1 72  ? 29.245  2.936   19.941  1.00 18.02  ?  72  ALA A C     1 
ATOM   541  O  O     . ALA A 1 72  ? 29.143  4.073   20.420  1.00 17.69  ?  72  ALA A O     1 
ATOM   542  C  CB    . ALA A 1 72  ? 31.048  2.644   18.220  1.00 17.71  ?  72  ALA A CB    1 
ATOM   543  N  N     . ARG A 1 73  ? 28.175  2.198   19.641  1.00 18.52  ?  73  ARG A N     1 
ATOM   544  C  CA    . ARG A 1 73  ? 26.850  2.700   19.973  1.00 17.61  ?  73  ARG A CA    1 
ATOM   545  C  C     . ARG A 1 73  ? 26.655  2.734   21.483  1.00 19.03  ?  73  ARG A C     1 
ATOM   546  O  O     . ARG A 1 73  ? 26.037  3.664   22.008  1.00 17.82  ?  73  ARG A O     1 
ATOM   547  C  CB    . ARG A 1 73  ? 25.769  1.857   19.296  1.00 19.43  ?  73  ARG A CB    1 
ATOM   548  C  CG    . ARG A 1 73  ? 25.581  2.158   17.809  1.00 18.35  ?  73  ARG A CG    1 
ATOM   549  C  CD    . ARG A 1 73  ? 24.294  1.545   17.246  1.00 18.29  ?  73  ARG A CD    1 
ATOM   550  N  NE    . ARG A 1 73  ? 24.364  1.372   15.802  1.00 19.38  ?  73  ARG A NE    1 
ATOM   551  C  CZ    . ARG A 1 73  ? 24.650  0.225   15.194  1.00 21.06  ?  73  ARG A CZ    1 
ATOM   552  N  NH1   . ARG A 1 73  ? 24.850  -0.890  15.877  1.00 17.68  ?  73  ARG A NH1   1 
ATOM   553  N  NH2   . ARG A 1 73  ? 24.740  0.199   13.864  1.00 20.13  ?  73  ARG A NH2   1 
ATOM   554  N  N     . ASN A 1 74  ? 27.211  1.750   22.201  1.00 20.92  ?  74  ASN A N     1 
ATOM   555  C  CA    . ASN A 1 74  ? 27.103  1.743   23.659  1.00 21.77  ?  74  ASN A CA    1 
ATOM   556  C  C     . ASN A 1 74  ? 27.808  2.944   24.260  1.00 19.82  ?  74  ASN A C     1 
ATOM   557  O  O     . ASN A 1 74  ? 27.276  3.583   25.177  1.00 22.39  ?  74  ASN A O     1 
ATOM   558  C  CB    . ASN A 1 74  ? 27.685  0.455   24.241  1.00 16.29  ?  74  ASN A CB    1 
ATOM   559  C  CG    . ASN A 1 74  ? 26.807  -0.720  23.996  1.00 19.09  ?  74  ASN A CG    1 
ATOM   560  O  OD1   . ASN A 1 74  ? 25.698  -0.569  23.490  1.00 20.84  ?  74  ASN A OD1   1 
ATOM   561  N  ND2   . ASN A 1 74  ? 27.292  -1.911  24.326  1.00 19.25  ?  74  ASN A ND2   1 
ATOM   562  N  N     . ALA A 1 75  ? 29.018  3.244   23.771  1.00 14.46  ?  75  ALA A N     1 
ATOM   563  C  CA    . ALA A 1 75  ? 29.727  4.460   24.169  1.00 20.42  ?  75  ALA A CA    1 
ATOM   564  C  C     . ALA A 1 75  ? 28.818  5.677   24.098  1.00 17.97  ?  75  ALA A C     1 
ATOM   565  O  O     . ALA A 1 75  ? 28.838  6.528   24.986  1.00 18.72  ?  75  ALA A O     1 
ATOM   566  C  CB    . ALA A 1 75  ? 30.964  4.681   23.290  1.00 15.17  ?  75  ALA A CB    1 
ATOM   567  N  N     . GLY A 1 76  ? 27.994  5.759   23.058  1.00 17.57  ?  76  GLY A N     1 
ATOM   568  C  CA    . GLY A 1 76  ? 27.064  6.865   22.945  1.00 16.88  ?  76  GLY A CA    1 
ATOM   569  C  C     . GLY A 1 76  ? 25.883  6.739   23.885  1.00 18.00  ?  76  GLY A C     1 
ATOM   570  O  O     . GLY A 1 76  ? 25.448  7.730   24.478  1.00 20.02  ?  76  GLY A O     1 
ATOM   571  N  N     . LEU A 1 77  ? 25.347  5.522   24.030  1.00 20.34  ?  77  LEU A N     1 
ATOM   572  C  CA    . LEU A 1 77  ? 24.184  5.308   24.898  1.00 24.05  ?  77  LEU A CA    1 
ATOM   573  C  C     . LEU A 1 77  ? 24.481  5.674   26.349  1.00 23.32  ?  77  LEU A C     1 
ATOM   574  O  O     . LEU A 1 77  ? 23.609  6.190   27.065  1.00 26.42  ?  77  LEU A O     1 
ATOM   575  C  CB    . LEU A 1 77  ? 23.727  3.849   24.827  1.00 23.60  ?  77  LEU A CB    1 
ATOM   576  C  CG    . LEU A 1 77  ? 23.119  3.285   23.538  1.00 24.26  ?  77  LEU A CG    1 
ATOM   577  C  CD1   . LEU A 1 77  ? 22.984  1.770   23.665  1.00 16.82  ?  77  LEU A CD1   1 
ATOM   578  C  CD2   . LEU A 1 77  ? 21.763  3.935   23.257  1.00 20.08  ?  77  LEU A CD2   1 
ATOM   579  N  N     . GLU A 1 78  ? 25.698  5.370   26.807  1.00 24.24  ?  78  GLU A N     1 
ATOM   580  C  CA    . GLU A 1 78  ? 26.080  5.608   28.194  1.00 27.30  ?  78  GLU A CA    1 
ATOM   581  C  C     . GLU A 1 78  ? 26.052  7.087   28.551  1.00 25.94  ?  78  GLU A C     1 
ATOM   582  O  O     . GLU A 1 78  ? 25.768  7.440   29.699  1.00 32.51  ?  78  GLU A O     1 
ATOM   583  C  CB    . GLU A 1 78  ? 27.475  5.044   28.445  1.00 27.07  ?  78  GLU A CB    1 
ATOM   584  C  CG    . GLU A 1 78  ? 27.525  3.544   28.538  1.00 30.64  ?  78  GLU A CG    1 
ATOM   585  C  CD    . GLU A 1 78  ? 28.937  3.036   28.744  1.00 46.33  ?  78  GLU A CD    1 
ATOM   586  O  OE1   . GLU A 1 78  ? 29.823  3.848   29.112  1.00 47.67  ?  78  GLU A OE1   1 
ATOM   587  O  OE2   . GLU A 1 78  ? 29.160  1.824   28.531  1.00 48.59  ?  78  GLU A OE2   1 
ATOM   588  N  N     . VAL A 1 79  ? 26.337  7.962   27.591  1.00 24.13  ?  79  VAL A N     1 
ATOM   589  C  CA    . VAL A 1 79  ? 26.429  9.398   27.842  1.00 26.45  ?  79  VAL A CA    1 
ATOM   590  C  C     . VAL A 1 79  ? 25.213  10.167  27.333  1.00 21.12  ?  79  VAL A C     1 
ATOM   591  O  O     . VAL A 1 79  ? 25.153  11.388  27.514  1.00 22.43  ?  79  VAL A O     1 
ATOM   592  C  CB    . VAL A 1 79  ? 27.726  9.983   27.240  1.00 28.11  ?  79  VAL A CB    1 
ATOM   593  C  CG1   . VAL A 1 79  ? 28.972  9.294   27.821  1.00 28.02  ?  79  VAL A CG1   1 
ATOM   594  C  CG2   . VAL A 1 79  ? 27.725  9.880   25.711  1.00 23.07  ?  79  VAL A CG2   1 
ATOM   595  N  N     . ALA A 1 80  ? 24.246  9.501   26.706  1.00 21.71  ?  80  ALA A N     1 
ATOM   596  C  CA    . ALA A 1 80  ? 23.112  10.198  26.106  1.00 22.27  ?  80  ALA A CA    1 
ATOM   597  C  C     . ALA A 1 80  ? 22.184  10.781  27.169  1.00 22.41  ?  80  ALA A C     1 
ATOM   598  O  O     . ALA A 1 80  ? 21.679  10.051  28.030  1.00 19.98  ?  80  ALA A O     1 
ATOM   599  C  CB    . ALA A 1 80  ? 22.325  9.244   25.204  1.00 21.30  ?  80  ALA A CB    1 
ATOM   600  N  N     . ARG A 1 81  ? 21.924  12.094  27.066  1.00 22.49  ?  81  ARG A N     1 
ATOM   601  C  CA    . ARG A 1 81  ? 21.069  12.846  27.984  1.00 22.49  ?  81  ARG A CA    1 
ATOM   602  C  C     . ARG A 1 81  ? 19.601  12.833  27.587  1.00 19.28  ?  81  ARG A C     1 
ATOM   603  O  O     . ARG A 1 81  ? 18.735  13.012  28.454  1.00 24.07  ?  81  ARG A O     1 
ATOM   604  C  CB    . ARG A 1 81  ? 21.503  14.319  28.061  1.00 25.70  ?  81  ARG A CB    1 
ATOM   605  C  CG    . ARG A 1 81  ? 22.958  14.588  28.421  1.00 33.30  ?  81  ARG A CG    1 
ATOM   606  C  CD    . ARG A 1 81  ? 23.214  16.112  28.598  1.00 39.07  ?  81  ARG A CD    1 
ATOM   607  N  NE    . ARG A 1 81  ? 23.323  16.834  27.329  1.00 36.44  ?  81  ARG A NE    1 
ATOM   608  C  CZ    . ARG A 1 81  ? 24.424  17.439  26.885  1.00 42.57  ?  81  ARG A CZ    1 
ATOM   609  N  NH1   . ARG A 1 81  ? 25.546  17.444  27.588  1.00 41.14  ?  81  ARG A NH1   1 
ATOM   610  N  NH2   . ARG A 1 81  ? 24.401  18.048  25.699  1.00 27.64  ?  81  ARG A NH2   1 
ATOM   611  N  N     . GLY A 1 82  ? 19.304  12.646  26.304  1.00 15.90  ?  82  GLY A N     1 
ATOM   612  C  CA    . GLY A 1 82  ? 17.933  12.760  25.830  1.00 15.25  ?  82  GLY A CA    1 
ATOM   613  C  C     . GLY A 1 82  ? 17.008  11.699  26.412  1.00 17.85  ?  82  GLY A C     1 
ATOM   614  O  O     . GLY A 1 82  ? 17.394  10.548  26.623  1.00 17.34  ?  82  GLY A O     1 
ATOM   615  N  N     . GLU A 1 83  ? 15.757  12.106  26.666  1.00 17.91  ?  83  GLU A N     1 
ATOM   616  C  CA    . GLU A 1 83  ? 14.693  11.151  26.967  1.00 13.47  ?  83  GLU A CA    1 
ATOM   617  C  C     . GLU A 1 83  ? 14.560  10.099  25.874  1.00 14.40  ?  83  GLU A C     1 
ATOM   618  O  O     . GLU A 1 83  ? 14.259  8.928   26.154  1.00 12.36  ?  83  GLU A O     1 
ATOM   619  C  CB    . GLU A 1 83  ? 13.366  11.893  27.138  1.00 17.14  ?  83  GLU A CB    1 
ATOM   620  C  CG    . GLU A 1 83  ? 12.165  10.956  27.252  1.00 15.14  ?  83  GLU A CG    1 
ATOM   621  C  CD    . GLU A 1 83  ? 10.905  11.650  27.729  1.00 19.05  ?  83  GLU A CD    1 
ATOM   622  O  OE1   . GLU A 1 83  ? 10.818  12.906  27.616  1.00 17.36  ?  83  GLU A OE1   1 
ATOM   623  O  OE2   . GLU A 1 83  ? 9.998   10.931  28.226  1.00 15.57  ?  83  GLU A OE2   1 
ATOM   624  N  N     . TYR A 1 84  ? 14.772  10.505  24.620  1.00 11.02  ?  84  TYR A N     1 
ATOM   625  C  CA    . TYR A 1 84  ? 14.712  9.628   23.462  1.00 12.35  ?  84  TYR A CA    1 
ATOM   626  C  C     . TYR A 1 84  ? 16.040  9.653   22.725  1.00 14.65  ?  84  TYR A C     1 
ATOM   627  O  O     . TYR A 1 84  ? 16.739  10.667  22.703  1.00 13.45  ?  84  TYR A O     1 
ATOM   628  C  CB    . TYR A 1 84  ? 13.571  10.029  22.519  1.00 8.93   ?  84  TYR A CB    1 
ATOM   629  C  CG    . TYR A 1 84  ? 12.273  10.101  23.260  1.00 15.20  ?  84  TYR A CG    1 
ATOM   630  C  CD1   . TYR A 1 84  ? 11.657  8.938   23.706  1.00 12.78  ?  84  TYR A CD1   1 
ATOM   631  C  CD2   . TYR A 1 84  ? 11.679  11.318  23.557  1.00 15.84  ?  84  TYR A CD2   1 
ATOM   632  C  CE1   . TYR A 1 84  ? 10.506  8.969   24.382  1.00 11.13  ?  84  TYR A CE1   1 
ATOM   633  C  CE2   . TYR A 1 84  ? 10.499  11.359  24.262  1.00 17.12  ?  84  TYR A CE2   1 
ATOM   634  C  CZ    . TYR A 1 84  ? 9.923   10.173  24.673  1.00 14.75  ?  84  TYR A CZ    1 
ATOM   635  O  OH    . TYR A 1 84  ? 8.742   10.159  25.375  1.00 17.49  ?  84  TYR A OH    1 
ATOM   636  N  N     . VAL A 1 85  ? 16.395  8.519   22.135  1.00 16.28  ?  85  VAL A N     1 
ATOM   637  C  CA    . VAL A 1 85  ? 17.628  8.384   21.377  1.00 13.54  ?  85  VAL A CA    1 
ATOM   638  C  C     . VAL A 1 85  ? 17.243  8.047   19.951  1.00 13.52  ?  85  VAL A C     1 
ATOM   639  O  O     . VAL A 1 85  ? 16.311  7.272   19.723  1.00 12.17  ?  85  VAL A O     1 
ATOM   640  C  CB    . VAL A 1 85  ? 18.558  7.304   21.969  1.00 14.35  ?  85  VAL A CB    1 
ATOM   641  C  CG1   . VAL A 1 85  ? 19.462  6.721   20.911  1.00 17.06  ?  85  VAL A CG1   1 
ATOM   642  C  CG2   . VAL A 1 85  ? 19.384  7.874   23.102  1.00 15.48  ?  85  VAL A CG2   1 
ATOM   643  N  N     . ALA A 1 86  ? 17.932  8.663   18.996  1.00 13.30  ?  86  ALA A N     1 
ATOM   644  C  CA    . ALA A 1 86  ? 17.771  8.365   17.584  1.00 14.56  ?  86  ALA A CA    1 
ATOM   645  C  C     . ALA A 1 86  ? 19.125  7.930   17.050  1.00 13.97  ?  86  ALA A C     1 
ATOM   646  O  O     . ALA A 1 86  ? 20.097  8.681   17.131  1.00 18.10  ?  86  ALA A O     1 
ATOM   647  C  CB    . ALA A 1 86  ? 17.253  9.583   16.813  1.00 16.87  ?  86  ALA A CB    1 
ATOM   648  N  N     . PHE A 1 87  ? 19.188  6.727   16.503  1.00 15.07  ?  87  PHE A N     1 
ATOM   649  C  CA    . PHE A 1 87  ? 20.431  6.254   15.918  1.00 15.37  ?  87  PHE A CA    1 
ATOM   650  C  C     . PHE A 1 87  ? 20.559  6.740   14.482  1.00 13.68  ?  87  PHE A C     1 
ATOM   651  O  O     . PHE A 1 87  ? 19.568  6.882   13.757  1.00 17.67  ?  87  PHE A O     1 
ATOM   652  C  CB    . PHE A 1 87  ? 20.493  4.728   15.961  1.00 16.08  ?  87  PHE A CB    1 
ATOM   653  C  CG    . PHE A 1 87  ? 20.421  4.159   17.347  1.00 12.10  ?  87  PHE A CG    1 
ATOM   654  C  CD1   . PHE A 1 87  ? 21.567  4.039   18.120  1.00 15.28  ?  87  PHE A CD1   1 
ATOM   655  C  CD2   . PHE A 1 87  ? 19.220  3.726   17.865  1.00 14.41  ?  87  PHE A CD2   1 
ATOM   656  C  CE1   . PHE A 1 87  ? 21.514  3.500   19.397  1.00 17.51  ?  87  PHE A CE1   1 
ATOM   657  C  CE2   . PHE A 1 87  ? 19.150  3.188   19.155  1.00 19.38  ?  87  PHE A CE2   1 
ATOM   658  C  CZ    . PHE A 1 87  ? 20.305  3.074   19.919  1.00 17.46  ?  87  PHE A CZ    1 
ATOM   659  N  N     . LEU A 1 88  ? 21.791  7.020   14.079  1.00 11.95  ?  88  LEU A N     1 
ATOM   660  C  CA    . LEU A 1 88  ? 22.077  7.346   12.687  1.00 15.53  ?  88  LEU A CA    1 
ATOM   661  C  C     . LEU A 1 88  ? 23.435  6.746   12.356  1.00 15.25  ?  88  LEU A C     1 
ATOM   662  O  O     . LEU A 1 88  ? 24.441  7.134   12.961  1.00 18.42  ?  88  LEU A O     1 
ATOM   663  C  CB    . LEU A 1 88  ? 22.057  8.860   12.456  1.00 16.82  ?  88  LEU A CB    1 
ATOM   664  C  CG    . LEU A 1 88  ? 22.224  9.340   11.009  1.00 14.39  ?  88  LEU A CG    1 
ATOM   665  C  CD1   . LEU A 1 88  ? 21.303  8.565   10.095  1.00 15.00  ?  88  LEU A CD1   1 
ATOM   666  C  CD2   . LEU A 1 88  ? 21.941  10.826  10.923  1.00 13.82  ?  88  LEU A CD2   1 
ATOM   667  N  N     . ASP A 1 89  ? 23.454  5.764   11.450  1.00 14.67  ?  89  ASP A N     1 
ATOM   668  C  CA    . ASP A 1 89  ? 24.715  5.248   10.917  1.00 18.35  ?  89  ASP A CA    1 
ATOM   669  C  C     . ASP A 1 89  ? 25.338  6.262   9.954   1.00 15.90  ?  89  ASP A C     1 
ATOM   670  O  O     . ASP A 1 89  ? 24.625  6.936   9.207   1.00 16.63  ?  89  ASP A O     1 
ATOM   671  C  CB    . ASP A 1 89  ? 24.481  3.917   10.199  1.00 18.16  ?  89  ASP A CB    1 
ATOM   672  C  CG    . ASP A 1 89  ? 24.052  2.789   11.156  1.00 19.93  ?  89  ASP A CG    1 
ATOM   673  O  OD1   . ASP A 1 89  ? 24.141  2.954   12.400  1.00 21.48  ?  89  ASP A OD1   1 
ATOM   674  O  OD2   . ASP A 1 89  ? 23.606  1.735   10.653  1.00 23.03  ?  89  ASP A OD2   1 
ATOM   675  N  N     . ASP A 1 90  ? 26.676  6.355   9.947   1.00 15.96  ?  90  ASP A N     1 
ATOM   676  C  CA    . ASP A 1 90  ? 27.332  7.460   9.235   1.00 18.59  ?  90  ASP A CA    1 
ATOM   677  C  C     . ASP A 1 90  ? 27.106  7.463   7.720   1.00 17.00  ?  90  ASP A C     1 
ATOM   678  O  O     . ASP A 1 90  ? 27.450  8.465   7.075   1.00 18.14  ?  90  ASP A O     1 
ATOM   679  C  CB    . ASP A 1 90  ? 28.848  7.495   9.491   1.00 16.35  ?  90  ASP A CB    1 
ATOM   680  C  CG    . ASP A 1 90  ? 29.553  6.199   9.122   1.00 20.83  ?  90  ASP A CG    1 
ATOM   681  O  OD1   . ASP A 1 90  ? 29.022  5.425   8.296   1.00 20.77  ?  90  ASP A OD1   1 
ATOM   682  O  OD2   . ASP A 1 90  ? 30.679  5.972   9.640   1.00 20.63  ?  90  ASP A OD2   1 
ATOM   683  N  N     . ASP A 1 91  ? 26.534  6.409   7.130   1.00 13.48  ?  91  ASP A N     1 
ATOM   684  C  CA    . ASP A 1 91  ? 26.287  6.375   5.691   1.00 16.07  ?  91  ASP A CA    1 
ATOM   685  C  C     . ASP A 1 91  ? 24.806  6.436   5.314   1.00 17.48  ?  91  ASP A C     1 
ATOM   686  O  O     . ASP A 1 91  ? 24.471  6.235   4.141   1.00 17.15  ?  91  ASP A O     1 
ATOM   687  C  CB    . ASP A 1 91  ? 26.945  5.136   5.058   1.00 19.83  ?  91  ASP A CB    1 
ATOM   688  C  CG    . ASP A 1 91  ? 26.474  3.827   5.674   1.00 21.68  ?  91  ASP A CG    1 
ATOM   689  O  OD1   . ASP A 1 91  ? 25.749  3.858   6.693   1.00 19.37  ?  91  ASP A OD1   1 
ATOM   690  O  OD2   . ASP A 1 91  ? 26.852  2.757   5.138   1.00 23.54  ?  91  ASP A OD2   1 
ATOM   691  N  N     . ASP A 1 92  ? 23.911  6.712   6.263   1.00 15.65  ?  92  ASP A N     1 
ATOM   692  C  CA    . ASP A 1 92  ? 22.500  6.949   5.978   1.00 15.08  ?  92  ASP A CA    1 
ATOM   693  C  C     . ASP A 1 92  ? 22.197  8.439   6.169   1.00 17.63  ?  92  ASP A C     1 
ATOM   694  O  O     . ASP A 1 92  ? 23.073  9.222   6.552   1.00 15.96  ?  92  ASP A O     1 
ATOM   695  C  CB    . ASP A 1 92  ? 21.627  6.063   6.866   1.00 17.53  ?  92  ASP A CB    1 
ATOM   696  C  CG    . ASP A 1 92  ? 22.025  4.580   6.775   1.00 25.89  ?  92  ASP A CG    1 
ATOM   697  O  OD1   . ASP A 1 92  ? 22.382  4.109   5.668   1.00 17.16  ?  92  ASP A OD1   1 
ATOM   698  O  OD2   . ASP A 1 92  ? 22.010  3.895   7.820   1.00 24.16  ?  92  ASP A OD2   1 
ATOM   699  N  N     . VAL A 1 93  ? 20.954  8.840   5.884   1.00 15.24  ?  93  VAL A N     1 
ATOM   700  C  CA    . VAL A 1 93  ? 20.515  10.209  6.158   1.00 16.68  ?  93  VAL A CA    1 
ATOM   701  C  C     . VAL A 1 93  ? 19.087  10.222  6.699   1.00 12.21  ?  93  VAL A C     1 
ATOM   702  O  O     . VAL A 1 93  ? 18.243  9.419   6.291   1.00 13.21  ?  93  VAL A O     1 
ATOM   703  C  CB    . VAL A 1 93  ? 20.610  11.103  4.908   1.00 16.76  ?  93  VAL A CB    1 
ATOM   704  C  CG1   . VAL A 1 93  ? 22.070  11.385  4.569   1.00 16.27  ?  93  VAL A CG1   1 
ATOM   705  C  CG2   . VAL A 1 93  ? 19.896  10.458  3.745   1.00 18.44  ?  93  VAL A CG2   1 
ATOM   706  N  N     . PHE A 1 94  ? 18.823  11.161  7.607   1.00 17.62  ?  94  PHE A N     1 
ATOM   707  C  CA    . PHE A 1 94  ? 17.474  11.501  8.044   1.00 14.71  ?  94  PHE A CA    1 
ATOM   708  C  C     . PHE A 1 94  ? 16.754  12.345  6.995   1.00 17.60  ?  94  PHE A C     1 
ATOM   709  O  O     . PHE A 1 94  ? 17.363  13.179  6.314   1.00 15.62  ?  94  PHE A O     1 
ATOM   710  C  CB    . PHE A 1 94  ? 17.513  12.315  9.344   1.00 14.20  ?  94  PHE A CB    1 
ATOM   711  C  CG    . PHE A 1 94  ? 17.928  11.538  10.557  1.00 13.22  ?  94  PHE A CG    1 
ATOM   712  C  CD1   . PHE A 1 94  ? 17.812  10.164  10.593  1.00 10.24  ?  94  PHE A CD1   1 
ATOM   713  C  CD2   . PHE A 1 94  ? 18.436  12.202  11.671  1.00 14.09  ?  94  PHE A CD2   1 
ATOM   714  C  CE1   . PHE A 1 94  ? 18.201  9.447   11.719  1.00 13.40  ?  94  PHE A CE1   1 
ATOM   715  C  CE2   . PHE A 1 94  ? 18.835  11.503  12.803  1.00 14.95  ?  94  PHE A CE2   1 
ATOM   716  C  CZ    . PHE A 1 94  ? 18.701  10.115  12.835  1.00 16.41  ?  94  PHE A CZ    1 
ATOM   717  N  N     . SER A 1 95  ? 15.438  12.163  6.904   1.00 13.71  ?  95  SER A N     1 
ATOM   718  C  CA    . SER A 1 95  ? 14.603  13.183  6.284   1.00 18.17  ?  95  SER A CA    1 
ATOM   719  C  C     . SER A 1 95  ? 14.319  14.301  7.293   1.00 20.25  ?  95  SER A C     1 
ATOM   720  O  O     . SER A 1 95  ? 14.412  14.087  8.509   1.00 15.33  ?  95  SER A O     1 
ATOM   721  C  CB    . SER A 1 95  ? 13.300  12.566  5.789   1.00 20.09  ?  95  SER A CB    1 
ATOM   722  O  OG    . SER A 1 95  ? 12.314  12.585  6.814   1.00 22.81  ?  95  SER A OG    1 
ATOM   723  N  N     . PRO A 1 96  ? 14.000  15.518  6.822   1.00 19.14  ?  96  PRO A N     1 
ATOM   724  C  CA    . PRO A 1 96  ? 13.755  16.619  7.778   1.00 22.36  ?  96  PRO A CA    1 
ATOM   725  C  C     . PRO A 1 96  ? 12.633  16.335  8.763   1.00 14.63  ?  96  PRO A C     1 
ATOM   726  O  O     . PRO A 1 96  ? 12.596  16.967  9.825   1.00 19.05  ?  96  PRO A O     1 
ATOM   727  C  CB    . PRO A 1 96  ? 13.424  17.824  6.870   1.00 15.80  ?  96  PRO A CB    1 
ATOM   728  C  CG    . PRO A 1 96  ? 14.099  17.487  5.573   1.00 21.77  ?  96  PRO A CG    1 
ATOM   729  C  CD    . PRO A 1 96  ? 13.964  15.991  5.427   1.00 15.23  ?  96  PRO A CD    1 
ATOM   730  N  N     . GLN A 1 97  ? 11.735  15.403  8.458   1.00 18.53  ?  97  GLN A N     1 
ATOM   731  C  CA    . GLN A 1 97  ? 10.615  15.058  9.335   1.00 21.23  ?  97  GLN A CA    1 
ATOM   732  C  C     . GLN A 1 97  ? 10.940  13.934  10.313  1.00 18.15  ?  97  GLN A C     1 
ATOM   733  O  O     . GLN A 1 97  ? 10.016  13.406  10.952  1.00 19.47  ?  97  GLN A O     1 
ATOM   734  C  CB    . GLN A 1 97  ? 9.393   14.652  8.501   1.00 19.44  ?  97  GLN A CB    1 
ATOM   735  C  CG    . GLN A 1 97  ? 8.732   15.802  7.744   1.00 25.47  ?  97  GLN A CG    1 
ATOM   736  C  CD    . GLN A 1 97  ? 9.500   16.208  6.490   1.00 19.56  ?  97  GLN A CD    1 
ATOM   737  O  OE1   . GLN A 1 97  ? 10.168  15.390  5.861   1.00 30.26  ?  97  GLN A OE1   1 
ATOM   738  N  NE2   . GLN A 1 97  ? 9.367   17.459  6.102   1.00 31.52  ?  97  GLN A NE2   1 
ATOM   739  N  N     . HIS A 1 98  ? 12.218  13.567  10.464  1.00 16.78  ?  98  HIS A N     1 
ATOM   740  C  CA    . HIS A 1 98  ? 12.550  12.369  11.229  1.00 15.94  ?  98  HIS A CA    1 
ATOM   741  C  C     . HIS A 1 98  ? 12.035  12.460  12.663  1.00 15.93  ?  98  HIS A C     1 
ATOM   742  O  O     . HIS A 1 98  ? 11.472  11.495  13.189  1.00 13.57  ?  98  HIS A O     1 
ATOM   743  C  CB    . HIS A 1 98  ? 14.056  12.121  11.219  1.00 13.10  ?  98  HIS A CB    1 
ATOM   744  C  CG    . HIS A 1 98  ? 14.442  10.726  11.612  1.00 12.25  ?  98  HIS A CG    1 
ATOM   745  N  ND1   . HIS A 1 98  ? 14.144  9.620   10.842  1.00 14.55  ?  98  HIS A ND1   1 
ATOM   746  C  CD2   . HIS A 1 98  ? 15.115  10.258  12.689  1.00 13.21  ?  98  HIS A CD2   1 
ATOM   747  C  CE1   . HIS A 1 98  ? 14.624  8.535   11.422  1.00 12.74  ?  98  HIS A CE1   1 
ATOM   748  N  NE2   . HIS A 1 98  ? 15.206  8.892   12.551  1.00 15.01  ?  98  HIS A NE2   1 
ATOM   749  N  N     . LEU A 1 99  ? 12.237  13.606  13.319  1.00 14.91  ?  99  LEU A N     1 
ATOM   750  C  CA    . LEU A 1 99  ? 11.847  13.712  14.718  1.00 14.87  ?  99  LEU A CA    1 
ATOM   751  C  C     . LEU A 1 99  ? 10.443  14.270  14.878  1.00 18.58  ?  99  LEU A C     1 
ATOM   752  O  O     . LEU A 1 99  ? 9.707   13.834  15.769  1.00 23.16  ?  99  LEU A O     1 
ATOM   753  C  CB    . LEU A 1 99  ? 12.839  14.576  15.501  1.00 16.26  ?  99  LEU A CB    1 
ATOM   754  C  CG    . LEU A 1 99  ? 14.310  14.136  15.558  1.00 20.41  ?  99  LEU A CG    1 
ATOM   755  C  CD1   . LEU A 1 99  ? 15.098  15.040  16.510  1.00 18.23  ?  99  LEU A CD1   1 
ATOM   756  C  CD2   . LEU A 1 99  ? 14.470  12.668  15.946  1.00 17.04  ?  99  LEU A CD2   1 
ATOM   757  N  N     . SER A 1 100 ? 10.047  15.224  14.033  1.00 20.05  ?  100 SER A N     1 
ATOM   758  C  CA    . SER A 1 100 ? 8.687   15.746  14.118  1.00 21.62  ?  100 SER A CA    1 
ATOM   759  C  C     . SER A 1 100 ? 7.653   14.659  13.836  1.00 24.31  ?  100 SER A C     1 
ATOM   760  O  O     . SER A 1 100 ? 6.532   14.717  14.358  1.00 22.43  ?  100 SER A O     1 
ATOM   761  C  CB    . SER A 1 100 ? 8.512   16.930  13.165  1.00 20.32  ?  100 SER A CB    1 
ATOM   762  O  OG    . SER A 1 100 ? 8.949   16.623  11.854  1.00 24.47  ?  100 SER A OG    1 
ATOM   763  N  N     . GLY A 1 101 ? 8.015   13.649  13.049  1.00 17.22  ?  101 GLY A N     1 
ATOM   764  C  CA    . GLY A 1 101 ? 7.108   12.565  12.730  1.00 13.75  ?  101 GLY A CA    1 
ATOM   765  C  C     . GLY A 1 101 ? 7.086   11.403  13.709  1.00 18.23  ?  101 GLY A C     1 
ATOM   766  O  O     . GLY A 1 101 ? 6.176   10.573  13.650  1.00 17.44  ?  101 GLY A O     1 
ATOM   767  N  N     . THR A 1 102 ? 8.062   11.310  14.608  1.00 19.06  ?  102 THR A N     1 
ATOM   768  C  CA    . THR A 1 102 ? 8.168   10.194  15.541  1.00 14.37  ?  102 THR A CA    1 
ATOM   769  C  C     . THR A 1 102 ? 7.978   10.596  16.991  1.00 15.69  ?  102 THR A C     1 
ATOM   770  O  O     . THR A 1 102 ? 7.433   9.814   17.786  1.00 12.25  ?  102 THR A O     1 
ATOM   771  C  CB    . THR A 1 102 ? 9.540   9.529   15.408  1.00 17.73  ?  102 THR A CB    1 
ATOM   772  O  OG1   . THR A 1 102 ? 10.562  10.530  15.554  1.00 14.79  ?  102 THR A OG1   1 
ATOM   773  C  CG2   . THR A 1 102 ? 9.662   8.851   14.062  1.00 17.06  ?  102 THR A CG2   1 
ATOM   774  N  N     . LEU A 1 103 ? 8.472   11.776  17.352  1.00 16.03  ?  103 LEU A N     1 
ATOM   775  C  CA    . LEU A 1 103 ? 8.360   12.239  18.728  1.00 18.52  ?  103 LEU A CA    1 
ATOM   776  C  C     . LEU A 1 103 ? 6.922   12.258  19.231  1.00 17.81  ?  103 LEU A C     1 
ATOM   777  O  O     . LEU A 1 103 ? 6.697   11.794  20.359  1.00 17.96  ?  103 LEU A O     1 
ATOM   778  C  CB    . LEU A 1 103 ? 9.022   13.612  18.857  1.00 18.41  ?  103 LEU A CB    1 
ATOM   779  C  CG    . LEU A 1 103 ? 10.494  13.571  19.293  1.00 24.22  ?  103 LEU A CG    1 
ATOM   780  C  CD1   . LEU A 1 103 ? 10.655  12.803  20.584  1.00 20.84  ?  103 LEU A CD1   1 
ATOM   781  C  CD2   . LEU A 1 103 ? 11.395  12.959  18.238  1.00 28.23  ?  103 LEU A CD2   1 
ATOM   782  N  N     . PRO A 1 104 ? 5.922   12.732  18.478  1.00 19.58  ?  104 PRO A N     1 
ATOM   783  C  CA    . PRO A 1 104 ? 4.540   12.642  18.987  1.00 18.39  ?  104 PRO A CA    1 
ATOM   784  C  C     . PRO A 1 104 ? 4.156   11.244  19.424  1.00 19.22  ?  104 PRO A C     1 
ATOM   785  O  O     . PRO A 1 104 ? 3.466   11.081  20.444  1.00 18.38  ?  104 PRO A O     1 
ATOM   786  C  CB    . PRO A 1 104 ? 3.694   13.110  17.801  1.00 22.46  ?  104 PRO A CB    1 
ATOM   787  C  CG    . PRO A 1 104 ? 4.615   14.028  17.027  1.00 26.81  ?  104 PRO A CG    1 
ATOM   788  C  CD    . PRO A 1 104 ? 6.000   13.463  17.198  1.00 20.22  ?  104 PRO A CD    1 
ATOM   789  N  N     . LEU A 1 105 ? 4.601   10.221  18.689  1.00 14.39  ?  105 LEU A N     1 
ATOM   790  C  CA    . LEU A 1 105 ? 4.290   8.857   19.090  1.00 12.23  ?  105 LEU A CA    1 
ATOM   791  C  C     . LEU A 1 105 ? 5.017   8.490   20.374  1.00 15.48  ?  105 LEU A C     1 
ATOM   792  O  O     . LEU A 1 105 ? 4.416   7.901   21.283  1.00 15.00  ?  105 LEU A O     1 
ATOM   793  C  CB    . LEU A 1 105 ? 4.640   7.881   17.980  1.00 13.22  ?  105 LEU A CB    1 
ATOM   794  C  CG    . LEU A 1 105 ? 3.622   7.891   16.837  1.00 21.93  ?  105 LEU A CG    1 
ATOM   795  C  CD1   . LEU A 1 105 ? 4.262   7.281   15.565  1.00 16.76  ?  105 LEU A CD1   1 
ATOM   796  C  CD2   . LEU A 1 105 ? 2.310   7.164   17.238  1.00 19.84  ?  105 LEU A CD2   1 
ATOM   797  N  N     . LEU A 1 106 ? 6.291   8.867   20.499  1.00 9.65   ?  106 LEU A N     1 
ATOM   798  C  CA    . LEU A 1 106 ? 7.028   8.484   21.702  1.00 10.67  ?  106 LEU A CA    1 
ATOM   799  C  C     . LEU A 1 106 ? 6.463   9.160   22.942  1.00 14.66  ?  106 LEU A C     1 
ATOM   800  O  O     . LEU A 1 106 ? 6.271   8.512   23.972  1.00 12.36  ?  106 LEU A O     1 
ATOM   801  C  CB    . LEU A 1 106 ? 8.500   8.807   21.547  1.00 8.96   ?  106 LEU A CB    1 
ATOM   802  C  CG    . LEU A 1 106 ? 9.144   7.899   20.483  1.00 16.39  ?  106 LEU A CG    1 
ATOM   803  C  CD1   . LEU A 1 106 ? 10.354  8.618   19.890  1.00 11.15  ?  106 LEU A CD1   1 
ATOM   804  C  CD2   . LEU A 1 106 ? 9.497   6.485   21.013  1.00 8.55   ?  106 LEU A CD2   1 
ATOM   805  N  N     . LYS A 1 107 ? 6.205   10.471  22.865  1.00 13.20  ?  107 LYS A N     1 
ATOM   806  C  CA    . LYS A 1 107 ? 5.601   11.180  23.989  1.00 14.33  ?  107 LYS A CA    1 
ATOM   807  C  C     . LYS A 1 107 ? 4.221   10.624  24.327  1.00 12.30  ?  107 LYS A C     1 
ATOM   808  O  O     . LYS A 1 107 ? 3.862   10.516  25.506  1.00 10.72  ?  107 LYS A O     1 
ATOM   809  C  CB    . LYS A 1 107 ? 5.527   12.673  23.670  1.00 11.97  ?  107 LYS A CB    1 
ATOM   810  C  CG    . LYS A 1 107 ? 6.901   13.280  23.565  1.00 16.28  ?  107 LYS A CG    1 
ATOM   811  C  CD    . LYS A 1 107 ? 6.931   14.452  22.634  1.00 23.91  ?  107 LYS A CD    1 
ATOM   812  C  CE    . LYS A 1 107 ? 6.338   15.664  23.284  1.00 18.91  ?  107 LYS A CE    1 
ATOM   813  N  NZ    . LYS A 1 107 ? 6.963   16.907  22.748  1.00 25.88  ?  107 LYS A NZ    1 
ATOM   814  N  N     . GLY A 1 108 ? 3.439   10.256  23.311  1.00 12.82  ?  108 GLY A N     1 
ATOM   815  C  CA    . GLY A 1 108 ? 2.117   9.693   23.539  1.00 13.09  ?  108 GLY A CA    1 
ATOM   816  C  C     . GLY A 1 108 ? 2.100   8.306   24.182  1.00 20.44  ?  108 GLY A C     1 
ATOM   817  O  O     . GLY A 1 108 ? 1.037   7.869   24.640  1.00 19.74  ?  108 GLY A O     1 
ATOM   818  N  N     . GLY A 1 109 ? 3.226   7.602   24.228  1.00 18.02  ?  109 GLY A N     1 
ATOM   819  C  CA    . GLY A 1 109 ? 3.231   6.370   24.994  1.00 15.56  ?  109 GLY A CA    1 
ATOM   820  C  C     . GLY A 1 109 ? 3.953   5.219   24.338  1.00 21.28  ?  109 GLY A C     1 
ATOM   821  O  O     . GLY A 1 109 ? 3.996   4.115   24.887  1.00 15.57  ?  109 GLY A O     1 
ATOM   822  N  N     . ALA A 1 110 ? 4.520   5.448   23.160  1.00 11.92  ?  110 ALA A N     1 
ATOM   823  C  CA    . ALA A 1 110 ? 5.377   4.410   22.614  1.00 12.88  ?  110 ALA A CA    1 
ATOM   824  C  C     . ALA A 1 110 ? 6.756   4.496   23.261  1.00 12.04  ?  110 ALA A C     1 
ATOM   825  O  O     . ALA A 1 110 ? 7.143   5.525   23.816  1.00 15.32  ?  110 ALA A O     1 
ATOM   826  C  CB    . ALA A 1 110 ? 5.475   4.543   21.097  1.00 13.22  ?  110 ALA A CB    1 
ATOM   827  N  N     . ASP A 1 111 ? 7.477   3.377   23.244  1.00 9.95   ?  111 ASP A N     1 
ATOM   828  C  CA    . ASP A 1 111 ? 8.870   3.350   23.666  1.00 9.67   ?  111 ASP A CA    1 
ATOM   829  C  C     . ASP A 1 111 ? 9.825   3.138   22.491  1.00 12.66  ?  111 ASP A C     1 
ATOM   830  O  O     . ASP A 1 111 ? 11.044  3.264   22.658  1.00 9.27   ?  111 ASP A O     1 
ATOM   831  C  CB    . ASP A 1 111 ? 9.107   2.234   24.695  1.00 8.32   ?  111 ASP A CB    1 
ATOM   832  C  CG    . ASP A 1 111 ? 8.024   2.181   25.805  1.00 13.49  ?  111 ASP A CG    1 
ATOM   833  O  OD1   . ASP A 1 111 ? 7.779   3.194   26.489  1.00 12.92  ?  111 ASP A OD1   1 
ATOM   834  O  OD2   . ASP A 1 111 ? 7.436   1.100   26.003  1.00 14.14  ?  111 ASP A OD2   1 
ATOM   835  N  N     . PHE A 1 112 ? 9.302   2.808   21.320  1.00 8.02   ?  112 PHE A N     1 
ATOM   836  C  CA    . PHE A 1 112 ? 10.130  2.360   20.214  1.00 11.81  ?  112 PHE A CA    1 
ATOM   837  C  C     . PHE A 1 112 ? 9.317   2.602   18.957  1.00 16.52  ?  112 PHE A C     1 
ATOM   838  O  O     . PHE A 1 112 ? 8.167   2.140   18.865  1.00 15.49  ?  112 PHE A O     1 
ATOM   839  C  CB    . PHE A 1 112 ? 10.513  0.891   20.366  1.00 12.20  ?  112 PHE A CB    1 
ATOM   840  C  CG    . PHE A 1 112 ? 11.452  0.380   19.287  1.00 12.38  ?  112 PHE A CG    1 
ATOM   841  C  CD1   . PHE A 1 112 ? 11.023  0.247   17.973  1.00 12.52  ?  112 PHE A CD1   1 
ATOM   842  C  CD2   . PHE A 1 112 ? 12.750  0.014   19.600  1.00 13.98  ?  112 PHE A CD2   1 
ATOM   843  C  CE1   . PHE A 1 112 ? 11.882  -0.235  16.965  1.00 14.00  ?  112 PHE A CE1   1 
ATOM   844  C  CE2   . PHE A 1 112 ? 13.613  -0.468  18.608  1.00 21.30  ?  112 PHE A CE2   1 
ATOM   845  C  CZ    . PHE A 1 112 ? 13.169  -0.593  17.287  1.00 18.52  ?  112 PHE A CZ    1 
ATOM   846  N  N     . VAL A 1 113 ? 9.897   3.371   18.035  1.00 10.17  ?  113 VAL A N     1 
ATOM   847  C  CA    . VAL A 1 113 ? 9.291   3.754   16.768  1.00 10.89  ?  113 VAL A CA    1 
ATOM   848  C  C     . VAL A 1 113 ? 10.319  3.460   15.677  1.00 14.75  ?  113 VAL A C     1 
ATOM   849  O  O     . VAL A 1 113 ? 11.508  3.751   15.848  1.00 13.55  ?  113 VAL A O     1 
ATOM   850  C  CB    . VAL A 1 113 ? 8.890   5.249   16.751  1.00 11.38  ?  113 VAL A CB    1 
ATOM   851  C  CG1   . VAL A 1 113 ? 8.259   5.617   15.435  1.00 13.77  ?  113 VAL A CG1   1 
ATOM   852  C  CG2   . VAL A 1 113 ? 7.920   5.587   17.908  1.00 15.06  ?  113 VAL A CG2   1 
ATOM   853  N  N     . TYR A 1 114 ? 9.877   2.851   14.575  1.00 10.31  ?  114 TYR A N     1 
ATOM   854  C  CA    . TYR A 1 114 ? 10.724  2.694   13.404  1.00 11.21  ?  114 TYR A CA    1 
ATOM   855  C  C     . TYR A 1 114 ? 9.963   3.233   12.207  1.00 12.71  ?  114 TYR A C     1 
ATOM   856  O  O     . TYR A 1 114 ? 8.730   3.173   12.166  1.00 12.46  ?  114 TYR A O     1 
ATOM   857  C  CB    . TYR A 1 114 ? 11.151  1.240   13.186  1.00 11.16  ?  114 TYR A CB    1 
ATOM   858  C  CG    . TYR A 1 114 ? 10.034  0.298   12.807  1.00 12.86  ?  114 TYR A CG    1 
ATOM   859  C  CD1   . TYR A 1 114 ? 9.181   -0.231  13.776  1.00 14.00  ?  114 TYR A CD1   1 
ATOM   860  C  CD2   . TYR A 1 114 ? 9.838   -0.074  11.482  1.00 14.38  ?  114 TYR A CD2   1 
ATOM   861  C  CE1   . TYR A 1 114 ? 8.161   -1.095  13.429  1.00 13.51  ?  114 TYR A CE1   1 
ATOM   862  C  CE2   . TYR A 1 114 ? 8.825   -0.951  11.122  1.00 18.14  ?  114 TYR A CE2   1 
ATOM   863  C  CZ    . TYR A 1 114 ? 7.980   -1.455  12.101  1.00 18.48  ?  114 TYR A CZ    1 
ATOM   864  O  OH    . TYR A 1 114 ? 6.961   -2.319  11.746  1.00 14.75  ?  114 TYR A OH    1 
ATOM   865  N  N     . VAL A 1 115 ? 10.693  3.820   11.257  1.00 9.55   ?  115 VAL A N     1 
ATOM   866  C  CA    . VAL A 1 115 ? 10.007  4.449   10.132  1.00 12.45  ?  115 VAL A CA    1 
ATOM   867  C  C     . VAL A 1 115 ? 10.266  3.668   8.850   1.00 17.34  ?  115 VAL A C     1 
ATOM   868  O  O     . VAL A 1 115 ? 10.934  2.623   8.864   1.00 15.88  ?  115 VAL A O     1 
ATOM   869  C  CB    . VAL A 1 115 ? 10.389  5.940   10.009  1.00 14.40  ?  115 VAL A CB    1 
ATOM   870  C  CG1   . VAL A 1 115 ? 10.020  6.670   11.336  1.00 10.77  ?  115 VAL A CG1   1 
ATOM   871  C  CG2   . VAL A 1 115 ? 11.868  6.136   9.690   1.00 9.48   ?  115 VAL A CG2   1 
ATOM   872  N  N     . ASN A 1 116 ? 9.669   4.123   7.752   1.00 18.27  ?  116 ASN A N     1 
ATOM   873  C  CA    . ASN A 1 116 ? 9.937   3.518   6.464   1.00 19.54  ?  116 ASN A CA    1 
ATOM   874  C  C     . ASN A 1 116 ? 11.404  3.703   6.111   1.00 18.91  ?  116 ASN A C     1 
ATOM   875  O  O     . ASN A 1 116 ? 12.085  4.581   6.639   1.00 18.15  ?  116 ASN A O     1 
ATOM   876  C  CB    . ASN A 1 116 ? 9.037   4.118   5.390   1.00 16.87  ?  116 ASN A CB    1 
ATOM   877  C  CG    . ASN A 1 116 ? 7.643   3.528   5.428   1.00 19.49  ?  116 ASN A CG    1 
ATOM   878  O  OD1   . ASN A 1 116 ? 7.395   2.573   6.155   1.00 21.18  ?  116 ASN A OD1   1 
ATOM   879  N  ND2   . ASN A 1 116 ? 6.731   4.085   4.648   1.00 20.34  ?  116 ASN A ND2   1 
ATOM   880  N  N     . ILE A 1 117 ? 11.897  2.819   5.247   1.00 15.00  ?  117 ILE A N     1 
ATOM   881  C  CA    . ILE A 1 117 ? 13.290  2.816   4.812   1.00 23.09  ?  117 ILE A CA    1 
ATOM   882  C  C     . ILE A 1 117 ? 13.312  2.744   3.296   1.00 20.10  ?  117 ILE A C     1 
ATOM   883  O  O     . ILE A 1 117 ? 12.755  1.805   2.713   1.00 23.21  ?  117 ILE A O     1 
ATOM   884  C  CB    . ILE A 1 117 ? 14.096  1.636   5.384   1.00 20.29  ?  117 ILE A CB    1 
ATOM   885  C  CG1   . ILE A 1 117 ? 14.195  1.694   6.911   1.00 21.35  ?  117 ILE A CG1   1 
ATOM   886  C  CG2   . ILE A 1 117 ? 15.477  1.626   4.781   1.00 14.13  ?  117 ILE A CG2   1 
ATOM   887  C  CD1   . ILE A 1 117 ? 14.797  0.412   7.509   1.00 16.56  ?  117 ILE A CD1   1 
ATOM   888  N  N     . ASN A 1 118 ? 13.965  3.719   2.663   1.00 19.87  ?  118 ASN A N     1 
ATOM   889  C  CA    . ASN A 1 118 ? 14.252  3.687   1.233   1.00 21.74  ?  118 ASN A CA    1 
ATOM   890  C  C     . ASN A 1 118 ? 15.673  3.183   1.047   1.00 22.94  ?  118 ASN A C     1 
ATOM   891  O  O     . ASN A 1 118 ? 16.635  3.856   1.444   1.00 20.33  ?  118 ASN A O     1 
ATOM   892  C  CB    . ASN A 1 118 ? 14.092  5.063   0.605   1.00 18.52  ?  118 ASN A CB    1 
ATOM   893  C  CG    . ASN A 1 118 ? 12.674  5.508   0.587   1.00 24.80  ?  118 ASN A CG    1 
ATOM   894  O  OD1   . ASN A 1 118 ? 11.786  4.730   0.228   1.00 28.18  ?  118 ASN A OD1   1 
ATOM   895  N  ND2   . ASN A 1 118 ? 12.430  6.752   0.995   1.00 13.66  ?  118 ASN A ND2   1 
ATOM   896  N  N     . ILE A 1 119 ? 15.802  2.002   0.447   1.00 23.13  ?  119 ILE A N     1 
ATOM   897  C  CA    . ILE A 1 119 ? 17.115  1.436   0.157   1.00 22.05  ?  119 ILE A CA    1 
ATOM   898  C  C     . ILE A 1 119 ? 17.615  2.148   -1.094  1.00 22.30  ?  119 ILE A C     1 
ATOM   899  O  O     . ILE A 1 119 ? 17.199  1.848   -2.216  1.00 23.14  ?  119 ILE A O     1 
ATOM   900  C  CB    . ILE A 1 119 ? 17.058  -0.082  -0.010  1.00 25.75  ?  119 ILE A CB    1 
ATOM   901  C  CG1   . ILE A 1 119 ? 16.971  -0.714  1.374   1.00 22.15  ?  119 ILE A CG1   1 
ATOM   902  C  CG2   . ILE A 1 119 ? 18.299  -0.626  -0.749  1.00 28.31  ?  119 ILE A CG2   1 
ATOM   903  C  CD1   . ILE A 1 119 ? 16.402  -2.098  1.358   1.00 30.22  ?  119 ILE A CD1   1 
ATOM   904  N  N     . ALA A 1 120 ? 18.479  3.134   -0.884  1.00 21.99  ?  120 ALA A N     1 
ATOM   905  C  CA    . ALA A 1 120 ? 18.932  4.031   -1.937  1.00 27.09  ?  120 ALA A CA    1 
ATOM   906  C  C     . ALA A 1 120 ? 20.134  3.434   -2.661  1.00 26.32  ?  120 ALA A C     1 
ATOM   907  O  O     . ALA A 1 120 ? 21.122  3.039   -2.028  1.00 23.71  ?  120 ALA A O     1 
ATOM   908  C  CB    . ALA A 1 120 ? 19.287  5.396   -1.350  1.00 21.91  ?  120 ALA A CB    1 
ATOM   909  N  N     . ARG A 1 121 ? 20.045  3.373   -3.987  1.00 25.09  ?  121 ARG A N     1 
ATOM   910  C  CA    . ARG A 1 121 ? 21.122  2.819   -4.804  1.00 29.80  ?  121 ARG A CA    1 
ATOM   911  C  C     . ARG A 1 121 ? 22.060  3.885   -5.361  1.00 34.51  ?  121 ARG A C     1 
ATOM   912  O  O     . ARG A 1 121 ? 23.080  3.538   -5.976  1.00 33.95  ?  121 ARG A O     1 
ATOM   913  C  CB    . ARG A 1 121 ? 20.539  1.988   -5.953  1.00 28.13  ?  121 ARG A CB    1 
ATOM   914  C  CG    . ARG A 1 121 ? 20.043  0.618   -5.509  1.00 31.66  ?  121 ARG A CG    1 
ATOM   915  C  CD    . ARG A 1 121 ? 18.949  0.103   -6.430  1.00 39.93  ?  121 ARG A CD    1 
ATOM   916  N  NE    . ARG A 1 121 ? 19.457  -0.182  -7.769  1.00 51.88  ?  121 ARG A NE    1 
ATOM   917  C  CZ    . ARG A 1 121 ? 20.070  -1.307  -8.114  1.00 47.09  ?  121 ARG A CZ    1 
ATOM   918  N  NH1   . ARG A 1 121 ? 20.264  -2.284  -7.243  1.00 44.72  ?  121 ARG A NH1   1 
ATOM   919  N  NH2   . ARG A 1 121 ? 20.498  -1.455  -9.364  1.00 43.23  ?  121 ARG A NH2   1 
ATOM   920  N  N     . THR A 1 122 ? 21.738  5.163   -5.172  1.00 25.81  ?  122 THR A N     1 
ATOM   921  C  CA    . THR A 1 122 ? 22.645  6.260   -5.459  1.00 30.25  ?  122 THR A CA    1 
ATOM   922  C  C     . THR A 1 122 ? 22.703  7.167   -4.234  1.00 35.00  ?  122 THR A C     1 
ATOM   923  O  O     . THR A 1 122 ? 21.764  7.206   -3.430  1.00 27.28  ?  122 THR A O     1 
ATOM   924  C  CB    . THR A 1 122 ? 22.204  7.039   -6.709  1.00 33.61  ?  122 THR A CB    1 
ATOM   925  O  OG1   . THR A 1 122 ? 20.826  7.403   -6.594  1.00 32.43  ?  122 THR A OG1   1 
ATOM   926  C  CG2   . THR A 1 122 ? 22.389  6.176   -7.965  1.00 31.59  ?  122 THR A CG2   1 
ATOM   927  N  N     . ARG A 1 123 ? 23.822  7.875   -4.074  1.00 28.30  ?  123 ARG A N     1 
ATOM   928  C  CA    . ARG A 1 123 ? 24.034  8.642   -2.854  1.00 26.91  ?  123 ARG A CA    1 
ATOM   929  C  C     . ARG A 1 123 ? 23.186  9.902   -2.882  1.00 28.74  ?  123 ARG A C     1 
ATOM   930  O  O     . ARG A 1 123 ? 23.192  10.632  -3.872  1.00 29.21  ?  123 ARG A O     1 
ATOM   931  C  CB    . ARG A 1 123 ? 25.515  8.980   -2.682  1.00 24.78  ?  123 ARG A CB    1 
ATOM   932  C  CG    . ARG A 1 123 ? 26.338  7.785   -2.178  1.00 27.64  ?  123 ARG A CG    1 
ATOM   933  C  CD    . ARG A 1 123 ? 27.359  8.153   -1.097  1.00 31.51  ?  123 ARG A CD    1 
ATOM   934  N  NE    . ARG A 1 123 ? 26.760  8.505   0.191   1.00 45.09  ?  123 ARG A NE    1 
ATOM   935  C  CZ    . ARG A 1 123 ? 26.534  7.668   1.205   1.00 41.44  ?  123 ARG A CZ    1 
ATOM   936  N  NH1   . ARG A 1 123 ? 26.804  6.368   1.118   1.00 33.72  ?  123 ARG A NH1   1 
ATOM   937  N  NH2   . ARG A 1 123 ? 26.032  8.150   2.345   1.00 32.10  ?  123 ARG A NH2   1 
ATOM   938  N  N     . VAL A 1 124 ? 22.433  10.141  -1.800  1.00 23.90  ?  124 VAL A N     1 
ATOM   939  C  CA    . VAL A 1 124 ? 21.584  11.318  -1.666  1.00 22.85  ?  124 VAL A CA    1 
ATOM   940  C  C     . VAL A 1 124 ? 21.867  11.991  -0.327  1.00 22.61  ?  124 VAL A C     1 
ATOM   941  O  O     . VAL A 1 124 ? 22.602  11.474  0.514   1.00 25.23  ?  124 VAL A O     1 
ATOM   942  C  CB    . VAL A 1 124 ? 20.080  10.987  -1.800  1.00 26.28  ?  124 VAL A CB    1 
ATOM   943  C  CG1   . VAL A 1 124 ? 19.782  10.485  -3.205  1.00 25.80  ?  124 VAL A CG1   1 
ATOM   944  C  CG2   . VAL A 1 124 ? 19.603  9.979   -0.711  1.00 23.03  ?  124 VAL A CG2   1 
ATOM   945  N  N     . THR A 1 125 ? 21.280  13.174  -0.152  1.00 18.16  ?  125 THR A N     1 
ATOM   946  C  CA    . THR A 1 125 ? 21.378  13.963  1.064   1.00 22.22  ?  125 THR A CA    1 
ATOM   947  C  C     . THR A 1 125 ? 20.052  13.902  1.829   1.00 22.72  ?  125 THR A C     1 
ATOM   948  O  O     . THR A 1 125 ? 19.085  13.260  1.402   1.00 20.00  ?  125 THR A O     1 
ATOM   949  C  CB    . THR A 1 125 ? 21.758  15.411  0.745   1.00 21.19  ?  125 THR A CB    1 
ATOM   950  O  OG1   . THR A 1 125 ? 20.725  16.009  -0.046  1.00 25.18  ?  125 THR A OG1   1 
ATOM   951  C  CG2   . THR A 1 125 ? 23.078  15.460  -0.024  1.00 25.31  ?  125 THR A CG2   1 
ATOM   952  N  N     . GLY A 1 126 ? 20.014  14.588  2.976   1.00 21.55  ?  126 GLY A N     1 
ATOM   953  C  CA    . GLY A 1 126 ? 18.813  14.550  3.808   1.00 22.92  ?  126 GLY A CA    1 
ATOM   954  C  C     . GLY A 1 126 ? 17.637  15.273  3.177   1.00 28.55  ?  126 GLY A C     1 
ATOM   955  O  O     . GLY A 1 126 ? 16.485  14.844  3.316   1.00 23.59  ?  126 GLY A O     1 
ATOM   956  N  N     . THR A 1 127 ? 17.910  16.369  2.458   1.00 26.04  ?  127 THR A N     1 
ATOM   957  C  CA    . THR A 1 127 ? 16.889  17.139  1.758   1.00 27.02  ?  127 THR A CA    1 
ATOM   958  C  C     . THR A 1 127 ? 16.624  16.635  0.333   1.00 28.04  ?  127 THR A C     1 
ATOM   959  O  O     . THR A 1 127 ? 15.853  17.269  -0.402  1.00 24.98  ?  127 THR A O     1 
ATOM   960  C  CB    . THR A 1 127 ? 17.286  18.620  1.714   1.00 27.65  ?  127 THR A CB    1 
ATOM   961  O  OG1   . THR A 1 127 ? 18.569  18.758  1.089   1.00 31.00  ?  127 THR A OG1   1 
ATOM   962  C  CG2   . THR A 1 127 ? 17.352  19.209  3.131   1.00 28.57  ?  127 THR A CG2   1 
ATOM   963  N  N     . THR A 1 128 ? 17.226  15.502  -0.068  1.00 24.55  ?  128 THR A N     1 
ATOM   964  C  CA    . THR A 1 128 ? 17.091  15.016  -1.438  1.00 27.68  ?  128 THR A CA    1 
ATOM   965  C  C     . THR A 1 128 ? 16.832  13.509  -1.512  1.00 28.54  ?  128 THR A C     1 
ATOM   966  O  O     . THR A 1 128 ? 17.266  12.853  -2.470  1.00 29.40  ?  128 THR A O     1 
ATOM   967  C  CB    . THR A 1 128 ? 18.342  15.346  -2.261  1.00 28.89  ?  128 THR A CB    1 
ATOM   968  O  OG1   . THR A 1 128 ? 19.508  14.898  -1.551  1.00 28.05  ?  128 THR A OG1   1 
ATOM   969  C  CG2   . THR A 1 128 ? 18.442  16.847  -2.539  1.00 22.05  ?  128 THR A CG2   1 
ATOM   970  N  N     . ILE A 1 129 ? 16.106  12.950  -0.540  1.00 20.96  ?  129 ILE A N     1 
ATOM   971  C  CA    . ILE A 1 129 ? 15.876  11.507  -0.515  1.00 23.04  ?  129 ILE A CA    1 
ATOM   972  C  C     . ILE A 1 129 ? 15.070  11.064  -1.733  1.00 30.05  ?  129 ILE A C     1 
ATOM   973  O  O     . ILE A 1 129 ? 15.311  9.983   -2.290  1.00 32.02  ?  129 ILE A O     1 
ATOM   974  C  CB    . ILE A 1 129 ? 15.185  11.086  0.799   1.00 29.81  ?  129 ILE A CB    1 
ATOM   975  C  CG1   . ILE A 1 129 ? 16.188  11.039  1.953   1.00 25.75  ?  129 ILE A CG1   1 
ATOM   976  C  CG2   . ILE A 1 129 ? 14.522  9.719   0.651   1.00 21.63  ?  129 ILE A CG2   1 
ATOM   977  C  CD1   . ILE A 1 129 ? 15.551  11.276  3.297   1.00 24.08  ?  129 ILE A CD1   1 
ATOM   978  N  N     . ALA A 1 130 ? 14.116  11.894  -2.183  1.00 25.16  ?  130 ALA A N     1 
ATOM   979  C  CA    . ALA A 1 130 ? 13.270  11.520  -3.321  1.00 32.20  ?  130 ALA A CA    1 
ATOM   980  C  C     . ALA A 1 130 ? 14.057  11.331  -4.616  1.00 34.40  ?  130 ALA A C     1 
ATOM   981  O  O     . ALA A 1 130 ? 13.562  10.673  -5.540  1.00 36.92  ?  130 ALA A O     1 
ATOM   982  C  CB    . ALA A 1 130 ? 12.174  12.563  -3.549  1.00 31.85  ?  130 ALA A CB    1 
ATOM   983  N  N     . ASP A 1 131 ? 15.265  11.883  -4.706  1.00 34.04  ?  131 ASP A N     1 
ATOM   984  C  CA    . ASP A 1 131 ? 16.110  11.701  -5.881  1.00 31.16  ?  131 ASP A CA    1 
ATOM   985  C  C     . ASP A 1 131 ? 16.871  10.383  -5.878  1.00 31.17  ?  131 ASP A C     1 
ATOM   986  O  O     . ASP A 1 131 ? 17.633  10.129  -6.816  1.00 34.64  ?  131 ASP A O     1 
ATOM   987  C  CB    . ASP A 1 131 ? 17.099  12.855  -5.979  1.00 34.59  ?  131 ASP A CB    1 
ATOM   988  C  CG    . ASP A 1 131 ? 16.407  14.189  -6.030  1.00 39.94  ?  131 ASP A CG    1 
ATOM   989  O  OD1   . ASP A 1 131 ? 15.338  14.277  -6.677  1.00 48.96  ?  131 ASP A OD1   1 
ATOM   990  O  OD2   . ASP A 1 131 ? 16.913  15.145  -5.405  1.00 48.51  ?  131 ASP A OD2   1 
ATOM   991  N  N     . ALA A 1 132 ? 16.689  9.546   -4.862  1.00 29.35  ?  132 ALA A N     1 
ATOM   992  C  CA    . ALA A 1 132 ? 17.408  8.283   -4.802  1.00 30.17  ?  132 ALA A CA    1 
ATOM   993  C  C     . ALA A 1 132 ? 16.818  7.283   -5.779  1.00 30.35  ?  132 ALA A C     1 
ATOM   994  O  O     . ALA A 1 132 ? 15.600  7.223   -5.963  1.00 31.38  ?  132 ALA A O     1 
ATOM   995  C  CB    . ALA A 1 132 ? 17.364  7.702   -3.391  1.00 27.14  ?  132 ALA A CB    1 
ATOM   996  N  N     . GLU A 1 133 ? 17.699  6.506   -6.420  1.00 29.21  ?  133 GLU A N     1 
ATOM   997  C  CA    . GLU A 1 133 ? 17.282  5.336   -7.183  1.00 31.76  ?  133 GLU A CA    1 
ATOM   998  C  C     . GLU A 1 133 ? 16.954  4.210   -6.204  1.00 29.99  ?  133 GLU A C     1 
ATOM   999  O  O     . GLU A 1 133 ? 17.808  3.809   -5.400  1.00 22.74  ?  133 GLU A O     1 
ATOM   1000 C  CB    . GLU A 1 133 ? 18.374  4.914   -8.170  1.00 33.41  ?  133 GLU A CB    1 
ATOM   1001 C  CG    . GLU A 1 133 ? 18.451  5.802   -9.425  1.00 45.25  ?  133 GLU A CG    1 
ATOM   1002 C  CD    . GLU A 1 133 ? 19.685  5.536   -10.283 1.00 52.59  ?  133 GLU A CD    1 
ATOM   1003 O  OE1   . GLU A 1 133 ? 20.218  6.497   -10.882 1.00 53.23  ?  133 GLU A OE1   1 
ATOM   1004 O  OE2   . GLU A 1 133 ? 20.118  4.365   -10.365 1.00 53.92  ?  133 GLU A OE2   1 
ATOM   1005 N  N     . VAL A 1 134 ? 15.713  3.721   -6.249  1.00 28.82  ?  134 VAL A N     1 
ATOM   1006 C  CA    . VAL A 1 134 ? 15.187  2.825   -5.223  1.00 31.58  ?  134 VAL A CA    1 
ATOM   1007 C  C     . VAL A 1 134 ? 14.403  1.701   -5.884  1.00 30.08  ?  134 VAL A C     1 
ATOM   1008 O  O     . VAL A 1 134 ? 13.362  1.952   -6.502  1.00 28.85  ?  134 VAL A O     1 
ATOM   1009 C  CB    . VAL A 1 134 ? 14.276  3.558   -4.223  1.00 30.66  ?  134 VAL A CB    1 
ATOM   1010 C  CG1   . VAL A 1 134 ? 13.867  2.595   -3.130  1.00 27.31  ?  134 VAL A CG1   1 
ATOM   1011 C  CG2   . VAL A 1 134 ? 14.972  4.796   -3.647  1.00 20.16  ?  134 VAL A CG2   1 
ATOM   1012 N  N     . LEU A 1 135 ? 14.875  0.463   -5.722  1.00 31.12  ?  135 LEU A N     1 
ATOM   1013 C  CA    . LEU A 1 135 ? 14.156  -0.711  -6.208  1.00 33.87  ?  135 LEU A CA    1 
ATOM   1014 C  C     . LEU A 1 135 ? 13.297  -1.369  -5.143  1.00 33.41  ?  135 LEU A C     1 
ATOM   1015 O  O     . LEU A 1 135 ? 12.275  -1.982  -5.475  1.00 36.15  ?  135 LEU A O     1 
ATOM   1016 C  CB    . LEU A 1 135 ? 15.129  -1.765  -6.751  1.00 34.47  ?  135 LEU A CB    1 
ATOM   1017 C  CG    . LEU A 1 135 ? 15.971  -1.410  -7.978  1.00 45.20  ?  135 LEU A CG    1 
ATOM   1018 C  CD1   . LEU A 1 135 ? 16.907  -2.577  -8.354  1.00 39.72  ?  135 LEU A CD1   1 
ATOM   1019 C  CD2   . LEU A 1 135 ? 15.086  -0.992  -9.149  1.00 40.77  ?  135 LEU A CD2   1 
ATOM   1020 N  N     . VAL A 1 136 ? 13.701  -1.290  -3.877  1.00 30.41  ?  136 VAL A N     1 
ATOM   1021 C  CA    . VAL A 1 136 ? 12.948  -1.897  -2.789  1.00 35.22  ?  136 VAL A CA    1 
ATOM   1022 C  C     . VAL A 1 136 ? 12.918  -0.932  -1.613  1.00 27.55  ?  136 VAL A C     1 
ATOM   1023 O  O     . VAL A 1 136 ? 13.844  -0.146  -1.399  1.00 27.61  ?  136 VAL A O     1 
ATOM   1024 C  CB    . VAL A 1 136 ? 13.523  -3.280  -2.370  1.00 36.47  ?  136 VAL A CB    1 
ATOM   1025 C  CG1   . VAL A 1 136 ? 13.481  -4.262  -3.533  1.00 31.56  ?  136 VAL A CG1   1 
ATOM   1026 C  CG2   . VAL A 1 136 ? 14.945  -3.153  -1.853  1.00 34.22  ?  136 VAL A CG2   1 
ATOM   1027 N  N     . ARG A 1 137 ? 11.821  -0.982  -0.866  1.00 30.14  ?  137 ARG A N     1 
ATOM   1028 C  CA    . ARG A 1 137 ? 11.629  -0.197  0.341   1.00 25.30  ?  137 ARG A CA    1 
ATOM   1029 C  C     . ARG A 1 137 ? 11.157  -1.118  1.460   1.00 31.57  ?  137 ARG A C     1 
ATOM   1030 O  O     . ARG A 1 137 ? 10.395  -2.061  1.217   1.00 28.73  ?  137 ARG A O     1 
ATOM   1031 C  CB    . ARG A 1 137 ? 10.600  0.924   0.134   1.00 26.03  ?  137 ARG A CB    1 
ATOM   1032 C  CG    . ARG A 1 137 ? 10.725  1.694   -1.166  1.00 29.35  ?  137 ARG A CG    1 
ATOM   1033 C  CD    . ARG A 1 137 ? 9.658   2.781   -1.228  1.00 34.92  ?  137 ARG A CD    1 
ATOM   1034 N  NE    . ARG A 1 137 ? 10.067  3.933   -2.023  1.00 37.84  ?  137 ARG A NE    1 
ATOM   1035 C  CZ    . ARG A 1 137 ? 10.149  3.936   -3.346  1.00 35.37  ?  137 ARG A CZ    1 
ATOM   1036 N  NH1   . ARG A 1 137 ? 9.865   2.855   -4.057  1.00 37.95  ?  137 ARG A NH1   1 
ATOM   1037 N  NH2   . ARG A 1 137 ? 10.526  5.051   -3.972  1.00 26.64  ?  137 ARG A NH2   1 
ATOM   1038 N  N     . LEU A 1 138 ? 11.612  -0.839  2.685   1.00 29.91  ?  138 LEU A N     1 
ATOM   1039 C  CA    . LEU A 1 138 ? 11.215  -1.588  3.880   1.00 24.15  ?  138 LEU A CA    1 
ATOM   1040 C  C     . LEU A 1 138 ? 10.148  -0.767  4.596   1.00 20.94  ?  138 LEU A C     1 
ATOM   1041 O  O     . LEU A 1 138 ? 10.455  0.212   5.286   1.00 20.12  ?  138 LEU A O     1 
ATOM   1042 C  CB    . LEU A 1 138 ? 12.410  -1.860  4.790   1.00 22.37  ?  138 LEU A CB    1 
ATOM   1043 C  CG    . LEU A 1 138 ? 13.581  -2.657  4.220   1.00 17.91  ?  138 LEU A CG    1 
ATOM   1044 C  CD1   . LEU A 1 138 ? 14.766  -2.687  5.190   1.00 14.46  ?  138 LEU A CD1   1 
ATOM   1045 C  CD2   . LEU A 1 138 ? 13.116  -4.056  3.921   1.00 19.95  ?  138 LEU A CD2   1 
ATOM   1046 N  N     . GLU A 1 139 ? 8.891   -1.160  4.411   1.00 18.55  ?  139 GLU A N     1 
ATOM   1047 C  CA    . GLU A 1 139 ? 7.741   -0.472  4.979   1.00 21.92  ?  139 GLU A CA    1 
ATOM   1048 C  C     . GLU A 1 139 ? 6.797   -1.458  5.654   1.00 18.88  ?  139 GLU A C     1 
ATOM   1049 O  O     . GLU A 1 139 ? 5.580   -1.350  5.516   1.00 26.75  ?  139 GLU A O     1 
ATOM   1050 C  CB    . GLU A 1 139 ? 6.985   0.310   3.902   1.00 26.40  ?  139 GLU A CB    1 
ATOM   1051 C  CG    . GLU A 1 139 ? 7.816   0.719   2.685   1.00 29.98  ?  139 GLU A CG    1 
ATOM   1052 C  CD    . GLU A 1 139 ? 7.037   1.557   1.643   1.00 37.74  ?  139 GLU A CD    1 
ATOM   1053 O  OE1   . GLU A 1 139 ? 6.007   1.069   1.118   1.00 42.17  ?  139 GLU A OE1   1 
ATOM   1054 O  OE2   . GLU A 1 139 ? 7.464   2.701   1.338   1.00 31.49  ?  139 GLU A OE2   1 
ATOM   1055 N  N     . PHE A 1 140 ? 7.326   -2.442  6.393   1.00 17.05  ?  140 PHE A N     1 
ATOM   1056 C  CA    . PHE A 1 140 ? 6.479   -3.514  6.930   1.00 17.08  ?  140 PHE A CA    1 
ATOM   1057 C  C     . PHE A 1 140 ? 5.785   -3.072  8.216   1.00 16.82  ?  140 PHE A C     1 
ATOM   1058 O  O     . PHE A 1 140 ? 6.468   -2.710  9.178   1.00 18.12  ?  140 PHE A O     1 
ATOM   1059 C  CB    . PHE A 1 140 ? 7.296   -4.772  7.209   1.00 15.57  ?  140 PHE A CB    1 
ATOM   1060 C  CG    . PHE A 1 140 ? 7.844   -5.419  5.978   1.00 14.18  ?  140 PHE A CG    1 
ATOM   1061 C  CD1   . PHE A 1 140 ? 7.045   -6.240  5.212   1.00 17.10  ?  140 PHE A CD1   1 
ATOM   1062 C  CD2   . PHE A 1 140 ? 9.154   -5.176  5.571   1.00 16.04  ?  140 PHE A CD2   1 
ATOM   1063 C  CE1   . PHE A 1 140 ? 7.544   -6.839  4.063   1.00 22.41  ?  140 PHE A CE1   1 
ATOM   1064 C  CE2   . PHE A 1 140 ? 9.660   -5.760  4.430   1.00 20.43  ?  140 PHE A CE2   1 
ATOM   1065 C  CZ    . PHE A 1 140 ? 8.851   -6.600  3.667   1.00 19.58  ?  140 PHE A CZ    1 
ATOM   1066 N  N     . PRO A 1 141 ? 4.455   -3.120  8.289   1.00 17.36  ?  141 PRO A N     1 
ATOM   1067 C  CA    . PRO A 1 141 ? 3.773   -2.833  9.561   1.00 16.89  ?  141 PRO A CA    1 
ATOM   1068 C  C     . PRO A 1 141 ? 4.163   -3.828  10.651  1.00 20.90  ?  141 PRO A C     1 
ATOM   1069 O  O     . PRO A 1 141 ? 4.762   -4.876  10.406  1.00 16.90  ?  141 PRO A O     1 
ATOM   1070 C  CB    . PRO A 1 141 ? 2.285   -2.939  9.202   1.00 19.80  ?  141 PRO A CB    1 
ATOM   1071 C  CG    . PRO A 1 141 ? 2.218   -2.748  7.695   1.00 16.04  ?  141 PRO A CG    1 
ATOM   1072 C  CD    . PRO A 1 141 ? 3.508   -3.339  7.178   1.00 16.65  ?  141 PRO A CD    1 
ATOM   1073 N  N     . TYR A 1 142 ? 3.818   -3.492  11.891  1.00 17.55  ?  142 TYR A N     1 
ATOM   1074 C  CA    . TYR A 1 142 ? 4.231   -4.305  13.036  1.00 20.09  ?  142 TYR A CA    1 
ATOM   1075 C  C     . TYR A 1 142 ? 3.088   -5.177  13.550  1.00 21.45  ?  142 TYR A C     1 
ATOM   1076 O  O     . TYR A 1 142 ? 2.892   -5.310  14.760  1.00 25.94  ?  142 TYR A O     1 
ATOM   1077 C  CB    . TYR A 1 142 ? 4.787   -3.405  14.142  1.00 16.67  ?  142 TYR A CB    1 
ATOM   1078 C  CG    . TYR A 1 142 ? 5.607   -4.099  15.223  1.00 18.57  ?  142 TYR A CG    1 
ATOM   1079 C  CD1   . TYR A 1 142 ? 6.944   -4.381  15.028  1.00 18.68  ?  142 TYR A CD1   1 
ATOM   1080 C  CD2   . TYR A 1 142 ? 5.053   -4.412  16.467  1.00 22.22  ?  142 TYR A CD2   1 
ATOM   1081 C  CE1   . TYR A 1 142 ? 7.698   -4.997  16.013  1.00 19.94  ?  142 TYR A CE1   1 
ATOM   1082 C  CE2   . TYR A 1 142 ? 5.803   -5.034  17.460  1.00 18.34  ?  142 TYR A CE2   1 
ATOM   1083 C  CZ    . TYR A 1 142 ? 7.126   -5.324  17.218  1.00 19.13  ?  142 TYR A CZ    1 
ATOM   1084 O  OH    . TYR A 1 142 ? 7.896   -5.931  18.184  1.00 19.40  ?  142 TYR A OH    1 
ATOM   1085 N  N     . ASP A 1 143 ? 2.307   -5.797  12.662  1.00 21.82  ?  143 ASP A N     1 
ATOM   1086 C  CA    . ASP A 1 143 ? 1.112   -6.521  13.094  1.00 25.07  ?  143 ASP A CA    1 
ATOM   1087 C  C     . ASP A 1 143 ? 1.192   -8.037  12.923  1.00 21.98  ?  143 ASP A C     1 
ATOM   1088 O  O     . ASP A 1 143 ? 0.204   -8.725  13.196  1.00 21.65  ?  143 ASP A O     1 
ATOM   1089 C  CB    . ASP A 1 143 ? -0.125  -5.986  12.357  1.00 21.36  ?  143 ASP A CB    1 
ATOM   1090 C  CG    . ASP A 1 143 ? 0.080   -5.885  10.852  1.00 31.84  ?  143 ASP A CG    1 
ATOM   1091 O  OD1   . ASP A 1 143 ? 1.104   -6.397  10.338  1.00 32.74  ?  143 ASP A OD1   1 
ATOM   1092 O  OD2   . ASP A 1 143 ? -0.794  -5.287  10.180  1.00 42.29  ?  143 ASP A OD2   1 
ATOM   1093 N  N     . ARG A 1 144 ? 2.332   -8.588  12.503  1.00 20.95  ?  144 ARG A N     1 
ATOM   1094 C  CA    . ARG A 1 144 ? 2.439   -10.028 12.306  1.00 18.74  ?  144 ARG A CA    1 
ATOM   1095 C  C     . ARG A 1 144 ? 3.651   -10.680 12.951  1.00 16.04  ?  144 ARG A C     1 
ATOM   1096 O  O     . ARG A 1 144 ? 3.856   -11.879 12.742  1.00 23.81  ?  144 ARG A O     1 
ATOM   1097 C  CB    . ARG A 1 144 ? 2.471   -10.370 10.812  1.00 27.05  ?  144 ARG A CB    1 
ATOM   1098 C  CG    . ARG A 1 144 ? 1.299   -9.862  10.053  1.00 26.18  ?  144 ARG A CG    1 
ATOM   1099 C  CD    . ARG A 1 144 ? 1.519   -10.036 8.579   1.00 25.78  ?  144 ARG A CD    1 
ATOM   1100 N  NE    . ARG A 1 144 ? 0.377   -9.484  7.868   1.00 30.96  ?  144 ARG A NE    1 
ATOM   1101 C  CZ    . ARG A 1 144 ? 0.016   -9.842  6.649   1.00 29.64  ?  144 ARG A CZ    1 
ATOM   1102 N  NH1   . ARG A 1 144 ? 0.701   -10.741 5.967   1.00 29.62  ?  144 ARG A NH1   1 
ATOM   1103 N  NH2   . ARG A 1 144 ? -1.056  -9.276  6.100   1.00 32.61  ?  144 ARG A NH2   1 
ATOM   1104 N  N     . GLY A 1 145 ? 4.469   -9.945  13.700  1.00 13.42  ?  145 GLY A N     1 
ATOM   1105 C  CA    . GLY A 1 145 ? 5.665   -10.558 14.265  1.00 16.14  ?  145 GLY A CA    1 
ATOM   1106 C  C     . GLY A 1 145 ? 6.791   -10.873 13.286  1.00 16.72  ?  145 GLY A C     1 
ATOM   1107 O  O     . GLY A 1 145 ? 7.591   -11.776 13.557  1.00 14.64  ?  145 GLY A O     1 
ATOM   1108 N  N     . LEU A 1 146 ? 6.887   -10.146 12.163  1.00 11.63  ?  146 LEU A N     1 
ATOM   1109 C  CA    . LEU A 1 146 ? 8.017   -10.347 11.246  1.00 17.68  ?  146 LEU A CA    1 
ATOM   1110 C  C     . LEU A 1 146 ? 9.355   -10.140 11.954  1.00 16.37  ?  146 LEU A C     1 
ATOM   1111 O  O     . LEU A 1 146 ? 10.327  -10.851 11.678  1.00 16.91  ?  146 LEU A O     1 
ATOM   1112 C  CB    . LEU A 1 146 ? 7.907   -9.410  10.046  1.00 12.62  ?  146 LEU A CB    1 
ATOM   1113 C  CG    . LEU A 1 146 ? 8.983   -9.467  8.938   1.00 18.18  ?  146 LEU A CG    1 
ATOM   1114 C  CD1   . LEU A 1 146 ? 9.059   -10.825 8.216   1.00 18.67  ?  146 LEU A CD1   1 
ATOM   1115 C  CD2   . LEU A 1 146 ? 8.754   -8.379  7.931   1.00 13.13  ?  146 LEU A CD2   1 
ATOM   1116 N  N     . LEU A 1 147 ? 9.417   -9.181  12.881  1.00 17.61  ?  147 LEU A N     1 
ATOM   1117 C  CA    . LEU A 1 147 ? 10.634  -8.956  13.659  1.00 14.84  ?  147 LEU A CA    1 
ATOM   1118 C  C     . LEU A 1 147 ? 11.058  -10.194 14.440  1.00 17.11  ?  147 LEU A C     1 
ATOM   1119 O  O     . LEU A 1 147 ? 12.248  -10.361 14.729  1.00 16.57  ?  147 LEU A O     1 
ATOM   1120 C  CB    . LEU A 1 147 ? 10.426  -7.793  14.628  1.00 15.89  ?  147 LEU A CB    1 
ATOM   1121 C  CG    . LEU A 1 147 ? 11.686  -7.394  15.399  1.00 18.16  ?  147 LEU A CG    1 
ATOM   1122 C  CD1   . LEU A 1 147 ? 12.755  -6.837  14.448  1.00 13.70  ?  147 LEU A CD1   1 
ATOM   1123 C  CD2   . LEU A 1 147 ? 11.350  -6.413  16.497  1.00 12.09  ?  147 LEU A CD2   1 
ATOM   1124 N  N     . ASP A 1 148 ? 10.101  -11.041 14.843  1.00 15.89  ?  148 ASP A N     1 
ATOM   1125 C  CA    . ASP A 1 148 ? 10.452  -12.290 15.521  1.00 18.04  ?  148 ASP A CA    1 
ATOM   1126 C  C     . ASP A 1 148 ? 11.078  -13.298 14.561  1.00 14.50  ?  148 ASP A C     1 
ATOM   1127 O  O     . ASP A 1 148 ? 11.845  -14.172 14.991  1.00 15.66  ?  148 ASP A O     1 
ATOM   1128 C  CB    . ASP A 1 148 ? 9.218   -12.918 16.206  1.00 18.80  ?  148 ASP A CB    1 
ATOM   1129 C  CG    . ASP A 1 148 ? 8.595   -12.029 17.288  1.00 24.40  ?  148 ASP A CG    1 
ATOM   1130 O  OD1   . ASP A 1 148 ? 8.667   -10.786 17.177  1.00 31.57  ?  148 ASP A OD1   1 
ATOM   1131 O  OD2   . ASP A 1 148 ? 8.009   -12.589 18.254  1.00 24.85  ?  148 ASP A OD2   1 
ATOM   1132 N  N     . VAL A 1 149 ? 10.773  -13.187 13.267  1.00 18.74  ?  149 VAL A N     1 
ATOM   1133 C  CA    . VAL A 1 149 ? 11.361  -14.066 12.252  1.00 14.16  ?  149 VAL A CA    1 
ATOM   1134 C  C     . VAL A 1 149 ? 12.775  -13.627 11.910  1.00 15.64  ?  149 VAL A C     1 
ATOM   1135 O  O     . VAL A 1 149 ? 13.735  -14.393 12.039  1.00 16.07  ?  149 VAL A O     1 
ATOM   1136 C  CB    . VAL A 1 149 ? 10.489  -14.081 10.989  1.00 13.29  ?  149 VAL A CB    1 
ATOM   1137 C  CG1   . VAL A 1 149 ? 11.116  -14.990 9.943   1.00 16.00  ?  149 VAL A CG1   1 
ATOM   1138 C  CG2   . VAL A 1 149 ? 9.071   -14.478 11.329  1.00 14.31  ?  149 VAL A CG2   1 
ATOM   1139 N  N     . THR A 1 150 ? 12.923  -12.385 11.453  1.00 15.56  ?  150 THR A N     1 
ATOM   1140 C  CA    . THR A 1 150 ? 14.243  -11.868 11.131  1.00 17.06  ?  150 THR A CA    1 
ATOM   1141 C  C     . THR A 1 150 ? 14.172  -10.341 11.075  1.00 19.20  ?  150 THR A C     1 
ATOM   1142 O  O     . THR A 1 150 ? 13.101  -9.737  11.200  1.00 15.69  ?  150 THR A O     1 
ATOM   1143 C  CB    . THR A 1 150 ? 14.782  -12.518 9.826   1.00 19.82  ?  150 THR A CB    1 
ATOM   1144 O  OG1   . THR A 1 150 ? 16.167  -12.200 9.647   1.00 25.63  ?  150 THR A OG1   1 
ATOM   1145 C  CG2   . THR A 1 150 ? 13.964  -12.132 8.571   1.00 12.61  ?  150 THR A CG2   1 
ATOM   1146 N  N     . ASN A 1 151 ? 15.343  -9.724  10.916  1.00 19.04  ?  151 ASN A N     1 
ATOM   1147 C  CA    . ASN A 1 151 ? 15.466  -8.273  10.980  1.00 16.77  ?  151 ASN A CA    1 
ATOM   1148 C  C     . ASN A 1 151 ? 14.806  -7.620  9.771   1.00 20.96  ?  151 ASN A C     1 
ATOM   1149 O  O     . ASN A 1 151 ? 15.138  -7.952  8.625   1.00 19.53  ?  151 ASN A O     1 
ATOM   1150 C  CB    . ASN A 1 151 ? 16.947  -7.893  11.037  1.00 17.07  ?  151 ASN A CB    1 
ATOM   1151 C  CG    . ASN A 1 151 ? 17.158  -6.466  11.487  1.00 22.82  ?  151 ASN A CG    1 
ATOM   1152 O  OD1   . ASN A 1 151 ? 16.314  -5.897  12.171  1.00 14.75  ?  151 ASN A OD1   1 
ATOM   1153 N  ND2   . ASN A 1 151 ? 18.273  -5.872  11.087  1.00 23.13  ?  151 ASN A ND2   1 
ATOM   1154 N  N     . HIS A 1 152 ? 13.882  -6.673  10.000  1.00 13.85  ?  152 HIS A N     1 
ATOM   1155 C  CA    . HIS A 1 152 ? 13.303  -5.980  8.849   1.00 19.33  ?  152 HIS A CA    1 
ATOM   1156 C  C     . HIS A 1 152 ? 13.508  -4.470  8.865   1.00 17.59  ?  152 HIS A C     1 
ATOM   1157 O  O     . HIS A 1 152 ? 12.910  -3.775  8.039   1.00 17.63  ?  152 HIS A O     1 
ATOM   1158 C  CB    . HIS A 1 152 ? 11.815  -6.327  8.648   1.00 12.88  ?  152 HIS A CB    1 
ATOM   1159 C  CG    . HIS A 1 152 ? 10.903  -5.955  9.773   1.00 17.82  ?  152 HIS A CG    1 
ATOM   1160 N  ND1   . HIS A 1 152 ? 10.237  -4.748  9.821   1.00 14.80  ?  152 HIS A ND1   1 
ATOM   1161 C  CD2   . HIS A 1 152 ? 10.455  -6.674  10.834  1.00 16.17  ?  152 HIS A CD2   1 
ATOM   1162 C  CE1   . HIS A 1 152 ? 9.470   -4.715  10.898  1.00 17.28  ?  152 HIS A CE1   1 
ATOM   1163 N  NE2   . HIS A 1 152 ? 9.580   -5.872  11.526  1.00 13.80  ?  152 HIS A NE2   1 
ATOM   1164 N  N     . PHE A 1 153 ? 14.374  -3.952  9.730   1.00 17.75  ?  153 PHE A N     1 
ATOM   1165 C  CA    . PHE A 1 153 ? 14.786  -2.562  9.651   1.00 17.37  ?  153 PHE A CA    1 
ATOM   1166 C  C     . PHE A 1 153 ? 16.182  -2.426  10.257  1.00 18.98  ?  153 PHE A C     1 
ATOM   1167 O  O     . PHE A 1 153 ? 16.846  -3.414  10.597  1.00 19.19  ?  153 PHE A O     1 
ATOM   1168 C  CB    . PHE A 1 153 ? 13.755  -1.618  10.308  1.00 17.48  ?  153 PHE A CB    1 
ATOM   1169 C  CG    . PHE A 1 153 ? 13.309  -2.033  11.672  1.00 15.75  ?  153 PHE A CG    1 
ATOM   1170 C  CD1   . PHE A 1 153 ? 14.072  -1.730  12.790  1.00 16.29  ?  153 PHE A CD1   1 
ATOM   1171 C  CD2   . PHE A 1 153 ? 12.100  -2.699  11.850  1.00 18.11  ?  153 PHE A CD2   1 
ATOM   1172 C  CE1   . PHE A 1 153 ? 13.637  -2.126  14.087  1.00 17.92  ?  153 PHE A CE1   1 
ATOM   1173 C  CE2   . PHE A 1 153 ? 11.657  -3.084  13.127  1.00 15.18  ?  153 PHE A CE2   1 
ATOM   1174 C  CZ    . PHE A 1 153 ? 12.430  -2.803  14.246  1.00 11.76  ?  153 PHE A CZ    1 
ATOM   1175 N  N     . ALA A 1 154 ? 16.639  -1.190  10.363  1.00 22.52  ?  154 ALA A N     1 
ATOM   1176 C  CA    . ALA A 1 154 ? 18.029  -0.901  10.674  1.00 18.56  ?  154 ALA A CA    1 
ATOM   1177 C  C     . ALA A 1 154 ? 18.063  0.229   11.662  1.00 10.82  ?  154 ALA A C     1 
ATOM   1178 O  O     . ALA A 1 154 ? 17.097  1.003   11.763  1.00 12.24  ?  154 ALA A O     1 
ATOM   1179 C  CB    . ALA A 1 154 ? 18.809  -0.536  9.406   1.00 13.97  ?  154 ALA A CB    1 
ATOM   1180 N  N     . PRO A 1 155 ? 19.154  0.383   12.431  1.00 14.37  ?  155 PRO A N     1 
ATOM   1181 C  CA    . PRO A 1 155 ? 19.171  1.388   13.508  1.00 16.17  ?  155 PRO A CA    1 
ATOM   1182 C  C     . PRO A 1 155 ? 18.831  2.796   13.048  1.00 17.35  ?  155 PRO A C     1 
ATOM   1183 O  O     . PRO A 1 155 ? 18.113  3.506   13.757  1.00 9.75   ?  155 PRO A O     1 
ATOM   1184 C  CB    . PRO A 1 155 ? 20.604  1.297   14.053  1.00 16.31  ?  155 PRO A CB    1 
ATOM   1185 C  CG    . PRO A 1 155 ? 21.039  -0.085  13.750  1.00 16.63  ?  155 PRO A CG    1 
ATOM   1186 C  CD    . PRO A 1 155 ? 20.374  -0.455  12.440  1.00 16.12  ?  155 PRO A CD    1 
ATOM   1187 N  N     . SER A 1 156 ? 19.311  3.221   11.873  1.00 15.03  ?  156 SER A N     1 
ATOM   1188 C  CA    . SER A 1 156 ? 19.002  4.567   11.394  1.00 14.98  ?  156 SER A CA    1 
ATOM   1189 C  C     . SER A 1 156 ? 17.504  4.861   11.298  1.00 15.99  ?  156 SER A C     1 
ATOM   1190 O  O     . SER A 1 156 ? 17.138  6.035   11.135  1.00 11.85  ?  156 SER A O     1 
ATOM   1191 C  CB    . SER A 1 156 ? 19.649  4.791   10.026  1.00 14.44  ?  156 SER A CB    1 
ATOM   1192 O  OG    . SER A 1 156 ? 21.052  4.850   10.181  1.00 16.42  ?  156 SER A OG    1 
ATOM   1193 N  N     . ALA A 1 157 ? 16.634  3.846   11.406  1.00 12.23  ?  157 ALA A N     1 
ATOM   1194 C  CA    . ALA A 1 157 ? 15.201  4.042   11.253  1.00 12.37  ?  157 ALA A CA    1 
ATOM   1195 C  C     . ALA A 1 157 ? 14.479  4.080   12.577  1.00 9.71   ?  157 ALA A C     1 
ATOM   1196 O  O     . ALA A 1 157 ? 13.258  4.190   12.581  1.00 6.59   ?  157 ALA A O     1 
ATOM   1197 C  CB    . ALA A 1 157 ? 14.575  2.948   10.386  1.00 8.02   ?  157 ALA A CB    1 
ATOM   1198 N  N     . VAL A 1 158 ? 15.212  4.041   13.687  1.00 10.66  ?  158 VAL A N     1 
ATOM   1199 C  CA    . VAL A 1 158 ? 14.669  3.757   15.003  1.00 11.27  ?  158 VAL A CA    1 
ATOM   1200 C  C     . VAL A 1 158 ? 14.827  4.991   15.882  1.00 12.07  ?  158 VAL A C     1 
ATOM   1201 O  O     . VAL A 1 158 ? 15.913  5.575   15.956  1.00 9.55   ?  158 VAL A O     1 
ATOM   1202 C  CB    . VAL A 1 158 ? 15.361  2.546   15.655  1.00 11.43  ?  158 VAL A CB    1 
ATOM   1203 C  CG1   . VAL A 1 158 ? 14.917  2.409   17.117  1.00 13.37  ?  158 VAL A CG1   1 
ATOM   1204 C  CG2   . VAL A 1 158 ? 15.034  1.248   14.896  1.00 13.99  ?  158 VAL A CG2   1 
ATOM   1205 N  N     . VAL A 1 159 ? 13.750  5.368   16.563  1.00 9.85   ?  159 VAL A N     1 
ATOM   1206 C  CA    . VAL A 1 159 ? 13.807  6.337   17.652  1.00 10.36  ?  159 VAL A CA    1 
ATOM   1207 C  C     . VAL A 1 159 ? 13.155  5.693   18.860  1.00 13.10  ?  159 VAL A C     1 
ATOM   1208 O  O     . VAL A 1 159 ? 12.027  5.196   18.768  1.00 12.81  ?  159 VAL A O     1 
ATOM   1209 C  CB    . VAL A 1 159 ? 13.106  7.660   17.314  1.00 10.74  ?  159 VAL A CB    1 
ATOM   1210 C  CG1   . VAL A 1 159 ? 13.443  8.685   18.385  1.00 14.55  ?  159 VAL A CG1   1 
ATOM   1211 C  CG2   . VAL A 1 159 ? 13.546  8.156   15.969  1.00 11.96  ?  159 VAL A CG2   1 
ATOM   1212 N  N     . CYS A 1 160 ? 13.856  5.699   19.990  1.00 12.55  ?  160 CYS A N     1 
ATOM   1213 C  CA    . CYS A 1 160 ? 13.377  4.919   21.107  1.00 11.53  ?  160 CYS A CA    1 
ATOM   1214 C  C     . CYS A 1 160 ? 13.719  5.620   22.409  1.00 15.64  ?  160 CYS A C     1 
ATOM   1215 O  O     . CYS A 1 160 ? 14.649  6.431   22.488  1.00 13.50  ?  160 CYS A O     1 
ATOM   1216 C  CB    . CYS A 1 160 ? 13.957  3.494   21.069  1.00 15.50  ?  160 CYS A CB    1 
ATOM   1217 S  SG    . CYS A 1 160 ? 15.728  3.402   21.433  1.00 20.86  ?  160 CYS A SG    1 
ATOM   1218 N  N     . ARG A 1 161 ? 12.912  5.296   23.421  1.00 11.07  ?  161 ARG A N     1 
ATOM   1219 C  CA    . ARG A 1 161 ? 13.106  5.768   24.779  1.00 15.27  ?  161 ARG A CA    1 
ATOM   1220 C  C     . ARG A 1 161 ? 14.439  5.260   25.329  1.00 15.77  ?  161 ARG A C     1 
ATOM   1221 O  O     . ARG A 1 161 ? 14.738  4.064   25.241  1.00 15.30  ?  161 ARG A O     1 
ATOM   1222 C  CB    . ARG A 1 161 ? 11.916  5.277   25.630  1.00 8.32   ?  161 ARG A CB    1 
ATOM   1223 C  CG    . ARG A 1 161 ? 11.861  5.775   27.005  1.00 12.46  ?  161 ARG A CG    1 
ATOM   1224 C  CD    . ARG A 1 161 ? 10.565  5.322   27.704  1.00 9.41   ?  161 ARG A CD    1 
ATOM   1225 N  NE    . ARG A 1 161 ? 9.352   5.738   27.008  1.00 6.25   ?  161 ARG A NE    1 
ATOM   1226 C  CZ    . ARG A 1 161 ? 8.860   6.965   27.078  1.00 10.16  ?  161 ARG A CZ    1 
ATOM   1227 N  NH1   . ARG A 1 161 ? 9.433   7.888   27.831  1.00 7.16   ?  161 ARG A NH1   1 
ATOM   1228 N  NH2   . ARG A 1 161 ? 7.791   7.285   26.344  1.00 10.65  ?  161 ARG A NH2   1 
ATOM   1229 N  N     . SER A 1 162 ? 15.236  6.184   25.907  1.00 13.66  ?  162 SER A N     1 
ATOM   1230 C  CA    . SER A 1 162 ? 16.619  6.018   26.366  1.00 16.06  ?  162 SER A CA    1 
ATOM   1231 C  C     . SER A 1 162 ? 16.967  4.602   26.809  1.00 20.28  ?  162 SER A C     1 
ATOM   1232 O  O     . SER A 1 162 ? 16.498  4.141   27.854  1.00 18.58  ?  162 SER A O     1 
ATOM   1233 C  CB    . SER A 1 162 ? 16.921  6.968   27.526  1.00 20.08  ?  162 SER A CB    1 
ATOM   1234 O  OG    . SER A 1 162 ? 18.154  6.628   28.149  1.00 22.13  ?  162 SER A OG    1 
ATOM   1235 N  N     . PRO A 1 163 ? 17.796  3.884   26.051  1.00 20.52  ?  163 PRO A N     1 
ATOM   1236 C  CA    . PRO A 1 163 ? 18.176  2.529   26.476  1.00 15.82  ?  163 PRO A CA    1 
ATOM   1237 C  C     . PRO A 1 163 ? 19.061  2.517   27.711  1.00 19.58  ?  163 PRO A C     1 
ATOM   1238 O  O     . PRO A 1 163 ? 19.067  1.511   28.428  1.00 20.15  ?  163 PRO A O     1 
ATOM   1239 C  CB    . PRO A 1 163 ? 18.905  1.965   25.247  1.00 21.08  ?  163 PRO A CB    1 
ATOM   1240 C  CG    . PRO A 1 163 ? 18.408  2.819   24.089  1.00 19.05  ?  163 PRO A CG    1 
ATOM   1241 C  CD    . PRO A 1 163 ? 18.269  4.192   24.691  1.00 17.50  ?  163 PRO A CD    1 
ATOM   1242 N  N     . ARG A 1 164 ? 19.801  3.595   27.994  1.00 19.33  ?  164 ARG A N     1 
ATOM   1243 C  CA    . ARG A 1 164 ? 20.556  3.641   29.243  1.00 22.68  ?  164 ARG A CA    1 
ATOM   1244 C  C     . ARG A 1 164 ? 19.626  3.623   30.454  1.00 25.48  ?  164 ARG A C     1 
ATOM   1245 O  O     . ARG A 1 164 ? 19.928  2.984   31.466  1.00 25.48  ?  164 ARG A O     1 
ATOM   1246 C  CB    . ARG A 1 164 ? 21.446  4.877   29.291  1.00 29.68  ?  164 ARG A CB    1 
ATOM   1247 C  CG    . ARG A 1 164 ? 21.831  5.278   30.716  1.00 34.72  ?  164 ARG A CG    1 
ATOM   1248 C  CD    . ARG A 1 164 ? 22.602  6.568   30.749  1.00 29.22  ?  164 ARG A CD    1 
ATOM   1249 N  NE    . ARG A 1 164 ? 21.726  7.725   30.667  1.00 35.34  ?  164 ARG A NE    1 
ATOM   1250 C  CZ    . ARG A 1 164 ? 22.143  8.981   30.764  1.00 35.36  ?  164 ARG A CZ    1 
ATOM   1251 N  NH1   . ARG A 1 164 ? 23.426  9.275   30.899  1.00 33.31  ?  164 ARG A NH1   1 
ATOM   1252 N  NH2   . ARG A 1 164 ? 21.249  9.966   30.733  1.00 40.36  ?  164 ARG A NH2   1 
ATOM   1253 N  N     . SER A 1 165 ? 18.488  4.315   30.372  1.00 22.09  ?  165 SER A N     1 
ATOM   1254 C  CA    . SER A 1 165 ? 17.552  4.291   31.492  1.00 27.34  ?  165 SER A CA    1 
ATOM   1255 C  C     . SER A 1 165 ? 16.957  2.897   31.697  1.00 25.93  ?  165 SER A C     1 
ATOM   1256 O  O     . SER A 1 165 ? 16.573  2.546   32.817  1.00 26.93  ?  165 SER A O     1 
ATOM   1257 C  CB    . SER A 1 165 ? 16.455  5.342   31.284  1.00 23.86  ?  165 SER A CB    1 
ATOM   1258 O  OG    . SER A 1 165 ? 15.535  4.968   30.263  1.00 18.85  ?  165 SER A OG    1 
ATOM   1259 N  N     . ALA A 1 166 ? 16.909  2.081   30.646  1.00 27.48  ?  166 ALA A N     1 
ATOM   1260 C  CA    . ALA A 1 166 ? 16.456  0.699   30.756  1.00 25.41  ?  166 ALA A CA    1 
ATOM   1261 C  C     . ALA A 1 166 ? 17.581  -0.271  31.093  1.00 23.93  ?  166 ALA A C     1 
ATOM   1262 O  O     . ALA A 1 166 ? 17.305  -1.442  31.389  1.00 30.02  ?  166 ALA A O     1 
ATOM   1263 C  CB    . ALA A 1 166 ? 15.786  0.261   29.447  1.00 20.84  ?  166 ALA A CB    1 
ATOM   1264 N  N     . GLY A 1 167 ? 18.830  0.187   31.069  1.00 21.60  ?  167 GLY A N     1 
ATOM   1265 C  CA    . GLY A 1 167 ? 19.964  -0.705  31.202  1.00 24.01  ?  167 GLY A CA    1 
ATOM   1266 C  C     . GLY A 1 167 ? 20.185  -1.612  30.017  1.00 23.60  ?  167 GLY A C     1 
ATOM   1267 O  O     . GLY A 1 167 ? 20.825  -2.655  30.159  1.00 29.79  ?  167 GLY A O     1 
ATOM   1268 N  N     . ALA A 1 168 ? 19.662  -1.251  28.847  1.00 20.42  ?  168 ALA A N     1 
ATOM   1269 C  CA    . ALA A 1 168 ? 19.703  -2.101  27.667  1.00 21.05  ?  168 ALA A CA    1 
ATOM   1270 C  C     . ALA A 1 168 ? 20.776  -1.595  26.711  1.00 25.10  ?  168 ALA A C     1 
ATOM   1271 O  O     . ALA A 1 168 ? 20.826  -0.392  26.410  1.00 20.95  ?  168 ALA A O     1 
ATOM   1272 C  CB    . ALA A 1 168 ? 18.343  -2.129  26.976  1.00 18.86  ?  168 ALA A CB    1 
ATOM   1273 N  N     . PHE A 1 169 ? 21.635  -2.507  26.241  1.00 16.01  ?  169 PHE A N     1 
ATOM   1274 C  CA    . PHE A 1 169 ? 22.784  -2.124  25.424  1.00 22.56  ?  169 PHE A CA    1 
ATOM   1275 C  C     . PHE A 1 169 ? 23.014  -3.141  24.314  1.00 15.77  ?  169 PHE A C     1 
ATOM   1276 O  O     . PHE A 1 169 ? 22.426  -4.227  24.291  1.00 14.02  ?  169 PHE A O     1 
ATOM   1277 C  CB    . PHE A 1 169 ? 24.059  -1.975  26.268  1.00 24.76  ?  169 PHE A CB    1 
ATOM   1278 C  CG    . PHE A 1 169 ? 24.012  -0.827  27.236  1.00 22.85  ?  169 PHE A CG    1 
ATOM   1279 C  CD1   . PHE A 1 169 ? 24.386  0.441   26.841  1.00 19.26  ?  169 PHE A CD1   1 
ATOM   1280 C  CD2   . PHE A 1 169 ? 23.580  -1.018  28.538  1.00 24.60  ?  169 PHE A CD2   1 
ATOM   1281 C  CE1   . PHE A 1 169 ? 24.332  1.517   27.730  1.00 25.14  ?  169 PHE A CE1   1 
ATOM   1282 C  CE2   . PHE A 1 169 ? 23.522  0.048   29.431  1.00 28.31  ?  169 PHE A CE2   1 
ATOM   1283 C  CZ    . PHE A 1 169 ? 23.904  1.320   29.019  1.00 25.34  ?  169 PHE A CZ    1 
ATOM   1284 N  N     . PHE A 1 170 ? 23.868  -2.760  23.369  1.00 18.57  ?  170 PHE A N     1 
ATOM   1285 C  CA    . PHE A 1 170 ? 24.239  -3.657  22.276  1.00 18.72  ?  170 PHE A CA    1 
ATOM   1286 C  C     . PHE A 1 170 ? 25.209  -4.733  22.761  1.00 14.53  ?  170 PHE A C     1 
ATOM   1287 O  O     . PHE A 1 170 ? 26.091  -4.477  23.589  1.00 17.34  ?  170 PHE A O     1 
ATOM   1288 C  CB    . PHE A 1 170 ? 24.863  -2.866  21.116  1.00 16.41  ?  170 PHE A CB    1 
ATOM   1289 C  CG    . PHE A 1 170 ? 23.856  -2.085  20.293  1.00 18.29  ?  170 PHE A CG    1 
ATOM   1290 C  CD1   . PHE A 1 170 ? 23.449  -0.813  20.691  1.00 16.14  ?  170 PHE A CD1   1 
ATOM   1291 C  CD2   . PHE A 1 170 ? 23.310  -2.630  19.134  1.00 13.52  ?  170 PHE A CD2   1 
ATOM   1292 C  CE1   . PHE A 1 170 ? 22.521  -0.098  19.943  1.00 17.54  ?  170 PHE A CE1   1 
ATOM   1293 C  CE2   . PHE A 1 170 ? 22.382  -1.927  18.381  1.00 14.04  ?  170 PHE A CE2   1 
ATOM   1294 C  CZ    . PHE A 1 170 ? 21.984  -0.659  18.786  1.00 18.14  ?  170 PHE A CZ    1 
ATOM   1295 N  N     . ASP A 1 171 ? 25.064  -5.940  22.221  1.00 16.97  ?  171 ASP A N     1 
ATOM   1296 C  CA    . ASP A 1 171 ? 25.972  -7.033  22.554  1.00 17.08  ?  171 ASP A CA    1 
ATOM   1297 C  C     . ASP A 1 171 ? 27.266  -6.876  21.750  1.00 18.97  ?  171 ASP A C     1 
ATOM   1298 O  O     . ASP A 1 171 ? 27.252  -6.905  20.511  1.00 19.32  ?  171 ASP A O     1 
ATOM   1299 C  CB    . ASP A 1 171 ? 25.276  -8.368  22.289  1.00 23.35  ?  171 ASP A CB    1 
ATOM   1300 C  CG    . ASP A 1 171 ? 26.115  -9.576  22.690  1.00 25.98  ?  171 ASP A CG    1 
ATOM   1301 O  OD1   . ASP A 1 171 ? 27.332  -9.417  22.965  1.00 25.98  ?  171 ASP A OD1   1 
ATOM   1302 O  OD2   . ASP A 1 171 ? 25.549  -10.697 22.696  1.00 22.94  ?  171 ASP A OD2   1 
ATOM   1303 N  N     . THR A 1 172 ? 28.390  -6.696  22.454  1.00 18.66  ?  172 THR A N     1 
ATOM   1304 C  CA    . THR A 1 172 ? 29.647  -6.408  21.770  1.00 18.77  ?  172 THR A CA    1 
ATOM   1305 C  C     . THR A 1 172 ? 30.222  -7.630  21.064  1.00 26.89  ?  172 THR A C     1 
ATOM   1306 O  O     . THR A 1 172 ? 31.077  -7.471  20.178  1.00 26.31  ?  172 THR A O     1 
ATOM   1307 C  CB    . THR A 1 172 ? 30.681  -5.845  22.754  1.00 22.97  ?  172 THR A CB    1 
ATOM   1308 O  OG1   . THR A 1 172 ? 30.720  -6.657  23.929  1.00 25.10  ?  172 THR A OG1   1 
ATOM   1309 C  CG2   . THR A 1 172 ? 30.342  -4.405  23.158  1.00 20.98  ?  172 THR A CG2   1 
ATOM   1310 N  N     . ALA A 1 173 ? 29.772  -8.838  21.434  1.00 22.80  ?  173 ALA A N     1 
ATOM   1311 C  CA    . ALA A 1 173 ? 30.182  -10.072 20.775  1.00 26.45  ?  173 ALA A CA    1 
ATOM   1312 C  C     . ALA A 1 173 ? 29.573  -10.240 19.388  1.00 28.30  ?  173 ALA A C     1 
ATOM   1313 O  O     . ALA A 1 173 ? 30.007  -11.128 18.645  1.00 30.49  ?  173 ALA A O     1 
ATOM   1314 C  CB    . ALA A 1 173 ? 29.801  -11.285 21.642  1.00 24.39  ?  173 ALA A CB    1 
ATOM   1315 N  N     . LEU A 1 174 ? 28.565  -9.453  19.029  1.00 21.58  ?  174 LEU A N     1 
ATOM   1316 C  CA    . LEU A 1 174 ? 27.909  -9.587  17.734  1.00 22.57  ?  174 LEU A CA    1 
ATOM   1317 C  C     . LEU A 1 174 ? 28.385  -8.462  16.826  1.00 24.81  ?  174 LEU A C     1 
ATOM   1318 O  O     . LEU A 1 174 ? 28.266  -7.282  17.186  1.00 22.07  ?  174 LEU A O     1 
ATOM   1319 C  CB    . LEU A 1 174 ? 26.391  -9.542  17.892  1.00 20.09  ?  174 LEU A CB    1 
ATOM   1320 C  CG    . LEU A 1 174 ? 25.766  -10.800 18.487  1.00 22.48  ?  174 LEU A CG    1 
ATOM   1321 C  CD1   . LEU A 1 174 ? 24.267  -10.616 18.619  1.00 24.50  ?  174 LEU A CD1   1 
ATOM   1322 C  CD2   . LEU A 1 174 ? 26.112  -12.023 17.626  1.00 21.55  ?  174 LEU A CD2   1 
ATOM   1323 N  N     . GLY A 1 175 ? 28.933  -8.822  15.663  1.00 22.05  ?  175 GLY A N     1 
ATOM   1324 C  CA    . GLY A 1 175 ? 29.364  -7.821  14.704  1.00 19.24  ?  175 GLY A CA    1 
ATOM   1325 C  C     . GLY A 1 175 ? 28.375  -7.665  13.566  1.00 23.14  ?  175 GLY A C     1 
ATOM   1326 O  O     . GLY A 1 175 ? 28.419  -6.686  12.810  1.00 20.81  ?  175 GLY A O     1 
ATOM   1327 N  N     . VAL A 1 176 ? 27.493  -8.653  13.420  1.00 21.12  ?  176 VAL A N     1 
ATOM   1328 C  CA    . VAL A 1 176 ? 26.436  -8.639  12.416  1.00 21.29  ?  176 VAL A CA    1 
ATOM   1329 C  C     . VAL A 1 176 ? 25.152  -9.086  13.108  1.00 24.53  ?  176 VAL A C     1 
ATOM   1330 O  O     . VAL A 1 176 ? 25.185  -9.900  14.043  1.00 16.54  ?  176 VAL A O     1 
ATOM   1331 C  CB    . VAL A 1 176 ? 26.791  -9.526  11.189  1.00 28.32  ?  176 VAL A CB    1 
ATOM   1332 C  CG1   . VAL A 1 176 ? 26.978  -10.958 11.570  1.00 23.43  ?  176 VAL A CG1   1 
ATOM   1333 C  CG2   . VAL A 1 176 ? 25.752  -9.400  10.068  1.00 32.03  ?  176 VAL A CG2   1 
ATOM   1334 N  N     . GLU A 1 177 ? 24.026  -8.503  12.688  1.00 22.95  ?  177 GLU A N     1 
ATOM   1335 C  CA    . GLU A 1 177 ? 22.741  -8.669  13.359  1.00 22.41  ?  177 GLU A CA    1 
ATOM   1336 C  C     . GLU A 1 177 ? 22.777  -8.177  14.809  1.00 22.20  ?  177 GLU A C     1 
ATOM   1337 O  O     . GLU A 1 177 ? 21.877  -8.507  15.605  1.00 18.26  ?  177 GLU A O     1 
ATOM   1338 C  CB    . GLU A 1 177 ? 22.266  -10.129 13.310  1.00 16.09  ?  177 GLU A CB    1 
ATOM   1339 C  CG    . GLU A 1 177 ? 21.624  -10.539 11.997  1.00 22.52  ?  177 GLU A CG    1 
ATOM   1340 C  CD    . GLU A 1 177 ? 21.686  -12.061 11.751  1.00 25.69  ?  177 GLU A CD    1 
ATOM   1341 O  OE1   . GLU A 1 177 ? 22.794  -12.639 11.756  1.00 19.27  ?  177 GLU A OE1   1 
ATOM   1342 O  OE2   . GLU A 1 177 ? 20.622  -12.675 11.530  1.00 28.77  ?  177 GLU A OE2   1 
ATOM   1343 N  N     . GLU A 1 178 ? 23.814  -7.417  15.184  1.00 17.92  ?  178 GLU A N     1 
ATOM   1344 C  CA    . GLU A 1 178 ? 23.813  -6.793  16.503  1.00 16.63  ?  178 GLU A CA    1 
ATOM   1345 C  C     . GLU A 1 178 ? 22.585  -5.925  16.686  1.00 15.75  ?  178 GLU A C     1 
ATOM   1346 O  O     . GLU A 1 178 ? 22.048  -5.847  17.792  1.00 15.48  ?  178 GLU A O     1 
ATOM   1347 C  CB    . GLU A 1 178 ? 25.080  -5.961  16.721  1.00 19.42  ?  178 GLU A CB    1 
ATOM   1348 C  CG    . GLU A 1 178 ? 25.026  -4.493  16.235  1.00 17.01  ?  178 GLU A CG    1 
ATOM   1349 C  CD    . GLU A 1 178 ? 25.180  -4.360  14.704  1.00 21.84  ?  178 GLU A CD    1 
ATOM   1350 O  OE1   . GLU A 1 178 ? 25.403  -5.382  14.019  1.00 20.79  ?  178 GLU A OE1   1 
ATOM   1351 O  OE2   . GLU A 1 178 ? 25.061  -3.235  14.181  1.00 19.71  ?  178 GLU A OE2   1 
ATOM   1352 N  N     . ASP A 1 179 ? 22.114  -5.286  15.611  1.00 15.51  ?  179 ASP A N     1 
ATOM   1353 C  CA    . ASP A 1 179 ? 20.933  -4.441  15.717  1.00 18.56  ?  179 ASP A CA    1 
ATOM   1354 C  C     . ASP A 1 179 ? 19.679  -5.273  15.951  1.00 15.60  ?  179 ASP A C     1 
ATOM   1355 O  O     . ASP A 1 179 ? 18.854  -4.925  16.808  1.00 12.11  ?  179 ASP A O     1 
ATOM   1356 C  CB    . ASP A 1 179 ? 20.797  -3.552  14.475  1.00 16.92  ?  179 ASP A CB    1 
ATOM   1357 C  CG    . ASP A 1 179 ? 20.707  -4.345  13.186  1.00 18.44  ?  179 ASP A CG    1 
ATOM   1358 O  OD1   . ASP A 1 179 ? 21.215  -5.481  13.147  1.00 22.46  ?  179 ASP A OD1   1 
ATOM   1359 O  OD2   . ASP A 1 179 ? 20.116  -3.830  12.211  1.00 15.34  ?  179 ASP A OD2   1 
ATOM   1360 N  N     . TRP A 1 180 ? 19.526  -6.391  15.231  1.00 14.78  ?  180 TRP A N     1 
ATOM   1361 C  CA    . TRP A 1 180 ? 18.393  -7.284  15.475  1.00 14.73  ?  180 TRP A CA    1 
ATOM   1362 C  C     . TRP A 1 180 ? 18.337  -7.739  16.936  1.00 16.44  ?  180 TRP A C     1 
ATOM   1363 O  O     . TRP A 1 180 ? 17.311  -7.588  17.616  1.00 19.51  ?  180 TRP A O     1 
ATOM   1364 C  CB    . TRP A 1 180 ? 18.469  -8.495  14.548  1.00 19.56  ?  180 TRP A CB    1 
ATOM   1365 C  CG    . TRP A 1 180 ? 17.197  -9.295  14.553  1.00 19.66  ?  180 TRP A CG    1 
ATOM   1366 C  CD1   . TRP A 1 180 ? 15.923  -8.798  14.545  1.00 13.83  ?  180 TRP A CD1   1 
ATOM   1367 C  CD2   . TRP A 1 180 ? 17.072  -10.727 14.558  1.00 20.89  ?  180 TRP A CD2   1 
ATOM   1368 N  NE1   . TRP A 1 180 ? 15.022  -9.826  14.533  1.00 20.25  ?  180 TRP A NE1   1 
ATOM   1369 C  CE2   . TRP A 1 180 ? 15.695  -11.022 14.555  1.00 20.57  ?  180 TRP A CE2   1 
ATOM   1370 C  CE3   . TRP A 1 180 ? 17.988  -11.784 14.564  1.00 20.08  ?  180 TRP A CE3   1 
ATOM   1371 C  CZ2   . TRP A 1 180 ? 15.206  -12.337 14.562  1.00 20.93  ?  180 TRP A CZ2   1 
ATOM   1372 C  CZ3   . TRP A 1 180 ? 17.502  -13.089 14.578  1.00 21.82  ?  180 TRP A CZ3   1 
ATOM   1373 C  CH2   . TRP A 1 180 ? 16.125  -13.353 14.571  1.00 20.18  ?  180 TRP A CH2   1 
ATOM   1374 N  N     . ASP A 1 181 ? 19.434  -8.319  17.431  1.00 13.32  ?  181 ASP A N     1 
ATOM   1375 C  CA    . ASP A 1 181 ? 19.535  -8.678  18.843  1.00 13.49  ?  181 ASP A CA    1 
ATOM   1376 C  C     . ASP A 1 181 ? 19.100  -7.526  19.755  1.00 16.65  ?  181 ASP A C     1 
ATOM   1377 O  O     . ASP A 1 181 ? 18.390  -7.743  20.752  1.00 14.88  ?  181 ASP A O     1 
ATOM   1378 C  CB    . ASP A 1 181 ? 20.975  -9.100  19.147  1.00 13.30  ?  181 ASP A CB    1 
ATOM   1379 C  CG    . ASP A 1 181 ? 21.191  -9.473  20.602  1.00 19.55  ?  181 ASP A CG    1 
ATOM   1380 O  OD1   . ASP A 1 181 ? 20.593  -10.479 21.061  1.00 19.51  ?  181 ASP A OD1   1 
ATOM   1381 O  OD2   . ASP A 1 181 ? 21.965  -8.761  21.290  1.00 17.07  ?  181 ASP A OD2   1 
ATOM   1382 N  N     . PHE A 1 182 ? 19.505  -6.291  19.422  1.00 14.40  ?  182 PHE A N     1 
ATOM   1383 C  CA    . PHE A 1 182 ? 19.170  -5.129  20.253  1.00 13.50  ?  182 PHE A CA    1 
ATOM   1384 C  C     . PHE A 1 182 ? 17.677  -4.823  20.214  1.00 10.97  ?  182 PHE A C     1 
ATOM   1385 O  O     . PHE A 1 182 ? 17.063  -4.557  21.251  1.00 15.06  ?  182 PHE A O     1 
ATOM   1386 C  CB    . PHE A 1 182 ? 19.974  -3.913  19.792  1.00 16.47  ?  182 PHE A CB    1 
ATOM   1387 C  CG    . PHE A 1 182 ? 19.713  -2.659  20.586  1.00 14.82  ?  182 PHE A CG    1 
ATOM   1388 C  CD1   . PHE A 1 182 ? 20.201  -2.523  21.880  1.00 18.28  ?  182 PHE A CD1   1 
ATOM   1389 C  CD2   . PHE A 1 182 ? 19.004  -1.612  20.033  1.00 12.82  ?  182 PHE A CD2   1 
ATOM   1390 C  CE1   . PHE A 1 182 ? 19.962  -1.360  22.617  1.00 13.56  ?  182 PHE A CE1   1 
ATOM   1391 C  CE2   . PHE A 1 182 ? 18.768  -0.454  20.764  1.00 13.24  ?  182 PHE A CE2   1 
ATOM   1392 C  CZ    . PHE A 1 182 ? 19.252  -0.333  22.048  1.00 12.68  ?  182 PHE A CZ    1 
ATOM   1393 N  N     . PHE A 1 183 ? 17.077  -4.836  19.024  1.00 9.73   ?  183 PHE A N     1 
ATOM   1394 C  CA    . PHE A 1 183 ? 15.647  -4.563  18.928  1.00 11.80  ?  183 PHE A CA    1 
ATOM   1395 C  C     . PHE A 1 183 ? 14.845  -5.623  19.670  1.00 15.85  ?  183 PHE A C     1 
ATOM   1396 O  O     . PHE A 1 183 ? 13.885  -5.299  20.377  1.00 20.04  ?  183 PHE A O     1 
ATOM   1397 C  CB    . PHE A 1 183 ? 15.202  -4.478  17.461  1.00 11.15  ?  183 PHE A CB    1 
ATOM   1398 C  CG    . PHE A 1 183 ? 16.004  -3.479  16.621  1.00 16.41  ?  183 PHE A CG    1 
ATOM   1399 C  CD1   . PHE A 1 183 ? 16.550  -2.358  17.189  1.00 9.36   ?  183 PHE A CD1   1 
ATOM   1400 C  CD2   . PHE A 1 183 ? 16.220  -3.698  15.265  1.00 15.49  ?  183 PHE A CD2   1 
ATOM   1401 C  CE1   . PHE A 1 183 ? 17.297  -1.453  16.416  1.00 16.10  ?  183 PHE A CE1   1 
ATOM   1402 C  CE2   . PHE A 1 183 ? 16.951  -2.784  14.497  1.00 18.15  ?  183 PHE A CE2   1 
ATOM   1403 C  CZ    . PHE A 1 183 ? 17.487  -1.666  15.079  1.00 11.87  ?  183 PHE A CZ    1 
ATOM   1404 N  N     . LEU A 1 184 ? 15.234  -6.897  19.538  1.00 14.52  ?  184 LEU A N     1 
ATOM   1405 C  CA    . LEU A 1 184 ? 14.573  -7.928  20.324  1.00 19.22  ?  184 LEU A CA    1 
ATOM   1406 C  C     . LEU A 1 184 ? 14.820  -7.728  21.814  1.00 15.78  ?  184 LEU A C     1 
ATOM   1407 O  O     . LEU A 1 184 ? 13.934  -7.991  22.629  1.00 14.46  ?  184 LEU A O     1 
ATOM   1408 C  CB    . LEU A 1 184 ? 15.027  -9.318  19.869  1.00 17.75  ?  184 LEU A CB    1 
ATOM   1409 C  CG    . LEU A 1 184 ? 14.621  -9.626  18.421  1.00 18.62  ?  184 LEU A CG    1 
ATOM   1410 C  CD1   . LEU A 1 184 ? 15.387  -10.798 17.927  1.00 14.60  ?  184 LEU A CD1   1 
ATOM   1411 C  CD2   . LEU A 1 184 ? 13.114  -9.900  18.343  1.00 19.69  ?  184 LEU A CD2   1 
ATOM   1412 N  N     . ARG A 1 185 ? 16.013  -7.249  22.192  1.00 16.02  ?  185 ARG A N     1 
ATOM   1413 C  CA    . ARG A 1 185 ? 16.276  -6.995  23.608  1.00 15.45  ?  185 ARG A CA    1 
ATOM   1414 C  C     . ARG A 1 185 ? 15.351  -5.910  24.155  1.00 16.48  ?  185 ARG A C     1 
ATOM   1415 O  O     . ARG A 1 185 ? 14.825  -6.034  25.267  1.00 14.59  ?  185 ARG A O     1 
ATOM   1416 C  CB    . ARG A 1 185 ? 17.744  -6.614  23.824  1.00 13.75  ?  185 ARG A CB    1 
ATOM   1417 C  CG    . ARG A 1 185 ? 18.071  -6.088  25.234  1.00 17.55  ?  185 ARG A CG    1 
ATOM   1418 C  CD    . ARG A 1 185 ? 19.590  -6.007  25.496  1.00 19.26  ?  185 ARG A CD    1 
ATOM   1419 N  NE    . ARG A 1 185 ? 20.237  -7.275  25.192  1.00 23.06  ?  185 ARG A NE    1 
ATOM   1420 C  CZ    . ARG A 1 185 ? 20.918  -7.529  24.081  1.00 22.36  ?  185 ARG A CZ    1 
ATOM   1421 N  NH1   . ARG A 1 185 ? 21.182  -6.577  23.199  1.00 21.17  ?  185 ARG A NH1   1 
ATOM   1422 N  NH2   . ARG A 1 185 ? 21.328  -8.770  23.841  1.00 18.25  ?  185 ARG A NH2   1 
ATOM   1423 N  N     . LEU A 1 186 ? 15.118  -4.845  23.385  1.00 15.12  ?  186 LEU A N     1 
ATOM   1424 C  CA    . LEU A 1 186 ? 14.150  -3.845  23.835  1.00 16.87  ?  186 LEU A CA    1 
ATOM   1425 C  C     . LEU A 1 186 ? 12.730  -4.407  23.835  1.00 16.45  ?  186 LEU A C     1 
ATOM   1426 O  O     . LEU A 1 186 ? 11.962  -4.180  24.776  1.00 13.51  ?  186 LEU A O     1 
ATOM   1427 C  CB    . LEU A 1 186 ? 14.223  -2.596  22.957  1.00 12.85  ?  186 LEU A CB    1 
ATOM   1428 C  CG    . LEU A 1 186 ? 15.552  -1.843  22.940  1.00 17.10  ?  186 LEU A CG    1 
ATOM   1429 C  CD1   . LEU A 1 186 ? 15.488  -0.579  22.031  1.00 16.03  ?  186 LEU A CD1   1 
ATOM   1430 C  CD2   . LEU A 1 186 ? 16.001  -1.495  24.358  1.00 12.57  ?  186 LEU A CD2   1 
ATOM   1431 N  N     . ALA A 1 187 ? 12.352  -5.133  22.783  1.00 14.56  ?  187 ALA A N     1 
ATOM   1432 C  CA    . ALA A 1 187 ? 10.943  -5.480  22.639  1.00 17.02  ?  187 ALA A CA    1 
ATOM   1433 C  C     . ALA A 1 187 ? 10.539  -6.577  23.626  1.00 19.89  ?  187 ALA A C     1 
ATOM   1434 O  O     . ALA A 1 187 ? 9.513   -6.466  24.309  1.00 20.01  ?  187 ALA A O     1 
ATOM   1435 C  CB    . ALA A 1 187 ? 10.649  -5.885  21.194  1.00 11.76  ?  187 ALA A CB    1 
ATOM   1436 N  N     . HIS A 1 188 ? 11.349  -7.624  23.740  1.00 15.15  ?  188 HIS A N     1 
ATOM   1437 C  CA    . HIS A 1 188 ? 11.048  -8.753  24.605  1.00 17.17  ?  188 HIS A CA    1 
ATOM   1438 C  C     . HIS A 1 188 ? 11.739  -8.664  25.950  1.00 20.64  ?  188 HIS A C     1 
ATOM   1439 O  O     . HIS A 1 188 ? 11.106  -8.909  26.981  1.00 24.48  ?  188 HIS A O     1 
ATOM   1440 C  CB    . HIS A 1 188 ? 11.435  -10.053 23.900  1.00 17.13  ?  188 HIS A CB    1 
ATOM   1441 C  CG    . HIS A 1 188 ? 10.626  -10.298 22.670  1.00 21.50  ?  188 HIS A CG    1 
ATOM   1442 N  ND1   . HIS A 1 188 ? 11.138  -10.893 21.543  1.00 26.12  ?  188 HIS A ND1   1 
ATOM   1443 C  CD2   . HIS A 1 188 ? 9.342   -9.982  22.376  1.00 30.25  ?  188 HIS A CD2   1 
ATOM   1444 C  CE1   . HIS A 1 188 ? 10.206  -10.942 20.607  1.00 29.39  ?  188 HIS A CE1   1 
ATOM   1445 N  NE2   . HIS A 1 188 ? 9.104   -10.397 21.087  1.00 23.95  ?  188 HIS A NE2   1 
ATOM   1446 N  N     . GLY A 1 189 ? 13.015  -8.288  25.974  1.00 17.98  ?  189 GLY A N     1 
ATOM   1447 C  CA    . GLY A 1 189 ? 13.711  -8.184  27.247  1.00 17.55  ?  189 GLY A CA    1 
ATOM   1448 C  C     . GLY A 1 189 ? 13.175  -7.059  28.110  1.00 22.34  ?  189 GLY A C     1 
ATOM   1449 O  O     . GLY A 1 189 ? 13.061  -7.204  29.329  1.00 25.24  ?  189 GLY A O     1 
ATOM   1450 N  N     . HIS A 1 190 ? 12.808  -5.935  27.496  1.00 20.85  ?  190 HIS A N     1 
ATOM   1451 C  CA    . HIS A 1 190 ? 12.411  -4.753  28.256  1.00 23.11  ?  190 HIS A CA    1 
ATOM   1452 C  C     . HIS A 1 190 ? 10.992  -4.298  27.950  1.00 17.72  ?  190 HIS A C     1 
ATOM   1453 O  O     . HIS A 1 190 ? 10.575  -3.241  28.430  1.00 21.63  ?  190 HIS A O     1 
ATOM   1454 C  CB    . HIS A 1 190 ? 13.411  -3.620  28.014  1.00 15.32  ?  190 HIS A CB    1 
ATOM   1455 C  CG    . HIS A 1 190 ? 14.784  -3.947  28.499  1.00 17.75  ?  190 HIS A CG    1 
ATOM   1456 N  ND1   . HIS A 1 190 ? 15.268  -3.518  29.716  1.00 21.03  ?  190 HIS A ND1   1 
ATOM   1457 C  CD2   . HIS A 1 190 ? 15.762  -4.707  27.952  1.00 15.99  ?  190 HIS A CD2   1 
ATOM   1458 C  CE1   . HIS A 1 190 ? 16.490  -3.988  29.893  1.00 24.95  ?  190 HIS A CE1   1 
ATOM   1459 N  NE2   . HIS A 1 190 ? 16.816  -4.710  28.834  1.00 19.64  ?  190 HIS A NE2   1 
ATOM   1460 N  N     . LYS A 1 191 ? 10.241  -5.072  27.173  1.00 15.08  ?  191 LYS A N     1 
ATOM   1461 C  CA    . LYS A 1 191 ? 8.827   -4.825  26.961  1.00 13.71  ?  191 LYS A CA    1 
ATOM   1462 C  C     . LYS A 1 191 ? 8.579   -3.477  26.291  1.00 14.72  ?  191 LYS A C     1 
ATOM   1463 O  O     . LYS A 1 191 ? 7.555   -2.844  26.549  1.00 12.82  ?  191 LYS A O     1 
ATOM   1464 C  CB    . LYS A 1 191 ? 8.042   -4.913  28.288  1.00 19.56  ?  191 LYS A CB    1 
ATOM   1465 C  CG    . LYS A 1 191 ? 7.968   -6.304  28.949  1.00 18.93  ?  191 LYS A CG    1 
ATOM   1466 C  CD    . LYS A 1 191 ? 9.297   -6.755  29.544  1.00 22.46  ?  191 LYS A CD    1 
ATOM   1467 C  CE    . LYS A 1 191 ? 9.796   -5.822  30.674  1.00 30.52  ?  191 LYS A CE    1 
ATOM   1468 N  NZ    . LYS A 1 191 ? 11.057  -6.354  31.328  1.00 27.66  ?  191 LYS A NZ    1 
ATOM   1469 N  N     . TYR A 1 192 ? 9.509   -3.006  25.448  1.00 11.94  ?  192 TYR A N     1 
ATOM   1470 C  CA    . TYR A 1 192 ? 9.269   -1.753  24.743  1.00 10.77  ?  192 TYR A CA    1 
ATOM   1471 C  C     . TYR A 1 192 ? 8.029   -1.901  23.882  1.00 12.64  ?  192 TYR A C     1 
ATOM   1472 O  O     . TYR A 1 192 ? 7.739   -2.987  23.364  1.00 13.09  ?  192 TYR A O     1 
ATOM   1473 C  CB    . TYR A 1 192 ? 10.468  -1.357  23.879  1.00 11.67  ?  192 TYR A CB    1 
ATOM   1474 C  CG    . TYR A 1 192 ? 11.479  -0.547  24.635  1.00 12.35  ?  192 TYR A CG    1 
ATOM   1475 C  CD1   . TYR A 1 192 ? 11.898  -0.937  25.897  1.00 15.15  ?  192 TYR A CD1   1 
ATOM   1476 C  CD2   . TYR A 1 192 ? 11.987  0.633   24.108  1.00 12.77  ?  192 TYR A CD2   1 
ATOM   1477 C  CE1   . TYR A 1 192 ? 12.822  -0.182  26.611  1.00 18.75  ?  192 TYR A CE1   1 
ATOM   1478 C  CE2   . TYR A 1 192 ? 12.901  1.395   24.808  1.00 15.11  ?  192 TYR A CE2   1 
ATOM   1479 C  CZ    . TYR A 1 192 ? 13.315  0.990   26.054  1.00 17.02  ?  192 TYR A CZ    1 
ATOM   1480 O  OH    . TYR A 1 192 ? 14.236  1.753   26.734  1.00 19.74  ?  192 TYR A OH    1 
ATOM   1481 N  N     . ARG A 1 193 ? 7.261   -0.822  23.781  1.00 9.75   ?  193 ARG A N     1 
ATOM   1482 C  CA    . ARG A 1 193 ? 6.047   -0.809  22.977  1.00 9.41   ?  193 ARG A CA    1 
ATOM   1483 C  C     . ARG A 1 193 ? 6.421   -0.254  21.619  1.00 12.57  ?  193 ARG A C     1 
ATOM   1484 O  O     . ARG A 1 193 ? 6.762   0.927   21.497  1.00 11.57  ?  193 ARG A O     1 
ATOM   1485 C  CB    . ARG A 1 193 ? 4.962   0.029   23.639  1.00 11.67  ?  193 ARG A CB    1 
ATOM   1486 C  CG    . ARG A 1 193 ? 4.410   -0.602  24.907  1.00 14.91  ?  193 ARG A CG    1 
ATOM   1487 C  CD    . ARG A 1 193 ? 3.774   0.487   25.758  1.00 20.74  ?  193 ARG A CD    1 
ATOM   1488 N  NE    . ARG A 1 193 ? 2.637   -0.025  26.517  1.00 36.77  ?  193 ARG A NE    1 
ATOM   1489 C  CZ    . ARG A 1 193 ? 1.861   0.725   27.293  1.00 30.44  ?  193 ARG A CZ    1 
ATOM   1490 N  NH1   . ARG A 1 193 ? 2.072   2.031   27.425  1.00 26.58  ?  193 ARG A NH1   1 
ATOM   1491 N  NH2   . ARG A 1 193 ? 0.838   0.156   27.926  1.00 21.48  ?  193 ARG A NH2   1 
ATOM   1492 N  N     . VAL A 1 194 ? 6.372   -1.103  20.615  1.00 12.94  ?  194 VAL A N     1 
ATOM   1493 C  CA    . VAL A 1 194 ? 6.872   -0.788  19.292  1.00 11.47  ?  194 VAL A CA    1 
ATOM   1494 C  C     . VAL A 1 194 ? 5.721   -0.306  18.432  1.00 16.01  ?  194 VAL A C     1 
ATOM   1495 O  O     . VAL A 1 194 ? 4.616   -0.873  18.454  1.00 11.83  ?  194 VAL A O     1 
ATOM   1496 C  CB    . VAL A 1 194 ? 7.563   -2.009  18.662  1.00 15.03  ?  194 VAL A CB    1 
ATOM   1497 C  CG1   . VAL A 1 194 ? 8.154   -1.609  17.326  1.00 13.53  ?  194 VAL A CG1   1 
ATOM   1498 C  CG2   . VAL A 1 194 ? 8.630   -2.534  19.603  1.00 10.22  ?  194 VAL A CG2   1 
ATOM   1499 N  N     . VAL A 1 195 ? 5.994   0.747   17.661  1.00 13.21  ?  195 VAL A N     1 
ATOM   1500 C  CA    . VAL A 1 195 ? 5.011   1.376   16.792  1.00 13.98  ?  195 VAL A CA    1 
ATOM   1501 C  C     . VAL A 1 195 ? 5.686   1.685   15.462  1.00 16.68  ?  195 VAL A C     1 
ATOM   1502 O  O     . VAL A 1 195 ? 6.808   2.202   15.434  1.00 11.46  ?  195 VAL A O     1 
ATOM   1503 C  CB    . VAL A 1 195 ? 4.434   2.648   17.446  1.00 15.00  ?  195 VAL A CB    1 
ATOM   1504 C  CG1   . VAL A 1 195 ? 3.776   3.527   16.425  1.00 20.20  ?  195 VAL A CG1   1 
ATOM   1505 C  CG2   . VAL A 1 195 ? 3.418   2.252   18.545  1.00 14.82  ?  195 VAL A CG2   1 
ATOM   1506 N  N     . HIS A 1 196 ? 5.023   1.338   14.366  1.00 16.54  ?  196 HIS A N     1 
ATOM   1507 C  CA    . HIS A 1 196 ? 5.507   1.661   13.033  1.00 21.22  ?  196 HIS A CA    1 
ATOM   1508 C  C     . HIS A 1 196 ? 4.974   3.027   12.633  1.00 20.00  ?  196 HIS A C     1 
ATOM   1509 O  O     . HIS A 1 196 ? 3.804   3.332   12.874  1.00 17.71  ?  196 HIS A O     1 
ATOM   1510 C  CB    . HIS A 1 196 ? 5.056   0.610   12.016  1.00 14.91  ?  196 HIS A CB    1 
ATOM   1511 C  CG    . HIS A 1 196 ? 5.497   0.899   10.616  1.00 18.75  ?  196 HIS A CG    1 
ATOM   1512 N  ND1   . HIS A 1 196 ? 4.683   0.689   9.524   1.00 21.87  ?  196 HIS A ND1   1 
ATOM   1513 C  CD2   . HIS A 1 196 ? 6.673   1.357   10.123  1.00 20.76  ?  196 HIS A CD2   1 
ATOM   1514 C  CE1   . HIS A 1 196 ? 5.338   1.006   8.418   1.00 21.06  ?  196 HIS A CE1   1 
ATOM   1515 N  NE2   . HIS A 1 196 ? 6.548   1.413   8.753   1.00 18.39  ?  196 HIS A NE2   1 
ATOM   1516 N  N     . GLN A 1 197 ? 5.836   3.847   12.022  1.00 17.40  ?  197 GLN A N     1 
ATOM   1517 C  CA    . GLN A 1 197 ? 5.452   5.177   11.549  1.00 15.83  ?  197 GLN A CA    1 
ATOM   1518 C  C     . GLN A 1 197 ? 5.702   5.253   10.050  1.00 17.04  ?  197 GLN A C     1 
ATOM   1519 O  O     . GLN A 1 197 ? 6.802   5.631   9.611   1.00 18.79  ?  197 GLN A O     1 
ATOM   1520 C  CB    . GLN A 1 197 ? 6.204   6.275   12.307  1.00 17.47  ?  197 GLN A CB    1 
ATOM   1521 C  CG    . GLN A 1 197 ? 6.183   7.684   11.668  1.00 13.88  ?  197 GLN A CG    1 
ATOM   1522 C  CD    . GLN A 1 197 ? 4.783   8.194   11.379  1.00 20.32  ?  197 GLN A CD    1 
ATOM   1523 O  OE1   . GLN A 1 197 ? 4.062   7.649   10.543  1.00 18.20  ?  197 GLN A OE1   1 
ATOM   1524 N  NE2   . GLN A 1 197 ? 4.401   9.276   12.056  1.00 22.39  ?  197 GLN A NE2   1 
ATOM   1525 N  N     . PRO A 1 198 ? 4.703   4.923   9.221   1.00 19.34  ?  198 PRO A N     1 
ATOM   1526 C  CA    . PRO A 1 198 ? 4.914   4.894   7.760   1.00 22.83  ?  198 PRO A CA    1 
ATOM   1527 C  C     . PRO A 1 198 ? 4.952   6.259   7.076   1.00 20.72  ?  198 PRO A C     1 
ATOM   1528 O  O     . PRO A 1 198 ? 5.294   6.316   5.885   1.00 21.92  ?  198 PRO A O     1 
ATOM   1529 C  CB    . PRO A 1 198 ? 3.717   4.079   7.257   1.00 21.28  ?  198 PRO A CB    1 
ATOM   1530 C  CG    . PRO A 1 198 ? 2.651   4.313   8.287   1.00 20.31  ?  198 PRO A CG    1 
ATOM   1531 C  CD    . PRO A 1 198 ? 3.372   4.424   9.603   1.00 20.52  ?  198 PRO A CD    1 
ATOM   1532 N  N     . GLU A 1 199 ? 4.618   7.348   7.770   1.00 23.31  ?  199 GLU A N     1 
ATOM   1533 C  CA    . GLU A 1 199 ? 4.626   8.689   7.179   1.00 25.66  ?  199 GLU A CA    1 
ATOM   1534 C  C     . GLU A 1 199 ? 6.028   9.286   7.054   1.00 21.02  ?  199 GLU A C     1 
ATOM   1535 O  O     . GLU A 1 199 ? 6.183   10.341  6.436   1.00 27.46  ?  199 GLU A O     1 
ATOM   1536 C  CB    . GLU A 1 199 ? 3.761   9.644   8.020   1.00 30.57  ?  199 GLU A CB    1 
ATOM   1537 C  CG    . GLU A 1 199 ? 2.300   9.232   8.364   1.00 34.27  ?  199 GLU A CG    1 
ATOM   1538 C  CD    . GLU A 1 199 ? 1.587   8.377   7.318   1.00 45.18  ?  199 GLU A CD    1 
ATOM   1539 O  OE1   . GLU A 1 199 ? 1.815   8.589   6.100   1.00 55.86  ?  199 GLU A OE1   1 
ATOM   1540 O  OE2   . GLU A 1 199 ? 0.768   7.511   7.712   1.00 49.13  ?  199 GLU A OE2   1 
ATOM   1541 N  N     . VAL A 1 200 ? 7.039   8.654   7.643   1.00 22.22  ?  200 VAL A N     1 
ATOM   1542 C  CA    . VAL A 1 200 ? 8.406   9.156   7.688   1.00 17.79  ?  200 VAL A CA    1 
ATOM   1543 C  C     . VAL A 1 200 ? 9.303   8.089   7.069   1.00 19.66  ?  200 VAL A C     1 
ATOM   1544 O  O     . VAL A 1 200 ? 9.069   6.887   7.252   1.00 17.10  ?  200 VAL A O     1 
ATOM   1545 C  CB    . VAL A 1 200 ? 8.830   9.473   9.145   1.00 15.38  ?  200 VAL A CB    1 
ATOM   1546 C  CG1   . VAL A 1 200 ? 10.298  9.864   9.252   1.00 14.32  ?  200 VAL A CG1   1 
ATOM   1547 C  CG2   . VAL A 1 200 ? 7.933   10.551  9.762   1.00 21.49  ?  200 VAL A CG2   1 
ATOM   1548 N  N     . ALA A 1 201 ? 10.315  8.522   6.330   1.00 16.80  ?  201 ALA A N     1 
ATOM   1549 C  CA    . ALA A 1 201 ? 11.248  7.603   5.708   1.00 19.69  ?  201 ALA A CA    1 
ATOM   1550 C  C     . ALA A 1 201 ? 12.657  8.136   5.879   1.00 16.26  ?  201 ALA A C     1 
ATOM   1551 O  O     . ALA A 1 201 ? 12.869  9.336   6.047   1.00 17.78  ?  201 ALA A O     1 
ATOM   1552 C  CB    . ALA A 1 201 ? 10.953  7.403   4.214   1.00 18.71  ?  201 ALA A CB    1 
ATOM   1553 N  N     . ILE A 1 202 ? 13.615  7.224   5.853   1.00 13.05  ?  202 ILE A N     1 
ATOM   1554 C  CA    . ILE A 1 202 ? 15.021  7.586   5.754   1.00 15.64  ?  202 ILE A CA    1 
ATOM   1555 C  C     . ILE A 1 202 ? 15.557  7.070   4.422   1.00 19.47  ?  202 ILE A C     1 
ATOM   1556 O  O     . ILE A 1 202 ? 14.859  6.389   3.660   1.00 17.81  ?  202 ILE A O     1 
ATOM   1557 C  CB    . ILE A 1 202 ? 15.846  7.008   6.915   1.00 14.41  ?  202 ILE A CB    1 
ATOM   1558 C  CG1   . ILE A 1 202 ? 15.750  5.475   6.888   1.00 14.67  ?  202 ILE A CG1   1 
ATOM   1559 C  CG2   . ILE A 1 202 ? 15.368  7.545   8.233   1.00 15.79  ?  202 ILE A CG2   1 
ATOM   1560 C  CD1   . ILE A 1 202 ? 16.993  4.757   7.408   1.00 12.58  ?  202 ILE A CD1   1 
ATOM   1561 N  N     . ALA A 1 203 ? 16.800  7.399   4.131   1.00 18.00  ?  203 ALA A N     1 
ATOM   1562 C  CA    . ALA A 1 203 ? 17.523  6.808   3.023   1.00 17.11  ?  203 ALA A CA    1 
ATOM   1563 C  C     . ALA A 1 203 ? 18.646  5.986   3.636   1.00 20.24  ?  203 ALA A C     1 
ATOM   1564 O  O     . ALA A 1 203 ? 19.443  6.505   4.431   1.00 16.05  ?  203 ALA A O     1 
ATOM   1565 C  CB    . ALA A 1 203 ? 18.059  7.876   2.067   1.00 16.88  ?  203 ALA A CB    1 
ATOM   1566 N  N     . LEU A 1 204 ? 18.653  4.697   3.326   1.00 18.84  ?  204 LEU A N     1 
ATOM   1567 C  CA    . LEU A 1 204 ? 19.701  3.777   3.731   1.00 18.56  ?  204 LEU A CA    1 
ATOM   1568 C  C     . LEU A 1 204 ? 20.435  3.368   2.459   1.00 23.55  ?  204 LEU A C     1 
ATOM   1569 O  O     . LEU A 1 204 ? 19.845  2.745   1.568   1.00 22.97  ?  204 LEU A O     1 
ATOM   1570 C  CB    . LEU A 1 204 ? 19.104  2.568   4.461   1.00 19.09  ?  204 LEU A CB    1 
ATOM   1571 C  CG    . LEU A 1 204 ? 20.086  1.567   5.070   1.00 21.68  ?  204 LEU A CG    1 
ATOM   1572 C  CD1   . LEU A 1 204 ? 19.774  1.250   6.520   1.00 25.98  ?  204 LEU A CD1   1 
ATOM   1573 C  CD2   . LEU A 1 204 ? 20.101  0.312   4.240   1.00 30.08  ?  204 LEU A CD2   1 
ATOM   1574 N  N     . HIS A 1 205 ? 21.703  3.743   2.357   1.00 24.87  ?  205 HIS A N     1 
ATOM   1575 C  CA    . HIS A 1 205 ? 22.443  3.580   1.113   1.00 26.30  ?  205 HIS A CA    1 
ATOM   1576 C  C     . HIS A 1 205 ? 23.012  2.174   1.035   1.00 24.92  ?  205 HIS A C     1 
ATOM   1577 O  O     . HIS A 1 205 ? 23.793  1.764   1.903   1.00 25.14  ?  205 HIS A O     1 
ATOM   1578 C  CB    . HIS A 1 205 ? 23.553  4.623   1.008   1.00 27.54  ?  205 HIS A CB    1 
ATOM   1579 C  CG    . HIS A 1 205 ? 23.043  6.027   0.930   1.00 25.37  ?  205 HIS A CG    1 
ATOM   1580 N  ND1   . HIS A 1 205 ? 23.124  6.905   1.989   1.00 24.86  ?  205 HIS A ND1   1 
ATOM   1581 C  CD2   . HIS A 1 205 ? 22.435  6.701   -0.074  1.00 23.00  ?  205 HIS A CD2   1 
ATOM   1582 C  CE1   . HIS A 1 205 ? 22.598  8.065   1.636   1.00 27.44  ?  205 HIS A CE1   1 
ATOM   1583 N  NE2   . HIS A 1 205 ? 22.173  7.966   0.389   1.00 25.11  ?  205 HIS A NE2   1 
ATOM   1584 N  N     . ARG A 1 206 ? 22.594  1.440   0.005   1.00 25.55  ?  206 ARG A N     1 
ATOM   1585 C  CA    . ARG A 1 206 ? 23.138  0.135   -0.377  1.00 29.66  ?  206 ARG A CA    1 
ATOM   1586 C  C     . ARG A 1 206 ? 23.589  0.275   -1.831  1.00 30.84  ?  206 ARG A C     1 
ATOM   1587 O  O     . ARG A 1 206 ? 22.876  -0.110  -2.762  1.00 33.13  ?  206 ARG A O     1 
ATOM   1588 C  CB    . ARG A 1 206 ? 22.085  -0.972  -0.209  1.00 31.67  ?  206 ARG A CB    1 
ATOM   1589 C  CG    . ARG A 1 206 ? 21.807  -1.350  1.235   1.00 33.50  ?  206 ARG A CG    1 
ATOM   1590 C  CD    . ARG A 1 206 ? 23.041  -1.981  1.882   1.00 42.01  ?  206 ARG A CD    1 
ATOM   1591 N  NE    . ARG A 1 206 ? 23.057  -2.024  3.348   1.00 49.82  ?  206 ARG A NE    1 
ATOM   1592 C  CZ    . ARG A 1 206 ? 22.065  -2.414  4.147   1.00 45.43  ?  206 ARG A CZ    1 
ATOM   1593 N  NH1   . ARG A 1 206 ? 20.919  -2.875  3.670   1.00 42.70  ?  206 ARG A NH1   1 
ATOM   1594 N  NH2   . ARG A 1 206 ? 22.240  -2.362  5.464   1.00 37.15  ?  206 ARG A NH2   1 
ATOM   1595 N  N     . ILE A 1 207 ? 24.758  0.872   -2.027  1.00 30.00  ?  207 ILE A N     1 
ATOM   1596 C  CA    . ILE A 1 207 ? 25.266  1.139   -3.372  1.00 39.31  ?  207 ILE A CA    1 
ATOM   1597 C  C     . ILE A 1 207 ? 25.885  -0.134  -3.948  1.00 37.37  ?  207 ILE A C     1 
ATOM   1598 O  O     . ILE A 1 207 ? 26.863  -0.653  -3.388  1.00 35.56  ?  207 ILE A O     1 
ATOM   1599 C  CB    . ILE A 1 207 ? 26.280  2.298   -3.361  1.00 38.09  ?  207 ILE A CB    1 
ATOM   1600 C  CG1   . ILE A 1 207 ? 25.780  3.467   -2.496  1.00 32.09  ?  207 ILE A CG1   1 
ATOM   1601 C  CG2   . ILE A 1 207 ? 26.570  2.773   -4.787  1.00 41.13  ?  207 ILE A CG2   1 
ATOM   1602 C  CD1   . ILE A 1 207 ? 24.741  4.360   -3.164  1.00 25.59  ?  207 ILE A CD1   1 
ATOM   1603 N  N     . PRO A 1 208 ? 25.349  -0.681  -5.045  1.00 37.46  ?  208 PRO A N     1 
ATOM   1604 C  CA    . PRO A 1 208 ? 25.993  -1.841  -5.678  1.00 45.00  ?  208 PRO A CA    1 
ATOM   1605 C  C     . PRO A 1 208 ? 27.363  -1.480  -6.237  1.00 51.29  ?  208 PRO A C     1 
ATOM   1606 O  O     . PRO A 1 208 ? 27.639  -0.327  -6.584  1.00 51.40  ?  208 PRO A O     1 
ATOM   1607 C  CB    . PRO A 1 208 ? 25.022  -2.233  -6.803  1.00 43.75  ?  208 PRO A CB    1 
ATOM   1608 C  CG    . PRO A 1 208 ? 23.745  -1.487  -6.516  1.00 43.34  ?  208 PRO A CG    1 
ATOM   1609 C  CD    . PRO A 1 208 ? 24.151  -0.246  -5.780  1.00 38.21  ?  208 PRO A CD    1 
ATOM   1610 N  N     . GLY A 1 209 ? 28.226  -2.489  -6.328  1.00 58.30  ?  209 GLY A N     1 
ATOM   1611 C  CA    . GLY A 1 209 ? 29.580  -2.271  -6.796  1.00 57.23  ?  209 GLY A CA    1 
ATOM   1612 C  C     . GLY A 1 209 ? 30.090  -3.352  -7.719  1.00 68.20  ?  209 GLY A C     1 
ATOM   1613 O  O     . GLY A 1 209 ? 29.624  -3.471  -8.856  1.00 72.04  ?  209 GLY A O     1 
ATOM   1614 N  N     . VAL A 1 210 ? 31.028  -4.161  -7.225  1.00 81.40  ?  210 VAL A N     1 
ATOM   1615 C  CA    . VAL A 1 210 ? 31.792  -5.076  -8.073  1.00 88.51  ?  210 VAL A CA    1 
ATOM   1616 C  C     . VAL A 1 210 ? 31.228  -6.497  -8.055  1.00 88.96  ?  210 VAL A C     1 
ATOM   1617 O  O     . VAL A 1 210 ? 31.325  -7.206  -9.058  1.00 89.40  ?  210 VAL A O     1 
ATOM   1618 C  CB    . VAL A 1 210 ? 33.279  -5.062  -7.655  1.00 83.75  ?  210 VAL A CB    1 
ATOM   1619 C  CG1   . VAL A 1 210 ? 34.099  -5.945  -8.588  1.00 80.31  ?  210 VAL A CG1   1 
ATOM   1620 C  CG2   . VAL A 1 210 ? 33.827  -3.640  -7.635  1.00 74.28  ?  210 VAL A CG2   1 
ATOM   1621 N  N     . GLU A 1 211 ? 30.644  -6.941  -6.933  1.00 87.59  ?  211 GLU A N     1 
ATOM   1622 C  CA    . GLU A 1 211 ? 30.238  -8.344  -6.788  1.00 91.85  ?  211 GLU A CA    1 
ATOM   1623 C  C     . GLU A 1 211 ? 29.386  -8.836  -7.959  1.00 97.39  ?  211 GLU A C     1 
ATOM   1624 O  O     . GLU A 1 211 ? 29.609  -9.940  -8.477  1.00 90.72  ?  211 GLU A O     1 
ATOM   1625 C  CB    . GLU A 1 211 ? 29.494  -8.542  -5.461  1.00 92.02  ?  211 GLU A CB    1 
ATOM   1626 C  CG    . GLU A 1 211 ? 28.723  -9.875  -5.317  1.00 86.88  ?  211 GLU A CG    1 
ATOM   1627 C  CD    . GLU A 1 211 ? 29.570  -11.130 -5.552  1.00 84.33  ?  211 GLU A CD    1 
ATOM   1628 O  OE1   . GLU A 1 211 ? 30.805  -11.101 -5.336  1.00 82.91  ?  211 GLU A OE1   1 
ATOM   1629 O  OE2   . GLU A 1 211 ? 28.990  -12.152 -5.979  1.00 75.10  ?  211 GLU A OE2   1 
ATOM   1630 N  N     . SER A 1 212 ? 28.416  -8.032  -8.400  1.00 98.18  ?  212 SER A N     1 
ATOM   1631 C  CA    . SER A 1 212 ? 27.562  -8.408  -9.523  1.00 98.32  ?  212 SER A CA    1 
ATOM   1632 C  C     . SER A 1 212 ? 28.257  -8.268  -10.874 1.00 98.69  ?  212 SER A C     1 
ATOM   1633 O  O     . SER A 1 212 ? 27.652  -8.601  -11.900 1.00 100.29 ?  212 SER A O     1 
ATOM   1634 C  CB    . SER A 1 212 ? 26.272  -7.580  -9.507  1.00 104.28 ?  212 SER A CB    1 
ATOM   1635 O  OG    . SER A 1 212 ? 25.338  -8.114  -8.576  1.00 105.29 ?  212 SER A OG    1 
ATOM   1636 N  N     . LEU A 1 213 ? 29.495  -7.770  -10.897 1.00 97.91  ?  213 LEU A N     1 
ATOM   1637 C  CA    . LEU A 1 213 ? 30.357  -7.827  -12.073 1.00 94.32  ?  213 LEU A CA    1 
ATOM   1638 C  C     . LEU A 1 213 ? 31.227  -9.081  -12.067 1.00 92.21  ?  213 LEU A C     1 
ATOM   1639 O  O     . LEU A 1 213 ? 31.638  -9.558  -13.133 1.00 87.14  ?  213 LEU A O     1 
ATOM   1640 C  CB    . LEU A 1 213 ? 31.243  -6.573  -12.146 1.00 92.85  ?  213 LEU A CB    1 
ATOM   1641 C  CG    . LEU A 1 213 ? 30.743  -5.123  -12.320 1.00 84.55  ?  213 LEU A CG    1 
ATOM   1642 C  CD1   . LEU A 1 213 ? 29.378  -4.813  -11.699 1.00 82.87  ?  213 LEU A CD1   1 
ATOM   1643 C  CD2   . LEU A 1 213 ? 31.792  -4.165  -11.756 1.00 66.84  ?  213 LEU A CD2   1 
ATOM   1644 N  N     . THR A 1 214 ? 31.508  -9.619  -10.879 1.00 91.89  ?  214 THR A N     1 
ATOM   1645 C  CA    . THR A 1 214 ? 32.161  -10.912 -10.716 1.00 90.04  ?  214 THR A CA    1 
ATOM   1646 C  C     . THR A 1 214 ? 31.115  -11.999 -10.473 1.00 92.15  ?  214 THR A C     1 
ATOM   1647 O  O     . THR A 1 214 ? 30.076  -12.033 -11.145 1.00 89.05  ?  214 THR A O     1 
ATOM   1648 C  CB    . THR A 1 214 ? 33.164  -10.872 -9.555  1.00 90.45  ?  214 THR A CB    1 
ATOM   1649 O  OG1   . THR A 1 214 ? 32.610  -10.127 -8.461  1.00 86.67  ?  214 THR A OG1   1 
ATOM   1650 C  CG2   . THR A 1 214 ? 34.469  -10.225 -9.993  1.00 83.15  ?  214 THR A CG2   1 
ATOM   1651 N  N     . THR A 1 215 ? 31.376  -12.874 -9.507  1.00 87.23  ?  215 THR A N     1 
ATOM   1652 C  CA    . THR A 1 215 ? 30.517  -14.017 -9.211  1.00 74.29  ?  215 THR A CA    1 
ATOM   1653 C  C     . THR A 1 215 ? 30.607  -14.294 -7.725  1.00 71.19  ?  215 THR A C     1 
ATOM   1654 O  O     . THR A 1 215 ? 31.450  -13.716 -7.022  1.00 69.56  ?  215 THR A O     1 
ATOM   1655 C  CB    . THR A 1 215 ? 30.937  -15.248 -10.028 1.00 65.73  ?  215 THR A CB    1 
ATOM   1656 O  OG1   . THR A 1 215 ? 32.369  -15.337 -10.066 1.00 67.55  ?  215 THR A OG1   1 
ATOM   1657 C  CG2   . THR A 1 215 ? 30.376  -15.179 -11.449 1.00 68.08  ?  215 THR A CG2   1 
ATOM   1658 N  N     . PRO A 1 216 ? 29.736  -15.164 -7.190  1.00 60.60  ?  216 PRO A N     1 
ATOM   1659 C  CA    . PRO A 1 216 ? 29.849  -15.548 -5.771  1.00 56.11  ?  216 PRO A CA    1 
ATOM   1660 C  C     . PRO A 1 216 ? 31.212  -16.137 -5.443  1.00 57.60  ?  216 PRO A C     1 
ATOM   1661 O  O     . PRO A 1 216 ? 31.574  -17.214 -5.919  1.00 65.15  ?  216 PRO A O     1 
ATOM   1662 C  CB    . PRO A 1 216 ? 28.738  -16.588 -5.595  1.00 45.21  ?  216 PRO A CB    1 
ATOM   1663 C  CG    . PRO A 1 216 ? 27.727  -16.226 -6.611  1.00 47.59  ?  216 PRO A CG    1 
ATOM   1664 C  CD    . PRO A 1 216 ? 28.475  -15.652 -7.788  1.00 48.81  ?  216 PRO A CD    1 
ATOM   1665 N  N     . THR A 1 217 ? 31.968  -15.419 -4.621  1.00 57.09  ?  217 THR A N     1 
ATOM   1666 C  CA    . THR A 1 217 ? 33.216  -15.931 -4.084  1.00 56.41  ?  217 THR A CA    1 
ATOM   1667 C  C     . THR A 1 217 ? 32.953  -16.805 -2.864  1.00 54.48  ?  217 THR A C     1 
ATOM   1668 O  O     . THR A 1 217 ? 31.831  -16.909 -2.367  1.00 53.13  ?  217 THR A O     1 
ATOM   1669 C  CB    . THR A 1 217 ? 34.163  -14.792 -3.707  1.00 56.07  ?  217 THR A CB    1 
ATOM   1670 O  OG1   . THR A 1 217 ? 35.311  -15.338 -3.045  1.00 61.21  ?  217 THR A OG1   1 
ATOM   1671 C  CG2   . THR A 1 217 ? 33.487  -13.809 -2.779  1.00 51.79  ?  217 THR A CG2   1 
ATOM   1672 N  N     . SER A 1 218 ? 34.019  -17.436 -2.374  1.00 58.31  ?  218 SER A N     1 
ATOM   1673 C  CA    . SER A 1 218 ? 33.910  -18.168 -1.122  1.00 56.78  ?  218 SER A CA    1 
ATOM   1674 C  C     . SER A 1 218 ? 33.833  -17.238 0.081   1.00 52.60  ?  218 SER A C     1 
ATOM   1675 O  O     . SER A 1 218 ? 33.792  -17.725 1.218   1.00 49.41  ?  218 SER A O     1 
ATOM   1676 C  CB    . SER A 1 218 ? 35.083  -19.143 -0.980  1.00 60.17  ?  218 SER A CB    1 
ATOM   1677 O  OG    . SER A 1 218 ? 34.738  -20.421 -1.496  1.00 56.79  ?  218 SER A OG    1 
ATOM   1678 N  N     . ASP A 1 219 ? 33.808  -15.922 -0.148  1.00 53.19  ?  219 ASP A N     1 
ATOM   1679 C  CA    . ASP A 1 219 ? 33.618  -14.938 0.912   1.00 48.41  ?  219 ASP A CA    1 
ATOM   1680 C  C     . ASP A 1 219 ? 32.161  -14.541 1.081   1.00 39.43  ?  219 ASP A C     1 
ATOM   1681 O  O     . ASP A 1 219 ? 31.750  -14.197 2.194   1.00 42.75  ?  219 ASP A O     1 
ATOM   1682 C  CB    . ASP A 1 219 ? 34.458  -13.687 0.634   1.00 52.57  ?  219 ASP A CB    1 
ATOM   1683 C  CG    . ASP A 1 219 ? 35.887  -13.834 1.106   1.00 59.89  ?  219 ASP A CG    1 
ATOM   1684 O  OD1   . ASP A 1 219 ? 36.438  -14.953 0.988   1.00 69.33  ?  219 ASP A OD1   1 
ATOM   1685 O  OD2   . ASP A 1 219 ? 36.458  -12.837 1.598   1.00 62.86  ?  219 ASP A OD2   1 
ATOM   1686 N  N     . ASP A 1 220 ? 31.371  -14.569 0.003   1.00 43.34  ?  220 ASP A N     1 
ATOM   1687 C  CA    . ASP A 1 220 ? 29.922  -14.478 0.157   1.00 38.47  ?  220 ASP A CA    1 
ATOM   1688 C  C     . ASP A 1 220 ? 29.392  -15.632 0.994   1.00 37.48  ?  220 ASP A C     1 
ATOM   1689 O  O     . ASP A 1 220 ? 28.400  -15.470 1.711   1.00 34.66  ?  220 ASP A O     1 
ATOM   1690 C  CB    . ASP A 1 220 ? 29.225  -14.469 -1.208  1.00 38.67  ?  220 ASP A CB    1 
ATOM   1691 C  CG    . ASP A 1 220 ? 29.749  -13.384 -2.129  1.00 56.80  ?  220 ASP A CG    1 
ATOM   1692 O  OD1   . ASP A 1 220 ? 29.467  -12.195 -1.865  1.00 62.62  ?  220 ASP A OD1   1 
ATOM   1693 O  OD2   . ASP A 1 220 ? 30.411  -13.717 -3.136  1.00 59.90  ?  220 ASP A OD2   1 
ATOM   1694 N  N     . ILE A 1 221 ? 30.039  -16.802 0.900   1.00 32.80  ?  221 ILE A N     1 
ATOM   1695 C  CA    . ILE A 1 221 ? 29.669  -17.962 1.705   1.00 34.00  ?  221 ILE A CA    1 
ATOM   1696 C  C     . ILE A 1 221 ? 30.138  -17.789 3.143   1.00 33.90  ?  221 ILE A C     1 
ATOM   1697 O  O     . ILE A 1 221 ? 29.428  -18.152 4.091   1.00 37.38  ?  221 ILE A O     1 
ATOM   1698 C  CB    . ILE A 1 221 ? 30.246  -19.247 1.081   1.00 35.09  ?  221 ILE A CB    1 
ATOM   1699 C  CG1   . ILE A 1 221 ? 29.831  -19.354 -0.388  1.00 39.22  ?  221 ILE A CG1   1 
ATOM   1700 C  CG2   . ILE A 1 221 ? 29.827  -20.465 1.883   1.00 28.67  ?  221 ILE A CG2   1 
ATOM   1701 C  CD1   . ILE A 1 221 ? 29.770  -20.773 -0.918  1.00 37.95  ?  221 ILE A CD1   1 
ATOM   1702 N  N     . ALA A 1 222 ? 31.344  -17.251 3.331   1.00 31.25  ?  222 ALA A N     1 
ATOM   1703 C  CA    . ALA A 1 222 ? 31.833  -17.009 4.683   1.00 34.70  ?  222 ALA A CA    1 
ATOM   1704 C  C     . ALA A 1 222 ? 30.934  -16.019 5.410   1.00 33.31  ?  222 ALA A C     1 
ATOM   1705 O  O     . ALA A 1 222 ? 30.541  -16.248 6.559   1.00 32.87  ?  222 ALA A O     1 
ATOM   1706 C  CB    . ALA A 1 222 ? 33.272  -16.498 4.648   1.00 27.78  ?  222 ALA A CB    1 
ATOM   1707 N  N     . ALA A 1 223 ? 30.581  -14.920 4.739   1.00 27.85  ?  223 ALA A N     1 
ATOM   1708 C  CA    . ALA A 1 223 ? 29.791  -13.880 5.385   1.00 30.54  ?  223 ALA A CA    1 
ATOM   1709 C  C     . ALA A 1 223 ? 28.389  -14.374 5.697   1.00 29.25  ?  223 ALA A C     1 
ATOM   1710 O  O     . ALA A 1 223 ? 27.863  -14.109 6.780   1.00 27.41  ?  223 ALA A O     1 
ATOM   1711 C  CB    . ALA A 1 223 ? 29.737  -12.634 4.504   1.00 29.41  ?  223 ALA A CB    1 
ATOM   1712 N  N     . LEU A 1 224 ? 27.776  -15.111 4.767   1.00 27.00  ?  224 LEU A N     1 
ATOM   1713 C  CA    . LEU A 1 224 ? 26.453  -15.653 5.027   1.00 26.46  ?  224 LEU A CA    1 
ATOM   1714 C  C     . LEU A 1 224 ? 26.498  -16.647 6.173   1.00 30.44  ?  224 LEU A C     1 
ATOM   1715 O  O     . LEU A 1 224 ? 25.602  -16.656 7.028   1.00 30.69  ?  224 LEU A O     1 
ATOM   1716 C  CB    . LEU A 1 224 ? 25.887  -16.308 3.771   1.00 31.15  ?  224 LEU A CB    1 
ATOM   1717 C  CG    . LEU A 1 224 ? 24.361  -16.459 3.661   1.00 40.05  ?  224 LEU A CG    1 
ATOM   1718 C  CD1   . LEU A 1 224 ? 23.986  -16.887 2.266   1.00 37.71  ?  224 LEU A CD1   1 
ATOM   1719 C  CD2   . LEU A 1 224 ? 23.756  -17.440 4.668   1.00 44.11  ?  224 LEU A CD2   1 
ATOM   1720 N  N     . LYS A 1 225 ? 27.531  -17.490 6.214   1.00 29.04  ?  225 LYS A N     1 
ATOM   1721 C  CA    . LYS A 1 225 ? 27.700  -18.396 7.348   1.00 32.15  ?  225 LYS A CA    1 
ATOM   1722 C  C     . LYS A 1 225 ? 27.641  -17.650 8.681   1.00 28.91  ?  225 LYS A C     1 
ATOM   1723 O  O     . LYS A 1 225 ? 26.973  -18.092 9.620   1.00 24.24  ?  225 LYS A O     1 
ATOM   1724 C  CB    . LYS A 1 225 ? 29.013  -19.157 7.223   1.00 31.99  ?  225 LYS A CB    1 
ATOM   1725 C  CG    . LYS A 1 225 ? 28.940  -20.529 7.824   1.00 37.35  ?  225 LYS A CG    1 
ATOM   1726 C  CD    . LYS A 1 225 ? 28.587  -21.565 6.764   1.00 39.39  ?  225 LYS A CD    1 
ATOM   1727 C  CE    . LYS A 1 225 ? 29.410  -21.380 5.503   1.00 39.84  ?  225 LYS A CE    1 
ATOM   1728 N  NZ    . LYS A 1 225 ? 29.007  -22.389 4.474   1.00 46.32  ?  225 LYS A NZ    1 
ATOM   1729 N  N     . VAL A 1 226 ? 28.331  -16.508 8.781   1.00 29.80  ?  226 VAL A N     1 
ATOM   1730 C  CA    . VAL A 1 226 ? 28.297  -15.761 10.036  1.00 27.76  ?  226 VAL A CA    1 
ATOM   1731 C  C     . VAL A 1 226 ? 26.909  -15.168 10.267  1.00 25.68  ?  226 VAL A C     1 
ATOM   1732 O  O     . VAL A 1 226 ? 26.395  -15.196 11.388  1.00 21.24  ?  226 VAL A O     1 
ATOM   1733 C  CB    . VAL A 1 226 ? 29.389  -14.681 10.061  1.00 34.57  ?  226 VAL A CB    1 
ATOM   1734 C  CG1   . VAL A 1 226 ? 29.083  -13.641 11.147  1.00 27.73  ?  226 VAL A CG1   1 
ATOM   1735 C  CG2   . VAL A 1 226 ? 30.753  -15.324 10.273  1.00 36.22  ?  226 VAL A CG2   1 
ATOM   1736 N  N     . TYR A 1 227 ? 26.276  -14.642 9.211   1.00 25.78  ?  227 TYR A N     1 
ATOM   1737 C  CA    . TYR A 1 227 ? 24.886  -14.202 9.316   1.00 25.80  ?  227 TYR A CA    1 
ATOM   1738 C  C     . TYR A 1 227 ? 23.983  -15.335 9.802   1.00 23.99  ?  227 TYR A C     1 
ATOM   1739 O  O     . TYR A 1 227 ? 23.187  -15.157 10.734  1.00 21.92  ?  227 TYR A O     1 
ATOM   1740 C  CB    . TYR A 1 227 ? 24.392  -13.653 7.969   1.00 27.18  ?  227 TYR A CB    1 
ATOM   1741 C  CG    . TYR A 1 227 ? 23.173  -12.763 8.122   1.00 29.75  ?  227 TYR A CG    1 
ATOM   1742 C  CD1   . TYR A 1 227 ? 21.912  -13.319 8.289   1.00 32.19  ?  227 TYR A CD1   1 
ATOM   1743 C  CD2   . TYR A 1 227 ? 23.280  -11.371 8.137   1.00 31.67  ?  227 TYR A CD2   1 
ATOM   1744 C  CE1   . TYR A 1 227 ? 20.784  -12.530 8.463   1.00 28.48  ?  227 TYR A CE1   1 
ATOM   1745 C  CE2   . TYR A 1 227 ? 22.144  -10.564 8.304   1.00 29.62  ?  227 TYR A CE2   1 
ATOM   1746 C  CZ    . TYR A 1 227 ? 20.898  -11.164 8.467   1.00 29.32  ?  227 TYR A CZ    1 
ATOM   1747 O  OH    . TYR A 1 227 ? 19.748  -10.427 8.647   1.00 26.22  ?  227 TYR A OH    1 
ATOM   1748 N  N     . GLU A 1 228 ? 24.085  -16.511 9.176   1.00 24.51  ?  228 GLU A N     1 
ATOM   1749 C  CA    . GLU A 1 228 ? 23.283  -17.653 9.612   1.00 21.05  ?  228 GLU A CA    1 
ATOM   1750 C  C     . GLU A 1 228 ? 23.553  -17.983 11.073  1.00 19.77  ?  228 GLU A C     1 
ATOM   1751 O  O     . GLU A 1 228 ? 22.623  -18.199 11.861  1.00 21.08  ?  228 GLU A O     1 
ATOM   1752 C  CB    . GLU A 1 228 ? 23.562  -18.877 8.732   1.00 25.94  ?  228 GLU A CB    1 
ATOM   1753 C  CG    . GLU A 1 228 ? 22.988  -20.157 9.346   1.00 35.05  ?  228 GLU A CG    1 
ATOM   1754 C  CD    . GLU A 1 228 ? 22.870  -21.326 8.375   1.00 33.80  ?  228 GLU A CD    1 
ATOM   1755 O  OE1   . GLU A 1 228 ? 23.829  -21.586 7.625   1.00 34.60  ?  228 GLU A OE1   1 
ATOM   1756 O  OE2   . GLU A 1 228 ? 21.802  -21.986 8.379   1.00 36.20  ?  228 GLU A OE2   1 
ATOM   1757 N  N     . ASP A 1 229 ? 24.827  -18.015 11.452  1.00 23.88  ?  229 ASP A N     1 
ATOM   1758 C  CA    . ASP A 1 229 ? 25.197  -18.399 12.809  1.00 24.79  ?  229 ASP A CA    1 
ATOM   1759 C  C     . ASP A 1 229 ? 24.598  -17.441 13.830  1.00 23.29  ?  229 ASP A C     1 
ATOM   1760 O  O     . ASP A 1 229 ? 23.965  -17.865 14.808  1.00 22.44  ?  229 ASP A O     1 
ATOM   1761 C  CB    . ASP A 1 229 ? 26.723  -18.432 12.928  1.00 25.62  ?  229 ASP A CB    1 
ATOM   1762 C  CG    . ASP A 1 229 ? 27.329  -19.713 12.361  1.00 36.54  ?  229 ASP A CG    1 
ATOM   1763 O  OD1   . ASP A 1 229 ? 26.681  -20.370 11.508  1.00 38.97  ?  229 ASP A OD1   1 
ATOM   1764 O  OD2   . ASP A 1 229 ? 28.458  -20.064 12.763  1.00 49.40  ?  229 ASP A OD2   1 
ATOM   1765 N  N     . ASN A 1 230 ? 24.796  -16.136 13.621  1.00 20.48  ?  230 ASN A N     1 
ATOM   1766 C  CA    . ASN A 1 230 ? 24.251  -15.145 14.539  1.00 18.59  ?  230 ASN A CA    1 
ATOM   1767 C  C     . ASN A 1 230 ? 22.732  -15.191 14.555  1.00 18.72  ?  230 ASN A C     1 
ATOM   1768 O  O     . ASN A 1 230 ? 22.120  -14.990 15.603  1.00 17.90  ?  230 ASN A O     1 
ATOM   1769 C  CB    . ASN A 1 230 ? 24.736  -13.755 14.144  1.00 20.00  ?  230 ASN A CB    1 
ATOM   1770 C  CG    . ASN A 1 230 ? 26.180  -13.530 14.503  1.00 20.69  ?  230 ASN A CG    1 
ATOM   1771 O  OD1   . ASN A 1 230 ? 26.763  -12.494 14.184  1.00 19.69  ?  230 ASN A OD1   1 
ATOM   1772 N  ND2   . ASN A 1 230 ? 26.769  -14.500 15.175  1.00 14.72  ?  230 ASN A ND2   1 
ATOM   1773 N  N     . TRP A 1 231 ? 22.111  -15.460 13.404  1.00 20.18  ?  231 TRP A N     1 
ATOM   1774 C  CA    . TRP A 1 231 ? 20.662  -15.602 13.360  1.00 17.09  ?  231 TRP A CA    1 
ATOM   1775 C  C     . TRP A 1 231 ? 20.195  -16.722 14.294  1.00 20.49  ?  231 TRP A C     1 
ATOM   1776 O  O     . TRP A 1 231 ? 19.266  -16.532 15.091  1.00 15.46  ?  231 TRP A O     1 
ATOM   1777 C  CB    . TRP A 1 231 ? 20.207  -15.841 11.912  1.00 19.22  ?  231 TRP A CB    1 
ATOM   1778 C  CG    . TRP A 1 231 ? 18.719  -15.908 11.776  1.00 23.01  ?  231 TRP A CG    1 
ATOM   1779 C  CD1   . TRP A 1 231 ? 17.854  -14.852 11.634  1.00 20.01  ?  231 TRP A CD1   1 
ATOM   1780 C  CD2   . TRP A 1 231 ? 17.904  -17.095 11.814  1.00 23.95  ?  231 TRP A CD2   1 
ATOM   1781 N  NE1   . TRP A 1 231 ? 16.553  -15.308 11.577  1.00 21.15  ?  231 TRP A NE1   1 
ATOM   1782 C  CE2   . TRP A 1 231 ? 16.552  -16.679 11.693  1.00 21.39  ?  231 TRP A CE2   1 
ATOM   1783 C  CE3   . TRP A 1 231 ? 18.184  -18.465 11.944  1.00 17.88  ?  231 TRP A CE3   1 
ATOM   1784 C  CZ2   . TRP A 1 231 ? 15.484  -17.585 11.686  1.00 17.02  ?  231 TRP A CZ2   1 
ATOM   1785 C  CZ3   . TRP A 1 231 ? 17.116  -19.371 11.953  1.00 18.95  ?  231 TRP A CZ3   1 
ATOM   1786 C  CH2   . TRP A 1 231 ? 15.782  -18.924 11.819  1.00 17.00  ?  231 TRP A CH2   1 
ATOM   1787 N  N     . HIS A 1 232 ? 20.842  -17.896 14.220  1.00 21.12  ?  232 HIS A N     1 
ATOM   1788 C  CA    . HIS A 1 232 ? 20.517  -18.989 15.142  1.00 22.10  ?  232 HIS A CA    1 
ATOM   1789 C  C     . HIS A 1 232 ? 20.812  -18.603 16.577  1.00 22.13  ?  232 HIS A C     1 
ATOM   1790 O  O     . HIS A 1 232 ? 20.051  -18.948 17.491  1.00 19.82  ?  232 HIS A O     1 
ATOM   1791 C  CB    . HIS A 1 232 ? 21.307  -20.250 14.800  1.00 19.87  ?  232 HIS A CB    1 
ATOM   1792 C  CG    . HIS A 1 232 ? 20.705  -21.054 13.695  1.00 24.57  ?  232 HIS A CG    1 
ATOM   1793 N  ND1   . HIS A 1 232 ? 21.265  -21.122 12.435  1.00 24.35  ?  232 HIS A ND1   1 
ATOM   1794 C  CD2   . HIS A 1 232 ? 19.587  -21.814 13.654  1.00 21.96  ?  232 HIS A CD2   1 
ATOM   1795 C  CE1   . HIS A 1 232 ? 20.510  -21.882 11.662  1.00 19.01  ?  232 HIS A CE1   1 
ATOM   1796 N  NE2   . HIS A 1 232 ? 19.489  -22.318 12.379  1.00 31.45  ?  232 HIS A NE2   1 
ATOM   1797 N  N     . LEU A 1 233 ? 21.941  -17.925 16.796  1.00 21.57  ?  233 LEU A N     1 
ATOM   1798 C  CA    . LEU A 1 233 ? 22.276  -17.425 18.121  1.00 23.32  ?  233 LEU A CA    1 
ATOM   1799 C  C     . LEU A 1 233 ? 21.113  -16.634 18.706  1.00 23.89  ?  233 LEU A C     1 
ATOM   1800 O  O     . LEU A 1 233 ? 20.566  -16.988 19.755  1.00 20.45  ?  233 LEU A O     1 
ATOM   1801 C  CB    . LEU A 1 233 ? 23.531  -16.550 18.043  1.00 21.02  ?  233 LEU A CB    1 
ATOM   1802 C  CG    . LEU A 1 233 ? 24.142  -16.169 19.395  1.00 24.59  ?  233 LEU A CG    1 
ATOM   1803 C  CD1   . LEU A 1 233 ? 25.640  -15.949 19.265  1.00 21.58  ?  233 LEU A CD1   1 
ATOM   1804 C  CD2   . LEU A 1 233 ? 23.462  -14.928 19.986  1.00 26.06  ?  233 LEU A CD2   1 
ATOM   1805 N  N     . ILE A 1 234 ? 20.719  -15.562 18.014  1.00 18.88  ?  234 ILE A N     1 
ATOM   1806 C  CA    . ILE A 1 234 ? 19.735  -14.629 18.545  1.00 16.72  ?  234 ILE A CA    1 
ATOM   1807 C  C     . ILE A 1 234 ? 18.375  -15.294 18.665  1.00 19.55  ?  234 ILE A C     1 
ATOM   1808 O  O     . ILE A 1 234 ? 17.595  -14.979 19.576  1.00 18.48  ?  234 ILE A O     1 
ATOM   1809 C  CB    . ILE A 1 234 ? 19.682  -13.375 17.659  1.00 14.14  ?  234 ILE A CB    1 
ATOM   1810 C  CG1   . ILE A 1 234 ? 21.070  -12.735 17.573  1.00 16.06  ?  234 ILE A CG1   1 
ATOM   1811 C  CG2   . ILE A 1 234 ? 18.660  -12.392 18.188  1.00 15.50  ?  234 ILE A CG2   1 
ATOM   1812 C  CD1   . ILE A 1 234 ? 21.165  -11.591 16.575  1.00 16.57  ?  234 ILE A CD1   1 
ATOM   1813 N  N     . CYS A 1 235 ? 18.073  -16.230 17.764  1.00 18.26  ?  235 CYS A N     1 
ATOM   1814 C  CA    . CYS A 1 235 ? 16.817  -16.967 17.839  1.00 21.27  ?  235 CYS A CA    1 
ATOM   1815 C  C     . CYS A 1 235 ? 16.728  -17.766 19.127  1.00 19.88  ?  235 CYS A C     1 
ATOM   1816 O  O     . CYS A 1 235 ? 15.691  -17.770 19.798  1.00 17.79  ?  235 CYS A O     1 
ATOM   1817 C  CB    . CYS A 1 235 ? 16.681  -17.887 16.632  1.00 18.56  ?  235 CYS A CB    1 
ATOM   1818 S  SG    . CYS A 1 235 ? 15.897  -17.079 15.275  1.00 19.89  ?  235 CYS A SG    1 
ATOM   1819 N  N     . GLU A 1 236 ? 17.812  -18.461 19.482  1.00 28.44  ?  236 GLU A N     1 
ATOM   1820 C  CA    . GLU A 1 236 ? 17.845  -19.180 20.751  1.00 30.04  ?  236 GLU A CA    1 
ATOM   1821 C  C     . GLU A 1 236 ? 17.716  -18.212 21.914  1.00 29.85  ?  236 GLU A C     1 
ATOM   1822 O  O     . GLU A 1 236 ? 17.007  -18.490 22.891  1.00 25.79  ?  236 GLU A O     1 
ATOM   1823 C  CB    . GLU A 1 236 ? 19.138  -19.994 20.864  1.00 29.46  ?  236 GLU A CB    1 
ATOM   1824 C  CG    . GLU A 1 236 ? 19.000  -21.313 21.597  1.00 42.58  ?  236 GLU A CG    1 
ATOM   1825 C  CD    . GLU A 1 236 ? 19.438  -21.228 23.050  1.00 57.77  ?  236 GLU A CD    1 
ATOM   1826 O  OE1   . GLU A 1 236 ? 19.564  -22.299 23.697  1.00 56.50  ?  236 GLU A OE1   1 
ATOM   1827 O  OE2   . GLU A 1 236 ? 19.656  -20.092 23.540  1.00 52.94  ?  236 GLU A OE2   1 
ATOM   1828 N  N     . ARG A 1 237 ? 18.383  -17.059 21.815  1.00 21.65  ?  237 ARG A N     1 
ATOM   1829 C  CA    . ARG A 1 237 ? 18.335  -16.073 22.888  1.00 20.73  ?  237 ARG A CA    1 
ATOM   1830 C  C     . ARG A 1 237 ? 16.929  -15.522 23.080  1.00 21.39  ?  237 ARG A C     1 
ATOM   1831 O  O     . ARG A 1 237 ? 16.452  -15.396 24.213  1.00 20.86  ?  237 ARG A O     1 
ATOM   1832 C  CB    . ARG A 1 237 ? 19.307  -14.934 22.598  1.00 23.87  ?  237 ARG A CB    1 
ATOM   1833 C  CG    . ARG A 1 237 ? 19.261  -13.844 23.629  1.00 20.55  ?  237 ARG A CG    1 
ATOM   1834 C  CD    . ARG A 1 237 ? 20.309  -12.806 23.354  1.00 22.64  ?  237 ARG A CD    1 
ATOM   1835 N  NE    . ARG A 1 237 ? 21.657  -13.271 23.637  1.00 20.72  ?  237 ARG A NE    1 
ATOM   1836 C  CZ    . ARG A 1 237 ? 22.749  -12.639 23.235  1.00 26.65  ?  237 ARG A CZ    1 
ATOM   1837 N  NH1   . ARG A 1 237 ? 22.679  -11.514 22.536  1.00 20.06  ?  237 ARG A NH1   1 
ATOM   1838 N  NH2   . ARG A 1 237 ? 23.940  -13.144 23.543  1.00 24.93  ?  237 ARG A NH2   1 
ATOM   1839 N  N     . TRP A 1 238 ? 16.250  -15.175 21.982  1.00 20.66  ?  238 TRP A N     1 
ATOM   1840 C  CA    . TRP A 1 238 ? 14.937  -14.525 22.033  1.00 20.57  ?  238 TRP A CA    1 
ATOM   1841 C  C     . TRP A 1 238 ? 13.886  -15.387 21.342  1.00 22.10  ?  238 TRP A C     1 
ATOM   1842 O  O     . TRP A 1 238 ? 13.661  -15.252 20.125  1.00 15.82  ?  238 TRP A O     1 
ATOM   1843 C  CB    . TRP A 1 238 ? 14.987  -13.135 21.401  1.00 14.13  ?  238 TRP A CB    1 
ATOM   1844 C  CG    . TRP A 1 238 ? 16.014  -12.248 22.014  1.00 16.79  ?  238 TRP A CG    1 
ATOM   1845 C  CD1   . TRP A 1 238 ? 17.210  -11.874 21.463  1.00 17.94  ?  238 TRP A CD1   1 
ATOM   1846 C  CD2   . TRP A 1 238 ? 15.944  -11.611 23.300  1.00 19.08  ?  238 TRP A CD2   1 
ATOM   1847 N  NE1   . TRP A 1 238 ? 17.881  -11.038 22.325  1.00 19.22  ?  238 TRP A NE1   1 
ATOM   1848 C  CE2   . TRP A 1 238 ? 17.130  -10.867 23.461  1.00 17.71  ?  238 TRP A CE2   1 
ATOM   1849 C  CE3   . TRP A 1 238 ? 14.993  -11.604 24.333  1.00 19.92  ?  238 TRP A CE3   1 
ATOM   1850 C  CZ2   . TRP A 1 238 ? 17.394  -10.128 24.609  1.00 17.48  ?  238 TRP A CZ2   1 
ATOM   1851 C  CZ3   . TRP A 1 238 ? 15.256  -10.868 25.470  1.00 17.46  ?  238 TRP A CZ3   1 
ATOM   1852 C  CH2   . TRP A 1 238 ? 16.446  -10.144 25.602  1.00 18.84  ?  238 TRP A CH2   1 
ATOM   1853 N  N     . PRO A 1 239 ? 13.215  -16.279 22.076  1.00 16.95  ?  239 PRO A N     1 
ATOM   1854 C  CA    . PRO A 1 239 ? 12.137  -17.063 21.462  1.00 16.23  ?  239 PRO A CA    1 
ATOM   1855 C  C     . PRO A 1 239 ? 11.042  -16.170 20.892  1.00 15.92  ?  239 PRO A C     1 
ATOM   1856 O  O     . PRO A 1 239 ? 10.665  -15.153 21.484  1.00 17.57  ?  239 PRO A O     1 
ATOM   1857 C  CB    . PRO A 1 239 ? 11.616  -17.926 22.620  1.00 16.19  ?  239 PRO A CB    1 
ATOM   1858 C  CG    . PRO A 1 239 ? 12.798  -18.077 23.527  1.00 18.26  ?  239 PRO A CG    1 
ATOM   1859 C  CD    . PRO A 1 239 ? 13.637  -16.829 23.378  1.00 17.14  ?  239 PRO A CD    1 
ATOM   1860 N  N     . ALA A 1 240 ? 10.528  -16.574 19.732  1.00 13.11  ?  240 ALA A N     1 
ATOM   1861 C  CA    . ALA A 1 240 ? 9.386   -15.900 19.136  1.00 16.87  ?  240 ALA A CA    1 
ATOM   1862 C  C     . ALA A 1 240 ? 8.249   -15.793 20.141  1.00 22.67  ?  240 ALA A C     1 
ATOM   1863 O  O     . ALA A 1 240 ? 8.001   -16.719 20.928  1.00 18.32  ?  240 ALA A O     1 
ATOM   1864 C  CB    . ALA A 1 240 ? 8.913   -16.662 17.899  1.00 15.20  ?  240 ALA A CB    1 
ATOM   1865 N  N     . ALA A 1 241 ? 7.549   -14.662 20.112  1.00 18.47  ?  241 ALA A N     1 
ATOM   1866 C  CA    . ALA A 1 241 ? 6.400   -14.483 20.994  1.00 20.01  ?  241 ALA A CA    1 
ATOM   1867 C  C     . ALA A 1 241 ? 5.077   -14.835 20.318  1.00 20.22  ?  241 ALA A C     1 
ATOM   1868 O  O     . ALA A 1 241 ? 4.021   -14.451 20.827  1.00 19.20  ?  241 ALA A O     1 
ATOM   1869 C  CB    . ALA A 1 241 ? 6.344   -13.052 21.526  1.00 21.26  ?  241 ALA A CB    1 
ATOM   1870 N  N     . THR A 1 242 ? 5.113   -15.532 19.179  1.00 17.73  ?  242 THR A N     1 
ATOM   1871 C  CA    . THR A 1 242 ? 3.922   -16.133 18.597  1.00 18.78  ?  242 THR A CA    1 
ATOM   1872 C  C     . THR A 1 242 ? 4.315   -17.408 17.884  1.00 25.10  ?  242 THR A C     1 
ATOM   1873 O  O     . THR A 1 242 ? 5.374   -17.495 17.253  1.00 23.06  ?  242 THR A O     1 
ATOM   1874 C  CB    . THR A 1 242 ? 3.169   -15.276 17.570  1.00 24.95  ?  242 THR A CB    1 
ATOM   1875 O  OG1   . THR A 1 242 ? 4.044   -14.976 16.471  1.00 25.80  ?  242 THR A OG1   1 
ATOM   1876 C  CG2   . THR A 1 242 ? 2.553   -14.002 18.196  1.00 21.25  ?  242 THR A CG2   1 
ATOM   1877 N  N     . GLU A 1 243 ? 3.406   -18.375 17.943  1.00 22.57  ?  243 GLU A N     1 
ATOM   1878 C  CA    . GLU A 1 243 ? 3.639   -19.668 17.322  1.00 28.79  ?  243 GLU A CA    1 
ATOM   1879 C  C     . GLU A 1 243 ? 3.749   -19.551 15.794  1.00 27.36  ?  243 GLU A C     1 
ATOM   1880 O  O     . GLU A 1 243 ? 4.540   -20.264 15.171  1.00 23.36  ?  243 GLU A O     1 
ATOM   1881 C  CB    . GLU A 1 243 ? 2.532   -20.594 17.827  1.00 24.93  ?  243 GLU A CB    1 
ATOM   1882 C  CG    . GLU A 1 243 ? 2.137   -21.800 17.090  1.00 36.99  ?  243 GLU A CG    1 
ATOM   1883 C  CD    . GLU A 1 243 ? 1.299   -21.384 15.907  1.00 49.14  ?  243 GLU A CD    1 
ATOM   1884 O  OE1   . GLU A 1 243 ? 1.396   -21.964 14.813  1.00 51.76  ?  243 GLU A OE1   1 
ATOM   1885 O  OE2   . GLU A 1 243 ? 0.635   -20.318 15.964  1.00 51.15  ?  243 GLU A OE2   1 
ATOM   1886 N  N     . ARG A 1 244 ? 2.984   -18.639 15.181  1.00 28.21  ?  244 ARG A N     1 
ATOM   1887 C  CA    . ARG A 1 244 ? 3.106   -18.396 13.745  1.00 29.02  ?  244 ARG A CA    1 
ATOM   1888 C  C     . ARG A 1 244 ? 4.499   -17.886 13.390  1.00 23.77  ?  244 ARG A C     1 
ATOM   1889 O  O     . ARG A 1 244 ? 5.115   -18.352 12.425  1.00 22.47  ?  244 ARG A O     1 
ATOM   1890 C  CB    . ARG A 1 244 ? 2.033   -17.406 13.272  1.00 26.03  ?  244 ARG A CB    1 
ATOM   1891 C  CG    . ARG A 1 244 ? 1.882   -17.295 11.745  1.00 39.05  ?  244 ARG A CG    1 
ATOM   1892 C  CD    . ARG A 1 244 ? 0.932   -18.350 11.163  1.00 44.94  ?  244 ARG A CD    1 
ATOM   1893 N  NE    . ARG A 1 244 ? -0.375  -17.814 10.790  1.00 43.16  ?  244 ARG A NE    1 
ATOM   1894 C  CZ    . ARG A 1 244 ? -0.674  -17.318 9.595   1.00 41.92  ?  244 ARG A CZ    1 
ATOM   1895 N  NH1   . ARG A 1 244 ? 0.235   -17.230 8.635   1.00 34.71  ?  244 ARG A NH1   1 
ATOM   1896 N  NH2   . ARG A 1 244 ? -1.916  -16.904 9.356   1.00 44.27  ?  244 ARG A NH2   1 
ATOM   1897 N  N     . ALA A 1 245 ? 5.015   -16.922 14.152  1.00 19.64  ?  245 ALA A N     1 
ATOM   1898 C  CA    . ALA A 1 245 ? 6.384   -16.489 13.886  1.00 22.51  ?  245 ALA A CA    1 
ATOM   1899 C  C     . ALA A 1 245 ? 7.374   -17.589 14.219  1.00 18.14  ?  245 ALA A C     1 
ATOM   1900 O  O     . ALA A 1 245 ? 8.417   -17.698 13.572  1.00 16.69  ?  245 ALA A O     1 
ATOM   1901 C  CB    . ALA A 1 245 ? 6.727   -15.215 14.662  1.00 18.75  ?  245 ALA A CB    1 
ATOM   1902 N  N     . GLU A 1 246 ? 7.064   -18.435 15.195  1.00 20.23  ?  246 GLU A N     1 
ATOM   1903 C  CA    . GLU A 1 246 ? 8.004   -19.507 15.501  1.00 26.63  ?  246 GLU A CA    1 
ATOM   1904 C  C     . GLU A 1 246 ? 8.108   -20.513 14.349  1.00 20.82  ?  246 GLU A C     1 
ATOM   1905 O  O     . GLU A 1 246 ? 9.211   -20.970 14.036  1.00 23.86  ?  246 GLU A O     1 
ATOM   1906 C  CB    . GLU A 1 246 ? 7.636   -20.175 16.824  1.00 23.76  ?  246 GLU A CB    1 
ATOM   1907 C  CG    . GLU A 1 246 ? 8.669   -21.207 17.267  1.00 32.51  ?  246 GLU A CG    1 
ATOM   1908 C  CD    . GLU A 1 246 ? 10.060  -20.596 17.491  1.00 34.91  ?  246 GLU A CD    1 
ATOM   1909 O  OE1   . GLU A 1 246 ? 10.256  -19.888 18.511  1.00 23.02  ?  246 GLU A OE1   1 
ATOM   1910 O  OE2   . GLU A 1 246 ? 10.971  -20.859 16.658  1.00 34.87  ?  246 GLU A OE2   1 
ATOM   1911 N  N     . GLN A 1 247 ? 6.988   -20.754 13.670  1.00 19.22  ?  247 GLN A N     1 
ATOM   1912 C  CA    . GLN A 1 247 ? 6.923   -21.662 12.502  1.00 26.50  ?  247 GLN A CA    1 
ATOM   1913 C  C     . GLN A 1 247 ? 7.620   -21.006 11.296  1.00 22.92  ?  247 GLN A C     1 
ATOM   1914 O  O     . GLN A 1 247 ? 8.332   -21.688 10.598  1.00 18.26  ?  247 GLN A O     1 
ATOM   1915 C  CB    . GLN A 1 247 ? 5.477   -22.050 12.181  1.00 28.51  ?  247 GLN A CB    1 
ATOM   1916 C  CG    . GLN A 1 247 ? 4.866   -23.138 13.065  1.00 38.67  ?  247 GLN A CG    1 
ATOM   1917 C  CD    . GLN A 1 247 ? 3.399   -23.447 12.818  1.00 49.21  ?  247 GLN A CD    1 
ATOM   1918 O  OE1   . GLN A 1 247 ? 2.866   -24.462 13.255  1.00 59.64  ?  247 GLN A OE1   1 
ATOM   1919 N  NE2   . GLN A 1 247 ? 2.684   -22.555 12.164  1.00 44.39  ?  247 GLN A NE2   1 
ATOM   1920 N  N     . VAL A 1 248 ? 7.483   -19.693 11.128  1.00 22.98  ?  248 VAL A N     1 
ATOM   1921 C  CA    . VAL A 1 248 ? 8.053   -19.039 9.959   1.00 17.33  ?  248 VAL A CA    1 
ATOM   1922 C  C     . VAL A 1 248 ? 9.556   -18.918 10.109  1.00 17.58  ?  248 VAL A C     1 
ATOM   1923 O  O     . VAL A 1 248 ? 10.276  -18.884 9.104   1.00 21.10  ?  248 VAL A O     1 
ATOM   1924 C  CB    . VAL A 1 248 ? 7.367   -17.689 9.694   1.00 22.58  ?  248 VAL A CB    1 
ATOM   1925 C  CG1   . VAL A 1 248 ? 8.060   -16.946 8.560   1.00 19.14  ?  248 VAL A CG1   1 
ATOM   1926 C  CG2   . VAL A 1 248 ? 5.913   -17.944 9.322   1.00 25.50  ?  248 VAL A CG2   1 
ATOM   1927 N  N     . ARG A 1 249 ? 10.059  -18.922 11.341  1.00 13.61  ?  249 ARG A N     1 
ATOM   1928 C  CA    . ARG A 1 249 ? 11.500  -18.950 11.539  1.00 12.94  ?  249 ARG A CA    1 
ATOM   1929 C  C     . ARG A 1 249 ? 12.140  -20.115 10.801  1.00 20.20  ?  249 ARG A C     1 
ATOM   1930 O  O     . ARG A 1 249 ? 13.258  -19.989 10.294  1.00 24.04  ?  249 ARG A O     1 
ATOM   1931 C  CB    . ARG A 1 249 ? 11.828  -19.027 13.027  1.00 17.80  ?  249 ARG A CB    1 
ATOM   1932 C  CG    . ARG A 1 249 ? 11.925  -17.677 13.723  1.00 23.79  ?  249 ARG A CG    1 
ATOM   1933 C  CD    . ARG A 1 249 ? 12.085  -17.873 15.221  1.00 21.49  ?  249 ARG A CD    1 
ATOM   1934 N  NE    . ARG A 1 249 ? 12.335  -16.619 15.920  1.00 19.33  ?  249 ARG A NE    1 
ATOM   1935 C  CZ    . ARG A 1 249 ? 12.879  -16.540 17.128  1.00 18.68  ?  249 ARG A CZ    1 
ATOM   1936 N  NH1   . ARG A 1 249 ? 13.278  -17.622 17.780  1.00 16.19  ?  249 ARG A NH1   1 
ATOM   1937 N  NH2   . ARG A 1 249 ? 13.020  -15.346 17.699  1.00 19.53  ?  249 ARG A NH2   1 
ATOM   1938 N  N     . ARG A 1 250 ? 11.442  -21.257 10.718  1.00 21.46  ?  250 ARG A N     1 
ATOM   1939 C  CA    . ARG A 1 250 ? 12.001  -22.431 10.055  1.00 23.45  ?  250 ARG A CA    1 
ATOM   1940 C  C     . ARG A 1 250 ? 12.199  -22.221 8.560   1.00 25.57  ?  250 ARG A C     1 
ATOM   1941 O  O     . ARG A 1 250 ? 12.906  -23.008 7.919   1.00 22.53  ?  250 ARG A O     1 
ATOM   1942 C  CB    . ARG A 1 250 ? 11.117  -23.661 10.286  1.00 19.17  ?  250 ARG A CB    1 
ATOM   1943 C  CG    . ARG A 1 250 ? 10.866  -23.988 11.744  1.00 24.40  ?  250 ARG A CG    1 
ATOM   1944 C  CD    . ARG A 1 250 ? 10.645  -25.483 11.966  1.00 41.95  ?  250 ARG A CD    1 
ATOM   1945 N  NE    . ARG A 1 250 ? 9.374   -25.959 11.427  1.00 49.52  ?  250 ARG A NE    1 
ATOM   1946 C  CZ    . ARG A 1 250 ? 8.869   -27.169 11.651  1.00 48.38  ?  250 ARG A CZ    1 
ATOM   1947 N  NH1   . ARG A 1 250 ? 9.492   -28.043 12.424  1.00 46.77  ?  250 ARG A NH1   1 
ATOM   1948 N  NH2   . ARG A 1 250 ? 7.718   -27.514 11.071  1.00 38.80  ?  250 ARG A NH2   1 
ATOM   1949 N  N     . PHE A 1 251 ? 11.594  -21.187 7.980   1.00 24.36  ?  251 PHE A N     1 
ATOM   1950 C  CA    . PHE A 1 251 ? 11.872  -20.922 6.580   1.00 26.03  ?  251 PHE A CA    1 
ATOM   1951 C  C     . PHE A 1 251 ? 13.247  -20.306 6.370   1.00 25.71  ?  251 PHE A C     1 
ATOM   1952 O  O     . PHE A 1 251 ? 13.793  -20.411 5.264   1.00 25.76  ?  251 PHE A O     1 
ATOM   1953 C  CB    . PHE A 1 251 ? 10.793  -20.024 5.991   1.00 22.33  ?  251 PHE A CB    1 
ATOM   1954 C  CG    . PHE A 1 251 ? 9.510   -20.743 5.696   1.00 28.19  ?  251 PHE A CG    1 
ATOM   1955 C  CD1   . PHE A 1 251 ? 8.428   -20.647 6.566   1.00 31.84  ?  251 PHE A CD1   1 
ATOM   1956 C  CD2   . PHE A 1 251 ? 9.371   -21.489 4.537   1.00 34.02  ?  251 PHE A CD2   1 
ATOM   1957 C  CE1   . PHE A 1 251 ? 7.223   -21.305 6.298   1.00 31.41  ?  251 PHE A CE1   1 
ATOM   1958 C  CE2   . PHE A 1 251 ? 8.181   -22.152 4.252   1.00 35.95  ?  251 PHE A CE2   1 
ATOM   1959 C  CZ    . PHE A 1 251 ? 7.098   -22.057 5.139   1.00 38.34  ?  251 PHE A CZ    1 
ATOM   1960 N  N     . MET A 1 252 ? 13.832  -19.672 7.389   1.00 24.35  ?  252 MET A N     1 
ATOM   1961 C  CA    . MET A 1 252 ? 15.081  -18.968 7.095   1.00 24.51  ?  252 MET A CA    1 
ATOM   1962 C  C     . MET A 1 252 ? 16.225  -19.920 6.757   1.00 25.78  ?  252 MET A C     1 
ATOM   1963 O  O     . MET A 1 252 ? 17.003  -19.615 5.843   1.00 28.63  ?  252 MET A O     1 
ATOM   1964 C  CB    . MET A 1 252 ? 15.474  -18.034 8.241   1.00 22.73  ?  252 MET A CB    1 
ATOM   1965 C  CG    . MET A 1 252 ? 14.499  -16.867 8.385   1.00 20.62  ?  252 MET A CG    1 
ATOM   1966 S  SD    . MET A 1 252 ? 14.727  -15.632 7.094   1.00 31.90  ?  252 MET A SD    1 
ATOM   1967 C  CE    . MET A 1 252 ? 16.468  -15.249 7.247   1.00 21.01  ?  252 MET A CE    1 
ATOM   1968 N  N     . PRO A 1 253 ? 16.382  -21.057 7.453   1.00 22.59  ?  253 PRO A N     1 
ATOM   1969 C  CA    . PRO A 1 253 ? 17.390  -22.038 7.001   1.00 22.44  ?  253 PRO A CA    1 
ATOM   1970 C  C     . PRO A 1 253 ? 17.109  -22.598 5.616   1.00 22.49  ?  253 PRO A C     1 
ATOM   1971 O  O     . PRO A 1 253 ? 18.050  -22.860 4.859   1.00 24.88  ?  253 PRO A O     1 
ATOM   1972 C  CB    . PRO A 1 253 ? 17.332  -23.121 8.087   1.00 27.77  ?  253 PRO A CB    1 
ATOM   1973 C  CG    . PRO A 1 253 ? 16.816  -22.388 9.300   1.00 24.51  ?  253 PRO A CG    1 
ATOM   1974 C  CD    . PRO A 1 253 ? 15.820  -21.427 8.764   1.00 19.86  ?  253 PRO A CD    1 
ATOM   1975 N  N     . VAL A 1 254 ? 15.837  -22.779 5.256   1.00 20.01  ?  254 VAL A N     1 
ATOM   1976 C  CA    . VAL A 1 254 ? 15.492  -23.121 3.878   1.00 21.54  ?  254 VAL A CA    1 
ATOM   1977 C  C     . VAL A 1 254 ? 16.087  -22.095 2.924   1.00 24.57  ?  254 VAL A C     1 
ATOM   1978 O  O     . VAL A 1 254 ? 16.722  -22.438 1.925   1.00 27.94  ?  254 VAL A O     1 
ATOM   1979 C  CB    . VAL A 1 254 ? 13.965  -23.213 3.718   1.00 23.71  ?  254 VAL A CB    1 
ATOM   1980 C  CG1   . VAL A 1 254 ? 13.537  -22.878 2.291   1.00 24.15  ?  254 VAL A CG1   1 
ATOM   1981 C  CG2   . VAL A 1 254 ? 13.482  -24.588 4.127   1.00 30.91  ?  254 VAL A CG2   1 
ATOM   1982 N  N     . MET A 1 255 ? 15.892  -20.815 3.231   1.00 26.17  ?  255 MET A N     1 
ATOM   1983 C  CA    . MET A 1 255 ? 16.438  -19.752 2.405   1.00 22.81  ?  255 MET A CA    1 
ATOM   1984 C  C     . MET A 1 255 ? 17.963  -19.754 2.439   1.00 23.36  ?  255 MET A C     1 
ATOM   1985 O  O     . MET A 1 255 ? 18.610  -19.535 1.408   1.00 21.97  ?  255 MET A O     1 
ATOM   1986 C  CB    . MET A 1 255 ? 15.868  -18.416 2.871   1.00 27.29  ?  255 MET A CB    1 
ATOM   1987 C  CG    . MET A 1 255 ? 16.350  -17.213 2.073   1.00 31.06  ?  255 MET A CG    1 
ATOM   1988 S  SD    . MET A 1 255 ? 17.886  -16.534 2.749   1.00 40.91  ?  255 MET A SD    1 
ATOM   1989 C  CE    . MET A 1 255 ? 17.238  -15.151 3.696   1.00 27.20  ?  255 MET A CE    1 
ATOM   1990 N  N     . TYR A 1 256 ? 18.557  -19.994 3.606   1.00 20.96  ?  256 TYR A N     1 
ATOM   1991 C  CA    . TYR A 1 256 ? 20.012  -19.997 3.681   1.00 23.79  ?  256 TYR A CA    1 
ATOM   1992 C  C     . TYR A 1 256 ? 20.596  -21.114 2.833   1.00 24.90  ?  256 TYR A C     1 
ATOM   1993 O  O     . TYR A 1 256 ? 21.590  -20.917 2.126   1.00 24.00  ?  256 TYR A O     1 
ATOM   1994 C  CB    . TYR A 1 256 ? 20.478  -20.143 5.129   1.00 25.25  ?  256 TYR A CB    1 
ATOM   1995 C  CG    . TYR A 1 256 ? 20.163  -18.955 6.004   1.00 30.60  ?  256 TYR A CG    1 
ATOM   1996 C  CD1   . TYR A 1 256 ? 20.319  -17.664 5.529   1.00 31.39  ?  256 TYR A CD1   1 
ATOM   1997 C  CD2   . TYR A 1 256 ? 19.728  -19.128 7.313   1.00 27.97  ?  256 TYR A CD2   1 
ATOM   1998 C  CE1   . TYR A 1 256 ? 20.039  -16.577 6.321   1.00 30.42  ?  256 TYR A CE1   1 
ATOM   1999 C  CE2   . TYR A 1 256 ? 19.449  -18.052 8.114   1.00 26.58  ?  256 TYR A CE2   1 
ATOM   2000 C  CZ    . TYR A 1 256 ? 19.603  -16.773 7.614   1.00 32.75  ?  256 TYR A CZ    1 
ATOM   2001 O  OH    . TYR A 1 256 ? 19.328  -15.685 8.411   1.00 27.66  ?  256 TYR A OH    1 
ATOM   2002 N  N     . GLN A 1 257 ? 19.994  -22.300 2.895   1.00 26.98  ?  257 GLN A N     1 
ATOM   2003 C  CA    . GLN A 1 257 ? 20.496  -23.413 2.099   1.00 31.13  ?  257 GLN A CA    1 
ATOM   2004 C  C     . GLN A 1 257 ? 20.414  -23.088 0.620   1.00 25.16  ?  257 GLN A C     1 
ATOM   2005 O  O     . GLN A 1 257 ? 21.345  -23.374 -0.139  1.00 25.25  ?  257 GLN A O     1 
ATOM   2006 C  CB    . GLN A 1 257 ? 19.718  -24.689 2.419   1.00 19.95  ?  257 GLN A CB    1 
ATOM   2007 C  CG    . GLN A 1 257 ? 20.127  -25.300 3.741   1.00 30.83  ?  257 GLN A CG    1 
ATOM   2008 C  CD    . GLN A 1 257 ? 21.631  -25.182 3.984   1.00 35.41  ?  257 GLN A CD    1 
ATOM   2009 O  OE1   . GLN A 1 257 ? 22.444  -25.622 3.158   1.00 31.86  ?  257 GLN A OE1   1 
ATOM   2010 N  NE2   . GLN A 1 257 ? 22.007  -24.587 5.120   1.00 36.08  ?  257 GLN A NE2   1 
ATOM   2011 N  N     . MET A 1 258 ? 19.311  -22.471 0.201   1.00 22.60  ?  258 MET A N     1 
ATOM   2012 C  CA    . MET A 1 258 ? 19.176  -22.082 -1.190  1.00 23.83  ?  258 MET A CA    1 
ATOM   2013 C  C     . MET A 1 258 ? 20.294  -21.133 -1.579  1.00 29.42  ?  258 MET A C     1 
ATOM   2014 O  O     . MET A 1 258 ? 20.901  -21.274 -2.651  1.00 28.51  ?  258 MET A O     1 
ATOM   2015 C  CB    . MET A 1 258 ? 17.817  -21.432 -1.401  1.00 25.04  ?  258 MET A CB    1 
ATOM   2016 C  CG    . MET A 1 258 ? 16.770  -22.369 -1.898  1.00 27.55  ?  258 MET A CG    1 
ATOM   2017 S  SD    . MET A 1 258 ? 15.165  -21.687 -1.491  1.00 42.46  ?  258 MET A SD    1 
ATOM   2018 C  CE    . MET A 1 258 ? 15.211  -20.200 -2.456  1.00 34.13  ?  258 MET A CE    1 
ATOM   2019 N  N     . ALA A 1 259 ? 20.618  -20.198 -0.685  1.00 23.71  ?  259 ALA A N     1 
ATOM   2020 C  CA    . ALA A 1 259 ? 21.668  -19.229 -0.958  1.00 28.36  ?  259 ALA A CA    1 
ATOM   2021 C  C     . ALA A 1 259 ? 23.028  -19.912 -1.088  1.00 28.97  ?  259 ALA A C     1 
ATOM   2022 O  O     . ALA A 1 259 ? 23.762  -19.673 -2.057  1.00 21.40  ?  259 ALA A O     1 
ATOM   2023 C  CB    . ALA A 1 259 ? 21.673  -18.159 0.137   1.00 24.12  ?  259 ALA A CB    1 
ATOM   2024 N  N     . TYR A 1 260 ? 23.382  -20.766 -0.119  1.00 20.01  ?  260 TYR A N     1 
ATOM   2025 C  CA    . TYR A 1 260 ? 24.637  -21.508 -0.196  1.00 23.23  ?  260 TYR A CA    1 
ATOM   2026 C  C     . TYR A 1 260 ? 24.750  -22.286 -1.502  1.00 26.04  ?  260 TYR A C     1 
ATOM   2027 O  O     . TYR A 1 260 ? 25.791  -22.263 -2.161  1.00 18.69  ?  260 TYR A O     1 
ATOM   2028 C  CB    . TYR A 1 260 ? 24.760  -22.475 0.974   1.00 24.52  ?  260 TYR A CB    1 
ATOM   2029 C  CG    . TYR A 1 260 ? 24.948  -21.817 2.305   1.00 29.53  ?  260 TYR A CG    1 
ATOM   2030 C  CD1   . TYR A 1 260 ? 25.921  -20.847 2.490   1.00 34.26  ?  260 TYR A CD1   1 
ATOM   2031 C  CD2   . TYR A 1 260 ? 24.163  -22.181 3.394   1.00 30.10  ?  260 TYR A CD2   1 
ATOM   2032 C  CE1   . TYR A 1 260 ? 26.095  -20.247 3.728   1.00 40.68  ?  260 TYR A CE1   1 
ATOM   2033 C  CE2   . TYR A 1 260 ? 24.328  -21.594 4.620   1.00 30.79  ?  260 TYR A CE2   1 
ATOM   2034 C  CZ    . TYR A 1 260 ? 25.292  -20.629 4.785   1.00 36.41  ?  260 TYR A CZ    1 
ATOM   2035 O  OH    . TYR A 1 260 ? 25.456  -20.046 6.011   1.00 35.97  ?  260 TYR A OH    1 
ATOM   2036 N  N     . ALA A 1 261 ? 23.694  -23.011 -1.875  1.00 29.51  ?  261 ALA A N     1 
ATOM   2037 C  CA    . ALA A 1 261 ? 23.757  -23.816 -3.089  1.00 27.72  ?  261 ALA A CA    1 
ATOM   2038 C  C     . ALA A 1 261 ? 24.013  -22.938 -4.304  1.00 27.71  ?  261 ALA A C     1 
ATOM   2039 O  O     . ALA A 1 261 ? 24.786  -23.308 -5.198  1.00 20.48  ?  261 ALA A O     1 
ATOM   2040 C  CB    . ALA A 1 261 ? 22.466  -24.615 -3.263  1.00 23.48  ?  261 ALA A CB    1 
ATOM   2041 N  N     . SER A 1 262 ? 23.375  -21.766 -4.345  1.00 23.75  ?  262 SER A N     1 
ATOM   2042 C  CA    . SER A 1 262 ? 23.591  -20.828 -5.443  1.00 30.85  ?  262 SER A CA    1 
ATOM   2043 C  C     . SER A 1 262 ? 25.043  -20.366 -5.484  1.00 27.81  ?  262 SER A C     1 
ATOM   2044 O  O     . SER A 1 262 ? 25.717  -20.480 -6.519  1.00 24.74  ?  262 SER A O     1 
ATOM   2045 C  CB    . SER A 1 262 ? 22.642  -19.637 -5.299  1.00 29.93  ?  262 SER A CB    1 
ATOM   2046 O  OG    . SER A 1 262 ? 22.301  -19.113 -6.565  1.00 33.14  ?  262 SER A OG    1 
ATOM   2047 N  N     . PHE A 1 263 ? 25.544  -19.853 -4.353  1.00 23.76  ?  263 PHE A N     1 
ATOM   2048 C  CA    . PHE A 1 263 ? 26.945  -19.461 -4.256  1.00 27.90  ?  263 PHE A CA    1 
ATOM   2049 C  C     . PHE A 1 263 ? 27.865  -20.582 -4.732  1.00 28.06  ?  263 PHE A C     1 
ATOM   2050 O  O     . PHE A 1 263 ? 28.732  -20.364 -5.583  1.00 28.54  ?  263 PHE A O     1 
ATOM   2051 C  CB    . PHE A 1 263 ? 27.291  -19.056 -2.820  1.00 24.50  ?  263 PHE A CB    1 
ATOM   2052 C  CG    . PHE A 1 263 ? 26.612  -17.783 -2.349  1.00 29.72  ?  263 PHE A CG    1 
ATOM   2053 C  CD1   . PHE A 1 263 ? 26.095  -16.870 -3.253  1.00 32.30  ?  263 PHE A CD1   1 
ATOM   2054 C  CD2   . PHE A 1 263 ? 26.485  -17.510 -0.990  1.00 35.01  ?  263 PHE A CD2   1 
ATOM   2055 C  CE1   . PHE A 1 263 ? 25.465  -15.701 -2.806  1.00 37.36  ?  263 PHE A CE1   1 
ATOM   2056 C  CE2   . PHE A 1 263 ? 25.861  -16.349 -0.542  1.00 33.05  ?  263 PHE A CE2   1 
ATOM   2057 C  CZ    . PHE A 1 263 ? 25.350  -15.447 -1.451  1.00 29.83  ?  263 PHE A CZ    1 
ATOM   2058 N  N     . GLU A 1 264 ? 27.672  -21.798 -4.213  1.00 28.01  ?  264 GLU A N     1 
ATOM   2059 C  CA    . GLU A 1 264 ? 28.562  -22.902 -4.573  1.00 25.24  ?  264 GLU A CA    1 
ATOM   2060 C  C     . GLU A 1 264 ? 28.527  -23.204 -6.066  1.00 25.42  ?  264 GLU A C     1 
ATOM   2061 O  O     . GLU A 1 264 ? 29.549  -23.589 -6.644  1.00 26.87  ?  264 GLU A O     1 
ATOM   2062 C  CB    . GLU A 1 264 ? 28.200  -24.150 -3.780  1.00 28.03  ?  264 GLU A CB    1 
ATOM   2063 C  CG    . GLU A 1 264 ? 29.188  -24.426 -2.669  1.00 35.13  ?  264 GLU A CG    1 
ATOM   2064 C  CD    . GLU A 1 264 ? 28.582  -25.248 -1.570  1.00 42.32  ?  264 GLU A CD    1 
ATOM   2065 O  OE1   . GLU A 1 264 ? 27.443  -25.719 -1.763  1.00 43.98  ?  264 GLU A OE1   1 
ATOM   2066 O  OE2   . GLU A 1 264 ? 29.245  -25.444 -0.528  1.00 50.50  ?  264 GLU A OE2   1 
ATOM   2067 N  N     . ALA A 1 265 ? 27.372  -23.040 -6.700  1.00 24.83  ?  265 ALA A N     1 
ATOM   2068 C  CA    . ALA A 1 265 ? 27.212  -23.196 -8.137  1.00 29.69  ?  265 ALA A CA    1 
ATOM   2069 C  C     . ALA A 1 265 ? 27.661  -21.963 -8.927  1.00 31.51  ?  265 ALA A C     1 
ATOM   2070 O  O     . ALA A 1 265 ? 27.400  -21.892 -10.134 1.00 31.73  ?  265 ALA A O     1 
ATOM   2071 C  CB    . ALA A 1 265 ? 25.748  -23.519 -8.459  1.00 24.40  ?  265 ALA A CB    1 
ATOM   2072 N  N     . GLY A 1 266 ? 28.296  -20.987 -8.278  1.00 32.45  ?  266 GLY A N     1 
ATOM   2073 C  CA    . GLY A 1 266 ? 28.768  -19.800 -8.973  1.00 26.99  ?  266 GLY A CA    1 
ATOM   2074 C  C     . GLY A 1 266 ? 27.685  -18.928 -9.574  1.00 37.16  ?  266 GLY A C     1 
ATOM   2075 O  O     . GLY A 1 266 ? 27.936  -18.248 -10.578 1.00 38.48  ?  266 GLY A O     1 
ATOM   2076 N  N     . VAL A 1 267 ? 26.491  -18.912 -8.983  1.00 34.96  ?  267 VAL A N     1 
ATOM   2077 C  CA    . VAL A 1 267 ? 25.357  -18.155 -9.518  1.00 29.02  ?  267 VAL A CA    1 
ATOM   2078 C  C     . VAL A 1 267 ? 24.962  -17.050 -8.543  1.00 38.72  ?  267 VAL A C     1 
ATOM   2079 O  O     . VAL A 1 267 ? 24.507  -17.343 -7.426  1.00 37.38  ?  267 VAL A O     1 
ATOM   2080 C  CB    . VAL A 1 267 ? 24.157  -19.071 -9.795  1.00 32.06  ?  267 VAL A CB    1 
ATOM   2081 C  CG1   . VAL A 1 267 ? 22.917  -18.235 -10.109 1.00 35.79  ?  267 VAL A CG1   1 
ATOM   2082 C  CG2   . VAL A 1 267 ? 24.473  -20.049 -10.920 1.00 34.98  ?  267 VAL A CG2   1 
ATOM   2083 N  N     . PRO A 1 268 ? 25.098  -15.781 -8.911  1.00 39.08  ?  268 PRO A N     1 
ATOM   2084 C  CA    . PRO A 1 268 ? 24.755  -14.707 -7.967  1.00 44.40  ?  268 PRO A CA    1 
ATOM   2085 C  C     . PRO A 1 268 ? 23.255  -14.637 -7.692  1.00 42.68  ?  268 PRO A C     1 
ATOM   2086 O  O     . PRO A 1 268 ? 22.417  -14.926 -8.552  1.00 40.64  ?  268 PRO A O     1 
ATOM   2087 C  CB    . PRO A 1 268 ? 25.254  -13.427 -8.656  1.00 48.46  ?  268 PRO A CB    1 
ATOM   2088 C  CG    . PRO A 1 268 ? 25.877  -13.835 -9.952  1.00 45.94  ?  268 PRO A CG    1 
ATOM   2089 C  CD    . PRO A 1 268 ? 25.733  -15.305 -10.152 1.00 38.50  ?  268 PRO A CD    1 
ATOM   2090 N  N     . LEU A 1 269 ? 22.922  -14.264 -6.459  1.00 41.54  ?  269 LEU A N     1 
ATOM   2091 C  CA    . LEU A 1 269 ? 21.536  -14.021 -6.087  1.00 34.25  ?  269 LEU A CA    1 
ATOM   2092 C  C     . LEU A 1 269 ? 21.150  -12.588 -6.424  1.00 38.23  ?  269 LEU A C     1 
ATOM   2093 O  O     . LEU A 1 269 ? 22.007  -11.730 -6.643  1.00 40.56  ?  269 LEU A O     1 
ATOM   2094 C  CB    . LEU A 1 269 ? 21.317  -14.268 -4.605  1.00 28.62  ?  269 LEU A CB    1 
ATOM   2095 C  CG    . LEU A 1 269 ? 21.765  -15.596 -4.027  1.00 32.00  ?  269 LEU A CG    1 
ATOM   2096 C  CD1   . LEU A 1 269 ? 22.072  -15.432 -2.556  1.00 27.73  ?  269 LEU A CD1   1 
ATOM   2097 C  CD2   . LEU A 1 269 ? 20.667  -16.617 -4.234  1.00 33.19  ?  269 LEU A CD2   1 
ATOM   2098 N  N     . ASP A 1 270 ? 19.841  -12.335 -6.465  1.00 43.23  ?  270 ASP A N     1 
ATOM   2099 C  CA    . ASP A 1 270 ? 19.358  -10.969 -6.643  1.00 41.32  ?  270 ASP A CA    1 
ATOM   2100 C  C     . ASP A 1 270 ? 19.993  -10.059 -5.601  1.00 36.42  ?  270 ASP A C     1 
ATOM   2101 O  O     . ASP A 1 270 ? 20.067  -10.411 -4.419  1.00 32.23  ?  270 ASP A O     1 
ATOM   2102 C  CB    . ASP A 1 270 ? 17.834  -10.918 -6.530  1.00 40.25  ?  270 ASP A CB    1 
ATOM   2103 C  CG    . ASP A 1 270 ? 17.282  -9.503  -6.695  1.00 47.28  ?  270 ASP A CG    1 
ATOM   2104 O  OD1   . ASP A 1 270 ? 16.743  -9.199  -7.788  1.00 50.29  ?  270 ASP A OD1   1 
ATOM   2105 O  OD2   . ASP A 1 270 ? 17.383  -8.695  -5.737  1.00 42.57  ?  270 ASP A OD2   1 
ATOM   2106 N  N     . HIS A 1 271 ? 20.476  -8.896  -6.053  1.00 36.41  ?  271 HIS A N     1 
ATOM   2107 C  CA    . HIS A 1 271 ? 21.144  -7.960  -5.153  1.00 36.06  ?  271 HIS A CA    1 
ATOM   2108 C  C     . HIS A 1 271 ? 20.294  -7.596  -3.939  1.00 34.90  ?  271 HIS A C     1 
ATOM   2109 O  O     . HIS A 1 271 ? 20.850  -7.200  -2.907  1.00 31.30  ?  271 HIS A O     1 
ATOM   2110 C  CB    . HIS A 1 271 ? 21.534  -6.685  -5.900  1.00 34.94  ?  271 HIS A CB    1 
ATOM   2111 C  CG    . HIS A 1 271 ? 22.215  -5.671  -5.031  1.00 43.97  ?  271 HIS A CG    1 
ATOM   2112 N  ND1   . HIS A 1 271 ? 21.598  -4.510  -4.613  1.00 49.45  ?  271 HIS A ND1   1 
ATOM   2113 C  CD2   . HIS A 1 271 ? 23.453  -5.656  -4.481  1.00 44.81  ?  271 HIS A CD2   1 
ATOM   2114 C  CE1   . HIS A 1 271 ? 22.431  -3.817  -3.855  1.00 44.60  ?  271 HIS A CE1   1 
ATOM   2115 N  NE2   . HIS A 1 271 ? 23.562  -4.493  -3.756  1.00 46.75  ?  271 HIS A NE2   1 
ATOM   2116 N  N     . HIS A 1 272 ? 18.964  -7.729  -4.032  1.00 30.21  ?  272 HIS A N     1 
ATOM   2117 C  CA    . HIS A 1 272 ? 18.048  -7.451  -2.929  1.00 33.50  ?  272 HIS A CA    1 
ATOM   2118 C  C     . HIS A 1 272 ? 17.360  -8.719  -2.414  1.00 32.74  ?  272 HIS A C     1 
ATOM   2119 O  O     . HIS A 1 272 ? 16.224  -8.659  -1.943  1.00 27.96  ?  272 HIS A O     1 
ATOM   2120 C  CB    . HIS A 1 272 ? 16.988  -6.437  -3.362  1.00 35.57  ?  272 HIS A CB    1 
ATOM   2121 C  CG    . HIS A 1 272 ? 17.532  -5.091  -3.740  1.00 44.34  ?  272 HIS A CG    1 
ATOM   2122 N  ND1   . HIS A 1 272 ? 18.396  -4.376  -2.936  1.00 48.42  ?  272 HIS A ND1   1 
ATOM   2123 C  CD2   . HIS A 1 272 ? 17.322  -4.327  -4.839  1.00 37.93  ?  272 HIS A CD2   1 
ATOM   2124 C  CE1   . HIS A 1 272 ? 18.698  -3.231  -3.526  1.00 44.67  ?  272 HIS A CE1   1 
ATOM   2125 N  NE2   . HIS A 1 272 ? 18.055  -3.175  -4.679  1.00 43.55  ?  272 HIS A NE2   1 
ATOM   2126 N  N     . TYR A 1 273 ? 18.025  -9.876  -2.501  1.00 29.04  ?  273 TYR A N     1 
ATOM   2127 C  CA    . TYR A 1 273 ? 17.355  -11.136 -2.188  1.00 28.24  ?  273 TYR A CA    1 
ATOM   2128 C  C     . TYR A 1 273 ? 16.861  -11.188 -0.749  1.00 25.81  ?  273 TYR A C     1 
ATOM   2129 O  O     . TYR A 1 273 ? 15.871  -11.869 -0.465  1.00 24.50  ?  273 TYR A O     1 
ATOM   2130 C  CB    . TYR A 1 273 ? 18.281  -12.319 -2.440  1.00 22.64  ?  273 TYR A CB    1 
ATOM   2131 C  CG    . TYR A 1 273 ? 19.371  -12.516 -1.393  1.00 22.88  ?  273 TYR A CG    1 
ATOM   2132 C  CD1   . TYR A 1 273 ? 20.545  -11.765 -1.422  1.00 25.47  ?  273 TYR A CD1   1 
ATOM   2133 C  CD2   . TYR A 1 273 ? 19.239  -13.471 -0.396  1.00 22.44  ?  273 TYR A CD2   1 
ATOM   2134 C  CE1   . TYR A 1 273 ? 21.547  -11.958 -0.476  1.00 21.09  ?  273 TYR A CE1   1 
ATOM   2135 C  CE2   . TYR A 1 273 ? 20.240  -13.672 0.543   1.00 21.51  ?  273 TYR A CE2   1 
ATOM   2136 C  CZ    . TYR A 1 273 ? 21.384  -12.920 0.496   1.00 22.51  ?  273 TYR A CZ    1 
ATOM   2137 O  OH    . TYR A 1 273 ? 22.369  -13.132 1.430   1.00 28.87  ?  273 TYR A OH    1 
ATOM   2138 N  N     . TYR A 1 274 ? 17.549  -10.517 0.175   1.00 28.95  ?  274 TYR A N     1 
ATOM   2139 C  CA    . TYR A 1 274 ? 17.086  -10.517 1.558   1.00 26.74  ?  274 TYR A CA    1 
ATOM   2140 C  C     . TYR A 1 274 ? 15.764  -9.769  1.676   1.00 23.02  ?  274 TYR A C     1 
ATOM   2141 O  O     . TYR A 1 274 ? 14.807  -10.276 2.267   1.00 25.43  ?  274 TYR A O     1 
ATOM   2142 C  CB    . TYR A 1 274 ? 18.154  -9.915  2.484   1.00 23.87  ?  274 TYR A CB    1 
ATOM   2143 C  CG    . TYR A 1 274 ? 17.767  -9.944  3.953   1.00 27.48  ?  274 TYR A CG    1 
ATOM   2144 C  CD1   . TYR A 1 274 ? 17.058  -8.888  4.527   1.00 21.03  ?  274 TYR A CD1   1 
ATOM   2145 C  CD2   . TYR A 1 274 ? 18.099  -11.030 4.760   1.00 25.33  ?  274 TYR A CD2   1 
ATOM   2146 C  CE1   . TYR A 1 274 ? 16.689  -8.912  5.864   1.00 26.04  ?  274 TYR A CE1   1 
ATOM   2147 C  CE2   . TYR A 1 274 ? 17.728  -11.071 6.105   1.00 30.24  ?  274 TYR A CE2   1 
ATOM   2148 C  CZ    . TYR A 1 274 ? 17.020  -10.006 6.656   1.00 30.16  ?  274 TYR A CZ    1 
ATOM   2149 O  OH    . TYR A 1 274 ? 16.650  -10.031 7.993   1.00 17.73  ?  274 TYR A OH    1 
ATOM   2150 N  N     . GLU A 1 275 ? 15.690  -8.570  1.091   1.00 23.97  ?  275 GLU A N     1 
ATOM   2151 C  CA    . GLU A 1 275 ? 14.493  -7.733  1.167   1.00 26.97  ?  275 GLU A CA    1 
ATOM   2152 C  C     . GLU A 1 275 ? 13.302  -8.359  0.450   1.00 26.20  ?  275 GLU A C     1 
ATOM   2153 O  O     . GLU A 1 275 ? 12.155  -8.175  0.879   1.00 22.23  ?  275 GLU A O     1 
ATOM   2154 C  CB    . GLU A 1 275 ? 14.789  -6.353  0.575   1.00 27.61  ?  275 GLU A CB    1 
ATOM   2155 C  CG    . GLU A 1 275 ? 15.791  -5.546  1.376   1.00 27.19  ?  275 GLU A CG    1 
ATOM   2156 C  CD    . GLU A 1 275 ? 17.245  -5.936  1.117   1.00 36.38  ?  275 GLU A CD    1 
ATOM   2157 O  OE1   . GLU A 1 275 ? 17.534  -6.608  0.098   1.00 38.73  ?  275 GLU A OE1   1 
ATOM   2158 O  OE2   . GLU A 1 275 ? 18.108  -5.562  1.942   1.00 39.93  ?  275 GLU A OE2   1 
ATOM   2159 N  N     . ARG A 1 276 ? 13.544  -9.076  -0.650  1.00 20.99  ?  276 ARG A N     1 
ATOM   2160 C  CA    . ARG A 1 276 ? 12.464  -9.813  -1.291  1.00 21.93  ?  276 ARG A CA    1 
ATOM   2161 C  C     . ARG A 1 276 ? 12.034  -10.999 -0.435  1.00 21.00  ?  276 ARG A C     1 
ATOM   2162 O  O     . ARG A 1 276 ? 10.875  -11.425 -0.486  1.00 19.15  ?  276 ARG A O     1 
ATOM   2163 C  CB    . ARG A 1 276 ? 12.905  -10.254 -2.687  1.00 27.81  ?  276 ARG A CB    1 
ATOM   2164 C  CG    . ARG A 1 276 ? 13.543  -9.099  -3.466  1.00 32.03  ?  276 ARG A CG    1 
ATOM   2165 C  CD    . ARG A 1 276 ? 13.545  -9.286  -4.958  1.00 32.45  ?  276 ARG A CD    1 
ATOM   2166 N  NE    . ARG A 1 276 ? 14.182  -8.145  -5.612  1.00 47.63  ?  276 ARG A NE    1 
ATOM   2167 C  CZ    . ARG A 1 276 ? 13.533  -7.132  -6.180  1.00 43.38  ?  276 ARG A CZ    1 
ATOM   2168 N  NH1   . ARG A 1 276 ? 12.210  -7.081  -6.202  1.00 52.22  ?  276 ARG A NH1   1 
ATOM   2169 N  NH2   . ARG A 1 276 ? 14.228  -6.145  -6.743  1.00 44.90  ?  276 ARG A NH2   1 
ATOM   2170 N  N     . THR A 1 277 ? 12.946  -11.532 0.369   1.00 18.26  ?  277 THR A N     1 
ATOM   2171 C  CA    . THR A 1 277 ? 12.567  -12.587 1.292   1.00 22.16  ?  277 THR A CA    1 
ATOM   2172 C  C     . THR A 1 277 ? 11.688  -12.035 2.420   1.00 22.26  ?  277 THR A C     1 
ATOM   2173 O  O     . THR A 1 277 ? 10.735  -12.691 2.860   1.00 19.56  ?  277 THR A O     1 
ATOM   2174 C  CB    . THR A 1 277 ? 13.829  -13.264 1.821   1.00 23.15  ?  277 THR A CB    1 
ATOM   2175 O  OG1   . THR A 1 277 ? 14.509  -13.906 0.729   1.00 25.83  ?  277 THR A OG1   1 
ATOM   2176 C  CG2   . THR A 1 277 ? 13.480  -14.304 2.886   1.00 26.78  ?  277 THR A CG2   1 
ATOM   2177 N  N     . LEU A 1 278 ? 11.963  -10.812 2.870   1.00 22.92  ?  278 LEU A N     1 
ATOM   2178 C  CA    . LEU A 1 278 ? 11.104  -10.191 3.868   1.00 18.02  ?  278 LEU A CA    1 
ATOM   2179 C  C     . LEU A 1 278 ? 9.657   -10.175 3.402   1.00 21.38  ?  278 LEU A C     1 
ATOM   2180 O  O     . LEU A 1 278 ? 8.752   -10.588 4.142   1.00 18.27  ?  278 LEU A O     1 
ATOM   2181 C  CB    . LEU A 1 278 ? 11.591  -8.782  4.179   1.00 13.93  ?  278 LEU A CB    1 
ATOM   2182 C  CG    . LEU A 1 278 ? 12.923  -8.750  4.938   1.00 18.99  ?  278 LEU A CG    1 
ATOM   2183 C  CD1   . LEU A 1 278 ? 13.173  -7.360  5.501   1.00 22.11  ?  278 LEU A CD1   1 
ATOM   2184 C  CD2   . LEU A 1 278 ? 12.993  -9.789  6.037   1.00 16.31  ?  278 LEU A CD2   1 
ATOM   2185 N  N     . GLN A 1 279 ? 9.425   -9.738  2.158   1.00 18.62  ?  279 GLN A N     1 
ATOM   2186 C  CA    . GLN A 1 279 ? 8.070   -9.723  1.606   1.00 20.20  ?  279 GLN A CA    1 
ATOM   2187 C  C     . GLN A 1 279 ? 7.437   -11.120 1.589   1.00 25.12  ?  279 GLN A C     1 
ATOM   2188 O  O     . GLN A 1 279 ? 6.247   -11.265 1.899   1.00 23.86  ?  279 GLN A O     1 
ATOM   2189 C  CB    . GLN A 1 279 ? 8.082   -9.112  0.209   1.00 22.62  ?  279 GLN A CB    1 
ATOM   2190 C  CG    . GLN A 1 279 ? 8.527   -7.627  0.172   1.00 34.64  ?  279 GLN A CG    1 
ATOM   2191 C  CD    . GLN A 1 279 ? 9.320   -7.256  -1.097  1.00 40.68  ?  279 GLN A CD    1 
ATOM   2192 O  OE1   . GLN A 1 279 ? 9.828   -6.133  -1.230  1.00 42.67  ?  279 GLN A OE1   1 
ATOM   2193 N  NE2   . GLN A 1 279 ? 9.439   -8.208  -2.020  1.00 35.83  ?  279 GLN A NE2   1 
ATOM   2194 N  N     . VAL A 1 280 ? 8.209   -12.164 1.239   1.00 23.74  ?  280 VAL A N     1 
ATOM   2195 C  CA    . VAL A 1 280 ? 7.666   -13.529 1.261   1.00 19.81  ?  280 VAL A CA    1 
ATOM   2196 C  C     . VAL A 1 280 ? 7.280   -13.922 2.680   1.00 21.60  ?  280 VAL A C     1 
ATOM   2197 O  O     . VAL A 1 280 ? 6.222   -14.521 2.920   1.00 20.20  ?  280 VAL A O     1 
ATOM   2198 C  CB    . VAL A 1 280 ? 8.672   -14.539 0.672   1.00 20.16  ?  280 VAL A CB    1 
ATOM   2199 C  CG1   . VAL A 1 280 ? 8.244   -15.955 0.994   1.00 18.32  ?  280 VAL A CG1   1 
ATOM   2200 C  CG2   . VAL A 1 280 ? 8.824   -14.367 -0.854  1.00 25.53  ?  280 VAL A CG2   1 
ATOM   2201 N  N     . LEU A 1 281 ? 8.153   -13.620 3.639   1.00 18.93  ?  281 LEU A N     1 
ATOM   2202 C  CA    . LEU A 1 281 ? 7.901   -14.039 5.009   1.00 23.11  ?  281 LEU A CA    1 
ATOM   2203 C  C     . LEU A 1 281 ? 6.748   -13.249 5.620   1.00 19.37  ?  281 LEU A C     1 
ATOM   2204 O  O     . LEU A 1 281 ? 5.960   -13.794 6.404   1.00 16.84  ?  281 LEU A O     1 
ATOM   2205 C  CB    . LEU A 1 281 ? 9.169   -13.882 5.843   1.00 23.36  ?  281 LEU A CB    1 
ATOM   2206 C  CG    . LEU A 1 281 ? 10.429  -14.660 5.473   1.00 23.38  ?  281 LEU A CG    1 
ATOM   2207 C  CD1   . LEU A 1 281 ? 11.609  -14.098 6.264   1.00 25.67  ?  281 LEU A CD1   1 
ATOM   2208 C  CD2   . LEU A 1 281 ? 10.275  -16.142 5.733   1.00 18.91  ?  281 LEU A CD2   1 
ATOM   2209 N  N     . TYR A 1 282 ? 6.632   -11.965 5.266   1.00 19.22  ?  282 TYR A N     1 
ATOM   2210 C  CA    . TYR A 1 282 ? 5.506   -11.165 5.734   1.00 18.86  ?  282 TYR A CA    1 
ATOM   2211 C  C     . TYR A 1 282 ? 4.178   -11.747 5.253   1.00 23.61  ?  282 TYR A C     1 
ATOM   2212 O  O     . TYR A 1 282 ? 3.188   -11.750 5.994   1.00 21.34  ?  282 TYR A O     1 
ATOM   2213 C  CB    . TYR A 1 282 ? 5.659   -9.708  5.281   1.00 20.39  ?  282 TYR A CB    1 
ATOM   2214 C  CG    . TYR A 1 282 ? 4.605   -8.798  5.865   1.00 18.29  ?  282 TYR A CG    1 
ATOM   2215 C  CD1   . TYR A 1 282 ? 4.735   -8.288  7.155   1.00 18.77  ?  282 TYR A CD1   1 
ATOM   2216 C  CD2   . TYR A 1 282 ? 3.454   -8.482  5.144   1.00 18.92  ?  282 TYR A CD2   1 
ATOM   2217 C  CE1   . TYR A 1 282 ? 3.757   -7.463  7.703   1.00 18.93  ?  282 TYR A CE1   1 
ATOM   2218 C  CE2   . TYR A 1 282 ? 2.469   -7.663  5.686   1.00 17.63  ?  282 TYR A CE2   1 
ATOM   2219 C  CZ    . TYR A 1 282 ? 2.627   -7.164  6.961   1.00 20.89  ?  282 TYR A CZ    1 
ATOM   2220 O  OH    . TYR A 1 282 ? 1.650   -6.367  7.501   1.00 25.81  ?  282 TYR A OH    1 
ATOM   2221 N  N     . ARG A 1 283 ? 4.135   -12.264 4.022   1.00 23.09  ?  283 ARG A N     1 
ATOM   2222 C  CA    . ARG A 1 283 ? 2.910   -12.926 3.575   1.00 29.55  ?  283 ARG A CA    1 
ATOM   2223 C  C     . ARG A 1 283 ? 2.679   -14.229 4.331   1.00 27.41  ?  283 ARG A C     1 
ATOM   2224 O  O     . ARG A 1 283 ? 1.545   -14.534 4.728   1.00 26.71  ?  283 ARG A O     1 
ATOM   2225 C  CB    . ARG A 1 283 ? 2.952   -13.186 2.073   1.00 28.26  ?  283 ARG A CB    1 
ATOM   2226 C  CG    . ARG A 1 283 ? 2.457   -12.019 1.240   1.00 34.62  ?  283 ARG A CG    1 
ATOM   2227 C  CD    . ARG A 1 283 ? 2.100   -12.473 -0.172  1.00 48.64  ?  283 ARG A CD    1 
ATOM   2228 N  NE    . ARG A 1 283 ? 3.220   -13.122 -0.850  1.00 39.80  ?  283 ARG A NE    1 
ATOM   2229 C  CZ    . ARG A 1 283 ? 4.272   -12.479 -1.344  1.00 39.46  ?  283 ARG A CZ    1 
ATOM   2230 N  NH1   . ARG A 1 283 ? 4.384   -11.163 -1.253  1.00 37.18  ?  283 ARG A NH1   1 
ATOM   2231 N  NH2   . ARG A 1 283 ? 5.236   -13.174 -1.942  1.00 42.52  ?  283 ARG A NH2   1 
ATOM   2232 N  N     . ALA A 1 284 ? 3.740   -14.998 4.562   1.00 25.41  ?  284 ALA A N     1 
ATOM   2233 C  CA    . ALA A 1 284 ? 3.574   -16.270 5.247   1.00 27.69  ?  284 ALA A CA    1 
ATOM   2234 C  C     . ALA A 1 284 ? 3.115   -16.097 6.681   1.00 26.25  ?  284 ALA A C     1 
ATOM   2235 O  O     . ALA A 1 284 ? 2.753   -17.088 7.312   1.00 24.87  ?  284 ALA A O     1 
ATOM   2236 C  CB    . ALA A 1 284 ? 4.874   -17.074 5.228   1.00 18.47  ?  284 ALA A CB    1 
ATOM   2237 N  N     . LEU A 1 285 ? 3.128   -14.877 7.214   1.00 27.49  ?  285 LEU A N     1 
ATOM   2238 C  CA    . LEU A 1 285 ? 2.733   -14.643 8.595   1.00 26.06  ?  285 LEU A CA    1 
ATOM   2239 C  C     . LEU A 1 285 ? 1.293   -14.174 8.740   1.00 30.57  ?  285 LEU A C     1 
ATOM   2240 O  O     . LEU A 1 285 ? 0.848   -13.938 9.868   1.00 31.29  ?  285 LEU A O     1 
ATOM   2241 C  CB    . LEU A 1 285 ? 3.657   -13.613 9.240   1.00 22.98  ?  285 LEU A CB    1 
ATOM   2242 C  CG    . LEU A 1 285 ? 5.068   -14.082 9.559   1.00 22.14  ?  285 LEU A CG    1 
ATOM   2243 C  CD1   . LEU A 1 285 ? 5.951   -12.867 9.666   1.00 22.35  ?  285 LEU A CD1   1 
ATOM   2244 C  CD2   . LEU A 1 285 ? 5.107   -14.865 10.841  1.00 24.15  ?  285 LEU A CD2   1 
ATOM   2245 N  N     . GLY A 1 286 ? 0.553   -14.017 7.648   1.00 28.65  ?  286 GLY A N     1 
ATOM   2246 C  CA    . GLY A 1 286 ? -0.758  -13.423 7.805   1.00 39.08  ?  286 GLY A CA    1 
ATOM   2247 C  C     . GLY A 1 286 ? -1.885  -14.005 6.977   1.00 50.52  ?  286 GLY A C     1 
ATOM   2248 O  O     . GLY A 1 286 ? -1.839  -15.172 6.568   1.00 44.88  ?  286 GLY A O     1 
ATOM   2249 N  N     . ASP A 1 287 ? -2.937  -13.173 6.783   1.00 59.92  ?  287 ASP A N     1 
ATOM   2250 C  CA    . ASP A 1 287 ? -4.049  -13.293 5.837   1.00 55.46  ?  287 ASP A CA    1 
ATOM   2251 C  C     . ASP A 1 287 ? -4.597  -14.727 5.862   1.00 56.27  ?  287 ASP A C     1 
ATOM   2252 O  O     . ASP A 1 287 ? -4.996  -15.166 6.950   1.00 58.97  ?  287 ASP A O     1 
ATOM   2253 C  CB    . ASP A 1 287 ? -3.577  -12.790 4.468   1.00 65.32  ?  287 ASP A CB    1 
ATOM   2254 C  CG    . ASP A 1 287 ? -2.612  -11.620 4.567   1.00 59.04  ?  287 ASP A CG    1 
ATOM   2255 O  OD1   . ASP A 1 287 ? -2.994  -10.573 5.144   1.00 60.52  ?  287 ASP A OD1   1 
ATOM   2256 O  OD2   . ASP A 1 287 ? -1.485  -11.747 4.037   1.00 56.24  ?  287 ASP A OD2   1 
ATOM   2257 N  N     . PRO A 1 288 ? -4.687  -15.515 4.727   1.00 53.45  ?  288 PRO A N     1 
ATOM   2258 C  CA    . PRO A 1 288 ? -4.755  -16.970 4.923   1.00 50.68  ?  288 PRO A CA    1 
ATOM   2259 C  C     . PRO A 1 288 ? -3.377  -17.603 4.816   1.00 53.27  ?  288 PRO A C     1 
ATOM   2260 O  O     . PRO A 1 288 ? -2.604  -17.271 3.908   1.00 49.73  ?  288 PRO A O     1 
ATOM   2261 C  CB    . PRO A 1 288 ? -5.694  -17.455 3.804   1.00 58.33  ?  288 PRO A CB    1 
ATOM   2262 C  CG    . PRO A 1 288 ? -6.008  -16.264 2.958   1.00 50.50  ?  288 PRO A CG    1 
ATOM   2263 C  CD    . PRO A 1 288 ? -5.055  -15.192 3.330   1.00 55.28  ?  288 PRO A CD    1 
ATOM   2264 N  N     . GLN A 1 289 ? -3.063  -18.507 5.744   1.00 47.11  ?  289 GLN A N     1 
ATOM   2265 C  CA    . GLN A 1 289 ? -1.755  -19.141 5.838   1.00 43.37  ?  289 GLN A CA    1 
ATOM   2266 C  C     . GLN A 1 289 ? -1.440  -19.904 4.556   1.00 46.01  ?  289 GLN A C     1 
ATOM   2267 O  O     . GLN A 1 289 ? -2.067  -20.936 4.280   1.00 46.28  ?  289 GLN A O     1 
ATOM   2268 C  CB    . GLN A 1 289 ? -1.709  -20.077 7.049   1.00 39.25  ?  289 GLN A CB    1 
ATOM   2269 C  CG    . GLN A 1 289 ? -0.341  -20.188 7.694   1.00 45.23  ?  289 GLN A CG    1 
ATOM   2270 C  CD    . GLN A 1 289 ? -0.141  -21.488 8.450   1.00 45.64  ?  289 GLN A CD    1 
ATOM   2271 O  OE1   . GLN A 1 289 ? -0.680  -21.673 9.543   1.00 48.21  ?  289 GLN A OE1   1 
ATOM   2272 N  NE2   . GLN A 1 289 ? 0.648   -22.392 7.875   1.00 45.53  ?  289 GLN A NE2   1 
ATOM   2273 N  N     . PRO A 1 290 ? -0.492  -19.434 3.742   1.00 44.78  ?  290 PRO A N     1 
ATOM   2274 C  CA    . PRO A 1 290 ? -0.125  -20.198 2.547   1.00 39.74  ?  290 PRO A CA    1 
ATOM   2275 C  C     . PRO A 1 290 ? 0.465   -21.550 2.927   1.00 40.42  ?  290 PRO A C     1 
ATOM   2276 O  O     . PRO A 1 290 ? 0.856   -21.793 4.074   1.00 40.05  ?  290 PRO A O     1 
ATOM   2277 C  CB    . PRO A 1 290 ? 0.908   -19.305 1.840   1.00 39.12  ?  290 PRO A CB    1 
ATOM   2278 C  CG    . PRO A 1 290 ? 1.380   -18.330 2.854   1.00 35.87  ?  290 PRO A CG    1 
ATOM   2279 C  CD    . PRO A 1 290 ? 0.276   -18.179 3.869   1.00 39.28  ?  290 PRO A CD    1 
ATOM   2280 N  N     . SER A 1 291 ? 0.498   -22.448 1.946   1.00 40.91  ?  291 SER A N     1 
ATOM   2281 C  CA    . SER A 1 291 ? 1.101   -23.755 2.158   1.00 40.32  ?  291 SER A CA    1 
ATOM   2282 C  C     . SER A 1 291 ? 2.621   -23.621 2.214   1.00 35.36  ?  291 SER A C     1 
ATOM   2283 O  O     . SER A 1 291 ? 3.187   -22.668 1.673   1.00 36.94  ?  291 SER A O     1 
ATOM   2284 C  CB    . SER A 1 291 ? 0.707   -24.723 1.044   1.00 36.17  ?  291 SER A CB    1 
ATOM   2285 O  OG    . SER A 1 291 ? 0.973   -24.166 -0.234  1.00 38.22  ?  291 SER A OG    1 
ATOM   2286 N  N     . PRO A 1 292 ? 3.302   -24.553 2.884   1.00 29.24  ?  292 PRO A N     1 
ATOM   2287 C  CA    . PRO A 1 292 ? 4.767   -24.462 2.964   1.00 32.07  ?  292 PRO A CA    1 
ATOM   2288 C  C     . PRO A 1 292 ? 5.464   -24.634 1.626   1.00 34.65  ?  292 PRO A C     1 
ATOM   2289 O  O     . PRO A 1 292 ? 6.578   -24.124 1.458   1.00 31.93  ?  292 PRO A O     1 
ATOM   2290 C  CB    . PRO A 1 292 ? 5.141   -25.588 3.938   1.00 32.55  ?  292 PRO A CB    1 
ATOM   2291 C  CG    . PRO A 1 292 ? 3.876   -25.902 4.677   1.00 40.46  ?  292 PRO A CG    1 
ATOM   2292 C  CD    . PRO A 1 292 ? 2.760   -25.630 3.727   1.00 36.68  ?  292 PRO A CD    1 
ATOM   2293 N  N     . ALA A 1 293 ? 4.862   -25.354 0.678   1.00 34.81  ?  293 ALA A N     1 
ATOM   2294 C  CA    . ALA A 1 293 ? 5.492   -25.514 -0.625  1.00 37.92  ?  293 ALA A CA    1 
ATOM   2295 C  C     . ALA A 1 293 ? 5.311   -24.272 -1.483  1.00 38.16  ?  293 ALA A C     1 
ATOM   2296 O  O     . ALA A 1 293 ? 6.182   -23.953 -2.298  1.00 38.70  ?  293 ALA A O     1 
ATOM   2297 C  CB    . ALA A 1 293 ? 4.936   -26.746 -1.345  1.00 37.49  ?  293 ALA A CB    1 
ATOM   2298 N  N     . GLN A 1 294 ? 4.193   -23.566 -1.315  1.00 35.55  ?  294 GLN A N     1 
ATOM   2299 C  CA    . GLN A 1 294 ? 4.020   -22.289 -1.992  1.00 34.81  ?  294 GLN A CA    1 
ATOM   2300 C  C     . GLN A 1 294 ? 5.051   -21.277 -1.513  1.00 36.17  ?  294 GLN A C     1 
ATOM   2301 O  O     . GLN A 1 294 ? 5.614   -20.522 -2.315  1.00 40.54  ?  294 GLN A O     1 
ATOM   2302 C  CB    . GLN A 1 294 ? 2.605   -21.762 -1.755  1.00 36.31  ?  294 GLN A CB    1 
ATOM   2303 C  CG    . GLN A 1 294 ? 2.297   -20.475 -2.488  1.00 42.66  ?  294 GLN A CG    1 
ATOM   2304 C  CD    . GLN A 1 294 ? 0.851   -20.383 -2.911  1.00 50.39  ?  294 GLN A CD    1 
ATOM   2305 O  OE1   . GLN A 1 294 ? 0.063   -19.643 -2.312  1.00 55.04  ?  294 GLN A OE1   1 
ATOM   2306 N  NE2   . GLN A 1 294 ? 0.481   -21.147 -3.940  1.00 50.30  ?  294 GLN A NE2   1 
ATOM   2307 N  N     . VAL A 1 295 ? 5.306   -21.242 -0.203  1.00 34.77  ?  295 VAL A N     1 
ATOM   2308 C  CA    . VAL A 1 295 ? 6.260   -20.285 0.345   1.00 36.14  ?  295 VAL A CA    1 
ATOM   2309 C  C     . VAL A 1 295 ? 7.674   -20.639 -0.094  1.00 37.14  ?  295 VAL A C     1 
ATOM   2310 O  O     . VAL A 1 295 ? 8.466   -19.754 -0.449  1.00 28.06  ?  295 VAL A O     1 
ATOM   2311 C  CB    . VAL A 1 295 ? 6.131   -20.224 1.877   1.00 34.76  ?  295 VAL A CB    1 
ATOM   2312 C  CG1   . VAL A 1 295 ? 7.207   -19.329 2.476   1.00 26.01  ?  295 VAL A CG1   1 
ATOM   2313 C  CG2   . VAL A 1 295 ? 4.738   -19.735 2.266   1.00 34.48  ?  295 VAL A CG2   1 
ATOM   2314 N  N     . GLU A 1 296 ? 8.009   -21.934 -0.090  1.00 33.56  ?  296 GLU A N     1 
ATOM   2315 C  CA    . GLU A 1 296 ? 9.323   -22.356 -0.569  1.00 37.18  ?  296 GLU A CA    1 
ATOM   2316 C  C     . GLU A 1 296 ? 9.533   -21.952 -2.024  1.00 33.68  ?  296 GLU A C     1 
ATOM   2317 O  O     . GLU A 1 296 ? 10.647  -21.577 -2.403  1.00 32.94  ?  296 GLU A O     1 
ATOM   2318 C  CB    . GLU A 1 296 ? 9.500   -23.868 -0.385  1.00 39.81  ?  296 GLU A CB    1 
ATOM   2319 C  CG    . GLU A 1 296 ? 10.849  -24.413 -0.884  1.00 48.93  ?  296 GLU A CG    1 
ATOM   2320 C  CD    . GLU A 1 296 ? 10.890  -25.942 -0.960  1.00 50.93  ?  296 GLU A CD    1 
ATOM   2321 O  OE1   . GLU A 1 296 ? 11.875  -26.546 -0.468  1.00 47.38  ?  296 GLU A OE1   1 
ATOM   2322 O  OE2   . GLU A 1 296 ? 9.930   -26.537 -1.505  1.00 45.42  ?  296 GLU A OE2   1 
ATOM   2323 N  N     . ASP A 1 297 ? 8.465   -21.970 -2.832  1.00 34.84  ?  297 ASP A N     1 
ATOM   2324 C  CA    . ASP A 1 297 ? 8.548   -21.511 -4.219  1.00 37.07  ?  297 ASP A CA    1 
ATOM   2325 C  C     . ASP A 1 297 ? 8.731   -19.996 -4.300  1.00 31.46  ?  297 ASP A C     1 
ATOM   2326 O  O     . ASP A 1 297 ? 9.474   -19.494 -5.148  1.00 31.96  ?  297 ASP A O     1 
ATOM   2327 C  CB    . ASP A 1 297 ? 7.288   -21.932 -4.981  1.00 40.20  ?  297 ASP A CB    1 
ATOM   2328 C  CG    . ASP A 1 297 ? 7.299   -23.409 -5.400  1.00 46.99  ?  297 ASP A CG    1 
ATOM   2329 O  OD1   . ASP A 1 297 ? 8.291   -24.135 -5.125  1.00 48.40  ?  297 ASP A OD1   1 
ATOM   2330 O  OD2   . ASP A 1 297 ? 6.291   -23.842 -6.005  1.00 49.12  ?  297 ASP A OD2   1 
ATOM   2331 N  N     . GLU A 1 298 ? 8.058   -19.248 -3.432  1.00 35.18  ?  298 GLU A N     1 
ATOM   2332 C  CA    . GLU A 1 298 ? 8.200   -17.796 -3.471  1.00 33.82  ?  298 GLU A CA    1 
ATOM   2333 C  C     . GLU A 1 298 ? 9.587   -17.359 -3.019  1.00 31.98  ?  298 GLU A C     1 
ATOM   2334 O  O     . GLU A 1 298 ? 10.137  -16.386 -3.553  1.00 29.53  ?  298 GLU A O     1 
ATOM   2335 C  CB    . GLU A 1 298 ? 7.124   -17.142 -2.616  1.00 29.70  ?  298 GLU A CB    1 
ATOM   2336 C  CG    . GLU A 1 298 ? 5.844   -16.872 -3.375  1.00 32.10  ?  298 GLU A CG    1 
ATOM   2337 C  CD    . GLU A 1 298 ? 4.673   -16.631 -2.444  1.00 42.33  ?  298 GLU A CD    1 
ATOM   2338 O  OE1   . GLU A 1 298 ? 4.610   -15.545 -1.816  1.00 40.89  ?  298 GLU A OE1   1 
ATOM   2339 O  OE2   . GLU A 1 298 ? 3.821   -17.533 -2.336  1.00 37.22  ?  298 GLU A OE2   1 
ATOM   2340 N  N     . LEU A 1 299 ? 10.166  -18.056 -2.034  1.00 29.14  ?  299 LEU A N     1 
ATOM   2341 C  CA    . LEU A 1 299 ? 11.560  -17.801 -1.679  1.00 29.91  ?  299 LEU A CA    1 
ATOM   2342 C  C     . LEU A 1 299 ? 12.465  -18.002 -2.885  1.00 35.00  ?  299 LEU A C     1 
ATOM   2343 O  O     . LEU A 1 299 ? 13.384  -17.206 -3.125  1.00 31.73  ?  299 LEU A O     1 
ATOM   2344 C  CB    . LEU A 1 299 ? 11.994  -18.715 -0.536  1.00 27.87  ?  299 LEU A CB    1 
ATOM   2345 C  CG    . LEU A 1 299 ? 11.292  -18.464 0.799   1.00 30.32  ?  299 LEU A CG    1 
ATOM   2346 C  CD1   . LEU A 1 299 ? 11.639  -19.564 1.797   1.00 25.36  ?  299 LEU A CD1   1 
ATOM   2347 C  CD2   . LEU A 1 299 ? 11.651  -17.096 1.352   1.00 28.27  ?  299 LEU A CD2   1 
ATOM   2348 N  N     . ARG A 1 300 ? 12.205  -19.058 -3.664  1.00 32.08  ?  300 ARG A N     1 
ATOM   2349 C  CA    . ARG A 1 300 ? 12.970  -19.296 -4.881  1.00 33.63  ?  300 ARG A CA    1 
ATOM   2350 C  C     . ARG A 1 300 ? 12.881  -18.104 -5.823  1.00 33.80  ?  300 ARG A C     1 
ATOM   2351 O  O     . ARG A 1 300 ? 13.908  -17.574 -6.263  1.00 35.29  ?  300 ARG A O     1 
ATOM   2352 C  CB    . ARG A 1 300 ? 12.486  -20.574 -5.566  1.00 44.92  ?  300 ARG A CB    1 
ATOM   2353 C  CG    . ARG A 1 300 ? 13.213  -21.833 -5.109  1.00 43.14  ?  300 ARG A CG    1 
ATOM   2354 C  CD    . ARG A 1 300 ? 12.706  -23.064 -5.845  1.00 51.26  ?  300 ARG A CD    1 
ATOM   2355 N  NE    . ARG A 1 300 ? 12.835  -24.280 -5.048  1.00 51.38  ?  300 ARG A NE    1 
ATOM   2356 C  CZ    . ARG A 1 300 ? 13.984  -24.884 -4.768  1.00 56.65  ?  300 ARG A CZ    1 
ATOM   2357 N  NH1   . ARG A 1 300 ? 15.142  -24.419 -5.217  1.00 38.37  ?  300 ARG A NH1   1 
ATOM   2358 N  NH2   . ARG A 1 300 ? 13.973  -25.983 -4.017  1.00 63.93  ?  300 ARG A NH2   1 
ATOM   2359 N  N     . ALA A 1 301 ? 11.657  -17.655 -6.131  1.00 29.02  ?  301 ALA A N     1 
ATOM   2360 C  CA    . ALA A 1 301 ? 11.509  -16.492 -6.999  1.00 32.18  ?  301 ALA A CA    1 
ATOM   2361 C  C     . ALA A 1 301 ? 12.124  -15.254 -6.376  1.00 35.58  ?  301 ALA A C     1 
ATOM   2362 O  O     . ALA A 1 301 ? 12.566  -14.357 -7.098  1.00 42.52  ?  301 ALA A O     1 
ATOM   2363 C  CB    . ALA A 1 301 ? 10.038  -16.229 -7.321  1.00 29.29  ?  301 ALA A CB    1 
ATOM   2364 N  N     . ALA A 1 302 ? 12.172  -15.185 -5.043  1.00 31.51  ?  302 ALA A N     1 
ATOM   2365 C  CA    . ALA A 1 302 ? 12.728  -14.005 -4.385  1.00 32.69  ?  302 ALA A CA    1 
ATOM   2366 C  C     . ALA A 1 302 ? 14.249  -13.975 -4.491  1.00 34.57  ?  302 ALA A C     1 
ATOM   2367 O  O     . ALA A 1 302 ? 14.848  -12.902 -4.642  1.00 30.55  ?  302 ALA A O     1 
ATOM   2368 C  CB    . ALA A 1 302 ? 12.286  -13.965 -2.919  1.00 31.88  ?  302 ALA A CB    1 
ATOM   2369 N  N     . LEU A 1 303 ? 14.888  -15.142 -4.420  1.00 33.58  ?  303 LEU A N     1 
ATOM   2370 C  CA    . LEU A 1 303 ? 16.338  -15.242 -4.509  1.00 33.25  ?  303 LEU A CA    1 
ATOM   2371 C  C     . LEU A 1 303 ? 16.858  -15.170 -5.943  1.00 40.39  ?  303 LEU A C     1 
ATOM   2372 O  O     . LEU A 1 303 ? 18.065  -14.971 -6.137  1.00 35.33  ?  303 LEU A O     1 
ATOM   2373 C  CB    . LEU A 1 303 ? 16.803  -16.544 -3.845  1.00 30.15  ?  303 LEU A CB    1 
ATOM   2374 C  CG    . LEU A 1 303 ? 17.423  -16.292 -2.470  1.00 30.98  ?  303 LEU A CG    1 
ATOM   2375 C  CD1   . LEU A 1 303 ? 16.377  -15.670 -1.537  1.00 29.33  ?  303 LEU A CD1   1 
ATOM   2376 C  CD2   . LEU A 1 303 ? 17.992  -17.560 -1.874  1.00 27.30  ?  303 LEU A CD2   1 
ATOM   2377 N  N     . GLU A 1 304 ? 15.978  -15.306 -6.940  1.00 37.65  ?  304 GLU A N     1 
ATOM   2378 C  CA    . GLU A 1 304 ? 16.360  -15.298 -8.346  1.00 44.03  ?  304 GLU A CA    1 
ATOM   2379 C  C     . GLU A 1 304 ? 16.400  -13.894 -8.938  1.00 45.51  ?  304 GLU A C     1 
ATOM   2380 O  O     . GLU A 1 304 ? 17.339  -13.553 -9.664  1.00 52.58  ?  304 GLU A O     1 
ATOM   2381 C  CB    . GLU A 1 304 ? 15.394  -16.172 -9.146  1.00 48.18  ?  304 GLU A CB    1 
ATOM   2382 C  CG    . GLU A 1 304 ? 15.617  -17.663 -8.921  1.00 52.60  ?  304 GLU A CG    1 
ATOM   2383 C  CD    . GLU A 1 304 ? 14.701  -18.530 -9.764  1.00 63.41  ?  304 GLU A CD    1 
ATOM   2384 O  OE1   . GLU A 1 304 ? 14.578  -18.263 -10.983 1.00 62.66  ?  304 GLU A OE1   1 
ATOM   2385 O  OE2   . GLU A 1 304 ? 14.092  -19.469 -9.199  1.00 64.50  ?  304 GLU A OE2   1 
ATOM   2386 N  N     . GLY A 1 305 ? 15.402  -13.073 -8.639  1.00 49.00  ?  305 GLY A N     1 
ATOM   2387 C  CA    . GLY A 1 305 ? 15.360  -11.705 -9.117  1.00 52.17  ?  305 GLY A CA    1 
ATOM   2388 C  C     . GLY A 1 305 ? 13.934  -11.239 -9.323  1.00 59.12  ?  305 GLY A C     1 
ATOM   2389 O  O     . GLY A 1 305 ? 13.627  -10.044 -9.210  1.00 51.66  ?  305 GLY A O     1 
ATOM   2390 N  N     . ARG A 1 306 ? 13.058  -12.197 -9.621  1.00 58.83  ?  306 ARG A N     1 
ATOM   2391 C  CA    . ARG A 1 306 ? 11.642  -11.946 -9.865  1.00 57.66  ?  306 ARG A CA    1 
ATOM   2392 C  C     . ARG A 1 306 ? 10.930  -11.433 -8.607  1.00 58.45  ?  306 ARG A C     1 
ATOM   2393 O  O     . ARG A 1 306 ? 11.159  -11.928 -7.498  1.00 53.98  ?  306 ARG A O     1 
ATOM   2394 C  CB    . ARG A 1 306 ? 10.968  -13.228 -10.374 1.00 58.39  ?  306 ARG A CB    1 
ATOM   2395 C  CG    . ARG A 1 306 ? 11.881  -14.124 -11.212 1.00 56.20  ?  306 ARG A CG    1 
ATOM   2396 C  CD    . ARG A 1 306 ? 11.091  -14.935 -12.232 1.00 69.97  ?  306 ARG A CD    1 
ATOM   2397 N  NE    . ARG A 1 306 ? 11.959  -15.720 -13.104 1.00 80.72  ?  306 ARG A NE    1 
ATOM   2398 C  CZ    . ARG A 1 306 ? 11.530  -16.575 -14.026 1.00 80.18  ?  306 ARG A CZ    1 
ATOM   2399 N  NH1   . ARG A 1 306 ? 10.239  -16.795 -14.219 1.00 77.44  ?  306 ARG A NH1   1 
ATOM   2400 N  NH2   . ARG A 1 306 ? 12.419  -17.232 -14.768 1.00 75.59  ?  306 ARG A NH2   1 
ATOM   2401 N  N     . MET B 1 1   ? 15.334  22.377  -41.930 1.00 21.27  ?  1   MET B N     1 
ATOM   2402 C  CA    . MET B 1 1   ? 15.629  21.225  -42.776 1.00 22.08  ?  1   MET B CA    1 
ATOM   2403 C  C     . MET B 1 1   ? 15.786  19.930  -41.997 1.00 12.69  ?  1   MET B C     1 
ATOM   2404 O  O     . MET B 1 1   ? 15.170  18.939  -42.365 1.00 15.13  ?  1   MET B O     1 
ATOM   2405 C  CB    . MET B 1 1   ? 16.879  21.456  -43.624 1.00 22.58  ?  1   MET B CB    1 
ATOM   2406 C  CG    . MET B 1 1   ? 16.524  21.648  -45.079 1.00 31.07  ?  1   MET B CG    1 
ATOM   2407 S  SD    . MET B 1 1   ? 17.917  22.084  -46.111 1.00 54.28  ?  1   MET B SD    1 
ATOM   2408 C  CE    . MET B 1 1   ? 18.353  20.447  -46.725 1.00 36.44  ?  1   MET B CE    1 
ATOM   2409 N  N     . LEU B 1 2   ? 16.601  19.937  -40.937 1.00 11.08  ?  2   LEU B N     1 
ATOM   2410 C  CA    . LEU B 1 2   ? 16.806  18.725  -40.150 1.00 12.81  ?  2   LEU B CA    1 
ATOM   2411 C  C     . LEU B 1 2   ? 15.647  18.462  -39.180 1.00 16.09  ?  2   LEU B C     1 
ATOM   2412 O  O     . LEU B 1 2   ? 15.099  17.351  -39.168 1.00 15.79  ?  2   LEU B O     1 
ATOM   2413 C  CB    . LEU B 1 2   ? 18.145  18.787  -39.399 1.00 15.82  ?  2   LEU B CB    1 
ATOM   2414 C  CG    . LEU B 1 2   ? 18.690  17.446  -38.860 1.00 22.12  ?  2   LEU B CG    1 
ATOM   2415 C  CD1   . LEU B 1 2   ? 18.509  16.289  -39.844 1.00 18.97  ?  2   LEU B CD1   1 
ATOM   2416 C  CD2   . LEU B 1 2   ? 20.145  17.552  -38.451 1.00 20.75  ?  2   LEU B CD2   1 
ATOM   2417 N  N     . VAL B 1 3   ? 15.249  19.450  -38.364 1.00 10.33  ?  3   VAL B N     1 
ATOM   2418 C  CA    . VAL B 1 3   ? 14.252  19.224  -37.298 1.00 18.00  ?  3   VAL B CA    1 
ATOM   2419 C  C     . VAL B 1 3   ? 13.208  20.335  -37.290 1.00 13.43  ?  3   VAL B C     1 
ATOM   2420 O  O     . VAL B 1 3   ? 13.548  21.517  -37.284 1.00 13.83  ?  3   VAL B O     1 
ATOM   2421 C  CB    . VAL B 1 3   ? 14.883  19.117  -35.892 1.00 16.91  ?  3   VAL B CB    1 
ATOM   2422 C  CG1   . VAL B 1 3   ? 13.802  19.115  -34.806 1.00 13.43  ?  3   VAL B CG1   1 
ATOM   2423 C  CG2   . VAL B 1 3   ? 15.718  17.856  -35.769 1.00 18.55  ?  3   VAL B CG2   1 
ATOM   2424 N  N     . SER B 1 4   ? 11.940  19.944  -37.276 1.00 16.54  ?  4   SER B N     1 
ATOM   2425 C  CA    . SER B 1 4   ? 10.808  20.839  -37.099 1.00 16.85  ?  4   SER B CA    1 
ATOM   2426 C  C     . SER B 1 4   ? 10.161  20.539  -35.750 1.00 13.88  ?  4   SER B C     1 
ATOM   2427 O  O     . SER B 1 4   ? 9.790   19.395  -35.490 1.00 14.97  ?  4   SER B O     1 
ATOM   2428 C  CB    . SER B 1 4   ? 9.800   20.645  -38.230 1.00 16.76  ?  4   SER B CB    1 
ATOM   2429 O  OG    . SER B 1 4   ? 10.275  21.243  -39.418 1.00 13.95  ?  4   SER B OG    1 
ATOM   2430 N  N     . VAL B 1 5   ? 10.046  21.555  -34.888 1.00 17.39  ?  5   VAL B N     1 
ATOM   2431 C  CA    . VAL B 1 5   ? 9.390   21.422  -33.585 1.00 16.88  ?  5   VAL B CA    1 
ATOM   2432 C  C     . VAL B 1 5   ? 7.989   22.012  -33.681 1.00 14.85  ?  5   VAL B C     1 
ATOM   2433 O  O     . VAL B 1 5   ? 7.804   23.120  -34.193 1.00 15.35  ?  5   VAL B O     1 
ATOM   2434 C  CB    . VAL B 1 5   ? 10.186  22.112  -32.465 1.00 14.20  ?  5   VAL B CB    1 
ATOM   2435 C  CG1   . VAL B 1 5   ? 9.453   21.943  -31.148 1.00 9.87   ?  5   VAL B CG1   1 
ATOM   2436 C  CG2   . VAL B 1 5   ? 11.584  21.555  -32.370 1.00 8.86   ?  5   VAL B CG2   1 
ATOM   2437 N  N     . ILE B 1 6   ? 7.004   21.287  -33.180 1.00 10.07  ?  6   ILE B N     1 
ATOM   2438 C  CA    . ILE B 1 6   ? 5.610   21.624  -33.408 1.00 12.62  ?  6   ILE B CA    1 
ATOM   2439 C  C     . ILE B 1 6   ? 4.936   21.756  -32.051 1.00 13.68  ?  6   ILE B C     1 
ATOM   2440 O  O     . ILE B 1 6   ? 4.830   20.775  -31.311 1.00 11.91  ?  6   ILE B O     1 
ATOM   2441 C  CB    . ILE B 1 6   ? 4.932   20.578  -34.294 1.00 13.27  ?  6   ILE B CB    1 
ATOM   2442 C  CG1   . ILE B 1 6   ? 5.665   20.574  -35.651 1.00 16.45  ?  6   ILE B CG1   1 
ATOM   2443 C  CG2   . ILE B 1 6   ? 3.452   20.847  -34.431 1.00 13.00  ?  6   ILE B CG2   1 
ATOM   2444 C  CD1   . ILE B 1 6   ? 4.876   20.053  -36.788 1.00 19.38  ?  6   ILE B CD1   1 
ATOM   2445 N  N     . ILE B 1 7   ? 4.530   22.975  -31.705 1.00 10.42  ?  7   ILE B N     1 
ATOM   2446 C  CA    . ILE B 1 7   ? 3.830   23.281  -30.463 1.00 13.31  ?  7   ILE B CA    1 
ATOM   2447 C  C     . ILE B 1 7   ? 2.413   23.704  -30.821 1.00 11.45  ?  7   ILE B C     1 
ATOM   2448 O  O     . ILE B 1 7   ? 2.215   24.813  -31.337 1.00 10.19  ?  7   ILE B O     1 
ATOM   2449 C  CB    . ILE B 1 7   ? 4.522   24.380  -29.646 1.00 12.46  ?  7   ILE B CB    1 
ATOM   2450 C  CG1   . ILE B 1 7   ? 6.015   24.110  -29.509 1.00 19.47  ?  7   ILE B CG1   1 
ATOM   2451 C  CG2   . ILE B 1 7   ? 3.942   24.405  -28.244 1.00 19.21  ?  7   ILE B CG2   1 
ATOM   2452 C  CD1   . ILE B 1 7   ? 6.687   25.118  -28.564 1.00 17.17  ?  7   ILE B CD1   1 
ATOM   2453 N  N     . PRO B 1 8   ? 1.407   22.860  -30.597 1.00 12.14  ?  8   PRO B N     1 
ATOM   2454 C  CA    . PRO B 1 8   ? 0.035   23.357  -30.520 1.00 16.38  ?  8   PRO B CA    1 
ATOM   2455 C  C     . PRO B 1 8   ? -0.139  24.094  -29.204 1.00 14.98  ?  8   PRO B C     1 
ATOM   2456 O  O     . PRO B 1 8   ? 0.502   23.768  -28.203 1.00 16.83  ?  8   PRO B O     1 
ATOM   2457 C  CB    . PRO B 1 8   ? -0.810  22.083  -30.572 1.00 19.37  ?  8   PRO B CB    1 
ATOM   2458 C  CG    . PRO B 1 8   ? 0.067   21.037  -29.914 1.00 18.28  ?  8   PRO B CG    1 
ATOM   2459 C  CD    . PRO B 1 8   ? 1.508   21.428  -30.258 1.00 12.27  ?  8   PRO B CD    1 
ATOM   2460 N  N     . THR B 1 9   ? -0.969  25.131  -29.211 1.00 15.30  ?  9   THR B N     1 
ATOM   2461 C  CA    . THR B 1 9   ? -1.115  25.904  -27.982 1.00 15.94  ?  9   THR B CA    1 
ATOM   2462 C  C     . THR B 1 9   ? -2.489  26.551  -27.938 1.00 18.41  ?  9   THR B C     1 
ATOM   2463 O  O     . THR B 1 9   ? -3.055  26.930  -28.970 1.00 14.41  ?  9   THR B O     1 
ATOM   2464 C  CB    . THR B 1 9   ? -0.002  26.955  -27.823 1.00 16.36  ?  9   THR B CB    1 
ATOM   2465 O  OG1   . THR B 1 9   ? 0.011   27.441  -26.472 1.00 16.80  ?  9   THR B OG1   1 
ATOM   2466 C  CG2   . THR B 1 9   ? -0.175  28.130  -28.802 1.00 14.26  ?  9   THR B CG2   1 
ATOM   2467 N  N     . TYR B 1 10  ? -3.023  26.660  -26.714 1.00 16.97  ?  10  TYR B N     1 
ATOM   2468 C  CA    . TYR B 1 10  ? -4.412  27.068  -26.525 1.00 16.26  ?  10  TYR B CA    1 
ATOM   2469 C  C     . TYR B 1 10  ? -4.557  27.626  -25.108 1.00 15.48  ?  10  TYR B C     1 
ATOM   2470 O  O     . TYR B 1 10  ? -4.659  26.858  -24.150 1.00 17.31  ?  10  TYR B O     1 
ATOM   2471 C  CB    . TYR B 1 10  ? -5.347  25.897  -26.769 1.00 17.32  ?  10  TYR B CB    1 
ATOM   2472 C  CG    . TYR B 1 10  ? -6.797  26.274  -26.712 1.00 20.77  ?  10  TYR B CG    1 
ATOM   2473 C  CD1   . TYR B 1 10  ? -7.326  27.217  -27.591 1.00 19.56  ?  10  TYR B CD1   1 
ATOM   2474 C  CD2   . TYR B 1 10  ? -7.647  25.696  -25.765 1.00 19.78  ?  10  TYR B CD2   1 
ATOM   2475 C  CE1   . TYR B 1 10  ? -8.669  27.572  -27.538 1.00 18.58  ?  10  TYR B CE1   1 
ATOM   2476 C  CE2   . TYR B 1 10  ? -8.973  26.041  -25.702 1.00 18.48  ?  10  TYR B CE2   1 
ATOM   2477 C  CZ    . TYR B 1 10  ? -9.485  26.979  -26.584 1.00 24.52  ?  10  TYR B CZ    1 
ATOM   2478 O  OH    . TYR B 1 10  ? -10.820 27.319  -26.507 1.00 29.43  ?  10  TYR B OH    1 
ATOM   2479 N  N     . ASN B 1 11  ? -4.538  28.957  -24.991 1.00 10.89  ?  11  ASN B N     1 
ATOM   2480 C  CA    . ASN B 1 11  ? -4.798  29.688  -23.740 1.00 19.81  ?  11  ASN B CA    1 
ATOM   2481 C  C     . ASN B 1 11  ? -3.746  29.397  -22.679 1.00 19.15  ?  11  ASN B C     1 
ATOM   2482 O  O     . ASN B 1 11  ? -4.043  29.401  -21.480 1.00 10.45  ?  11  ASN B O     1 
ATOM   2483 C  CB    . ASN B 1 11  ? -6.205  29.408  -23.187 1.00 10.52  ?  11  ASN B CB    1 
ATOM   2484 C  CG    . ASN B 1 11  ? -7.286  29.993  -24.066 1.00 11.43  ?  11  ASN B CG    1 
ATOM   2485 O  OD1   . ASN B 1 11  ? -7.162  31.120  -24.527 1.00 17.61  ?  11  ASN B OD1   1 
ATOM   2486 N  ND2   . ASN B 1 11  ? -8.333  29.228  -24.331 1.00 9.21   ?  11  ASN B ND2   1 
ATOM   2487 N  N     . ARG B 1 12  ? -2.509  29.137  -23.115 1.00 14.16  ?  12  ARG B N     1 
ATOM   2488 C  CA    . ARG B 1 12  ? -1.396  28.898  -22.195 1.00 16.63  ?  12  ARG B CA    1 
ATOM   2489 C  C     . ARG B 1 12  ? -0.161  29.719  -22.554 1.00 22.31  ?  12  ARG B C     1 
ATOM   2490 O  O     . ARG B 1 12  ? 0.952   29.194  -22.585 1.00 21.05  ?  12  ARG B O     1 
ATOM   2491 C  CB    . ARG B 1 12  ? -1.054  27.413  -22.153 1.00 19.95  ?  12  ARG B CB    1 
ATOM   2492 C  CG    . ARG B 1 12  ? -2.210  26.523  -21.732 1.00 22.59  ?  12  ARG B CG    1 
ATOM   2493 C  CD    . ARG B 1 12  ? -1.749  25.085  -21.699 1.00 21.19  ?  12  ARG B CD    1 
ATOM   2494 N  NE    . ARG B 1 12  ? -2.793  24.183  -21.251 1.00 21.91  ?  12  ARG B NE    1 
ATOM   2495 C  CZ    . ARG B 1 12  ? -2.759  22.871  -21.432 1.00 23.17  ?  12  ARG B CZ    1 
ATOM   2496 N  NH1   . ARG B 1 12  ? -1.777  22.296  -22.110 1.00 12.71  ?  12  ARG B NH1   1 
ATOM   2497 N  NH2   . ARG B 1 12  ? -3.717  22.116  -20.896 1.00 20.77  ?  12  ARG B NH2   1 
ATOM   2498 N  N     . PRO B 1 13  ? -0.313  31.031  -22.787 1.00 22.26  ?  13  PRO B N     1 
ATOM   2499 C  CA    . PRO B 1 13  ? 0.839   31.804  -23.284 1.00 18.14  ?  13  PRO B CA    1 
ATOM   2500 C  C     . PRO B 1 13  ? 2.013   31.752  -22.331 1.00 19.24  ?  13  PRO B C     1 
ATOM   2501 O  O     . PRO B 1 13  ? 3.174   31.806  -22.750 1.00 21.92  ?  13  PRO B O     1 
ATOM   2502 C  CB    . PRO B 1 13  ? 0.275   33.227  -23.409 1.00 18.96  ?  13  PRO B CB    1 
ATOM   2503 C  CG    . PRO B 1 13  ? -0.760  33.284  -22.268 1.00 17.97  ?  13  PRO B CG    1 
ATOM   2504 C  CD    . PRO B 1 13  ? -1.395  31.908  -22.292 1.00 16.63  ?  13  PRO B CD    1 
ATOM   2505 N  N     . GLU B 1 14  ? 1.770   31.664  -21.044 1.00 15.53  ?  14  GLU B N     1 
ATOM   2506 C  CA    . GLU B 1 14  ? 2.895   31.669  -20.086 1.00 22.08  ?  14  GLU B CA    1 
ATOM   2507 C  C     . GLU B 1 14  ? 3.598   30.300  -20.092 1.00 23.66  ?  14  GLU B C     1 
ATOM   2508 O  O     . GLU B 1 14  ? 4.804   30.290  -20.083 1.00 23.17  ?  14  GLU B O     1 
ATOM   2509 C  CB    . GLU B 1 14  ? 2.460   32.371  -18.790 1.00 26.59  ?  14  GLU B CB    1 
ATOM   2510 C  CG    . GLU B 1 14  ? 2.061   33.838  -19.047 1.00 28.07  ?  14  GLU B CG    1 
ATOM   2511 C  CD    . GLU B 1 14  ? 1.095   34.615  -18.154 1.00 16.54  ?  14  GLU B CD    1 
ATOM   2512 O  OE1   . GLU B 1 14  ? 0.339   35.514  -18.665 1.00 11.21  ?  14  GLU B OE1   1 
ATOM   2513 O  OE2   . GLU B 1 14  ? 1.139   34.372  -16.950 1.00 32.65  ?  14  GLU B OE2   1 
ATOM   2514 N  N     . ARG B 1 15  ? 2.863   29.194  -20.141 1.00 17.44  ?  15  ARG B N     1 
ATOM   2515 C  CA    . ARG B 1 15  ? 3.510   27.890  -20.255 1.00 21.65  ?  15  ARG B CA    1 
ATOM   2516 C  C     . ARG B 1 15  ? 4.256   27.791  -21.581 1.00 19.97  ?  15  ARG B C     1 
ATOM   2517 O  O     . ARG B 1 15  ? 5.373   27.260  -21.643 1.00 16.81  ?  15  ARG B O     1 
ATOM   2518 C  CB    . ARG B 1 15  ? 2.461   26.784  -20.109 1.00 17.17  ?  15  ARG B CB    1 
ATOM   2519 C  CG    . ARG B 1 15  ? 1.521   26.995  -18.887 1.00 27.50  ?  15  ARG B CG    1 
ATOM   2520 C  CD    . ARG B 1 15  ? 2.019   26.228  -17.669 1.00 26.68  ?  15  ARG B CD    1 
ATOM   2521 N  NE    . ARG B 1 15  ? 2.897   27.050  -16.845 1.00 33.08  ?  15  ARG B NE    1 
ATOM   2522 C  CZ    . ARG B 1 15  ? 2.543   27.677  -15.718 1.00 43.90  ?  15  ARG B CZ    1 
ATOM   2523 N  NH1   . ARG B 1 15  ? 1.400   27.438  -15.087 1.00 34.47  ?  15  ARG B NH1   1 
ATOM   2524 N  NH2   . ARG B 1 15  ? 3.387   28.514  -15.149 1.00 44.77  ?  15  ARG B NH2   1 
ATOM   2525 N  N     . LEU B 1 16  ? 3.665   28.366  -22.635 1.00 18.62  ?  16  LEU B N     1 
ATOM   2526 C  CA    . LEU B 1 16  ? 4.273   28.402  -23.957 1.00 19.18  ?  16  LEU B CA    1 
ATOM   2527 C  C     . LEU B 1 16  ? 5.637   29.077  -23.926 1.00 21.99  ?  16  LEU B C     1 
ATOM   2528 O  O     . LEU B 1 16  ? 6.565   28.665  -24.642 1.00 16.36  ?  16  LEU B O     1 
ATOM   2529 C  CB    . LEU B 1 16  ? 3.340   29.136  -24.924 1.00 15.23  ?  16  LEU B CB    1 
ATOM   2530 C  CG    . LEU B 1 16  ? 3.969   29.379  -26.302 1.00 14.62  ?  16  LEU B CG    1 
ATOM   2531 C  CD1   . LEU B 1 16  ? 4.226   28.037  -26.974 1.00 11.42  ?  16  LEU B CD1   1 
ATOM   2532 C  CD2   . LEU B 1 16  ? 3.061   30.233  -27.142 1.00 12.20  ?  16  LEU B CD2   1 
ATOM   2533 N  N     . ALA B 1 17  ? 5.770   30.130  -23.116 1.00 19.73  ?  17  ALA B N     1 
ATOM   2534 C  CA    . ALA B 1 17  ? 7.062   30.788  -22.965 1.00 19.81  ?  17  ALA B CA    1 
ATOM   2535 C  C     . ALA B 1 17  ? 8.096   29.826  -22.400 1.00 21.65  ?  17  ALA B C     1 
ATOM   2536 O  O     . ALA B 1 17  ? 9.245   29.805  -22.847 1.00 21.83  ?  17  ALA B O     1 
ATOM   2537 C  CB    . ALA B 1 17  ? 6.920   32.012  -22.063 1.00 21.54  ?  17  ALA B CB    1 
ATOM   2538 N  N     . VAL B 1 18  ? 7.690   29.001  -21.432 1.00 20.61  ?  18  VAL B N     1 
ATOM   2539 C  CA    . VAL B 1 18  ? 8.607   28.053  -20.809 1.00 20.45  ?  18  VAL B CA    1 
ATOM   2540 C  C     . VAL B 1 18  ? 8.956   26.917  -21.773 1.00 21.78  ?  18  VAL B C     1 
ATOM   2541 O  O     . VAL B 1 18  ? 10.119  26.502  -21.864 1.00 19.71  ?  18  VAL B O     1 
ATOM   2542 C  CB    . VAL B 1 18  ? 7.996   27.526  -19.499 1.00 19.31  ?  18  VAL B CB    1 
ATOM   2543 C  CG1   . VAL B 1 18  ? 8.792   26.331  -18.976 1.00 19.40  ?  18  VAL B CG1   1 
ATOM   2544 C  CG2   . VAL B 1 18  ? 7.952   28.639  -18.451 1.00 17.35  ?  18  VAL B CG2   1 
ATOM   2545 N  N     . ALA B 1 19  ? 7.957   26.384  -22.490 1.00 18.45  ?  19  ALA B N     1 
ATOM   2546 C  CA    . ALA B 1 19  ? 8.232   25.361  -23.496 1.00 20.18  ?  19  ALA B CA    1 
ATOM   2547 C  C     . ALA B 1 19  ? 9.153   25.896  -24.588 1.00 19.51  ?  19  ALA B C     1 
ATOM   2548 O  O     . ALA B 1 19  ? 10.109  25.222  -24.986 1.00 15.99  ?  19  ALA B O     1 
ATOM   2549 C  CB    . ALA B 1 19  ? 6.930   24.843  -24.103 1.00 16.62  ?  19  ALA B CB    1 
ATOM   2550 N  N     . LEU B 1 20  ? 8.906   27.122  -25.064 1.00 21.52  ?  20  LEU B N     1 
ATOM   2551 C  CA    . LEU B 1 20  ? 9.779   27.682  -26.093 1.00 20.00  ?  20  LEU B CA    1 
ATOM   2552 C  C     . LEU B 1 20  ? 11.191  27.907  -25.557 1.00 21.09  ?  20  LEU B C     1 
ATOM   2553 O  O     . LEU B 1 20  ? 12.175  27.718  -26.284 1.00 18.41  ?  20  LEU B O     1 
ATOM   2554 C  CB    . LEU B 1 20  ? 9.188   28.975  -26.648 1.00 19.22  ?  20  LEU B CB    1 
ATOM   2555 C  CG    . LEU B 1 20  ? 8.039   28.812  -27.646 1.00 15.94  ?  20  LEU B CG    1 
ATOM   2556 C  CD1   . LEU B 1 20  ? 7.401   30.159  -27.933 1.00 12.65  ?  20  LEU B CD1   1 
ATOM   2557 C  CD2   . LEU B 1 20  ? 8.501   28.145  -28.945 1.00 14.06  ?  20  LEU B CD2   1 
ATOM   2558 N  N     . GLN B 1 21  ? 11.322  28.282  -24.282 1.00 19.11  ?  21  GLN B N     1 
ATOM   2559 C  CA    . GLN B 1 21  ? 12.666  28.413  -23.729 1.00 21.97  ?  21  GLN B CA    1 
ATOM   2560 C  C     . GLN B 1 21  ? 13.391  27.072  -23.691 1.00 24.08  ?  21  GLN B C     1 
ATOM   2561 O  O     . GLN B 1 21  ? 14.607  27.026  -23.909 1.00 19.15  ?  21  GLN B O     1 
ATOM   2562 C  CB    . GLN B 1 21  ? 12.627  29.026  -22.335 1.00 19.56  ?  21  GLN B CB    1 
ATOM   2563 C  CG    . GLN B 1 21  ? 14.009  29.211  -21.721 1.00 24.47  ?  21  GLN B CG    1 
ATOM   2564 C  CD    . GLN B 1 21  ? 14.870  30.218  -22.503 1.00 43.62  ?  21  GLN B CD    1 
ATOM   2565 O  OE1   . GLN B 1 21  ? 14.354  31.019  -23.294 1.00 39.45  ?  21  GLN B OE1   1 
ATOM   2566 N  NE2   . GLN B 1 21  ? 16.185  30.177  -22.284 1.00 41.17  ?  21  GLN B NE2   1 
ATOM   2567 N  N     . SER B 1 22  ? 12.673  25.972  -23.390 1.00 17.39  ?  22  SER B N     1 
ATOM   2568 C  CA    . SER B 1 22  ? 13.309  24.660  -23.376 1.00 16.93  ?  22  SER B CA    1 
ATOM   2569 C  C     . SER B 1 22  ? 13.791  24.243  -24.761 1.00 18.10  ?  22  SER B C     1 
ATOM   2570 O  O     . SER B 1 22  ? 14.635  23.346  -24.870 1.00 15.96  ?  22  SER B O     1 
ATOM   2571 C  CB    . SER B 1 22  ? 12.364  23.597  -22.813 1.00 19.18  ?  22  SER B CB    1 
ATOM   2572 O  OG    . SER B 1 22  ? 11.431  23.128  -23.771 1.00 16.13  ?  22  SER B OG    1 
ATOM   2573 N  N     . VAL B 1 23  ? 13.259  24.859  -25.817 1.00 17.31  ?  23  VAL B N     1 
ATOM   2574 C  CA    . VAL B 1 23  ? 13.797  24.663  -27.160 1.00 20.67  ?  23  VAL B CA    1 
ATOM   2575 C  C     . VAL B 1 23  ? 15.090  25.451  -27.330 1.00 21.32  ?  23  VAL B C     1 
ATOM   2576 O  O     . VAL B 1 23  ? 16.091  24.917  -27.812 1.00 23.85  ?  23  VAL B O     1 
ATOM   2577 C  CB    . VAL B 1 23  ? 12.751  25.060  -28.224 1.00 21.87  ?  23  VAL B CB    1 
ATOM   2578 C  CG1   . VAL B 1 23  ? 13.277  24.784  -29.614 1.00 16.55  ?  23  VAL B CG1   1 
ATOM   2579 C  CG2   . VAL B 1 23  ? 11.417  24.334  -27.997 1.00 18.09  ?  23  VAL B CG2   1 
ATOM   2580 N  N     . GLN B 1 24  ? 15.082  26.726  -26.916 1.00 20.22  ?  24  GLN B N     1 
ATOM   2581 C  CA    . GLN B 1 24  ? 16.271  27.578  -26.957 1.00 21.28  ?  24  GLN B CA    1 
ATOM   2582 C  C     . GLN B 1 24  ? 17.451  26.959  -26.226 1.00 20.18  ?  24  GLN B C     1 
ATOM   2583 O  O     . GLN B 1 24  ? 18.597  27.107  -26.654 1.00 16.70  ?  24  GLN B O     1 
ATOM   2584 C  CB    . GLN B 1 24  ? 15.965  28.933  -26.324 1.00 26.56  ?  24  GLN B CB    1 
ATOM   2585 C  CG    . GLN B 1 24  ? 15.506  30.020  -27.266 1.00 34.30  ?  24  GLN B CG    1 
ATOM   2586 C  CD    . GLN B 1 24  ? 15.125  31.286  -26.510 1.00 46.28  ?  24  GLN B CD    1 
ATOM   2587 O  OE1   . GLN B 1 24  ? 15.754  31.642  -25.502 1.00 47.80  ?  24  GLN B OE1   1 
ATOM   2588 N  NE2   . GLN B 1 24  ? 14.065  31.953  -26.968 1.00 40.40  ?  24  GLN B NE2   1 
ATOM   2589 N  N     . THR B 1 25  ? 17.202  26.301  -25.102 1.00 16.79  ?  25  THR B N     1 
ATOM   2590 C  CA    . THR B 1 25  ? 18.281  25.689  -24.337 1.00 18.68  ?  25  THR B CA    1 
ATOM   2591 C  C     . THR B 1 25  ? 18.679  24.310  -24.860 1.00 21.33  ?  25  THR B C     1 
ATOM   2592 O  O     . THR B 1 25  ? 19.473  23.627  -24.210 1.00 19.88  ?  25  THR B O     1 
ATOM   2593 C  CB    . THR B 1 25  ? 17.904  25.606  -22.854 1.00 20.69  ?  25  THR B CB    1 
ATOM   2594 O  OG1   . THR B 1 25  ? 16.769  24.742  -22.679 1.00 15.49  ?  25  THR B OG1   1 
ATOM   2595 C  CG2   . THR B 1 25  ? 17.576  27.022  -22.318 1.00 20.73  ?  25  THR B CG2   1 
ATOM   2596 N  N     . LEU B 1 26  ? 18.176  23.887  -26.017 1.00 20.05  ?  26  LEU B N     1 
ATOM   2597 C  CA    . LEU B 1 26  ? 18.638  22.627  -26.581 1.00 27.76  ?  26  LEU B CA    1 
ATOM   2598 C  C     . LEU B 1 26  ? 20.094  22.749  -27.015 1.00 26.39  ?  26  LEU B C     1 
ATOM   2599 O  O     . LEU B 1 26  ? 20.510  23.775  -27.556 1.00 27.93  ?  26  LEU B O     1 
ATOM   2600 C  CB    . LEU B 1 26  ? 17.773  22.212  -27.774 1.00 25.23  ?  26  LEU B CB    1 
ATOM   2601 C  CG    . LEU B 1 26  ? 16.406  21.598  -27.467 1.00 20.39  ?  26  LEU B CG    1 
ATOM   2602 C  CD1   . LEU B 1 26  ? 15.573  21.495  -28.723 1.00 15.62  ?  26  LEU B CD1   1 
ATOM   2603 C  CD2   . LEU B 1 26  ? 16.580  20.247  -26.843 1.00 21.51  ?  26  LEU B CD2   1 
ATOM   2604 N  N     . ASP B 1 27  ? 20.871  21.695  -26.764 1.00 33.45  ?  27  ASP B N     1 
ATOM   2605 C  CA    . ASP B 1 27  ? 22.227  21.567  -27.308 1.00 34.45  ?  27  ASP B CA    1 
ATOM   2606 C  C     . ASP B 1 27  ? 22.107  21.154  -28.774 1.00 34.39  ?  27  ASP B C     1 
ATOM   2607 O  O     . ASP B 1 27  ? 22.125  19.972  -29.127 1.00 35.52  ?  27  ASP B O     1 
ATOM   2608 C  CB    . ASP B 1 27  ? 23.051  20.566  -26.499 1.00 35.46  ?  27  ASP B CB    1 
ATOM   2609 C  CG    . ASP B 1 27  ? 24.540  20.613  -26.847 1.00 46.77  ?  27  ASP B CG    1 
ATOM   2610 O  OD1   . ASP B 1 27  ? 24.910  20.305  -28.007 1.00 50.16  ?  27  ASP B OD1   1 
ATOM   2611 O  OD2   . ASP B 1 27  ? 25.346  20.975  -25.961 1.00 52.03  ?  27  ASP B OD2   1 
ATOM   2612 N  N     . PHE B 1 28  ? 21.989  22.144  -29.648 1.00 32.69  ?  28  PHE B N     1 
ATOM   2613 C  CA    . PHE B 1 28  ? 21.689  21.839  -31.035 1.00 32.31  ?  28  PHE B CA    1 
ATOM   2614 C  C     . PHE B 1 28  ? 21.957  23.079  -31.878 1.00 37.42  ?  28  PHE B C     1 
ATOM   2615 O  O     . PHE B 1 28  ? 21.636  24.193  -31.453 1.00 35.18  ?  28  PHE B O     1 
ATOM   2616 C  CB    . PHE B 1 28  ? 20.228  21.388  -31.178 1.00 31.41  ?  28  PHE B CB    1 
ATOM   2617 C  CG    . PHE B 1 28  ? 19.949  20.674  -32.450 1.00 28.89  ?  28  PHE B CG    1 
ATOM   2618 C  CD1   . PHE B 1 28  ? 20.422  19.391  -32.648 1.00 30.93  ?  28  PHE B CD1   1 
ATOM   2619 C  CD2   . PHE B 1 28  ? 19.235  21.287  -33.461 1.00 30.42  ?  28  PHE B CD2   1 
ATOM   2620 C  CE1   . PHE B 1 28  ? 20.194  18.740  -33.830 1.00 27.81  ?  28  PHE B CE1   1 
ATOM   2621 C  CE2   . PHE B 1 28  ? 18.992  20.627  -34.654 1.00 29.28  ?  28  PHE B CE2   1 
ATOM   2622 C  CZ    . PHE B 1 28  ? 19.474  19.353  -34.836 1.00 25.20  ?  28  PHE B CZ    1 
ATOM   2623 N  N     . ASP B 1 29  ? 22.555  22.885  -33.062 1.00 37.02  ?  29  ASP B N     1 
ATOM   2624 C  CA    . ASP B 1 29  ? 22.750  23.998  -33.987 1.00 37.37  ?  29  ASP B CA    1 
ATOM   2625 C  C     . ASP B 1 29  ? 21.397  24.491  -34.477 1.00 40.71  ?  29  ASP B C     1 
ATOM   2626 O  O     . ASP B 1 29  ? 20.694  23.777  -35.205 1.00 31.50  ?  29  ASP B O     1 
ATOM   2627 C  CB    . ASP B 1 29  ? 23.616  23.613  -35.179 1.00 43.09  ?  29  ASP B CB    1 
ATOM   2628 C  CG    . ASP B 1 29  ? 23.683  24.731  -36.207 1.00 40.23  ?  29  ASP B CG    1 
ATOM   2629 O  OD1   . ASP B 1 29  ? 24.074  25.850  -35.819 1.00 45.97  ?  29  ASP B OD1   1 
ATOM   2630 O  OD2   . ASP B 1 29  ? 23.314  24.519  -37.382 1.00 39.06  ?  29  ASP B OD2   1 
ATOM   2631 N  N     . SER B 1 30  ? 21.049  25.724  -34.097 1.00 38.52  ?  30  SER B N     1 
ATOM   2632 C  CA    . SER B 1 30  ? 19.728  26.273  -34.370 1.00 40.21  ?  30  SER B CA    1 
ATOM   2633 C  C     . SER B 1 30  ? 19.507  26.589  -35.844 1.00 37.60  ?  30  SER B C     1 
ATOM   2634 O  O     . SER B 1 30  ? 18.369  26.884  -36.225 1.00 39.61  ?  30  SER B O     1 
ATOM   2635 C  CB    . SER B 1 30  ? 19.490  27.532  -33.513 1.00 47.86  ?  30  SER B CB    1 
ATOM   2636 O  OG    . SER B 1 30  ? 20.328  28.619  -33.896 1.00 40.08  ?  30  SER B OG    1 
ATOM   2637 N  N     . GLU B 1 31  ? 20.547  26.528  -36.683 1.00 39.71  ?  31  GLU B N     1 
ATOM   2638 C  CA    . GLU B 1 31  ? 20.343  26.738  -38.115 1.00 40.67  ?  31  GLU B CA    1 
ATOM   2639 C  C     . GLU B 1 31  ? 19.613  25.573  -38.770 1.00 32.46  ?  31  GLU B C     1 
ATOM   2640 O  O     . GLU B 1 31  ? 19.036  25.747  -39.849 1.00 36.74  ?  31  GLU B O     1 
ATOM   2641 C  CB    . GLU B 1 31  ? 21.684  26.978  -38.822 1.00 41.96  ?  31  GLU B CB    1 
ATOM   2642 C  CG    . GLU B 1 31  ? 22.600  27.921  -38.059 1.00 45.56  ?  31  GLU B CG    1 
ATOM   2643 C  CD    . GLU B 1 31  ? 21.922  29.249  -37.734 1.00 55.84  ?  31  GLU B CD    1 
ATOM   2644 O  OE1   . GLU B 1 31  ? 21.179  29.775  -38.595 1.00 60.39  ?  31  GLU B OE1   1 
ATOM   2645 O  OE2   . GLU B 1 31  ? 22.110  29.751  -36.601 1.00 60.80  ?  31  GLU B OE2   1 
ATOM   2646 N  N     . GLN B 1 32  ? 19.621  24.398  -38.146 1.00 27.31  ?  32  GLN B N     1 
ATOM   2647 C  CA    . GLN B 1 32  ? 18.952  23.215  -38.679 1.00 27.49  ?  32  GLN B CA    1 
ATOM   2648 C  C     . GLN B 1 32  ? 17.630  22.925  -37.967 1.00 24.74  ?  32  GLN B C     1 
ATOM   2649 O  O     . GLN B 1 32  ? 17.182  21.775  -37.940 1.00 24.45  ?  32  GLN B O     1 
ATOM   2650 C  CB    . GLN B 1 32  ? 19.879  22.004  -38.580 1.00 22.04  ?  32  GLN B CB    1 
ATOM   2651 C  CG    . GLN B 1 32  ? 21.083  22.019  -39.549 1.00 34.66  ?  32  GLN B CG    1 
ATOM   2652 C  CD    . GLN B 1 32  ? 20.831  21.245  -40.845 1.00 32.88  ?  32  GLN B CD    1 
ATOM   2653 O  OE1   . GLN B 1 32  ? 19.721  21.266  -41.407 1.00 26.77  ?  32  GLN B OE1   1 
ATOM   2654 N  NE2   . GLN B 1 32  ? 21.859  20.536  -41.313 1.00 38.47  ?  32  GLN B NE2   1 
ATOM   2655 N  N     . LEU B 1 33  ? 16.995  23.949  -37.397 1.00 24.85  ?  33  LEU B N     1 
ATOM   2656 C  CA    . LEU B 1 33  ? 15.843  23.784  -36.518 1.00 19.06  ?  33  LEU B CA    1 
ATOM   2657 C  C     . LEU B 1 33  ? 14.823  24.880  -36.784 1.00 21.95  ?  33  LEU B C     1 
ATOM   2658 O  O     . LEU B 1 33  ? 15.157  26.067  -36.726 1.00 18.72  ?  33  LEU B O     1 
ATOM   2659 C  CB    . LEU B 1 33  ? 16.277  23.839  -35.047 1.00 22.93  ?  33  LEU B CB    1 
ATOM   2660 C  CG    . LEU B 1 33  ? 15.198  23.667  -33.974 1.00 23.21  ?  33  LEU B CG    1 
ATOM   2661 C  CD1   . LEU B 1 33  ? 15.672  22.695  -32.929 1.00 19.43  ?  33  LEU B CD1   1 
ATOM   2662 C  CD2   . LEU B 1 33  ? 14.886  24.976  -33.313 1.00 23.21  ?  33  LEU B CD2   1 
ATOM   2663 N  N     . GLU B 1 34  ? 13.581  24.493  -37.062 1.00 19.58  ?  34  GLU B N     1 
ATOM   2664 C  CA    . GLU B 1 34  ? 12.487  25.452  -37.085 1.00 18.08  ?  34  GLU B CA    1 
ATOM   2665 C  C     . GLU B 1 34  ? 11.443  25.048  -36.046 1.00 17.02  ?  34  GLU B C     1 
ATOM   2666 O  O     . GLU B 1 34  ? 11.250  23.865  -35.752 1.00 14.50  ?  34  GLU B O     1 
ATOM   2667 C  CB    . GLU B 1 34  ? 11.843  25.559  -38.473 1.00 15.19  ?  34  GLU B CB    1 
ATOM   2668 C  CG    . GLU B 1 34  ? 11.177  24.256  -38.938 1.00 20.74  ?  34  GLU B CG    1 
ATOM   2669 C  CD    . GLU B 1 34  ? 10.219  24.433  -40.124 1.00 25.58  ?  34  GLU B CD    1 
ATOM   2670 O  OE1   . GLU B 1 34  ? 10.022  25.579  -40.587 1.00 33.83  ?  34  GLU B OE1   1 
ATOM   2671 O  OE2   . GLU B 1 34  ? 9.661   23.421  -40.601 1.00 23.12  ?  34  GLU B OE2   1 
ATOM   2672 N  N     . VAL B 1 35  ? 10.782  26.044  -35.480 1.00 18.51  ?  35  VAL B N     1 
ATOM   2673 C  CA    . VAL B 1 35  ? 9.714   25.838  -34.511 1.00 13.38  ?  35  VAL B CA    1 
ATOM   2674 C  C     . VAL B 1 35  ? 8.429   26.324  -35.142 1.00 13.15  ?  35  VAL B C     1 
ATOM   2675 O  O     . VAL B 1 35  ? 8.401   27.387  -35.773 1.00 15.26  ?  35  VAL B O     1 
ATOM   2676 C  CB    . VAL B 1 35  ? 9.989   26.581  -33.199 1.00 14.30  ?  35  VAL B CB    1 
ATOM   2677 C  CG1   . VAL B 1 35  ? 8.926   26.215  -32.153 1.00 15.66  ?  35  VAL B CG1   1 
ATOM   2678 C  CG2   . VAL B 1 35  ? 11.402  26.308  -32.719 1.00 10.83  ?  35  VAL B CG2   1 
ATOM   2679 N  N     . ILE B 1 36  ? 7.365   25.554  -34.988 1.00 11.65  ?  36  ILE B N     1 
ATOM   2680 C  CA    . ILE B 1 36  ? 6.064   25.952  -35.508 1.00 16.08  ?  36  ILE B CA    1 
ATOM   2681 C  C     . ILE B 1 36  ? 5.068   25.970  -34.362 1.00 13.96  ?  36  ILE B C     1 
ATOM   2682 O  O     . ILE B 1 36  ? 4.792   24.937  -33.744 1.00 11.12  ?  36  ILE B O     1 
ATOM   2683 C  CB    . ILE B 1 36  ? 5.610   25.042  -36.655 1.00 18.07  ?  36  ILE B CB    1 
ATOM   2684 C  CG1   . ILE B 1 36  ? 6.761   24.922  -37.669 1.00 19.48  ?  36  ILE B CG1   1 
ATOM   2685 C  CG2   . ILE B 1 36  ? 4.320   25.565  -37.276 1.00 13.61  ?  36  ILE B CG2   1 
ATOM   2686 C  CD1   . ILE B 1 36  ? 6.353   24.403  -39.013 1.00 25.80  ?  36  ILE B CD1   1 
ATOM   2687 N  N     . VAL B 1 37  ? 4.544   27.149  -34.068 1.00 16.18  ?  37  VAL B N     1 
ATOM   2688 C  CA    . VAL B 1 37  ? 3.560   27.322  -33.011 1.00 13.87  ?  37  VAL B CA    1 
ATOM   2689 C  C     . VAL B 1 37  ? 2.196   27.471  -33.665 1.00 13.94  ?  37  VAL B C     1 
ATOM   2690 O  O     . VAL B 1 37  ? 2.011   28.337  -34.524 1.00 13.68  ?  37  VAL B O     1 
ATOM   2691 C  CB    . VAL B 1 37  ? 3.893   28.531  -32.129 1.00 13.33  ?  37  VAL B CB    1 
ATOM   2692 C  CG1   . VAL B 1 37  ? 2.832   28.659  -30.997 1.00 7.97   ?  37  VAL B CG1   1 
ATOM   2693 C  CG2   . VAL B 1 37  ? 5.281   28.378  -31.553 1.00 10.22  ?  37  VAL B CG2   1 
ATOM   2694 N  N     . VAL B 1 38  ? 1.248   26.610  -33.297 1.00 10.05  ?  38  VAL B N     1 
ATOM   2695 C  CA    . VAL B 1 38  ? -0.096  26.659  -33.861 1.00 12.56  ?  38  VAL B CA    1 
ATOM   2696 C  C     . VAL B 1 38  ? -1.047  27.084  -32.734 1.00 15.12  ?  38  VAL B C     1 
ATOM   2697 O  O     . VAL B 1 38  ? -1.366  26.307  -31.826 1.00 8.42   ?  38  VAL B O     1 
ATOM   2698 C  CB    . VAL B 1 38  ? -0.496  25.325  -34.505 1.00 11.68  ?  38  VAL B CB    1 
ATOM   2699 C  CG1   . VAL B 1 38  ? -1.880  25.422  -35.161 1.00 9.13   ?  38  VAL B CG1   1 
ATOM   2700 C  CG2   . VAL B 1 38  ? 0.576   24.911  -35.603 1.00 13.91  ?  38  VAL B CG2   1 
ATOM   2701 N  N     . ASN B 1 39  ? -1.485  28.339  -32.775 1.00 14.90  ?  39  ASN B N     1 
ATOM   2702 C  CA    . ASN B 1 39  ? -2.495  28.828  -31.839 1.00 14.56  ?  39  ASN B CA    1 
ATOM   2703 C  C     . ASN B 1 39  ? -3.858  28.279  -32.247 1.00 17.88  ?  39  ASN B C     1 
ATOM   2704 O  O     . ASN B 1 39  ? -4.345  28.574  -33.344 1.00 16.74  ?  39  ASN B O     1 
ATOM   2705 C  CB    . ASN B 1 39  ? -2.499  30.355  -31.833 1.00 17.22  ?  39  ASN B CB    1 
ATOM   2706 C  CG    . ASN B 1 39  ? -3.380  30.945  -30.722 1.00 23.54  ?  39  ASN B CG    1 
ATOM   2707 O  OD1   . ASN B 1 39  ? -3.955  30.221  -29.906 1.00 16.75  ?  39  ASN B OD1   1 
ATOM   2708 N  ND2   . ASN B 1 39  ? -3.479  32.268  -30.693 1.00 19.92  ?  39  ASN B ND2   1 
ATOM   2709 N  N     . ASP B 1 40  ? -4.479  27.475  -31.375 1.00 16.23  ?  40  ASP B N     1 
ATOM   2710 C  CA    . ASP B 1 40  ? -5.755  26.851  -31.723 1.00 18.98  ?  40  ASP B CA    1 
ATOM   2711 C  C     . ASP B 1 40  ? -6.912  27.810  -31.475 1.00 22.96  ?  40  ASP B C     1 
ATOM   2712 O  O     . ASP B 1 40  ? -7.905  27.436  -30.839 1.00 21.58  ?  40  ASP B O     1 
ATOM   2713 C  CB    . ASP B 1 40  ? -5.965  25.548  -30.937 1.00 17.67  ?  40  ASP B CB    1 
ATOM   2714 C  CG    . ASP B 1 40  ? -6.963  24.603  -31.617 1.00 25.04  ?  40  ASP B CG    1 
ATOM   2715 O  OD1   . ASP B 1 40  ? -7.248  24.807  -32.816 1.00 26.29  ?  40  ASP B OD1   1 
ATOM   2716 O  OD2   . ASP B 1 40  ? -7.455  23.648  -30.967 1.00 20.89  ?  40  ASP B OD2   1 
ATOM   2717 N  N     . HIS B 1 41  ? -6.782  29.047  -31.970 1.00 23.14  ?  41  HIS B N     1 
ATOM   2718 C  CA    . HIS B 1 41  ? -7.802  30.084  -31.814 1.00 23.37  ?  41  HIS B CA    1 
ATOM   2719 C  C     . HIS B 1 41  ? -8.081  30.356  -30.341 1.00 22.63  ?  41  HIS B C     1 
ATOM   2720 O  O     . HIS B 1 41  ? -9.227  30.517  -29.923 1.00 25.67  ?  41  HIS B O     1 
ATOM   2721 C  CB    . HIS B 1 41  ? -9.086  29.723  -32.565 1.00 30.35  ?  41  HIS B CB    1 
ATOM   2722 C  CG    . HIS B 1 41  ? -9.942  30.904  -32.894 1.00 35.27  ?  41  HIS B CG    1 
ATOM   2723 N  ND1   . HIS B 1 41  ? -11.256 31.009  -32.488 1.00 33.81  ?  41  HIS B ND1   1 
ATOM   2724 C  CD2   . HIS B 1 41  ? -9.663  32.046  -33.567 1.00 36.22  ?  41  HIS B CD2   1 
ATOM   2725 C  CE1   . HIS B 1 41  ? -11.752 32.159  -32.907 1.00 36.25  ?  41  HIS B CE1   1 
ATOM   2726 N  NE2   . HIS B 1 41  ? -10.806 32.809  -33.561 1.00 33.00  ?  41  HIS B NE2   1 
ATOM   2727 N  N     . GLY B 1 42  ? -7.014  30.367  -29.544 1.00 19.75  ?  42  GLY B N     1 
ATOM   2728 C  CA    . GLY B 1 42  ? -7.067  30.817  -28.177 1.00 15.55  ?  42  GLY B CA    1 
ATOM   2729 C  C     . GLY B 1 42  ? -6.547  32.231  -28.045 1.00 25.15  ?  42  GLY B C     1 
ATOM   2730 O  O     . GLY B 1 42  ? -6.367  32.964  -29.028 1.00 18.87  ?  42  GLY B O     1 
ATOM   2731 N  N     . THR B 1 43  ? -6.283  32.612  -26.808 1.00 21.95  ?  43  THR B N     1 
ATOM   2732 C  CA    . THR B 1 43  ? -5.756  33.935  -26.536 1.00 22.09  ?  43  THR B CA    1 
ATOM   2733 C  C     . THR B 1 43  ? -4.472  34.173  -27.356 1.00 21.85  ?  43  THR B C     1 
ATOM   2734 O  O     . THR B 1 43  ? -3.707  33.238  -27.575 1.00 17.87  ?  43  THR B O     1 
ATOM   2735 C  CB    . THR B 1 43  ? -5.484  34.074  -25.042 1.00 19.21  ?  43  THR B CB    1 
ATOM   2736 O  OG1   . THR B 1 43  ? -5.343  35.456  -24.700 1.00 21.14  ?  43  THR B OG1   1 
ATOM   2737 C  CG2   . THR B 1 43  ? -4.235  33.299  -24.645 1.00 18.41  ?  43  THR B CG2   1 
ATOM   2738 N  N     . PRO B 1 44  ? -4.229  35.409  -27.809 1.00 26.89  ?  44  PRO B N     1 
ATOM   2739 C  CA    . PRO B 1 44  ? -3.089  35.653  -28.716 1.00 19.31  ?  44  PRO B CA    1 
ATOM   2740 C  C     . PRO B 1 44  ? -1.741  35.404  -28.051 1.00 24.83  ?  44  PRO B C     1 
ATOM   2741 O  O     . PRO B 1 44  ? -1.550  35.672  -26.864 1.00 23.97  ?  44  PRO B O     1 
ATOM   2742 C  CB    . PRO B 1 44  ? -3.252  37.139  -29.084 1.00 23.31  ?  44  PRO B CB    1 
ATOM   2743 C  CG    . PRO B 1 44  ? -4.676  37.487  -28.758 1.00 26.28  ?  44  PRO B CG    1 
ATOM   2744 C  CD    . PRO B 1 44  ? -5.016  36.632  -27.570 1.00 24.59  ?  44  PRO B CD    1 
ATOM   2745 N  N     . VAL B 1 45  ? -0.782  34.899  -28.841 1.00 23.17  ?  45  VAL B N     1 
ATOM   2746 C  CA    . VAL B 1 45  ? 0.548   34.604  -28.314 1.00 21.05  ?  45  VAL B CA    1 
ATOM   2747 C  C     . VAL B 1 45  ? 1.606   35.219  -29.225 1.00 25.91  ?  45  VAL B C     1 
ATOM   2748 O  O     . VAL B 1 45  ? 2.764   34.783  -29.242 1.00 27.67  ?  45  VAL B O     1 
ATOM   2749 C  CB    . VAL B 1 45  ? 0.768   33.087  -28.165 1.00 23.29  ?  45  VAL B CB    1 
ATOM   2750 C  CG1   . VAL B 1 45  ? -0.113  32.509  -27.045 1.00 18.52  ?  45  VAL B CG1   1 
ATOM   2751 C  CG2   . VAL B 1 45  ? 0.522   32.380  -29.495 1.00 21.86  ?  45  VAL B CG2   1 
ATOM   2752 N  N     . ASP B 1 46  ? 1.212   36.240  -29.991 1.00 27.02  ?  46  ASP B N     1 
ATOM   2753 C  CA    . ASP B 1 46  ? 2.147   36.908  -30.894 1.00 29.40  ?  46  ASP B CA    1 
ATOM   2754 C  C     . ASP B 1 46  ? 3.337   37.498  -30.140 1.00 25.38  ?  46  ASP B C     1 
ATOM   2755 O  O     . ASP B 1 46  ? 4.465   37.466  -30.635 1.00 24.98  ?  46  ASP B O     1 
ATOM   2756 C  CB    . ASP B 1 46  ? 1.414   37.990  -31.686 1.00 31.35  ?  46  ASP B CB    1 
ATOM   2757 C  CG    . ASP B 1 46  ? 0.253   37.430  -32.514 1.00 35.86  ?  46  ASP B CG    1 
ATOM   2758 O  OD1   . ASP B 1 46  ? -0.836  37.179  -31.944 1.00 33.52  ?  46  ASP B OD1   1 
ATOM   2759 O  OD2   . ASP B 1 46  ? 0.424   37.253  -33.741 1.00 41.49  ?  46  ASP B OD2   1 
ATOM   2760 N  N     . ASP B 1 47  ? 3.114   38.022  -28.933 1.00 24.85  ?  47  ASP B N     1 
ATOM   2761 C  CA    . ASP B 1 47  ? 4.218   38.598  -28.165 1.00 31.43  ?  47  ASP B CA    1 
ATOM   2762 C  C     . ASP B 1 47  ? 5.155   37.517  -27.653 1.00 24.64  ?  47  ASP B C     1 
ATOM   2763 O  O     . ASP B 1 47  ? 6.383   37.668  -27.710 1.00 24.43  ?  47  ASP B O     1 
ATOM   2764 C  CB    . ASP B 1 47  ? 3.695   39.422  -26.985 1.00 27.67  ?  47  ASP B CB    1 
ATOM   2765 C  CG    . ASP B 1 47  ? 2.605   40.384  -27.388 1.00 40.44  ?  47  ASP B CG    1 
ATOM   2766 O  OD1   . ASP B 1 47  ? 1.436   39.945  -27.463 1.00 42.00  ?  47  ASP B OD1   1 
ATOM   2767 O  OD2   . ASP B 1 47  ? 2.920   41.572  -27.637 1.00 40.09  ?  47  ASP B OD2   1 
ATOM   2768 N  N     . VAL B 1 48  ? 4.592   36.440  -27.101 1.00 20.84  ?  48  VAL B N     1 
ATOM   2769 C  CA    . VAL B 1 48  ? 5.425   35.351  -26.604 1.00 21.27  ?  48  VAL B CA    1 
ATOM   2770 C  C     . VAL B 1 48  ? 6.325   34.824  -27.713 1.00 15.95  ?  48  VAL B C     1 
ATOM   2771 O  O     . VAL B 1 48  ? 7.525   34.621  -27.514 1.00 16.87  ?  48  VAL B O     1 
ATOM   2772 C  CB    . VAL B 1 48  ? 4.559   34.227  -26.017 1.00 15.56  ?  48  VAL B CB    1 
ATOM   2773 C  CG1   . VAL B 1 48  ? 5.454   33.059  -25.615 1.00 17.60  ?  48  VAL B CG1   1 
ATOM   2774 C  CG2   . VAL B 1 48  ? 3.766   34.733  -24.829 1.00 17.63  ?  48  VAL B CG2   1 
ATOM   2775 N  N     . VAL B 1 49  ? 5.767   34.620  -28.902 1.00 16.10  ?  49  VAL B N     1 
ATOM   2776 C  CA    . VAL B 1 49  ? 6.536   33.957  -29.943 1.00 22.19  ?  49  VAL B CA    1 
ATOM   2777 C  C     . VAL B 1 49  ? 7.548   34.911  -30.569 1.00 27.60  ?  49  VAL B C     1 
ATOM   2778 O  O     . VAL B 1 49  ? 8.641   34.479  -30.945 1.00 28.20  ?  49  VAL B O     1 
ATOM   2779 C  CB    . VAL B 1 49  ? 5.580   33.335  -30.976 1.00 24.44  ?  49  VAL B CB    1 
ATOM   2780 C  CG1   . VAL B 1 49  ? 6.335   32.835  -32.192 1.00 22.26  ?  49  VAL B CG1   1 
ATOM   2781 C  CG2   . VAL B 1 49  ? 4.801   32.166  -30.328 1.00 24.10  ?  49  VAL B CG2   1 
ATOM   2782 N  N     . GLU B 1 50  ? 7.234   36.216  -30.661 1.00 25.80  ?  50  GLU B N     1 
ATOM   2783 C  CA    . GLU B 1 50  ? 8.230   37.175  -31.147 1.00 26.39  ?  50  GLU B CA    1 
ATOM   2784 C  C     . GLU B 1 50  ? 9.419   37.256  -30.201 1.00 27.34  ?  50  GLU B C     1 
ATOM   2785 O  O     . GLU B 1 50  ? 10.567  37.363  -30.642 1.00 27.68  ?  50  GLU B O     1 
ATOM   2786 C  CB    . GLU B 1 50  ? 7.632   38.573  -31.319 1.00 31.38  ?  50  GLU B CB    1 
ATOM   2787 C  CG    . GLU B 1 50  ? 6.766   38.764  -32.541 1.00 36.18  ?  50  GLU B CG    1 
ATOM   2788 C  CD    . GLU B 1 50  ? 5.849   39.976  -32.405 1.00 45.45  ?  50  GLU B CD    1 
ATOM   2789 O  OE1   . GLU B 1 50  ? 4.674   39.810  -31.998 1.00 46.91  ?  50  GLU B OE1   1 
ATOM   2790 O  OE2   . GLU B 1 50  ? 6.307   41.098  -32.719 1.00 42.81  ?  50  GLU B OE2   1 
ATOM   2791 N  N     . ALA B 1 51  ? 9.166   37.215  -28.893 1.00 25.99  ?  51  ALA B N     1 
ATOM   2792 C  CA    . ALA B 1 51  ? 10.280  37.238  -27.953 1.00 28.99  ?  51  ALA B CA    1 
ATOM   2793 C  C     . ALA B 1 51  ? 11.179  36.014  -28.128 1.00 31.24  ?  51  ALA B C     1 
ATOM   2794 O  O     . ALA B 1 51  ? 12.408  36.123  -28.039 1.00 29.08  ?  51  ALA B O     1 
ATOM   2795 C  CB    . ALA B 1 51  ? 9.753   37.339  -26.524 1.00 21.48  ?  51  ALA B CB    1 
ATOM   2796 N  N     . ALA B 1 52  ? 10.585  34.840  -28.389 1.00 28.65  ?  52  ALA B N     1 
ATOM   2797 C  CA    . ALA B 1 52  ? 11.384  33.637  -28.629 1.00 28.19  ?  52  ALA B CA    1 
ATOM   2798 C  C     . ALA B 1 52  ? 12.066  33.668  -29.992 1.00 27.79  ?  52  ALA B C     1 
ATOM   2799 O  O     . ALA B 1 52  ? 13.166  33.120  -30.146 1.00 27.75  ?  52  ALA B O     1 
ATOM   2800 C  CB    . ALA B 1 52  ? 10.514  32.385  -28.519 1.00 19.60  ?  52  ALA B CB    1 
ATOM   2801 N  N     . GLY B 1 53  ? 11.429  34.284  -30.992 1.00 27.52  ?  53  GLY B N     1 
ATOM   2802 C  CA    . GLY B 1 53  ? 11.987  34.352  -32.334 1.00 28.24  ?  53  GLY B CA    1 
ATOM   2803 C  C     . GLY B 1 53  ? 13.303  35.105  -32.429 1.00 34.20  ?  53  GLY B C     1 
ATOM   2804 O  O     . GLY B 1 53  ? 13.973  35.029  -33.472 1.00 30.31  ?  53  GLY B O     1 
ATOM   2805 N  N     . ARG B 1 54  ? 13.673  35.839  -31.373 1.00 32.46  ?  54  ARG B N     1 
ATOM   2806 C  CA    . ARG B 1 54  ? 14.992  36.460  -31.306 1.00 40.08  ?  54  ARG B CA    1 
ATOM   2807 C  C     . ARG B 1 54  ? 16.091  35.428  -31.511 1.00 37.34  ?  54  ARG B C     1 
ATOM   2808 O  O     . ARG B 1 54  ? 16.991  35.611  -32.340 1.00 45.76  ?  54  ARG B O     1 
ATOM   2809 C  CB    . ARG B 1 54  ? 15.181  37.150  -29.953 1.00 38.86  ?  54  ARG B CB    1 
ATOM   2810 C  CG    . ARG B 1 54  ? 14.436  38.453  -29.770 1.00 38.54  ?  54  ARG B CG    1 
ATOM   2811 C  CD    . ARG B 1 54  ? 14.075  39.110  -31.080 1.00 48.35  ?  54  ARG B CD    1 
ATOM   2812 N  NE    . ARG B 1 54  ? 13.104  40.175  -30.860 1.00 53.68  ?  54  ARG B NE    1 
ATOM   2813 C  CZ    . ARG B 1 54  ? 13.431  41.426  -30.559 1.00 53.63  ?  54  ARG B CZ    1 
ATOM   2814 N  NH1   . ARG B 1 54  ? 14.698  41.797  -30.428 1.00 46.10  ?  54  ARG B NH1   1 
ATOM   2815 N  NH2   . ARG B 1 54  ? 12.464  42.322  -30.367 1.00 52.84  ?  54  ARG B NH2   1 
ATOM   2816 N  N     . SER B 1 55  ? 16.024  34.328  -30.760 1.00 35.94  ?  55  SER B N     1 
ATOM   2817 C  CA    . SER B 1 55  ? 17.065  33.312  -30.732 1.00 37.98  ?  55  SER B CA    1 
ATOM   2818 C  C     . SER B 1 55  ? 16.699  32.039  -31.492 1.00 32.66  ?  55  SER B C     1 
ATOM   2819 O  O     . SER B 1 55  ? 17.500  31.102  -31.515 1.00 32.77  ?  55  SER B O     1 
ATOM   2820 C  CB    . SER B 1 55  ? 17.393  32.964  -29.280 1.00 46.48  ?  55  SER B CB    1 
ATOM   2821 O  OG    . SER B 1 55  ? 17.611  34.143  -28.528 1.00 49.58  ?  55  SER B OG    1 
ATOM   2822 N  N     . LEU B 1 56  ? 15.518  31.985  -32.110 1.00 26.39  ?  56  LEU B N     1 
ATOM   2823 C  CA    . LEU B 1 56  ? 14.990  30.777  -32.722 1.00 26.72  ?  56  LEU B CA    1 
ATOM   2824 C  C     . LEU B 1 56  ? 14.327  31.144  -34.037 1.00 21.43  ?  56  LEU B C     1 
ATOM   2825 O  O     . LEU B 1 56  ? 13.838  32.261  -34.210 1.00 21.65  ?  56  LEU B O     1 
ATOM   2826 C  CB    . LEU B 1 56  ? 13.941  30.078  -31.820 1.00 23.19  ?  56  LEU B CB    1 
ATOM   2827 C  CG    . LEU B 1 56  ? 14.296  29.238  -30.588 1.00 26.07  ?  56  LEU B CG    1 
ATOM   2828 C  CD1   . LEU B 1 56  ? 13.035  28.928  -29.775 1.00 20.70  ?  56  LEU B CD1   1 
ATOM   2829 C  CD2   . LEU B 1 56  ? 14.997  27.969  -30.965 1.00 26.31  ?  56  LEU B CD2   1 
ATOM   2830 N  N     . ASN B 1 57  ? 14.284  30.178  -34.951 1.00 23.47  ?  57  ASN B N     1 
ATOM   2831 C  CA    . ASN B 1 57  ? 13.556  30.302  -36.219 1.00 23.97  ?  57  ASN B CA    1 
ATOM   2832 C  C     . ASN B 1 57  ? 12.125  29.812  -35.986 1.00 24.05  ?  57  ASN B C     1 
ATOM   2833 O  O     . ASN B 1 57  ? 11.854  28.606  -36.025 1.00 16.03  ?  57  ASN B O     1 
ATOM   2834 C  CB    . ASN B 1 57  ? 14.298  29.521  -37.305 1.00 22.76  ?  57  ASN B CB    1 
ATOM   2835 C  CG    . ASN B 1 57  ? 13.536  29.424  -38.627 1.00 27.68  ?  57  ASN B CG    1 
ATOM   2836 O  OD1   . ASN B 1 57  ? 12.474  30.016  -38.816 1.00 29.89  ?  57  ASN B OD1   1 
ATOM   2837 N  ND2   . ASN B 1 57  ? 14.122  28.702  -39.575 1.00 33.03  ?  57  ASN B ND2   1 
ATOM   2838 N  N     . VAL B 1 58  ? 11.201  30.743  -35.717 1.00 20.98  ?  58  VAL B N     1 
ATOM   2839 C  CA    . VAL B 1 58  ? 9.863   30.394  -35.241 1.00 16.89  ?  58  VAL B CA    1 
ATOM   2840 C  C     . VAL B 1 58  ? 8.828   30.987  -36.179 1.00 18.87  ?  58  VAL B C     1 
ATOM   2841 O  O     . VAL B 1 58  ? 8.973   32.120  -36.646 1.00 24.25  ?  58  VAL B O     1 
ATOM   2842 C  CB    . VAL B 1 58  ? 9.587   30.883  -33.803 1.00 20.75  ?  58  VAL B CB    1 
ATOM   2843 C  CG1   . VAL B 1 58  ? 8.376   30.125  -33.184 1.00 17.30  ?  58  VAL B CG1   1 
ATOM   2844 C  CG2   . VAL B 1 58  ? 10.827  30.795  -32.939 1.00 21.23  ?  58  VAL B CG2   1 
ATOM   2845 N  N     . ARG B 1 59  ? 7.775   30.225  -36.427 1.00 16.58  ?  59  ARG B N     1 
ATOM   2846 C  CA    . ARG B 1 59  ? 6.623   30.657  -37.198 1.00 18.82  ?  59  ARG B CA    1 
ATOM   2847 C  C     . ARG B 1 59  ? 5.357   30.351  -36.406 1.00 20.39  ?  59  ARG B C     1 
ATOM   2848 O  O     . ARG B 1 59  ? 5.239   29.280  -35.799 1.00 16.24  ?  59  ARG B O     1 
ATOM   2849 C  CB    . ARG B 1 59  ? 6.614   29.961  -38.542 1.00 23.16  ?  59  ARG B CB    1 
ATOM   2850 C  CG    . ARG B 1 59  ? 5.401   30.213  -39.388 1.00 26.64  ?  59  ARG B CG    1 
ATOM   2851 C  CD    . ARG B 1 59  ? 5.358   29.158  -40.480 1.00 24.29  ?  59  ARG B CD    1 
ATOM   2852 N  NE    . ARG B 1 59  ? 4.106   29.189  -41.229 1.00 30.91  ?  59  ARG B NE    1 
ATOM   2853 C  CZ    . ARG B 1 59  ? 3.977   28.776  -42.484 1.00 35.23  ?  59  ARG B CZ    1 
ATOM   2854 N  NH1   . ARG B 1 59  ? 5.020   28.339  -43.178 1.00 31.59  ?  59  ARG B NH1   1 
ATOM   2855 N  NH2   . ARG B 1 59  ? 2.773   28.797  -43.053 1.00 34.63  ?  59  ARG B NH2   1 
ATOM   2856 N  N     . LEU B 1 60  ? 4.422   31.295  -36.397 1.00 18.69  ?  60  LEU B N     1 
ATOM   2857 C  CA    . LEU B 1 60  ? 3.170   31.166  -35.663 1.00 17.89  ?  60  LEU B CA    1 
ATOM   2858 C  C     . LEU B 1 60  ? 2.019   30.981  -36.647 1.00 18.98  ?  60  LEU B C     1 
ATOM   2859 O  O     . LEU B 1 60  ? 1.880   31.758  -37.592 1.00 21.44  ?  60  LEU B O     1 
ATOM   2860 C  CB    . LEU B 1 60  ? 2.923   32.408  -34.797 1.00 24.51  ?  60  LEU B CB    1 
ATOM   2861 C  CG    . LEU B 1 60  ? 1.558   32.588  -34.100 1.00 22.40  ?  60  LEU B CG    1 
ATOM   2862 C  CD1   . LEU B 1 60  ? 1.303   31.476  -33.105 1.00 14.21  ?  60  LEU B CD1   1 
ATOM   2863 C  CD2   . LEU B 1 60  ? 1.459   33.950  -33.420 1.00 24.10  ?  60  LEU B CD2   1 
ATOM   2864 N  N     . ILE B 1 61  ? 1.192   29.963  -36.426 1.00 20.67  ?  61  ILE B N     1 
ATOM   2865 C  CA    . ILE B 1 61  ? -0.052  29.786  -37.169 1.00 20.10  ?  61  ILE B CA    1 
ATOM   2866 C  C     . ILE B 1 61  ? -1.219  30.025  -36.216 1.00 26.61  ?  61  ILE B C     1 
ATOM   2867 O  O     . ILE B 1 61  ? -1.289  29.403  -35.149 1.00 23.06  ?  61  ILE B O     1 
ATOM   2868 C  CB    . ILE B 1 61  ? -0.133  28.392  -37.811 1.00 25.51  ?  61  ILE B CB    1 
ATOM   2869 C  CG1   . ILE B 1 61  ? 0.943   28.244  -38.899 1.00 26.35  ?  61  ILE B CG1   1 
ATOM   2870 C  CG2   . ILE B 1 61  ? -1.525  28.163  -38.397 1.00 21.91  ?  61  ILE B CG2   1 
ATOM   2871 C  CD1   . ILE B 1 61  ? 1.145   26.818  -39.385 1.00 23.95  ?  61  ILE B CD1   1 
ATOM   2872 N  N     . ASP B 1 62  ? -2.124  30.940  -36.587 1.00 27.69  ?  62  ASP B N     1 
ATOM   2873 C  CA    . ASP B 1 62  ? -3.364  31.159  -35.848 1.00 25.09  ?  62  ASP B CA    1 
ATOM   2874 C  C     . ASP B 1 62  ? -4.518  30.490  -36.589 1.00 27.78  ?  62  ASP B C     1 
ATOM   2875 O  O     . ASP B 1 62  ? -4.837  30.867  -37.723 1.00 26.26  ?  62  ASP B O     1 
ATOM   2876 C  CB    . ASP B 1 62  ? -3.642  32.651  -35.662 1.00 36.24  ?  62  ASP B CB    1 
ATOM   2877 C  CG    . ASP B 1 62  ? -2.533  33.361  -34.895 1.00 41.66  ?  62  ASP B CG    1 
ATOM   2878 O  OD1   . ASP B 1 62  ? -2.444  33.203  -33.647 1.00 32.28  ?  62  ASP B OD1   1 
ATOM   2879 O  OD2   . ASP B 1 62  ? -1.737  34.070  -35.560 1.00 46.46  ?  62  ASP B OD2   1 
ATOM   2880 N  N     . GLN B 1 63  ? -5.139  29.502  -35.945 1.00 26.15  ?  63  GLN B N     1 
ATOM   2881 C  CA    . GLN B 1 63  ? -6.258  28.802  -36.552 1.00 23.16  ?  63  GLN B CA    1 
ATOM   2882 C  C     . GLN B 1 63  ? -7.491  29.704  -36.576 1.00 31.39  ?  63  GLN B C     1 
ATOM   2883 O  O     . GLN B 1 63  ? -7.739  30.453  -35.620 1.00 32.14  ?  63  GLN B O     1 
ATOM   2884 C  CB    . GLN B 1 63  ? -6.567  27.518  -35.783 1.00 25.36  ?  63  GLN B CB    1 
ATOM   2885 C  CG    . GLN B 1 63  ? -5.451  26.468  -35.788 1.00 24.81  ?  63  GLN B CG    1 
ATOM   2886 C  CD    . GLN B 1 63  ? -5.330  25.746  -37.121 1.00 20.94  ?  63  GLN B CD    1 
ATOM   2887 O  OE1   . GLN B 1 63  ? -4.783  26.287  -38.080 1.00 24.40  ?  63  GLN B OE1   1 
ATOM   2888 N  NE2   . GLN B 1 63  ? -5.843  24.522  -37.185 1.00 21.86  ?  63  GLN B NE2   1 
ATOM   2889 N  N     . PRO B 1 64  ? -8.293  29.649  -37.644 1.00 30.51  ?  64  PRO B N     1 
ATOM   2890 C  CA    . PRO B 1 64  ? -9.470  30.532  -37.695 1.00 35.38  ?  64  PRO B CA    1 
ATOM   2891 C  C     . PRO B 1 64  ? -10.497 30.178  -36.642 1.00 37.67  ?  64  PRO B C     1 
ATOM   2892 O  O     . PRO B 1 64  ? -11.133 31.075  -36.075 1.00 36.69  ?  64  PRO B O     1 
ATOM   2893 C  CB    . PRO B 1 64  ? -10.015 30.328  -39.117 1.00 37.16  ?  64  PRO B CB    1 
ATOM   2894 C  CG    . PRO B 1 64  ? -9.347  29.126  -39.661 1.00 37.29  ?  64  PRO B CG    1 
ATOM   2895 C  CD    . PRO B 1 64  ? -8.292  28.642  -38.715 1.00 36.27  ?  64  PRO B CD    1 
ATOM   2896 N  N     . SER B 1 65  ? -10.681 28.886  -36.365 1.00 33.90  ?  65  SER B N     1 
ATOM   2897 C  CA    . SER B 1 65  ? -11.545 28.431  -35.288 1.00 33.08  ?  65  SER B CA    1 
ATOM   2898 C  C     . SER B 1 65  ? -10.821 27.374  -34.467 1.00 28.28  ?  65  SER B C     1 
ATOM   2899 O  O     . SER B 1 65  ? -9.777  26.845  -34.858 1.00 26.67  ?  65  SER B O     1 
ATOM   2900 C  CB    . SER B 1 65  ? -12.874 27.873  -35.818 1.00 31.17  ?  65  SER B CB    1 
ATOM   2901 O  OG    . SER B 1 65  ? -12.668 27.023  -36.926 1.00 35.80  ?  65  SER B OG    1 
ATOM   2902 N  N     . GLN B 1 66  ? -11.392 27.068  -33.313 1.00 26.45  ?  66  GLN B N     1 
ATOM   2903 C  CA    . GLN B 1 66  ? -10.829 26.027  -32.473 1.00 28.39  ?  66  GLN B CA    1 
ATOM   2904 C  C     . GLN B 1 66  ? -10.995 24.673  -33.165 1.00 30.73  ?  66  GLN B C     1 
ATOM   2905 O  O     . GLN B 1 66  ? -12.055 24.378  -33.724 1.00 30.22  ?  66  GLN B O     1 
ATOM   2906 C  CB    . GLN B 1 66  ? -11.507 26.035  -31.109 1.00 26.72  ?  66  GLN B CB    1 
ATOM   2907 C  CG    . GLN B 1 66  ? -10.625 25.416  -30.062 1.00 30.05  ?  66  GLN B CG    1 
ATOM   2908 C  CD    . GLN B 1 66  ? -11.369 24.499  -29.150 1.00 30.11  ?  66  GLN B CD    1 
ATOM   2909 O  OE1   . GLN B 1 66  ? -12.132 24.945  -28.297 1.00 38.27  ?  66  GLN B OE1   1 
ATOM   2910 N  NE2   . GLN B 1 66  ? -11.162 23.193  -29.327 1.00 32.57  ?  66  GLN B NE2   1 
ATOM   2911 N  N     . SER B 1 67  ? -9.935  23.857  -33.173 1.00 23.00  ?  67  SER B N     1 
ATOM   2912 C  CA    . SER B 1 67  ? -9.997  22.591  -33.882 1.00 25.25  ?  67  SER B CA    1 
ATOM   2913 C  C     . SER B 1 67  ? -9.476  21.419  -33.069 1.00 28.60  ?  67  SER B C     1 
ATOM   2914 O  O     . SER B 1 67  ? -9.441  20.295  -33.592 1.00 28.45  ?  67  SER B O     1 
ATOM   2915 C  CB    . SER B 1 67  ? -9.219  22.675  -35.208 1.00 25.57  ?  67  SER B CB    1 
ATOM   2916 O  OG    . SER B 1 67  ? -7.885  23.118  -35.007 1.00 29.57  ?  67  SER B OG    1 
ATOM   2917 N  N     . GLY B 1 68  ? -9.058  21.645  -31.820 1.00 20.84  ?  68  GLY B N     1 
ATOM   2918 C  CA    . GLY B 1 68  ? -8.504  20.596  -30.991 1.00 20.58  ?  68  GLY B CA    1 
ATOM   2919 C  C     . GLY B 1 68  ? -7.048  20.294  -31.296 1.00 19.55  ?  68  GLY B C     1 
ATOM   2920 O  O     . GLY B 1 68  ? -6.507  20.701  -32.330 1.00 15.46  ?  68  GLY B O     1 
ATOM   2921 N  N     . PRO B 1 69  ? -6.394  19.550  -30.391 1.00 20.46  ?  69  PRO B N     1 
ATOM   2922 C  CA    . PRO B 1 69  ? -4.978  19.174  -30.600 1.00 20.81  ?  69  PRO B CA    1 
ATOM   2923 C  C     . PRO B 1 69  ? -4.682  18.521  -31.948 1.00 22.28  ?  69  PRO B C     1 
ATOM   2924 O  O     . PRO B 1 69  ? -3.665  18.849  -32.580 1.00 19.20  ?  69  PRO B O     1 
ATOM   2925 C  CB    . PRO B 1 69  ? -4.700  18.191  -29.448 1.00 21.24  ?  69  PRO B CB    1 
ATOM   2926 C  CG    . PRO B 1 69  ? -6.033  17.837  -28.876 1.00 24.03  ?  69  PRO B CG    1 
ATOM   2927 C  CD    . PRO B 1 69  ? -6.935  19.003  -29.137 1.00 23.50  ?  69  PRO B CD    1 
ATOM   2928 N  N     . SER B 1 70  ? -5.535  17.592  -32.397 1.00 19.26  ?  70  SER B N     1 
ATOM   2929 C  CA    . SER B 1 70  ? -5.343  16.974  -33.706 1.00 18.76  ?  70  SER B CA    1 
ATOM   2930 C  C     . SER B 1 70  ? -5.284  18.017  -34.817 1.00 22.55  ?  70  SER B C     1 
ATOM   2931 O  O     . SER B 1 70  ? -4.431  17.939  -35.716 1.00 18.98  ?  70  SER B O     1 
ATOM   2932 C  CB    . SER B 1 70  ? -6.461  15.975  -33.976 1.00 19.04  ?  70  SER B CB    1 
ATOM   2933 O  OG    . SER B 1 70  ? -6.264  14.756  -33.252 1.00 22.74  ?  70  SER B OG    1 
ATOM   2934 N  N     . GLY B 1 71  ? -6.186  18.999  -34.784 1.00 16.83  ?  71  GLY B N     1 
ATOM   2935 C  CA    . GLY B 1 71  ? -6.216  19.971  -35.861 1.00 19.20  ?  71  GLY B CA    1 
ATOM   2936 C  C     . GLY B 1 71  ? -5.048  20.929  -35.783 1.00 18.31  ?  71  GLY B C     1 
ATOM   2937 O  O     . GLY B 1 71  ? -4.471  21.307  -36.803 1.00 17.89  ?  71  GLY B O     1 
ATOM   2938 N  N     . ALA B 1 72  ? -4.676  21.323  -34.566 1.00 17.94  ?  72  ALA B N     1 
ATOM   2939 C  CA    . ALA B 1 72  ? -3.556  22.236  -34.406 1.00 19.51  ?  72  ALA B CA    1 
ATOM   2940 C  C     . ALA B 1 72  ? -2.260  21.586  -34.875 1.00 17.46  ?  72  ALA B C     1 
ATOM   2941 O  O     . ALA B 1 72  ? -1.522  22.164  -35.682 1.00 16.80  ?  72  ALA B O     1 
ATOM   2942 C  CB    . ALA B 1 72  ? -3.456  22.701  -32.949 1.00 14.18  ?  72  ALA B CB    1 
ATOM   2943 N  N     . ARG B 1 73  ? -1.977  20.374  -34.388 1.00 17.08  ?  73  ARG B N     1 
ATOM   2944 C  CA    . ARG B 1 73  ? -0.767  19.664  -34.796 1.00 15.41  ?  73  ARG B CA    1 
ATOM   2945 C  C     . ARG B 1 73  ? -0.734  19.456  -36.303 1.00 15.91  ?  73  ARG B C     1 
ATOM   2946 O  O     . ARG B 1 73  ? 0.303   19.662  -36.949 1.00 15.24  ?  73  ARG B O     1 
ATOM   2947 C  CB    . ARG B 1 73  ? -0.686  18.314  -34.082 1.00 15.22  ?  73  ARG B CB    1 
ATOM   2948 C  CG    . ARG B 1 73  ? -0.498  18.403  -32.589 1.00 20.07  ?  73  ARG B CG    1 
ATOM   2949 C  CD    . ARG B 1 73  ? -0.039  17.079  -32.020 1.00 17.96  ?  73  ARG B CD    1 
ATOM   2950 N  NE    . ARG B 1 73  ? 0.083   17.097  -30.571 1.00 16.07  ?  73  ARG B NE    1 
ATOM   2951 C  CZ    . ARG B 1 73  ? -0.858  16.660  -29.747 1.00 18.95  ?  73  ARG B CZ    1 
ATOM   2952 N  NH1   . ARG B 1 73  ? -2.003  16.170  -30.202 1.00 18.55  ?  73  ARG B NH1   1 
ATOM   2953 N  NH2   . ARG B 1 73  ? -0.647  16.716  -28.438 1.00 20.23  ?  73  ARG B NH2   1 
ATOM   2954 N  N     . ASN B 1 74  ? -1.861  19.032  -36.881 1.00 17.03  ?  74  ASN B N     1 
ATOM   2955 C  CA    . ASN B 1 74  ? -1.923  18.839  -38.323 1.00 15.13  ?  74  ASN B CA    1 
ATOM   2956 C  C     . ASN B 1 74  ? -1.569  20.114  -39.082 1.00 16.34  ?  74  ASN B C     1 
ATOM   2957 O  O     . ASN B 1 74  ? -0.951  20.043  -40.155 1.00 15.69  ?  74  ASN B O     1 
ATOM   2958 C  CB    . ASN B 1 74  ? -3.309  18.338  -38.721 1.00 14.73  ?  74  ASN B CB    1 
ATOM   2959 C  CG    . ASN B 1 74  ? -3.481  16.836  -38.488 1.00 18.00  ?  74  ASN B CG    1 
ATOM   2960 O  OD1   . ASN B 1 74  ? -2.542  16.144  -38.078 1.00 14.22  ?  74  ASN B OD1   1 
ATOM   2961 N  ND2   . ASN B 1 74  ? -4.682  16.328  -38.760 1.00 15.39  ?  74  ASN B ND2   1 
ATOM   2962 N  N     . ALA B 1 75  ? -1.931  21.283  -38.540 1.00 13.68  ?  75  ALA B N     1 
ATOM   2963 C  CA    . ALA B 1 75  ? -1.609  22.551  -39.198 1.00 13.02  ?  75  ALA B CA    1 
ATOM   2964 C  C     . ALA B 1 75  ? -0.108  22.804  -39.208 1.00 14.49  ?  75  ALA B C     1 
ATOM   2965 O  O     . ALA B 1 75  ? 0.420   23.388  -40.159 1.00 16.21  ?  75  ALA B O     1 
ATOM   2966 C  CB    . ALA B 1 75  ? -2.337  23.711  -38.505 1.00 15.99  ?  75  ALA B CB    1 
ATOM   2967 N  N     . GLY B 1 76  ? 0.591   22.387  -38.155 1.00 10.67  ?  76  GLY B N     1 
ATOM   2968 C  CA    . GLY B 1 76  ? 2.029   22.511  -38.124 1.00 14.19  ?  76  GLY B CA    1 
ATOM   2969 C  C     . GLY B 1 76  ? 2.704   21.447  -38.977 1.00 17.44  ?  76  GLY B C     1 
ATOM   2970 O  O     . GLY B 1 76  ? 3.701   21.727  -39.648 1.00 13.12  ?  76  GLY B O     1 
ATOM   2971 N  N     . LEU B 1 77  ? 2.171   20.220  -38.938 1.00 13.73  ?  77  LEU B N     1 
ATOM   2972 C  CA    . LEU B 1 77  ? 2.729   19.119  -39.724 1.00 15.20  ?  77  LEU B CA    1 
ATOM   2973 C  C     . LEU B 1 77  ? 2.720   19.439  -41.203 1.00 16.56  ?  77  LEU B C     1 
ATOM   2974 O  O     . LEU B 1 77  ? 3.650   19.079  -41.937 1.00 21.21  ?  77  LEU B O     1 
ATOM   2975 C  CB    . LEU B 1 77  ? 1.923   17.838  -39.484 1.00 11.07  ?  77  LEU B CB    1 
ATOM   2976 C  CG    . LEU B 1 77  ? 2.131   17.149  -38.152 1.00 11.30  ?  77  LEU B CG    1 
ATOM   2977 C  CD1   . LEU B 1 77  ? 1.316   15.814  -38.094 1.00 18.16  ?  77  LEU B CD1   1 
ATOM   2978 C  CD2   . LEU B 1 77  ? 3.612   16.908  -37.952 1.00 13.25  ?  77  LEU B CD2   1 
ATOM   2979 N  N     . GLU B 1 78  ? 1.659   20.090  -41.665 1.00 18.54  ?  78  GLU B N     1 
ATOM   2980 C  CA    . GLU B 1 78  ? 1.469   20.327  -43.088 1.00 26.19  ?  78  GLU B CA    1 
ATOM   2981 C  C     . GLU B 1 78  ? 2.467   21.340  -43.656 1.00 21.44  ?  78  GLU B C     1 
ATOM   2982 O  O     . GLU B 1 78  ? 2.748   21.313  -44.859 1.00 18.65  ?  78  GLU B O     1 
ATOM   2983 C  CB    . GLU B 1 78  ? 0.025   20.779  -43.295 1.00 24.32  ?  78  GLU B CB    1 
ATOM   2984 C  CG    . GLU B 1 78  ? -0.905  19.607  -43.453 1.00 28.16  ?  78  GLU B CG    1 
ATOM   2985 C  CD    . GLU B 1 78  ? -2.331  20.018  -43.710 1.00 41.32  ?  78  GLU B CD    1 
ATOM   2986 O  OE1   . GLU B 1 78  ? -2.537  21.042  -44.394 1.00 50.87  ?  78  GLU B OE1   1 
ATOM   2987 O  OE2   . GLU B 1 78  ? -3.247  19.325  -43.210 1.00 47.66  ?  78  GLU B OE2   1 
ATOM   2988 N  N     . VAL B 1 79  ? 3.020   22.211  -42.811 1.00 21.99  ?  79  VAL B N     1 
ATOM   2989 C  CA    . VAL B 1 79  ? 3.983   23.225  -43.227 1.00 25.10  ?  79  VAL B CA    1 
ATOM   2990 C  C     . VAL B 1 79  ? 5.398   22.931  -42.739 1.00 24.40  ?  79  VAL B C     1 
ATOM   2991 O  O     . VAL B 1 79  ? 6.336   23.660  -43.120 1.00 18.86  ?  79  VAL B O     1 
ATOM   2992 C  CB    . VAL B 1 79  ? 3.535   24.622  -42.753 1.00 25.43  ?  79  VAL B CB    1 
ATOM   2993 C  CG1   . VAL B 1 79  ? 2.088   24.867  -43.162 1.00 19.56  ?  79  VAL B CG1   1 
ATOM   2994 C  CG2   . VAL B 1 79  ? 3.657   24.720  -41.248 1.00 19.79  ?  79  VAL B CG2   1 
ATOM   2995 N  N     . ALA B 1 80  ? 5.587   21.889  -41.922 1.00 22.43  ?  80  ALA B N     1 
ATOM   2996 C  CA    . ALA B 1 80  ? 6.899   21.570  -41.372 1.00 20.64  ?  80  ALA B CA    1 
ATOM   2997 C  C     . ALA B 1 80  ? 7.842   21.094  -42.468 1.00 21.28  ?  80  ALA B C     1 
ATOM   2998 O  O     . ALA B 1 80  ? 7.495   20.210  -43.261 1.00 22.77  ?  80  ALA B O     1 
ATOM   2999 C  CB    . ALA B 1 80  ? 6.773   20.504  -40.286 1.00 18.83  ?  80  ALA B CB    1 
ATOM   3000 N  N     . ARG B 1 81  ? 9.044   21.674  -42.500 1.00 20.15  ?  81  ARG B N     1 
ATOM   3001 C  CA    . ARG B 1 81  ? 10.048  21.360  -43.511 1.00 22.02  ?  81  ARG B CA    1 
ATOM   3002 C  C     . ARG B 1 81  ? 11.082  20.338  -43.047 1.00 22.07  ?  81  ARG B C     1 
ATOM   3003 O  O     . ARG B 1 81  ? 11.863  19.847  -43.880 1.00 19.17  ?  81  ARG B O     1 
ATOM   3004 C  CB    . ARG B 1 81  ? 10.768  22.639  -43.952 1.00 18.00  ?  81  ARG B CB    1 
ATOM   3005 C  CG    . ARG B 1 81  ? 9.816   23.718  -44.460 1.00 28.75  ?  81  ARG B CG    1 
ATOM   3006 C  CD    . ARG B 1 81  ? 10.565  24.948  -44.955 1.00 34.07  ?  81  ARG B CD    1 
ATOM   3007 N  NE    . ARG B 1 81  ? 11.178  25.662  -43.839 1.00 45.13  ?  81  ARG B NE    1 
ATOM   3008 C  CZ    . ARG B 1 81  ? 10.784  26.847  -43.382 1.00 49.62  ?  81  ARG B CZ    1 
ATOM   3009 N  NH1   . ARG B 1 81  ? 9.806   27.524  -43.966 1.00 46.83  ?  81  ARG B NH1   1 
ATOM   3010 N  NH2   . ARG B 1 81  ? 11.390  27.366  -42.312 1.00 32.22  ?  81  ARG B NH2   1 
ATOM   3011 N  N     . GLY B 1 82  ? 11.089  19.990  -41.761 1.00 12.35  ?  82  GLY B N     1 
ATOM   3012 C  CA    . GLY B 1 82  ? 12.136  19.143  -41.233 1.00 9.98   ?  82  GLY B CA    1 
ATOM   3013 C  C     . GLY B 1 82  ? 12.056  17.726  -41.767 1.00 12.19  ?  82  GLY B C     1 
ATOM   3014 O  O     . GLY B 1 82  ? 10.990  17.215  -42.119 1.00 12.42  ?  82  GLY B O     1 
ATOM   3015 N  N     . GLU B 1 83  ? 13.216  17.080  -41.847 1.00 12.53  ?  83  GLU B N     1 
ATOM   3016 C  CA    . GLU B 1 83  ? 13.203  15.658  -42.151 1.00 12.49  ?  83  GLU B CA    1 
ATOM   3017 C  C     . GLU B 1 83  ? 12.567  14.901  -40.998 1.00 11.05  ?  83  GLU B C     1 
ATOM   3018 O  O     . GLU B 1 83  ? 11.812  13.950  -41.212 1.00 11.56  ?  83  GLU B O     1 
ATOM   3019 C  CB    . GLU B 1 83  ? 14.628  15.168  -42.437 1.00 13.68  ?  83  GLU B CB    1 
ATOM   3020 C  CG    . GLU B 1 83  ? 14.803  13.645  -42.462 1.00 11.84  ?  83  GLU B CG    1 
ATOM   3021 C  CD    . GLU B 1 83  ? 16.203  13.243  -42.890 1.00 17.71  ?  83  GLU B CD    1 
ATOM   3022 O  OE1   . GLU B 1 83  ? 17.139  14.048  -42.680 1.00 16.70  ?  83  GLU B OE1   1 
ATOM   3023 O  OE2   . GLU B 1 83  ? 16.376  12.113  -43.428 1.00 17.39  ?  83  GLU B OE2   1 
ATOM   3024 N  N     . TYR B 1 84  ? 12.821  15.370  -39.776 1.00 12.43  ?  84  TYR B N     1 
ATOM   3025 C  CA    . TYR B 1 84  ? 12.334  14.824  -38.521 1.00 11.55  ?  84  TYR B CA    1 
ATOM   3026 C  C     . TYR B 1 84  ? 11.499  15.866  -37.791 1.00 12.52  ?  84  TYR B C     1 
ATOM   3027 O  O     . TYR B 1 84  ? 11.767  17.072  -37.863 1.00 13.49  ?  84  TYR B O     1 
ATOM   3028 C  CB    . TYR B 1 84  ? 13.508  14.399  -37.641 1.00 11.71  ?  84  TYR B CB    1 
ATOM   3029 C  CG    . TYR B 1 84  ? 14.392  13.409  -38.338 1.00 12.57  ?  84  TYR B CG    1 
ATOM   3030 C  CD1   . TYR B 1 84  ? 13.982  12.091  -38.502 1.00 11.35  ?  84  TYR B CD1   1 
ATOM   3031 C  CD2   . TYR B 1 84  ? 15.615  13.793  -38.876 1.00 13.99  ?  84  TYR B CD2   1 
ATOM   3032 C  CE1   . TYR B 1 84  ? 14.776  11.167  -39.163 1.00 10.91  ?  84  TYR B CE1   1 
ATOM   3033 C  CE2   . TYR B 1 84  ? 16.423  12.878  -39.554 1.00 12.24  ?  84  TYR B CE2   1 
ATOM   3034 C  CZ    . TYR B 1 84  ? 15.995  11.563  -39.690 1.00 15.69  ?  84  TYR B CZ    1 
ATOM   3035 O  OH    . TYR B 1 84  ? 16.791  10.631  -40.360 1.00 17.39  ?  84  TYR B OH    1 
ATOM   3036 N  N     . VAL B 1 85  ? 10.493  15.390  -37.072 1.00 16.51  ?  85  VAL B N     1 
ATOM   3037 C  CA    . VAL B 1 85  ? 9.562   16.249  -36.362 1.00 12.34  ?  85  VAL B CA    1 
ATOM   3038 C  C     . VAL B 1 85  ? 9.598   15.892  -34.885 1.00 12.95  ?  85  VAL B C     1 
ATOM   3039 O  O     . VAL B 1 85  ? 9.487   14.716  -34.515 1.00 13.55  ?  85  VAL B O     1 
ATOM   3040 C  CB    . VAL B 1 85  ? 8.136   16.118  -36.919 1.00 15.37  ?  85  VAL B CB    1 
ATOM   3041 C  CG1   . VAL B 1 85  ? 7.124   16.690  -35.926 1.00 15.62  ?  85  VAL B CG1   1 
ATOM   3042 C  CG2   . VAL B 1 85  ? 8.048   16.819  -38.296 1.00 14.38  ?  85  VAL B CG2   1 
ATOM   3043 N  N     . ALA B 1 86  ? 9.748   16.908  -34.045 1.00 10.00  ?  86  ALA B N     1 
ATOM   3044 C  CA    . ALA B 1 86  ? 9.710   16.744  -32.605 1.00 11.71  ?  86  ALA B CA    1 
ATOM   3045 C  C     . ALA B 1 86  ? 8.487   17.483  -32.104 1.00 16.28  ?  86  ALA B C     1 
ATOM   3046 O  O     . ALA B 1 86  ? 8.304   18.659  -32.426 1.00 16.63  ?  86  ALA B O     1 
ATOM   3047 C  CB    . ALA B 1 86  ? 10.981  17.282  -31.948 1.00 10.40  ?  86  ALA B CB    1 
ATOM   3048 N  N     . PHE B 1 87  ? 7.628   16.785  -31.370 1.00 18.98  ?  87  PHE B N     1 
ATOM   3049 C  CA    . PHE B 1 87  ? 6.426   17.399  -30.831 1.00 16.15  ?  87  PHE B CA    1 
ATOM   3050 C  C     . PHE B 1 87  ? 6.702   17.964  -29.449 1.00 15.91  ?  87  PHE B C     1 
ATOM   3051 O  O     . PHE B 1 87  ? 7.544   17.459  -28.700 1.00 16.32  ?  87  PHE B O     1 
ATOM   3052 C  CB    . PHE B 1 87  ? 5.288   16.384  -30.762 1.00 16.97  ?  87  PHE B CB    1 
ATOM   3053 C  CG    . PHE B 1 87  ? 4.829   15.894  -32.099 1.00 16.07  ?  87  PHE B CG    1 
ATOM   3054 C  CD1   . PHE B 1 87  ? 3.996   16.669  -32.881 1.00 12.76  ?  87  PHE B CD1   1 
ATOM   3055 C  CD2   . PHE B 1 87  ? 5.224   14.645  -32.570 1.00 17.57  ?  87  PHE B CD2   1 
ATOM   3056 C  CE1   . PHE B 1 87  ? 3.562   16.214  -34.113 1.00 15.26  ?  87  PHE B CE1   1 
ATOM   3057 C  CE2   . PHE B 1 87  ? 4.793   14.182  -33.801 1.00 15.99  ?  87  PHE B CE2   1 
ATOM   3058 C  CZ    . PHE B 1 87  ? 3.960   14.969  -34.577 1.00 17.13  ?  87  PHE B CZ    1 
ATOM   3059 N  N     . LEU B 1 88  ? 5.990   19.026  -29.106 1.00 16.57  ?  88  LEU B N     1 
ATOM   3060 C  CA    . LEU B 1 88  ? 6.108   19.557  -27.755 1.00 15.20  ?  88  LEU B CA    1 
ATOM   3061 C  C     . LEU B 1 88  ? 4.789   20.218  -27.403 1.00 17.07  ?  88  LEU B C     1 
ATOM   3062 O  O     . LEU B 1 88  ? 4.400   21.201  -28.037 1.00 18.40  ?  88  LEU B O     1 
ATOM   3063 C  CB    . LEU B 1 88  ? 7.270   20.533  -27.644 1.00 18.06  ?  88  LEU B CB    1 
ATOM   3064 C  CG    . LEU B 1 88  ? 7.442   21.328  -26.346 1.00 19.89  ?  88  LEU B CG    1 
ATOM   3065 C  CD1   . LEU B 1 88  ? 7.844   20.413  -25.218 1.00 15.20  ?  88  LEU B CD1   1 
ATOM   3066 C  CD2   . LEU B 1 88  ? 8.512   22.401  -26.595 1.00 20.60  ?  88  LEU B CD2   1 
ATOM   3067 N  N     . ASP B 1 89  ? 4.091   19.658  -26.420 1.00 15.01  ?  89  ASP B N     1 
ATOM   3068 C  CA    . ASP B 1 89  ? 2.921   20.335  -25.889 1.00 15.35  ?  89  ASP B CA    1 
ATOM   3069 C  C     . ASP B 1 89  ? 3.357   21.564  -25.112 1.00 17.51  ?  89  ASP B C     1 
ATOM   3070 O  O     . ASP B 1 89  ? 4.424   21.588  -24.488 1.00 16.08  ?  89  ASP B O     1 
ATOM   3071 C  CB    . ASP B 1 89  ? 2.106   19.404  -24.991 1.00 16.90  ?  89  ASP B CB    1 
ATOM   3072 C  CG    . ASP B 1 89  ? 1.465   18.260  -25.759 1.00 21.20  ?  89  ASP B CG    1 
ATOM   3073 O  OD1   . ASP B 1 89  ? 1.578   18.225  -27.008 1.00 23.05  ?  89  ASP B OD1   1 
ATOM   3074 O  OD2   . ASP B 1 89  ? 0.844   17.391  -25.106 1.00 30.69  ?  89  ASP B OD2   1 
ATOM   3075 N  N     . ASP B 1 90  ? 2.509   22.593  -25.136 1.00 19.46  ?  90  ASP B N     1 
ATOM   3076 C  CA    . ASP B 1 90  ? 2.906   23.871  -24.556 1.00 17.43  ?  90  ASP B CA    1 
ATOM   3077 C  C     . ASP B 1 90  ? 3.027   23.857  -23.023 1.00 19.22  ?  90  ASP B C     1 
ATOM   3078 O  O     . ASP B 1 90  ? 3.531   24.833  -22.459 1.00 19.15  ?  90  ASP B O     1 
ATOM   3079 C  CB    . ASP B 1 90  ? 1.949   24.960  -25.069 1.00 18.17  ?  90  ASP B CB    1 
ATOM   3080 C  CG    . ASP B 1 90  ? 0.537   24.847  -24.513 1.00 24.71  ?  90  ASP B CG    1 
ATOM   3081 O  OD1   . ASP B 1 90  ? -0.246  25.808  -24.719 1.00 22.71  ?  90  ASP B OD1   1 
ATOM   3082 O  OD2   . ASP B 1 90  ? 0.199   23.815  -23.883 1.00 25.83  ?  90  ASP B OD2   1 
ATOM   3083 N  N     . ASP B 1 91  ? 2.663   22.770  -22.338 1.00 13.22  ?  91  ASP B N     1 
ATOM   3084 C  CA    . ASP B 1 91  ? 2.812   22.699  -20.887 1.00 21.49  ?  91  ASP B CA    1 
ATOM   3085 C  C     . ASP B 1 91  ? 3.881   21.696  -20.446 1.00 25.25  ?  91  ASP B C     1 
ATOM   3086 O  O     . ASP B 1 91  ? 3.901   21.299  -19.270 1.00 24.46  ?  91  ASP B O     1 
ATOM   3087 C  CB    . ASP B 1 91  ? 1.469   22.377  -20.208 1.00 13.02  ?  91  ASP B CB    1 
ATOM   3088 C  CG    . ASP B 1 91  ? 0.824   21.104  -20.737 1.00 20.15  ?  91  ASP B CG    1 
ATOM   3089 O  OD1   . ASP B 1 91  ? 1.232   20.631  -21.819 1.00 28.06  ?  91  ASP B OD1   1 
ATOM   3090 O  OD2   . ASP B 1 91  ? -0.079  20.544  -20.066 1.00 26.89  ?  91  ASP B OD2   1 
ATOM   3091 N  N     . ASP B 1 92  ? 4.767   21.292  -21.360 1.00 18.76  ?  92  ASP B N     1 
ATOM   3092 C  CA    . ASP B 1 92  ? 5.877   20.371  -21.129 1.00 23.33  ?  92  ASP B CA    1 
ATOM   3093 C  C     . ASP B 1 92  ? 7.191   21.039  -21.536 1.00 23.59  ?  92  ASP B C     1 
ATOM   3094 O  O     . ASP B 1 92  ? 7.203   22.125  -22.119 1.00 16.65  ?  92  ASP B O     1 
ATOM   3095 C  CB    . ASP B 1 92  ? 5.694   19.060  -21.920 1.00 18.22  ?  92  ASP B CB    1 
ATOM   3096 C  CG    . ASP B 1 92  ? 4.455   18.281  -21.507 1.00 24.97  ?  92  ASP B CG    1 
ATOM   3097 O  OD1   . ASP B 1 92  ? 4.046   18.363  -20.324 1.00 27.97  ?  92  ASP B OD1   1 
ATOM   3098 O  OD2   . ASP B 1 92  ? 3.869   17.589  -22.371 1.00 24.66  ?  92  ASP B OD2   1 
ATOM   3099 N  N     . VAL B 1 93  ? 8.318   20.390  -21.224 1.00 18.23  ?  93  VAL B N     1 
ATOM   3100 C  CA    . VAL B 1 93  ? 9.630   20.952  -21.529 1.00 21.02  ?  93  VAL B CA    1 
ATOM   3101 C  C     . VAL B 1 93  ? 10.567  19.846  -21.996 1.00 19.23  ?  93  VAL B C     1 
ATOM   3102 O  O     . VAL B 1 93  ? 10.530  18.728  -21.469 1.00 15.51  ?  93  VAL B O     1 
ATOM   3103 C  CB    . VAL B 1 93  ? 10.260  21.694  -20.326 1.00 19.56  ?  93  VAL B CB    1 
ATOM   3104 C  CG1   . VAL B 1 93  ? 9.528   22.993  -20.033 1.00 18.50  ?  93  VAL B CG1   1 
ATOM   3105 C  CG2   . VAL B 1 93  ? 10.334  20.809  -19.115 1.00 18.87  ?  93  VAL B CG2   1 
ATOM   3106 N  N     . PHE B 1 94  ? 11.411  20.173  -22.985 1.00 19.98  ?  94  PHE B N     1 
ATOM   3107 C  CA    . PHE B 1 94  ? 12.518  19.314  -23.411 1.00 18.71  ?  94  PHE B CA    1 
ATOM   3108 C  C     . PHE B 1 94  ? 13.687  19.434  -22.441 1.00 21.54  ?  94  PHE B C     1 
ATOM   3109 O  O     . PHE B 1 94  ? 13.928  20.495  -21.854 1.00 20.77  ?  94  PHE B O     1 
ATOM   3110 C  CB    . PHE B 1 94  ? 13.060  19.714  -24.790 1.00 18.61  ?  94  PHE B CB    1 
ATOM   3111 C  CG    . PHE B 1 94  ? 12.132  19.454  -25.944 1.00 18.63  ?  94  PHE B CG    1 
ATOM   3112 C  CD1   . PHE B 1 94  ? 11.144  18.479  -25.879 1.00 15.83  ?  94  PHE B CD1   1 
ATOM   3113 C  CD2   . PHE B 1 94  ? 12.270  20.195  -27.112 1.00 12.62  ?  94  PHE B CD2   1 
ATOM   3114 C  CE1   . PHE B 1 94  ? 10.305  18.257  -26.964 1.00 12.57  ?  94  PHE B CE1   1 
ATOM   3115 C  CE2   . PHE B 1 94  ? 11.436  19.985  -28.188 1.00 12.94  ?  94  PHE B CE2   1 
ATOM   3116 C  CZ    . PHE B 1 94  ? 10.460  19.017  -28.119 1.00 13.93  ?  94  PHE B CZ    1 
ATOM   3117 N  N     . SER B 1 95  ? 14.438  18.350  -22.307 1.00 21.16  ?  95  SER B N     1 
ATOM   3118 C  CA    . SER B 1 95  ? 15.758  18.438  -21.702 1.00 24.56  ?  95  SER B CA    1 
ATOM   3119 C  C     . SER B 1 95  ? 16.737  18.944  -22.748 1.00 19.97  ?  95  SER B C     1 
ATOM   3120 O  O     . SER B 1 95  ? 16.440  18.913  -23.939 1.00 22.40  ?  95  SER B O     1 
ATOM   3121 C  CB    . SER B 1 95  ? 16.206  17.073  -21.179 1.00 25.00  ?  95  SER B CB    1 
ATOM   3122 O  OG    . SER B 1 95  ? 16.925  16.348  -22.176 1.00 27.25  ?  95  SER B OG    1 
ATOM   3123 N  N     . PRO B 1 96  ? 17.910  19.427  -22.336 1.00 20.72  ?  96  PRO B N     1 
ATOM   3124 C  CA    . PRO B 1 96  ? 18.859  19.957  -23.326 1.00 20.56  ?  96  PRO B CA    1 
ATOM   3125 C  C     . PRO B 1 96  ? 19.401  18.920  -24.303 1.00 23.36  ?  96  PRO B C     1 
ATOM   3126 O  O     . PRO B 1 96  ? 19.952  19.309  -25.342 1.00 20.28  ?  96  PRO B O     1 
ATOM   3127 C  CB    . PRO B 1 96  ? 19.975  20.548  -22.454 1.00 22.71  ?  96  PRO B CB    1 
ATOM   3128 C  CG    . PRO B 1 96  ? 19.275  20.899  -21.166 1.00 24.39  ?  96  PRO B CG    1 
ATOM   3129 C  CD    . PRO B 1 96  ? 18.318  19.760  -20.957 1.00 19.16  ?  96  PRO B CD    1 
ATOM   3130 N  N     . GLN B 1 97  ? 19.257  17.623  -24.022 1.00 23.05  ?  97  GLN B N     1 
ATOM   3131 C  CA    . GLN B 1 97  ? 19.715  16.564  -24.917 1.00 24.62  ?  97  GLN B CA    1 
ATOM   3132 C  C     . GLN B 1 97  ? 18.585  15.956  -25.742 1.00 20.96  ?  97  GLN B C     1 
ATOM   3133 O  O     . GLN B 1 97  ? 18.755  14.861  -26.287 1.00 17.88  ?  97  GLN B O     1 
ATOM   3134 C  CB    . GLN B 1 97  ? 20.420  15.453  -24.132 1.00 21.77  ?  97  GLN B CB    1 
ATOM   3135 C  CG    . GLN B 1 97  ? 21.617  15.905  -23.310 1.00 20.24  ?  97  GLN B CG    1 
ATOM   3136 C  CD    . GLN B 1 97  ? 21.191  16.571  -22.023 1.00 34.04  ?  97  GLN B CD    1 
ATOM   3137 O  OE1   . GLN B 1 97  ? 21.672  17.655  -21.683 1.00 33.86  ?  97  GLN B OE1   1 
ATOM   3138 N  NE2   . GLN B 1 97  ? 20.251  15.941  -21.308 1.00 32.67  ?  97  GLN B NE2   1 
ATOM   3139 N  N     . HIS B 1 98  ? 17.435  16.637  -25.841 1.00 21.22  ?  98  HIS B N     1 
ATOM   3140 C  CA    . HIS B 1 98  ? 16.280  16.031  -26.500 1.00 21.05  ?  98  HIS B CA    1 
ATOM   3141 C  C     . HIS B 1 98  ? 16.602  15.618  -27.927 1.00 16.33  ?  98  HIS B C     1 
ATOM   3142 O  O     . HIS B 1 98  ? 16.177  14.551  -28.383 1.00 14.34  ?  98  HIS B O     1 
ATOM   3143 C  CB    . HIS B 1 98  ? 15.087  16.981  -26.508 1.00 14.46  ?  98  HIS B CB    1 
ATOM   3144 C  CG    . HIS B 1 98  ? 13.786  16.301  -26.817 1.00 17.76  ?  98  HIS B CG    1 
ATOM   3145 N  ND1   . HIS B 1 98  ? 13.295  15.258  -26.057 1.00 13.87  ?  98  HIS B ND1   1 
ATOM   3146 C  CD2   . HIS B 1 98  ? 12.878  16.508  -27.802 1.00 15.57  ?  98  HIS B CD2   1 
ATOM   3147 C  CE1   . HIS B 1 98  ? 12.139  14.857  -26.559 1.00 13.56  ?  98  HIS B CE1   1 
ATOM   3148 N  NE2   . HIS B 1 98  ? 11.858  15.602  -27.612 1.00 10.38  ?  98  HIS B NE2   1 
ATOM   3149 N  N     . LEU B 1 99  ? 17.304  16.469  -28.661 1.00 19.79  ?  99  LEU B N     1 
ATOM   3150 C  CA    . LEU B 1 99  ? 17.630  16.143  -30.043 1.00 21.08  ?  99  LEU B CA    1 
ATOM   3151 C  C     . LEU B 1 99  ? 18.975  15.452  -30.157 1.00 19.48  ?  99  LEU B C     1 
ATOM   3152 O  O     . LEU B 1 99  ? 19.099  14.465  -30.887 1.00 23.90  ?  99  LEU B O     1 
ATOM   3153 C  CB    . LEU B 1 99  ? 17.606  17.406  -30.903 1.00 21.08  ?  99  LEU B CB    1 
ATOM   3154 C  CG    . LEU B 1 99  ? 16.230  18.067  -30.890 1.00 22.46  ?  99  LEU B CG    1 
ATOM   3155 C  CD1   . LEU B 1 99  ? 16.255  19.395  -31.619 1.00 20.43  ?  99  LEU B CD1   1 
ATOM   3156 C  CD2   . LEU B 1 99  ? 15.188  17.104  -31.483 1.00 17.67  ?  99  LEU B CD2   1 
ATOM   3157 N  N     . SER B 1 100 ? 19.977  15.933  -29.419 1.00 18.50  ?  100 SER B N     1 
ATOM   3158 C  CA    . SER B 1 100 ? 21.299  15.324  -29.494 1.00 27.22  ?  100 SER B CA    1 
ATOM   3159 C  C     . SER B 1 100 ? 21.255  13.856  -29.086 1.00 23.95  ?  100 SER B C     1 
ATOM   3160 O  O     . SER B 1 100 ? 22.047  13.048  -29.587 1.00 19.84  ?  100 SER B O     1 
ATOM   3161 C  CB    . SER B 1 100 ? 22.295  16.104  -28.624 1.00 29.52  ?  100 SER B CB    1 
ATOM   3162 O  OG    . SER B 1 100 ? 21.978  15.987  -27.235 1.00 28.40  ?  100 SER B OG    1 
ATOM   3163 N  N     . GLY B 1 101 ? 20.317  13.489  -28.212 1.00 22.57  ?  101 GLY B N     1 
ATOM   3164 C  CA    . GLY B 1 101 ? 20.123  12.108  -27.825 1.00 21.22  ?  101 GLY B CA    1 
ATOM   3165 C  C     . GLY B 1 101 ? 19.181  11.287  -28.693 1.00 22.67  ?  101 GLY B C     1 
ATOM   3166 O  O     . GLY B 1 101 ? 19.093  10.070  -28.491 1.00 21.90  ?  101 GLY B O     1 
ATOM   3167 N  N     . THR B 1 102 ? 18.449  11.901  -29.637 1.00 17.48  ?  102 THR B N     1 
ATOM   3168 C  CA    . THR B 1 102 ? 17.523  11.143  -30.475 1.00 19.14  ?  102 THR B CA    1 
ATOM   3169 C  C     . THR B 1 102 ? 17.872  11.131  -31.953 1.00 18.64  ?  102 THR B C     1 
ATOM   3170 O  O     . THR B 1 102 ? 17.597  10.132  -32.628 1.00 15.72  ?  102 THR B O     1 
ATOM   3171 C  CB    . THR B 1 102 ? 16.102  11.685  -30.346 1.00 17.37  ?  102 THR B CB    1 
ATOM   3172 O  OG1   . THR B 1 102 ? 16.102  13.075  -30.679 1.00 15.24  ?  102 THR B OG1   1 
ATOM   3173 C  CG2   . THR B 1 102 ? 15.590  11.491  -28.928 1.00 17.38  ?  102 THR B CG2   1 
ATOM   3174 N  N     . LEU B 1 103 ? 18.441  12.216  -32.475 1.00 15.94  ?  103 LEU B N     1 
ATOM   3175 C  CA    . LEU B 1 103 ? 18.717  12.293  -33.907 1.00 20.50  ?  103 LEU B CA    1 
ATOM   3176 C  C     . LEU B 1 103 ? 19.674  11.225  -34.414 1.00 14.78  ?  103 LEU B C     1 
ATOM   3177 O  O     . LEU B 1 103 ? 19.420  10.697  -35.507 1.00 16.24  ?  103 LEU B O     1 
ATOM   3178 C  CB    . LEU B 1 103 ? 19.242  13.692  -34.260 1.00 15.99  ?  103 LEU B CB    1 
ATOM   3179 C  CG    . LEU B 1 103 ? 18.126  14.701  -34.536 1.00 18.03  ?  103 LEU B CG    1 
ATOM   3180 C  CD1   . LEU B 1 103 ? 18.752  16.021  -34.846 1.00 25.29  ?  103 LEU B CD1   1 
ATOM   3181 C  CD2   . LEU B 1 103 ? 17.220  14.276  -35.701 1.00 19.07  ?  103 LEU B CD2   1 
ATOM   3182 N  N     . PRO B 1 104 ? 20.768  10.866  -33.723 1.00 15.84  ?  104 PRO B N     1 
ATOM   3183 C  CA    . PRO B 1 104 ? 21.622  9.798   -34.271 1.00 15.57  ?  104 PRO B CA    1 
ATOM   3184 C  C     . PRO B 1 104 ? 20.874  8.491   -34.487 1.00 18.33  ?  104 PRO B C     1 
ATOM   3185 O  O     . PRO B 1 104 ? 21.164  7.787   -35.462 1.00 15.61  ?  104 PRO B O     1 
ATOM   3186 C  CB    . PRO B 1 104 ? 22.731  9.655   -33.218 1.00 20.99  ?  104 PRO B CB    1 
ATOM   3187 C  CG    . PRO B 1 104 ? 22.718  10.903  -32.432 1.00 14.49  ?  104 PRO B CG    1 
ATOM   3188 C  CD    . PRO B 1 104 ? 21.286  11.358  -32.430 1.00 20.22  ?  104 PRO B CD    1 
ATOM   3189 N  N     . LEU B 1 105 ? 19.905  8.159   -33.610 1.00 15.30  ?  105 LEU B N     1 
ATOM   3190 C  CA    . LEU B 1 105 ? 19.076  6.965   -33.789 1.00 15.65  ?  105 LEU B CA    1 
ATOM   3191 C  C     . LEU B 1 105 ? 18.200  7.057   -35.035 1.00 17.24  ?  105 LEU B C     1 
ATOM   3192 O  O     . LEU B 1 105 ? 18.033  6.068   -35.762 1.00 13.80  ?  105 LEU B O     1 
ATOM   3193 C  CB    . LEU B 1 105 ? 18.188  6.753   -32.564 1.00 18.63  ?  105 LEU B CB    1 
ATOM   3194 C  CG    . LEU B 1 105 ? 18.865  6.184   -31.327 1.00 26.21  ?  105 LEU B CG    1 
ATOM   3195 C  CD1   . LEU B 1 105 ? 17.856  6.118   -30.164 1.00 20.83  ?  105 LEU B CD1   1 
ATOM   3196 C  CD2   . LEU B 1 105 ? 19.450  4.807   -31.658 1.00 14.60  ?  105 LEU B CD2   1 
ATOM   3197 N  N     . LEU B 1 106 ? 17.583  8.221   -35.260 1.00 13.85  ?  106 LEU B N     1 
ATOM   3198 C  CA    . LEU B 1 106 ? 16.759  8.416   -36.450 1.00 14.32  ?  106 LEU B CA    1 
ATOM   3199 C  C     . LEU B 1 106 ? 17.606  8.491   -37.720 1.00 15.11  ?  106 LEU B C     1 
ATOM   3200 O  O     . LEU B 1 106 ? 17.202  7.972   -38.776 1.00 10.30  ?  106 LEU B O     1 
ATOM   3201 C  CB    . LEU B 1 106 ? 15.942  9.689   -36.302 1.00 13.39  ?  106 LEU B CB    1 
ATOM   3202 C  CG    . LEU B 1 106 ? 14.909  9.674   -35.165 1.00 14.51  ?  106 LEU B CG    1 
ATOM   3203 C  CD1   . LEU B 1 106 ? 14.643  11.097  -34.724 1.00 11.65  ?  106 LEU B CD1   1 
ATOM   3204 C  CD2   . LEU B 1 106 ? 13.631  8.991   -35.595 1.00 11.56  ?  106 LEU B CD2   1 
ATOM   3205 N  N     . LYS B 1 107 ? 18.752  9.185   -37.651 1.00 10.57  ?  107 LYS B N     1 
ATOM   3206 C  CA    . LYS B 1 107 ? 19.667  9.218   -38.791 1.00 15.01  ?  107 LYS B CA    1 
ATOM   3207 C  C     . LYS B 1 107 ? 20.157  7.811   -39.081 1.00 15.16  ?  107 LYS B C     1 
ATOM   3208 O  O     . LYS B 1 107 ? 20.221  7.393   -40.241 1.00 14.33  ?  107 LYS B O     1 
ATOM   3209 C  CB    . LYS B 1 107 ? 20.858  10.149  -38.519 1.00 8.93   ?  107 LYS B CB    1 
ATOM   3210 C  CG    . LYS B 1 107 ? 20.510  11.629  -38.612 1.00 16.78  ?  107 LYS B CG    1 
ATOM   3211 C  CD    . LYS B 1 107 ? 21.420  12.508  -37.756 1.00 25.95  ?  107 LYS B CD    1 
ATOM   3212 C  CE    . LYS B 1 107 ? 21.831  13.781  -38.507 1.00 24.89  ?  107 LYS B CE    1 
ATOM   3213 N  NZ    . LYS B 1 107 ? 22.967  14.537  -37.861 1.00 26.74  ?  107 LYS B NZ    1 
ATOM   3214 N  N     . GLY B 1 108 ? 20.440  7.051   -38.021 1.00 14.24  ?  108 GLY B N     1 
ATOM   3215 C  CA    . GLY B 1 108 ? 20.839  5.658   -38.097 1.00 19.73  ?  108 GLY B CA    1 
ATOM   3216 C  C     . GLY B 1 108 ? 19.778  4.722   -38.636 1.00 17.19  ?  108 GLY B C     1 
ATOM   3217 O  O     . GLY B 1 108 ? 20.080  3.544   -38.853 1.00 22.21  ?  108 GLY B O     1 
ATOM   3218 N  N     . GLY B 1 109 ? 18.559  5.203   -38.872 1.00 14.62  ?  109 GLY B N     1 
ATOM   3219 C  CA    . GLY B 1 109 ? 17.528  4.384   -39.490 1.00 13.42  ?  109 GLY B CA    1 
ATOM   3220 C  C     . GLY B 1 109 ? 16.300  4.085   -38.634 1.00 18.89  ?  109 GLY B C     1 
ATOM   3221 O  O     . GLY B 1 109 ? 15.410  3.368   -39.110 1.00 17.17  ?  109 GLY B O     1 
ATOM   3222 N  N     . ALA B 1 110 ? 16.170  4.573   -37.405 1.00 15.34  ?  110 ALA B N     1 
ATOM   3223 C  CA    . ALA B 1 110 ? 14.862  4.510   -36.755 1.00 16.30  ?  110 ALA B CA    1 
ATOM   3224 C  C     . ALA B 1 110 ? 13.936  5.526   -37.408 1.00 13.90  ?  110 ALA B C     1 
ATOM   3225 O  O     . ALA B 1 110 ? 14.382  6.508   -38.015 1.00 14.07  ?  110 ALA B O     1 
ATOM   3226 C  CB    . ALA B 1 110 ? 14.969  4.784   -35.254 1.00 10.29  ?  110 ALA B CB    1 
ATOM   3227 N  N     . ASP B 1 111 ? 12.639  5.252   -37.348 1.00 10.00  ?  111 ASP B N     1 
ATOM   3228 C  CA    . ASP B 1 111 ? 11.668  6.215   -37.844 1.00 11.91  ?  111 ASP B CA    1 
ATOM   3229 C  C     . ASP B 1 111 ? 10.946  6.956   -36.730 1.00 11.21  ?  111 ASP B C     1 
ATOM   3230 O  O     . ASP B 1 111 ? 10.364  8.014   -36.986 1.00 8.68   ?  111 ASP B O     1 
ATOM   3231 C  CB    . ASP B 1 111 ? 10.618  5.538   -38.735 1.00 11.11  ?  111 ASP B CB    1 
ATOM   3232 C  CG    . ASP B 1 111 ? 11.224  4.757   -39.893 1.00 17.92  ?  111 ASP B CG    1 
ATOM   3233 O  OD1   . ASP B 1 111 ? 12.110  5.279   -40.638 1.00 19.58  ?  111 ASP B OD1   1 
ATOM   3234 O  OD2   . ASP B 1 111 ? 10.772  3.614   -40.087 1.00 13.07  ?  111 ASP B OD2   1 
ATOM   3235 N  N     . PHE B 1 112 ? 10.970  6.429   -35.515 1.00 14.71  ?  112 PHE B N     1 
ATOM   3236 C  CA    . PHE B 1 112 ? 10.153  6.936   -34.413 1.00 11.16  ?  112 PHE B CA    1 
ATOM   3237 C  C     . PHE B 1 112 ? 10.955  6.678   -33.151 1.00 11.92  ?  112 PHE B C     1 
ATOM   3238 O  O     . PHE B 1 112 ? 11.292  5.523   -32.877 1.00 14.26  ?  112 PHE B O     1 
ATOM   3239 C  CB    . PHE B 1 112 ? 8.810   6.208   -34.399 1.00 15.03  ?  112 PHE B CB    1 
ATOM   3240 C  CG    . PHE B 1 112 ? 7.812   6.686   -33.344 1.00 14.62  ?  112 PHE B CG    1 
ATOM   3241 C  CD1   . PHE B 1 112 ? 8.091   6.606   -31.997 1.00 14.91  ?  112 PHE B CD1   1 
ATOM   3242 C  CD2   . PHE B 1 112 ? 6.571   7.150   -33.732 1.00 15.49  ?  112 PHE B CD2   1 
ATOM   3243 C  CE1   . PHE B 1 112 ? 7.156   7.013   -31.050 1.00 22.37  ?  112 PHE B CE1   1 
ATOM   3244 C  CE2   . PHE B 1 112 ? 5.629   7.556   -32.801 1.00 20.93  ?  112 PHE B CE2   1 
ATOM   3245 C  CZ    . PHE B 1 112 ? 5.923   7.486   -31.458 1.00 19.11  ?  112 PHE B CZ    1 
ATOM   3246 N  N     . VAL B 1 113 ? 11.321  7.734   -32.426 1.00 10.65  ?  113 VAL B N     1 
ATOM   3247 C  CA    . VAL B 1 113 ? 12.025  7.599   -31.152 1.00 12.66  ?  113 VAL B CA    1 
ATOM   3248 C  C     . VAL B 1 113 ? 11.147  8.202   -30.070 1.00 16.08  ?  113 VAL B C     1 
ATOM   3249 O  O     . VAL B 1 113 ? 10.715  9.357   -30.194 1.00 14.66  ?  113 VAL B O     1 
ATOM   3250 C  CB    . VAL B 1 113 ? 13.405  8.290   -31.162 1.00 16.32  ?  113 VAL B CB    1 
ATOM   3251 C  CG1   . VAL B 1 113 ? 14.066  8.174   -29.786 1.00 15.78  ?  113 VAL B CG1   1 
ATOM   3252 C  CG2   . VAL B 1 113 ? 14.319  7.704   -32.242 1.00 17.49  ?  113 VAL B CG2   1 
ATOM   3253 N  N     . TYR B 1 114 ? 10.879  7.434   -29.013 1.00 12.49  ?  114 TYR B N     1 
ATOM   3254 C  CA    . TYR B 1 114 ? 10.249  7.986   -27.818 1.00 15.21  ?  114 TYR B CA    1 
ATOM   3255 C  C     . TYR B 1 114 ? 11.218  7.901   -26.643 1.00 16.83  ?  114 TYR B C     1 
ATOM   3256 O  O     . TYR B 1 114 ? 11.995  6.949   -26.532 1.00 15.21  ?  114 TYR B O     1 
ATOM   3257 C  CB    . TYR B 1 114 ? 8.916   7.297   -27.504 1.00 15.16  ?  114 TYR B CB    1 
ATOM   3258 C  CG    . TYR B 1 114 ? 8.990   5.877   -27.004 1.00 14.59  ?  114 TYR B CG    1 
ATOM   3259 C  CD1   . TYR B 1 114 ? 9.023   4.800   -27.887 1.00 16.94  ?  114 TYR B CD1   1 
ATOM   3260 C  CD2   . TYR B 1 114 ? 8.998   5.608   -25.646 1.00 18.11  ?  114 TYR B CD2   1 
ATOM   3261 C  CE1   . TYR B 1 114 ? 9.078   3.486   -27.416 1.00 17.77  ?  114 TYR B CE1   1 
ATOM   3262 C  CE2   . TYR B 1 114 ? 9.056   4.314   -25.168 1.00 16.91  ?  114 TYR B CE2   1 
ATOM   3263 C  CZ    . TYR B 1 114 ? 9.095   3.256   -26.051 1.00 19.06  ?  114 TYR B CZ    1 
ATOM   3264 O  OH    . TYR B 1 114 ? 9.162   1.973   -25.550 1.00 18.98  ?  114 TYR B OH    1 
ATOM   3265 N  N     . VAL B 1 115 ? 11.210  8.930   -25.796 1.00 17.05  ?  115 VAL B N     1 
ATOM   3266 C  CA    . VAL B 1 115 ? 12.167  8.998   -24.693 1.00 17.04  ?  115 VAL B CA    1 
ATOM   3267 C  C     . VAL B 1 115 ? 11.476  8.779   -23.344 1.00 18.19  ?  115 VAL B C     1 
ATOM   3268 O  O     . VAL B 1 115 ? 10.261  8.542   -23.278 1.00 14.18  ?  115 VAL B O     1 
ATOM   3269 C  CB    . VAL B 1 115 ? 12.941  10.329  -24.734 1.00 20.02  ?  115 VAL B CB    1 
ATOM   3270 C  CG1   . VAL B 1 115 ? 13.590  10.523  -26.129 1.00 12.11  ?  115 VAL B CG1   1 
ATOM   3271 C  CG2   . VAL B 1 115 ? 12.050  11.509  -24.383 1.00 13.59  ?  115 VAL B CG2   1 
ATOM   3272 N  N     . ASN B 1 116 ? 12.256  8.798   -22.267 1.00 15.02  ?  116 ASN B N     1 
ATOM   3273 C  CA    . ASN B 1 116 ? 11.693  8.595   -20.944 1.00 20.36  ?  116 ASN B CA    1 
ATOM   3274 C  C     . ASN B 1 116 ? 10.894  9.833   -20.533 1.00 21.04  ?  116 ASN B C     1 
ATOM   3275 O  O     . ASN B 1 116 ? 11.109  10.935  -21.051 1.00 22.70  ?  116 ASN B O     1 
ATOM   3276 C  CB    . ASN B 1 116 ? 12.806  8.309   -19.935 1.00 20.41  ?  116 ASN B CB    1 
ATOM   3277 C  CG    . ASN B 1 116 ? 13.161  6.835   -19.843 1.00 20.50  ?  116 ASN B CG    1 
ATOM   3278 O  OD1   . ASN B 1 116 ? 12.570  5.988   -20.527 1.00 19.20  ?  116 ASN B OD1   1 
ATOM   3279 N  ND2   . ASN B 1 116 ? 14.150  6.519   -18.996 1.00 15.01  ?  116 ASN B ND2   1 
ATOM   3280 N  N     . ILE B 1 117 ? 9.964   9.653   -19.593 1.00 16.46  ?  117 ILE B N     1 
ATOM   3281 C  CA    . ILE B 1 117 ? 9.027   10.713  -19.226 1.00 22.26  ?  117 ILE B CA    1 
ATOM   3282 C  C     . ILE B 1 117 ? 9.010   10.870  -17.714 1.00 24.98  ?  117 ILE B C     1 
ATOM   3283 O  O     . ILE B 1 117 ? 8.532   9.978   -17.000 1.00 25.24  ?  117 ILE B O     1 
ATOM   3284 C  CB    . ILE B 1 117 ? 7.602   10.448  -19.730 1.00 21.43  ?  117 ILE B CB    1 
ATOM   3285 C  CG1   . ILE B 1 117 ? 7.538   10.344  -21.253 1.00 18.26  ?  117 ILE B CG1   1 
ATOM   3286 C  CG2   . ILE B 1 117 ? 6.697   11.560  -19.260 1.00 20.07  ?  117 ILE B CG2   1 
ATOM   3287 C  CD1   . ILE B 1 117 ? 6.160   9.982   -21.758 1.00 12.86  ?  117 ILE B CD1   1 
ATOM   3288 N  N     . ASN B 1 118 ? 9.470   12.016  -17.227 1.00 24.01  ?  118 ASN B N     1 
ATOM   3289 C  CA    . ASN B 1 118 ? 9.275   12.392  -15.832 1.00 25.80  ?  118 ASN B CA    1 
ATOM   3290 C  C     . ASN B 1 118 ? 7.935   13.097  -15.706 1.00 24.50  ?  118 ASN B C     1 
ATOM   3291 O  O     . ASN B 1 118 ? 7.720   14.154  -16.315 1.00 24.21  ?  118 ASN B O     1 
ATOM   3292 C  CB    . ASN B 1 118 ? 10.400  13.293  -15.324 1.00 24.30  ?  118 ASN B CB    1 
ATOM   3293 C  CG    . ASN B 1 118 ? 11.752  12.637  -15.442 1.00 27.22  ?  118 ASN B CG    1 
ATOM   3294 O  OD1   . ASN B 1 118 ? 12.052  11.692  -14.722 1.00 26.89  ?  118 ASN B OD1   1 
ATOM   3295 N  ND2   . ASN B 1 118 ? 12.577  13.133  -16.356 1.00 29.80  ?  118 ASN B ND2   1 
ATOM   3296 N  N     . ILE B 1 119 ? 7.032   12.510  -14.927 1.00 24.41  ?  119 ILE B N     1 
ATOM   3297 C  CA    . ILE B 1 119 ? 5.751   13.154  -14.657 1.00 27.70  ?  119 ILE B CA    1 
ATOM   3298 C  C     . ILE B 1 119 ? 5.978   14.135  -13.513 1.00 26.78  ?  119 ILE B C     1 
ATOM   3299 O  O     . ILE B 1 119 ? 5.998   13.751  -12.343 1.00 27.33  ?  119 ILE B O     1 
ATOM   3300 C  CB    . ILE B 1 119 ? 4.655   12.139  -14.345 1.00 26.39  ?  119 ILE B CB    1 
ATOM   3301 C  CG1   . ILE B 1 119 ? 4.458   11.273  -15.583 1.00 25.53  ?  119 ILE B CG1   1 
ATOM   3302 C  CG2   . ILE B 1 119 ? 3.363   12.846  -13.993 1.00 23.69  ?  119 ILE B CG2   1 
ATOM   3303 C  CD1   . ILE B 1 119 ? 3.608   10.142  -15.365 1.00 31.66  ?  119 ILE B CD1   1 
ATOM   3304 N  N     . ALA B 1 120 ? 6.179   15.409  -13.864 1.00 24.21  ?  120 ALA B N     1 
ATOM   3305 C  CA    . ALA B 1 120 ? 6.510   16.447  -12.897 1.00 26.96  ?  120 ALA B CA    1 
ATOM   3306 C  C     . ALA B 1 120 ? 5.256   16.931  -12.182 1.00 25.66  ?  120 ALA B C     1 
ATOM   3307 O  O     . ALA B 1 120 ? 4.285   17.339  -12.829 1.00 24.07  ?  120 ALA B O     1 
ATOM   3308 C  CB    . ALA B 1 120 ? 7.193   17.623  -13.596 1.00 26.14  ?  120 ALA B CB    1 
ATOM   3309 N  N     . ARG B 1 121 ? 5.285   16.902  -10.848 1.00 23.96  ?  121 ARG B N     1 
ATOM   3310 C  CA    . ARG B 1 121 ? 4.192   17.441  -10.046 1.00 28.48  ?  121 ARG B CA    1 
ATOM   3311 C  C     . ARG B 1 121 ? 4.395   18.895  -9.627  1.00 29.45  ?  121 ARG B C     1 
ATOM   3312 O  O     . ARG B 1 121 ? 3.464   19.500  -9.084  1.00 35.99  ?  121 ARG B O     1 
ATOM   3313 C  CB    . ARG B 1 121 ? 3.977   16.572  -8.814  1.00 28.70  ?  121 ARG B CB    1 
ATOM   3314 C  CG    . ARG B 1 121 ? 3.549   15.168  -9.174  1.00 32.75  ?  121 ARG B CG    1 
ATOM   3315 C  CD    . ARG B 1 121 ? 3.908   14.195  -8.079  1.00 37.28  ?  121 ARG B CD    1 
ATOM   3316 N  NE    . ARG B 1 121 ? 3.224   14.540  -6.840  1.00 36.99  ?  121 ARG B NE    1 
ATOM   3317 C  CZ    . ARG B 1 121 ? 1.938   14.306  -6.619  1.00 42.50  ?  121 ARG B CZ    1 
ATOM   3318 N  NH1   . ARG B 1 121 ? 1.186   13.690  -7.520  1.00 38.18  ?  121 ARG B NH1   1 
ATOM   3319 N  NH2   . ARG B 1 121 ? 1.394   14.698  -5.465  1.00 37.64  ?  121 ARG B NH2   1 
ATOM   3320 N  N     . THR B 1 122 ? 5.572   19.469  -9.862  1.00 27.35  ?  122 THR B N     1 
ATOM   3321 C  CA    . THR B 1 122 ? 5.803   20.897  -9.719  1.00 30.45  ?  122 THR B CA    1 
ATOM   3322 C  C     . THR B 1 122 ? 6.384   21.416  -11.023 1.00 29.27  ?  122 THR B C     1 
ATOM   3323 O  O     . THR B 1 122 ? 6.911   20.644  -11.830 1.00 29.99  ?  122 THR B O     1 
ATOM   3324 C  CB    . THR B 1 122 ? 6.754   21.216  -8.565  1.00 33.53  ?  122 THR B CB    1 
ATOM   3325 O  OG1   . THR B 1 122 ? 8.004   20.543  -8.777  1.00 33.84  ?  122 THR B OG1   1 
ATOM   3326 C  CG2   . THR B 1 122 ? 6.143   20.751  -7.252  1.00 32.84  ?  122 THR B CG2   1 
ATOM   3327 N  N     . ARG B 1 123 ? 6.300   22.732  -11.227 1.00 25.39  ?  123 ARG B N     1 
ATOM   3328 C  CA    . ARG B 1 123 ? 6.729   23.309  -12.497 1.00 27.66  ?  123 ARG B CA    1 
ATOM   3329 C  C     . ARG B 1 123 ? 8.241   23.503  -12.533 1.00 31.35  ?  123 ARG B C     1 
ATOM   3330 O  O     . ARG B 1 123 ? 8.835   24.009  -11.572 1.00 32.32  ?  123 ARG B O     1 
ATOM   3331 C  CB    . ARG B 1 123 ? 6.014   24.629  -12.745 1.00 25.30  ?  123 ARG B CB    1 
ATOM   3332 C  CG    . ARG B 1 123 ? 4.641   24.397  -13.312 1.00 28.22  ?  123 ARG B CG    1 
ATOM   3333 C  CD    . ARG B 1 123 ? 4.358   25.293  -14.475 1.00 40.76  ?  123 ARG B CD    1 
ATOM   3334 N  NE    . ARG B 1 123 ? 5.341   25.210  -15.552 1.00 42.12  ?  123 ARG B NE    1 
ATOM   3335 C  CZ    . ARG B 1 123 ? 5.101   24.653  -16.734 1.00 37.55  ?  123 ARG B CZ    1 
ATOM   3336 N  NH1   . ARG B 1 123 ? 3.967   24.006  -16.975 1.00 37.17  ?  123 ARG B NH1   1 
ATOM   3337 N  NH2   . ARG B 1 123 ? 6.027   24.724  -17.688 1.00 26.68  ?  123 ARG B NH2   1 
ATOM   3338 N  N     . VAL B 1 124 ? 8.863   23.079  -13.644 1.00 29.91  ?  124 VAL B N     1 
ATOM   3339 C  CA    . VAL B 1 124 ? 10.292  23.247  -13.894 1.00 28.34  ?  124 VAL B CA    1 
ATOM   3340 C  C     . VAL B 1 124 ? 10.500  23.765  -15.316 1.00 28.48  ?  124 VAL B C     1 
ATOM   3341 O  O     . VAL B 1 124 ? 9.575   23.828  -16.127 1.00 31.69  ?  124 VAL B O     1 
ATOM   3342 C  CB    . VAL B 1 124 ? 11.092  21.941  -13.693 1.00 30.86  ?  124 VAL B CB    1 
ATOM   3343 C  CG1   . VAL B 1 124 ? 11.026  21.485  -12.261 1.00 32.25  ?  124 VAL B CG1   1 
ATOM   3344 C  CG2   . VAL B 1 124 ? 10.598  20.848  -14.635 1.00 29.91  ?  124 VAL B CG2   1 
ATOM   3345 N  N     . THR B 1 125 ? 11.744  24.133  -15.608 1.00 29.03  ?  125 THR B N     1 
ATOM   3346 C  CA    . THR B 1 125 ? 12.177  24.582  -16.925 1.00 26.10  ?  125 THR B CA    1 
ATOM   3347 C  C     . THR B 1 125 ? 12.960  23.477  -17.622 1.00 22.51  ?  125 THR B C     1 
ATOM   3348 O  O     . THR B 1 125 ? 13.231  22.422  -17.053 1.00 23.40  ?  125 THR B O     1 
ATOM   3349 C  CB    . THR B 1 125 ? 13.049  25.830  -16.811 1.00 29.69  ?  125 THR B CB    1 
ATOM   3350 O  OG1   . THR B 1 125 ? 14.274  25.469  -16.169 1.00 32.64  ?  125 THR B OG1   1 
ATOM   3351 C  CG2   . THR B 1 125 ? 12.352  26.909  -15.991 1.00 20.99  ?  125 THR B CG2   1 
ATOM   3352 N  N     . GLY B 1 126 ? 13.367  23.753  -18.866 1.00 30.07  ?  126 GLY B N     1 
ATOM   3353 C  CA    . GLY B 1 126 ? 14.195  22.802  -19.594 1.00 26.85  ?  126 GLY B CA    1 
ATOM   3354 C  C     . GLY B 1 126 ? 15.499  22.481  -18.890 1.00 26.73  ?  126 GLY B C     1 
ATOM   3355 O  O     . GLY B 1 126 ? 15.989  21.351  -18.963 1.00 29.12  ?  126 GLY B O     1 
ATOM   3356 N  N     . THR B 1 127 ? 16.071  23.458  -18.194 1.00 21.44  ?  127 THR B N     1 
ATOM   3357 C  CA    . THR B 1 127 ? 17.358  23.315  -17.528 1.00 23.66  ?  127 THR B CA    1 
ATOM   3358 C  C     . THR B 1 127 ? 17.250  22.876  -16.073 1.00 30.02  ?  127 THR B C     1 
ATOM   3359 O  O     . THR B 1 127 ? 18.284  22.722  -15.417 1.00 33.59  ?  127 THR B O     1 
ATOM   3360 C  CB    . THR B 1 127 ? 18.131  24.640  -17.595 1.00 23.67  ?  127 THR B CB    1 
ATOM   3361 O  OG1   . THR B 1 127 ? 17.320  25.701  -17.058 1.00 35.56  ?  127 THR B OG1   1 
ATOM   3362 C  CG2   . THR B 1 127 ? 18.492  24.969  -19.026 1.00 18.75  ?  127 THR B CG2   1 
ATOM   3363 N  N     . THR B 1 128 ? 16.043  22.681  -15.539 1.00 31.27  ?  128 THR B N     1 
ATOM   3364 C  CA    . THR B 1 128 ? 15.884  22.313  -14.132 1.00 34.42  ?  128 THR B CA    1 
ATOM   3365 C  C     . THR B 1 128 ? 14.947  21.127  -13.978 1.00 33.47  ?  128 THR B C     1 
ATOM   3366 O  O     . THR B 1 128 ? 14.154  21.062  -13.035 1.00 37.28  ?  128 THR B O     1 
ATOM   3367 C  CB    . THR B 1 128 ? 15.378  23.489  -13.292 1.00 36.11  ?  128 THR B CB    1 
ATOM   3368 O  OG1   . THR B 1 128 ? 14.085  23.897  -13.758 1.00 34.85  ?  128 THR B OG1   1 
ATOM   3369 C  CG2   . THR B 1 128 ? 16.345  24.678  -13.365 1.00 31.67  ?  128 THR B CG2   1 
ATOM   3370 N  N     . ILE B 1 129 ? 15.030  20.159  -14.894 1.00 32.49  ?  129 ILE B N     1 
ATOM   3371 C  CA    . ILE B 1 129 ? 14.174  18.981  -14.793 1.00 33.85  ?  129 ILE B CA    1 
ATOM   3372 C  C     . ILE B 1 129 ? 14.513  18.177  -13.546 1.00 35.78  ?  129 ILE B C     1 
ATOM   3373 O  O     . ILE B 1 129 ? 13.651  17.482  -12.995 1.00 37.11  ?  129 ILE B O     1 
ATOM   3374 C  CB    . ILE B 1 129 ? 14.287  18.129  -16.077 1.00 35.92  ?  129 ILE B CB    1 
ATOM   3375 C  CG1   . ILE B 1 129 ? 13.585  18.814  -17.255 1.00 30.62  ?  129 ILE B CG1   1 
ATOM   3376 C  CG2   . ILE B 1 129 ? 13.712  16.742  -15.876 1.00 26.28  ?  129 ILE B CG2   1 
ATOM   3377 C  CD1   . ILE B 1 129 ? 13.832  18.115  -18.586 1.00 28.36  ?  129 ILE B CD1   1 
ATOM   3378 N  N     . ALA B 1 130 ? 15.756  18.277  -13.061 1.00 36.97  ?  130 ALA B N     1 
ATOM   3379 C  CA    . ALA B 1 130 ? 16.160  17.505  -11.886 1.00 37.83  ?  130 ALA B CA    1 
ATOM   3380 C  C     . ALA B 1 130 ? 15.353  17.899  -10.655 1.00 41.13  ?  130 ALA B C     1 
ATOM   3381 O  O     . ALA B 1 130 ? 15.008  17.044  -9.828  1.00 39.39  ?  130 ALA B O     1 
ATOM   3382 C  CB    . ALA B 1 130 ? 17.651  17.694  -11.616 1.00 35.34  ?  130 ALA B CB    1 
ATOM   3383 N  N     . ASP B 1 131 ? 15.033  19.187  -10.527 1.00 37.50  ?  131 ASP B N     1 
ATOM   3384 C  CA    . ASP B 1 131 ? 14.405  19.737  -9.333  1.00 38.76  ?  131 ASP B CA    1 
ATOM   3385 C  C     . ASP B 1 131 ? 12.913  19.461  -9.254  1.00 39.43  ?  131 ASP B C     1 
ATOM   3386 O  O     . ASP B 1 131 ? 12.280  19.861  -8.266  1.00 39.04  ?  131 ASP B O     1 
ATOM   3387 C  CB    . ASP B 1 131 ? 14.620  21.253  -9.269  1.00 35.49  ?  131 ASP B CB    1 
ATOM   3388 C  CG    . ASP B 1 131 ? 15.995  21.670  -9.738  1.00 42.91  ?  131 ASP B CG    1 
ATOM   3389 O  OD1   . ASP B 1 131 ? 16.857  20.777  -9.941  1.00 45.99  ?  131 ASP B OD1   1 
ATOM   3390 O  OD2   . ASP B 1 131 ? 16.208  22.895  -9.910  1.00 44.28  ?  131 ASP B OD2   1 
ATOM   3391 N  N     . ALA B 1 132 ? 12.330  18.835  -10.267 1.00 32.07  ?  132 ALA B N     1 
ATOM   3392 C  CA    . ALA B 1 132 ? 10.903  18.578  -10.234 1.00 34.21  ?  132 ALA B CA    1 
ATOM   3393 C  C     . ALA B 1 132 ? 10.576  17.600  -9.121  1.00 30.94  ?  132 ALA B C     1 
ATOM   3394 O  O     . ALA B 1 132 ? 11.415  16.806  -8.696  1.00 32.76  ?  132 ALA B O     1 
ATOM   3395 C  CB    . ALA B 1 132 ? 10.421  18.029  -11.576 1.00 33.97  ?  132 ALA B CB    1 
ATOM   3396 N  N     . GLU B 1 133 ? 9.352   17.687  -8.624  1.00 36.01  ?  133 GLU B N     1 
ATOM   3397 C  CA    . GLU B 1 133 ? 8.825   16.677  -7.720  1.00 33.11  ?  133 GLU B CA    1 
ATOM   3398 C  C     . GLU B 1 133 ? 8.237   15.574  -8.580  1.00 29.94  ?  133 GLU B C     1 
ATOM   3399 O  O     . GLU B 1 133 ? 7.295   15.816  -9.345  1.00 28.56  ?  133 GLU B O     1 
ATOM   3400 C  CB    . GLU B 1 133 ? 7.766   17.257  -6.777  1.00 35.02  ?  133 GLU B CB    1 
ATOM   3401 C  CG    . GLU B 1 133 ? 8.322   17.826  -5.479  1.00 42.42  ?  133 GLU B CG    1 
ATOM   3402 C  CD    . GLU B 1 133 ? 7.250   18.036  -4.412  1.00 58.77  ?  133 GLU B CD    1 
ATOM   3403 O  OE1   . GLU B 1 133 ? 7.614   18.204  -3.224  1.00 58.65  ?  133 GLU B OE1   1 
ATOM   3404 O  OE2   . GLU B 1 133 ? 6.045   18.038  -4.760  1.00 54.41  ?  133 GLU B OE2   1 
ATOM   3405 N  N     . VAL B 1 134 ? 8.796   14.374  -8.467  1.00 29.12  ?  134 VAL B N     1 
ATOM   3406 C  CA    . VAL B 1 134 ? 8.422   13.262  -9.323  1.00 26.47  ?  134 VAL B CA    1 
ATOM   3407 C  C     . VAL B 1 134 ? 8.123   12.056  -8.450  1.00 31.78  ?  134 VAL B C     1 
ATOM   3408 O  O     . VAL B 1 134 ? 8.936   11.686  -7.598  1.00 38.30  ?  134 VAL B O     1 
ATOM   3409 C  CB    . VAL B 1 134 ? 9.534   12.935  -10.339 1.00 32.13  ?  134 VAL B CB    1 
ATOM   3410 C  CG1   . VAL B 1 134 ? 9.156   11.701  -11.180 1.00 29.96  ?  134 VAL B CG1   1 
ATOM   3411 C  CG2   . VAL B 1 134 ? 9.820   14.155  -11.222 1.00 22.40  ?  134 VAL B CG2   1 
ATOM   3412 N  N     . LEU B 1 135 ? 6.958   11.447  -8.656  1.00 25.13  ?  135 LEU B N     1 
ATOM   3413 C  CA    . LEU B 1 135 ? 6.651   10.162  -8.045  1.00 34.40  ?  135 LEU B CA    1 
ATOM   3414 C  C     . LEU B 1 135 ? 6.579   9.027   -9.047  1.00 34.33  ?  135 LEU B C     1 
ATOM   3415 O  O     . LEU B 1 135 ? 6.884   7.890   -8.691  1.00 35.71  ?  135 LEU B O     1 
ATOM   3416 C  CB    . LEU B 1 135 ? 5.328   10.226  -7.260  1.00 34.66  ?  135 LEU B CB    1 
ATOM   3417 C  CG    . LEU B 1 135 ? 5.341   10.891  -5.874  1.00 36.16  ?  135 LEU B CG    1 
ATOM   3418 C  CD1   . LEU B 1 135 ? 6.196   10.080  -4.908  1.00 31.45  ?  135 LEU B CD1   1 
ATOM   3419 C  CD2   . LEU B 1 135 ? 5.802   12.355  -5.892  1.00 36.23  ?  135 LEU B CD2   1 
ATOM   3420 N  N     . VAL B 1 136 ? 6.205   9.309   -10.291 1.00 37.16  ?  136 VAL B N     1 
ATOM   3421 C  CA    . VAL B 1 136 ? 6.111   8.292   -11.328 1.00 34.52  ?  136 VAL B CA    1 
ATOM   3422 C  C     . VAL B 1 136 ? 6.937   8.737   -12.525 1.00 34.46  ?  136 VAL B C     1 
ATOM   3423 O  O     . VAL B 1 136 ? 6.936   9.921   -12.891 1.00 34.91  ?  136 VAL B O     1 
ATOM   3424 C  CB    . VAL B 1 136 ? 4.647   8.028   -11.741 1.00 39.25  ?  136 VAL B CB    1 
ATOM   3425 C  CG1   . VAL B 1 136 ? 4.571   7.521   -13.169 1.00 37.41  ?  136 VAL B CG1   1 
ATOM   3426 C  CG2   . VAL B 1 136 ? 3.998   7.037   -10.787 1.00 43.58  ?  136 VAL B CG2   1 
ATOM   3427 N  N     . ARG B 1 137 ? 7.673   7.790   -13.107 1.00 29.29  ?  137 ARG B N     1 
ATOM   3428 C  CA    . ARG B 1 137 ? 8.331   7.959   -14.396 1.00 32.91  ?  137 ARG B CA    1 
ATOM   3429 C  C     . ARG B 1 137 ? 7.771   6.925   -15.361 1.00 36.84  ?  137 ARG B C     1 
ATOM   3430 O  O     . ARG B 1 137 ? 7.381   5.823   -14.954 1.00 36.08  ?  137 ARG B O     1 
ATOM   3431 C  CB    . ARG B 1 137 ? 9.846   7.798   -14.287 1.00 24.27  ?  137 ARG B CB    1 
ATOM   3432 C  CG    . ARG B 1 137 ? 10.507  8.899   -13.485 1.00 33.03  ?  137 ARG B CG    1 
ATOM   3433 C  CD    . ARG B 1 137 ? 11.787  8.434   -12.794 1.00 32.02  ?  137 ARG B CD    1 
ATOM   3434 N  NE    . ARG B 1 137 ? 12.216  9.405   -11.790 1.00 37.35  ?  137 ARG B NE    1 
ATOM   3435 C  CZ    . ARG B 1 137 ? 11.838  9.378   -10.518 1.00 40.89  ?  137 ARG B CZ    1 
ATOM   3436 N  NH1   . ARG B 1 137 ? 11.057  8.415   -10.046 1.00 36.40  ?  137 ARG B NH1   1 
ATOM   3437 N  NH2   . ARG B 1 137 ? 12.262  10.333  -9.695  1.00 39.56  ?  137 ARG B NH2   1 
ATOM   3438 N  N     . LEU B 1 138 ? 7.694   7.298   -16.634 1.00 23.40  ?  138 LEU B N     1 
ATOM   3439 C  CA    . LEU B 1 138 ? 7.229   6.404   -17.688 1.00 23.28  ?  138 LEU B CA    1 
ATOM   3440 C  C     . LEU B 1 138 ? 8.451   6.049   -18.521 1.00 24.46  ?  138 LEU B C     1 
ATOM   3441 O  O     . LEU B 1 138 ? 9.053   6.925   -19.148 1.00 21.40  ?  138 LEU B O     1 
ATOM   3442 C  CB    . LEU B 1 138 ? 6.134   7.056   -18.528 1.00 23.61  ?  138 LEU B CB    1 
ATOM   3443 C  CG    . LEU B 1 138 ? 4.776   7.305   -17.860 1.00 24.08  ?  138 LEU B CG    1 
ATOM   3444 C  CD1   . LEU B 1 138 ? 3.853   8.000   -18.826 1.00 24.05  ?  138 LEU B CD1   1 
ATOM   3445 C  CD2   . LEU B 1 138 ? 4.154   6.000   -17.425 1.00 28.45  ?  138 LEU B CD2   1 
ATOM   3446 N  N     . GLU B 1 139 ? 8.842   4.772   -18.486 1.00 23.64  ?  139 GLU B N     1 
ATOM   3447 C  CA    . GLU B 1 139 ? 10.156  4.357   -18.965 1.00 23.41  ?  139 GLU B CA    1 
ATOM   3448 C  C     . GLU B 1 139 ? 10.090  2.966   -19.574 1.00 22.15  ?  139 GLU B C     1 
ATOM   3449 O  O     . GLU B 1 139 ? 11.036  2.182   -19.463 1.00 24.61  ?  139 GLU B O     1 
ATOM   3450 C  CB    . GLU B 1 139 ? 11.194  4.359   -17.840 1.00 26.80  ?  139 GLU B CB    1 
ATOM   3451 C  CG    . GLU B 1 139 ? 11.337  5.658   -17.070 1.00 29.90  ?  139 GLU B CG    1 
ATOM   3452 C  CD    . GLU B 1 139 ? 12.467  5.588   -16.051 1.00 36.91  ?  139 GLU B CD    1 
ATOM   3453 O  OE1   . GLU B 1 139 ? 12.820  4.458   -15.638 1.00 36.06  ?  139 GLU B OE1   1 
ATOM   3454 O  OE2   . GLU B 1 139 ? 12.993  6.655   -15.656 1.00 34.08  ?  139 GLU B OE2   1 
ATOM   3455 N  N     . PHE B 1 140 ? 8.993   2.650   -20.226 1.00 19.73  ?  140 PHE B N     1 
ATOM   3456 C  CA    . PHE B 1 140 ? 8.745   1.282   -20.632 1.00 21.15  ?  140 PHE B CA    1 
ATOM   3457 C  C     . PHE B 1 140 ? 9.463   0.971   -21.939 1.00 23.09  ?  140 PHE B C     1 
ATOM   3458 O  O     . PHE B 1 140 ? 9.209   1.644   -22.945 1.00 21.15  ?  140 PHE B O     1 
ATOM   3459 C  CB    . PHE B 1 140 ? 7.256   1.063   -20.787 1.00 19.60  ?  140 PHE B CB    1 
ATOM   3460 C  CG    . PHE B 1 140 ? 6.503   1.067   -19.484 1.00 23.68  ?  140 PHE B CG    1 
ATOM   3461 C  CD1   . PHE B 1 140 ? 6.495   -0.058  -18.665 1.00 21.82  ?  140 PHE B CD1   1 
ATOM   3462 C  CD2   . PHE B 1 140 ? 5.776   2.182   -19.093 1.00 21.53  ?  140 PHE B CD2   1 
ATOM   3463 C  CE1   . PHE B 1 140 ? 5.785   -0.066  -17.482 1.00 22.72  ?  140 PHE B CE1   1 
ATOM   3464 C  CE2   . PHE B 1 140 ? 5.058   2.176   -17.902 1.00 23.56  ?  140 PHE B CE2   1 
ATOM   3465 C  CZ    . PHE B 1 140 ? 5.060   1.052   -17.101 1.00 19.19  ?  140 PHE B CZ    1 
ATOM   3466 N  N     . PRO B 1 141 ? 10.337  -0.036  -21.978 1.00 26.77  ?  141 PRO B N     1 
ATOM   3467 C  CA    . PRO B 1 141 ? 10.951  -0.452  -23.253 1.00 22.27  ?  141 PRO B CA    1 
ATOM   3468 C  C     . PRO B 1 141 ? 9.897   -0.878  -24.267 1.00 22.78  ?  141 PRO B C     1 
ATOM   3469 O  O     . PRO B 1 141 ? 8.712   -1.024  -23.963 1.00 24.52  ?  141 PRO B O     1 
ATOM   3470 C  CB    . PRO B 1 141 ? 11.851  -1.635  -22.865 1.00 26.33  ?  141 PRO B CB    1 
ATOM   3471 C  CG    . PRO B 1 141 ? 11.912  -1.632  -21.348 1.00 29.10  ?  141 PRO B CG    1 
ATOM   3472 C  CD    . PRO B 1 141 ? 10.706  -0.908  -20.849 1.00 25.09  ?  141 PRO B CD    1 
ATOM   3473 N  N     . TYR B 1 142 ? 10.346  -1.106  -25.499 1.00 24.32  ?  142 TYR B N     1 
ATOM   3474 C  CA    . TYR B 1 142 ? 9.436   -1.385  -26.610 1.00 24.83  ?  142 TYR B CA    1 
ATOM   3475 C  C     . TYR B 1 142 ? 9.369   -2.869  -26.948 1.00 22.87  ?  142 TYR B C     1 
ATOM   3476 O  O     . TYR B 1 142 ? 9.260   -3.240  -28.115 1.00 29.28  ?  142 TYR B O     1 
ATOM   3477 C  CB    . TYR B 1 142 ? 9.840   -0.574  -27.846 1.00 18.53  ?  142 TYR B CB    1 
ATOM   3478 C  CG    . TYR B 1 142 ? 8.686   -0.425  -28.809 1.00 16.42  ?  142 TYR B CG    1 
ATOM   3479 C  CD1   . TYR B 1 142 ? 7.544   0.271   -28.443 1.00 20.06  ?  142 TYR B CD1   1 
ATOM   3480 C  CD2   . TYR B 1 142 ? 8.704   -1.033  -30.049 1.00 15.45  ?  142 TYR B CD2   1 
ATOM   3481 C  CE1   . TYR B 1 142 ? 6.462   0.385   -29.309 1.00 17.41  ?  142 TYR B CE1   1 
ATOM   3482 C  CE2   . TYR B 1 142 ? 7.625   -0.925  -30.921 1.00 14.75  ?  142 TYR B CE2   1 
ATOM   3483 C  CZ    . TYR B 1 142 ? 6.513   -0.214  -30.547 1.00 15.97  ?  142 TYR B CZ    1 
ATOM   3484 O  OH    . TYR B 1 142 ? 5.444   -0.102  -31.414 1.00 18.32  ?  142 TYR B OH    1 
ATOM   3485 N  N     . ASP B 1 143 ? 9.425   -3.757  -25.963 1.00 26.28  ?  143 ASP B N     1 
ATOM   3486 C  CA    . ASP B 1 143 ? 9.595   -5.172  -26.280 1.00 28.27  ?  143 ASP B CA    1 
ATOM   3487 C  C     . ASP B 1 143 ? 8.315   -5.991  -26.216 1.00 28.25  ?  143 ASP B C     1 
ATOM   3488 O  O     . ASP B 1 143 ? 8.244   -7.031  -26.873 1.00 27.30  ?  143 ASP B O     1 
ATOM   3489 C  CB    . ASP B 1 143 ? 10.628  -5.816  -25.341 1.00 31.69  ?  143 ASP B CB    1 
ATOM   3490 C  CG    . ASP B 1 143 ? 10.428  -5.417  -23.886 1.00 34.46  ?  143 ASP B CG    1 
ATOM   3491 O  OD1   . ASP B 1 143 ? 9.292   -5.060  -23.523 1.00 35.47  ?  143 ASP B OD1   1 
ATOM   3492 O  OD2   . ASP B 1 143 ? 11.402  -5.461  -23.102 1.00 41.26  ?  143 ASP B OD2   1 
ATOM   3493 N  N     . ARG B 1 144 ? 7.310   -5.577  -25.444 1.00 26.13  ?  144 ARG B N     1 
ATOM   3494 C  CA    . ARG B 1 144 ? 6.194   -6.467  -25.140 1.00 25.46  ?  144 ARG B CA    1 
ATOM   3495 C  C     . ARG B 1 144 ? 4.907   -6.103  -25.865 1.00 24.54  ?  144 ARG B C     1 
ATOM   3496 O  O     . ARG B 1 144 ? 3.866   -6.712  -25.597 1.00 24.46  ?  144 ARG B O     1 
ATOM   3497 C  CB    . ARG B 1 144 ? 5.955   -6.502  -23.633 1.00 24.88  ?  144 ARG B CB    1 
ATOM   3498 C  CG    . ARG B 1 144 ? 7.069   -7.207  -22.899 1.00 31.09  ?  144 ARG B CG    1 
ATOM   3499 C  CD    . ARG B 1 144 ? 6.853   -7.217  -21.414 1.00 29.85  ?  144 ARG B CD    1 
ATOM   3500 N  NE    . ARG B 1 144 ? 8.114   -7.477  -20.732 1.00 31.32  ?  144 ARG B NE    1 
ATOM   3501 C  CZ    . ARG B 1 144 ? 8.229   -7.659  -19.424 1.00 41.39  ?  144 ARG B CZ    1 
ATOM   3502 N  NH1   . ARG B 1 144 ? 7.175   -7.596  -18.619 1.00 34.84  ?  144 ARG B NH1   1 
ATOM   3503 N  NH2   . ARG B 1 144 ? 9.432   -7.901  -18.907 1.00 41.12  ?  144 ARG B NH2   1 
ATOM   3504 N  N     . GLY B 1 145 ? 4.943   -5.130  -26.768 1.00 16.71  ?  145 GLY B N     1 
ATOM   3505 C  CA    . GLY B 1 145 ? 3.705   -4.702  -27.384 1.00 16.22  ?  145 GLY B CA    1 
ATOM   3506 C  C     . GLY B 1 145 ? 2.751   -3.947  -26.475 1.00 13.49  ?  145 GLY B C     1 
ATOM   3507 O  O     . GLY B 1 145 ? 1.565   -3.879  -26.783 1.00 14.46  ?  145 GLY B O     1 
ATOM   3508 N  N     . LEU B 1 146 ? 3.233   -3.379  -25.363 1.00 14.65  ?  146 LEU B N     1 
ATOM   3509 C  CA    . LEU B 1 146 ? 2.375   -2.559  -24.491 1.00 15.82  ?  146 LEU B CA    1 
ATOM   3510 C  C     . LEU B 1 146 ? 1.636   -1.447  -25.247 1.00 16.32  ?  146 LEU B C     1 
ATOM   3511 O  O     . LEU B 1 146 ? 0.491   -1.128  -24.907 1.00 15.90  ?  146 LEU B O     1 
ATOM   3512 C  CB    . LEU B 1 146 ? 3.215   -1.956  -23.362 1.00 11.19  ?  146 LEU B CB    1 
ATOM   3513 C  CG    . LEU B 1 146 ? 2.549   -1.005  -22.357 1.00 17.89  ?  146 LEU B CG    1 
ATOM   3514 C  CD1   . LEU B 1 146 ? 1.505   -1.731  -21.490 1.00 20.69  ?  146 LEU B CD1   1 
ATOM   3515 C  CD2   . LEU B 1 146 ? 3.595   -0.328  -21.471 1.00 16.14  ?  146 LEU B CD2   1 
ATOM   3516 N  N     . LEU B 1 147 ? 2.270   -0.854  -26.277 1.00 15.62  ?  147 LEU B N     1 
ATOM   3517 C  CA    . LEU B 1 147 ? 1.631   0.182   -27.101 1.00 15.81  ?  147 LEU B CA    1 
ATOM   3518 C  C     . LEU B 1 147 ? 0.431   -0.357  -27.873 1.00 16.73  ?  147 LEU B C     1 
ATOM   3519 O  O     . LEU B 1 147 ? -0.471  0.408   -28.240 1.00 12.83  ?  147 LEU B O     1 
ATOM   3520 C  CB    . LEU B 1 147 ? 2.646   0.781   -28.088 1.00 15.77  ?  147 LEU B CB    1 
ATOM   3521 C  CG    . LEU B 1 147 ? 2.129   1.927   -28.978 1.00 17.72  ?  147 LEU B CG    1 
ATOM   3522 C  CD1   . LEU B 1 147 ? 1.741   3.115   -28.138 1.00 11.20  ?  147 LEU B CD1   1 
ATOM   3523 C  CD2   . LEU B 1 147 ? 3.120   2.373   -30.084 1.00 12.95  ?  147 LEU B CD2   1 
ATOM   3524 N  N     . ASP B 1 148 ? 0.416   -1.665  -28.152 1.00 19.24  ?  148 ASP B N     1 
ATOM   3525 C  CA    . ASP B 1 148 ? -0.795  -2.302  -28.667 1.00 18.06  ?  148 ASP B CA    1 
ATOM   3526 C  C     . ASP B 1 148 ? -1.922  -2.280  -27.636 1.00 12.74  ?  148 ASP B C     1 
ATOM   3527 O  O     . ASP B 1 148 ? -3.105  -2.270  -28.000 1.00 12.65  ?  148 ASP B O     1 
ATOM   3528 C  CB    . ASP B 1 148 ? -0.495  -3.750  -29.074 1.00 17.41  ?  148 ASP B CB    1 
ATOM   3529 C  CG    . ASP B 1 148 ? 0.158   -3.852  -30.439 1.00 28.35  ?  148 ASP B CG    1 
ATOM   3530 O  OD1   . ASP B 1 148 ? 0.239   -2.805  -31.120 1.00 32.75  ?  148 ASP B OD1   1 
ATOM   3531 O  OD2   . ASP B 1 148 ? 0.574   -4.972  -30.835 1.00 30.69  ?  148 ASP B OD2   1 
ATOM   3532 N  N     . VAL B 1 149 ? -1.583  -2.317  -26.354 1.00 12.17  ?  149 VAL B N     1 
ATOM   3533 C  CA    . VAL B 1 149 ? -2.626  -2.475  -25.336 1.00 16.33  ?  149 VAL B CA    1 
ATOM   3534 C  C     . VAL B 1 149 ? -3.254  -1.133  -25.005 1.00 15.54  ?  149 VAL B C     1 
ATOM   3535 O  O     . VAL B 1 149 ? -4.477  -0.962  -25.070 1.00 16.95  ?  149 VAL B O     1 
ATOM   3536 C  CB    . VAL B 1 149 ? -2.054  -3.159  -24.084 1.00 14.92  ?  149 VAL B CB    1 
ATOM   3537 C  CG1   . VAL B 1 149 ? -3.100  -3.185  -22.964 1.00 20.10  ?  149 VAL B CG1   1 
ATOM   3538 C  CG2   . VAL B 1 149 ? -1.641  -4.569  -24.421 1.00 13.61  ?  149 VAL B CG2   1 
ATOM   3539 N  N     . THR B 1 150 ? -2.422  -0.155  -24.684 1.00 18.62  ?  150 THR B N     1 
ATOM   3540 C  CA    . THR B 1 150 ? -2.883  1.201   -24.456 1.00 17.23  ?  150 THR B CA    1 
ATOM   3541 C  C     . THR B 1 150 ? -1.661  2.102   -24.565 1.00 16.09  ?  150 THR B C     1 
ATOM   3542 O  O     . THR B 1 150 ? -0.537  1.623   -24.685 1.00 14.80  ?  150 THR B O     1 
ATOM   3543 C  CB    . THR B 1 150 ? -3.606  1.291   -23.105 1.00 19.43  ?  150 THR B CB    1 
ATOM   3544 O  OG1   . THR B 1 150 ? -4.487  2.417   -23.104 1.00 24.78  ?  150 THR B OG1   1 
ATOM   3545 C  CG2   . THR B 1 150 ? -2.628  1.384   -21.966 1.00 18.93  ?  150 THR B CG2   1 
ATOM   3546 N  N     . ASN B 1 151 ? -1.888  3.415   -24.538 1.00 18.79  ?  151 ASN B N     1 
ATOM   3547 C  CA    . ASN B 1 151 ? -0.793  4.360   -24.729 1.00 13.57  ?  151 ASN B CA    1 
ATOM   3548 C  C     . ASN B 1 151 ? 0.102   4.464   -23.492 1.00 17.54  ?  151 ASN B C     1 
ATOM   3549 O  O     . ASN B 1 151 ? -0.378  4.516   -22.351 1.00 17.77  ?  151 ASN B O     1 
ATOM   3550 C  CB    . ASN B 1 151 ? -1.366  5.728   -25.070 1.00 20.09  ?  151 ASN B CB    1 
ATOM   3551 C  CG    . ASN B 1 151 ? -0.296  6.747   -25.350 1.00 21.72  ?  151 ASN B CG    1 
ATOM   3552 O  OD1   . ASN B 1 151 ? 0.878   6.400   -25.557 1.00 16.24  ?  151 ASN B OD1   1 
ATOM   3553 N  ND2   . ASN B 1 151 ? -0.684  8.032   -25.323 1.00 24.33  ?  151 ASN B ND2   1 
ATOM   3554 N  N     . HIS B 1 152 ? 1.421   4.526   -23.721 1.00 14.36  ?  152 HIS B N     1 
ATOM   3555 C  CA    . HIS B 1 152 ? 2.367   4.655   -22.616 1.00 12.92  ?  152 HIS B CA    1 
ATOM   3556 C  C     . HIS B 1 152 ? 3.383   5.766   -22.825 1.00 15.23  ?  152 HIS B C     1 
ATOM   3557 O  O     . HIS B 1 152 ? 4.373   5.826   -22.077 1.00 17.34  ?  152 HIS B O     1 
ATOM   3558 C  CB    . HIS B 1 152 ? 3.101   3.332   -22.317 1.00 18.64  ?  152 HIS B CB    1 
ATOM   3559 C  CG    . HIS B 1 152 ? 3.899   2.753   -23.463 1.00 15.66  ?  152 HIS B CG    1 
ATOM   3560 N  ND1   . HIS B 1 152 ? 5.268   2.905   -23.571 1.00 15.67  ?  152 HIS B ND1   1 
ATOM   3561 C  CD2   . HIS B 1 152 ? 3.534   1.937   -24.485 1.00 14.49  ?  152 HIS B CD2   1 
ATOM   3562 C  CE1   . HIS B 1 152 ? 5.705   2.231   -24.626 1.00 16.69  ?  152 HIS B CE1   1 
ATOM   3563 N  NE2   . HIS B 1 152 ? 4.673   1.631   -25.196 1.00 13.58  ?  152 HIS B NE2   1 
ATOM   3564 N  N     . PHE B 1 153 ? 3.173   6.647   -23.801 1.00 11.59  ?  153 PHE B N     1 
ATOM   3565 C  CA    . PHE B 1 153 ? 3.975   7.868   -23.879 1.00 19.96  ?  153 PHE B CA    1 
ATOM   3566 C  C     . PHE B 1 153 ? 3.132   8.998   -24.469 1.00 16.16  ?  153 PHE B C     1 
ATOM   3567 O  O     . PHE B 1 153 ? 1.934   8.851   -24.704 1.00 20.89  ?  153 PHE B O     1 
ATOM   3568 C  CB    . PHE B 1 153 ? 5.296   7.647   -24.649 1.00 16.73  ?  153 PHE B CB    1 
ATOM   3569 C  CG    . PHE B 1 153 ? 5.172   6.887   -25.940 1.00 16.50  ?  153 PHE B CG    1 
ATOM   3570 C  CD1   . PHE B 1 153 ? 4.915   7.545   -27.131 1.00 16.27  ?  153 PHE B CD1   1 
ATOM   3571 C  CD2   . PHE B 1 153 ? 5.423   5.517   -25.986 1.00 19.81  ?  153 PHE B CD2   1 
ATOM   3572 C  CE1   . PHE B 1 153 ? 4.857   6.829   -28.355 1.00 15.47  ?  153 PHE B CE1   1 
ATOM   3573 C  CE2   . PHE B 1 153 ? 5.366   4.804   -27.195 1.00 15.76  ?  153 PHE B CE2   1 
ATOM   3574 C  CZ    . PHE B 1 153 ? 5.078   5.464   -28.374 1.00 13.37  ?  153 PHE B CZ    1 
ATOM   3575 N  N     . ALA B 1 154 ? 3.752   10.149  -24.677 1.00 21.28  ?  154 ALA B N     1 
ATOM   3576 C  CA    . ALA B 1 154 ? 3.008   11.339  -25.056 1.00 21.36  ?  154 ALA B CA    1 
ATOM   3577 C  C     . ALA B 1 154 ? 3.794   12.093  -26.107 1.00 20.95  ?  154 ALA B C     1 
ATOM   3578 O  O     . ALA B 1 154 ? 5.009   11.890  -26.246 1.00 20.32  ?  154 ALA B O     1 
ATOM   3579 C  CB    . ALA B 1 154 ? 2.727   12.219  -23.828 1.00 20.20  ?  154 ALA B CB    1 
ATOM   3580 N  N     . PRO B 1 155 ? 3.142   12.964  -26.893 1.00 24.25  ?  155 PRO B N     1 
ATOM   3581 C  CA    . PRO B 1 155 ? 3.833   13.530  -28.064 1.00 18.59  ?  155 PRO B CA    1 
ATOM   3582 C  C     . PRO B 1 155 ? 5.092   14.301  -27.718 1.00 16.79  ?  155 PRO B C     1 
ATOM   3583 O  O     . PRO B 1 155 ? 6.043   14.284  -28.508 1.00 16.19  ?  155 PRO B O     1 
ATOM   3584 C  CB    . PRO B 1 155 ? 2.766   14.427  -28.711 1.00 19.28  ?  155 PRO B CB    1 
ATOM   3585 C  CG    . PRO B 1 155 ? 1.452   13.817  -28.273 1.00 18.79  ?  155 PRO B CG    1 
ATOM   3586 C  CD    . PRO B 1 155 ? 1.724   13.383  -26.842 1.00 18.19  ?  155 PRO B CD    1 
ATOM   3587 N  N     . SER B 1 156 ? 5.154   14.943  -26.551 1.00 14.19  ?  156 SER B N     1 
ATOM   3588 C  CA    . SER B 1 156 ? 6.348   15.703  -26.192 1.00 15.26  ?  156 SER B CA    1 
ATOM   3589 C  C     . SER B 1 156 ? 7.570   14.816  -26.011 1.00 17.15  ?  156 SER B C     1 
ATOM   3590 O  O     . SER B 1 156 ? 8.686   15.337  -25.903 1.00 18.06  ?  156 SER B O     1 
ATOM   3591 C  CB    . SER B 1 156 ? 6.097   16.505  -24.912 1.00 21.87  ?  156 SER B CB    1 
ATOM   3592 O  OG    . SER B 1 156 ? 4.917   17.277  -25.029 1.00 14.06  ?  156 SER B OG    1 
ATOM   3593 N  N     . ALA B 1 157 ? 7.394   13.498  -25.996 1.00 14.47  ?  157 ALA B N     1 
ATOM   3594 C  CA    . ALA B 1 157 ? 8.490   12.568  -25.808 1.00 18.43  ?  157 ALA B CA    1 
ATOM   3595 C  C     . ALA B 1 157 ? 8.926   11.927  -27.113 1.00 15.05  ?  157 ALA B C     1 
ATOM   3596 O  O     . ALA B 1 157 ? 9.775   11.034  -27.102 1.00 14.03  ?  157 ALA B O     1 
ATOM   3597 C  CB    . ALA B 1 157 ? 8.094   11.486  -24.804 1.00 11.63  ?  157 ALA B CB    1 
ATOM   3598 N  N     . VAL B 1 158 ? 8.365   12.370  -28.229 1.00 11.60  ?  158 VAL B N     1 
ATOM   3599 C  CA    . VAL B 1 158 ? 8.439   11.663  -29.495 1.00 12.01  ?  158 VAL B CA    1 
ATOM   3600 C  C     . VAL B 1 158 ? 9.170   12.552  -30.493 1.00 14.25  ?  158 VAL B C     1 
ATOM   3601 O  O     . VAL B 1 158 ? 8.873   13.752  -30.585 1.00 12.84  ?  158 VAL B O     1 
ATOM   3602 C  CB    . VAL B 1 158 ? 7.031   11.302  -29.999 1.00 13.29  ?  158 VAL B CB    1 
ATOM   3603 C  CG1   . VAL B 1 158 ? 7.082   10.927  -31.474 1.00 15.16  ?  158 VAL B CG1   1 
ATOM   3604 C  CG2   . VAL B 1 158 ? 6.429   10.155  -29.154 1.00 12.18  ?  158 VAL B CG2   1 
ATOM   3605 N  N     . VAL B 1 159 ? 10.163  11.974  -31.183 1.00 13.09  ?  159 VAL B N     1 
ATOM   3606 C  CA    . VAL B 1 159 ? 10.808  12.547  -32.371 1.00 14.39  ?  159 VAL B CA    1 
ATOM   3607 C  C     . VAL B 1 159 ? 10.709  11.492  -33.466 1.00 14.59  ?  159 VAL B C     1 
ATOM   3608 O  O     . VAL B 1 159 ? 11.114  10.340  -33.261 1.00 15.04  ?  159 VAL B O     1 
ATOM   3609 C  CB    . VAL B 1 159 ? 12.278  12.953  -32.136 1.00 12.77  ?  159 VAL B CB    1 
ATOM   3610 C  CG1   . VAL B 1 159 ? 12.824  13.686  -33.347 1.00 13.31  ?  159 VAL B CG1   1 
ATOM   3611 C  CG2   . VAL B 1 159 ? 12.422  13.866  -30.914 1.00 11.47  ?  159 VAL B CG2   1 
ATOM   3612 N  N     . CYS B 1 160 ? 10.134  11.866  -34.610 1.00 13.84  ?  160 CYS B N     1 
ATOM   3613 C  CA    . CYS B 1 160 ? 9.829   10.885  -35.645 1.00 15.11  ?  160 CYS B CA    1 
ATOM   3614 C  C     . CYS B 1 160 ? 10.072  11.463  -37.040 1.00 13.13  ?  160 CYS B C     1 
ATOM   3615 O  O     . CYS B 1 160 ? 10.056  12.679  -37.248 1.00 10.70  ?  160 CYS B O     1 
ATOM   3616 C  CB    . CYS B 1 160 ? 8.382   10.410  -35.523 1.00 12.70  ?  160 CYS B CB    1 
ATOM   3617 S  SG    . CYS B 1 160 ? 7.179   11.702  -35.925 1.00 19.11  ?  160 CYS B SG    1 
ATOM   3618 N  N     . ARG B 1 161 ? 10.296  10.551  -37.988 1.00 14.92  ?  161 ARG B N     1 
ATOM   3619 C  CA    . ARG B 1 161 ? 10.458  10.884  -39.397 1.00 14.42  ?  161 ARG B CA    1 
ATOM   3620 C  C     . ARG B 1 161 ? 9.195   11.555  -39.923 1.00 16.51  ?  161 ARG B C     1 
ATOM   3621 O  O     . ARG B 1 161 ? 8.081   11.098  -39.656 1.00 15.91  ?  161 ARG B O     1 
ATOM   3622 C  CB    . ARG B 1 161 ? 10.771  9.612   -40.205 1.00 12.15  ?  161 ARG B CB    1 
ATOM   3623 C  CG    . ARG B 1 161 ? 11.277  9.857   -41.629 1.00 12.51  ?  161 ARG B CG    1 
ATOM   3624 C  CD    . ARG B 1 161 ? 11.837  8.550   -42.293 1.00 13.49  ?  161 ARG B CD    1 
ATOM   3625 N  NE    . ARG B 1 161 ? 12.958  7.994   -41.541 1.00 8.76   ?  161 ARG B NE    1 
ATOM   3626 C  CZ    . ARG B 1 161 ? 14.189  8.484   -41.542 1.00 9.78   ?  161 ARG B CZ    1 
ATOM   3627 N  NH1   . ARG B 1 161 ? 14.534  9.517   -42.320 1.00 9.72   ?  161 ARG B NH1   1 
ATOM   3628 N  NH2   . ARG B 1 161 ? 15.090  7.959   -40.716 1.00 9.94   ?  161 ARG B NH2   1 
ATOM   3629 N  N     . SER B 1 162 ? 9.382   12.649  -40.678 1.00 20.68  ?  162 SER B N     1 
ATOM   3630 C  CA    . SER B 1 162 ? 8.353   13.636  -41.023 1.00 20.87  ?  162 SER B CA    1 
ATOM   3631 C  C     . SER B 1 162 ? 6.999   12.999  -41.327 1.00 23.83  ?  162 SER B C     1 
ATOM   3632 O  O     . SER B 1 162 ? 6.889   12.206  -42.269 1.00 20.19  ?  162 SER B O     1 
ATOM   3633 C  CB    . SER B 1 162 ? 8.799   14.470  -42.223 1.00 17.06  ?  162 SER B CB    1 
ATOM   3634 O  OG    . SER B 1 162 ? 7.673   14.903  -42.963 1.00 17.45  ?  162 SER B OG    1 
ATOM   3635 N  N     . PRO B 1 163 ? 5.958   13.302  -40.542 1.00 19.05  ?  163 PRO B N     1 
ATOM   3636 C  CA    . PRO B 1 163 ? 4.625   12.756  -40.858 1.00 18.61  ?  163 PRO B CA    1 
ATOM   3637 C  C     . PRO B 1 163 ? 4.034   13.278  -42.161 1.00 16.65  ?  163 PRO B C     1 
ATOM   3638 O  O     . PRO B 1 163 ? 3.277   12.545  -42.802 1.00 18.89  ?  163 PRO B O     1 
ATOM   3639 C  CB    . PRO B 1 163 ? 3.767   13.177  -39.643 1.00 18.41  ?  163 PRO B CB    1 
ATOM   3640 C  CG    . PRO B 1 163 ? 4.763   13.398  -38.523 1.00 19.54  ?  163 PRO B CG    1 
ATOM   3641 C  CD    . PRO B 1 163 ? 6.011   13.933  -39.210 1.00 17.01  ?  163 PRO B CD    1 
ATOM   3642 N  N     . ARG B 1 164 ? 4.328   14.521  -42.568 1.00 16.51  ?  164 ARG B N     1 
ATOM   3643 C  CA    . ARG B 1 164 ? 3.797   15.038  -43.831 1.00 16.73  ?  164 ARG B CA    1 
ATOM   3644 C  C     . ARG B 1 164 ? 4.335   14.275  -45.045 1.00 19.10  ?  164 ARG B C     1 
ATOM   3645 O  O     . ARG B 1 164 ? 3.581   13.968  -45.978 1.00 15.36  ?  164 ARG B O     1 
ATOM   3646 C  CB    . ARG B 1 164 ? 4.120   16.523  -43.960 1.00 25.61  ?  164 ARG B CB    1 
ATOM   3647 C  CG    . ARG B 1 164 ? 4.321   16.979  -45.402 1.00 25.64  ?  164 ARG B CG    1 
ATOM   3648 C  CD    . ARG B 1 164 ? 4.366   18.481  -45.495 1.00 26.18  ?  164 ARG B CD    1 
ATOM   3649 N  NE    . ARG B 1 164 ? 5.721   18.994  -45.637 1.00 26.01  ?  164 ARG B NE    1 
ATOM   3650 C  CZ    . ARG B 1 164 ? 6.005   20.220  -46.065 1.00 34.56  ?  164 ARG B CZ    1 
ATOM   3651 N  NH1   . ARG B 1 164 ? 5.051   21.089  -46.362 1.00 29.94  ?  164 ARG B NH1   1 
ATOM   3652 N  NH2   . ARG B 1 164 ? 7.277   20.588  -46.189 1.00 38.61  ?  164 ARG B NH2   1 
ATOM   3653 N  N     . SER B 1 165 ? 5.639   13.985  -45.070 1.00 15.67  ?  165 SER B N     1 
ATOM   3654 C  CA    . SER B 1 165 ? 6.178   13.153  -46.150 1.00 24.55  ?  165 SER B CA    1 
ATOM   3655 C  C     . SER B 1 165 ? 5.467   11.806  -46.227 1.00 27.49  ?  165 SER B C     1 
ATOM   3656 O  O     . SER B 1 165 ? 5.200   11.304  -47.321 1.00 29.77  ?  165 SER B O     1 
ATOM   3657 C  CB    . SER B 1 165 ? 7.682   12.940  -45.971 1.00 19.78  ?  165 SER B CB    1 
ATOM   3658 O  OG    . SER B 1 165 ? 8.398   14.043  -46.518 1.00 39.78  ?  165 SER B OG    1 
ATOM   3659 N  N     . ALA B 1 166 ? 5.152   11.208  -45.074 1.00 28.16  ?  166 ALA B N     1 
ATOM   3660 C  CA    . ALA B 1 166 ? 4.451   9.931   -45.012 1.00 26.64  ?  166 ALA B CA    1 
ATOM   3661 C  C     . ALA B 1 166 ? 2.952   10.064  -45.246 1.00 23.20  ?  166 ALA B C     1 
ATOM   3662 O  O     . ALA B 1 166 ? 2.256   9.042   -45.302 1.00 24.32  ?  166 ALA B O     1 
ATOM   3663 C  CB    . ALA B 1 166 ? 4.686   9.268   -43.647 1.00 20.99  ?  166 ALA B CB    1 
ATOM   3664 N  N     . GLY B 1 167 ? 2.435   11.284  -45.366 1.00 18.60  ?  167 GLY B N     1 
ATOM   3665 C  CA    . GLY B 1 167 ? 1.000   11.471  -45.451 1.00 18.73  ?  167 GLY B CA    1 
ATOM   3666 C  C     . GLY B 1 167 ? 0.240   10.986  -44.232 1.00 21.19  ?  167 GLY B C     1 
ATOM   3667 O  O     . GLY B 1 167 ? -0.932  10.614  -44.351 1.00 22.29  ?  167 GLY B O     1 
ATOM   3668 N  N     . ALA B 1 168 ? 0.870   10.977  -43.058 1.00 17.47  ?  168 ALA B N     1 
ATOM   3669 C  CA    . ALA B 1 168 ? 0.223   10.543  -41.826 1.00 19.76  ?  168 ALA B CA    1 
ATOM   3670 C  C     . ALA B 1 168 ? -0.104  11.756  -40.961 1.00 19.10  ?  168 ALA B C     1 
ATOM   3671 O  O     . ALA B 1 168 ? 0.707   12.688  -40.846 1.00 17.85  ?  168 ALA B O     1 
ATOM   3672 C  CB    . ALA B 1 168 ? 1.107   9.563   -41.052 1.00 16.10  ?  168 ALA B CB    1 
ATOM   3673 N  N     . PHE B 1 169 ? -1.290  11.737  -40.352 1.00 15.77  ?  169 PHE B N     1 
ATOM   3674 C  CA    . PHE B 1 169 ? -1.817  12.902  -39.652 1.00 16.13  ?  169 PHE B CA    1 
ATOM   3675 C  C     . PHE B 1 169 ? -2.646  12.445  -38.465 1.00 16.74  ?  169 PHE B C     1 
ATOM   3676 O  O     . PHE B 1 169 ? -2.991  11.269  -38.337 1.00 11.98  ?  169 PHE B O     1 
ATOM   3677 C  CB    . PHE B 1 169 ? -2.676  13.794  -40.576 1.00 17.82  ?  169 PHE B CB    1 
ATOM   3678 C  CG    . PHE B 1 169 ? -1.883  14.479  -41.665 1.00 20.18  ?  169 PHE B CG    1 
ATOM   3679 C  CD1   . PHE B 1 169 ? -1.134  15.604  -41.386 1.00 18.91  ?  169 PHE B CD1   1 
ATOM   3680 C  CD2   . PHE B 1 169 ? -1.864  13.970  -42.955 1.00 21.11  ?  169 PHE B CD2   1 
ATOM   3681 C  CE1   . PHE B 1 169 ? -0.380  16.216  -42.375 1.00 20.94  ?  169 PHE B CE1   1 
ATOM   3682 C  CE2   . PHE B 1 169 ? -1.124  14.582  -43.935 1.00 21.76  ?  169 PHE B CE2   1 
ATOM   3683 C  CZ    . PHE B 1 169 ? -0.381  15.708  -43.641 1.00 19.51  ?  169 PHE B CZ    1 
ATOM   3684 N  N     . PHE B 1 170 ? -2.963  13.408  -37.599 1.00 15.89  ?  170 PHE B N     1 
ATOM   3685 C  CA    . PHE B 1 170 ? -3.856  13.181  -36.470 1.00 13.74  ?  170 PHE B CA    1 
ATOM   3686 C  C     . PHE B 1 170 ? -5.308  13.191  -36.924 1.00 17.54  ?  170 PHE B C     1 
ATOM   3687 O  O     . PHE B 1 170 ? -5.710  13.988  -37.781 1.00 11.94  ?  170 PHE B O     1 
ATOM   3688 C  CB    . PHE B 1 170 ? -3.664  14.244  -35.393 1.00 10.43  ?  170 PHE B CB    1 
ATOM   3689 C  CG    . PHE B 1 170 ? -2.379  14.119  -34.633 1.00 10.66  ?  170 PHE B CG    1 
ATOM   3690 C  CD1   . PHE B 1 170 ? -1.196  14.622  -35.158 1.00 16.97  ?  170 PHE B CD1   1 
ATOM   3691 C  CD2   . PHE B 1 170 ? -2.354  13.533  -33.390 1.00 10.66  ?  170 PHE B CD2   1 
ATOM   3692 C  CE1   . PHE B 1 170 ? -0.001  14.520  -34.451 1.00 17.78  ?  170 PHE B CE1   1 
ATOM   3693 C  CE2   . PHE B 1 170 ? -1.178  13.424  -32.685 1.00 11.11  ?  170 PHE B CE2   1 
ATOM   3694 C  CZ    . PHE B 1 170 ? 0.001   13.908  -33.212 1.00 14.52  ?  170 PHE B CZ    1 
ATOM   3695 N  N     . ASP B 1 171 ? -6.090  12.288  -36.332 1.00 17.29  ?  171 ASP B N     1 
ATOM   3696 C  CA    . ASP B 1 171 ? -7.530  12.224  -36.542 1.00 22.18  ?  171 ASP B CA    1 
ATOM   3697 C  C     . ASP B 1 171 ? -8.189  13.423  -35.851 1.00 22.55  ?  171 ASP B C     1 
ATOM   3698 O  O     . ASP B 1 171 ? -8.166  13.526  -34.619 1.00 18.32  ?  171 ASP B O     1 
ATOM   3699 C  CB    . ASP B 1 171 ? -8.036  10.892  -35.988 1.00 21.35  ?  171 ASP B CB    1 
ATOM   3700 C  CG    . ASP B 1 171 ? -9.469  10.589  -36.372 1.00 25.72  ?  171 ASP B CG    1 
ATOM   3701 O  OD1   . ASP B 1 171 ? -10.199 11.507  -36.814 1.00 30.91  ?  171 ASP B OD1   1 
ATOM   3702 O  OD2   . ASP B 1 171 ? -9.870  9.411   -36.226 1.00 30.58  ?  171 ASP B OD2   1 
ATOM   3703 N  N     . THR B 1 172 ? -8.779  14.338  -36.635 1.00 27.37  ?  172 THR B N     1 
ATOM   3704 C  CA    . THR B 1 172 ? -9.378  15.535  -36.043 1.00 27.15  ?  172 THR B CA    1 
ATOM   3705 C  C     . THR B 1 172 ? -10.687 15.250  -35.318 1.00 28.90  ?  172 THR B C     1 
ATOM   3706 O  O     . THR B 1 172 ? -11.229 16.166  -34.686 1.00 27.49  ?  172 THR B O     1 
ATOM   3707 C  CB    . THR B 1 172 ? -9.630  16.616  -37.097 1.00 27.86  ?  172 THR B CB    1 
ATOM   3708 O  OG1   . THR B 1 172 ? -10.552 16.127  -38.082 1.00 31.97  ?  172 THR B OG1   1 
ATOM   3709 C  CG2   . THR B 1 172 ? -8.314  17.059  -37.777 1.00 21.25  ?  172 THR B CG2   1 
ATOM   3710 N  N     . ALA B 1 173 ? -11.212 14.023  -35.396 1.00 22.36  ?  173 ALA B N     1 
ATOM   3711 C  CA    . ALA B 1 173 ? -12.419 13.656  -34.654 1.00 25.99  ?  173 ALA B CA    1 
ATOM   3712 C  C     . ALA B 1 173 ? -12.122 13.141  -33.252 1.00 25.87  ?  173 ALA B C     1 
ATOM   3713 O  O     . ALA B 1 173 ? -13.053 12.975  -32.454 1.00 30.17  ?  173 ALA B O     1 
ATOM   3714 C  CB    . ALA B 1 173 ? -13.221 12.593  -35.415 1.00 27.16  ?  173 ALA B CB    1 
ATOM   3715 N  N     . LEU B 1 174 ? -10.857 12.894  -32.929 1.00 23.61  ?  174 LEU B N     1 
ATOM   3716 C  CA    . LEU B 1 174 ? -10.460 12.398  -31.620 1.00 22.66  ?  174 LEU B CA    1 
ATOM   3717 C  C     . LEU B 1 174 ? -9.898  13.558  -30.804 1.00 21.36  ?  174 LEU B C     1 
ATOM   3718 O  O     . LEU B 1 174 ? -8.909  14.179  -31.206 1.00 21.60  ?  174 LEU B O     1 
ATOM   3719 C  CB    . LEU B 1 174 ? -9.433  11.273  -31.767 1.00 21.27  ?  174 LEU B CB    1 
ATOM   3720 C  CG    . LEU B 1 174 ? -10.001 9.965   -32.315 1.00 23.83  ?  174 LEU B CG    1 
ATOM   3721 C  CD1   . LEU B 1 174 ? -8.940  8.876   -32.295 1.00 21.27  ?  174 LEU B CD1   1 
ATOM   3722 C  CD2   . LEU B 1 174 ? -11.249 9.538   -31.508 1.00 27.17  ?  174 LEU B CD2   1 
ATOM   3723 N  N     . GLY B 1 175 ? -10.534 13.851  -29.667 1.00 25.96  ?  175 GLY B N     1 
ATOM   3724 C  CA    . GLY B 1 175 ? -10.116 14.942  -28.802 1.00 20.20  ?  175 GLY B CA    1 
ATOM   3725 C  C     . GLY B 1 175 ? -9.322  14.448  -27.612 1.00 25.78  ?  175 GLY B C     1 
ATOM   3726 O  O     . GLY B 1 175 ? -8.641  15.230  -26.940 1.00 25.19  ?  175 GLY B O     1 
ATOM   3727 N  N     . VAL B 1 176 ? -9.417  13.141  -27.344 1.00 20.32  ?  176 VAL B N     1 
ATOM   3728 C  CA    . VAL B 1 176 ? -8.590  12.454  -26.362 1.00 18.90  ?  176 VAL B CA    1 
ATOM   3729 C  C     . VAL B 1 176 ? -8.060  11.178  -27.008 1.00 18.51  ?  176 VAL B C     1 
ATOM   3730 O  O     . VAL B 1 176 ? -8.694  10.590  -27.895 1.00 14.13  ?  176 VAL B O     1 
ATOM   3731 C  CB    . VAL B 1 176 ? -9.358  12.115  -25.058 1.00 23.94  ?  176 VAL B CB    1 
ATOM   3732 C  CG1   . VAL B 1 176 ? -9.979  13.366  -24.454 1.00 24.22  ?  176 VAL B CG1   1 
ATOM   3733 C  CG2   . VAL B 1 176 ? -10.396 11.064  -25.306 1.00 20.46  ?  176 VAL B CG2   1 
ATOM   3734 N  N     . GLU B 1 177 ? -6.883  10.754  -26.554 1.00 14.33  ?  177 GLU B N     1 
ATOM   3735 C  CA    . GLU B 1 177 ? -6.187  9.602   -27.114 1.00 22.31  ?  177 GLU B CA    1 
ATOM   3736 C  C     . GLU B 1 177 ? -5.876  9.772   -28.591 1.00 16.38  ?  177 GLU B C     1 
ATOM   3737 O  O     . GLU B 1 177 ? -5.593  8.787   -29.277 1.00 15.51  ?  177 GLU B O     1 
ATOM   3738 C  CB    . GLU B 1 177 ? -6.977  8.309   -26.898 1.00 15.25  ?  177 GLU B CB    1 
ATOM   3739 C  CG    . GLU B 1 177 ? -6.828  7.782   -25.513 1.00 19.30  ?  177 GLU B CG    1 
ATOM   3740 C  CD    . GLU B 1 177 ? -7.859  6.736   -25.219 1.00 29.02  ?  177 GLU B CD    1 
ATOM   3741 O  OE1   . GLU B 1 177 ? -7.554  5.525   -25.359 1.00 33.55  ?  177 GLU B OE1   1 
ATOM   3742 O  OE2   . GLU B 1 177 ? -8.994  7.137   -24.904 1.00 25.05  ?  177 GLU B OE2   1 
ATOM   3743 N  N     . GLU B 1 178 ? -5.953  11.001  -29.109 1.00 13.93  ?  178 GLU B N     1 
ATOM   3744 C  CA    . GLU B 1 178 ? -5.552  11.222  -30.491 1.00 15.45  ?  178 GLU B CA    1 
ATOM   3745 C  C     . GLU B 1 178 ? -4.070  10.925  -30.672 1.00 12.59  ?  178 GLU B C     1 
ATOM   3746 O  O     . GLU B 1 178 ? -3.646  10.502  -31.754 1.00 14.62  ?  178 GLU B O     1 
ATOM   3747 C  CB    . GLU B 1 178 ? -5.903  12.653  -30.924 1.00 16.96  ?  178 GLU B CB    1 
ATOM   3748 C  CG    . GLU B 1 178 ? -4.941  13.751  -30.464 1.00 15.04  ?  178 GLU B CG    1 
ATOM   3749 C  CD    . GLU B 1 178 ? -4.928  13.982  -28.956 1.00 25.74  ?  178 GLU B CD    1 
ATOM   3750 O  OE1   . GLU B 1 178 ? -5.760  13.386  -28.216 1.00 24.00  ?  178 GLU B OE1   1 
ATOM   3751 O  OE2   . GLU B 1 178 ? -4.056  14.764  -28.506 1.00 30.44  ?  178 GLU B OE2   1 
ATOM   3752 N  N     . ASP B 1 179 ? -3.274  11.115  -29.615 1.00 12.96  ?  179 ASP B N     1 
ATOM   3753 C  CA    . ASP B 1 179 ? -1.864  10.756  -29.664 1.00 11.32  ?  179 ASP B CA    1 
ATOM   3754 C  C     . ASP B 1 179 ? -1.685  9.258   -29.820 1.00 18.18  ?  179 ASP B C     1 
ATOM   3755 O  O     . ASP B 1 179 ? -0.848  8.807   -30.620 1.00 13.21  ?  179 ASP B O     1 
ATOM   3756 C  CB    . ASP B 1 179 ? -1.127  11.232  -28.404 1.00 14.70  ?  179 ASP B CB    1 
ATOM   3757 C  CG    . ASP B 1 179 ? -1.887  10.936  -27.100 1.00 22.94  ?  179 ASP B CG    1 
ATOM   3758 O  OD1   . ASP B 1 179 ? -3.122  10.693  -27.125 1.00 15.22  ?  179 ASP B OD1   1 
ATOM   3759 O  OD2   . ASP B 1 179 ? -1.211  10.880  -26.038 1.00 24.94  ?  179 ASP B OD2   1 
ATOM   3760 N  N     . TRP B 1 180 ? -2.439  8.466   -29.045 1.00 14.13  ?  180 TRP B N     1 
ATOM   3761 C  CA    . TRP B 1 180 ? -2.314  7.014   -29.142 1.00 13.08  ?  180 TRP B CA    1 
ATOM   3762 C  C     . TRP B 1 180 ? -2.627  6.543   -30.547 1.00 13.61  ?  180 TRP B C     1 
ATOM   3763 O  O     . TRP B 1 180 ? -1.866  5.774   -31.140 1.00 16.71  ?  180 TRP B O     1 
ATOM   3764 C  CB    . TRP B 1 180 ? -3.240  6.318   -28.140 1.00 13.00  ?  180 TRP B CB    1 
ATOM   3765 C  CG    . TRP B 1 180 ? -3.001  4.830   -28.096 1.00 14.60  ?  180 TRP B CG    1 
ATOM   3766 C  CD1   . TRP B 1 180 ? -1.793  4.192   -28.137 1.00 13.27  ?  180 TRP B CD1   1 
ATOM   3767 C  CD2   . TRP B 1 180 ? -3.994  3.800   -28.003 1.00 20.27  ?  180 TRP B CD2   1 
ATOM   3768 N  NE1   . TRP B 1 180 ? -1.970  2.828   -28.087 1.00 13.38  ?  180 TRP B NE1   1 
ATOM   3769 C  CE2   . TRP B 1 180 ? -3.313  2.560   -27.999 1.00 22.06  ?  180 TRP B CE2   1 
ATOM   3770 C  CE3   . TRP B 1 180 ? -5.394  3.803   -27.926 1.00 16.99  ?  180 TRP B CE3   1 
ATOM   3771 C  CZ2   . TRP B 1 180 ? -3.990  1.331   -27.906 1.00 17.19  ?  180 TRP B CZ2   1 
ATOM   3772 C  CZ3   . TRP B 1 180 ? -6.057  2.584   -27.843 1.00 18.97  ?  180 TRP B CZ3   1 
ATOM   3773 C  CH2   . TRP B 1 180 ? -5.352  1.368   -27.840 1.00 15.68  ?  180 TRP B CH2   1 
ATOM   3774 N  N     . ASP B 1 181 ? -3.755  7.000   -31.095 1.00 13.84  ?  181 ASP B N     1 
ATOM   3775 C  CA    . ASP B 1 181 ? -4.155  6.616   -32.443 1.00 13.33  ?  181 ASP B CA    1 
ATOM   3776 C  C     . ASP B 1 181 ? -3.100  7.024   -33.479 1.00 16.39  ?  181 ASP B C     1 
ATOM   3777 O  O     . ASP B 1 181 ? -2.872  6.303   -34.460 1.00 11.16  ?  181 ASP B O     1 
ATOM   3778 C  CB    . ASP B 1 181 ? -5.515  7.246   -32.745 1.00 13.42  ?  181 ASP B CB    1 
ATOM   3779 C  CG    . ASP B 1 181 ? -5.944  7.078   -34.184 1.00 19.95  ?  181 ASP B CG    1 
ATOM   3780 O  OD1   . ASP B 1 181 ? -6.402  5.959   -34.530 1.00 19.42  ?  181 ASP B OD1   1 
ATOM   3781 O  OD2   . ASP B 1 181 ? -5.825  8.068   -34.966 1.00 18.99  ?  181 ASP B OD2   1 
ATOM   3782 N  N     . PHE B 1 182 ? -2.428  8.159   -33.261 1.00 11.64  ?  182 PHE B N     1 
ATOM   3783 C  CA    . PHE B 1 182 ? -1.417  8.632   -34.214 1.00 13.88  ?  182 PHE B CA    1 
ATOM   3784 C  C     . PHE B 1 182 ? -0.163  7.773   -34.158 1.00 14.03  ?  182 PHE B C     1 
ATOM   3785 O  O     . PHE B 1 182 ? 0.418   7.441   -35.198 1.00 11.18  ?  182 PHE B O     1 
ATOM   3786 C  CB    . PHE B 1 182 ? -1.073  10.093  -33.924 1.00 12.16  ?  182 PHE B CB    1 
ATOM   3787 C  CG    . PHE B 1 182 ? 0.018   10.655  -34.797 1.00 16.34  ?  182 PHE B CG    1 
ATOM   3788 C  CD1   . PHE B 1 182 ? -0.239  10.993  -36.125 1.00 12.35  ?  182 PHE B CD1   1 
ATOM   3789 C  CD2   . PHE B 1 182 ? 1.291   10.871  -34.279 1.00 12.53  ?  182 PHE B CD2   1 
ATOM   3790 C  CE1   . PHE B 1 182 ? 0.773   11.528  -36.929 1.00 20.35  ?  182 PHE B CE1   1 
ATOM   3791 C  CE2   . PHE B 1 182 ? 2.287   11.397  -35.052 1.00 14.64  ?  182 PHE B CE2   1 
ATOM   3792 C  CZ    . PHE B 1 182 ? 2.036   11.734  -36.393 1.00 16.10  ?  182 PHE B CZ    1 
ATOM   3793 N  N     . PHE B 1 183 ? 0.250   7.378   -32.950 1.00 16.11  ?  183 PHE B N     1 
ATOM   3794 C  CA    . PHE B 1 183 ? 1.391   6.480   -32.807 1.00 17.02  ?  183 PHE B CA    1 
ATOM   3795 C  C     . PHE B 1 183 ? 1.123   5.133   -33.470 1.00 14.91  ?  183 PHE B C     1 
ATOM   3796 O  O     . PHE B 1 183 ? 2.016   4.549   -34.097 1.00 12.80  ?  183 PHE B O     1 
ATOM   3797 C  CB    . PHE B 1 183 ? 1.721   6.273   -31.328 1.00 14.98  ?  183 PHE B CB    1 
ATOM   3798 C  CG    . PHE B 1 183 ? 1.986   7.543   -30.571 1.00 14.39  ?  183 PHE B CG    1 
ATOM   3799 C  CD1   . PHE B 1 183 ? 2.612   8.624   -31.185 1.00 11.93  ?  183 PHE B CD1   1 
ATOM   3800 C  CD2   . PHE B 1 183 ? 1.581   7.659   -29.228 1.00 13.61  ?  183 PHE B CD2   1 
ATOM   3801 C  CE1   . PHE B 1 183 ? 2.853   9.798   -30.486 1.00 8.40   ?  183 PHE B CE1   1 
ATOM   3802 C  CE2   . PHE B 1 183 ? 1.824   8.815   -28.517 1.00 11.66  ?  183 PHE B CE2   1 
ATOM   3803 C  CZ    . PHE B 1 183 ? 2.460   9.897   -29.140 1.00 12.27  ?  183 PHE B CZ    1 
ATOM   3804 N  N     . LEU B 1 184 ? -0.100  4.621   -33.333 1.00 14.53  ?  184 LEU B N     1 
ATOM   3805 C  CA    . LEU B 1 184 ? -0.455  3.367   -33.984 1.00 14.55  ?  184 LEU B CA    1 
ATOM   3806 C  C     . LEU B 1 184 ? -0.487  3.523   -35.497 1.00 17.47  ?  184 LEU B C     1 
ATOM   3807 O  O     . LEU B 1 184 ? -0.134  2.589   -36.230 1.00 15.77  ?  184 LEU B O     1 
ATOM   3808 C  CB    . LEU B 1 184 ? -1.807  2.885   -33.477 1.00 12.75  ?  184 LEU B CB    1 
ATOM   3809 C  CG    . LEU B 1 184 ? -1.802  2.533   -31.992 1.00 17.23  ?  184 LEU B CG    1 
ATOM   3810 C  CD1   . LEU B 1 184 ? -3.130  1.936   -31.589 1.00 19.41  ?  184 LEU B CD1   1 
ATOM   3811 C  CD2   . LEU B 1 184 ? -0.651  1.572   -31.651 1.00 20.25  ?  184 LEU B CD2   1 
ATOM   3812 N  N     . ARG B 1 185 ? -0.950  4.678   -35.982 1.00 11.26  ?  185 ARG B N     1 
ATOM   3813 C  CA    . ARG B 1 185 ? -0.970  4.922   -37.418 1.00 18.21  ?  185 ARG B CA    1 
ATOM   3814 C  C     . ARG B 1 185 ? 0.442   4.875   -37.989 1.00 19.17  ?  185 ARG B C     1 
ATOM   3815 O  O     . ARG B 1 185 ? 0.666   4.323   -39.071 1.00 14.76  ?  185 ARG B O     1 
ATOM   3816 C  CB    . ARG B 1 185 ? -1.627  6.274   -37.714 1.00 15.67  ?  185 ARG B CB    1 
ATOM   3817 C  CG    . ARG B 1 185 ? -1.548  6.715   -39.164 1.00 14.67  ?  185 ARG B CG    1 
ATOM   3818 C  CD    . ARG B 1 185 ? -2.559  7.816   -39.464 1.00 19.87  ?  185 ARG B CD    1 
ATOM   3819 N  NE    . ARG B 1 185 ? -3.881  7.435   -38.988 1.00 21.80  ?  185 ARG B NE    1 
ATOM   3820 C  CZ    . ARG B 1 185 ? -4.485  7.961   -37.933 1.00 21.80  ?  185 ARG B CZ    1 
ATOM   3821 N  NH1   . ARG B 1 185 ? -3.980  9.006   -37.298 1.00 14.48  ?  185 ARG B NH1   1 
ATOM   3822 N  NH2   . ARG B 1 185 ? -5.604  7.394   -37.476 1.00 24.73  ?  185 ARG B NH2   1 
ATOM   3823 N  N     . LEU B 1 186 ? 1.410   5.433   -37.255 1.00 17.72  ?  186 LEU B N     1 
ATOM   3824 C  CA    . LEU B 1 186 ? 2.793   5.405   -37.705 1.00 17.77  ?  186 LEU B CA    1 
ATOM   3825 C  C     . LEU B 1 186 ? 3.367   3.996   -37.608 1.00 15.77  ?  186 LEU B C     1 
ATOM   3826 O  O     . LEU B 1 186 ? 3.948   3.481   -38.569 1.00 17.66  ?  186 LEU B O     1 
ATOM   3827 C  CB    . LEU B 1 186 ? 3.624   6.399   -36.888 1.00 15.89  ?  186 LEU B CB    1 
ATOM   3828 C  CG    . LEU B 1 186 ? 3.299   7.892   -37.097 1.00 18.71  ?  186 LEU B CG    1 
ATOM   3829 C  CD1   . LEU B 1 186 ? 4.221   8.802   -36.298 1.00 10.82  ?  186 LEU B CD1   1 
ATOM   3830 C  CD2   . LEU B 1 186 ? 3.351   8.254   -38.569 1.00 18.20  ?  186 LEU B CD2   1 
ATOM   3831 N  N     . ALA B 1 187 ? 3.217   3.356   -36.457 1.00 16.45  ?  187 ALA B N     1 
ATOM   3832 C  CA    . ALA B 1 187 ? 3.858   2.060   -36.251 1.00 19.83  ?  187 ALA B CA    1 
ATOM   3833 C  C     . ALA B 1 187 ? 3.182   0.969   -37.067 1.00 19.66  ?  187 ALA B C     1 
ATOM   3834 O  O     . ALA B 1 187 ? 3.857   0.108   -37.649 1.00 16.34  ?  187 ALA B O     1 
ATOM   3835 C  CB    . ALA B 1 187 ? 3.844   1.705   -34.766 1.00 18.67  ?  187 ALA B CB    1 
ATOM   3836 N  N     . HIS B 1 188 ? 1.852   0.986   -37.115 1.00 19.21  ?  188 HIS B N     1 
ATOM   3837 C  CA    . HIS B 1 188 ? 1.088   -0.062  -37.777 1.00 24.22  ?  188 HIS B CA    1 
ATOM   3838 C  C     . HIS B 1 188 ? 0.702   0.328   -39.190 1.00 21.89  ?  188 HIS B C     1 
ATOM   3839 O  O     . HIS B 1 188 ? 0.876   -0.463  -40.119 1.00 23.07  ?  188 HIS B O     1 
ATOM   3840 C  CB    . HIS B 1 188 ? -0.177  -0.401  -36.973 1.00 21.82  ?  188 HIS B CB    1 
ATOM   3841 C  CG    . HIS B 1 188 ? 0.103   -1.118  -35.697 1.00 28.52  ?  188 HIS B CG    1 
ATOM   3842 N  ND1   . HIS B 1 188 ? -0.766  -2.039  -35.156 1.00 36.04  ?  188 HIS B ND1   1 
ATOM   3843 C  CD2   . HIS B 1 188 ? 1.157   -1.048  -34.849 1.00 33.33  ?  188 HIS B CD2   1 
ATOM   3844 C  CE1   . HIS B 1 188 ? -0.257  -2.512  -34.033 1.00 38.42  ?  188 HIS B CE1   1 
ATOM   3845 N  NE2   . HIS B 1 188 ? 0.910   -1.927  -33.824 1.00 35.26  ?  188 HIS B NE2   1 
ATOM   3846 N  N     . GLY B 1 189 ? 0.162   1.534   -39.368 1.00 17.21  ?  189 GLY B N     1 
ATOM   3847 C  CA    . GLY B 1 189 ? -0.223  1.952   -40.704 1.00 19.82  ?  189 GLY B CA    1 
ATOM   3848 C  C     . GLY B 1 189 ? 0.970   2.105   -41.633 1.00 20.00  ?  189 GLY B C     1 
ATOM   3849 O  O     . GLY B 1 189 ? 0.953   1.605   -42.759 1.00 22.96  ?  189 GLY B O     1 
ATOM   3850 N  N     . HIS B 1 190 ? 2.033   2.772   -41.164 1.00 20.33  ?  190 HIS B N     1 
ATOM   3851 C  CA    . HIS B 1 190 ? 3.141   3.193   -42.024 1.00 24.89  ?  190 HIS B CA    1 
ATOM   3852 C  C     . HIS B 1 190 ? 4.453   2.473   -41.739 1.00 21.96  ?  190 HIS B C     1 
ATOM   3853 O  O     . HIS B 1 190 ? 5.486   2.848   -42.310 1.00 26.22  ?  190 HIS B O     1 
ATOM   3854 C  CB    . HIS B 1 190 ? 3.352   4.706   -41.912 1.00 17.72  ?  190 HIS B CB    1 
ATOM   3855 C  CG    . HIS B 1 190 ? 2.213   5.507   -42.458 1.00 21.16  ?  190 HIS B CG    1 
ATOM   3856 N  ND1   . HIS B 1 190 ? 1.021   5.668   -41.780 1.00 20.78  ?  190 HIS B ND1   1 
ATOM   3857 C  CD2   . HIS B 1 190 ? 2.084   6.195   -43.617 1.00 19.99  ?  190 HIS B CD2   1 
ATOM   3858 C  CE1   . HIS B 1 190 ? 0.206   6.420   -42.500 1.00 16.30  ?  190 HIS B CE1   1 
ATOM   3859 N  NE2   . HIS B 1 190 ? 0.828   6.752   -43.619 1.00 24.20  ?  190 HIS B NE2   1 
ATOM   3860 N  N     . LYS B 1 191 ? 4.446   1.473   -40.861 1.00 19.28  ?  191 LYS B N     1 
ATOM   3861 C  CA    . LYS B 1 191 ? 5.580   0.578   -40.620 1.00 23.38  ?  191 LYS B CA    1 
ATOM   3862 C  C     . LYS B 1 191 ? 6.797   1.277   -40.014 1.00 22.39  ?  191 LYS B C     1 
ATOM   3863 O  O     . LYS B 1 191 ? 7.929   0.789   -40.152 1.00 18.96  ?  191 LYS B O     1 
ATOM   3864 C  CB    . LYS B 1 191 ? 5.987   -0.156  -41.904 1.00 22.62  ?  191 LYS B CB    1 
ATOM   3865 C  CG    . LYS B 1 191 ? 4.892   -1.072  -42.445 1.00 26.87  ?  191 LYS B CG    1 
ATOM   3866 C  CD    . LYS B 1 191 ? 4.092   -1.720  -41.312 1.00 24.77  ?  191 LYS B CD    1 
ATOM   3867 C  CE    . LYS B 1 191 ? 3.074   -2.724  -41.846 1.00 35.95  ?  191 LYS B CE    1 
ATOM   3868 N  NZ    . LYS B 1 191 ? 2.459   -3.540  -40.747 1.00 47.72  ?  191 LYS B NZ    1 
ATOM   3869 N  N     . TYR B 1 192 ? 6.585   2.406   -39.344 1.00 17.12  ?  192 TYR B N     1 
ATOM   3870 C  CA    . TYR B 1 192 ? 7.656   3.134   -38.683 1.00 14.30  ?  192 TYR B CA    1 
ATOM   3871 C  C     . TYR B 1 192 ? 8.422   2.212   -37.746 1.00 17.56  ?  192 TYR B C     1 
ATOM   3872 O  O     . TYR B 1 192 ? 7.824   1.462   -36.970 1.00 19.55  ?  192 TYR B O     1 
ATOM   3873 C  CB    . TYR B 1 192 ? 7.063   4.312   -37.896 1.00 20.20  ?  192 TYR B CB    1 
ATOM   3874 C  CG    . TYR B 1 192 ? 6.960   5.574   -38.702 1.00 18.48  ?  192 TYR B CG    1 
ATOM   3875 C  CD1   . TYR B 1 192 ? 6.508   5.541   -40.014 1.00 21.18  ?  192 TYR B CD1   1 
ATOM   3876 C  CD2   . TYR B 1 192 ? 7.344   6.793   -38.169 1.00 14.57  ?  192 TYR B CD2   1 
ATOM   3877 C  CE1   . TYR B 1 192 ? 6.426   6.701   -40.772 1.00 25.99  ?  192 TYR B CE1   1 
ATOM   3878 C  CE2   . TYR B 1 192 ? 7.282   7.954   -38.925 1.00 15.52  ?  192 TYR B CE2   1 
ATOM   3879 C  CZ    . TYR B 1 192 ? 6.805   7.906   -40.218 1.00 18.82  ?  192 TYR B CZ    1 
ATOM   3880 O  OH    . TYR B 1 192 ? 6.738   9.056   -40.976 1.00 22.71  ?  192 TYR B OH    1 
ATOM   3881 N  N     . ARG B 1 193 ? 9.747   2.274   -37.817 1.00 16.93  ?  193 ARG B N     1 
ATOM   3882 C  CA    . ARG B 1 193 ? 10.606  1.468   -36.953 1.00 18.03  ?  193 ARG B CA    1 
ATOM   3883 C  C     . ARG B 1 193 ? 10.777  2.206   -35.629 1.00 15.10  ?  193 ARG B C     1 
ATOM   3884 O  O     . ARG B 1 193 ? 11.341  3.310   -35.584 1.00 10.46  ?  193 ARG B O     1 
ATOM   3885 C  CB    . ARG B 1 193 ? 11.950  1.183   -37.625 1.00 9.66   ?  193 ARG B CB    1 
ATOM   3886 C  CG    . ARG B 1 193 ? 11.837  0.243   -38.806 1.00 19.04  ?  193 ARG B CG    1 
ATOM   3887 C  CD    . ARG B 1 193 ? 13.068  0.296   -39.767 1.00 20.83  ?  193 ARG B CD    1 
ATOM   3888 N  NE    . ARG B 1 193 ? 13.034  1.495   -40.603 1.00 24.48  ?  193 ARG B NE    1 
ATOM   3889 C  CZ    . ARG B 1 193 ? 14.051  1.976   -41.315 1.00 29.19  ?  193 ARG B CZ    1 
ATOM   3890 N  NH1   . ARG B 1 193 ? 15.149  1.259   -41.542 1.00 17.84  ?  193 ARG B NH1   1 
ATOM   3891 N  NH2   . ARG B 1 193 ? 13.957  3.203   -41.827 1.00 23.30  ?  193 ARG B NH2   1 
ATOM   3892 N  N     . VAL B 1 194 ? 10.275  1.606   -34.549 1.00 13.46  ?  194 VAL B N     1 
ATOM   3893 C  CA    . VAL B 1 194 ? 10.159  2.284   -33.268 1.00 11.56  ?  194 VAL B CA    1 
ATOM   3894 C  C     . VAL B 1 194 ? 11.339  1.892   -32.396 1.00 13.27  ?  194 VAL B C     1 
ATOM   3895 O  O     . VAL B 1 194 ? 11.694  0.711   -32.312 1.00 19.57  ?  194 VAL B O     1 
ATOM   3896 C  CB    . VAL B 1 194 ? 8.829   1.952   -32.571 1.00 15.66  ?  194 VAL B CB    1 
ATOM   3897 C  CG1   . VAL B 1 194 ? 8.794   2.615   -31.213 1.00 13.89  ?  194 VAL B CG1   1 
ATOM   3898 C  CG2   . VAL B 1 194 ? 7.651   2.409   -33.407 1.00 12.06  ?  194 VAL B CG2   1 
ATOM   3899 N  N     . VAL B 1 195 ? 11.951  2.890   -31.760 1.00 17.63  ?  195 VAL B N     1 
ATOM   3900 C  CA    . VAL B 1 195 ? 13.087  2.715   -30.863 1.00 19.80  ?  195 VAL B CA    1 
ATOM   3901 C  C     . VAL B 1 195 ? 12.840  3.527   -29.590 1.00 25.28  ?  195 VAL B C     1 
ATOM   3902 O  O     . VAL B 1 195 ? 12.385  4.678   -29.645 1.00 16.90  ?  195 VAL B O     1 
ATOM   3903 C  CB    . VAL B 1 195 ? 14.407  3.144   -31.536 1.00 19.33  ?  195 VAL B CB    1 
ATOM   3904 C  CG1   . VAL B 1 195 ? 15.518  3.209   -30.516 1.00 19.60  ?  195 VAL B CG1   1 
ATOM   3905 C  CG2   . VAL B 1 195 ? 14.774  2.169   -32.692 1.00 14.56  ?  195 VAL B CG2   1 
ATOM   3906 N  N     . HIS B 1 196 ? 13.143  2.920   -28.445 1.00 19.78  ?  196 HIS B N     1 
ATOM   3907 C  CA    . HIS B 1 196 ? 13.078  3.581   -27.151 1.00 21.50  ?  196 HIS B CA    1 
ATOM   3908 C  C     . HIS B 1 196 ? 14.454  4.128   -26.780 1.00 21.73  ?  196 HIS B C     1 
ATOM   3909 O  O     . HIS B 1 196 ? 15.466  3.435   -26.925 1.00 22.66  ?  196 HIS B O     1 
ATOM   3910 C  CB    . HIS B 1 196 ? 12.592  2.590   -26.091 1.00 23.38  ?  196 HIS B CB    1 
ATOM   3911 C  CG    . HIS B 1 196 ? 12.560  3.150   -24.706 1.00 23.22  ?  196 HIS B CG    1 
ATOM   3912 N  ND1   . HIS B 1 196 ? 12.787  2.376   -23.591 1.00 22.23  ?  196 HIS B ND1   1 
ATOM   3913 C  CD2   . HIS B 1 196 ? 12.328  4.405   -24.255 1.00 22.46  ?  196 HIS B CD2   1 
ATOM   3914 C  CE1   . HIS B 1 196 ? 12.694  3.130   -22.509 1.00 24.19  ?  196 HIS B CE1   1 
ATOM   3915 N  NE2   . HIS B 1 196 ? 12.419  4.367   -22.884 1.00 23.61  ?  196 HIS B NE2   1 
ATOM   3916 N  N     . GLN B 1 197 ? 14.495  5.365   -26.288 1.00 21.65  ?  197 GLN B N     1 
ATOM   3917 C  CA    . GLN B 1 197 ? 15.749  6.017   -25.909 1.00 25.11  ?  197 GLN B CA    1 
ATOM   3918 C  C     . GLN B 1 197 ? 15.693  6.417   -24.435 1.00 22.57  ?  197 GLN B C     1 
ATOM   3919 O  O     . GLN B 1 197 ? 15.279  7.535   -24.095 1.00 18.62  ?  197 GLN B O     1 
ATOM   3920 C  CB    . GLN B 1 197 ? 16.033  7.213   -26.823 1.00 14.45  ?  197 GLN B CB    1 
ATOM   3921 C  CG    . GLN B 1 197 ? 17.118  8.180   -26.357 1.00 20.77  ?  197 GLN B CG    1 
ATOM   3922 C  CD    . GLN B 1 197 ? 18.485  7.544   -26.116 1.00 25.18  ?  197 GLN B CD    1 
ATOM   3923 O  OE1   . GLN B 1 197 ? 18.625  6.629   -25.308 1.00 21.05  ?  197 GLN B OE1   1 
ATOM   3924 N  NE2   . GLN B 1 197 ? 19.509  8.045   -26.821 1.00 22.62  ?  197 GLN B NE2   1 
ATOM   3925 N  N     . PRO B 1 198 ? 16.102  5.533   -23.520 1.00 25.47  ?  198 PRO B N     1 
ATOM   3926 C  CA    . PRO B 1 198 ? 16.036  5.856   -22.083 1.00 20.99  ?  198 PRO B CA    1 
ATOM   3927 C  C     . PRO B 1 198 ? 17.151  6.763   -21.589 1.00 23.93  ?  198 PRO B C     1 
ATOM   3928 O  O     . PRO B 1 198 ? 17.164  7.105   -20.401 1.00 27.14  ?  198 PRO B O     1 
ATOM   3929 C  CB    . PRO B 1 198 ? 16.135  4.476   -21.423 1.00 23.98  ?  198 PRO B CB    1 
ATOM   3930 C  CG    . PRO B 1 198 ? 17.029  3.683   -22.375 1.00 23.57  ?  198 PRO B CG    1 
ATOM   3931 C  CD    . PRO B 1 198 ? 16.676  4.196   -23.774 1.00 24.17  ?  198 PRO B CD    1 
ATOM   3932 N  N     . GLU B 1 199 ? 18.095  7.145   -22.448 1.00 20.53  ?  199 GLU B N     1 
ATOM   3933 C  CA    . GLU B 1 199 ? 19.166  8.053   -22.060 1.00 19.83  ?  199 GLU B CA    1 
ATOM   3934 C  C     . GLU B 1 199 ? 18.702  9.494   -22.019 1.00 22.53  ?  199 GLU B C     1 
ATOM   3935 O  O     . GLU B 1 199 ? 19.419  10.352  -21.484 1.00 24.35  ?  199 GLU B O     1 
ATOM   3936 C  CB    . GLU B 1 199 ? 20.345  7.945   -23.040 1.00 25.21  ?  199 GLU B CB    1 
ATOM   3937 C  CG    . GLU B 1 199 ? 21.086  6.605   -23.096 1.00 31.87  ?  199 GLU B CG    1 
ATOM   3938 C  CD    . GLU B 1 199 ? 21.218  5.911   -21.746 1.00 45.78  ?  199 GLU B CD    1 
ATOM   3939 O  OE1   . GLU B 1 199 ? 21.482  6.598   -20.724 1.00 52.70  ?  199 GLU B OE1   1 
ATOM   3940 O  OE2   . GLU B 1 199 ? 21.083  4.665   -21.709 1.00 52.21  ?  199 GLU B OE2   1 
ATOM   3941 N  N     . VAL B 1 200 ? 17.546  9.785   -22.615 1.00 22.24  ?  200 VAL B N     1 
ATOM   3942 C  CA    . VAL B 1 200 ? 16.961  11.117  -22.598 1.00 22.03  ?  200 VAL B CA    1 
ATOM   3943 C  C     . VAL B 1 200 ? 15.644  11.042  -21.834 1.00 21.37  ?  200 VAL B C     1 
ATOM   3944 O  O     . VAL B 1 200 ? 14.983  10.001  -21.811 1.00 16.44  ?  200 VAL B O     1 
ATOM   3945 C  CB    . VAL B 1 200 ? 16.750  11.660  -24.026 1.00 17.73  ?  200 VAL B CB    1 
ATOM   3946 C  CG1   . VAL B 1 200 ? 16.322  13.109  -23.996 1.00 22.06  ?  200 VAL B CG1   1 
ATOM   3947 C  CG2   . VAL B 1 200 ? 18.048  11.526  -24.847 1.00 24.00  ?  200 VAL B CG2   1 
ATOM   3948 N  N     . ALA B 1 201 ? 15.266  12.152  -21.199 1.00 20.20  ?  201 ALA B N     1 
ATOM   3949 C  CA    . ALA B 1 201 ? 13.975  12.264  -20.538 1.00 20.22  ?  201 ALA B CA    1 
ATOM   3950 C  C     . ALA B 1 201 ? 13.436  13.670  -20.733 1.00 20.04  ?  201 ALA B C     1 
ATOM   3951 O  O     . ALA B 1 201 ? 14.190  14.616  -20.963 1.00 22.19  ?  201 ALA B O     1 
ATOM   3952 C  CB    . ALA B 1 201 ? 14.064  11.940  -19.039 1.00 19.38  ?  201 ALA B CB    1 
ATOM   3953 N  N     . ILE B 1 202 ? 12.115  13.792  -20.671 1.00 20.80  ?  202 ILE B N     1 
ATOM   3954 C  CA    . ILE B 1 202 ? 11.458  15.086  -20.626 1.00 22.59  ?  202 ILE B CA    1 
ATOM   3955 C  C     . ILE B 1 202 ? 10.766  15.222  -19.275 1.00 21.22  ?  202 ILE B C     1 
ATOM   3956 O  O     . ILE B 1 202 ? 10.665  14.271  -18.503 1.00 22.85  ?  202 ILE B O     1 
ATOM   3957 C  CB    . ILE B 1 202 ? 10.458  15.279  -21.786 1.00 20.29  ?  202 ILE B CB    1 
ATOM   3958 C  CG1   . ILE B 1 202 ? 9.363   14.207  -21.746 1.00 20.33  ?  202 ILE B CG1   1 
ATOM   3959 C  CG2   . ILE B 1 202 ? 11.178  15.282  -23.110 1.00 19.26  ?  202 ILE B CG2   1 
ATOM   3960 C  CD1   . ILE B 1 202 ? 8.001   14.684  -22.242 1.00 15.89  ?  202 ILE B CD1   1 
ATOM   3961 N  N     . ALA B 1 203 ? 10.298  16.430  -18.984 1.00 20.47  ?  203 ALA B N     1 
ATOM   3962 C  CA    . ALA B 1 203 ? 9.379   16.650  -17.880 1.00 19.92  ?  203 ALA B CA    1 
ATOM   3963 C  C     . ALA B 1 203 ? 7.999   16.886  -18.469 1.00 21.22  ?  203 ALA B C     1 
ATOM   3964 O  O     . ALA B 1 203 ? 7.801   17.842  -19.232 1.00 20.56  ?  203 ALA B O     1 
ATOM   3965 C  CB    . ALA B 1 203 ? 9.811   17.825  -17.009 1.00 24.63  ?  203 ALA B CB    1 
ATOM   3966 N  N     . LEU B 1 204 ? 7.071   15.980  -18.162 1.00 20.10  ?  204 LEU B N     1 
ATOM   3967 C  CA    . LEU B 1 204 ? 5.663   16.130  -18.504 1.00 22.37  ?  204 LEU B CA    1 
ATOM   3968 C  C     . LEU B 1 204 ? 4.926   16.602  -17.257 1.00 24.24  ?  204 LEU B C     1 
ATOM   3969 O  O     . LEU B 1 204 ? 4.906   15.901  -16.236 1.00 24.18  ?  204 LEU B O     1 
ATOM   3970 C  CB    . LEU B 1 204 ? 5.076   14.815  -19.011 1.00 25.52  ?  204 LEU B CB    1 
ATOM   3971 C  CG    . LEU B 1 204 ? 3.687   14.892  -19.648 1.00 28.99  ?  204 LEU B CG    1 
ATOM   3972 C  CD1   . LEU B 1 204 ? 3.590   13.935  -20.827 1.00 29.32  ?  204 LEU B CD1   1 
ATOM   3973 C  CD2   . LEU B 1 204 ? 2.594   14.601  -18.619 1.00 26.85  ?  204 LEU B CD2   1 
ATOM   3974 N  N     . HIS B 1 205 ? 4.316   17.777  -17.341 1.00 24.40  ?  205 HIS B N     1 
ATOM   3975 C  CA    . HIS B 1 205 ? 3.782   18.450  -16.164 1.00 25.25  ?  205 HIS B CA    1 
ATOM   3976 C  C     . HIS B 1 205 ? 2.375   17.951  -15.842 1.00 25.54  ?  205 HIS B C     1 
ATOM   3977 O  O     . HIS B 1 205 ? 1.472   18.018  -16.684 1.00 28.29  ?  205 HIS B O     1 
ATOM   3978 C  CB    . HIS B 1 205 ? 3.792   19.958  -16.388 1.00 24.72  ?  205 HIS B CB    1 
ATOM   3979 C  CG    . HIS B 1 205 ? 5.127   20.586  -16.143 1.00 26.16  ?  205 HIS B CG    1 
ATOM   3980 N  ND1   . HIS B 1 205 ? 5.793   21.319  -17.101 1.00 25.66  ?  205 HIS B ND1   1 
ATOM   3981 C  CD2   . HIS B 1 205 ? 5.919   20.590  -15.045 1.00 24.69  ?  205 HIS B CD2   1 
ATOM   3982 C  CE1   . HIS B 1 205 ? 6.936   21.754  -16.601 1.00 26.75  ?  205 HIS B CE1   1 
ATOM   3983 N  NE2   . HIS B 1 205 ? 7.037   21.323  -15.355 1.00 27.10  ?  205 HIS B NE2   1 
ATOM   3984 N  N     . ARG B 1 206 ? 2.195   17.435  -14.629 1.00 22.23  ?  206 ARG B N     1 
ATOM   3985 C  CA    . ARG B 1 206 ? 0.869   17.092  -14.104 1.00 28.67  ?  206 ARG B CA    1 
ATOM   3986 C  C     . ARG B 1 206 ? 0.837   17.571  -12.652 1.00 29.08  ?  206 ARG B C     1 
ATOM   3987 O  O     . ARG B 1 206 ? 1.168   16.816  -11.733 1.00 32.46  ?  206 ARG B O     1 
ATOM   3988 C  CB    . ARG B 1 206 ? 0.570   15.605  -14.225 1.00 27.86  ?  206 ARG B CB    1 
ATOM   3989 C  CG    . ARG B 1 206 ? 0.839   15.026  -15.606 1.00 40.58  ?  206 ARG B CG    1 
ATOM   3990 C  CD    . ARG B 1 206 ? -0.361  14.259  -16.149 1.00 44.29  ?  206 ARG B CD    1 
ATOM   3991 N  NE    . ARG B 1 206 ? -0.420  12.930  -15.554 1.00 49.55  ?  206 ARG B NE    1 
ATOM   3992 C  CZ    . ARG B 1 206 ? -1.331  12.531  -14.676 1.00 46.48  ?  206 ARG B CZ    1 
ATOM   3993 N  NH1   . ARG B 1 206 ? -2.317  13.325  -14.289 1.00 41.80  ?  206 ARG B NH1   1 
ATOM   3994 N  NH2   . ARG B 1 206 ? -1.240  11.309  -14.161 1.00 49.64  ?  206 ARG B NH2   1 
ATOM   3995 N  N     . ILE B 1 207 ? 0.451   18.830  -12.461 1.00 23.10  ?  207 ILE B N     1 
ATOM   3996 C  CA    . ILE B 1 207 ? 0.358   19.451  -11.138 1.00 38.29  ?  207 ILE B CA    1 
ATOM   3997 C  C     . ILE B 1 207 ? -0.963  19.098  -10.454 1.00 36.13  ?  207 ILE B C     1 
ATOM   3998 O  O     . ILE B 1 207 ? -2.039  19.424  -10.975 1.00 39.74  ?  207 ILE B O     1 
ATOM   3999 C  CB    . ILE B 1 207 ? 0.520   20.973  -11.255 1.00 36.81  ?  207 ILE B CB    1 
ATOM   4000 C  CG1   . ILE B 1 207 ? 1.602   21.288  -12.297 1.00 34.66  ?  207 ILE B CG1   1 
ATOM   4001 C  CG2   . ILE B 1 207 ? 0.828   21.590  -9.900  1.00 31.03  ?  207 ILE B CG2   1 
ATOM   4002 C  CD1   . ILE B 1 207 ? 1.408   22.628  -12.979 1.00 41.59  ?  207 ILE B CD1   1 
ATOM   4003 N  N     . PRO B 1 208 ? -0.943  18.461  -9.285  1.00 36.65  ?  208 PRO B N     1 
ATOM   4004 C  CA    . PRO B 1 208 ? -2.210  18.092  -8.625  1.00 39.54  ?  208 PRO B CA    1 
ATOM   4005 C  C     . PRO B 1 208 ? -3.002  19.330  -8.226  1.00 36.13  ?  208 PRO B C     1 
ATOM   4006 O  O     . PRO B 1 208 ? -2.533  20.164  -7.453  1.00 41.02  ?  208 PRO B O     1 
ATOM   4007 C  CB    . PRO B 1 208 ? -1.755  17.288  -7.398  1.00 34.41  ?  208 PRO B CB    1 
ATOM   4008 C  CG    . PRO B 1 208 ? -0.294  17.040  -7.583  1.00 39.36  ?  208 PRO B CG    1 
ATOM   4009 C  CD    . PRO B 1 208 ? 0.227   18.148  -8.449  1.00 35.83  ?  208 PRO B CD    1 
ATOM   4010 N  N     . GLY B 1 209 ? -4.207  19.448  -8.765  1.00 34.33  ?  209 GLY B N     1 
ATOM   4011 C  CA    . GLY B 1 209 ? -5.077  20.572  -8.502  1.00 37.96  ?  209 GLY B CA    1 
ATOM   4012 C  C     . GLY B 1 209 ? -6.195  20.243  -7.538  1.00 39.17  ?  209 GLY B C     1 
ATOM   4013 O  O     . GLY B 1 209 ? -6.085  19.324  -6.719  1.00 35.97  ?  209 GLY B O     1 
ATOM   4014 N  N     . VAL B 1 210 ? -7.294  20.998  -7.653  1.00 41.71  ?  210 VAL B N     1 
ATOM   4015 C  CA    . VAL B 1 210 ? -8.497  20.818  -6.844  1.00 40.07  ?  210 VAL B CA    1 
ATOM   4016 C  C     . VAL B 1 210 ? -9.074  19.415  -6.973  1.00 42.50  ?  210 VAL B C     1 
ATOM   4017 O  O     . VAL B 1 210 ? -9.901  19.010  -6.154  1.00 42.14  ?  210 VAL B O     1 
ATOM   4018 C  CB    . VAL B 1 210 ? -9.534  21.896  -7.244  1.00 34.23  ?  210 VAL B CB    1 
ATOM   4019 C  CG1   . VAL B 1 210 ? -10.727 21.914  -6.306  1.00 36.56  ?  210 VAL B CG1   1 
ATOM   4020 C  CG2   . VAL B 1 210 ? -8.873  23.254  -7.276  1.00 34.59  ?  210 VAL B CG2   1 
ATOM   4021 N  N     . GLU B 1 211 ? -8.642  18.657  -7.984  1.00 47.06  ?  211 GLU B N     1 
ATOM   4022 C  CA    . GLU B 1 211 ? -8.999  17.245  -8.094  1.00 51.41  ?  211 GLU B CA    1 
ATOM   4023 C  C     . GLU B 1 211 ? -8.811  16.488  -6.783  1.00 49.22  ?  211 GLU B C     1 
ATOM   4024 O  O     . GLU B 1 211 ? -9.589  15.578  -6.475  1.00 49.98  ?  211 GLU B O     1 
ATOM   4025 C  CB    . GLU B 1 211 ? -8.148  16.593  -9.182  1.00 54.77  ?  211 GLU B CB    1 
ATOM   4026 C  CG    . GLU B 1 211 ? -6.676  17.016  -9.127  1.00 51.06  ?  211 GLU B CG    1 
ATOM   4027 C  CD    . GLU B 1 211 ? -5.729  15.941  -9.633  1.00 53.69  ?  211 GLU B CD    1 
ATOM   4028 O  OE1   . GLU B 1 211 ? -5.986  15.378  -10.720 1.00 57.45  ?  211 GLU B OE1   1 
ATOM   4029 O  OE2   . GLU B 1 211 ? -4.725  15.661  -8.941  1.00 55.00  ?  211 GLU B OE2   1 
ATOM   4030 N  N     . SER B 1 212 ? -7.795  16.853  -6.001  1.00 49.90  ?  212 SER B N     1 
ATOM   4031 C  CA    . SER B 1 212 ? -7.348  16.079  -4.850  1.00 51.79  ?  212 SER B CA    1 
ATOM   4032 C  C     . SER B 1 212 ? -8.113  16.379  -3.563  1.00 54.41  ?  212 SER B C     1 
ATOM   4033 O  O     . SER B 1 212 ? -7.794  15.792  -2.525  1.00 60.02  ?  212 SER B O     1 
ATOM   4034 C  CB    . SER B 1 212 ? -5.853  16.313  -4.612  1.00 55.63  ?  212 SER B CB    1 
ATOM   4035 O  OG    . SER B 1 212 ? -5.613  17.581  -4.022  1.00 53.58  ?  212 SER B OG    1 
ATOM   4036 N  N     . LEU B 1 213 ? -9.099  17.273  -3.591  1.00 45.74  ?  213 LEU B N     1 
ATOM   4037 C  CA    . LEU B 1 213 ? -9.936  17.505  -2.425  1.00 47.06  ?  213 LEU B CA    1 
ATOM   4038 C  C     . LEU B 1 213 ? -11.422 17.399  -2.732  1.00 51.60  ?  213 LEU B C     1 
ATOM   4039 O  O     . LEU B 1 213 ? -12.243 17.610  -1.827  1.00 52.80  ?  213 LEU B O     1 
ATOM   4040 C  CB    . LEU B 1 213 ? -9.636  18.879  -1.808  1.00 51.16  ?  213 LEU B CB    1 
ATOM   4041 C  CG    . LEU B 1 213 ? -9.618  20.085  -2.749  1.00 47.44  ?  213 LEU B CG    1 
ATOM   4042 C  CD1   . LEU B 1 213 ? -10.971 20.785  -2.762  1.00 43.38  ?  213 LEU B CD1   1 
ATOM   4043 C  CD2   . LEU B 1 213 ? -8.518  21.043  -2.336  1.00 38.51  ?  213 LEU B CD2   1 
ATOM   4044 N  N     . THR B 1 214 ? -11.789 17.092  -3.974  1.00 48.22  ?  214 THR B N     1 
ATOM   4045 C  CA    . THR B 1 214 ? -13.179 16.908  -4.366  1.00 50.43  ?  214 THR B CA    1 
ATOM   4046 C  C     . THR B 1 214 ? -13.466 15.422  -4.520  1.00 47.64  ?  214 THR B C     1 
ATOM   4047 O  O     . THR B 1 214 ? -12.691 14.691  -5.146  1.00 49.21  ?  214 THR B O     1 
ATOM   4048 C  CB    . THR B 1 214 ? -13.498 17.636  -5.673  1.00 49.38  ?  214 THR B CB    1 
ATOM   4049 O  OG1   . THR B 1 214 ? -12.640 17.149  -6.713  1.00 49.40  ?  214 THR B OG1   1 
ATOM   4050 C  CG2   . THR B 1 214 ? -13.329 19.152  -5.515  1.00 47.28  ?  214 THR B CG2   1 
ATOM   4051 N  N     . THR B 1 215 ? -14.569 14.984  -3.940  1.00 52.72  ?  215 THR B N     1 
ATOM   4052 C  CA    . THR B 1 215 ? -15.003 13.614  -4.124  1.00 56.19  ?  215 THR B CA    1 
ATOM   4053 C  C     . THR B 1 215 ? -15.522 13.435  -5.551  1.00 54.51  ?  215 THR B C     1 
ATOM   4054 O  O     . THR B 1 215 ? -16.114 14.363  -6.115  1.00 55.23  ?  215 THR B O     1 
ATOM   4055 C  CB    . THR B 1 215 ? -16.081 13.264  -3.096  1.00 50.52  ?  215 THR B CB    1 
ATOM   4056 O  OG1   . THR B 1 215 ? -17.341 13.807  -3.514  1.00 47.37  ?  215 THR B OG1   1 
ATOM   4057 C  CG2   . THR B 1 215 ? -15.703 13.851  -1.729  1.00 42.25  ?  215 THR B CG2   1 
ATOM   4058 N  N     . PRO B 1 216 ? -15.279 12.278  -6.169  1.00 45.95  ?  216 PRO B N     1 
ATOM   4059 C  CA    . PRO B 1 216 ? -15.691 12.067  -7.566  1.00 52.25  ?  216 PRO B CA    1 
ATOM   4060 C  C     . PRO B 1 216 ? -17.188 12.264  -7.771  1.00 54.99  ?  216 PRO B C     1 
ATOM   4061 O  O     . PRO B 1 216 ? -18.012 11.648  -7.090  1.00 55.12  ?  216 PRO B O     1 
ATOM   4062 C  CB    . PRO B 1 216 ? -15.286 10.614  -7.840  1.00 50.92  ?  216 PRO B CB    1 
ATOM   4063 C  CG    . PRO B 1 216 ? -14.250 10.289  -6.832  1.00 49.26  ?  216 PRO B CG    1 
ATOM   4064 C  CD    . PRO B 1 216 ? -14.408 11.206  -5.659  1.00 46.89  ?  216 PRO B CD    1 
ATOM   4065 N  N     . THR B 1 217 ? -17.535 13.110  -8.747  1.00 56.90  ?  217 THR B N     1 
ATOM   4066 C  CA    . THR B 1 217 ? -18.936 13.386  -9.065  1.00 63.18  ?  217 THR B CA    1 
ATOM   4067 C  C     . THR B 1 217 ? -19.478 12.373  -10.070 1.00 62.89  ?  217 THR B C     1 
ATOM   4068 O  O     . THR B 1 217 ? -19.047 11.215  -10.082 1.00 60.41  ?  217 THR B O     1 
ATOM   4069 C  CB    . THR B 1 217 ? -19.093 14.811  -9.614  1.00 60.71  ?  217 THR B CB    1 
ATOM   4070 O  OG1   . THR B 1 217 ? -18.553 14.881  -10.940 1.00 62.23  ?  217 THR B OG1   1 
ATOM   4071 C  CG2   . THR B 1 217 ? -18.364 15.808  -8.731  1.00 57.88  ?  217 THR B CG2   1 
ATOM   4072 N  N     . SER B 1 218 ? -20.437 12.785  -10.902 1.00 61.76  ?  218 SER B N     1 
ATOM   4073 C  CA    . SER B 1 218 ? -20.837 11.985  -12.054 1.00 58.53  ?  218 SER B CA    1 
ATOM   4074 C  C     . SER B 1 218 ? -20.155 12.442  -13.329 1.00 59.79  ?  218 SER B C     1 
ATOM   4075 O  O     . SER B 1 218 ? -19.902 11.621  -14.216 1.00 57.25  ?  218 SER B O     1 
ATOM   4076 C  CB    . SER B 1 218 ? -22.354 12.040  -12.273 1.00 63.23  ?  218 SER B CB    1 
ATOM   4077 O  OG    . SER B 1 218 ? -22.757 13.302  -12.778 1.00 68.56  ?  218 SER B OG    1 
ATOM   4078 N  N     . ASP B 1 219 ? -19.856 13.738  -13.438 1.00 62.72  ?  219 ASP B N     1 
ATOM   4079 C  CA    . ASP B 1 219 ? -19.131 14.257  -14.590 1.00 57.84  ?  219 ASP B CA    1 
ATOM   4080 C  C     . ASP B 1 219 ? -17.702 13.745  -14.646 1.00 57.48  ?  219 ASP B C     1 
ATOM   4081 O  O     . ASP B 1 219 ? -17.042 13.912  -15.677 1.00 55.04  ?  219 ASP B O     1 
ATOM   4082 C  CB    . ASP B 1 219 ? -19.147 15.783  -14.562 1.00 61.62  ?  219 ASP B CB    1 
ATOM   4083 C  CG    . ASP B 1 219 ? -20.491 16.338  -14.129 1.00 65.91  ?  219 ASP B CG    1 
ATOM   4084 O  OD1   . ASP B 1 219 ? -21.479 16.170  -14.877 1.00 62.49  ?  219 ASP B OD1   1 
ATOM   4085 O  OD2   . ASP B 1 219 ? -20.556 16.933  -13.032 1.00 68.03  ?  219 ASP B OD2   1 
ATOM   4086 N  N     . ASP B 1 220 ? -17.207 13.145  -13.560 1.00 60.10  ?  220 ASP B N     1 
ATOM   4087 C  CA    . ASP B 1 220 ? -15.975 12.368  -13.639 1.00 59.74  ?  220 ASP B CA    1 
ATOM   4088 C  C     . ASP B 1 220 ? -16.200 11.085  -14.435 1.00 53.31  ?  220 ASP B C     1 
ATOM   4089 O  O     . ASP B 1 220 ? -15.325 10.661  -15.200 1.00 46.09  ?  220 ASP B O     1 
ATOM   4090 C  CB    . ASP B 1 220 ? -15.457 12.048  -12.231 1.00 60.24  ?  220 ASP B CB    1 
ATOM   4091 C  CG    . ASP B 1 220 ? -15.212 13.299  -11.384 1.00 64.84  ?  220 ASP B CG    1 
ATOM   4092 O  OD1   . ASP B 1 220 ? -14.124 13.902  -11.516 1.00 65.89  ?  220 ASP B OD1   1 
ATOM   4093 O  OD2   . ASP B 1 220 ? -16.098 13.666  -10.572 1.00 60.74  ?  220 ASP B OD2   1 
ATOM   4094 N  N     . ILE B 1 221 ? -17.371 10.458  -14.267 1.00 50.05  ?  221 ILE B N     1 
ATOM   4095 C  CA    . ILE B 1 221 ? -17.726 9.282   -15.059 1.00 46.99  ?  221 ILE B CA    1 
ATOM   4096 C  C     . ILE B 1 221 ? -17.794 9.631   -16.544 1.00 47.59  ?  221 ILE B C     1 
ATOM   4097 O  O     . ILE B 1 221 ? -17.456 8.806   -17.405 1.00 41.85  ?  221 ILE B O     1 
ATOM   4098 C  CB    . ILE B 1 221 ? -19.060 8.695   -14.547 1.00 49.59  ?  221 ILE B CB    1 
ATOM   4099 C  CG1   . ILE B 1 221 ? -18.855 7.967   -13.216 1.00 48.35  ?  221 ILE B CG1   1 
ATOM   4100 C  CG2   . ILE B 1 221 ? -19.695 7.759   -15.583 1.00 45.46  ?  221 ILE B CG2   1 
ATOM   4101 C  CD1   . ILE B 1 221 ? -20.026 7.084   -12.818 1.00 42.76  ?  221 ILE B CD1   1 
ATOM   4102 N  N     . ALA B 1 222 ? -18.197 10.865  -16.869 1.00 46.34  ?  222 ALA B N     1 
ATOM   4103 C  CA    . ALA B 1 222 ? -18.428 11.237  -18.261 1.00 39.19  ?  222 ALA B CA    1 
ATOM   4104 C  C     . ALA B 1 222 ? -17.121 11.361  -19.039 1.00 41.04  ?  222 ALA B C     1 
ATOM   4105 O  O     . ALA B 1 222 ? -17.053 10.964  -20.210 1.00 34.48  ?  222 ALA B O     1 
ATOM   4106 C  CB    . ALA B 1 222 ? -19.219 12.543  -18.325 1.00 45.55  ?  222 ALA B CB    1 
ATOM   4107 N  N     . ALA B 1 223 ? -16.079 11.921  -18.416 1.00 40.85  ?  223 ALA B N     1 
ATOM   4108 C  CA    . ALA B 1 223 ? -14.797 12.057  -19.099 1.00 37.68  ?  223 ALA B CA    1 
ATOM   4109 C  C     . ALA B 1 223 ? -14.141 10.698  -19.309 1.00 40.38  ?  223 ALA B C     1 
ATOM   4110 O  O     . ALA B 1 223 ? -13.550 10.442  -20.368 1.00 36.70  ?  223 ALA B O     1 
ATOM   4111 C  CB    . ALA B 1 223 ? -13.871 12.984  -18.311 1.00 41.89  ?  223 ALA B CB    1 
ATOM   4112 N  N     . LEU B 1 224 ? -14.248 9.807   -18.318 1.00 39.06  ?  224 LEU B N     1 
ATOM   4113 C  CA    . LEU B 1 224 ? -13.651 8.483   -18.462 1.00 36.90  ?  224 LEU B CA    1 
ATOM   4114 C  C     . LEU B 1 224 ? -14.349 7.680   -19.556 1.00 36.68  ?  224 LEU B C     1 
ATOM   4115 O  O     . LEU B 1 224 ? -13.690 7.053   -20.398 1.00 26.23  ?  224 LEU B O     1 
ATOM   4116 C  CB    . LEU B 1 224 ? -13.702 7.751   -17.130 1.00 32.34  ?  224 LEU B CB    1 
ATOM   4117 C  CG    . LEU B 1 224 ? -12.701 6.611   -17.017 1.00 35.86  ?  224 LEU B CG    1 
ATOM   4118 C  CD1   . LEU B 1 224 ? -11.362 7.027   -17.598 1.00 33.83  ?  224 LEU B CD1   1 
ATOM   4119 C  CD2   . LEU B 1 224 ? -12.548 6.222   -15.564 1.00 40.72  ?  224 LEU B CD2   1 
ATOM   4120 N  N     . LYS B 1 225 ? -15.684 7.703   -19.568 1.00 34.95  ?  225 LYS B N     1 
ATOM   4121 C  CA    . LYS B 1 225 ? -16.419 7.105   -20.676 1.00 33.08  ?  225 LYS B CA    1 
ATOM   4122 C  C     . LYS B 1 225 ? -15.920 7.610   -22.030 1.00 27.79  ?  225 LYS B C     1 
ATOM   4123 O  O     . LYS B 1 225 ? -15.916 6.852   -23.004 1.00 28.92  ?  225 LYS B O     1 
ATOM   4124 C  CB    . LYS B 1 225 ? -17.907 7.395   -20.514 1.00 33.45  ?  225 LYS B CB    1 
ATOM   4125 C  CG    . LYS B 1 225 ? -18.779 6.877   -21.643 1.00 40.89  ?  225 LYS B CG    1 
ATOM   4126 C  CD    . LYS B 1 225 ? -18.756 5.350   -21.736 1.00 37.56  ?  225 LYS B CD    1 
ATOM   4127 C  CE    . LYS B 1 225 ? -19.792 4.860   -22.750 1.00 40.16  ?  225 LYS B CE    1 
ATOM   4128 N  NZ    . LYS B 1 225 ? -20.652 5.965   -23.291 1.00 43.76  ?  225 LYS B NZ    1 
ATOM   4129 N  N     . VAL B 1 226 ? -15.501 8.879   -22.117 1.00 29.61  ?  226 VAL B N     1 
ATOM   4130 C  CA    . VAL B 1 226 ? -14.917 9.385   -23.358 1.00 28.07  ?  226 VAL B CA    1 
ATOM   4131 C  C     . VAL B 1 226 ? -13.602 8.668   -23.642 1.00 24.22  ?  226 VAL B C     1 
ATOM   4132 O  O     . VAL B 1 226 ? -13.379 8.156   -24.742 1.00 24.36  ?  226 VAL B O     1 
ATOM   4133 C  CB    . VAL B 1 226 ? -14.723 10.914  -23.288 1.00 32.09  ?  226 VAL B CB    1 
ATOM   4134 C  CG1   . VAL B 1 226 ? -13.911 11.416  -24.488 1.00 21.16  ?  226 VAL B CG1   1 
ATOM   4135 C  CG2   . VAL B 1 226 ? -16.054 11.636  -23.233 1.00 28.04  ?  226 VAL B CG2   1 
ATOM   4136 N  N     . TYR B 1 227 ? -12.725 8.600   -22.637 1.00 26.71  ?  227 TYR B N     1 
ATOM   4137 C  CA    . TYR B 1 227 ? -11.484 7.842   -22.769 1.00 26.16  ?  227 TYR B CA    1 
ATOM   4138 C  C     . TYR B 1 227 ? -11.754 6.375   -23.129 1.00 29.74  ?  227 TYR B C     1 
ATOM   4139 O  O     . TYR B 1 227 ? -11.053 5.797   -23.968 1.00 27.33  ?  227 TYR B O     1 
ATOM   4140 C  CB    . TYR B 1 227 ? -10.679 7.960   -21.466 1.00 27.82  ?  227 TYR B CB    1 
ATOM   4141 C  CG    . TYR B 1 227 ? -9.203  7.683   -21.629 1.00 36.09  ?  227 TYR B CG    1 
ATOM   4142 C  CD1   . TYR B 1 227 ? -8.336  8.670   -22.080 1.00 33.01  ?  227 TYR B CD1   1 
ATOM   4143 C  CD2   . TYR B 1 227 ? -8.674  6.420   -21.359 1.00 37.62  ?  227 TYR B CD2   1 
ATOM   4144 C  CE1   . TYR B 1 227 ? -6.965  8.413   -22.246 1.00 39.84  ?  227 TYR B CE1   1 
ATOM   4145 C  CE2   . TYR B 1 227 ? -7.305  6.145   -21.534 1.00 41.34  ?  227 TYR B CE2   1 
ATOM   4146 C  CZ    . TYR B 1 227 ? -6.456  7.149   -21.982 1.00 39.34  ?  227 TYR B CZ    1 
ATOM   4147 O  OH    . TYR B 1 227 ? -5.104  6.899   -22.154 1.00 37.26  ?  227 TYR B OH    1 
ATOM   4148 N  N     . GLU B 1 228 ? -12.785 5.759   -22.530 1.00 25.16  ?  228 GLU B N     1 
ATOM   4149 C  CA    . GLU B 1 228 ? -13.076 4.361   -22.834 1.00 27.24  ?  228 GLU B CA    1 
ATOM   4150 C  C     . GLU B 1 228 ? -13.588 4.179   -24.260 1.00 24.32  ?  228 GLU B C     1 
ATOM   4151 O  O     . GLU B 1 228 ? -13.146 3.265   -24.966 1.00 25.88  ?  228 GLU B O     1 
ATOM   4152 C  CB    . GLU B 1 228 ? -14.081 3.774   -21.844 1.00 30.17  ?  228 GLU B CB    1 
ATOM   4153 C  CG    . GLU B 1 228 ? -14.411 2.323   -22.179 1.00 27.39  ?  228 GLU B CG    1 
ATOM   4154 C  CD    . GLU B 1 228 ? -15.451 1.678   -21.256 1.00 42.33  ?  228 GLU B CD    1 
ATOM   4155 O  OE1   . GLU B 1 228 ? -16.242 2.406   -20.605 1.00 34.47  ?  228 GLU B OE1   1 
ATOM   4156 O  OE2   . GLU B 1 228 ? -15.471 0.426   -21.196 1.00 40.79  ?  228 GLU B OE2   1 
ATOM   4157 N  N     . ASP B 1 229 ? -14.542 5.007   -24.695 1.00 21.91  ?  229 ASP B N     1 
ATOM   4158 C  CA    . ASP B 1 229 ? -15.130 4.818   -26.023 1.00 23.10  ?  229 ASP B CA    1 
ATOM   4159 C  C     . ASP B 1 229 ? -14.083 5.006   -27.123 1.00 28.91  ?  229 ASP B C     1 
ATOM   4160 O  O     . ASP B 1 229 ? -14.053 4.258   -28.115 1.00 24.07  ?  229 ASP B O     1 
ATOM   4161 C  CB    . ASP B 1 229 ? -16.296 5.794   -26.239 1.00 27.81  ?  229 ASP B CB    1 
ATOM   4162 C  CG    . ASP B 1 229 ? -17.544 5.439   -25.413 1.00 38.07  ?  229 ASP B CG    1 
ATOM   4163 O  OD1   . ASP B 1 229 ? -17.723 4.247   -25.066 1.00 36.07  ?  229 ASP B OD1   1 
ATOM   4164 O  OD2   . ASP B 1 229 ? -18.360 6.356   -25.130 1.00 36.71  ?  229 ASP B OD2   1 
ATOM   4165 N  N     . ASN B 1 230 ? -13.217 6.006   -26.962 1.00 25.02  ?  230 ASN B N     1 
ATOM   4166 C  CA    . ASN B 1 230 ? -12.138 6.210   -27.919 1.00 26.77  ?  230 ASN B CA    1 
ATOM   4167 C  C     . ASN B 1 230 ? -11.138 5.071   -27.860 1.00 24.56  ?  230 ASN B C     1 
ATOM   4168 O  O     . ASN B 1 230 ? -10.551 4.710   -28.885 1.00 21.82  ?  230 ASN B O     1 
ATOM   4169 C  CB    . ASN B 1 230 ? -11.462 7.557   -27.652 1.00 19.70  ?  230 ASN B CB    1 
ATOM   4170 C  CG    . ASN B 1 230 ? -12.312 8.708   -28.110 1.00 23.23  ?  230 ASN B CG    1 
ATOM   4171 O  OD1   . ASN B 1 230 ? -13.380 8.495   -28.692 1.00 22.00  ?  230 ASN B OD1   1 
ATOM   4172 N  ND2   . ASN B 1 230 ? -11.865 9.936   -27.847 1.00 25.58  ?  230 ASN B ND2   1 
ATOM   4173 N  N     . TRP B 1 231 ? -10.960 4.467   -26.684 1.00 25.03  ?  231 TRP B N     1 
ATOM   4174 C  CA    . TRP B 1 231 ? -10.032 3.350   -26.600 1.00 23.40  ?  231 TRP B CA    1 
ATOM   4175 C  C     . TRP B 1 231 ? -10.552 2.159   -27.393 1.00 22.24  ?  231 TRP B C     1 
ATOM   4176 O  O     . TRP B 1 231 ? -9.785  1.490   -28.092 1.00 18.33  ?  231 TRP B O     1 
ATOM   4177 C  CB    . TRP B 1 231 ? -9.772  2.983   -25.138 1.00 24.03  ?  231 TRP B CB    1 
ATOM   4178 C  CG    . TRP B 1 231 ? -8.868  1.795   -24.988 1.00 24.30  ?  231 TRP B CG    1 
ATOM   4179 C  CD1   . TRP B 1 231 ? -7.497  1.794   -24.963 1.00 19.18  ?  231 TRP B CD1   1 
ATOM   4180 C  CD2   . TRP B 1 231 ? -9.275  0.426   -24.849 1.00 24.10  ?  231 TRP B CD2   1 
ATOM   4181 N  NE1   . TRP B 1 231 ? -7.034  0.510   -24.808 1.00 21.28  ?  231 TRP B NE1   1 
ATOM   4182 C  CE2   . TRP B 1 231 ? -8.105  -0.349  -24.741 1.00 25.34  ?  231 TRP B CE2   1 
ATOM   4183 C  CE3   . TRP B 1 231 ? -10.516 -0.215  -24.800 1.00 21.73  ?  231 TRP B CE3   1 
ATOM   4184 C  CZ2   . TRP B 1 231 ? -8.143  -1.745  -24.601 1.00 20.37  ?  231 TRP B CZ2   1 
ATOM   4185 C  CZ3   . TRP B 1 231 ? -10.550 -1.590  -24.658 1.00 24.73  ?  231 TRP B CZ3   1 
ATOM   4186 C  CH2   . TRP B 1 231 ? -9.371  -2.340  -24.558 1.00 25.01  ?  231 TRP B CH2   1 
ATOM   4187 N  N     . HIS B 1 232 ? -11.856 1.896   -27.313 1.00 25.78  ?  232 HIS B N     1 
ATOM   4188 C  CA    . HIS B 1 232 ? -12.451 0.823   -28.103 1.00 24.73  ?  232 HIS B CA    1 
ATOM   4189 C  C     . HIS B 1 232 ? -12.386 1.139   -29.588 1.00 19.75  ?  232 HIS B C     1 
ATOM   4190 O  O     . HIS B 1 232 ? -12.111 0.250   -30.404 1.00 28.13  ?  232 HIS B O     1 
ATOM   4191 C  CB    . HIS B 1 232 ? -13.904 0.602   -27.679 1.00 24.80  ?  232 HIS B CB    1 
ATOM   4192 C  CG    . HIS B 1 232 ? -14.062 -0.148  -26.393 1.00 28.68  ?  232 HIS B CG    1 
ATOM   4193 N  ND1   . HIS B 1 232 ? -14.199 0.482   -25.173 1.00 31.01  ?  232 HIS B ND1   1 
ATOM   4194 C  CD2   . HIS B 1 232 ? -14.149 -1.476  -26.141 1.00 31.15  ?  232 HIS B CD2   1 
ATOM   4195 C  CE1   . HIS B 1 232 ? -14.347 -0.427  -24.224 1.00 35.30  ?  232 HIS B CE1   1 
ATOM   4196 N  NE2   . HIS B 1 232 ? -14.324 -1.623  -24.784 1.00 32.42  ?  232 HIS B NE2   1 
ATOM   4197 N  N     . LEU B 1 233 ? -12.646 2.397   -29.952 1.00 20.59  ?  233 LEU B N     1 
ATOM   4198 C  CA    . LEU B 1 233 ? -12.559 2.833   -31.348 1.00 22.83  ?  233 LEU B CA    1 
ATOM   4199 C  C     . LEU B 1 233 ? -11.180 2.550   -31.937 1.00 24.14  ?  233 LEU B C     1 
ATOM   4200 O  O     . LEU B 1 233 ? -11.056 1.960   -33.016 1.00 22.25  ?  233 LEU B O     1 
ATOM   4201 C  CB    . LEU B 1 233 ? -12.870 4.335   -31.440 1.00 22.65  ?  233 LEU B CB    1 
ATOM   4202 C  CG    . LEU B 1 233 ? -12.680 5.075   -32.780 1.00 30.28  ?  233 LEU B CG    1 
ATOM   4203 C  CD1   . LEU B 1 233 ? -13.673 6.217   -32.859 1.00 34.14  ?  233 LEU B CD1   1 
ATOM   4204 C  CD2   . LEU B 1 233 ? -11.240 5.589   -33.035 1.00 24.31  ?  233 LEU B CD2   1 
ATOM   4205 N  N     . ILE B 1 234 ? -10.132 3.013   -31.260 1.00 23.10  ?  234 ILE B N     1 
ATOM   4206 C  CA    . ILE B 1 234 ? -8.785  2.847   -31.781 1.00 22.23  ?  234 ILE B CA    1 
ATOM   4207 C  C     . ILE B 1 234 ? -8.400  1.376   -31.780 1.00 23.51  ?  234 ILE B C     1 
ATOM   4208 O  O     . ILE B 1 234 ? -7.700  0.903   -32.686 1.00 22.76  ?  234 ILE B O     1 
ATOM   4209 C  CB    . ILE B 1 234 ? -7.802  3.689   -30.952 1.00 23.92  ?  234 ILE B CB    1 
ATOM   4210 C  CG1   . ILE B 1 234 ? -8.192  5.175   -30.981 1.00 22.17  ?  234 ILE B CG1   1 
ATOM   4211 C  CG2   . ILE B 1 234 ? -6.382  3.483   -31.460 1.00 23.10  ?  234 ILE B CG2   1 
ATOM   4212 C  CD1   . ILE B 1 234 ? -7.651  5.952   -29.780 1.00 17.95  ?  234 ILE B CD1   1 
ATOM   4213 N  N     . CYS B 1 235 ? -8.860  0.633   -30.763 1.00 21.48  ?  235 CYS B N     1 
ATOM   4214 C  CA    . CYS B 1 235 ? -8.554  -0.794  -30.642 1.00 23.93  ?  235 CYS B CA    1 
ATOM   4215 C  C     . CYS B 1 235 ? -9.064  -1.587  -31.834 1.00 22.32  ?  235 CYS B C     1 
ATOM   4216 O  O     . CYS B 1 235 ? -8.413  -2.533  -32.288 1.00 23.12  ?  235 CYS B O     1 
ATOM   4217 C  CB    . CYS B 1 235 ? -9.170  -1.346  -29.361 1.00 16.40  ?  235 CYS B CB    1 
ATOM   4218 S  SG    . CYS B 1 235 ? -8.000  -1.398  -28.017 1.00 19.10  ?  235 CYS B SG    1 
ATOM   4219 N  N     . GLU B 1 236 ? -10.263 -1.262  -32.304 1.00 25.67  ?  236 GLU B N     1 
ATOM   4220 C  CA    . GLU B 1 236 ? -10.798 -1.896  -33.495 1.00 28.19  ?  236 GLU B CA    1 
ATOM   4221 C  C     . GLU B 1 236 ? -10.137 -1.351  -34.750 1.00 28.66  ?  236 GLU B C     1 
ATOM   4222 O  O     . GLU B 1 236 ? -9.963  -2.088  -35.724 1.00 30.13  ?  236 GLU B O     1 
ATOM   4223 C  CB    . GLU B 1 236 ? -12.312 -1.684  -33.546 1.00 31.46  ?  236 GLU B CB    1 
ATOM   4224 C  CG    . GLU B 1 236 ? -13.097 -2.838  -34.134 1.00 46.59  ?  236 GLU B CG    1 
ATOM   4225 C  CD    . GLU B 1 236 ? -14.426 -2.390  -34.721 1.00 57.95  ?  236 GLU B CD    1 
ATOM   4226 O  OE1   . GLU B 1 236 ? -14.406 -1.672  -35.747 1.00 55.90  ?  236 GLU B OE1   1 
ATOM   4227 O  OE2   . GLU B 1 236 ? -15.489 -2.747  -34.151 1.00 55.94  ?  236 GLU B OE2   1 
ATOM   4228 N  N     . ARG B 1 237 ? -9.759  -0.067  -34.741 1.00 24.60  ?  237 ARG B N     1 
ATOM   4229 C  CA    . ARG B 1 237 ? -9.072  0.512   -35.891 1.00 23.49  ?  237 ARG B CA    1 
ATOM   4230 C  C     . ARG B 1 237 ? -7.695  -0.111  -36.076 1.00 20.62  ?  237 ARG B C     1 
ATOM   4231 O  O     . ARG B 1 237 ? -7.275  -0.369  -37.205 1.00 18.46  ?  237 ARG B O     1 
ATOM   4232 C  CB    . ARG B 1 237 ? -8.967  2.028   -35.721 1.00 23.58  ?  237 ARG B CB    1 
ATOM   4233 C  CG    . ARG B 1 237 ? -8.156  2.741   -36.802 1.00 22.85  ?  237 ARG B CG    1 
ATOM   4234 C  CD    . ARG B 1 237 ? -8.082  4.244   -36.524 1.00 27.19  ?  237 ARG B CD    1 
ATOM   4235 N  NE    . ARG B 1 237 ? -9.352  4.928   -36.754 1.00 27.21  ?  237 ARG B NE    1 
ATOM   4236 C  CZ    . ARG B 1 237 ? -9.591  6.198   -36.452 1.00 23.08  ?  237 ARG B CZ    1 
ATOM   4237 N  NH1   . ARG B 1 237 ? -8.688  6.947   -35.838 1.00 19.68  ?  237 ARG B NH1   1 
ATOM   4238 N  NH2   . ARG B 1 237 ? -10.763 6.732   -36.781 1.00 22.52  ?  237 ARG B NH2   1 
ATOM   4239 N  N     . TRP B 1 238 ? -6.987  -0.378  -34.977 1.00 22.83  ?  238 TRP B N     1 
ATOM   4240 C  CA    . TRP B 1 238 ? -5.641  -0.947  -35.001 1.00 20.63  ?  238 TRP B CA    1 
ATOM   4241 C  C     . TRP B 1 238 ? -5.617  -2.242  -34.188 1.00 26.76  ?  238 TRP B C     1 
ATOM   4242 O  O     . TRP B 1 238 ? -5.333  -2.230  -32.977 1.00 24.07  ?  238 TRP B O     1 
ATOM   4243 C  CB    . TRP B 1 238 ? -4.626  0.069   -34.481 1.00 17.71  ?  238 TRP B CB    1 
ATOM   4244 C  CG    . TRP B 1 238 ? -4.703  1.428   -35.199 1.00 24.04  ?  238 TRP B CG    1 
ATOM   4245 C  CD1   . TRP B 1 238 ? -5.237  2.594   -34.704 1.00 18.34  ?  238 TRP B CD1   1 
ATOM   4246 C  CD2   . TRP B 1 238 ? -4.229  1.743   -36.527 1.00 18.64  ?  238 TRP B CD2   1 
ATOM   4247 N  NE1   . TRP B 1 238 ? -5.126  3.599   -35.635 1.00 16.72  ?  238 TRP B NE1   1 
ATOM   4248 C  CE2   . TRP B 1 238 ? -4.517  3.106   -36.761 1.00 16.57  ?  238 TRP B CE2   1 
ATOM   4249 C  CE3   . TRP B 1 238 ? -3.591  1.006   -37.536 1.00 17.14  ?  238 TRP B CE3   1 
ATOM   4250 C  CZ2   . TRP B 1 238 ? -4.190  3.744   -37.965 1.00 16.75  ?  238 TRP B CZ2   1 
ATOM   4251 C  CZ3   . TRP B 1 238 ? -3.266  1.646   -38.733 1.00 14.35  ?  238 TRP B CZ3   1 
ATOM   4252 C  CH2   . TRP B 1 238 ? -3.557  2.997   -38.931 1.00 14.81  ?  238 TRP B CH2   1 
ATOM   4253 N  N     . PRO B 1 239 ? -5.907  -3.386  -34.812 1.00 25.42  ?  239 PRO B N     1 
ATOM   4254 C  CA    . PRO B 1 239 ? -5.807  -4.666  -34.098 1.00 26.50  ?  239 PRO B CA    1 
ATOM   4255 C  C     . PRO B 1 239 ? -4.392  -4.942  -33.618 1.00 28.89  ?  239 PRO B C     1 
ATOM   4256 O  O     . PRO B 1 239 ? -3.408  -4.586  -34.270 1.00 32.78  ?  239 PRO B O     1 
ATOM   4257 C  CB    . PRO B 1 239 ? -6.242  -5.693  -35.148 1.00 29.16  ?  239 PRO B CB    1 
ATOM   4258 C  CG    . PRO B 1 239 ? -7.110  -4.925  -36.081 1.00 35.62  ?  239 PRO B CG    1 
ATOM   4259 C  CD    . PRO B 1 239 ? -6.501  -3.543  -36.151 1.00 29.18  ?  239 PRO B CD    1 
ATOM   4260 N  N     . ALA B 1 240 ? -4.305  -5.605  -32.467 1.00 26.29  ?  240 ALA B N     1 
ATOM   4261 C  CA    . ALA B 1 240 ? -3.019  -5.893  -31.850 1.00 27.27  ?  240 ALA B CA    1 
ATOM   4262 C  C     . ALA B 1 240 ? -2.162  -6.753  -32.773 1.00 36.64  ?  240 ALA B C     1 
ATOM   4263 O  O     . ALA B 1 240 ? -2.666  -7.572  -33.546 1.00 33.23  ?  240 ALA B O     1 
ATOM   4264 C  CB    . ALA B 1 240 ? -3.221  -6.598  -30.508 1.00 24.80  ?  240 ALA B CB    1 
ATOM   4265 N  N     . ALA B 1 241 ? -0.851  -6.559  -32.690 1.00 32.13  ?  241 ALA B N     1 
ATOM   4266 C  CA    . ALA B 1 241 ? 0.048   -7.258  -33.594 1.00 30.71  ?  241 ALA B CA    1 
ATOM   4267 C  C     . ALA B 1 241 ? 0.427   -8.653  -33.103 1.00 35.23  ?  241 ALA B C     1 
ATOM   4268 O  O     . ALA B 1 241 ? 0.932   -9.453  -33.897 1.00 32.64  ?  241 ALA B O     1 
ATOM   4269 C  CB    . ALA B 1 241 ? 1.310   -6.419  -33.826 1.00 35.38  ?  241 ALA B CB    1 
ATOM   4270 N  N     . THR B 1 242 ? 0.210   -8.957  -31.821 1.00 31.53  ?  242 THR B N     1 
ATOM   4271 C  CA    . THR B 1 242 ? 0.434   -10.284 -31.261 1.00 30.48  ?  242 THR B CA    1 
ATOM   4272 C  C     . THR B 1 242 ? -0.809  -10.733 -30.505 1.00 30.89  ?  242 THR B C     1 
ATOM   4273 O  O     . THR B 1 242 ? -1.653  -9.915  -30.125 1.00 34.04  ?  242 THR B O     1 
ATOM   4274 C  CB    . THR B 1 242 ? 1.633   -10.311 -30.305 1.00 35.03  ?  242 THR B CB    1 
ATOM   4275 O  OG1   . THR B 1 242 ? 1.221   -9.823  -29.024 1.00 32.41  ?  242 THR B OG1   1 
ATOM   4276 C  CG2   . THR B 1 242 ? 2.781   -9.450  -30.837 1.00 33.47  ?  242 THR B CG2   1 
ATOM   4277 N  N     . GLU B 1 243 ? -0.904  -12.047 -30.260 1.00 34.63  ?  243 GLU B N     1 
ATOM   4278 C  CA    . GLU B 1 243 ? -2.064  -12.576 -29.535 1.00 33.26  ?  243 GLU B CA    1 
ATOM   4279 C  C     . GLU B 1 243 ? -2.006  -12.259 -28.046 1.00 29.40  ?  243 GLU B C     1 
ATOM   4280 O  O     . GLU B 1 243 ? -3.052  -12.054 -27.421 1.00 33.77  ?  243 GLU B O     1 
ATOM   4281 C  CB    . GLU B 1 243 ? -2.187  -14.092 -29.727 1.00 39.19  ?  243 GLU B CB    1 
ATOM   4282 C  CG    . GLU B 1 243 ? -3.030  -14.514 -30.929 1.00 34.32  ?  243 GLU B CG    1 
ATOM   4283 C  CD    . GLU B 1 243 ? -4.494  -14.112 -30.820 1.00 37.94  ?  243 GLU B CD    1 
ATOM   4284 O  OE1   . GLU B 1 243 ? -4.970  -13.835 -29.693 1.00 47.81  ?  243 GLU B OE1   1 
ATOM   4285 O  OE2   . GLU B 1 243 ? -5.169  -14.066 -31.876 1.00 44.69  ?  243 GLU B OE2   1 
ATOM   4286 N  N     . ARG B 1 244 ? -0.810  -12.230 -27.455 1.00 29.81  ?  244 ARG B N     1 
ATOM   4287 C  CA    . ARG B 1 244 ? -0.704  -11.882 -26.041 1.00 31.60  ?  244 ARG B CA    1 
ATOM   4288 C  C     . ARG B 1 244 ? -1.205  -10.461 -25.790 1.00 33.97  ?  244 ARG B C     1 
ATOM   4289 O  O     . ARG B 1 244 ? -1.931  -10.216 -24.821 1.00 28.75  ?  244 ARG B O     1 
ATOM   4290 C  CB    . ARG B 1 244 ? 0.744   -12.051 -25.566 1.00 33.40  ?  244 ARG B CB    1 
ATOM   4291 C  CG    . ARG B 1 244 ? 1.058   -11.491 -24.169 1.00 37.59  ?  244 ARG B CG    1 
ATOM   4292 C  CD    . ARG B 1 244 ? 0.315   -12.215 -23.032 1.00 41.40  ?  244 ARG B CD    1 
ATOM   4293 N  NE    . ARG B 1 244 ? 0.894   -13.519 -22.718 1.00 55.42  ?  244 ARG B NE    1 
ATOM   4294 C  CZ    . ARG B 1 244 ? 1.986   -13.724 -21.989 1.00 53.20  ?  244 ARG B CZ    1 
ATOM   4295 N  NH1   . ARG B 1 244 ? 2.645   -12.723 -21.428 1.00 46.94  ?  244 ARG B NH1   1 
ATOM   4296 N  NH2   . ARG B 1 244 ? 2.427   -14.968 -21.816 1.00 51.19  ?  244 ARG B NH2   1 
ATOM   4297 N  N     . ALA B 1 245 ? -0.856  -9.519  -26.674 1.00 28.63  ?  245 ALA B N     1 
ATOM   4298 C  CA    . ALA B 1 245 ? -1.319  -8.138  -26.514 1.00 35.63  ?  245 ALA B CA    1 
ATOM   4299 C  C     . ALA B 1 245 ? -2.837  -8.038  -26.615 1.00 30.09  ?  245 ALA B C     1 
ATOM   4300 O  O     . ALA B 1 245 ? -3.468  -7.293  -25.858 1.00 25.29  ?  245 ALA B O     1 
ATOM   4301 C  CB    . ALA B 1 245 ? -0.669  -7.234  -27.560 1.00 21.81  ?  245 ALA B CB    1 
ATOM   4302 N  N     . GLU B 1 246 ? -3.439  -8.760  -27.567 1.00 33.08  ?  246 GLU B N     1 
ATOM   4303 C  CA    . GLU B 1 246 ? -4.890  -8.757  -27.706 1.00 37.39  ?  246 GLU B CA    1 
ATOM   4304 C  C     . GLU B 1 246 ? -5.556  -9.489  -26.545 1.00 37.27  ?  246 GLU B C     1 
ATOM   4305 O  O     . GLU B 1 246 ? -6.745  -9.274  -26.278 1.00 37.55  ?  246 GLU B O     1 
ATOM   4306 C  CB    . GLU B 1 246 ? -5.281  -9.370  -29.062 1.00 38.60  ?  246 GLU B CB    1 
ATOM   4307 C  CG    . GLU B 1 246 ? -6.759  -9.206  -29.467 1.00 41.94  ?  246 GLU B CG    1 
ATOM   4308 C  CD    . GLU B 1 246 ? -7.082  -7.857  -30.144 1.00 43.46  ?  246 GLU B CD    1 
ATOM   4309 O  OE1   . GLU B 1 246 ? -6.315  -7.392  -31.027 1.00 33.76  ?  246 GLU B OE1   1 
ATOM   4310 O  OE2   . GLU B 1 246 ? -8.124  -7.257  -29.782 1.00 39.75  ?  246 GLU B OE2   1 
ATOM   4311 N  N     . GLN B 1 247 ? -4.802  -10.322 -25.833 1.00 33.41  ?  247 GLN B N     1 
ATOM   4312 C  CA    . GLN B 1 247 ? -5.302  -10.917 -24.603 1.00 35.05  ?  247 GLN B CA    1 
ATOM   4313 C  C     . GLN B 1 247 ? -5.253  -9.907  -23.461 1.00 35.12  ?  247 GLN B C     1 
ATOM   4314 O  O     . GLN B 1 247 ? -6.210  -9.772  -22.694 1.00 29.31  ?  247 GLN B O     1 
ATOM   4315 C  CB    . GLN B 1 247 ? -4.481  -12.168 -24.261 1.00 38.25  ?  247 GLN B CB    1 
ATOM   4316 C  CG    . GLN B 1 247 ? -4.899  -13.462 -24.984 1.00 33.95  ?  247 GLN B CG    1 
ATOM   4317 C  CD    . GLN B 1 247 ? -6.362  -13.468 -25.418 1.00 50.72  ?  247 GLN B CD    1 
ATOM   4318 O  OE1   . GLN B 1 247 ? -6.683  -13.202 -26.580 1.00 50.17  ?  247 GLN B OE1   1 
ATOM   4319 N  NE2   . GLN B 1 247 ? -7.260  -13.780 -24.477 1.00 54.97  ?  247 GLN B NE2   1 
ATOM   4320 N  N     . VAL B 1 248 ? -4.144  -9.175  -23.335 1.00 31.19  ?  248 VAL B N     1 
ATOM   4321 C  CA    . VAL B 1 248 ? -4.029  -8.225  -22.237 1.00 31.28  ?  248 VAL B CA    1 
ATOM   4322 C  C     . VAL B 1 248 ? -4.925  -7.005  -22.456 1.00 26.99  ?  248 VAL B C     1 
ATOM   4323 O  O     . VAL B 1 248 ? -5.290  -6.327  -21.487 1.00 26.36  ?  248 VAL B O     1 
ATOM   4324 C  CB    . VAL B 1 248 ? -2.538  -7.877  -22.050 1.00 30.76  ?  248 VAL B CB    1 
ATOM   4325 C  CG1   . VAL B 1 248 ? -2.347  -6.552  -21.306 1.00 23.75  ?  248 VAL B CG1   1 
ATOM   4326 C  CG2   . VAL B 1 248 ? -1.837  -9.026  -21.322 1.00 21.48  ?  248 VAL B CG2   1 
ATOM   4327 N  N     . ARG B 1 249 ? -5.350  -6.754  -23.701 1.00 23.37  ?  249 ARG B N     1 
ATOM   4328 C  CA    . ARG B 1 249 ? -6.250  -5.636  -23.974 1.00 27.52  ?  249 ARG B CA    1 
ATOM   4329 C  C     . ARG B 1 249 ? -7.534  -5.734  -23.160 1.00 31.11  ?  249 ARG B C     1 
ATOM   4330 O  O     . ARG B 1 249 ? -8.066  -4.714  -22.706 1.00 27.18  ?  249 ARG B O     1 
ATOM   4331 C  CB    . ARG B 1 249 ? -6.593  -5.576  -25.456 1.00 22.18  ?  249 ARG B CB    1 
ATOM   4332 C  CG    . ARG B 1 249 ? -5.569  -4.872  -26.294 1.00 20.45  ?  249 ARG B CG    1 
ATOM   4333 C  CD    . ARG B 1 249 ? -6.102  -4.619  -27.694 1.00 20.68  ?  249 ARG B CD    1 
ATOM   4334 N  NE    . ARG B 1 249 ? -5.284  -3.607  -28.352 1.00 21.49  ?  249 ARG B NE    1 
ATOM   4335 C  CZ    . ARG B 1 249 ? -5.468  -3.169  -29.589 1.00 24.06  ?  249 ARG B CZ    1 
ATOM   4336 N  NH1   . ARG B 1 249 ? -6.405  -3.676  -30.378 1.00 27.05  ?  249 ARG B NH1   1 
ATOM   4337 N  NH2   . ARG B 1 249 ? -4.702  -2.188  -30.040 1.00 18.95  ?  249 ARG B NH2   1 
ATOM   4338 N  N     . ARG B 1 250 ? -8.058  -6.948  -22.977 1.00 27.06  ?  250 ARG B N     1 
ATOM   4339 C  CA    . ARG B 1 250 ? -9.342  -7.114  -22.305 1.00 29.14  ?  250 ARG B CA    1 
ATOM   4340 C  C     . ARG B 1 250 ? -9.286  -6.744  -20.830 1.00 26.78  ?  250 ARG B C     1 
ATOM   4341 O  O     . ARG B 1 250 ? -10.325 -6.763  -20.165 1.00 28.40  ?  250 ARG B O     1 
ATOM   4342 C  CB    . ARG B 1 250 ? -9.834  -8.552  -22.459 1.00 28.00  ?  250 ARG B CB    1 
ATOM   4343 C  CG    . ARG B 1 250 ? -9.187  -9.520  -21.493 1.00 31.44  ?  250 ARG B CG    1 
ATOM   4344 C  CD    . ARG B 1 250 ? -9.210  -10.951 -22.036 1.00 43.92  ?  250 ARG B CD    1 
ATOM   4345 N  NE    . ARG B 1 250 ? -8.767  -11.914 -21.032 1.00 50.07  ?  250 ARG B NE    1 
ATOM   4346 C  CZ    . ARG B 1 250 ? -7.557  -11.946 -20.484 1.00 52.94  ?  250 ARG B CZ    1 
ATOM   4347 N  NH1   . ARG B 1 250 ? -6.573  -11.181 -20.929 1.00 45.33  ?  250 ARG B NH1   1 
ATOM   4348 N  NH2   . ARG B 1 250 ? -7.323  -12.786 -19.476 1.00 57.83  ?  250 ARG B NH2   1 
ATOM   4349 N  N     . PHE B 1 251 ? -8.105  -6.433  -20.301 1.00 25.80  ?  251 PHE B N     1 
ATOM   4350 C  CA    . PHE B 1 251 ? -8.009  -5.926  -18.943 1.00 28.80  ?  251 PHE B CA    1 
ATOM   4351 C  C     . PHE B 1 251 ? -8.311  -4.431  -18.851 1.00 32.04  ?  251 PHE B C     1 
ATOM   4352 O  O     . PHE B 1 251 ? -8.566  -3.934  -17.751 1.00 30.28  ?  251 PHE B O     1 
ATOM   4353 C  CB    . PHE B 1 251 ? -6.618  -6.229  -18.377 1.00 28.60  ?  251 PHE B CB    1 
ATOM   4354 C  CG    . PHE B 1 251 ? -6.403  -7.679  -18.057 1.00 30.45  ?  251 PHE B CG    1 
ATOM   4355 C  CD1   . PHE B 1 251 ? -5.325  -8.368  -18.578 1.00 30.67  ?  251 PHE B CD1   1 
ATOM   4356 C  CD2   . PHE B 1 251 ? -7.299  -8.361  -17.250 1.00 33.79  ?  251 PHE B CD2   1 
ATOM   4357 C  CE1   . PHE B 1 251 ? -5.130  -9.714  -18.285 1.00 40.47  ?  251 PHE B CE1   1 
ATOM   4358 C  CE2   . PHE B 1 251 ? -7.113  -9.714  -16.957 1.00 40.98  ?  251 PHE B CE2   1 
ATOM   4359 C  CZ    . PHE B 1 251 ? -6.026  -10.386 -17.470 1.00 38.12  ?  251 PHE B CZ    1 
ATOM   4360 N  N     . MET B 1 252 ? -8.294  -3.707  -19.981 1.00 26.07  ?  252 MET B N     1 
ATOM   4361 C  CA    . MET B 1 252 ? -8.598  -2.280  -19.932 1.00 30.30  ?  252 MET B CA    1 
ATOM   4362 C  C     . MET B 1 252 ? -10.058 -2.040  -19.576 1.00 31.08  ?  252 MET B C     1 
ATOM   4363 O  O     . MET B 1 252 ? -10.323 -1.203  -18.696 1.00 29.99  ?  252 MET B O     1 
ATOM   4364 C  CB    . MET B 1 252 ? -8.216  -1.609  -21.256 1.00 28.37  ?  252 MET B CB    1 
ATOM   4365 C  CG    . MET B 1 252 ? -6.721  -1.426  -21.483 1.00 24.87  ?  252 MET B CG    1 
ATOM   4366 S  SD    . MET B 1 252 ? -5.900  -0.550  -20.152 1.00 27.56  ?  252 MET B SD    1 
ATOM   4367 C  CE    . MET B 1 252 ? -6.709  1.042   -20.303 1.00 27.15  ?  252 MET B CE    1 
ATOM   4368 N  N     . PRO B 1 253 ? -11.043 -2.711  -20.196 1.00 30.43  ?  253 PRO B N     1 
ATOM   4369 C  CA    . PRO B 1 253 ? -12.424 -2.542  -19.710 1.00 36.86  ?  253 PRO B CA    1 
ATOM   4370 C  C     . PRO B 1 253 ? -12.583 -2.912  -18.243 1.00 34.87  ?  253 PRO B C     1 
ATOM   4371 O  O     . PRO B 1 253 ? -13.345 -2.253  -17.518 1.00 30.14  ?  253 PRO B O     1 
ATOM   4372 C  CB    . PRO B 1 253 ? -13.232 -3.465  -20.638 1.00 32.35  ?  253 PRO B CB    1 
ATOM   4373 C  CG    . PRO B 1 253 ? -12.428 -3.505  -21.891 1.00 26.18  ?  253 PRO B CG    1 
ATOM   4374 C  CD    . PRO B 1 253 ? -11.009 -3.570  -21.393 1.00 26.80  ?  253 PRO B CD    1 
ATOM   4375 N  N     . VAL B 1 254 ? -11.862 -3.937  -17.776 1.00 29.12  ?  254 VAL B N     1 
ATOM   4376 C  CA    . VAL B 1 254 ? -11.873 -4.251  -16.348 1.00 29.60  ?  254 VAL B CA    1 
ATOM   4377 C  C     . VAL B 1 254 ? -11.430 -3.037  -15.541 1.00 30.64  ?  254 VAL B C     1 
ATOM   4378 O  O     . VAL B 1 254 ? -12.078 -2.645  -14.563 1.00 31.15  ?  254 VAL B O     1 
ATOM   4379 C  CB    . VAL B 1 254 ? -10.993 -5.482  -16.058 1.00 31.47  ?  254 VAL B CB    1 
ATOM   4380 C  CG1   . VAL B 1 254 ? -10.786 -5.650  -14.565 1.00 31.89  ?  254 VAL B CG1   1 
ATOM   4381 C  CG2   . VAL B 1 254 ? -11.622 -6.731  -16.645 1.00 21.51  ?  254 VAL B CG2   1 
ATOM   4382 N  N     . MET B 1 255 ? -10.325 -2.411  -15.952 1.00 31.94  ?  255 MET B N     1 
ATOM   4383 C  CA    . MET B 1 255 ? -9.842  -1.210  -15.274 1.00 34.70  ?  255 MET B CA    1 
ATOM   4384 C  C     . MET B 1 255 ? -10.885 -0.093  -15.295 1.00 35.04  ?  255 MET B C     1 
ATOM   4385 O  O     . MET B 1 255 ? -11.155 0.537   -14.262 1.00 32.13  ?  255 MET B O     1 
ATOM   4386 C  CB    . MET B 1 255 ? -8.524  -0.766  -15.911 1.00 35.29  ?  255 MET B CB    1 
ATOM   4387 C  CG    . MET B 1 255 ? -7.806  0.412   -15.248 1.00 36.63  ?  255 MET B CG    1 
ATOM   4388 S  SD    . MET B 1 255 ? -8.476  2.024   -15.696 1.00 48.71  ?  255 MET B SD    1 
ATOM   4389 C  CE    . MET B 1 255 ? -7.314  2.517   -16.992 1.00 26.73  ?  255 MET B CE    1 
ATOM   4390 N  N     . TYR B 1 256 ? -11.482 0.169   -16.463 1.00 29.20  ?  256 TYR B N     1 
ATOM   4391 C  CA    . TYR B 1 256 ? -12.503 1.211   -16.547 1.00 33.50  ?  256 TYR B CA    1 
ATOM   4392 C  C     . TYR B 1 256 ? -13.673 0.930   -15.607 1.00 35.99  ?  256 TYR B C     1 
ATOM   4393 O  O     . TYR B 1 256 ? -14.177 1.846   -14.946 1.00 29.95  ?  256 TYR B O     1 
ATOM   4394 C  CB    . TYR B 1 256 ? -13.014 1.344   -17.978 1.00 33.04  ?  256 TYR B CB    1 
ATOM   4395 C  CG    . TYR B 1 256 ? -12.032 1.984   -18.929 1.00 36.08  ?  256 TYR B CG    1 
ATOM   4396 C  CD1   . TYR B 1 256 ? -11.683 3.324   -18.814 1.00 35.64  ?  256 TYR B CD1   1 
ATOM   4397 C  CD2   . TYR B 1 256 ? -11.475 1.247   -19.968 1.00 37.49  ?  256 TYR B CD2   1 
ATOM   4398 C  CE1   . TYR B 1 256 ? -10.781 3.906   -19.709 1.00 37.57  ?  256 TYR B CE1   1 
ATOM   4399 C  CE2   . TYR B 1 256 ? -10.586 1.804   -20.851 1.00 32.71  ?  256 TYR B CE2   1 
ATOM   4400 C  CZ    . TYR B 1 256 ? -10.241 3.130   -20.722 1.00 39.33  ?  256 TYR B CZ    1 
ATOM   4401 O  OH    . TYR B 1 256 ? -9.348  3.657   -21.627 1.00 46.28  ?  256 TYR B OH    1 
ATOM   4402 N  N     . GLN B 1 257 ? -14.127 -0.328  -15.548 1.00 35.60  ?  257 GLN B N     1 
ATOM   4403 C  CA    . GLN B 1 257 ? -15.235 -0.689  -14.663 1.00 34.33  ?  257 GLN B CA    1 
ATOM   4404 C  C     . GLN B 1 257 ? -14.871 -0.427  -13.212 1.00 31.73  ?  257 GLN B C     1 
ATOM   4405 O  O     . GLN B 1 257 ? -15.652 0.163   -12.459 1.00 36.67  ?  257 GLN B O     1 
ATOM   4406 C  CB    . GLN B 1 257 ? -15.615 -2.159  -14.857 1.00 33.31  ?  257 GLN B CB    1 
ATOM   4407 C  CG    . GLN B 1 257 ? -16.503 -2.420  -16.047 1.00 34.62  ?  257 GLN B CG    1 
ATOM   4408 C  CD    . GLN B 1 257 ? -17.198 -1.166  -16.540 1.00 37.00  ?  257 GLN B CD    1 
ATOM   4409 O  OE1   . GLN B 1 257 ? -18.092 -0.637  -15.885 1.00 47.96  ?  257 GLN B OE1   1 
ATOM   4410 N  NE2   . GLN B 1 257 ? -16.779 -0.678  -17.703 1.00 52.10  ?  257 GLN B NE2   1 
ATOM   4411 N  N     . MET B 1 258 ? -13.677 -0.857  -12.809 1.00 29.38  ?  258 MET B N     1 
ATOM   4412 C  CA    . MET B 1 258 ? -13.184 -0.559  -11.472 1.00 31.48  ?  258 MET B CA    1 
ATOM   4413 C  C     . MET B 1 258 ? -13.216 0.936   -11.188 1.00 37.43  ?  258 MET B C     1 
ATOM   4414 O  O     . MET B 1 258 ? -13.586 1.361   -10.088 1.00 38.70  ?  258 MET B O     1 
ATOM   4415 C  CB    . MET B 1 258 ? -11.769 -1.101  -11.318 1.00 25.77  ?  258 MET B CB    1 
ATOM   4416 C  CG    . MET B 1 258 ? -11.687 -2.610  -11.412 1.00 36.58  ?  258 MET B CG    1 
ATOM   4417 S  SD    . MET B 1 258 ? -10.063 -3.211  -10.923 1.00 49.45  ?  258 MET B SD    1 
ATOM   4418 C  CE    . MET B 1 258 ? -9.493  -1.833  -9.921  1.00 38.86  ?  258 MET B CE    1 
ATOM   4419 N  N     . ALA B 1 259 ? -12.846 1.755   -12.174 1.00 34.95  ?  259 ALA B N     1 
ATOM   4420 C  CA    . ALA B 1 259 ? -12.803 3.188   -11.928 1.00 34.32  ?  259 ALA B CA    1 
ATOM   4421 C  C     . ALA B 1 259 ? -14.198 3.800   -11.878 1.00 30.97  ?  259 ALA B C     1 
ATOM   4422 O  O     . ALA B 1 259 ? -14.402 4.782   -11.159 1.00 35.56  ?  259 ALA B O     1 
ATOM   4423 C  CB    . ALA B 1 259 ? -11.940 3.881   -12.985 1.00 36.48  ?  259 ALA B CB    1 
ATOM   4424 N  N     . TYR B 1 260 ? -15.162 3.262   -12.638 1.00 26.91  ?  260 TYR B N     1 
ATOM   4425 C  CA    . TYR B 1 260 ? -16.533 3.756   -12.537 1.00 31.65  ?  260 TYR B CA    1 
ATOM   4426 C  C     . TYR B 1 260 ? -17.116 3.429   -11.168 1.00 37.23  ?  260 TYR B C     1 
ATOM   4427 O  O     . TYR B 1 260 ? -17.647 4.310   -10.476 1.00 33.35  ?  260 TYR B O     1 
ATOM   4428 C  CB    . TYR B 1 260 ? -17.419 3.161   -13.632 1.00 25.58  ?  260 TYR B CB    1 
ATOM   4429 C  CG    . TYR B 1 260 ? -17.004 3.463   -15.045 1.00 36.46  ?  260 TYR B CG    1 
ATOM   4430 C  CD1   . TYR B 1 260 ? -16.603 4.744   -15.421 1.00 41.81  ?  260 TYR B CD1   1 
ATOM   4431 C  CD2   . TYR B 1 260 ? -17.014 2.463   -16.017 1.00 38.76  ?  260 TYR B CD2   1 
ATOM   4432 C  CE1   . TYR B 1 260 ? -16.219 5.017   -16.728 1.00 41.92  ?  260 TYR B CE1   1 
ATOM   4433 C  CE2   . TYR B 1 260 ? -16.628 2.721   -17.320 1.00 37.47  ?  260 TYR B CE2   1 
ATOM   4434 C  CZ    . TYR B 1 260 ? -16.233 4.003   -17.677 1.00 41.16  ?  260 TYR B CZ    1 
ATOM   4435 O  OH    . TYR B 1 260 ? -15.850 4.264   -18.983 1.00 40.51  ?  260 TYR B OH    1 
ATOM   4436 N  N     . ALA B 1 261 ? -17.023 2.156   -10.771 1.00 33.45  ?  261 ALA B N     1 
ATOM   4437 C  CA    . ALA B 1 261 ? -17.436 1.734   -9.438  1.00 38.19  ?  261 ALA B CA    1 
ATOM   4438 C  C     . ALA B 1 261 ? -16.851 2.644   -8.378  1.00 40.00  ?  261 ALA B C     1 
ATOM   4439 O  O     . ALA B 1 261 ? -17.538 3.023   -7.420  1.00 43.59  ?  261 ALA B O     1 
ATOM   4440 C  CB    . ALA B 1 261 ? -17.003 0.288   -9.189  1.00 34.84  ?  261 ALA B CB    1 
ATOM   4441 N  N     . SER B 1 262 ? -15.584 3.019   -8.541  1.00 36.40  ?  262 SER B N     1 
ATOM   4442 C  CA    . SER B 1 262 ? -14.979 3.938   -7.589  1.00 41.45  ?  262 SER B CA    1 
ATOM   4443 C  C     . SER B 1 262 ? -15.700 5.278   -7.598  1.00 43.14  ?  262 SER B C     1 
ATOM   4444 O  O     . SER B 1 262 ? -15.987 5.845   -6.535  1.00 41.95  ?  262 SER B O     1 
ATOM   4445 C  CB    . SER B 1 262 ? -13.498 4.115   -7.901  1.00 37.16  ?  262 SER B CB    1 
ATOM   4446 O  OG    . SER B 1 262 ? -12.837 4.783   -6.843  1.00 40.60  ?  262 SER B OG    1 
ATOM   4447 N  N     . PHE B 1 263 ? -16.024 5.789   -8.789  1.00 41.49  ?  263 PHE B N     1 
ATOM   4448 C  CA    . PHE B 1 263 ? -16.652 7.103   -8.878  1.00 44.92  ?  263 PHE B CA    1 
ATOM   4449 C  C     . PHE B 1 263 ? -18.028 7.087   -8.219  1.00 46.23  ?  263 PHE B C     1 
ATOM   4450 O  O     . PHE B 1 263 ? -18.361 7.967   -7.415  1.00 36.88  ?  263 PHE B O     1 
ATOM   4451 C  CB    . PHE B 1 263 ? -16.758 7.540   -10.339 1.00 37.87  ?  263 PHE B CB    1 
ATOM   4452 C  CG    . PHE B 1 263 ? -15.450 8.005   -10.944 1.00 44.12  ?  263 PHE B CG    1 
ATOM   4453 C  CD1   . PHE B 1 263 ? -14.343 8.262   -10.147 1.00 47.98  ?  263 PHE B CD1   1 
ATOM   4454 C  CD2   . PHE B 1 263 ? -15.331 8.181   -12.316 1.00 42.08  ?  263 PHE B CD2   1 
ATOM   4455 C  CE1   . PHE B 1 263 ? -13.141 8.695   -10.708 1.00 41.98  ?  263 PHE B CE1   1 
ATOM   4456 C  CE2   . PHE B 1 263 ? -14.126 8.616   -12.885 1.00 40.28  ?  263 PHE B CE2   1 
ATOM   4457 C  CZ    . PHE B 1 263 ? -13.035 8.869   -12.079 1.00 33.57  ?  263 PHE B CZ    1 
ATOM   4458 N  N     . GLU B 1 264 ? -18.838 6.079   -8.540  1.00 40.13  ?  264 GLU B N     1 
ATOM   4459 C  CA    . GLU B 1 264 ? -20.162 5.999   -7.947  1.00 46.28  ?  264 GLU B CA    1 
ATOM   4460 C  C     . GLU B 1 264 ? -20.105 5.876   -6.432  1.00 44.61  ?  264 GLU B C     1 
ATOM   4461 O  O     . GLU B 1 264 ? -21.052 6.289   -5.754  1.00 44.58  ?  264 GLU B O     1 
ATOM   4462 C  CB    . GLU B 1 264 ? -20.927 4.839   -8.572  1.00 44.69  ?  264 GLU B CB    1 
ATOM   4463 C  CG    . GLU B 1 264 ? -21.065 5.019   -10.072 1.00 48.23  ?  264 GLU B CG    1 
ATOM   4464 C  CD    . GLU B 1 264 ? -22.315 4.374   -10.643 1.00 59.17  ?  264 GLU B CD    1 
ATOM   4465 O  OE1   . GLU B 1 264 ? -23.333 5.089   -10.823 1.00 51.94  ?  264 GLU B OE1   1 
ATOM   4466 O  OE2   . GLU B 1 264 ? -22.268 3.156   -10.929 1.00 63.49  ?  264 GLU B OE2   1 
ATOM   4467 N  N     . ALA B 1 265 ? -19.006 5.359   -5.886  1.00 44.23  ?  265 ALA B N     1 
ATOM   4468 C  CA    . ALA B 1 265 ? -18.804 5.282   -4.445  1.00 41.97  ?  265 ALA B CA    1 
ATOM   4469 C  C     . ALA B 1 265 ? -18.092 6.504   -3.876  1.00 40.46  ?  265 ALA B C     1 
ATOM   4470 O  O     . ALA B 1 265 ? -17.667 6.469   -2.717  1.00 36.74  ?  265 ALA B O     1 
ATOM   4471 C  CB    . ALA B 1 265 ? -18.014 4.021   -4.090  1.00 38.11  ?  265 ALA B CB    1 
ATOM   4472 N  N     . GLY B 1 266 ? -17.928 7.566   -4.664  1.00 46.03  ?  266 GLY B N     1 
ATOM   4473 C  CA    . GLY B 1 266 ? -17.267 8.770   -4.178  1.00 38.28  ?  266 GLY B CA    1 
ATOM   4474 C  C     . GLY B 1 266 ? -15.835 8.569   -3.737  1.00 39.83  ?  266 GLY B C     1 
ATOM   4475 O  O     . GLY B 1 266 ? -15.328 9.346   -2.922  1.00 39.27  ?  266 GLY B O     1 
ATOM   4476 N  N     . VAL B 1 267 ? -15.162 7.551   -4.259  1.00 40.75  ?  267 VAL B N     1 
ATOM   4477 C  CA    . VAL B 1 267 ? -13.789 7.227   -3.878  1.00 43.09  ?  267 VAL B CA    1 
ATOM   4478 C  C     . VAL B 1 267 ? -12.856 7.811   -4.929  1.00 45.26  ?  267 VAL B C     1 
ATOM   4479 O  O     . VAL B 1 267 ? -12.948 7.428   -6.106  1.00 42.51  ?  267 VAL B O     1 
ATOM   4480 C  CB    . VAL B 1 267 ? -13.583 5.711   -3.732  1.00 41.97  ?  267 VAL B CB    1 
ATOM   4481 C  CG1   . VAL B 1 267 ? -12.195 5.413   -3.176  1.00 37.16  ?  267 VAL B CG1   1 
ATOM   4482 C  CG2   . VAL B 1 267 ? -14.655 5.136   -2.811  1.00 43.72  ?  267 VAL B CG2   1 
ATOM   4483 N  N     . PRO B 1 268 ? -11.981 8.744   -4.574  1.00 49.58  ?  268 PRO B N     1 
ATOM   4484 C  CA    . PRO B 1 268 ? -11.047 9.279   -5.568  1.00 51.20  ?  268 PRO B CA    1 
ATOM   4485 C  C     . PRO B 1 268 ? -9.937  8.285   -5.874  1.00 46.57  ?  268 PRO B C     1 
ATOM   4486 O  O     . PRO B 1 268 ? -9.429  7.595   -4.986  1.00 43.42  ?  268 PRO B O     1 
ATOM   4487 C  CB    . PRO B 1 268 ? -10.508 10.558  -4.910  1.00 54.89  ?  268 PRO B CB    1 
ATOM   4488 C  CG    . PRO B 1 268 ? -10.796 10.407  -3.445  1.00 52.38  ?  268 PRO B CG    1 
ATOM   4489 C  CD    . PRO B 1 268 ? -11.994 9.520   -3.321  1.00 49.66  ?  268 PRO B CD    1 
ATOM   4490 N  N     . LEU B 1 269 ? -9.582  8.211   -7.156  1.00 53.44  ?  269 LEU B N     1 
ATOM   4491 C  CA    . LEU B 1 269 ? -8.499  7.369   -7.640  1.00 49.97  ?  269 LEU B CA    1 
ATOM   4492 C  C     . LEU B 1 269 ? -7.143  8.009   -7.356  1.00 42.20  ?  269 LEU B C     1 
ATOM   4493 O  O     . LEU B 1 269 ? -7.021  9.222   -7.174  1.00 38.42  ?  269 LEU B O     1 
ATOM   4494 C  CB    . LEU B 1 269 ? -8.635  7.124   -9.146  1.00 45.15  ?  269 LEU B CB    1 
ATOM   4495 C  CG    . LEU B 1 269 ? -9.918  6.460   -9.642  1.00 43.82  ?  269 LEU B CG    1 
ATOM   4496 C  CD1   . LEU B 1 269 ? -9.972  6.445   -11.160 1.00 37.74  ?  269 LEU B CD1   1 
ATOM   4497 C  CD2   . LEU B 1 269 ? -10.010 5.058   -9.088  1.00 41.60  ?  269 LEU B CD2   1 
ATOM   4498 N  N     . ASP B 1 270 ? -6.117  7.163   -7.324  1.00 48.73  ?  270 ASP B N     1 
ATOM   4499 C  CA    . ASP B 1 270 ? -4.736  7.628   -7.295  1.00 47.64  ?  270 ASP B CA    1 
ATOM   4500 C  C     . ASP B 1 270 ? -4.495  8.659   -8.398  1.00 42.94  ?  270 ASP B C     1 
ATOM   4501 O  O     . ASP B 1 270 ? -5.012  8.525   -9.510  1.00 43.38  ?  270 ASP B O     1 
ATOM   4502 C  CB    . ASP B 1 270 ? -3.808  6.420   -7.469  1.00 46.93  ?  270 ASP B CB    1 
ATOM   4503 C  CG    . ASP B 1 270 ? -2.364  6.729   -7.139  1.00 51.80  ?  270 ASP B CG    1 
ATOM   4504 O  OD1   . ASP B 1 270 ? -1.689  7.390   -7.967  1.00 50.04  ?  270 ASP B OD1   1 
ATOM   4505 O  OD2   . ASP B 1 270 ? -1.905  6.292   -6.056  1.00 51.06  ?  270 ASP B OD2   1 
ATOM   4506 N  N     . HIS B 1 271 ? -3.724  9.710   -8.081  1.00 35.86  ?  271 HIS B N     1 
ATOM   4507 C  CA    . HIS B 1 271 ? -3.409  10.730  -9.083  1.00 48.03  ?  271 HIS B CA    1 
ATOM   4508 C  C     . HIS B 1 271 ? -2.577  10.171  -10.235 1.00 43.93  ?  271 HIS B C     1 
ATOM   4509 O  O     . HIS B 1 271 ? -2.564  10.764  -11.319 1.00 45.77  ?  271 HIS B O     1 
ATOM   4510 C  CB    . HIS B 1 271 ? -2.671  11.915  -8.438  1.00 47.05  ?  271 HIS B CB    1 
ATOM   4511 C  CG    . HIS B 1 271 ? -2.301  13.014  -9.400  1.00 47.77  ?  271 HIS B CG    1 
ATOM   4512 N  ND1   . HIS B 1 271 ? -1.034  13.559  -9.459  1.00 46.80  ?  271 HIS B ND1   1 
ATOM   4513 C  CD2   . HIS B 1 271 ? -3.035  13.679  -10.327 1.00 48.08  ?  271 HIS B CD2   1 
ATOM   4514 C  CE1   . HIS B 1 271 ? -1.002  14.508  -10.380 1.00 39.40  ?  271 HIS B CE1   1 
ATOM   4515 N  NE2   . HIS B 1 271 ? -2.203  14.599  -10.923 1.00 41.13  ?  271 HIS B NE2   1 
ATOM   4516 N  N     . HIS B 1 272 ? -1.895  9.044   -10.029 1.00 38.38  ?  272 HIS B N     1 
ATOM   4517 C  CA    . HIS B 1 272 ? -1.081  8.414   -11.061 1.00 43.76  ?  272 HIS B CA    1 
ATOM   4518 C  C     . HIS B 1 272 ? -1.615  7.031   -11.431 1.00 42.12  ?  272 HIS B C     1 
ATOM   4519 O  O     . HIS B 1 272 ? -0.865  6.176   -11.902 1.00 43.96  ?  272 HIS B O     1 
ATOM   4520 C  CB    . HIS B 1 272 ? 0.380   8.340   -10.614 1.00 38.13  ?  272 HIS B CB    1 
ATOM   4521 C  CG    . HIS B 1 272 ? 1.018   9.686   -10.435 1.00 44.74  ?  272 HIS B CG    1 
ATOM   4522 N  ND1   . HIS B 1 272 ? 0.991   10.658  -11.414 1.00 42.72  ?  272 HIS B ND1   1 
ATOM   4523 C  CD2   . HIS B 1 272 ? 1.680   10.228  -9.385  1.00 40.58  ?  272 HIS B CD2   1 
ATOM   4524 C  CE1   . HIS B 1 272 ? 1.616   11.738  -10.978 1.00 41.59  ?  272 HIS B CE1   1 
ATOM   4525 N  NE2   . HIS B 1 272 ? 2.044   11.505  -9.750  1.00 40.42  ?  272 HIS B NE2   1 
ATOM   4526 N  N     . TYR B 1 273 ? -2.923  6.818   -11.259 1.00 38.09  ?  273 TYR B N     1 
ATOM   4527 C  CA    . TYR B 1 273 ? -3.497  5.487   -11.432 1.00 35.70  ?  273 TYR B CA    1 
ATOM   4528 C  C     . TYR B 1 273 ? -3.268  4.926   -12.837 1.00 32.63  ?  273 TYR B C     1 
ATOM   4529 O  O     . TYR B 1 273 ? -3.090  3.713   -12.999 1.00 27.83  ?  273 TYR B O     1 
ATOM   4530 C  CB    . TYR B 1 273 ? -4.987  5.523   -11.107 1.00 34.89  ?  273 TYR B CB    1 
ATOM   4531 C  CG    . TYR B 1 273 ? -5.878  6.053   -12.210 1.00 28.34  ?  273 TYR B CG    1 
ATOM   4532 C  CD1   . TYR B 1 273 ? -6.169  7.404   -12.308 1.00 36.65  ?  273 TYR B CD1   1 
ATOM   4533 C  CD2   . TYR B 1 273 ? -6.461  5.194   -13.128 1.00 34.60  ?  273 TYR B CD2   1 
ATOM   4534 C  CE1   . TYR B 1 273 ? -6.997  7.887   -13.302 1.00 33.03  ?  273 TYR B CE1   1 
ATOM   4535 C  CE2   . TYR B 1 273 ? -7.278  5.666   -14.127 1.00 32.95  ?  273 TYR B CE2   1 
ATOM   4536 C  CZ    . TYR B 1 273 ? -7.546  7.009   -14.209 1.00 35.29  ?  273 TYR B CZ    1 
ATOM   4537 O  OH    . TYR B 1 273 ? -8.370  7.471   -15.208 1.00 35.92  ?  273 TYR B OH    1 
ATOM   4538 N  N     . TYR B 1 274 ? -3.308  5.775   -13.872 1.00 32.80  ?  274 TYR B N     1 
ATOM   4539 C  CA    . TYR B 1 274 ? -3.107  5.261   -15.230 1.00 35.75  ?  274 TYR B CA    1 
ATOM   4540 C  C     . TYR B 1 274 ? -1.663  4.822   -15.434 1.00 28.92  ?  274 TYR B C     1 
ATOM   4541 O  O     . TYR B 1 274 ? -1.399  3.780   -16.041 1.00 28.24  ?  274 TYR B O     1 
ATOM   4542 C  CB    . TYR B 1 274 ? -3.514  6.311   -16.272 1.00 31.70  ?  274 TYR B CB    1 
ATOM   4543 C  CG    . TYR B 1 274 ? -3.346  5.860   -17.710 1.00 30.02  ?  274 TYR B CG    1 
ATOM   4544 C  CD1   . TYR B 1 274 ? -4.327  5.098   -18.350 1.00 34.13  ?  274 TYR B CD1   1 
ATOM   4545 C  CD2   . TYR B 1 274 ? -2.203  6.198   -18.435 1.00 33.79  ?  274 TYR B CD2   1 
ATOM   4546 C  CE1   . TYR B 1 274 ? -4.170  4.681   -19.684 1.00 28.86  ?  274 TYR B CE1   1 
ATOM   4547 C  CE2   . TYR B 1 274 ? -2.037  5.786   -19.758 1.00 28.59  ?  274 TYR B CE2   1 
ATOM   4548 C  CZ    . TYR B 1 274 ? -3.020  5.032   -20.373 1.00 24.59  ?  274 TYR B CZ    1 
ATOM   4549 O  OH    . TYR B 1 274 ? -2.828  4.629   -21.670 1.00 22.93  ?  274 TYR B OH    1 
ATOM   4550 N  N     . GLU B 1 275 ? -0.719  5.576   -14.882 1.00 31.61  ?  275 GLU B N     1 
ATOM   4551 C  CA    . GLU B 1 275 ? 0.682   5.183   -14.950 1.00 31.02  ?  275 GLU B CA    1 
ATOM   4552 C  C     . GLU B 1 275 ? 0.973   3.935   -14.120 1.00 30.32  ?  275 GLU B C     1 
ATOM   4553 O  O     . GLU B 1 275 ? 1.874   3.163   -14.464 1.00 27.04  ?  275 GLU B O     1 
ATOM   4554 C  CB    . GLU B 1 275 ? 1.548   6.357   -14.501 1.00 39.39  ?  275 GLU B CB    1 
ATOM   4555 C  CG    . GLU B 1 275 ? 1.460   7.583   -15.423 1.00 33.66  ?  275 GLU B CG    1 
ATOM   4556 C  CD    . GLU B 1 275 ? 0.256   8.504   -15.165 1.00 45.11  ?  275 GLU B CD    1 
ATOM   4557 O  OE1   . GLU B 1 275 ? -0.155  8.654   -14.002 1.00 44.22  ?  275 GLU B OE1   1 
ATOM   4558 O  OE2   . GLU B 1 275 ? -0.265  9.108   -16.132 1.00 51.92  ?  275 GLU B OE2   1 
ATOM   4559 N  N     . ARG B 1 276 ? 0.238   3.716   -13.024 1.00 34.16  ?  276 ARG B N     1 
ATOM   4560 C  CA    . ARG B 1 276 ? 0.401   2.478   -12.264 1.00 28.34  ?  276 ARG B CA    1 
ATOM   4561 C  C     . ARG B 1 276 ? -0.271  1.302   -12.954 1.00 28.09  ?  276 ARG B C     1 
ATOM   4562 O  O     . ARG B 1 276 ? 0.189   0.159   -12.828 1.00 25.53  ?  276 ARG B O     1 
ATOM   4563 C  CB    . ARG B 1 276 ? -0.153  2.648   -10.846 1.00 35.47  ?  276 ARG B CB    1 
ATOM   4564 C  CG    . ARG B 1 276 ? 0.332   3.913   -10.176 1.00 41.37  ?  276 ARG B CG    1 
ATOM   4565 C  CD    . ARG B 1 276 ? 0.084   3.951   -8.677  1.00 48.59  ?  276 ARG B CD    1 
ATOM   4566 N  NE    . ARG B 1 276 ? 0.556   5.224   -8.144  1.00 47.04  ?  276 ARG B NE    1 
ATOM   4567 C  CZ    . ARG B 1 276 ? 1.735   5.398   -7.563  1.00 43.24  ?  276 ARG B CZ    1 
ATOM   4568 N  NH1   . ARG B 1 276 ? 2.579   4.395   -7.398  1.00 44.14  ?  276 ARG B NH1   1 
ATOM   4569 N  NH2   . ARG B 1 276 ? 2.080   6.611   -7.145  1.00 36.64  ?  276 ARG B NH2   1 
ATOM   4570 N  N     . THR B 1 277 ? -1.355  1.565   -13.682 1.00 26.37  ?  277 THR B N     1 
ATOM   4571 C  CA    . THR B 1 277 ? -1.980  0.529   -14.499 1.00 26.79  ?  277 THR B CA    1 
ATOM   4572 C  C     . THR B 1 277 ? -1.054  0.054   -15.625 1.00 29.35  ?  277 THR B C     1 
ATOM   4573 O  O     . THR B 1 277 ? -1.090  -1.122  -16.012 1.00 24.98  ?  277 THR B O     1 
ATOM   4574 C  CB    . THR B 1 277 ? -3.302  1.070   -15.042 1.00 30.50  ?  277 THR B CB    1 
ATOM   4575 O  OG1   . THR B 1 277 ? -4.202  1.292   -13.941 1.00 30.12  ?  277 THR B OG1   1 
ATOM   4576 C  CG2   . THR B 1 277 ? -3.936  0.117   -16.045 1.00 25.65  ?  277 THR B CG2   1 
ATOM   4577 N  N     . LEU B 1 278 ? -0.204  0.940   -16.149 1.00 26.02  ?  278 LEU B N     1 
ATOM   4578 C  CA    . LEU B 1 278 ? 0.751   0.513   -17.165 1.00 21.42  ?  278 LEU B CA    1 
ATOM   4579 C  C     . LEU B 1 278 ? 1.774   -0.443  -16.584 1.00 24.43  ?  278 LEU B C     1 
ATOM   4580 O  O     . LEU B 1 278 ? 2.215   -1.365  -17.274 1.00 25.15  ?  278 LEU B O     1 
ATOM   4581 C  CB    . LEU B 1 278 ? 1.475   1.714   -17.780 1.00 16.17  ?  278 LEU B CB    1 
ATOM   4582 C  CG    . LEU B 1 278 ? 0.609   2.732   -18.508 1.00 20.00  ?  278 LEU B CG    1 
ATOM   4583 C  CD1   . LEU B 1 278 ? 1.463   3.936   -18.947 1.00 22.99  ?  278 LEU B CD1   1 
ATOM   4584 C  CD2   . LEU B 1 278 ? -0.098  2.070   -19.674 1.00 17.52  ?  278 LEU B CD2   1 
ATOM   4585 N  N     . GLN B 1 279 ? 2.208   -0.209  -15.338 1.00 22.57  ?  279 GLN B N     1 
ATOM   4586 C  CA    . GLN B 1 279 ? 3.146   -1.134  -14.716 1.00 23.91  ?  279 GLN B CA    1 
ATOM   4587 C  C     . GLN B 1 279 ? 2.522   -2.514  -14.597 1.00 32.36  ?  279 GLN B C     1 
ATOM   4588 O  O     . GLN B 1 279 ? 3.180   -3.533  -14.856 1.00 32.38  ?  279 GLN B O     1 
ATOM   4589 C  CB    . GLN B 1 279 ? 3.588   -0.618  -13.348 1.00 26.51  ?  279 GLN B CB    1 
ATOM   4590 C  CG    . GLN B 1 279 ? 4.863   0.208   -13.370 1.00 34.75  ?  279 GLN B CG    1 
ATOM   4591 C  CD    . GLN B 1 279 ? 6.112   -0.606  -13.028 1.00 43.33  ?  279 GLN B CD    1 
ATOM   4592 O  OE1   . GLN B 1 279 ? 6.311   -1.016  -11.883 1.00 55.65  ?  279 GLN B OE1   1 
ATOM   4593 N  NE2   . GLN B 1 279 ? 6.958   -0.840  -14.023 1.00 41.37  ?  279 GLN B NE2   1 
ATOM   4594 N  N     . VAL B 1 280 ? 1.233   -2.558  -14.253 1.00 31.12  ?  280 VAL B N     1 
ATOM   4595 C  CA    . VAL B 1 280 ? 0.519   -3.827  -14.157 1.00 30.88  ?  280 VAL B CA    1 
ATOM   4596 C  C     . VAL B 1 280 ? 0.438   -4.495  -15.524 1.00 34.19  ?  280 VAL B C     1 
ATOM   4597 O  O     . VAL B 1 280 ? 0.723   -5.691  -15.669 1.00 31.62  ?  280 VAL B O     1 
ATOM   4598 C  CB    . VAL B 1 280 ? -0.880  -3.606  -13.559 1.00 25.89  ?  280 VAL B CB    1 
ATOM   4599 C  CG1   . VAL B 1 280 ? -1.620  -4.937  -13.453 1.00 34.98  ?  280 VAL B CG1   1 
ATOM   4600 C  CG2   . VAL B 1 280 ? -0.766  -2.927  -12.217 1.00 27.97  ?  280 VAL B CG2   1 
ATOM   4601 N  N     . LEU B 1 281 ? 0.034   -3.733  -16.547 1.00 27.74  ?  281 LEU B N     1 
ATOM   4602 C  CA    . LEU B 1 281 ? -0.146  -4.318  -17.869 1.00 26.23  ?  281 LEU B CA    1 
ATOM   4603 C  C     . LEU B 1 281 ? 1.178   -4.771  -18.456 1.00 26.17  ?  281 LEU B C     1 
ATOM   4604 O  O     . LEU B 1 281 ? 1.215   -5.756  -19.204 1.00 24.27  ?  281 LEU B O     1 
ATOM   4605 C  CB    . LEU B 1 281 ? -0.818  -3.321  -18.805 1.00 25.31  ?  281 LEU B CB    1 
ATOM   4606 C  CG    . LEU B 1 281 ? -2.248  -2.896  -18.467 1.00 28.20  ?  281 LEU B CG    1 
ATOM   4607 C  CD1   . LEU B 1 281 ? -2.598  -1.562  -19.171 1.00 30.40  ?  281 LEU B CD1   1 
ATOM   4608 C  CD2   . LEU B 1 281 ? -3.244  -3.982  -18.832 1.00 25.36  ?  281 LEU B CD2   1 
ATOM   4609 N  N     . TYR B 1 282 ? 2.270   -4.075  -18.123 1.00 24.96  ?  282 TYR B N     1 
ATOM   4610 C  CA    . TYR B 1 282 ? 3.573   -4.429  -18.680 1.00 29.29  ?  282 TYR B CA    1 
ATOM   4611 C  C     . TYR B 1 282 ? 4.015   -5.806  -18.197 1.00 29.68  ?  282 TYR B C     1 
ATOM   4612 O  O     . TYR B 1 282 ? 4.606   -6.581  -18.959 1.00 29.76  ?  282 TYR B O     1 
ATOM   4613 C  CB    . TYR B 1 282 ? 4.601   -3.358  -18.314 1.00 20.32  ?  282 TYR B CB    1 
ATOM   4614 C  CG    . TYR B 1 282 ? 5.949   -3.556  -18.964 1.00 26.53  ?  282 TYR B CG    1 
ATOM   4615 C  CD1   . TYR B 1 282 ? 6.146   -3.276  -20.320 1.00 26.46  ?  282 TYR B CD1   1 
ATOM   4616 C  CD2   . TYR B 1 282 ? 7.031   -4.016  -18.224 1.00 26.60  ?  282 TYR B CD2   1 
ATOM   4617 C  CE1   . TYR B 1 282 ? 7.386   -3.462  -20.920 1.00 25.23  ?  282 TYR B CE1   1 
ATOM   4618 C  CE2   . TYR B 1 282 ? 8.271   -4.201  -18.810 1.00 29.88  ?  282 TYR B CE2   1 
ATOM   4619 C  CZ    . TYR B 1 282 ? 8.440   -3.926  -20.155 1.00 27.53  ?  282 TYR B CZ    1 
ATOM   4620 O  OH    . TYR B 1 282 ? 9.672   -4.119  -20.720 1.00 34.22  ?  282 TYR B OH    1 
ATOM   4621 N  N     . ARG B 1 283 ? 3.703   -6.139  -16.941 1.00 30.19  ?  283 ARG B N     1 
ATOM   4622 C  CA    . ARG B 1 283 ? 3.991   -7.477  -16.430 1.00 34.52  ?  283 ARG B CA    1 
ATOM   4623 C  C     . ARG B 1 283 ? 3.056   -8.524  -17.026 1.00 28.33  ?  283 ARG B C     1 
ATOM   4624 O  O     . ARG B 1 283 ? 3.466   -9.666  -17.243 1.00 31.35  ?  283 ARG B O     1 
ATOM   4625 C  CB    . ARG B 1 283 ? 3.903   -7.481  -14.904 1.00 36.09  ?  283 ARG B CB    1 
ATOM   4626 C  CG    . ARG B 1 283 ? 4.673   -6.353  -14.260 1.00 36.67  ?  283 ARG B CG    1 
ATOM   4627 C  CD    . ARG B 1 283 ? 4.663   -6.460  -12.749 1.00 42.61  ?  283 ARG B CD    1 
ATOM   4628 N  NE    . ARG B 1 283 ? 3.492   -5.803  -12.182 1.00 39.99  ?  283 ARG B NE    1 
ATOM   4629 C  CZ    . ARG B 1 283 ? 3.518   -4.658  -11.512 1.00 45.39  ?  283 ARG B CZ    1 
ATOM   4630 N  NH1   . ARG B 1 283 ? 4.648   -3.989  -11.328 1.00 45.56  ?  283 ARG B NH1   1 
ATOM   4631 N  NH2   . ARG B 1 283 ? 2.380   -4.164  -11.026 1.00 44.48  ?  283 ARG B NH2   1 
ATOM   4632 N  N     . ALA B 1 284 ? 1.809   -8.152  -17.319 1.00 29.44  ?  284 ALA B N     1 
ATOM   4633 C  CA    . ALA B 1 284 ? 0.878   -9.078  -17.952 1.00 28.68  ?  284 ALA B CA    1 
ATOM   4634 C  C     . ALA B 1 284 ? 1.306   -9.486  -19.351 1.00 32.31  ?  284 ALA B C     1 
ATOM   4635 O  O     . ALA B 1 284 ? 0.667   -10.367 -19.942 1.00 33.32  ?  284 ALA B O     1 
ATOM   4636 C  CB    . ALA B 1 284 ? -0.520  -8.459  -18.012 1.00 22.73  ?  284 ALA B CB    1 
ATOM   4637 N  N     . LEU B 1 285 ? 2.361   -8.877  -19.892 1.00 32.81  ?  285 LEU B N     1 
ATOM   4638 C  CA    . LEU B 1 285 ? 2.747   -9.058  -21.282 1.00 31.67  ?  285 LEU B CA    1 
ATOM   4639 C  C     . LEU B 1 285 ? 3.969   -9.941  -21.470 1.00 36.74  ?  285 LEU B C     1 
ATOM   4640 O  O     . LEU B 1 285 ? 4.337   -10.217 -22.617 1.00 43.37  ?  285 LEU B O     1 
ATOM   4641 C  CB    . LEU B 1 285 ? 3.011   -7.699  -21.936 1.00 18.75  ?  285 LEU B CB    1 
ATOM   4642 C  CG    . LEU B 1 285 ? 1.726   -7.001  -22.349 1.00 23.21  ?  285 LEU B CG    1 
ATOM   4643 C  CD1   . LEU B 1 285 ? 1.954   -5.500  -22.519 1.00 19.78  ?  285 LEU B CD1   1 
ATOM   4644 C  CD2   . LEU B 1 285 ? 1.175   -7.628  -23.606 1.00 17.61  ?  285 LEU B CD2   1 
ATOM   4645 N  N     . GLY B 1 286 ? 4.620   -10.383 -20.397 1.00 36.26  ?  286 GLY B N     1 
ATOM   4646 C  CA    . GLY B 1 286 ? 5.811   -11.190 -20.593 1.00 49.15  ?  286 GLY B CA    1 
ATOM   4647 C  C     . GLY B 1 286 ? 6.075   -12.240 -19.536 1.00 55.34  ?  286 GLY B C     1 
ATOM   4648 O  O     . GLY B 1 286 ? 5.177   -12.584 -18.757 1.00 49.08  ?  286 GLY B O     1 
ATOM   4649 N  N     . ASP B 1 287 ? 7.311   -12.793 -19.555 1.00 67.57  ?  287 ASP B N     1 
ATOM   4650 C  CA    . ASP B 1 287 ? 7.956   -13.559 -18.485 1.00 59.50  ?  287 ASP B CA    1 
ATOM   4651 C  C     . ASP B 1 287 ? 7.003   -14.649 -17.971 1.00 62.55  ?  287 ASP B C     1 
ATOM   4652 O  O     . ASP B 1 287 ? 6.288   -15.228 -18.801 1.00 66.96  ?  287 ASP B O     1 
ATOM   4653 C  CB    . ASP B 1 287 ? 8.441   -12.551 -17.434 1.00 65.23  ?  287 ASP B CB    1 
ATOM   4654 C  CG    . ASP B 1 287 ? 9.042   -11.283 -18.066 1.00 61.25  ?  287 ASP B CG    1 
ATOM   4655 O  OD1   . ASP B 1 287 ? 9.657   -11.376 -19.158 1.00 47.55  ?  287 ASP B OD1   1 
ATOM   4656 O  OD2   . ASP B 1 287 ? 8.903   -10.195 -17.458 1.00 54.39  ?  287 ASP B OD2   1 
ATOM   4657 N  N     . PRO B 1 288 ? 6.952   -15.013 -16.681 1.00 67.45  ?  288 PRO B N     1 
ATOM   4658 C  CA    . PRO B 1 288 ? 5.778   -15.781 -16.226 1.00 62.46  ?  288 PRO B CA    1 
ATOM   4659 C  C     . PRO B 1 288 ? 4.515   -14.938 -16.332 1.00 55.84  ?  288 PRO B C     1 
ATOM   4660 O  O     . PRO B 1 288 ? 4.382   -13.915 -15.658 1.00 57.77  ?  288 PRO B O     1 
ATOM   4661 C  CB    . PRO B 1 288 ? 6.112   -16.129 -14.767 1.00 56.66  ?  288 PRO B CB    1 
ATOM   4662 C  CG    . PRO B 1 288 ? 7.195   -15.188 -14.381 1.00 63.77  ?  288 PRO B CG    1 
ATOM   4663 C  CD    . PRO B 1 288 ? 8.001   -15.070 -15.644 1.00 66.99  ?  288 PRO B CD    1 
ATOM   4664 N  N     . GLN B 1 289 ? 3.600   -15.364 -17.191 1.00 49.89  ?  289 GLN B N     1 
ATOM   4665 C  CA    . GLN B 1 289 ? 2.324   -14.681 -17.346 1.00 51.18  ?  289 GLN B CA    1 
ATOM   4666 C  C     . GLN B 1 289 ? 1.504   -14.846 -16.074 1.00 56.78  ?  289 GLN B C     1 
ATOM   4667 O  O     . GLN B 1 289 ? 1.117   -15.977 -15.748 1.00 57.35  ?  289 GLN B O     1 
ATOM   4668 C  CB    . GLN B 1 289 ? 1.562   -15.240 -18.544 1.00 49.33  ?  289 GLN B CB    1 
ATOM   4669 C  CG    . GLN B 1 289 ? 0.149   -14.688 -18.684 1.00 50.64  ?  289 GLN B CG    1 
ATOM   4670 C  CD    . GLN B 1 289 ? -0.602  -15.306 -19.849 1.00 53.79  ?  289 GLN B CD    1 
ATOM   4671 O  OE1   . GLN B 1 289 ? -0.059  -16.129 -20.588 1.00 51.30  ?  289 GLN B OE1   1 
ATOM   4672 N  NE2   . GLN B 1 289 ? -1.857  -14.909 -20.022 1.00 54.32  ?  289 GLN B NE2   1 
ATOM   4673 N  N     . PRO B 1 290 ? 1.218   -13.780 -15.330 1.00 52.25  ?  290 PRO B N     1 
ATOM   4674 C  CA    . PRO B 1 290 ? 0.440   -13.942 -14.102 1.00 51.94  ?  290 PRO B CA    1 
ATOM   4675 C  C     . PRO B 1 290 ? -0.963  -14.437 -14.416 1.00 56.52  ?  290 PRO B C     1 
ATOM   4676 O  O     . PRO B 1 290 ? -1.432  -14.386 -15.557 1.00 51.34  ?  290 PRO B O     1 
ATOM   4677 C  CB    . PRO B 1 290 ? 0.423   -12.530 -13.502 1.00 53.20  ?  290 PRO B CB    1 
ATOM   4678 C  CG    . PRO B 1 290 ? 0.547   -11.639 -14.692 1.00 50.84  ?  290 PRO B CG    1 
ATOM   4679 C  CD    . PRO B 1 290 ? 1.499   -12.362 -15.616 1.00 47.81  ?  290 PRO B CD    1 
ATOM   4680 N  N     . SER B 1 291 ? -1.627  -14.948 -13.382 1.00 56.16  ?  291 SER B N     1 
ATOM   4681 C  CA    . SER B 1 291 ? -2.989  -15.416 -13.550 1.00 53.70  ?  291 SER B CA    1 
ATOM   4682 C  C     . SER B 1 291 ? -3.911  -14.226 -13.801 1.00 52.06  ?  291 SER B C     1 
ATOM   4683 O  O     . SER B 1 291 ? -3.674  -13.130 -13.284 1.00 49.26  ?  291 SER B O     1 
ATOM   4684 C  CB    . SER B 1 291 ? -3.460  -16.187 -12.314 1.00 58.10  ?  291 SER B CB    1 
ATOM   4685 O  OG    . SER B 1 291 ? -3.257  -15.459 -11.104 1.00 53.19  ?  291 SER B OG    1 
ATOM   4686 N  N     . PRO B 1 292 ? -4.960  -14.411 -14.614 1.00 52.57  ?  292 PRO B N     1 
ATOM   4687 C  CA    . PRO B 1 292 ? -5.987  -13.366 -14.755 1.00 48.45  ?  292 PRO B CA    1 
ATOM   4688 C  C     . PRO B 1 292 ? -6.476  -12.819 -13.420 1.00 52.52  ?  292 PRO B C     1 
ATOM   4689 O  O     . PRO B 1 292 ? -6.958  -11.683 -13.344 1.00 49.09  ?  292 PRO B O     1 
ATOM   4690 C  CB    . PRO B 1 292 ? -7.117  -14.079 -15.514 1.00 49.43  ?  292 PRO B CB    1 
ATOM   4691 C  CG    . PRO B 1 292 ? -6.512  -15.382 -16.057 1.00 53.71  ?  292 PRO B CG    1 
ATOM   4692 C  CD    . PRO B 1 292 ? -5.062  -15.436 -15.666 1.00 55.62  ?  292 PRO B CD    1 
ATOM   4693 N  N     . ALA B 1 293 ? -6.352  -13.619 -12.357 1.00 54.04  ?  293 ALA B N     1 
ATOM   4694 C  CA    . ALA B 1 293 ? -6.771  -13.178 -11.034 1.00 49.50  ?  293 ALA B CA    1 
ATOM   4695 C  C     . ALA B 1 293 ? -5.717  -12.315 -10.353 1.00 49.92  ?  293 ALA B C     1 
ATOM   4696 O  O     . ALA B 1 293 ? -6.071  -11.405 -9.596  1.00 48.50  ?  293 ALA B O     1 
ATOM   4697 C  CB    . ALA B 1 293 ? -7.104  -14.387 -10.158 1.00 53.93  ?  293 ALA B CB    1 
ATOM   4698 N  N     . GLN B 1 294 ? -4.430  -12.576 -10.593 1.00 44.03  ?  294 GLN B N     1 
ATOM   4699 C  CA    . GLN B 1 294 ? -3.400  -11.762 -9.953  1.00 50.28  ?  294 GLN B CA    1 
ATOM   4700 C  C     . GLN B 1 294 ? -3.324  -10.369 -10.569 1.00 52.35  ?  294 GLN B C     1 
ATOM   4701 O  O     . GLN B 1 294 ? -2.963  -9.399  -9.885  1.00 44.54  ?  294 GLN B O     1 
ATOM   4702 C  CB    . GLN B 1 294 ? -2.047  -12.460 -10.041 1.00 53.10  ?  294 GLN B CB    1 
ATOM   4703 C  CG    . GLN B 1 294 ? -0.980  -11.879 -9.128  1.00 54.25  ?  294 GLN B CG    1 
ATOM   4704 C  CD    . GLN B 1 294 ? 0.420   -12.110 -9.670  1.00 61.72  ?  294 GLN B CD    1 
ATOM   4705 O  OE1   . GLN B 1 294 ? 0.740   -13.206 -10.138 1.00 60.01  ?  294 GLN B OE1   1 
ATOM   4706 N  NE2   . GLN B 1 294 ? 1.262   -11.077 -9.613  1.00 63.52  ?  294 GLN B NE2   1 
ATOM   4707 N  N     . VAL B 1 295 ? -3.663  -10.250 -11.851 1.00 49.97  ?  295 VAL B N     1 
ATOM   4708 C  CA    . VAL B 1 295 ? -3.701  -8.938  -12.479 1.00 48.09  ?  295 VAL B CA    1 
ATOM   4709 C  C     . VAL B 1 295 ? -4.801  -8.086  -11.850 1.00 46.35  ?  295 VAL B C     1 
ATOM   4710 O  O     . VAL B 1 295 ? -4.605  -6.892  -11.586 1.00 44.78  ?  295 VAL B O     1 
ATOM   4711 C  CB    . VAL B 1 295 ? -3.877  -9.097  -13.998 1.00 47.09  ?  295 VAL B CB    1 
ATOM   4712 C  CG1   . VAL B 1 295 ? -3.768  -7.747  -14.697 1.00 42.16  ?  295 VAL B CG1   1 
ATOM   4713 C  CG2   . VAL B 1 295 ? -2.854  -10.102 -14.545 1.00 41.88  ?  295 VAL B CG2   1 
ATOM   4714 N  N     . GLU B 1 296 ? -5.962  -8.693  -11.573 1.00 50.58  ?  296 GLU B N     1 
ATOM   4715 C  CA    . GLU B 1 296 ? -7.040  -7.992  -10.876 1.00 44.51  ?  296 GLU B CA    1 
ATOM   4716 C  C     . GLU B 1 296 ? -6.553  -7.397  -9.558  1.00 45.47  ?  296 GLU B C     1 
ATOM   4717 O  O     . GLU B 1 296 ? -6.892  -6.255  -9.219  1.00 45.89  ?  296 GLU B O     1 
ATOM   4718 C  CB    . GLU B 1 296 ? -8.221  -8.947  -10.648 1.00 49.28  ?  296 GLU B CB    1 
ATOM   4719 C  CG    . GLU B 1 296 ? -9.320  -8.430  -9.703  1.00 58.96  ?  296 GLU B CG    1 
ATOM   4720 C  CD    . GLU B 1 296 ? -9.728  -9.446  -8.627  1.00 66.00  ?  296 GLU B CD    1 
ATOM   4721 O  OE1   . GLU B 1 296 ? -10.601 -9.117  -7.785  1.00 59.00  ?  296 GLU B OE1   1 
ATOM   4722 O  OE2   . GLU B 1 296 ? -9.180  -10.575 -8.627  1.00 63.86  ?  296 GLU B OE2   1 
ATOM   4723 N  N     . ASP B 1 297 ? -5.735  -8.146  -8.814  1.00 45.94  ?  297 ASP B N     1 
ATOM   4724 C  CA    . ASP B 1 297 ? -5.192  -7.632  -7.559  1.00 45.28  ?  297 ASP B CA    1 
ATOM   4725 C  C     . ASP B 1 297 ? -4.368  -6.370  -7.788  1.00 47.20  ?  297 ASP B C     1 
ATOM   4726 O  O     . ASP B 1 297 ? -4.538  -5.366  -7.084  1.00 40.76  ?  297 ASP B O     1 
ATOM   4727 C  CB    . ASP B 1 297 ? -4.334  -8.694  -6.863  1.00 46.87  ?  297 ASP B CB    1 
ATOM   4728 C  CG    . ASP B 1 297 ? -4.922  -10.095 -6.957  1.00 61.79  ?  297 ASP B CG    1 
ATOM   4729 O  OD1   . ASP B 1 297 ? -6.169  -10.227 -6.977  1.00 68.31  ?  297 ASP B OD1   1 
ATOM   4730 O  OD2   . ASP B 1 297 ? -4.131  -11.068 -6.995  1.00 58.37  ?  297 ASP B OD2   1 
ATOM   4731 N  N     . GLU B 1 298 ? -3.452  -6.407  -8.762  1.00 45.78  ?  298 GLU B N     1 
ATOM   4732 C  CA    . GLU B 1 298 ? -2.552  -5.274  -8.940  1.00 43.74  ?  298 GLU B CA    1 
ATOM   4733 C  C     . GLU B 1 298 ? -3.272  -4.071  -9.534  1.00 39.41  ?  298 GLU B C     1 
ATOM   4734 O  O     . GLU B 1 298 ? -2.907  -2.929  -9.234  1.00 34.71  ?  298 GLU B O     1 
ATOM   4735 C  CB    . GLU B 1 298 ? -1.360  -5.676  -9.805  1.00 48.14  ?  298 GLU B CB    1 
ATOM   4736 C  CG    . GLU B 1 298 ? -0.278  -6.427  -9.047  1.00 47.21  ?  298 GLU B CG    1 
ATOM   4737 C  CD    . GLU B 1 298 ? 0.545   -7.322  -9.959  1.00 56.48  ?  298 GLU B CD    1 
ATOM   4738 O  OE1   . GLU B 1 298 ? 1.020   -6.824  -11.006 1.00 51.57  ?  298 GLU B OE1   1 
ATOM   4739 O  OE2   . GLU B 1 298 ? 0.714   -8.521  -9.633  1.00 55.77  ?  298 GLU B OE2   1 
ATOM   4740 N  N     . LEU B 1 299 ? -4.289  -4.303  -10.371 1.00 40.22  ?  299 LEU B N     1 
ATOM   4741 C  CA    . LEU B 1 299 ? -5.107  -3.203  -10.878 1.00 36.11  ?  299 LEU B CA    1 
ATOM   4742 C  C     . LEU B 1 299 ? -5.798  -2.478  -9.733  1.00 44.82  ?  299 LEU B C     1 
ATOM   4743 O  O     . LEU B 1 299 ? -5.827  -1.241  -9.690  1.00 46.66  ?  299 LEU B O     1 
ATOM   4744 C  CB    . LEU B 1 299 ? -6.142  -3.726  -11.874 1.00 31.57  ?  299 LEU B CB    1 
ATOM   4745 C  CG    . LEU B 1 299 ? -5.682  -4.175  -13.259 1.00 40.80  ?  299 LEU B CG    1 
ATOM   4746 C  CD1   . LEU B 1 299 ? -6.894  -4.392  -14.154 1.00 39.55  ?  299 LEU B CD1   1 
ATOM   4747 C  CD2   . LEU B 1 299 ? -4.716  -3.179  -13.891 1.00 32.13  ?  299 LEU B CD2   1 
ATOM   4748 N  N     . ARG B 1 300 ? -6.372  -3.244  -8.799  1.00 38.64  ?  300 ARG B N     1 
ATOM   4749 C  CA    . ARG B 1 300 ? -6.911  -2.672  -7.574  1.00 42.43  ?  300 ARG B CA    1 
ATOM   4750 C  C     . ARG B 1 300 ? -5.886  -1.779  -6.890  1.00 41.33  ?  300 ARG B C     1 
ATOM   4751 O  O     . ARG B 1 300 ? -6.173  -0.621  -6.567  1.00 42.67  ?  300 ARG B O     1 
ATOM   4752 C  CB    . ARG B 1 300 ? -7.356  -3.794  -6.629  1.00 47.67  ?  300 ARG B CB    1 
ATOM   4753 C  CG    . ARG B 1 300 ? -8.735  -4.360  -6.919  1.00 48.94  ?  300 ARG B CG    1 
ATOM   4754 C  CD    . ARG B 1 300 ? -8.812  -5.838  -6.555  1.00 54.40  ?  300 ARG B CD    1 
ATOM   4755 N  NE    . ARG B 1 300 ? -9.115  -6.057  -5.145  1.00 57.96  ?  300 ARG B NE    1 
ATOM   4756 C  CZ    . ARG B 1 300 ? -8.204  -6.263  -4.201  1.00 60.22  ?  300 ARG B CZ    1 
ATOM   4757 N  NH1   . ARG B 1 300 ? -6.909  -6.268  -4.478  1.00 53.54  ?  300 ARG B NH1   1 
ATOM   4758 N  NH2   . ARG B 1 300 ? -8.603  -6.483  -2.951  1.00 55.10  ?  300 ARG B NH2   1 
ATOM   4759 N  N     . ALA B 1 301 ? -4.675  -2.301  -6.665  1.00 38.10  ?  301 ALA B N     1 
ATOM   4760 C  CA    . ALA B 1 301 ? -3.649  -1.511  -5.990  1.00 40.88  ?  301 ALA B CA    1 
ATOM   4761 C  C     . ALA B 1 301 ? -3.273  -0.282  -6.809  1.00 50.71  ?  301 ALA B C     1 
ATOM   4762 O  O     . ALA B 1 301 ? -3.039  0.801   -6.253  1.00 49.77  ?  301 ALA B O     1 
ATOM   4763 C  CB    . ALA B 1 301 ? -2.418  -2.371  -5.711  1.00 40.72  ?  301 ALA B CB    1 
ATOM   4764 N  N     . ALA B 1 302 ? -3.209  -0.429  -8.136  1.00 49.75  ?  302 ALA B N     1 
ATOM   4765 C  CA    . ALA B 1 302 ? -2.890  0.714   -8.985  1.00 45.16  ?  302 ALA B CA    1 
ATOM   4766 C  C     . ALA B 1 302 ? -3.890  1.844   -8.774  1.00 46.77  ?  302 ALA B C     1 
ATOM   4767 O  O     . ALA B 1 302 ? -3.502  3.015   -8.668  1.00 48.51  ?  302 ALA B O     1 
ATOM   4768 C  CB    . ALA B 1 302 ? -2.855  0.286   -10.456 1.00 35.89  ?  302 ALA B CB    1 
ATOM   4769 N  N     . LEU B 1 303 ? -5.181  1.509   -8.665  1.00 38.00  ?  303 LEU B N     1 
ATOM   4770 C  CA    . LEU B 1 303 ? -6.209  2.545   -8.628  1.00 45.05  ?  303 LEU B CA    1 
ATOM   4771 C  C     . LEU B 1 303 ? -6.375  3.138   -7.234  1.00 43.18  ?  303 LEU B C     1 
ATOM   4772 O  O     . LEU B 1 303 ? -6.622  4.342   -7.104  1.00 42.92  ?  303 LEU B O     1 
ATOM   4773 C  CB    . LEU B 1 303 ? -7.540  1.984   -9.143  1.00 38.75  ?  303 LEU B CB    1 
ATOM   4774 C  CG    . LEU B 1 303 ? -7.748  2.144   -10.658 1.00 36.42  ?  303 LEU B CG    1 
ATOM   4775 C  CD1   . LEU B 1 303 ? -6.661  1.406   -11.458 1.00 34.92  ?  303 LEU B CD1   1 
ATOM   4776 C  CD2   . LEU B 1 303 ? -9.142  1.710   -11.121 1.00 27.93  ?  303 LEU B CD2   1 
ATOM   4777 N  N     . GLU B 1 304 ? -6.220  2.324   -6.191  1.00 46.44  ?  304 GLU B N     1 
ATOM   4778 C  CA    . GLU B 1 304 ? -6.269  2.806   -4.816  1.00 52.63  ?  304 GLU B CA    1 
ATOM   4779 C  C     . GLU B 1 304 ? -4.995  3.565   -4.459  1.00 58.94  ?  304 GLU B C     1 
ATOM   4780 O  O     . GLU B 1 304 ? -4.892  4.777   -4.689  1.00 57.94  ?  304 GLU B O     1 
ATOM   4781 C  CB    . GLU B 1 304 ? -6.487  1.633   -3.856  1.00 49.39  ?  304 GLU B CB    1 
ATOM   4782 C  CG    . GLU B 1 304 ? -7.948  1.381   -3.529  1.00 50.33  ?  304 GLU B CG    1 
ATOM   4783 C  CD    . GLU B 1 304 ? -8.347  -0.072  -3.683  1.00 52.75  ?  304 GLU B CD    1 
ATOM   4784 O  OE1   . GLU B 1 304 ? -7.520  -0.956  -3.377  1.00 56.11  ?  304 GLU B OE1   1 
ATOM   4785 O  OE2   . GLU B 1 304 ? -9.493  -0.333  -4.112  1.00 54.27  ?  304 GLU B OE2   1 
ATOM   4786 N  N     . GLY B 1 305 ? -4.027  2.854   -3.883  1.00 63.24  ?  305 GLY B N     1 
ATOM   4787 C  CA    . GLY B 1 305 ? -2.737  3.416   -3.522  1.00 68.57  ?  305 GLY B CA    1 
ATOM   4788 C  C     . GLY B 1 305 ? -1.717  2.301   -3.495  1.00 67.97  ?  305 GLY B C     1 
ATOM   4789 O  O     . GLY B 1 305 ? -2.063  1.122   -3.578  1.00 67.70  ?  305 GLY B O     1 
ATOM   4790 N  N     . ARG B 1 306 ? -0.448  2.692   -3.365  1.00 72.65  ?  306 ARG B N     1 
ATOM   4791 C  CA    . ARG B 1 306 ? 0.692   1.782   -3.542  1.00 71.16  ?  306 ARG B CA    1 
ATOM   4792 C  C     . ARG B 1 306 ? 0.594   1.140   -4.926  1.00 67.53  ?  306 ARG B C     1 
ATOM   4793 O  O     . ARG B 1 306 ? -0.097  1.654   -5.813  1.00 64.54  ?  306 ARG B O     1 
ATOM   4794 C  CB    . ARG B 1 306 ? 0.767   0.719   -2.410  1.00 69.62  ?  306 ARG B CB    1 
ATOM   4795 C  CG    . ARG B 1 306 ? 0.082   -0.659  -2.641  1.00 66.03  ?  306 ARG B CG    1 
ATOM   4796 C  CD    . ARG B 1 306 ? 0.912   -1.647  -3.468  1.00 63.41  ?  306 ARG B CD    1 
ATOM   4797 N  NE    . ARG B 1 306 ? 0.261   -2.947  -3.606  1.00 65.44  ?  306 ARG B NE    1 
ATOM   4798 C  CZ    . ARG B 1 306 ? 0.502   -3.803  -4.591  1.00 60.79  ?  306 ARG B CZ    1 
ATOM   4799 N  NH1   . ARG B 1 306 ? 1.333   -3.507  -5.576  1.00 53.74  ?  306 ARG B NH1   1 
ATOM   4800 N  NH2   . ARG B 1 306 ? -0.126  -4.978  -4.600  1.00 59.30  ?  306 ARG B NH2   1 
HETATM 4801 N  N1    . UDP C 2 .   ? 30.931  0.998   12.557  1.00 21.46  ?  401 UDP A N1    1 
HETATM 4802 C  C2    . UDP C 2 .   ? 31.646  1.122   13.739  1.00 18.11  ?  401 UDP A C2    1 
HETATM 4803 N  N3    . UDP C 2 .   ? 32.675  0.226   13.885  1.00 25.80  ?  401 UDP A N3    1 
HETATM 4804 C  C4    . UDP C 2 .   ? 33.054  -0.761  12.993  1.00 24.28  ?  401 UDP A C4    1 
HETATM 4805 C  C5    . UDP C 2 .   ? 32.266  -0.828  11.795  1.00 20.03  ?  401 UDP A C5    1 
HETATM 4806 C  C6    . UDP C 2 .   ? 31.255  0.039   11.620  1.00 22.49  ?  401 UDP A C6    1 
HETATM 4807 O  O2    . UDP C 2 .   ? 31.397  1.960   14.587  1.00 22.51  ?  401 UDP A O2    1 
HETATM 4808 O  O4    . UDP C 2 .   ? 34.000  -1.498  13.275  1.00 27.91  ?  401 UDP A O4    1 
HETATM 4809 C  "C1'" . UDP C 2 .   ? 29.805  1.923   12.311  1.00 20.28  ?  401 UDP A "C1'" 1 
HETATM 4810 C  "C2'" . UDP C 2 .   ? 29.753  2.508   10.901  1.00 20.82  ?  401 UDP A "C2'" 1 
HETATM 4811 O  "O2'" . UDP C 2 .   ? 30.618  3.613   10.732  1.00 21.15  ?  401 UDP A "O2'" 1 
HETATM 4812 C  "C3'" . UDP C 2 .   ? 28.265  2.870   10.790  1.00 21.41  ?  401 UDP A "C3'" 1 
HETATM 4813 C  "C4'" . UDP C 2 .   ? 27.595  1.717   11.548  1.00 15.38  ?  401 UDP A "C4'" 1 
HETATM 4814 O  "O4'" . UDP C 2 .   ? 28.608  1.185   12.434  1.00 14.00  ?  401 UDP A "O4'" 1 
HETATM 4815 O  "O3'" . UDP C 2 .   ? 28.001  4.111   11.434  1.00 21.47  ?  401 UDP A "O3'" 1 
HETATM 4816 C  "C5'" . UDP C 2 .   ? 27.083  0.602   10.674  1.00 17.21  ?  401 UDP A "C5'" 1 
HETATM 4817 O  "O5'" . UDP C 2 .   ? 28.197  0.030   9.929   1.00 26.18  ?  401 UDP A "O5'" 1 
HETATM 4818 P  PA    . UDP C 2 .   ? 27.899  -0.325  8.400   1.00 23.33  ?  401 UDP A PA    1 
HETATM 4819 O  O1A   . UDP C 2 .   ? 29.077  -0.971  7.759   1.00 31.48  -1 401 UDP A O1A   1 
HETATM 4820 O  O2A   . UDP C 2 .   ? 27.301  0.866   7.742   1.00 22.60  ?  401 UDP A O2A   1 
HETATM 4821 O  O3A   . UDP C 2 .   ? 26.753  -1.396  8.674   1.00 20.72  ?  401 UDP A O3A   1 
HETATM 4822 P  PB    . UDP C 2 .   ? 25.622  -2.081  7.747   1.00 44.25  ?  401 UDP A PB    1 
HETATM 4823 O  O1B   . UDP C 2 .   ? 24.742  -2.767  8.783   1.00 39.77  ?  401 UDP A O1B   1 
HETATM 4824 O  O2B   . UDP C 2 .   ? 26.340  -3.054  6.818   1.00 46.72  -1 401 UDP A O2B   1 
HETATM 4825 O  O3B   . UDP C 2 .   ? 24.961  -0.917  7.016   1.00 24.36  -1 401 UDP A O3B   1 
HETATM 4826 MG MG    . MG  D 3 .   ? 25.518  1.259   6.380   1.00 11.25  ?  402 MG  A MG    1 
HETATM 4827 N  N1    . UDP E 2 .   ? -4.440  22.039  -27.210 1.00 19.56  ?  401 UDP B N1    1 
HETATM 4828 C  C2    . UDP E 2 .   ? -4.898  22.666  -28.361 1.00 19.06  ?  401 UDP B C2    1 
HETATM 4829 N  N3    . UDP E 2 .   ? -6.263  22.793  -28.442 1.00 20.40  ?  401 UDP B N3    1 
HETATM 4830 C  C4    . UDP E 2 .   ? -7.194  22.362  -27.515 1.00 16.18  ?  401 UDP B C4    1 
HETATM 4831 C  C5    . UDP E 2 .   ? -6.643  21.717  -26.356 1.00 14.98  ?  401 UDP B C5    1 
HETATM 4832 C  C6    . UDP E 2 .   ? -5.311  21.582  -26.244 1.00 18.46  ?  401 UDP B C6    1 
HETATM 4833 O  O2    . UDP E 2 .   ? -4.160  23.084  -29.236 1.00 20.01  ?  401 UDP B O2    1 
HETATM 4834 O  O4    . UDP E 2 .   ? -8.390  22.542  -27.742 1.00 17.86  ?  401 UDP B O4    1 
HETATM 4835 C  "C1'" . UDP E 2 .   ? -2.981  21.839  -27.068 1.00 21.71  ?  401 UDP B "C1'" 1 
HETATM 4836 C  "C2'" . UDP E 2 .   ? -2.354  22.306  -25.759 1.00 22.62  ?  401 UDP B "C2'" 1 
HETATM 4837 O  "O2'" . UDP E 2 .   ? -2.005  23.672  -25.899 1.00 21.51  ?  401 UDP B "O2'" 1 
HETATM 4838 C  "C3'" . UDP E 2 .   ? -1.136  21.377  -25.659 1.00 19.57  ?  401 UDP B "C3'" 1 
HETATM 4839 C  "C4'" . UDP E 2 .   ? -1.650  20.072  -26.281 1.00 21.54  ?  401 UDP B "C4'" 1 
HETATM 4840 O  "O4'" . UDP E 2 .   ? -2.713  20.455  -27.185 1.00 18.60  ?  401 UDP B "O4'" 1 
HETATM 4841 O  "O3'" . UDP E 2 .   ? -0.062  21.882  -26.447 1.00 21.06  ?  401 UDP B "O3'" 1 
HETATM 4842 C  "C5'" . UDP E 2 .   ? -2.141  19.031  -25.301 1.00 24.66  ?  401 UDP B "C5'" 1 
HETATM 4843 O  "O5'" . UDP E 2 .   ? -3.201  19.579  -24.487 1.00 21.35  ?  401 UDP B "O5'" 1 
HETATM 4844 P  PA    . UDP E 2 .   ? -3.207  19.172  -22.940 1.00 18.62  ?  401 UDP B PA    1 
HETATM 4845 O  O1A   . UDP E 2 .   ? -1.916  19.505  -22.284 1.00 19.66  ?  401 UDP B O1A   1 
HETATM 4846 O  O2A   . UDP E 2 .   ? -4.429  19.736  -22.310 1.00 21.72  -1 401 UDP B O2A   1 
HETATM 4847 O  O3A   . UDP E 2 .   ? -3.284  17.577  -23.021 1.00 29.92  ?  401 UDP B O3A   1 
HETATM 4848 P  PB    . UDP E 2 .   ? -3.070  16.446  -21.878 1.00 46.28  ?  401 UDP B PB    1 
HETATM 4849 O  O1B   . UDP E 2 .   ? -1.649  16.617  -21.345 1.00 22.61  -1 401 UDP B O1B   1 
HETATM 4850 O  O2B   . UDP E 2 .   ? -3.335  15.150  -22.627 1.00 38.94  ?  401 UDP B O2B   1 
HETATM 4851 O  O3B   . UDP E 2 .   ? -4.098  16.750  -20.798 1.00 41.83  -1 401 UDP B O3B   1 
HETATM 4852 MG MG    . MG  F 3 .   ? -0.293  18.583  -21.011 1.00 11.56  ?  402 MG  B MG    1 
HETATM 4853 O  O     . HOH G 4 .   ? 6.963   -6.291  20.164  1.00 27.92  ?  501 HOH A O     1 
HETATM 4854 O  O     . HOH G 4 .   ? 23.812  -4.558  9.729   1.00 21.05  ?  502 HOH A O     1 
HETATM 4855 O  O     . HOH G 4 .   ? 6.461   18.453  24.286  1.00 31.91  ?  503 HOH A O     1 
HETATM 4856 O  O     . HOH G 4 .   ? 13.512  -25.189 7.917   1.00 35.04  ?  504 HOH A O     1 
HETATM 4857 O  O     . HOH G 4 .   ? 31.332  -4.423  19.142  1.00 26.16  ?  505 HOH A O     1 
HETATM 4858 O  O     . HOH G 4 .   ? 21.872  20.605  3.500   1.00 29.53  ?  506 HOH A O     1 
HETATM 4859 O  O     . HOH G 4 .   ? 23.624  3.686   14.498  1.00 19.39  ?  507 HOH A O     1 
HETATM 4860 O  O     . HOH G 4 .   ? 18.351  -9.044  -9.407  1.00 47.13  ?  508 HOH A O     1 
HETATM 4861 O  O     . HOH G 4 .   ? 33.594  -19.822 2.183   1.00 41.14  ?  509 HOH A O     1 
HETATM 4862 O  O     . HOH G 4 .   ? -4.144  -15.294 9.133   1.00 44.22  ?  510 HOH A O     1 
HETATM 4863 O  O     . HOH G 4 .   ? 12.117  -20.337 19.894  1.00 30.14  ?  511 HOH A O     1 
HETATM 4864 O  O     . HOH G 4 .   ? 28.884  3.297   3.234   1.00 34.81  ?  512 HOH A O     1 
HETATM 4865 O  O     . HOH G 4 .   ? 5.150   -12.858 16.829  1.00 22.98  ?  513 HOH A O     1 
HETATM 4866 O  O     . HOH G 4 .   ? 10.396  -0.111  7.686   1.00 24.65  ?  514 HOH A O     1 
HETATM 4867 O  O     . HOH G 4 .   ? 19.940  17.638  24.426  1.00 19.37  ?  515 HOH A O     1 
HETATM 4868 O  O     . HOH G 4 .   ? 27.284  0.629   -8.793  1.00 37.89  ?  516 HOH A O     1 
HETATM 4869 O  O     . HOH G 4 .   ? 26.550  -12.873 22.236  1.00 29.11  ?  517 HOH A O     1 
HETATM 4870 O  O     . HOH G 4 .   ? 14.679  14.470  1.701   1.00 22.30  ?  518 HOH A O     1 
HETATM 4871 O  O     . HOH G 4 .   ? 14.895  16.255  -4.520  1.00 33.13  ?  519 HOH A O     1 
HETATM 4872 O  O     . HOH G 4 .   ? 1.775   4.189   13.999  1.00 31.96  ?  520 HOH A O     1 
HETATM 4873 O  O     . HOH G 4 .   ? 31.910  0.790   24.135  1.00 25.38  ?  521 HOH A O     1 
HETATM 4874 O  O     . HOH G 4 .   ? 16.610  -0.003  -3.787  1.00 26.73  ?  522 HOH A O     1 
HETATM 4875 O  O     . HOH G 4 .   ? 24.712  -3.838  3.844   1.00 42.95  ?  523 HOH A O     1 
HETATM 4876 O  O     . HOH G 4 .   ? 5.347   3.681   0.419   1.00 46.14  ?  524 HOH A O     1 
HETATM 4877 O  O     . HOH G 4 .   ? 13.690  25.359  23.671  1.00 42.35  ?  525 HOH A O     1 
HETATM 4878 O  O     . HOH G 4 .   ? 38.264  11.769  15.984  1.00 30.80  ?  526 HOH A O     1 
HETATM 4879 O  O     . HOH G 4 .   ? 8.140   -26.382 -3.299  1.00 37.74  ?  527 HOH A O     1 
HETATM 4880 O  O     . HOH G 4 .   ? 8.995   -14.540 23.305  1.00 18.52  ?  528 HOH A O     1 
HETATM 4881 O  O     . HOH G 4 .   ? 17.103  16.890  -7.249  1.00 40.71  ?  529 HOH A O     1 
HETATM 4882 O  O     . HOH G 4 .   ? 37.971  13.153  22.149  1.00 32.52  ?  530 HOH A O     1 
HETATM 4883 O  O     . HOH G 4 .   ? 19.450  8.940   27.480  1.00 24.68  ?  531 HOH A O     1 
HETATM 4884 O  O     . HOH G 4 .   ? 8.276   18.581  10.349  1.00 40.08  ?  532 HOH A O     1 
HETATM 4885 O  O     . HOH G 4 .   ? 20.311  -23.568 7.016   1.00 36.84  ?  533 HOH A O     1 
HETATM 4886 O  O     . HOH G 4 .   ? 13.672  14.291  -1.367  1.00 27.86  ?  534 HOH A O     1 
HETATM 4887 O  O     . HOH G 4 .   ? 21.227  -3.437  9.926   1.00 20.79  ?  535 HOH A O     1 
HETATM 4888 O  O     . HOH G 4 .   ? 25.829  13.650  26.495  1.00 24.85  ?  536 HOH A O     1 
HETATM 4889 O  O     . HOH G 4 .   ? 7.086   -5.487  23.372  1.00 19.55  ?  537 HOH A O     1 
HETATM 4890 O  O     . HOH G 4 .   ? 27.853  -11.769 7.880   1.00 32.54  ?  538 HOH A O     1 
HETATM 4891 O  O     . HOH G 4 .   ? 22.676  15.190  4.488   1.00 17.82  ?  539 HOH A O     1 
HETATM 4892 O  O     . HOH G 4 .   ? 23.624  1.475   8.072   1.00 17.25  ?  540 HOH A O     1 
HETATM 4893 O  O     . HOH G 4 .   ? 8.623   -9.690  27.070  1.00 35.90  ?  541 HOH A O     1 
HETATM 4894 O  O     . HOH G 4 .   ? 2.769   12.747  26.289  1.00 15.22  ?  542 HOH A O     1 
HETATM 4895 O  O     . HOH G 4 .   ? 24.985  -13.281 -5.208  1.00 37.85  ?  543 HOH A O     1 
HETATM 4896 O  O     . HOH G 4 .   ? 4.554   2.745   4.079   1.00 25.77  ?  544 HOH A O     1 
HETATM 4897 O  O     . HOH G 4 .   ? -0.328  7.220   26.790  1.00 29.00  ?  545 HOH A O     1 
HETATM 4898 O  O     . HOH G 4 .   ? 18.286  -10.831 10.807  1.00 20.86  ?  546 HOH A O     1 
HETATM 4899 O  O     . HOH G 4 .   ? 34.709  8.376   9.880   1.00 22.91  ?  547 HOH A O     1 
HETATM 4900 O  O     . HOH G 4 .   ? 2.955   -22.091 5.667   1.00 36.80  ?  548 HOH A O     1 
HETATM 4901 O  O     . HOH G 4 .   ? 25.086  10.559  0.329   1.00 25.55  ?  549 HOH A O     1 
HETATM 4902 O  O     . HOH G 4 .   ? 2.075   0.616   10.009  1.00 21.49  ?  550 HOH A O     1 
HETATM 4903 O  O     . HOH G 4 .   ? 13.300  -7.428  -9.542  1.00 48.88  ?  551 HOH A O     1 
HETATM 4904 O  O     . HOH G 4 .   ? 3.092   -19.726 7.360   1.00 34.10  ?  552 HOH A O     1 
HETATM 4905 O  O     . HOH G 4 .   ? 2.410   -1.168  16.985  1.00 14.99  ?  553 HOH A O     1 
HETATM 4906 O  O     . HOH G 4 .   ? 8.677   -14.410 -4.611  1.00 33.60  ?  554 HOH A O     1 
HETATM 4907 O  O     . HOH G 4 .   ? 32.212  -17.753 8.024   1.00 36.59  ?  555 HOH A O     1 
HETATM 4908 O  O     . HOH G 4 .   ? -0.906  -21.783 -1.001  1.00 42.54  ?  556 HOH A O     1 
HETATM 4909 O  O     . HOH G 4 .   ? 10.170  11.601  5.507   1.00 24.52  ?  557 HOH A O     1 
HETATM 4910 O  O     . HOH G 4 .   ? 18.529  -3.431  32.739  1.00 35.72  ?  558 HOH A O     1 
HETATM 4911 O  O     . HOH G 4 .   ? 21.661  20.635  18.717  1.00 29.61  ?  559 HOH A O     1 
HETATM 4912 O  O     . HOH G 4 .   ? 17.230  16.094  7.258   1.00 9.31   ?  560 HOH A O     1 
HETATM 4913 O  O     . HOH G 4 .   ? -1.699  -10.643 13.269  1.00 39.25  ?  561 HOH A O     1 
HETATM 4914 O  O     . HOH G 4 .   ? -1.274  9.016   23.819  1.00 32.71  ?  562 HOH A O     1 
HETATM 4915 O  O     . HOH G 4 .   ? 13.472  -20.448 17.619  1.00 21.06  ?  563 HOH A O     1 
HETATM 4916 O  O     . HOH G 4 .   ? 21.143  1.907   9.502   1.00 19.15  ?  564 HOH A O     1 
HETATM 4917 O  O     . HOH G 4 .   ? 9.180   -4.478  0.887   1.00 31.50  ?  565 HOH A O     1 
HETATM 4918 O  O     . HOH G 4 .   ? 4.993   -7.350  11.531  1.00 12.76  ?  566 HOH A O     1 
HETATM 4919 O  O     . HOH G 4 .   ? 16.852  7.320   14.080  1.00 13.20  ?  567 HOH A O     1 
HETATM 4920 O  O     . HOH G 4 .   ? 36.862  7.517   11.641  1.00 25.12  ?  568 HOH A O     1 
HETATM 4921 O  O     . HOH G 4 .   ? 23.119  -6.491  20.296  1.00 16.24  ?  569 HOH A O     1 
HETATM 4922 O  O     . HOH G 4 .   ? 41.206  0.875   9.662   1.00 38.48  ?  570 HOH A O     1 
HETATM 4923 O  O     . HOH G 4 .   ? 6.915   -10.285 19.443  1.00 30.39  ?  571 HOH A O     1 
HETATM 4924 O  O     . HOH G 4 .   ? 13.649  10.639  8.331   1.00 15.86  ?  572 HOH A O     1 
HETATM 4925 O  O     . HOH G 4 .   ? 5.038   -7.693  15.162  1.00 21.64  ?  573 HOH A O     1 
HETATM 4926 O  O     . HOH G 4 .   ? 26.956  29.163  13.607  1.00 39.06  ?  574 HOH A O     1 
HETATM 4927 O  O     . HOH G 4 .   ? 34.534  -3.733  11.749  1.00 31.21  ?  575 HOH A O     1 
HETATM 4928 O  O     . HOH G 4 .   ? 8.339   -19.426 20.510  1.00 23.21  ?  576 HOH A O     1 
HETATM 4929 O  O     . HOH G 4 .   ? 19.293  -22.497 -4.541  1.00 27.73  ?  577 HOH A O     1 
HETATM 4930 O  O     . HOH G 4 .   ? 2.924   -11.930 21.136  1.00 30.62  ?  578 HOH A O     1 
HETATM 4931 O  O     . HOH G 4 .   ? 25.534  9.392   5.294   1.00 17.13  ?  579 HOH A O     1 
HETATM 4932 O  O     . HOH G 4 .   ? 25.231  -26.353 -0.214  1.00 28.81  ?  580 HOH A O     1 
HETATM 4933 O  O     . HOH G 4 .   ? 12.162  16.441  12.514  1.00 15.17  ?  581 HOH A O     1 
HETATM 4934 O  O     . HOH G 4 .   ? 16.911  -24.938 0.734   1.00 21.21  ?  582 HOH A O     1 
HETATM 4935 O  O     . HOH G 4 .   ? 12.050  -13.435 23.197  1.00 22.63  ?  583 HOH A O     1 
HETATM 4936 O  O     . HOH G 4 .   ? 25.317  -5.463  8.329   1.00 33.69  ?  584 HOH A O     1 
HETATM 4937 O  O     . HOH G 4 .   ? 23.182  -25.651 0.453   1.00 22.64  ?  585 HOH A O     1 
HETATM 4938 O  O     . HOH G 4 .   ? 29.826  -4.780  17.068  1.00 20.14  ?  586 HOH A O     1 
HETATM 4939 O  O     . HOH G 4 .   ? 17.556  23.604  10.111  1.00 32.02  ?  587 HOH A O     1 
HETATM 4940 O  O     . HOH G 4 .   ? 36.354  14.842  21.426  1.00 38.36  ?  588 HOH A O     1 
HETATM 4941 O  O     . HOH G 4 .   ? 13.996  8.264   28.879  1.00 13.42  ?  589 HOH A O     1 
HETATM 4942 O  O     . HOH G 4 .   ? 5.249   -3.573  21.385  1.00 22.14  ?  590 HOH A O     1 
HETATM 4943 O  O     . HOH G 4 .   ? 20.723  17.373  4.879   1.00 22.12  ?  591 HOH A O     1 
HETATM 4944 O  O     . HOH G 4 .   ? 6.929   -1.528  0.506   1.00 36.73  ?  592 HOH A O     1 
HETATM 4945 O  O     . HOH G 4 .   ? -1.637  8.829   7.041   1.00 38.07  ?  593 HOH A O     1 
HETATM 4946 O  O     . HOH G 4 .   ? 1.596   -5.595  17.255  1.00 34.26  ?  594 HOH A O     1 
HETATM 4947 O  O     . HOH G 4 .   ? -0.967  -5.631  6.721   1.00 37.28  ?  595 HOH A O     1 
HETATM 4948 O  O     . HOH G 4 .   ? 7.480   -8.256  16.623  1.00 26.09  ?  596 HOH A O     1 
HETATM 4949 O  O     . HOH G 4 .   ? 23.711  -1.083  10.912  1.00 22.42  ?  597 HOH A O     1 
HETATM 4950 O  O     . HOH G 4 .   ? 10.047  -2.545  8.046   1.00 13.06  ?  598 HOH A O     1 
HETATM 4951 O  O     . HOH G 4 .   ? 26.974  29.335  16.283  1.00 63.51  ?  599 HOH A O     1 
HETATM 4952 O  O     . HOH G 4 .   ? 12.224  2.366   28.648  1.00 19.42  ?  600 HOH A O     1 
HETATM 4953 O  O     . HOH G 4 .   ? 34.487  5.368   25.322  1.00 34.72  ?  601 HOH A O     1 
HETATM 4954 O  O     . HOH G 4 .   ? 6.381   16.111  10.732  1.00 34.68  ?  602 HOH A O     1 
HETATM 4955 O  O     . HOH G 4 .   ? 0.466   -17.426 15.739  1.00 29.46  ?  603 HOH A O     1 
HETATM 4956 O  O     . HOH G 4 .   ? 1.443   2.556   11.470  1.00 18.14  ?  604 HOH A O     1 
HETATM 4957 O  O     . HOH G 4 .   ? 30.811  -3.074  8.613   1.00 30.84  ?  605 HOH A O     1 
HETATM 4958 O  O     . HOH G 4 .   ? 20.845  5.858   26.383  1.00 23.27  ?  606 HOH A O     1 
HETATM 4959 O  O     . HOH G 4 .   ? 21.710  -17.829 22.247  1.00 26.87  ?  607 HOH A O     1 
HETATM 4960 O  O     . HOH G 4 .   ? 1.411   -2.634  28.271  1.00 28.31  ?  608 HOH A O     1 
HETATM 4961 O  O     . HOH G 4 .   ? 25.565  -23.879 7.620   1.00 33.59  ?  609 HOH A O     1 
HETATM 4962 O  O     . HOH G 4 .   ? 4.413   -16.096 1.317   1.00 31.76  ?  610 HOH A O     1 
HETATM 4963 O  O     . HOH G 4 .   ? 5.668   -1.904  28.531  1.00 19.12  ?  611 HOH A O     1 
HETATM 4964 O  O     . HOH G 4 .   ? 1.965   -1.309  12.321  1.00 16.55  ?  612 HOH A O     1 
HETATM 4965 O  O     . HOH G 4 .   ? 30.973  6.470   26.946  1.00 23.52  ?  613 HOH A O     1 
HETATM 4966 O  O     . HOH G 4 .   ? 7.700   -3.451  3.089   1.00 26.53  ?  614 HOH A O     1 
HETATM 4967 O  O     . HOH G 4 .   ? 7.192   -24.276 9.922   1.00 30.34  ?  615 HOH A O     1 
HETATM 4968 O  O     . HOH G 4 .   ? 30.122  -1.778  25.014  1.00 34.75  ?  616 HOH A O     1 
HETATM 4969 O  O     . HOH G 4 .   ? 33.547  17.029  21.593  1.00 31.07  ?  617 HOH A O     1 
HETATM 4970 O  O     . HOH G 4 .   ? 18.802  8.642   31.697  1.00 26.88  ?  618 HOH A O     1 
HETATM 4971 O  O     . HOH G 4 .   ? 27.283  3.491   1.592   1.00 32.29  ?  619 HOH A O     1 
HETATM 4972 O  O     . HOH G 4 .   ? 7.316   7.528   4.101   1.00 31.84  ?  620 HOH A O     1 
HETATM 4973 O  O     . HOH G 4 .   ? 29.533  -11.565 14.637  1.00 21.25  ?  621 HOH A O     1 
HETATM 4974 O  O     . HOH G 4 .   ? 38.192  0.998   7.046   1.00 34.30  ?  622 HOH A O     1 
HETATM 4975 O  O     . HOH G 4 .   ? 28.660  21.629  20.155  1.00 26.93  ?  623 HOH A O     1 
HETATM 4976 O  O     . HOH G 4 .   ? 30.073  12.712  30.179  1.00 30.88  ?  624 HOH A O     1 
HETATM 4977 O  O     . HOH G 4 .   ? 30.812  -4.975  12.393  1.00 23.16  ?  625 HOH A O     1 
HETATM 4978 O  O     . HOH G 4 .   ? 7.298   13.092  6.716   1.00 32.18  ?  626 HOH A O     1 
HETATM 4979 O  O     . HOH G 4 .   ? 19.320  -6.336  28.774  1.00 35.90  ?  627 HOH A O     1 
HETATM 4980 O  O     . HOH G 4 .   ? 20.748  25.897  15.376  1.00 34.13  ?  628 HOH A O     1 
HETATM 4981 O  O     . HOH G 4 .   ? 23.808  1.599   4.898   1.00 20.42  ?  629 HOH A O     1 
HETATM 4982 O  O     . HOH G 4 .   ? 19.897  -8.434  0.192   1.00 31.24  ?  630 HOH A O     1 
HETATM 4983 O  O     . HOH G 4 .   ? 3.621   0.903   5.233   1.00 24.98  ?  631 HOH A O     1 
HETATM 4984 O  O     . HOH G 4 .   ? 23.245  -3.437  11.785  1.00 26.43  ?  632 HOH A O     1 
HETATM 4985 O  O     . HOH G 4 .   ? 24.940  24.991  18.847  1.00 40.64  ?  633 HOH A O     1 
HETATM 4986 O  O     . HOH G 4 .   ? 3.345   -2.887  20.333  1.00 28.32  ?  634 HOH A O     1 
HETATM 4987 O  O     . HOH G 4 .   ? 26.674  -0.893  4.510   1.00 32.03  ?  635 HOH A O     1 
HETATM 4988 O  O     . HOH G 4 .   ? 5.427   17.134  15.834  1.00 32.20  ?  636 HOH A O     1 
HETATM 4989 O  O     . HOH G 4 .   ? 32.377  1.967   8.722   1.00 28.91  ?  637 HOH A O     1 
HETATM 4990 O  O     . HOH G 4 .   ? 21.881  -5.005  27.986  1.00 23.98  ?  638 HOH A O     1 
HETATM 4991 O  O     . HOH G 4 .   ? 19.512  -5.024  31.581  1.00 35.42  ?  639 HOH A O     1 
HETATM 4992 O  O     . HOH G 4 .   ? 2.289   -0.022  14.577  1.00 16.17  ?  640 HOH A O     1 
HETATM 4993 O  O     . HOH G 4 .   ? 10.856  21.011  18.027  1.00 22.58  ?  641 HOH A O     1 
HETATM 4994 O  O     . HOH G 4 .   ? 25.292  -5.888  10.990  1.00 33.50  ?  642 HOH A O     1 
HETATM 4995 O  O     . HOH G 4 .   ? 16.199  24.483  13.548  1.00 43.35  ?  643 HOH A O     1 
HETATM 4996 O  O     . HOH G 4 .   ? 36.264  -11.049 -0.902  1.00 52.68  ?  644 HOH A O     1 
HETATM 4997 O  O     . HOH G 4 .   ? 19.995  12.703  31.409  1.00 44.38  ?  645 HOH A O     1 
HETATM 4998 O  O     . HOH G 4 .   ? 26.493  24.446  20.510  1.00 39.12  ?  646 HOH A O     1 
HETATM 4999 O  O     . HOH G 4 .   ? 27.018  -25.950 1.553   1.00 36.33  ?  647 HOH A O     1 
HETATM 5000 O  O     . HOH G 4 .   ? 9.654   19.272  15.466  1.00 27.74  ?  648 HOH A O     1 
HETATM 5001 O  O     . HOH G 4 .   ? 9.625   -2.513  -2.418  1.00 34.25  ?  649 HOH A O     1 
HETATM 5002 O  O     . HOH G 4 .   ? 26.657  -12.929 1.419   1.00 37.27  ?  650 HOH A O     1 
HETATM 5003 O  O     . HOH G 4 .   ? 16.898  -4.946  7.908   1.00 30.95  ?  651 HOH A O     1 
HETATM 5004 O  O     . HOH G 4 .   ? -2.572  -7.257  8.579   1.00 37.78  ?  652 HOH A O     1 
HETATM 5005 O  O     . HOH G 4 .   ? 22.190  -0.721  8.438   1.00 31.48  ?  653 HOH A O     1 
HETATM 5006 O  O     . HOH G 4 .   ? 27.595  -5.286  10.112  1.00 31.72  ?  654 HOH A O     1 
HETATM 5007 O  O     . HOH G 4 .   ? 37.174  0.896   23.088  1.00 32.31  ?  655 HOH A O     1 
HETATM 5008 O  O     . HOH G 4 .   ? 12.856  15.303  27.945  1.00 25.95  ?  656 HOH A O     1 
HETATM 5009 O  O     . HOH G 4 .   ? 11.249  -20.164 -14.975 1.00 44.07  ?  657 HOH A O     1 
HETATM 5010 O  O     . HOH G 4 .   ? 7.082   -7.050  13.109  1.00 14.32  ?  658 HOH A O     1 
HETATM 5011 O  O     . HOH G 4 .   ? 16.148  -18.005 26.013  1.00 30.65  ?  659 HOH A O     1 
HETATM 5012 O  O     . HOH G 4 .   ? 14.539  -24.796 -0.802  1.00 44.61  ?  660 HOH A O     1 
HETATM 5013 O  O     . HOH G 4 .   ? 0.548   9.736   20.199  1.00 36.00  ?  661 HOH A O     1 
HETATM 5014 O  O     . HOH G 4 .   ? 1.628   6.391   20.651  1.00 27.88  ?  662 HOH A O     1 
HETATM 5015 O  O     . HOH G 4 .   ? 20.616  -10.570 26.440  1.00 25.91  ?  663 HOH A O     1 
HETATM 5016 O  O     . HOH G 4 .   ? 17.074  -16.035 27.343  1.00 40.47  ?  664 HOH A O     1 
HETATM 5017 O  O     . HOH G 4 .   ? 23.026  -5.269  7.571   1.00 35.44  ?  665 HOH A O     1 
HETATM 5018 O  O     . HOH G 4 .   ? 20.296  -4.406  -0.221  1.00 39.33  ?  666 HOH A O     1 
HETATM 5019 O  O     . HOH G 4 .   ? 2.519   -7.657  17.039  1.00 32.52  ?  667 HOH A O     1 
HETATM 5020 O  O     . HOH G 4 .   ? 4.883   -4.550  25.650  1.00 23.52  ?  668 HOH A O     1 
HETATM 5021 O  O     . HOH G 4 .   ? 18.724  -4.982  5.150   1.00 41.68  ?  669 HOH A O     1 
HETATM 5022 O  O     . HOH G 4 .   ? 32.573  -9.013  17.621  1.00 33.60  ?  670 HOH A O     1 
HETATM 5023 O  O     . HOH G 4 .   ? 24.801  -21.115 14.849  1.00 39.10  ?  671 HOH A O     1 
HETATM 5024 O  O     . HOH G 4 .   ? 11.812  10.805  3.149   1.00 29.48  ?  672 HOH A O     1 
HETATM 5025 O  O     . HOH G 4 .   ? -1.232  -12.700 12.287  1.00 37.06  ?  673 HOH A O     1 
HETATM 5026 O  O     . HOH G 4 .   ? 17.572  -13.673 27.002  1.00 31.09  ?  674 HOH A O     1 
HETATM 5027 O  O     . HOH G 4 .   ? 15.957  26.366  16.354  1.00 39.19  ?  675 HOH A O     1 
HETATM 5028 O  O     . HOH G 4 .   ? 26.459  -10.957 6.380   1.00 27.36  ?  676 HOH A O     1 
HETATM 5029 O  O     . HOH G 4 .   ? 41.941  7.613   20.283  1.00 31.11  ?  677 HOH A O     1 
HETATM 5030 O  O     . HOH G 4 .   ? 6.324   -5.944  -1.510  1.00 56.40  ?  678 HOH A O     1 
HETATM 5031 O  O     . HOH G 4 .   ? 29.686  -3.044  10.869  1.00 26.63  ?  679 HOH A O     1 
HETATM 5032 O  O     . HOH G 4 .   ? 29.360  28.770  10.019  1.00 53.25  ?  680 HOH A O     1 
HETATM 5033 O  O     . HOH G 4 .   ? 3.761   -3.128  27.851  1.00 33.09  ?  681 HOH A O     1 
HETATM 5034 O  O     . HOH G 4 .   ? 34.650  -2.209  9.835   1.00 34.07  ?  682 HOH A O     1 
HETATM 5035 O  O     . HOH G 4 .   ? 24.181  -20.637 17.474  1.00 44.23  ?  683 HOH A O     1 
HETATM 5036 O  O     . HOH G 4 .   ? -2.144  -11.983 10.144  1.00 37.40  ?  684 HOH A O     1 
HETATM 5037 O  O     . HOH G 4 .   ? 19.767  -25.796 7.647   1.00 39.14  ?  685 HOH A O     1 
HETATM 5038 O  O     . HOH G 4 .   ? 16.458  11.537  30.852  1.00 37.06  ?  686 HOH A O     1 
HETATM 5039 O  O     . HOH G 4 .   ? 31.744  10.103  30.143  1.00 27.84  ?  687 HOH A O     1 
HETATM 5040 O  O     . HOH G 4 .   ? 33.880  9.487   26.936  1.00 34.24  ?  688 HOH A O     1 
HETATM 5041 O  O     . HOH G 4 .   ? 6.233   16.364  19.177  1.00 33.51  ?  689 HOH A O     1 
HETATM 5042 O  O     . HOH G 4 .   ? 29.953  -22.532 -12.746 1.00 37.94  ?  690 HOH A O     1 
HETATM 5043 O  O     . HOH G 4 .   ? 34.091  -0.624  23.963  1.00 36.05  ?  691 HOH A O     1 
HETATM 5044 O  O     . HOH G 4 .   ? 24.528  -28.105 -1.470  1.00 29.94  ?  692 HOH A O     1 
HETATM 5045 O  O     . HOH G 4 .   ? 34.770  11.687  26.109  1.00 28.05  ?  693 HOH A O     1 
HETATM 5046 O  O     . HOH G 4 .   ? 34.277  -7.247  -5.587  1.00 51.85  ?  694 HOH A O     1 
HETATM 5047 O  O     . HOH G 4 .   ? 34.402  -9.310  19.129  1.00 40.90  ?  695 HOH A O     1 
HETATM 5048 O  O     . HOH G 4 .   ? 32.781  -9.607  15.239  1.00 28.89  ?  696 HOH A O     1 
HETATM 5049 O  O     . HOH G 4 .   ? 7.053   17.260  17.344  1.00 35.57  ?  697 HOH A O     1 
HETATM 5050 O  O     . HOH G 4 .   ? 0.369   1.989   14.339  1.00 26.78  ?  698 HOH A O     1 
HETATM 5051 O  O     . HOH G 4 .   ? 2.547   -8.704  1.497   1.00 39.72  ?  699 HOH A O     1 
HETATM 5052 O  O     . HOH G 4 .   ? 31.522  -18.861 9.971   1.00 35.81  ?  700 HOH A O     1 
HETATM 5053 O  O     . HOH G 4 .   ? 15.990  9.241   30.546  1.00 19.31  ?  701 HOH A O     1 
HETATM 5054 O  O     . HOH G 4 .   ? 24.020  -6.412  27.461  1.00 33.19  ?  702 HOH A O     1 
HETATM 5055 O  O     . HOH G 4 .   ? 4.146   -10.822 18.048  1.00 23.16  ?  703 HOH A O     1 
HETATM 5056 O  O     . HOH G 4 .   ? 12.149  13.222  2.574   1.00 35.30  ?  704 HOH A O     1 
HETATM 5057 O  O     . HOH G 4 .   ? 3.078   -5.214  19.120  1.00 28.86  ?  705 HOH A O     1 
HETATM 5058 O  O     . HOH G 4 .   ? 3.450   15.985  20.323  1.00 26.10  ?  706 HOH A O     1 
HETATM 5059 O  O     . HOH G 4 .   ? 11.864  -14.007 25.599  1.00 28.51  ?  707 HOH A O     1 
HETATM 5060 O  O     . HOH G 4 .   ? 6.740   -14.906 -6.193  1.00 33.90  ?  708 HOH A O     1 
HETATM 5061 O  O     . HOH G 4 .   ? 34.083  -10.794 -2.130  1.00 48.73  ?  709 HOH A O     1 
HETATM 5062 O  O     . HOH G 4 .   ? 5.528   -3.716  1.374   1.00 33.42  ?  710 HOH A O     1 
HETATM 5063 O  O     . HOH G 4 .   ? 19.270  -11.975 27.817  1.00 39.53  ?  711 HOH A O     1 
HETATM 5064 O  O     . HOH G 4 .   ? 4.452   -6.794  26.914  1.00 27.29  ?  712 HOH A O     1 
HETATM 5065 O  O     . HOH G 4 .   ? 4.559   -6.578  29.131  1.00 27.36  ?  713 HOH A O     1 
HETATM 5066 O  O     . HOH H 4 .   ? -5.741  18.440  -21.069 1.00 30.12  ?  501 HOH B O     1 
HETATM 5067 O  O     . HOH H 4 .   ? -3.606  12.991  -23.097 1.00 30.22  ?  502 HOH B O     1 
HETATM 5068 O  O     . HOH H 4 .   ? -3.810  17.174  -42.954 1.00 33.94  ?  503 HOH B O     1 
HETATM 5069 O  O     . HOH H 4 .   ? 15.055  34.276  -35.281 1.00 23.92  ?  504 HOH B O     1 
HETATM 5070 O  O     . HOH H 4 .   ? -0.416  39.355  -28.576 1.00 27.22  ?  505 HOH B O     1 
HETATM 5071 O  O     . HOH H 4 .   ? -8.950  -5.163  -29.931 1.00 22.84  ?  506 HOH B O     1 
HETATM 5072 O  O     . HOH H 4 .   ? -5.491  21.633  -38.823 1.00 24.99  ?  507 HOH B O     1 
HETATM 5073 O  O     . HOH H 4 .   ? -17.371 -1.550  -33.628 1.00 45.48  ?  508 HOH B O     1 
HETATM 5074 O  O     . HOH H 4 .   ? 15.153  36.477  -34.856 1.00 40.50  ?  509 HOH B O     1 
HETATM 5075 O  O     . HOH H 4 .   ? -0.462  -15.010 -10.990 1.00 47.89  ?  510 HOH B O     1 
HETATM 5076 O  O     . HOH H 4 .   ? -16.021 -4.978  -34.578 1.00 42.97  ?  511 HOH B O     1 
HETATM 5077 O  O     . HOH H 4 .   ? -6.604  19.945  -23.166 1.00 35.39  ?  512 HOH B O     1 
HETATM 5078 O  O     . HOH H 4 .   ? 15.353  23.940  -40.174 1.00 20.49  ?  513 HOH B O     1 
HETATM 5079 O  O     . HOH H 4 .   ? -12.675 1.972   -34.733 1.00 32.54  ?  514 HOH B O     1 
HETATM 5080 O  O     . HOH H 4 .   ? -22.957 7.173   -6.845  1.00 37.89  ?  515 HOH B O     1 
HETATM 5081 O  O     . HOH H 4 .   ? 23.139  13.972  -26.545 1.00 31.97  ?  516 HOH B O     1 
HETATM 5082 O  O     . HOH H 4 .   ? 8.045   -7.445  -16.352 1.00 42.04  ?  517 HOH B O     1 
HETATM 5083 O  O     . HOH H 4 .   ? 16.440  1.239   -26.473 1.00 35.02  ?  518 HOH B O     1 
HETATM 5084 O  O     . HOH H 4 .   ? 12.646  31.484  -24.981 1.00 34.84  ?  519 HOH B O     1 
HETATM 5085 O  O     . HOH H 4 .   ? 10.753  14.447  -45.964 1.00 18.96  ?  520 HOH B O     1 
HETATM 5086 O  O     . HOH H 4 .   ? 9.584   15.643  -29.181 1.00 13.07  ?  521 HOH B O     1 
HETATM 5087 O  O     . HOH H 4 .   ? -4.961  4.589   -24.184 1.00 25.38  ?  522 HOH B O     1 
HETATM 5088 O  O     . HOH H 4 .   ? -12.357 17.583  0.659   1.00 40.14  ?  523 HOH B O     1 
HETATM 5089 O  O     . HOH H 4 .   ? 17.627  14.201  -21.130 1.00 25.08  ?  524 HOH B O     1 
HETATM 5090 O  O     . HOH H 4 .   ? -3.200  18.025  -4.486  1.00 49.88  ?  525 HOH B O     1 
HETATM 5091 O  O     . HOH H 4 .   ? 12.820  34.646  -35.669 1.00 30.74  ?  526 HOH B O     1 
HETATM 5092 O  O     . HOH H 4 .   ? 16.211  22.321  -23.065 1.00 14.64  ?  527 HOH B O     1 
HETATM 5093 O  O     . HOH H 4 .   ? 24.336  30.918  -36.765 1.00 47.50  ?  528 HOH B O     1 
HETATM 5094 O  O     . HOH H 4 .   ? 17.265  28.497  -37.823 1.00 37.80  ?  529 HOH B O     1 
HETATM 5095 O  O     . HOH H 4 .   ? -12.679 26.385  -25.073 1.00 29.22  ?  530 HOH B O     1 
HETATM 5096 O  O     . HOH H 4 .   ? -9.348  17.653  -26.732 1.00 25.28  ?  531 HOH B O     1 
HETATM 5097 O  O     . HOH H 4 .   ? 12.000  -4.575  -19.814 1.00 36.37  ?  532 HOH B O     1 
HETATM 5098 O  O     . HOH H 4 .   ? 1.051   17.536  -22.574 1.00 23.50  ?  533 HOH B O     1 
HETATM 5099 O  O     . HOH H 4 .   ? 19.985  30.570  -31.697 1.00 37.06  ?  534 HOH B O     1 
HETATM 5100 O  O     . HOH H 4 .   ? 27.421  20.682  -27.750 1.00 39.77  ?  535 HOH B O     1 
HETATM 5101 O  O     . HOH H 4 .   ? -3.615  30.751  -27.009 1.00 13.36  ?  536 HOH B O     1 
HETATM 5102 O  O     . HOH H 4 .   ? -5.213  19.945  -41.698 1.00 33.93  ?  537 HOH B O     1 
HETATM 5103 O  O     . HOH H 4 .   ? -3.490  16.109  -26.394 1.00 32.09  ?  538 HOH B O     1 
HETATM 5104 O  O     . HOH H 4 .   ? -4.834  6.381   -41.128 1.00 23.31  ?  539 HOH B O     1 
HETATM 5105 O  O     . HOH H 4 .   ? 5.107   12.001  -10.361 1.00 22.97  ?  540 HOH B O     1 
HETATM 5106 O  O     . HOH H 4 .   ? 6.198   32.004  -18.748 1.00 28.76  ?  541 HOH B O     1 
HETATM 5107 O  O     . HOH H 4 .   ? -2.466  11.181  -46.356 1.00 17.40  ?  542 HOH B O     1 
HETATM 5108 O  O     . HOH H 4 .   ? 17.783  3.740   -28.040 1.00 29.43  ?  543 HOH B O     1 
HETATM 5109 O  O     . HOH H 4 .   ? 6.318   -0.649  -36.818 1.00 24.23  ?  544 HOH B O     1 
HETATM 5110 O  O     . HOH H 4 .   ? 21.355  24.391  -22.589 1.00 29.63  ?  545 HOH B O     1 
HETATM 5111 O  O     . HOH H 4 .   ? -4.479  10.931  -24.912 1.00 27.27  ?  546 HOH B O     1 
HETATM 5112 O  O     . HOH H 4 .   ? 9.188   34.436  -25.512 1.00 21.33  ?  547 HOH B O     1 
HETATM 5113 O  O     . HOH H 4 .   ? 9.171   6.394   -22.275 1.00 28.45  ?  548 HOH B O     1 
HETATM 5114 O  O     . HOH H 4 .   ? 3.067   15.433  -24.891 1.00 26.10  ?  549 HOH B O     1 
HETATM 5115 O  O     . HOH H 4 .   ? -11.520 29.457  -27.853 1.00 28.46  ?  550 HOH B O     1 
HETATM 5116 O  O     . HOH H 4 .   ? -7.770  14.166  -39.393 1.00 23.93  ?  551 HOH B O     1 
HETATM 5117 O  O     . HOH H 4 .   ? 1.234   7.483   -47.147 1.00 32.07  ?  552 HOH B O     1 
HETATM 5118 O  O     . HOH H 4 .   ? -1.825  34.589  -31.501 1.00 25.57  ?  553 HOH B O     1 
HETATM 5119 O  O     . HOH H 4 .   ? 13.824  0.377   -28.389 1.00 23.40  ?  554 HOH B O     1 
HETATM 5120 O  O     . HOH H 4 .   ? 8.357   17.487  -42.067 1.00 22.58  ?  555 HOH B O     1 
HETATM 5121 O  O     . HOH H 4 .   ? 23.534  20.506  -33.718 1.00 30.07  ?  556 HOH B O     1 
HETATM 5122 O  O     . HOH H 4 .   ? 5.959   -1.496  -33.618 1.00 25.12  ?  557 HOH B O     1 
HETATM 5123 O  O     . HOH H 4 .   ? -0.353  -2.956  -8.469  1.00 44.52  ?  558 HOH B O     1 
HETATM 5124 O  O     . HOH H 4 .   ? -8.281  16.773  -31.185 1.00 21.53  ?  559 HOH B O     1 
HETATM 5125 O  O     . HOH H 4 .   ? 19.700  18.364  -27.828 1.00 21.86  ?  560 HOH B O     1 
HETATM 5126 O  O     . HOH H 4 .   ? 23.511  7.884   -36.738 1.00 24.03  ?  561 HOH B O     1 
HETATM 5127 O  O     . HOH H 4 .   ? -2.592  37.275  -24.994 1.00 31.81  ?  562 HOH B O     1 
HETATM 5128 O  O     . HOH H 4 .   ? -5.026  10.550  -34.358 1.00 12.57  ?  563 HOH B O     1 
HETATM 5129 O  O     . HOH H 4 .   ? 13.696  1.832   -19.511 1.00 29.74  ?  564 HOH B O     1 
HETATM 5130 O  O     . HOH H 4 .   ? -7.688  36.754  -24.833 1.00 23.34  ?  565 HOH B O     1 
HETATM 5131 O  O     . HOH H 4 .   ? 14.615  15.785  -23.435 1.00 22.91  ?  566 HOH B O     1 
HETATM 5132 O  O     . HOH H 4 .   ? 6.674   23.023  -47.321 1.00 39.08  ?  567 HOH B O     1 
HETATM 5133 O  O     . HOH H 4 .   ? -1.001  15.588  -25.919 1.00 27.86  ?  568 HOH B O     1 
HETATM 5134 O  O     . HOH H 4 .   ? -10.084 30.340  -26.075 1.00 19.52  ?  569 HOH B O     1 
HETATM 5135 O  O     . HOH H 4 .   ? 17.798  19.527  -14.336 1.00 35.83  ?  570 HOH B O     1 
HETATM 5136 O  O     . HOH H 4 .   ? 6.734   -2.716  -24.730 1.00 18.53  ?  571 HOH B O     1 
HETATM 5137 O  O     . HOH H 4 .   ? -6.943  -15.626 -29.136 1.00 32.01  ?  572 HOH B O     1 
HETATM 5138 O  O     . HOH H 4 .   ? 10.375  12.983  -48.075 1.00 28.26  ?  573 HOH B O     1 
HETATM 5139 O  O     . HOH H 4 .   ? 1.473   18.044  -19.461 1.00 23.17  ?  574 HOH B O     1 
HETATM 5140 O  O     . HOH H 4 .   ? -9.589  17.530  -32.971 1.00 31.75  ?  575 HOH B O     1 
HETATM 5141 O  O     . HOH H 4 .   ? 7.388   26.079  -42.360 1.00 36.91  ?  576 HOH B O     1 
HETATM 5142 O  O     . HOH H 4 .   ? 25.306  21.715  -30.336 1.00 37.71  ?  577 HOH B O     1 
HETATM 5143 O  O     . HOH H 4 .   ? 6.852   4.415   -21.892 1.00 18.20  ?  578 HOH B O     1 
HETATM 5144 O  O     . HOH H 4 .   ? 12.174  25.992  -20.095 1.00 20.79  ?  579 HOH B O     1 
HETATM 5145 O  O     . HOH H 4 .   ? 14.954  25.779  -20.874 1.00 24.03  ?  580 HOH B O     1 
HETATM 5146 O  O     . HOH H 4 .   ? 19.656  4.331   -26.450 1.00 30.13  ?  581 HOH B O     1 
HETATM 5147 O  O     . HOH H 4 .   ? -6.020  31.728  -33.868 1.00 35.75  ?  582 HOH B O     1 
HETATM 5148 O  O     . HOH H 4 .   ? 16.982  19.683  -16.984 1.00 31.57  ?  583 HOH B O     1 
HETATM 5149 O  O     . HOH H 4 .   ? 13.064  -0.690  -25.876 1.00 17.20  ?  584 HOH B O     1 
HETATM 5150 O  O     . HOH H 4 .   ? 8.406   10.033  -43.105 1.00 27.47  ?  585 HOH B O     1 
HETATM 5151 O  O     . HOH H 4 .   ? -0.444  20.299  -14.644 1.00 25.17  ?  586 HOH B O     1 
HETATM 5152 O  O     . HOH H 4 .   ? -1.447  29.995  -25.537 1.00 19.88  ?  587 HOH B O     1 
HETATM 5153 O  O     . HOH H 4 .   ? 5.453   17.084  -41.194 1.00 18.70  ?  588 HOH B O     1 
HETATM 5154 O  O     . HOH H 4 .   ? 19.161  3.517   -35.829 1.00 22.52  ?  589 HOH B O     1 
HETATM 5155 O  O     . HOH H 4 .   ? -8.798  27.007  -22.700 1.00 16.88  ?  590 HOH B O     1 
HETATM 5156 O  O     . HOH H 4 .   ? 6.018   24.663  -20.833 1.00 19.51  ?  591 HOH B O     1 
HETATM 5157 O  O     . HOH H 4 .   ? -13.908 27.826  -32.355 1.00 37.13  ?  592 HOH B O     1 
HETATM 5158 O  O     . HOH H 4 .   ? 24.115  14.569  -40.422 1.00 26.13  ?  593 HOH B O     1 
HETATM 5159 O  O     . HOH H 4 .   ? 1.469   22.888  -16.311 1.00 31.90  ?  594 HOH B O     1 
HETATM 5160 O  O     . HOH H 4 .   ? -12.964 12.469  -28.406 1.00 19.44  ?  595 HOH B O     1 
HETATM 5161 O  O     . HOH H 4 .   ? 21.393  9.717   -19.571 1.00 31.31  ?  596 HOH B O     1 
HETATM 5162 O  O     . HOH H 4 .   ? 12.938  -1.083  -30.509 1.00 23.74  ?  597 HOH B O     1 
HETATM 5163 O  O     . HOH H 4 .   ? 2.643   18.606  -29.615 1.00 21.52  ?  598 HOH B O     1 
HETATM 5164 O  O     . HOH H 4 .   ? 10.344  31.882  -24.448 1.00 23.34  ?  599 HOH B O     1 
HETATM 5165 O  O     . HOH H 4 .   ? -12.805 -7.397  -21.403 1.00 29.46  ?  600 HOH B O     1 
HETATM 5166 O  O     . HOH H 4 .   ? 23.727  17.114  -25.277 1.00 37.32  ?  601 HOH B O     1 
HETATM 5167 O  O     . HOH H 4 .   ? -12.493 8.910   -35.198 1.00 33.47  ?  602 HOH B O     1 
HETATM 5168 O  O     . HOH H 4 .   ? -3.345  8.844   -23.321 1.00 27.57  ?  603 HOH B O     1 
HETATM 5169 O  O     . HOH H 4 .   ? -1.173  24.849  -42.059 1.00 19.93  ?  604 HOH B O     1 
HETATM 5170 O  O     . HOH H 4 .   ? 7.147   40.404  -28.200 1.00 37.93  ?  605 HOH B O     1 
HETATM 5171 O  O     . HOH H 4 .   ? -0.839  14.066  -23.601 1.00 35.21  ?  606 HOH B O     1 
HETATM 5172 O  O     . HOH H 4 .   ? 14.583  0.160   -24.078 1.00 18.98  ?  607 HOH B O     1 
HETATM 5173 O  O     . HOH H 4 .   ? -2.222  18.333  -19.070 1.00 24.44  ?  608 HOH B O     1 
HETATM 5174 O  O     . HOH H 4 .   ? -1.699  21.833  -47.082 1.00 45.09  ?  609 HOH B O     1 
HETATM 5175 O  O     . HOH H 4 .   ? 5.370   -0.889  -26.521 1.00 15.29  ?  610 HOH B O     1 
HETATM 5176 O  O     . HOH H 4 .   ? -6.817  5.952   -39.726 1.00 35.85  ?  611 HOH B O     1 
HETATM 5177 O  O     . HOH H 4 .   ? 24.073  14.130  -31.416 1.00 27.23  ?  612 HOH B O     1 
HETATM 5178 O  O     . HOH H 4 .   ? 15.327  4.780   -14.138 1.00 40.37  ?  613 HOH B O     1 
HETATM 5179 O  O     . HOH H 4 .   ? 16.059  27.639  -34.400 1.00 30.55  ?  614 HOH B O     1 
HETATM 5180 O  O     . HOH H 4 .   ? -0.125  34.474  -38.003 1.00 30.36  ?  615 HOH B O     1 
HETATM 5181 O  O     . HOH H 4 .   ? 13.088  1.788   -17.364 1.00 36.86  ?  616 HOH B O     1 
HETATM 5182 O  O     . HOH H 4 .   ? -5.772  27.627  -19.855 1.00 17.92  ?  617 HOH B O     1 
HETATM 5183 O  O     . HOH H 4 .   ? -0.125  21.688  -6.584  1.00 39.62  ?  618 HOH B O     1 
HETATM 5184 O  O     . HOH H 4 .   ? -14.650 17.904  -0.082  1.00 38.18  ?  619 HOH B O     1 
HETATM 5185 O  O     . HOH H 4 .   ? -1.382  -0.888  -42.033 1.00 26.97  ?  620 HOH B O     1 
HETATM 5186 O  O     . HOH H 4 .   ? 4.764   24.029  -9.013  1.00 32.84  ?  621 HOH B O     1 
HETATM 5187 O  O     . HOH H 4 .   ? 15.750  28.006  -15.512 1.00 34.89  ?  622 HOH B O     1 
HETATM 5188 O  O     . HOH H 4 .   ? -13.118 -0.519  -7.760  1.00 41.86  ?  623 HOH B O     1 
HETATM 5189 O  O     . HOH H 4 .   ? -5.343  15.686  -24.836 1.00 27.78  ?  624 HOH B O     1 
HETATM 5190 O  O     . HOH H 4 .   ? 15.760  0.614   -37.755 1.00 19.16  ?  625 HOH B O     1 
HETATM 5191 O  O     . HOH H 4 .   ? -5.122  25.114  -19.443 1.00 25.48  ?  626 HOH B O     1 
HETATM 5192 O  O     . HOH H 4 .   ? -9.373  25.328  -37.560 1.00 34.44  ?  627 HOH B O     1 
HETATM 5193 O  O     . HOH H 4 .   ? 1.610   -13.817 -29.677 1.00 36.31  ?  628 HOH B O     1 
HETATM 5194 O  O     . HOH H 4 .   ? 5.399   34.086  -37.474 1.00 23.05  ?  629 HOH B O     1 
HETATM 5195 O  O     . HOH H 4 .   ? 21.521  17.544  -42.235 1.00 27.53  ?  630 HOH B O     1 
HETATM 5196 O  O     . HOH H 4 .   ? 1.042   44.079  -27.164 1.00 44.33  ?  631 HOH B O     1 
HETATM 5197 O  O     . HOH H 4 .   ? -6.583  18.274  -40.388 1.00 30.93  ?  632 HOH B O     1 
HETATM 5198 O  O     . HOH H 4 .   ? -5.309  11.066  -12.880 1.00 40.41  ?  633 HOH B O     1 
HETATM 5199 O  O     . HOH H 4 .   ? -10.564 22.806  -25.407 1.00 34.82  ?  634 HOH B O     1 
HETATM 5200 O  O     . HOH H 4 .   ? -3.468  10.144  -42.172 1.00 29.44  ?  635 HOH B O     1 
HETATM 5201 O  O     . HOH H 4 .   ? 2.064   -12.004 -6.570  1.00 50.21  ?  636 HOH B O     1 
HETATM 5202 O  O     . HOH H 4 .   ? -7.077  15.798  -40.944 1.00 30.92  ?  637 HOH B O     1 
HETATM 5203 O  O     . HOH H 4 .   ? 8.274   4.450   -43.028 1.00 30.84  ?  638 HOH B O     1 
HETATM 5204 O  O     . HOH H 4 .   ? 13.124  -1.312  -34.521 1.00 26.77  ?  639 HOH B O     1 
HETATM 5205 O  O     . HOH H 4 .   ? -12.711 1.005   -36.779 1.00 35.92  ?  640 HOH B O     1 
HETATM 5206 O  O     . HOH H 4 .   ? 23.866  12.642  -35.233 1.00 35.58  ?  641 HOH B O     1 
HETATM 5207 O  O     . HOH H 4 .   ? 6.938   15.896  -48.916 1.00 38.45  ?  642 HOH B O     1 
HETATM 5208 O  O     . HOH H 4 .   ? -11.245 -5.882  -8.480  1.00 66.12  ?  643 HOH B O     1 
HETATM 5209 O  O     . HOH H 4 .   ? 7.970   2.425   -44.555 1.00 40.80  ?  644 HOH B O     1 
HETATM 5210 O  O     . HOH H 4 .   ? 16.040  28.388  -19.422 1.00 32.58  ?  645 HOH B O     1 
HETATM 5211 O  O     . HOH H 4 .   ? -10.381 -11.451 -18.048 1.00 40.68  ?  646 HOH B O     1 
HETATM 5212 O  O     . HOH H 4 .   ? -18.675 -3.438  -35.241 1.00 46.50  ?  647 HOH B O     1 
HETATM 5213 O  O     . HOH H 4 .   ? -10.258 11.342  -20.983 1.00 35.23  ?  648 HOH B O     1 
HETATM 5214 O  O     . HOH H 4 .   ? -5.596  10.879  -40.663 1.00 24.01  ?  649 HOH B O     1 
HETATM 5215 O  O     . HOH H 4 .   ? 25.405  23.876  -31.186 1.00 31.96  ?  650 HOH B O     1 
HETATM 5216 O  O     . HOH H 4 .   ? 25.981  14.831  -35.779 1.00 36.18  ?  651 HOH B O     1 
HETATM 5217 O  O     . HOH H 4 .   ? 17.494  1.164   -36.367 1.00 30.21  ?  652 HOH B O     1 
HETATM 5218 O  O     . HOH H 4 .   ? -11.134 -5.281  -31.381 1.00 37.82  ?  653 HOH B O     1 
HETATM 5219 O  O     . HOH H 4 .   ? 21.470  3.835   -35.058 1.00 29.04  ?  654 HOH B O     1 
HETATM 5220 O  O     . HOH H 4 .   ? 25.125  12.801  -27.060 1.00 35.98  ?  655 HOH B O     1 
HETATM 5221 O  O     . HOH H 4 .   ? 11.714  34.788  -24.295 1.00 29.89  ?  656 HOH B O     1 
HETATM 5222 O  O     . HOH H 4 .   ? 17.876  30.240  -41.063 1.00 44.17  ?  657 HOH B O     1 
HETATM 5223 O  O     . HOH H 4 .   ? 16.765  -0.339  -28.071 1.00 27.09  ?  658 HOH B O     1 
HETATM 5224 O  O     . HOH H 4 .   ? -14.992 27.606  -26.751 1.00 39.61  ?  659 HOH B O     1 
HETATM 5225 O  O     . HOH H 4 .   ? 15.132  -1.764  -32.629 1.00 30.72  ?  660 HOH B O     1 
HETATM 5226 O  O     . HOH H 4 .   ? 13.743  -3.489  -26.546 1.00 26.27  ?  661 HOH B O     1 
HETATM 5227 O  O     . HOH H 4 .   ? 5.224   14.876  -49.834 1.00 39.42  ?  662 HOH B O     1 
HETATM 5228 O  O     . HOH H 4 .   ? 13.146  -5.268  -28.166 1.00 38.39  ?  663 HOH B O     1 
HETATM 5229 O  O     . HOH H 4 .   ? 25.475  14.825  -24.852 1.00 40.35  ?  664 HOH B O     1 
HETATM 5230 O  O     . HOH H 4 .   ? -11.143 25.657  -22.447 1.00 28.00  ?  665 HOH B O     1 
HETATM 5231 O  O     . HOH H 4 .   ? -4.490  39.581  -31.459 1.00 30.43  ?  666 HOH B O     1 
HETATM 5232 O  O     . HOH H 4 .   ? 22.129  27.241  -23.239 1.00 38.54  ?  667 HOH B O     1 
HETATM 5233 O  O     . HOH H 4 .   ? 21.316  26.108  -20.722 1.00 37.99  ?  668 HOH B O     1 
HETATM 5234 O  O     . HOH H 4 .   ? -6.318  6.862   -42.993 1.00 30.34  ?  669 HOH B O     1 
HETATM 5235 O  O     . HOH H 4 .   ? 25.074  10.473  -35.769 1.00 30.20  ?  670 HOH B O     1 
HETATM 5236 O  O     . HOH H 4 .   ? -1.855  27.251  -41.936 1.00 36.60  ?  671 HOH B O     1 
HETATM 5237 O  O     . HOH H 4 .   ? 14.216  -2.204  -29.012 1.00 38.84  ?  672 HOH B O     1 
HETATM 5238 O  O     . HOH H 4 .   ? -8.116  11.575  -21.450 1.00 37.08  ?  673 HOH B O     1 
HETATM 5239 O  O     . HOH H 4 .   ? 27.917  13.577  -35.500 1.00 35.16  ?  674 HOH B O     1 
HETATM 5240 O  O     . HOH H 4 .   ? 10.246  16.321  -51.390 1.00 26.78  ?  675 HOH B O     1 
# 
