data_8OX3
# 
_entry.id   8OX3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8OX3         pdb_00008ox3 10.2210/pdb8ox3/pdb 
WWPDB D_1292130225 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        8OX3 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              robert.gilbert@magd.ox.ac.uk 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Gilbert 
_pdbx_contact_author.name_mi            'J. C.' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9336-5604 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, T.'          1 0000-0001-7268-0306 
'Bannerji, N.'    2 0000-0002-1179-3152 
'Jackson, D.J.'   3 0000-0002-4133-9364 
'Gilbert, R.J.C.' 4 0000-0001-9336-5604 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;A novel sliding interaction with hyaluronan underlies the mode of action of LYVE-1, the receptor for leucocyte entry and trafficking in the lymphatics
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Bano, F.'        1  0000-0003-0634-7091 
primary 'Bannerji, S.'    2  0000-0002-1179-3152 
primary 'Ni, T.'          3  0000-0001-7268-0306 
primary 'Green, D.E.'     4  0000-0002-6237-0889 
primary 'DeAngelis, P.L.' 5  0000-0002-8843-1344 
primary 'Paci, E.'        6  0000-0002-4891-2768 
primary 'Lepsik, M.'      7  0000-0003-2607-8132 
primary 'Gilbert, R.J.C.' 8  0000-0001-9336-5604 
primary 'Richter, R.P.'   9  0000-0003-3071-2837 
primary 'Jackson, D.J.'   10 0000-0002-4133-9364 
# 
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 'Lymphatic vessel endothelial hyaluronic acid receptor 1' 34609.551 1   ? ? ? ? 
2 branched    man 
;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid
;
1155.965  1   ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2   ? ? ? ? 
4 non-polymer syn GLYCEROL 92.094    1   ? ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   3   ? ? ? ? 
6 non-polymer syn 'CHLORIDE ION' 35.453    1   ? ? ? ? 
7 water       nat water 18.015    173 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'LYVE-1,Cell surface retention sequence-binding protein 1,CRSBP-1,Extracellular link domain-containing protein 1' 
# 
_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       
;MLQHTSLVLLLASIWTTRHPVQGADLVQDLSISTCRIMGVALVGRNKNPQMNFTEANEACKMLGLTLASRDQVESAQKSG
FETCSYGWVGEQFSVIPRIFSNPRCGKNGKGVLIWNAPSSQKFKAYCHNSSDTWVNSCIPEIVTTFYPVLDTQTPATEFS
VSSSAYLASSPDSTTPVSATTRAPPLTSMARKTKKICITEVYTEPITMATETEAFVASGAAFKNEAAGFGGVPTALLVLA
LLFFGAAAVLAVCYVKRYVKAFPFTTKNQQKEMIETKVVKEEKADDVNANEESKKTIKNPEEAKSPPKTTVRCLEAEV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLQHTSLVLLLASIWTTRHPVQGADLVQDLSISTCRIMGVALVGRNKNPQMNFTEANEACKMLGLTLASRDQVESAQKSG
FETCSYGWVGEQFSVIPRIFSNPRCGKNGKGVLIWNAPSSQKFKAYCHNSSDTWVNSCIPEIVTTFYPVLDTQTPATEFS
VSSSAYLASSPDSTTPVSATTRAPPLTSMARKTKKICITEVYTEPITMATETEAFVASGAAFKNEAAGFGGVPTALLVLA
LLFFGAAAVLAVCYVKRYVKAFPFTTKNQQKEMIETKVVKEEKADDVNANEESKKTIKNPEEAKSPPKTTVRCLEAEV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
4 GLYCEROL                                 GOL 
5 'DI(HYDROXYETHYL)ETHER'                  PEG 
6 'CHLORIDE ION'                           CL  
7 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   GLN n 
1 4   HIS n 
1 5   THR n 
1 6   SER n 
1 7   LEU n 
1 8   VAL n 
1 9   LEU n 
1 10  LEU n 
1 11  LEU n 
1 12  ALA n 
1 13  SER n 
1 14  ILE n 
1 15  TRP n 
1 16  THR n 
1 17  THR n 
1 18  ARG n 
1 19  HIS n 
1 20  PRO n 
1 21  VAL n 
1 22  GLN n 
1 23  GLY n 
1 24  ALA n 
1 25  ASP n 
1 26  LEU n 
1 27  VAL n 
1 28  GLN n 
1 29  ASP n 
1 30  LEU n 
1 31  SER n 
1 32  ILE n 
1 33  SER n 
1 34  THR n 
1 35  CYS n 
1 36  ARG n 
1 37  ILE n 
1 38  MET n 
1 39  GLY n 
1 40  VAL n 
1 41  ALA n 
1 42  LEU n 
1 43  VAL n 
1 44  GLY n 
1 45  ARG n 
1 46  ASN n 
1 47  LYS n 
1 48  ASN n 
1 49  PRO n 
1 50  GLN n 
1 51  MET n 
1 52  ASN n 
1 53  PHE n 
1 54  THR n 
1 55  GLU n 
1 56  ALA n 
1 57  ASN n 
1 58  GLU n 
1 59  ALA n 
1 60  CYS n 
1 61  LYS n 
1 62  MET n 
1 63  LEU n 
1 64  GLY n 
1 65  LEU n 
1 66  THR n 
1 67  LEU n 
1 68  ALA n 
1 69  SER n 
1 70  ARG n 
1 71  ASP n 
1 72  GLN n 
1 73  VAL n 
1 74  GLU n 
1 75  SER n 
1 76  ALA n 
1 77  GLN n 
1 78  LYS n 
1 79  SER n 
1 80  GLY n 
1 81  PHE n 
1 82  GLU n 
1 83  THR n 
1 84  CYS n 
1 85  SER n 
1 86  TYR n 
1 87  GLY n 
1 88  TRP n 
1 89  VAL n 
1 90  GLY n 
1 91  GLU n 
1 92  GLN n 
1 93  PHE n 
1 94  SER n 
1 95  VAL n 
1 96  ILE n 
1 97  PRO n 
1 98  ARG n 
1 99  ILE n 
1 100 PHE n 
1 101 SER n 
1 102 ASN n 
1 103 PRO n 
1 104 ARG n 
1 105 CYS n 
1 106 GLY n 
1 107 LYS n 
1 108 ASN n 
1 109 GLY n 
1 110 LYS n 
1 111 GLY n 
1 112 VAL n 
1 113 LEU n 
1 114 ILE n 
1 115 TRP n 
1 116 ASN n 
1 117 ALA n 
1 118 PRO n 
1 119 SER n 
1 120 SER n 
1 121 GLN n 
1 122 LYS n 
1 123 PHE n 
1 124 LYS n 
1 125 ALA n 
1 126 TYR n 
1 127 CYS n 
1 128 HIS n 
1 129 ASN n 
1 130 SER n 
1 131 SER n 
1 132 ASP n 
1 133 THR n 
1 134 TRP n 
1 135 VAL n 
1 136 ASN n 
1 137 SER n 
1 138 CYS n 
1 139 ILE n 
1 140 PRO n 
1 141 GLU n 
1 142 ILE n 
1 143 VAL n 
1 144 THR n 
1 145 THR n 
1 146 PHE n 
1 147 TYR n 
1 148 PRO n 
1 149 VAL n 
1 150 LEU n 
1 151 ASP n 
1 152 THR n 
1 153 GLN n 
1 154 THR n 
1 155 PRO n 
1 156 ALA n 
1 157 THR n 
1 158 GLU n 
1 159 PHE n 
1 160 SER n 
1 161 VAL n 
1 162 SER n 
1 163 SER n 
1 164 SER n 
1 165 ALA n 
1 166 TYR n 
1 167 LEU n 
1 168 ALA n 
1 169 SER n 
1 170 SER n 
1 171 PRO n 
1 172 ASP n 
1 173 SER n 
1 174 THR n 
1 175 THR n 
1 176 PRO n 
1 177 VAL n 
1 178 SER n 
1 179 ALA n 
1 180 THR n 
1 181 THR n 
1 182 ARG n 
1 183 ALA n 
1 184 PRO n 
1 185 PRO n 
1 186 LEU n 
1 187 THR n 
1 188 SER n 
1 189 MET n 
1 190 ALA n 
1 191 ARG n 
1 192 LYS n 
1 193 THR n 
1 194 LYS n 
1 195 LYS n 
1 196 ILE n 
1 197 CYS n 
1 198 ILE n 
1 199 THR n 
1 200 GLU n 
1 201 VAL n 
1 202 TYR n 
1 203 THR n 
1 204 GLU n 
1 205 PRO n 
1 206 ILE n 
1 207 THR n 
1 208 MET n 
1 209 ALA n 
1 210 THR n 
1 211 GLU n 
1 212 THR n 
1 213 GLU n 
1 214 ALA n 
1 215 PHE n 
1 216 VAL n 
1 217 ALA n 
1 218 SER n 
1 219 GLY n 
1 220 ALA n 
1 221 ALA n 
1 222 PHE n 
1 223 LYS n 
1 224 ASN n 
1 225 GLU n 
1 226 ALA n 
1 227 ALA n 
1 228 GLY n 
1 229 PHE n 
1 230 GLY n 
1 231 GLY n 
1 232 VAL n 
1 233 PRO n 
1 234 THR n 
1 235 ALA n 
1 236 LEU n 
1 237 LEU n 
1 238 VAL n 
1 239 LEU n 
1 240 ALA n 
1 241 LEU n 
1 242 LEU n 
1 243 PHE n 
1 244 PHE n 
1 245 GLY n 
1 246 ALA n 
1 247 ALA n 
1 248 ALA n 
1 249 VAL n 
1 250 LEU n 
1 251 ALA n 
1 252 VAL n 
1 253 CYS n 
1 254 TYR n 
1 255 VAL n 
1 256 LYS n 
1 257 ARG n 
1 258 TYR n 
1 259 VAL n 
1 260 LYS n 
1 261 ALA n 
1 262 PHE n 
1 263 PRO n 
1 264 PHE n 
1 265 THR n 
1 266 THR n 
1 267 LYS n 
1 268 ASN n 
1 269 GLN n 
1 270 GLN n 
1 271 LYS n 
1 272 GLU n 
1 273 MET n 
1 274 ILE n 
1 275 GLU n 
1 276 THR n 
1 277 LYS n 
1 278 VAL n 
1 279 VAL n 
1 280 LYS n 
1 281 GLU n 
1 282 GLU n 
1 283 LYS n 
1 284 ALA n 
1 285 ASP n 
1 286 ASP n 
1 287 VAL n 
1 288 ASN n 
1 289 ALA n 
1 290 ASN n 
1 291 GLU n 
1 292 GLU n 
1 293 SER n 
1 294 LYS n 
1 295 LYS n 
1 296 THR n 
1 297 ILE n 
1 298 LYS n 
1 299 ASN n 
1 300 PRO n 
1 301 GLU n 
1 302 GLU n 
1 303 ALA n 
1 304 LYS n 
1 305 SER n 
1 306 PRO n 
1 307 PRO n 
1 308 LYS n 
1 309 THR n 
1 310 THR n 
1 311 VAL n 
1 312 ARG n 
1 313 CYS n 
1 314 LEU n 
1 315 GLU n 
1 316 ALA n 
1 317 GLU n 
1 318 VAL 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                   318 
_entity_src_gen.gene_src_common_name               'house mouse' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Lyve1, Crsbp1, Xlkd1' 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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            'CHO K1' 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpNAcb1-4DGlcpAb1-3DGlcpNAcb1-4DGlcpAb1-3DGlcpNAcb1-4DGlcpAb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/2,6,5/[a2122A-1b_1-5][a2122h-1b_1-5_2*NCC/3=O]/1-2-1-2-1-2/a4-b1_b3-c1_c4-d1_d3-e1_e4-f1' WURCS PDB2Glycan 1.1.0 
3 2 
'[][D-1-deoxy-GlcpA]{[(4+1)][b-D-GlcpNAc]{[(3+1)][b-D-GlcpA]{[(4+1)][b-D-GlcpNAc]{[(3+1)][b-D-GlcpA]{[(4+1)][b-D-GlcpNAc]{}}}}}}' 
LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 BDP O4 HO4 sing ? 
2 2 3 BDP C1 O1 2 NAG O3 HO3 sing ? 
3 2 4 NAG C1 O1 3 BDP O4 HO4 sing ? 
4 2 5 BDP C1 O1 4 NAG O3 HO3 sing ? 
5 2 6 NAG C1 O1 5 BDP O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
BDP 'D-saccharide, beta linking' . 'beta-D-glucopyranuronic acid'           
'beta-D-glucuronic acid; D-glucuronic acid; glucuronic acid' 'C6 H10 O7'      194.139 
CL  non-polymer                  . 'CHLORIDE ION'                           ? 'Cl -1'          35.453  
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  
GOL non-polymer                  . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PEG non-polymer                  . 'DI(HYDROXYETHYL)ETHER'                  ? 'C4 H10 O3'      106.120 
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 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BDP 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpAb                        
BDP 'COMMON NAME'                         GMML     1.0 'b-D-glucopyranuronic acid'    
BDP 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpA                      
BDP 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcA                           
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   LEU 7   7   ?   ?   ?   A . n 
A 1 8   VAL 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  ALA 12  12  ?   ?   ?   A . n 
A 1 13  SER 13  13  ?   ?   ?   A . n 
A 1 14  ILE 14  14  ?   ?   ?   A . n 
A 1 15  TRP 15  15  ?   ?   ?   A . n 
A 1 16  THR 16  16  ?   ?   ?   A . n 
A 1 17  THR 17  17  ?   ?   ?   A . n 
A 1 18  ARG 18  18  ?   ?   ?   A . n 
A 1 19  HIS 19  19  ?   ?   ?   A . n 
A 1 20  PRO 20  20  ?   ?   ?   A . n 
A 1 21  VAL 21  21  ?   ?   ?   A . n 
A 1 22  GLN 22  22  ?   ?   ?   A . n 
A 1 23  GLY 23  23  ?   ?   ?   A . n 
A 1 24  ALA 24  24  ?   ?   ?   A . n 
A 1 25  ASP 25  25  ?   ?   ?   A . n 
A 1 26  LEU 26  26  ?   ?   ?   A . n 
A 1 27  VAL 27  27  ?   ?   ?   A . n 
A 1 28  GLN 28  28  ?   ?   ?   A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  CYS 35  35  35  CYS CYS A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  MET 38  38  38  MET MET A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  CYS 84  84  84  CYS CYS A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 CYS 105 105 105 CYS CYS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 TRP 115 115 115 TRP TRP A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 CYS 138 138 138 CYS CYS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 ILE 142 142 ?   ?   ?   A . n 
A 1 143 VAL 143 143 ?   ?   ?   A . n 
A 1 144 THR 144 144 ?   ?   ?   A . n 
A 1 145 THR 145 145 ?   ?   ?   A . n 
A 1 146 PHE 146 146 ?   ?   ?   A . n 
A 1 147 TYR 147 147 ?   ?   ?   A . n 
A 1 148 PRO 148 148 ?   ?   ?   A . n 
A 1 149 VAL 149 149 ?   ?   ?   A . n 
A 1 150 LEU 150 150 ?   ?   ?   A . n 
A 1 151 ASP 151 151 ?   ?   ?   A . n 
A 1 152 THR 152 152 ?   ?   ?   A . n 
A 1 153 GLN 153 153 ?   ?   ?   A . n 
A 1 154 THR 154 154 ?   ?   ?   A . n 
A 1 155 PRO 155 155 ?   ?   ?   A . n 
A 1 156 ALA 156 156 ?   ?   ?   A . n 
A 1 157 THR 157 157 ?   ?   ?   A . n 
A 1 158 GLU 158 158 ?   ?   ?   A . n 
A 1 159 PHE 159 159 ?   ?   ?   A . n 
A 1 160 SER 160 160 ?   ?   ?   A . n 
A 1 161 VAL 161 161 ?   ?   ?   A . n 
A 1 162 SER 162 162 ?   ?   ?   A . n 
A 1 163 SER 163 163 ?   ?   ?   A . n 
A 1 164 SER 164 164 ?   ?   ?   A . n 
A 1 165 ALA 165 165 ?   ?   ?   A . n 
A 1 166 TYR 166 166 ?   ?   ?   A . n 
A 1 167 LEU 167 167 ?   ?   ?   A . n 
A 1 168 ALA 168 168 ?   ?   ?   A . n 
A 1 169 SER 169 169 ?   ?   ?   A . n 
A 1 170 SER 170 170 ?   ?   ?   A . n 
A 1 171 PRO 171 171 ?   ?   ?   A . n 
A 1 172 ASP 172 172 ?   ?   ?   A . n 
A 1 173 SER 173 173 ?   ?   ?   A . n 
A 1 174 THR 174 174 ?   ?   ?   A . n 
A 1 175 THR 175 175 ?   ?   ?   A . n 
A 1 176 PRO 176 176 ?   ?   ?   A . n 
A 1 177 VAL 177 177 ?   ?   ?   A . n 
A 1 178 SER 178 178 ?   ?   ?   A . n 
A 1 179 ALA 179 179 ?   ?   ?   A . n 
A 1 180 THR 180 180 ?   ?   ?   A . n 
A 1 181 THR 181 181 ?   ?   ?   A . n 
A 1 182 ARG 182 182 ?   ?   ?   A . n 
A 1 183 ALA 183 183 ?   ?   ?   A . n 
A 1 184 PRO 184 184 ?   ?   ?   A . n 
A 1 185 PRO 185 185 ?   ?   ?   A . n 
A 1 186 LEU 186 186 ?   ?   ?   A . n 
A 1 187 THR 187 187 ?   ?   ?   A . n 
A 1 188 SER 188 188 ?   ?   ?   A . n 
A 1 189 MET 189 189 ?   ?   ?   A . n 
A 1 190 ALA 190 190 ?   ?   ?   A . n 
A 1 191 ARG 191 191 ?   ?   ?   A . n 
A 1 192 LYS 192 192 ?   ?   ?   A . n 
A 1 193 THR 193 193 ?   ?   ?   A . n 
A 1 194 LYS 194 194 ?   ?   ?   A . n 
A 1 195 LYS 195 195 ?   ?   ?   A . n 
A 1 196 ILE 196 196 ?   ?   ?   A . n 
A 1 197 CYS 197 197 ?   ?   ?   A . n 
A 1 198 ILE 198 198 ?   ?   ?   A . n 
A 1 199 THR 199 199 ?   ?   ?   A . n 
A 1 200 GLU 200 200 ?   ?   ?   A . n 
A 1 201 VAL 201 201 ?   ?   ?   A . n 
A 1 202 TYR 202 202 ?   ?   ?   A . n 
A 1 203 THR 203 203 ?   ?   ?   A . n 
A 1 204 GLU 204 204 ?   ?   ?   A . n 
A 1 205 PRO 205 205 ?   ?   ?   A . n 
A 1 206 ILE 206 206 ?   ?   ?   A . n 
A 1 207 THR 207 207 ?   ?   ?   A . n 
A 1 208 MET 208 208 ?   ?   ?   A . n 
A 1 209 ALA 209 209 ?   ?   ?   A . n 
A 1 210 THR 210 210 ?   ?   ?   A . n 
A 1 211 GLU 211 211 ?   ?   ?   A . n 
A 1 212 THR 212 212 ?   ?   ?   A . n 
A 1 213 GLU 213 213 ?   ?   ?   A . n 
A 1 214 ALA 214 214 ?   ?   ?   A . n 
A 1 215 PHE 215 215 ?   ?   ?   A . n 
A 1 216 VAL 216 216 ?   ?   ?   A . n 
A 1 217 ALA 217 217 ?   ?   ?   A . n 
A 1 218 SER 218 218 ?   ?   ?   A . n 
A 1 219 GLY 219 219 ?   ?   ?   A . n 
A 1 220 ALA 220 220 ?   ?   ?   A . n 
A 1 221 ALA 221 221 ?   ?   ?   A . n 
A 1 222 PHE 222 222 ?   ?   ?   A . n 
A 1 223 LYS 223 223 ?   ?   ?   A . n 
A 1 224 ASN 224 224 ?   ?   ?   A . n 
A 1 225 GLU 225 225 ?   ?   ?   A . n 
A 1 226 ALA 226 226 ?   ?   ?   A . n 
A 1 227 ALA 227 227 ?   ?   ?   A . n 
A 1 228 GLY 228 228 ?   ?   ?   A . n 
A 1 229 PHE 229 229 ?   ?   ?   A . n 
A 1 230 GLY 230 230 ?   ?   ?   A . n 
A 1 231 GLY 231 231 ?   ?   ?   A . n 
A 1 232 VAL 232 232 ?   ?   ?   A . n 
A 1 233 PRO 233 233 ?   ?   ?   A . n 
A 1 234 THR 234 234 ?   ?   ?   A . n 
A 1 235 ALA 235 235 ?   ?   ?   A . n 
A 1 236 LEU 236 236 ?   ?   ?   A . n 
A 1 237 LEU 237 237 ?   ?   ?   A . n 
A 1 238 VAL 238 238 ?   ?   ?   A . n 
A 1 239 LEU 239 239 ?   ?   ?   A . n 
A 1 240 ALA 240 240 ?   ?   ?   A . n 
A 1 241 LEU 241 241 ?   ?   ?   A . n 
A 1 242 LEU 242 242 ?   ?   ?   A . n 
A 1 243 PHE 243 243 ?   ?   ?   A . n 
A 1 244 PHE 244 244 ?   ?   ?   A . n 
A 1 245 GLY 245 245 ?   ?   ?   A . n 
A 1 246 ALA 246 246 ?   ?   ?   A . n 
A 1 247 ALA 247 247 ?   ?   ?   A . n 
A 1 248 ALA 248 248 ?   ?   ?   A . n 
A 1 249 VAL 249 249 ?   ?   ?   A . n 
A 1 250 LEU 250 250 ?   ?   ?   A . n 
A 1 251 ALA 251 251 ?   ?   ?   A . n 
A 1 252 VAL 252 252 ?   ?   ?   A . n 
A 1 253 CYS 253 253 ?   ?   ?   A . n 
A 1 254 TYR 254 254 ?   ?   ?   A . n 
A 1 255 VAL 255 255 ?   ?   ?   A . n 
A 1 256 LYS 256 256 ?   ?   ?   A . n 
A 1 257 ARG 257 257 ?   ?   ?   A . n 
A 1 258 TYR 258 258 ?   ?   ?   A . n 
A 1 259 VAL 259 259 ?   ?   ?   A . n 
A 1 260 LYS 260 260 ?   ?   ?   A . n 
A 1 261 ALA 261 261 ?   ?   ?   A . n 
A 1 262 PHE 262 262 ?   ?   ?   A . n 
A 1 263 PRO 263 263 ?   ?   ?   A . n 
A 1 264 PHE 264 264 ?   ?   ?   A . n 
A 1 265 THR 265 265 ?   ?   ?   A . n 
A 1 266 THR 266 266 ?   ?   ?   A . n 
A 1 267 LYS 267 267 ?   ?   ?   A . n 
A 1 268 ASN 268 268 ?   ?   ?   A . n 
A 1 269 GLN 269 269 ?   ?   ?   A . n 
A 1 270 GLN 270 270 ?   ?   ?   A . n 
A 1 271 LYS 271 271 ?   ?   ?   A . n 
A 1 272 GLU 272 272 ?   ?   ?   A . n 
A 1 273 MET 273 273 ?   ?   ?   A . n 
A 1 274 ILE 274 274 ?   ?   ?   A . n 
A 1 275 GLU 275 275 ?   ?   ?   A . n 
A 1 276 THR 276 276 ?   ?   ?   A . n 
A 1 277 LYS 277 277 ?   ?   ?   A . n 
A 1 278 VAL 278 278 ?   ?   ?   A . n 
A 1 279 VAL 279 279 ?   ?   ?   A . n 
A 1 280 LYS 280 280 ?   ?   ?   A . n 
A 1 281 GLU 281 281 ?   ?   ?   A . n 
A 1 282 GLU 282 282 ?   ?   ?   A . n 
A 1 283 LYS 283 283 ?   ?   ?   A . n 
A 1 284 ALA 284 284 ?   ?   ?   A . n 
A 1 285 ASP 285 285 ?   ?   ?   A . n 
A 1 286 ASP 286 286 ?   ?   ?   A . n 
A 1 287 VAL 287 287 ?   ?   ?   A . n 
A 1 288 ASN 288 288 ?   ?   ?   A . n 
A 1 289 ALA 289 289 ?   ?   ?   A . n 
A 1 290 ASN 290 290 ?   ?   ?   A . n 
A 1 291 GLU 291 291 ?   ?   ?   A . n 
A 1 292 GLU 292 292 ?   ?   ?   A . n 
A 1 293 SER 293 293 ?   ?   ?   A . n 
A 1 294 LYS 294 294 ?   ?   ?   A . n 
A 1 295 LYS 295 295 ?   ?   ?   A . n 
A 1 296 THR 296 296 ?   ?   ?   A . n 
A 1 297 ILE 297 297 ?   ?   ?   A . n 
A 1 298 LYS 298 298 ?   ?   ?   A . n 
A 1 299 ASN 299 299 ?   ?   ?   A . n 
A 1 300 PRO 300 300 ?   ?   ?   A . n 
A 1 301 GLU 301 301 ?   ?   ?   A . n 
A 1 302 GLU 302 302 ?   ?   ?   A . n 
A 1 303 ALA 303 303 ?   ?   ?   A . n 
A 1 304 LYS 304 304 ?   ?   ?   A . n 
A 1 305 SER 305 305 ?   ?   ?   A . n 
A 1 306 PRO 306 306 ?   ?   ?   A . n 
A 1 307 PRO 307 307 ?   ?   ?   A . n 
A 1 308 LYS 308 308 ?   ?   ?   A . n 
A 1 309 THR 309 309 ?   ?   ?   A . n 
A 1 310 THR 310 310 ?   ?   ?   A . n 
A 1 311 VAL 311 311 ?   ?   ?   A . n 
A 1 312 ARG 312 312 ?   ?   ?   A . n 
A 1 313 CYS 313 313 ?   ?   ?   A . n 
A 1 314 LEU 314 314 ?   ?   ?   A . n 
A 1 315 GLU 315 315 ?   ?   ?   A . n 
A 1 316 ALA 316 316 ?   ?   ?   A . n 
A 1 317 GLU 317 317 ?   ?   ?   A . n 
A 1 318 VAL 318 318 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 BDP 1 C BDP 1 C BDP 1174 n 
B 2 NAG 2 C NAG 2 C NAG 1175 n 
B 2 BDP 3 C BDP 3 C BDP 1176 n 
B 2 NAG 4 C NAG 4 C NAG 1177 n 
B 2 BDP 5 C BDP 5 C BDP 1178 n 
B 2 NAG 6 C NAG 6 C NAG 1179 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 BDP ? ? BDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 NAG 1   401 201 NAG NAG A . 
D 3 NAG 1   402 202 NAG NAG A . 
E 4 GOL 1   403 1   GOL GOL A . 
F 5 PEG 1   404 1   PEG PEG A . 
G 5 PEG 1   405 2   PEG PEG A . 
H 5 PEG 1   406 3   PEG PEG A . 
I 6 CL  1   407 1   CL  CL  A . 
J 7 HOH 1   501 43  HOH HOH A . 
J 7 HOH 2   502 161 HOH HOH A . 
J 7 HOH 3   503 124 HOH HOH A . 
J 7 HOH 4   504 158 HOH HOH A . 
J 7 HOH 5   505 125 HOH HOH A . 
J 7 HOH 6   506 160 HOH HOH A . 
J 7 HOH 7   507 101 HOH HOH A . 
J 7 HOH 8   508 71  HOH HOH A . 
J 7 HOH 9   509 92  HOH HOH A . 
J 7 HOH 10  510 103 HOH HOH A . 
J 7 HOH 11  511 58  HOH HOH A . 
J 7 HOH 12  512 13  HOH HOH A . 
J 7 HOH 13  513 142 HOH HOH A . 
J 7 HOH 14  514 166 HOH HOH A . 
J 7 HOH 15  515 9   HOH HOH A . 
J 7 HOH 16  516 22  HOH HOH A . 
J 7 HOH 17  517 73  HOH HOH A . 
J 7 HOH 18  518 48  HOH HOH A . 
J 7 HOH 19  519 38  HOH HOH A . 
J 7 HOH 20  520 97  HOH HOH A . 
J 7 HOH 21  521 54  HOH HOH A . 
J 7 HOH 22  522 162 HOH HOH A . 
J 7 HOH 23  523 12  HOH HOH A . 
J 7 HOH 24  524 1   HOH HOH A . 
J 7 HOH 25  525 129 HOH HOH A . 
J 7 HOH 26  526 104 HOH HOH A . 
J 7 HOH 27  527 6   HOH HOH A . 
J 7 HOH 28  528 139 HOH HOH A . 
J 7 HOH 29  529 113 HOH HOH A . 
J 7 HOH 30  530 74  HOH HOH A . 
J 7 HOH 31  531 53  HOH HOH A . 
J 7 HOH 32  532 50  HOH HOH A . 
J 7 HOH 33  533 2   HOH HOH A . 
J 7 HOH 34  534 16  HOH HOH A . 
J 7 HOH 35  535 27  HOH HOH A . 
J 7 HOH 36  536 8   HOH HOH A . 
J 7 HOH 37  537 148 HOH HOH A . 
J 7 HOH 38  538 7   HOH HOH A . 
J 7 HOH 39  539 40  HOH HOH A . 
J 7 HOH 40  540 4   HOH HOH A . 
J 7 HOH 41  541 19  HOH HOH A . 
J 7 HOH 42  542 119 HOH HOH A . 
J 7 HOH 43  543 49  HOH HOH A . 
J 7 HOH 44  544 174 HOH HOH A . 
J 7 HOH 45  545 57  HOH HOH A . 
J 7 HOH 46  546 21  HOH HOH A . 
J 7 HOH 47  547 72  HOH HOH A . 
J 7 HOH 48  548 35  HOH HOH A . 
J 7 HOH 49  549 51  HOH HOH A . 
J 7 HOH 50  550 52  HOH HOH A . 
J 7 HOH 51  551 81  HOH HOH A . 
J 7 HOH 52  552 10  HOH HOH A . 
J 7 HOH 53  553 11  HOH HOH A . 
J 7 HOH 54  554 44  HOH HOH A . 
J 7 HOH 55  555 20  HOH HOH A . 
J 7 HOH 56  556 91  HOH HOH A . 
J 7 HOH 57  557 96  HOH HOH A . 
J 7 HOH 58  558 60  HOH HOH A . 
J 7 HOH 59  559 68  HOH HOH A . 
J 7 HOH 60  560 31  HOH HOH A . 
J 7 HOH 61  561 87  HOH HOH A . 
J 7 HOH 62  562 26  HOH HOH A . 
J 7 HOH 63  563 30  HOH HOH A . 
J 7 HOH 64  564 32  HOH HOH A . 
J 7 HOH 65  565 15  HOH HOH A . 
J 7 HOH 66  566 175 HOH HOH A . 
J 7 HOH 67  567 29  HOH HOH A . 
J 7 HOH 68  568 94  HOH HOH A . 
J 7 HOH 69  569 99  HOH HOH A . 
J 7 HOH 70  570 108 HOH HOH A . 
J 7 HOH 71  571 168 HOH HOH A . 
J 7 HOH 72  572 86  HOH HOH A . 
J 7 HOH 73  573 122 HOH HOH A . 
J 7 HOH 74  574 106 HOH HOH A . 
J 7 HOH 75  575 138 HOH HOH A . 
J 7 HOH 76  576 24  HOH HOH A . 
J 7 HOH 77  577 3   HOH HOH A . 
J 7 HOH 78  578 80  HOH HOH A . 
J 7 HOH 79  579 70  HOH HOH A . 
J 7 HOH 80  580 67  HOH HOH A . 
J 7 HOH 81  581 105 HOH HOH A . 
J 7 HOH 82  582 42  HOH HOH A . 
J 7 HOH 83  583 76  HOH HOH A . 
J 7 HOH 84  584 82  HOH HOH A . 
J 7 HOH 85  585 62  HOH HOH A . 
J 7 HOH 86  586 65  HOH HOH A . 
J 7 HOH 87  587 5   HOH HOH A . 
J 7 HOH 88  588 159 HOH HOH A . 
J 7 HOH 89  589 56  HOH HOH A . 
J 7 HOH 90  590 100 HOH HOH A . 
J 7 HOH 91  591 14  HOH HOH A . 
J 7 HOH 92  592 134 HOH HOH A . 
J 7 HOH 93  593 55  HOH HOH A . 
J 7 HOH 94  594 28  HOH HOH A . 
J 7 HOH 95  595 79  HOH HOH A . 
J 7 HOH 96  596 112 HOH HOH A . 
J 7 HOH 97  597 98  HOH HOH A . 
J 7 HOH 98  598 118 HOH HOH A . 
J 7 HOH 99  599 41  HOH HOH A . 
J 7 HOH 100 600 154 HOH HOH A . 
J 7 HOH 101 601 17  HOH HOH A . 
J 7 HOH 102 602 46  HOH HOH A . 
J 7 HOH 103 603 18  HOH HOH A . 
J 7 HOH 104 604 102 HOH HOH A . 
J 7 HOH 105 605 66  HOH HOH A . 
J 7 HOH 106 606 164 HOH HOH A . 
J 7 HOH 107 607 109 HOH HOH A . 
J 7 HOH 108 608 126 HOH HOH A . 
J 7 HOH 109 609 163 HOH HOH A . 
J 7 HOH 110 610 39  HOH HOH A . 
J 7 HOH 111 611 114 HOH HOH A . 
J 7 HOH 112 612 95  HOH HOH A . 
J 7 HOH 113 613 110 HOH HOH A . 
J 7 HOH 114 614 157 HOH HOH A . 
J 7 HOH 115 615 156 HOH HOH A . 
J 7 HOH 116 616 151 HOH HOH A . 
J 7 HOH 117 617 127 HOH HOH A . 
J 7 HOH 118 618 47  HOH HOH A . 
J 7 HOH 119 619 123 HOH HOH A . 
J 7 HOH 120 620 34  HOH HOH A . 
J 7 HOH 121 621 121 HOH HOH A . 
J 7 HOH 122 622 63  HOH HOH A . 
J 7 HOH 123 623 88  HOH HOH A . 
J 7 HOH 124 624 75  HOH HOH A . 
J 7 HOH 125 625 78  HOH HOH A . 
J 7 HOH 126 626 107 HOH HOH A . 
J 7 HOH 127 627 128 HOH HOH A . 
J 7 HOH 128 628 145 HOH HOH A . 
J 7 HOH 129 629 132 HOH HOH A . 
J 7 HOH 130 630 155 HOH HOH A . 
J 7 HOH 131 631 167 HOH HOH A . 
J 7 HOH 132 632 77  HOH HOH A . 
J 7 HOH 133 633 171 HOH HOH A . 
J 7 HOH 134 634 169 HOH HOH A . 
J 7 HOH 135 635 140 HOH HOH A . 
J 7 HOH 136 636 143 HOH HOH A . 
J 7 HOH 137 637 144 HOH HOH A . 
J 7 HOH 138 638 59  HOH HOH A . 
J 7 HOH 139 639 69  HOH HOH A . 
J 7 HOH 140 640 93  HOH HOH A . 
J 7 HOH 141 641 150 HOH HOH A . 
J 7 HOH 142 642 83  HOH HOH A . 
J 7 HOH 143 643 117 HOH HOH A . 
J 7 HOH 144 644 120 HOH HOH A . 
J 7 HOH 145 645 147 HOH HOH A . 
J 7 HOH 146 646 146 HOH HOH A . 
J 7 HOH 147 647 172 HOH HOH A . 
J 7 HOH 148 648 137 HOH HOH A . 
J 7 HOH 149 649 23  HOH HOH A . 
J 7 HOH 150 650 85  HOH HOH A . 
J 7 HOH 151 651 25  HOH HOH A . 
J 7 HOH 152 652 111 HOH HOH A . 
J 7 HOH 153 653 115 HOH HOH A . 
J 7 HOH 154 654 33  HOH HOH A . 
J 7 HOH 155 655 89  HOH HOH A . 
J 7 HOH 156 656 149 HOH HOH A . 
J 7 HOH 157 657 45  HOH HOH A . 
J 7 HOH 158 658 135 HOH HOH A . 
J 7 HOH 159 659 152 HOH HOH A . 
J 7 HOH 160 660 84  HOH HOH A . 
J 7 HOH 161 661 116 HOH HOH A . 
J 7 HOH 162 662 36  HOH HOH A . 
J 7 HOH 163 663 141 HOH HOH A . 
J 7 HOH 164 664 136 HOH HOH A . 
J 7 HOH 165 665 131 HOH HOH A . 
J 7 HOH 166 666 173 HOH HOH A . 
J 7 HOH 167 667 165 HOH HOH A . 
J 7 HOH 168 668 37  HOH HOH A . 
J 7 HOH 169 669 61  HOH HOH A . 
J 7 HOH 170 670 64  HOH HOH A . 
J 7 HOH 171 671 170 HOH HOH A . 
J 7 HOH 172 672 90  HOH HOH A . 
J 7 HOH 173 673 133 HOH HOH A . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     C 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     BDP 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O1 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    B 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    BDP 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O1 
# 
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 ? ? ? 1.21rc1_4899 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .            4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.272 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8OX3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.107 
_cell.length_a_esd                 ? 
_cell.length_b                     56.963 
_cell.length_b_esd                 ? 
_cell.length_c                     30.908 
_cell.length_c_esd                 ? 
_cell.volume                       145526.474 
_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                         8OX3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8OX3 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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              6.5 
_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% PEG5000, 0.1M bis-Tris pH6.5, 18 mg/ml' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-03-10 
_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   0.9686 
_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                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          7.90 
_reflns.entry_id                                       8OX3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.05 
_reflns.d_resolution_low                               46.95 
_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                                     46097 
_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                           83 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.1 
_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                                0.101 
_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                                   1 
_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                                    1.05 
_reflns_shell.d_res_low                                     1.07 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             193 
_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                               1.075 
_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                                  0.4 
_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                               14.03 
_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                                 8OX3 
_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                            1.05 
_refine.ls_d_res_low                             46.90 
_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                     46051 
_refine.ls_number_reflns_R_free                  2211 
_refine.ls_number_reflns_R_work                  43840 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    69.05 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1512 
_refine.ls_R_factor_R_free                       0.1629 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1506 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 18.4149 
_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                            0.0690 
_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                       1.05 
_refine_hist.d_res_low                        46.90 
_refine_hist.number_atoms_solvent             173 
_refine_hist.number_atoms_total               1175 
_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        868 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         134 
_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' ? 0.0117  ? 1065 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1891  ? 1436 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0932  ? 173  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0058  ? 176  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.5972 ? 357  ? f_dihedral_angle_d ? ? 
# 
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' 1.05 1.07  . . 9   275  6.88  . . . . 0.3161 . . . . . . . . . . . 0.4067 
'X-RAY DIFFRACTION' 1.07 1.10  . . 25  541  13.68 . . . . 0.2207 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 1.10 1.13  . . 47  817  21.08 . . . . 0.1781 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 1.13 1.16  . . 76  1180 30.10 . . . . 0.1674 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 1.16 1.19  . . 80  1632 41.20 . . . . 0.1562 . . . . . . . . . . . 0.1674 
'X-RAY DIFFRACTION' 1.19 1.23  . . 99  2160 54.41 . . . . 0.1515 . . . . . . . . . . . 0.1438 
'X-RAY DIFFRACTION' 1.23 1.27  . . 128 2961 74.33 . . . . 0.1534 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 1.27 1.32  . . 196 3684 93.09 . . . . 0.1552 . . . . . . . . . . . 0.1668 
'X-RAY DIFFRACTION' 1.32 1.38  . . 194 3690 93.73 . . . . 0.1554 . . . . . . . . . . . 0.1740 
'X-RAY DIFFRACTION' 1.38 1.46  . . 171 3747 94.23 . . . . 0.1473 . . . . . . . . . . . 0.1583 
'X-RAY DIFFRACTION' 1.46 1.55  . . 182 3792 95.05 . . . . 0.1435 . . . . . . . . . . . 0.1570 
'X-RAY DIFFRACTION' 1.55 1.67  . . 197 3768 95.40 . . . . 0.1404 . . . . . . . . . . . 0.1614 
'X-RAY DIFFRACTION' 1.67 1.83  . . 205 3827 96.23 . . . . 0.1496 . . . . . . . . . . . 0.1502 
'X-RAY DIFFRACTION' 1.83 2.10  . . 229 3804 96.90 . . . . 0.1463 . . . . . . . . . . . 0.1593 
'X-RAY DIFFRACTION' 2.10 2.65  . . 171 3946 97.84 . . . . 0.1533 . . . . . . . . . . . 0.1544 
'X-RAY DIFFRACTION' 2.65 46.90 . . 202 4016 98.90 . . . . 0.1502 . . . . . . . . . . . 0.1645 
# 
_struct.entry_id                     8OX3 
_struct.title                        
;Structure of the murine LYVE-1 (lymphatic vessel endothelial receptor-1) hyaluronan binding domain bound with octasaccharide hyaluronan.
;
_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        8OX3 
_struct_keywords.text            'Hyaluronan binding, cell migration, lymphatic system, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LYVE1_MOUSE 
_struct_ref.pdbx_db_accession          Q8BHC0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLQHTSLVLLLASIWTTRHPVQGADLVQDLSISTCRIMGVALVGRNKNPQMNFTEANEACKMLGLTLASRDQVESAQKSG
FETCSYGWVGEQFSVIPRIFSNPRCGKNGKGVLIWNAPSSQKFKAYCHNSSDTWVNSCIPEIVTTFYPVLDTQTPATEFS
VSSSAYLASSPDSTTPVSATTRAPPLTSMARKTKKICITEVYTEPITMATETEAFVASGAAFKNEAAGFGGVPTALLVLA
LLFFGAAAVLAVCYVKRYVKAFPFTTKNQQKEMIETKVVKEEKADDVNANEESKKTIKNPEEAKSPPKTTVRCLEAEV
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8OX3 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 318 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8BHC0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  318 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       318 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3840 ? 
1 MORE         22   ? 
1 'SSA (A^2)'  6200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'assay for oligomerization' 
_pdbx_struct_assembly_auth_evidence.details                'sedimentation velocity ultracentrifugation' 
# 
_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 ASN A 52  ? LEU A 63  ? ASN A 52  LEU A 63  1 ? 12 
HELX_P HELX_P2 AA2 SER A 69  ? SER A 79  ? SER A 69  SER A 79  1 ? 11 
HELX_P HELX_P3 AA3 CYS A 105 ? GLY A 109 ? CYS A 105 GLY A 109 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 35  SG  ? ? ? 1_555 A CYS 138 SG ? ? A CYS 35  A CYS 138 1_555 ? ? ? ? ? ? ? 2.056 ? ?               
disulf2 disulf ?    ? A CYS 60  SG  ? ? ? 1_555 A CYS 127 SG ? ? A CYS 60  A CYS 127 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf3 disulf ?    ? A CYS 84  SG  ? ? ? 1_555 A CYS 105 SG ? ? A CYS 84  A CYS 105 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
covale1 covale one  ? A ASN 52  ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 52  A NAG 401 1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale2 covale one  ? A ASN 129 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 129 A NAG 402 1_555 ? ? ? ? ? ? ? 1.424 ? N-Glycosylation 
covale3 covale both ? B BDP .   O4  ? ? ? 1_555 B NAG .   C1 ? ? C BDP 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.429 ? ?               
covale4 covale both ? B NAG .   O3  ? ? ? 1_555 B BDP .   C1 ? ? C NAG 2   C BDP 3   1_555 ? ? ? ? ? ? ? 1.431 ? ?               
covale5 covale both ? B BDP .   O4  ? ? ? 1_555 B NAG .   C1 ? ? C BDP 3   C NAG 4   1_555 ? ? ? ? ? ? ? 1.428 ? ?               
covale6 covale both ? B NAG .   O3  ? ? ? 1_555 B BDP .   C1 ? ? C NAG 4   C BDP 5   1_555 ? ? ? ? ? ? ? 1.418 ? ?               
covale7 covale both ? B BDP .   O4  ? ? ? 1_555 B NAG .   C1 ? ? C BDP 5   C NAG 6   1_555 ? ? ? ? ? ? ? 1.435 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG C .  ? ASN A 52  ? NAG A 401 ? 1_555 ASN A 52  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .  ? ASN A 129 ? NAG A 402 ? 1_555 ASN A 129 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 CYS A 35 ? CYS A 138 ? CYS A 35  ? 1_555 CYS A 138 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS A 60 ? CYS A 127 ? CYS A 60  ? 1_555 CYS A 127 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS A 84 ? CYS A 105 ? CYS A 84  ? 1_555 CYS A 105 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASN 
_struct_mon_prot_cis.label_seq_id           48 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASN 
_struct_mon_prot_cis.auth_seq_id            48 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    49 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     49 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.41 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? 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 LEU A 30  ? ILE A 32  ? LEU A 30  ILE A 32  
AA1 2 VAL A 40  ? ARG A 45  ? VAL A 40  ARG A 45  
AA1 3 LYS A 124 ? HIS A 128 ? LYS A 124 HIS A 128 
AA1 4 THR A 66  ? LEU A 67  ? THR A 66  LEU A 67  
AA2 1 LEU A 30  ? ILE A 32  ? LEU A 30  ILE A 32  
AA2 2 VAL A 40  ? ARG A 45  ? VAL A 40  ARG A 45  
AA2 3 LYS A 124 ? HIS A 128 ? LYS A 124 HIS A 128 
AA2 4 GLY A 87  ? TRP A 88  ? GLY A 87  TRP A 88  
AA2 5 SER A 94  ? ARG A 98  ? SER A 94  ARG A 98  
AA2 6 GLY A 111 ? TRP A 115 ? GLY A 111 TRP A 115 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER A 31  ? N SER A 31  O GLY A 44  ? O GLY A 44  
AA1 2 3 N VAL A 43  ? N VAL A 43  O ALA A 125 ? O ALA A 125 
AA1 3 4 O HIS A 128 ? O HIS A 128 N THR A 66  ? N THR A 66  
AA2 1 2 N SER A 31  ? N SER A 31  O GLY A 44  ? O GLY A 44  
AA2 2 3 N VAL A 43  ? N VAL A 43  O ALA A 125 ? O ALA A 125 
AA2 3 4 O LYS A 124 ? O LYS A 124 N TRP A 88  ? N TRP A 88  
AA2 4 5 N GLY A 87  ? N GLY A 87  O VAL A 95  ? O VAL A 95  
AA2 5 6 N ARG A 98  ? N ARG A 98  O GLY A 111 ? O GLY A 111 
# 
_pdbx_entry_details.entry_id                   8OX3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O4  A PEG 404 ? ? O A HOH 501 ? ? 2.06 
2 1 O   A HOH 561 ? ? O A HOH 627 ? ? 2.13 
3 1 OD1 A ASN 48  ? ? O A HOH 502 ? ? 2.14 
4 1 O   A HOH 570 ? ? O A HOH 607 ? ? 2.16 
5 1 O   A HOH 528 ? ? O A HOH 637 ? ? 2.16 
6 1 O   A HOH 595 ? ? O A HOH 616 ? ? 2.17 
7 1 O   A HOH 592 ? ? O A HOH 627 ? ? 2.17 
8 1 O   A HOH 504 ? ? O A HOH 617 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 550 ? ? 1_555 O A HOH 575 ? ? 1_556 2.12 
2 1 O A HOH 506 ? ? 1_555 O A HOH 508 ? ? 2_756 2.14 
3 1 O A HOH 503 ? ? 1_555 O A HOH 575 ? ? 2_755 2.15 
# 
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 GLN A 50  ? ? -84.05 -146.90 
2 1 LYS A 124 ? ? -79.91 -167.92 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     656 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   J 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A LEU 2   ? A LEU 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A HIS 4   ? A HIS 4   
5   1 Y 1 A THR 5   ? A THR 5   
6   1 Y 1 A SER 6   ? A SER 6   
7   1 Y 1 A LEU 7   ? A LEU 7   
8   1 Y 1 A VAL 8   ? A VAL 8   
9   1 Y 1 A LEU 9   ? A LEU 9   
10  1 Y 1 A LEU 10  ? A LEU 10  
11  1 Y 1 A LEU 11  ? A LEU 11  
12  1 Y 1 A ALA 12  ? A ALA 12  
13  1 Y 1 A SER 13  ? A SER 13  
14  1 Y 1 A ILE 14  ? A ILE 14  
15  1 Y 1 A TRP 15  ? A TRP 15  
16  1 Y 1 A THR 16  ? A THR 16  
17  1 Y 1 A THR 17  ? A THR 17  
18  1 Y 1 A ARG 18  ? A ARG 18  
19  1 Y 1 A HIS 19  ? A HIS 19  
20  1 Y 1 A PRO 20  ? A PRO 20  
21  1 Y 1 A VAL 21  ? A VAL 21  
22  1 Y 1 A GLN 22  ? A GLN 22  
23  1 Y 1 A GLY 23  ? A GLY 23  
24  1 Y 1 A ALA 24  ? A ALA 24  
25  1 Y 1 A ASP 25  ? A ASP 25  
26  1 Y 1 A LEU 26  ? A LEU 26  
27  1 Y 1 A VAL 27  ? A VAL 27  
28  1 Y 1 A GLN 28  ? A GLN 28  
29  1 Y 1 A ILE 142 ? A ILE 142 
30  1 Y 1 A VAL 143 ? A VAL 143 
31  1 Y 1 A THR 144 ? A THR 144 
32  1 Y 1 A THR 145 ? A THR 145 
33  1 Y 1 A PHE 146 ? A PHE 146 
34  1 Y 1 A TYR 147 ? A TYR 147 
35  1 Y 1 A PRO 148 ? A PRO 148 
36  1 Y 1 A VAL 149 ? A VAL 149 
37  1 Y 1 A LEU 150 ? A LEU 150 
38  1 Y 1 A ASP 151 ? A ASP 151 
39  1 Y 1 A THR 152 ? A THR 152 
40  1 Y 1 A GLN 153 ? A GLN 153 
41  1 Y 1 A THR 154 ? A THR 154 
42  1 Y 1 A PRO 155 ? A PRO 155 
43  1 Y 1 A ALA 156 ? A ALA 156 
44  1 Y 1 A THR 157 ? A THR 157 
45  1 Y 1 A GLU 158 ? A GLU 158 
46  1 Y 1 A PHE 159 ? A PHE 159 
47  1 Y 1 A SER 160 ? A SER 160 
48  1 Y 1 A VAL 161 ? A VAL 161 
49  1 Y 1 A SER 162 ? A SER 162 
50  1 Y 1 A SER 163 ? A SER 163 
51  1 Y 1 A SER 164 ? A SER 164 
52  1 Y 1 A ALA 165 ? A ALA 165 
53  1 Y 1 A TYR 166 ? A TYR 166 
54  1 Y 1 A LEU 167 ? A LEU 167 
55  1 Y 1 A ALA 168 ? A ALA 168 
56  1 Y 1 A SER 169 ? A SER 169 
57  1 Y 1 A SER 170 ? A SER 170 
58  1 Y 1 A PRO 171 ? A PRO 171 
59  1 Y 1 A ASP 172 ? A ASP 172 
60  1 Y 1 A SER 173 ? A SER 173 
61  1 Y 1 A THR 174 ? A THR 174 
62  1 Y 1 A THR 175 ? A THR 175 
63  1 Y 1 A PRO 176 ? A PRO 176 
64  1 Y 1 A VAL 177 ? A VAL 177 
65  1 Y 1 A SER 178 ? A SER 178 
66  1 Y 1 A ALA 179 ? A ALA 179 
67  1 Y 1 A THR 180 ? A THR 180 
68  1 Y 1 A THR 181 ? A THR 181 
69  1 Y 1 A ARG 182 ? A ARG 182 
70  1 Y 1 A ALA 183 ? A ALA 183 
71  1 Y 1 A PRO 184 ? A PRO 184 
72  1 Y 1 A PRO 185 ? A PRO 185 
73  1 Y 1 A LEU 186 ? A LEU 186 
74  1 Y 1 A THR 187 ? A THR 187 
75  1 Y 1 A SER 188 ? A SER 188 
76  1 Y 1 A MET 189 ? A MET 189 
77  1 Y 1 A ALA 190 ? A ALA 190 
78  1 Y 1 A ARG 191 ? A ARG 191 
79  1 Y 1 A LYS 192 ? A LYS 192 
80  1 Y 1 A THR 193 ? A THR 193 
81  1 Y 1 A LYS 194 ? A LYS 194 
82  1 Y 1 A LYS 195 ? A LYS 195 
83  1 Y 1 A ILE 196 ? A ILE 196 
84  1 Y 1 A CYS 197 ? A CYS 197 
85  1 Y 1 A ILE 198 ? A ILE 198 
86  1 Y 1 A THR 199 ? A THR 199 
87  1 Y 1 A GLU 200 ? A GLU 200 
88  1 Y 1 A VAL 201 ? A VAL 201 
89  1 Y 1 A TYR 202 ? A TYR 202 
90  1 Y 1 A THR 203 ? A THR 203 
91  1 Y 1 A GLU 204 ? A GLU 204 
92  1 Y 1 A PRO 205 ? A PRO 205 
93  1 Y 1 A ILE 206 ? A ILE 206 
94  1 Y 1 A THR 207 ? A THR 207 
95  1 Y 1 A MET 208 ? A MET 208 
96  1 Y 1 A ALA 209 ? A ALA 209 
97  1 Y 1 A THR 210 ? A THR 210 
98  1 Y 1 A GLU 211 ? A GLU 211 
99  1 Y 1 A THR 212 ? A THR 212 
100 1 Y 1 A GLU 213 ? A GLU 213 
101 1 Y 1 A ALA 214 ? A ALA 214 
102 1 Y 1 A PHE 215 ? A PHE 215 
103 1 Y 1 A VAL 216 ? A VAL 216 
104 1 Y 1 A ALA 217 ? A ALA 217 
105 1 Y 1 A SER 218 ? A SER 218 
106 1 Y 1 A GLY 219 ? A GLY 219 
107 1 Y 1 A ALA 220 ? A ALA 220 
108 1 Y 1 A ALA 221 ? A ALA 221 
109 1 Y 1 A PHE 222 ? A PHE 222 
110 1 Y 1 A LYS 223 ? A LYS 223 
111 1 Y 1 A ASN 224 ? A ASN 224 
112 1 Y 1 A GLU 225 ? A GLU 225 
113 1 Y 1 A ALA 226 ? A ALA 226 
114 1 Y 1 A ALA 227 ? A ALA 227 
115 1 Y 1 A GLY 228 ? A GLY 228 
116 1 Y 1 A PHE 229 ? A PHE 229 
117 1 Y 1 A GLY 230 ? A GLY 230 
118 1 Y 1 A GLY 231 ? A GLY 231 
119 1 Y 1 A VAL 232 ? A VAL 232 
120 1 Y 1 A PRO 233 ? A PRO 233 
121 1 Y 1 A THR 234 ? A THR 234 
122 1 Y 1 A ALA 235 ? A ALA 235 
123 1 Y 1 A LEU 236 ? A LEU 236 
124 1 Y 1 A LEU 237 ? A LEU 237 
125 1 Y 1 A VAL 238 ? A VAL 238 
126 1 Y 1 A LEU 239 ? A LEU 239 
127 1 Y 1 A ALA 240 ? A ALA 240 
128 1 Y 1 A LEU 241 ? A LEU 241 
129 1 Y 1 A LEU 242 ? A LEU 242 
130 1 Y 1 A PHE 243 ? A PHE 243 
131 1 Y 1 A PHE 244 ? A PHE 244 
132 1 Y 1 A GLY 245 ? A GLY 245 
133 1 Y 1 A ALA 246 ? A ALA 246 
134 1 Y 1 A ALA 247 ? A ALA 247 
135 1 Y 1 A ALA 248 ? A ALA 248 
136 1 Y 1 A VAL 249 ? A VAL 249 
137 1 Y 1 A LEU 250 ? A LEU 250 
138 1 Y 1 A ALA 251 ? A ALA 251 
139 1 Y 1 A VAL 252 ? A VAL 252 
140 1 Y 1 A CYS 253 ? A CYS 253 
141 1 Y 1 A TYR 254 ? A TYR 254 
142 1 Y 1 A VAL 255 ? A VAL 255 
143 1 Y 1 A LYS 256 ? A LYS 256 
144 1 Y 1 A ARG 257 ? A ARG 257 
145 1 Y 1 A TYR 258 ? A TYR 258 
146 1 Y 1 A VAL 259 ? A VAL 259 
147 1 Y 1 A LYS 260 ? A LYS 260 
148 1 Y 1 A ALA 261 ? A ALA 261 
149 1 Y 1 A PHE 262 ? A PHE 262 
150 1 Y 1 A PRO 263 ? A PRO 263 
151 1 Y 1 A PHE 264 ? A PHE 264 
152 1 Y 1 A THR 265 ? A THR 265 
153 1 Y 1 A THR 266 ? A THR 266 
154 1 Y 1 A LYS 267 ? A LYS 267 
155 1 Y 1 A ASN 268 ? A ASN 268 
156 1 Y 1 A GLN 269 ? A GLN 269 
157 1 Y 1 A GLN 270 ? A GLN 270 
158 1 Y 1 A LYS 271 ? A LYS 271 
159 1 Y 1 A GLU 272 ? A GLU 272 
160 1 Y 1 A MET 273 ? A MET 273 
161 1 Y 1 A ILE 274 ? A ILE 274 
162 1 Y 1 A GLU 275 ? A GLU 275 
163 1 Y 1 A THR 276 ? A THR 276 
164 1 Y 1 A LYS 277 ? A LYS 277 
165 1 Y 1 A VAL 278 ? A VAL 278 
166 1 Y 1 A VAL 279 ? A VAL 279 
167 1 Y 1 A LYS 280 ? A LYS 280 
168 1 Y 1 A GLU 281 ? A GLU 281 
169 1 Y 1 A GLU 282 ? A GLU 282 
170 1 Y 1 A LYS 283 ? A LYS 283 
171 1 Y 1 A ALA 284 ? A ALA 284 
172 1 Y 1 A ASP 285 ? A ASP 285 
173 1 Y 1 A ASP 286 ? A ASP 286 
174 1 Y 1 A VAL 287 ? A VAL 287 
175 1 Y 1 A ASN 288 ? A ASN 288 
176 1 Y 1 A ALA 289 ? A ALA 289 
177 1 Y 1 A ASN 290 ? A ASN 290 
178 1 Y 1 A GLU 291 ? A GLU 291 
179 1 Y 1 A GLU 292 ? A GLU 292 
180 1 Y 1 A SER 293 ? A SER 293 
181 1 Y 1 A LYS 294 ? A LYS 294 
182 1 Y 1 A LYS 295 ? A LYS 295 
183 1 Y 1 A THR 296 ? A THR 296 
184 1 Y 1 A ILE 297 ? A ILE 297 
185 1 Y 1 A LYS 298 ? A LYS 298 
186 1 Y 1 A ASN 299 ? A ASN 299 
187 1 Y 1 A PRO 300 ? A PRO 300 
188 1 Y 1 A GLU 301 ? A GLU 301 
189 1 Y 1 A GLU 302 ? A GLU 302 
190 1 Y 1 A ALA 303 ? A ALA 303 
191 1 Y 1 A LYS 304 ? A LYS 304 
192 1 Y 1 A SER 305 ? A SER 305 
193 1 Y 1 A PRO 306 ? A PRO 306 
194 1 Y 1 A PRO 307 ? A PRO 307 
195 1 Y 1 A LYS 308 ? A LYS 308 
196 1 Y 1 A THR 309 ? A THR 309 
197 1 Y 1 A THR 310 ? A THR 310 
198 1 Y 1 A VAL 311 ? A VAL 311 
199 1 Y 1 A ARG 312 ? A ARG 312 
200 1 Y 1 A CYS 313 ? A CYS 313 
201 1 Y 1 A LEU 314 ? A LEU 314 
202 1 Y 1 A GLU 315 ? A GLU 315 
203 1 Y 1 A ALA 316 ? A ALA 316 
204 1 Y 1 A GLU 317 ? A GLU 317 
205 1 Y 1 A VAL 318 ? A VAL 318 
# 
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  
BDP C1   C  N R 74  
BDP C2   C  N R 75  
BDP C3   C  N S 76  
BDP C4   C  N S 77  
BDP C5   C  N S 78  
BDP C6   C  N N 79  
BDP O2   O  N N 80  
BDP O3   O  N N 81  
BDP O4   O  N N 82  
BDP O5   O  N N 83  
BDP O6A  O  N N 84  
BDP O1   O  N N 85  
BDP O6B  O  N N 86  
BDP H1   H  N N 87  
BDP H2   H  N N 88  
BDP H3   H  N N 89  
BDP H4   H  N N 90  
BDP H5   H  N N 91  
BDP HO2  H  N N 92  
BDP HO3  H  N N 93  
BDP HO4  H  N N 94  
BDP HO1  H  N N 95  
BDP HO6B H  N N 96  
CL  CL   CL N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
GLN N    N  N N 112 
GLN CA   C  N S 113 
GLN C    C  N N 114 
GLN O    O  N N 115 
GLN CB   C  N N 116 
GLN CG   C  N N 117 
GLN CD   C  N N 118 
GLN OE1  O  N N 119 
GLN NE2  N  N N 120 
GLN OXT  O  N N 121 
GLN H    H  N N 122 
GLN H2   H  N N 123 
GLN HA   H  N N 124 
GLN HB2  H  N N 125 
GLN HB3  H  N N 126 
GLN HG2  H  N N 127 
GLN HG3  H  N N 128 
GLN HE21 H  N N 129 
GLN HE22 H  N N 130 
GLN HXT  H  N N 131 
GLU N    N  N N 132 
GLU CA   C  N S 133 
GLU C    C  N N 134 
GLU O    O  N N 135 
GLU CB   C  N N 136 
GLU CG   C  N N 137 
GLU CD   C  N N 138 
GLU OE1  O  N N 139 
GLU OE2  O  N N 140 
GLU OXT  O  N N 141 
GLU H    H  N N 142 
GLU H2   H  N N 143 
GLU HA   H  N N 144 
GLU HB2  H  N N 145 
GLU HB3  H  N N 146 
GLU HG2  H  N N 147 
GLU HG3  H  N N 148 
GLU HE2  H  N N 149 
GLU HXT  H  N N 150 
GLY N    N  N N 151 
GLY CA   C  N N 152 
GLY C    C  N N 153 
GLY O    O  N N 154 
GLY OXT  O  N N 155 
GLY H    H  N N 156 
GLY H2   H  N N 157 
GLY HA2  H  N N 158 
GLY HA3  H  N N 159 
GLY HXT  H  N N 160 
GOL C1   C  N N 161 
GOL O1   O  N N 162 
GOL C2   C  N N 163 
GOL O2   O  N N 164 
GOL C3   C  N N 165 
GOL O3   O  N N 166 
GOL H11  H  N N 167 
GOL H12  H  N N 168 
GOL HO1  H  N N 169 
GOL H2   H  N N 170 
GOL HO2  H  N N 171 
GOL H31  H  N N 172 
GOL H32  H  N N 173 
GOL HO3  H  N N 174 
HIS N    N  N N 175 
HIS CA   C  N S 176 
HIS C    C  N N 177 
HIS O    O  N N 178 
HIS CB   C  N N 179 
HIS CG   C  Y N 180 
HIS ND1  N  Y N 181 
HIS CD2  C  Y N 182 
HIS CE1  C  Y N 183 
HIS NE2  N  Y N 184 
HIS OXT  O  N N 185 
HIS H    H  N N 186 
HIS H2   H  N N 187 
HIS HA   H  N N 188 
HIS HB2  H  N N 189 
HIS HB3  H  N N 190 
HIS HD1  H  N N 191 
HIS HD2  H  N N 192 
HIS HE1  H  N N 193 
HIS HE2  H  N N 194 
HIS HXT  H  N N 195 
HOH O    O  N N 196 
HOH H1   H  N N 197 
HOH H2   H  N N 198 
ILE N    N  N N 199 
ILE CA   C  N S 200 
ILE C    C  N N 201 
ILE O    O  N N 202 
ILE CB   C  N S 203 
ILE CG1  C  N N 204 
ILE CG2  C  N N 205 
ILE CD1  C  N N 206 
ILE OXT  O  N N 207 
ILE H    H  N N 208 
ILE H2   H  N N 209 
ILE HA   H  N N 210 
ILE HB   H  N N 211 
ILE HG12 H  N N 212 
ILE HG13 H  N N 213 
ILE HG21 H  N N 214 
ILE HG22 H  N N 215 
ILE HG23 H  N N 216 
ILE HD11 H  N N 217 
ILE HD12 H  N N 218 
ILE HD13 H  N N 219 
ILE HXT  H  N N 220 
LEU N    N  N N 221 
LEU CA   C  N S 222 
LEU C    C  N N 223 
LEU O    O  N N 224 
LEU CB   C  N N 225 
LEU CG   C  N N 226 
LEU CD1  C  N N 227 
LEU CD2  C  N N 228 
LEU OXT  O  N N 229 
LEU H    H  N N 230 
LEU H2   H  N N 231 
LEU HA   H  N N 232 
LEU HB2  H  N N 233 
LEU HB3  H  N N 234 
LEU HG   H  N N 235 
LEU HD11 H  N N 236 
LEU HD12 H  N N 237 
LEU HD13 H  N N 238 
LEU HD21 H  N N 239 
LEU HD22 H  N N 240 
LEU HD23 H  N N 241 
LEU HXT  H  N N 242 
LYS N    N  N N 243 
LYS CA   C  N S 244 
LYS C    C  N N 245 
LYS O    O  N N 246 
LYS CB   C  N N 247 
LYS CG   C  N N 248 
LYS CD   C  N N 249 
LYS CE   C  N N 250 
LYS NZ   N  N N 251 
LYS OXT  O  N N 252 
LYS H    H  N N 253 
LYS H2   H  N N 254 
LYS HA   H  N N 255 
LYS HB2  H  N N 256 
LYS HB3  H  N N 257 
LYS HG2  H  N N 258 
LYS HG3  H  N N 259 
LYS HD2  H  N N 260 
LYS HD3  H  N N 261 
LYS HE2  H  N N 262 
LYS HE3  H  N N 263 
LYS HZ1  H  N N 264 
LYS HZ2  H  N N 265 
LYS HZ3  H  N N 266 
LYS HXT  H  N N 267 
MET N    N  N N 268 
MET CA   C  N S 269 
MET C    C  N N 270 
MET O    O  N N 271 
MET CB   C  N N 272 
MET CG   C  N N 273 
MET SD   S  N N 274 
MET CE   C  N N 275 
MET OXT  O  N N 276 
MET H    H  N N 277 
MET H2   H  N N 278 
MET HA   H  N N 279 
MET HB2  H  N N 280 
MET HB3  H  N N 281 
MET HG2  H  N N 282 
MET HG3  H  N N 283 
MET HE1  H  N N 284 
MET HE2  H  N N 285 
MET HE3  H  N N 286 
MET HXT  H  N N 287 
NAG C1   C  N R 288 
NAG C2   C  N R 289 
NAG C3   C  N R 290 
NAG C4   C  N S 291 
NAG C5   C  N R 292 
NAG C6   C  N N 293 
NAG C7   C  N N 294 
NAG C8   C  N N 295 
NAG N2   N  N N 296 
NAG O1   O  N N 297 
NAG O3   O  N N 298 
NAG O4   O  N N 299 
NAG O5   O  N N 300 
NAG O6   O  N N 301 
NAG O7   O  N N 302 
NAG H1   H  N N 303 
NAG H2   H  N N 304 
NAG H3   H  N N 305 
NAG H4   H  N N 306 
NAG H5   H  N N 307 
NAG H61  H  N N 308 
NAG H62  H  N N 309 
NAG H81  H  N N 310 
NAG H82  H  N N 311 
NAG H83  H  N N 312 
NAG HN2  H  N N 313 
NAG HO1  H  N N 314 
NAG HO3  H  N N 315 
NAG HO4  H  N N 316 
NAG HO6  H  N N 317 
PEG C1   C  N N 318 
PEG O1   O  N N 319 
PEG C2   C  N N 320 
PEG O2   O  N N 321 
PEG C3   C  N N 322 
PEG C4   C  N N 323 
PEG O4   O  N N 324 
PEG H11  H  N N 325 
PEG H12  H  N N 326 
PEG HO1  H  N N 327 
PEG H21  H  N N 328 
PEG H22  H  N N 329 
PEG H31  H  N N 330 
PEG H32  H  N N 331 
PEG H41  H  N N 332 
PEG H42  H  N N 333 
PEG HO4  H  N N 334 
PHE N    N  N N 335 
PHE CA   C  N S 336 
PHE C    C  N N 337 
PHE O    O  N N 338 
PHE CB   C  N N 339 
PHE CG   C  Y N 340 
PHE CD1  C  Y N 341 
PHE CD2  C  Y N 342 
PHE CE1  C  Y N 343 
PHE CE2  C  Y N 344 
PHE CZ   C  Y N 345 
PHE OXT  O  N N 346 
PHE H    H  N N 347 
PHE H2   H  N N 348 
PHE HA   H  N N 349 
PHE HB2  H  N N 350 
PHE HB3  H  N N 351 
PHE HD1  H  N N 352 
PHE HD2  H  N N 353 
PHE HE1  H  N N 354 
PHE HE2  H  N N 355 
PHE HZ   H  N N 356 
PHE HXT  H  N N 357 
PRO N    N  N N 358 
PRO CA   C  N S 359 
PRO C    C  N N 360 
PRO O    O  N N 361 
PRO CB   C  N N 362 
PRO CG   C  N N 363 
PRO CD   C  N N 364 
PRO OXT  O  N N 365 
PRO H    H  N N 366 
PRO HA   H  N N 367 
PRO HB2  H  N N 368 
PRO HB3  H  N N 369 
PRO HG2  H  N N 370 
PRO HG3  H  N N 371 
PRO HD2  H  N N 372 
PRO HD3  H  N N 373 
PRO HXT  H  N N 374 
SER N    N  N N 375 
SER CA   C  N S 376 
SER C    C  N N 377 
SER O    O  N N 378 
SER CB   C  N N 379 
SER OG   O  N N 380 
SER OXT  O  N N 381 
SER H    H  N N 382 
SER H2   H  N N 383 
SER HA   H  N N 384 
SER HB2  H  N N 385 
SER HB3  H  N N 386 
SER HG   H  N N 387 
SER HXT  H  N N 388 
THR N    N  N N 389 
THR CA   C  N S 390 
THR C    C  N N 391 
THR O    O  N N 392 
THR CB   C  N R 393 
THR OG1  O  N N 394 
THR CG2  C  N N 395 
THR OXT  O  N N 396 
THR H    H  N N 397 
THR H2   H  N N 398 
THR HA   H  N N 399 
THR HB   H  N N 400 
THR HG1  H  N N 401 
THR HG21 H  N N 402 
THR HG22 H  N N 403 
THR HG23 H  N N 404 
THR HXT  H  N N 405 
TRP N    N  N N 406 
TRP CA   C  N S 407 
TRP C    C  N N 408 
TRP O    O  N N 409 
TRP CB   C  N N 410 
TRP CG   C  Y N 411 
TRP CD1  C  Y N 412 
TRP CD2  C  Y N 413 
TRP NE1  N  Y N 414 
TRP CE2  C  Y N 415 
TRP CE3  C  Y N 416 
TRP CZ2  C  Y N 417 
TRP CZ3  C  Y N 418 
TRP CH2  C  Y N 419 
TRP OXT  O  N N 420 
TRP H    H  N N 421 
TRP H2   H  N N 422 
TRP HA   H  N N 423 
TRP HB2  H  N N 424 
TRP HB3  H  N N 425 
TRP HD1  H  N N 426 
TRP HE1  H  N N 427 
TRP HE3  H  N N 428 
TRP HZ2  H  N N 429 
TRP HZ3  H  N N 430 
TRP HH2  H  N N 431 
TRP HXT  H  N N 432 
TYR N    N  N N 433 
TYR CA   C  N S 434 
TYR C    C  N N 435 
TYR O    O  N N 436 
TYR CB   C  N N 437 
TYR CG   C  Y N 438 
TYR CD1  C  Y N 439 
TYR CD2  C  Y N 440 
TYR CE1  C  Y N 441 
TYR CE2  C  Y N 442 
TYR CZ   C  Y N 443 
TYR OH   O  N N 444 
TYR OXT  O  N N 445 
TYR H    H  N N 446 
TYR H2   H  N N 447 
TYR HA   H  N N 448 
TYR HB2  H  N N 449 
TYR HB3  H  N N 450 
TYR HD1  H  N N 451 
TYR HD2  H  N N 452 
TYR HE1  H  N N 453 
TYR HE2  H  N N 454 
TYR HH   H  N N 455 
TYR HXT  H  N N 456 
VAL N    N  N N 457 
VAL CA   C  N S 458 
VAL C    C  N N 459 
VAL O    O  N N 460 
VAL CB   C  N N 461 
VAL CG1  C  N N 462 
VAL CG2  C  N N 463 
VAL OXT  O  N N 464 
VAL H    H  N N 465 
VAL H2   H  N N 466 
VAL HA   H  N N 467 
VAL HB   H  N N 468 
VAL HG11 H  N N 469 
VAL HG12 H  N N 470 
VAL HG13 H  N N 471 
VAL HG21 H  N N 472 
VAL HG22 H  N N 473 
VAL HG23 H  N N 474 
VAL HXT  H  N N 475 
# 
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  
BDP C1  C2   sing N N 70  
BDP C1  O5   sing N N 71  
BDP C1  O1   sing N N 72  
BDP C1  H1   sing N N 73  
BDP C2  C3   sing N N 74  
BDP C2  O2   sing N N 75  
BDP C2  H2   sing N N 76  
BDP C3  C4   sing N N 77  
BDP C3  O3   sing N N 78  
BDP C3  H3   sing N N 79  
BDP C4  C5   sing N N 80  
BDP C4  O4   sing N N 81  
BDP C4  H4   sing N N 82  
BDP C5  C6   sing N N 83  
BDP C5  O5   sing N N 84  
BDP C5  H5   sing N N 85  
BDP C6  O6A  doub N N 86  
BDP C6  O6B  sing N N 87  
BDP O2  HO2  sing N N 88  
BDP O3  HO3  sing N N 89  
BDP O4  HO4  sing N N 90  
BDP O1  HO1  sing N N 91  
BDP O6B HO6B sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
GLN N   CA   sing N N 106 
GLN N   H    sing N N 107 
GLN N   H2   sing N N 108 
GLN CA  C    sing N N 109 
GLN CA  CB   sing N N 110 
GLN CA  HA   sing N N 111 
GLN C   O    doub N N 112 
GLN C   OXT  sing N N 113 
GLN CB  CG   sing N N 114 
GLN CB  HB2  sing N N 115 
GLN CB  HB3  sing N N 116 
GLN CG  CD   sing N N 117 
GLN CG  HG2  sing N N 118 
GLN CG  HG3  sing N N 119 
GLN CD  OE1  doub N N 120 
GLN CD  NE2  sing N N 121 
GLN NE2 HE21 sing N N 122 
GLN NE2 HE22 sing N N 123 
GLN OXT HXT  sing N N 124 
GLU N   CA   sing N N 125 
GLU N   H    sing N N 126 
GLU N   H2   sing N N 127 
GLU CA  C    sing N N 128 
GLU CA  CB   sing N N 129 
GLU CA  HA   sing N N 130 
GLU C   O    doub N N 131 
GLU C   OXT  sing N N 132 
GLU CB  CG   sing N N 133 
GLU CB  HB2  sing N N 134 
GLU CB  HB3  sing N N 135 
GLU CG  CD   sing N N 136 
GLU CG  HG2  sing N N 137 
GLU CG  HG3  sing N N 138 
GLU CD  OE1  doub N N 139 
GLU CD  OE2  sing N N 140 
GLU OE2 HE2  sing N N 141 
GLU OXT HXT  sing N N 142 
GLY N   CA   sing N N 143 
GLY N   H    sing N N 144 
GLY N   H2   sing N N 145 
GLY CA  C    sing N N 146 
GLY CA  HA2  sing N N 147 
GLY CA  HA3  sing N N 148 
GLY C   O    doub N N 149 
GLY C   OXT  sing N N 150 
GLY OXT HXT  sing N N 151 
GOL C1  O1   sing N N 152 
GOL C1  C2   sing N N 153 
GOL C1  H11  sing N N 154 
GOL C1  H12  sing N N 155 
GOL O1  HO1  sing N N 156 
GOL C2  O2   sing N N 157 
GOL C2  C3   sing N N 158 
GOL C2  H2   sing N N 159 
GOL O2  HO2  sing N N 160 
GOL C3  O3   sing N N 161 
GOL C3  H31  sing N N 162 
GOL C3  H32  sing N N 163 
GOL O3  HO3  sing N N 164 
HIS N   CA   sing N N 165 
HIS N   H    sing N N 166 
HIS N   H2   sing N N 167 
HIS CA  C    sing N N 168 
HIS CA  CB   sing N N 169 
HIS CA  HA   sing N N 170 
HIS C   O    doub N N 171 
HIS C   OXT  sing N N 172 
HIS CB  CG   sing N N 173 
HIS CB  HB2  sing N N 174 
HIS CB  HB3  sing N N 175 
HIS CG  ND1  sing Y N 176 
HIS CG  CD2  doub Y N 177 
HIS ND1 CE1  doub Y N 178 
HIS ND1 HD1  sing N N 179 
HIS CD2 NE2  sing Y N 180 
HIS CD2 HD2  sing N N 181 
HIS CE1 NE2  sing Y N 182 
HIS CE1 HE1  sing N N 183 
HIS NE2 HE2  sing N N 184 
HIS OXT HXT  sing N N 185 
HOH O   H1   sing N N 186 
HOH O   H2   sing N N 187 
ILE N   CA   sing N N 188 
ILE N   H    sing N N 189 
ILE N   H2   sing N N 190 
ILE CA  C    sing N N 191 
ILE CA  CB   sing N N 192 
ILE CA  HA   sing N N 193 
ILE C   O    doub N N 194 
ILE C   OXT  sing N N 195 
ILE CB  CG1  sing N N 196 
ILE CB  CG2  sing N N 197 
ILE CB  HB   sing N N 198 
ILE CG1 CD1  sing N N 199 
ILE CG1 HG12 sing N N 200 
ILE CG1 HG13 sing N N 201 
ILE CG2 HG21 sing N N 202 
ILE CG2 HG22 sing N N 203 
ILE CG2 HG23 sing N N 204 
ILE CD1 HD11 sing N N 205 
ILE CD1 HD12 sing N N 206 
ILE CD1 HD13 sing N N 207 
ILE OXT HXT  sing N N 208 
LEU N   CA   sing N N 209 
LEU N   H    sing N N 210 
LEU N   H2   sing N N 211 
LEU CA  C    sing N N 212 
LEU CA  CB   sing N N 213 
LEU CA  HA   sing N N 214 
LEU C   O    doub N N 215 
LEU C   OXT  sing N N 216 
LEU CB  CG   sing N N 217 
LEU CB  HB2  sing N N 218 
LEU CB  HB3  sing N N 219 
LEU CG  CD1  sing N N 220 
LEU CG  CD2  sing N N 221 
LEU CG  HG   sing N N 222 
LEU CD1 HD11 sing N N 223 
LEU CD1 HD12 sing N N 224 
LEU CD1 HD13 sing N N 225 
LEU CD2 HD21 sing N N 226 
LEU CD2 HD22 sing N N 227 
LEU CD2 HD23 sing N N 228 
LEU OXT HXT  sing N N 229 
LYS N   CA   sing N N 230 
LYS N   H    sing N N 231 
LYS N   H2   sing N N 232 
LYS CA  C    sing N N 233 
LYS CA  CB   sing N N 234 
LYS CA  HA   sing N N 235 
LYS C   O    doub N N 236 
LYS C   OXT  sing N N 237 
LYS CB  CG   sing N N 238 
LYS CB  HB2  sing N N 239 
LYS CB  HB3  sing N N 240 
LYS CG  CD   sing N N 241 
LYS CG  HG2  sing N N 242 
LYS CG  HG3  sing N N 243 
LYS CD  CE   sing N N 244 
LYS CD  HD2  sing N N 245 
LYS CD  HD3  sing N N 246 
LYS CE  NZ   sing N N 247 
LYS CE  HE2  sing N N 248 
LYS CE  HE3  sing N N 249 
LYS NZ  HZ1  sing N N 250 
LYS NZ  HZ2  sing N N 251 
LYS NZ  HZ3  sing N N 252 
LYS OXT HXT  sing N N 253 
MET N   CA   sing N N 254 
MET N   H    sing N N 255 
MET N   H2   sing N N 256 
MET CA  C    sing N N 257 
MET CA  CB   sing N N 258 
MET CA  HA   sing N N 259 
MET C   O    doub N N 260 
MET C   OXT  sing N N 261 
MET CB  CG   sing N N 262 
MET CB  HB2  sing N N 263 
MET CB  HB3  sing N N 264 
MET CG  SD   sing N N 265 
MET CG  HG2  sing N N 266 
MET CG  HG3  sing N N 267 
MET SD  CE   sing N N 268 
MET CE  HE1  sing N N 269 
MET CE  HE2  sing N N 270 
MET CE  HE3  sing N N 271 
MET OXT HXT  sing N N 272 
NAG C1  C2   sing N N 273 
NAG C1  O1   sing N N 274 
NAG C1  O5   sing N N 275 
NAG C1  H1   sing N N 276 
NAG C2  C3   sing N N 277 
NAG C2  N2   sing N N 278 
NAG C2  H2   sing N N 279 
NAG C3  C4   sing N N 280 
NAG C3  O3   sing N N 281 
NAG C3  H3   sing N N 282 
NAG C4  C5   sing N N 283 
NAG C4  O4   sing N N 284 
NAG C4  H4   sing N N 285 
NAG C5  C6   sing N N 286 
NAG C5  O5   sing N N 287 
NAG C5  H5   sing N N 288 
NAG C6  O6   sing N N 289 
NAG C6  H61  sing N N 290 
NAG C6  H62  sing N N 291 
NAG C7  C8   sing N N 292 
NAG C7  N2   sing N N 293 
NAG C7  O7   doub N N 294 
NAG C8  H81  sing N N 295 
NAG C8  H82  sing N N 296 
NAG C8  H83  sing N N 297 
NAG N2  HN2  sing N N 298 
NAG O1  HO1  sing N N 299 
NAG O3  HO3  sing N N 300 
NAG O4  HO4  sing N N 301 
NAG O6  HO6  sing N N 302 
PEG C1  O1   sing N N 303 
PEG C1  C2   sing N N 304 
PEG C1  H11  sing N N 305 
PEG C1  H12  sing N N 306 
PEG O1  HO1  sing N N 307 
PEG C2  O2   sing N N 308 
PEG C2  H21  sing N N 309 
PEG C2  H22  sing N N 310 
PEG O2  C3   sing N N 311 
PEG C3  C4   sing N N 312 
PEG C3  H31  sing N N 313 
PEG C3  H32  sing N N 314 
PEG C4  O4   sing N N 315 
PEG C4  H41  sing N N 316 
PEG C4  H42  sing N N 317 
PEG O4  HO4  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
_em_software.category              'MODEL REFINEMENT' 
_em_software.details               ? 
_em_software.id                    1 
_em_software.image_processing_id   ? 
_em_software.fitting_id            ? 
_em_software.imaging_id            ? 
_em_software.name                  PHENIX 
_em_software.version               1.21rc1_4899 
# 
_pdbx_audit_support.funding_organization   'Medical Research Council (MRC, United Kingdom)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 BDP 1 n 
2 NAG 2 n 
2 BDP 3 n 
2 NAG 4 n 
2 BDP 5 n 
2 NAG 6 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Previously solved apo mLYVE1 structure' 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8OX3 
_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.fract_transf_matrix[1][1]   0.011613 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003390 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017555 
_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]   0.033704 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASP A 1 29  ? 80.20800  42.82600 4.13800   1.000 22.92832 ? 29  ASP A N   1 
ATOM   2    C  CA  . ASP A 1 29  ? 80.96600  41.82900 3.40000   1.000 22.00820 ? 29  ASP A CA  1 
ATOM   3    C  C   . ASP A 1 29  ? 82.43500  41.94800 3.79500   1.000 19.91286 ? 29  ASP A C   1 
ATOM   4    O  O   . ASP A 1 29  ? 82.85100  42.96800 4.34600   1.000 23.00351 ? 29  ASP A O   1 
ATOM   5    C  CB  . ASP A 1 29  ? 80.77300  42.03300 1.89400   1.000 24.19098 ? 29  ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 29  ? 79.33900  41.78900 1.44900   1.000 26.24682 ? 29  ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 29  ? 78.53700  41.29400 2.26700   1.000 27.75222 ? 29  ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 29  ? 79.01100  42.08100 0.28100   1.000 26.45431 ? 29  ASP A OD2 1 
ATOM   9    N  N   . LEU A 1 30  ? 83.21800  40.90700 3.54100   1.000 13.47528 ? 30  LEU A N   1 
ATOM   10   C  CA  . LEU A 1 30  ? 84.63500  40.92600 3.84900   1.000 10.51451 ? 30  LEU A CA  1 
ATOM   11   C  C   . LEU A 1 30  ? 85.42000  41.03300 2.55300   1.000 9.20489  ? 30  LEU A C   1 
ATOM   12   O  O   . LEU A 1 30  ? 84.98200  40.55800 1.50100   1.000 11.35919 ? 30  LEU A O   1 
ATOM   13   C  CB  . LEU A 1 30  ? 85.06100  39.63600 4.55600   1.000 12.07145 ? 30  LEU A CB  1 
ATOM   14   C  CG  . LEU A 1 30  ? 84.59900  39.43600 6.00500   1.000 13.97473 ? 30  LEU A CG  1 
ATOM   15   C  CD1 . LEU A 1 30  ? 84.98500  38.05000 6.49600   1.000 13.89402 ? 30  LEU A CD1 1 
ATOM   16   C  CD2 . LEU A 1 30  ? 85.19100  40.50500 6.90400   1.000 15.44553 ? 30  LEU A CD2 1 
ATOM   17   N  N   A SER A 1 31  ? 86.57300  41.68100 2.63600   0.540 7.35900  ? 31  SER A N   1 
ATOM   18   N  N   B SER A 1 31  ? 86.59200  41.65100 2.63200   0.460 9.76697  ? 31  SER A N   1 
ATOM   19   C  CA  A SER A 1 31  ? 87.56100  41.65300 1.57500   0.540 6.93247  ? 31  SER A CA  1 
ATOM   20   C  CA  B SER A 1 31  ? 87.53800  41.69800 1.52700   0.460 11.53723 ? 31  SER A CA  1 
ATOM   21   C  C   A SER A 1 31  ? 88.47400  40.45900 1.80400   0.540 6.55779  ? 31  SER A C   1 
ATOM   22   C  C   B SER A 1 31  ? 88.56500  40.59300 1.72500   0.460 11.36957 ? 31  SER A C   1 
ATOM   23   O  O   A SER A 1 31  ? 88.87500  40.18000 2.93700   0.540 6.25022  ? 31  SER A O   1 
ATOM   24   O  O   B SER A 1 31  ? 89.18800  40.50800 2.78600   0.460 11.94925 ? 31  SER A O   1 
ATOM   25   C  CB  A SER A 1 31  ? 88.38700  42.93700 1.61000   0.540 9.66859  ? 31  SER A CB  1 
ATOM   26   C  CB  B SER A 1 31  ? 88.24900  43.05000 1.49400   0.460 14.37540 ? 31  SER A CB  1 
ATOM   27   O  OG  A SER A 1 31  ? 89.34500  42.95700 0.56900   0.540 11.99316 ? 31  SER A OG  1 
ATOM   28   O  OG  B SER A 1 31  ? 87.33100  44.10700 1.28400   0.460 16.76752 ? 31  SER A OG  1 
ATOM   29   N  N   A ILE A 1 32  ? 88.79500  39.75300 0.72500   0.540 6.18972  ? 32  ILE A N   1 
ATOM   30   N  N   B ILE A 1 32  ? 88.74300  39.75200 0.70800   0.460 10.36408 ? 32  ILE A N   1 
ATOM   31   C  CA  A ILE A 1 32  ? 89.64900  38.57600 0.79700   0.540 5.90092  ? 32  ILE A CA  1 
ATOM   32   C  CA  B ILE A 1 32  ? 89.65600  38.61900 0.78300   0.460 9.47502  ? 32  ILE A CA  1 
ATOM   33   C  C   A ILE A 1 32  ? 90.60500  38.58800 -0.38700  0.540 6.41478  ? 32  ILE A C   1 
ATOM   34   C  C   B ILE A 1 32  ? 90.63600  38.67100 -0.38000  0.460 9.27178  ? 32  ILE A C   1 
ATOM   35   O  O   A ILE A 1 32  ? 90.24500  39.02300 -1.48600  0.540 6.35796  ? 32  ILE A O   1 
ATOM   36   O  O   B ILE A 1 32  ? 90.32100  39.18500 -1.45800  0.460 11.25445 ? 32  ILE A O   1 
ATOM   37   C  CB  A ILE A 1 32  ? 88.82500  37.27100 0.84300   0.540 6.69528  ? 32  ILE A CB  1 
ATOM   38   C  CB  B ILE A 1 32  ? 88.90900  37.26700 0.78900   0.460 10.22897 ? 32  ILE A CB  1 
ATOM   39   C  CG1 A ILE A 1 32  ? 89.73300  36.08100 1.15300   0.540 7.56595  ? 32  ILE A CG1 1 
ATOM   40   C  CG1 B ILE A 1 32  ? 88.20500  37.03600 -0.55000  0.460 12.16454 ? 32  ILE A CG1 1 
ATOM   41   C  CG2 A ILE A 1 32  ? 88.07600  37.04800 -0.46500  0.540 7.84308  ? 32  ILE A CG2 1 
ATOM   42   C  CG2 B ILE A 1 32  ? 87.91300  37.21000 1.92900   0.460 10.37554 ? 32  ILE A CG2 1 
ATOM   43   C  CD1 A ILE A 1 32  ? 88.98500  34.79100 1.42400   0.540 10.20560 ? 32  ILE A CD1 1 
ATOM   44   C  CD1 B ILE A 1 32  ? 87.62100  35.65600 -0.70300  0.460 13.70406 ? 32  ILE A CD1 1 
ATOM   45   N  N   . SER A 1 33  ? 91.83100  38.12500 -0.15600  1.000 7.13677  ? 33  SER A N   1 
ATOM   46   C  CA  . SER A 1 33  ? 92.76700  37.91100 -1.25000  1.000 7.18978  ? 33  SER A CA  1 
ATOM   47   C  C   . SER A 1 33  ? 92.09100  37.05300 -2.30500  1.000 8.15258  ? 33  SER A C   1 
ATOM   48   O  O   . SER A 1 33  ? 91.48100  36.02900 -1.98900  1.000 9.85771  ? 33  SER A O   1 
ATOM   49   C  CB  . SER A 1 33  ? 93.98800  37.14400 -0.73900  1.000 8.23413  ? 33  SER A CB  1 
ATOM   50   O  OG  . SER A 1 33  ? 94.69800  37.84700 0.25900   1.000 7.90679  ? 33  SER A OG  1 
ATOM   51   N  N   . THR A 1 34  ? 92.19900  37.46700 -3.56400  1.000 9.52044  ? 34  THR A N   1 
ATOM   52   C  CA  . THR A 1 34  ? 91.57900  36.69100 -4.63300  1.000 13.53695 ? 34  THR A CA  1 
ATOM   53   C  C   . THR A 1 34  ? 92.24600  35.33300 -4.78500  1.000 12.30752 ? 34  THR A C   1 
ATOM   54   O  O   . THR A 1 34  ? 91.57000  34.31200 -4.95600  1.000 16.07650 ? 34  THR A O   1 
ATOM   55   C  CB  . THR A 1 34  ? 91.65000  37.47400 -5.94200  1.000 17.52631 ? 34  THR A CB  1 
ATOM   56   O  OG1 . THR A 1 34  ? 91.34600  38.85700 -5.69400  1.000 19.35711 ? 34  THR A OG1 1 
ATOM   57   C  CG2 . THR A 1 34  ? 90.69400  36.89300 -6.97000  1.000 19.12754 ? 34  THR A CG2 1 
ATOM   58   N  N   . CYS A 1 35  ? 93.57000  35.30800 -4.70200  1.000 8.88842  ? 35  CYS A N   1 
ATOM   59   C  CA  . CYS A 1 35  ? 94.37600  34.10900 -4.87900  1.000 8.64798  ? 35  CYS A CA  1 
ATOM   60   C  C   . CYS A 1 35  ? 95.15800  33.88100 -3.59700  1.000 8.38547  ? 35  CYS A C   1 
ATOM   61   O  O   . CYS A 1 35  ? 95.91500  34.75600 -3.15900  1.000 10.08504 ? 35  CYS A O   1 
ATOM   62   C  CB  . CYS A 1 35  ? 95.31300  34.29300 -6.07200  1.000 10.66811 ? 35  CYS A CB  1 
ATOM   63   S  SG  . CYS A 1 35  ? 94.42500  34.70700 -7.59900  1.000 12.56151 ? 35  CYS A SG  1 
ATOM   64   N  N   . ARG A 1 36  ? 94.93300  32.73300 -2.97100  1.000 5.60142  ? 36  ARG A N   1 
ATOM   65   C  CA  . ARG A 1 36  ? 95.61000  32.40600 -1.72900  1.000 5.76521  ? 36  ARG A CA  1 
ATOM   66   C  C   . ARG A 1 36  ? 96.97600  31.82200 -2.03100  1.000 4.68997  ? 36  ARG A C   1 
ATOM   67   O  O   . ARG A 1 36  ? 97.11700  31.00500 -2.93500  1.000 5.58769  ? 36  ARG A O   1 
ATOM   68   C  CB  . ARG A 1 36  ? 94.78100  31.39900 -0.93800  1.000 6.42494  ? 36  ARG A CB  1 
ATOM   69   C  CG  . ARG A 1 36  ? 93.44600  31.98000 -0.48300  1.000 7.38925  ? 36  ARG A CG  1 
ATOM   70   C  CD  . ARG A 1 36  ? 92.56600  30.96400 0.24700   1.000 8.24583  ? 36  ARG A CD  1 
ATOM   71   N  NE  . ARG A 1 36  ? 92.37300  29.76700 -0.54800  1.000 7.34667  ? 36  ARG A NE  1 
ATOM   72   C  CZ  . ARG A 1 36  ? 91.57400  29.67900 -1.60200  1.000 7.94647  ? 36  ARG A CZ  1 
ATOM   73   N  NH1 . ARG A 1 36  ? 90.84800  30.71800 -2.01100  1.000 9.84778  ? 36  ARG A NH1 1 
ATOM   74   N  NH2 . ARG A 1 36  ? 91.49500  28.54200 -2.25500  1.000 7.79976  ? 36  ARG A NH2 1 
ATOM   75   N  N   . ILE A 1 37  ? 97.98100  32.23300 -1.26700  1.000 4.91497  ? 37  ILE A N   1 
ATOM   76   C  CA  . ILE A 1 37  ? 99.35300  31.77800 -1.46600  1.000 4.51549  ? 37  ILE A CA  1 
ATOM   77   C  C   . ILE A 1 37  ? 99.72300  30.91800 -0.26800  1.000 4.67583  ? 37  ILE A C   1 
ATOM   78   O  O   . ILE A 1 37  ? 99.62900  31.37700 0.87700   1.000 5.33807  ? 37  ILE A O   1 
ATOM   79   C  CB  . ILE A 1 37  ? 100.32700 32.95700 -1.61700  1.000 5.91613  ? 37  ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 37  ? 99.86300  33.91800 -2.71400  1.000 8.78355  ? 37  ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 37  ? 101.74900 32.45300 -1.86300  1.000 6.29756  ? 37  ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 37  ? 99.69600  33.29900 -4.04400  1.000 11.85471 ? 37  ILE A CD1 1 
ATOM   83   N  N   . MET A 1 38  ? 100.11100 29.66700 -0.52200  1.000 5.03971  ? 38  MET A N   1 
ATOM   84   C  CA  . MET A 1 38  ? 100.34900 28.71600 0.56400   1.000 5.27071  ? 38  MET A CA  1 
ATOM   85   C  C   . MET A 1 38  ? 99.18100  28.68700 1.54100   1.000 4.84075  ? 38  MET A C   1 
ATOM   86   O  O   . MET A 1 38  ? 99.35700  28.60500 2.75800   1.000 5.54959  ? 38  MET A O   1 
ATOM   87   C  CB  . MET A 1 38  ? 101.70600 28.92500 1.24800   1.000 5.76666  ? 38  MET A CB  1 
ATOM   88   C  CG  . MET A 1 38  ? 102.94300 28.83900 0.33100   1.000 7.47006  ? 38  MET A CG  1 
ATOM   89   S  SD  . MET A 1 38  ? 103.06100 27.20500 -0.45000  1.000 8.43651  ? 38  MET A SD  1 
ATOM   90   C  CE  . MET A 1 38  ? 103.83400 26.33000 0.90800   1.000 10.81703 ? 38  MET A CE  1 
ATOM   91   N  N   . GLY A 1 39  ? 97.96800  28.75100 0.99100   1.000 4.85080  ? 39  GLY A N   1 
ATOM   92   C  CA  . GLY A 1 39  ? 96.78000  28.69400 1.80500   1.000 4.86077  ? 39  GLY A CA  1 
ATOM   93   C  C   . GLY A 1 39  ? 96.40100  29.96800 2.51500   1.000 4.94339  ? 39  GLY A C   1 
ATOM   94   O  O   . GLY A 1 39  ? 95.37900  29.97200 3.20700   1.000 5.50582  ? 39  GLY A O   1 
ATOM   95   N  N   . VAL A 1 40  ? 97.15400  31.03600 2.36900   1.000 4.38563  ? 40  VAL A N   1 
ATOM   96   C  CA  . VAL A 1 40  ? 96.95500  32.24600 3.16000   1.000 4.53689  ? 40  VAL A CA  1 
ATOM   97   C  C   . VAL A 1 40  ? 96.20200  33.29900 2.36600   1.000 4.43154  ? 40  VAL A C   1 
ATOM   98   O  O   . VAL A 1 40  ? 96.49900  33.55200 1.19100   1.000 4.93567  ? 40  VAL A O   1 
ATOM   99   C  CB  . VAL A 1 40  ? 98.29400  32.80500 3.67200   1.000 5.28225  ? 40  VAL A CB  1 
ATOM   100  C  CG1 . VAL A 1 40  ? 98.08700  34.14600 4.38400   1.000 6.24068  ? 40  VAL A CG1 1 
ATOM   101  C  CG2 . VAL A 1 40  ? 98.97700  31.80700 4.57300   1.000 6.34983  ? 40  VAL A CG2 1 
ATOM   102  N  N   . ALA A 1 41  ? 95.24900  33.94000 3.04300   1.000 4.87673  ? 41  ALA A N   1 
ATOM   103  C  CA  . ALA A 1 41  ? 94.55100  35.10300 2.51900   1.000 6.40500  ? 41  ALA A CA  1 
ATOM   104  C  C   . ALA A 1 41  ? 94.59500  36.23200 3.53500   1.000 4.75714  ? 41  ALA A C   1 
ATOM   105  O  O   . ALA A 1 41  ? 94.49800  35.99700 4.74600   1.000 5.70831  ? 41  ALA A O   1 
ATOM   106  C  CB  . ALA A 1 41  ? 93.08300  34.78800 2.23900   1.000 7.31758  ? 41  ALA A CB  1 
ATOM   107  N  N   . LEU A 1 42  ? 94.70400  37.46200 3.03000   1.000 4.81884  ? 42  LEU A N   1 
ATOM   108  C  CA  . LEU A 1 42  ? 94.39800  38.65200 3.81500   1.000 5.12054  ? 42  LEU A CA  1 
ATOM   109  C  C   . LEU A 1 42  ? 92.89100  38.84900 3.82000   1.000 4.98799  ? 42  LEU A C   1 
ATOM   110  O  O   . LEU A 1 42  ? 92.25700  38.86400 2.76000   1.000 5.68205  ? 42  LEU A O   1 
ATOM   111  C  CB  . LEU A 1 42  ? 95.06500  39.87300 3.18000   1.000 5.61506  ? 42  LEU A CB  1 
ATOM   112  C  CG  . LEU A 1 42  ? 94.71600  41.20200 3.85200   1.000 6.48309  ? 42  LEU A CG  1 
ATOM   113  C  CD1 . LEU A 1 42  ? 95.32700  41.27300 5.24200   1.000 6.59208  ? 42  LEU A CD1 1 
ATOM   114  C  CD2 . LEU A 1 42  ? 95.20000  42.35600 3.00800   1.000 7.34438  ? 42  LEU A CD2 1 
ATOM   115  N  N   . VAL A 1 43  ? 92.31800  39.01300 5.00800   1.000 5.04046  ? 43  VAL A N   1 
ATOM   116  C  CA  . VAL A 1 43  ? 90.88600  39.18800 5.18400   1.000 6.11703  ? 43  VAL A CA  1 
ATOM   117  C  C   . VAL A 1 43  ? 90.66800  40.46500 5.98000   1.000 6.31065  ? 43  VAL A C   1 
ATOM   118  O  O   . VAL A 1 43  ? 91.25100  40.64700 7.05400   1.000 7.18521  ? 43  VAL A O   1 
ATOM   119  C  CB  . VAL A 1 43  ? 90.27900  37.97200 5.90600   1.000 6.81992  ? 43  VAL A CB  1 
ATOM   120  C  CG1 . VAL A 1 43  ? 88.83100  38.22800 6.27200   1.000 8.77767  ? 43  VAL A CG1 1 
ATOM   121  C  CG2 . VAL A 1 43  ? 90.39100  36.73400 5.03400   1.000 8.12409  ? 43  VAL A CG2 1 
ATOM   122  N  N   . GLY A 1 44  ? 89.85100  41.36000 5.45200   1.000 6.72506  ? 44  GLY A N   1 
ATOM   123  C  CA  . GLY A 1 44  ? 89.59500  42.61300 6.12900   1.000 8.21499  ? 44  GLY A CA  1 
ATOM   124  C  C   . GLY A 1 44  ? 88.12500  42.96100 6.06000   1.000 9.90611  ? 44  GLY A C   1 
ATOM   125  O  O   . GLY A 1 44  ? 87.38200  42.42900 5.24000   1.000 11.01097 ? 44  GLY A O   1 
ATOM   126  N  N   . ARG A 1 45  ? 87.70700  43.84900 6.95000   1.000 11.41272 ? 45  ARG A N   1 
ATOM   127  C  CA  . ARG A 1 45  ? 86.40200  44.45900 6.78400   1.000 15.92524 ? 45  ARG A CA  1 
ATOM   128  C  C   . ARG A 1 45  ? 86.46100  45.43900 5.62100   1.000 18.60507 ? 45  ARG A C   1 
ATOM   129  O  O   . ARG A 1 45  ? 87.50200  46.02900 5.33400   1.000 18.81634 ? 45  ARG A O   1 
ATOM   130  C  CB  . ARG A 1 45  ? 86.01900  45.20300 8.05600   1.000 19.43972 ? 45  ARG A CB  1 
ATOM   131  C  CG  . ARG A 1 45  ? 85.90800  44.30900 9.27200   1.000 22.81120 ? 45  ARG A CG  1 
ATOM   132  C  CD  . ARG A 1 45  ? 84.48500  43.87400 9.50200   1.000 27.17765 ? 45  ARG A CD  1 
ATOM   133  N  NE  . ARG A 1 45  ? 84.35100  43.04700 10.69600  1.000 30.58865 ? 45  ARG A NE  1 
ATOM   134  C  CZ  . ARG A 1 45  ? 84.28700  43.52600 11.93400  1.000 33.01041 ? 45  ARG A CZ  1 
ATOM   135  N  NH1 . ARG A 1 45  ? 84.34800  44.83300 12.15200  1.000 33.95956 ? 45  ARG A NH1 1 
ATOM   136  N  NH2 . ARG A 1 45  ? 84.16200  42.69500 12.96000  1.000 33.67686 ? 45  ARG A NH2 1 
ATOM   137  N  N   . ASN A 1 46  ? 85.32200  45.61600 4.94700   1.000 24.04156 ? 46  ASN A N   1 
ATOM   138  C  CA  . ASN A 1 46  ? 85.30100  46.47300 3.76600   1.000 29.15335 ? 46  ASN A CA  1 
ATOM   139  C  C   . ASN A 1 46  ? 85.58700  47.93100 4.10300   1.000 31.70890 ? 46  ASN A C   1 
ATOM   140  O  O   . ASN A 1 46  ? 86.09700  48.67200 3.25500   1.000 31.45283 ? 46  ASN A O   1 
ATOM   141  C  CB  . ASN A 1 46  ? 83.96800  46.34400 3.03500   1.000 33.73038 ? 46  ASN A CB  1 
ATOM   142  C  CG  . ASN A 1 46  ? 83.95300  45.19000 2.05700   1.000 37.70654 ? 46  ASN A CG  1 
ATOM   143  O  OD1 . ASN A 1 46  ? 84.98600  44.82200 1.49700   1.000 38.46252 ? 46  ASN A OD1 1 
ATOM   144  N  ND2 . ASN A 1 46  ? 82.77500  44.62300 1.83000   1.000 40.97896 ? 46  ASN A ND2 1 
ATOM   145  N  N   . LYS A 1 47  ? 85.26400  48.36400 5.31900   1.000 34.68173 ? 47  LYS A N   1 
ATOM   146  C  CA  . LYS A 1 47  ? 85.55900  49.71900 5.75700   1.000 37.49575 ? 47  LYS A CA  1 
ATOM   147  C  C   . LYS A 1 47  ? 85.93700  49.68100 7.23200   1.000 35.96234 ? 47  LYS A C   1 
ATOM   148  O  O   . LYS A 1 47  ? 85.63200  48.72200 7.94700   1.000 35.53147 ? 47  LYS A O   1 
ATOM   149  C  CB  . LYS A 1 47  ? 84.37300  50.66600 5.48900   1.000 41.74613 ? 47  LYS A CB  1 
ATOM   150  C  CG  . LYS A 1 47  ? 84.65100  52.14400 5.74600   1.000 45.75690 ? 47  LYS A CG  1 
ATOM   151  C  CD  . LYS A 1 47  ? 83.43100  53.00400 5.45100   1.000 48.76537 ? 47  LYS A CD  1 
ATOM   152  C  CE  . LYS A 1 47  ? 83.17300  53.12600 3.95600   1.000 50.71033 ? 47  LYS A CE  1 
ATOM   153  N  NZ  . LYS A 1 47  ? 84.24000  53.90700 3.26700   1.000 51.39865 ? 47  LYS A NZ  1 
ATOM   154  N  N   . ASN A 1 48  ? 86.63700  50.72200 7.67500   1.000 35.42120 ? 48  ASN A N   1 
ATOM   155  C  CA  . ASN A 1 48  ? 87.00800  50.82600 9.07600   1.000 35.17877 ? 48  ASN A CA  1 
ATOM   156  C  C   . ASN A 1 48  ? 85.75000  50.88100 9.94400   1.000 31.90302 ? 48  ASN A C   1 
ATOM   157  O  O   . ASN A 1 48  ? 84.70300  51.36800 9.50500   1.000 32.05322 ? 48  ASN A O   1 
ATOM   158  C  CB  . ASN A 1 48  ? 87.84600  52.08300 9.29300   1.000 37.47241 ? 48  ASN A CB  1 
ATOM   159  C  CG  . ASN A 1 48  ? 89.28800  51.89100 8.88500   1.000 39.74855 ? 48  ASN A CG  1 
ATOM   160  O  OD1 . ASN A 1 48  ? 89.71100  50.77800 8.57500   1.000 39.87052 ? 48  ASN A OD1 1 
ATOM   161  N  ND2 . ASN A 1 48  ? 90.05300  52.97600 8.87700   1.000 41.20855 ? 48  ASN A ND2 1 
ATOM   162  N  N   . PRO A 1 49  ? 85.82200  50.39300 11.19300  1.000 28.57648 ? 49  PRO A N   1 
ATOM   163  C  CA  . PRO A 1 49  ? 87.02900  49.86700 11.83800  1.000 25.98654 ? 49  PRO A CA  1 
ATOM   164  C  C   . PRO A 1 49  ? 87.33100  48.41400 11.48400  1.000 21.59521 ? 49  PRO A C   1 
ATOM   165  O  O   . PRO A 1 49  ? 86.43700  47.66100 11.09300  1.000 22.49444 ? 49  PRO A O   1 
ATOM   166  C  CB  . PRO A 1 49  ? 86.69300  49.97900 13.32400  1.000 27.82356 ? 49  PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 49  ? 85.22100  49.75900 13.37000  1.000 28.84161 ? 49  PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 49  ? 84.66200  50.37200 12.10400  1.000 28.74156 ? 49  PRO A CD  1 
ATOM   169  N  N   . GLN A 1 50  ? 88.59900  48.02900 11.63000  1.000 16.51586 ? 50  GLN A N   1 
ATOM   170  C  CA  . GLN A 1 50  ? 88.99800  46.64000 11.44300  1.000 13.64051 ? 50  GLN A CA  1 
ATOM   171  C  C   . GLN A 1 50  ? 88.76300  45.85500 12.72800  1.000 12.62001 ? 50  GLN A C   1 
ATOM   172  O  O   . GLN A 1 50  ? 87.81900  46.14900 13.46400  1.000 13.58400 ? 50  GLN A O   1 
ATOM   173  C  CB  . GLN A 1 50  ? 90.43100  46.54800 10.91700  1.000 12.64523 ? 50  GLN A CB  1 
ATOM   174  C  CG  . GLN A 1 50  ? 90.59800  47.18900 9.54800   1.000 13.66558 ? 50  GLN A CG  1 
ATOM   175  C  CD  . GLN A 1 50  ? 89.73900  46.52700 8.48600   1.000 13.21128 ? 50  GLN A CD  1 
ATOM   176  O  OE1 . GLN A 1 50  ? 89.48300  45.32100 8.54200   1.000 13.07297 ? 50  GLN A OE1 1 
ATOM   177  N  NE2 . GLN A 1 50  ? 89.30700  47.30400 7.50100   1.000 15.49913 ? 50  GLN A NE2 1 
ATOM   178  N  N   . MET A 1 51  ? 89.59800  44.86300 13.02100  1.000 10.36270 ? 51  MET A N   1 
ATOM   179  C  CA  . MET A 1 51  ? 89.16600  43.76200 13.87000  1.000 10.01735 ? 51  MET A CA  1 
ATOM   180  C  C   . MET A 1 51  ? 90.15900  43.58200 15.00800  1.000 9.96308  ? 51  MET A C   1 
ATOM   181  O  O   . MET A 1 51  ? 91.37100  43.55900 14.77300  1.000 9.57698  ? 51  MET A O   1 
ATOM   182  C  CB  . MET A 1 51  ? 89.18900  42.54100 12.96900  1.000 10.77841 ? 51  MET A CB  1 
ATOM   183  C  CG  . MET A 1 51  ? 87.96600  42.45600 12.08800  1.000 11.39138 ? 51  MET A CG  1 
ATOM   184  S  SD  . MET A 1 51  ? 88.02000  41.05300 10.97900  1.000 11.33303 ? 51  MET A SD  1 
ATOM   185  C  CE  . MET A 1 51  ? 89.34300  41.60100 9.90600   1.000 12.27444 ? 51  MET A CE  1 
ATOM   186  N  N   . ASN A 1 52  ? 89.65800  43.44900 16.23400  1.000 9.78674  ? 52  ASN A N   1 
ATOM   187  C  CA  . ASN A 1 52  ? 90.53100  43.02000 17.31900  1.000 10.14239 ? 52  ASN A CA  1 
ATOM   188  C  C   . ASN A 1 52  ? 90.84100  41.52900 17.16100  1.000 9.47318  ? 52  ASN A C   1 
ATOM   189  O  O   . ASN A 1 52  ? 90.39000  40.87700 16.22000  1.000 9.49420  ? 52  ASN A O   1 
ATOM   190  C  CB  . ASN A 1 52  ? 89.97000  43.46400 18.67300  1.000 11.65538 ? 52  ASN A CB  1 
ATOM   191  C  CG  . ASN A 1 52  ? 88.75900  42.66100 19.13600  1.000 14.08140 ? 52  ASN A CG  1 
ATOM   192  O  OD1 . ASN A 1 52  ? 88.42200  41.59400 18.62400  1.000 13.92394 ? 52  ASN A OD1 1 
ATOM   193  N  ND2 . ASN A 1 52  ? 88.09300  43.20200 20.13400  1.000 16.10510 ? 52  ASN A ND2 1 
ATOM   194  N  N   . PHE A 1 53  ? 91.65700  40.97800 18.06500  1.000 9.63178  ? 53  PHE A N   1 
ATOM   195  C  CA  . PHE A 1 53  ? 92.09600  39.59200 17.89200  1.000 9.52190  ? 53  PHE A CA  1 
ATOM   196  C  C   . PHE A 1 53  ? 90.91200  38.63300 17.83100  1.000 9.52404  ? 53  PHE A C   1 
ATOM   197  O  O   . PHE A 1 53  ? 90.82800  37.77300 16.94200  1.000 10.22524 ? 53  PHE A O   1 
ATOM   198  C  CB  . PHE A 1 53  ? 93.06600  39.19700 19.00100  1.000 9.93255  ? 53  PHE A CB  1 
ATOM   199  C  CG  . PHE A 1 53  ? 93.50500  37.76400 18.94000  1.000 10.23717 ? 53  PHE A CG  1 
ATOM   200  C  CD1 . PHE A 1 53  ? 94.41800  37.34200 17.98500  1.000 10.46489 ? 53  PHE A CD1 1 
ATOM   201  C  CD2 . PHE A 1 53  ? 93.00700  36.83500 19.83700  1.000 13.09905 ? 53  PHE A CD2 1 
ATOM   202  C  CE1 . PHE A 1 53  ? 94.83700  36.02000 17.93000  1.000 11.81511 ? 53  PHE A CE1 1 
ATOM   203  C  CE2 . PHE A 1 53  ? 93.42000  35.51500 19.79000  1.000 14.33595 ? 53  PHE A CE2 1 
ATOM   204  C  CZ  . PHE A 1 53  ? 94.33600  35.10700 18.83900  1.000 13.76025 ? 53  PHE A CZ  1 
ATOM   205  N  N   . THR A 1 54  ? 89.98000  38.77500 18.76800  1.000 10.22683 ? 54  THR A N   1 
ATOM   206  C  CA  . THR A 1 54  ? 88.79700  37.91900 18.79400  1.000 10.18105 ? 54  THR A CA  1 
ATOM   207  C  C   . THR A 1 54  ? 87.99400  38.04900 17.50700  1.000 9.65738  ? 54  THR A C   1 
ATOM   208  O  O   . THR A 1 54  ? 87.56300  37.04300 16.92600  1.000 9.78268  ? 54  THR A O   1 
ATOM   209  C  CB  . THR A 1 54  ? 87.94200  38.27400 20.01300  1.000 12.20761 ? 54  THR A CB  1 
ATOM   210  O  OG1 . THR A 1 54  ? 88.66900  37.94500 21.20200  1.000 14.98378 ? 54  THR A OG1 1 
ATOM   211  C  CG2 . THR A 1 54  ? 86.60900  37.53800 19.97500  1.000 13.81378 ? 54  THR A CG2 1 
ATOM   212  N  N   . GLU A 1 55  ? 87.80500  39.28300 17.03400  1.000 9.04441  ? 55  GLU A N   1 
ATOM   213  C  CA  . GLU A 1 55  ? 87.03500  39.51700 15.81900  1.000 9.40741  ? 55  GLU A CA  1 
ATOM   214  C  C   . GLU A 1 55  ? 87.74100  38.94300 14.59400  1.000 8.87594  ? 55  GLU A C   1 
ATOM   215  O  O   . GLU A 1 55  ? 87.09000  38.43300 13.67600  1.000 8.23531  ? 55  GLU A O   1 
ATOM   216  C  CB  . GLU A 1 55  ? 86.80000  41.01600 15.63200  1.000 11.02982 ? 55  GLU A CB  1 
ATOM   217  C  CG  . GLU A 1 55  ? 85.83900  41.62000 16.63400  1.000 12.36277 ? 55  GLU A CG  1 
ATOM   218  C  CD  . GLU A 1 55  ? 85.82700  43.14000 16.61700  1.000 15.54704 ? 55  GLU A CD  1 
ATOM   219  O  OE1 . GLU A 1 55  ? 86.90300  43.76600 16.50900  1.000 15.25852 ? 55  GLU A OE1 1 
ATOM   220  O  OE2 . GLU A 1 55  ? 84.72300  43.71900 16.73200  1.000 17.96649 ? 55  GLU A OE2 1 
ATOM   221  N  N   . ALA A 1 56  ? 89.07100  39.02600 14.55500  1.000 8.47310  ? 56  ALA A N   1 
ATOM   222  C  CA  . ALA A 1 56  ? 89.81700  38.50100 13.41500  1.000 8.02978  ? 56  ALA A CA  1 
ATOM   223  C  C   . ALA A 1 56  ? 89.72400  36.98300 13.37300  1.000 8.08618  ? 56  ALA A C   1 
ATOM   224  O  O   . ALA A 1 56  ? 89.48800  36.37800 12.30800  1.000 7.71246  ? 56  ALA A O   1 
ATOM   225  C  CB  . ALA A 1 56  ? 91.27300  38.95400 13.53100  1.000 8.45582  ? 56  ALA A CB  1 
ATOM   226  N  N   A ASN A 1 57  ? 89.89300  36.35600 14.52800  0.628 8.21370  ? 57  ASN A N   1 
ATOM   227  N  N   B ASN A 1 57  ? 89.90800  36.33200 14.52800  0.372 8.43103  ? 57  ASN A N   1 
ATOM   228  C  CA  A ASN A 1 57  ? 89.69700  34.92200 14.61200  0.628 8.18836  ? 57  ASN A CA  1 
ATOM   229  C  CA  B ASN A 1 57  ? 89.68300  34.88900 14.59700  0.372 8.56356  ? 57  ASN A CA  1 
ATOM   230  C  C   A ASN A 1 57  ? 88.30300  34.53800 14.12700  0.628 7.76391  ? 57  ASN A C   1 
ATOM   231  C  C   B ASN A 1 57  ? 88.29100  34.54200 14.09400  0.372 7.77510  ? 57  ASN A C   1 
ATOM   232  O  O   A ASN A 1 57  ? 88.13500  33.56200 13.37700  0.628 7.95258  ? 57  ASN A O   1 
ATOM   233  O  O   B ASN A 1 57  ? 88.10600  33.58200 13.33100  0.372 8.04642  ? 57  ASN A O   1 
ATOM   234  C  CB  A ASN A 1 57  ? 89.88700  34.51500 16.06400  0.628 9.22931  ? 57  ASN A CB  1 
ATOM   235  C  CB  B ASN A 1 57  ? 89.82800  34.39000 16.03700  0.372 9.87859  ? 57  ASN A CB  1 
ATOM   236  C  CG  A ASN A 1 57  ? 89.73400  33.05900 16.26100  0.628 8.67991  ? 57  ASN A CG  1 
ATOM   237  C  CG  B ASN A 1 57  ? 91.24000  33.96600 16.38000  0.372 10.15206 ? 57  ASN A CG  1 
ATOM   238  O  OD1 A ASN A 1 57  ? 90.53700  32.28500 15.75200  0.628 9.93562  ? 57  ASN A OD1 1 
ATOM   239  O  OD1 B ASN A 1 57  ? 91.68400  32.86700 16.03900  0.372 10.34160 ? 57  ASN A OD1 1 
ATOM   240  N  ND2 A ASN A 1 57  ? 88.70000  32.65400 16.98500  0.628 9.00915  ? 57  ASN A ND2 1 
ATOM   241  N  ND2 B ASN A 1 57  ? 91.94300  34.82700 17.09000  0.372 9.86214  ? 57  ASN A ND2 1 
ATOM   242  N  N   . GLU A 1 58  ? 87.29100  35.31200 14.52700  1.000 7.23256  ? 58  GLU A N   1 
ATOM   243  C  CA  . GLU A 1 58  ? 85.93100  34.96800 14.16700  1.000 6.93386  ? 58  GLU A CA  1 
ATOM   244  C  C   . GLU A 1 58  ? 85.70200  35.14600 12.66200  1.000 7.16197  ? 58  GLU A C   1 
ATOM   245  O  O   . GLU A 1 58  ? 84.98000  34.35200 12.04800  1.000 7.70995  ? 58  GLU A O   1 
ATOM   246  C  CB  . GLU A 1 58  ? 84.96000  35.79300 15.00400  1.000 8.09426  ? 58  GLU A CB  1 
ATOM   247  C  CG  . GLU A 1 58  ? 83.59200  35.15200 15.03600  1.000 8.92701  ? 58  GLU A CG  1 
ATOM   248  C  CD  . GLU A 1 58  ? 83.57700  33.90500 15.93600  1.000 9.56115  ? 58  GLU A CD  1 
ATOM   249  O  OE1 . GLU A 1 58  ? 84.53300  33.70800 16.72100  1.000 11.12726 ? 58  GLU A OE1 1 
ATOM   250  O  OE2 . GLU A 1 58  ? 82.65600  33.06700 15.81000  1.000 11.45305 ? 58  GLU A OE2 1 
ATOM   251  N  N   . ALA A 1 59  ? 86.31500  36.16500 12.04900  1.000 7.09241  ? 59  ALA A N   1 
ATOM   252  C  CA  . ALA A 1 59  ? 86.19300  36.34400 10.60600  1.000 7.40262  ? 59  ALA A CA  1 
ATOM   253  C  C   . ALA A 1 59  ? 86.72200  35.12600 9.86900   1.000 7.02282  ? 59  ALA A C   1 
ATOM   254  O  O   . ALA A 1 59  ? 86.08100  34.61500 8.94500   1.000 7.68428  ? 59  ALA A O   1 
ATOM   255  C  CB  . ALA A 1 59  ? 86.93100  37.60800 10.16200  1.000 7.64471  ? 59  ALA A CB  1 
ATOM   256  N  N   . CYS A 1 60  ? 87.90500  34.64600 10.26100  1.000 6.45412  ? 60  CYS A N   1 
ATOM   257  C  CA  . CYS A 1 60  ? 88.42800  33.45300 9.59800   1.000 7.22687  ? 60  CYS A CA  1 
ATOM   258  C  C   . CYS A 1 60  ? 87.48300  32.27300 9.78500   1.000 7.02070  ? 60  CYS A C   1 
ATOM   259  O  O   . CYS A 1 60  ? 87.20300  31.52400 8.83800   1.000 7.50048  ? 60  CYS A O   1 
ATOM   260  C  CB  . CYS A 1 60  ? 89.81900  33.10400 10.12500  1.000 7.64308  ? 60  CYS A CB  1 
ATOM   261  S  SG  . CYS A 1 60  ? 91.09300  34.34100 9.82500   1.000 7.57984  ? 60  CYS A SG  1 
ATOM   262  N  N   . LYS A 1 61  ? 86.98600  32.08800 11.01500  1.000 7.04893  ? 61  LYS A N   1 
ATOM   263  C  CA  . LYS A 1 61  ? 86.09100  30.96400 11.28800  1.000 7.95119  ? 61  LYS A CA  1 
ATOM   264  C  C   . LYS A 1 61  ? 84.83200  31.02800 10.44200  1.000 8.04456  ? 61  LYS A C   1 
ATOM   265  O  O   . LYS A 1 61  ? 84.31900  29.99600 9.99500   1.000 8.49077  ? 61  LYS A O   1 
ATOM   266  C  CB  . LYS A 1 61  ? 85.70700  30.94100 12.76300  1.000 8.60337  ? 61  LYS A CB  1 
ATOM   267  C  CG  . LYS A 1 61  ? 86.81700  30.50400 13.67800  1.000 11.38738 ? 61  LYS A CG  1 
ATOM   268  C  CD  . LYS A 1 61  ? 86.50100  30.83000 15.13100  1.000 12.51881 ? 61  LYS A CD  1 
ATOM   269  C  CE  . LYS A 1 61  ? 85.16500  30.26100 15.59700  1.000 13.04189 ? 61  LYS A CE  1 
ATOM   270  N  NZ  . LYS A 1 61  ? 84.76500  30.86400 16.90700  1.000 12.15732 ? 61  LYS A NZ  1 
ATOM   271  N  N   . MET A 1 62  ? 84.29900  32.22800 10.23500  1.000 7.67129  ? 62  MET A N   1 
ATOM   272  C  CA  . MET A 1 62  ? 83.05400  32.36000 9.49900   1.000 8.21652  ? 62  MET A CA  1 
ATOM   273  C  C   . MET A 1 62  ? 83.25300  31.93100 8.05100   1.000 8.77416  ? 62  MET A C   1 
ATOM   274  O  O   . MET A 1 62  ? 82.32000  31.42900 7.41400   1.000 9.48117  ? 62  MET A O   1 
ATOM   275  C  CB  . MET A 1 62  ? 82.62300  33.81500 9.59400   1.000 8.06076  ? 62  MET A CB  1 
ATOM   276  C  CG  . MET A 1 62  ? 81.97700  34.07200 10.92900  1.000 9.13483  ? 62  MET A CG  1 
ATOM   277  S  SD  . MET A 1 62  ? 81.66300  35.80800 11.25300  1.000 10.50456 ? 62  MET A SD  1 
ATOM   278  C  CE  . MET A 1 62  ? 80.08700  36.01400 10.44000  1.000 12.43086 ? 62  MET A CE  1 
ATOM   279  N  N   . LEU A 1 63  ? 84.46900  32.09900 7.52700   1.000 9.27572  ? 63  LEU A N   1 
ATOM   280  C  CA  . LEU A 1 63  ? 84.84500  31.62700 6.20200   1.000 10.49764 ? 63  LEU A CA  1 
ATOM   281  C  C   . LEU A 1 63  ? 85.22600  30.15300 6.18400   1.000 10.62610 ? 63  LEU A C   1 
ATOM   282  O  O   . LEU A 1 63  ? 85.59300  29.64100 5.11900   1.000 11.87339 ? 63  LEU A O   1 
ATOM   283  C  CB  . LEU A 1 63  ? 86.01600  32.46600 5.68100   1.000 11.65669 ? 63  LEU A CB  1 
ATOM   284  C  CG  . LEU A 1 63  ? 85.70900  33.94900 5.47200   1.000 12.47274 ? 63  LEU A CG  1 
ATOM   285  C  CD1 . LEU A 1 63  ? 86.98400  34.72200 5.11100   1.000 13.05504 ? 63  LEU A CD1 1 
ATOM   286  C  CD2 . LEU A 1 63  ? 84.63000  34.13300 4.40600   1.000 13.91605 ? 63  LEU A CD2 1 
ATOM   287  N  N   . GLY A 1 64  ? 85.15400  29.45500 7.31400   1.000 10.33059 ? 64  GLY A N   1 
ATOM   288  C  CA  . GLY A 1 64  ? 85.58400  28.07300 7.36800   1.000 11.53715 ? 64  GLY A CA  1 
ATOM   289  C  C   . GLY A 1 64  ? 87.08000  27.90100 7.42600   1.000 11.59031 ? 64  GLY A C   1 
ATOM   290  O  O   . GLY A 1 64  ? 87.58100  26.79900 7.16600   1.000 14.66899 ? 64  GLY A O   1 
ATOM   291  N  N   . LEU A 1 65  ? 87.80900  28.96100 7.74500   1.000 9.61203  ? 65  LEU A N   1 
ATOM   292  C  CA  . LEU A 1 65  ? 89.25800  28.96200 7.81300   1.000 9.53725  ? 65  LEU A CA  1 
ATOM   293  C  C   . LEU A 1 65  ? 89.69400  29.09000 9.26500   1.000 9.44647  ? 65  LEU A C   1 
ATOM   294  O  O   . LEU A 1 65  ? 88.86500  29.15500 10.17600  1.000 10.22316 ? 65  LEU A O   1 
ATOM   295  C  CB  . LEU A 1 65  ? 89.81600  30.12000 6.98400   1.000 9.60646  ? 65  LEU A CB  1 
ATOM   296  C  CG  . LEU A 1 65  ? 89.27300  30.20300 5.55800   1.000 10.30472 ? 65  LEU A CG  1 
ATOM   297  C  CD1 . LEU A 1 65  ? 89.77900  31.46300 4.87100   1.000 11.83774 ? 65  LEU A CD1 1 
ATOM   298  C  CD2 . LEU A 1 65  ? 89.63200  28.95400 4.76300   1.000 12.84440 ? 65  LEU A CD2 1 
ATOM   299  N  N   . THR A 1 66  ? 91.00300  29.10600 9.48200   1.000 8.43142  ? 66  THR A N   1 
ATOM   300  C  CA  . THR A 1 66  ? 91.56200  29.39800 10.78900  1.000 8.95046  ? 66  THR A CA  1 
ATOM   301  C  C   . THR A 1 66  ? 92.41100  30.65000 10.65600  1.000 7.06813  ? 66  THR A C   1 
ATOM   302  O  O   . THR A 1 66  ? 92.82800  31.02200 9.55800   1.000 7.85917  ? 66  THR A O   1 
ATOM   303  C  CB  . THR A 1 66  ? 92.46100  28.26000 11.29500  1.000 11.59559 ? 66  THR A CB  1 
ATOM   304  O  OG1 . THR A 1 66  ? 93.59700  28.12500 10.43300  1.000 13.61275 ? 66  THR A OG1 1 
ATOM   305  C  CG2 . THR A 1 66  ? 91.69800  26.93900 11.34800  1.000 12.87668 ? 66  THR A CG2 1 
ATOM   306  N  N   . LEU A 1 67  ? 92.68800  31.29400 11.77800  1.000 7.05817  ? 67  LEU A N   1 
ATOM   307  C  CA  . LEU A 1 67  ? 93.67000  32.36200 11.76600  1.000 6.96836  ? 67  LEU A CA  1 
ATOM   308  C  C   . LEU A 1 67  ? 95.03100  31.74700 11.47500  1.000 7.97948  ? 67  LEU A C   1 
ATOM   309  O  O   . LEU A 1 67  ? 95.39900  30.72200 12.06500  1.000 10.91950 ? 67  LEU A O   1 
ATOM   310  C  CB  . LEU A 1 67  ? 93.65800  33.06700 13.12100  1.000 9.84892  ? 67  LEU A CB  1 
ATOM   311  C  CG  . LEU A 1 67  ? 94.24600  34.47800 13.20800  1.000 10.76874 ? 67  LEU A CG  1 
ATOM   312  C  CD1 . LEU A 1 67  ? 93.49700  35.45400 12.31900  1.000 8.38638  ? 67  LEU A CD1 1 
ATOM   313  C  CD2 . LEU A 1 67  ? 94.21200  34.95100 14.63700  1.000 11.33269 ? 67  LEU A CD2 1 
ATOM   314  N  N   . ALA A 1 68  ? 95.75100  32.33500 10.52800  1.000 6.51408  ? 68  ALA A N   1 
ATOM   315  C  CA  . ALA A 1 68  ? 97.04800  31.80900 10.13300  1.000 7.11885  ? 68  ALA A CA  1 
ATOM   316  C  C   . ALA A 1 68  ? 98.05300  31.99500 11.26000  1.000 6.61739  ? 68  ALA A C   1 
ATOM   317  O  O   . ALA A 1 68  ? 97.91600  32.89400 12.09600  1.000 7.43850  ? 68  ALA A O   1 
ATOM   318  C  CB  . ALA A 1 68  ? 97.56400  32.55700 8.89900   1.000 7.19704  ? 68  ALA A CB  1 
ATOM   319  N  N   . SER A 1 69  ? 99.06600  31.13600 11.28500  1.000 6.82339  ? 69  SER A N   1 
ATOM   320  C  CA  . SER A 1 69  ? 100.21300 31.33900 12.15200  1.000 6.82155  ? 69  SER A CA  1 
ATOM   321  C  C   . SER A 1 69  ? 101.22500 32.24500 11.45900  1.000 6.43469  ? 69  SER A C   1 
ATOM   322  O  O   . SER A 1 69  ? 101.22000 32.42000 10.23200  1.000 6.20925  ? 69  SER A O   1 
ATOM   323  C  CB  . SER A 1 69  ? 100.89300 30.00400 12.43100  1.000 8.22540  ? 69  SER A CB  1 
ATOM   324  O  OG  . SER A 1 69  ? 101.43900 29.48600 11.22900  1.000 8.27868  ? 69  SER A OG  1 
ATOM   325  N  N   . ARG A 1 70  ? 102.14200 32.79300 12.26100  1.000 6.53420  ? 70  ARG A N   1 
ATOM   326  C  CA  . ARG A 1 70  ? 103.24400 33.55700 11.69200  1.000 6.67392  ? 70  ARG A CA  1 
ATOM   327  C  C   . ARG A 1 70  ? 104.02400 32.72700 10.67500  1.000 6.59012  ? 70  ARG A C   1 
ATOM   328  O  O   . ARG A 1 70  ? 104.38100 33.22700 9.60300   1.000 6.78742  ? 70  ARG A O   1 
ATOM   329  C  CB  . ARG A 1 70  ? 104.16800 34.05800 12.80500  1.000 7.77961  ? 70  ARG A CB  1 
ATOM   330  C  CG  . ARG A 1 70  ? 105.21500 35.06900 12.33000  1.000 9.75430  ? 70  ARG A CG  1 
ATOM   331  C  CD  . ARG A 1 70  ? 106.57800 34.85500 12.97900  1.000 12.75590 ? 70  ARG A CD  1 
ATOM   332  N  NE  . ARG A 1 70  ? 107.14700 33.61200 12.47600  1.000 14.92764 ? 70  ARG A NE  1 
ATOM   333  C  CZ  . ARG A 1 70  ? 107.89400 33.51500 11.38200  1.000 15.78385 ? 70  ARG A CZ  1 
ATOM   334  N  NH1 . ARG A 1 70  ? 108.22600 34.59600 10.68800  1.000 15.94250 ? 70  ARG A NH1 1 
ATOM   335  N  NH2 . ARG A 1 70  ? 108.32900 32.32600 10.98900  1.000 16.23206 ? 70  ARG A NH2 1 
ATOM   336  N  N   . ASP A 1 71  ? 104.28300 31.45000 10.98400  1.000 6.58154  ? 71  ASP A N   1 
ATOM   337  C  CA  . ASP A 1 71  ? 105.01700 30.59500 10.05400  1.000 7.41151  ? 71  ASP A CA  1 
ATOM   338  C  C   . ASP A 1 71  ? 104.26700 30.43300 8.73900   1.000 6.95382  ? 71  ASP A C   1 
ATOM   339  O  O   . ASP A 1 71  ? 104.87700 30.38800 7.66400   1.000 7.17429  ? 71  ASP A O   1 
ATOM   340  C  CB  . ASP A 1 71  ? 105.25100 29.21500 10.66500  1.000 9.38341  ? 71  ASP A CB  1 
ATOM   341  C  CG  . ASP A 1 71  ? 106.38500 29.18500 11.67300  1.000 13.15975 ? 71  ASP A CG  1 
ATOM   342  O  OD1 . ASP A 1 71  ? 107.08400 30.20100 11.86700  1.000 14.37652 ? 71  ASP A OD1 1 
ATOM   343  O  OD2 . ASP A 1 71  ? 106.59000 28.10600 12.26700  1.000 15.32066 ? 71  ASP A OD2 1 
ATOM   344  N  N   . GLN A 1 72  ? 102.93900 30.33000 8.79800   1.000 6.52694  ? 72  GLN A N   1 
ATOM   345  C  CA  . GLN A 1 72  ? 102.16500 30.20000 7.56700   1.000 6.10939  ? 72  GLN A CA  1 
ATOM   346  C  C   . GLN A 1 72  ? 102.25600 31.46300 6.72400   1.000 5.71459  ? 72  GLN A C   1 
ATOM   347  O  O   . GLN A 1 72  ? 102.36700 31.39500 5.48800   1.000 5.30463  ? 72  GLN A O   1 
ATOM   348  C  CB  . GLN A 1 72  ? 100.71100 29.83400 7.88000   1.000 6.58964  ? 72  GLN A CB  1 
ATOM   349  C  CG  . GLN A 1 72  ? 100.58400 28.37600 8.26600   1.000 7.04019  ? 72  GLN A CG  1 
ATOM   350  C  CD  . GLN A 1 72  ? 99.26800  28.01700 8.92400   1.000 7.47203  ? 72  GLN A CD  1 
ATOM   351  O  OE1 . GLN A 1 72  ? 98.56700  28.87300 9.47700   1.000 7.51538  ? 72  GLN A OE1 1 
ATOM   352  N  NE2 . GLN A 1 72  ? 98.93600  26.72900 8.89000   1.000 8.90249  ? 72  GLN A NE2 1 
ATOM   353  N  N   . VAL A 1 73  ? 102.24800 32.62900 7.37100   1.000 4.86295  ? 73  VAL A N   1 
ATOM   354  C  CA  . VAL A 1 73  ? 102.41400 33.86600 6.61700   1.000 5.00774  ? 73  VAL A CA  1 
ATOM   355  C  C   . VAL A 1 73  ? 103.81000 33.94600 6.01300   1.000 5.32489  ? 73  VAL A C   1 
ATOM   356  O  O   . VAL A 1 73  ? 103.98300 34.38400 4.86900   1.000 5.47500  ? 73  VAL A O   1 
ATOM   357  C  CB  . VAL A 1 73  ? 102.06100 35.10000 7.46500   1.000 5.52953  ? 73  VAL A CB  1 
ATOM   358  C  CG1 . VAL A 1 73  ? 102.32200 36.36500 6.66800   1.000 6.52687  ? 73  VAL A CG1 1 
ATOM   359  C  CG2 . VAL A 1 73  ? 100.60900 35.03300 7.90000   1.000 5.99852  ? 73  VAL A CG2 1 
ATOM   360  N  N   . GLU A 1 74  ? 104.82500 33.50900 6.75500   1.000 6.08839  ? 74  GLU A N   1 
ATOM   361  C  CA  . GLU A 1 74  ? 106.17600 33.48900 6.20100   1.000 7.43550  ? 74  GLU A CA  1 
ATOM   362  C  C   . GLU A 1 74  ? 106.28900 32.56500 4.99100   1.000 6.48082  ? 74  GLU A C   1 
ATOM   363  O  O   . GLU A 1 74  ? 106.93600 32.90700 3.99500   1.000 6.61687  ? 74  GLU A O   1 
ATOM   364  C  CB  . GLU A 1 74  ? 107.19200 33.09000 7.26100   1.000 12.15307 ? 74  GLU A CB  1 
ATOM   365  C  CG  . GLU A 1 74  ? 108.62200 33.16000 6.74100   1.000 20.72652 ? 74  GLU A CG  1 
ATOM   366  C  CD  . GLU A 1 74  ? 109.64200 32.72900 7.77500   1.000 31.36120 ? 74  GLU A CD  1 
ATOM   367  O  OE1 . GLU A 1 74  ? 109.54900 33.19200 8.92800   1.000 37.62554 ? 74  GLU A OE1 1 
ATOM   368  O  OE2 . GLU A 1 74  ? 110.54700 31.93900 7.43400   1.000 34.01314 ? 74  GLU A OE2 1 
ATOM   369  N  N   A SER A 1 75  ? 105.68300 31.38000 5.06200   0.626 5.74145  ? 75  SER A N   1 
ATOM   370  N  N   B SER A 1 75  ? 105.69900 31.37500 5.07400   0.374 6.34305  ? 75  SER A N   1 
ATOM   371  C  CA  A SER A 1 75  ? 105.70300 30.48800 3.90400   0.626 6.92827  ? 75  SER A CA  1 
ATOM   372  C  CA  B SER A 1 75  ? 105.68300 30.48100 3.92100   0.374 6.85305  ? 75  SER A CA  1 
ATOM   373  C  C   A SER A 1 75  ? 105.03900 31.14500 2.69900   0.626 4.77630  ? 75  SER A C   1 
ATOM   374  C  C   B SER A 1 75  ? 105.06800 31.18200 2.71200   0.374 6.78268  ? 75  SER A C   1 
ATOM   375  O  O   A SER A 1 75  ? 105.53800 31.05500 1.56300   0.626 4.75476  ? 75  SER A O   1 
ATOM   376  O  O   B SER A 1 75  ? 105.63700 31.18400 1.60300   0.374 9.40610  ? 75  SER A O   1 
ATOM   377  C  CB  A SER A 1 75  ? 105.00700 29.17500 4.24900   0.626 8.60911  ? 75  SER A CB  1 
ATOM   378  C  CB  B SER A 1 75  ? 104.90100 29.22000 4.28900   0.374 6.66169  ? 75  SER A CB  1 
ATOM   379  O  OG  A SER A 1 75  ? 105.76200 28.45300 5.20000   0.626 10.68130 ? 75  SER A OG  1 
ATOM   380  O  OG  B SER A 1 75  ? 104.79600 28.32800 3.20300   0.374 6.92872  ? 75  SER A OG  1 
ATOM   381  N  N   . ALA A 1 76  ? 103.92000 31.83100 2.92600   1.000 5.25277  ? 76  ALA A N   1 
ATOM   382  C  CA  . ALA A 1 76  ? 103.28300 32.56900 1.84400   1.000 5.24013  ? 76  ALA A CA  1 
ATOM   383  C  C   . ALA A 1 76  ? 104.20600 33.64800 1.28100   1.000 4.53341  ? 76  ALA A C   1 
ATOM   384  O  O   . ALA A 1 76  ? 104.34200 33.79500 0.05900   1.000 5.08285  ? 76  ALA A O   1 
ATOM   385  C  CB  . ALA A 1 76  ? 101.96600 33.16800 2.33100   1.000 4.84462  ? 76  ALA A CB  1 
ATOM   386  N  N   . GLN A 1 77  ? 104.85500 34.41100 2.15900   1.000 5.25932  ? 77  GLN A N   1 
ATOM   387  C  CA  . GLN A 1 77  ? 105.74400 35.47500 1.71200   1.000 5.21154  ? 77  GLN A CA  1 
ATOM   388  C  C   . GLN A 1 77  ? 106.87500 34.91300 0.86200   1.000 6.44801  ? 77  GLN A C   1 
ATOM   389  O  O   . GLN A 1 77  ? 107.28200 35.52900 -0.13000  1.000 6.30244  ? 77  GLN A O   1 
ATOM   390  C  CB  . GLN A 1 77  ? 106.28900 36.21900 2.93400   1.000 5.91784  ? 77  GLN A CB  1 
ATOM   391  C  CG  . GLN A 1 77  ? 107.09100 37.46900 2.60900   1.000 6.93810  ? 77  GLN A CG  1 
ATOM   392  C  CD  . GLN A 1 77  ? 108.57700 37.20900 2.48300   1.000 7.72509  ? 77  GLN A CD  1 
ATOM   393  O  OE1 . GLN A 1 77  ? 109.03200 36.06100 2.58800   1.000 9.62599  ? 77  GLN A OE1 1 
ATOM   394  N  NE2 . GLN A 1 77  ? 109.34600 38.26700 2.24600   1.000 8.18873  ? 77  GLN A NE2 1 
ATOM   395  N  N   . LYS A 1 78  ? 107.39100 33.74000 1.23600   1.000 6.25891  ? 78  LYS A N   1 
ATOM   396  C  CA  . LYS A 1 78  ? 108.46500 33.12100 0.47700   1.000 7.56588  ? 78  LYS A CA  1 
ATOM   397  C  C   . LYS A 1 78  ? 107.98700 32.59400 -0.86300  1.000 7.69076  ? 78  LYS A C   1 
ATOM   398  O  O   . LYS A 1 78  ? 108.81900 32.29800 -1.73400  1.000 9.38973  ? 78  LYS A O   1 
ATOM   399  C  CB  . LYS A 1 78  ? 109.09700 32.01000 1.29600   1.000 9.12346  ? 78  LYS A CB  1 
ATOM   400  C  CG  . LYS A 1 78  ? 109.90300 32.51400 2.47600   1.000 12.88584 ? 78  LYS A CG  1 
ATOM   401  C  CD  . LYS A 1 78  ? 110.52000 31.35100 3.22800   1.000 16.59023 ? 78  LYS A CD  1 
ATOM   402  C  CE  . LYS A 1 78  ? 111.37300 31.82600 4.39300   1.000 20.48431 ? 78  LYS A CE  1 
ATOM   403  N  NZ  . LYS A 1 78  ? 112.22300 30.72900 4.93400   1.000 23.57817 ? 78  LYS A NZ  1 
ATOM   404  N  N   . SER A 1 79  ? 106.67400 32.46200 -1.04400  1.000 7.20155  ? 79  SER A N   1 
ATOM   405  C  CA  . SER A 1 79  ? 106.14200 32.16300 -2.37200  1.000 7.41480  ? 79  SER A CA  1 
ATOM   406  C  C   . SER A 1 79  ? 105.47900 33.35800 -3.06700  1.000 6.67500  ? 79  SER A C   1 
ATOM   407  O  O   . SER A 1 79  ? 104.66800 33.16400 -3.98000  1.000 8.57764  ? 79  SER A O   1 
ATOM   408  C  CB  . SER A 1 79  ? 105.21400 30.95700 -2.32100  1.000 7.30661  ? 79  SER A CB  1 
ATOM   409  O  OG  . SER A 1 79  ? 105.98300 29.77500 -2.20900  1.000 8.13991  ? 79  SER A OG  1 
ATOM   410  N  N   . GLY A 1 80  ? 105.80800 34.58400 -2.67200  1.000 6.98584  ? 80  GLY A N   1 
ATOM   411  C  CA  . GLY A 1 80  ? 105.39100 35.75500 -3.42700  1.000 6.90728  ? 80  GLY A CA  1 
ATOM   412  C  C   . GLY A 1 80  ? 104.27700 36.58300 -2.82500  1.000 7.00480  ? 80  GLY A C   1 
ATOM   413  O  O   . GLY A 1 80  ? 103.84200 37.54900 -3.47100  1.000 8.17150  ? 80  GLY A O   1 
ATOM   414  N  N   . PHE A 1 81  ? 103.80600 36.26000 -1.62400  1.000 5.76499  ? 81  PHE A N   1 
ATOM   415  C  CA  . PHE A 1 81  ? 102.71700 36.99400 -0.98100  1.000 5.93282  ? 81  PHE A CA  1 
ATOM   416  C  C   . PHE A 1 81  ? 103.25300 38.24300 -0.28500  1.000 6.31142  ? 81  PHE A C   1 
ATOM   417  O  O   . PHE A 1 81  ? 104.11400 38.14800 0.58800   1.000 6.40788  ? 81  PHE A O   1 
ATOM   418  C  CB  . PHE A 1 81  ? 102.09100 36.05500 0.04800   1.000 6.50101  ? 81  PHE A CB  1 
ATOM   419  C  CG  . PHE A 1 81  ? 100.82800 36.55900 0.68400   1.000 6.94081  ? 81  PHE A CG  1 
ATOM   420  C  CD1 . PHE A 1 81  ? 99.69300  36.77900 -0.06900  1.000 9.56249  ? 81  PHE A CD1 1 
ATOM   421  C  CD2 . PHE A 1 81  ? 100.76000 36.75400 2.04800   1.000 8.39964  ? 81  PHE A CD2 1 
ATOM   422  C  CE1 . PHE A 1 81  ? 98.50800  37.21400 0.53700   1.000 11.18930 ? 81  PHE A CE1 1 
ATOM   423  C  CE2 . PHE A 1 81  ? 99.57700  37.18000 2.65900   1.000 9.57986  ? 81  PHE A CE2 1 
ATOM   424  C  CZ  . PHE A 1 81  ? 98.46100  37.41200 1.90100   1.000 10.54260 ? 81  PHE A CZ  1 
ATOM   425  N  N   . GLU A 1 82  ? 102.74400 39.41700 -0.65300  1.000 6.91030  ? 82  GLU A N   1 
ATOM   426  C  CA  . GLU A 1 82  ? 102.97300 40.60100 0.16800   1.000 7.71999  ? 82  GLU A CA  1 
ATOM   427  C  C   . GLU A 1 82  ? 101.70300 41.43600 0.16900   1.000 6.43463  ? 82  GLU A C   1 
ATOM   428  O  O   . GLU A 1 82  ? 100.88200 41.37500 -0.75100  1.000 7.45388  ? 82  GLU A O   1 
ATOM   429  C  CB  . GLU A 1 82  ? 104.15300 41.53100 -0.21500  1.000 12.29726 ? 82  GLU A CB  1 
ATOM   430  C  CG  . GLU A 1 82  ? 104.01300 42.23400 -1.54300  1.000 12.16929 ? 82  GLU A CG  1 
ATOM   431  C  CD  . GLU A 1 82  ? 105.13500 43.23800 -1.87600  1.000 10.07907 ? 82  GLU A CD  1 
ATOM   432  O  OE1 . GLU A 1 82  ? 106.08800 43.48400 -1.07900  1.000 8.12782  ? 82  GLU A OE1 1 
ATOM   433  O  OE2 . GLU A 1 82  ? 105.04600 43.78300 -2.99100  1.000 10.16856 ? 82  GLU A OE2 1 
ATOM   434  N  N   . THR A 1 83  ? 101.55800 42.23100 1.21700   1.000 5.79864  ? 83  THR A N   1 
ATOM   435  C  CA  . THR A 1 83  ? 100.42800 43.13500 1.34300   1.000 6.62220  ? 83  THR A CA  1 
ATOM   436  C  C   . THR A 1 83  ? 100.93200 44.43400 1.94800   1.000 5.54240  ? 83  THR A C   1 
ATOM   437  O  O   . THR A 1 83  ? 102.06800 44.52000 2.42700   1.000 6.09670  ? 83  THR A O   1 
ATOM   438  C  CB  . THR A 1 83  ? 99.33200  42.58800 2.27300   1.000 7.21202  ? 83  THR A CB  1 
ATOM   439  O  OG1 . THR A 1 83  ? 99.73400  42.81400 3.62600   1.000 7.08404  ? 83  THR A OG1 1 
ATOM   440  C  CG2 . THR A 1 83  ? 99.04800  41.10700 2.03500   1.000 7.89385  ? 83  THR A CG2 1 
ATOM   441  N  N   . CYS A 1 84  ? 100.06400 45.44200 1.96200   1.000 5.74683  ? 84  CYS A N   1 
ATOM   442  C  CA  . CYS A 1 84  ? 100.34600 46.61900 2.77700   1.000 6.65434  ? 84  CYS A CA  1 
ATOM   443  C  C   . CYS A 1 84  ? 99.33000  46.76500 3.89800   1.000 6.23049  ? 84  CYS A C   1 
ATOM   444  O  O   . CYS A 1 84  ? 98.80300  47.85500 4.13200   1.000 7.96056  ? 84  CYS A O   1 
ATOM   445  C  CB  . CYS A 1 84  ? 100.46000 47.90100 1.95600   1.000 8.04482  ? 84  CYS A CB  1 
ATOM   446  S  SG  . CYS A 1 84  ? 101.19400 49.27800 2.89200   1.000 9.25082  ? 84  CYS A SG  1 
ATOM   447  N  N   . SER A 1 85  ? 99.06800  45.67000 4.60300   1.000 5.77062  ? 85  SER A N   1 
ATOM   448  C  CA  . SER A 1 85  ? 98.18200  45.68600 5.75500   1.000 5.95420  ? 85  SER A CA  1 
ATOM   449  C  C   . SER A 1 85  ? 98.75600  44.81700 6.85900   1.000 5.77317  ? 85  SER A C   1 
ATOM   450  O  O   . SER A 1 85  ? 99.15000  43.67500 6.61100   1.000 6.21431  ? 85  SER A O   1 
ATOM   451  C  CB  . SER A 1 85  ? 96.81400  45.11500 5.38800   1.000 8.06736  ? 85  SER A CB  1 
ATOM   452  O  OG  . SER A 1 85  ? 96.15100  45.92800 4.44600   1.000 9.46327  ? 85  SER A OG  1 
ATOM   453  N  N   . TYR A 1 86  ? 98.73800  45.33300 8.08500   1.000 6.03453  ? 86  TYR A N   1 
ATOM   454  C  CA  . TYR A 1 86  ? 98.98600  44.49000 9.24400   1.000 5.82831  ? 86  TYR A CA  1 
ATOM   455  C  C   . TYR A 1 86  ? 97.74300  43.66500 9.55200   1.000 5.57562  ? 86  TYR A C   1 
ATOM   456  O  O   . TYR A 1 86  ? 96.61200  44.15500 9.45700   1.000 6.39777  ? 86  TYR A O   1 
ATOM   457  C  CB  . TYR A 1 86  ? 99.37200  45.34100 10.45200  1.000 6.38198  ? 86  TYR A CB  1 
ATOM   458  C  CG  . TYR A 1 86  ? 100.86300 45.51800 10.59900  1.000 6.33901  ? 86  TYR A CG  1 
ATOM   459  C  CD1 . TYR A 1 86  ? 101.63400 44.51500 11.15900  1.000 6.09913  ? 86  TYR A CD1 1 
ATOM   460  C  CD2 . TYR A 1 86  ? 101.49700 46.65900 10.13900  1.000 6.93916  ? 86  TYR A CD2 1 
ATOM   461  C  CE1 . TYR A 1 86  ? 102.98600 44.64800 11.28300  1.000 7.40732  ? 86  TYR A CE1 1 
ATOM   462  C  CE2 . TYR A 1 86  ? 102.85900 46.81400 10.26900  1.000 7.37378  ? 86  TYR A CE2 1 
ATOM   463  C  CZ  . TYR A 1 86  ? 103.59800 45.80000 10.84000  1.000 7.45767  ? 86  TYR A CZ  1 
ATOM   464  O  OH  . TYR A 1 86  ? 104.95400 45.92200 10.98800  1.000 9.30836  ? 86  TYR A OH  1 
ATOM   465  N  N   . GLY A 1 87  ? 97.96300  42.41400 9.92600   1.000 5.44155  ? 87  GLY A N   1 
ATOM   466  C  CA  . GLY A 1 87  ? 96.87200  41.52000 10.25700  1.000 5.49805  ? 87  GLY A CA  1 
ATOM   467  C  C   . GLY A 1 87  ? 97.25300  40.58600 11.38400  1.000 5.16424  ? 87  GLY A C   1 
ATOM   468  O  O   . GLY A 1 87  ? 98.41000  40.18900 11.53200  1.000 5.24579  ? 87  GLY A O   1 
ATOM   469  N  N   . TRP A 1 88  ? 96.24500  40.21200 12.16600  1.000 5.24100  ? 88  TRP A N   1 
ATOM   470  C  CA  . TRP A 1 88  ? 96.42900  39.29300 13.27500  1.000 5.39556  ? 88  TRP A CA  1 
ATOM   471  C  C   . TRP A 1 88  ? 96.82300  37.90300 12.78300  1.000 5.30871  ? 88  TRP A C   1 
ATOM   472  O  O   . TRP A 1 88  ? 96.35300  37.42300 11.74700  1.000 5.45741  ? 88  TRP A O   1 
ATOM   473  C  CB  . TRP A 1 88  ? 95.11800  39.16600 14.04700  1.000 6.16066  ? 88  TRP A CB  1 
ATOM   474  C  CG  . TRP A 1 88  ? 94.80900  40.33500 14.90700  1.000 6.33489  ? 88  TRP A CG  1 
ATOM   475  C  CD1 . TRP A 1 88  ? 93.82900  41.26300 14.70800  1.000 6.36881  ? 88  TRP A CD1 1 
ATOM   476  C  CD2 . TRP A 1 88  ? 95.47100  40.70100 16.11700  1.000 6.49310  ? 88  TRP A CD2 1 
ATOM   477  N  NE1 . TRP A 1 88  ? 93.83700  42.18700 15.73100  1.000 6.82758  ? 88  TRP A NE1 1 
ATOM   478  C  CE2 . TRP A 1 88  ? 94.83500  41.86000 16.60900  1.000 6.93548  ? 88  TRP A CE2 1 
ATOM   479  C  CE3 . TRP A 1 88  ? 96.53900  40.15700 16.84000  1.000 6.82788  ? 88  TRP A CE3 1 
ATOM   480  C  CZ2 . TRP A 1 88  ? 95.24100  42.49300 17.77700  1.000 8.33877  ? 88  TRP A CZ2 1 
ATOM   481  C  CZ3 . TRP A 1 88  ? 96.93800  40.78000 18.00100  1.000 7.97326  ? 88  TRP A CZ3 1 
ATOM   482  C  CH2 . TRP A 1 88  ? 96.29400  41.94200 18.45700  1.000 8.59347  ? 88  TRP A CH2 1 
ATOM   483  N  N   . VAL A 1 89  ? 97.66200  37.23800 13.57800  1.000 5.75732  ? 89  VAL A N   1 
ATOM   484  C  CA  . VAL A 1 89  ? 97.97100  35.82200 13.43400  1.000 6.00217  ? 89  VAL A CA  1 
ATOM   485  C  C   . VAL A 1 89  ? 97.73100  35.14300 14.77700  1.000 6.63092  ? 89  VAL A C   1 
ATOM   486  O  O   . VAL A 1 89  ? 97.52900  35.79400 15.80500  1.000 7.38690  ? 89  VAL A O   1 
ATOM   487  C  CB  . VAL A 1 89  ? 99.41000  35.56000 12.93300  1.000 6.38036  ? 89  VAL A CB  1 
ATOM   488  C  CG1 . VAL A 1 89  ? 99.57100  36.04600 11.50000  1.000 7.81216  ? 89  VAL A CG1 1 
ATOM   489  C  CG2 . VAL A 1 89  ? 100.44500 36.20100 13.84900  1.000 7.14299  ? 89  VAL A CG2 1 
ATOM   490  N  N   . GLY A 1 90  ? 97.75800  33.80600 14.75000  1.000 7.79091  ? 90  GLY A N   1 
ATOM   491  C  CA  . GLY A 1 90  ? 97.39100  33.00300 15.90900  1.000 9.27885  ? 90  GLY A CA  1 
ATOM   492  C  C   . GLY A 1 90  ? 98.26900  33.21000 17.12600  1.000 9.65631  ? 90  GLY A C   1 
ATOM   493  O  O   . GLY A 1 90  ? 97.83600  32.92300 18.25000  1.000 11.50957 ? 90  GLY A O   1 
ATOM   494  N  N   . GLU A 1 91  ? 99.49000  33.69700 16.93600  1.000 9.09586  ? 91  GLU A N   1 
ATOM   495  C  CA  . GLU A 1 91  ? 100.37700 34.00200 18.05300  1.000 9.58621  ? 91  GLU A CA  1 
ATOM   496  C  C   . GLU A 1 91  ? 99.92500  35.22100 18.84500  1.000 9.78367  ? 91  GLU A C   1 
ATOM   497  O  O   . GLU A 1 91  ? 100.57700 35.57300 19.83800  1.000 11.59036 ? 91  GLU A O   1 
ATOM   498  C  CB  . GLU A 1 91  ? 101.79900 34.23100 17.54300  1.000 10.88297 ? 91  GLU A CB  1 
ATOM   499  C  CG  . GLU A 1 91  ? 102.56200 32.96700 17.18900  1.000 11.88456 ? 91  GLU A CG  1 
ATOM   500  C  CD  . GLU A 1 91  ? 102.16500 32.37200 15.84600  1.000 11.96846 ? 91  GLU A CD  1 
ATOM   501  O  OE1 . GLU A 1 91  ? 101.50700 33.05400 15.04000  1.000 10.26939 ? 91  GLU A OE1 1 
ATOM   502  O  OE2 . GLU A 1 91  ? 102.50400 31.19100 15.61100  1.000 14.30688 ? 91  GLU A OE2 1 
ATOM   503  N  N   . GLN A 1 92  ? 98.85100  35.88600 18.42200  1.000 9.09209  ? 92  GLN A N   1 
ATOM   504  C  CA  . GLN A 1 92  ? 98.29800  37.04000 19.13200  1.000 9.46465  ? 92  GLN A CA  1 
ATOM   505  C  C   . GLN A 1 92  ? 99.23500  38.24700 19.04200  1.000 9.13446  ? 92  GLN A C   1 
ATOM   506  O  O   . GLN A 1 92  ? 99.41200  38.99300 20.00700  1.000 10.33014 ? 92  GLN A O   1 
ATOM   507  C  CB  . GLN A 1 92  ? 97.89300  36.72000 20.57500  1.000 11.17303 ? 92  GLN A CB  1 
ATOM   508  C  CG  . GLN A 1 92  ? 96.86900  37.67800 21.14900  1.000 14.07780 ? 92  GLN A CG  1 
ATOM   509  C  CD  . GLN A 1 92  ? 96.32300  37.20800 22.48300  1.000 15.17051 ? 92  GLN A CD  1 
ATOM   510  O  OE1 . GLN A 1 92  ? 96.02200  36.02700 22.66600  1.000 16.42363 ? 92  GLN A OE1 1 
ATOM   511  N  NE2 . GLN A 1 92  ? 96.21400  38.12800 23.43400  1.000 15.92229 ? 92  GLN A NE2 1 
ATOM   512  N  N   . PHE A 1 93  ? 99.86200  38.40500 17.88100  1.000 7.53399  ? 93  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 93  ? 100.46100 39.65800 17.45500  1.000 7.12903  ? 93  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 93  ? 100.05500 39.86500 16.00500  1.000 6.55524  ? 93  PHE A C   1 
ATOM   515  O  O   . PHE A 1 93  ? 99.42100  39.00000 15.39400  1.000 6.02137  ? 93  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 93  ? 101.97800 39.72500 17.69000  1.000 7.41384  ? 93  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 93  ? 102.76500 38.54600 17.16300  1.000 7.72724  ? 93  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 93  ? 102.86100 38.29000 15.81000  1.000 7.72292  ? 93  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 93  ? 103.47500 37.73400 18.03300  1.000 9.40732  ? 93  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 93  ? 103.60300 37.22000 15.33300  1.000 8.12658  ? 93  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 93  ? 104.22500 36.66600 17.56700  1.000 10.94219 ? 93  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 93  ? 104.28500 36.40600 16.21700  1.000 9.92812  ? 93  PHE A CZ  1 
ATOM   523  N  N   A SER A 1 94  ? 100.40500 41.02600 15.45500  0.537 7.72770  ? 94  SER A N   1 
ATOM   524  N  N   B SER A 1 94  ? 100.40700 41.01500 15.44600  0.463 5.45690  ? 94  SER A N   1 
ATOM   525  C  CA  A SER A 1 94  ? 100.06200 41.37300 14.08300  0.537 9.48398  ? 94  SER A CA  1 
ATOM   526  C  CA  B SER A 1 94  ? 100.05400 41.29400 14.06600  0.463 5.65816  ? 94  SER A CA  1 
ATOM   527  C  C   A SER A 1 94  ? 101.31100 41.28600 13.21600  0.537 7.86637  ? 94  SER A C   1 
ATOM   528  C  C   B SER A 1 94  ? 101.31000 41.26800 13.21300  0.463 5.86086  ? 94  SER A C   1 
ATOM   529  O  O   A SER A 1 94  ? 102.42000 41.51000 13.69600  0.537 7.67274  ? 94  SER A O   1 
ATOM   530  O  O   B SER A 1 94  ? 102.41300 41.51200 13.70100  0.463 5.79646  ? 94  SER A O   1 
ATOM   531  C  CB  A SER A 1 94  ? 99.50200  42.79700 14.02000  0.537 13.86967 ? 94  SER A CB  1 
ATOM   532  C  CB  B SER A 1 94  ? 99.37300  42.65100 13.94200  0.463 7.21382  ? 94  SER A CB  1 
ATOM   533  O  OG  A SER A 1 94  ? 98.93900  43.07200 12.75100  0.537 20.22640 ? 94  SER A OG  1 
ATOM   534  O  OG  B SER A 1 94  ? 98.37800  42.77000 14.93600  0.463 8.98861  ? 94  SER A OG  1 
ATOM   535  N  N   . VAL A 1 95  ? 101.13400 40.95800 11.93300  1.000 5.84828  ? 95  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 95  ? 102.25300 40.84100 11.00900  1.000 5.10346  ? 95  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 95  ? 101.92600 41.51000 9.68800   1.000 5.04762  ? 95  VAL A C   1 
ATOM   538  O  O   . VAL A 1 95  ? 100.76400 41.73200 9.34300   1.000 4.68868  ? 95  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 95  ? 102.68800 39.38300 10.73700  1.000 5.78687  ? 95  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 95  ? 102.98200 38.63300 12.02900  1.000 7.49609  ? 95  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 95  ? 101.64500 38.65600 9.89100   1.000 6.29061  ? 95  VAL A CG2 1 
ATOM   542  N  N   . ILE A 1 96  ? 102.98300 41.80600 8.93700   1.000 4.71149  ? 96  ILE A N   1 
ATOM   543  C  CA  . ILE A 1 96  ? 102.82900 42.25400 7.55600   1.000 5.01962  ? 96  ILE A CA  1 
ATOM   544  C  C   . ILE A 1 96  ? 103.87700 41.55100 6.70300   1.000 4.71455  ? 96  ILE A C   1 
ATOM   545  O  O   . ILE A 1 96  ? 105.06600 41.56400 7.05400   1.000 5.90994  ? 96  ILE A O   1 
ATOM   546  C  CB  . ILE A 1 96  ? 102.88800 43.78700 7.44500   1.000 5.54867  ? 96  ILE A CB  1 
ATOM   547  C  CG1 . ILE A 1 96  ? 102.55300 44.24600 6.02000   1.000 6.22548  ? 96  ILE A CG1 1 
ATOM   548  C  CG2 . ILE A 1 96  ? 104.24000 44.32700 7.90500   1.000 5.79733  ? 96  ILE A CG2 1 
ATOM   549  C  CD1 . ILE A 1 96  ? 102.41600 45.75100 5.88600   1.000 7.08989  ? 96  ILE A CD1 1 
ATOM   550  N  N   . PRO A 1 97  ? 103.48100 40.88800 5.62300   1.000 4.94626  ? 97  PRO A N   1 
ATOM   551  C  CA  . PRO A 1 97  ? 104.46100 40.27300 4.72300   1.000 4.90664  ? 97  PRO A CA  1 
ATOM   552  C  C   . PRO A 1 97  ? 104.90600 41.25800 3.65800   1.000 4.94221  ? 97  PRO A C   1 
ATOM   553  O  O   . PRO A 1 97  ? 104.07400 41.82200 2.94100   1.000 5.66996  ? 97  PRO A O   1 
ATOM   554  C  CB  . PRO A 1 97  ? 103.67200 39.11900 4.10600   1.000 5.58542  ? 97  PRO A CB  1 
ATOM   555  C  CG  . PRO A 1 97  ? 102.26100 39.62600 4.06300   1.000 5.68808  ? 97  PRO A CG  1 
ATOM   556  C  CD  . PRO A 1 97  ? 102.09800 40.60700 5.19800   1.000 5.51532  ? 97  PRO A CD  1 
ATOM   557  N  N   . ARG A 1 98  ? 106.21200 41.47200 3.55400   1.000 5.33441  ? 98  ARG A N   1 
ATOM   558  C  CA  . ARG A 1 98  ? 106.78800 42.43700 2.63400   1.000 5.28552  ? 98  ARG A CA  1 
ATOM   559  C  C   . ARG A 1 98  ? 107.88400 41.77200 1.82300   1.000 5.75419  ? 98  ARG A C   1 
ATOM   560  O  O   . ARG A 1 98  ? 108.75800 41.09300 2.37100   1.000 6.37453  ? 98  ARG A O   1 
ATOM   561  C  CB  . ARG A 1 98  ? 107.39600 43.62000 3.38800   1.000 5.63989  ? 98  ARG A CB  1 
ATOM   562  C  CG  . ARG A 1 98  ? 106.39300 44.47300 4.14300   1.000 5.85221  ? 98  ARG A CG  1 
ATOM   563  C  CD  . ARG A 1 98  ? 105.31100 45.04500 3.24800   1.000 5.47872  ? 98  ARG A CD  1 
ATOM   564  N  NE  . ARG A 1 98  ? 105.90300 45.78700 2.12700   1.000 5.75179  ? 98  ARG A NE  1 
ATOM   565  C  CZ  . ARG A 1 98  ? 105.26200 46.10700 1.00100   1.000 5.78584  ? 98  ARG A CZ  1 
ATOM   566  N  NH1 . ARG A 1 98  ? 104.00000 45.74700 0.81100   1.000 6.93294  ? 98  ARG A NH1 1 
ATOM   567  N  NH2 . ARG A 1 98  ? 105.89500 46.77300 0.04700   1.000 7.26915  ? 98  ARG A NH2 1 
ATOM   568  N  N   . ILE A 1 99  ? 107.84700 41.98400 0.52400   1.000 6.04692  ? 99  ILE A N   1 
ATOM   569  C  CA  . ILE A 1 99  ? 108.89300 41.53200 -0.37200  1.000 6.41039  ? 99  ILE A CA  1 
ATOM   570  C  C   . ILE A 1 99  ? 109.72800 42.70300 -0.86400  1.000 6.73410  ? 99  ILE A C   1 
ATOM   571  O  O   . ILE A 1 99  ? 110.95800 42.65900 -0.83300  1.000 8.33735  ? 99  ILE A O   1 
ATOM   572  C  CB  . ILE A 1 99  ? 108.30000 40.71300 -1.54000  1.000 7.73615  ? 99  ILE A CB  1 
ATOM   573  C  CG1 . ILE A 1 99  ? 107.66700 39.42900 -0.99700  1.000 8.81109  ? 99  ILE A CG1 1 
ATOM   574  C  CG2 . ILE A 1 99  ? 109.36100 40.41500 -2.58500  1.000 9.08224  ? 99  ILE A CG2 1 
ATOM   575  C  CD1 . ILE A 1 99  ? 106.78000 38.71600 -1.99300  1.000 9.58394  ? 99  ILE A CD1 1 
ATOM   576  N  N   . PHE A 1 100 ? 109.07100 43.77400 -1.28100  1.000 6.93059  ? 100 PHE A N   1 
ATOM   577  C  CA  . PHE A 1 100 ? 109.71600 45.02700 -1.62900  1.000 7.32183  ? 100 PHE A CA  1 
ATOM   578  C  C   . PHE A 1 100 ? 109.60800 45.97400 -0.44900  1.000 7.02687  ? 100 PHE A C   1 
ATOM   579  O  O   . PHE A 1 100 ? 108.59600 46.00400 0.25100   1.000 7.93615  ? 100 PHE A O   1 
ATOM   580  C  CB  . PHE A 1 100 ? 109.01000 45.65500 -2.82400  1.000 8.72498  ? 100 PHE A CB  1 
ATOM   581  C  CG  . PHE A 1 100 ? 109.28400 44.94400 -4.08500  1.000 9.74673  ? 100 PHE A CG  1 
ATOM   582  C  CD1 . PHE A 1 100 ? 108.59600 43.79100 -4.40700  1.000 10.16570 ? 100 PHE A CD1 1 
ATOM   583  C  CD2 . PHE A 1 100 ? 110.27400 45.39400 -4.93600  1.000 10.97885 ? 100 PHE A CD2 1 
ATOM   584  C  CE1 . PHE A 1 100 ? 108.87100 43.11800 -5.57300  1.000 11.63591 ? 100 PHE A CE1 1 
ATOM   585  C  CE2 . PHE A 1 100 ? 110.55000 44.72400 -6.10100  1.000 12.53166 ? 100 PHE A CE2 1 
ATOM   586  C  CZ  . PHE A 1 100 ? 109.84900 43.58200 -6.41400  1.000 11.36514 ? 100 PHE A CZ  1 
ATOM   587  N  N   A SER A 1 101 ? 110.63500 46.79200 -0.24800  0.220 7.67670  ? 101 SER A N   1 
ATOM   588  N  N   B SER A 1 101 ? 110.67800 46.70500 -0.18900  0.780 6.45143  ? 101 SER A N   1 
ATOM   589  C  CA  A SER A 1 101 ? 110.64500 47.73500 0.86600   0.220 8.71814  ? 101 SER A CA  1 
ATOM   590  C  CA  B SER A 1 101 ? 110.59500 47.72200 0.84000   0.780 7.58315  ? 101 SER A CA  1 
ATOM   591  C  C   A SER A 1 101 ? 109.90800 49.01500 0.48900   0.220 7.72572  ? 101 SER A C   1 
ATOM   592  C  C   B SER A 1 101 ? 109.69500 48.84800 0.35700   0.780 8.61100  ? 101 SER A C   1 
ATOM   593  O  O   A SER A 1 101 ? 110.27800 49.69000 -0.47900  0.220 6.71197  ? 101 SER A O   1 
ATOM   594  O  O   B SER A 1 101 ? 109.70600 49.22200 -0.81900  0.780 10.16602 ? 101 SER A O   1 
ATOM   595  C  CB  A SER A 1 101 ? 112.07300 48.05100 1.29400   0.220 10.39712 ? 101 SER A CB  1 
ATOM   596  C  CB  B SER A 1 101 ? 111.97800 48.26200 1.17400   0.780 8.59081  ? 101 SER A CB  1 
ATOM   597  O  OG  A SER A 1 101 ? 112.45200 47.21900 2.37300   0.220 12.73801 ? 101 SER A OG  1 
ATOM   598  O  OG  B SER A 1 101 ? 112.61000 48.73900 0.01400   0.780 10.52621 ? 101 SER A OG  1 
ATOM   599  N  N   . ASN A 1 102 ? 108.88300 49.36300 1.27300   1.000 7.26373  ? 102 ASN A N   1 
ATOM   600  C  CA  . ASN A 1 102 ? 108.07800 50.53400 1.01000   1.000 7.20951  ? 102 ASN A CA  1 
ATOM   601  C  C   . ASN A 1 102 ? 107.94400 51.30300 2.31400   1.000 7.05422  ? 102 ASN A C   1 
ATOM   602  O  O   . ASN A 1 102 ? 107.59700 50.70200 3.34100   1.000 7.36268  ? 102 ASN A O   1 
ATOM   603  C  CB  . ASN A 1 102 ? 106.69400 50.13100 0.49800   1.000 9.53543  ? 102 ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 102 ? 105.88800 51.31300 0.02100   1.000 11.22031 ? 102 ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 102 ? 105.52000 52.18600 0.80800   1.000 10.14720 ? 102 ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 102 ? 105.62500 51.36500 -1.28300  1.000 13.71245 ? 102 ASN A ND2 1 
ATOM   607  N  N   . PRO A 1 103 ? 108.19800 52.61100 2.31500   1.000 7.49124  ? 103 PRO A N   1 
ATOM   608  C  CA  . PRO A 1 103 ? 108.19100 53.35500 3.58700   1.000 8.11404  ? 103 PRO A CA  1 
ATOM   609  C  C   . PRO A 1 103 ? 106.87700 53.29800 4.33800   1.000 7.74177  ? 103 PRO A C   1 
ATOM   610  O  O   . PRO A 1 103 ? 106.87300 53.47100 5.56400   1.000 9.53883  ? 103 PRO A O   1 
ATOM   611  C  CB  . PRO A 1 103 ? 108.52200 54.79400 3.17000   1.000 9.87037  ? 103 PRO A CB  1 
ATOM   612  C  CG  . PRO A 1 103 ? 108.39500 54.82900 1.68200   1.000 12.64899 ? 103 PRO A CG  1 
ATOM   613  C  CD  . PRO A 1 103 ? 108.62500 53.44600 1.17900   1.000 9.79970  ? 103 PRO A CD  1 
ATOM   614  N  N   . ARG A 1 104 ? 105.76400 53.06700 3.65000   1.000 7.93526  ? 104 ARG A N   1 
ATOM   615  C  CA  . ARG A 1 104 ? 104.45100 53.09400 4.27800   1.000 8.29139  ? 104 ARG A CA  1 
ATOM   616  C  C   . ARG A 1 104 ? 103.93200 51.71300 4.65300   1.000 7.54485  ? 104 ARG A C   1 
ATOM   617  O  O   . ARG A 1 104 ? 102.79600 51.59500 5.12500   1.000 8.76031  ? 104 ARG A O   1 
ATOM   618  C  CB  . ARG A 1 104 ? 103.46200 53.84800 3.39500   1.000 12.48172 ? 104 ARG A CB  1 
ATOM   619  C  CG  . ARG A 1 104 ? 103.57200 55.35300 3.62000   1.000 17.81208 ? 104 ARG A CG  1 
ATOM   620  C  CD  . ARG A 1 104 ? 102.98500 56.17300 2.49500   1.000 22.00516 ? 104 ARG A CD  1 
ATOM   621  N  NE  . ARG A 1 104 ? 103.91500 56.24600 1.37400   1.000 25.21990 ? 104 ARG A NE  1 
ATOM   622  C  CZ  . ARG A 1 104 ? 104.96500 57.06300 1.31900   1.000 28.51064 ? 104 ARG A CZ  1 
ATOM   623  N  NH1 . ARG A 1 104 ? 105.23000 57.89000 2.32400   1.000 29.34678 ? 104 ARG A NH1 1 
ATOM   624  N  NH2 . ARG A 1 104 ? 105.75400 57.04800 0.25600   1.000 28.54178 ? 104 ARG A NH2 1 
ATOM   625  N  N   . CYS A 1 105 ? 104.74200 50.67400 4.48000   1.000 7.55844  ? 105 CYS A N   1 
ATOM   626  C  CA  . CYS A 1 105 ? 104.31700 49.30000 4.73400   1.000 7.95605  ? 105 CYS A CA  1 
ATOM   627  C  C   . CYS A 1 105 ? 105.36900 48.61100 5.59000   1.000 7.92367  ? 105 CYS A C   1 
ATOM   628  O  O   . CYS A 1 105 ? 106.46900 48.32800 5.11100   1.000 10.01901 ? 105 CYS A O   1 
ATOM   629  C  CB  . CYS A 1 105 ? 104.11000 48.54800 3.41300   1.000 9.13048  ? 105 CYS A CB  1 
ATOM   630  S  SG  . CYS A 1 105 ? 103.10500 49.43100 2.18700   1.000 9.54306  ? 105 CYS A SG  1 
ATOM   631  N  N   . GLY A 1 106 ? 105.03800 48.30700 6.83700   1.000 7.86950  ? 106 GLY A N   1 
ATOM   632  C  CA  . GLY A 1 106 ? 106.03400 47.68900 7.69300   1.000 7.72968  ? 106 GLY A CA  1 
ATOM   633  C  C   . GLY A 1 106 ? 107.26800 48.53000 7.90700   1.000 7.55636  ? 106 GLY A C   1 
ATOM   634  O  O   . GLY A 1 106 ? 108.36500 47.97900 8.05100   1.000 8.24384  ? 106 GLY A O   1 
ATOM   635  N  N   . LYS A 1 107 ? 107.11700 49.85500 7.92800   1.000 8.67436  ? 107 LYS A N   1 
ATOM   636  C  CA  . LYS A 1 107 ? 108.22800 50.78600 8.11300   1.000 10.06142 ? 107 LYS A CA  1 
ATOM   637  C  C   . LYS A 1 107 ? 109.43900 50.42100 7.27500   1.000 8.44620  ? 107 LYS A C   1 
ATOM   638  O  O   . LYS A 1 107 ? 110.57100 50.39800 7.75900   1.000 8.78348  ? 107 LYS A O   1 
ATOM   639  C  CB  . LYS A 1 107 ? 108.60600 51.01100 9.57400   1.000 15.62050 ? 107 LYS A CB  1 
ATOM   640  C  CG  . LYS A 1 107 ? 107.52800 51.62500 10.43500  1.000 19.93820 ? 107 LYS A CG  1 
ATOM   641  C  CD  . LYS A 1 107 ? 108.15300 52.14000 11.72000  1.000 27.18534 ? 107 LYS A CD  1 
ATOM   642  C  CE  . LYS A 1 107 ? 107.15500 52.90100 12.56500  1.000 33.76215 ? 107 LYS A CE  1 
ATOM   643  N  NZ  . LYS A 1 107 ? 107.52700 52.88600 14.00500  1.000 35.20290 ? 107 LYS A NZ  1 
ATOM   644  N  N   . ASN A 1 108 ? 109.19100 50.15800 5.99800   1.000 7.00521  ? 108 ASN A N   1 
ATOM   645  C  CA  . ASN A 1 108 ? 110.23800 49.93400 5.00800   1.000 7.19033  ? 108 ASN A CA  1 
ATOM   646  C  C   . ASN A 1 108 ? 110.91200 48.57100 5.12700   1.000 7.20957  ? 108 ASN A C   1 
ATOM   647  O  O   . ASN A 1 108 ? 111.91100 48.32700 4.43800   1.000 8.84219  ? 108 ASN A O   1 
ATOM   648  C  CB  . ASN A 1 108 ? 111.29300 51.04800 5.01700   1.000 7.80765  ? 108 ASN A CB  1 
ATOM   649  C  CG  . ASN A 1 108 ? 111.95100 51.22500 3.68700   1.000 9.02024  ? 108 ASN A CG  1 
ATOM   650  O  OD1 . ASN A 1 108 ? 111.27400 51.34500 2.66300   1.000 9.78573  ? 108 ASN A OD1 1 
ATOM   651  N  ND2 . ASN A 1 108 ? 113.28100 51.24800 3.68600   1.000 10.51230 ? 108 ASN A ND2 1 
ATOM   652  N  N   . GLY A 1 109 ? 110.40400 47.67400 5.97300   1.000 6.69857  ? 109 GLY A N   1 
ATOM   653  C  CA  . GLY A 1 109 ? 111.06700 46.40400 6.19100   1.000 7.45576  ? 109 GLY A CA  1 
ATOM   654  C  C   . GLY A 1 109 ? 110.78200 45.39200 5.09700   1.000 6.38163  ? 109 GLY A C   1 
ATOM   655  O  O   . GLY A 1 109 ? 109.91000 45.57100 4.24800   1.000 6.86737  ? 109 GLY A O   1 
ATOM   656  N  N   . LYS A 1 110 ? 111.54000 44.30000 5.13200   1.000 6.75934  ? 110 LYS A N   1 
ATOM   657  C  CA  . LYS A 1 110 ? 111.31600 43.16300 4.25600   1.000 7.09717  ? 110 LYS A CA  1 
ATOM   658  C  C   . LYS A 1 110 ? 111.23400 41.91000 5.11100   1.000 7.08074  ? 110 LYS A C   1 
ATOM   659  O  O   . LYS A 1 110 ? 111.90900 41.79400 6.13600   1.000 9.23070  ? 110 LYS A O   1 
ATOM   660  C  CB  . LYS A 1 110 ? 112.45600 42.99700 3.25900   1.000 8.28325  ? 110 LYS A CB  1 
ATOM   661  C  CG  . LYS A 1 110 ? 112.54500 44.09400 2.22000   1.000 10.32586 ? 110 LYS A CG  1 
ATOM   662  C  CD  . LYS A 1 110 ? 113.71300 43.81100 1.28600   1.000 13.71005 ? 110 LYS A CD  1 
ATOM   663  C  CE  . LYS A 1 110 ? 114.14500 45.02700 0.50200   1.000 17.39644 ? 110 LYS A CE  1 
ATOM   664  N  NZ  . LYS A 1 110 ? 115.20800 44.65400 -0.47800  1.000 19.28318 ? 110 LYS A NZ  1 
ATOM   665  N  N   . GLY A 1 111 ? 110.43800 40.95400 4.66000   1.000 6.69980  ? 111 GLY A N   1 
ATOM   666  C  CA  . GLY A 1 111 ? 110.22000 39.73300 5.40800   1.000 7.72976  ? 111 GLY A CA  1 
ATOM   667  C  C   . GLY A 1 111 ? 108.81400 39.67200 5.96300   1.000 7.75597  ? 111 GLY A C   1 
ATOM   668  O  O   . GLY A 1 111 ? 107.86200 40.10100 5.31300   1.000 11.34574 ? 111 GLY A O   1 
ATOM   669  N  N   . VAL A 1 112 ? 108.63000 39.07200 7.12200   1.000 7.34285  ? 112 VAL A N   1 
ATOM   670  C  CA  . VAL A 1 112 ? 107.35500 39.12300 7.82000   1.000 7.41040  ? 112 VAL A CA  1 
ATOM   671  C  C   . VAL A 1 112 ? 107.60900 39.93600 9.07500   1.000 7.60564  ? 112 VAL A C   1 
ATOM   672  O  O   . VAL A 1 112 ? 108.35000 39.50300 9.97200   1.000 9.46030  ? 112 VAL A O   1 
ATOM   673  C  CB  . VAL A 1 112 ? 106.82000 37.72300 8.13900   1.000 7.81137  ? 112 VAL A CB  1 
ATOM   674  C  CG1 . VAL A 1 112 ? 105.57600 37.80700 9.02000   1.000 9.70629  ? 112 VAL A CG1 1 
ATOM   675  C  CG2 . VAL A 1 112 ? 106.51300 36.98300 6.85900   1.000 9.31673  ? 112 VAL A CG2 1 
ATOM   676  N  N   . LEU A 1 113 ? 107.04900 41.14400 9.13300   1.000 6.60394  ? 113 LEU A N   1 
ATOM   677  C  CA  . LEU A 1 113 ? 107.46500 42.10400 10.15000  1.000 7.00745  ? 113 LEU A CA  1 
ATOM   678  C  C   . LEU A 1 113 ? 106.37900 41.99100 11.22100  1.000 6.64258  ? 113 LEU A C   1 
ATOM   679  O  O   . LEU A 1 113 ? 105.19600 41.81400 10.88900  1.000 6.74543  ? 113 LEU A O   1 
ATOM   680  C  CB  . LEU A 1 113 ? 107.41900 43.51800 9.56900   1.000 9.33487  ? 113 LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 113 ? 108.58400 44.05100 8.68900   1.000 14.27561 ? 113 LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 113 ? 110.00300 44.20800 9.31300   1.000 20.09900 ? 113 LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 113 ? 108.52800 43.37400 7.27600   1.000 17.28262 ? 113 LEU A CD2 1 
ATOM   684  N  N   . ILE A 1 114 ? 106.77400 42.11700 12.49600  1.000 7.34559  ? 114 ILE A N   1 
ATOM   685  C  CA  . ILE A 1 114 ? 105.90600 41.88500 13.65000  1.000 7.70143  ? 114 ILE A CA  1 
ATOM   686  C  C   . ILE A 1 114 ? 105.59800 43.19800 14.35800  1.000 8.26198  ? 114 ILE A C   1 
ATOM   687  O  O   . ILE A 1 114 ? 106.48500 44.02900 14.57200  1.000 9.42438  ? 114 ILE A O   1 
ATOM   688  C  CB  . ILE A 1 114 ? 106.56300 40.88200 14.61600  1.000 9.57633  ? 114 ILE A CB  1 
ATOM   689  C  CG1 . ILE A 1 114 ? 106.73300 39.52900 13.93300  1.000 12.39241 ? 114 ILE A CG1 1 
ATOM   690  C  CG2 . ILE A 1 114 ? 105.75700 40.75600 15.90400  1.000 10.71748 ? 114 ILE A CG2 1 
ATOM   691  C  CD1 . ILE A 1 114 ? 107.44500 38.51800 14.78000  1.000 14.18577 ? 114 ILE A CD1 1 
ATOM   692  N  N   . TRP A 1 115 ? 104.34200 43.35700 14.74900  1.000 8.02125  ? 115 TRP A N   1 
ATOM   693  C  CA  . TRP A 1 115 ? 103.88800 44.46000 15.57800  1.000 7.98995  ? 115 TRP A CA  1 
ATOM   694  C  C   . TRP A 1 115 ? 103.16200 43.81700 16.75200  1.000 8.81425  ? 115 TRP A C   1 
ATOM   695  O  O   . TRP A 1 115 ? 102.09900 43.20400 16.57600  1.000 9.00910  ? 115 TRP A O   1 
ATOM   696  C  CB  . TRP A 1 115 ? 102.95400 45.35500 14.77200  1.000 8.58531  ? 115 TRP A CB  1 
ATOM   697  C  CG  . TRP A 1 115 ? 102.45600 46.60100 15.42900  1.000 9.54090  ? 115 TRP A CG  1 
ATOM   698  C  CD1 . TRP A 1 115 ? 102.56500 46.97200 16.74800  1.000 10.92570 ? 115 TRP A CD1 1 
ATOM   699  C  CD2 . TRP A 1 115 ? 101.76100 47.65600 14.77200  1.000 10.02789 ? 115 TRP A CD2 1 
ATOM   700  N  NE1 . TRP A 1 115 ? 101.96500 48.19700 16.93400  1.000 12.08403 ? 115 TRP A NE1 1 
ATOM   701  C  CE2 . TRP A 1 115 ? 101.46100 48.63300 15.73600  1.000 12.18352 ? 115 TRP A CE2 1 
ATOM   702  C  CE3 . TRP A 1 115 ? 101.35500 47.85900 13.45100  1.000 10.45467 ? 115 TRP A CE3 1 
ATOM   703  C  CZ2 . TRP A 1 115 ? 100.78000 49.80400 15.41500  1.000 12.60744 ? 115 TRP A CZ2 1 
ATOM   704  C  CZ3 . TRP A 1 115 ? 100.67700 49.00300 13.13600  1.000 11.76703 ? 115 TRP A CZ3 1 
ATOM   705  C  CH2 . TRP A 1 115 ? 100.39200 49.96500 14.11100  1.000 12.37355 ? 115 TRP A CH2 1 
ATOM   706  N  N   . ASN A 1 116 ? 103.77500 43.89800 17.92900  1.000 9.37410  ? 116 ASN A N   1 
ATOM   707  C  CA  . ASN A 1 116 ? 103.18800 43.36100 19.15000  1.000 10.90302 ? 116 ASN A CA  1 
ATOM   708  C  C   . ASN A 1 116 ? 102.28000 44.43800 19.72100  1.000 10.57467 ? 116 ASN A C   1 
ATOM   709  O  O   . ASN A 1 116 ? 102.76600 45.43900 20.25100  1.000 14.72585 ? 116 ASN A O   1 
ATOM   710  C  CB  . ASN A 1 116 ? 104.29000 43.04900 20.15500  1.000 13.88893 ? 116 ASN A CB  1 
ATOM   711  C  CG  . ASN A 1 116 ? 105.12300 41.85800 19.75100  1.000 17.06618 ? 116 ASN A CG  1 
ATOM   712  O  OD1 . ASN A 1 116 ? 104.64900 40.72300 19.75300  1.000 19.98081 ? 116 ASN A OD1 1 
ATOM   713  N  ND2 . ASN A 1 116 ? 106.37600 42.10900 19.40500  1.000 18.03325 ? 116 ASN A ND2 1 
ATOM   714  N  N   . ALA A 1 117 ? 100.97700 44.24500 19.61300  1.000 11.68581 ? 117 ALA A N   1 
ATOM   715  C  CA  . ALA A 1 117 ? 99.99000  45.20500 20.07800  1.000 12.81205 ? 117 ALA A CA  1 
ATOM   716  C  C   . ALA A 1 117 ? 98.95700  44.49000 20.93300  1.000 11.79025 ? 117 ALA A C   1 
ATOM   717  O  O   . ALA A 1 117 ? 98.76000  43.27600 20.79500  1.000 12.18492 ? 117 ALA A O   1 
ATOM   718  C  CB  . ALA A 1 117 ? 99.29200  45.87800 18.88700  1.000 14.74115 ? 117 ALA A CB  1 
ATOM   719  N  N   . PRO A 1 118 ? 98.27500  45.21300 21.82500  1.000 11.48749 ? 118 PRO A N   1 
ATOM   720  C  CA  . PRO A 1 118 ? 97.24600  44.57600 22.65400  1.000 10.97790 ? 118 PRO A CA  1 
ATOM   721  C  C   . PRO A 1 118 ? 96.15400  43.94200 21.81000  1.000 10.37823 ? 118 PRO A C   1 
ATOM   722  O  O   . PRO A 1 118 ? 95.84800  44.38900 20.70200  1.000 10.07647 ? 118 PRO A O   1 
ATOM   723  C  CB  . PRO A 1 118 ? 96.69100  45.73800 23.48400  1.000 12.47567 ? 118 PRO A CB  1 
ATOM   724  C  CG  . PRO A 1 118 ? 97.80000  46.71200 23.53500  1.000 13.85206 ? 118 PRO A CG  1 
ATOM   725  C  CD  . PRO A 1 118 ? 98.48200  46.62200 22.20300  1.000 13.18759 ? 118 PRO A CD  1 
ATOM   726  N  N   . SER A 1 119 ? 95.55600  42.88900 22.36800  1.000 10.91332 ? 119 SER A N   1 
ATOM   727  C  CA  . SER A 1 119 ? 94.52100  42.14000 21.67000  1.000 11.17764 ? 119 SER A CA  1 
ATOM   728  C  C   . SER A 1 119 ? 93.30100  42.98700 21.34300  1.000 10.45858 ? 119 SER A C   1 
ATOM   729  O  O   . SER A 1 119 ? 92.49000  42.58200 20.50300  1.000 10.92517 ? 119 SER A O   1 
ATOM   730  C  CB  . SER A 1 119 ? 94.11100  40.93000 22.50500  1.000 12.84659 ? 119 SER A CB  1 
ATOM   731  O  OG  . SER A 1 119 ? 93.53400  41.33500 23.72900  1.000 13.61468 ? 119 SER A OG  1 
ATOM   732  N  N   . SER A 1 120 ? 93.15100  44.15000 21.98300  1.000 11.51800 ? 120 SER A N   1 
ATOM   733  C  CA  . SER A 1 120 ? 92.03900  45.04900 21.69900  1.000 12.82228 ? 120 SER A CA  1 
ATOM   734  C  C   . SER A 1 120 ? 92.25500  45.89000 20.44500  1.000 12.68685 ? 120 SER A C   1 
ATOM   735  O  O   . SER A 1 120 ? 91.29500  46.48300 19.94300  1.000 13.65244 ? 120 SER A O   1 
ATOM   736  C  CB  . SER A 1 120 ? 91.84700  46.00300 22.87900  1.000 14.25537 ? 120 SER A CB  1 
ATOM   737  O  OG  . SER A 1 120 ? 93.09300  46.55700 23.26000  1.000 15.08124 ? 120 SER A OG  1 
ATOM   738  N  N   . GLN A 1 121 ? 93.48000  45.97300 19.93900  1.000 11.60410 ? 121 GLN A N   1 
ATOM   739  C  CA  . GLN A 1 121 ? 93.77100  46.85100 18.81400  1.000 11.00624 ? 121 GLN A CA  1 
ATOM   740  C  C   . GLN A 1 121 ? 93.23700  46.26800 17.50700  1.000 9.84181  ? 121 GLN A C   1 
ATOM   741  O  O   . GLN A 1 121 ? 93.20700  45.05300 17.31200  1.000 10.46033 ? 121 GLN A O   1 
ATOM   742  C  CB  . GLN A 1 121 ? 95.27800  47.07900 18.71800  1.000 12.92221 ? 121 GLN A CB  1 
ATOM   743  C  CG  . GLN A 1 121 ? 95.68000  48.13500 17.70100  1.000 16.13790 ? 121 GLN A CG  1 
ATOM   744  C  CD  . GLN A 1 121 ? 97.02800  48.75900 18.00000  1.000 18.17517 ? 121 GLN A CD  1 
ATOM   745  O  OE1 . GLN A 1 121 ? 97.51200  48.71500 19.13000  1.000 20.26799 ? 121 GLN A OE1 1 
ATOM   746  N  NE2 . GLN A 1 121 ? 97.64000  49.35100 16.98300  1.000 18.95712 ? 121 GLN A NE2 1 
ATOM   747  N  N   . LYS A 1 122 ? 92.82000  47.15500 16.60000  1.000 10.03634 ? 122 LYS A N   1 
ATOM   748  C  CA  . LYS A 1 122 ? 92.19100  46.74500 15.34600  1.000 10.59825 ? 122 LYS A CA  1 
ATOM   749  C  C   . LYS A 1 122 ? 93.21300  46.56100 14.23000  1.000 9.27250  ? 122 LYS A C   1 
ATOM   750  O  O   . LYS A 1 122 ? 93.99700  47.47100 13.93000  1.000 10.50402 ? 122 LYS A O   1 
ATOM   751  C  CB  . LYS A 1 122 ? 91.15400  47.77000 14.89000  1.000 13.26279 ? 122 LYS A CB  1 
ATOM   752  C  CG  . LYS A 1 122 ? 90.14900  48.16200 15.94300  1.000 15.61959 ? 122 LYS A CG  1 
ATOM   753  C  CD  . LYS A 1 122 ? 89.37600  46.98400 16.48300  1.000 17.83456 ? 122 LYS A CD  1 
ATOM   754  C  CE  . LYS A 1 122 ? 88.10200  47.47200 17.16100  1.000 20.89480 ? 122 LYS A CE  1 
ATOM   755  N  NZ  . LYS A 1 122 ? 87.20600  46.35900 17.57100  1.000 22.81533 ? 122 LYS A NZ  1 
ATOM   756  N  N   . PHE A 1 123 ? 93.16400  45.39500 13.58700  1.000 8.16185  ? 123 PHE A N   1 
ATOM   757  C  CA  . PHE A 1 123 ? 93.98100  45.06600 12.43000  1.000 7.48358  ? 123 PHE A CA  1 
ATOM   758  C  C   . PHE A 1 123 ? 93.12900  44.22300 11.48800  1.000 6.91840  ? 123 PHE A C   1 
ATOM   759  O  O   . PHE A 1 123 ? 91.98800  43.86400 11.80100  1.000 7.67076  ? 123 PHE A O   1 
ATOM   760  C  CB  . PHE A 1 123 ? 95.21600  44.25200 12.83400  1.000 7.77867  ? 123 PHE A CB  1 
ATOM   761  C  CG  . PHE A 1 123 ? 96.19800  44.99300 13.69300  1.000 7.97250  ? 123 PHE A CG  1 
ATOM   762  C  CD1 . PHE A 1 123 ? 97.07200  45.91900 13.14300  1.000 8.92544  ? 123 PHE A CD1 1 
ATOM   763  C  CD2 . PHE A 1 123 ? 96.26300  44.74900 15.05100  1.000 9.11162  ? 123 PHE A CD2 1 
ATOM   764  C  CE1 . PHE A 1 123 ? 97.98400  46.59100 13.93500  1.000 10.51886 ? 123 PHE A CE1 1 
ATOM   765  C  CE2 . PHE A 1 123 ? 97.17700  45.41600 15.84400  1.000 10.55181 ? 123 PHE A CE2 1 
ATOM   766  C  CZ  . PHE A 1 123 ? 98.03900  46.33200 15.28400  1.000 10.84211 ? 123 PHE A CZ  1 
ATOM   767  N  N   . LYS A 1 124 ? 93.68500  43.87800 10.33500  1.000 6.85778  ? 124 LYS A N   1 
ATOM   768  C  CA  . LYS A 1 124 ? 93.04100  42.89500 9.47800   1.000 6.09204  ? 124 LYS A CA  1 
ATOM   769  C  C   . LYS A 1 124 ? 93.36400  41.51200 10.03100  1.000 5.94785  ? 124 LYS A C   1 
ATOM   770  O  O   . LYS A 1 124 ? 93.85800  41.37800 11.15300  1.000 6.12378  ? 124 LYS A O   1 
ATOM   771  C  CB  . LYS A 1 124 ? 93.44900  43.12900 8.03100   1.000 7.18794  ? 124 LYS A CB  1 
ATOM   772  C  CG  . LYS A 1 124 ? 92.88900  44.43500 7.47700   1.000 8.35597  ? 124 LYS A CG  1 
ATOM   773  C  CD  . LYS A 1 124 ? 93.19900  44.59100 6.00300   1.000 9.55012  ? 124 LYS A CD  1 
ATOM   774  C  CE  . LYS A 1 124 ? 92.74500  45.92500 5.45900   1.000 11.51436 ? 124 LYS A CE  1 
ATOM   775  N  NZ  . LYS A 1 124 ? 93.19700  46.08800 4.05400   1.000 14.19507 ? 124 LYS A NZ  1 
ATOM   776  N  N   . ALA A 1 125 ? 93.08000  40.46400 9.26100   1.000 6.23276  ? 125 ALA A N   1 
ATOM   777  C  CA  . ALA A 1 125 ? 93.35500  39.09400 9.66800   1.000 5.96304  ? 125 ALA A CA  1 
ATOM   778  C  C   . ALA A 1 125 ? 94.11000  38.38300 8.55700   1.000 5.16414  ? 125 ALA A C   1 
ATOM   779  O  O   . ALA A 1 125 ? 93.85000  38.61800 7.37600   1.000 6.23627  ? 125 ALA A O   1 
ATOM   780  C  CB  . ALA A 1 125 ? 92.05500  38.32700 9.92300   1.000 7.02064  ? 125 ALA A CB  1 
ATOM   781  N  N   . TYR A 1 126 ? 95.03000  37.50400 8.92600   1.000 5.00512  ? 126 TYR A N   1 
ATOM   782  C  CA  . TYR A 1 126 ? 95.56600  36.52600 7.98300   1.000 4.87738  ? 126 TYR A CA  1 
ATOM   783  C  C   . TYR A 1 126 ? 94.90400  35.19400 8.29500   1.000 5.19994  ? 126 TYR A C   1 
ATOM   784  O  O   . TYR A 1 126 ? 94.96800  34.72500 9.43400   1.000 5.90667  ? 126 TYR A O   1 
ATOM   785  C  CB  . TYR A 1 126 ? 97.09500  36.42800 8.06300   1.000 5.67663  ? 126 TYR A CB  1 
ATOM   786  C  CG  . TYR A 1 126 ? 97.69600  37.64800 7.43300   1.000 4.41259  ? 126 TYR A CG  1 
ATOM   787  C  CD1 . TYR A 1 126 ? 97.65800  37.83200 6.05900   1.000 5.64314  ? 126 TYR A CD1 1 
ATOM   788  C  CD2 . TYR A 1 126 ? 98.18900  38.68100 8.22600   1.000 5.73045  ? 126 TYR A CD2 1 
ATOM   789  C  CE1 . TYR A 1 126 ? 98.13400  38.99600 5.48700   1.000 6.21305  ? 126 TYR A CE1 1 
ATOM   790  C  CE2 . TYR A 1 126 ? 98.66700  39.84400 7.65800   1.000 5.52876  ? 126 TYR A CE2 1 
ATOM   791  C  CZ  . TYR A 1 126 ? 98.62800  40.00400 6.29000   1.000 5.32836  ? 126 TYR A CZ  1 
ATOM   792  O  OH  . TYR A 1 126 ? 99.06800  41.15800 5.69500   1.000 6.86486  ? 126 TYR A OH  1 
ATOM   793  N  N   . CYS A 1 127 ? 94.22300  34.62100 7.30900   1.000 5.18383  ? 127 CYS A N   1 
ATOM   794  C  CA  . CYS A 1 127 ? 93.54700  33.35000 7.48800   1.000 5.94660  ? 127 CYS A CA  1 
ATOM   795  C  C   . CYS A 1 127 ? 94.27200  32.29000 6.67600   1.000 5.83118  ? 127 CYS A C   1 
ATOM   796  O  O   . CYS A 1 127 ? 94.90100  32.59600 5.65700   1.000 7.44195  ? 127 CYS A O   1 
ATOM   797  C  CB  . CYS A 1 127 ? 92.08100  33.42600 7.04100   1.000 7.69853  ? 127 CYS A CB  1 
ATOM   798  S  SG  . CYS A 1 127 ? 91.06700  34.72100 7.83100   1.000 8.04516  ? 127 CYS A SG  1 
ATOM   799  N  N   . HIS A 1 128 ? 94.16700  31.03900 7.11800   1.000 5.85101  ? 128 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 128 ? 94.79800  29.92500 6.42800   1.000 5.45068  ? 128 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 128 ? 93.75900  28.86600 6.09100   1.000 5.39123  ? 128 HIS A C   1 
ATOM   802  O  O   . HIS A 1 128 ? 92.89800  28.53800 6.91500   1.000 6.12852  ? 128 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 128 ? 95.91800  29.30600 7.25500   1.000 5.74455  ? 128 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 128 ? 96.63600  28.19600 6.55400   1.000 7.62824  ? 128 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 128 ? 96.35900  26.86300 6.76800   1.000 8.82574  ? 128 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 128 ? 97.61800  28.23200 5.62300   1.000 8.23897  ? 128 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 128 ? 97.14800  26.12600 6.00400   1.000 10.02522 ? 128 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 128 ? 97.91800  26.93200 5.29800   1.000 9.81580  ? 128 HIS A NE2 1 
ATOM   809  N  N   . ASN A 1 129 ? 93.86300  28.34400 4.87200   1.000 5.55911  ? 129 ASN A N   1 
ATOM   810  C  CA  . ASN A 1 129 ? 92.96500  27.32600 4.35100   1.000 5.56762  ? 129 ASN A CA  1 
ATOM   811  C  C   . ASN A 1 129 ? 93.74500  26.02000 4.25700   1.000 5.75808  ? 129 ASN A C   1 
ATOM   812  O  O   . ASN A 1 129 ? 94.56900  25.85000 3.35600   1.000 6.23923  ? 129 ASN A O   1 
ATOM   813  C  CB  . ASN A 1 129 ? 92.47400  27.77800 2.98300   1.000 5.76994  ? 129 ASN A CB  1 
ATOM   814  C  CG  . ASN A 1 129 ? 91.46300  26.85200 2.39700   1.000 5.59037  ? 129 ASN A CG  1 
ATOM   815  O  OD1 . ASN A 1 129 ? 91.33300  25.69900 2.81000   1.000 7.08146  ? 129 ASN A OD1 1 
ATOM   816  N  ND2 . ASN A 1 129 ? 90.72200  27.35000 1.42600   1.000 6.07723  ? 129 ASN A ND2 1 
ATOM   817  N  N   . SER A 1 130 ? 93.47400  25.09900 5.18000   1.000 6.42237  ? 130 SER A N   1 
ATOM   818  C  CA  . SER A 1 130 ? 94.18100  23.82400 5.21700   1.000 8.88103  ? 130 SER A CA  1 
ATOM   819  C  C   . SER A 1 130 ? 93.81300  22.90600 4.05800   1.000 8.87385  ? 130 SER A C   1 
ATOM   820  O  O   . SER A 1 130 ? 94.47100  21.87800 3.87300   1.000 11.04081 ? 130 SER A O   1 
ATOM   821  C  CB  . SER A 1 130 ? 93.93100  23.11900 6.54800   1.000 11.13620 ? 130 SER A CB  1 
ATOM   822  O  OG  . SER A 1 130 ? 92.55400  22.87500 6.71000   1.000 12.86097 ? 130 SER A OG  1 
ATOM   823  N  N   . SER A 1 131 ? 92.79100  23.24300 3.27200   1.000 7.64220  ? 131 SER A N   1 
ATOM   824  C  CA  . SER A 1 131 ? 92.42300  22.41700 2.13300   1.000 8.09405  ? 131 SER A CA  1 
ATOM   825  C  C   . SER A 1 131 ? 93.18400  22.77900 0.86500   1.000 7.58009  ? 131 SER A C   1 
ATOM   826  O  O   . SER A 1 131 ? 93.15900  22.00200 -0.09000  1.000 8.76304  ? 131 SER A O   1 
ATOM   827  C  CB  . SER A 1 131 ? 90.92000  22.51200 1.86700   1.000 9.93704  ? 131 SER A CB  1 
ATOM   828  O  OG  . SER A 1 131 ? 90.19300  21.99400 2.96600   1.000 12.72292 ? 131 SER A OG  1 
ATOM   829  N  N   . ASP A 1 132 ? 93.85800  23.92100 0.81700   1.000 7.03923  ? 132 ASP A N   1 
ATOM   830  C  CA  . ASP A 1 132 ? 94.58500  24.27800 -0.39500  1.000 6.74289  ? 132 ASP A CA  1 
ATOM   831  C  C   . ASP A 1 132 ? 95.73700  23.31700 -0.62800  1.000 6.75402  ? 132 ASP A C   1 
ATOM   832  O  O   . ASP A 1 132 ? 96.47800  22.97700 0.29800   1.000 8.61847  ? 132 ASP A O   1 
ATOM   833  C  CB  . ASP A 1 132 ? 95.14600  25.69000 -0.28600  1.000 7.10750  ? 132 ASP A CB  1 
ATOM   834  C  CG  . ASP A 1 132 ? 94.13100  26.73700 -0.64800  1.000 6.35017  ? 132 ASP A CG  1 
ATOM   835  O  OD1 . ASP A 1 132 ? 93.45400  26.57600 -1.68900  1.000 6.70092  ? 132 ASP A OD1 1 
ATOM   836  O  OD2 . ASP A 1 132 ? 94.00300  27.70800 0.11700   1.000 6.26687  ? 132 ASP A OD2 1 
ATOM   837  N  N   . THR A 1 133 ? 95.89200  22.88900 -1.88000  1.000 7.04670  ? 133 THR A N   1 
ATOM   838  C  CA  . THR A 1 133 ? 97.01100  22.05600 -2.28200  1.000 8.40917  ? 133 THR A CA  1 
ATOM   839  C  C   . THR A 1 133 ? 97.93500  22.71500 -3.28900  1.000 8.04340  ? 133 THR A C   1 
ATOM   840  O  O   . THR A 1 133 ? 98.96300  22.12100 -3.62400  1.000 9.76297  ? 133 THR A O   1 
ATOM   841  C  CB  . THR A 1 133 ? 96.52800  20.70700 -2.83900  1.000 11.08116 ? 133 THR A CB  1 
ATOM   842  O  OG1 . THR A 1 133 ? 95.75000  20.92500 -4.01800  1.000 11.70750 ? 133 THR A OG1 1 
ATOM   843  C  CG2 . THR A 1 133 ? 95.69900  19.97100 -1.79900  1.000 12.65623 ? 133 THR A CG2 1 
ATOM   844  N  N   . TRP A 1 134 ? 97.61200  23.90100 -3.78700  1.000 6.29833  ? 134 TRP A N   1 
ATOM   845  C  CA  . TRP A 1 134 ? 98.48900  24.59800 -4.71300  1.000 5.86396  ? 134 TRP A CA  1 
ATOM   846  C  C   . TRP A 1 134 ? 99.22600  25.71700 -3.99400  1.000 5.90087  ? 134 TRP A C   1 
ATOM   847  O  O   . TRP A 1 134 ? 98.73800  26.28100 -3.00900  1.000 6.14303  ? 134 TRP A O   1 
ATOM   848  C  CB  . TRP A 1 134 ? 97.71500  25.21200 -5.87600  1.000 5.73629  ? 134 TRP A CB  1 
ATOM   849  C  CG  . TRP A 1 134 ? 96.99600  24.23500 -6.73300  1.000 7.15544  ? 134 TRP A CG  1 
ATOM   850  C  CD1 . TRP A 1 134 ? 97.17800  22.88400 -6.78200  1.000 8.03362  ? 134 TRP A CD1 1 
ATOM   851  C  CD2 . TRP A 1 134 ? 95.95800  24.53700 -7.66400  1.000 7.58680  ? 134 TRP A CD2 1 
ATOM   852  N  NE1 . TRP A 1 134 ? 96.31500  22.32400 -7.69900  1.000 8.70286  ? 134 TRP A NE1 1 
ATOM   853  C  CE2 . TRP A 1 134 ? 95.55100  23.32400 -8.24800  1.000 9.06221  ? 134 TRP A CE2 1 
ATOM   854  C  CE3 . TRP A 1 134 ? 95.33300  25.71900 -8.06700  1.000 7.89825  ? 134 TRP A CE3 1 
ATOM   855  C  CZ2 . TRP A 1 134 ? 94.54100  23.26400 -9.21100  1.000 9.77620  ? 134 TRP A CZ2 1 
ATOM   856  C  CZ3 . TRP A 1 134 ? 94.33300  25.65700 -9.00600  1.000 9.52401  ? 134 TRP A CZ3 1 
ATOM   857  C  CH2 . TRP A 1 134 ? 93.94500  24.43800 -9.57200  1.000 9.88834  ? 134 TRP A CH2 1 
ATOM   858  N  N   . VAL A 1 135 ? 100.40800 26.04600 -4.52000  1.000 5.45439  ? 135 VAL A N   1 
ATOM   859  C  CA  . VAL A 1 135 ? 101.15900 27.19400 -4.01700  1.000 5.98138  ? 135 VAL A CA  1 
ATOM   860  C  C   . VAL A 1 135 ? 100.34300 28.46700 -4.15900  1.000 5.76577  ? 135 VAL A C   1 
ATOM   861  O  O   . VAL A 1 135 ? 100.31100 29.31300 -3.25700  1.000 5.77716  ? 135 VAL A O   1 
ATOM   862  C  CB  . VAL A 1 135 ? 102.50900 27.30900 -4.74600  1.000 7.09175  ? 135 VAL A CB  1 
ATOM   863  C  CG1 . VAL A 1 135 ? 103.24900 28.54300 -4.26000  1.000 8.34136  ? 135 VAL A CG1 1 
ATOM   864  C  CG2 . VAL A 1 135 ? 103.33800 26.06800 -4.51200  1.000 7.58717  ? 135 VAL A CG2 1 
ATOM   865  N  N   . ASN A 1 136 ? 99.68600  28.63600 -5.29700  1.000 5.33699  ? 136 ASN A N   1 
ATOM   866  C  CA  . ASN A 1 136 ? 98.84000  29.78300 -5.56300  1.000 5.52811  ? 136 ASN A CA  1 
ATOM   867  C  C   . ASN A 1 136 ? 97.51800  29.21100 -6.03100  1.000 4.78063  ? 136 ASN A C   1 
ATOM   868  O  O   . ASN A 1 136 ? 97.48200  28.47400 -7.02200  1.000 5.92413  ? 136 ASN A O   1 
ATOM   869  C  CB  . ASN A 1 136 ? 99.48900  30.62200 -6.66500  1.000 6.47453  ? 136 ASN A CB  1 
ATOM   870  C  CG  . ASN A 1 136 ? 98.72100  31.88300 -6.98700  1.000 7.81897  ? 136 ASN A CG  1 
ATOM   871  O  OD1 . ASN A 1 136 ? 97.49700  31.88600 -7.06300  1.000 7.77724  ? 136 ASN A OD1 1 
ATOM   872  N  ND2 . ASN A 1 136 ? 99.45100  32.97000 -7.22600  1.000 12.49604 ? 136 ASN A ND2 1 
ATOM   873  N  N   . SER A 1 137 ? 96.43900  29.53600 -5.31800  1.000 4.94657  ? 137 SER A N   1 
ATOM   874  C  CA  . SER A 1 137 ? 95.15500  28.92200 -5.64200  1.000 6.04622  ? 137 SER A CA  1 
ATOM   875  C  C   . SER A 1 137 ? 94.63700  29.31100 -7.02000  1.000 7.17389  ? 137 SER A C   1 
ATOM   876  O  O   . SER A 1 137 ? 93.65200  28.72300 -7.48200  1.000 7.77242  ? 137 SER A O   1 
ATOM   877  C  CB  . SER A 1 137 ? 94.12600  29.22500 -4.55100  1.000 6.90339  ? 137 SER A CB  1 
ATOM   878  O  OG  . SER A 1 137 ? 93.81200  30.60300 -4.50600  1.000 6.43880  ? 137 SER A OG  1 
ATOM   879  N  N   . CYS A 1 138 ? 95.29100  30.25500 -7.69700  1.000 6.88626  ? 138 CYS A N   1 
ATOM   880  C  CA  . CYS A 1 138 ? 94.93900  30.63300 -9.05800  1.000 8.95514  ? 138 CYS A CA  1 
ATOM   881  C  C   . CYS A 1 138 ? 95.91900  30.11600 -10.10300 1.000 8.17114  ? 138 CYS A C   1 
ATOM   882  O  O   . CYS A 1 138 ? 95.79200  30.47600 -11.28000 1.000 10.17986 ? 138 CYS A O   1 
ATOM   883  C  CB  . CYS A 1 138 ? 94.83500  32.15700 -9.17500  1.000 10.98418 ? 138 CYS A CB  1 
ATOM   884  S  SG  . CYS A 1 138 ? 93.56500  32.91700 -8.13300  1.000 12.13337 ? 138 CYS A SG  1 
ATOM   885  N  N   . ILE A 1 139 ? 96.89800  29.31000 -9.71900  1.000 7.51694  ? 139 ILE A N   1 
ATOM   886  C  CA  . ILE A 1 139 ? 97.84000  28.72900 -10.66500 1.000 8.27009  ? 139 ILE A CA  1 
ATOM   887  C  C   . ILE A 1 139 ? 97.76600  27.21300 -10.54900 1.000 8.03033  ? 139 ILE A C   1 
ATOM   888  O  O   . ILE A 1 139 ? 98.33400  26.61900 -9.63100  1.000 7.64209  ? 139 ILE A O   1 
ATOM   889  C  CB  . ILE A 1 139 ? 99.27500  29.24600 -10.45500 1.000 9.63972  ? 139 ILE A CB  1 
ATOM   890  C  CG1 . ILE A 1 139 ? 99.30500  30.77400 -10.54500 1.000 11.33380 ? 139 ILE A CG1 1 
ATOM   891  C  CG2 . ILE A 1 139 ? 100.22200 28.62600 -11.49000 1.000 10.65302 ? 139 ILE A CG2 1 
ATOM   892  C  CD1 . ILE A 1 139 ? 100.66100 31.39200 -10.25900 1.000 12.09546 ? 139 ILE A CD1 1 
ATOM   893  N  N   . PRO A 1 140 ? 97.06200  26.55100 -11.46700 1.000 8.23579  ? 140 PRO A N   1 
ATOM   894  C  CA  . PRO A 1 140 ? 96.87400  25.10100 -11.34900 1.000 9.75447  ? 140 PRO A CA  1 
ATOM   895  C  C   . PRO A 1 140 ? 98.18800  24.33800 -11.38300 1.000 9.53571  ? 140 PRO A C   1 
ATOM   896  O  O   . PRO A 1 140 ? 99.14300  24.71600 -12.06600 1.000 10.88229 ? 140 PRO A O   1 
ATOM   897  C  CB  . PRO A 1 140 ? 96.00300  24.75700 -12.56400 1.000 12.02174 ? 140 PRO A CB  1 
ATOM   898  C  CG  . PRO A 1 140 ? 95.26800  26.02600 -12.86000 1.000 12.78188 ? 140 PRO A CG  1 
ATOM   899  C  CD  . PRO A 1 140 ? 96.23200  27.13600 -12.53400 1.000 10.44484 ? 140 PRO A CD  1 
ATOM   900  N  N   . GLU A 1 141 ? 98.22100  23.24700 -10.62300 1.000 10.34139 ? 141 GLU A N   1 
ATOM   901  C  CA  . GLU A 1 141 ? 99.33600  22.30900 -10.60400 1.000 11.66309 ? 141 GLU A CA  1 
ATOM   902  C  C   . GLU A 1 141 ? 98.87900  20.95200 -11.11400 1.000 15.09848 ? 141 GLU A C   1 
ATOM   903  O  O   . GLU A 1 141 ? 97.76000  20.53400 -10.82700 1.000 17.34802 ? 141 GLU A O   1 
ATOM   904  C  CB  . GLU A 1 141 ? 99.89500  22.18700 -9.18900  1.000 11.82147 ? 141 GLU A CB  1 
ATOM   905  C  CG  . GLU A 1 141 ? 100.36900 23.52500 -8.69200  1.000 10.48907 ? 141 GLU A CG  1 
ATOM   906  C  CD  . GLU A 1 141 ? 100.81700 23.55300 -7.24000  1.000 10.10228 ? 141 GLU A CD  1 
ATOM   907  O  OE1 . GLU A 1 141 ? 100.77700 22.51000 -6.53500  1.000 10.09523 ? 141 GLU A OE1 1 
ATOM   908  O  OE2 . GLU A 1 141 ? 101.23000 24.65300 -6.82700  1.000 8.55081  ? 141 GLU A OE2 1 
HETATM 909  C  C1  . BDP B 2 .   ? 110.01300 45.99300 19.18600  1.000 30.42352 ? 1   BDP C C1  1 
HETATM 910  C  C2  . BDP B 2 .   ? 110.55900 46.22300 17.78500  1.000 30.52106 ? 1   BDP C C2  1 
HETATM 911  C  C3  . BDP B 2 .   ? 109.84400 47.26300 17.04600  1.000 29.73710 ? 1   BDP C C3  1 
HETATM 912  C  C4  . BDP B 2 .   ? 108.35400 47.19500 17.13600  1.000 26.89966 ? 1   BDP C C4  1 
HETATM 913  C  C5  . BDP B 2 .   ? 107.86500 46.94500 18.55200  1.000 28.58000 ? 1   BDP C C5  1 
HETATM 914  C  C6  . BDP B 2 .   ? 106.41400 46.65900 18.51300  1.000 29.32302 ? 1   BDP C C6  1 
HETATM 915  O  O2  . BDP B 2 .   ? 111.97000 46.60000 17.88700  1.000 31.40918 ? 1   BDP C O2  1 
HETATM 916  O  O3  . BDP B 2 .   ? 110.24200 47.13400 15.58800  1.000 31.93184 ? 1   BDP C O3  1 
HETATM 917  O  O4  . BDP B 2 .   ? 107.36800 48.09000 16.71000  1.000 21.50810 ? 1   BDP C O4  1 
HETATM 918  O  O5  . BDP B 2 .   ? 108.54600 45.81400 19.17000  1.000 29.95398 ? 1   BDP C O5  1 
HETATM 919  O  O6A . BDP B 2 .   ? 106.02700 45.54300 18.18300  1.000 26.66281 ? 1   BDP C O6A 1 
HETATM 920  O  O6B . BDP B 2 .   ? 105.59100 47.54800 18.79900  1.000 31.27889 ? 1   BDP C O6B 1 
HETATM 921  C  C1  . NAG B 2 .   ? 106.66200 47.91900 15.47900  1.000 15.89881 ? 2   NAG C C1  1 
HETATM 922  C  C2  . NAG B 2 .   ? 106.07800 49.26400 15.06200  1.000 13.25692 ? 2   NAG C C2  1 
HETATM 923  C  C3  . NAG B 2 .   ? 105.47300 49.23200 13.66600  1.000 11.57098 ? 2   NAG C C3  1 
HETATM 924  C  C4  . NAG B 2 .   ? 106.46900 48.61300 12.69100  1.000 12.05181 ? 2   NAG C C4  1 
HETATM 925  C  C5  . NAG B 2 .   ? 106.96000 47.27500 13.22800  1.000 14.11453 ? 2   NAG C C5  1 
HETATM 926  C  C6  . NAG B 2 .   ? 107.98400 46.64900 12.29800  1.000 17.30331 ? 2   NAG C C6  1 
HETATM 927  C  C7  . NAG B 2 .   ? 105.14400 50.95500 16.51800  1.000 18.12110 ? 2   NAG C C7  1 
HETATM 928  C  C8  . NAG B 2 .   ? 104.03400 51.33100 17.45400  1.000 18.01444 ? 2   NAG C C8  1 
HETATM 929  N  N2  . NAG B 2 .   ? 105.08400 49.72800 16.00800  1.000 15.35623 ? 2   NAG C N2  1 
HETATM 930  O  O3  . NAG B 2 .   ? 105.22200 50.59900 13.33600  1.000 10.98077 ? 2   NAG C O3  1 
HETATM 931  O  O4  . NAG B 2 .   ? 105.87800 48.41600 11.40100  1.000 11.33263 ? 2   NAG C O4  1 
HETATM 932  O  O5  . NAG B 2 .   ? 107.58200 47.47600 14.49200  1.000 15.53011 ? 2   NAG C O5  1 
HETATM 933  O  O6  . NAG B 2 .   ? 109.19800 47.40600 12.36000  1.000 20.95596 ? 2   NAG C O6  1 
HETATM 934  O  O7  . NAG B 2 .   ? 106.04100 51.73000 16.24200  1.000 19.00655 ? 2   NAG C O7  1 
HETATM 935  C  C1  . BDP B 2 .   ? 104.02600 50.78200 12.57100  1.000 11.49526 ? 3   BDP C C1  1 
HETATM 936  C  C2  . BDP B 2 .   ? 103.55200 52.20800 12.74800  1.000 11.88118 ? 3   BDP C C2  1 
HETATM 937  C  C3  . BDP B 2 .   ? 102.41100 52.47200 11.86800  1.000 11.52399 ? 3   BDP C C3  1 
HETATM 938  C  C4  . BDP B 2 .   ? 102.70300 52.20000 10.42900  1.000 10.18847 ? 3   BDP C C4  1 
HETATM 939  C  C5  . BDP B 2 .   ? 103.16200 50.76300 10.31100  1.000 10.53435 ? 3   BDP C C5  1 
HETATM 940  C  C6  . BDP B 2 .   ? 103.63100 50.40500 8.95600   1.000 10.53836 ? 3   BDP C C6  1 
HETATM 941  O  O2  . BDP B 2 .   ? 103.20600 52.43600 14.14800  1.000 13.91146 ? 3   BDP C O2  1 
HETATM 942  O  O3  . BDP B 2 .   ? 102.00500 53.90900 12.05200  1.000 12.98255 ? 3   BDP C O3  1 
HETATM 943  O  O4  . BDP B 2 .   ? 101.49000 52.34300 9.69300   1.000 11.10208 ? 3   BDP C O4  1 
HETATM 944  O  O5  . BDP B 2 .   ? 104.31400 50.55500 11.16600  1.000 11.14688 ? 3   BDP C O5  1 
HETATM 945  O  O6A . BDP B 2 .   ? 103.10800 49.44800 8.35700   1.000 10.36391 ? 3   BDP C O6A 1 
HETATM 946  O  O6B . BDP B 2 .   ? 104.56000 51.04200 8.45500   1.000 11.23826 ? 3   BDP C O6B 1 
HETATM 947  C  C1  . NAG B 2 .   ? 101.63500 53.13000 8.51000   1.000 11.39876 ? 4   NAG C C1  1 
HETATM 948  C  C2  . NAG B 2 .   ? 100.51800 52.71800 7.53700   1.000 10.25897 ? 4   NAG C C2  1 
HETATM 949  C  C3  . NAG B 2 .   ? 100.44300 53.67400 6.33900   1.000 10.96570 ? 4   NAG C C3  1 
HETATM 950  C  C4  . NAG B 2 .   ? 100.51200 55.13500 6.76400   1.000 12.56571 ? 4   NAG C C4  1 
HETATM 951  C  C5  . NAG B 2 .   ? 101.68000 55.35300 7.70700   1.000 13.08238 ? 4   NAG C C5  1 
HETATM 952  C  C6  . NAG B 2 .   ? 101.74900 56.76100 8.24600   1.000 15.66687 ? 4   NAG C C6  1 
HETATM 953  C  C7  . NAG B 2 .   ? 100.03800 50.28800 7.48400   1.000 9.44839  ? 4   NAG C C7  1 
HETATM 954  C  C8  . NAG B 2 .   ? 100.41200 48.97800 6.85300   1.000 8.69047  ? 4   NAG C C8  1 
HETATM 955  N  N2  . NAG B 2 .   ? 100.73100 51.35700 7.06900   1.000 9.18922  ? 4   NAG C N2  1 
HETATM 956  O  O3  . NAG B 2 .   ? 99.19900  53.46300 5.68300   1.000 12.06449 ? 4   NAG C O3  1 
HETATM 957  O  O4  . NAG B 2 .   ? 100.68200 55.96800 5.62400   1.000 14.80565 ? 4   NAG C O4  1 
HETATM 958  O  O5  . NAG B 2 .   ? 101.51300 54.49000 8.83400   1.000 12.29757 ? 4   NAG C O5  1 
HETATM 959  O  O6  . NAG B 2 .   ? 100.56700 57.08300 8.96400   1.000 18.94455 ? 4   NAG C O6  1 
HETATM 960  O  O7  . NAG B 2 .   ? 99.16000  50.37000 8.33400   1.000 11.54423 ? 4   NAG C O7  1 
HETATM 961  C  C1  . BDP B 2 .   ? 99.30100  52.67200 4.51000   1.000 12.14154 ? 5   BDP C C1  1 
HETATM 962  C  C2  . BDP B 2 .   ? 97.93500  52.08200 4.24900   1.000 13.47149 ? 5   BDP C C2  1 
HETATM 963  C  C3  . BDP B 2 .   ? 97.93400  51.29400 3.02500   1.000 14.80919 ? 5   BDP C C3  1 
HETATM 964  C  C4  . BDP B 2 .   ? 98.45600  52.05100 1.85500   1.000 13.87435 ? 5   BDP C C4  1 
HETATM 965  C  C5  . BDP B 2 .   ? 99.80300  52.68400 2.17100   1.000 14.05732 ? 5   BDP C C5  1 
HETATM 966  C  C6  . BDP B 2 .   ? 100.23200 53.61400 1.11200   1.000 16.48623 ? 5   BDP C C6  1 
HETATM 967  O  O2  . BDP B 2 .   ? 97.57900  51.25000 5.39200   1.000 15.36395 ? 5   BDP C O2  1 
HETATM 968  O  O3  . BDP B 2 .   ? 96.51500  50.86000 2.72300   1.000 16.83843 ? 5   BDP C O3  1 
HETATM 969  O  O4  . BDP B 2 .   ? 98.60900  51.10500 0.80000   1.000 15.68746 ? 5   BDP C O4  1 
HETATM 970  O  O5  . BDP B 2 .   ? 99.73700  53.48400 3.37800   1.000 13.60463 ? 5   BDP C O5  1 
HETATM 971  O  O6A . BDP B 2 .   ? 100.97000 53.20200 0.21000   1.000 17.48225 ? 5   BDP C O6A 1 
HETATM 972  O  O6B . BDP B 2 .   ? 99.85800  54.78300 1.13800   1.000 18.96549 ? 5   BDP C O6B 1 
HETATM 973  C  C1  . NAG B 2 .   ? 98.12300  51.61900 -0.44800  1.000 19.24734 ? 6   NAG C C1  1 
HETATM 974  C  C2  . NAG B 2 .   ? 98.77400  50.80800 -1.56300  1.000 20.13495 ? 6   NAG C C2  1 
HETATM 975  C  C3  . NAG B 2 .   ? 98.28000  51.29600 -2.92200  1.000 23.15341 ? 6   NAG C C3  1 
HETATM 976  C  C4  . NAG B 2 .   ? 96.75700  51.28100 -2.96300  1.000 24.66837 ? 6   NAG C C4  1 
HETATM 977  C  C5  . NAG B 2 .   ? 96.18600  52.05000 -1.77200  1.000 24.76409 ? 6   NAG C C5  1 
HETATM 978  C  C6  . NAG B 2 .   ? 94.68000  51.97400 -1.68000  1.000 28.33346 ? 6   NAG C C6  1 
HETATM 979  C  C7  . NAG B 2 .   ? 101.00500 49.79200 -1.46000  1.000 18.87133 ? 6   NAG C C7  1 
HETATM 980  C  C8  . NAG B 2 .   ? 102.47900 50.04700 -1.37900  1.000 19.75859 ? 6   NAG C C8  1 
HETATM 981  N  N2  . NAG B 2 .   ? 100.22400 50.87700 -1.48800  1.000 19.32127 ? 6   NAG C N2  1 
HETATM 982  O  O3  . NAG B 2 .   ? 98.81200  50.46900 -3.95200  1.000 24.23082 ? 6   NAG C O3  1 
HETATM 983  O  O4  . NAG B 2 .   ? 96.29800  51.87800 -4.16900  1.000 25.90147 ? 6   NAG C O4  1 
HETATM 984  O  O5  . NAG B 2 .   ? 96.70500  51.51500 -0.54500  1.000 22.17288 ? 6   NAG C O5  1 
HETATM 985  O  O6  . NAG B 2 .   ? 94.25000  50.67300 -1.30400  1.000 30.10719 ? 6   NAG C O6  1 
HETATM 986  O  O7  . NAG B 2 .   ? 100.54200 48.65600 -1.50100  1.000 19.10067 ? 6   NAG C O7  1 
HETATM 987  C  C1  . NAG C 3 .   ? 86.93600  42.57400 20.71200  1.000 19.84645 ? 401 NAG A C1  1 
HETATM 988  C  C2  . NAG C 3 .   ? 86.89200  42.86300 22.21500  1.000 21.79400 ? 401 NAG A C2  1 
HETATM 989  C  C3  . NAG C 3 .   ? 85.64700  42.23800 22.83800  1.000 23.53943 ? 401 NAG A C3  1 
HETATM 990  C  C4  . NAG C 3 .   ? 84.39300  42.68400 22.09800  1.000 24.27784 ? 401 NAG A C4  1 
HETATM 991  C  C5  . NAG C 3 .   ? 84.53200  42.43300 20.59700  1.000 23.75686 ? 401 NAG A C5  1 
HETATM 992  C  C6  . NAG C 3 .   ? 83.39100  43.02000 19.79600  1.000 25.50910 ? 401 NAG A C6  1 
HETATM 993  C  C7  . NAG C 3 .   ? 89.05800  43.18600 23.32600  1.000 25.26491 ? 401 NAG A C7  1 
HETATM 994  C  C8  . NAG C 3 .   ? 90.22200  42.51400 23.98800  1.000 25.43611 ? 401 NAG A C8  1 
HETATM 995  N  N2  . NAG C 3 .   ? 88.09200  42.37700 22.87600  1.000 23.09183 ? 401 NAG A N2  1 
HETATM 996  O  O3  . NAG C 3 .   ? 85.56100  42.60100 24.21300  1.000 23.76744 ? 401 NAG A O3  1 
HETATM 997  O  O4  . NAG C 3 .   ? 83.26900  41.96700 22.59900  1.000 26.00106 ? 401 NAG A O4  1 
HETATM 998  O  O5  . NAG C 3 .   ? 85.73400  43.04100 20.09700  1.000 21.25988 ? 401 NAG A O5  1 
HETATM 999  O  O6  . NAG C 3 .   ? 83.11100  42.24200 18.64100  1.000 27.30583 ? 401 NAG A O6  1 
HETATM 1000 O  O7  . NAG C 3 .   ? 88.99500  44.40500 23.20100  1.000 27.32039 ? 401 NAG A O7  1 
HETATM 1001 C  C1  . NAG D 3 .   ? 89.76000  26.55700 0.73800   1.000 6.89230  ? 402 NAG A C1  1 
HETATM 1002 C  C2  . NAG D 3 .   ? 88.74900  27.41100 -0.02200  1.000 7.87039  ? 402 NAG A C2  1 
HETATM 1003 C  C3  . NAG D 3 .   ? 87.85300  26.52300 -0.87800  1.000 8.72344  ? 402 NAG A C3  1 
HETATM 1004 C  C4  . NAG D 3 .   ? 88.69300  25.63400 -1.78200  1.000 9.75382  ? 402 NAG A C4  1 
HETATM 1005 C  C5  . NAG D 3 .   ? 89.68900  24.84100 -0.94300  1.000 8.51014  ? 402 NAG A C5  1 
HETATM 1006 C  C6  . NAG D 3 .   ? 90.63200  23.99300 -1.76600  1.000 8.73899  ? 402 NAG A C6  1 
HETATM 1007 C  C7  . NAG D 3 .   ? 88.26300  29.46900 1.23100   1.000 8.99375  ? 402 NAG A C7  1 
HETATM 1008 C  C8  . NAG D 3 .   ? 87.28800  30.17300 2.13000   1.000 9.95338  ? 402 NAG A C8  1 
HETATM 1009 N  N2  . NAG D 3 .   ? 87.94100  28.21900 0.87800   1.000 8.39871  ? 402 NAG A N2  1 
HETATM 1010 O  O3  . NAG D 3 .   ? 86.96000  27.31900 -1.65100  1.000 10.24256 ? 402 NAG A O3  1 
HETATM 1011 O  O4  . NAG D 3 .   ? 87.84300  24.73800 -2.48600  1.000 11.64312 ? 402 NAG A O4  1 
HETATM 1012 O  O5  . NAG D 3 .   ? 90.50100  25.74700 -0.18800  1.000 7.25420  ? 402 NAG A O5  1 
HETATM 1013 O  O6  . NAG D 3 .   ? 91.46500  24.78500 -2.60100  1.000 9.06672  ? 402 NAG A O6  1 
HETATM 1014 O  O7  . NAG D 3 .   ? 89.30500  29.99600 0.86700   1.000 10.13973 ? 402 NAG A O7  1 
HETATM 1015 C  C1  A GOL E 4 .   ? 92.96300  23.36600 -6.01000  0.514 17.98834 ? 403 GOL A C1  1 
HETATM 1016 C  C1  B GOL E 4 .   ? 92.76800  23.53100 -5.91800  0.486 7.50550  ? 403 GOL A C1  1 
HETATM 1017 O  O1  A GOL E 4 .   ? 91.64200  23.69300 -5.70300  0.514 17.74750 ? 403 GOL A O1  1 
HETATM 1018 O  O1  B GOL E 4 .   ? 92.57100  22.15400 -6.08200  0.486 10.19941 ? 403 GOL A O1  1 
HETATM 1019 C  C2  A GOL E 4 .   ? 93.82900  23.67700 -4.76400  0.514 18.01144 ? 403 GOL A C2  1 
HETATM 1020 C  C2  B GOL E 4 .   ? 93.88900  23.75400 -4.85400  0.486 5.84212  ? 403 GOL A C2  1 
HETATM 1021 O  O2  A GOL E 4 .   ? 93.28000  23.14400 -3.60600  0.514 17.96496 ? 403 GOL A O2  1 
HETATM 1022 O  O2  B GOL E 4 .   ? 93.55600  23.19400 -3.63000  0.486 5.82988  ? 403 GOL A O2  1 
HETATM 1023 C  C3  A GOL E 4 .   ? 93.93900  25.22400 -4.71600  0.514 18.14589 ? 403 GOL A C3  1 
HETATM 1024 C  C3  B GOL E 4 .   ? 94.06500  25.30300 -4.73100  0.486 5.23120  ? 403 GOL A C3  1 
HETATM 1025 O  O3  A GOL E 4 .   ? 94.82400  25.54000 -3.68500  0.514 18.08680 ? 403 GOL A O3  1 
HETATM 1026 O  O3  B GOL E 4 .   ? 95.08300  25.54700 -3.79200  0.486 4.39049  ? 403 GOL A O3  1 
HETATM 1027 C  C1  . PEG F 5 .   ? 99.54800  24.93500 3.29900   1.000 33.70689 ? 404 PEG A C1  1 
HETATM 1028 O  O1  . PEG F 5 .   ? 100.31100 25.86400 4.01100   1.000 35.00923 ? 404 PEG A O1  1 
HETATM 1029 C  C2  . PEG F 5 .   ? 99.38500  25.37800 1.84500   1.000 31.15217 ? 404 PEG A C2  1 
HETATM 1030 O  O2  . PEG F 5 .   ? 99.85000  24.37600 0.99400   1.000 33.57406 ? 404 PEG A O2  1 
HETATM 1031 C  C3  . PEG F 5 .   ? 99.97200  24.81800 -0.32200  1.000 31.60722 ? 404 PEG A C3  1 
HETATM 1032 C  C4  . PEG F 5 .   ? 100.49400 23.65700 -1.15300  1.000 32.85153 ? 404 PEG A C4  1 
HETATM 1033 O  O4  . PEG F 5 .   ? 101.48600 22.99900 -0.42100  1.000 33.93466 ? 404 PEG A O4  1 
HETATM 1034 C  C1  . PEG G 5 .   ? 99.76900  18.51100 -3.12700  1.000 49.11600 ? 405 PEG A C1  1 
HETATM 1035 O  O1  . PEG G 5 .   ? 100.79000 18.59600 -4.09000  1.000 48.07731 ? 405 PEG A O1  1 
HETATM 1036 C  C2  . PEG G 5 .   ? 99.86900  19.70900 -2.18600  1.000 49.05646 ? 405 PEG A C2  1 
HETATM 1037 O  O2  . PEG G 5 .   ? 99.21100  19.49500 -0.97200  1.000 50.83694 ? 405 PEG A O2  1 
HETATM 1038 C  C3  . PEG G 5 .   ? 99.76100  20.25200 0.06900   1.000 50.71916 ? 405 PEG A C3  1 
HETATM 1039 C  C4  . PEG G 5 .   ? 98.70000  20.89400 0.95000   1.000 50.57002 ? 405 PEG A C4  1 
HETATM 1040 O  O4  . PEG G 5 .   ? 97.95100  19.88700 1.57200   1.000 50.29277 ? 405 PEG A O4  1 
HETATM 1041 C  C1  . PEG H 5 .   ? 91.62700  38.39100 22.81800  1.000 49.90741 ? 406 PEG A C1  1 
HETATM 1042 O  O1  . PEG H 5 .   ? 91.03500  39.61700 23.14900  1.000 50.48689 ? 406 PEG A O1  1 
HETATM 1043 C  C2  . PEG H 5 .   ? 91.11900  37.31900 23.77300  1.000 49.22456 ? 406 PEG A C2  1 
HETATM 1044 O  O2  . PEG H 5 .   ? 92.07200  37.10700 24.77400  1.000 48.89934 ? 406 PEG A O2  1 
HETATM 1045 C  C3  . PEG H 5 .   ? 91.64100  37.44000 26.06500  1.000 47.57226 ? 406 PEG A C3  1 
HETATM 1046 C  C4  . PEG H 5 .   ? 91.88500  38.92300 26.34000  1.000 46.53744 ? 406 PEG A C4  1 
HETATM 1047 O  O4  . PEG H 5 .   ? 93.06400  39.32100 25.69400  1.000 44.81778 ? 406 PEG A O4  1 
HETATM 1048 CL CL  . CL  I 6 .   ? 96.59000  24.08700 2.88600   1.000 32.13954 ? 407 CL  A CL  1 
HETATM 1049 O  O   . HOH J 7 .   ? 103.480   22.992   0.082     1.000 15.53763 ? 501 HOH A O   1 
HETATM 1050 O  O   . HOH J 7 .   ? 90.42200  49.52700 6.98700   1.000 54.46290 ? 502 HOH A O   1 
HETATM 1051 O  O   . HOH J 7 .   ? 77.77700  39.92900 3.80900   1.000 30.05460 ? 503 HOH A O   1 
HETATM 1052 O  O   . HOH J 7 .   ? 108.55100 50.54900 -2.20900  1.000 40.54663 ? 504 HOH A O   1 
HETATM 1053 O  O   . HOH J 7 .   ? 95.78300  20.40200 1.82500   1.000 43.15205 ? 505 HOH A O   1 
HETATM 1054 O  O   . HOH J 7 .   ? 81.179    42.367   21.822    1.000 53.44639 ? 506 HOH A O   1 
HETATM 1055 O  O   . HOH J 7 .   ? 90.36900  40.56200 21.09800  1.000 15.85830 ? 507 HOH A O   1 
HETATM 1056 O  O   . HOH J 7 .   ? 82.49300  43.97400 6.44500   1.000 20.17154 ? 508 HOH A O   1 
HETATM 1057 O  O   . HOH J 7 .   ? 97.10600  33.90000 22.64000  1.000 43.69895 ? 509 HOH A O   1 
HETATM 1058 O  O   . HOH J 7 .   ? 80.65300  45.23100 4.02200   1.000 39.70027 ? 510 HOH A O   1 
HETATM 1059 O  O   . HOH J 7 .   ? 97.28600  36.49300 -4.23500  1.000 34.94135 ? 511 HOH A O   1 
HETATM 1060 O  O   . HOH J 7 .   ? 80.51400  41.50000 -1.61000  1.000 11.74328 ? 512 HOH A O   1 
HETATM 1061 O  O   . HOH J 7 .   ? 105.32200 54.71500 -0.49100  1.000 45.88404 ? 513 HOH A O   1 
HETATM 1062 O  O   . HOH J 7 .   ? 102.91500 40.45300 21.55400  1.000 40.22236 ? 514 HOH A O   1 
HETATM 1063 O  O   . HOH J 7 .   ? 91.47300  30.43600 14.28600  1.000 11.15482 ? 515 HOH A O   1 
HETATM 1064 O  O   . HOH J 7 .   ? 102.44200 26.53900 5.32000   1.000 18.48345 ? 516 HOH A O   1 
HETATM 1065 O  O   . HOH J 7 .   ? 98.15300  40.91100 21.70400  1.000 28.65163 ? 517 HOH A O   1 
HETATM 1066 O  O   . HOH J 7 .   ? 89.48900  45.50100 3.69200   1.000 22.17515 ? 518 HOH A O   1 
HETATM 1067 O  O   . HOH J 7 .   ? 84.67200  27.53900 10.87100  1.000 24.49110 ? 519 HOH A O   1 
HETATM 1068 O  O   . HOH J 7 .   ? 95.62700  40.09700 -0.75000  1.000 21.34304 ? 520 HOH A O   1 
HETATM 1069 O  O   . HOH J 7 .   ? 84.00300  29.76000 3.01100   1.000 17.61943 ? 521 HOH A O   1 
HETATM 1070 O  O   . HOH J 7 .   ? 85.50800  45.98500 14.73900  1.000 41.51448 ? 522 HOH A O   1 
HETATM 1071 O  O   . HOH J 7 .   ? 102.02700 26.92300 11.55100  1.000 13.35297 ? 523 HOH A O   1 
HETATM 1072 O  O   . HOH J 7 .   ? 108.15700 47.41900 3.24700   1.000 5.93868  ? 524 HOH A O   1 
HETATM 1073 O  O   . HOH J 7 .   ? 93.48300  48.84100 21.92500  1.000 22.61618 ? 525 HOH A O   1 
HETATM 1074 O  O   . HOH J 7 .   ? 81.451    30.769   16.474    1.000 36.00874 ? 526 HOH A O   1 
HETATM 1075 O  O   . HOH J 7 .   ? 106.96100 29.18400 0.27600   1.000 10.31741 ? 527 HOH A O   1 
HETATM 1076 O  O   . HOH J 7 .   ? 95.57500  31.62800 18.89000  1.000 19.70362 ? 528 HOH A O   1 
HETATM 1077 O  O   . HOH J 7 .   ? 88.68200  24.31100 -5.00000  1.000 35.93534 ? 529 HOH A O   1 
HETATM 1078 O  O   . HOH J 7 .   ? 82.856    29.504   18.227    1.000 23.50068 ? 530 HOH A O   1 
HETATM 1079 O  O   . HOH J 7 .   ? 107.09600 29.54000 -4.64700  1.000 16.51658 ? 531 HOH A O   1 
HETATM 1080 O  O   . HOH J 7 .   ? 103.74200 29.69400 17.47600  1.000 20.30766 ? 532 HOH A O   1 
HETATM 1081 O  O   . HOH J 7 .   ? 101.19700 28.86100 4.70800   1.000 7.61095  ? 533 HOH A O   1 
HETATM 1082 O  O   . HOH J 7 .   ? 99.56000  26.10200 -14.33800 1.000 17.39215 ? 534 HOH A O   1 
HETATM 1083 O  O   . HOH J 7 .   ? 99.89600  19.96600 -6.42600  1.000 15.28167 ? 535 HOH A O   1 
HETATM 1084 O  O   . HOH J 7 .   ? 104.17600 30.31500 13.67300  1.000 10.62291 ? 536 HOH A O   1 
HETATM 1085 O  O   . HOH J 7 .   ? 100.90700 41.17600 20.58300  1.000 23.90188 ? 537 HOH A O   1 
HETATM 1086 O  O   . HOH J 7 .   ? 80.97200  31.28200 5.06900   1.000 11.40324 ? 538 HOH A O   1 
HETATM 1087 O  O   . HOH J 7 .   ? 111.10900 48.76600 -3.09200  1.000 20.30248 ? 539 HOH A O   1 
HETATM 1088 O  O   . HOH J 7 .   ? 100.25700 27.01900 -7.72400  1.000 6.99050  ? 540 HOH A O   1 
HETATM 1089 O  O   . HOH J 7 .   ? 108.70500 37.24400 11.43500  1.000 14.76107 ? 541 HOH A O   1 
HETATM 1090 O  O   . HOH J 7 .   ? 81.87800  39.97800 21.36500  1.000 37.29413 ? 542 HOH A O   1 
HETATM 1091 O  O   . HOH J 7 .   ? 90.41700  33.58400 -1.42600  1.000 23.22365 ? 543 HOH A O   1 
HETATM 1092 O  O   . HOH J 7 .   ? 105.13200 53.56600 7.66700   1.000 13.71085 ? 544 HOH A O   1 
HETATM 1093 O  O   . HOH J 7 .   ? 88.66600  45.97900 20.53300  1.000 18.86326 ? 545 HOH A O   1 
HETATM 1094 O  O   . HOH J 7 .   ? 91.351    29.475   -8.769    1.000 14.73748 ? 546 HOH A O   1 
HETATM 1095 O  O   . HOH J 7 .   ? 85.75100  26.84800 -4.06800  1.000 34.80137 ? 547 HOH A O   1 
HETATM 1096 O  O   . HOH J 7 .   ? 86.84500  34.49500 17.97900  1.000 13.11686 ? 548 HOH A O   1 
HETATM 1097 O  O   . HOH J 7 .   ? 94.17000  47.26300 25.68700  1.000 17.98017 ? 549 HOH A O   1 
HETATM 1098 O  O   . HOH J 7 .   ? 87.36300  38.62800 23.52100  1.000 20.39965 ? 550 HOH A O   1 
HETATM 1099 O  O   . HOH J 7 .   ? 111.55600 32.35800 -1.48100  1.000 27.46163 ? 551 HOH A O   1 
HETATM 1100 O  O   . HOH J 7 .   ? 91.77200  26.05600 7.28500   1.000 13.63860 ? 552 HOH A O   1 
HETATM 1101 O  O   . HOH J 7 .   ? 105.07100 46.52300 -2.74200  1.000 12.21905 ? 553 HOH A O   1 
HETATM 1102 O  O   . HOH J 7 .   ? 109.56000 36.15500 -1.56000  1.000 18.70446 ? 554 HOH A O   1 
HETATM 1103 O  O   . HOH J 7 .   ? 95.74500  49.51900 14.55200  1.000 21.79312 ? 555 HOH A O   1 
HETATM 1104 O  O   . HOH J 7 .   ? 109.085   54.375   6.954     1.000 19.60508 ? 556 HOH A O   1 
HETATM 1105 O  O   . HOH J 7 .   ? 97.071    19.423   -5.927    1.000 18.10426 ? 557 HOH A O   1 
HETATM 1106 O  O   . HOH J 7 .   ? 90.36800  50.06900 12.24400  1.000 25.42839 ? 558 HOH A O   1 
HETATM 1107 O  O   . HOH J 7 .   ? 110.25000 47.14900 9.90400   1.000 21.53309 ? 559 HOH A O   1 
HETATM 1108 O  O   . HOH J 7 .   ? 96.37700  28.26200 11.06400  1.000 14.25369 ? 560 HOH A O   1 
HETATM 1109 O  O   . HOH J 7 .   ? 90.02600  28.25200 -4.60600  1.000 31.01403 ? 561 HOH A O   1 
HETATM 1110 O  O   . HOH J 7 .   ? 112.44600 40.45000 0.00300   1.000 17.17871 ? 562 HOH A O   1 
HETATM 1111 O  O   . HOH J 7 .   ? 88.14700  27.47600 12.28800  1.000 24.60638 ? 563 HOH A O   1 
HETATM 1112 O  O   . HOH J 7 .   ? 85.17500  24.27800 -1.79600  1.000 20.33327 ? 564 HOH A O   1 
HETATM 1113 O  O   . HOH J 7 .   ? 105.355   41.805   -4.940    1.000 13.74712 ? 565 HOH A O   1 
HETATM 1114 O  O   . HOH J 7 .   ? 102.64200 43.71000 -4.41800  1.000 14.29809 ? 566 HOH A O   1 
HETATM 1115 O  O   . HOH J 7 .   ? 112.04900 48.69200 9.41600   1.000 20.42812 ? 567 HOH A O   1 
HETATM 1116 O  O   . HOH J 7 .   ? 89.45900  25.39300 8.70900   1.000 28.35241 ? 568 HOH A O   1 
HETATM 1117 O  O   . HOH J 7 .   ? 91.35800  20.74600 5.32300   1.000 28.85256 ? 569 HOH A O   1 
HETATM 1118 O  O   . HOH J 7 .   ? 97.09600  45.75100 1.80200   1.000 16.24481 ? 570 HOH A O   1 
HETATM 1119 O  O   . HOH J 7 .   ? 96.06900  49.57600 21.39100  1.000 36.21219 ? 571 HOH A O   1 
HETATM 1120 O  O   . HOH J 7 .   ? 99.36600  42.78000 17.82300  1.000 25.31715 ? 572 HOH A O   1 
HETATM 1121 O  O   . HOH J 7 .   ? 100.00800 16.09600 -5.14300  1.000 23.46726 ? 573 HOH A O   1 
HETATM 1122 O  O   . HOH J 7 .   ? 93.03100  20.16100 -4.12400  1.000 25.11620 ? 574 HOH A O   1 
HETATM 1123 O  O   . HOH J 7 .   ? 94.80500  37.94200 -4.55200  1.000 29.17986 ? 575 HOH A O   1 
HETATM 1124 O  O   . HOH J 7 .   ? 94.50000  26.01100 8.72600   1.000 16.85658 ? 576 HOH A O   1 
HETATM 1125 O  O   . HOH J 7 .   ? 97.26500  28.36500 -1.77900  1.000 5.98160  ? 577 HOH A O   1 
HETATM 1126 O  O   . HOH J 7 .   ? 94.29600  31.91500 16.58900  1.000 22.87754 ? 578 HOH A O   1 
HETATM 1127 O  O   . HOH J 7 .   ? 102.754   34.714   -5.385    1.000 35.42798 ? 579 HOH A O   1 
HETATM 1128 O  O   . HOH J 7 .   ? 98.43900  39.88800 23.71900  1.000 20.71458 ? 580 HOH A O   1 
HETATM 1129 O  O   . HOH J 7 .   ? 102.131   46.198   -1.297    1.000 17.43462 ? 581 HOH A O   1 
HETATM 1130 O  O   . HOH J 7 .   ? 96.31300  48.79600 5.21500   1.000 18.31303 ? 582 HOH A O   1 
HETATM 1131 O  O   . HOH J 7 .   ? 103.76100 25.16600 -8.09300  1.000 21.00201 ? 583 HOH A O   1 
HETATM 1132 O  O   . HOH J 7 .   ? 112.44600 40.70900 8.75300   1.000 28.55948 ? 584 HOH A O   1 
HETATM 1133 O  O   . HOH J 7 .   ? 95.88400  19.60200 -8.58100  1.000 23.49183 ? 585 HOH A O   1 
HETATM 1134 O  O   . HOH J 7 .   ? 107.55400 29.28800 7.54000   1.000 24.31807 ? 586 HOH A O   1 
HETATM 1135 O  O   . HOH J 7 .   ? 97.68600  47.99700 8.52000   1.000 11.47862 ? 587 HOH A O   1 
HETATM 1136 O  O   . HOH J 7 .   ? 86.97800  26.96800 10.41000  1.000 52.44092 ? 588 HOH A O   1 
HETATM 1137 O  O   . HOH J 7 .   ? 94.56300  29.83900 14.69700  1.000 28.54921 ? 589 HOH A O   1 
HETATM 1138 O  O   . HOH J 7 .   ? 99.77900  30.18800 15.69600  1.000 27.81692 ? 590 HOH A O   1 
HETATM 1139 O  O   . HOH J 7 .   ? 109.64700 42.25900 12.94100  1.000 15.35159 ? 591 HOH A O   1 
HETATM 1140 O  O   . HOH J 7 .   ? 91.45000  26.87700 -6.99700  1.000 33.52162 ? 592 HOH A O   1 
HETATM 1141 O  O   . HOH J 7 .   ? 106.61100 31.62000 14.56400  1.000 22.56304 ? 593 HOH A O   1 
HETATM 1142 O  O   . HOH J 7 .   ? 91.62100  43.81600 3.04800   1.000 19.50240 ? 594 HOH A O   1 
HETATM 1143 O  O   . HOH J 7 .   ? 111.14100 38.05900 8.30100   1.000 28.26119 ? 595 HOH A O   1 
HETATM 1144 O  O   . HOH J 7 .   ? 85.87900  24.48000 6.49000   1.000 35.01479 ? 596 HOH A O   1 
HETATM 1145 O  O   . HOH J 7 .   ? 101.78500 37.53900 21.70200  1.000 37.48399 ? 597 HOH A O   1 
HETATM 1146 O  O   . HOH J 7 .   ? 103.84100 52.91900 -3.08000  1.000 39.61392 ? 598 HOH A O   1 
HETATM 1147 O  O   . HOH J 7 .   ? 112.29200 38.65200 2.19400   1.000 24.54474 ? 599 HOH A O   1 
HETATM 1148 O  O   . HOH J 7 .   ? 95.79200  47.01000 9.65300   1.000 31.90205 ? 600 HOH A O   1 
HETATM 1149 O  O   . HOH J 7 .   ? 112.78200 46.46100 -2.28400  1.000 14.85224 ? 601 HOH A O   1 
HETATM 1150 O  O   . HOH J 7 .   ? 84.46500  39.62900 12.90600  1.000 28.46514 ? 602 HOH A O   1 
HETATM 1151 O  O   . HOH J 7 .   ? 113.56600 44.53900 7.31600   1.000 14.79441 ? 603 HOH A O   1 
HETATM 1152 O  O   . HOH J 7 .   ? 92.74600  50.08400 17.24700  1.000 19.61183 ? 604 HOH A O   1 
HETATM 1153 O  O   . HOH J 7 .   ? 100.47700 24.91600 7.05500   1.000 21.55454 ? 605 HOH A O   1 
HETATM 1154 O  O   . HOH J 7 .   ? 89.755    44.779   26.100    1.000 48.49959 ? 606 HOH A O   1 
HETATM 1155 O  O   . HOH J 7 .   ? 97.83300  44.82600 -0.00600  1.000 27.11137 ? 607 HOH A O   1 
HETATM 1156 O  O   . HOH J 7 .   ? 103.22900 53.76500 -0.41300  1.000 34.77688 ? 608 HOH A O   1 
HETATM 1157 O  O   . HOH J 7 .   ? 112.62300 50.56500 -2.43800  1.000 39.34491 ? 609 HOH A O   1 
HETATM 1158 O  O   . HOH J 7 .   ? 100.61900 43.79600 -2.60800  1.000 18.96896 ? 610 HOH A O   1 
HETATM 1159 O  O   . HOH J 7 .   ? 98.78800  32.42100 21.12200  1.000 32.08273 ? 611 HOH A O   1 
HETATM 1160 O  O   . HOH J 7 .   ? 96.78300  25.29500 10.56500  1.000 39.93279 ? 612 HOH A O   1 
HETATM 1161 O  O   . HOH J 7 .   ? 100.31600 49.98600 18.82800  1.000 24.72029 ? 613 HOH A O   1 
HETATM 1162 O  O   . HOH J 7 .   ? 102.18900 24.24600 -11.89000 1.000 36.18197 ? 614 HOH A O   1 
HETATM 1163 O  O   . HOH J 7 .   ? 106.95100 38.68400 19.45500  1.000 33.97964 ? 615 HOH A O   1 
HETATM 1164 O  O   . HOH J 7 .   ? 110.42500 36.56500 6.90100   1.000 40.19825 ? 616 HOH A O   1 
HETATM 1165 O  O   . HOH J 7 .   ? 109.86200 52.30000 -2.09500  1.000 35.42745 ? 617 HOH A O   1 
HETATM 1166 O  O   . HOH J 7 .   ? 104.05500 27.12200 7.44600   1.000 19.87119 ? 618 HOH A O   1 
HETATM 1167 O  O   . HOH J 7 .   ? 102.591   32.624   -6.245    1.000 35.58173 ? 619 HOH A O   1 
HETATM 1168 O  O   . HOH J 7 .   ? 106.27800 48.90700 -3.09700  1.000 17.63459 ? 620 HOH A O   1 
HETATM 1169 O  O   . HOH J 7 .   ? 90.37500  22.41500 -8.33500  1.000 35.98700 ? 621 HOH A O   1 
HETATM 1170 O  O   . HOH J 7 .   ? 88.06900  32.10300 -1.20300  1.000 18.93985 ? 622 HOH A O   1 
HETATM 1171 O  O   . HOH J 7 .   ? 105.66700 31.16000 -6.30400  1.000 39.78489 ? 623 HOH A O   1 
HETATM 1172 O  O   . HOH J 7 .   ? 88.398    25.118   4.121     1.000 31.03862 ? 624 HOH A O   1 
HETATM 1173 O  O   . HOH J 7 .   ? 107.56300 26.86600 1.96200   1.000 31.82207 ? 625 HOH A O   1 
HETATM 1174 O  O   . HOH J 7 .   ? 97.64800  29.78300 14.41600  1.000 37.37336 ? 626 HOH A O   1 
HETATM 1175 O  O   . HOH J 7 .   ? 89.70700  26.49000 -5.76200  1.000 37.60733 ? 627 HOH A O   1 
HETATM 1176 O  O   . HOH J 7 .   ? 91.46500  49.80400 19.19500  1.000 49.66383 ? 628 HOH A O   1 
HETATM 1177 O  O   . HOH J 7 .   ? 103.57200 27.44100 13.70900  1.000 22.98585 ? 629 HOH A O   1 
HETATM 1178 O  O   . HOH J 7 .   ? 99.48900  52.20200 17.43500  1.000 35.99114 ? 630 HOH A O   1 
HETATM 1179 O  O   . HOH J 7 .   ? 100.68300 56.98800 0.20700   1.000 38.97153 ? 631 HOH A O   1 
HETATM 1180 O  O   . HOH J 7 .   ? 108.76900 35.97600 -4.03000  1.000 31.62554 ? 632 HOH A O   1 
HETATM 1181 O  O   . HOH J 7 .   ? 85.57200  24.27400 8.67100   1.000 47.01846 ? 633 HOH A O   1 
HETATM 1182 O  O   . HOH J 7 .   ? 94.59700  18.58200 1.31700   1.000 39.08589 ? 634 HOH A O   1 
HETATM 1183 O  O   . HOH J 7 .   ? 106.677   54.113   17.363    1.000 20.75401 ? 635 HOH A O   1 
HETATM 1184 O  O   . HOH J 7 .   ? 108.94000 49.07600 -4.41200  1.000 34.03311 ? 636 HOH A O   1 
HETATM 1185 O  O   . HOH J 7 .   ? 95.39100  30.14600 17.32500  1.000 49.74775 ? 637 HOH A O   1 
HETATM 1186 O  O   . HOH J 7 .   ? 96.34700  48.43900 1.21300   1.000 26.47192 ? 638 HOH A O   1 
HETATM 1187 O  O   . HOH J 7 .   ? 105.455   25.101   14.408    1.000 26.85338 ? 639 HOH A O   1 
HETATM 1188 O  O   . HOH J 7 .   ? 97.278    17.199   -4.887    1.000 33.15500 ? 640 HOH A O   1 
HETATM 1189 O  O   . HOH J 7 .   ? 113.54200 42.60500 9.62700   1.000 30.15120 ? 641 HOH A O   1 
HETATM 1190 O  O   . HOH J 7 .   ? 97.88800  27.08900 12.93800  1.000 33.43293 ? 642 HOH A O   1 
HETATM 1191 O  O   . HOH J 7 .   ? 90.353    47.157   26.194    1.000 31.87769 ? 643 HOH A O   1 
HETATM 1192 O  O   . HOH J 7 .   ? 101.96300 58.33500 4.72400   1.000 39.07867 ? 644 HOH A O   1 
HETATM 1193 O  O   . HOH J 7 .   ? 115.19900 40.63300 0.24500   1.000 35.82219 ? 645 HOH A O   1 
HETATM 1194 O  O   . HOH J 7 .   ? 89.16500  20.28600 -7.43500  1.000 41.93554 ? 646 HOH A O   1 
HETATM 1195 O  O   . HOH J 7 .   ? 101.75800 39.94900 23.37800  1.000 41.83233 ? 647 HOH A O   1 
HETATM 1196 O  O   . HOH J 7 .   ? 83.04400  39.12100 14.90100  1.000 45.27667 ? 648 HOH A O   1 
HETATM 1197 O  O   . HOH J 7 .   ? 102.55800 28.26800 -8.58400  1.000 15.47937 ? 649 HOH A O   1 
HETATM 1198 O  O   . HOH J 7 .   ? 100.39900 38.11000 24.08000  1.000 25.97446 ? 650 HOH A O   1 
HETATM 1199 O  O   . HOH J 7 .   ? 89.549    28.332   14.403    1.000 15.70651 ? 651 HOH A O   1 
HETATM 1200 O  O   . HOH J 7 .   ? 106.32300 33.49700 16.70800  1.000 29.30439 ? 652 HOH A O   1 
HETATM 1201 O  O   . HOH J 7 .   ? 110.63500 37.84700 13.29800  1.000 33.98714 ? 653 HOH A O   1 
HETATM 1202 O  O   . HOH J 7 .   ? 101.191   18.622   -8.473    1.000 17.66349 ? 654 HOH A O   1 
HETATM 1203 O  O   . HOH J 7 .   ? 88.81800  24.88100 11.12800  1.000 39.82473 ? 655 HOH A O   1 
HETATM 1204 O  O   . HOH J 7 .   ? 86.10710  32.90800 0.00000   0.50  36.16522 ? 656 HOH A O   1 
HETATM 1205 O  O   . HOH J 7 .   ? 103.33600 25.72800 9.70500   1.000 22.78010 ? 657 HOH A O   1 
HETATM 1206 O  O   . HOH J 7 .   ? 102.15800 26.75800 -14.69600 1.000 34.52837 ? 658 HOH A O   1 
HETATM 1207 O  O   . HOH J 7 .   ? 102.475   21.678   -11.761   1.000 31.44853 ? 659 HOH A O   1 
HETATM 1208 O  O   . HOH J 7 .   ? 103.72800 30.84000 -7.80400  1.000 27.55073 ? 660 HOH A O   1 
HETATM 1209 O  O   . HOH J 7 .   ? 109.285   57.212   6.821     1.000 38.29391 ? 661 HOH A O   1 
HETATM 1210 O  O   . HOH J 7 .   ? 102.750   27.332   18.200    1.000 19.78774 ? 662 HOH A O   1 
HETATM 1211 O  O   . HOH J 7 .   ? 105.64300 55.44700 9.59800   1.000 31.69279 ? 663 HOH A O   1 
HETATM 1212 O  O   . HOH J 7 .   ? 102.39700 23.41700 8.64300   1.000 34.77257 ? 664 HOH A O   1 
HETATM 1213 O  O   . HOH J 7 .   ? 105.68500 33.06500 18.89500  1.000 40.47953 ? 665 HOH A O   1 
HETATM 1214 O  O   . HOH J 7 .   ? 108.69600 37.77700 18.43200  1.000 42.42213 ? 666 HOH A O   1 
HETATM 1215 O  O   . HOH J 7 .   ? 100.20400 21.89400 10.05900  1.000 38.43717 ? 667 HOH A O   1 
HETATM 1216 O  O   . HOH J 7 .   ? 99.02300  56.29700 3.51400   1.000 21.28947 ? 668 HOH A O   1 
HETATM 1217 O  O   . HOH J 7 .   ? 96.59200  52.59100 7.72200   1.000 25.27665 ? 669 HOH A O   1 
HETATM 1218 O  O   . HOH J 7 .   ? 98.84700  51.29800 11.00000  1.000 20.91133 ? 670 HOH A O   1 
HETATM 1219 O  O   . HOH J 7 .   ? 112.86500 44.90200 13.98600  1.000 41.62362 ? 671 HOH A O   1 
HETATM 1220 O  O   . HOH J 7 .   ? 94.63500  52.72600 2.37400   1.000 38.48576 ? 672 HOH A O   1 
HETATM 1221 O  O   . HOH J 7 .   ? 99.31900  53.93800 11.48700  1.000 29.09555 ? 673 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP A 29  ? 0.19600 0.34080 0.33438 0.04869  0.00774  -0.08979 29  ASP A N   
2    C  CA  . ASP A 29  ? 0.18362 0.32719 0.32540 0.02911  0.00779  -0.08407 29  ASP A CA  
3    C  C   . ASP A 29  ? 0.16445 0.27910 0.31304 0.00398  -0.00810 -0.08206 29  ASP A C   
4    O  O   . ASP A 29  ? 0.18673 0.30571 0.38158 0.00492  -0.02925 -0.09029 29  ASP A O   
5    C  CB  . ASP A 29  ? 0.20553 0.35394 0.35968 0.02991  0.00102  -0.07224 29  ASP A CB  
6    C  CG  . ASP A 29  ? 0.21634 0.38712 0.39380 0.04425  -0.00740 -0.04181 29  ASP A CG  
7    O  OD1 . ASP A 29  ? 0.22263 0.39920 0.43263 0.04120  -0.02634 -0.04038 29  ASP A OD1 
8    O  OD2 . ASP A 29  ? 0.21795 0.39839 0.38880 0.05518  -0.02462 -0.04371 29  ASP A OD2 
9    N  N   . LEU A 30  ? 0.13727 0.20325 0.17148 -0.01717 -0.01576 -0.03583 30  LEU A N   
10   C  CA  . LEU A 30  ? 0.12127 0.17211 0.10612 -0.02425 -0.01679 -0.02403 30  LEU A CA  
11   C  C   . LEU A 30  ? 0.09875 0.15384 0.09715 -0.02126 -0.01626 -0.01002 30  LEU A C   
12   O  O   . LEU A 30  ? 0.12053 0.19261 0.11846 -0.04908 -0.02101 -0.01987 30  LEU A O   
13   C  CB  . LEU A 30  ? 0.13407 0.21230 0.11229 -0.03103 0.00635  0.01221  30  LEU A CB  
14   C  CG  . LEU A 30  ? 0.14497 0.23176 0.15425 -0.04164 0.02440  0.02533  30  LEU A CG  
15   C  CD1 . LEU A 30  ? 0.14757 0.22785 0.15249 -0.04564 0.00852  0.05012  30  LEU A CD1 
16   C  CD2 . LEU A 30  ? 0.15974 0.25617 0.17094 -0.03453 0.03016  0.01036  30  LEU A CD2 
17   N  N   A SER A 31  ? 0.07383 0.12559 0.08019 -0.00355 -0.01596 -0.02599 31  SER A N   
18   N  N   B SER A 31  ? 0.09322 0.16371 0.11417 0.00180  0.00304  -0.02420 31  SER A N   
19   C  CA  A SER A 31  ? 0.06537 0.11998 0.07805 0.00781  -0.01309 -0.00297 31  SER A CA  
20   C  CA  B SER A 31  ? 0.10271 0.17909 0.15655 0.01567  0.01605  -0.01740 31  SER A CA  
21   C  C   A SER A 31  ? 0.05203 0.10853 0.08861 0.02519  -0.02331 0.00424  31  SER A C   
22   C  C   B SER A 31  ? 0.09865 0.17881 0.15453 0.03005  0.00953  -0.01222 31  SER A C   
23   O  O   A SER A 31  ? 0.04824 0.11813 0.07110 0.03247  -0.01130 -0.00140 31  SER A O   
24   O  O   B SER A 31  ? 0.10390 0.19850 0.15162 0.04345  0.00519  -0.02537 31  SER A O   
25   C  CB  A SER A 31  ? 0.08289 0.13989 0.14459 -0.00196 -0.00372 0.02574  31  SER A CB  
26   C  CB  B SER A 31  ? 0.12296 0.20036 0.22288 0.00796  0.02311  -0.00616 31  SER A CB  
27   O  OG  A SER A 31  ? 0.09741 0.15650 0.20177 -0.00830 -0.02285 0.03270  31  SER A OG  
28   O  OG  B SER A 31  ? 0.14129 0.21415 0.28165 0.00636  0.03350  0.00662  31  SER A OG  
29   N  N   A ILE A 32  ? 0.05702 0.09581 0.08236 0.01971  -0.02231 0.00052  32  ILE A N   
30   N  N   B ILE A 32  ? 0.09505 0.16616 0.13258 0.02531  0.01629  -0.01338 32  ILE A N   
31   C  CA  A ILE A 32  ? 0.06675 0.09402 0.06343 0.00954  -0.00821 -0.00323 32  ILE A CA  
32   C  CA  B ILE A 32  ? 0.10013 0.15830 0.10158 0.02104  0.02293  -0.00664 32  ILE A CA  
33   C  C   A ILE A 32  ? 0.07007 0.09732 0.07634 0.01087  -0.00157 0.01004  32  ILE A C   
34   C  C   B ILE A 32  ? 0.09419 0.14513 0.11296 0.01903  0.02023  0.00624  32  ILE A C   
35   O  O   A ILE A 32  ? 0.07489 0.10460 0.06209 0.00989  -0.00399 0.01093  32  ILE A O   
36   O  O   B ILE A 32  ? 0.10732 0.17049 0.14980 0.02488  0.03183  0.01907  32  ILE A O   
37   C  CB  A ILE A 32  ? 0.07428 0.10367 0.07644 -0.01675 -0.00855 0.00186  32  ILE A CB  
38   C  CB  B ILE A 32  ? 0.11222 0.16998 0.10645 0.01076  0.03213  -0.00150 32  ILE A CB  
39   C  CG1 A ILE A 32  ? 0.07990 0.10460 0.10297 -0.01329 0.02071  0.01722  32  ILE A CG1 
40   C  CG1 B ILE A 32  ? 0.12186 0.18029 0.16005 0.00067  0.03922  -0.01556 32  ILE A CG1 
41   C  CG2 A ILE A 32  ? 0.07637 0.11343 0.10820 -0.03544 -0.01344 -0.00504 32  ILE A CG2 
42   C  CG2 B ILE A 32  ? 0.11355 0.17085 0.10982 0.01888  0.04123  0.01413  32  ILE A CG2 
43   C  CD1 A ILE A 32  ? 0.09766 0.11948 0.17063 -0.00598 0.01162  0.00989  32  ILE A CD1 
44   C  CD1 B ILE A 32  ? 0.12924 0.18537 0.20608 0.00187  0.03991  -0.03318 32  ILE A CD1 
45   N  N   . SER A 33  ? 0.08069 0.11789 0.07258 0.01100  0.00907  0.00017  33  SER A N   
46   C  CA  . SER A 33  ? 0.09115 0.12063 0.06141 0.01129  0.01988  0.00231  33  SER A CA  
47   C  C   . SER A 33  ? 0.11327 0.12117 0.07532 0.02534  0.02569  0.02150  33  SER A C   
48   O  O   . SER A 33  ? 0.13744 0.12336 0.11375 -0.00690 0.03072  -0.02541 33  SER A O   
49   C  CB  . SER A 33  ? 0.09108 0.12846 0.09332 0.01754  0.01249  0.01026  33  SER A CB  
50   O  OG  . SER A 33  ? 0.08520 0.12958 0.08564 0.02228  0.02025  0.00099  33  SER A OG  
51   N  N   . THR A 34  ? 0.12440 0.16931 0.06802 0.06647  -0.00307 -0.01622 34  THR A N   
52   C  CA  . THR A 34  ? 0.15201 0.21215 0.15018 0.08236  -0.00719 -0.02161 34  THR A CA  
53   C  C   . THR A 34  ? 0.14032 0.19160 0.13571 0.04607  -0.00946 -0.04284 34  THR A C   
54   O  O   . THR A 34  ? 0.14237 0.24051 0.22795 0.03369  -0.00864 -0.08145 34  THR A O   
55   C  CB  . THR A 34  ? 0.18981 0.25784 0.21827 0.12469  -0.00981 0.01528  34  THR A CB  
56   O  OG1 . THR A 34  ? 0.21425 0.27920 0.24204 0.13668  0.00062  0.05018  34  THR A OG1 
57   C  CG2 . THR A 34  ? 0.21092 0.27692 0.23892 0.09861  -0.00655 -0.01919 34  THR A CG2 
58   N  N   . CYS A 35  ? 0.13736 0.13798 0.06238 0.04871  -0.00008 0.00222  35  CYS A N   
59   C  CA  . CYS A 35  ? 0.14357 0.12362 0.06140 0.03941  -0.01107 0.02169  35  CYS A CA  
60   C  C   . CYS A 35  ? 0.12082 0.10588 0.09190 0.02317  -0.02842 0.01261  35  CYS A C   
61   O  O   . CYS A 35  ? 0.14019 0.11814 0.12486 0.00255  -0.02030 0.03595  35  CYS A O   
62   C  CB  . CYS A 35  ? 0.17364 0.14511 0.08659 0.04470  0.01004  0.02084  35  CYS A CB  
63   S  SG  . CYS A 35  ? 0.19182 0.16395 0.12151 0.07510  0.02402  0.01711  35  CYS A SG  
64   N  N   . ARG A 36  ? 0.07900 0.07511 0.05872 0.03539  0.00071  0.00606  36  ARG A N   
65   C  CA  . ARG A 36  ? 0.06477 0.07321 0.08107 0.01372  0.00022  0.00674  36  ARG A CA  
66   C  C   . ARG A 36  ? 0.05814 0.04620 0.07385 0.01622  -0.00522 -0.00412 36  ARG A C   
67   O  O   . ARG A 36  ? 0.06878 0.07729 0.06624 0.01849  -0.00127 -0.02139 36  ARG A O   
68   C  CB  . ARG A 36  ? 0.07307 0.08361 0.08744 0.00692  0.01155  -0.01122 36  ARG A CB  
69   C  CG  . ARG A 36  ? 0.08275 0.08999 0.10802 0.00761  0.03177  -0.02663 36  ARG A CG  
70   C  CD  . ARG A 36  ? 0.09558 0.09342 0.12430 -0.00293 0.02822  -0.01239 36  ARG A CD  
71   N  NE  . ARG A 36  ? 0.08746 0.08656 0.10512 -0.00115 0.00481  -0.00892 36  ARG A NE  
72   C  CZ  . ARG A 36  ? 0.08636 0.09504 0.12053 0.02181  -0.00168 -0.00991 36  ARG A CZ  
73   N  NH1 . ARG A 36  ? 0.09887 0.11191 0.16339 0.03024  -0.00670 -0.00695 36  ARG A NH1 
74   N  NH2 . ARG A 36  ? 0.10032 0.10142 0.09462 0.01520  -0.01491 -0.01914 36  ARG A NH2 
75   N  N   . ILE A 37  ? 0.05953 0.04702 0.08019 0.01215  0.01037  -0.00396 37  ILE A N   
76   C  CA  . ILE A 37  ? 0.05396 0.04510 0.07251 0.00131  0.00388  -0.00026 37  ILE A CA  
77   C  C   . ILE A 37  ? 0.05282 0.04367 0.08117 -0.00622 0.01119  -0.01213 37  ILE A C   
78   O  O   . ILE A 37  ? 0.05749 0.05486 0.09048 0.00439  0.00924  -0.00514 37  ILE A O   
79   C  CB  . ILE A 37  ? 0.06643 0.07204 0.08632 0.00505  -0.00466 0.00567  37  ILE A CB  
80   C  CG1 . ILE A 37  ? 0.10407 0.11647 0.11320 -0.00697 -0.00090 0.04133  37  ILE A CG1 
81   C  CG2 . ILE A 37  ? 0.05298 0.09848 0.08782 0.01596  0.00353  0.00553  37  ILE A CG2 
82   C  CD1 . ILE A 37  ? 0.12557 0.13633 0.18852 -0.01385 0.01687  0.01934  37  ILE A CD1 
83   N  N   . MET A 38  ? 0.06358 0.06309 0.06482 -0.00562 -0.00014 -0.00353 38  MET A N   
84   C  CA  . MET A 38  ? 0.07088 0.06796 0.06143 0.00304  0.00908  -0.00745 38  MET A CA  
85   C  C   . MET A 38  ? 0.07226 0.04843 0.06323 0.00168  -0.00839 -0.00854 38  MET A C   
86   O  O   . MET A 38  ? 0.07797 0.06144 0.07145 -0.00300 -0.00665 -0.00100 38  MET A O   
87   C  CB  . MET A 38  ? 0.07280 0.08057 0.06574 0.01947  0.00815  -0.00738 38  MET A CB  
88   C  CG  . MET A 38  ? 0.08323 0.09224 0.10836 0.01252  0.01679  -0.02487 38  MET A CG  
89   S  SD  . MET A 38  ? 0.09435 0.11422 0.11198 0.02297  0.01157  -0.03123 38  MET A SD  
90   C  CE  . MET A 38  ? 0.12359 0.12258 0.16482 0.04556  0.00472  -0.00904 38  MET A CE  
91   N  N   . GLY A 39  ? 0.06119 0.04691 0.07622 0.00471  0.00078  -0.00309 39  GLY A N   
92   C  CA  . GLY A 39  ? 0.05237 0.05099 0.08133 -0.00121 0.00621  -0.00243 39  GLY A CA  
93   C  C   . GLY A 39  ? 0.05363 0.05959 0.07461 0.00082  -0.00151 -0.01135 39  GLY A C   
94   O  O   . GLY A 39  ? 0.05382 0.07234 0.08304 -0.01028 0.01537  -0.01578 39  GLY A O   
95   N  N   . VAL A 40  ? 0.05514 0.04300 0.06849 0.00177  -0.00078 -0.00346 40  VAL A N   
96   C  CA  . VAL A 40  ? 0.06463 0.04368 0.06407 0.00025  -0.00217 -0.00004 40  VAL A CA  
97   C  C   . VAL A 40  ? 0.06585 0.04043 0.06210 0.00318  0.00925  -0.01851 40  VAL A C   
98   O  O   . VAL A 40  ? 0.06479 0.05846 0.06429 0.00887  0.00233  -0.01401 40  VAL A O   
99   C  CB  . VAL A 40  ? 0.07365 0.05713 0.06992 0.00202  0.00304  -0.00712 40  VAL A CB  
100  C  CG1 . VAL A 40  ? 0.08233 0.06982 0.08497 0.00116  -0.01899 -0.01882 40  VAL A CG1 
101  C  CG2 . VAL A 40  ? 0.07696 0.07582 0.08849 0.02001  0.00327  -0.01353 40  VAL A CG2 
102  N  N   . ALA A 41  ? 0.07051 0.04558 0.06920 0.00910  0.00364  -0.01305 41  ALA A N   
103  C  CA  . ALA A 41  ? 0.07867 0.05725 0.10745 0.01152  -0.00438 -0.00939 41  ALA A CA  
104  C  C   . ALA A 41  ? 0.07066 0.05176 0.05833 0.00024  0.00551  -0.00691 41  ALA A C   
105  O  O   . ALA A 41  ? 0.09339 0.05462 0.06888 0.00605  -0.00183 -0.00400 41  ALA A O   
106  C  CB  . ALA A 41  ? 0.08217 0.07786 0.11800 0.00504  -0.02589 -0.04022 41  ALA A CB  
107  N  N   . LEU A 42  ? 0.05745 0.06385 0.06179 -0.00151 0.00655  -0.00340 42  LEU A N   
108  C  CA  . LEU A 42  ? 0.05242 0.05238 0.08976 0.00020  0.00950  -0.01022 42  LEU A CA  
109  C  C   . LEU A 42  ? 0.05157 0.06153 0.07642 0.00281  -0.00169 -0.01385 42  LEU A C   
110  O  O   . LEU A 42  ? 0.05380 0.09522 0.06688 0.00110  -0.00233 -0.00778 42  LEU A O   
111  C  CB  . LEU A 42  ? 0.06390 0.05613 0.09332 -0.00174 0.01413  -0.00501 42  LEU A CB  
112  C  CG  . LEU A 42  ? 0.07654 0.06391 0.10588 0.00064  0.00296  -0.00618 42  LEU A CG  
113  C  CD1 . LEU A 42  ? 0.07897 0.08631 0.08518 -0.00743 -0.01365 -0.01074 42  LEU A CD1 
114  C  CD2 . LEU A 42  ? 0.09521 0.06552 0.11832 -0.00489 0.00138  0.01130  42  LEU A CD2 
115  N  N   . VAL A 43  ? 0.04719 0.07512 0.06921 0.00875  0.01476  -0.01188 43  VAL A N   
116  C  CA  . VAL A 43  ? 0.06229 0.08790 0.08222 -0.00436 0.00651  -0.01775 43  VAL A CA  
117  C  C   . VAL A 43  ? 0.07101 0.09183 0.07694 0.00897  -0.00009 -0.01318 43  VAL A C   
118  O  O   . VAL A 43  ? 0.07601 0.12312 0.07387 0.02724  -0.00454 -0.02419 43  VAL A O   
119  C  CB  . VAL A 43  ? 0.07876 0.10047 0.07990 -0.00492 0.00749  -0.00655 43  VAL A CB  
120  C  CG1 . VAL A 43  ? 0.07625 0.14254 0.11472 -0.01075 0.01424  0.00934  43  VAL A CG1 
121  C  CG2 . VAL A 43  ? 0.10186 0.08993 0.11689 -0.01182 0.01532  -0.01407 43  VAL A CG2 
122  N  N   . GLY A 44  ? 0.08217 0.08904 0.08431 0.01792  -0.00650 -0.01060 44  GLY A N   
123  C  CA  . GLY A 44  ? 0.09215 0.11154 0.10844 0.03059  -0.00504 -0.04165 44  GLY A CA  
124  C  C   . GLY A 44  ? 0.11584 0.15211 0.10844 0.04755  -0.01695 -0.05430 44  GLY A C   
125  O  O   . GLY A 44  ? 0.11546 0.16902 0.13389 0.04142  -0.01204 -0.06592 44  GLY A O   
126  N  N   . ARG A 45  ? 0.14980 0.18061 0.10322 0.08362  -0.02853 -0.05529 45  ARG A N   
127  C  CA  . ARG A 45  ? 0.21947 0.24389 0.14172 0.11534  -0.02059 -0.06632 45  ARG A CA  
128  C  C   . ARG A 45  ? 0.27347 0.28814 0.14530 0.14831  -0.05467 -0.06556 45  ARG A C   
129  O  O   . ARG A 45  ? 0.27651 0.27743 0.16099 0.15335  -0.06093 -0.06435 45  ARG A O   
130  C  CB  . ARG A 45  ? 0.24694 0.28351 0.20817 0.12936  0.00986  -0.07433 45  ARG A CB  
131  C  CG  . ARG A 45  ? 0.27223 0.32680 0.26769 0.11589  0.05355  -0.06063 45  ARG A CG  
132  C  CD  . ARG A 45  ? 0.30039 0.36753 0.36470 0.09323  0.05998  -0.00866 45  ARG A CD  
133  N  NE  . ARG A 45  ? 0.31932 0.40443 0.43847 0.08570  0.06970  -0.00102 45  ARG A NE  
134  C  CZ  . ARG A 45  ? 0.33153 0.43277 0.48995 0.08886  0.08447  -0.00026 45  ARG A CZ  
135  N  NH1 . ARG A 45  ? 0.34031 0.43966 0.51034 0.09564  0.09211  -0.00450 45  ARG A NH1 
136  N  NH2 . ARG A 45  ? 0.33094 0.45075 0.49787 0.08336  0.09649  0.00705  45  ARG A NH2 
137  N  N   . ASN A 46  ? 0.33102 0.36490 0.21755 0.14208  -0.08839 -0.02051 46  ASN A N   
138  C  CA  . ASN A 46  ? 0.39741 0.45787 0.25241 0.12400  -0.10518 0.01813  46  ASN A CA  
139  C  C   . ASN A 46  ? 0.43183 0.47048 0.30248 0.12773  -0.10915 0.02779  46  ASN A C   
140  O  O   . ASN A 46  ? 0.43152 0.46374 0.29980 0.12272  -0.10511 0.02687  46  ASN A O   
141  C  CB  . ASN A 46  ? 0.42260 0.55041 0.30860 0.10806  -0.10344 0.02826  46  ASN A CB  
142  C  CG  . ASN A 46  ? 0.44056 0.62023 0.37188 0.09823  -0.07784 0.03830  46  ASN A CG  
143  O  OD1 . ASN A 46  ? 0.45665 0.63591 0.36884 0.10729  -0.08177 0.03732  46  ASN A OD1 
144  N  ND2 . ASN A 46  ? 0.45943 0.67903 0.41855 0.08618  -0.05817 0.03835  46  ASN A ND2 
145  N  N   . LYS A 47  ? 0.46425 0.47858 0.37492 0.13626  -0.11818 0.04389  47  LYS A N   
146  C  CA  . LYS A 47  ? 0.49532 0.47863 0.45072 0.14073  -0.10696 0.03967  47  LYS A CA  
147  C  C   . LYS A 47  ? 0.49258 0.43839 0.43544 0.14428  -0.08792 0.01123  47  LYS A C   
148  O  O   . LYS A 47  ? 0.49379 0.42960 0.42664 0.14796  -0.10011 -0.00407 47  LYS A O   
149  C  CB  . LYS A 47  ? 0.52810 0.51903 0.53903 0.13792  -0.10647 0.06042  47  LYS A CB  
150  C  CG  . LYS A 47  ? 0.55148 0.57308 0.61400 0.13417  -0.10515 0.09511  47  LYS A CG  
151  C  CD  . LYS A 47  ? 0.56275 0.62146 0.66865 0.13190  -0.10734 0.11399  47  LYS A CD  
152  C  CE  . LYS A 47  ? 0.57206 0.64597 0.70873 0.12885  -0.10086 0.11927  47  LYS A CE  
153  N  NZ  . LYS A 47  ? 0.57384 0.65047 0.72860 0.12659  -0.10234 0.13071  47  LYS A NZ  
154  N  N   . ASN A 48  ? 0.48841 0.41264 0.44479 0.14512  -0.06969 0.01256  48  ASN A N   
155  C  CA  . ASN A 48  ? 0.48428 0.39123 0.46112 0.14622  -0.06300 0.02051  48  ASN A CA  
156  C  C   . ASN A 48  ? 0.44232 0.35084 0.41901 0.15974  -0.04902 -0.00793 48  ASN A C   
157  O  O   . ASN A 48  ? 0.44036 0.34586 0.43165 0.17578  -0.04240 -0.02063 48  ASN A O   
158  C  CB  . ASN A 48  ? 0.51471 0.41000 0.49907 0.13320  -0.06310 0.04058  48  ASN A CB  
159  C  CG  . ASN A 48  ? 0.53809 0.42590 0.54627 0.12432  -0.04942 0.06523  48  ASN A CG  
160  O  OD1 . ASN A 48  ? 0.55635 0.42708 0.53147 0.12240  -0.05113 0.08425  48  ASN A OD1 
161  N  ND2 . ASN A 48  ? 0.55983 0.43391 0.57199 0.11913  -0.04011 0.07159  48  ASN A ND2 
162  N  N   . PRO A 49  ? 0.39863 0.31107 0.37607 0.15799  -0.03659 -0.03007 49  PRO A N   
163  C  CA  . PRO A 49  ? 0.36151 0.28915 0.33671 0.14704  -0.03287 -0.04403 49  PRO A CA  
164  C  C   . PRO A 49  ? 0.31025 0.24000 0.27027 0.12939  -0.03155 -0.04697 49  PRO A C   
165  O  O   . PRO A 49  ? 0.31166 0.25047 0.29255 0.13846  -0.04220 -0.03476 49  PRO A O   
166  C  CB  . PRO A 49  ? 0.37207 0.31428 0.37082 0.15005  -0.03332 -0.04257 49  PRO A CB  
167  C  CG  . PRO A 49  ? 0.38510 0.32039 0.39037 0.14364  -0.02603 -0.03802 49  PRO A CG  
168  C  CD  . PRO A 49  ? 0.39319 0.31353 0.38532 0.14934  -0.03270 -0.03224 49  PRO A CD  
169  N  N   . GLN A 50  ? 0.25388 0.18549 0.18816 0.09945  -0.01755 -0.05359 50  GLN A N   
170  C  CA  . GLN A 50  ? 0.19667 0.15863 0.16297 0.06510  -0.00038 -0.03394 50  GLN A CA  
171  C  C   . GLN A 50  ? 0.16615 0.16054 0.15281 0.04031  0.01519  -0.00827 50  GLN A C   
172  O  O   . GLN A 50  ? 0.16643 0.18544 0.16427 0.04992  0.04425  0.00521  50  GLN A O   
173  C  CB  . GLN A 50  ? 0.19490 0.15255 0.13301 0.04636  0.01245  -0.00525 50  GLN A CB  
174  C  CG  . GLN A 50  ? 0.20465 0.15193 0.16265 0.04481  -0.01154 -0.01235 50  GLN A CG  
175  C  CD  . GLN A 50  ? 0.20844 0.15603 0.13749 0.05491  -0.02503 -0.00420 50  GLN A CD  
176  O  OE1 . GLN A 50  ? 0.19759 0.14616 0.15296 0.04996  -0.02146 -0.04062 50  GLN A OE1 
177  N  NE2 . GLN A 50  ? 0.22377 0.18146 0.18367 0.05360  -0.03364 -0.00695 50  GLN A NE2 
178  N  N   . MET A 51  ? 0.14243 0.14403 0.10727 0.01151  0.00052  -0.03162 51  MET A N   
179  C  CA  . MET A 51  ? 0.12498 0.14499 0.11064 -0.01642 0.00686  -0.03760 51  MET A CA  
180  C  C   . MET A 51  ? 0.11660 0.14930 0.11265 -0.02490 0.02352  -0.05503 51  MET A C   
181  O  O   . MET A 51  ? 0.11077 0.14603 0.10708 -0.02479 0.03196  -0.03536 51  MET A O   
182  C  CB  . MET A 51  ? 0.13044 0.16002 0.11907 -0.02340 0.01666  -0.05973 51  MET A CB  
183  C  CG  . MET A 51  ? 0.13275 0.17437 0.12570 -0.02816 0.01809  -0.05135 51  MET A CG  
184  S  SD  . MET A 51  ? 0.13634 0.17299 0.12127 -0.03860 0.01268  -0.04037 51  MET A SD  
185  C  CE  . MET A 51  ? 0.14423 0.18484 0.13731 -0.02854 0.05332  -0.04466 51  MET A CE  
186  N  N   . ASN A 52  ? 0.12317 0.15362 0.09506 -0.02906 0.03740  -0.04389 52  ASN A N   
187  C  CA  . ASN A 52  ? 0.12182 0.16892 0.09462 -0.02080 0.04366  -0.05181 52  ASN A CA  
188  C  C   . ASN A 52  ? 0.11131 0.16141 0.08722 -0.04376 0.03896  -0.02708 52  ASN A C   
189  O  O   . ASN A 52  ? 0.10943 0.15122 0.10009 -0.04575 0.03999  -0.04016 52  ASN A O   
190  C  CB  . ASN A 52  ? 0.13563 0.20912 0.09810 -0.02407 0.04537  -0.04206 52  ASN A CB  
191  C  CG  . ASN A 52  ? 0.15233 0.25812 0.12459 -0.02449 0.03066  -0.06174 52  ASN A CG  
192  O  OD1 . ASN A 52  ? 0.14207 0.25971 0.12727 -0.04285 0.05806  -0.05223 52  ASN A OD1 
193  N  ND2 . ASN A 52  ? 0.18427 0.30404 0.12360 -0.00774 0.04584  -0.06993 52  ASN A ND2 
194  N  N   . PHE A 53  ? 0.11283 0.17009 0.08305 -0.04560 0.02451  -0.03782 53  PHE A N   
195  C  CA  . PHE A 53  ? 0.11748 0.17149 0.07282 -0.05506 0.01931  -0.03207 53  PHE A CA  
196  C  C   . PHE A 53  ? 0.11312 0.18269 0.06606 -0.06550 0.01615  -0.02447 53  PHE A C   
197  O  O   . PHE A 53  ? 0.12369 0.17310 0.09172 -0.07092 0.02767  -0.03938 53  PHE A O   
198  C  CB  . PHE A 53  ? 0.13582 0.15835 0.08323 -0.05300 0.02624  -0.03792 53  PHE A CB  
199  C  CG  . PHE A 53  ? 0.15972 0.15642 0.07283 -0.05093 0.03945  -0.03013 53  PHE A CG  
200  C  CD1 . PHE A 53  ? 0.16698 0.14543 0.08520 -0.06278 0.01926  -0.02343 53  PHE A CD1 
201  C  CD2 . PHE A 53  ? 0.19860 0.17177 0.12734 -0.04447 0.05367  -0.01540 53  PHE A CD2 
202  C  CE1 . PHE A 53  ? 0.18246 0.15609 0.11037 -0.07012 0.03350  -0.02746 53  PHE A CE1 
203  C  CE2 . PHE A 53  ? 0.21468 0.18121 0.14881 -0.04410 0.06498  -0.02055 53  PHE A CE2 
204  C  CZ  . PHE A 53  ? 0.20718 0.17444 0.14121 -0.05429 0.05502  -0.04519 53  PHE A CZ  
205  N  N   . THR A 54  ? 0.10626 0.19568 0.08662 -0.07527 0.02255  -0.03499 54  THR A N   
206  C  CA  . THR A 54  ? 0.10153 0.21199 0.07331 -0.06643 0.01047  -0.00911 54  THR A CA  
207  C  C   . THR A 54  ? 0.10014 0.18608 0.08071 -0.05565 0.03050  -0.02050 54  THR A C   
208  O  O   . THR A 54  ? 0.11601 0.17729 0.07840 -0.06768 0.01274  -0.00175 54  THR A O   
209  C  CB  . THR A 54  ? 0.11558 0.26221 0.08604 -0.05767 0.01375  -0.00796 54  THR A CB  
210  O  OG1 . THR A 54  ? 0.14079 0.30811 0.12041 -0.03645 0.02439  0.00352  54  THR A OG1 
211  C  CG2 . THR A 54  ? 0.12122 0.26284 0.14080 -0.06646 0.04461  -0.01301 54  THR A CG2 
212  N  N   . GLU A 55  ? 0.09437 0.16885 0.08042 -0.04181 0.03605  -0.02832 55  GLU A N   
213  C  CA  . GLU A 55  ? 0.10533 0.16281 0.08929 -0.03343 0.03071  -0.01888 55  GLU A CA  
214  C  C   . GLU A 55  ? 0.09570 0.14324 0.09830 -0.03919 0.02604  -0.01831 55  GLU A C   
215  O  O   . GLU A 55  ? 0.09030 0.14352 0.07908 -0.03099 0.02256  -0.01776 55  GLU A O   
216  C  CB  . GLU A 55  ? 0.11462 0.18216 0.12230 -0.02864 0.02944  -0.03609 55  GLU A CB  
217  C  CG  . GLU A 55  ? 0.11983 0.20177 0.14813 -0.02329 0.06145  -0.06415 55  GLU A CG  
218  C  CD  . GLU A 55  ? 0.12507 0.24085 0.22480 -0.01837 0.07047  -0.07767 55  GLU A CD  
219  O  OE1 . GLU A 55  ? 0.12545 0.24659 0.20771 -0.01554 0.07130  -0.07398 55  GLU A OE1 
220  O  OE2 . GLU A 55  ? 0.13064 0.26222 0.28978 -0.01202 0.05538  -0.07399 55  GLU A OE2 
221  N  N   . ALA A 56  ? 0.08960 0.14886 0.08349 -0.04719 0.02621  -0.02789 56  ALA A N   
222  C  CA  . ALA A 56  ? 0.08414 0.15447 0.06648 -0.04405 0.02152  -0.02492 56  ALA A CA  
223  C  C   . ALA A 56  ? 0.08656 0.15866 0.06202 -0.03359 0.02695  -0.01180 56  ALA A C   
224  O  O   . ALA A 56  ? 0.08685 0.15266 0.05353 -0.04418 0.01811  -0.02037 56  ALA A O   
225  C  CB  . ALA A 56  ? 0.08319 0.15368 0.08441 -0.04379 0.02837  -0.03056 56  ALA A CB  
226  N  N   A ASN A 57  ? 0.08950 0.15731 0.06528 -0.02879 0.02302  -0.00873 57  ASN A N   
227  N  N   B ASN A 57  ? 0.08965 0.16264 0.06804 -0.02929 0.02779  -0.01403 57  ASN A N   
228  C  CA  A ASN A 57  ? 0.09270 0.13998 0.07844 -0.01647 -0.00087 0.00414  57  ASN A CA  
229  C  CA  B ASN A 57  ? 0.09466 0.15149 0.07923 -0.02144 0.02134  -0.01088 57  ASN A CA  
230  C  C   A ASN A 57  ? 0.08563 0.13350 0.07587 -0.02209 0.01392  -0.00098 57  ASN A C   
231  C  C   B ASN A 57  ? 0.08671 0.13775 0.07095 -0.02669 0.02185  -0.00852 57  ASN A C   
232  O  O   A ASN A 57  ? 0.08357 0.13722 0.08137 -0.02223 0.00122  -0.01177 57  ASN A O   
233  O  O   B ASN A 57  ? 0.08826 0.13673 0.08074 -0.02995 0.01318  -0.01155 57  ASN A O   
234  C  CB  A ASN A 57  ? 0.10926 0.14244 0.09897 -0.00438 -0.01153 0.02529  57  ASN A CB  
235  C  CB  B ASN A 57  ? 0.11136 0.16249 0.10149 -0.01249 0.02535  -0.00356 57  ASN A CB  
236  C  CG  A ASN A 57  ? 0.11767 0.13294 0.07919 -0.00910 0.00340  0.02276  57  ASN A CG  
237  C  CG  B ASN A 57  ? 0.12193 0.15971 0.10410 -0.01312 0.04286  0.00351  57  ASN A CG  
238  O  OD1 A ASN A 57  ? 0.12440 0.13461 0.11850 -0.00303 0.04400  -0.02312 57  ASN A OD1 
239  O  OD1 B ASN A 57  ? 0.13236 0.16830 0.09228 -0.01653 0.03364  0.03291  57  ASN A OD1 
240  N  ND2 A ASN A 57  ? 0.12013 0.12750 0.09468 -0.02453 0.00128  0.04319  57  ASN A ND2 
241  N  ND2 B ASN A 57  ? 0.12222 0.15801 0.09448 -0.01278 0.04844  0.00222  57  ASN A ND2 
242  N  N   . GLU A 58  ? 0.07409 0.12887 0.07185 -0.02875 0.01967  -0.01016 58  GLU A N   
243  C  CA  . GLU A 58  ? 0.06639 0.13447 0.06259 -0.01907 0.02585  -0.02220 58  GLU A CA  
244  C  C   . GLU A 58  ? 0.07140 0.12549 0.07523 -0.02825 0.01695  -0.02037 58  GLU A C   
245  O  O   . GLU A 58  ? 0.07243 0.13532 0.08519 -0.03175 0.00499  -0.03103 58  GLU A O   
246  C  CB  . GLU A 58  ? 0.07163 0.13333 0.10258 -0.01642 0.03060  -0.02189 58  GLU A CB  
247  C  CG  . GLU A 58  ? 0.07664 0.15040 0.11215 -0.02610 0.04536  -0.00587 58  GLU A CG  
248  C  CD  . GLU A 58  ? 0.08105 0.16109 0.12114 -0.02023 0.05191  -0.00308 58  GLU A CD  
249  O  OE1 . GLU A 58  ? 0.08199 0.19668 0.14412 0.00636  0.00771  0.02017  58  GLU A OE1 
250  O  OE2 . GLU A 58  ? 0.09533 0.16267 0.17717 -0.02855 0.04794  -0.00244 58  GLU A OE2 
251  N  N   . ALA A 59  ? 0.07668 0.12024 0.07255 -0.02173 0.01453  -0.01836 59  ALA A N   
252  C  CA  . ALA A 59  ? 0.08122 0.12459 0.07545 -0.01929 0.01404  -0.01506 59  ALA A CA  
253  C  C   . ALA A 59  ? 0.06201 0.12266 0.08217 -0.02459 0.01485  -0.01551 59  ALA A C   
254  O  O   . ALA A 59  ? 0.06165 0.13687 0.09345 -0.01697 0.01006  -0.02719 59  ALA A O   
255  C  CB  . ALA A 59  ? 0.09494 0.11607 0.07946 -0.01045 0.00481  0.00572  59  ALA A CB  
256  N  N   . CYS A 60  ? 0.05415 0.11333 0.07775 -0.02354 0.00565  -0.00714 60  CYS A N   
257  C  CA  . CYS A 60  ? 0.05354 0.11448 0.10657 -0.02493 0.00221  -0.01631 60  CYS A CA  
258  C  C   . CYS A 60  ? 0.05740 0.14122 0.06814 -0.02347 -0.00064 -0.02569 60  CYS A C   
259  O  O   . CYS A 60  ? 0.06914 0.14495 0.07089 -0.02393 0.00544  -0.01627 60  CYS A O   
260  C  CB  . CYS A 60  ? 0.05830 0.12342 0.10869 -0.03869 0.00479  -0.00905 60  CYS A CB  
261  S  SG  . CYS A 60  ? 0.06650 0.13398 0.08752 -0.02045 0.01621  -0.02180 60  CYS A SG  
262  N  N   . LYS A 61  ? 0.05446 0.13868 0.07469 -0.03101 0.00550  -0.01693 61  LYS A N   
263  C  CA  . LYS A 61  ? 0.07428 0.14610 0.08173 -0.02674 0.00919  -0.01719 61  LYS A CA  
264  C  C   . LYS A 61  ? 0.07441 0.15124 0.08002 -0.03612 0.01421  -0.00769 61  LYS A C   
265  O  O   . LYS A 61  ? 0.08121 0.15380 0.08761 -0.04597 0.01039  -0.03022 61  LYS A O   
266  C  CB  . LYS A 61  ? 0.09208 0.14815 0.08666 -0.02188 0.01731  -0.00599 61  LYS A CB  
267  C  CG  . LYS A 61  ? 0.11551 0.17318 0.14398 -0.01970 0.01281  -0.00249 61  LYS A CG  
268  C  CD  . LYS A 61  ? 0.13674 0.20615 0.13277 -0.01512 0.00547  0.01194  61  LYS A CD  
269  C  CE  . LYS A 61  ? 0.15014 0.22355 0.12184 0.00103  0.02160  0.03260  61  LYS A CE  
270  N  NZ  . LYS A 61  ? 0.14727 0.22528 0.08937 0.01087  -0.00293 0.03162  61  LYS A NZ  
271  N  N   . MET A 62  ? 0.07458 0.14831 0.06859 -0.03639 0.01507  0.01080  62  MET A N   
272  C  CA  . MET A 62  ? 0.07781 0.16579 0.06859 -0.01561 0.00401  -0.01344 62  MET A CA  
273  C  C   . MET A 62  ? 0.07063 0.18320 0.07955 -0.02920 0.00394  -0.01456 62  MET A C   
274  O  O   . MET A 62  ? 0.07154 0.19900 0.08971 -0.03640 -0.00638 -0.03438 62  MET A O   
275  C  CB  . MET A 62  ? 0.08388 0.15810 0.06429 0.00282  0.00735  -0.01016 62  MET A CB  
276  C  CG  . MET A 62  ? 0.08936 0.15011 0.10760 0.01734  0.01826  0.00494  62  MET A CG  
277  S  SD  . MET A 62  ? 0.10988 0.16185 0.12740 0.01015  -0.00028 -0.01911 62  MET A SD  
278  C  CE  . MET A 62  ? 0.12275 0.17915 0.17042 -0.00459 0.00197  0.00997  62  MET A CE  
279  N  N   . LEU A 63  ? 0.07852 0.19408 0.07983 -0.02394 0.02814  -0.00902 63  LEU A N   
280  C  CA  . LEU A 63  ? 0.08078 0.21787 0.10021 -0.03232 0.02141  -0.02228 63  LEU A CA  
281  C  C   . LEU A 63  ? 0.09024 0.20158 0.11193 -0.03706 0.02453  -0.05079 63  LEU A C   
282  O  O   . LEU A 63  ? 0.11177 0.21631 0.12305 -0.03678 0.03152  -0.07596 63  LEU A O   
283  C  CB  . LEU A 63  ? 0.09235 0.23329 0.11726 -0.02004 0.02528  -0.00310 63  LEU A CB  
284  C  CG  . LEU A 63  ? 0.10843 0.24925 0.11623 -0.03590 -0.00178 -0.00424 63  LEU A CG  
285  C  CD1 . LEU A 63  ? 0.11138 0.25844 0.12621 -0.04754 0.03359  0.02794  63  LEU A CD1 
286  C  CD2 . LEU A 63  ? 0.12655 0.26045 0.14175 -0.02818 -0.01728 -0.01912 63  LEU A CD2 
287  N  N   . GLY A 64  ? 0.09392 0.16819 0.13040 -0.02725 0.02143  -0.05656 64  GLY A N   
288  C  CA  . GLY A 64  ? 0.10788 0.15247 0.17800 -0.03154 0.02419  -0.05677 64  GLY A CA  
289  C  C   . GLY A 64  ? 0.11933 0.14201 0.17904 -0.03497 0.03542  -0.06506 64  GLY A C   
290  O  O   . GLY A 64  ? 0.13747 0.15859 0.26130 -0.04974 0.03691  -0.09234 64  GLY A O   
291  N  N   . LEU A 65  ? 0.09973 0.13828 0.12720 -0.04933 0.03319  -0.05898 65  LEU A N   
292  C  CA  . LEU A 65  ? 0.10326 0.14632 0.11279 -0.04732 0.03175  -0.04397 65  LEU A CA  
293  C  C   . LEU A 65  ? 0.11809 0.12632 0.11452 -0.04806 0.02474  -0.03595 65  LEU A C   
294  O  O   . LEU A 65  ? 0.12605 0.14719 0.11519 -0.03109 0.03620  -0.02235 65  LEU A O   
295  C  CB  . LEU A 65  ? 0.09798 0.16420 0.10282 -0.03509 0.01464  -0.05104 65  LEU A CB  
296  C  CG  . LEU A 65  ? 0.10370 0.18812 0.09971 -0.02384 0.00801  -0.05564 65  LEU A CG  
297  C  CD1 . LEU A 65  ? 0.10729 0.19904 0.14344 -0.04342 -0.01617 0.01142  65  LEU A CD1 
298  C  CD2 . LEU A 65  ? 0.12427 0.22299 0.14076 0.00620  0.01726  -0.08755 65  LEU A CD2 
299  N  N   . THR A 66  ? 0.12164 0.10131 0.09741 -0.05642 0.01601  -0.02212 66  THR A N   
300  C  CA  . THR A 66  ? 0.12846 0.09389 0.11773 -0.05021 0.02827  -0.00655 66  THR A CA  
301  C  C   . THR A 66  ? 0.11145 0.09195 0.06515 -0.04296 0.01774  -0.00649 66  THR A C   
302  O  O   . THR A 66  ? 0.11905 0.11443 0.06513 -0.04661 0.02993  -0.01159 66  THR A O   
303  C  CB  . THR A 66  ? 0.16261 0.11112 0.16685 -0.04258 0.02313  0.02297  66  THR A CB  
304  O  OG1 . THR A 66  ? 0.18432 0.13955 0.19335 -0.01494 0.00648  0.00957  66  THR A OG1 
305  C  CG2 . THR A 66  ? 0.17923 0.10872 0.20130 -0.04185 0.03456  0.02298  66  THR A CG2 
306  N  N   . LEU A 67  ? 0.11425 0.08244 0.07149 -0.03716 0.00142  0.00451  67  LEU A N   
307  C  CA  . LEU A 67  ? 0.12533 0.07159 0.06785 -0.03085 -0.01400 -0.01585 67  LEU A CA  
308  C  C   . LEU A 67  ? 0.11629 0.07545 0.11143 -0.02963 -0.01101 0.01605  67  LEU A C   
309  O  O   . LEU A 67  ? 0.12262 0.10483 0.18744 -0.02324 0.00597  0.05490  67  LEU A O   
310  C  CB  . LEU A 67  ? 0.15910 0.07927 0.13584 -0.03499 -0.01810 0.00483  67  LEU A CB  
311  C  CG  . LEU A 67  ? 0.16484 0.07632 0.16801 -0.01212 -0.02491 -0.01950 67  LEU A CG  
312  C  CD1 . LEU A 67  ? 0.14749 0.07099 0.10017 -0.01795 -0.01734 -0.00453 67  LEU A CD1 
313  C  CD2 . LEU A 67  ? 0.18588 0.10624 0.13847 0.00537  -0.04891 -0.03073 67  LEU A CD2 
314  N  N   . ALA A 68  ? 0.10022 0.07090 0.07639 -0.03386 -0.01092 0.01407  68  ALA A N   
315  C  CA  . ALA A 68  ? 0.09978 0.07914 0.09156 -0.02349 -0.01662 0.00609  68  ALA A CA  
316  C  C   . ALA A 68  ? 0.09587 0.07160 0.08396 -0.01807 -0.00685 0.00620  68  ALA A C   
317  O  O   . ALA A 68  ? 0.10361 0.08039 0.09863 -0.01679 -0.00678 -0.00447 68  ALA A O   
318  C  CB  . ALA A 68  ? 0.10047 0.09022 0.08276 -0.02331 -0.00997 0.01383  68  ALA A CB  
319  N  N   . SER A 69  ? 0.09139 0.07385 0.09403 -0.01260 -0.00534 0.01728  69  SER A N   
320  C  CA  . SER A 69  ? 0.09757 0.07773 0.08389 -0.00800 -0.00556 0.01673  69  SER A CA  
321  C  C   . SER A 69  ? 0.09688 0.08057 0.06703 0.00056  0.00002  0.01052  69  SER A C   
322  O  O   . SER A 69  ? 0.09363 0.07466 0.06764 0.00285  -0.01419 0.00549  69  SER A O   
323  C  CB  . SER A 69  ? 0.11861 0.08617 0.10775 -0.00091 -0.00701 0.00753  69  SER A CB  
324  O  OG  . SER A 69  ? 0.12477 0.07727 0.11251 0.00040  -0.00423 0.02063  69  SER A OG  
325  N  N   . ARG A 70  ? 0.09323 0.08257 0.07247 -0.00699 -0.02160 0.00680  70  ARG A N   
326  C  CA  . ARG A 70  ? 0.08625 0.09183 0.07550 -0.01787 -0.00833 -0.00960 70  ARG A CA  
327  C  C   . ARG A 70  ? 0.08914 0.08826 0.07299 -0.01732 -0.02447 0.00755  70  ARG A C   
328  O  O   . ARG A 70  ? 0.08636 0.08889 0.08264 -0.01331 -0.00524 0.00871  70  ARG A O   
329  C  CB  . ARG A 70  ? 0.09838 0.11288 0.08434 -0.01782 -0.02006 -0.00541 70  ARG A CB  
330  C  CG  . ARG A 70  ? 0.10862 0.15055 0.11145 -0.02720 -0.00959 -0.01130 70  ARG A CG  
331  C  CD  . ARG A 70  ? 0.12537 0.17558 0.18371 -0.02120 -0.01707 -0.01545 70  ARG A CD  
332  N  NE  . ARG A 70  ? 0.14089 0.18832 0.23797 -0.00396 -0.02276 -0.04215 70  ARG A NE  
333  C  CZ  . ARG A 70  ? 0.15400 0.18609 0.25962 -0.00089 -0.02644 -0.03806 70  ARG A CZ  
334  N  NH1 . ARG A 70  ? 0.16357 0.18860 0.25357 -0.00910 -0.04744 -0.03486 70  ARG A NH1 
335  N  NH2 . ARG A 70  ? 0.15844 0.17043 0.28788 0.01042  -0.02579 -0.07173 70  ARG A NH2 
336  N  N   . ASP A 71  ? 0.09765 0.08267 0.06975 0.00023  -0.02123 0.00224  71  ASP A N   
337  C  CA  . ASP A 71  ? 0.11111 0.09053 0.07996 0.01245  -0.03677 0.00232  71  ASP A CA  
338  C  C   . ASP A 71  ? 0.09288 0.08292 0.08842 0.00204  -0.02494 0.00674  71  ASP A C   
339  O  O   . ASP A 71  ? 0.09524 0.09283 0.08451 0.01203  -0.00676 0.00695  71  ASP A O   
340  C  CB  . ASP A 71  ? 0.14214 0.12237 0.09202 0.02199  -0.04971 0.02399  71  ASP A CB  
341  C  CG  . ASP A 71  ? 0.16833 0.15007 0.18161 0.02585  -0.04513 0.04684  71  ASP A CG  
342  O  OD1 . ASP A 71  ? 0.18064 0.17131 0.19429 0.01796  -0.06570 0.00561  71  ASP A OD1 
343  O  OD2 . ASP A 71  ? 0.17919 0.18095 0.22197 0.03052  -0.03121 0.07311  71  ASP A OD2 
344  N  N   . GLN A 72  ? 0.08540 0.06693 0.09566 -0.00894 -0.01940 0.01134  72  GLN A N   
345  C  CA  . GLN A 72  ? 0.07930 0.06226 0.09057 -0.00426 -0.00118 0.00781  72  GLN A CA  
346  C  C   . GLN A 72  ? 0.06606 0.05417 0.09690 0.00152  -0.00081 0.00007  72  GLN A C   
347  O  O   . GLN A 72  ? 0.06151 0.07106 0.06898 0.00033  0.00476  0.00169  72  GLN A O   
348  C  CB  . GLN A 72  ? 0.08665 0.06081 0.10292 -0.01160 0.00167  0.02342  72  GLN A CB  
349  C  CG  . GLN A 72  ? 0.10170 0.06074 0.10505 -0.00944 0.01053  0.01181  72  GLN A CG  
350  C  CD  . GLN A 72  ? 0.11366 0.06058 0.10967 -0.01203 0.00876  0.01242  72  GLN A CD  
351  O  OE1 . GLN A 72  ? 0.10413 0.07780 0.10363 -0.02163 0.01339  0.00011  72  GLN A OE1 
352  N  NE2 . GLN A 72  ? 0.12459 0.05886 0.15480 -0.02466 0.00362  0.01072  72  GLN A NE2 
353  N  N   . VAL A 73  ? 0.07226 0.04975 0.06276 0.00132  0.00034  -0.00284 73  VAL A N   
354  C  CA  . VAL A 73  ? 0.07521 0.05271 0.06235 0.00124  0.01620  0.00585  73  VAL A CA  
355  C  C   . VAL A 73  ? 0.07966 0.05375 0.06891 0.00327  0.00051  -0.00332 73  VAL A C   
356  O  O   . VAL A 73  ? 0.07068 0.06777 0.06958 0.00497  0.00733  -0.00303 73  VAL A O   
357  C  CB  . VAL A 73  ? 0.07341 0.05917 0.07752 0.00388  0.01123  0.00101  73  VAL A CB  
358  C  CG1 . VAL A 73  ? 0.08752 0.06526 0.09522 -0.00158 0.02273  0.00838  73  VAL A CG1 
359  C  CG2 . VAL A 73  ? 0.07882 0.08508 0.06402 0.00861  0.00644  0.01424  73  VAL A CG2 
360  N  N   . GLU A 74  ? 0.08179 0.05979 0.08976 0.01296  -0.00660 -0.01630 74  GLU A N   
361  C  CA  . GLU A 74  ? 0.09816 0.09672 0.08763 0.02225  -0.01396 -0.02908 74  GLU A CA  
362  C  C   . GLU A 74  ? 0.07787 0.06653 0.10184 0.01162  -0.01662 0.00360  74  GLU A C   
363  O  O   . GLU A 74  ? 0.08051 0.07799 0.09291 0.00575  0.00001  0.00015  74  GLU A O   
364  C  CB  . GLU A 74  ? 0.15184 0.19594 0.11398 0.02956  -0.02268 -0.05223 74  GLU A CB  
365  C  CG  . GLU A 74  ? 0.21556 0.31713 0.25482 0.04172  0.00283  -0.05824 74  GLU A CG  
366  C  CD  . GLU A 74  ? 0.31596 0.43515 0.44047 0.05543  0.04156  -0.04465 74  GLU A CD  
367  O  OE1 . GLU A 74  ? 0.40123 0.53173 0.49663 0.05764  0.06833  -0.03607 74  GLU A OE1 
368  O  OE2 . GLU A 74  ? 0.31874 0.46699 0.50662 0.06271  0.04677  -0.03448 74  GLU A OE2 
369  N  N   A SER A 75  ? 0.07671 0.05491 0.08653 0.01325  -0.00948 0.00538  75  SER A N   
370  N  N   B SER A 75  ? 0.08717 0.06259 0.09125 0.01295  -0.00792 0.00094  75  SER A N   
371  C  CA  A SER A 75  ? 0.08637 0.06917 0.10771 0.02218  0.00088  -0.00057 75  SER A CA  
372  C  CA  B SER A 75  ? 0.09601 0.06096 0.10341 0.01966  0.00747  -0.00266 75  SER A CA  
373  C  C   A SER A 75  ? 0.07311 0.04733 0.06104 0.02412  -0.00697 0.00199  75  SER A C   
374  C  C   B SER A 75  ? 0.08800 0.06485 0.10486 0.02363  0.00583  0.00349  75  SER A C   
375  O  O   A SER A 75  ? 0.07721 0.04773 0.05572 0.00317  0.00809  -0.01735 75  SER A O   
376  O  O   B SER A 75  ? 0.10719 0.09698 0.15322 0.01880  0.00811  -0.00151 75  SER A O   
377  C  CB  A SER A 75  ? 0.10686 0.08201 0.13824 0.02053  0.00595  0.00755  75  SER A CB  
378  C  CB  B SER A 75  ? 0.10849 0.04594 0.09869 0.01689  0.00901  -0.00155 75  SER A CB  
379  O  OG  A SER A 75  ? 0.12164 0.09635 0.18785 0.01619  0.01246  -0.01292 75  SER A OG  
380  O  OG  B SER A 75  ? 0.11641 0.05145 0.09540 0.00945  0.01211  -0.01545 75  SER A OG  
381  N  N   . ALA A 76  ? 0.07065 0.04649 0.08243 0.01750  -0.00544 -0.00177 76  ALA A N   
382  C  CA  . ALA A 76  ? 0.05949 0.05545 0.08416 0.00388  0.00124  0.01223  76  ALA A CA  
383  C  C   . ALA A 76  ? 0.05935 0.05508 0.05782 0.00149  0.00495  0.00313  76  ALA A C   
384  O  O   . ALA A 76  ? 0.06532 0.06287 0.06493 -0.00333 0.00230  -0.00322 76  ALA A O   
385  C  CB  . ALA A 76  ? 0.05019 0.05246 0.08143 0.01593  0.01079  0.00338  76  ALA A CB  
386  N  N   . GLN A 77  ? 0.06475 0.05467 0.08040 -0.00351 0.00763  -0.00404 77  GLN A N   
387  C  CA  . GLN A 77  ? 0.06767 0.06187 0.06848 0.00367  0.00551  -0.01234 77  GLN A CA  
388  C  C   . GLN A 77  ? 0.07262 0.07466 0.09771 0.01080  0.00185  -0.00650 77  GLN A C   
389  O  O   . GLN A 77  ? 0.07202 0.07281 0.09463 0.00339  0.01911  -0.00936 77  GLN A O   
390  C  CB  . GLN A 77  ? 0.06868 0.05646 0.09971 -0.01117 0.00289  -0.02371 77  GLN A CB  
391  C  CG  . GLN A 77  ? 0.06982 0.05677 0.13703 -0.00515 -0.00973 -0.00910 77  GLN A CG  
392  C  CD  . GLN A 77  ? 0.07853 0.06606 0.14893 -0.00581 -0.01080 -0.01554 77  GLN A CD  
393  O  OE1 . GLN A 77  ? 0.09358 0.07448 0.19768 0.00679  -0.01386 -0.01508 77  GLN A OE1 
394  N  NE2 . GLN A 77  ? 0.07079 0.08888 0.15147 -0.02625 0.00331  -0.01866 77  GLN A NE2 
395  N  N   . LYS A 78  ? 0.06792 0.08752 0.08237 0.01618  0.00256  -0.01477 78  LYS A N   
396  C  CA  . LYS A 78  ? 0.08304 0.09846 0.10597 0.01170  0.00722  -0.01599 78  LYS A CA  
397  C  C   . LYS A 78  ? 0.09292 0.08354 0.11575 0.00795  0.03535  -0.00970 78  LYS A C   
398  O  O   . LYS A 78  ? 0.09225 0.12232 0.14219 0.01065  0.02132  -0.02879 78  LYS A O   
399  C  CB  . LYS A 78  ? 0.09570 0.12446 0.12649 0.01831  -0.00798 -0.02027 78  LYS A CB  
400  C  CG  . LYS A 78  ? 0.12009 0.17554 0.19398 0.03224  -0.01779 -0.00448 78  LYS A CG  
401  C  CD  . LYS A 78  ? 0.14146 0.24538 0.24352 0.04032  -0.03274 0.01658  78  LYS A CD  
402  C  CE  . LYS A 78  ? 0.15516 0.30135 0.32180 0.04742  -0.03293 0.03505  78  LYS A CE  
403  N  NZ  . LYS A 78  ? 0.18983 0.32523 0.38080 0.05072  -0.03093 0.03730  78  LYS A NZ  
404  N  N   . SER A 79  ? 0.09539 0.06486 0.11337 -0.00463 0.01885  -0.02617 79  SER A N   
405  C  CA  . SER A 79  ? 0.10186 0.07216 0.10771 -0.00345 0.01661  -0.01840 79  SER A CA  
406  C  C   . SER A 79  ? 0.11425 0.07283 0.06653 -0.00191 0.02401  -0.01821 79  SER A C   
407  O  O   . SER A 79  ? 0.13303 0.08299 0.10990 -0.00760 0.00583  -0.01215 79  SER A O   
408  C  CB  . SER A 79  ? 0.10364 0.06553 0.10845 -0.01227 0.00333  -0.00918 79  SER A CB  
409  O  OG  . SER A 79  ? 0.11943 0.05991 0.12993 0.00589  0.00629  -0.01413 79  SER A OG  
410  N  N   . GLY A 80  ? 0.11617 0.06473 0.08453 0.00858  0.03787  -0.01895 80  GLY A N   
411  C  CA  . GLY A 80  ? 0.11992 0.05481 0.08771 0.02034  0.02007  0.00013  80  GLY A CA  
412  C  C   . GLY A 80  ? 0.11711 0.05248 0.09656 0.00878  0.01656  -0.00289 80  GLY A C   
413  O  O   . GLY A 80  ? 0.12991 0.07477 0.10580 0.01831  0.01259  0.00588  80  GLY A O   
414  N  N   . PHE A 81  ? 0.09350 0.05411 0.07144 -0.00862 0.00800  -0.01556 81  PHE A N   
415  C  CA  . PHE A 81  ? 0.08223 0.05593 0.08726 0.00773  0.01803  -0.02154 81  PHE A CA  
416  C  C   . PHE A 81  ? 0.08548 0.06878 0.08554 0.00823  0.02284  -0.00683 81  PHE A C   
417  O  O   . PHE A 81  ? 0.08499 0.06095 0.09754 -0.00685 0.00041  -0.01574 81  PHE A O   
418  C  CB  . PHE A 81  ? 0.06396 0.07296 0.11008 0.01854  0.00467  -0.02174 81  PHE A CB  
419  C  CG  . PHE A 81  ? 0.07038 0.07968 0.11365 0.00616  0.01718  -0.02489 81  PHE A CG  
420  C  CD1 . PHE A 81  ? 0.08600 0.13005 0.14728 0.03647  0.01778  -0.02638 81  PHE A CD1 
421  C  CD2 . PHE A 81  ? 0.08227 0.09558 0.14129 -0.00799 0.03175  -0.04048 81  PHE A CD2 
422  C  CE1 . PHE A 81  ? 0.09897 0.13864 0.18753 0.03646  0.02537  -0.02477 81  PHE A CE1 
423  C  CE2 . PHE A 81  ? 0.08912 0.09712 0.17776 -0.01202 0.03115  -0.05069 81  PHE A CE2 
424  C  CZ  . PHE A 81  ? 0.09375 0.11089 0.19592 0.00524  0.02589  -0.03144 81  PHE A CZ  
425  N  N   . GLU A 82  ? 0.10124 0.06558 0.09574 0.01437  0.01380  -0.01167 82  GLU A N   
426  C  CA  . GLU A 82  ? 0.09371 0.07263 0.12699 0.00037  0.03029  0.01252  82  GLU A CA  
427  C  C   . GLU A 82  ? 0.08147 0.07073 0.09228 0.01180  0.00671  0.01152  82  GLU A C   
428  O  O   . GLU A 82  ? 0.09242 0.08132 0.10947 0.01345  0.00944  -0.00421 82  GLU A O   
429  C  CB  . GLU A 82  ? 0.11967 0.12359 0.22397 -0.00216 0.02919  0.05072  82  GLU A CB  
430  C  CG  . GLU A 82  ? 0.13222 0.15890 0.17125 -0.01153 -0.00005 0.05021  82  GLU A CG  
431  C  CD  . GLU A 82  ? 0.13319 0.12612 0.12365 -0.02543 -0.01183 0.02917  82  GLU A CD  
432  O  OE1 . GLU A 82  ? 0.12645 0.10174 0.08063 -0.01337 0.02075  0.00595  82  GLU A OE1 
433  O  OE2 . GLU A 82  ? 0.14355 0.13164 0.11117 -0.02876 -0.01470 0.04177  82  GLU A OE2 
434  N  N   . THR A 83  ? 0.07519 0.06331 0.08182 -0.00373 0.02539  0.01999  83  THR A N   
435  C  CA  . THR A 83  ? 0.07638 0.06498 0.11026 0.00384  0.02330  -0.00488 83  THR A CA  
436  C  C   . THR A 83  ? 0.08066 0.06199 0.06793 -0.00582 0.01284  0.00598  83  THR A C   
437  O  O   . THR A 83  ? 0.07587 0.07130 0.08448 -0.00457 0.01380  0.00210  83  THR A O   
438  C  CB  . THR A 83  ? 0.09176 0.06810 0.11417 -0.00512 0.01928  -0.01117 83  THR A CB  
439  O  OG1 . THR A 83  ? 0.09909 0.07622 0.09386 -0.00289 0.01868  0.00665  83  THR A OG1 
440  C  CG2 . THR A 83  ? 0.09896 0.08196 0.11901 -0.01588 0.01733  -0.00814 83  THR A CG2 
441  N  N   . CYS A 84  ? 0.09954 0.05468 0.06413 -0.00105 0.00337  0.00539  84  CYS A N   
442  C  CA  . CYS A 84  ? 0.11362 0.05815 0.08107 -0.00586 0.01276  0.00992  84  CYS A CA  
443  C  C   . CYS A 84  ? 0.09956 0.05679 0.08037 -0.01322 0.01073  -0.00845 84  CYS A C   
444  O  O   . CYS A 84  ? 0.12580 0.06366 0.11301 -0.00635 0.02731  -0.00623 84  CYS A O   
445  C  CB  . CYS A 84  ? 0.13395 0.08046 0.09126 -0.01152 0.02953  0.01639  84  CYS A CB  
446  S  SG  . CYS A 84  ? 0.14591 0.07717 0.12841 -0.01627 0.02570  0.00055  84  CYS A SG  
447  N  N   . SER A 85  ? 0.08151 0.06691 0.07083 -0.00915 0.00960  0.00154  85  SER A N   
448  C  CA  . SER A 85  ? 0.08125 0.08168 0.06330 -0.01678 0.00441  0.00486  85  SER A CA  
449  C  C   . SER A 85  ? 0.08733 0.06366 0.06836 -0.01578 0.00652  0.00537  85  SER A C   
450  O  O   . SER A 85  ? 0.10023 0.04958 0.08631 -0.01067 0.00867  -0.00074 85  SER A O   
451  C  CB  . SER A 85  ? 0.07949 0.11988 0.10715 -0.01217 0.00174  0.02099  85  SER A CB  
452  O  OG  . SER A 85  ? 0.09495 0.11402 0.15059 -0.00544 -0.01062 0.02197  85  SER A OG  
453  N  N   . TYR A 86  ? 0.08929 0.06889 0.07111 -0.00872 0.02200  0.00299  86  TYR A N   
454  C  CA  . TYR A 86  ? 0.08281 0.07405 0.06460 -0.02011 0.01406  -0.01043 86  TYR A CA  
455  C  C   . TYR A 86  ? 0.07188 0.07913 0.06083 -0.01445 0.01241  -0.00292 86  TYR A C   
456  O  O   . TYR A 86  ? 0.07172 0.08061 0.09076 -0.01087 0.01932  0.00467  86  TYR A O   
457  C  CB  . TYR A 86  ? 0.08887 0.08323 0.07038 -0.01938 0.00528  -0.00274 86  TYR A CB  
458  C  CG  . TYR A 86  ? 0.09260 0.07679 0.07146 -0.03137 0.01898  -0.00503 86  TYR A CG  
459  C  CD1 . TYR A 86  ? 0.09720 0.08306 0.05147 -0.03009 -0.00109 -0.01085 86  TYR A CD1 
460  C  CD2 . TYR A 86  ? 0.09904 0.08252 0.08210 -0.03188 0.02847  -0.01532 86  TYR A CD2 
461  C  CE1 . TYR A 86  ? 0.10085 0.09901 0.08159 -0.04293 0.00732  -0.01148 86  TYR A CE1 
462  C  CE2 . TYR A 86  ? 0.10089 0.09532 0.08396 -0.03972 0.00754  -0.01418 86  TYR A CE2 
463  C  CZ  . TYR A 86  ? 0.09461 0.10823 0.08053 -0.03803 0.01533  -0.01789 86  TYR A CZ  
464  O  OH  . TYR A 86  ? 0.09503 0.12444 0.13421 -0.03092 -0.00027 -0.04429 86  TYR A OH  
465  N  N   . GLY A 87  ? 0.07564 0.06823 0.06289 -0.01910 0.00873  0.00416  87  GLY A N   
466  C  CA  . GLY A 87  ? 0.07330 0.06431 0.07129 -0.02249 0.00282  0.00555  87  GLY A CA  
467  C  C   . GLY A 87  ? 0.07087 0.06305 0.06230 -0.01473 -0.00352 -0.01027 87  GLY A C   
468  O  O   . GLY A 87  ? 0.06093 0.07366 0.06473 -0.01689 0.00945  0.00268  87  GLY A O   
469  N  N   . TRP A 88  ? 0.07594 0.06933 0.05387 -0.02590 0.01401  -0.00599 88  TRP A N   
470  C  CA  . TRP A 88  ? 0.07862 0.07179 0.05459 -0.03076 0.00336  -0.00521 88  TRP A CA  
471  C  C   . TRP A 88  ? 0.08907 0.06981 0.04283 -0.03725 0.00924  0.00404  88  TRP A C   
472  O  O   . TRP A 88  ? 0.08496 0.06685 0.05555 -0.02519 0.00336  0.00243  88  TRP A O   
473  C  CB  . TRP A 88  ? 0.08168 0.08588 0.06652 -0.02699 0.02978  -0.01309 88  TRP A CB  
474  C  CG  . TRP A 88  ? 0.07617 0.09074 0.07379 -0.03222 0.02818  0.00020  88  TRP A CG  
475  C  CD1 . TRP A 88  ? 0.07367 0.08638 0.08194 -0.02619 0.02808  0.00475  88  TRP A CD1 
476  C  CD2 . TRP A 88  ? 0.08081 0.08841 0.07749 -0.03320 0.02344  -0.01503 88  TRP A CD2 
477  N  NE1 . TRP A 88  ? 0.08439 0.09000 0.08503 -0.02022 0.03747  -0.01657 88  TRP A NE1 
478  C  CE2 . TRP A 88  ? 0.09327 0.08522 0.08503 -0.02350 0.02461  -0.02235 88  TRP A CE2 
479  C  CE3 . TRP A 88  ? 0.08509 0.10174 0.07259 -0.03241 0.01232  -0.02365 88  TRP A CE3 
480  C  CZ2 . TRP A 88  ? 0.11176 0.10953 0.09555 -0.01846 0.02634  -0.02758 88  TRP A CZ2 
481  C  CZ3 . TRP A 88  ? 0.10023 0.11471 0.08801 -0.02479 0.01928  -0.02128 88  TRP A CZ3 
482  C  CH2 . TRP A 88  ? 0.11285 0.11460 0.09906 -0.01675 0.01275  -0.03249 88  TRP A CH2 
483  N  N   . VAL A 89  ? 0.09925 0.06267 0.05684 -0.02875 -0.00073 0.00913  89  VAL A N   
484  C  CA  . VAL A 89  ? 0.10730 0.07151 0.04925 -0.02641 -0.00363 0.00833  89  VAL A CA  
485  C  C   . VAL A 89  ? 0.12093 0.08221 0.04880 -0.02437 0.00210  0.00301  89  VAL A C   
486  O  O   . VAL A 89  ? 0.12365 0.09545 0.06157 -0.02059 0.01011  0.01251  89  VAL A O   
487  C  CB  . VAL A 89  ? 0.10529 0.08531 0.05183 -0.01704 0.01044  -0.00026 89  VAL A CB  
488  C  CG1 . VAL A 89  ? 0.10754 0.11242 0.07686 -0.02105 0.01262  0.00104  89  VAL A CG1 
489  C  CG2 . VAL A 89  ? 0.10610 0.07770 0.08760 -0.02332 -0.00701 -0.00401 89  VAL A CG2 
490  N  N   . GLY A 90  ? 0.14005 0.07721 0.07876 -0.02371 0.01121  0.01715  90  GLY A N   
491  C  CA  . GLY A 90  ? 0.15913 0.10685 0.08657 -0.02809 0.01221  0.02192  90  GLY A CA  
492  C  C   . GLY A 90  ? 0.17043 0.11160 0.08486 -0.03127 0.01525  0.03418  90  GLY A C   
493  O  O   . GLY A 90  ? 0.17239 0.14885 0.11607 -0.04236 0.01428  0.04609  90  GLY A O   
494  N  N   . GLU A 91  ? 0.16666 0.09822 0.08072 -0.01074 0.00754  0.01158  91  GLU A N   
495  C  CA  . GLU A 91  ? 0.17303 0.11790 0.07331 -0.00858 0.01543  0.00099  91  GLU A CA  
496  C  C   . GLU A 91  ? 0.17386 0.12249 0.07538 -0.01069 0.00675  0.00126  91  GLU A C   
497  O  O   . GLU A 91  ? 0.18796 0.14620 0.10623 -0.01067 -0.00646 -0.00086 91  GLU A O   
498  C  CB  . GLU A 91  ? 0.17573 0.13535 0.10242 -0.00110 -0.00504 -0.00938 91  GLU A CB  
499  C  CG  . GLU A 91  ? 0.19113 0.14627 0.11417 0.01486  -0.01585 -0.00727 91  GLU A CG  
500  C  CD  . GLU A 91  ? 0.19839 0.14417 0.11218 0.01888  -0.00832 0.01817  91  GLU A CD  
501  O  OE1 . GLU A 91  ? 0.18472 0.13337 0.07211 0.00755  -0.01544 0.00247  91  GLU A OE1 
502  O  OE2 . GLU A 91  ? 0.22409 0.15599 0.16352 0.02382  -0.01274 0.00714  91  GLU A OE2 
503  N  N   . GLN A 92  ? 0.16942 0.10563 0.07041 -0.00813 0.02828  0.00257  92  GLN A N   
504  C  CA  . GLN A 92  ? 0.17712 0.11376 0.06873 -0.03095 0.02991  -0.00742 92  GLN A CA  
505  C  C   . GLN A 92  ? 0.15647 0.12003 0.07057 -0.02845 0.02881  -0.01207 92  GLN A C   
506  O  O   . GLN A 92  ? 0.17181 0.14258 0.07811 -0.03727 0.02554  -0.01091 92  GLN A O   
507  C  CB  . GLN A 92  ? 0.20604 0.13398 0.08450 -0.03236 0.04733  0.01888  92  GLN A CB  
508  C  CG  . GLN A 92  ? 0.24300 0.15623 0.13567 -0.03673 0.04131  -0.00781 92  GLN A CG  
509  C  CD  . GLN A 92  ? 0.26881 0.17433 0.13327 -0.04013 0.04961  -0.00083 92  GLN A CD  
510  O  OE1 . GLN A 92  ? 0.28269 0.19136 0.14997 -0.06316 0.05272  0.02781  92  GLN A OE1 
511  N  NE2 . GLN A 92  ? 0.27385 0.18425 0.14688 -0.02863 0.05840  0.00840  92  GLN A NE2 
512  N  N   . PHE A 93  ? 0.12790 0.11301 0.04534 -0.02045 0.01302  0.00752  93  PHE A N   
513  C  CA  . PHE A 93  ? 0.11036 0.10425 0.05626 -0.02388 0.00169  0.00193  93  PHE A CA  
514  C  C   . PHE A 93  ? 0.09815 0.08962 0.06130 -0.01780 0.00286  -0.00474 93  PHE A C   
515  O  O   . PHE A 93  ? 0.08845 0.07763 0.06270 -0.02422 0.00390  -0.01040 93  PHE A O   
516  C  CB  . PHE A 93  ? 0.11311 0.10619 0.06239 -0.01298 -0.01525 -0.00580 93  PHE A CB  
517  C  CG  . PHE A 93  ? 0.11433 0.11901 0.06026 -0.01543 -0.00639 -0.00896 93  PHE A CG  
518  C  CD1 . PHE A 93  ? 0.11665 0.10856 0.06823 -0.02227 -0.00426 -0.01236 93  PHE A CD1 
519  C  CD2 . PHE A 93  ? 0.12495 0.13625 0.09624 0.00106  -0.00333 0.00188  93  PHE A CD2 
520  C  CE1 . PHE A 93  ? 0.11426 0.12267 0.07184 -0.02146 -0.00145 0.00114  93  PHE A CE1 
521  C  CE2 . PHE A 93  ? 0.13292 0.14804 0.13479 -0.00171 -0.00735 0.02454  93  PHE A CE2 
522  C  CZ  . PHE A 93  ? 0.12258 0.14294 0.11170 -0.01028 -0.00856 0.01522  93  PHE A CZ  
523  N  N   A SER A 94  ? 0.12564 0.10528 0.06270 -0.01598 0.03085  -0.00057 94  SER A N   
524  N  N   B SER A 94  ? 0.08876 0.07163 0.04694 -0.02033 0.01340  -0.00165 94  SER A N   
525  C  CA  A SER A 94  ? 0.13396 0.14487 0.08152 -0.00096 0.05882  0.00558  94  SER A CA  
526  C  CA  B SER A 94  ? 0.08715 0.08666 0.04118 -0.00740 0.01279  0.00608  94  SER A CA  
527  C  C   A SER A 94  ? 0.11334 0.10236 0.08319 -0.01421 0.03261  -0.00560 94  SER A C   
528  C  C   B SER A 94  ? 0.08252 0.07094 0.06923 -0.01847 0.01045  -0.00964 94  SER A C   
529  O  O   A SER A 94  ? 0.10322 0.11769 0.07062 -0.02761 0.02749  0.00403  94  SER A O   
530  O  O   B SER A 94  ? 0.07230 0.08499 0.06295 -0.03316 -0.00444 -0.00866 94  SER A O   
531  C  CB  A SER A 94  ? 0.16530 0.21071 0.15097 0.02498  0.09156  0.00087  94  SER A CB  
532  C  CB  B SER A 94  ? 0.09038 0.12030 0.06341 0.01933  0.01109  0.00919  94  SER A CB  
533  O  OG  A SER A 94  ? 0.24853 0.24053 0.27945 0.02876  0.09560  0.00103  94  SER A OG  
534  O  OG  B SER A 94  ? 0.09538 0.12469 0.12146 0.02218  0.00093  -0.00269 94  SER A OG  
535  N  N   . VAL A 95  ? 0.08932 0.06941 0.06347 -0.02128 0.02555  -0.00796 95  VAL A N   
536  C  CA  . VAL A 95  ? 0.07428 0.06684 0.05279 -0.01550 0.00292  0.00106  95  VAL A CA  
537  C  C   . VAL A 95  ? 0.06863 0.06474 0.05842 -0.00442 0.00425  -0.00924 95  VAL A C   
538  O  O   . VAL A 95  ? 0.06305 0.06389 0.05121 -0.01771 0.01301  -0.00872 95  VAL A O   
539  C  CB  . VAL A 95  ? 0.09786 0.06217 0.05984 -0.02184 0.00206  0.00007  95  VAL A CB  
540  C  CG1 . VAL A 95  ? 0.11995 0.07187 0.09299 -0.01400 -0.00793 0.02095  95  VAL A CG1 
541  C  CG2 . VAL A 95  ? 0.10470 0.06074 0.07358 -0.02652 0.00071  0.00040  95  VAL A CG2 
542  N  N   . ILE A 96  ? 0.07158 0.06166 0.04577 -0.01296 0.00581  0.00198  96  ILE A N   
543  C  CA  . ILE A 96  ? 0.07410 0.06940 0.04722 -0.01425 0.00264  -0.00836 96  ILE A CA  
544  C  C   . ILE A 96  ? 0.06710 0.06720 0.04483 -0.01226 -0.01037 0.00008  96  ILE A C   
545  O  O   . ILE A 96  ? 0.07173 0.08082 0.07200 -0.00640 -0.00285 -0.01649 96  ILE A O   
546  C  CB  . ILE A 96  ? 0.08728 0.06350 0.06005 -0.02076 0.00669  -0.00619 96  ILE A CB  
547  C  CG1 . ILE A 96  ? 0.09984 0.06288 0.07382 -0.01137 0.00631  0.00693  96  ILE A CG1 
548  C  CG2 . ILE A 96  ? 0.08580 0.05407 0.08040 -0.02156 0.00644  -0.01560 96  ILE A CG2 
549  C  CD1 . ILE A 96  ? 0.11829 0.07322 0.07787 -0.01121 0.00252  0.01031  96  ILE A CD1 
550  N  N   . PRO A 97  ? 0.07498 0.05772 0.05524 -0.01638 0.00066  0.00702  97  PRO A N   
551  C  CA  . PRO A 97  ? 0.07277 0.05306 0.06061 -0.01801 0.00556  -0.00344 97  PRO A CA  
552  C  C   . PRO A 97  ? 0.06553 0.05623 0.06602 -0.01855 -0.00022 -0.00290 97  PRO A C   
553  O  O   . PRO A 97  ? 0.06567 0.06609 0.08368 -0.01453 -0.00145 0.01597  97  PRO A O   
554  C  CB  . PRO A 97  ? 0.07803 0.05038 0.08381 -0.01758 -0.00033 0.00369  97  PRO A CB  
555  C  CG  . PRO A 97  ? 0.07802 0.06105 0.07705 -0.00959 0.00025  -0.00689 97  PRO A CG  
556  C  CD  . PRO A 97  ? 0.07448 0.07007 0.06502 -0.02134 -0.00290 -0.01004 97  PRO A CD  
557  N  N   . ARG A 98  ? 0.07175 0.05763 0.07330 -0.01699 0.00324  -0.00460 98  ARG A N   
558  C  CA  . ARG A 98  ? 0.07886 0.05858 0.06339 -0.01574 0.01895  0.00493  98  ARG A CA  
559  C  C   . ARG A 98  ? 0.08844 0.05115 0.07904 -0.01101 0.01002  -0.00354 98  ARG A C   
560  O  O   . ARG A 98  ? 0.09844 0.05732 0.08645 0.00087  0.02424  -0.01047 98  ARG A O   
561  C  CB  . ARG A 98  ? 0.07727 0.06497 0.07206 -0.02026 0.01562  -0.00267 98  ARG A CB  
562  C  CG  . ARG A 98  ? 0.07693 0.07350 0.07193 -0.01214 0.01913  -0.00092 98  ARG A CG  
563  C  CD  . ARG A 98  ? 0.08038 0.06725 0.06054 -0.01574 0.01941  0.00481  98  ARG A CD  
564  N  NE  . ARG A 98  ? 0.07903 0.04963 0.08988 -0.01667 0.01772  -0.00329 98  ARG A NE  
565  C  CZ  . ARG A 98  ? 0.07375 0.05896 0.08713 -0.02330 0.02606  -0.01961 98  ARG A CZ  
566  N  NH1 . ARG A 98  ? 0.09194 0.06945 0.10203 -0.02101 0.02492  -0.01143 98  ARG A NH1 
567  N  NH2 . ARG A 98  ? 0.08949 0.08413 0.10258 -0.03103 0.03923  -0.00586 98  ARG A NH2 
568  N  N   . ILE A 99  ? 0.09318 0.06656 0.07001 -0.01237 0.02351  -0.01069 99  ILE A N   
569  C  CA  . ILE A 99  ? 0.09620 0.08710 0.06027 -0.02760 0.02037  -0.02249 99  ILE A CA  
570  C  C   . ILE A 99  ? 0.09240 0.09100 0.07246 -0.03899 0.00976  -0.01782 99  ILE A C   
571  O  O   . ILE A 99  ? 0.09053 0.10221 0.12404 -0.02670 0.00824  -0.00192 99  ILE A O   
572  C  CB  . ILE A 99  ? 0.11120 0.09482 0.08792 -0.03300 0.04267  -0.03270 99  ILE A CB  
573  C  CG1 . ILE A 99  ? 0.12211 0.08567 0.12699 -0.04929 0.04001  -0.01828 99  ILE A CG1 
574  C  CG2 . ILE A 99  ? 0.11728 0.10459 0.12321 -0.01789 0.04379  -0.04201 99  ILE A CG2 
575  C  CD1 . ILE A 99  ? 0.13497 0.09377 0.13540 -0.04128 0.03486  -0.04152 99  ILE A CD1 
576  N  N   . PHE A 100 ? 0.10801 0.08346 0.07187 -0.02967 0.02067  -0.00162 100 PHE A N   
577  C  CA  . PHE A 100 ? 0.12008 0.09528 0.06284 -0.02522 0.03358  -0.00645 100 PHE A CA  
578  C  C   . PHE A 100 ? 0.10015 0.09157 0.07527 -0.02283 0.02330  -0.01659 100 PHE A C   
579  O  O   . PHE A 100 ? 0.09442 0.11042 0.09670 -0.02527 0.03486  -0.02999 100 PHE A O   
580  C  CB  . PHE A 100 ? 0.14649 0.11892 0.06610 -0.02576 0.01754  0.00626  100 PHE A CB  
581  C  CG  . PHE A 100 ? 0.15902 0.14200 0.06931 -0.03260 0.01445  -0.00323 100 PHE A CG  
582  C  CD1 . PHE A 100 ? 0.16368 0.14417 0.07840 -0.02567 0.00255  -0.01375 100 PHE A CD1 
583  C  CD2 . PHE A 100 ? 0.16935 0.16909 0.07871 -0.02905 0.04090  -0.00385 100 PHE A CD2 
584  C  CE1 . PHE A 100 ? 0.16898 0.15846 0.11467 -0.01664 0.00082  -0.01839 100 PHE A CE1 
585  C  CE2 . PHE A 100 ? 0.17462 0.18034 0.12118 -0.02722 0.03593  -0.01937 100 PHE A CE2 
586  C  CZ  . PHE A 100 ? 0.17283 0.16369 0.09531 -0.02449 0.03224  -0.03380 100 PHE A CZ  
587  N  N   A SER A 101 ? 0.10439 0.09030 0.09699 -0.02559 0.02457  -0.01457 101 SER A N   
588  N  N   B SER A 101 ? 0.09738 0.08452 0.06323 -0.02640 0.01304  -0.01062 101 SER A N   
589  C  CA  A SER A 101 ? 0.11389 0.09878 0.11858 -0.02599 0.03206  -0.01104 101 SER A CA  
590  C  CA  B SER A 101 ? 0.11236 0.08695 0.08881 -0.03065 0.02961  -0.00929 101 SER A CA  
591  C  C   A SER A 101 ? 0.11574 0.08536 0.09244 -0.02676 0.03851  -0.00138 101 SER A C   
592  C  C   B SER A 101 ? 0.12271 0.09998 0.10449 -0.03332 0.04293  0.00910  101 SER A C   
593  O  O   A SER A 101 ? 0.10362 0.07797 0.07344 -0.01976 0.03750  0.01876  101 SER A O   
594  O  O   B SER A 101 ? 0.14493 0.12907 0.11226 -0.03450 0.05375  0.00401  101 SER A O   
595  C  CB  A SER A 101 ? 0.12031 0.12284 0.15189 -0.02655 0.03112  -0.01571 101 SER A CB  
596  C  CB  B SER A 101 ? 0.11892 0.10275 0.10474 -0.03664 0.04273  -0.03597 101 SER A CB  
597  O  OG  A SER A 101 ? 0.12863 0.14576 0.20960 -0.02098 0.01573  -0.00824 101 SER A OG  
598  O  OG  B SER A 101 ? 0.12723 0.11939 0.15332 -0.04084 0.05294  -0.01945 101 SER A OG  
599  N  N   . ASN A 102 ? 0.11483 0.07357 0.08759 -0.02614 0.04094  0.00316  102 ASN A N   
600  C  CA  . ASN A 102 ? 0.12155 0.07214 0.08024 -0.01476 0.01977  0.00649  102 ASN A CA  
601  C  C   . ASN A 102 ? 0.11314 0.05294 0.10194 -0.01909 0.01890  0.00820  102 ASN A C   
602  O  O   . ASN A 102 ? 0.11872 0.05933 0.10170 -0.00908 0.02327  -0.00052 102 ASN A O   
603  C  CB  . ASN A 102 ? 0.13588 0.11545 0.11097 -0.01883 0.00424  -0.00048 102 ASN A CB  
604  C  CG  . ASN A 102 ? 0.14780 0.13636 0.14216 -0.01190 -0.00561 -0.00007 102 ASN A CG  
605  O  OD1 . ASN A 102 ? 0.13795 0.10708 0.14051 -0.00943 -0.00283 0.01690  102 ASN A OD1 
606  N  ND2 . ASN A 102 ? 0.17464 0.17740 0.16897 0.00214  -0.02161 0.00735  102 ASN A ND2 
607  N  N   . PRO A 103 ? 0.12210 0.04774 0.11479 -0.01518 0.01466  -0.00320 103 PRO A N   
608  C  CA  . PRO A 103 ? 0.12442 0.04210 0.14178 -0.01996 0.01263  0.00263  103 PRO A CA  
609  C  C   . PRO A 103 ? 0.11514 0.05187 0.12714 -0.01068 0.01901  -0.02622 103 PRO A C   
610  O  O   . PRO A 103 ? 0.11908 0.09421 0.14914 -0.02292 0.03011  -0.03456 103 PRO A O   
611  C  CB  . PRO A 103 ? 0.14207 0.05554 0.17742 -0.02318 0.01206  0.02055  103 PRO A CB  
612  C  CG  . PRO A 103 ? 0.16201 0.09856 0.22004 -0.01753 0.02088  0.03234  103 PRO A CG  
613  C  CD  . PRO A 103 ? 0.14119 0.07836 0.15279 -0.02366 0.02097  0.04700  103 PRO A CD  
614  N  N   . ARG A 104 ? 0.11012 0.04761 0.14377 -0.00883 0.02216  0.00829  104 ARG A N   
615  C  CA  . ARG A 104 ? 0.12166 0.06066 0.13272 0.00187  0.01992  0.01064  104 ARG A CA  
616  C  C   . ARG A 104 ? 0.11727 0.05311 0.11629 -0.01228 0.02466  0.01383  104 ARG A C   
617  O  O   . ARG A 104 ? 0.11214 0.07094 0.14976 -0.01824 0.03906  -0.01483 104 ARG A O   
618  C  CB  . ARG A 104 ? 0.16029 0.08685 0.22711 0.00420  0.03447  0.05851  104 ARG A CB  
619  C  CG  . ARG A 104 ? 0.22250 0.13750 0.31679 0.00275  0.02501  0.07586  104 ARG A CG  
620  C  CD  . ARG A 104 ? 0.28000 0.18609 0.37001 -0.00970 0.03640  0.09780  104 ARG A CD  
621  N  NE  . ARG A 104 ? 0.32504 0.21108 0.42213 -0.02423 0.03796  0.09192  104 ARG A NE  
622  C  CZ  . ARG A 104 ? 0.38203 0.24584 0.45541 -0.03107 0.04427  0.08977  104 ARG A CZ  
623  N  NH1 . ARG A 104 ? 0.40891 0.24655 0.45959 -0.04200 0.05821  0.09323  104 ARG A NH1 
624  N  NH2 . ARG A 104 ? 0.38994 0.25365 0.44087 -0.03214 0.05286  0.10062  104 ARG A NH2 
625  N  N   . CYS A 105 ? 0.11577 0.04530 0.12612 -0.01628 0.03027  0.01110  105 CYS A N   
626  C  CA  . CYS A 105 ? 0.13165 0.05466 0.11599 -0.01624 0.03706  0.00369  105 CYS A CA  
627  C  C   . CYS A 105 ? 0.12379 0.07023 0.10704 0.00354  0.04352  0.00635  105 CYS A C   
628  O  O   . CYS A 105 ? 0.13953 0.10350 0.13764 0.03522  0.06101  0.01743  105 CYS A O   
629  C  CB  . CYS A 105 ? 0.14924 0.06628 0.13140 -0.01517 0.03063  -0.00206 105 CYS A CB  
630  S  SG  . CYS A 105 ? 0.15418 0.08794 0.12048 -0.02647 0.02472  0.00731  105 CYS A SG  
631  N  N   . GLY A 106 ? 0.11258 0.07500 0.11143 -0.01518 0.02855  -0.00012 106 GLY A N   
632  C  CA  . GLY A 106 ? 0.10167 0.08177 0.11025 -0.02089 0.02453  0.00112  106 GLY A CA  
633  C  C   . GLY A 106 ? 0.10753 0.07488 0.10470 -0.01334 0.02216  -0.00462 106 GLY A C   
634  O  O   . GLY A 106 ? 0.10239 0.08308 0.12776 -0.01625 0.02004  -0.00807 106 GLY A O   
635  N  N   . LYS A 107 ? 0.12525 0.08768 0.11666 -0.02150 0.02537  -0.02481 107 LYS A N   
636  C  CA  . LYS A 107 ? 0.16006 0.11185 0.11038 -0.02890 0.02471  -0.03263 107 LYS A CA  
637  C  C   . LYS A 107 ? 0.12275 0.08052 0.11764 -0.02044 0.00378  -0.01847 107 LYS A C   
638  O  O   . LYS A 107 ? 0.11245 0.10065 0.12063 -0.01757 -0.01215 -0.01425 107 LYS A O   
639  C  CB  . LYS A 107 ? 0.24417 0.19187 0.15747 -0.04159 0.05492  -0.05044 107 LYS A CB  
640  C  CG  . LYS A 107 ? 0.30473 0.26315 0.18968 -0.04701 0.09554  -0.09934 107 LYS A CG  
641  C  CD  . LYS A 107 ? 0.39022 0.32930 0.31340 -0.05242 0.11762  -0.09948 107 LYS A CD  
642  C  CE  . LYS A 107 ? 0.48883 0.39243 0.40154 -0.05110 0.12309  -0.10232 107 LYS A CE  
643  N  NZ  . LYS A 107 ? 0.48532 0.41500 0.43723 -0.05121 0.14176  -0.09211 107 LYS A NZ  
644  N  N   . ASN A 108 ? 0.10244 0.05077 0.11296 -0.02595 0.00959  -0.01507 108 ASN A N   
645  C  CA  . ASN A 108 ? 0.09540 0.06306 0.11474 -0.03528 0.01048  -0.00847 108 ASN A CA  
646  C  C   . ASN A 108 ? 0.09021 0.07650 0.10722 -0.02699 0.01169  -0.01359 108 ASN A C   
647  O  O   . ASN A 108 ? 0.08770 0.10603 0.14224 -0.02744 0.01879  -0.01135 108 ASN A O   
648  C  CB  . ASN A 108 ? 0.09907 0.08377 0.11381 -0.04978 0.02701  -0.01053 108 ASN A CB  
649  C  CG  . ASN A 108 ? 0.11172 0.09739 0.13362 -0.05583 0.02859  -0.03157 108 ASN A CG  
650  O  OD1 . ASN A 108 ? 0.13413 0.10803 0.12965 -0.05601 0.03215  -0.02843 108 ASN A OD1 
651  N  ND2 . ASN A 108 ? 0.11307 0.10702 0.17934 -0.05045 0.05176  -0.04029 108 ASN A ND2 
652  N  N   . GLY A 109 ? 0.08474 0.07084 0.09894 -0.02212 0.00038  -0.00490 109 GLY A N   
653  C  CA  . GLY A 109 ? 0.08614 0.06734 0.12981 -0.02017 0.01825  -0.00882 109 GLY A CA  
654  C  C   . GLY A 109 ? 0.08275 0.06762 0.09210 -0.01790 0.01119  -0.00001 109 GLY A C   
655  O  O   . GLY A 109 ? 0.09080 0.07581 0.09431 -0.01963 0.00321  -0.00265 109 GLY A O   
656  N  N   . LYS A 110 ? 0.08989 0.07822 0.08871 -0.00735 0.00798  -0.00700 110 LYS A N   
657  C  CA  . LYS A 110 ? 0.09421 0.08591 0.08953 -0.00932 0.01176  -0.00379 110 LYS A CA  
658  C  C   . LYS A 110 ? 0.08484 0.09087 0.09332 -0.00436 -0.01204 -0.01772 110 LYS A C   
659  O  O   . LYS A 110 ? 0.11000 0.09769 0.14303 -0.01249 -0.02610 0.00859  110 LYS A O   
660  C  CB  . LYS A 110 ? 0.12570 0.10144 0.08758 -0.01826 0.03736  -0.00187 110 LYS A CB  
661  C  CG  . LYS A 110 ? 0.15308 0.13234 0.10692 -0.02164 0.04867  -0.00868 110 LYS A CG  
662  C  CD  . LYS A 110 ? 0.17736 0.17202 0.17155 -0.02360 0.06733  -0.00071 110 LYS A CD  
663  C  CE  . LYS A 110 ? 0.18906 0.20976 0.26216 -0.01909 0.09648  -0.00501 110 LYS A CE  
664  N  NZ  . LYS A 110 ? 0.18857 0.24127 0.30283 -0.01861 0.11090  -0.01858 110 LYS A NZ  
665  N  N   . GLY A 111 ? 0.08209 0.07861 0.09386 -0.00808 -0.00212 0.00015  111 GLY A N   
666  C  CA  . GLY A 111 ? 0.08325 0.09250 0.11795 -0.00953 0.00015  0.00851  111 GLY A CA  
667  C  C   . GLY A 111 ? 0.09019 0.11169 0.09281 0.01305  -0.00669 0.01201  111 GLY A C   
668  O  O   . GLY A 111 ? 0.10663 0.19685 0.12761 0.03186  -0.00388 0.07344  111 GLY A O   
669  N  N   . VAL A 112 ? 0.08920 0.09128 0.09852 0.00512  0.00513  0.00522  112 VAL A N   
670  C  CA  . VAL A 112 ? 0.09958 0.07919 0.10279 -0.00990 -0.00178 -0.00959 112 VAL A CA  
671  C  C   . VAL A 112 ? 0.10080 0.08867 0.09952 -0.00836 -0.01018 0.00307  112 VAL A C   
672  O  O   . VAL A 112 ? 0.12114 0.10255 0.13576 0.00384  -0.03728 -0.00257 112 VAL A O   
673  C  CB  . VAL A 112 ? 0.11821 0.07390 0.10468 -0.02123 0.02025  -0.00445 112 VAL A CB  
674  C  CG1 . VAL A 112 ? 0.12369 0.10433 0.14078 -0.01422 0.04847  0.00453  112 VAL A CG1 
675  C  CG2 . VAL A 112 ? 0.12984 0.08334 0.14082 -0.01286 0.01398  -0.01177 112 VAL A CG2 
676  N  N   . LEU A 113 ? 0.08768 0.08670 0.07654 -0.01609 0.00995  -0.01601 113 LEU A N   
677  C  CA  . LEU A 113 ? 0.08898 0.10209 0.07519 -0.03218 0.00752  0.00016  113 LEU A CA  
678  C  C   . LEU A 113 ? 0.07817 0.10789 0.06633 -0.02880 -0.00752 -0.00856 113 LEU A C   
679  O  O   . LEU A 113 ? 0.07231 0.11385 0.07014 -0.01789 -0.00222 0.00158  113 LEU A O   
680  C  CB  . LEU A 113 ? 0.12570 0.14778 0.08120 -0.03822 0.03711  0.00001  113 LEU A CB  
681  C  CG  . LEU A 113 ? 0.16543 0.22227 0.15471 -0.04515 0.05137  0.00473  113 LEU A CG  
682  C  CD1 . LEU A 113 ? 0.20793 0.27714 0.27860 -0.02980 0.07609  0.00997  113 LEU A CD1 
683  C  CD2 . LEU A 113 ? 0.18759 0.23339 0.23568 -0.06311 0.04640  -0.01418 113 LEU A CD2 
684  N  N   . ILE A 114 ? 0.08387 0.11992 0.07531 -0.02521 -0.00318 -0.01827 114 ILE A N   
685  C  CA  . ILE A 114 ? 0.09749 0.13415 0.06098 -0.02844 0.00697  -0.01119 114 ILE A CA  
686  C  C   . ILE A 114 ? 0.08988 0.14716 0.07687 -0.03859 0.00604  -0.01955 114 ILE A C   
687  O  O   . ILE A 114 ? 0.08166 0.15284 0.12359 -0.04033 0.01777  -0.04022 114 ILE A O   
688  C  CB  . ILE A 114 ? 0.12551 0.14658 0.09176 -0.01379 -0.00139 -0.02614 114 ILE A CB  
689  C  CG1 . ILE A 114 ? 0.14056 0.16798 0.16232 0.00984  -0.01221 -0.00280 114 ILE A CG1 
690  C  CG2 . ILE A 114 ? 0.13347 0.15889 0.11485 -0.01958 -0.00169 -0.00994 114 ILE A CG2 
691  C  CD1 . ILE A 114 ? 0.14459 0.18925 0.20516 0.02258  -0.02303 -0.00288 114 ILE A CD1 
692  N  N   . TRP A 115 ? 0.09515 0.14287 0.06675 -0.04510 -0.00814 -0.02454 115 TRP A N   
693  C  CA  . TRP A 115 ? 0.10788 0.13132 0.06438 -0.03203 0.01099  -0.03963 115 TRP A CA  
694  C  C   . TRP A 115 ? 0.11085 0.13974 0.08431 -0.03611 0.00711  -0.03369 115 TRP A C   
695  O  O   . TRP A 115 ? 0.10430 0.14041 0.09759 -0.03999 0.02075  -0.04923 115 TRP A O   
696  C  CB  . TRP A 115 ? 0.12134 0.13007 0.07479 -0.02431 0.01026  -0.03839 115 TRP A CB  
697  C  CG  . TRP A 115 ? 0.14082 0.13024 0.09145 -0.03024 0.01902  -0.03369 115 TRP A CG  
698  C  CD1 . TRP A 115 ? 0.16173 0.13292 0.12047 -0.02114 0.04152  -0.04208 115 TRP A CD1 
699  C  CD2 . TRP A 115 ? 0.13900 0.12420 0.11781 -0.04296 0.01702  -0.04307 115 TRP A CD2 
700  N  NE1 . TRP A 115 ? 0.17226 0.13598 0.15090 -0.01559 0.03328  -0.03399 115 TRP A NE1 
701  C  CE2 . TRP A 115 ? 0.15444 0.12989 0.17860 -0.02808 0.02970  -0.02575 115 TRP A CE2 
702  C  CE3 . TRP A 115 ? 0.13904 0.12491 0.13329 -0.05670 0.00999  -0.01512 115 TRP A CE3 
703  C  CZ2 . TRP A 115 ? 0.15279 0.13148 0.19475 -0.02975 0.04440  -0.00540 115 TRP A CZ2 
704  C  CZ3 . TRP A 115 ? 0.14212 0.11488 0.19009 -0.04969 0.00227  -0.00529 115 TRP A CZ3 
705  C  CH2 . TRP A 115 ? 0.14683 0.12793 0.19538 -0.04005 0.01859  0.00071  115 TRP A CH2 
706  N  N   . ASN A 116 ? 0.12444 0.15239 0.07934 -0.04288 0.00887  -0.03072 116 ASN A N   
707  C  CA  . ASN A 116 ? 0.15003 0.17554 0.08869 -0.04303 0.01654  -0.02746 116 ASN A CA  
708  C  C   . ASN A 116 ? 0.15621 0.16908 0.07651 -0.04925 0.01585  -0.04311 116 ASN A C   
709  O  O   . ASN A 116 ? 0.16605 0.19207 0.20140 -0.05180 0.03335  -0.07541 116 ASN A O   
710  C  CB  . ASN A 116 ? 0.18535 0.21494 0.12742 -0.02694 0.00046  -0.01359 116 ASN A CB  
711  C  CG  . ASN A 116 ? 0.21045 0.25917 0.17882 -0.01743 0.00348  -0.03288 116 ASN A CG  
712  O  OD1 . ASN A 116 ? 0.22854 0.27821 0.25243 -0.01487 -0.02122 -0.04432 116 ASN A OD1 
713  N  ND2 . ASN A 116 ? 0.21877 0.27914 0.18727 -0.00916 0.02220  -0.02454 116 ASN A ND2 
714  N  N   . ALA A 117 ? 0.15995 0.15715 0.12691 -0.04144 -0.02331 -0.05898 117 ALA A N   
715  C  CA  . ALA A 117 ? 0.16465 0.17776 0.14439 -0.03665 -0.00827 -0.03266 117 ALA A CA  
716  C  C   . ALA A 117 ? 0.16160 0.16680 0.11957 -0.02666 -0.01656 -0.05421 117 ALA A C   
717  O  O   . ALA A 117 ? 0.16663 0.16384 0.13250 -0.02969 -0.01488 -0.05121 117 ALA A O   
718  C  CB  . ALA A 117 ? 0.17339 0.20619 0.18052 -0.04376 0.00590  0.01193  117 ALA A CB  
719  N  N   . PRO A 118 ? 0.16568 0.16292 0.10788 -0.01459 -0.00531 -0.05251 118 PRO A N   
720  C  CA  . PRO A 118 ? 0.16431 0.15665 0.09616 -0.02271 -0.00921 -0.04867 118 PRO A CA  
721  C  C   . PRO A 118 ? 0.15073 0.15807 0.08552 -0.02226 0.01137  -0.06072 118 PRO A C   
722  O  O   . PRO A 118 ? 0.13648 0.16943 0.07695 -0.02029 0.01517  -0.04543 118 PRO A O   
723  C  CB  . PRO A 118 ? 0.17499 0.15800 0.14103 -0.01628 -0.01132 -0.06671 118 PRO A CB  
724  C  CG  . PRO A 118 ? 0.17836 0.16113 0.18683 -0.00578 -0.00673 -0.04123 118 PRO A CG  
725  C  CD  . PRO A 118 ? 0.17276 0.15578 0.17253 -0.00930 0.00507  -0.03847 118 PRO A CD  
726  N  N   . SER A 119 ? 0.14928 0.15726 0.10812 -0.03194 0.01078  -0.06272 119 SER A N   
727  C  CA  . SER A 119 ? 0.15362 0.16807 0.10301 -0.02834 0.00591  -0.04525 119 SER A CA  
728  C  C   . SER A 119 ? 0.14777 0.17551 0.07409 -0.02666 0.00982  -0.04603 119 SER A C   
729  O  O   . SER A 119 ? 0.13276 0.18104 0.10131 -0.02309 0.01637  -0.05516 119 SER A O   
730  C  CB  . SER A 119 ? 0.16952 0.17539 0.14320 -0.03260 0.01312  -0.04290 119 SER A CB  
731  O  OG  . SER A 119 ? 0.18054 0.17736 0.15939 -0.03012 0.02006  -0.03061 119 SER A OG  
732  N  N   . SER A 120 ? 0.15477 0.18314 0.09972 -0.01658 0.01360  -0.07070 120 SER A N   
733  C  CA  . SER A 120 ? 0.16482 0.19892 0.12345 -0.01045 0.02253  -0.07983 120 SER A CA  
734  C  C   . SER A 120 ? 0.16100 0.19311 0.12793 -0.01287 0.01892  -0.07892 120 SER A C   
735  O  O   . SER A 120 ? 0.16910 0.19257 0.15706 -0.00481 0.01023  -0.06254 120 SER A O   
736  C  CB  . SER A 120 ? 0.18536 0.21614 0.14013 -0.00271 0.02279  -0.08798 120 SER A CB  
737  O  OG  . SER A 120 ? 0.19859 0.21997 0.15446 0.00549  0.01204  -0.10034 120 SER A OG  
738  N  N   . GLN A 121 ? 0.15285 0.17492 0.11313 -0.01260 0.01597  -0.05869 121 GLN A N   
739  C  CA  . GLN A 121 ? 0.14839 0.17353 0.09627 -0.01754 -0.00728 -0.05135 121 GLN A CA  
740  C  C   . GLN A 121 ? 0.14029 0.15700 0.07665 -0.00692 0.00650  -0.04942 121 GLN A C   
741  O  O   . GLN A 121 ? 0.14157 0.14478 0.11110 -0.01098 0.00114  -0.04471 121 GLN A O   
742  C  CB  . GLN A 121 ? 0.16394 0.19254 0.13451 -0.03240 -0.00650 -0.04656 121 GLN A CB  
743  C  CG  . GLN A 121 ? 0.18722 0.22314 0.20280 -0.03652 -0.00056 -0.04122 121 GLN A CG  
744  C  CD  . GLN A 121 ? 0.20446 0.24037 0.24575 -0.04395 -0.00440 -0.04064 121 GLN A CD  
745  O  OE1 . GLN A 121 ? 0.21012 0.24273 0.31724 -0.04611 -0.01785 -0.03527 121 GLN A OE1 
746  N  NE2 . GLN A 121 ? 0.21575 0.25441 0.25013 -0.05274 -0.00686 -0.04357 121 GLN A NE2 
747  N  N   . LYS A 122 ? 0.14087 0.14471 0.09576 0.00114  0.00816  -0.05726 122 LYS A N   
748  C  CA  . LYS A 122 ? 0.13927 0.14243 0.12099 0.01572  0.00264  -0.04635 122 LYS A CA  
749  C  C   . LYS A 122 ? 0.12931 0.10000 0.12300 0.00445  0.01505  -0.05313 122 LYS A C   
750  O  O   . LYS A 122 ? 0.15423 0.08985 0.15503 -0.00701 0.03054  -0.05577 122 LYS A O   
751  C  CB  . LYS A 122 ? 0.15923 0.18231 0.16239 0.03162  0.02206  -0.04727 122 LYS A CB  
752  C  CG  . LYS A 122 ? 0.17488 0.21272 0.20587 0.03392  0.03643  -0.06836 122 LYS A CG  
753  C  CD  . LYS A 122 ? 0.19442 0.22953 0.25368 0.03415  0.04859  -0.09658 122 LYS A CD  
754  C  CE  . LYS A 122 ? 0.21239 0.25315 0.32837 0.01670  0.05143  -0.08308 122 LYS A CE  
755  N  NZ  . LYS A 122 ? 0.22339 0.26772 0.37577 0.00767  0.04445  -0.09353 122 LYS A NZ  
756  N  N   . PHE A 123 ? 0.10262 0.10364 0.10385 0.00864  0.00656  -0.03209 123 PHE A N   
757  C  CA  . PHE A 123 ? 0.09452 0.10956 0.08026 0.00404  0.01128  -0.03181 123 PHE A CA  
758  C  C   . PHE A 123 ? 0.08587 0.11031 0.06669 0.00986  0.00171  -0.01049 123 PHE A C   
759  O  O   . PHE A 123 ? 0.08886 0.10508 0.09752 0.00965  0.00516  -0.02924 123 PHE A O   
760  C  CB  . PHE A 123 ? 0.09511 0.11320 0.08724 -0.00803 0.00826  -0.03529 123 PHE A CB  
761  C  CG  . PHE A 123 ? 0.09267 0.11000 0.10025 -0.02211 0.01222  -0.03639 123 PHE A CG  
762  C  CD1 . PHE A 123 ? 0.09409 0.12566 0.11938 -0.02200 0.03002  -0.04078 123 PHE A CD1 
763  C  CD2 . PHE A 123 ? 0.10633 0.12050 0.11937 -0.03138 -0.01229 -0.00954 123 PHE A CD2 
764  C  CE1 . PHE A 123 ? 0.10869 0.12748 0.16350 -0.03138 0.02418  -0.03167 123 PHE A CE1 
765  C  CE2 . PHE A 123 ? 0.12151 0.12790 0.15151 -0.02445 -0.00932 -0.03540 123 PHE A CE2 
766  C  CZ  . PHE A 123 ? 0.12533 0.13527 0.15135 -0.02505 0.00251  -0.04666 123 PHE A CZ  
767  N  N   . LYS A 124 ? 0.08757 0.09108 0.08192 0.00194  0.00334  -0.01481 124 LYS A N   
768  C  CA  . LYS A 124 ? 0.08528 0.08711 0.05908 -0.00494 0.00451  -0.01550 124 LYS A CA  
769  C  C   . LYS A 124 ? 0.07832 0.08027 0.06740 -0.00031 0.00749  -0.02035 124 LYS A C   
770  O  O   . LYS A 124 ? 0.08483 0.08085 0.06700 -0.00607 0.00499  -0.01743 124 LYS A O   
771  C  CB  . LYS A 124 ? 0.10144 0.09231 0.07935 -0.01158 0.00216  0.00875  124 LYS A CB  
772  C  CG  . LYS A 124 ? 0.12141 0.09616 0.09992 0.00249  0.00721  0.02540  124 LYS A CG  
773  C  CD  . LYS A 124 ? 0.12730 0.10702 0.12854 0.01137  -0.00599 0.02454  124 LYS A CD  
774  C  CE  . LYS A 124 ? 0.14443 0.14012 0.15294 0.02207  -0.00934 0.03544  124 LYS A CE  
775  N  NZ  . LYS A 124 ? 0.16479 0.17096 0.20360 0.01592  0.00584  0.05943  124 LYS A NZ  
776  N  N   . ALA A 125 ? 0.08167 0.07328 0.08187 0.01282  0.00334  -0.00536 125 ALA A N   
777  C  CA  . ALA A 125 ? 0.08381 0.06998 0.07278 0.00214  0.00399  -0.01193 125 ALA A CA  
778  C  C   . ALA A 125 ? 0.06471 0.06789 0.06361 0.00441  -0.00661 -0.00660 125 ALA A C   
779  O  O   . ALA A 125 ? 0.06983 0.08758 0.07954 0.01499  -0.00236 -0.01075 125 ALA A O   
780  C  CB  . ALA A 125 ? 0.08494 0.10173 0.08008 0.00298  0.00232  -0.00268 125 ALA A CB  
781  N  N   . TYR A 126 ? 0.05482 0.06713 0.06822 -0.00299 0.00445  0.00051  126 TYR A N   
782  C  CA  . TYR A 126 ? 0.05983 0.05128 0.07421 -0.00347 0.01434  -0.00318 126 TYR A CA  
783  C  C   . TYR A 126 ? 0.06822 0.05819 0.07117 -0.01604 0.01992  -0.00109 126 TYR A C   
784  O  O   . TYR A 126 ? 0.07941 0.06468 0.08033 -0.01912 0.01118  0.00743  126 TYR A O   
785  C  CB  . TYR A 126 ? 0.06063 0.06337 0.09169 -0.01026 0.00754  -0.00473 126 TYR A CB  
786  C  CG  . TYR A 126 ? 0.05369 0.04735 0.06662 -0.01401 0.01555  0.01456  126 TYR A CG  
787  C  CD1 . TYR A 126 ? 0.06479 0.05553 0.09408 -0.00790 0.02397  0.01343  126 TYR A CD1 
788  C  CD2 . TYR A 126 ? 0.05667 0.05827 0.10279 -0.00374 0.00380  -0.00256 126 TYR A CD2 
789  C  CE1 . TYR A 126 ? 0.07261 0.06305 0.10041 -0.00085 0.02070  0.00188  126 TYR A CE1 
790  C  CE2 . TYR A 126 ? 0.05893 0.05739 0.09375 -0.00866 0.01541  0.00069  126 TYR A CE2 
791  C  CZ  . TYR A 126 ? 0.06169 0.05658 0.08418 -0.00464 0.02129  0.00214  126 TYR A CZ  
792  O  OH  . TYR A 126 ? 0.08128 0.05848 0.12107 -0.01090 0.03786  0.00741  126 TYR A OH  
793  N  N   . CYS A 127 ? 0.06782 0.05266 0.07648 -0.01219 0.01660  -0.00080 127 CYS A N   
794  C  CA  . CYS A 127 ? 0.07206 0.07122 0.08267 -0.00567 0.01030  -0.00389 127 CYS A CA  
795  C  C   . CYS A 127 ? 0.08442 0.07832 0.05882 -0.00509 0.01886  -0.00534 127 CYS A C   
796  O  O   . CYS A 127 ? 0.10820 0.08186 0.09270 0.00836  0.03240  0.00400  127 CYS A O   
797  C  CB  . CYS A 127 ? 0.07191 0.09945 0.12115 -0.00187 0.00898  -0.00907 127 CYS A CB  
798  S  SG  . CYS A 127 ? 0.07868 0.12414 0.10286 -0.00522 0.02333  -0.00131 127 CYS A SG  
799  N  N   . HIS A 128 ? 0.08389 0.06150 0.07693 -0.01227 0.01826  -0.01110 128 HIS A N   
800  C  CA  . HIS A 128 ? 0.08201 0.06294 0.06215 -0.02022 0.01399  -0.00598 128 HIS A CA  
801  C  C   . HIS A 128 ? 0.08501 0.06133 0.05850 -0.01027 0.01650  0.00343  128 HIS A C   
802  O  O   . HIS A 128 ? 0.09659 0.06321 0.07306 -0.02378 0.01841  0.00016  128 HIS A O   
803  C  CB  . HIS A 128 ? 0.08524 0.07678 0.05624 -0.01262 -0.00338 -0.00481 128 HIS A CB  
804  C  CG  . HIS A 128 ? 0.08539 0.08051 0.12393 -0.01047 -0.00042 -0.00994 128 HIS A CG  
805  N  ND1 . HIS A 128 ? 0.09129 0.08730 0.15676 -0.00454 -0.00857 -0.00520 128 HIS A ND1 
806  C  CD2 . HIS A 128 ? 0.08950 0.09225 0.13129 0.00121  0.00130  -0.02741 128 HIS A CD2 
807  C  CE1 . HIS A 128 ? 0.09737 0.09451 0.18903 0.00035  -0.01695 -0.02205 128 HIS A CE1 
808  N  NE2 . HIS A 128 ? 0.09848 0.11205 0.16242 0.00742  -0.00230 -0.05425 128 HIS A NE2 
809  N  N   . ASN A 129 ? 0.07742 0.06284 0.07096 -0.00678 0.01510  -0.00882 129 ASN A N   
810  C  CA  . ASN A 129 ? 0.07640 0.05570 0.07944 -0.00452 0.01049  -0.00869 129 ASN A CA  
811  C  C   . ASN A 129 ? 0.08555 0.06860 0.06463 -0.00341 0.00522  0.00042  129 ASN A C   
812  O  O   . ASN A 129 ? 0.08526 0.06008 0.09172 -0.00265 0.00375  -0.00882 129 ASN A O   
813  C  CB  . ASN A 129 ? 0.07434 0.06569 0.07920 -0.01136 0.00982  -0.00995 129 ASN A CB  
814  C  CG  . ASN A 129 ? 0.06258 0.07781 0.07202 -0.01285 0.00546  -0.00975 129 ASN A CG  
815  O  OD1 . ASN A 129 ? 0.07830 0.08229 0.10847 -0.02679 -0.00416 0.00105  129 ASN A OD1 
816  N  ND2 . ASN A 129 ? 0.05561 0.10945 0.06585 -0.00657 -0.00310 -0.01418 129 ASN A ND2 
817  N  N   . SER A 130 ? 0.10855 0.06478 0.07069 -0.00243 0.00103  0.01125  130 SER A N   
818  C  CA  . SER A 130 ? 0.13712 0.07201 0.12831 0.00329  -0.01930 0.02874  130 SER A CA  
819  C  C   . SER A 130 ? 0.14143 0.06105 0.13468 -0.00101 -0.01271 0.01508  130 SER A C   
820  O  O   . SER A 130 ? 0.15107 0.08201 0.18642 0.00798  -0.03318 -0.00099 130 SER A O   
821  C  CB  . SER A 130 ? 0.16656 0.11423 0.14233 0.01012  -0.01383 0.03891  130 SER A CB  
822  O  OG  . SER A 130 ? 0.18406 0.13219 0.17240 0.00358  0.02051  0.03459  130 SER A OG  
823  N  N   . SER A 131 ? 0.12970 0.06543 0.09524 -0.01009 0.00082  0.01403  131 SER A N   
824  C  CA  . SER A 131 ? 0.12380 0.09499 0.08874 -0.01817 -0.00130 0.00010  131 SER A CA  
825  C  C   . SER A 131 ? 0.10768 0.07521 0.10512 -0.00937 0.00223  -0.01601 131 SER A C   
826  O  O   . SER A 131 ? 0.12365 0.08439 0.12491 -0.02285 0.00638  -0.01995 131 SER A O   
827  C  CB  . SER A 131 ? 0.13437 0.12559 0.11761 -0.03493 0.00791  -0.01377 131 SER A CB  
828  O  OG  . SER A 131 ? 0.14813 0.15445 0.18083 -0.04134 0.03529  -0.01741 131 SER A OG  
829  N  N   . ASP A 132 ? 0.08511 0.06748 0.11487 -0.00687 0.00726  -0.00413 132 ASP A N   
830  C  CA  . ASP A 132 ? 0.08497 0.06235 0.10889 -0.00048 -0.00429 0.00229  132 ASP A CA  
831  C  C   . ASP A 132 ? 0.09138 0.06138 0.10386 0.01699  -0.00406 0.00073  132 ASP A C   
832  O  O   . ASP A 132 ? 0.10471 0.10680 0.11595 0.02461  -0.00353 -0.00611 132 ASP A O   
833  C  CB  . ASP A 132 ? 0.08230 0.06844 0.11930 -0.01046 -0.00514 0.00300  132 ASP A CB  
834  C  CG  . ASP A 132 ? 0.07974 0.07231 0.08923 -0.00388 -0.00858 -0.00135 132 ASP A CG  
835  O  OD1 . ASP A 132 ? 0.08241 0.07831 0.09388 0.00256  -0.01356 -0.00809 132 ASP A OD1 
836  O  OD2 . ASP A 132 ? 0.08378 0.06751 0.08683 -0.00213 0.00214  -0.00872 132 ASP A OD2 
837  N  N   . THR A 133 ? 0.11254 0.06997 0.08523 0.01104  0.01550  -0.00554 133 THR A N   
838  C  CA  . THR A 133 ? 0.12033 0.06866 0.13052 0.00637  0.01537  -0.01543 133 THR A CA  
839  C  C   . THR A 133 ? 0.10106 0.06607 0.13849 0.01648  0.01378  -0.00612 133 THR A C   
840  O  O   . THR A 133 ? 0.11195 0.07052 0.18847 0.03359  0.03423  0.01096  133 THR A O   
841  C  CB  . THR A 133 ? 0.14544 0.09119 0.18440 -0.01422 0.01632  -0.00745 133 THR A CB  
842  O  OG1 . THR A 133 ? 0.15046 0.10912 0.18525 -0.01132 0.01303  -0.02628 133 THR A OG1 
843  C  CG2 . THR A 133 ? 0.16280 0.10048 0.21760 -0.02361 0.04168  0.01686  133 THR A CG2 
844  N  N   . TRP A 134 ? 0.07488 0.06227 0.10216 0.01075  0.00553  -0.00517 134 TRP A N   
845  C  CA  . TRP A 134 ? 0.07252 0.06139 0.08889 0.00454  -0.00483 -0.00089 134 TRP A CA  
846  C  C   . TRP A 134 ? 0.07215 0.05969 0.09236 0.01674  0.00882  -0.01048 134 TRP A C   
847  O  O   . TRP A 134 ? 0.07849 0.06860 0.08632 0.01608  0.00906  -0.01114 134 TRP A O   
848  C  CB  . TRP A 134 ? 0.07056 0.07211 0.07528 0.00635  -0.01030 -0.01628 134 TRP A CB  
849  C  CG  . TRP A 134 ? 0.08750 0.08129 0.10309 0.01333  0.00670  -0.01684 134 TRP A CG  
850  C  CD1 . TRP A 134 ? 0.10477 0.08720 0.11327 0.00269  -0.00784 -0.02135 134 TRP A CD1 
851  C  CD2 . TRP A 134 ? 0.09858 0.09505 0.09463 0.00104  -0.00707 -0.01353 134 TRP A CD2 
852  N  NE1 . TRP A 134 ? 0.11420 0.10380 0.11267 -0.00044 -0.00061 -0.02486 134 TRP A NE1 
853  C  CE2 . TRP A 134 ? 0.11337 0.11183 0.11912 -0.00803 -0.00926 -0.01069 134 TRP A CE2 
854  C  CE3 . TRP A 134 ? 0.10414 0.11632 0.07964 0.00585  -0.01473 -0.00173 134 TRP A CE3 
855  C  CZ2 . TRP A 134 ? 0.12563 0.12866 0.11716 -0.02524 -0.01250 -0.00766 134 TRP A CZ2 
856  C  CZ3 . TRP A 134 ? 0.11854 0.14886 0.09446 -0.00985 -0.01989 0.00241  134 TRP A CZ3 
857  C  CH2 . TRP A 134 ? 0.12938 0.15220 0.09413 -0.01828 -0.01412 0.00132  134 TRP A CH2 
858  N  N   . VAL A 135 ? 0.06911 0.06388 0.07425 0.00868  0.00819  -0.00506 135 VAL A N   
859  C  CA  . VAL A 135 ? 0.06413 0.06680 0.09633 0.01680  0.01385  -0.00423 135 VAL A CA  
860  C  C   . VAL A 135 ? 0.06797 0.08026 0.07084 0.01450  0.00568  -0.00232 135 VAL A C   
861  O  O   . VAL A 135 ? 0.07581 0.07224 0.07146 0.01152  0.00281  -0.01396 135 VAL A O   
862  C  CB  . VAL A 135 ? 0.06835 0.08314 0.11796 0.01426  0.01410  -0.01312 135 VAL A CB  
863  C  CG1 . VAL A 135 ? 0.08715 0.09558 0.13421 -0.01968 0.01748  -0.05029 135 VAL A CG1 
864  C  CG2 . VAL A 135 ? 0.06075 0.09736 0.13017 0.03261  0.01207  0.00043  135 VAL A CG2 
865  N  N   . ASN A 136 ? 0.05878 0.07351 0.07049 0.01688  -0.01214 0.00098  136 ASN A N   
866  C  CA  . ASN A 136 ? 0.06702 0.05520 0.08782 0.00903  -0.00081 -0.00845 136 ASN A CA  
867  C  C   . ASN A 136 ? 0.06308 0.05478 0.06378 0.02009  0.00346  0.01532  136 ASN A C   
868  O  O   . ASN A 136 ? 0.07863 0.07661 0.06985 0.02221  -0.00245 -0.00969 136 ASN A O   
869  C  CB  . ASN A 136 ? 0.08848 0.07020 0.08732 0.01712  0.02128  0.00789  136 ASN A CB  
870  C  CG  . ASN A 136 ? 0.11597 0.08075 0.10036 0.01849  0.05557  0.01777  136 ASN A CG  
871  O  OD1 . ASN A 136 ? 0.11861 0.07469 0.10220 0.02294  0.01158  0.01596  136 ASN A OD1 
872  N  ND2 . ASN A 136 ? 0.13753 0.10065 0.23661 0.02149  0.07514  0.03565  136 ASN A ND2 
873  N  N   . SER A 137 ? 0.05712 0.06235 0.06848 0.01645  -0.00426 -0.00185 137 SER A N   
874  C  CA  . SER A 137 ? 0.07290 0.07662 0.08021 0.00945  -0.01621 -0.00199 137 SER A CA  
875  C  C   . SER A 137 ? 0.08612 0.07278 0.11367 0.01357  -0.01964 -0.00640 137 SER A C   
876  O  O   . SER A 137 ? 0.08370 0.09395 0.11766 0.01486  -0.02566 -0.00124 137 SER A O   
877  C  CB  . SER A 137 ? 0.07586 0.08499 0.10145 0.01081  0.00040  -0.01897 137 SER A CB  
878  O  OG  . SER A 137 ? 0.06773 0.08326 0.09366 0.01816  -0.01226 -0.00652 137 SER A OG  
879  N  N   . CYS A 138 ? 0.10559 0.08587 0.07019 0.02401  -0.01323 0.00834  138 CYS A N   
880  C  CA  . CYS A 138 ? 0.14268 0.10382 0.09375 0.05157  -0.00391 0.01253  138 CYS A CA  
881  C  C   . CYS A 138 ? 0.14602 0.10057 0.06387 0.04958  -0.01012 0.00195  138 CYS A C   
882  O  O   . CYS A 138 ? 0.15984 0.13124 0.09571 0.05803  -0.00369 0.00827  138 CYS A O   
883  C  CB  . CYS A 138 ? 0.17446 0.11993 0.12297 0.08280  0.01873  0.00893  138 CYS A CB  
884  S  SG  . CYS A 138 ? 0.18510 0.14686 0.12905 0.09179  0.00628  0.02409  138 CYS A SG  
885  N  N   . ILE A 139 ? 0.13430 0.07080 0.08051 0.02069  0.00678  -0.00331 139 ILE A N   
886  C  CA  . ILE A 139 ? 0.13024 0.08757 0.09642 0.01677  0.01385  -0.01965 139 ILE A CA  
887  C  C   . ILE A 139 ? 0.12812 0.08932 0.08767 0.01600  0.00511  -0.01792 139 ILE A C   
888  O  O   . ILE A 139 ? 0.12449 0.08697 0.07890 0.00931  0.00878  -0.01385 139 ILE A O   
889  C  CB  . ILE A 139 ? 0.13369 0.11571 0.11687 0.00119  0.02069  -0.00426 139 ILE A CB  
890  C  CG1 . ILE A 139 ? 0.14299 0.12982 0.15783 -0.00363 0.01686  0.00061  139 ILE A CG1 
891  C  CG2 . ILE A 139 ? 0.13800 0.13984 0.12693 0.00105  0.02146  -0.01970 139 ILE A CG2 
892  C  CD1 . ILE A 139 ? 0.15426 0.13839 0.16693 -0.01511 0.03813  -0.00180 139 ILE A CD1 
893  N  N   . PRO A 140 ? 0.14110 0.09229 0.07954 0.03158  -0.01573 -0.02140 140 PRO A N   
894  C  CA  . PRO A 140 ? 0.15553 0.08942 0.12567 0.02721  -0.03241 -0.03720 140 PRO A CA  
895  C  C   . PRO A 140 ? 0.16514 0.08582 0.11135 0.02227  -0.00161 -0.03800 140 PRO A C   
896  O  O   . PRO A 140 ? 0.17423 0.10920 0.13004 0.01701  0.02472  -0.01194 140 PRO A O   
897  C  CB  . PRO A 140 ? 0.16496 0.12422 0.16758 0.01598  -0.05062 -0.02840 140 PRO A CB  
898  C  CG  . PRO A 140 ? 0.16458 0.13371 0.18736 0.02463  -0.05114 -0.02457 140 PRO A CG  
899  C  CD  . PRO A 140 ? 0.15172 0.11068 0.13446 0.03743  -0.04557 -0.02749 140 PRO A CD  
900  N  N   . GLU A 141 ? 0.17658 0.08240 0.13394 0.02675  -0.02416 -0.01533 141 GLU A N   
901  C  CA  . GLU A 141 ? 0.18664 0.10213 0.15438 0.02757  -0.01097 -0.01430 141 GLU A CA  
902  C  C   . GLU A 141 ? 0.20586 0.13709 0.23072 0.00551  -0.02458 -0.02482 141 GLU A C   
903  O  O   . GLU A 141 ? 0.22220 0.16231 0.27463 -0.00438 -0.02576 -0.05527 141 GLU A O   
904  C  CB  . GLU A 141 ? 0.17698 0.12070 0.15148 0.03155  -0.00595 -0.02624 141 GLU A CB  
905  C  CG  . GLU A 141 ? 0.15847 0.10830 0.13177 0.02298  -0.00823 -0.00960 141 GLU A CG  
906  C  CD  . GLU A 141 ? 0.13803 0.11461 0.13120 0.01581  -0.00167 -0.01714 141 GLU A CD  
907  O  OE1 . GLU A 141 ? 0.12252 0.10559 0.15546 0.01507  0.00807  -0.02382 141 GLU A OE1 
908  O  OE2 . GLU A 141 ? 0.13150 0.10703 0.08636 0.02502  0.02868  -0.00924 141 GLU A OE2 
909  C  C1  . BDP B .   ? 0.30441 0.37960 0.47195 -0.04898 -0.03157 0.06109  1   BDP C C1  
910  C  C2  . BDP B .   ? 0.30556 0.38369 0.47041 -0.04126 -0.02718 0.06963  1   BDP C C2  
911  C  C3  . BDP B .   ? 0.30491 0.37727 0.44769 -0.04067 -0.03024 0.05679  1   BDP C C3  
912  C  C4  . BDP B .   ? 0.29022 0.33602 0.39582 -0.03927 -0.04384 0.04093  1   BDP C C4  
913  C  C5  . BDP B .   ? 0.30086 0.36451 0.42055 -0.04774 -0.04400 0.05865  1   BDP C C5  
914  C  C6  . BDP B .   ? 0.30915 0.37627 0.42872 -0.05457 -0.04716 0.05524  1   BDP C C6  
915  O  O2  . BDP B .   ? 0.30939 0.39582 0.48820 -0.03155 -0.02799 0.07576  1   BDP C O2  
916  O  O3  . BDP B .   ? 0.31660 0.39678 0.49989 -0.04215 -0.03055 0.03591  1   BDP C O3  
917  O  O4  . BDP B .   ? 0.26705 0.25956 0.29060 -0.03632 -0.06511 0.02115  1   BDP C O4  
918  O  O5  . BDP B .   ? 0.30346 0.37762 0.45703 -0.04741 -0.04449 0.05638  1   BDP C O5  
919  O  O6A . BDP B .   ? 0.30060 0.35125 0.36122 -0.09573 -0.05840 0.03346  1   BDP C O6A 
920  O  O6B . BDP B .   ? 0.32097 0.39834 0.46914 -0.03320 -0.04762 0.06143  1   BDP C O6B 
921  C  C1  . NAG B .   ? 0.23350 0.17583 0.19475 -0.04780 -0.06623 -0.00813 2   NAG C C1  
922  C  C2  . NAG B .   ? 0.21821 0.14408 0.14141 -0.05554 -0.02851 -0.01535 2   NAG C C2  
923  C  C3  . NAG B .   ? 0.18585 0.11665 0.13715 -0.05350 -0.02195 -0.02109 2   NAG C C3  
924  C  C4  . NAG B .   ? 0.18422 0.11034 0.16335 -0.03837 -0.03438 -0.01648 2   NAG C C4  
925  C  C5  . NAG B .   ? 0.20527 0.14641 0.18461 -0.04059 -0.06130 -0.02887 2   NAG C C5  
926  C  C6  . NAG B .   ? 0.21179 0.19566 0.25000 -0.04134 -0.05486 -0.05295 2   NAG C C6  
927  C  C7  . NAG B .   ? 0.26220 0.18838 0.23794 -0.05228 0.02329  -0.05708 2   NAG C C7  
928  C  C8  . NAG B .   ? 0.27166 0.18255 0.23026 -0.04386 0.03709  -0.04948 2   NAG C C8  
929  N  N2  . NAG B .   ? 0.24213 0.16846 0.17288 -0.05088 0.00016  -0.02503 2   NAG C N2  
930  O  O3  . NAG B .   ? 0.16870 0.09891 0.14961 -0.03266 -0.00527 -0.02566 2   NAG C O3  
931  O  O4  . NAG B .   ? 0.16354 0.08024 0.18681 -0.03540 -0.02385 -0.02964 2   NAG C O4  
932  O  O5  . NAG B .   ? 0.21896 0.14709 0.22402 -0.04643 -0.09067 -0.02019 2   NAG C O5  
933  O  O6  . NAG B .   ? 0.22224 0.23544 0.33855 -0.03720 -0.04186 -0.06750 2   NAG C O6  
934  O  O7  . NAG B .   ? 0.26739 0.19729 0.25747 -0.06148 0.03300  -0.11165 2   NAG C O7  
935  C  C1  . BDP B .   ? 0.16886 0.11066 0.15725 -0.01688 0.00673  -0.03729 3   BDP C C1  
936  C  C2  . BDP B .   ? 0.17974 0.12782 0.14388 -0.00269 -0.00018 -0.03980 3   BDP C C2  
937  C  C3  . BDP B .   ? 0.16790 0.12800 0.14196 -0.00210 0.00765  -0.04749 3   BDP C C3  
938  C  C4  . BDP B .   ? 0.15200 0.11996 0.11516 0.00096  0.02530  -0.04957 3   BDP C C4  
939  C  C5  . BDP B .   ? 0.14637 0.12212 0.13176 0.00293  0.03099  -0.03166 3   BDP C C5  
940  C  C6  . BDP B .   ? 0.13688 0.11717 0.14636 0.00177  0.04721  -0.01682 3   BDP C C6  
941  O  O2  . BDP B .   ? 0.19890 0.15327 0.17641 -0.00721 0.00839  -0.06115 3   BDP C O2  
942  O  O3  . BDP B .   ? 0.17697 0.13544 0.18087 0.00651  0.01271  -0.05979 3   BDP C O3  
943  O  O4  . BDP B .   ? 0.15562 0.10626 0.15995 -0.00689 0.02896  -0.03317 3   BDP C O4  
944  O  O5  . BDP B .   ? 0.15294 0.12150 0.14909 -0.00873 0.01724  -0.03053 3   BDP C O5  
945  O  O6A . BDP B .   ? 0.12776 0.12821 0.13782 -0.00195 0.04028  -0.02768 3   BDP C O6A 
946  O  O6B . BDP B .   ? 0.13908 0.12123 0.16669 -0.00202 0.05776  -0.02689 3   BDP C O6B 
947  C  C1  . NAG B .   ? 0.16045 0.08387 0.18878 -0.00772 0.01065  -0.04108 4   NAG C C1  
948  C  C2  . NAG B .   ? 0.15068 0.08330 0.15582 -0.00921 0.00127  -0.03334 4   NAG C C2  
949  C  C3  . NAG B .   ? 0.16070 0.09126 0.16469 -0.00153 -0.01223 -0.04928 4   NAG C C3  
950  C  C4  . NAG B .   ? 0.18605 0.09027 0.20112 -0.00010 -0.00545 -0.01595 4   NAG C C4  
951  C  C5  . NAG B .   ? 0.19277 0.08901 0.21529 -0.00693 -0.00523 -0.01669 4   NAG C C5  
952  C  C6  . NAG B .   ? 0.21471 0.11470 0.26586 -0.00398 -0.01080 -0.00683 4   NAG C C6  
953  C  C7  . NAG B .   ? 0.13158 0.11190 0.11551 -0.02128 0.02561  -0.03035 4   NAG C C7  
954  C  C8  . NAG B .   ? 0.13007 0.11531 0.08482 -0.02673 0.01785  -0.00821 4   NAG C C8  
955  N  N2  . NAG B .   ? 0.13346 0.09760 0.11809 -0.01800 0.01743  -0.03076 4   NAG C N2  
956  O  O3  . NAG B .   ? 0.15149 0.12124 0.18567 0.00999  -0.02573 -0.05474 4   NAG C O3  
957  O  O4  . NAG B .   ? 0.20914 0.10177 0.25163 0.01311  0.00248  0.00944  4   NAG C O4  
958  O  O5  . NAG B .   ? 0.17710 0.08814 0.20201 -0.00856 0.00352  -0.03856 4   NAG C O5  
959  O  O6  . NAG B .   ? 0.23304 0.16229 0.32447 0.00604  -0.02890 -0.04068 4   NAG C O6  
960  O  O7  . NAG B .   ? 0.14311 0.13962 0.15590 -0.02916 0.05033  -0.04748 4   NAG C O7  
961  C  C1  . BDP B .   ? 0.16519 0.15035 0.14578 0.00826  -0.01610 -0.04317 5   BDP C C1  
962  C  C2  . BDP B .   ? 0.16783 0.18485 0.15918 -0.00042 -0.02434 -0.04410 5   BDP C C2  
963  C  C3  . BDP B .   ? 0.17053 0.19857 0.19358 0.01013  -0.04304 -0.05999 5   BDP C C3  
964  C  C4  . BDP B .   ? 0.18662 0.19354 0.14701 0.02756  -0.04204 -0.05805 5   BDP C C4  
965  C  C5  . BDP B .   ? 0.20117 0.17318 0.15977 0.02382  -0.02640 -0.03267 5   BDP C C5  
966  C  C6  . BDP B .   ? 0.23161 0.18742 0.20736 0.02976  -0.01293 -0.01044 5   BDP C C6  
967  O  O2  . BDP B .   ? 0.16864 0.20210 0.21302 -0.01475 0.00615  -0.04541 5   BDP C O2  
968  O  O3  . BDP B .   ? 0.17071 0.22515 0.24392 -0.00775 -0.04280 -0.06733 5   BDP C O3  
969  O  O4  . BDP B .   ? 0.20031 0.22687 0.16887 0.03121  -0.04484 -0.06036 5   BDP C O4  
970  O  O5  . BDP B .   ? 0.18620 0.14460 0.18612 0.01753  -0.02923 -0.01495 5   BDP C O5  
971  O  O6A . BDP B .   ? 0.23720 0.21243 0.21462 0.02269  0.01797  0.01485  5   BDP C O6A 
972  O  O6B . BDP B .   ? 0.25265 0.19529 0.27267 0.03737  -0.00626 -0.01856 5   BDP C O6B 
973  C  C1  . NAG B .   ? 0.22419 0.27396 0.23316 0.02920  -0.06108 -0.07325 6   NAG C C1  
974  C  C2  . NAG B .   ? 0.23734 0.28511 0.24259 0.00992  -0.06085 -0.08179 6   NAG C C2  
975  C  C3  . NAG B .   ? 0.24748 0.31628 0.31596 0.00652  -0.08449 -0.07987 6   NAG C C3  
976  C  C4  . NAG B .   ? 0.26004 0.34391 0.33334 0.01885  -0.10138 -0.06096 6   NAG C C4  
977  C  C5  . NAG B .   ? 0.25351 0.34050 0.34692 0.01889  -0.10190 -0.07217 6   NAG C C5  
978  C  C6  . NAG B .   ? 0.26010 0.37089 0.44555 0.00366  -0.09948 -0.04487 6   NAG C C6  
979  C  C7  . NAG B .   ? 0.24723 0.24931 0.22048 -0.01228 -0.04004 -0.06028 6   NAG C C7  
980  C  C8  . NAG B .   ? 0.25159 0.25473 0.24441 -0.00748 -0.03440 -0.06287 6   NAG C C8  
981  N  N2  . NAG B .   ? 0.24179 0.26784 0.22449 -0.00560 -0.03866 -0.08178 6   NAG C N2  
982  O  O3  . NAG B .   ? 0.24837 0.32312 0.34917 -0.00587 -0.09037 -0.09713 6   NAG C O3  
983  O  O4  . NAG B .   ? 0.27264 0.37072 0.34078 0.02138  -0.11545 -0.04527 6   NAG C O4  
984  O  O5  . NAG B .   ? 0.24216 0.30974 0.29057 0.02758  -0.07900 -0.09763 6   NAG C O5  
985  O  O6  . NAG B .   ? 0.26421 0.39472 0.48501 -0.01240 -0.09854 -0.04491 6   NAG C O6  
986  O  O7  . NAG B .   ? 0.25134 0.23797 0.23643 -0.01423 -0.03698 -0.01912 6   NAG C O7  
987  C  C1  . NAG C .   ? 0.21780 0.37943 0.15685 -0.00117 0.07269  -0.06089 401 NAG A C1  
988  C  C2  . NAG C .   ? 0.23786 0.41308 0.17713 0.00438  0.08877  -0.05396 401 NAG A C2  
989  C  C3  . NAG C .   ? 0.24296 0.44794 0.20349 0.01002  0.10331  -0.04093 401 NAG A C3  
990  C  C4  . NAG C .   ? 0.24883 0.44908 0.22454 0.01514  0.11915  -0.03242 401 NAG A C4  
991  C  C5  . NAG C .   ? 0.22676 0.45922 0.21667 0.01414  0.10130  -0.03785 401 NAG A C5  
992  C  C6  . NAG C .   ? 0.23584 0.46725 0.26614 0.00835  0.09548  -0.03851 401 NAG A C6  
993  C  C7  . NAG C .   ? 0.25304 0.46565 0.24126 -0.01734 0.09493  -0.05792 401 NAG A C7  
994  C  C8  . NAG C .   ? 0.25906 0.47423 0.23317 -0.01391 0.09761  -0.05936 401 NAG A C8  
995  N  N2  . NAG C .   ? 0.23609 0.44398 0.19732 -0.01476 0.09772  -0.04817 401 NAG A N2  
996  O  O3  . NAG C .   ? 0.24047 0.45955 0.20304 0.00747  0.10153  -0.03244 401 NAG A O3  
997  O  O4  . NAG C .   ? 0.24098 0.47614 0.27081 0.01851  0.13385  -0.01674 401 NAG A O4  
998  O  O5  . NAG C .   ? 0.22092 0.41044 0.17641 0.01229  0.07781  -0.06291 401 NAG A O5  
999  O  O6  . NAG C .   ? 0.24709 0.48824 0.30216 0.00731  0.10094  -0.04334 401 NAG A O6  
1000 O  O7  . NAG C .   ? 0.26457 0.48490 0.28858 -0.02381 0.09645  -0.06004 401 NAG A O7  
1001 C  C1  . NAG D .   ? 0.05162 0.12839 0.08187 -0.00537 0.00164  -0.01910 402 NAG A C1  
1002 C  C2  . NAG D .   ? 0.05910 0.15490 0.08504 0.00545  0.00012  0.00089  402 NAG A C2  
1003 C  C3  . NAG D .   ? 0.05705 0.19274 0.08166 0.00109  -0.01100 -0.01310 402 NAG A C3  
1004 C  C4  . NAG D .   ? 0.07329 0.19936 0.09795 -0.01569 -0.00762 -0.04235 402 NAG A C4  
1005 C  C5  . NAG D .   ? 0.06795 0.15942 0.09598 -0.01668 -0.00671 -0.03934 402 NAG A C5  
1006 C  C6  . NAG D .   ? 0.07529 0.14264 0.11411 -0.02094 0.00524  -0.03625 402 NAG A C6  
1007 C  C7  . NAG D .   ? 0.08045 0.14059 0.12069 0.01054  0.02431  -0.00045 402 NAG A C7  
1008 C  C8  . NAG D .   ? 0.07990 0.16996 0.12832 0.01820  0.02215  -0.00876 402 NAG A C8  
1009 N  N2  . NAG D .   ? 0.07057 0.15704 0.09150 0.01306  0.01173  -0.00615 402 NAG A N2  
1010 O  O3  . NAG D .   ? 0.06404 0.23030 0.09483 0.01279  0.00836  -0.00728 402 NAG A O3  
1011 O  O4  . NAG D .   ? 0.08797 0.23313 0.12129 -0.02637 -0.00886 -0.03922 402 NAG A O4  
1012 O  O5  . NAG D .   ? 0.06028 0.12955 0.08580 -0.01154 -0.01021 -0.02303 402 NAG A O5  
1013 O  O6  . NAG D .   ? 0.07808 0.14011 0.12630 -0.01314 0.01398  -0.04768 402 NAG A O6  
1014 O  O7  . NAG D .   ? 0.09623 0.12818 0.16086 0.00181  0.03858  0.00584  402 NAG A O7  
1015 C  C1  A GOL E .   ? 0.12608 0.29717 0.26023 0.01469  -0.03055 0.00881  403 GOL A C1  
1016 C  C1  B GOL E .   ? 0.11050 0.07711 0.09756 -0.01240 0.00869  -0.04247 403 GOL A C1  
1017 O  O1  A GOL E .   ? 0.12315 0.30590 0.24527 0.01316  -0.01987 -0.01426 403 GOL A O1  
1018 O  O1  B GOL E .   ? 0.12763 0.11099 0.14891 -0.02140 0.01210  -0.03622 403 GOL A O1  
1019 C  C2  A GOL E .   ? 0.13073 0.29665 0.25697 0.01000  -0.03569 0.01932  403 GOL A C2  
1020 C  C2  B GOL E .   ? 0.10125 0.06061 0.06012 -0.01439 0.01420  -0.01765 403 GOL A C2  
1021 O  O2  A GOL E .   ? 0.13081 0.29687 0.25490 0.01094  -0.02091 0.02300  403 GOL A O2  
1022 O  O2  B GOL E .   ? 0.10694 0.04304 0.07153 -0.01550 0.02882  -0.00115 403 GOL A O2  
1023 C  C3  A GOL E .   ? 0.13492 0.29512 0.25942 0.01094  -0.05137 0.03008  403 GOL A C3  
1024 C  C3  B GOL E .   ? 0.09604 0.05933 0.04339 -0.00032 -0.01091 -0.02353 403 GOL A C3  
1025 O  O3  A GOL E .   ? 0.13598 0.28867 0.26256 0.01379  -0.05624 0.03305  403 GOL A O3  
1026 O  O3  B GOL E .   ? 0.07749 0.05514 0.03419 0.01081  0.01151  -0.01694 403 GOL A O3  
1027 C  C1  . PEG F .   ? 0.54334 0.42349 0.31388 -0.14535 0.15769  -0.15230 404 PEG A C1  
1028 O  O1  . PEG F .   ? 0.54195 0.44384 0.34440 -0.12929 0.17678  -0.12918 404 PEG A O1  
1029 C  C2  . PEG F .   ? 0.49156 0.40090 0.29118 -0.13006 0.14579  -0.15407 404 PEG A C2  
1030 O  O2  . PEG F .   ? 0.54200 0.42013 0.31353 -0.15465 0.13375  -0.17064 404 PEG A O2  
1031 C  C3  . PEG F .   ? 0.49914 0.41960 0.28219 -0.11942 0.11668  -0.16344 404 PEG A C3  
1032 C  C4  . PEG F .   ? 0.53032 0.42925 0.28864 -0.10928 0.12249  -0.16479 404 PEG A C4  
1033 O  O4  . PEG F .   ? 0.55326 0.43569 0.30041 -0.10402 0.13294  -0.16748 404 PEG A O4  
1034 C  C1  . PEG G .   ? 0.63337 0.85308 0.37973 0.22991  0.07107  -0.05429 405 PEG A C1  
1035 O  O1  . PEG G .   ? 0.62912 0.84989 0.34771 0.23225  0.08324  -0.05029 405 PEG A O1  
1036 C  C2  . PEG G .   ? 0.63539 0.85398 0.37454 0.22798  0.06968  -0.07538 405 PEG A C2  
1037 O  O2  . PEG G .   ? 0.63967 0.86203 0.42987 0.22331  0.05605  -0.06153 405 PEG A O2  
1038 C  C3  . PEG G .   ? 0.64044 0.86756 0.41910 0.21946  0.04373  -0.06513 405 PEG A C3  
1039 C  C4  . PEG G .   ? 0.63998 0.86881 0.41263 0.21570  0.03776  -0.06041 405 PEG A C4  
1040 O  O4  . PEG G .   ? 0.63910 0.86848 0.40331 0.21260  0.03860  -0.04926 405 PEG A O4  
1041 C  C1  . PEG H .   ? 0.71272 0.58850 0.59504 -0.02945 -0.00234 0.25510  406 PEG A C1  
1042 O  O1  . PEG H .   ? 0.71366 0.59859 0.60603 -0.03354 0.00194  0.24807  406 PEG A O1  
1043 C  C2  . PEG H .   ? 0.71214 0.58146 0.57671 -0.02534 -0.01161 0.27247  406 PEG A C2  
1044 O  O2  . PEG H .   ? 0.71084 0.57225 0.57487 -0.02224 -0.01964 0.27212  406 PEG A O2  
1045 C  C3  . PEG H .   ? 0.70912 0.55203 0.54638 -0.01469 -0.02996 0.29144  406 PEG A C3  
1046 C  C4  . PEG H .   ? 0.70907 0.52842 0.53073 -0.00460 -0.03699 0.29741  406 PEG A C4  
1047 O  O4  . PEG H .   ? 0.70660 0.50889 0.48737 0.00661  -0.03374 0.29660  406 PEG A O4  
1048 CL CL  . CL  I .   ? 0.51923 0.40886 0.29307 -0.03376 0.00157  -0.12528 407 CL  A CL  
# 
